data_9BBV
# 
_entry.id   9BBV 
# 
_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   9BBV         pdb_00009bbv 10.2210/pdb9bbv/pdb 
WWPDB D_1000282105 ?            ?                   
# 
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                        9BBV 
_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                 5 
_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 
'Nayak, A.'   1 0000-0001-8735-4132 
'Afsar, M.'   2 0000-0002-3062-9219 
'Nayak, D.'   3 0000-0003-3680-0846 
'Olsen, S.K.' 4 0000-0002-1265-7101 
# 
_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 6j 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 'Nayak, A.'   1 0000-0001-8735-4132 
primary 'Afsar, M.'   2 0000-0002-3062-9219 
primary 'Nayak, D.'   3 0000-0003-3680-0846 
primary 'Olsen, S.K.' 4 0000-0002-1265-7101 
# 
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-{(1E,2R)-1-imino-3-[(3R)-2-oxopyrrolidin-3-yl]propan-2-yl}-N~2~-[4-(2-methyl-2H-indazol-4-yl)benzoyl]-L-leucinamide' 502.608   
1  ?         ? ? ? 
3 water       nat water 18.015    27 ?         ? ? ? 
# 
_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-{(1E,2R)-1-imino-3-[(3R)-2-oxopyrrolidin-3-yl]propan-2-yl}-N~2~-[4-(2-methyl-2H-indazol-4-yl)benzoyl]-L-leucinamide' A1ALD 
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 
A1ALD non-polymer         . 
'N-{(1E,2R)-1-imino-3-[(3R)-2-oxopyrrolidin-3-yl]propan-2-yl}-N~2~-[4-(2-methyl-2H-indazol-4-yl)benzoyl]-L-leucinamide' ? 
'C28 H34 N6 O3'  502.608 
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 ARG 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 ARG 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 ARG 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 ARG 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 GLU 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        A1ALD 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1ALD 
_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 A1ALD 1  401 401 A1ALD LIG A . 
C 3 HOH   1  501 25  HOH   HOH A . 
C 3 HOH   2  502 4   HOH   HOH A . 
C 3 HOH   3  503 22  HOH   HOH A . 
C 3 HOH   4  504 26  HOH   HOH A . 
C 3 HOH   5  505 11  HOH   HOH A . 
C 3 HOH   6  506 15  HOH   HOH A . 
C 3 HOH   7  507 10  HOH   HOH A . 
C 3 HOH   8  508 1   HOH   HOH A . 
C 3 HOH   9  509 21  HOH   HOH A . 
C 3 HOH   10 510 13  HOH   HOH A . 
C 3 HOH   11 511 18  HOH   HOH A . 
C 3 HOH   12 512 8   HOH   HOH A . 
C 3 HOH   13 513 2   HOH   HOH A . 
C 3 HOH   14 514 19  HOH   HOH A . 
C 3 HOH   15 515 9   HOH   HOH A . 
C 3 HOH   16 516 12  HOH   HOH A . 
C 3 HOH   17 517 20  HOH   HOH A . 
C 3 HOH   18 518 23  HOH   HOH A . 
C 3 HOH   19 519 16  HOH   HOH A . 
C 3 HOH   20 520 7   HOH   HOH A . 
C 3 HOH   21 521 14  HOH   HOH A . 
C 3 HOH   22 522 24  HOH   HOH A . 
C 3 HOH   23 523 3   HOH   HOH A . 
C 3 HOH   24 524 6   HOH   HOH A . 
C 3 HOH   25 525 17  HOH   HOH A . 
C 3 HOH   26 526 5   HOH   HOH A . 
C 3 HOH   27 527 27  HOH   HOH A . 
# 
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                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9BBV 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     45.454 
_cell.length_a_esd                 ? 
_cell.length_b                     63.933 
_cell.length_b_esd                 ? 
_cell.length_c                     105.904 
_cell.length_c_esd                 ? 
_cell.volume                       307758.145 
_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                         9BBV 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                18 
_symmetry.space_group_name_Hall            'P 2 2ab' 
_symmetry.space_group_name_H-M             'P 21 21 2' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9BBV 
_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             2.27 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          45.92 
_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              7.5 
_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    '12.5%(w/v) PEG 4K, 20%(v/v) 1,2,6-hexanetriol 0.01 M of each Polyamine 0.1 M BES/TEA' 
_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                          46.34 
_reflns.entry_id                                       9BBV 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.38 
_reflns.d_resolution_low                               63.76 
_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                                     12746 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.9 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                13.0 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          7.9 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                0.082 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.993 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.282 
_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                                    2.38 
_reflns_shell.d_res_low                                     2.47 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.1 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1281 
_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                               0.659 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.397 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          99.8 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  2.387 
_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                               49.49 
_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                                 9BBV 
_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                            2.46 
_refine.ls_d_res_low                             41.77 
_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                     11355 
_refine.ls_number_reflns_R_free                  1135 
_refine.ls_number_reflns_R_work                  10220 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    96.79 
_refine.ls_percent_reflns_R_free                 10.00 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2246 
_refine.ls_R_factor_R_free                       0.2578 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2209 
_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                          1.35 
_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                 25.7527 
_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                            0.3302 
_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                       2.46 
_refine_hist.d_res_low                        41.77 
_refine_hist.number_atoms_solvent             27 
_refine_hist.number_atoms_total               2411 
_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        2347 
_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' ? 0.0023 ? 2439 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.5317 ? 3317 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0416 ? 372  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0040 ? 429  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 6.4363 ? 330  ? 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' 2.46 2.57  . . 122 1105 86.71 . . . . 0.3125 . . . . . . . . . . . 0.3924 
'X-RAY DIFFRACTION' 2.57 2.71  . . 144 1294 99.58 . . . . 0.2818 . . . . . . . . . . . 0.3064 
'X-RAY DIFFRACTION' 2.71 2.88  . . 144 1287 98.96 . . . . 0.2790 . . . . . . . . . . . 0.3295 
'X-RAY DIFFRACTION' 2.88 3.10  . . 140 1269 98.81 . . . . 0.2840 . . . . . . . . . . . 0.2832 
'X-RAY DIFFRACTION' 3.10 3.41  . . 142 1273 96.65 . . . . 0.2474 . . . . . . . . . . . 0.3201 
'X-RAY DIFFRACTION' 3.41 3.91  . . 142 1289 98.08 . . . . 0.2230 . . . . . . . . . . . 0.2688 
'X-RAY DIFFRACTION' 3.91 4.92  . . 147 1320 97.87 . . . . 0.1769 . . . . . . . . . . . 0.2337 
'X-RAY DIFFRACTION' 4.92 41.77 . . 154 1383 97.40 . . . . 0.1828 . . . . . . . . . . . 0.1832 
# 
_struct.entry_id                     9BBV 
_struct.title                        'SARS-CoV-2 Mpro in complex with compound 6j 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        9BBV 
_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              9BBV 
_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)' 5020  ? 
1 MORE         -26   ? 
1 'SSA (A^2)'  25500 ? 
# 
_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 ASN A 53  ? ARG A 60  ? ASN A 53  ARG A 60  1 ? 8  
HELX_P HELX_P4  AA4 SER A 62  ? HIS A 64  ? SER A 62  HIS A 64  5 ? 3  
HELX_P HELX_P5  AA5 ILE A 200 ? ASN A 214 ? ILE A 200 ASN A 214 1 ? 15 
HELX_P HELX_P6  AA6 THR A 226 ? LYS A 236 ? THR A 226 LYS A 236 1 ? 11 
HELX_P HELX_P7  AA7 THR A 243 ? LEU A 250 ? THR A 243 LEU A 250 1 ? 8  
HELX_P HELX_P8  AA8 LEU A 250 ? GLY A 258 ? LEU A 250 GLY A 258 1 ? 9  
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 ? GLY A 302 ? THR A 292 GLY A 302 1 ? 11 
# 
_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           A1ALD 
_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            A1ALD 
_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               1.801 
_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                      A1ALD 
_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                       A1ALD 
_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                        A1ALD 
_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 LEU A 67  ? O LEU A 67  N THR A 21  ? N THR A 21  
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 ILE A 78  ? N ILE A 78  
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 VAL A 114 ? N VAL A 114 O TYR A 126 ? O TYR A 126 
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                   9BBV 
_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_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   OG 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   SER 
_pdbx_validate_close_contact.auth_seq_id_1    254 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   ILE 
_pdbx_validate_close_contact.auth_seq_id_2    259 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_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  ? ? 57.50   -134.90 
2 1 ASN A 51  ? ? -162.67 73.70   
3 1 ARG A 60  ? ? -64.10  9.73    
4 1 ASN A 84  ? ? 59.08   -120.93 
5 1 TYR A 154 ? ? 54.97   -79.96  
6 1 HIS A 164 ? ? -132.20 -39.07  
7 1 PRO A 184 ? ? -91.33  54.63   
# 
_pdbx_struct_special_symmetry.id              1 
_pdbx_struct_special_symmetry.PDB_model_num   1 
_pdbx_struct_special_symmetry.auth_asym_id    A 
_pdbx_struct_special_symmetry.auth_comp_id    HOH 
_pdbx_struct_special_symmetry.auth_seq_id     504 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   C 
_pdbx_struct_special_symmetry.label_comp_id   HOH 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z           
2 x+1/2,-y+1/2,-z 
3 -x+1/2,y+1/2,-z 
4 -x,-y,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         -1.78477886199 
_pdbx_refine_tls.origin_y         12.9920958673 
_pdbx_refine_tls.origin_z         -27.1845108585 
_pdbx_refine_tls.T[1][1]          0.367889486596 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          0.0446642295455 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          -0.0335828066535 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.335592903918 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          -0.0311125241142 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.362626860719 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          1.01554583161 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          0.169754959971 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          -0.399527096208 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          0.529684578912 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          -0.0741173989788 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          0.875589625805 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          0.010605275162 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          -0.187403640041 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          0.160552999459 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          -0.00805991254756 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          -0.0100602798594 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          -0.00551668708254 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          -0.0187436002749 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          0.0571198862406 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          0.0138250932613 
_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 
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      A 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       527 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   5.89 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
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 
A1ALD C13  C N S 1   
A1ALD C17  C N N 2   
A1ALD C22  C Y N 3   
A1ALD C24  C Y N 4   
A1ALD C26  C Y N 5   
A1ALD C28  C Y N 6   
A1ALD C02  C N N 7   
A1ALD C04  C N S 8   
A1ALD C05  C N N 9   
A1ALD C06  C N N 10  
A1ALD C07  C N N 11  
A1ALD C08  C N N 12  
A1ALD C09  C N N 13  
A1ALD C11  C N S 14  
A1ALD C12  C N N 15  
A1ALD C14  C N N 16  
A1ALD C16  C N N 17  
A1ALD C19  C N N 18  
A1ALD C23  C Y N 19  
A1ALD C25  C Y N 20  
A1ALD C27  C Y N 21  
A1ALD C29  C Y N 22  
A1ALD C30  C Y N 23  
A1ALD C33  C N N 24  
A1ALD C34  C Y N 25  
A1ALD C35  C Y N 26  
A1ALD C36  C Y N 27  
A1ALD C37  C Y N 28  
A1ALD N03  N N N 29  
A1ALD N10  N N N 30  
A1ALD N15  N N N 31  
A1ALD N20  N N N 32  
A1ALD N31  N Y N 33  
A1ALD N32  N Y N 34  
A1ALD O01  O N N 35  
A1ALD O18  O N N 36  
A1ALD O21  O N N 37  
A1ALD H131 H N N 38  
A1ALD H171 H N N 39  
A1ALD H172 H N N 40  
A1ALD H241 H N N 41  
A1ALD H281 H N N 42  
A1ALD H041 H N N 43  
A1ALD H052 H N N 44  
A1ALD H051 H N N 45  
A1ALD H061 H N N 46  
A1ALD H071 H N N 47  
A1ALD H073 H N N 48  
A1ALD H072 H N N 49  
A1ALD H081 H N N 50  
A1ALD H082 H N N 51  
A1ALD H083 H N N 52  
A1ALD H111 H N N 53  
A1ALD H121 H N N 54  
A1ALD H122 H N N 55  
A1ALD H162 H N N 56  
A1ALD H161 H N N 57  
A1ALD H191 H N N 58  
A1ALD H231 H N N 59  
A1ALD H271 H N N 60  
A1ALD H291 H N N 61  
A1ALD H333 H N N 62  
A1ALD H332 H N N 63  
A1ALD H331 H N N 64  
A1ALD H341 H N N 65  
A1ALD H361 H N N 66  
A1ALD H371 H N N 67  
A1ALD H031 H N N 68  
A1ALD H101 H N N 69  
A1ALD H151 H N N 70  
A1ALD H201 H N N 71  
ALA   N    N N N 72  
ALA   CA   C N S 73  
ALA   C    C N N 74  
ALA   O    O N N 75  
ALA   CB   C N N 76  
ALA   OXT  O N N 77  
ALA   H    H N N 78  
ALA   H2   H N N 79  
ALA   HA   H N N 80  
ALA   HB1  H N N 81  
ALA   HB2  H N N 82  
ALA   HB3  H N N 83  
ALA   HXT  H N N 84  
ARG   N    N N N 85  
ARG   CA   C N S 86  
ARG   C    C N N 87  
ARG   O    O N N 88  
ARG   CB   C N N 89  
ARG   CG   C N N 90  
ARG   CD   C N N 91  
ARG   NE   N N N 92  
ARG   CZ   C N N 93  
ARG   NH1  N N N 94  
ARG   NH2  N N N 95  
ARG   OXT  O N N 96  
ARG   H    H N N 97  
ARG   H2   H N N 98  
ARG   HA   H N N 99  
ARG   HB2  H N N 100 
ARG   HB3  H N N 101 
ARG   HG2  H N N 102 
ARG   HG3  H N N 103 
ARG   HD2  H N N 104 
ARG   HD3  H N N 105 
ARG   HE   H N N 106 
ARG   HH11 H N N 107 
ARG   HH12 H N N 108 
ARG   HH21 H N N 109 
ARG   HH22 H N N 110 
ARG   HXT  H N N 111 
ASN   N    N N N 112 
ASN   CA   C N S 113 
ASN   C    C N N 114 
ASN   O    O N N 115 
ASN   CB   C N N 116 
ASN   CG   C N N 117 
ASN   OD1  O N N 118 
ASN   ND2  N N N 119 
ASN   OXT  O N N 120 
ASN   H    H N N 121 
ASN   H2   H N N 122 
ASN   HA   H N N 123 
ASN   HB2  H N N 124 
ASN   HB3  H N N 125 
ASN   HD21 H N N 126 
ASN   HD22 H N N 127 
ASN   HXT  H N N 128 
ASP   N    N N N 129 
ASP   CA   C N S 130 
ASP   C    C N N 131 
ASP   O    O N N 132 
ASP   CB   C N N 133 
ASP   CG   C N N 134 
ASP   OD1  O N N 135 
ASP   OD2  O N N 136 
ASP   OXT  O N N 137 
ASP   H    H N N 138 
ASP   H2   H N N 139 
ASP   HA   H N N 140 
ASP   HB2  H N N 141 
ASP   HB3  H N N 142 
ASP   HD2  H N N 143 
ASP   HXT  H N N 144 
CYS   N    N N N 145 
CYS   CA   C N R 146 
CYS   C    C N N 147 
CYS   O    O N N 148 
CYS   CB   C N N 149 
CYS   SG   S N N 150 
CYS   OXT  O N N 151 
CYS   H    H N N 152 
CYS   H2   H N N 153 
CYS   HA   H N N 154 
CYS   HB2  H N N 155 
CYS   HB3  H N N 156 
CYS   HG   H N N 157 
CYS   HXT  H N N 158 
GLN   N    N N N 159 
GLN   CA   C N S 160 
GLN   C    C N N 161 
GLN   O    O N N 162 
GLN   CB   C N N 163 
GLN   CG   C N N 164 
GLN   CD   C N N 165 
GLN   OE1  O N N 166 
GLN   NE2  N N N 167 
GLN   OXT  O N N 168 
GLN   H    H N N 169 
GLN   H2   H N N 170 
GLN   HA   H N N 171 
GLN   HB2  H N N 172 
GLN   HB3  H N N 173 
GLN   HG2  H N N 174 
GLN   HG3  H N N 175 
GLN   HE21 H N N 176 
GLN   HE22 H N N 177 
GLN   HXT  H N N 178 
GLU   N    N N N 179 
GLU   CA   C N S 180 
GLU   C    C N N 181 
GLU   O    O N N 182 
GLU   CB   C N N 183 
GLU   CG   C N N 184 
GLU   CD   C N N 185 
GLU   OE1  O N N 186 
GLU   OE2  O N N 187 
GLU   OXT  O N N 188 
GLU   H    H N N 189 
GLU   H2   H N N 190 
GLU   HA   H N N 191 
GLU   HB2  H N N 192 
GLU   HB3  H N N 193 
GLU   HG2  H N N 194 
GLU   HG3  H N N 195 
GLU   HE2  H N N 196 
GLU   HXT  H N N 197 
GLY   N    N N N 198 
GLY   CA   C N N 199 
GLY   C    C N N 200 
GLY   O    O N N 201 
GLY   OXT  O N N 202 
GLY   H    H N N 203 
GLY   H2   H N N 204 
GLY   HA2  H N N 205 
GLY   HA3  H N N 206 
GLY   HXT  H N N 207 
HIS   N    N N N 208 
HIS   CA   C N S 209 
HIS   C    C N N 210 
HIS   O    O N N 211 
HIS   CB   C N N 212 
HIS   CG   C Y N 213 
HIS   ND1  N Y N 214 
HIS   CD2  C Y N 215 
HIS   CE1  C Y N 216 
HIS   NE2  N Y N 217 
HIS   OXT  O N N 218 
HIS   H    H N N 219 
HIS   H2   H N N 220 
HIS   HA   H N N 221 
HIS   HB2  H N N 222 
HIS   HB3  H N N 223 
HIS   HD1  H N N 224 
HIS   HD2  H N N 225 
HIS   HE1  H N N 226 
HIS   HE2  H N N 227 
HIS   HXT  H N N 228 
HOH   O    O N N 229 
HOH   H1   H N N 230 
HOH   H2   H N N 231 
ILE   N    N N N 232 
ILE   CA   C N S 233 
ILE   C    C N N 234 
ILE   O    O N N 235 
ILE   CB   C N S 236 
ILE   CG1  C N N 237 
ILE   CG2  C N N 238 
ILE   CD1  C N N 239 
ILE   OXT  O N N 240 
ILE   H    H N N 241 
ILE   H2   H N N 242 
ILE   HA   H N N 243 
ILE   HB   H N N 244 
ILE   HG12 H N N 245 
ILE   HG13 H N N 246 
ILE   HG21 H N N 247 
ILE   HG22 H N N 248 
ILE   HG23 H N N 249 
ILE   HD11 H N N 250 
ILE   HD12 H N N 251 
ILE   HD13 H N N 252 
ILE   HXT  H N N 253 
LEU   N    N N N 254 
LEU   CA   C N S 255 
LEU   C    C N N 256 
LEU   O    O N N 257 
LEU   CB   C N N 258 
LEU   CG   C N N 259 
LEU   CD1  C N N 260 
LEU   CD2  C N N 261 
LEU   OXT  O N N 262 
LEU   H    H N N 263 
LEU   H2   H N N 264 
LEU   HA   H N N 265 
LEU   HB2  H N N 266 
LEU   HB3  H N N 267 
LEU   HG   H N N 268 
LEU   HD11 H N N 269 
LEU   HD12 H N N 270 
LEU   HD13 H N N 271 
LEU   HD21 H N N 272 
LEU   HD22 H N N 273 
LEU   HD23 H N N 274 
LEU   HXT  H N N 275 
LYS   N    N N N 276 
LYS   CA   C N S 277 
LYS   C    C N N 278 
LYS   O    O N N 279 
LYS   CB   C N N 280 
LYS   CG   C N N 281 
LYS   CD   C N N 282 
LYS   CE   C N N 283 
LYS   NZ   N N N 284 
LYS   OXT  O N N 285 
LYS   H    H N N 286 
LYS   H2   H N N 287 
LYS   HA   H N N 288 
LYS   HB2  H N N 289 
LYS   HB3  H N N 290 
LYS   HG2  H N N 291 
LYS   HG3  H N N 292 
LYS   HD2  H N N 293 
LYS   HD3  H N N 294 
LYS   HE2  H N N 295 
LYS   HE3  H N N 296 
LYS   HZ1  H N N 297 
LYS   HZ2  H N N 298 
LYS   HZ3  H N N 299 
LYS   HXT  H N N 300 
MET   N    N N N 301 
MET   CA   C N S 302 
MET   C    C N N 303 
MET   O    O N N 304 
MET   CB   C N N 305 
MET   CG   C N N 306 
MET   SD   S N N 307 
MET   CE   C N N 308 
MET   OXT  O N N 309 
MET   H    H N N 310 
MET   H2   H N N 311 
MET   HA   H N N 312 
MET   HB2  H N N 313 
MET   HB3  H N N 314 
MET   HG2  H N N 315 
MET   HG3  H N N 316 
MET   HE1  H N N 317 
MET   HE2  H N N 318 
MET   HE3  H N N 319 
MET   HXT  H N N 320 
PHE   N    N N N 321 
PHE   CA   C N S 322 
PHE   C    C N N 323 
PHE   O    O N N 324 
PHE   CB   C N N 325 
PHE   CG   C Y N 326 
PHE   CD1  C Y N 327 
PHE   CD2  C Y N 328 
PHE   CE1  C Y N 329 
PHE   CE2  C Y N 330 
PHE   CZ   C Y N 331 
PHE   OXT  O N N 332 
PHE   H    H N N 333 
PHE   H2   H N N 334 
PHE   HA   H N N 335 
PHE   HB2  H N N 336 
PHE   HB3  H N N 337 
PHE   HD1  H N N 338 
PHE   HD2  H N N 339 
PHE   HE1  H N N 340 
PHE   HE2  H N N 341 
PHE   HZ   H N N 342 
PHE   HXT  H N N 343 
PRO   N    N N N 344 
PRO   CA   C N S 345 
PRO   C    C N N 346 
PRO   O    O N N 347 
PRO   CB   C N N 348 
PRO   CG   C N N 349 
PRO   CD   C N N 350 
PRO   OXT  O N N 351 
PRO   H    H N N 352 
PRO   HA   H N N 353 
PRO   HB2  H N N 354 
PRO   HB3  H N N 355 
PRO   HG2  H N N 356 
PRO   HG3  H N N 357 
PRO   HD2  H N N 358 
PRO   HD3  H N N 359 
PRO   HXT  H N N 360 
SER   N    N N N 361 
SER   CA   C N S 362 
SER   C    C N N 363 
SER   O    O N N 364 
SER   CB   C N N 365 
SER   OG   O N N 366 
SER   OXT  O N N 367 
SER   H    H N N 368 
SER   H2   H N N 369 
SER   HA   H N N 370 
SER   HB2  H N N 371 
SER   HB3  H N N 372 
SER   HG   H N N 373 
SER   HXT  H N N 374 
THR   N    N N N 375 
THR   CA   C N S 376 
THR   C    C N N 377 
THR   O    O N N 378 
THR   CB   C N R 379 
THR   OG1  O N N 380 
THR   CG2  C N N 381 
THR   OXT  O N N 382 
THR   H    H N N 383 
THR   H2   H N N 384 
THR   HA   H N N 385 
THR   HB   H N N 386 
THR   HG1  H N N 387 
THR   HG21 H N N 388 
THR   HG22 H N N 389 
THR   HG23 H N N 390 
THR   HXT  H N N 391 
TRP   N    N N N 392 
TRP   CA   C N S 393 
TRP   C    C N N 394 
TRP   O    O N N 395 
TRP   CB   C N N 396 
TRP   CG   C Y N 397 
TRP   CD1  C Y N 398 
TRP   CD2  C Y N 399 
TRP   NE1  N Y N 400 
TRP   CE2  C Y N 401 
TRP   CE3  C Y N 402 
TRP   CZ2  C Y N 403 
TRP   CZ3  C Y N 404 
TRP   CH2  C Y N 405 
TRP   OXT  O N N 406 
TRP   H    H N N 407 
TRP   H2   H N N 408 
TRP   HA   H N N 409 
TRP   HB2  H N N 410 
TRP   HB3  H N N 411 
TRP   HD1  H N N 412 
TRP   HE1  H N N 413 
TRP   HE3  H N N 414 
TRP   HZ2  H N N 415 
TRP   HZ3  H N N 416 
TRP   HH2  H N N 417 
TRP   HXT  H N N 418 
TYR   N    N N N 419 
TYR   CA   C N S 420 
TYR   C    C N N 421 
TYR   O    O N N 422 
TYR   CB   C N N 423 
TYR   CG   C Y N 424 
TYR   CD1  C Y N 425 
TYR   CD2  C Y N 426 
TYR   CE1  C Y N 427 
TYR   CE2  C Y N 428 
TYR   CZ   C Y N 429 
TYR   OH   O N N 430 
TYR   OXT  O N N 431 
TYR   H    H N N 432 
TYR   H2   H N N 433 
TYR   HA   H N N 434 
TYR   HB2  H N N 435 
TYR   HB3  H N N 436 
TYR   HD1  H N N 437 
TYR   HD2  H N N 438 
TYR   HE1  H N N 439 
TYR   HE2  H N N 440 
TYR   HH   H N N 441 
TYR   HXT  H N N 442 
VAL   N    N N N 443 
VAL   CA   C N S 444 
VAL   C    C N N 445 
VAL   O    O N N 446 
VAL   CB   C N N 447 
VAL   CG1  C N N 448 
VAL   CG2  C N N 449 
VAL   OXT  O N N 450 
VAL   H    H N N 451 
VAL   H2   H N N 452 
VAL   HA   H N N 453 
VAL   HB   H N N 454 
VAL   HG11 H N N 455 
VAL   HG12 H N N 456 
VAL   HG13 H N N 457 
VAL   HG21 H N N 458 
VAL   HG22 H N N 459 
VAL   HG23 H N N 460 
VAL   HXT  H N N 461 
# 
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 
A1ALD C02 O01  doub N N 1   
A1ALD C07 C06  sing N N 2   
A1ALD C08 C06  sing N N 3   
A1ALD C06 C05  sing N N 4   
A1ALD C05 C04  sing N N 5   
A1ALD C09 C04  sing N N 6   
A1ALD C14 C13  sing N N 7   
A1ALD C17 C16  sing N N 8   
A1ALD C16 N15  sing N N 9   
A1ALD N15 C14  sing N N 10  
A1ALD O18 C14  doub N N 11  
A1ALD C13 C12  sing N N 12  
A1ALD C12 C11  sing N N 13  
A1ALD C19 C11  sing N N 14  
A1ALD N20 C19  doub N N 15  
A1ALD C11 N10  sing N N 16  
A1ALD N10 C09  sing N N 17  
A1ALD O21 C09  doub N N 18  
A1ALD C04 N03  sing N N 19  
A1ALD N03 C02  sing N N 20  
A1ALD C22 C02  sing N N 21  
A1ALD C23 C22  doub Y N 22  
A1ALD C27 C26  doub Y N 23  
A1ALD N31 C30  doub Y N 24  
A1ALD N32 N31  sing Y N 25  
A1ALD C33 N32  sing N N 26  
A1ALD C34 N32  sing Y N 27  
A1ALD C35 C34  doub Y N 28  
A1ALD C30 C29  sing Y N 29  
A1ALD C29 C28  doub Y N 30  
A1ALD C28 C27  sing Y N 31  
A1ALD C26 C25  sing N N 32  
A1ALD C36 C25  sing Y N 33  
A1ALD C37 C36  doub Y N 34  
A1ALD C25 C24  doub Y N 35  
A1ALD C24 C23  sing Y N 36  
A1ALD C13 C17  sing N N 37  
A1ALD C22 C37  sing Y N 38  
A1ALD C26 C35  sing Y N 39  
A1ALD C30 C35  sing Y N 40  
A1ALD C13 H131 sing N N 41  
A1ALD C17 H171 sing N N 42  
A1ALD C17 H172 sing N N 43  
A1ALD C24 H241 sing N N 44  
A1ALD C28 H281 sing N N 45  
A1ALD C04 H041 sing N N 46  
A1ALD C05 H052 sing N N 47  
A1ALD C05 H051 sing N N 48  
A1ALD C06 H061 sing N N 49  
A1ALD C07 H071 sing N N 50  
A1ALD C07 H073 sing N N 51  
A1ALD C07 H072 sing N N 52  
A1ALD C08 H081 sing N N 53  
A1ALD C08 H082 sing N N 54  
A1ALD C08 H083 sing N N 55  
A1ALD C11 H111 sing N N 56  
A1ALD C12 H121 sing N N 57  
A1ALD C12 H122 sing N N 58  
A1ALD C16 H162 sing N N 59  
A1ALD C16 H161 sing N N 60  
A1ALD C19 H191 sing N N 61  
A1ALD C23 H231 sing N N 62  
A1ALD C27 H271 sing N N 63  
A1ALD C29 H291 sing N N 64  
A1ALD C33 H333 sing N N 65  
A1ALD C33 H332 sing N N 66  
A1ALD C33 H331 sing N N 67  
A1ALD C34 H341 sing N N 68  
A1ALD C36 H361 sing N N 69  
A1ALD C37 H371 sing N N 70  
A1ALD N03 H031 sing N N 71  
A1ALD N10 H101 sing N N 72  
A1ALD N15 H151 sing N N 73  
A1ALD N20 H201 sing N N 74  
ALA   N   CA   sing N N 75  
ALA   N   H    sing N N 76  
ALA   N   H2   sing N N 77  
ALA   CA  C    sing N N 78  
ALA   CA  CB   sing N N 79  
ALA   CA  HA   sing N N 80  
ALA   C   O    doub N N 81  
ALA   C   OXT  sing N N 82  
ALA   CB  HB1  sing N N 83  
ALA   CB  HB2  sing N N 84  
ALA   CB  HB3  sing N N 85  
ALA   OXT HXT  sing N N 86  
ARG   N   CA   sing N N 87  
ARG   N   H    sing N N 88  
ARG   N   H2   sing N N 89  
ARG   CA  C    sing N N 90  
ARG   CA  CB   sing N N 91  
ARG   CA  HA   sing N N 92  
ARG   C   O    doub N N 93  
ARG   C   OXT  sing N N 94  
ARG   CB  CG   sing N N 95  
ARG   CB  HB2  sing N N 96  
ARG   CB  HB3  sing N N 97  
ARG   CG  CD   sing N N 98  
ARG   CG  HG2  sing N N 99  
ARG   CG  HG3  sing N N 100 
ARG   CD  NE   sing N N 101 
ARG   CD  HD2  sing N N 102 
ARG   CD  HD3  sing N N 103 
ARG   NE  CZ   sing N N 104 
ARG   NE  HE   sing N N 105 
ARG   CZ  NH1  sing N N 106 
ARG   CZ  NH2  doub N N 107 
ARG   NH1 HH11 sing N N 108 
ARG   NH1 HH12 sing N N 109 
ARG   NH2 HH21 sing N N 110 
ARG   NH2 HH22 sing N N 111 
ARG   OXT HXT  sing N N 112 
ASN   N   CA   sing N N 113 
ASN   N   H    sing N N 114 
ASN   N   H2   sing N N 115 
ASN   CA  C    sing N N 116 
ASN   CA  CB   sing N N 117 
ASN   CA  HA   sing N N 118 
ASN   C   O    doub N N 119 
ASN   C   OXT  sing N N 120 
ASN   CB  CG   sing N N 121 
ASN   CB  HB2  sing N N 122 
ASN   CB  HB3  sing N N 123 
ASN   CG  OD1  doub N N 124 
ASN   CG  ND2  sing N N 125 
ASN   ND2 HD21 sing N N 126 
ASN   ND2 HD22 sing N N 127 
ASN   OXT HXT  sing N N 128 
ASP   N   CA   sing N N 129 
ASP   N   H    sing N N 130 
ASP   N   H2   sing N N 131 
ASP   CA  C    sing N N 132 
ASP   CA  CB   sing N N 133 
ASP   CA  HA   sing N N 134 
ASP   C   O    doub N N 135 
ASP   C   OXT  sing N N 136 
ASP   CB  CG   sing N N 137 
ASP   CB  HB2  sing N N 138 
ASP   CB  HB3  sing N N 139 
ASP   CG  OD1  doub N N 140 
ASP   CG  OD2  sing N N 141 
ASP   OD2 HD2  sing N N 142 
ASP   OXT HXT  sing N N 143 
CYS   N   CA   sing N N 144 
CYS   N   H    sing N N 145 
CYS   N   H2   sing N N 146 
CYS   CA  C    sing N N 147 
CYS   CA  CB   sing N N 148 
CYS   CA  HA   sing N N 149 
CYS   C   O    doub N N 150 
CYS   C   OXT  sing N N 151 
CYS   CB  SG   sing N N 152 
CYS   CB  HB2  sing N N 153 
CYS   CB  HB3  sing N N 154 
CYS   SG  HG   sing N N 155 
CYS   OXT HXT  sing N N 156 
GLN   N   CA   sing N N 157 
GLN   N   H    sing N N 158 
GLN   N   H2   sing N N 159 
GLN   CA  C    sing N N 160 
GLN   CA  CB   sing N N 161 
GLN   CA  HA   sing N N 162 
GLN   C   O    doub N N 163 
GLN   C   OXT  sing N N 164 
GLN   CB  CG   sing N N 165 
GLN   CB  HB2  sing N N 166 
GLN   CB  HB3  sing N N 167 
GLN   CG  CD   sing N N 168 
GLN   CG  HG2  sing N N 169 
GLN   CG  HG3  sing N N 170 
GLN   CD  OE1  doub N N 171 
GLN   CD  NE2  sing N N 172 
GLN   NE2 HE21 sing N N 173 
GLN   NE2 HE22 sing N N 174 
GLN   OXT HXT  sing N N 175 
GLU   N   CA   sing N N 176 
GLU   N   H    sing N N 177 
GLU   N   H2   sing N N 178 
GLU   CA  C    sing N N 179 
GLU   CA  CB   sing N N 180 
GLU   CA  HA   sing N N 181 
GLU   C   O    doub N N 182 
GLU   C   OXT  sing N N 183 
GLU   CB  CG   sing N N 184 
GLU   CB  HB2  sing N N 185 
GLU   CB  HB3  sing N N 186 
GLU   CG  CD   sing N N 187 
GLU   CG  HG2  sing N N 188 
GLU   CG  HG3  sing N N 189 
GLU   CD  OE1  doub N N 190 
GLU   CD  OE2  sing N N 191 
GLU   OE2 HE2  sing N N 192 
GLU   OXT HXT  sing N N 193 
GLY   N   CA   sing N N 194 
GLY   N   H    sing N N 195 
GLY   N   H2   sing N N 196 
GLY   CA  C    sing N N 197 
GLY   CA  HA2  sing N N 198 
GLY   CA  HA3  sing N N 199 
GLY   C   O    doub N N 200 
GLY   C   OXT  sing N N 201 
GLY   OXT HXT  sing N N 202 
HIS   N   CA   sing N N 203 
HIS   N   H    sing N N 204 
HIS   N   H2   sing N N 205 
HIS   CA  C    sing N N 206 
HIS   CA  CB   sing N N 207 
HIS   CA  HA   sing N N 208 
HIS   C   O    doub N N 209 
HIS   C   OXT  sing N N 210 
HIS   CB  CG   sing N N 211 
HIS   CB  HB2  sing N N 212 
HIS   CB  HB3  sing N N 213 
HIS   CG  ND1  sing Y N 214 
HIS   CG  CD2  doub Y N 215 
HIS   ND1 CE1  doub Y N 216 
HIS   ND1 HD1  sing N N 217 
HIS   CD2 NE2  sing Y N 218 
HIS   CD2 HD2  sing N N 219 
HIS   CE1 NE2  sing Y N 220 
HIS   CE1 HE1  sing N N 221 
HIS   NE2 HE2  sing N N 222 
HIS   OXT HXT  sing N N 223 
HOH   O   H1   sing N N 224 
HOH   O   H2   sing N N 225 
ILE   N   CA   sing N N 226 
ILE   N   H    sing N N 227 
ILE   N   H2   sing N N 228 
ILE   CA  C    sing N N 229 
ILE   CA  CB   sing N N 230 
ILE   CA  HA   sing N N 231 
ILE   C   O    doub N N 232 
ILE   C   OXT  sing N N 233 
ILE   CB  CG1  sing N N 234 
ILE   CB  CG2  sing N N 235 
ILE   CB  HB   sing N N 236 
ILE   CG1 CD1  sing N N 237 
ILE   CG1 HG12 sing N N 238 
ILE   CG1 HG13 sing N N 239 
ILE   CG2 HG21 sing N N 240 
ILE   CG2 HG22 sing N N 241 
ILE   CG2 HG23 sing N N 242 
ILE   CD1 HD11 sing N N 243 
ILE   CD1 HD12 sing N N 244 
ILE   CD1 HD13 sing N N 245 
ILE   OXT HXT  sing N N 246 
LEU   N   CA   sing N N 247 
LEU   N   H    sing N N 248 
LEU   N   H2   sing N N 249 
LEU   CA  C    sing N N 250 
LEU   CA  CB   sing N N 251 
LEU   CA  HA   sing N N 252 
LEU   C   O    doub N N 253 
LEU   C   OXT  sing N N 254 
LEU   CB  CG   sing N N 255 
LEU   CB  HB2  sing N N 256 
LEU   CB  HB3  sing N N 257 
LEU   CG  CD1  sing N N 258 
LEU   CG  CD2  sing N N 259 
LEU   CG  HG   sing N N 260 
LEU   CD1 HD11 sing N N 261 
LEU   CD1 HD12 sing N N 262 
LEU   CD1 HD13 sing N N 263 
LEU   CD2 HD21 sing N N 264 
LEU   CD2 HD22 sing N N 265 
LEU   CD2 HD23 sing N N 266 
LEU   OXT HXT  sing N N 267 
LYS   N   CA   sing N N 268 
LYS   N   H    sing N N 269 
LYS   N   H2   sing N N 270 
LYS   CA  C    sing N N 271 
LYS   CA  CB   sing N N 272 
LYS   CA  HA   sing N N 273 
LYS   C   O    doub N N 274 
LYS   C   OXT  sing N N 275 
LYS   CB  CG   sing N N 276 
LYS   CB  HB2  sing N N 277 
LYS   CB  HB3  sing N N 278 
LYS   CG  CD   sing N N 279 
LYS   CG  HG2  sing N N 280 
LYS   CG  HG3  sing N N 281 
LYS   CD  CE   sing N N 282 
LYS   CD  HD2  sing N N 283 
LYS   CD  HD3  sing N N 284 
LYS   CE  NZ   sing N N 285 
LYS   CE  HE2  sing N N 286 
LYS   CE  HE3  sing N N 287 
LYS   NZ  HZ1  sing N N 288 
LYS   NZ  HZ2  sing N N 289 
LYS   NZ  HZ3  sing N N 290 
LYS   OXT HXT  sing N N 291 
MET   N   CA   sing N N 292 
MET   N   H    sing N N 293 
MET   N   H2   sing N N 294 
MET   CA  C    sing N N 295 
MET   CA  CB   sing N N 296 
MET   CA  HA   sing N N 297 
MET   C   O    doub N N 298 
MET   C   OXT  sing N N 299 
MET   CB  CG   sing N N 300 
MET   CB  HB2  sing N N 301 
MET   CB  HB3  sing N N 302 
MET   CG  SD   sing N N 303 
MET   CG  HG2  sing N N 304 
MET   CG  HG3  sing N N 305 
MET   SD  CE   sing N N 306 
MET   CE  HE1  sing N N 307 
MET   CE  HE2  sing N N 308 
MET   CE  HE3  sing N N 309 
MET   OXT HXT  sing N N 310 
PHE   N   CA   sing N N 311 
PHE   N   H    sing N N 312 
PHE   N   H2   sing N N 313 
PHE   CA  C    sing N N 314 
PHE   CA  CB   sing N N 315 
PHE   CA  HA   sing N N 316 
PHE   C   O    doub N N 317 
PHE   C   OXT  sing N N 318 
PHE   CB  CG   sing N N 319 
PHE   CB  HB2  sing N N 320 
PHE   CB  HB3  sing N N 321 
PHE   CG  CD1  doub Y N 322 
PHE   CG  CD2  sing Y N 323 
PHE   CD1 CE1  sing Y N 324 
PHE   CD1 HD1  sing N N 325 
PHE   CD2 CE2  doub Y N 326 
PHE   CD2 HD2  sing N N 327 
PHE   CE1 CZ   doub Y N 328 
PHE   CE1 HE1  sing N N 329 
PHE   CE2 CZ   sing Y N 330 
PHE   CE2 HE2  sing N N 331 
PHE   CZ  HZ   sing N N 332 
PHE   OXT HXT  sing N N 333 
PRO   N   CA   sing N N 334 
PRO   N   CD   sing N N 335 
PRO   N   H    sing N N 336 
PRO   CA  C    sing N N 337 
PRO   CA  CB   sing N N 338 
PRO   CA  HA   sing N N 339 
PRO   C   O    doub N N 340 
PRO   C   OXT  sing N N 341 
PRO   CB  CG   sing N N 342 
PRO   CB  HB2  sing N N 343 
PRO   CB  HB3  sing N N 344 
PRO   CG  CD   sing N N 345 
PRO   CG  HG2  sing N N 346 
PRO   CG  HG3  sing N N 347 
PRO   CD  HD2  sing N N 348 
PRO   CD  HD3  sing N N 349 
PRO   OXT HXT  sing N N 350 
SER   N   CA   sing N N 351 
SER   N   H    sing N N 352 
SER   N   H2   sing N N 353 
SER   CA  C    sing N N 354 
SER   CA  CB   sing N N 355 
SER   CA  HA   sing N N 356 
SER   C   O    doub N N 357 
SER   C   OXT  sing N N 358 
SER   CB  OG   sing N N 359 
SER   CB  HB2  sing N N 360 
SER   CB  HB3  sing N N 361 
SER   OG  HG   sing N N 362 
SER   OXT HXT  sing N N 363 
THR   N   CA   sing N N 364 
THR   N   H    sing N N 365 
THR   N   H2   sing N N 366 
THR   CA  C    sing N N 367 
THR   CA  CB   sing N N 368 
THR   CA  HA   sing N N 369 
THR   C   O    doub N N 370 
THR   C   OXT  sing N N 371 
THR   CB  OG1  sing N N 372 
THR   CB  CG2  sing N N 373 
THR   CB  HB   sing N N 374 
THR   OG1 HG1  sing N N 375 
THR   CG2 HG21 sing N N 376 
THR   CG2 HG22 sing N N 377 
THR   CG2 HG23 sing N N 378 
THR   OXT HXT  sing N N 379 
TRP   N   CA   sing N N 380 
TRP   N   H    sing N N 381 
TRP   N   H2   sing N N 382 
TRP   CA  C    sing N N 383 
TRP   CA  CB   sing N N 384 
TRP   CA  HA   sing N N 385 
TRP   C   O    doub N N 386 
TRP   C   OXT  sing N N 387 
TRP   CB  CG   sing N N 388 
TRP   CB  HB2  sing N N 389 
TRP   CB  HB3  sing N N 390 
TRP   CG  CD1  doub Y N 391 
TRP   CG  CD2  sing Y N 392 
TRP   CD1 NE1  sing Y N 393 
TRP   CD1 HD1  sing N N 394 
TRP   CD2 CE2  doub Y N 395 
TRP   CD2 CE3  sing Y N 396 
TRP   NE1 CE2  sing Y N 397 
TRP   NE1 HE1  sing N N 398 
TRP   CE2 CZ2  sing Y N 399 
TRP   CE3 CZ3  doub Y N 400 
TRP   CE3 HE3  sing N N 401 
TRP   CZ2 CH2  doub Y N 402 
TRP   CZ2 HZ2  sing N N 403 
TRP   CZ3 CH2  sing Y N 404 
TRP   CZ3 HZ3  sing N N 405 
TRP   CH2 HH2  sing N N 406 
TRP   OXT HXT  sing N N 407 
TYR   N   CA   sing N N 408 
TYR   N   H    sing N N 409 
TYR   N   H2   sing N N 410 
TYR   CA  C    sing N N 411 
TYR   CA  CB   sing N N 412 
TYR   CA  HA   sing N N 413 
TYR   C   O    doub N N 414 
TYR   C   OXT  sing N N 415 
TYR   CB  CG   sing N N 416 
TYR   CB  HB2  sing N N 417 
TYR   CB  HB3  sing N N 418 
TYR   CG  CD1  doub Y N 419 
TYR   CG  CD2  sing Y N 420 
TYR   CD1 CE1  sing Y N 421 
TYR   CD1 HD1  sing N N 422 
TYR   CD2 CE2  doub Y N 423 
TYR   CD2 HD2  sing N N 424 
TYR   CE1 CZ   doub Y N 425 
TYR   CE1 HE1  sing N N 426 
TYR   CE2 CZ   sing Y N 427 
TYR   CE2 HE2  sing N N 428 
TYR   CZ  OH   sing N N 429 
TYR   OH  HH   sing N N 430 
TYR   OXT HXT  sing N N 431 
VAL   N   CA   sing N N 432 
VAL   N   H    sing N N 433 
VAL   N   H2   sing N N 434 
VAL   CA  C    sing N N 435 
VAL   CA  CB   sing N N 436 
VAL   CA  HA   sing N N 437 
VAL   C   O    doub N N 438 
VAL   C   OXT  sing N N 439 
VAL   CB  CG1  sing N N 440 
VAL   CB  CG2  sing N N 441 
VAL   CB  HB   sing N N 442 
VAL   CG1 HG11 sing N N 443 
VAL   CG1 HG12 sing N N 444 
VAL   CG1 HG13 sing N N 445 
VAL   CG2 HG21 sing N N 446 
VAL   CG2 HG22 sing N N 447 
VAL   CG2 HG23 sing N N 448 
VAL   OXT HXT  sing N N 449 
# 
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     'P 21 21 2' 
_space_group.name_Hall        'P 2 2ab' 
_space_group.IT_number        18 
_space_group.crystal_system   orthorhombic 
_space_group.id               1 
# 
_atom_sites.entry_id                    9BBV 
_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]   0.022000 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.015641 
_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]   0.009443 
_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   ? 15.37085  -6.98278 -30.80650 1.000 51.94161  ? 1   SER   A N   1 
ATOM   2    C CA  . SER   A 1 1   ? 15.05041  -6.20796 -31.99848 1.000 52.03333  ? 1   SER   A CA  1 
ATOM   3    C C   . SER   A 1 1   ? 13.54572  -6.16524 -32.24414 1.000 52.86321  ? 1   SER   A C   1 
ATOM   4    O O   . SER   A 1 1   ? 12.75786  -6.61333 -31.41118 1.000 51.60069  ? 1   SER   A O   1 
ATOM   5    C CB  . SER   A 1 1   ? 15.77033  -6.78168 -33.21922 1.000 54.19284  ? 1   SER   A CB  1 
ATOM   6    O OG  . SER   A 1 1   ? 17.15710  -6.92891 -32.96611 1.000 61.01948  ? 1   SER   A OG  1 
ATOM   7    N N   . GLY   A 1 2   ? 13.15754  -5.63398 -33.39734 1.000 54.82245  ? 2   GLY   A N   1 
ATOM   8    C CA  . GLY   A 1 2   ? 11.76546  -5.37692 -33.69485 1.000 51.38163  ? 2   GLY   A CA  1 
ATOM   9    C C   . GLY   A 1 2   ? 11.35801  -3.95907 -33.33107 1.000 51.75141  ? 2   GLY   A C   1 
ATOM   10   O O   . GLY   A 1 2   ? 11.97673  -3.29057 -32.50405 1.000 57.22624  ? 2   GLY   A O   1 
ATOM   11   N N   . PHE   A 1 3   ? 10.29178  -3.49244 -33.97606 1.000 51.61282  ? 3   PHE   A N   1 
ATOM   12   C CA  . PHE   A 1 3   ? 9.80452   -2.13943 -33.74788 1.000 47.05456  ? 3   PHE   A CA  1 
ATOM   13   C C   . PHE   A 1 3   ? 8.28607   -2.14799 -33.70855 1.000 45.85887  ? 3   PHE   A C   1 
ATOM   14   O O   . PHE   A 1 3   ? 7.64024   -2.64499 -34.63576 1.000 45.13203  ? 3   PHE   A O   1 
ATOM   15   C CB  . PHE   A 1 3   ? 10.30398  -1.17619 -34.82874 1.000 46.23308  ? 3   PHE   A CB  1 
ATOM   16   C CG  . PHE   A 1 3   ? 10.22449  0.26675  -34.42833 1.000 47.00727  ? 3   PHE   A CG  1 
ATOM   17   C CD1 . PHE   A 1 3   ? 11.17154  0.81294  -33.57732 1.000 47.81439  ? 3   PHE   A CD1 1 
ATOM   18   C CD2 . PHE   A 1 3   ? 9.20359   1.07677  -34.89730 1.000 44.14783  ? 3   PHE   A CD2 1 
ATOM   19   C CE1 . PHE   A 1 3   ? 11.10192  2.13924  -33.20011 1.000 46.75118  ? 3   PHE   A CE1 1 
ATOM   20   C CE2 . PHE   A 1 3   ? 9.12937   2.40546  -34.52627 1.000 42.94516  ? 3   PHE   A CE2 1 
ATOM   21   C CZ  . PHE   A 1 3   ? 10.08014  2.93750  -33.67680 1.000 45.87050  ? 3   PHE   A CZ  1 
ATOM   22   N N   . ARG   A 1 4   ? 7.72409   -1.59355 -32.63631 1.000 47.73957  ? 4   ARG   A N   1 
ATOM   23   C CA  . ARG   A 1 4   ? 6.28730   -1.60320 -32.41297 1.000 46.93428  ? 4   ARG   A CA  1 
ATOM   24   C C   . ARG   A 1 4   ? 5.84791   -0.26073 -31.85018 1.000 46.15160  ? 4   ARG   A C   1 
ATOM   25   O O   . ARG   A 1 4   ? 6.63337   0.45215  -31.21971 1.000 45.81231  ? 4   ARG   A O   1 
ATOM   26   C CB  . ARG   A 1 4   ? 5.87587   -2.71855 -31.44049 1.000 43.65873  ? 4   ARG   A CB  1 
ATOM   27   C CG  . ARG   A 1 4   ? 6.27529   -4.11652 -31.87278 1.000 45.83166  ? 4   ARG   A CG  1 
ATOM   28   C CD  . ARG   A 1 4   ? 5.45024   -4.57078 -33.05926 1.000 47.42782  ? 4   ARG   A CD  1 
ATOM   29   N NE  . ARG   A 1 4   ? 4.02408   -4.48772 -32.77229 1.000 47.54114  ? 4   ARG   A NE  1 
ATOM   30   C CZ  . ARG   A 1 4   ? 3.33799   -5.41150 -32.11453 1.000 49.78232  ? 4   ARG   A CZ  1 
ATOM   31   N NH1 . ARG   A 1 4   ? 3.91637   -6.51391 -31.66654 1.000 50.29511  ? 4   ARG   A NH1 1 
ATOM   32   N NH2 . ARG   A 1 4   ? 2.03947   -5.22317 -31.89815 1.000 52.10156  ? 4   ARG   A NH2 1 
ATOM   33   N N   . LYS   A 1 5   ? 4.58318   0.08025  -32.08975 1.000 46.84109  ? 5   LYS   A N   1 
ATOM   34   C CA  . LYS   A 1 5   ? 3.96645   1.18500  -31.36843 1.000 48.11022  ? 5   LYS   A CA  1 
ATOM   35   C C   . LYS   A 1 5   ? 3.88051   0.82365  -29.89283 1.000 46.90075  ? 5   LYS   A C   1 
ATOM   36   O O   . LYS   A 1 5   ? 3.23583   -0.16281 -29.52210 1.000 49.01879  ? 5   LYS   A O   1 
ATOM   37   C CB  . LYS   A 1 5   ? 2.57814   1.48850  -31.93122 1.000 48.94286  ? 5   LYS   A CB  1 
ATOM   38   C CG  . LYS   A 1 5   ? 2.09851   2.91066  -31.66719 1.000 48.04353  ? 5   LYS   A CG  1 
ATOM   39   C CD  . LYS   A 1 5   ? 1.85435   3.66983  -32.96307 1.000 50.77522  ? 5   LYS   A CD  1 
ATOM   40   C CE  . LYS   A 1 5   ? 0.41467   3.51966  -33.42790 1.000 55.20543  ? 5   LYS   A CE  1 
ATOM   41   N NZ  . LYS   A 1 5   ? 0.17370   4.20207  -34.72845 1.000 63.22752  ? 5   LYS   A NZ  1 
ATOM   42   N N   . MET   A 1 6   ? 4.54197   1.61248  -29.05182 1.000 45.57073  ? 6   MET   A N   1 
ATOM   43   C CA  . MET   A 1 6   ? 4.70825   1.27834  -27.64521 1.000 45.50961  ? 6   MET   A CA  1 
ATOM   44   C C   . MET   A 1 6   ? 4.19206   2.41332  -26.77664 1.000 42.43155  ? 6   MET   A C   1 
ATOM   45   O O   . MET   A 1 6   ? 4.51472   3.58143  -27.01537 1.000 45.04267  ? 6   MET   A O   1 
ATOM   46   C CB  . MET   A 1 6   ? 6.17840   0.98782  -27.32827 1.000 44.85939  ? 6   MET   A CB  1 
ATOM   47   C CG  . MET   A 1 6   ? 6.38586   0.01383  -26.18563 1.000 45.41455  ? 6   MET   A CG  1 
ATOM   48   S SD  . MET   A 1 6   ? 8.13059   -0.24285 -25.81859 1.000 52.22401  ? 6   MET   A SD  1 
ATOM   49   C CE  . MET   A 1 6   ? 8.61581   -1.24081 -27.22302 1.000 45.35087  ? 6   MET   A CE  1 
ATOM   50   N N   . ALA   A 1 7   ? 3.39423   2.06401  -25.77395 1.000 37.26110  ? 7   ALA   A N   1 
ATOM   51   C CA  . ALA   A 1 7   ? 2.86774   3.01231  -24.80780 1.000 40.51502  ? 7   ALA   A CA  1 
ATOM   52   C C   . ALA   A 1 7   ? 3.59046   2.85203  -23.47712 1.000 39.90331  ? 7   ALA   A C   1 
ATOM   53   O O   . ALA   A 1 7   ? 4.15106   1.79646  -23.17045 1.000 42.36802  ? 7   ALA   A O   1 
ATOM   54   C CB  . ALA   A 1 7   ? 1.35813   2.82516  -24.61591 1.000 38.65104  ? 7   ALA   A CB  1 
ATOM   55   N N   . PHE   A 1 8   ? 3.57688   3.92269  -22.68977 1.000 40.83166  ? 8   PHE   A N   1 
ATOM   56   C CA  . PHE   A 1 8   ? 4.22545   3.89760  -21.39116 1.000 40.80623  ? 8   PHE   A CA  1 
ATOM   57   C C   . PHE   A 1 8   ? 3.48109   2.95866  -20.44273 1.000 40.87233  ? 8   PHE   A C   1 
ATOM   58   O O   . PHE   A 1 8   ? 2.27779   2.73243  -20.59776 1.000 40.43383  ? 8   PHE   A O   1 
ATOM   59   C CB  . PHE   A 1 8   ? 4.27397   5.30101  -20.79247 1.000 42.75881  ? 8   PHE   A CB  1 
ATOM   60   C CG  . PHE   A 1 8   ? 5.36583   6.16275  -21.35476 1.000 44.70324  ? 8   PHE   A CG  1 
ATOM   61   C CD1 . PHE   A 1 8   ? 6.64825   6.10751  -20.83435 1.000 47.85726  ? 8   PHE   A CD1 1 
ATOM   62   C CD2 . PHE   A 1 8   ? 5.11117   7.02515  -22.40707 1.000 43.84855  ? 8   PHE   A CD2 1 
ATOM   63   C CE1 . PHE   A 1 8   ? 7.65597   6.89789  -21.35190 1.000 50.38929  ? 8   PHE   A CE1 1 
ATOM   64   C CE2 . PHE   A 1 8   ? 6.11514   7.81731  -22.92985 1.000 48.02237  ? 8   PHE   A CE2 1 
ATOM   65   C CZ  . PHE   A 1 8   ? 7.38918   7.75412  -22.40118 1.000 49.15922  ? 8   PHE   A CZ  1 
ATOM   66   N N   . PRO   A 1 9   ? 4.17778   2.38711  -19.46185 1.000 40.67084  ? 9   PRO   A N   1 
ATOM   67   C CA  . PRO   A 1 9   ? 3.48299   1.62139  -18.41861 1.000 42.87496  ? 9   PRO   A CA  1 
ATOM   68   C C   . PRO   A 1 9   ? 2.51947   2.51809  -17.65484 1.000 45.29475  ? 9   PRO   A C   1 
ATOM   69   O O   . PRO   A 1 9   ? 2.89684   3.57917  -17.15361 1.000 45.59977  ? 9   PRO   A O   1 
ATOM   70   C CB  . PRO   A 1 9   ? 4.62357   1.11481  -17.52789 1.000 41.85923  ? 9   PRO   A CB  1 
ATOM   71   C CG  . PRO   A 1 9   ? 5.84652   1.18947  -18.38907 1.000 43.22375  ? 9   PRO   A CG  1 
ATOM   72   C CD  . PRO   A 1 9   ? 5.63950   2.35954  -19.29208 1.000 42.06861  ? 9   PRO   A CD  1 
ATOM   73   N N   . SER   A 1 10  ? 1.26367   2.08338  -17.57174 1.000 40.60205  ? 10  SER   A N   1 
ATOM   74   C CA  . SER   A 1 10  ? 0.17784   2.91889  -17.07695 1.000 42.54599  ? 10  SER   A CA  1 
ATOM   75   C C   . SER   A 1 10  ? -0.09978  2.73342  -15.59010 1.000 43.45603  ? 10  SER   A C   1 
ATOM   76   O O   . SER   A 1 10  ? -1.12901  3.21152  -15.10459 1.000 45.78860  ? 10  SER   A O   1 
ATOM   77   C CB  . SER   A 1 10  ? -1.09710  2.64316  -17.87756 1.000 44.30620  ? 10  SER   A CB  1 
ATOM   78   O OG  . SER   A 1 10  ? -1.52672  1.30273  -17.70698 1.000 44.97964  ? 10  SER   A OG  1 
ATOM   79   N N   . GLY   A 1 11  ? 0.79621   2.07034  -14.85591 1.000 46.40404  ? 11  GLY   A N   1 
ATOM   80   C CA  . GLY   A 1 11  ? 0.50999   1.75107  -13.46405 1.000 45.34350  ? 11  GLY   A CA  1 
ATOM   81   C C   . GLY   A 1 11  ? 0.29204   2.98061  -12.60154 1.000 47.31235  ? 11  GLY   A C   1 
ATOM   82   O O   . GLY   A 1 11  ? -0.67524  3.05539  -11.83863 1.000 45.75393  ? 11  GLY   A O   1 
ATOM   83   N N   . LYS   A 1 12  ? 1.19103   3.96349  -12.71123 1.000 47.14011  ? 12  LYS   A N   1 
ATOM   84   C CA  . LYS   A 1 12  ? 1.09553   5.15365  -11.86967 1.000 45.91299  ? 12  LYS   A CA  1 
ATOM   85   C C   . LYS   A 1 12  ? -0.18986  5.92452  -12.14093 1.000 46.54245  ? 12  LYS   A C   1 
ATOM   86   O O   . LYS   A 1 12  ? -0.83773  6.41525  -11.20857 1.000 46.67556  ? 12  LYS   A O   1 
ATOM   87   C CB  . LYS   A 1 12  ? 2.31196   6.05245  -12.09074 1.000 49.99203  ? 12  LYS   A CB  1 
ATOM   88   C CG  . LYS   A 1 12  ? 3.63134   5.43272  -11.66580 1.000 50.72294  ? 12  LYS   A CG  1 
ATOM   89   C CD  . LYS   A 1 12  ? 4.78051   5.95638  -12.51250 1.000 51.52960  ? 12  LYS   A CD  1 
ATOM   90   C CE  . LYS   A 1 12  ? 6.05776   6.08012  -11.69725 1.000 62.58994  ? 12  LYS   A CE  1 
ATOM   91   N NZ  . LYS   A 1 12  ? 7.17618   5.29880  -12.29404 1.000 69.37984  ? 12  LYS   A NZ  1 
ATOM   92   N N   . VAL   A 1 13  ? -0.57617  6.03984  -13.41300 1.000 45.09705  ? 13  VAL   A N   1 
ATOM   93   C CA  . VAL   A 1 13  ? -1.79341  6.76717  -13.75384 1.000 42.53767  ? 13  VAL   A CA  1 
ATOM   94   C C   . VAL   A 1 13  ? -3.02972  5.99058  -13.31653 1.000 43.91058  ? 13  VAL   A C   1 
ATOM   95   O O   . VAL   A 1 13  ? -4.06345  6.58854  -12.99212 1.000 42.04663  ? 13  VAL   A O   1 
ATOM   96   C CB  . VAL   A 1 13  ? -1.81825  7.07277  -15.26296 1.000 41.82855  ? 13  VAL   A CB  1 
ATOM   97   C CG1 . VAL   A 1 13  ? -2.98718  7.98055  -15.60790 1.000 44.79806  ? 13  VAL   A CG1 1 
ATOM   98   C CG2 . VAL   A 1 13  ? -0.50245  7.70080  -15.69674 1.000 43.84198  ? 13  VAL   A CG2 1 
ATOM   99   N N   . GLU   A 1 14  ? -2.94824  4.65687  -13.28909 1.000 45.01283  ? 14  GLU   A N   1 
ATOM   100  C CA  . GLU   A 1 14  ? -4.10180  3.85031  -12.89900 1.000 44.57668  ? 14  GLU   A CA  1 
ATOM   101  C C   . GLU   A 1 14  ? -4.54471  4.16149  -11.47490 1.000 47.25535  ? 14  GLU   A C   1 
ATOM   102  O O   . GLU   A 1 14  ? -5.74677  4.23396  -11.19304 1.000 47.70393  ? 14  GLU   A O   1 
ATOM   103  C CB  . GLU   A 1 14  ? -3.77821  2.36365  -13.04260 1.000 45.42773  ? 14  GLU   A CB  1 
ATOM   104  C CG  . GLU   A 1 14  ? -3.85588  1.84444  -14.46622 1.000 46.92781  ? 14  GLU   A CG  1 
ATOM   105  C CD  . GLU   A 1 14  ? -3.29225  0.44526  -14.60496 1.000 47.32665  ? 14  GLU   A CD  1 
ATOM   106  O OE1 . GLU   A 1 14  ? -3.80487  -0.47397 -13.93211 1.000 45.32279  ? 14  GLU   A OE1 1 
ATOM   107  O OE2 . GLU   A 1 14  ? -2.33182  0.26636  -15.38336 1.000 45.38576  ? 14  GLU   A OE2 1 
ATOM   108  N N   . GLY   A 1 15  ? -3.59139  4.35194  -10.56465 1.000 43.44518  ? 15  GLY   A N   1 
ATOM   109  C CA  . GLY   A 1 15  ? -3.91605  4.66303  -9.18632  1.000 44.80819  ? 15  GLY   A CA  1 
ATOM   110  C C   . GLY   A 1 15  ? -4.51504  6.03244  -8.95832  1.000 45.15289  ? 15  GLY   A C   1 
ATOM   111  O O   . GLY   A 1 15  ? -4.87168  6.35217  -7.82018  1.000 46.30501  ? 15  GLY   A O   1 
ATOM   112  N N   . CYS   A 1 16  ? -4.63827  6.84957  -10.00537 1.000 43.28595  ? 16  CYS   A N   1 
ATOM   113  C CA  . CYS   A 1 16  ? -5.18978  8.19043  -9.88875  1.000 43.60039  ? 16  CYS   A CA  1 
ATOM   114  C C   . CYS   A 1 16  ? -6.56766  8.33607  -10.51511 1.000 43.54369  ? 16  CYS   A C   1 
ATOM   115  O O   . CYS   A 1 16  ? -7.19941  9.38333  -10.33888 1.000 44.27082  ? 16  CYS   A O   1 
ATOM   116  C CB  . CYS   A 1 16  ? -4.24193  9.21117  -10.53373 1.000 43.28988  ? 16  CYS   A CB  1 
ATOM   117  S SG  . CYS   A 1 16  ? -2.53028  9.06394  -9.99524  1.000 47.07644  ? 16  CYS   A SG  1 
ATOM   118  N N   . MET   A 1 17  ? -7.04776  7.32822  -11.23725 1.000 41.87364  ? 17  MET   A N   1 
ATOM   119  C CA  . MET   A 1 17  ? -8.32490  7.43322  -11.92658 1.000 42.05174  ? 17  MET   A CA  1 
ATOM   120  C C   . MET   A 1 17  ? -9.47414  7.20191  -10.95401 1.000 43.16842  ? 17  MET   A C   1 
ATOM   121  O O   . MET   A 1 17  ? -9.49454  6.20620  -10.22316 1.000 43.47695  ? 17  MET   A O   1 
ATOM   122  C CB  . MET   A 1 17  ? -8.39266  6.43177  -13.07806 1.000 41.22289  ? 17  MET   A CB  1 
ATOM   123  C CG  . MET   A 1 17  ? -7.35107  6.66348  -14.16247 1.000 41.48559  ? 17  MET   A CG  1 
ATOM   124  S SD  . MET   A 1 17  ? -7.24164  8.38586  -14.69060 1.000 47.91050  ? 17  MET   A SD  1 
ATOM   125  C CE  . MET   A 1 17  ? -8.89856  8.66670  -15.31425 1.000 42.44422  ? 17  MET   A CE  1 
ATOM   126  N N   . VAL   A 1 18  ? -10.42848 8.13228  -10.94459 1.000 40.48153  ? 18  VAL   A N   1 
ATOM   127  C CA  . VAL   A 1 18  ? -11.62746 8.02941  -10.12742 1.000 40.25818  ? 18  VAL   A CA  1 
ATOM   128  C C   . VAL   A 1 18  ? -12.83653 8.31061  -11.00697 1.000 41.48520  ? 18  VAL   A C   1 
ATOM   129  O O   . VAL   A 1 18  ? -12.73153 8.90770  -12.08068 1.000 42.08637  ? 18  VAL   A O   1 
ATOM   130  C CB  . VAL   A 1 18  ? -11.60962 8.99486  -8.92294  1.000 41.26987  ? 18  VAL   A CB  1 
ATOM   131  C CG1 . VAL   A 1 18  ? -10.49626 8.62536  -7.95836  1.000 41.80450  ? 18  VAL   A CG1 1 
ATOM   132  C CG2 . VAL   A 1 18  ? -11.46312 10.43011 -9.39889  1.000 39.51926  ? 18  VAL   A CG2 1 
ATOM   133  N N   . GLN   A 1 19  ? -13.99655 7.86715  -10.53298 1.000 44.04850  ? 19  GLN   A N   1 
ATOM   134  C CA  . GLN   A 1 19  ? -15.25686 8.09851  -11.22310 1.000 42.39646  ? 19  GLN   A CA  1 
ATOM   135  C C   . GLN   A 1 19  ? -15.93409 9.33706  -10.65118 1.000 43.01718  ? 19  GLN   A C   1 
ATOM   136  O O   . GLN   A 1 19  ? -16.02949 9.49185  -9.42983  1.000 44.93873  ? 19  GLN   A O   1 
ATOM   137  C CB  . GLN   A 1 19  ? -16.17771 6.88508  -11.09023 1.000 44.68234  ? 19  GLN   A CB  1 
ATOM   138  C CG  . GLN   A 1 19  ? -17.55474 7.09060  -11.70019 1.000 47.05119  ? 19  GLN   A CG  1 
ATOM   139  C CD  . GLN   A 1 19  ? -18.40458 5.83715  -11.66648 1.000 48.72101  ? 19  GLN   A CD  1 
ATOM   140  O OE1 . GLN   A 1 19  ? -18.81497 5.32298  -12.70585 1.000 50.35697  ? 19  GLN   A OE1 1 
ATOM   141  N NE2 . GLN   A 1 19  ? -18.67476 5.33843  -10.46592 1.000 50.29340  ? 19  GLN   A NE2 1 
ATOM   142  N N   . VAL   A 1 20  ? -16.39876 10.21648 -11.53424 1.000 43.47297  ? 20  VAL   A N   1 
ATOM   143  C CA  . VAL   A 1 20  ? -17.11981 11.42283 -11.14770 1.000 46.59903  ? 20  VAL   A CA  1 
ATOM   144  C C   . VAL   A 1 20  ? -18.53172 11.33406 -11.70611 1.000 49.37649  ? 20  VAL   A C   1 
ATOM   145  O O   . VAL   A 1 20  ? -18.71645 11.08638 -12.90364 1.000 51.87111  ? 20  VAL   A O   1 
ATOM   146  C CB  . VAL   A 1 20  ? -16.41485 12.69693 -11.64709 1.000 46.24229  ? 20  VAL   A CB  1 
ATOM   147  C CG1 . VAL   A 1 20  ? -17.18107 13.93445 -11.20068 1.000 41.69328  ? 20  VAL   A CG1 1 
ATOM   148  C CG2 . VAL   A 1 20  ? -14.98113 12.74014 -11.14420 1.000 43.82899  ? 20  VAL   A CG2 1 
ATOM   149  N N   . THR   A 1 21  ? -19.52299 11.53379 -10.83989 1.000 47.94015  ? 21  THR   A N   1 
ATOM   150  C CA  . THR   A 1 21  ? -20.92636 11.50634 -11.23236 1.000 46.92213  ? 21  THR   A CA  1 
ATOM   151  C C   . THR   A 1 21  ? -21.61736 12.74044 -10.67652 1.000 49.98231  ? 21  THR   A C   1 
ATOM   152  O O   . THR   A 1 21  ? -21.69067 12.91759 -9.45590  1.000 52.26466  ? 21  THR   A O   1 
ATOM   153  C CB  . THR   A 1 21  ? -21.62164 10.23610 -10.73502 1.000 49.13631  ? 21  THR   A CB  1 
ATOM   154  O OG1 . THR   A 1 21  ? -21.06555 9.09514  -11.39872 1.000 49.20388  ? 21  THR   A OG1 1 
ATOM   155  C CG2 . THR   A 1 21  ? -23.11525 10.30260 -11.01758 1.000 50.26092  ? 21  THR   A CG2 1 
ATOM   156  N N   . CYS   A 1 22  ? -22.11554 13.59039 -11.56928 1.000 48.18068  ? 22  CYS   A N   1 
ATOM   157  C CA  . CYS   A 1 22  ? -22.90652 14.75849 -11.20054 1.000 51.17591  ? 22  CYS   A CA  1 
ATOM   158  C C   . CYS   A 1 22  ? -24.31536 14.54775 -11.73955 1.000 51.19542  ? 22  CYS   A C   1 
ATOM   159  O O   . CYS   A 1 22  ? -24.53335 14.58963 -12.95557 1.000 50.89218  ? 22  CYS   A O   1 
ATOM   160  C CB  . CYS   A 1 22  ? -22.28736 16.04198 -11.74858 1.000 52.03314  ? 22  CYS   A CB  1 
ATOM   161  S SG  . CYS   A 1 22  ? -23.20745 17.54452 -11.34137 1.000 58.54440  ? 22  CYS   A SG  1 
ATOM   162  N N   . GLY   A 1 23  ? -25.26459 14.31335 -10.83671 1.000 48.79546  ? 23  GLY   A N   1 
ATOM   163  C CA  . GLY   A 1 23  ? -26.62889 14.03039 -11.23450 1.000 50.65460  ? 23  GLY   A CA  1 
ATOM   164  C C   . GLY   A 1 23  ? -26.75446 12.71260 -11.97026 1.000 52.13717  ? 23  GLY   A C   1 
ATOM   165  O O   . GLY   A 1 23  ? -26.89437 11.65513 -11.34833 1.000 54.17085  ? 23  GLY   A O   1 
ATOM   166  N N   . THR   A 1 24  ? -26.69899 12.76210 -13.30172 1.000 52.18499  ? 24  THR   A N   1 
ATOM   167  C CA  . THR   A 1 24  ? -26.76809 11.56330 -14.12231 1.000 52.01214  ? 24  THR   A CA  1 
ATOM   168  C C   . THR   A 1 24  ? -25.57898 11.38914 -15.05348 1.000 54.86112  ? 24  THR   A C   1 
ATOM   169  O O   . THR   A 1 24  ? -25.30908 10.25763 -15.47296 1.000 55.50659  ? 24  THR   A O   1 
ATOM   170  C CB  . THR   A 1 24  ? -28.05857 11.55673 -14.95905 1.000 58.87239  ? 24  THR   A CB  1 
ATOM   171  O OG1 . THR   A 1 24  ? -28.27623 12.85821 -15.51852 1.000 59.69028  ? 24  THR   A OG1 1 
ATOM   172  C CG2 . THR   A 1 24  ? -29.24867 11.18114 -14.09058 1.000 63.53129  ? 24  THR   A CG2 1 
ATOM   173  N N   . THR   A 1 25  ? -24.86643 12.46175 -15.38693 1.000 53.26640  ? 25  THR   A N   1 
ATOM   174  C CA  . THR   A 1 25  ? -23.68397 12.34229 -16.22757 1.000 53.86584  ? 25  THR   A CA  1 
ATOM   175  C C   . THR   A 1 25  ? -22.52982 11.75523 -15.42555 1.000 50.49274  ? 25  THR   A C   1 
ATOM   176  O O   . THR   A 1 25  ? -22.24870 12.19332 -14.30582 1.000 49.96443  ? 25  THR   A O   1 
ATOM   177  C CB  . THR   A 1 25  ? -23.29002 13.70356 -16.79886 1.000 52.63785  ? 25  THR   A CB  1 
ATOM   178  O OG1 . THR   A 1 25  ? -24.46964 14.45546 -17.10806 1.000 55.62574  ? 25  THR   A OG1 1 
ATOM   179  C CG2 . THR   A 1 25  ? -22.45894 13.53015 -18.06208 1.000 52.71432  ? 25  THR   A CG2 1 
ATOM   180  N N   . THR   A 1 26  ? -21.85929 10.76337 -16.00370 1.000 50.53032  ? 26  THR   A N   1 
ATOM   181  C CA  . THR   A 1 26  ? -20.75011 10.08183 -15.35553 1.000 48.76332  ? 26  THR   A CA  1 
ATOM   182  C C   . THR   A 1 26  ? -19.57090 10.00586 -16.31220 1.000 45.15828  ? 26  THR   A C   1 
ATOM   183  O O   . THR   A 1 26  ? -19.73298 9.66948  -17.48947 1.000 45.39094  ? 26  THR   A O   1 
ATOM   184  C CB  . THR   A 1 26  ? -21.14622 8.67037  -14.90115 1.000 46.56616  ? 26  THR   A CB  1 
ATOM   185  O OG1 . THR   A 1 26  ? -22.18080 8.75691  -13.91285 1.000 54.32779  ? 26  THR   A OG1 1 
ATOM   186  C CG2 . THR   A 1 26  ? -19.95320 7.94395  -14.30480 1.000 44.96366  ? 26  THR   A CG2 1 
ATOM   187  N N   . LEU   A 1 27  ? -18.38908 10.32679 -15.79751 1.000 46.10058  ? 27  LEU   A N   1 
ATOM   188  C CA  . LEU   A 1 27  ? -17.14340 10.24944 -16.55007 1.000 45.43165  ? 27  LEU   A CA  1 
ATOM   189  C C   . LEU   A 1 27  ? -15.99382 10.13794 -15.55301 1.000 43.77993  ? 27  LEU   A C   1 
ATOM   190  O O   . LEU   A 1 27  ? -16.20584 9.92244  -14.35440 1.000 42.70180  ? 27  LEU   A O   1 
ATOM   191  C CB  . LEU   A 1 27  ? -16.98074 11.44356 -17.50060 1.000 43.85200  ? 27  LEU   A CB  1 
ATOM   192  C CG  . LEU   A 1 27  ? -17.03964 12.88495 -16.98661 1.000 42.96905  ? 27  LEU   A CG  1 
ATOM   193  C CD1 . LEU   A 1 27  ? -16.53316 13.83274 -18.05533 1.000 48.56483  ? 27  LEU   A CD1 1 
ATOM   194  C CD2 . LEU   A 1 27  ? -18.45348 13.27754 -16.62447 1.000 48.42116  ? 27  LEU   A CD2 1 
ATOM   195  N N   . ASN   A 1 28  ? -14.77243 10.29099 -16.04894 1.000 41.56315  ? 28  ASN   A N   1 
ATOM   196  C CA  . ASN   A 1 28  ? -13.57589 9.98969  -15.28042 1.000 43.77153  ? 28  ASN   A CA  1 
ATOM   197  C C   . ASN   A 1 28  ? -12.91450 11.25740 -14.75445 1.000 44.63249  ? 28  ASN   A C   1 
ATOM   198  O O   . ASN   A 1 28  ? -13.03078 12.33718 -15.34130 1.000 44.92453  ? 28  ASN   A O   1 
ATOM   199  C CB  . ASN   A 1 28  ? -12.58221 9.20046  -16.13275 1.000 40.06931  ? 28  ASN   A CB  1 
ATOM   200  C CG  . ASN   A 1 28  ? -13.26319 8.16229  -17.00120 1.000 45.07647  ? 28  ASN   A CG  1 
ATOM   201  O OD1 . ASN   A 1 28  ? -13.56973 7.06054  -16.54645 1.000 44.60442  ? 28  ASN   A OD1 1 
ATOM   202  N ND2 . ASN   A 1 28  ? -13.50650 8.51054  -18.25947 1.000 45.42242  ? 28  ASN   A ND2 1 
ATOM   203  N N   . GLY   A 1 29  ? -12.21012 11.10574 -13.63229 1.000 38.05649  ? 29  GLY   A N   1 
ATOM   204  C CA  . GLY   A 1 29  ? -11.48795 12.20379 -13.03235 1.000 37.86570  ? 29  GLY   A CA  1 
ATOM   205  C C   . GLY   A 1 29  ? -10.06035 11.81515 -12.72620 1.000 42.22331  ? 29  GLY   A C   1 
ATOM   206  O O   . GLY   A 1 29  ? -9.70107  10.63634 -12.67924 1.000 42.03287  ? 29  GLY   A O   1 
ATOM   207  N N   . LEU   A 1 30  ? -9.23116  12.83590 -12.51321 1.000 42.98241  ? 30  LEU   A N   1 
ATOM   208  C CA  . LEU   A 1 30  ? -7.81622  12.66151 -12.20278 1.000 43.51817  ? 30  LEU   A CA  1 
ATOM   209  C C   . LEU   A 1 30  ? -7.57915  13.11458 -10.76665 1.000 45.55611  ? 30  LEU   A C   1 
ATOM   210  O O   . LEU   A 1 30  ? -7.69765  14.30484 -10.45718 1.000 45.53560  ? 30  LEU   A O   1 
ATOM   211  C CB  . LEU   A 1 30  ? -6.94158  13.43883 -13.18400 1.000 42.46683  ? 30  LEU   A CB  1 
ATOM   212  C CG  . LEU   A 1 30  ? -5.43112  13.27099 -13.01087 1.000 44.87832  ? 30  LEU   A CG  1 
ATOM   213  C CD1 . LEU   A 1 30  ? -5.00737  11.84973 -13.35306 1.000 45.11027  ? 30  LEU   A CD1 1 
ATOM   214  C CD2 . LEU   A 1 30  ? -4.67903  14.27617 -13.86993 1.000 44.50239  ? 30  LEU   A CD2 1 
ATOM   215  N N   . TRP   A 1 31  ? -7.22993  12.16705 -9.89925  1.000 42.48758  ? 31  TRP   A N   1 
ATOM   216  C CA  . TRP   A 1 31  ? -7.11406  12.40144 -8.46075  1.000 42.11368  ? 31  TRP   A CA  1 
ATOM   217  C C   . TRP   A 1 31  ? -5.63507  12.49333 -8.09395  1.000 44.67545  ? 31  TRP   A C   1 
ATOM   218  O O   . TRP   A 1 31  ? -4.95199  11.47502 -7.95819  1.000 42.27364  ? 31  TRP   A O   1 
ATOM   219  C CB  . TRP   A 1 31  ? -7.82050  11.28811 -7.69312  1.000 40.26387  ? 31  TRP   A CB  1 
ATOM   220  C CG  . TRP   A 1 31  ? -7.84854  11.45856 -6.20514  1.000 43.42756  ? 31  TRP   A CG  1 
ATOM   221  C CD1 . TRP   A 1 31  ? -7.77425  12.62864 -5.50693  1.000 45.37160  ? 31  TRP   A CD1 1 
ATOM   222  C CD2 . TRP   A 1 31  ? -7.98050  10.41708 -5.22993  1.000 45.80071  ? 31  TRP   A CD2 1 
ATOM   223  N NE1 . TRP   A 1 31  ? -7.84203  12.37848 -4.15676  1.000 43.67152  ? 31  TRP   A NE1 1 
ATOM   224  C CE2 . TRP   A 1 31  ? -7.96969  11.02843 -3.96102  1.000 44.02350  ? 31  TRP   A CE2 1 
ATOM   225  C CE3 . TRP   A 1 31  ? -8.10134  9.02576  -5.30749  1.000 44.33787  ? 31  TRP   A CE3 1 
ATOM   226  C CZ2 . TRP   A 1 31  ? -8.07754  10.29731 -2.77936  1.000 48.84833  ? 31  TRP   A CZ2 1 
ATOM   227  C CZ3 . TRP   A 1 31  ? -8.20657  8.30183  -4.13414  1.000 44.00493  ? 31  TRP   A CZ3 1 
ATOM   228  C CH2 . TRP   A 1 31  ? -8.19305  8.93833  -2.88700  1.000 49.91923  ? 31  TRP   A CH2 1 
ATOM   229  N N   . LEU   A 1 32  ? -5.14303  13.72036 -7.93612  1.000 47.93566  ? 32  LEU   A N   1 
ATOM   230  C CA  . LEU   A 1 32  ? -3.77733  13.98208 -7.50151  1.000 50.73872  ? 32  LEU   A CA  1 
ATOM   231  C C   . LEU   A 1 32  ? -3.81978  14.84527 -6.25057  1.000 53.03301  ? 32  LEU   A C   1 
ATOM   232  O O   . LEU   A 1 32  ? -4.44861  15.90925 -6.24947  1.000 51.98088  ? 32  LEU   A O   1 
ATOM   233  C CB  . LEU   A 1 32  ? -2.96395  14.67591 -8.59550  1.000 47.42428  ? 32  LEU   A CB  1 
ATOM   234  C CG  . LEU   A 1 32  ? -3.00130  14.03666 -9.98314  1.000 47.54910  ? 32  LEU   A CG  1 
ATOM   235  C CD1 . LEU   A 1 32  ? -2.48159  15.01143 -11.02988 1.000 44.52787  ? 32  LEU   A CD1 1 
ATOM   236  C CD2 . LEU   A 1 32  ? -2.20280  12.74348 -9.99664  1.000 46.38142  ? 32  LEU   A CD2 1 
ATOM   237  N N   . ASP   A 1 33  ? -3.14303  14.39018 -5.19880  1.000 53.92980  ? 33  ASP   A N   1 
ATOM   238  C CA  . ASP   A 1 33  ? -3.21562  15.00297 -3.86573  1.000 56.13948  ? 33  ASP   A CA  1 
ATOM   239  C C   . ASP   A 1 33  ? -4.69062  14.97867 -3.46421  1.000 51.43958  ? 33  ASP   A C   1 
ATOM   240  O O   . ASP   A 1 33  ? -5.35048  13.94582 -3.65690  1.000 50.52275  ? 33  ASP   A O   1 
ATOM   241  C CB  . ASP   A 1 33  ? -2.54987  16.37483 -3.87672  1.000 57.16593  ? 33  ASP   A CB  1 
ATOM   242  C CG  . ASP   A 1 33  ? -1.10624  16.31809 -4.34048  1.000 62.30849  ? 33  ASP   A CG  1 
ATOM   243  O OD1 . ASP   A 1 33  ? -0.42101  15.32027 -4.03460  1.000 64.05238  ? 33  ASP   A OD1 1 
ATOM   244  O OD2 . ASP   A 1 33  ? -0.65458  17.27152 -5.00899  1.000 63.64869  ? 33  ASP   A OD2 1 
ATOM   245  N N   . ASP   A 1 34  ? -5.24645  16.06283 -2.92546  1.000 49.73591  ? 34  ASP   A N   1 
ATOM   246  C CA  . ASP   A 1 34  ? -6.64736  16.10209 -2.52446  1.000 53.52513  ? 34  ASP   A CA  1 
ATOM   247  C C   . ASP   A 1 34  ? -7.50186  16.89579 -3.50981  1.000 52.56529  ? 34  ASP   A C   1 
ATOM   248  O O   . ASP   A 1 34  ? -8.48711  17.52643 -3.11945  1.000 51.91374  ? 34  ASP   A O   1 
ATOM   249  C CB  . ASP   A 1 34  ? -6.78439  16.67321 -1.11326  1.000 53.38332  ? 34  ASP   A CB  1 
ATOM   250  C CG  . ASP   A 1 34  ? -6.33302  18.11864 -1.01917  1.000 53.36602  ? 34  ASP   A CG  1 
ATOM   251  O OD1 . ASP   A 1 34  ? -5.50803  18.54369 -1.85514  1.000 56.44927  ? 34  ASP   A OD1 1 
ATOM   252  O OD2 . ASP   A 1 34  ? -6.80413  18.83051 -0.10699  1.000 55.15462  ? 34  ASP   A OD2 1 
ATOM   253  N N   . VAL   A 1 35  ? -7.13847  16.87202 -4.79021  1.000 49.01027  ? 35  VAL   A N   1 
ATOM   254  C CA  . VAL   A 1 35  ? -7.86442  17.58959 -5.83131  1.000 48.27216  ? 35  VAL   A CA  1 
ATOM   255  C C   . VAL   A 1 35  ? -8.14308  16.62891 -6.97843  1.000 48.78596  ? 35  VAL   A C   1 
ATOM   256  O O   . VAL   A 1 35  ? -7.24250  15.90756 -7.42206  1.000 49.09206  ? 35  VAL   A O   1 
ATOM   257  C CB  . VAL   A 1 35  ? -7.08155  18.81840 -6.33296  1.000 48.98920  ? 35  VAL   A CB  1 
ATOM   258  C CG1 . VAL   A 1 35  ? -7.82234  19.48852 -7.48114  1.000 46.24835  ? 35  VAL   A CG1 1 
ATOM   259  C CG2 . VAL   A 1 35  ? -6.85004  19.80242 -5.19437  1.000 47.20671  ? 35  VAL   A CG2 1 
ATOM   260  N N   . VAL   A 1 36  ? -9.38597  16.61908 -7.45547  1.000 43.66552  ? 36  VAL   A N   1 
ATOM   261  C CA  . VAL   A 1 36  ? -9.80056  15.79117 -8.58222  1.000 43.99829  ? 36  VAL   A CA  1 
ATOM   262  C C   . VAL   A 1 36  ? -10.07704 16.70052 -9.77148  1.000 42.96298  ? 36  VAL   A C   1 
ATOM   263  O O   . VAL   A 1 36  ? -10.74644 17.73156 -9.63194  1.000 38.81472  ? 36  VAL   A O   1 
ATOM   264  C CB  . VAL   A 1 36  ? -11.03457 14.93946 -8.23683  1.000 45.90184  ? 36  VAL   A CB  1 
ATOM   265  C CG1 . VAL   A 1 36  ? -11.45390 14.10130 -9.43447  1.000 43.52004  ? 36  VAL   A CG1 1 
ATOM   266  C CG2 . VAL   A 1 36  ? -10.74293 14.04847 -7.03947  1.000 44.37091  ? 36  VAL   A CG2 1 
ATOM   267  N N   . TYR   A 1 37  ? -9.55727  16.32064 -10.93558 1.000 45.01013  ? 37  TYR   A N   1 
ATOM   268  C CA  . TYR   A 1 37  ? -9.72437  17.07293 -12.17030 1.000 44.13966  ? 37  TYR   A CA  1 
ATOM   269  C C   . TYR   A 1 37  ? -10.58145 16.27009 -13.13844 1.000 45.93364  ? 37  TYR   A C   1 
ATOM   270  O O   . TYR   A 1 37  ? -10.39446 15.05907 -13.28263 1.000 47.31869  ? 37  TYR   A O   1 
ATOM   271  C CB  . TYR   A 1 37  ? -8.37159  17.38749 -12.82099 1.000 47.04874  ? 37  TYR   A CB  1 
ATOM   272  C CG  . TYR   A 1 37  ? -7.37065  18.07783 -11.91694 1.000 44.96261  ? 37  TYR   A CG  1 
ATOM   273  C CD1 . TYR   A 1 37  ? -6.73786  17.39026 -10.88731 1.000 44.10141  ? 37  TYR   A CD1 1 
ATOM   274  C CD2 . TYR   A 1 37  ? -7.05510  19.41756 -12.09820 1.000 46.46254  ? 37  TYR   A CD2 1 
ATOM   275  C CE1 . TYR   A 1 37  ? -5.82440  18.01789 -10.06405 1.000 48.35088  ? 37  TYR   A CE1 1 
ATOM   276  C CE2 . TYR   A 1 37  ? -6.14197  20.05411 -11.27915 1.000 47.47056  ? 37  TYR   A CE2 1 
ATOM   277  C CZ  . TYR   A 1 37  ? -5.53035  19.34974 -10.26443 1.000 48.24796  ? 37  TYR   A CZ  1 
ATOM   278  O OH  . TYR   A 1 37  ? -4.62144  19.98019 -9.44743  1.000 49.85830  ? 37  TYR   A OH  1 
ATOM   279  N N   . CYS   A 1 38  ? -11.51521 16.94536 -13.80318 1.000 48.90289  ? 38  CYS   A N   1 
ATOM   280  C CA  . CYS   A 1 38  ? -12.41988 16.29342 -14.74080 1.000 46.80355  ? 38  CYS   A CA  1 
ATOM   281  C C   . CYS   A 1 38  ? -12.96437 17.34777 -15.69577 1.000 46.89896  ? 38  CYS   A C   1 
ATOM   282  O O   . CYS   A 1 38  ? -12.95921 18.54153 -15.37208 1.000 46.78853  ? 38  CYS   A O   1 
ATOM   283  C CB  . CYS   A 1 38  ? -13.56631 15.57956 -14.00455 1.000 42.89164  ? 38  CYS   A CB  1 
ATOM   284  S SG  . CYS   A 1 38  ? -14.82727 16.68178 -13.32722 1.000 50.03172  ? 38  CYS   A SG  1 
ATOM   285  N N   . PRO   A 1 39  ? -13.42318 16.94241 -16.88336 1.000 43.82809  ? 39  PRO   A N   1 
ATOM   286  C CA  . PRO   A 1 39  ? -14.04208 17.91045 -17.79895 1.000 44.97527  ? 39  PRO   A CA  1 
ATOM   287  C C   . PRO   A 1 39  ? -15.27028 18.54919 -17.16996 1.000 46.04192  ? 39  PRO   A C   1 
ATOM   288  O O   . PRO   A 1 39  ? -16.03423 17.89907 -16.45372 1.000 43.99481  ? 39  PRO   A O   1 
ATOM   289  C CB  . PRO   A 1 39  ? -14.41090 17.06221 -19.02228 1.000 44.38885  ? 39  PRO   A CB  1 
ATOM   290  C CG  . PRO   A 1 39  ? -13.53677 15.86033 -18.93814 1.000 46.00306  ? 39  PRO   A CG  1 
ATOM   291  C CD  . PRO   A 1 39  ? -13.33183 15.59910 -17.47914 1.000 46.17514  ? 39  PRO   A CD  1 
ATOM   292  N N   . ARG   A 1 40  ? -15.45722 19.84075 -17.44927 1.000 43.67046  ? 40  ARG   A N   1 
ATOM   293  C CA  . ARG   A 1 40  ? -16.51555 20.59141 -16.78577 1.000 46.10405  ? 40  ARG   A CA  1 
ATOM   294  C C   . ARG   A 1 40  ? -17.90673 20.22376 -17.28541 1.000 45.92296  ? 40  ARG   A C   1 
ATOM   295  O O   . ARG   A 1 40  ? -18.89128 20.54344 -16.61166 1.000 49.46348  ? 40  ARG   A O   1 
ATOM   296  C CB  . ARG   A 1 40  ? -16.28460 22.09269 -16.95258 1.000 46.94509  ? 40  ARG   A CB  1 
ATOM   297  C CG  . ARG   A 1 40  ? -16.51426 22.60656 -18.35683 1.000 46.49034  ? 40  ARG   A CG  1 
ATOM   298  C CD  . ARG   A 1 40  ? -16.20914 24.08923 -18.43986 1.000 44.51903  ? 40  ARG   A CD  1 
ATOM   299  N NE  . ARG   A 1 40  ? -16.02848 24.52789 -19.81741 1.000 44.31875  ? 40  ARG   A NE  1 
ATOM   300  C CZ  . ARG   A 1 40  ? -16.08410 25.79139 -20.21398 1.000 46.69680  ? 40  ARG   A CZ  1 
ATOM   301  N NH1 . ARG   A 1 40  ? -16.31754 26.77410 -19.35967 1.000 50.05978  ? 40  ARG   A NH1 1 
ATOM   302  N NH2 . ARG   A 1 40  ? -15.90904 26.07518 -21.50124 1.000 43.79548  ? 40  ARG   A NH2 1 
ATOM   303  N N   . HIS   A 1 41  ? -18.02179 19.55698 -18.43370 1.000 48.82622  ? 41  HIS   A N   1 
ATOM   304  C CA  . HIS   A 1 41  ? -19.33493 19.13727 -18.91060 1.000 50.38698  ? 41  HIS   A CA  1 
ATOM   305  C C   . HIS   A 1 41  ? -19.87835 17.92888 -18.15131 1.000 51.14115  ? 41  HIS   A C   1 
ATOM   306  O O   . HIS   A 1 41  ? -20.87337 17.33591 -18.58199 1.000 49.85011  ? 41  HIS   A O   1 
ATOM   307  C CB  . HIS   A 1 41  ? -19.29624 18.86249 -20.41917 1.000 48.05074  ? 41  HIS   A CB  1 
ATOM   308  C CG  . HIS   A 1 41  ? -18.56897 17.61112 -20.79899 1.000 49.06230  ? 41  HIS   A CG  1 
ATOM   309  N ND1 . HIS   A 1 41  ? -19.13905 16.35989 -20.70635 1.000 47.80056  ? 41  HIS   A ND1 1 
ATOM   310  C CD2 . HIS   A 1 41  ? -17.32194 17.42094 -21.29087 1.000 49.72768  ? 41  HIS   A CD2 1 
ATOM   311  C CE1 . HIS   A 1 41  ? -18.27139 15.45191 -21.11637 1.000 48.35375  ? 41  HIS   A CE1 1 
ATOM   312  N NE2 . HIS   A 1 41  ? -17.16096 16.06952 -21.47654 1.000 46.47469  ? 41  HIS   A NE2 1 
ATOM   313  N N   . VAL   A 1 42  ? -19.24528 17.56218 -17.03341 1.000 50.24491  ? 42  VAL   A N   1 
ATOM   314  C CA  . VAL   A 1 42  ? -19.83995 16.62181 -16.08834 1.000 49.19754  ? 42  VAL   A CA  1 
ATOM   315  C C   . VAL   A 1 42  ? -21.17711 17.13716 -15.57267 1.000 51.78587  ? 42  VAL   A C   1 
ATOM   316  O O   . VAL   A 1 42  ? -22.08607 16.34924 -15.27800 1.000 55.47259  ? 42  VAL   A O   1 
ATOM   317  C CB  . VAL   A 1 42  ? -18.84968 16.35288 -14.93520 1.000 47.28794  ? 42  VAL   A CB  1 
ATOM   318  C CG1 . VAL   A 1 42  ? -18.45788 17.65389 -14.25158 1.000 48.50126  ? 42  VAL   A CG1 1 
ATOM   319  C CG2 . VAL   A 1 42  ? -19.45483 15.39592 -13.92215 1.000 48.82878  ? 42  VAL   A CG2 1 
ATOM   320  N N   . ILE   A 1 43  ? -21.32672 18.46244 -15.46919 1.000 51.59199  ? 43  ILE   A N   1 
ATOM   321  C CA  . ILE   A 1 43  ? -22.50694 19.06394 -14.85967 1.000 55.12213  ? 43  ILE   A CA  1 
ATOM   322  C C   . ILE   A 1 43  ? -23.63945 19.29404 -15.85100 1.000 56.60834  ? 43  ILE   A C   1 
ATOM   323  O O   . ILE   A 1 43  ? -24.69992 19.80024 -15.45794 1.000 60.05193  ? 43  ILE   A O   1 
ATOM   324  C CB  . ILE   A 1 43  ? -22.12147 20.39269 -14.17991 1.000 56.45558  ? 43  ILE   A CB  1 
ATOM   325  C CG1 . ILE   A 1 43  ? -21.80652 21.45687 -15.23353 1.000 53.20546  ? 43  ILE   A CG1 1 
ATOM   326  C CG2 . ILE   A 1 43  ? -20.92921 20.18874 -13.25859 1.000 51.90921  ? 43  ILE   A CG2 1 
ATOM   327  C CD1 . ILE   A 1 43  ? -21.19130 22.71560 -14.66397 1.000 53.72337  ? 43  ILE   A CD1 1 
ATOM   328  N N   . CYS   A 1 44  ? -23.45591 18.94006 -17.11829 1.000 56.82610  ? 44  CYS   A N   1 
ATOM   329  C CA  . CYS   A 1 44  ? -24.48491 19.14539 -18.12494 1.000 57.22006  ? 44  CYS   A CA  1 
ATOM   330  C C   . CYS   A 1 44  ? -25.45032 17.97095 -18.16207 1.000 58.53685  ? 44  CYS   A C   1 
ATOM   331  O O   . CYS   A 1 44  ? -25.09903 16.83752 -17.82388 1.000 59.60594  ? 44  CYS   A O   1 
ATOM   332  C CB  . CYS   A 1 44  ? -23.86784 19.32765 -19.51263 1.000 57.89503  ? 44  CYS   A CB  1 
ATOM   333  S SG  . CYS   A 1 44  ? -22.68322 20.67358 -19.65001 1.000 57.33290  ? 44  CYS   A SG  1 
ATOM   334  N N   . THR   A 1 45  ? -26.67938 18.25801 -18.57688 1.000 56.72589  ? 45  THR   A N   1 
ATOM   335  C CA  . THR   A 1 45  ? -27.59853 17.21016 -18.97911 1.000 58.76992  ? 45  THR   A CA  1 
ATOM   336  C C   . THR   A 1 45  ? -27.30526 16.82669 -20.42618 1.000 61.19475  ? 45  THR   A C   1 
ATOM   337  O O   . THR   A 1 45  ? -26.36824 17.33014 -21.05262 1.000 59.79888  ? 45  THR   A O   1 
ATOM   338  C CB  . THR   A 1 45  ? -29.04583 17.67022 -18.81785 1.000 58.28237  ? 45  THR   A CB  1 
ATOM   339  O OG1 . THR   A 1 45  ? -29.20285 18.97156 -19.39894 1.000 57.56748  ? 45  THR   A OG1 1 
ATOM   340  C CG2 . THR   A 1 45  ? -29.42579 17.72933 -17.34735 1.000 55.62392  ? 45  THR   A CG2 1 
ATOM   341  N N   . SER   A 1 46  ? -28.11425 15.92036 -20.97307 1.000 60.93052  ? 46  SER   A N   1 
ATOM   342  C CA  . SER   A 1 46  ? -28.01912 15.64136 -22.40049 1.000 62.18671  ? 46  SER   A CA  1 
ATOM   343  C C   . SER   A 1 46  ? -28.44414 16.85429 -23.21755 1.000 65.46421  ? 46  SER   A C   1 
ATOM   344  O O   . SER   A 1 46  ? -27.89878 17.10927 -24.29789 1.000 65.97963  ? 46  SER   A O   1 
ATOM   345  C CB  . SER   A 1 46  ? -28.87278 14.42523 -22.75726 1.000 64.72448  ? 46  SER   A CB  1 
ATOM   346  O OG  . SER   A 1 46  ? -28.32657 13.72561 -23.86126 1.000 67.40645  ? 46  SER   A OG  1 
ATOM   347  N N   . GLU   A 1 47  ? -29.40361 17.62733 -22.70260 1.000 64.63029  ? 47  GLU   A N   1 
ATOM   348  C CA  . GLU   A 1 47  ? -29.97159 18.74815 -23.44085 1.000 62.16855  ? 47  GLU   A CA  1 
ATOM   349  C C   . GLU   A 1 47  ? -29.18620 20.04258 -23.27541 1.000 63.66933  ? 47  GLU   A C   1 
ATOM   350  O O   . GLU   A 1 47  ? -29.39901 20.97975 -24.05186 1.000 68.18034  ? 47  GLU   A O   1 
ATOM   351  C CB  . GLU   A 1 47  ? -31.41714 18.98609 -23.00376 1.000 62.64415  ? 47  GLU   A CB  1 
ATOM   352  C CG  . GLU   A 1 47  ? -32.31039 19.53924 -24.09852 1.000 66.96623  ? 47  GLU   A CG  1 
ATOM   353  C CD  . GLU   A 1 47  ? -33.77244 19.53100 -23.70943 1.000 75.95215  ? 47  GLU   A CD  1 
ATOM   354  O OE1 . GLU   A 1 47  ? -34.10550 18.92716 -22.66844 1.000 78.70349  ? 47  GLU   A OE1 1 
ATOM   355  O OE2 . GLU   A 1 47  ? -34.58701 20.13440 -24.43878 1.000 76.70922  ? 47  GLU   A OE2 1 
ATOM   356  N N   . ASP   A 1 48  ? -28.30602 20.13337 -22.27878 1.000 64.60946  ? 48  ASP   A N   1 
ATOM   357  C CA  . ASP   A 1 48  ? -27.51583 21.34587 -22.10784 1.000 63.30855  ? 48  ASP   A CA  1 
ATOM   358  C C   . ASP   A 1 48  ? -26.26865 21.35806 -22.97851 1.000 60.20671  ? 48  ASP   A C   1 
ATOM   359  O O   . ASP   A 1 48  ? -25.73598 22.43585 -23.25859 1.000 55.97171  ? 48  ASP   A O   1 
ATOM   360  C CB  . ASP   A 1 48  ? -27.11443 21.52027 -20.64065 1.000 62.17065  ? 48  ASP   A CB  1 
ATOM   361  C CG  . ASP   A 1 48  ? -28.18895 22.20308 -19.82045 1.000 65.69026  ? 48  ASP   A CG  1 
ATOM   362  O OD1 . ASP   A 1 48  ? -28.87548 23.09108 -20.36808 1.000 71.73785  ? 48  ASP   A OD1 1 
ATOM   363  O OD2 . ASP   A 1 48  ? -28.34106 21.85943 -18.62884 1.000 64.12254  ? 48  ASP   A OD2 1 
ATOM   364  N N   . MET   A 1 49  ? -25.81035 20.19086 -23.43133 1.000 62.30806  ? 49  MET   A N   1 
ATOM   365  C CA  . MET   A 1 49  ? -24.52817 20.07389 -24.11460 1.000 59.24077  ? 49  MET   A CA  1 
ATOM   366  C C   . MET   A 1 49  ? -24.51097 20.71193 -25.49879 1.000 56.17190  ? 49  MET   A C   1 
ATOM   367  O O   . MET   A 1 49  ? -23.42603 20.87964 -26.06437 1.000 52.66329  ? 49  MET   A O   1 
ATOM   368  C CB  . MET   A 1 49  ? -24.14386 18.59865 -24.22281 1.000 61.83293  ? 49  MET   A CB  1 
ATOM   369  C CG  . MET   A 1 49  ? -23.60794 18.00824 -22.92946 1.000 61.65889  ? 49  MET   A CG  1 
ATOM   370  S SD  . MET   A 1 49  ? -23.61488 16.20565 -22.93593 1.000 64.36274  ? 49  MET   A SD  1 
ATOM   371  C CE  . MET   A 1 49  ? -23.04559 15.86353 -24.59904 1.000 58.73047  ? 49  MET   A CE  1 
ATOM   372  N N   . LEU   A 1 50  ? -25.66507 21.06987 -26.05995 1.000 55.63844  ? 50  LEU   A N   1 
ATOM   373  C CA  . LEU   A 1 50  ? -25.68863 21.66009 -27.39370 1.000 54.07262  ? 50  LEU   A CA  1 
ATOM   374  C C   . LEU   A 1 50  ? -25.33745 23.14418 -27.39709 1.000 55.22110  ? 50  LEU   A C   1 
ATOM   375  O O   . LEU   A 1 50  ? -24.89663 23.65790 -28.43194 1.000 58.03914  ? 50  LEU   A O   1 
ATOM   376  C CB  . LEU   A 1 50  ? -27.05621 21.43717 -28.05053 1.000 53.37959  ? 50  LEU   A CB  1 
ATOM   377  C CG  . LEU   A 1 50  ? -27.66897 20.02985 -28.05363 1.000 55.96535  ? 50  LEU   A CG  1 
ATOM   378  C CD1 . LEU   A 1 50  ? -28.34490 19.63509 -26.73422 1.000 60.57028  ? 50  LEU   A CD1 1 
ATOM   379  C CD2 . LEU   A 1 50  ? -28.63601 19.90300 -29.22667 1.000 55.87844  ? 50  LEU   A CD2 1 
ATOM   380  N N   . ASN   A 1 51  ? -25.52900 23.83870 -26.27801 1.000 55.73332  ? 51  ASN   A N   1 
ATOM   381  C CA  . ASN   A 1 51  ? -25.05802 25.20793 -26.09746 1.000 58.49651  ? 51  ASN   A CA  1 
ATOM   382  C C   . ASN   A 1 51  ? -25.05328 25.53819 -24.61063 1.000 57.43524  ? 51  ASN   A C   1 
ATOM   383  O O   . ASN   A 1 51  ? -25.91319 26.29149 -24.13587 1.000 55.23845  ? 51  ASN   A O   1 
ATOM   384  C CB  . ASN   A 1 51  ? -25.92526 26.20827 -26.86462 1.000 57.08123  ? 51  ASN   A CB  1 
ATOM   385  C CG  . ASN   A 1 51  ? -25.15963 27.46096 -27.25511 1.000 57.85090  ? 51  ASN   A CG  1 
ATOM   386  O OD1 . ASN   A 1 51  ? -23.94089 27.53499 -27.08959 1.000 57.59183  ? 51  ASN   A OD1 1 
ATOM   387  N ND2 . ASN   A 1 51  ? -25.87228 28.45205 -27.77702 1.000 54.82946  ? 51  ASN   A ND2 1 
ATOM   388  N N   . PRO   A 1 52  ? -24.10711 24.99976 -23.84873 1.000 55.89363  ? 52  PRO   A N   1 
ATOM   389  C CA  . PRO   A 1 52  ? -24.16531 25.13262 -22.39193 1.000 60.03219  ? 52  PRO   A CA  1 
ATOM   390  C C   . PRO   A 1 52  ? -23.58460 26.44290 -21.88921 1.000 57.41513  ? 52  PRO   A C   1 
ATOM   391  O O   . PRO   A 1 52  ? -22.71390 27.05489 -22.51230 1.000 56.80328  ? 52  PRO   A O   1 
ATOM   392  C CB  . PRO   A 1 52  ? -23.32525 23.94698 -21.90537 1.000 57.00044  ? 52  PRO   A CB  1 
ATOM   393  C CG  . PRO   A 1 52  ? -22.31689 23.75669 -22.98975 1.000 54.21823  ? 52  PRO   A CG  1 
ATOM   394  C CD  . PRO   A 1 52  ? -22.97511 24.16304 -24.28581 1.000 54.08542  ? 52  PRO   A CD  1 
ATOM   395  N N   . ASN   A 1 53  ? -24.08986 26.86360 -20.73409 1.000 53.61110  ? 53  ASN   A N   1 
ATOM   396  C CA  . ASN   A 1 53  ? -23.52259 27.95965 -19.95368 1.000 54.81168  ? 53  ASN   A CA  1 
ATOM   397  C C   . ASN   A 1 53  ? -22.94187 27.31544 -18.69721 1.000 54.98631  ? 53  ASN   A C   1 
ATOM   398  O O   . ASN   A 1 53  ? -23.64488 27.10094 -17.70802 1.000 56.79631  ? 53  ASN   A O   1 
ATOM   399  C CB  . ASN   A 1 53  ? -24.57200 29.02060 -19.62233 1.000 52.83627  ? 53  ASN   A CB  1 
ATOM   400  C CG  . ASN   A 1 53  ? -23.96626 30.27881 -19.02091 1.000 52.48521  ? 53  ASN   A CG  1 
ATOM   401  O OD1 . ASN   A 1 53  ? -22.96841 30.22503 -18.30210 1.000 51.80127  ? 53  ASN   A OD1 1 
ATOM   402  N ND2 . ASN   A 1 53  ? -24.57303 31.42184 -19.31511 1.000 53.30886  ? 53  ASN   A ND2 1 
ATOM   403  N N   . TYR   A 1 54  ? -21.64660 26.99776 -18.75015 1.000 55.00016  ? 54  TYR   A N   1 
ATOM   404  C CA  . TYR   A 1 54  ? -21.01876 26.26473 -17.65661 1.000 53.43813  ? 54  TYR   A CA  1 
ATOM   405  C C   . TYR   A 1 54  ? -20.98805 27.07957 -16.37001 1.000 56.56970  ? 54  TYR   A C   1 
ATOM   406  O O   . TYR   A 1 54  ? -21.06951 26.50854 -15.27664 1.000 57.49645  ? 54  TYR   A O   1 
ATOM   407  C CB  . TYR   A 1 54  ? -19.60817 25.84359 -18.06027 1.000 52.62348  ? 54  TYR   A CB  1 
ATOM   408  C CG  . TYR   A 1 54  ? -19.58162 24.79726 -19.15085 1.000 51.44329  ? 54  TYR   A CG  1 
ATOM   409  C CD1 . TYR   A 1 54  ? -19.89854 23.47418 -18.87905 1.000 51.39854  ? 54  TYR   A CD1 1 
ATOM   410  C CD2 . TYR   A 1 54  ? -19.25751 25.13695 -20.45634 1.000 49.59807  ? 54  TYR   A CD2 1 
ATOM   411  C CE1 . TYR   A 1 54  ? -19.87491 22.51653 -19.87406 1.000 52.14762  ? 54  TYR   A CE1 1 
ATOM   412  C CE2 . TYR   A 1 54  ? -19.23147 24.18631 -21.45747 1.000 50.81937  ? 54  TYR   A CE2 1 
ATOM   413  C CZ  . TYR   A 1 54  ? -19.54390 22.87739 -21.16181 1.000 51.63697  ? 54  TYR   A CZ  1 
ATOM   414  O OH  . TYR   A 1 54  ? -19.52307 21.92769 -22.15865 1.000 51.08919  ? 54  TYR   A OH  1 
ATOM   415  N N   . GLU   A 1 55  ? -20.87327 28.40498 -16.47430 1.000 56.04841  ? 55  GLU   A N   1 
ATOM   416  C CA  . GLU   A 1 55  ? -20.91369 29.24425 -15.28133 1.000 55.42327  ? 55  GLU   A CA  1 
ATOM   417  C C   . GLU   A 1 55  ? -22.28578 29.17903 -14.62311 1.000 55.44973  ? 55  GLU   A C   1 
ATOM   418  O O   . GLU   A 1 55  ? -22.39727 29.03417 -13.40009 1.000 55.98037  ? 55  GLU   A O   1 
ATOM   419  C CB  . GLU   A 1 55  ? -20.55076 30.68524 -15.64381 1.000 56.00754  ? 55  GLU   A CB  1 
ATOM   420  C CG  . GLU   A 1 55  ? -19.08671 30.89100 -16.01176 1.000 56.19111  ? 55  GLU   A CG  1 
ATOM   421  C CD  . GLU   A 1 55  ? -18.78967 30.54672 -17.46096 1.000 57.48133  ? 55  GLU   A CD  1 
ATOM   422  O OE1 . GLU   A 1 55  ? -19.74702 30.31178 -18.22849 1.000 56.48591  ? 55  GLU   A OE1 1 
ATOM   423  O OE2 . GLU   A 1 55  ? -17.59763 30.51140 -17.83262 1.000 54.76363  ? 55  GLU   A OE2 1 
ATOM   424  N N   . ASP   A 1 56  ? -23.34491 29.27632 -15.42952 1.000 56.44650  ? 56  ASP   A N   1 
ATOM   425  C CA  . ASP   A 1 56  ? -24.70292 29.15239 -14.91044 1.000 59.01393  ? 56  ASP   A CA  1 
ATOM   426  C C   . ASP   A 1 56  ? -24.90496 27.77848 -14.27904 1.000 57.90653  ? 56  ASP   A C   1 
ATOM   427  O O   . ASP   A 1 56  ? -25.38176 27.66596 -13.14357 1.000 58.57553  ? 56  ASP   A O   1 
ATOM   428  C CB  . ASP   A 1 56  ? -25.69840 29.40223 -16.05270 1.000 61.40097  ? 56  ASP   A CB  1 
ATOM   429  C CG  . ASP   A 1 56  ? -27.16003 29.13916 -15.67219 1.000 68.85877  ? 56  ASP   A CG  1 
ATOM   430  O OD1 . ASP   A 1 56  ? -27.46769 28.74098 -14.53153 1.000 74.59167  ? 56  ASP   A OD1 1 
ATOM   431  O OD2 . ASP   A 1 56  ? -28.02629 29.33992 -16.55009 1.000 69.92027  ? 56  ASP   A OD2 1 
ATOM   432  N N   . LEU   A 1 57  ? -24.52161 26.71984 -14.99743 1.000 56.66247  ? 57  LEU   A N   1 
ATOM   433  C CA  . LEU   A 1 57  ? -24.72008 25.36433 -14.49375 1.000 57.75142  ? 57  LEU   A CA  1 
ATOM   434  C C   . LEU   A 1 57  ? -23.97849 25.14005 -13.18084 1.000 58.55374  ? 57  LEU   A C   1 
ATOM   435  O O   . LEU   A 1 57  ? -24.48733 24.46043 -12.28244 1.000 59.48382  ? 57  LEU   A O   1 
ATOM   436  C CB  . LEU   A 1 57  ? -24.26997 24.34862 -15.54382 1.000 54.50547  ? 57  LEU   A CB  1 
ATOM   437  C CG  . LEU   A 1 57  ? -25.20905 24.08557 -16.72227 1.000 54.56441  ? 57  LEU   A CG  1 
ATOM   438  C CD1 . LEU   A 1 57  ? -24.68279 22.94098 -17.57186 1.000 53.26402  ? 57  LEU   A CD1 1 
ATOM   439  C CD2 . LEU   A 1 57  ? -26.61889 23.78965 -16.23988 1.000 53.04031  ? 57  LEU   A CD2 1 
ATOM   440  N N   . LEU   A 1 58  ? -22.78160 25.71616 -13.04312 1.000 58.14882  ? 58  LEU   A N   1 
ATOM   441  C CA  . LEU   A 1 58  ? -21.97033 25.45240 -11.85881 1.000 57.25170  ? 58  LEU   A CA  1 
ATOM   442  C C   . LEU   A 1 58  ? -22.51942 26.15936 -10.62221 1.000 55.47651  ? 58  LEU   A C   1 
ATOM   443  O O   . LEU   A 1 58  ? -22.25635 25.72231 -9.49560  1.000 52.70718  ? 58  LEU   A O   1 
ATOM   444  C CB  . LEU   A 1 58  ? -20.51998 25.86361 -12.12265 1.000 53.50274  ? 58  LEU   A CB  1 
ATOM   445  C CG  . LEU   A 1 58  ? -19.48817 25.59282 -11.02523 1.000 49.47941  ? 58  LEU   A CG  1 
ATOM   446  C CD1 . LEU   A 1 58  ? -19.46797 24.11568 -10.66481 1.000 49.96631  ? 58  LEU   A CD1 1 
ATOM   447  C CD2 . LEU   A 1 58  ? -18.10579 26.05277 -11.46308 1.000 52.07389  ? 58  LEU   A CD2 1 
ATOM   448  N N   . ILE   A 1 59  ? -23.28272 27.24139 -10.80810 1.000 56.78479  ? 59  ILE   A N   1 
ATOM   449  C CA  . ILE   A 1 59  ? -23.87850 27.95435 -9.67522  1.000 56.84016  ? 59  ILE   A CA  1 
ATOM   450  C C   . ILE   A 1 59  ? -24.74628 27.01068 -8.85387  1.000 58.51797  ? 59  ILE   A C   1 
ATOM   451  O O   . ILE   A 1 59  ? -24.52149 26.80171 -7.65592  1.000 61.17448  ? 59  ILE   A O   1 
ATOM   452  C CB  . ILE   A 1 59  ? -24.70327 29.15736 -10.16361 1.000 60.16159  ? 59  ILE   A CB  1 
ATOM   453  C CG1 . ILE   A 1 59  ? -23.80069 30.27589 -10.67678 1.000 56.37205  ? 59  ILE   A CG1 1 
ATOM   454  C CG2 . ILE   A 1 59  ? -25.60894 29.67030 -9.04584  1.000 61.70576  ? 59  ILE   A CG2 1 
ATOM   455  C CD1 . ILE   A 1 59  ? -24.49752 31.62175 -10.73102 1.000 61.32711  ? 59  ILE   A CD1 1 
ATOM   456  N N   . ARG   A 1 60  ? -25.75756 26.42990 -9.49565  1.000 56.13083  ? 60  ARG   A N   1 
ATOM   457  C CA  . ARG   A 1 60  ? -26.77004 25.55646 -8.90539  1.000 61.29618  ? 60  ARG   A CA  1 
ATOM   458  C C   . ARG   A 1 60  ? -26.19985 24.26339 -8.35431  1.000 60.91850  ? 60  ARG   A C   1 
ATOM   459  O O   . ARG   A 1 60  ? -27.00515 23.39412 -7.99334  1.000 64.42817  ? 60  ARG   A O   1 
ATOM   460  C CB  . ARG   A 1 60  ? -27.84127 25.25006 -9.95089  1.000 65.52832  ? 60  ARG   A CB  1 
ATOM   461  C CG  . ARG   A 1 60  ? -28.28007 26.46993 -10.75313 1.000 68.32583  ? 60  ARG   A CG  1 
ATOM   462  C CD  . ARG   A 1 60  ? -29.12790 26.07618 -11.94674 1.000 71.25876  ? 60  ARG   A CD  1 
ATOM   463  N NE  . ARG   A 1 60  ? -29.13742 27.11017 -12.97383 1.000 69.73668  ? 60  ARG   A NE  1 
ATOM   464  C CZ  . ARG   A 1 60  ? -30.21319 27.46786 -13.66046 1.000 76.53997  ? 60  ARG   A CZ  1 
ATOM   465  N NH1 . ARG   A 1 60  ? -31.39529 26.92239 -13.42476 1.000 84.18580  ? 60  ARG   A NH1 1 
ATOM   466  N NH2 . ARG   A 1 60  ? -30.09993 28.39318 -14.60920 1.000 74.99400  ? 60  ARG   A NH2 1 
ATOM   467  N N   . LYS   A 1 61  ? -24.88242 24.09903 -8.25956  1.000 60.85689  ? 61  LYS   A N   1 
ATOM   468  C CA  . LYS   A 1 61  ? -24.27104 22.89277 -7.72208  1.000 59.16048  ? 61  LYS   A CA  1 
ATOM   469  C C   . LYS   A 1 61  ? -23.58041 23.21360 -6.40548  1.000 59.55340  ? 61  LYS   A C   1 
ATOM   470  O O   . LYS   A 1 61  ? -22.78948 24.15991 -6.32829  1.000 59.08968  ? 61  LYS   A O   1 
ATOM   471  C CB  . LYS   A 1 61  ? -23.26032 22.30339 -8.70717  1.000 59.73365  ? 61  LYS   A CB  1 
ATOM   472  C CG  . LYS   A 1 61  ? -23.74137 22.25518 -10.14230 1.000 57.99118  ? 61  LYS   A CG  1 
ATOM   473  C CD  . LYS   A 1 61  ? -24.70530 21.10484 -10.35901 1.000 60.15632  ? 61  LYS   A CD  1 
ATOM   474  C CE  . LYS   A 1 61  ? -24.98168 20.88820 -11.83689 1.000 58.84081  ? 61  LYS   A CE  1 
ATOM   475  N NZ  . LYS   A 1 61  ? -26.11053 21.73161 -12.32220 1.000 57.23793  ? 61  LYS   A NZ  1 
ATOM   476  N N   . SER   A 1 62  ? -23.88197 22.42997 -5.37827  1.000 62.75066  ? 62  SER   A N   1 
ATOM   477  C CA  . SER   A 1 62  ? -23.12941 22.45384 -4.13531  1.000 59.47334  ? 62  SER   A CA  1 
ATOM   478  C C   . SER   A 1 62  ? -22.10538 21.32422 -4.14459  1.000 56.33336  ? 62  SER   A C   1 
ATOM   479  O O   . SER   A 1 62  ? -22.03714 20.52156 -5.07839  1.000 55.76588  ? 62  SER   A O   1 
ATOM   480  C CB  . SER   A 1 62  ? -24.06567 22.33583 -2.92801  1.000 60.02023  ? 62  SER   A CB  1 
ATOM   481  O OG  . SER   A 1 62  ? -24.33192 20.98026 -2.61417  1.000 62.87524  ? 62  SER   A OG  1 
ATOM   482  N N   . ASN   A 1 63  ? -21.29801 21.26977 -3.08305  1.000 58.48614  ? 63  ASN   A N   1 
ATOM   483  C CA  . ASN   A 1 63  ? -20.25421 20.25243 -3.00636  1.000 54.83120  ? 63  ASN   A CA  1 
ATOM   484  C C   . ASN   A 1 63  ? -20.83469 18.84427 -3.03412  1.000 56.22067  ? 63  ASN   A C   1 
ATOM   485  O O   . ASN   A 1 63  ? -20.16544 17.90558 -3.48113  1.000 55.08967  ? 63  ASN   A O   1 
ATOM   486  C CB  . ASN   A 1 63  ? -19.41875 20.45581 -1.74264  1.000 54.94519  ? 63  ASN   A CB  1 
ATOM   487  C CG  . ASN   A 1 63  ? -18.48654 21.64535 -1.84646  1.000 55.05269  ? 63  ASN   A CG  1 
ATOM   488  O OD1 . ASN   A 1 63  ? -18.19293 22.12526 -2.94123  1.000 53.12076  ? 63  ASN   A OD1 1 
ATOM   489  N ND2 . ASN   A 1 63  ? -18.02432 22.13580 -0.70248  1.000 56.32398  ? 63  ASN   A ND2 1 
ATOM   490  N N   . HIS   A 1 64  ? -22.07889 18.67967 -2.58219  1.000 57.14023  ? 64  HIS   A N   1 
ATOM   491  C CA  . HIS   A 1 64  ? -22.66922 17.35402 -2.45205  1.000 56.66693  ? 64  HIS   A CA  1 
ATOM   492  C C   . HIS   A 1 64  ? -23.25263 16.82743 -3.75622  1.000 53.92744  ? 64  HIS   A C   1 
ATOM   493  O O   . HIS   A 1 64  ? -23.50653 15.62241 -3.85905  1.000 56.64958  ? 64  HIS   A O   1 
ATOM   494  C CB  . HIS   A 1 64  ? -23.75655 17.36684 -1.37584  1.000 59.46067  ? 64  HIS   A CB  1 
ATOM   495  C CG  . HIS   A 1 64  ? -23.34264 18.04194 -0.10463  1.000 64.86551  ? 64  HIS   A CG  1 
ATOM   496  N ND1 . HIS   A 1 64  ? -23.18143 19.40746 -0.00373  1.000 62.49831  ? 64  HIS   A ND1 1 
ATOM   497  C CD2 . HIS   A 1 64  ? -23.05572 17.53842 1.11910   1.000 62.11439  ? 64  HIS   A CD2 1 
ATOM   498  C CE1 . HIS   A 1 64  ? -22.81227 19.71568 1.22663   1.000 61.05228  ? 64  HIS   A CE1 1 
ATOM   499  N NE2 . HIS   A 1 64  ? -22.72923 18.59970 1.92827   1.000 61.78476  ? 64  HIS   A NE2 1 
ATOM   500  N N   . ASN   A 1 65  ? -23.47261 17.69155 -4.74957  1.000 54.63316  ? 65  ASN   A N   1 
ATOM   501  C CA  . ASN   A 1 65  ? -23.99216 17.23574 -6.03365  1.000 53.81889  ? 65  ASN   A CA  1 
ATOM   502  C C   . ASN   A 1 65  ? -22.98469 16.40595 -6.81795  1.000 54.64360  ? 65  ASN   A C   1 
ATOM   503  O O   . ASN   A 1 65  ? -23.35584 15.82040 -7.84104  1.000 56.55677  ? 65  ASN   A O   1 
ATOM   504  C CB  . ASN   A 1 65  ? -24.43693 18.43034 -6.88048  1.000 56.74777  ? 65  ASN   A CB  1 
ATOM   505  C CG  . ASN   A 1 65  ? -25.71869 19.06115 -6.37396  1.000 57.95128  ? 65  ASN   A CG  1 
ATOM   506  O OD1 . ASN   A 1 65  ? -25.82156 20.28249 -6.26862  1.000 58.46945  ? 65  ASN   A OD1 1 
ATOM   507  N ND2 . ASN   A 1 65  ? -26.70580 18.22903 -6.05914  1.000 55.93540  ? 65  ASN   A ND2 1 
ATOM   508  N N   . PHE   A 1 66  ? -21.73483 16.33770 -6.36882  1.000 55.11577  ? 66  PHE   A N   1 
ATOM   509  C CA  . PHE   A 1 66  ? -20.68212 15.60438 -7.05681  1.000 52.29066  ? 66  PHE   A CA  1 
ATOM   510  C C   . PHE   A 1 66  ? -20.38615 14.31267 -6.30871  1.000 49.55195  ? 66  PHE   A C   1 
ATOM   511  O O   . PHE   A 1 66  ? -20.16924 14.32893 -5.09212  1.000 49.54620  ? 66  PHE   A O   1 
ATOM   512  C CB  . PHE   A 1 66  ? -19.41825 16.45657 -7.17420  1.000 51.37653  ? 66  PHE   A CB  1 
ATOM   513  C CG  . PHE   A 1 66  ? -19.61946 17.72231 -7.94971  1.000 50.24364  ? 66  PHE   A CG  1 
ATOM   514  C CD1 . PHE   A 1 66  ? -19.77883 17.68659 -9.32402  1.000 49.61014  ? 66  PHE   A CD1 1 
ATOM   515  C CD2 . PHE   A 1 66  ? -19.66847 18.94620 -7.30430  1.000 51.67941  ? 66  PHE   A CD2 1 
ATOM   516  C CE1 . PHE   A 1 66  ? -19.97119 18.84836 -10.04338 1.000 50.81053  ? 66  PHE   A CE1 1 
ATOM   517  C CE2 . PHE   A 1 66  ? -19.86145 20.11379 -8.01834  1.000 52.19338  ? 66  PHE   A CE2 1 
ATOM   518  C CZ  . PHE   A 1 66  ? -20.01294 20.06415 -9.39046  1.000 53.01578  ? 66  PHE   A CZ  1 
ATOM   519  N N   . LEU   A 1 67  ? -20.37536 13.20138 -7.03874  1.000 50.56291  ? 67  LEU   A N   1 
ATOM   520  C CA  . LEU   A 1 67  ? -20.16745 11.87140 -6.47138  1.000 51.88567  ? 67  LEU   A CA  1 
ATOM   521  C C   . LEU   A 1 67  ? -18.84967 11.31961 -7.00895  1.000 51.15809  ? 67  LEU   A C   1 
ATOM   522  O O   . LEU   A 1 67  ? -18.79905 10.77215 -8.11432  1.000 50.61207  ? 67  LEU   A O   1 
ATOM   523  C CB  . LEU   A 1 67  ? -21.34085 10.95341 -6.80770  1.000 52.20082  ? 67  LEU   A CB  1 
ATOM   524  C CG  . LEU   A 1 67  ? -21.32094 9.53699  -6.22599  1.000 59.27296  ? 67  LEU   A CG  1 
ATOM   525  C CD1 . LEU   A 1 67  ? -21.20076 9.56724  -4.70784  1.000 56.55485  ? 67  LEU   A CD1 1 
ATOM   526  C CD2 . LEU   A 1 67  ? -22.55809 8.75950  -6.65937  1.000 54.86282  ? 67  LEU   A CD2 1 
ATOM   527  N N   . VAL   A 1 68  ? -17.78508 11.46648 -6.22407  1.000 49.85568  ? 68  VAL   A N   1 
ATOM   528  C CA  . VAL   A 1 68  ? -16.46943 10.93792 -6.56630  1.000 47.92058  ? 68  VAL   A CA  1 
ATOM   529  C C   . VAL   A 1 68  ? -16.28110 9.61034  -5.84682  1.000 48.68321  ? 68  VAL   A C   1 
ATOM   530  O O   . VAL   A 1 68  ? -16.49654 9.51735  -4.63123  1.000 48.41014  ? 68  VAL   A O   1 
ATOM   531  C CB  . VAL   A 1 68  ? -15.35344 11.92943 -6.19650  1.000 48.17386  ? 68  VAL   A CB  1 
ATOM   532  C CG1 . VAL   A 1 68  ? -14.02476 11.47449 -6.78657  1.000 42.94598  ? 68  VAL   A CG1 1 
ATOM   533  C CG2 . VAL   A 1 68  ? -15.70776 13.32861 -6.67554  1.000 46.51656  ? 68  VAL   A CG2 1 
ATOM   534  N N   . GLN   A 1 69  ? -15.87823 8.58294  -6.59396  1.000 49.57137  ? 69  GLN   A N   1 
ATOM   535  C CA  . GLN   A 1 69  ? -15.72202 7.23736  -6.05162  1.000 51.89923  ? 69  GLN   A CA  1 
ATOM   536  C C   . GLN   A 1 69  ? -14.41638 6.64087  -6.55067  1.000 49.67858  ? 69  GLN   A C   1 
ATOM   537  O O   . GLN   A 1 69  ? -14.19560 6.55098  -7.76217  1.000 46.56952  ? 69  GLN   A O   1 
ATOM   538  C CB  . GLN   A 1 69  ? -16.90018 6.34263  -6.44733  1.000 51.96855  ? 69  GLN   A CB  1 
ATOM   539  C CG  . GLN   A 1 69  ? -18.21362 6.73650  -5.80136  1.000 55.10625  ? 69  GLN   A CG  1 
ATOM   540  C CD  . GLN   A 1 69  ? -19.41241 6.28460  -6.60548  1.000 56.95249  ? 69  GLN   A CD  1 
ATOM   541  O OE1 . GLN   A 1 69  ? -19.56415 6.64937  -7.77166  1.000 54.04504  ? 69  GLN   A OE1 1 
ATOM   542  N NE2 . GLN   A 1 69  ? -20.27531 5.48799  -5.98538  1.000 58.03323  ? 69  GLN   A NE2 1 
ATOM   543  N N   . ALA   A 1 70  ? -13.55974 6.23280  -5.61838  1.000 50.93981  ? 70  ALA   A N   1 
ATOM   544  C CA  . ALA   A 1 70  ? -12.32771 5.51362  -5.92216  1.000 51.18523  ? 70  ALA   A CA  1 
ATOM   545  C C   . ALA   A 1 70  ? -12.50063 4.08206  -5.43133  1.000 57.68470  ? 70  ALA   A C   1 
ATOM   546  O O   . ALA   A 1 70  ? -12.42885 3.82061  -4.22583  1.000 59.07766  ? 70  ALA   A O   1 
ATOM   547  C CB  . ALA   A 1 70  ? -11.12153 6.18273  -5.26808  1.000 47.09384  ? 70  ALA   A CB  1 
ATOM   548  N N   . GLY   A 1 71  ? -12.73138 3.15908  -6.36155  1.000 57.26689  ? 71  GLY   A N   1 
ATOM   549  C CA  . GLY   A 1 71  ? -13.04036 1.79758  -5.96029  1.000 61.83845  ? 71  GLY   A CA  1 
ATOM   550  C C   . GLY   A 1 71  ? -14.43377 1.72191  -5.36707  1.000 68.28536  ? 71  GLY   A C   1 
ATOM   551  O O   . GLY   A 1 71  ? -15.38929 2.31183  -5.88330  1.000 66.54431  ? 71  GLY   A O   1 
ATOM   552  N N   . ASN   A 1 72  ? -14.55693 0.99240  -4.25902  1.000 67.63006  ? 72  ASN   A N   1 
ATOM   553  C CA  . ASN   A 1 72  ? -15.82383 0.86797  -3.55241  1.000 71.11537  ? 72  ASN   A CA  1 
ATOM   554  C C   . ASN   A 1 72  ? -15.91180 1.79236  -2.34390  1.000 71.15000  ? 72  ASN   A C   1 
ATOM   555  O O   . ASN   A 1 72  ? -16.69446 1.52791  -1.42517  1.000 72.99231  ? 72  ASN   A O   1 
ATOM   556  C CB  . ASN   A 1 72  ? -16.05871 -0.58205 -3.12773  1.000 74.13733  ? 72  ASN   A CB  1 
ATOM   557  C CG  . ASN   A 1 72  ? -16.96418 -1.32852 -4.08827  1.000 80.14520  ? 72  ASN   A CG  1 
ATOM   558  O OD1 . ASN   A 1 72  ? -17.85924 -0.74180 -4.69858  1.000 79.39142  ? 72  ASN   A OD1 1 
ATOM   559  N ND2 . ASN   A 1 72  ? -16.73859 -2.62949 -4.22487  1.000 83.47758  ? 72  ASN   A ND2 1 
ATOM   560  N N   . VAL   A 1 73  ? -15.12695 2.86678  -2.32276  1.000 70.53582  ? 73  VAL   A N   1 
ATOM   561  C CA  . VAL   A 1 73  ? -15.19440 3.86976  -1.26852  1.000 65.80012  ? 73  VAL   A CA  1 
ATOM   562  C C   . VAL   A 1 73  ? -15.54583 5.20966  -1.90077  1.000 62.12462  ? 73  VAL   A C   1 
ATOM   563  O O   . VAL   A 1 73  ? -15.14827 5.49886  -3.03547  1.000 58.88757  ? 73  VAL   A O   1 
ATOM   564  C CB  . VAL   A 1 73  ? -13.87734 3.95523  -0.46275  1.000 65.94596  ? 73  VAL   A CB  1 
ATOM   565  C CG1 . VAL   A 1 73  ? -13.34247 2.55969  -0.16673  1.000 66.63744  ? 73  VAL   A CG1 1 
ATOM   566  C CG2 . VAL   A 1 73  ? -12.82859 4.78842  -1.18939  1.000 61.58554  ? 73  VAL   A CG2 1 
ATOM   567  N N   . GLN   A 1 74  ? -16.32225 6.01055  -1.17741  1.000 64.58281  ? 74  GLN   A N   1 
ATOM   568  C CA  . GLN   A 1 74  ? -16.69464 7.33999  -1.63504  1.000 58.40344  ? 74  GLN   A CA  1 
ATOM   569  C C   . GLN   A 1 74  ? -15.73020 8.37169  -1.07075  1.000 56.07472  ? 74  GLN   A C   1 
ATOM   570  O O   . GLN   A 1 74  ? -15.27772 8.25883  0.07208   1.000 58.66205  ? 74  GLN   A O   1 
ATOM   571  C CB  . GLN   A 1 74  ? -18.12484 7.68653  -1.21549  1.000 58.47000  ? 74  GLN   A CB  1 
ATOM   572  C CG  . GLN   A 1 74  ? -19.16526 7.50688  -2.30962  1.000 63.79223  ? 74  GLN   A CG  1 
ATOM   573  C CD  . GLN   A 1 74  ? -20.45949 6.90407  -1.79509  1.000 70.94597  ? 74  GLN   A CD  1 
ATOM   574  O OE1 . GLN   A 1 74  ? -20.63551 6.71609  -0.59102  1.000 78.77088  ? 74  GLN   A OE1 1 
ATOM   575  N NE2 . GLN   A 1 74  ? -21.37653 6.60390  -2.70829  1.000 69.30615  ? 74  GLN   A NE2 1 
ATOM   576  N N   . LEU   A 1 75  ? -15.41569 9.37523  -1.88140  1.000 56.26079  ? 75  LEU   A N   1 
ATOM   577  C CA  . LEU   A 1 75  ? -14.58750 10.49558 -1.46244  1.000 56.31072  ? 75  LEU   A CA  1 
ATOM   578  C C   . LEU   A 1 75  ? -15.46895 11.72647 -1.31348  1.000 54.83831  ? 75  LEU   A C   1 
ATOM   579  O O   . LEU   A 1 75  ? -16.21264 12.07941 -2.23520  1.000 54.31607  ? 75  LEU   A O   1 
ATOM   580  C CB  . LEU   A 1 75  ? -13.45664 10.75069 -2.46179  1.000 55.80596  ? 75  LEU   A CB  1 
ATOM   581  C CG  . LEU   A 1 75  ? -12.64641 9.51387  -2.86180  1.000 51.49538  ? 75  LEU   A CG  1 
ATOM   582  C CD1 . LEU   A 1 75  ? -11.57956 9.86395  -3.88918  1.000 46.08367  ? 75  LEU   A CD1 1 
ATOM   583  C CD2 . LEU   A 1 75  ? -12.02158 8.86366  -1.63682  1.000 50.72778  ? 75  LEU   A CD2 1 
ATOM   584  N N   . ARG   A 1 76  ? -15.39138 12.36544 -0.15026  1.000 57.06975  ? 76  ARG   A N   1 
ATOM   585  C CA  . ARG   A 1 76  ? -16.26124 13.48933 0.16113   1.000 56.30206  ? 76  ARG   A CA  1 
ATOM   586  C C   . ARG   A 1 76  ? -15.71384 14.76728 -0.46211  1.000 57.32549  ? 76  ARG   A C   1 
ATOM   587  O O   . ARG   A 1 76  ? -14.55346 15.12854 -0.24614  1.000 58.71026  ? 76  ARG   A O   1 
ATOM   588  C CB  . ARG   A 1 76  ? -16.39898 13.64546 1.67447   1.000 55.92356  ? 76  ARG   A CB  1 
ATOM   589  C CG  . ARG   A 1 76  ? -17.73643 14.20552 2.11771   1.000 55.56229  ? 76  ARG   A CG  1 
ATOM   590  C CD  . ARG   A 1 76  ? -17.77085 14.41182 3.62059   1.000 55.91069  ? 76  ARG   A CD  1 
ATOM   591  N NE  . ARG   A 1 76  ? -18.42504 15.66237 3.98346   1.000 60.88212  ? 76  ARG   A NE  1 
ATOM   592  C CZ  . ARG   A 1 76  ? -19.71578 15.77635 4.26390   1.000 59.80283  ? 76  ARG   A CZ  1 
ATOM   593  N NH1 . ARG   A 1 76  ? -20.52648 14.73139 4.22298   1.000 58.55079  ? 76  ARG   A NH1 1 
ATOM   594  N NH2 . ARG   A 1 76  ? -20.20586 16.96897 4.59100   1.000 54.37608  ? 76  ARG   A NH2 1 
ATOM   595  N N   . VAL   A 1 77  ? -16.55092 15.44653 -1.23924  1.000 54.11283  ? 77  VAL   A N   1 
ATOM   596  C CA  . VAL   A 1 77  ? -16.14722 16.67667 -1.91219  1.000 51.11773  ? 77  VAL   A CA  1 
ATOM   597  C C   . VAL   A 1 77  ? -16.26286 17.83247 -0.92466  1.000 54.87783  ? 77  VAL   A C   1 
ATOM   598  O O   . VAL   A 1 77  ? -17.33307 18.08739 -0.36822  1.000 54.10911  ? 77  VAL   A O   1 
ATOM   599  C CB  . VAL   A 1 77  ? -16.99929 16.93202 -3.16253  1.000 49.20148  ? 77  VAL   A CB  1 
ATOM   600  C CG1 . VAL   A 1 77  ? -16.55911 18.21595 -3.85042  1.000 49.55127  ? 77  VAL   A CG1 1 
ATOM   601  C CG2 . VAL   A 1 77  ? -16.90072 15.75364 -4.11653  1.000 49.95579  ? 77  VAL   A CG2 1 
ATOM   602  N N   . ILE   A 1 78  ? -15.14974 18.53217 -0.70852  1.000 56.72883  ? 78  ILE   A N   1 
ATOM   603  C CA  . ILE   A 1 78  ? -15.09728 19.62015 0.25255   1.000 56.58175  ? 78  ILE   A CA  1 
ATOM   604  C C   . ILE   A 1 78  ? -15.14542 20.99364 -0.41296  1.000 53.52572  ? 78  ILE   A C   1 
ATOM   605  O O   . ILE   A 1 78  ? -15.68420 21.93761 0.17369   1.000 60.52241  ? 78  ILE   A O   1 
ATOM   606  C CB  . ILE   A 1 78  ? -13.84487 19.47976 1.15218   1.000 56.05239  ? 78  ILE   A CB  1 
ATOM   607  C CG1 . ILE   A 1 78  ? -14.17420 18.70957 2.44076   1.000 59.25355  ? 78  ILE   A CG1 1 
ATOM   608  C CG2 . ILE   A 1 78  ? -13.21786 20.83001 1.48506   1.000 54.36280  ? 78  ILE   A CG2 1 
ATOM   609  C CD1 . ILE   A 1 78  ? -14.98539 17.43810 2.25303   1.000 59.01014  ? 78  ILE   A CD1 1 
ATOM   610  N N   . GLY   A 1 79  ? -14.62778 21.12433 -1.63840  1.000 52.62542  ? 79  GLY   A N   1 
ATOM   611  C CA  . GLY   A 1 79  ? -14.75736 22.35219 -2.39550  1.000 51.00159  ? 79  GLY   A CA  1 
ATOM   612  C C   . GLY   A 1 79  ? -14.80596 22.04264 -3.87699  1.000 51.66896  ? 79  GLY   A C   1 
ATOM   613  O O   . GLY   A 1 79  ? -14.60882 20.90079 -4.29719  1.000 49.98912  ? 79  GLY   A O   1 
ATOM   614  N N   . HIS   A 1 80  ? -15.07855 23.07692 -4.67146  1.000 51.62262  ? 80  HIS   A N   1 
ATOM   615  C CA  . HIS   A 1 80  ? -15.08966 22.91449 -6.11966  1.000 50.66534  ? 80  HIS   A CA  1 
ATOM   616  C C   . HIS   A 1 80  ? -14.87411 24.26659 -6.78499  1.000 49.01409  ? 80  HIS   A C   1 
ATOM   617  O O   . HIS   A 1 80  ? -15.35247 25.29122 -6.29323  1.000 49.89569  ? 80  HIS   A O   1 
ATOM   618  C CB  . HIS   A 1 80  ? -16.39743 22.27565 -6.61236  1.000 52.28904  ? 80  HIS   A CB  1 
ATOM   619  C CG  . HIS   A 1 80  ? -17.60086 23.15480 -6.46829  1.000 52.41447  ? 80  HIS   A CG  1 
ATOM   620  N ND1 . HIS   A 1 80  ? -18.42879 23.10915 -5.36738  1.000 54.28094  ? 80  HIS   A ND1 1 
ATOM   621  C CD2 . HIS   A 1 80  ? -18.12365 24.09319 -7.29305  1.000 52.80170  ? 80  HIS   A CD2 1 
ATOM   622  C CE1 . HIS   A 1 80  ? -19.40593 23.98557 -5.51716  1.000 54.87459  ? 80  HIS   A CE1 1 
ATOM   623  N NE2 . HIS   A 1 80  ? -19.24361 24.59642 -6.67696  1.000 52.71501  ? 80  HIS   A NE2 1 
ATOM   624  N N   . SER   A 1 81  ? -14.14404 24.25445 -7.89848  1.000 47.00514  ? 81  SER   A N   1 
ATOM   625  C CA  . SER   A 1 81  ? -13.88057 25.45528 -8.67892  1.000 47.98797  ? 81  SER   A CA  1 
ATOM   626  C C   . SER   A 1 81  ? -13.54744 25.03616 -10.10238 1.000 50.45389  ? 81  SER   A C   1 
ATOM   627  O O   . SER   A 1 81  ? -13.09276 23.91579 -10.34765 1.000 51.47664  ? 81  SER   A O   1 
ATOM   628  C CB  . SER   A 1 81  ? -12.74062 26.28470 -8.07814  1.000 50.59292  ? 81  SER   A CB  1 
ATOM   629  O OG  . SER   A 1 81  ? -11.47867 25.77445 -8.47324  1.000 47.96433  ? 81  SER   A OG  1 
ATOM   630  N N   . MET   A 1 82  ? -13.77595 25.95272 -11.03779 1.000 49.28450  ? 82  MET   A N   1 
ATOM   631  C CA  . MET   A 1 82  ? -13.57410 25.69787 -12.45770 1.000 48.59124  ? 82  MET   A CA  1 
ATOM   632  C C   . MET   A 1 82  ? -12.38218 26.49815 -12.96377 1.000 49.81258  ? 82  MET   A C   1 
ATOM   633  O O   . MET   A 1 82  ? -12.27522 27.69895 -12.69396 1.000 50.02640  ? 82  MET   A O   1 
ATOM   634  C CB  . MET   A 1 82  ? -14.82911 26.05365 -13.25911 1.000 49.77355  ? 82  MET   A CB  1 
ATOM   635  C CG  . MET   A 1 82  ? -14.62800 26.05247 -14.76644 1.000 50.65685  ? 82  MET   A CG  1 
ATOM   636  S SD  . MET   A 1 82  ? -16.07869 26.63274 -15.66805 1.000 57.88290  ? 82  MET   A SD  1 
ATOM   637  C CE  . MET   A 1 82  ? -15.42531 28.11652 -16.43126 1.000 57.49808  ? 82  MET   A CE  1 
ATOM   638  N N   . GLN   A 1 83  ? -11.49015 25.83045 -13.69218 1.000 48.36259  ? 83  GLN   A N   1 
ATOM   639  C CA  . GLN   A 1 83  ? -10.35345 26.47251 -14.34970 1.000 48.11884  ? 83  GLN   A CA  1 
ATOM   640  C C   . GLN   A 1 83  ? -10.47292 26.19804 -15.84515 1.000 48.00857  ? 83  GLN   A C   1 
ATOM   641  O O   . GLN   A 1 83  ? -10.12949 25.10635 -16.31093 1.000 49.70433  ? 83  GLN   A O   1 
ATOM   642  C CB  . GLN   A 1 83  ? -9.02579  25.96607 -13.79260 1.000 47.28069  ? 83  GLN   A CB  1 
ATOM   643  C CG  . GLN   A 1 83  ? -7.81447  26.73216 -14.30694 1.000 47.73362  ? 83  GLN   A CG  1 
ATOM   644  C CD  . GLN   A 1 83  ? -6.50334  26.18481 -13.77745 1.000 50.65691  ? 83  GLN   A CD  1 
ATOM   645  O OE1 . GLN   A 1 83  ? -6.48275  25.22175 -13.01136 1.000 50.01479  ? 83  GLN   A OE1 1 
ATOM   646  N NE2 . GLN   A 1 83  ? -5.39839  26.79865 -14.18588 1.000 50.44875  ? 83  GLN   A NE2 1 
ATOM   647  N N   . ASN   A 1 84  ? -10.96126 27.19262 -16.58829 1.000 45.68679  ? 84  ASN   A N   1 
ATOM   648  C CA  . ASN   A 1 84  ? -11.18833 27.09577 -18.03401 1.000 47.12762  ? 84  ASN   A CA  1 
ATOM   649  C C   . ASN   A 1 84  ? -12.16479 25.95238 -18.27759 1.000 48.79756  ? 84  ASN   A C   1 
ATOM   650  O O   . ASN   A 1 84  ? -13.28840 26.00410 -17.74293 1.000 48.08469  ? 84  ASN   A O   1 
ATOM   651  C CB  . ASN   A 1 84  ? -9.83692  26.99072 -18.74717 1.000 49.65482  ? 84  ASN   A CB  1 
ATOM   652  C CG  . ASN   A 1 84  ? -9.03739  28.28079 -18.68026 1.000 51.62992  ? 84  ASN   A CG  1 
ATOM   653  O OD1 . ASN   A 1 84  ? -7.95516  28.32504 -18.09420 1.000 52.73227  ? 84  ASN   A OD1 1 
ATOM   654  N ND2 . ASN   A 1 84  ? -9.56780  29.33812 -19.28403 1.000 48.13014  ? 84  ASN   A ND2 1 
ATOM   655  N N   . CYS   A 1 85  ? -11.81261 24.92145 -19.04326 1.000 48.85585  ? 85  CYS   A N   1 
ATOM   656  C CA  . CYS   A 1 85  ? -12.72988 23.83272 -19.35240 1.000 47.84668  ? 85  CYS   A CA  1 
ATOM   657  C C   . CYS   A 1 85  ? -12.59685 22.64880 -18.40369 1.000 48.41209  ? 85  CYS   A C   1 
ATOM   658  O O   . CYS   A 1 85  ? -13.24737 21.62204 -18.62566 1.000 47.67308  ? 85  CYS   A O   1 
ATOM   659  C CB  . CYS   A 1 85  ? -12.51858 23.35541 -20.79214 1.000 45.95097  ? 85  CYS   A CB  1 
ATOM   660  S SG  . CYS   A 1 85  ? -13.08756 24.51490 -22.04922 1.000 47.44968  ? 85  CYS   A SG  1 
ATOM   661  N N   . VAL   A 1 86  ? -11.78371 22.76535 -17.35722 1.000 45.74773  ? 86  VAL   A N   1 
ATOM   662  C CA  . VAL   A 1 86  ? -11.54690 21.68639 -16.40597 1.000 47.42385  ? 86  VAL   A CA  1 
ATOM   663  C C   . VAL   A 1 86  ? -12.17287 22.05671 -15.06865 1.000 47.44231  ? 86  VAL   A C   1 
ATOM   664  O O   . VAL   A 1 86  ? -12.05525 23.19908 -14.60985 1.000 47.53109  ? 86  VAL   A O   1 
ATOM   665  C CB  . VAL   A 1 86  ? -10.03877 21.39868 -16.25733 1.000 46.87399  ? 86  VAL   A CB  1 
ATOM   666  C CG1 . VAL   A 1 86  ? -9.73772  20.74167 -14.91998 1.000 48.00926  ? 86  VAL   A CG1 1 
ATOM   667  C CG2 . VAL   A 1 86  ? -9.56201  20.50759 -17.39277 1.000 46.31164  ? 86  VAL   A CG2 1 
ATOM   668  N N   . LEU   A 1 87  ? -12.85552 21.09260 -14.45688 1.000 46.47548  ? 87  LEU   A N   1 
ATOM   669  C CA  . LEU   A 1 87  ? -13.39073 21.24552 -13.11330 1.000 46.93081  ? 87  LEU   A CA  1 
ATOM   670  C C   . LEU   A 1 87  ? -12.38854 20.72250 -12.09067 1.000 47.65830  ? 87  LEU   A C   1 
ATOM   671  O O   . LEU   A 1 87  ? -11.63819 19.77922 -12.35428 1.000 48.13855  ? 87  LEU   A O   1 
ATOM   672  C CB  . LEU   A 1 87  ? -14.72151 20.50212 -12.97315 1.000 49.00011  ? 87  LEU   A CB  1 
ATOM   673  C CG  . LEU   A 1 87  ? -15.52372 20.73559 -11.69122 1.000 47.76541  ? 87  LEU   A CG  1 
ATOM   674  C CD1 . LEU   A 1 87  ? -15.77494 22.22114 -11.46968 1.000 50.17305  ? 87  LEU   A CD1 1 
ATOM   675  C CD2 . LEU   A 1 87  ? -16.83548 19.96581 -11.73221 1.000 50.02581  ? 87  LEU   A CD2 1 
ATOM   676  N N   . LYS   A 1 88  ? -12.37927 21.35017 -10.91574 1.000 47.46312  ? 88  LYS   A N   1 
ATOM   677  C CA  . LYS   A 1 88  ? -11.46080 20.99266 -9.84010  1.000 46.78552  ? 88  LYS   A CA  1 
ATOM   678  C C   . LYS   A 1 88  ? -12.25365 20.80991 -8.55584  1.000 46.49788  ? 88  LYS   A C   1 
ATOM   679  O O   . LYS   A 1 88  ? -12.87926 21.75818 -8.07194  1.000 47.99801  ? 88  LYS   A O   1 
ATOM   680  C CB  . LYS   A 1 88  ? -10.38027 22.06285 -9.65826  1.000 45.14787  ? 88  LYS   A CB  1 
ATOM   681  C CG  . LYS   A 1 88  ? -9.47278  22.23213 -10.86568 1.000 47.99411  ? 88  LYS   A CG  1 
ATOM   682  C CD  . LYS   A 1 88  ? -8.19957  22.98292 -10.51225 1.000 44.93791  ? 88  LYS   A CD  1 
ATOM   683  C CE  . LYS   A 1 88  ? -8.44459  24.48095 -10.44750 1.000 46.25938  ? 88  LYS   A CE  1 
ATOM   684  N NZ  . LYS   A 1 88  ? -7.17724  25.24996 -10.56875 1.000 48.21558  ? 88  LYS   A NZ  1 
ATOM   685  N N   . LEU   A 1 89  ? -12.22126 19.59912 -8.00461  1.000 45.12551  ? 89  LEU   A N   1 
ATOM   686  C CA  . LEU   A 1 89  ? -12.94914 19.25760 -6.78809  1.000 47.18079  ? 89  LEU   A CA  1 
ATOM   687  C C   . LEU   A 1 89  ? -11.95335 18.94936 -5.67827  1.000 47.15250  ? 89  LEU   A C   1 
ATOM   688  O O   . LEU   A 1 89  ? -11.11555 18.05300 -5.82442  1.000 48.00512  ? 89  LEU   A O   1 
ATOM   689  C CB  . LEU   A 1 89  ? -13.87143 18.06040 -7.01935  1.000 42.96460  ? 89  LEU   A CB  1 
ATOM   690  C CG  . LEU   A 1 89  ? -14.67338 18.03724 -8.32036  1.000 44.98264  ? 89  LEU   A CG  1 
ATOM   691  C CD1 . LEU   A 1 89  ? -15.16874 16.63086 -8.61345  1.000 40.30896  ? 89  LEU   A CD1 1 
ATOM   692  C CD2 . LEU   A 1 89  ? -15.83647 19.01179 -8.24695  1.000 48.60703  ? 89  LEU   A CD2 1 
ATOM   693  N N   . LYS   A 1 90  ? -12.04851 19.68415 -4.57316  1.000 45.80841  ? 90  LYS   A N   1 
ATOM   694  C CA  . LYS   A 1 90  ? -11.22290 19.42505 -3.40053  1.000 48.29414  ? 90  LYS   A CA  1 
ATOM   695  C C   . LYS   A 1 90  ? -11.90317 18.36649 -2.54096  1.000 52.80916  ? 90  LYS   A C   1 
ATOM   696  O O   . LYS   A 1 90  ? -13.06189 18.53249 -2.14470  1.000 56.15333  ? 90  LYS   A O   1 
ATOM   697  C CB  . LYS   A 1 90  ? -10.99139 20.70347 -2.59730  1.000 51.15811  ? 90  LYS   A CB  1 
ATOM   698  C CG  . LYS   A 1 90  ? -10.08655 20.50963 -1.39010  1.000 53.23424  ? 90  LYS   A CG  1 
ATOM   699  C CD  . LYS   A 1 90  ? -8.82720  21.35568 -1.48897  1.000 53.70809  ? 90  LYS   A CD  1 
ATOM   700  C CE  . LYS   A 1 90  ? -8.93414  22.60858 -0.63318  1.000 59.51045  ? 90  LYS   A CE  1 
ATOM   701  N NZ  . LYS   A 1 90  ? -7.64791  23.35756 -0.57892  1.000 62.63567  ? 90  LYS   A NZ  1 
ATOM   702  N N   . VAL   A 1 91  ? -11.18835 17.28180 -2.25865  1.000 52.00660  ? 91  VAL   A N   1 
ATOM   703  C CA  . VAL   A 1 91  ? -11.72536 16.18155 -1.47231  1.000 55.59737  ? 91  VAL   A CA  1 
ATOM   704  C C   . VAL   A 1 91  ? -11.00482 16.12044 -0.13094  1.000 57.21803  ? 91  VAL   A C   1 
ATOM   705  O O   . VAL   A 1 91  ? -9.86954  16.58051 0.02296   1.000 57.61771  ? 91  VAL   A O   1 
ATOM   706  C CB  . VAL   A 1 91  ? -11.62233 14.83473 -2.21864  1.000 52.48969  ? 91  VAL   A CB  1 
ATOM   707  C CG1 . VAL   A 1 91  ? -12.68222 14.75052 -3.30449  1.000 51.37661  ? 91  VAL   A CG1 1 
ATOM   708  C CG2 . VAL   A 1 91  ? -10.23716 14.66348 -2.81577  1.000 51.12373  ? 91  VAL   A CG2 1 
ATOM   709  N N   . ASP   A 1 92  ? -11.68686 15.53366 0.85528   1.000 57.49343  ? 92  ASP   A N   1 
ATOM   710  C CA  . ASP   A 1 92  ? -11.16739 15.45206 2.21628   1.000 57.90802  ? 92  ASP   A CA  1 
ATOM   711  C C   . ASP   A 1 92  ? -10.03740 14.44186 2.37095   1.000 58.78906  ? 92  ASP   A C   1 
ATOM   712  O O   . ASP   A 1 92  ? -9.52181  14.28731 3.48407   1.000 61.60410  ? 92  ASP   A O   1 
ATOM   713  C CB  . ASP   A 1 92  ? -12.30042 15.11332 3.19096   1.000 61.54027  ? 92  ASP   A CB  1 
ATOM   714  C CG  . ASP   A 1 92  ? -12.96843 13.78229 2.88051   1.000 67.19102  ? 92  ASP   A CG  1 
ATOM   715  O OD1 . ASP   A 1 92  ? -12.83518 13.29368 1.73650   1.000 61.41397  ? 92  ASP   A OD1 1 
ATOM   716  O OD2 . ASP   A 1 92  ? -13.63071 13.22645 3.78254   1.000 64.18391  ? 92  ASP   A OD2 1 
ATOM   717  N N   . THR   A 1 93  ? -9.63937  13.75622 1.30221   1.000 59.26761  ? 93  THR   A N   1 
ATOM   718  C CA  . THR   A 1 93  ? -8.57396  12.76541 1.36801   1.000 58.18659  ? 93  THR   A CA  1 
ATOM   719  C C   . THR   A 1 93  ? -7.64528  12.95304 0.17990   1.000 59.15724  ? 93  THR   A C   1 
ATOM   720  O O   . THR   A 1 93  ? -8.10776  13.10766 -0.95412  1.000 57.61477  ? 93  THR   A O   1 
ATOM   721  C CB  . THR   A 1 93  ? -9.13713  11.33803 1.37509   1.000 58.36148  ? 93  THR   A CB  1 
ATOM   722  O OG1 . THR   A 1 93  ? -10.02090 11.17584 2.49042   1.000 65.15952  ? 93  THR   A OG1 1 
ATOM   723  C CG2 . THR   A 1 93  ? -8.01290  10.31759 1.47554   1.000 58.29865  ? 93  THR   A CG2 1 
ATOM   724  N N   . ALA   A 1 94  ? -6.34244  12.94620 0.44139   1.000 57.53595  ? 94  ALA   A N   1 
ATOM   725  C CA  . ALA   A 1 94  ? -5.35152  12.99351 -0.62065  1.000 55.95510  ? 94  ALA   A CA  1 
ATOM   726  C C   . ALA   A 1 94  ? -5.01082  11.57959 -1.06713  1.000 54.82480  ? 94  ALA   A C   1 
ATOM   727  O O   . ALA   A 1 94  ? -4.89059  10.66791 -0.24388  1.000 58.40088  ? 94  ALA   A O   1 
ATOM   728  C CB  . ALA   A 1 94  ? -4.08995  13.71996 -0.15787  1.000 56.76073  ? 94  ALA   A CB  1 
ATOM   729  N N   . ASN   A 1 95  ? -4.86193  11.40363 -2.37672  1.000 51.98192  ? 95  ASN   A N   1 
ATOM   730  C CA  . ASN   A 1 95  ? -4.60326  10.09017 -2.95140  1.000 52.73748  ? 95  ASN   A CA  1 
ATOM   731  C C   . ASN   A 1 95  ? -3.27261  9.54421  -2.44831  1.000 53.26944  ? 95  ASN   A C   1 
ATOM   732  O O   . ASN   A 1 95  ? -2.21512  10.11712 -2.74057  1.000 53.30475  ? 95  ASN   A O   1 
ATOM   733  C CB  . ASN   A 1 95  ? -4.60933  10.16744 -4.47915  1.000 50.35117  ? 95  ASN   A CB  1 
ATOM   734  C CG  . ASN   A 1 95  ? -4.44170  8.81052  -5.13700  1.000 49.54005  ? 95  ASN   A CG  1 
ATOM   735  O OD1 . ASN   A 1 95  ? -4.52830  7.77191  -4.48261  1.000 49.55788  ? 95  ASN   A OD1 1 
ATOM   736  N ND2 . ASN   A 1 95  ? -4.19789  8.81495  -6.44255  1.000 50.01117  ? 95  ASN   A ND2 1 
ATOM   737  N N   . PRO   A 1 96  ? -3.28147  8.44216  -1.69115  1.000 53.63835  ? 96  PRO   A N   1 
ATOM   738  C CA  . PRO   A 1 96  ? -2.01392  7.85558  -1.22868  1.000 53.32203  ? 96  PRO   A CA  1 
ATOM   739  C C   . PRO   A 1 96  ? -1.18017  7.25378  -2.34585  1.000 54.74694  ? 96  PRO   A C   1 
ATOM   740  O O   . PRO   A 1 96  ? -0.00640  6.93613  -2.11396  1.000 54.97273  ? 96  PRO   A O   1 
ATOM   741  C CB  . PRO   A 1 96  ? -2.46851  6.78117  -0.23431  1.000 52.68037  ? 96  PRO   A CB  1 
ATOM   742  C CG  . PRO   A 1 96  ? -3.83683  6.40300  -0.69998  1.000 57.35845  ? 96  PRO   A CG  1 
ATOM   743  C CD  . PRO   A 1 96  ? -4.45078  7.66186  -1.24900  1.000 52.39120  ? 96  PRO   A CD  1 
ATOM   744  N N   . LYS   A 1 97  ? -1.74487  7.08328  -3.53958  1.000 54.24361  ? 97  LYS   A N   1 
ATOM   745  C CA  . LYS   A 1 97  ? -1.01099  6.60174  -4.69980  1.000 51.94644  ? 97  LYS   A CA  1 
ATOM   746  C C   . LYS   A 1 97  ? -0.57371  7.73419  -5.62007  1.000 49.68371  ? 97  LYS   A C   1 
ATOM   747  O O   . LYS   A 1 97  ? -0.16094  7.47197  -6.75459  1.000 48.36861  ? 97  LYS   A O   1 
ATOM   748  C CB  . LYS   A 1 97  ? -1.85950  5.59306  -5.47665  1.000 48.71420  ? 97  LYS   A CB  1 
ATOM   749  C CG  . LYS   A 1 97  ? -2.09250  4.28335  -4.74127  1.000 48.37842  ? 97  LYS   A CG  1 
ATOM   750  C CD  . LYS   A 1 97  ? -3.39497  3.63123  -5.17791  1.000 52.56962  ? 97  LYS   A CD  1 
ATOM   751  C CE  . LYS   A 1 97  ? -3.30889  2.11534  -5.10845  1.000 54.39449  ? 97  LYS   A CE  1 
ATOM   752  N NZ  . LYS   A 1 97  ? -4.29544  1.46489  -6.01461  1.000 55.24493  ? 97  LYS   A NZ  1 
ATOM   753  N N   . THR   A 1 98  ? -0.65620  8.97883  -5.15926  1.000 51.14931  ? 98  THR   A N   1 
ATOM   754  C CA  . THR   A 1 98  ? -0.27716  10.12773 -5.97123  1.000 50.06791  ? 98  THR   A CA  1 
ATOM   755  C C   . THR   A 1 98  ? 1.19114   10.03355 -6.36883  1.000 49.44842  ? 98  THR   A C   1 
ATOM   756  O O   . THR   A 1 98  ? 2.05862   9.93972  -5.48756  1.000 49.61960  ? 98  THR   A O   1 
ATOM   757  C CB  . THR   A 1 98  ? -0.52169  11.43244 -5.21627  1.000 52.46981  ? 98  THR   A CB  1 
ATOM   758  O OG1 . THR   A 1 98  ? -1.92835  11.63097 -5.03945  1.000 54.20060  ? 98  THR   A OG1 1 
ATOM   759  C CG2 . THR   A 1 98  ? 0.05774   12.61195 -5.98664  1.000 52.61476  ? 98  THR   A CG2 1 
ATOM   760  N N   . PRO   A 1 99  ? 1.51121   10.04893 -7.65539  1.000 49.01268  ? 99  PRO   A N   1 
ATOM   761  C CA  . PRO   A 1 99  ? 2.91089   10.02886 -8.07957  1.000 47.59529  ? 99  PRO   A CA  1 
ATOM   762  C C   . PRO   A 1 99  ? 3.47039   11.44328 -8.16700  1.000 49.15151  ? 99  PRO   A C   1 
ATOM   763  O O   . PRO   A 1 99  ? 2.75583   12.43738 -8.02683  1.000 49.18353  ? 99  PRO   A O   1 
ATOM   764  C CB  . PRO   A 1 99  ? 2.83004   9.38611  -9.46830  1.000 48.25389  ? 99  PRO   A CB  1 
ATOM   765  C CG  . PRO   A 1 99  ? 1.51333   9.87118  -10.00013 1.000 47.34620  ? 99  PRO   A CG  1 
ATOM   766  C CD  . PRO   A 1 99  ? 0.59144   10.05024 -8.80579  1.000 47.49914  ? 99  PRO   A CD  1 
ATOM   767  N N   . LYS   A 1 100 ? 4.77788   11.51263 -8.39152  1.000 51.20938  ? 100 LYS   A N   1 
ATOM   768  C CA  . LYS   A 1 100 ? 5.39941   12.76968 -8.78167  1.000 51.31010  ? 100 LYS   A CA  1 
ATOM   769  C C   . LYS   A 1 100 ? 4.90309   13.13869 -10.17298 1.000 50.55406  ? 100 LYS   A C   1 
ATOM   770  O O   . LYS   A 1 100 ? 5.03979   12.34840 -11.11218 1.000 50.14162  ? 100 LYS   A O   1 
ATOM   771  C CB  . LYS   A 1 100 ? 6.91937   12.63524 -8.75977  1.000 55.31896  ? 100 LYS   A CB  1 
ATOM   772  C CG  . LYS   A 1 100 ? 7.67227   13.84886 -9.27531  1.000 53.46963  ? 100 LYS   A CG  1 
ATOM   773  C CD  . LYS   A 1 100 ? 9.17358   13.63238 -9.16859  1.000 58.16888  ? 100 LYS   A CD  1 
ATOM   774  C CE  . LYS   A 1 100 ? 9.94958   14.85813 -9.61587  1.000 58.75817  ? 100 LYS   A CE  1 
ATOM   775  N NZ  . LYS   A 1 100 ? 11.41698  14.66425 -9.45544  1.000 63.53261  ? 100 LYS   A NZ  1 
ATOM   776  N N   . TYR   A 1 101 ? 4.30281   14.31884 -10.31097 1.000 46.99398  ? 101 TYR   A N   1 
ATOM   777  C CA  . TYR   A 1 101 ? 3.66209   14.67571 -11.56677 1.000 50.64527  ? 101 TYR   A CA  1 
ATOM   778  C C   . TYR   A 1 101 ? 3.99631   16.10940 -11.95048 1.000 48.11392  ? 101 TYR   A C   1 
ATOM   779  O O   . TYR   A 1 101 ? 4.49437   16.90103 -11.14583 1.000 48.60428  ? 101 TYR   A O   1 
ATOM   780  C CB  . TYR   A 1 101 ? 2.13955   14.47989 -11.50104 1.000 46.72761  ? 101 TYR   A CB  1 
ATOM   781  C CG  . TYR   A 1 101 ? 1.42606   15.36371 -10.50205 1.000 48.21887  ? 101 TYR   A CG  1 
ATOM   782  C CD1 . TYR   A 1 101 ? 0.94343   16.61441 -10.86885 1.000 48.46578  ? 101 TYR   A CD1 1 
ATOM   783  C CD2 . TYR   A 1 101 ? 1.22199   14.94103 -9.19517  1.000 48.34725  ? 101 TYR   A CD2 1 
ATOM   784  C CE1 . TYR   A 1 101 ? 0.28578   17.42184 -9.95844  1.000 45.83864  ? 101 TYR   A CE1 1 
ATOM   785  C CE2 . TYR   A 1 101 ? 0.56554   15.74036 -8.27873  1.000 50.64179  ? 101 TYR   A CE2 1 
ATOM   786  C CZ  . TYR   A 1 101 ? 0.09972   16.97927 -8.66501  1.000 49.55180  ? 101 TYR   A CZ  1 
ATOM   787  O OH  . TYR   A 1 101 ? -0.55405  17.77729 -7.75455  1.000 54.14143  ? 101 TYR   A OH  1 
ATOM   788  N N   . LYS   A 1 102 ? 3.71073   16.42495 -13.21201 1.000 47.84326  ? 102 LYS   A N   1 
ATOM   789  C CA  . LYS   A 1 102 ? 3.87463   17.75770 -13.76828 1.000 50.21079  ? 102 LYS   A CA  1 
ATOM   790  C C   . LYS   A 1 102 ? 2.73865   18.00585 -14.75021 1.000 49.89170  ? 102 LYS   A C   1 
ATOM   791  O O   . LYS   A 1 102 ? 2.16266   17.07007 -15.31025 1.000 50.44184  ? 102 LYS   A O   1 
ATOM   792  C CB  . LYS   A 1 102 ? 5.23520   17.91628 -14.46613 1.000 54.21377  ? 102 LYS   A CB  1 
ATOM   793  C CG  . LYS   A 1 102 ? 5.60046   19.34747 -14.84130 1.000 59.48145  ? 102 LYS   A CG  1 
ATOM   794  C CD  . LYS   A 1 102 ? 6.14137   20.12262 -13.65107 1.000 65.48439  ? 102 LYS   A CD  1 
ATOM   795  C CE  . LYS   A 1 102 ? 7.36113   20.94359 -14.04232 1.000 74.33709  ? 102 LYS   A CE  1 
ATOM   796  N NZ  . LYS   A 1 102 ? 7.81263   21.83791 -12.94092 1.000 76.20573  ? 102 LYS   A NZ  1 
ATOM   797  N N   . PHE   A 1 103 ? 2.40810   19.27923 -14.94449 1.000 50.15901  ? 103 PHE   A N   1 
ATOM   798  C CA  . PHE   A 1 103 ? 1.39537   19.69413 -15.90996 1.000 49.63074  ? 103 PHE   A CA  1 
ATOM   799  C C   . PHE   A 1 103 ? 2.10186   20.40270 -17.05831 1.000 51.44102  ? 103 PHE   A C   1 
ATOM   800  O O   . PHE   A 1 103 ? 2.55583   21.54225 -16.90649 1.000 51.66465  ? 103 PHE   A O   1 
ATOM   801  C CB  . PHE   A 1 103 ? 0.35060   20.59892 -15.26036 1.000 48.78030  ? 103 PHE   A CB  1 
ATOM   802  C CG  . PHE   A 1 103 ? -0.68656  19.85579 -14.46788 1.000 47.72198  ? 103 PHE   A CG  1 
ATOM   803  C CD1 . PHE   A 1 103 ? -0.68396  18.47138 -14.42290 1.000 48.57212  ? 103 PHE   A CD1 1 
ATOM   804  C CD2 . PHE   A 1 103 ? -1.66616  20.54201 -13.76943 1.000 47.42436  ? 103 PHE   A CD2 1 
ATOM   805  C CE1 . PHE   A 1 103 ? -1.63713  17.78500 -13.69397 1.000 47.07053  ? 103 PHE   A CE1 1 
ATOM   806  C CE2 . PHE   A 1 103 ? -2.62278  19.86168 -13.03912 1.000 46.80530  ? 103 PHE   A CE2 1 
ATOM   807  C CZ  . PHE   A 1 103 ? -2.60816  18.48155 -13.00158 1.000 48.06511  ? 103 PHE   A CZ  1 
ATOM   808  N N   . VAL   A 1 104 ? 2.19891   19.72815 -18.20109 1.000 48.71060  ? 104 VAL   A N   1 
ATOM   809  C CA  . VAL   A 1 104 ? 2.88519   20.27076 -19.36485 1.000 48.98168  ? 104 VAL   A CA  1 
ATOM   810  C C   . VAL   A 1 104 ? 1.88320   20.45153 -20.49601 1.000 46.65298  ? 104 VAL   A C   1 
ATOM   811  O O   . VAL   A 1 104 ? 0.89583   19.71696 -20.60942 1.000 48.32520  ? 104 VAL   A O   1 
ATOM   812  C CB  . VAL   A 1 104 ? 4.06774   19.37674 -19.80925 1.000 48.28398  ? 104 VAL   A CB  1 
ATOM   813  C CG1 . VAL   A 1 104 ? 4.86388   18.90794 -18.60000 1.000 43.98863  ? 104 VAL   A CG1 1 
ATOM   814  C CG2 . VAL   A 1 104 ? 3.57988   18.18527 -20.62494 1.000 46.95980  ? 104 VAL   A CG2 1 
ATOM   815  N N   . ARG   A 1 105 ? 2.13194   21.46396 -21.32083 1.000 42.97235  ? 105 ARG   A N   1 
ATOM   816  C CA  . ARG   A 1 105 ? 1.37945   21.69594 -22.54794 1.000 45.10585  ? 105 ARG   A CA  1 
ATOM   817  C C   . ARG   A 1 105 ? 2.29217   21.31749 -23.70548 1.000 46.91998  ? 105 ARG   A C   1 
ATOM   818  O O   . ARG   A 1 105 ? 3.22359   22.05928 -24.03630 1.000 50.08003  ? 105 ARG   A O   1 
ATOM   819  C CB  . ARG   A 1 105 ? 0.91582   23.14751 -22.65568 1.000 45.70015  ? 105 ARG   A CB  1 
ATOM   820  C CG  . ARG   A 1 105 ? 0.42786   23.53867 -24.04423 1.000 43.35106  ? 105 ARG   A CG  1 
ATOM   821  C CD  . ARG   A 1 105 ? -1.07061  23.78333 -24.05371 1.000 42.31311  ? 105 ARG   A CD  1 
ATOM   822  N NE  . ARG   A 1 105 ? -1.48258  24.64212 -25.15731 1.000 44.55534  ? 105 ARG   A NE  1 
ATOM   823  C CZ  . ARG   A 1 105 ? -2.74302  24.84936 -25.51397 1.000 45.19115  ? 105 ARG   A CZ  1 
ATOM   824  N NH1 . ARG   A 1 105 ? -3.74680  24.27768 -24.86905 1.000 45.39298  ? 105 ARG   A NH1 1 
ATOM   825  N NH2 . ARG   A 1 105 ? -3.00306  25.64926 -26.54446 1.000 47.35236  ? 105 ARG   A NH2 1 
ATOM   826  N N   . ILE   A 1 106 ? 2.03515   20.15894 -24.30809 1.000 44.74937  ? 106 ILE   A N   1 
ATOM   827  C CA  . ILE   A 1 106 ? 2.90856   19.63398 -25.35024 1.000 50.50635  ? 106 ILE   A CA  1 
ATOM   828  C C   . ILE   A 1 106 ? 2.69180   20.41329 -26.64069 1.000 50.30513  ? 106 ILE   A C   1 
ATOM   829  O O   . ILE   A 1 106 ? 1.70806   21.14925 -26.78185 1.000 47.94710  ? 106 ILE   A O   1 
ATOM   830  C CB  . ILE   A 1 106 ? 2.67976   18.12534 -25.56153 1.000 47.45334  ? 106 ILE   A CB  1 
ATOM   831  C CG1 . ILE   A 1 106 ? 1.18359   17.81114 -25.64354 1.000 45.88409  ? 106 ILE   A CG1 1 
ATOM   832  C CG2 . ILE   A 1 106 ? 3.33226   17.32490 -24.43201 1.000 44.36091  ? 106 ILE   A CG2 1 
ATOM   833  C CD1 . ILE   A 1 106 ? 0.61976   17.79313 -27.04902 1.000 45.06037  ? 106 ILE   A CD1 1 
ATOM   834  N N   . GLN   A 1 107 ? 3.61235   20.25560 -27.58632 1.000 51.08945  ? 107 GLN   A N   1 
ATOM   835  C CA  . GLN   A 1 107 ? 3.66444   20.87941 -28.89624 1.000 49.13843  ? 107 GLN   A CA  1 
ATOM   836  C C   . GLN   A 1 107 ? 3.13033   19.92936 -29.96246 1.000 47.66138  ? 107 GLN   A C   1 
ATOM   837  O O   . GLN   A 1 107 ? 3.11711   18.71011 -29.76419 1.000 47.13222  ? 107 GLN   A O   1 
ATOM   838  C CB  . GLN   A 1 107 ? 5.10510   21.27338 -29.23900 1.000 50.88370  ? 107 GLN   A CB  1 
ATOM   839  C CG  . GLN   A 1 107 ? 5.54046   22.61425 -28.66727 1.000 57.40255  ? 107 GLN   A CG  1 
ATOM   840  C CD  . GLN   A 1 107 ? 4.96563   23.79259 -29.43012 1.000 62.92922  ? 107 GLN   A CD  1 
ATOM   841  O OE1 . GLN   A 1 107 ? 5.57225   24.28537 -30.38229 1.000 66.07473  ? 107 GLN   A OE1 1 
ATOM   842  N NE2 . GLN   A 1 107 ? 3.79278   24.25374 -29.01265 1.000 63.05938  ? 107 GLN   A NE2 1 
ATOM   843  N N   . PRO   A 1 108 ? 2.66722   20.44968 -31.09919 1.000 47.84933  ? 108 PRO   A N   1 
ATOM   844  C CA  . PRO   A 1 108 ? 2.26481   19.56099 -32.19576 1.000 44.55072  ? 108 PRO   A CA  1 
ATOM   845  C C   . PRO   A 1 108 ? 3.43695   18.71367 -32.66798 1.000 45.35993  ? 108 PRO   A C   1 
ATOM   846  O O   . PRO   A 1 108 ? 4.58127   19.17036 -32.71398 1.000 50.03417  ? 108 PRO   A O   1 
ATOM   847  C CB  . PRO   A 1 108 ? 1.78684   20.52902 -33.28549 1.000 42.99189  ? 108 PRO   A CB  1 
ATOM   848  C CG  . PRO   A 1 108 ? 2.37487   21.86014 -32.91275 1.000 47.62296  ? 108 PRO   A CG  1 
ATOM   849  C CD  . PRO   A 1 108 ? 2.42033   21.86562 -31.41897 1.000 49.71041  ? 108 PRO   A CD  1 
ATOM   850  N N   . GLY   A 1 109 ? 3.14153   17.46149 -33.00863 1.000 43.17109  ? 109 GLY   A N   1 
ATOM   851  C CA  . GLY   A 1 109 ? 4.14514   16.50626 -33.41251 1.000 40.09679  ? 109 GLY   A CA  1 
ATOM   852  C C   . GLY   A 1 109 ? 4.62629   15.59023 -32.30569 1.000 40.82803  ? 109 GLY   A C   1 
ATOM   853  O O   . GLY   A 1 109 ? 5.11878   14.49486 -32.59890 1.000 41.57763  ? 109 GLY   A O   1 
ATOM   854  N N   . GLN   A 1 110 ? 4.50433   16.00797 -31.04945 1.000 44.00437  ? 110 GLN   A N   1 
ATOM   855  C CA  . GLN   A 1 110 ? 4.90796   15.16841 -29.93459 1.000 43.24904  ? 110 GLN   A CA  1 
ATOM   856  C C   . GLN   A 1 110 ? 3.86699   14.08277 -29.67717 1.000 42.59354  ? 110 GLN   A C   1 
ATOM   857  O O   . GLN   A 1 110 ? 2.69481   14.20884 -30.04102 1.000 42.17117  ? 110 GLN   A O   1 
ATOM   858  C CB  . GLN   A 1 110 ? 5.11317   16.01165 -28.67689 1.000 42.20372  ? 110 GLN   A CB  1 
ATOM   859  C CG  . GLN   A 1 110 ? 6.19979   17.06470 -28.81104 1.000 44.75549  ? 110 GLN   A CG  1 
ATOM   860  C CD  . GLN   A 1 110 ? 6.46182   17.80393 -27.51212 1.000 47.69506  ? 110 GLN   A CD  1 
ATOM   861  O OE1 . GLN   A 1 110 ? 5.55411   18.38628 -26.92055 1.000 50.22346  ? 110 GLN   A OE1 1 
ATOM   862  N NE2 . GLN   A 1 110 ? 7.71120   17.78470 -27.06298 1.000 48.59980  ? 110 GLN   A NE2 1 
ATOM   863  N N   . THR   A 1 111 ? 4.31049   13.00631 -29.03617 1.000 42.66085  ? 111 THR   A N   1 
ATOM   864  C CA  . THR   A 1 111 ? 3.45751   11.86703 -28.73228 1.000 44.18271  ? 111 THR   A CA  1 
ATOM   865  C C   . THR   A 1 111 ? 3.20652   11.76417 -27.23321 1.000 44.26777  ? 111 THR   A C   1 
ATOM   866  O O   . THR   A 1 111 ? 3.85083   12.42801 -26.41589 1.000 44.05963  ? 111 THR   A O   1 
ATOM   867  C CB  . THR   A 1 111 ? 4.07452   10.55805 -29.24243 1.000 43.51801  ? 111 THR   A CB  1 
ATOM   868  O OG1 . THR   A 1 111 ? 5.42650   10.44959 -28.77985 1.000 40.63078  ? 111 THR   A OG1 1 
ATOM   869  C CG2 . THR   A 1 111 ? 4.04199   10.50018 -30.76297 1.000 46.00864  ? 111 THR   A CG2 1 
ATOM   870  N N   . PHE   A 1 112 ? 2.25003   10.90571 -26.88560 1.000 45.05886  ? 112 PHE   A N   1 
ATOM   871  C CA  . PHE   A 1 112 ? 1.94584   10.59773 -25.49584 1.000 44.59445  ? 112 PHE   A CA  1 
ATOM   872  C C   . PHE   A 1 112 ? 1.10425   9.33144  -25.45366 1.000 43.01182  ? 112 PHE   A C   1 
ATOM   873  O O   . PHE   A 1 112 ? 0.54691   8.89911  -26.46624 1.000 41.58105  ? 112 PHE   A O   1 
ATOM   874  C CB  . PHE   A 1 112 ? 1.22271   11.75767 -24.79584 1.000 44.80880  ? 112 PHE   A CB  1 
ATOM   875  C CG  . PHE   A 1 112 ? -0.01984  12.22587 -25.50517 1.000 44.53452  ? 112 PHE   A CG  1 
ATOM   876  C CD1 . PHE   A 1 112 ? -1.24930  11.64518 -25.23679 1.000 42.83272  ? 112 PHE   A CD1 1 
ATOM   877  C CD2 . PHE   A 1 112 ? 0.03986   13.25701 -26.42887 1.000 43.40257  ? 112 PHE   A CD2 1 
ATOM   878  C CE1 . PHE   A 1 112 ? -2.39106  12.07712 -25.88285 1.000 42.86452  ? 112 PHE   A CE1 1 
ATOM   879  C CE2 . PHE   A 1 112 ? -1.10005  13.69233 -27.07806 1.000 42.60266  ? 112 PHE   A CE2 1 
ATOM   880  C CZ  . PHE   A 1 112 ? -2.31661  13.10087 -26.80430 1.000 43.41592  ? 112 PHE   A CZ  1 
ATOM   881  N N   . SER   A 1 113 ? 1.02460   8.74047  -24.26534 1.000 43.83952  ? 113 SER   A N   1 
ATOM   882  C CA  . SER   A 1 113 ? 0.21198   7.55310  -24.04775 1.000 41.45536  ? 113 SER   A CA  1 
ATOM   883  C C   . SER   A 1 113 ? -1.15834  7.95436  -23.52100 1.000 44.43377  ? 113 SER   A C   1 
ATOM   884  O O   . SER   A 1 113 ? -1.27722  8.87111  -22.70433 1.000 44.93529  ? 113 SER   A O   1 
ATOM   885  C CB  . SER   A 1 113 ? 0.89380   6.60067  -23.06403 1.000 42.64073  ? 113 SER   A CB  1 
ATOM   886  O OG  . SER   A 1 113 ? 2.15567   6.17876  -23.55144 1.000 43.56057  ? 113 SER   A OG  1 
ATOM   887  N N   . VAL   A 1 114 ? -2.19167  7.26487  -23.99644 1.000 42.99871  ? 114 VAL   A N   1 
ATOM   888  C CA  . VAL   A 1 114 ? -3.57096  7.52093  -23.59639 1.000 40.89007  ? 114 VAL   A CA  1 
ATOM   889  C C   . VAL   A 1 114 ? -4.06631  6.31875  -22.80764 1.000 40.54101  ? 114 VAL   A C   1 
ATOM   890  O O   . VAL   A 1 114 ? -4.04731  5.18852  -23.30993 1.000 41.80382  ? 114 VAL   A O   1 
ATOM   891  C CB  . VAL   A 1 114 ? -4.47645  7.78545  -24.80891 1.000 43.70335  ? 114 VAL   A CB  1 
ATOM   892  C CG1 . VAL   A 1 114 ? -5.94036  7.68069  -24.40851 1.000 38.84944  ? 114 VAL   A CG1 1 
ATOM   893  C CG2 . VAL   A 1 114 ? -4.18316  9.14782  -25.40441 1.000 42.10879  ? 114 VAL   A CG2 1 
ATOM   894  N N   . LEU   A 1 115 ? -4.50974  6.55828  -21.57646 1.000 38.73257  ? 115 LEU   A N   1 
ATOM   895  C CA  . LEU   A 1 115 ? -5.15669  5.53162  -20.76297 1.000 42.10738  ? 115 LEU   A CA  1 
ATOM   896  C C   . LEU   A 1 115 ? -6.66436  5.72574  -20.88947 1.000 37.80755  ? 115 LEU   A C   1 
ATOM   897  O O   . LEU   A 1 115 ? -7.24501  6.60645  -20.24984 1.000 38.91292  ? 115 LEU   A O   1 
ATOM   898  C CB  . LEU   A 1 115 ? -4.69948  5.60534  -19.31013 1.000 38.13622  ? 115 LEU   A CB  1 
ATOM   899  C CG  . LEU   A 1 115 ? -5.35949  4.57155  -18.39382 1.000 41.69092  ? 115 LEU   A CG  1 
ATOM   900  C CD1 . LEU   A 1 115 ? -5.01270  3.15942  -18.84367 1.000 43.29332  ? 115 LEU   A CD1 1 
ATOM   901  C CD2 . LEU   A 1 115 ? -4.96445  4.78856  -16.94084 1.000 43.40598  ? 115 LEU   A CD2 1 
ATOM   902  N N   . ALA   A 1 116 ? -7.29512  4.90342  -21.72448 1.000 36.01584  ? 116 ALA   A N   1 
ATOM   903  C CA  . ALA   A 1 116 ? -8.73269  4.98991  -21.94814 1.000 37.56286  ? 116 ALA   A CA  1 
ATOM   904  C C   . ALA   A 1 116 ? -9.46846  4.38285  -20.75997 1.000 38.49757  ? 116 ALA   A C   1 
ATOM   905  O O   . ALA   A 1 116 ? -9.25053  3.21542  -20.41844 1.000 41.85157  ? 116 ALA   A O   1 
ATOM   906  C CB  . ALA   A 1 116 ? -9.11351  4.27953  -23.24460 1.000 39.35784  ? 116 ALA   A CB  1 
ATOM   907  N N   . CYS   A 1 117 ? -10.33847 5.17052  -20.13159 1.000 38.94993  ? 117 CYS   A N   1 
ATOM   908  C CA  . CYS   A 1 117 ? -11.03504 4.75021  -18.92601 1.000 40.36047  ? 117 CYS   A CA  1 
ATOM   909  C C   . CYS   A 1 117 ? -12.53718 4.90094  -19.10490 1.000 39.28341  ? 117 CYS   A C   1 
ATOM   910  O O   . CYS   A 1 117 ? -13.00786 5.71726  -19.90104 1.000 38.58863  ? 117 CYS   A O   1 
ATOM   911  C CB  . CYS   A 1 117 ? -10.58404 5.56060  -17.70299 1.000 41.97697  ? 117 CYS   A CB  1 
ATOM   912  S SG  . CYS   A 1 117 ? -8.89080  5.23022  -17.17196 1.000 45.53778  ? 117 CYS   A SG  1 
ATOM   913  N N   . TYR   A 1 118 ? -13.28417 4.09560  -18.35270 1.000 40.53300  ? 118 TYR   A N   1 
ATOM   914  C CA  . TYR   A 1 118 ? -14.73747 4.19190  -18.30486 1.000 43.57878  ? 118 TYR   A CA  1 
ATOM   915  C C   . TYR   A 1 118 ? -15.19222 3.85592  -16.89352 1.000 42.81800  ? 118 TYR   A C   1 
ATOM   916  O O   . TYR   A 1 118 ? -14.75211 2.85251  -16.32368 1.000 42.93026  ? 118 TYR   A O   1 
ATOM   917  C CB  . TYR   A 1 118 ? -15.40069 3.25657  -19.32484 1.000 41.05210  ? 118 TYR   A CB  1 
ATOM   918  C CG  . TYR   A 1 118 ? -14.97027 3.50896  -20.75262 1.000 41.49510  ? 118 TYR   A CG  1 
ATOM   919  C CD1 . TYR   A 1 118 ? -15.65775 4.40779  -21.55614 1.000 40.22385  ? 118 TYR   A CD1 1 
ATOM   920  C CD2 . TYR   A 1 118 ? -13.87595 2.84865  -21.29653 1.000 41.12545  ? 118 TYR   A CD2 1 
ATOM   921  C CE1 . TYR   A 1 118 ? -15.26562 4.64323  -22.85903 1.000 41.99853  ? 118 TYR   A CE1 1 
ATOM   922  C CE2 . TYR   A 1 118 ? -13.47606 3.07929  -22.59759 1.000 40.28553  ? 118 TYR   A CE2 1 
ATOM   923  C CZ  . TYR   A 1 118 ? -14.17387 3.97677  -23.37444 1.000 40.39489  ? 118 TYR   A CZ  1 
ATOM   924  O OH  . TYR   A 1 118 ? -13.78058 4.20943  -24.67245 1.000 45.38788  ? 118 TYR   A OH  1 
ATOM   925  N N   . ASN   A 1 119 ? -16.06137 4.70180  -16.33633 1.000 42.97161  ? 119 ASN   A N   1 
ATOM   926  C CA  . ASN   A 1 119 ? -16.54381 4.54932  -14.96256 1.000 43.55084  ? 119 ASN   A CA  1 
ATOM   927  C C   . ASN   A 1 119 ? -15.38415 4.53942  -13.96789 1.000 44.61132  ? 119 ASN   A C   1 
ATOM   928  O O   . ASN   A 1 119 ? -15.38767 3.79347  -12.98656 1.000 44.85347  ? 119 ASN   A O   1 
ATOM   929  C CB  . ASN   A 1 119 ? -17.40357 3.29171  -14.81211 1.000 41.72055  ? 119 ASN   A CB  1 
ATOM   930  C CG  . ASN   A 1 119 ? -18.71844 3.39300  -15.55956 1.000 48.42426  ? 119 ASN   A CG  1 
ATOM   931  O OD1 . ASN   A 1 119 ? -18.77617 3.17512  -16.77040 1.000 49.80072  ? 119 ASN   A OD1 1 
ATOM   932  N ND2 . ASN   A 1 119 ? -19.78422 3.72407  -14.84005 1.000 49.17334  ? 119 ASN   A ND2 1 
ATOM   933  N N   . GLY   A 1 120 ? -14.37880 5.37336  -14.22807 1.000 43.94264  ? 120 GLY   A N   1 
ATOM   934  C CA  . GLY   A 1 120 ? -13.22917 5.47377  -13.35152 1.000 45.07996  ? 120 GLY   A CA  1 
ATOM   935  C C   . GLY   A 1 120 ? -12.31192 4.27320  -13.33879 1.000 43.02280  ? 120 GLY   A C   1 
ATOM   936  O O   . GLY   A 1 120 ? -11.47183 4.16717  -12.44054 1.000 46.23172  ? 120 GLY   A O   1 
ATOM   937  N N   . SER   A 1 121 ? -12.43894 3.36462  -14.30499 1.000 43.66920  ? 121 SER   A N   1 
ATOM   938  C CA  . SER   A 1 121 ? -11.62193 2.16381  -14.33792 1.000 45.66954  ? 121 SER   A CA  1 
ATOM   939  C C   . SER   A 1 121 ? -10.95267 2.02234  -15.69924 1.000 45.08278  ? 121 SER   A C   1 
ATOM   940  O O   . SER   A 1 121 ? -11.58833 2.25271  -16.73483 1.000 42.49954  ? 121 SER   A O   1 
ATOM   941  C CB  . SER   A 1 121 ? -12.46197 0.91469  -14.04160 1.000 47.76306  ? 121 SER   A CB  1 
ATOM   942  O OG  . SER   A 1 121 ? -13.47172 1.19257  -13.08803 1.000 52.63449  ? 121 SER   A OG  1 
ATOM   943  N N   . PRO   A 1 122 ? -9.67877  1.64069  -15.72665 1.000 49.11574  ? 122 PRO   A N   1 
ATOM   944  C CA  . PRO   A 1 122 ? -8.95619  1.57670  -17.00164 1.000 45.29095  ? 122 PRO   A CA  1 
ATOM   945  C C   . PRO   A 1 122 ? -9.44231  0.43616  -17.88317 1.000 45.32405  ? 122 PRO   A C   1 
ATOM   946  O O   . PRO   A 1 122 ? -9.83115  -0.63410 -17.40859 1.000 49.72171  ? 122 PRO   A O   1 
ATOM   947  C CB  . PRO   A 1 122 ? -7.49783  1.36134  -16.57382 1.000 46.32956  ? 122 PRO   A CB  1 
ATOM   948  C CG  . PRO   A 1 122 ? -7.45294  1.70610  -15.11486 1.000 46.62483  ? 122 PRO   A CG  1 
ATOM   949  C CD  . PRO   A 1 122 ? -8.80146  1.36412  -14.57931 1.000 47.35572  ? 122 PRO   A CD  1 
ATOM   950  N N   . SER   A 1 123 ? -9.41240  0.68337  -19.19411 1.000 42.79311  ? 123 SER   A N   1 
ATOM   951  C CA  . SER   A 1 123 ? -9.79977  -0.30949 -20.18425 1.000 44.94258  ? 123 SER   A CA  1 
ATOM   952  C C   . SER   A 1 123 ? -8.71651  -0.61696 -21.20443 1.000 43.45088  ? 123 SER   A C   1 
ATOM   953  O O   . SER   A 1 123 ? -8.77615  -1.67822 -21.83451 1.000 47.32754  ? 123 SER   A O   1 
ATOM   954  C CB  . SER   A 1 123 ? -11.06266 0.14037  -20.93655 1.000 46.16293  ? 123 SER   A CB  1 
ATOM   955  O OG  . SER   A 1 123 ? -11.45751 -0.82852 -21.89366 1.000 53.42210  ? 123 SER   A OG  1 
ATOM   956  N N   . GLY   A 1 124 ? -7.74186  0.26355  -21.38574 1.000 40.36828  ? 124 GLY   A N   1 
ATOM   957  C CA  . GLY   A 1 124 ? -6.68700  0.02341  -22.34927 1.000 43.56792  ? 124 GLY   A CA  1 
ATOM   958  C C   . GLY   A 1 124 ? -5.77814  1.22475  -22.44438 1.000 41.65836  ? 124 GLY   A C   1 
ATOM   959  O O   . GLY   A 1 124 ? -6.06833  2.30458  -21.92042 1.000 42.26169  ? 124 GLY   A O   1 
ATOM   960  N N   . VAL   A 1 125 ? -4.66073  1.01955  -23.13526 1.000 38.72385  ? 125 VAL   A N   1 
ATOM   961  C CA  . VAL   A 1 125 ? -3.64258  2.04987  -23.29404 1.000 40.19414  ? 125 VAL   A CA  1 
ATOM   962  C C   . VAL   A 1 125 ? -3.10408  1.99337  -24.71834 1.000 40.09339  ? 125 VAL   A C   1 
ATOM   963  O O   . VAL   A 1 125 ? -2.95381  0.91188  -25.29707 1.000 40.78409  ? 125 VAL   A O   1 
ATOM   964  C CB  . VAL   A 1 125 ? -2.51428  1.88857  -22.24960 1.000 40.66567  ? 125 VAL   A CB  1 
ATOM   965  C CG1 . VAL   A 1 125 ? -1.77676  0.57201  -22.44120 1.000 40.13912  ? 125 VAL   A CG1 1 
ATOM   966  C CG2 . VAL   A 1 125 ? -1.55294  3.06662  -22.30285 1.000 41.43101  ? 125 VAL   A CG2 1 
ATOM   967  N N   . TYR   A 1 126 ? -2.83876  3.16544  -25.29126 1.000 40.34127  ? 126 TYR   A N   1 
ATOM   968  C CA  . TYR   A 1 126 ? -2.26385  3.26137  -26.62682 1.000 41.22024  ? 126 TYR   A CA  1 
ATOM   969  C C   . TYR   A 1 126 ? -1.53291  4.59280  -26.74593 1.000 40.10117  ? 126 TYR   A C   1 
ATOM   970  O O   . TYR   A 1 126 ? -1.59410  5.44094  -25.85255 1.000 39.66188  ? 126 TYR   A O   1 
ATOM   971  C CB  . TYR   A 1 126 ? -3.33552  3.10581  -27.71427 1.000 42.76123  ? 126 TYR   A CB  1 
ATOM   972  C CG  . TYR   A 1 126 ? -4.52588  4.02669  -27.55952 1.000 42.18095  ? 126 TYR   A CG  1 
ATOM   973  C CD1 . TYR   A 1 126 ? -4.54102  5.28081  -28.15440 1.000 42.73793  ? 126 TYR   A CD1 1 
ATOM   974  C CD2 . TYR   A 1 126 ? -5.63688  3.63962  -26.81985 1.000 43.84080  ? 126 TYR   A CD2 1 
ATOM   975  C CE1 . TYR   A 1 126 ? -5.62754  6.12378  -28.01500 1.000 45.00907  ? 126 TYR   A CE1 1 
ATOM   976  C CE2 . TYR   A 1 126 ? -6.72678  4.47769  -26.67464 1.000 43.23209  ? 126 TYR   A CE2 1 
ATOM   977  C CZ  . TYR   A 1 126 ? -6.71615  5.71739  -27.27484 1.000 41.93982  ? 126 TYR   A CZ  1 
ATOM   978  O OH  . TYR   A 1 126 ? -7.79766  6.55398  -27.13415 1.000 43.58944  ? 126 TYR   A OH  1 
ATOM   979  N N   . GLN   A 1 127 ? -0.83462  4.76114  -27.86640 1.000 43.21060  ? 127 GLN   A N   1 
ATOM   980  C CA  . GLN   A 1 127 ? 0.01145   5.92019  -28.11633 1.000 42.80194  ? 127 GLN   A CA  1 
ATOM   981  C C   . GLN   A 1 127 ? -0.63024  6.83426  -29.15102 1.000 43.74339  ? 127 GLN   A C   1 
ATOM   982  O O   . GLN   A 1 127 ? -1.19073  6.36449  -30.14513 1.000 45.57474  ? 127 GLN   A O   1 
ATOM   983  C CB  . GLN   A 1 127 ? 1.39826   5.48504  -28.59949 1.000 43.05055  ? 127 GLN   A CB  1 
ATOM   984  C CG  . GLN   A 1 127 ? 2.47581   6.55386  -28.49282 1.000 42.68780  ? 127 GLN   A CG  1 
ATOM   985  C CD  . GLN   A 1 127 ? 3.01975   6.71557  -27.08444 1.000 45.52954  ? 127 GLN   A CD  1 
ATOM   986  O OE1 . GLN   A 1 127 ? 3.90808   7.53269  -26.84273 1.000 50.18521  ? 127 GLN   A OE1 1 
ATOM   987  N NE2 . GLN   A 1 127 ? 2.48985   5.93836  -26.14812 1.000 43.31807  ? 127 GLN   A NE2 1 
ATOM   988  N N   . CYS   A 1 128 ? -0.53439  8.14239  -28.91961 1.000 43.10226  ? 128 CYS   A N   1 
ATOM   989  C CA  . CYS   A 1 128 ? -1.13400  9.13202  -29.80267 1.000 44.71657  ? 128 CYS   A CA  1 
ATOM   990  C C   . CYS   A 1 128 ? -0.15731  10.27161 -30.04664 1.000 44.14648  ? 128 CYS   A C   1 
ATOM   991  O O   . CYS   A 1 128 ? 0.61218   10.64970 -29.16140 1.000 44.54855  ? 128 CYS   A O   1 
ATOM   992  C CB  . CYS   A 1 128 ? -2.43530  9.69702  -29.21928 1.000 45.21107  ? 128 CYS   A CB  1 
ATOM   993  S SG  . CYS   A 1 128 ? -3.89273  8.68132  -29.51350 1.000 54.10685  ? 128 CYS   A SG  1 
ATOM   994  N N   . ALA   A 1 129 ? -0.20668  10.82377 -31.25461 1.000 42.65181  ? 129 ALA   A N   1 
ATOM   995  C CA  . ALA   A 1 129 ? 0.56094   12.00544 -31.61701 1.000 42.25671  ? 129 ALA   A CA  1 
ATOM   996  C C   . ALA   A 1 129 ? -0.37661  13.19742 -31.74567 1.000 39.70269  ? 129 ALA   A C   1 
ATOM   997  O O   . ALA   A 1 129 ? -1.47514  13.07603 -32.29596 1.000 42.12635  ? 129 ALA   A O   1 
ATOM   998  C CB  . ALA   A 1 129 ? 1.31859   11.79111 -32.92984 1.000 43.17941  ? 129 ALA   A CB  1 
ATOM   999  N N   . MET   A 1 130 ? 0.05170   14.34707 -31.23136 1.000 40.78001  ? 130 MET   A N   1 
ATOM   1000 C CA  . MET   A 1 130 ? -0.74559  15.56394 -31.33862 1.000 41.19578  ? 130 MET   A CA  1 
ATOM   1001 C C   . MET   A 1 130 ? -0.53542  16.15510 -32.72682 1.000 42.52441  ? 130 MET   A C   1 
ATOM   1002 O O   . MET   A 1 130 ? 0.55735   16.63239 -33.05096 1.000 43.46558  ? 130 MET   A O   1 
ATOM   1003 C CB  . MET   A 1 130 ? -0.37955  16.54590 -30.22981 1.000 39.70937  ? 130 MET   A CB  1 
ATOM   1004 C CG  . MET   A 1 130 ? -0.79742  17.97769 -30.48951 1.000 41.54150  ? 130 MET   A CG  1 
ATOM   1005 S SD  . MET   A 1 130 ? -2.53684  18.27103 -30.10775 1.000 44.47730  ? 130 MET   A SD  1 
ATOM   1006 C CE  . MET   A 1 130 ? -2.67090  17.64018 -28.43896 1.000 38.07805  ? 130 MET   A CE  1 
ATOM   1007 N N   . ARG   A 1 131 ? -1.58591  16.10769 -33.54961 1.000 40.15589  ? 131 ARG   A N   1 
ATOM   1008 C CA  . ARG   A 1 131 ? -1.47459  16.45663 -34.95417 1.000 42.19402  ? 131 ARG   A CA  1 
ATOM   1009 C C   . ARG   A 1 131 ? -1.12552  17.93396 -35.11836 1.000 42.43562  ? 131 ARG   A C   1 
ATOM   1010 O O   . ARG   A 1 131 ? -1.31374  18.73576 -34.19991 1.000 42.70580  ? 131 ARG   A O   1 
ATOM   1011 C CB  . ARG   A 1 131 ? -2.78098  16.14072 -35.68366 1.000 43.13168  ? 131 ARG   A CB  1 
ATOM   1012 C CG  . ARG   A 1 131 ? -3.16552  14.66630 -35.69768 1.000 42.91033  ? 131 ARG   A CG  1 
ATOM   1013 C CD  . ARG   A 1 131 ? -1.99640  13.78682 -36.09742 1.000 40.02149  ? 131 ARG   A CD  1 
ATOM   1014 N NE  . ARG   A 1 131 ? -1.51282  14.10438 -37.43536 1.000 43.14510  ? 131 ARG   A NE  1 
ATOM   1015 C CZ  . ARG   A 1 131 ? -0.47445  13.51801 -38.01563 1.000 45.77078  ? 131 ARG   A CZ  1 
ATOM   1016 N NH1 . ARG   A 1 131 ? 0.21505   12.56850 -37.40352 1.000 45.56297  ? 131 ARG   A NH1 1 
ATOM   1017 N NH2 . ARG   A 1 131 ? -0.11800  13.89427 -39.24051 1.000 44.57561  ? 131 ARG   A NH2 1 
ATOM   1018 N N   . PRO   A 1 132 ? -0.58782  18.31003 -36.28102 1.000 45.54472  ? 132 PRO   A N   1 
ATOM   1019 C CA  . PRO   A 1 132 ? -0.33174  19.73629 -36.53427 1.000 44.53930  ? 132 PRO   A CA  1 
ATOM   1020 C C   . PRO   A 1 132 ? -1.57772  20.60414 -36.45453 1.000 46.03255  ? 132 PRO   A C   1 
ATOM   1021 O O   . PRO   A 1 132 ? -1.46341  21.80581 -36.17974 1.000 47.26541  ? 132 PRO   A O   1 
ATOM   1022 C CB  . PRO   A 1 132 ? 0.26860   19.73072 -37.94579 1.000 46.28132  ? 132 PRO   A CB  1 
ATOM   1023 C CG  . PRO   A 1 132 ? 0.91756   18.39830 -38.06354 1.000 45.59846  ? 132 PRO   A CG  1 
ATOM   1024 C CD  . PRO   A 1 132 ? 0.04002   17.44682 -37.29732 1.000 44.59219  ? 132 PRO   A CD  1 
ATOM   1025 N N   . ASN   A 1 133 ? -2.76408  20.04266 -36.68937 1.000 45.27643  ? 133 ASN   A N   1 
ATOM   1026 C CA  . ASN   A 1 133 ? -4.00845  20.78485 -36.53118 1.000 44.99519  ? 133 ASN   A CA  1 
ATOM   1027 C C   . ASN   A 1 133 ? -4.59184  20.65703 -35.12882 1.000 45.03706  ? 133 ASN   A C   1 
ATOM   1028 O O   . ASN   A 1 133 ? -5.76376  20.99180 -34.92547 1.000 45.10919  ? 133 ASN   A O   1 
ATOM   1029 C CB  . ASN   A 1 133 ? -5.03956  20.34317 -37.57900 1.000 51.13283  ? 133 ASN   A CB  1 
ATOM   1030 C CG  . ASN   A 1 133 ? -5.37934  18.86358 -37.49690 1.000 47.72454  ? 133 ASN   A CG  1 
ATOM   1031 O OD1 . ASN   A 1 133 ? -5.02341  18.17753 -36.54100 1.000 47.42615  ? 133 ASN   A OD1 1 
ATOM   1032 N ND2 . ASN   A 1 133 ? -6.08366  18.36783 -38.50848 1.000 47.12589  ? 133 ASN   A ND2 1 
ATOM   1033 N N   . PHE   A 1 134 ? -3.80123  20.16605 -34.17104 1.000 41.22461  ? 134 PHE   A N   1 
ATOM   1034 C CA  . PHE   A 1 134 ? -4.16669  20.10373 -32.75632 1.000 42.09895  ? 134 PHE   A CA  1 
ATOM   1035 C C   . PHE   A 1 134 ? -5.31805  19.13730 -32.48961 1.000 41.46651  ? 134 PHE   A C   1 
ATOM   1036 O O   . PHE   A 1 134 ? -6.12305  19.35280 -31.58121 1.000 44.19913  ? 134 PHE   A O   1 
ATOM   1037 C CB  . PHE   A 1 134 ? -4.48577  21.49690 -32.20347 1.000 43.93477  ? 134 PHE   A CB  1 
ATOM   1038 C CG  . PHE   A 1 134 ? -3.30945  22.43082 -32.22303 1.000 44.14374  ? 134 PHE   A CG  1 
ATOM   1039 C CD1 . PHE   A 1 134 ? -2.29257  22.30229 -31.29115 1.000 44.13818  ? 134 PHE   A CD1 1 
ATOM   1040 C CD2 . PHE   A 1 134 ? -3.20986  23.42415 -33.18362 1.000 43.22435  ? 134 PHE   A CD2 1 
ATOM   1041 C CE1 . PHE   A 1 134 ? -1.20185  23.15384 -31.30954 1.000 45.07521  ? 134 PHE   A CE1 1 
ATOM   1042 C CE2 . PHE   A 1 134 ? -2.12147  24.27917 -33.20697 1.000 45.36955  ? 134 PHE   A CE2 1 
ATOM   1043 C CZ  . PHE   A 1 134 ? -1.11653  24.14291 -32.26842 1.000 42.76817  ? 134 PHE   A CZ  1 
ATOM   1044 N N   . THR   A 1 135 ? -5.40097  18.06688 -33.26947 1.000 41.92915  ? 135 THR   A N   1 
ATOM   1045 C CA  . THR   A 1 135 ? -6.27361  16.94035 -32.98002 1.000 43.11526  ? 135 THR   A CA  1 
ATOM   1046 C C   . THR   A 1 135 ? -5.42129  15.71008 -32.70007 1.000 42.51256  ? 135 THR   A C   1 
ATOM   1047 O O   . THR   A 1 135 ? -4.20373  15.71124 -32.89510 1.000 43.97560  ? 135 THR   A O   1 
ATOM   1048 C CB  . THR   A 1 135 ? -7.23905  16.66934 -34.14132 1.000 41.71022  ? 135 THR   A CB  1 
ATOM   1049 O OG1 . THR   A 1 135 ? -6.50266  16.22380 -35.28745 1.000 41.79758  ? 135 THR   A OG1 1 
ATOM   1050 C CG2 . THR   A 1 135 ? -8.01436  17.92798 -34.49805 1.000 41.52324  ? 135 THR   A CG2 1 
ATOM   1051 N N   . ILE   A 1 136 ? -6.06953  14.65540 -32.21539 1.000 41.51820  ? 136 ILE   A N   1 
ATOM   1052 C CA  . ILE   A 1 136 ? -5.42593  13.36049 -32.03433 1.000 43.21125  ? 136 ILE   A CA  1 
ATOM   1053 C C   . ILE   A 1 136 ? -6.35510  12.28467 -32.57464 1.000 43.61810  ? 136 ILE   A C   1 
ATOM   1054 O O   . ILE   A 1 136 ? -7.58216  12.39962 -32.47474 1.000 44.34848  ? 136 ILE   A O   1 
ATOM   1055 C CB  . ILE   A 1 136 ? -5.05808  13.08117 -30.55796 1.000 43.23262  ? 136 ILE   A CB  1 
ATOM   1056 C CG1 . ILE   A 1 136 ? -6.31183  12.93276 -29.69331 1.000 42.59700  ? 136 ILE   A CG1 1 
ATOM   1057 C CG2 . ILE   A 1 136 ? -4.13327  14.16356 -30.00776 1.000 42.87984  ? 136 ILE   A CG2 1 
ATOM   1058 C CD1 . ILE   A 1 136 ? -6.12364  12.00349 -28.51513 1.000 44.97126  ? 136 ILE   A CD1 1 
ATOM   1059 N N   . LYS   A 1 137 ? -5.76722  11.24999 -33.17076 1.000 42.80178  ? 137 LYS   A N   1 
ATOM   1060 C CA  . LYS   A 1 137 ? -6.52466  10.11535 -33.69428 1.000 42.78171  ? 137 LYS   A CA  1 
ATOM   1061 C C   . LYS   A 1 137 ? -6.52854  9.03806  -32.61928 1.000 45.60339  ? 137 LYS   A C   1 
ATOM   1062 O O   . LYS   A 1 137 ? -5.63891  8.18869  -32.55314 1.000 46.74057  ? 137 LYS   A O   1 
ATOM   1063 C CB  . LYS   A 1 137 ? -5.92252  9.61769  -35.00224 1.000 42.87331  ? 137 LYS   A CB  1 
ATOM   1064 C CG  . LYS   A 1 137 ? -5.38146  10.72355 -35.89829 1.000 47.72571  ? 137 LYS   A CG  1 
ATOM   1065 C CD  . LYS   A 1 137 ? -5.91626  10.59844 -37.31831 1.000 50.53438  ? 137 LYS   A CD  1 
ATOM   1066 C CE  . LYS   A 1 137 ? -5.35499  11.68779 -38.22078 1.000 53.37087  ? 137 LYS   A CE  1 
ATOM   1067 N NZ  . LYS   A 1 137 ? -6.08829  11.77767 -39.51483 1.000 58.43687  ? 137 LYS   A NZ  1 
ATOM   1068 N N   . GLY   A 1 138 ? -7.54390  9.08174  -31.75511 1.000 44.82298  ? 138 GLY   A N   1 
ATOM   1069 C CA  . GLY   A 1 138 ? -7.65784  8.17974  -30.64135 1.000 42.86912  ? 138 GLY   A CA  1 
ATOM   1070 C C   . GLY   A 1 138 ? -8.74099  7.13708  -30.83800 1.000 44.39977  ? 138 GLY   A C   1 
ATOM   1071 O O   . GLY   A 1 138 ? -9.16343  6.83543  -31.95868 1.000 46.93911  ? 138 GLY   A O   1 
ATOM   1072 N N   . SER   A 1 139 ? -9.19457  6.57659  -29.71571 1.000 44.01520  ? 139 SER   A N   1 
ATOM   1073 C CA  . SER   A 1 139 ? -10.23873 5.54941  -29.72365 1.000 43.14571  ? 139 SER   A CA  1 
ATOM   1074 C C   . SER   A 1 139 ? -11.02603 5.70632  -28.42171 1.000 42.74868  ? 139 SER   A C   1 
ATOM   1075 O O   . SER   A 1 139 ? -10.65491 5.15006  -27.38617 1.000 43.83880  ? 139 SER   A O   1 
ATOM   1076 C CB  . SER   A 1 139 ? -9.64992  4.15448  -29.86333 1.000 45.76355  ? 139 SER   A CB  1 
ATOM   1077 O OG  . SER   A 1 139 ? -10.65401 3.16600  -29.72478 1.000 49.56693  ? 139 SER   A OG  1 
ATOM   1078 N N   . PHE   A 1 140 ? -12.11427 6.46876  -28.49214 1.000 46.74918  ? 140 PHE   A N   1 
ATOM   1079 C CA  . PHE   A 1 140 ? -12.88288 6.84690  -27.31470 1.000 45.89540  ? 140 PHE   A CA  1 
ATOM   1080 C C   . PHE   A 1 140 ? -14.35680 6.54813  -27.53858 1.000 47.39398  ? 140 PHE   A C   1 
ATOM   1081 O O   . PHE   A 1 140 ? -14.91944 6.92010  -28.57312 1.000 46.51454  ? 140 PHE   A O   1 
ATOM   1082 C CB  . PHE   A 1 140 ? -12.69569 8.33357  -26.99253 1.000 42.22958  ? 140 PHE   A CB  1 
ATOM   1083 C CG  . PHE   A 1 140 ? -11.29363 8.69987  -26.59308 1.000 44.80213  ? 140 PHE   A CG  1 
ATOM   1084 C CD1 . PHE   A 1 140 ? -10.80737 8.37215  -25.33724 1.000 42.79776  ? 140 PHE   A CD1 1 
ATOM   1085 C CD2 . PHE   A 1 140 ? -10.46519 9.38228  -27.46966 1.000 44.02953  ? 140 PHE   A CD2 1 
ATOM   1086 C CE1 . PHE   A 1 140 ? -9.51940  8.71254  -24.96596 1.000 42.05237  ? 140 PHE   A CE1 1 
ATOM   1087 C CE2 . PHE   A 1 140 ? -9.17642  9.72588  -27.10439 1.000 41.76008  ? 140 PHE   A CE2 1 
ATOM   1088 C CZ  . PHE   A 1 140 ? -8.70351  9.39107  -25.85112 1.000 41.01702  ? 140 PHE   A CZ  1 
ATOM   1089 N N   . LEU   A 1 141 ? -14.97708 5.88667  -26.56622 1.000 45.79027  ? 141 LEU   A N   1 
ATOM   1090 C CA  . LEU   A 1 141 ? -16.41043 5.65280  -26.56278 1.000 43.90827  ? 141 LEU   A CA  1 
ATOM   1091 C C   . LEU   A 1 141 ? -17.09380 6.70523  -25.69296 1.000 46.42027  ? 141 LEU   A C   1 
ATOM   1092 O O   . LEU   A 1 141 ? -16.45812 7.61520  -25.15431 1.000 44.85997  ? 141 LEU   A O   1 
ATOM   1093 C CB  . LEU   A 1 141 ? -16.72479 4.24198  -26.06124 1.000 41.49010  ? 141 LEU   A CB  1 
ATOM   1094 C CG  . LEU   A 1 141 ? -16.34566 3.05154  -26.94481 1.000 54.30846  ? 141 LEU   A CG  1 
ATOM   1095 C CD1 . LEU   A 1 141 ? -17.27794 1.87988  -26.67432 1.000 61.87094  ? 141 LEU   A CD1 1 
ATOM   1096 C CD2 . LEU   A 1 141 ? -16.36907 3.42791  -28.41816 1.000 53.00243  ? 141 LEU   A CD2 1 
ATOM   1097 N N   . ASN   A 1 142 ? -18.41042 6.57861  -25.55469 1.000 44.95215  ? 142 ASN   A N   1 
ATOM   1098 C CA  . ASN   A 1 142 ? -19.14084 7.44075  -24.63737 1.000 43.26130  ? 142 ASN   A CA  1 
ATOM   1099 C C   . ASN   A 1 142 ? -18.72449 7.14650  -23.20157 1.000 45.33375  ? 142 ASN   A C   1 
ATOM   1100 O O   . ASN   A 1 142 ? -18.57734 5.98724  -22.80517 1.000 46.85601  ? 142 ASN   A O   1 
ATOM   1101 C CB  . ASN   A 1 142 ? -20.64715 7.24772  -24.80467 1.000 46.00997  ? 142 ASN   A CB  1 
ATOM   1102 C CG  . ASN   A 1 142 ? -21.21738 8.07836  -25.93634 1.000 46.36141  ? 142 ASN   A CG  1 
ATOM   1103 O OD1 . ASN   A 1 142 ? -21.81191 7.54790  -26.87402 1.000 46.43171  ? 142 ASN   A OD1 1 
ATOM   1104 N ND2 . ASN   A 1 142 ? -21.03685 9.39149  -25.85414 1.000 50.02058  ? 142 ASN   A ND2 1 
ATOM   1105 N N   . GLY   A 1 143 ? -18.52318 8.20776  -22.42164 1.000 44.54982  ? 143 GLY   A N   1 
ATOM   1106 C CA  . GLY   A 1 143 ? -18.05232 8.07980  -21.06048 1.000 44.20721  ? 143 GLY   A CA  1 
ATOM   1107 C C   . GLY   A 1 143 ? -16.54660 8.06057  -20.90545 1.000 41.79700  ? 143 GLY   A C   1 
ATOM   1108 O O   . GLY   A 1 143 ? -16.05632 8.06666  -19.76863 1.000 41.64076  ? 143 GLY   A O   1 
ATOM   1109 N N   . SER   A 1 144 ? -15.79774 8.03731  -22.00977 1.000 41.27741  ? 144 SER   A N   1 
ATOM   1110 C CA  . SER   A 1 144 ? -14.34174 8.07306  -21.95925 1.000 40.00677  ? 144 SER   A CA  1 
ATOM   1111 C C   . SER   A 1 144 ? -13.79698 9.41923  -21.50729 1.000 41.59944  ? 144 SER   A C   1 
ATOM   1112 O O   . SER   A 1 144 ? -12.60942 9.50183  -21.17404 1.000 40.24691  ? 144 SER   A O   1 
ATOM   1113 C CB  . SER   A 1 144 ? -13.76241 7.74171  -23.33222 1.000 39.93677  ? 144 SER   A CB  1 
ATOM   1114 O OG  . SER   A 1 144 ? -14.20559 8.68240  -24.29322 1.000 40.99610  ? 144 SER   A OG  1 
ATOM   1115 N N   . CYS   A 1 145 ? -14.62178 10.46555 -21.50125 1.000 42.71050  ? 145 CYS   A N   1 
ATOM   1116 C CA  . CYS   A 1 145 ? -14.14765 11.79197 -21.13388 1.000 42.23443  ? 145 CYS   A CA  1 
ATOM   1117 C C   . CYS   A 1 145 ? -13.58480 11.78210 -19.71901 1.000 44.38292  ? 145 CYS   A C   1 
ATOM   1118 O O   . CYS   A 1 145 ? -14.09956 11.09842 -18.82989 1.000 45.10702  ? 145 CYS   A O   1 
ATOM   1119 C CB  . CYS   A 1 145 ? -15.28107 12.80842 -21.25362 1.000 44.71029  ? 145 CYS   A CB  1 
ATOM   1120 S SG  . CYS   A 1 145 ? -15.61324 13.35051 -22.94468 1.000 52.25001  ? 145 CYS   A SG  1 
ATOM   1121 N N   . GLY   A 1 146 ? -12.51229 12.54243 -19.51860 1.000 43.10178  ? 146 GLY   A N   1 
ATOM   1122 C CA  . GLY   A 1 146 ? -11.73219 12.48745 -18.30838 1.000 43.18659  ? 146 GLY   A CA  1 
ATOM   1123 C C   . GLY   A 1 146 ? -10.48536 11.63756 -18.42011 1.000 42.11993  ? 146 GLY   A C   1 
ATOM   1124 O O   . GLY   A 1 146 ? -9.57825  11.77895 -17.59184 1.000 38.25458  ? 146 GLY   A O   1 
ATOM   1125 N N   . SER   A 1 147 ? -10.42568 10.75438 -19.41476 1.000 41.30635  ? 147 SER   A N   1 
ATOM   1126 C CA  . SER   A 1 147 ? -9.20672  10.00901 -19.68587 1.000 38.96862  ? 147 SER   A CA  1 
ATOM   1127 C C   . SER   A 1 147 ? -8.07192  10.97375 -20.00605 1.000 43.02567  ? 147 SER   A C   1 
ATOM   1128 O O   . SER   A 1 147 ? -8.27316  12.02322 -20.62397 1.000 41.33517  ? 147 SER   A O   1 
ATOM   1129 C CB  . SER   A 1 147 ? -9.42443  9.03880  -20.84626 1.000 39.87339  ? 147 SER   A CB  1 
ATOM   1130 O OG  . SER   A 1 147 ? -10.57074 8.23609  -20.62273 1.000 41.76671  ? 147 SER   A OG  1 
ATOM   1131 N N   . VAL   A 1 148 ? -6.86829  10.61699 -19.57098 1.000 43.36274  ? 148 VAL   A N   1 
ATOM   1132 C CA  . VAL   A 1 148 ? -5.73637  11.52937 -19.63458 1.000 43.67925  ? 148 VAL   A CA  1 
ATOM   1133 C C   . VAL   A 1 148 ? -4.65011  10.94782 -20.52734 1.000 42.88261  ? 148 VAL   A C   1 
ATOM   1134 O O   . VAL   A 1 148 ? -4.47421  9.72879  -20.62540 1.000 41.37552  ? 148 VAL   A O   1 
ATOM   1135 C CB  . VAL   A 1 148 ? -5.17914  11.84298 -18.22768 1.000 42.57249  ? 148 VAL   A CB  1 
ATOM   1136 C CG1 . VAL   A 1 148 ? -6.26698  12.44100 -17.35068 1.000 41.01147  ? 148 VAL   A CG1 1 
ATOM   1137 C CG2 . VAL   A 1 148 ? -4.60409  10.59045 -17.58542 1.000 44.06230  ? 148 VAL   A CG2 1 
ATOM   1138 N N   . GLY   A 1 149 ? -3.93336  11.84196 -21.19915 1.000 40.28273  ? 149 GLY   A N   1 
ATOM   1139 C CA  . GLY   A 1 149 ? -2.71962  11.49592 -21.90833 1.000 42.50277  ? 149 GLY   A CA  1 
ATOM   1140 C C   . GLY   A 1 149 ? -1.51987  11.92284 -21.08426 1.000 44.90163  ? 149 GLY   A C   1 
ATOM   1141 O O   . GLY   A 1 149 ? -1.58114  12.89806 -20.33874 1.000 41.97106  ? 149 GLY   A O   1 
ATOM   1142 N N   . PHE   A 1 150 ? -0.42173  11.18267 -21.21804 1.000 43.09746  ? 150 PHE   A N   1 
ATOM   1143 C CA  . PHE   A 1 150 ? 0.71074   11.41816 -20.33466 1.000 43.29014  ? 150 PHE   A CA  1 
ATOM   1144 C C   . PHE   A 1 150 ? 1.99550   10.89618 -20.96000 1.000 45.75634  ? 150 PHE   A C   1 
ATOM   1145 O O   . PHE   A 1 150 ? 1.98021   10.08429 -21.88911 1.000 43.98743  ? 150 PHE   A O   1 
ATOM   1146 C CB  . PHE   A 1 150 ? 0.49156   10.75919 -18.96866 1.000 41.17357  ? 150 PHE   A CB  1 
ATOM   1147 C CG  . PHE   A 1 150 ? 0.45570   9.25880  -19.02215 1.000 41.25850  ? 150 PHE   A CG  1 
ATOM   1148 C CD1 . PHE   A 1 150 ? -0.70016  8.59393  -19.39626 1.000 41.18028  ? 150 PHE   A CD1 1 
ATOM   1149 C CD2 . PHE   A 1 150 ? 1.57738   8.51291  -18.69987 1.000 41.41379  ? 150 PHE   A CD2 1 
ATOM   1150 C CE1 . PHE   A 1 150 ? -0.73780  7.21489  -19.44882 1.000 41.61540  ? 150 PHE   A CE1 1 
ATOM   1151 C CE2 . PHE   A 1 150 ? 1.54641   7.13222  -18.75014 1.000 42.87504  ? 150 PHE   A CE2 1 
ATOM   1152 C CZ  . PHE   A 1 150 ? 0.38637   6.48231  -19.12474 1.000 43.00395  ? 150 PHE   A CZ  1 
ATOM   1153 N N   . ASN   A 1 151 ? 3.11072   11.38693 -20.42344 1.000 40.92325  ? 151 ASN   A N   1 
ATOM   1154 C CA  . ASN   A 1 151 ? 4.43610   10.83784 -20.65724 1.000 44.70656  ? 151 ASN   A CA  1 
ATOM   1155 C C   . ASN   A 1 151 ? 5.11043   10.64385 -19.30707 1.000 50.28012  ? 151 ASN   A C   1 
ATOM   1156 O O   . ASN   A 1 151 ? 4.80497   11.35197 -18.34374 1.000 50.30240  ? 151 ASN   A O   1 
ATOM   1157 C CB  . ASN   A 1 151 ? 5.28796   11.75809 -21.53907 1.000 46.00476  ? 151 ASN   A CB  1 
ATOM   1158 C CG  . ASN   A 1 151 ? 4.86015   11.73632 -22.99028 1.000 45.94028  ? 151 ASN   A CG  1 
ATOM   1159 O OD1 . ASN   A 1 151 ? 4.05545   12.56080 -23.42471 1.000 47.70832  ? 151 ASN   A OD1 1 
ATOM   1160 N ND2 . ASN   A 1 151 ? 5.40115   10.79490 -23.75164 1.000 43.77088  ? 151 ASN   A ND2 1 
ATOM   1161 N N   . ILE   A 1 152 ? 6.03467   9.68748  -19.23975 1.000 47.74295  ? 152 ILE   A N   1 
ATOM   1162 C CA  . ILE   A 1 152 ? 6.72098   9.34345  -17.99912 1.000 54.72438  ? 152 ILE   A CA  1 
ATOM   1163 C C   . ILE   A 1 152 ? 8.20899   9.63220  -18.15411 1.000 62.53743  ? 152 ILE   A C   1 
ATOM   1164 O O   . ILE   A 1 152 ? 8.83385   9.20931  -19.13513 1.000 59.72782  ? 152 ILE   A O   1 
ATOM   1165 C CB  . ILE   A 1 152 ? 6.48617   7.87364  -17.60469 1.000 51.59665  ? 152 ILE   A CB  1 
ATOM   1166 C CG1 . ILE   A 1 152 ? 4.98812   7.55508  -17.59049 1.000 47.61794  ? 152 ILE   A CG1 1 
ATOM   1167 C CG2 . ILE   A 1 152 ? 7.11025   7.58246  -16.25145 1.000 57.59295  ? 152 ILE   A CG2 1 
ATOM   1168 C CD1 . ILE   A 1 152 ? 4.64053   6.27103  -16.85947 1.000 44.87176  ? 152 ILE   A CD1 1 
ATOM   1169 N N   . ASP   A 1 153 ? 8.76520   10.35910 -17.18472 1.000 64.11772  ? 153 ASP   A N   1 
ATOM   1170 C CA  . ASP   A 1 153 ? 10.18947  10.67161 -17.10260 1.000 66.17240  ? 153 ASP   A CA  1 
ATOM   1171 C C   . ASP   A 1 153 ? 10.66347  9.96774  -15.83277 1.000 71.61965  ? 153 ASP   A C   1 
ATOM   1172 O O   . ASP   A 1 153 ? 10.42980  10.45652 -14.72232 1.000 74.22301  ? 153 ASP   A O   1 
ATOM   1173 C CB  . ASP   A 1 153 ? 10.40975  12.19666 -17.07924 1.000 71.33846  ? 153 ASP   A CB  1 
ATOM   1174 C CG  . ASP   A 1 153 ? 11.86349  12.60989 -16.79602 1.000 90.12509  ? 153 ASP   A CG  1 
ATOM   1175 O OD1 . ASP   A 1 153 ? 12.60513  11.90282 -16.08844 1.000 92.17822  ? 153 ASP   A OD1 1 
ATOM   1176 O OD2 . ASP   A 1 153 ? 12.28326  13.66452 -17.31313 1.000 109.32252 ? 153 ASP   A OD2 1 
ATOM   1177 N N   . TYR   A 1 154 ? 11.28734  8.80050  -16.00105 1.000 71.54402  ? 154 TYR   A N   1 
ATOM   1178 C CA  . TYR   A 1 154 ? 11.84222  8.03893  -14.88743 1.000 72.34040  ? 154 TYR   A CA  1 
ATOM   1179 C C   . TYR   A 1 154 ? 10.79366  7.75906  -13.81504 1.000 67.22412  ? 154 TYR   A C   1 
ATOM   1180 O O   . TYR   A 1 154 ? 10.22894  6.66140  -13.75430 1.000 76.12290  ? 154 TYR   A O   1 
ATOM   1181 C CB  . TYR   A 1 154 ? 13.03568  8.78882  -14.28997 1.000 79.61220  ? 154 TYR   A CB  1 
ATOM   1182 C CG  . TYR   A 1 154 ? 13.69679  8.09145  -13.12670 1.000 90.20571  ? 154 TYR   A CG  1 
ATOM   1183 C CD1 . TYR   A 1 154 ? 13.93322  6.72391  -13.15405 1.000 86.12549  ? 154 TYR   A CD1 1 
ATOM   1184 C CD2 . TYR   A 1 154 ? 14.08917  8.80390  -12.00086 1.000 94.85674  ? 154 TYR   A CD2 1 
ATOM   1185 C CE1 . TYR   A 1 154 ? 14.53929  6.08429  -12.09175 1.000 89.64357  ? 154 TYR   A CE1 1 
ATOM   1186 C CE2 . TYR   A 1 154 ? 14.69578  8.17427  -10.93339 1.000 90.33910  ? 154 TYR   A CE2 1 
ATOM   1187 C CZ  . TYR   A 1 154 ? 14.91892  6.81331  -10.98335 1.000 92.90151  ? 154 TYR   A CZ  1 
ATOM   1188 O OH  . TYR   A 1 154 ? 15.52352  6.17624  -9.92336  1.000 92.54304  ? 154 TYR   A OH  1 
ATOM   1189 N N   . ASP   A 1 155 ? 10.52687  8.75152  -12.96516 1.000 75.94087  ? 155 ASP   A N   1 
ATOM   1190 C CA  . ASP   A 1 155 ? 9.54302   8.62276  -11.90266 1.000 72.33022  ? 155 ASP   A CA  1 
ATOM   1191 C C   . ASP   A 1 155 ? 8.43623   9.66475  -11.96356 1.000 64.77430  ? 155 ASP   A C   1 
ATOM   1192 O O   . ASP   A 1 155 ? 7.43874   9.52012  -11.24734 1.000 57.03248  ? 155 ASP   A O   1 
ATOM   1193 C CB  . ASP   A 1 155 ? 10.22526  8.71105  -10.52855 1.000 69.86209  ? 155 ASP   A CB  1 
ATOM   1194 C CG  . ASP   A 1 155 ? 10.91019  10.04607 -10.30342 1.000 69.35146  ? 155 ASP   A CG  1 
ATOM   1195 O OD1 . ASP   A 1 155 ? 11.44290  10.62128 -11.27701 1.000 71.68501  ? 155 ASP   A OD1 1 
ATOM   1196 O OD2 . ASP   A 1 155 ? 10.91053  10.52189 -9.14848  1.000 68.51782  ? 155 ASP   A OD2 1 
ATOM   1197 N N   . CYS   A 1 156 ? 8.57540   10.70011 -12.78730 1.000 68.57316  ? 156 CYS   A N   1 
ATOM   1198 C CA  . CYS   A 1 156 ? 7.62262   11.80150 -12.83627 1.000 61.06946  ? 156 CYS   A CA  1 
ATOM   1199 C C   . CYS   A 1 156 ? 6.65089   11.58480 -13.99039 1.000 57.90140  ? 156 CYS   A C   1 
ATOM   1200 O O   . CYS   A 1 156 ? 7.07348   11.41871 -15.13989 1.000 59.00212  ? 156 CYS   A O   1 
ATOM   1201 C CB  . CYS   A 1 156 ? 8.34912   13.13774 -12.98680 1.000 60.68086  ? 156 CYS   A CB  1 
ATOM   1202 S SG  . CYS   A 1 156 ? 7.29251   14.50623 -13.50316 1.000 60.25023  ? 156 CYS   A SG  1 
ATOM   1203 N N   . VAL   A 1 157 ? 5.35688   11.59097 -13.68287 1.000 55.73323  ? 157 VAL   A N   1 
ATOM   1204 C CA  . VAL   A 1 157 ? 4.31235   11.42821 -14.68855 1.000 53.17912  ? 157 VAL   A CA  1 
ATOM   1205 C C   . VAL   A 1 157 ? 3.92718   12.80542 -15.21290 1.000 50.35188  ? 157 VAL   A C   1 
ATOM   1206 O O   . VAL   A 1 157 ? 3.40606   13.63932 -14.46591 1.000 51.01699  ? 157 VAL   A O   1 
ATOM   1207 C CB  . VAL   A 1 157 ? 3.08920   10.70178 -14.11022 1.000 50.40350  ? 157 VAL   A CB  1 
ATOM   1208 C CG1 . VAL   A 1 157 ? 2.00392   10.57220 -15.17091 1.000 48.57804  ? 157 VAL   A CG1 1 
ATOM   1209 C CG2 . VAL   A 1 157 ? 3.48389   9.33701  -13.56545 1.000 50.84514  ? 157 VAL   A CG2 1 
ATOM   1210 N N   . SER   A 1 158 ? 4.16807   13.04294 -16.49894 1.000 47.46046  ? 158 SER   A N   1 
ATOM   1211 C CA  . SER   A 1 158 ? 3.88331   14.33349 -17.12401 1.000 48.95378  ? 158 SER   A CA  1 
ATOM   1212 C C   . SER   A 1 158 ? 2.52938   14.25210 -17.82165 1.000 47.29743  ? 158 SER   A C   1 
ATOM   1213 O O   . SER   A 1 158 ? 2.42227   13.73246 -18.93499 1.000 48.38977  ? 158 SER   A O   1 
ATOM   1214 C CB  . SER   A 1 158 ? 4.99073   14.71878 -18.09874 1.000 47.87534  ? 158 SER   A CB  1 
ATOM   1215 O OG  . SER   A 1 158 ? 6.18729   15.03138 -17.40824 1.000 56.87092  ? 158 SER   A OG  1 
ATOM   1216 N N   . PHE   A 1 159 ? 1.49556   14.77354 -17.16462 1.000 44.02370  ? 159 PHE   A N   1 
ATOM   1217 C CA  . PHE   A 1 159 ? 0.16666   14.82972 -17.75771 1.000 43.34970  ? 159 PHE   A CA  1 
ATOM   1218 C C   . PHE   A 1 159 ? 0.09228   15.99224 -18.74010 1.000 43.66029  ? 159 PHE   A C   1 
ATOM   1219 O O   . PHE   A 1 159 ? 0.52488   17.10692 -18.42972 1.000 44.36703  ? 159 PHE   A O   1 
ATOM   1220 C CB  . PHE   A 1 159 ? -0.90082  14.98072 -16.67319 1.000 43.22969  ? 159 PHE   A CB  1 
ATOM   1221 C CG  . PHE   A 1 159 ? -0.98519  13.80994 -15.73018 1.000 41.92310  ? 159 PHE   A CG  1 
ATOM   1222 C CD1 . PHE   A 1 159 ? -1.65392  12.65258 -16.09598 1.000 40.43093  ? 159 PHE   A CD1 1 
ATOM   1223 C CD2 . PHE   A 1 159 ? -0.40440  13.87207 -14.47338 1.000 43.90195  ? 159 PHE   A CD2 1 
ATOM   1224 C CE1 . PHE   A 1 159 ? -1.73590  11.57645 -15.22847 1.000 43.23066  ? 159 PHE   A CE1 1 
ATOM   1225 C CE2 . PHE   A 1 159 ? -0.48304  12.79903 -13.60112 1.000 44.31245  ? 159 PHE   A CE2 1 
ATOM   1226 C CZ  . PHE   A 1 159 ? -1.15020  11.65069 -13.97917 1.000 42.31357  ? 159 PHE   A CZ  1 
ATOM   1227 N N   . CYS   A 1 160 ? -0.46025  15.73245 -19.92707 1.000 42.01644  ? 160 CYS   A N   1 
ATOM   1228 C CA  . CYS   A 1 160 ? -0.51392  16.73711 -20.97969 1.000 43.73178  ? 160 CYS   A CA  1 
ATOM   1229 C C   . CYS   A 1 160 ? -1.85553  16.83942 -21.69056 1.000 43.80492  ? 160 CYS   A C   1 
ATOM   1230 O O   . CYS   A 1 160 ? -2.07156  17.82298 -22.40681 1.000 44.31546  ? 160 CYS   A O   1 
ATOM   1231 C CB  . CYS   A 1 160 ? 0.57237   16.46806 -22.03374 1.000 44.49089  ? 160 CYS   A CB  1 
ATOM   1232 S SG  . CYS   A 1 160 ? 0.38344   14.90393 -22.92950 1.000 45.58370  ? 160 CYS   A SG  1 
ATOM   1233 N N   . TYR   A 1 161 ? -2.75805  15.87610 -21.52258 1.000 43.59611  ? 161 TYR   A N   1 
ATOM   1234 C CA  . TYR   A 1 161 ? -3.98342  15.85495 -22.30613 1.000 44.46326  ? 161 TYR   A CA  1 
ATOM   1235 C C   . TYR   A 1 161 ? -5.12223  15.29710 -21.46743 1.000 42.25764  ? 161 TYR   A C   1 
ATOM   1236 O O   . TYR   A 1 161 ? -4.91951  14.43122 -20.61296 1.000 39.97099  ? 161 TYR   A O   1 
ATOM   1237 C CB  . TYR   A 1 161 ? -3.80392  15.02409 -23.58465 1.000 42.78275  ? 161 TYR   A CB  1 
ATOM   1238 C CG  . TYR   A 1 161 ? -5.04470  14.90990 -24.44249 1.000 40.59879  ? 161 TYR   A CG  1 
ATOM   1239 C CD1 . TYR   A 1 161 ? -5.33066  15.86361 -25.40866 1.000 40.51901  ? 161 TYR   A CD1 1 
ATOM   1240 C CD2 . TYR   A 1 161 ? -5.92010  13.84007 -24.29883 1.000 40.95219  ? 161 TYR   A CD2 1 
ATOM   1241 C CE1 . TYR   A 1 161 ? -6.45632  15.76328 -26.20002 1.000 40.36647  ? 161 TYR   A CE1 1 
ATOM   1242 C CE2 . TYR   A 1 161 ? -7.05049  13.73224 -25.08541 1.000 37.49803  ? 161 TYR   A CE2 1 
ATOM   1243 C CZ  . TYR   A 1 161 ? -7.31455  14.69706 -26.03379 1.000 39.94019  ? 161 TYR   A CZ  1 
ATOM   1244 O OH  . TYR   A 1 161 ? -8.43907  14.59377 -26.82077 1.000 39.64214  ? 161 TYR   A OH  1 
ATOM   1245 N N   . MET   A 1 162 ? -6.32387  15.80898 -21.72300 1.000 44.24563  ? 162 MET   A N   1 
ATOM   1246 C CA  . MET   A 1 162 ? -7.54260  15.27988 -21.12859 1.000 43.57268  ? 162 MET   A CA  1 
ATOM   1247 C C   . MET   A 1 162 ? -8.63009  15.29179 -22.18939 1.000 41.47386  ? 162 MET   A C   1 
ATOM   1248 O O   . MET   A 1 162 ? -8.88712  16.33124 -22.80369 1.000 40.90829  ? 162 MET   A O   1 
ATOM   1249 C CB  . MET   A 1 162 ? -7.97300  16.09324 -19.90439 1.000 42.45161  ? 162 MET   A CB  1 
ATOM   1250 C CG  . MET   A 1 162 ? -8.50403  15.22863 -18.77898 1.000 47.19568  ? 162 MET   A CG  1 
ATOM   1251 S SD  . MET   A 1 162 ? -9.60402  16.06919 -17.63121 1.000 49.79365  ? 162 MET   A SD  1 
ATOM   1252 C CE  . MET   A 1 162 ? -9.59154  14.86909 -16.30511 1.000 43.72199  ? 162 MET   A CE  1 
ATOM   1253 N N   . HIS   A 1 163 ? -9.26366  14.14168 -22.40212 1.000 40.48213  ? 163 HIS   A N   1 
ATOM   1254 C CA  . HIS   A 1 163 ? -10.19258 13.99035 -23.51248 1.000 41.64425  ? 163 HIS   A CA  1 
ATOM   1255 C C   . HIS   A 1 163 ? -11.51308 14.69463 -23.22899 1.000 41.42724  ? 163 HIS   A C   1 
ATOM   1256 O O   . HIS   A 1 163 ? -12.04899 14.62748 -22.11889 1.000 38.90620  ? 163 HIS   A O   1 
ATOM   1257 C CB  . HIS   A 1 163 ? -10.44274 12.51339 -23.80927 1.000 38.15931  ? 163 HIS   A CB  1 
ATOM   1258 C CG  . HIS   A 1 163 ? -11.31510 12.28680 -25.00249 1.000 39.32228  ? 163 HIS   A CG  1 
ATOM   1259 N ND1 . HIS   A 1 163 ? -10.98491 12.74662 -26.25887 1.000 35.55035  ? 163 HIS   A ND1 1 
ATOM   1260 C CD2 . HIS   A 1 163 ? -12.50716 11.65849 -25.13222 1.000 39.39394  ? 163 HIS   A CD2 1 
ATOM   1261 C CE1 . HIS   A 1 163 ? -11.93503 12.40932 -27.11191 1.000 41.68059  ? 163 HIS   A CE1 1 
ATOM   1262 N NE2 . HIS   A 1 163 ? -12.86996 11.74774 -26.45416 1.000 42.38133  ? 163 HIS   A NE2 1 
ATOM   1263 N N   . HIS   A 1 164 ? -12.03779 15.35871 -24.24962 1.000 42.56395  ? 164 HIS   A N   1 
ATOM   1264 C CA  . HIS   A 1 164 ? -13.23841 16.18173 -24.15918 1.000 44.20786  ? 164 HIS   A CA  1 
ATOM   1265 C C   . HIS   A 1 164 ? -14.24220 15.90943 -25.26873 1.000 45.92382  ? 164 HIS   A C   1 
ATOM   1266 O O   . HIS   A 1 164 ? -15.44819 15.90059 -25.00843 1.000 44.88274  ? 164 HIS   A O   1 
ATOM   1267 C CB  . HIS   A 1 164 ? -12.85198 17.67380 -24.19503 1.000 42.08737  ? 164 HIS   A CB  1 
ATOM   1268 C CG  . HIS   A 1 164 ? -12.65228 18.29091 -22.84558 1.000 45.10472  ? 164 HIS   A CG  1 
ATOM   1269 N ND1 . HIS   A 1 164 ? -11.44925 18.24111 -22.17417 1.000 44.84420  ? 164 HIS   A ND1 1 
ATOM   1270 C CD2 . HIS   A 1 164 ? -13.49475 18.99740 -22.05507 1.000 43.23970  ? 164 HIS   A CD2 1 
ATOM   1271 C CE1 . HIS   A 1 164 ? -11.56350 18.87782 -21.02230 1.000 41.61302  ? 164 HIS   A CE1 1 
ATOM   1272 N NE2 . HIS   A 1 164 ? -12.79465 19.34658 -20.92578 1.000 44.10604  ? 164 HIS   A NE2 1 
ATOM   1273 N N   . MET   A 1 165 ? -13.77931 15.68279 -26.49669 1.000 41.53863  ? 165 MET   A N   1 
ATOM   1274 C CA  . MET   A 1 165 ? -14.64286 15.82648 -27.65778 1.000 44.50946  ? 165 MET   A CA  1 
ATOM   1275 C C   . MET   A 1 165 ? -14.17405 14.93212 -28.79563 1.000 47.89408  ? 165 MET   A C   1 
ATOM   1276 O O   . MET   A 1 165 ? -12.98786 14.61123 -28.90932 1.000 46.52647  ? 165 MET   A O   1 
ATOM   1277 C CB  . MET   A 1 165 ? -14.65853 17.28433 -28.12622 1.000 45.22658  ? 165 MET   A CB  1 
ATOM   1278 C CG  . MET   A 1 165 ? -15.92351 17.73084 -28.82219 1.000 50.17736  ? 165 MET   A CG  1 
ATOM   1279 S SD  . MET   A 1 165 ? -15.96833 19.52711 -28.96269 1.000 62.87927  ? 165 MET   A SD  1 
ATOM   1280 C CE  . MET   A 1 165 ? -14.21928 19.92484 -28.93133 1.000 44.60490  ? 165 MET   A CE  1 
ATOM   1281 N N   . GLU   A 1 166 ? -15.12229 14.54715 -29.64683 1.000 44.81000  ? 166 GLU   A N   1 
ATOM   1282 C CA  . GLU   A 1 166 ? -14.83232 13.91075 -30.92408 1.000 44.99235  ? 166 GLU   A CA  1 
ATOM   1283 C C   . GLU   A 1 166 ? -15.37605 14.79112 -32.03827 1.000 44.61562  ? 166 GLU   A C   1 
ATOM   1284 O O   . GLU   A 1 166 ? -16.53925 15.20526 -31.99499 1.000 45.17182  ? 166 GLU   A O   1 
ATOM   1285 C CB  . GLU   A 1 166 ? -15.44170 12.50990 -31.01577 1.000 44.27839  ? 166 GLU   A CB  1 
ATOM   1286 C CG  . GLU   A 1 166 ? -15.13782 11.81056 -32.33316 1.000 46.57497  ? 166 GLU   A CG  1 
ATOM   1287 C CD  . GLU   A 1 166 ? -15.75102 10.42862 -32.42601 1.000 51.72091  ? 166 GLU   A CD  1 
ATOM   1288 O OE1 . GLU   A 1 166 ? -15.65880 9.66608  -31.44074 1.000 51.17863  ? 166 GLU   A OE1 1 
ATOM   1289 O OE2 . GLU   A 1 166 ? -16.32515 10.10587 -33.48735 1.000 53.71789  ? 166 GLU   A OE2 1 
ATOM   1290 N N   . LEU   A 1 167 ? -14.53702 15.07774 -33.02531 1.000 42.38894  ? 167 LEU   A N   1 
ATOM   1291 C CA  . LEU   A 1 167 ? -14.93326 15.93944 -34.12430 1.000 42.48465  ? 167 LEU   A CA  1 
ATOM   1292 C C   . LEU   A 1 167 ? -15.75596 15.16022 -35.14558 1.000 42.02652  ? 167 LEU   A C   1 
ATOM   1293 O O   . LEU   A 1 167 ? -15.70223 13.92883 -35.18889 1.000 44.97821  ? 167 LEU   A O   1 
ATOM   1294 C CB  . LEU   A 1 167 ? -13.69913 16.54789 -34.78526 1.000 45.27323  ? 167 LEU   A CB  1 
ATOM   1295 C CG  . LEU   A 1 167 ? -13.00326 17.68686 -34.03222 1.000 43.95082  ? 167 LEU   A CG  1 
ATOM   1296 C CD1 . LEU   A 1 167 ? -14.02324 18.60929 -33.37618 1.000 42.01529  ? 167 LEU   A CD1 1 
ATOM   1297 C CD2 . LEU   A 1 167 ? -12.01228 17.15252 -33.00709 1.000 43.12139  ? 167 LEU   A CD2 1 
ATOM   1298 N N   . PRO   A 1 168 ? -16.54364 15.85882 -35.97073 1.000 45.29565  ? 168 PRO   A N   1 
ATOM   1299 C CA  . PRO   A 1 168 ? -17.35161 15.16052 -36.98592 1.000 44.51285  ? 168 PRO   A CA  1 
ATOM   1300 C C   . PRO   A 1 168 ? -16.55817 14.22671 -37.88487 1.000 45.94362  ? 168 PRO   A C   1 
ATOM   1301 O O   . PRO   A 1 168 ? -17.12938 13.27142 -38.42699 1.000 46.22123  ? 168 PRO   A O   1 
ATOM   1302 C CB  . PRO   A 1 168 ? -17.96479 16.31607 -37.78507 1.000 41.93337  ? 168 PRO   A CB  1 
ATOM   1303 C CG  . PRO   A 1 168 ? -18.08611 17.41828 -36.79652 1.000 45.38978  ? 168 PRO   A CG  1 
ATOM   1304 C CD  . PRO   A 1 168 ? -16.92286 17.27844 -35.84647 1.000 43.24044  ? 168 PRO   A CD  1 
ATOM   1305 N N   . THR   A 1 169 ? -15.25995 14.46441 -38.05865 1.000 42.69369  ? 169 THR   A N   1 
ATOM   1306 C CA  . THR   A 1 169 ? -14.44339 13.62203 -38.92215 1.000 45.02366  ? 169 THR   A CA  1 
ATOM   1307 C C   . THR   A 1 169 ? -13.93582 12.36395 -38.22873 1.000 47.00775  ? 169 THR   A C   1 
ATOM   1308 O O   . THR   A 1 169 ? -13.28456 11.54136 -38.88069 1.000 49.39769  ? 169 THR   A O   1 
ATOM   1309 C CB  . THR   A 1 169 ? -13.25743 14.42107 -39.46865 1.000 48.11275  ? 169 THR   A CB  1 
ATOM   1310 O OG1 . THR   A 1 169 ? -12.38258 14.78286 -38.39270 1.000 48.13239  ? 169 THR   A OG1 1 
ATOM   1311 C CG2 . THR   A 1 169 ? -13.74455 15.68119 -40.16904 1.000 51.11350  ? 169 THR   A CG2 1 
ATOM   1312 N N   . GLY   A 1 170 ? -14.21390 12.18721 -36.93848 1.000 44.81989  ? 170 GLY   A N   1 
ATOM   1313 C CA  . GLY   A 1 170 ? -13.79584 11.01409 -36.20827 1.000 44.68143  ? 170 GLY   A CA  1 
ATOM   1314 C C   . GLY   A 1 170 ? -12.58219 11.21486 -35.32393 1.000 45.71250  ? 170 GLY   A C   1 
ATOM   1315 O O   . GLY   A 1 170 ? -12.34297 10.39249 -34.43172 1.000 47.55467  ? 170 GLY   A O   1 
ATOM   1316 N N   . VAL   A 1 171 ? -11.81047 12.27883 -35.54606 1.000 44.83710  ? 171 VAL   A N   1 
ATOM   1317 C CA  . VAL   A 1 171 ? -10.66117 12.58441 -34.70080 1.000 43.31284  ? 171 VAL   A CA  1 
ATOM   1318 C C   . VAL   A 1 171 ? -11.16612 13.13668 -33.37442 1.000 42.09030  ? 171 VAL   A C   1 
ATOM   1319 O O   . VAL   A 1 171 ? -12.37383 13.32100 -33.18696 1.000 41.64121  ? 171 VAL   A O   1 
ATOM   1320 C CB  . VAL   A 1 171 ? -9.69820  13.56957 -35.38873 1.000 43.20030  ? 171 VAL   A CB  1 
ATOM   1321 C CG1 . VAL   A 1 171 ? -9.29334  13.04604 -36.75878 1.000 44.82784  ? 171 VAL   A CG1 1 
ATOM   1322 C CG2 . VAL   A 1 171 ? -10.33357 14.94525 -35.50247 1.000 41.22325  ? 171 VAL   A CG2 1 
ATOM   1323 N N   . HIS   A 1 172 ? -10.25213 13.40996 -32.44688 1.000 40.55700  ? 172 HIS   A N   1 
ATOM   1324 C CA  . HIS   A 1 172 ? -10.62375 13.78836 -31.09284 1.000 41.08836  ? 172 HIS   A CA  1 
ATOM   1325 C C   . HIS   A 1 172 ? -9.86534  15.03600 -30.66380 1.000 40.60751  ? 172 HIS   A C   1 
ATOM   1326 O O   . HIS   A 1 172 ? -8.74790  15.29346 -31.11901 1.000 43.84339  ? 172 HIS   A O   1 
ATOM   1327 C CB  . HIS   A 1 172 ? -10.35997 12.63747 -30.11604 1.000 40.90108  ? 172 HIS   A CB  1 
ATOM   1328 C CG  . HIS   A 1 172 ? -11.02880 11.35610 -30.50804 1.000 45.04206  ? 172 HIS   A CG  1 
ATOM   1329 N ND1 . HIS   A 1 172 ? -10.36169 10.33251 -31.14660 1.000 44.43377  ? 172 HIS   A ND1 1 
ATOM   1330 C CD2 . HIS   A 1 172 ? -12.30921 10.93828 -30.36505 1.000 46.32327  ? 172 HIS   A CD2 1 
ATOM   1331 C CE1 . HIS   A 1 172 ? -11.20033 9.33725  -31.37394 1.000 44.90455  ? 172 HIS   A CE1 1 
ATOM   1332 N NE2 . HIS   A 1 172 ? -12.38858 9.67919  -30.90907 1.000 47.59129  ? 172 HIS   A NE2 1 
ATOM   1333 N N   . ALA   A 1 173 ? -10.49378 15.81272 -29.78318 1.000 40.22553  ? 173 ALA   A N   1 
ATOM   1334 C CA  . ALA   A 1 173 ? -9.92947  17.05387 -29.27677 1.000 38.54103  ? 173 ALA   A CA  1 
ATOM   1335 C C   . ALA   A 1 173 ? -10.07859 17.10748 -27.76420 1.000 38.55764  ? 173 ALA   A C   1 
ATOM   1336 O O   . ALA   A 1 173 ? -11.04954 16.59581 -27.19969 1.000 40.03983  ? 173 ALA   A O   1 
ATOM   1337 C CB  . ALA   A 1 173 ? -10.60425 18.27986 -29.90161 1.000 37.37722  ? 173 ALA   A CB  1 
ATOM   1338 N N   . GLY   A 1 174 ? -9.10925  17.73929 -27.11453 1.000 40.38239  ? 174 GLY   A N   1 
ATOM   1339 C CA  . GLY   A 1 174 ? -9.13513  17.85289 -25.67612 1.000 41.46310  ? 174 GLY   A CA  1 
ATOM   1340 C C   . GLY   A 1 174 ? -8.33017  19.04009 -25.19992 1.000 40.64433  ? 174 GLY   A C   1 
ATOM   1341 O O   . GLY   A 1 174 ? -7.89665  19.88228 -25.98921 1.000 37.80678  ? 174 GLY   A O   1 
ATOM   1342 N N   . THR   A 1 175 ? -8.13521  19.09323 -23.88778 1.000 39.16929  ? 175 THR   A N   1 
ATOM   1343 C CA  . THR   A 1 175 ? -7.44912  20.19433 -23.23432 1.000 40.61538  ? 175 THR   A CA  1 
ATOM   1344 C C   . THR   A 1 175 ? -6.22824  19.67820 -22.48618 1.000 44.04656  ? 175 THR   A C   1 
ATOM   1345 O O   . THR   A 1 175 ? -6.03313  18.47124 -22.31608 1.000 41.99042  ? 175 THR   A O   1 
ATOM   1346 C CB  . THR   A 1 175 ? -8.37742  20.92123 -22.25295 1.000 41.93699  ? 175 THR   A CB  1 
ATOM   1347 O OG1 . THR   A 1 175 ? -8.56564  20.10692 -21.08861 1.000 40.20033  ? 175 THR   A OG1 1 
ATOM   1348 C CG2 . THR   A 1 175 ? -9.72775  21.19140 -22.89179 1.000 40.80573  ? 175 THR   A CG2 1 
ATOM   1349 N N   . ASP   A 1 176 ? -5.40215  20.61695 -22.03296 1.000 45.40316  ? 176 ASP   A N   1 
ATOM   1350 C CA  . ASP   A 1 176 ? -4.36531  20.30128 -21.06234 1.000 45.80670  ? 176 ASP   A CA  1 
ATOM   1351 C C   . ASP   A 1 176 ? -5.02127  20.20779 -19.68546 1.000 46.86889  ? 176 ASP   A C   1 
ATOM   1352 O O   . ASP   A 1 176 ? -6.24677  20.26546 -19.55105 1.000 43.29674  ? 176 ASP   A O   1 
ATOM   1353 C CB  . ASP   A 1 176 ? -3.23739  21.33107 -21.12463 1.000 45.95754  ? 176 ASP   A CB  1 
ATOM   1354 C CG  . ASP   A 1 176 ? -3.73127  22.76324 -20.99244 1.000 47.22199  ? 176 ASP   A CG  1 
ATOM   1355 O OD1 . ASP   A 1 176 ? -4.55698  23.04278 -20.09846 1.000 48.52126  ? 176 ASP   A OD1 1 
ATOM   1356 O OD2 . ASP   A 1 176 ? -3.28208  23.61803 -21.78517 1.000 46.96373  ? 176 ASP   A OD2 1 
ATOM   1357 N N   . LEU   A 1 177 ? -4.21822  20.07217 -18.63693 1.000 45.33913  ? 177 LEU   A N   1 
ATOM   1358 C CA  . LEU   A 1 177 ? -4.76094  19.93329 -17.29383 1.000 47.33657  ? 177 LEU   A CA  1 
ATOM   1359 C C   . LEU   A 1 177 ? -5.07252  21.27560 -16.63858 1.000 48.59449  ? 177 LEU   A C   1 
ATOM   1360 O O   . LEU   A 1 177 ? -5.33091  21.31757 -15.43147 1.000 47.38714  ? 177 LEU   A O   1 
ATOM   1361 C CB  . LEU   A 1 177 ? -3.80525  19.11978 -16.41765 1.000 48.68213  ? 177 LEU   A CB  1 
ATOM   1362 C CG  . LEU   A 1 177 ? -4.01640  17.60081 -16.45074 1.000 46.00488  ? 177 LEU   A CG  1 
ATOM   1363 C CD1 . LEU   A 1 177 ? -5.41455  17.24867 -15.95754 1.000 42.77314  ? 177 LEU   A CD1 1 
ATOM   1364 C CD2 . LEU   A 1 177 ? -3.76196  17.00966 -17.83544 1.000 44.58289  ? 177 LEU   A CD2 1 
ATOM   1365 N N   . GLU   A 1 178 ? -5.06139  22.36638 -17.40423 1.000 48.72336  ? 178 GLU   A N   1 
ATOM   1366 C CA  . GLU   A 1 178 ? -5.50739  23.66859 -16.92693 1.000 48.48681  ? 178 GLU   A CA  1 
ATOM   1367 C C   . GLU   A 1 178 ? -6.81374  24.10465 -17.57803 1.000 48.17848  ? 178 GLU   A C   1 
ATOM   1368 O O   . GLU   A 1 178 ? -7.22924  25.25524 -17.40488 1.000 50.00400  ? 178 GLU   A O   1 
ATOM   1369 C CB  . GLU   A 1 178 ? -4.42756  24.72554 -17.16879 1.000 51.96550  ? 178 GLU   A CB  1 
ATOM   1370 C CG  . GLU   A 1 178 ? -3.20637  24.59123 -16.27693 1.000 54.77361  ? 178 GLU   A CG  1 
ATOM   1371 C CD  . GLU   A 1 178 ? -2.15510  25.64185 -16.57640 1.000 58.01462  ? 178 GLU   A CD  1 
ATOM   1372 O OE1 . GLU   A 1 178 ? -2.36319  26.44234 -17.51311 1.000 59.11316  ? 178 GLU   A OE1 1 
ATOM   1373 O OE2 . GLU   A 1 178 ? -1.12401  25.67119 -15.87214 1.000 57.84589  ? 178 GLU   A OE2 1 
ATOM   1374 N N   . GLY   A 1 179 ? -7.46333  23.22018 -18.32947 1.000 48.55757  ? 179 GLY   A N   1 
ATOM   1375 C CA  . GLY   A 1 179 ? -8.70540  23.54455 -18.99720 1.000 46.93884  ? 179 GLY   A CA  1 
ATOM   1376 C C   . GLY   A 1 179 ? -8.56326  24.21643 -20.34289 1.000 45.59812  ? 179 GLY   A C   1 
ATOM   1377 O O   . GLY   A 1 179 ? -9.57823  24.62111 -20.92228 1.000 50.01572  ? 179 GLY   A O   1 
ATOM   1378 N N   . ASN   A 1 180 ? -7.34575  24.34499 -20.86255 1.000 43.19801  ? 180 ASN   A N   1 
ATOM   1379 C CA  . ASN   A 1 180 ? -7.09215  25.05387 -22.11007 1.000 43.70632  ? 180 ASN   A CA  1 
ATOM   1380 C C   . ASN   A 1 180 ? -7.07164  24.06039 -23.26547 1.000 43.27216  ? 180 ASN   A C   1 
ATOM   1381 O O   . ASN   A 1 180 ? -6.22642  23.15991 -23.30096 1.000 41.91419  ? 180 ASN   A O   1 
ATOM   1382 C CB  . ASN   A 1 180 ? -5.77323  25.82206 -22.03804 1.000 46.27046  ? 180 ASN   A CB  1 
ATOM   1383 C CG  . ASN   A 1 180 ? -5.81063  26.95156 -21.02654 1.000 48.47936  ? 180 ASN   A CG  1 
ATOM   1384 O OD1 . ASN   A 1 180 ? -6.80565  27.66759 -20.91312 1.000 47.91095  ? 180 ASN   A OD1 1 
ATOM   1385 N ND2 . ASN   A 1 180 ? -4.72183  27.11609 -20.28415 1.000 53.56762  ? 180 ASN   A ND2 1 
ATOM   1386 N N   . PHE   A 1 181 ? -7.99308  24.23607 -24.20947 1.000 42.33264  ? 181 PHE   A N   1 
ATOM   1387 C CA  . PHE   A 1 181 ? -8.09046  23.33716 -25.35109 1.000 41.00991  ? 181 PHE   A CA  1 
ATOM   1388 C C   . PHE   A 1 181 ? -6.84295  23.42166 -26.22308 1.000 43.84065  ? 181 PHE   A C   1 
ATOM   1389 O O   . PHE   A 1 181 ? -6.18112  24.45973 -26.30555 1.000 41.48777  ? 181 PHE   A O   1 
ATOM   1390 C CB  . PHE   A 1 181 ? -9.32342  23.67691 -26.19391 1.000 41.14487  ? 181 PHE   A CB  1 
ATOM   1391 C CG  . PHE   A 1 181 ? -10.50889 22.78877 -25.93422 1.000 43.36232  ? 181 PHE   A CG  1 
ATOM   1392 C CD1 . PHE   A 1 181 ? -10.58050 21.52313 -26.49468 1.000 43.42033  ? 181 PHE   A CD1 1 
ATOM   1393 C CD2 . PHE   A 1 181 ? -11.56073 23.22681 -25.14548 1.000 41.41552  ? 181 PHE   A CD2 1 
ATOM   1394 C CE1 . PHE   A 1 181 ? -11.67399 20.70537 -26.26170 1.000 44.88900  ? 181 PHE   A CE1 1 
ATOM   1395 C CE2 . PHE   A 1 181 ? -12.65498 22.41456 -24.90884 1.000 44.07056  ? 181 PHE   A CE2 1 
ATOM   1396 C CZ  . PHE   A 1 181 ? -12.71184 21.15261 -25.46774 1.000 45.08372  ? 181 PHE   A CZ  1 
ATOM   1397 N N   . TYR   A 1 182 ? -6.52377  22.30673 -26.87723 1.000 41.65627  ? 182 TYR   A N   1 
ATOM   1398 C CA  . TYR   A 1 182 ? -5.54486  22.28960 -27.95834 1.000 38.91450  ? 182 TYR   A CA  1 
ATOM   1399 C C   . TYR   A 1 182 ? -6.27762  22.63538 -29.24875 1.000 39.42244  ? 182 TYR   A C   1 
ATOM   1400 O O   . TYR   A 1 182 ? -7.13251  21.87146 -29.70713 1.000 42.46829  ? 182 TYR   A O   1 
ATOM   1401 C CB  . TYR   A 1 182 ? -4.86044  20.92924 -28.06696 1.000 40.26019  ? 182 TYR   A CB  1 
ATOM   1402 C CG  . TYR   A 1 182 ? -3.89594  20.60902 -26.94776 1.000 39.69652  ? 182 TYR   A CG  1 
ATOM   1403 C CD1 . TYR   A 1 182 ? -2.57798  21.04331 -26.99630 1.000 39.28007  ? 182 TYR   A CD1 1 
ATOM   1404 C CD2 . TYR   A 1 182 ? -4.29537  19.85146 -25.85550 1.000 37.71945  ? 182 TYR   A CD2 1 
ATOM   1405 C CE1 . TYR   A 1 182 ? -1.68848  20.74523 -25.98105 1.000 40.54817  ? 182 TYR   A CE1 1 
ATOM   1406 C CE2 . TYR   A 1 182 ? -3.41224  19.54820 -24.83522 1.000 39.09018  ? 182 TYR   A CE2 1 
ATOM   1407 C CZ  . TYR   A 1 182 ? -2.11005  19.99762 -24.90345 1.000 39.11486  ? 182 TYR   A CZ  1 
ATOM   1408 O OH  . TYR   A 1 182 ? -1.22455  19.69976 -23.89187 1.000 40.07147  ? 182 TYR   A OH  1 
ATOM   1409 N N   . GLY   A 1 183 ? -5.96219  23.79243 -29.82182 1.000 38.78924  ? 183 GLY   A N   1 
ATOM   1410 C CA  . GLY   A 1 183 ? -6.59210  24.22566 -31.04473 1.000 42.49389  ? 183 GLY   A CA  1 
ATOM   1411 C C   . GLY   A 1 183 ? -7.80113  25.10824 -30.79797 1.000 45.70488  ? 183 GLY   A C   1 
ATOM   1412 O O   . GLY   A 1 183 ? -8.11940  25.46414 -29.66016 1.000 41.94609  ? 183 GLY   A O   1 
ATOM   1413 N N   . PRO   A 1 184 ? -8.50108  25.47267 -31.88271 1.000 45.06243  ? 184 PRO   A N   1 
ATOM   1414 C CA  . PRO   A 1 184 ? -9.65224  26.39163 -31.78031 1.000 50.03494  ? 184 PRO   A CA  1 
ATOM   1415 C C   . PRO   A 1 184 ? -10.98156 25.67411 -31.58583 1.000 50.43054  ? 184 PRO   A C   1 
ATOM   1416 O O   . PRO   A 1 184 ? -11.94075 25.87881 -32.33880 1.000 57.29141  ? 184 PRO   A O   1 
ATOM   1417 C CB  . PRO   A 1 184 ? -9.59679  27.12483 -33.12995 1.000 46.39043  ? 184 PRO   A CB  1 
ATOM   1418 C CG  . PRO   A 1 184 ? -9.08228  26.07503 -34.08074 1.000 45.26238  ? 184 PRO   A CG  1 
ATOM   1419 C CD  . PRO   A 1 184 ? -8.20921  25.12004 -33.27854 1.000 43.69868  ? 184 PRO   A CD  1 
ATOM   1420 N N   . PHE   A 1 185 ? -11.05647 24.82908 -30.56256 1.000 49.45804  ? 185 PHE   A N   1 
ATOM   1421 C CA  . PHE   A 1 185 ? -12.24958 24.04811 -30.27970 1.000 48.11061  ? 185 PHE   A CA  1 
ATOM   1422 C C   . PHE   A 1 185 ? -12.86066 24.46477 -28.94777 1.000 48.60626  ? 185 PHE   A C   1 
ATOM   1423 O O   . PHE   A 1 185 ? -12.17948 24.98052 -28.05692 1.000 49.53972  ? 185 PHE   A O   1 
ATOM   1424 C CB  . PHE   A 1 185 ? -11.93092 22.54906 -30.26735 1.000 47.34263  ? 185 PHE   A CB  1 
ATOM   1425 C CG  . PHE   A 1 185 ? -11.16248 22.08455 -31.47240 1.000 47.50530  ? 185 PHE   A CG  1 
ATOM   1426 C CD1 . PHE   A 1 185 ? -11.75438 22.07029 -32.72493 1.000 44.22219  ? 185 PHE   A CD1 1 
ATOM   1427 C CD2 . PHE   A 1 185 ? -9.84804  21.66260 -31.35297 1.000 42.68794  ? 185 PHE   A CD2 1 
ATOM   1428 C CE1 . PHE   A 1 185 ? -11.04926 21.64329 -33.83653 1.000 46.80610  ? 185 PHE   A CE1 1 
ATOM   1429 C CE2 . PHE   A 1 185 ? -9.13788  21.23497 -32.45984 1.000 41.84460  ? 185 PHE   A CE2 1 
ATOM   1430 C CZ  . PHE   A 1 185 ? -9.73891  21.22517 -33.70308 1.000 44.92692  ? 185 PHE   A CZ  1 
ATOM   1431 N N   . VAL   A 1 186 ? -14.16825 24.23461 -28.82715 1.000 47.88358  ? 186 VAL   A N   1 
ATOM   1432 C CA  . VAL   A 1 186 ? -14.92108 24.53965 -27.61806 1.000 46.35386  ? 186 VAL   A CA  1 
ATOM   1433 C C   . VAL   A 1 186 ? -15.70784 23.30365 -27.20690 1.000 47.70089  ? 186 VAL   A C   1 
ATOM   1434 O O   . VAL   A 1 186 ? -16.10900 22.49096 -28.04606 1.000 48.17584  ? 186 VAL   A O   1 
ATOM   1435 C CB  . VAL   A 1 186 ? -15.86698 25.74751 -27.81231 1.000 47.71620  ? 186 VAL   A CB  1 
ATOM   1436 C CG1 . VAL   A 1 186 ? -15.07170 27.00340 -28.13866 1.000 43.98169  ? 186 VAL   A CG1 1 
ATOM   1437 C CG2 . VAL   A 1 186 ? -16.88270 25.45981 -28.90869 1.000 45.91864  ? 186 VAL   A CG2 1 
ATOM   1438 N N   . ASP   A 1 187 ? -15.92942 23.16596 -25.90064 1.000 44.61229  ? 187 ASP   A N   1 
ATOM   1439 C CA  . ASP   A 1 187 ? -16.65684 22.02334 -25.34794 1.000 45.15112  ? 187 ASP   A CA  1 
ATOM   1440 C C   . ASP   A 1 187 ? -18.15121 22.27134 -25.51954 1.000 46.24045  ? 187 ASP   A C   1 
ATOM   1441 O O   . ASP   A 1 187 ? -18.83293 22.76534 -24.62008 1.000 47.28641  ? 187 ASP   A O   1 
ATOM   1442 C CB  . ASP   A 1 187 ? -16.28825 21.80285 -23.88535 1.000 44.40646  ? 187 ASP   A CB  1 
ATOM   1443 C CG  . ASP   A 1 187 ? -16.20237 23.09704 -23.10238 1.000 46.80418  ? 187 ASP   A CG  1 
ATOM   1444 O OD1 . ASP   A 1 187 ? -16.37464 24.17437 -23.70959 1.000 47.95386  ? 187 ASP   A OD1 1 
ATOM   1445 O OD2 . ASP   A 1 187 ? -15.96216 23.03213 -21.87767 1.000 47.01505  ? 187 ASP   A OD2 1 
ATOM   1446 N N   . ARG   A 1 188 ? -18.66883 21.91349 -26.69411 1.000 46.42540  ? 188 ARG   A N   1 
ATOM   1447 C CA  . ARG   A 1 188 ? -20.07293 22.13294 -27.01930 1.000 47.77349  ? 188 ARG   A CA  1 
ATOM   1448 C C   . ARG   A 1 188 ? -20.45856 21.20600 -28.16103 1.000 48.90250  ? 188 ARG   A C   1 
ATOM   1449 O O   . ARG   A 1 188 ? -19.71967 21.09537 -29.14372 1.000 49.66046  ? 188 ARG   A O   1 
ATOM   1450 C CB  . ARG   A 1 188 ? -20.32033 23.59567 -27.40363 1.000 48.72570  ? 188 ARG   A CB  1 
ATOM   1451 C CG  . ARG   A 1 188 ? -21.73827 23.90559 -27.83706 1.000 52.69628  ? 188 ARG   A CG  1 
ATOM   1452 C CD  . ARG   A 1 188 ? -21.82387 25.29772 -28.44872 1.000 54.76770  ? 188 ARG   A CD  1 
ATOM   1453 N NE  . ARG   A 1 188 ? -22.87572 25.40017 -29.45382 1.000 55.29522  ? 188 ARG   A NE  1 
ATOM   1454 C CZ  . ARG   A 1 188 ? -23.30482 26.54187 -29.97538 1.000 58.12628  ? 188 ARG   A CZ  1 
ATOM   1455 N NH1 . ARG   A 1 188 ? -22.79540 27.70571 -29.60540 1.000 56.58470  ? 188 ARG   A NH1 1 
ATOM   1456 N NH2 . ARG   A 1 188 ? -24.26829 26.51540 -30.89235 1.000 56.91804  ? 188 ARG   A NH2 1 
ATOM   1457 N N   . GLN   A 1 189 ? -21.60704 20.54075 -28.02983 1.000 49.76169  ? 189 GLN   A N   1 
ATOM   1458 C CA  . GLN   A 1 189 ? -22.08310 19.61887 -29.06106 1.000 48.79128  ? 189 GLN   A CA  1 
ATOM   1459 C C   . GLN   A 1 189 ? -22.55447 20.43595 -30.26118 1.000 48.17661  ? 189 GLN   A C   1 
ATOM   1460 O O   . GLN   A 1 189 ? -23.74076 20.71996 -30.44393 1.000 46.15173  ? 189 GLN   A O   1 
ATOM   1461 C CB  . GLN   A 1 189 ? -23.19071 18.71956 -28.52306 1.000 49.42522  ? 189 GLN   A CB  1 
ATOM   1462 C CG  . GLN   A 1 189 ? -23.65583 17.65296 -29.50916 1.000 46.91326  ? 189 GLN   A CG  1 
ATOM   1463 C CD  . GLN   A 1 189 ? -24.78586 16.79905 -28.96442 1.000 47.24920  ? 189 GLN   A CD  1 
ATOM   1464 O OE1 . GLN   A 1 189 ? -24.85295 16.52937 -27.76578 1.000 49.43823  ? 189 GLN   A OE1 1 
ATOM   1465 N NE2 . GLN   A 1 189 ? -25.68286 16.37086 -29.84596 1.000 42.22959  ? 189 GLN   A NE2 1 
ATOM   1466 N N   . THR   A 1 190 ? -21.59191 20.82653 -31.09317 1.000 50.00013  ? 190 THR   A N   1 
ATOM   1467 C CA  . THR   A 1 190 ? -21.87817 21.56238 -32.31446 1.000 49.65945  ? 190 THR   A CA  1 
ATOM   1468 C C   . THR   A 1 190 ? -20.81218 21.22258 -33.34563 1.000 47.88044  ? 190 THR   A C   1 
ATOM   1469 O O   . THR   A 1 190 ? -19.70426 20.79949 -33.00557 1.000 45.81464  ? 190 THR   A O   1 
ATOM   1470 C CB  . THR   A 1 190 ? -21.93781 23.07648 -32.06609 1.000 51.06000  ? 190 THR   A CB  1 
ATOM   1471 O OG1 . THR   A 1 190 ? -22.44353 23.73623 -33.23342 1.000 48.78137  ? 190 THR   A OG1 1 
ATOM   1472 C CG2 . THR   A 1 190 ? -20.55649 23.62582 -31.73269 1.000 48.92942  ? 190 THR   A CG2 1 
ATOM   1473 N N   . ALA   A 1 191 ? -21.16401 21.40578 -34.61579 1.000 47.97966  ? 191 ALA   A N   1 
ATOM   1474 C CA  . ALA   A 1 191 ? -20.26497 21.04936 -35.70643 1.000 47.17023  ? 191 ALA   A CA  1 
ATOM   1475 C C   . ALA   A 1 191 ? -19.04396 21.95915 -35.69724 1.000 47.62791  ? 191 ALA   A C   1 
ATOM   1476 O O   . ALA   A 1 191 ? -19.17361 23.18695 -35.74601 1.000 48.36136  ? 191 ALA   A O   1 
ATOM   1477 C CB  . ALA   A 1 191 ? -20.99131 21.14171 -37.04431 1.000 45.64294  ? 191 ALA   A CB  1 
ATOM   1478 N N   . GLN   A 1 192 ? -17.85911 21.35612 -35.62668 1.000 45.98498  ? 192 GLN   A N   1 
ATOM   1479 C CA  . GLN   A 1 192 ? -16.60502 22.09118 -35.67097 1.000 49.11472  ? 192 GLN   A CA  1 
ATOM   1480 C C   . GLN   A 1 192 ? -15.64245 21.37603 -36.60598 1.000 50.01174  ? 192 GLN   A C   1 
ATOM   1481 O O   . GLN   A 1 192 ? -15.65350 20.14698 -36.71220 1.000 47.15198  ? 192 GLN   A O   1 
ATOM   1482 C CB  . GLN   A 1 192 ? -15.97598 22.23437 -34.27882 1.000 46.55205  ? 192 GLN   A CB  1 
ATOM   1483 C CG  . GLN   A 1 192 ? -16.85041 22.95789 -33.26742 1.000 42.32486  ? 192 GLN   A CG  1 
ATOM   1484 C CD  . GLN   A 1 192 ? -16.21365 23.02287 -31.89384 1.000 47.11718  ? 192 GLN   A CD  1 
ATOM   1485 O OE1 . GLN   A 1 192 ? -15.08089 23.48020 -31.74490 1.000 49.03686  ? 192 GLN   A OE1 1 
ATOM   1486 N NE2 . GLN   A 1 192 ? -16.93896 22.56291 -30.88133 1.000 45.63602  ? 192 GLN   A NE2 1 
ATOM   1487 N N   . ALA   A 1 193 ? -14.80623 22.15855 -37.28094 1.000 48.20718  ? 193 ALA   A N   1 
ATOM   1488 C CA  . ALA   A 1 193 ? -13.84335 21.63881 -38.23901 1.000 48.81270  ? 193 ALA   A CA  1 
ATOM   1489 C C   . ALA   A 1 193 ? -12.42969 21.97828 -37.79233 1.000 49.63385  ? 193 ALA   A C   1 
ATOM   1490 O O   . ALA   A 1 193 ? -12.16105 23.09703 -37.34239 1.000 51.04933  ? 193 ALA   A O   1 
ATOM   1491 C CB  . ALA   A 1 193 ? -14.09620 22.20549 -39.63945 1.000 47.66780  ? 193 ALA   A CB  1 
ATOM   1492 N N   . ALA   A 1 194 ? -11.53242 21.00763 -37.91465 1.000 45.11570  ? 194 ALA   A N   1 
ATOM   1493 C CA  . ALA   A 1 194 ? -10.12087 21.23833 -37.66172 1.000 50.93403  ? 194 ALA   A CA  1 
ATOM   1494 C C   . ALA   A 1 194 ? -9.44468  21.76982 -38.92025 1.000 52.36907  ? 194 ALA   A C   1 
ATOM   1495 O O   . ALA   A 1 194 ? -9.93778  21.60414 -40.03848 1.000 52.21066  ? 194 ALA   A O   1 
ATOM   1496 C CB  . ALA   A 1 194 ? -9.43464  19.95340 -37.19731 1.000 46.29880  ? 194 ALA   A CB  1 
ATOM   1497 N N   . GLY   A 1 195 ? -8.30580  22.42758 -38.72343 1.000 51.80030  ? 195 GLY   A N   1 
ATOM   1498 C CA  . GLY   A 1 195 ? -7.52115  22.87856 -39.85392 1.000 53.66121  ? 195 GLY   A CA  1 
ATOM   1499 C C   . GLY   A 1 195 ? -6.99406  21.71755 -40.67379 1.000 53.94326  ? 195 GLY   A C   1 
ATOM   1500 O O   . GLY   A 1 195 ? -6.94726  20.57036 -40.22618 1.000 51.98583  ? 195 GLY   A O   1 
ATOM   1501 N N   . THR   A 1 196 ? -6.60394  22.02410 -41.90845 1.000 57.97020  ? 196 THR   A N   1 
ATOM   1502 C CA  . THR   A 1 196 ? -6.04178  20.99889 -42.77653 1.000 53.61667  ? 196 THR   A CA  1 
ATOM   1503 C C   . THR   A 1 196 ? -4.75183  20.45992 -42.16975 1.000 55.42497  ? 196 THR   A C   1 
ATOM   1504 O O   . THR   A 1 196 ? -3.89325  21.22558 -41.72190 1.000 58.38031  ? 196 THR   A O   1 
ATOM   1505 C CB  . THR   A 1 196 ? -5.79350  21.56289 -44.17755 1.000 54.18457  ? 196 THR   A CB  1 
ATOM   1506 O OG1 . THR   A 1 196 ? -4.93146  20.68141 -44.90771 1.000 55.90294  ? 196 THR   A OG1 1 
ATOM   1507 C CG2 . THR   A 1 196 ? -5.16718  22.95125 -44.10338 1.000 55.43084  ? 196 THR   A CG2 1 
ATOM   1508 N N   . ASP   A 1 197 ? -4.63026  19.13760 -42.13044 1.000 55.84237  ? 197 ASP   A N   1 
ATOM   1509 C CA  . ASP   A 1 197 ? -3.52361  18.49681 -41.43835 1.000 50.84265  ? 197 ASP   A CA  1 
ATOM   1510 C C   . ASP   A 1 197 ? -2.32243  18.33030 -42.36448 1.000 51.40695  ? 197 ASP   A C   1 
ATOM   1511 O O   . ASP   A 1 197 ? -2.44819  18.28948 -43.59056 1.000 54.56307  ? 197 ASP   A O   1 
ATOM   1512 C CB  . ASP   A 1 197 ? -3.95019  17.13772 -40.88246 1.000 46.99965  ? 197 ASP   A CB  1 
ATOM   1513 C CG  . ASP   A 1 197 ? -3.14722  16.73270 -39.66368 1.000 48.45048  ? 197 ASP   A CG  1 
ATOM   1514 O OD1 . ASP   A 1 197 ? -2.70110  17.63654 -38.92607 1.000 48.87979  ? 197 ASP   A OD1 1 
ATOM   1515 O OD2 . ASP   A 1 197 ? -2.96004  15.51695 -39.44373 1.000 47.62690  ? 197 ASP   A OD2 1 
ATOM   1516 N N   . THR   A 1 198 ? -1.14290  18.23968 -41.75352 1.000 49.50457  ? 198 THR   A N   1 
ATOM   1517 C CA  . THR   A 1 198 ? 0.11191   18.06430 -42.46962 1.000 49.36677  ? 198 THR   A CA  1 
ATOM   1518 C C   . THR   A 1 198 ? 0.86125   16.86912 -41.89310 1.000 48.81767  ? 198 THR   A C   1 
ATOM   1519 O O   . THR   A 1 198 ? 0.53853   16.36288 -40.81475 1.000 47.22417  ? 198 THR   A O   1 
ATOM   1520 C CB  . THR   A 1 198 ? 0.98831   19.32412 -42.39420 1.000 47.13293  ? 198 THR   A CB  1 
ATOM   1521 O OG1 . THR   A 1 198 ? 1.38589   19.55278 -41.03743 1.000 48.27667  ? 198 THR   A OG1 1 
ATOM   1522 C CG2 . THR   A 1 198 ? 0.23044   20.54033 -42.90456 1.000 49.72060  ? 198 THR   A CG2 1 
ATOM   1523 N N   . THR   A 1 199 ? 1.87619   16.41848 -42.62683 1.000 44.85447  ? 199 THR   A N   1 
ATOM   1524 C CA  . THR   A 1 199 ? 2.69705   15.29203 -42.20339 1.000 43.58831  ? 199 THR   A CA  1 
ATOM   1525 C C   . THR   A 1 199 ? 3.89535   15.79916 -41.41070 1.000 44.06562  ? 199 THR   A C   1 
ATOM   1526 O O   . THR   A 1 199 ? 4.60798   16.70252 -41.86066 1.000 43.84812  ? 199 THR   A O   1 
ATOM   1527 C CB  . THR   A 1 199 ? 3.16895   14.47850 -43.40930 1.000 45.35418  ? 199 THR   A CB  1 
ATOM   1528 O OG1 . THR   A 1 199 ? 2.04194   13.85822 -44.04061 1.000 46.02327  ? 199 THR   A OG1 1 
ATOM   1529 C CG2 . THR   A 1 199 ? 4.14768   13.40019 -42.97070 1.000 38.79349  ? 199 THR   A CG2 1 
ATOM   1530 N N   . ILE   A 1 200 ? 4.11355   15.21478 -40.23391 1.000 38.64250  ? 200 ILE   A N   1 
ATOM   1531 C CA  . ILE   A 1 200 ? 5.20064   15.62501 -39.34689 1.000 39.61443  ? 200 ILE   A CA  1 
ATOM   1532 C C   . ILE   A 1 200 ? 6.49442   15.04574 -39.91341 1.000 37.75867  ? 200 ILE   A C   1 
ATOM   1533 O O   . ILE   A 1 200 ? 6.75937   13.84877 -39.79413 1.000 39.00907  ? 200 ILE   A O   1 
ATOM   1534 C CB  . ILE   A 1 200 ? 4.95862   15.17729 -37.90498 1.000 39.96250  ? 200 ILE   A CB  1 
ATOM   1535 C CG1 . ILE   A 1 200 ? 3.54142   15.55834 -37.47127 1.000 41.93154  ? 200 ILE   A CG1 1 
ATOM   1536 C CG2 . ILE   A 1 200 ? 5.98335   15.80726 -36.97742 1.000 37.90980  ? 200 ILE   A CG2 1 
ATOM   1537 C CD1 . ILE   A 1 200 ? 2.91856   14.59364 -36.48735 1.000 41.08095  ? 200 ILE   A CD1 1 
ATOM   1538 N N   . THR   A 1 201 ? 7.31364   15.90767 -40.52036 1.000 35.60372  ? 201 THR   A N   1 
ATOM   1539 C CA  . THR   A 1 201 ? 8.47784   15.44178 -41.26777 1.000 39.63582  ? 201 THR   A CA  1 
ATOM   1540 C C   . THR   A 1 201 ? 9.52128   14.80547 -40.35619 1.000 36.84410  ? 201 THR   A C   1 
ATOM   1541 O O   . THR   A 1 201 ? 10.10388  13.77156 -40.70357 1.000 33.05838  ? 201 THR   A O   1 
ATOM   1542 C CB  . THR   A 1 201 ? 9.08769   16.60399 -42.05008 1.000 39.74221  ? 201 THR   A CB  1 
ATOM   1543 O OG1 . THR   A 1 201 ? 8.09071   17.17462 -42.90702 1.000 39.80949  ? 201 THR   A OG1 1 
ATOM   1544 C CG2 . THR   A 1 201 ? 10.25898  16.12502 -42.89521 1.000 39.12595  ? 201 THR   A CG2 1 
ATOM   1545 N N   . VAL   A 1 202 ? 9.77304   15.40596 -39.19039 1.000 30.06388  ? 202 VAL   A N   1 
ATOM   1546 C CA  . VAL   A 1 202 ? 10.79721  14.88205 -38.28953 1.000 35.12622  ? 202 VAL   A CA  1 
ATOM   1547 C C   . VAL   A 1 202 ? 10.44682  13.46911 -37.85231 1.000 40.02424  ? 202 VAL   A C   1 
ATOM   1548 O O   . VAL   A 1 202 ? 11.31133  12.58564 -37.79290 1.000 35.93676  ? 202 VAL   A O   1 
ATOM   1549 C CB  . VAL   A 1 202 ? 10.96823  15.81388 -37.07800 1.000 39.92889  ? 202 VAL   A CB  1 
ATOM   1550 C CG1 . VAL   A 1 202 ? 12.01216  15.25707 -36.11567 1.000 34.56275  ? 202 VAL   A CG1 1 
ATOM   1551 C CG2 . VAL   A 1 202 ? 11.33430  17.18875 -37.54177 1.000 41.21393  ? 202 VAL   A CG2 1 
ATOM   1552 N N   . ASN   A 1 203 ? 9.17212   13.23379 -37.54179 1.000 36.71134  ? 203 ASN   A N   1 
ATOM   1553 C CA  . ASN   A 1 203 ? 8.74903   11.90501 -37.12570 1.000 30.62136  ? 203 ASN   A CA  1 
ATOM   1554 C C   . ASN   A 1 203 ? 8.90601   10.89251 -38.25249 1.000 30.99133  ? 203 ASN   A C   1 
ATOM   1555 O O   . ASN   A 1 203 ? 9.15553   9.71011  -37.99192 1.000 46.16492  ? 203 ASN   A O   1 
ATOM   1556 C CB  . ASN   A 1 203 ? 7.30225   11.95349 -36.63861 1.000 40.56567  ? 203 ASN   A CB  1 
ATOM   1557 C CG  . ASN   A 1 203 ? 7.12957   12.82036 -35.40232 1.000 38.60948  ? 203 ASN   A CG  1 
ATOM   1558 O OD1 . ASN   A 1 203 ? 8.10460   13.30104 -34.82366 1.000 39.89615  ? 203 ASN   A OD1 1 
ATOM   1559 N ND2 . ASN   A 1 203 ? 5.88232   13.02919 -34.99661 1.000 39.07384  ? 203 ASN   A ND2 1 
ATOM   1560 N N   . VAL   A 1 204 ? 8.77439   11.33276 -39.50628 1.000 39.42609  ? 204 VAL   A N   1 
ATOM   1561 C CA  . VAL   A 1 204 ? 8.98488   10.42964 -40.63463 1.000 34.32693  ? 204 VAL   A CA  1 
ATOM   1562 C C   . VAL   A 1 204 ? 10.45071  10.02382 -40.72271 1.000 30.63499  ? 204 VAL   A C   1 
ATOM   1563 O O   . VAL   A 1 204 ? 10.77655  8.84483  -40.90236 1.000 43.31100  ? 204 VAL   A O   1 
ATOM   1564 C CB  . VAL   A 1 204 ? 8.50396   11.07746 -41.94548 1.000 36.55017  ? 204 VAL   A CB  1 
ATOM   1565 C CG1 . VAL   A 1 204 ? 8.79419   10.16147 -43.12581 1.000 33.55092  ? 204 VAL   A CG1 1 
ATOM   1566 C CG2 . VAL   A 1 204 ? 7.02516   11.39032 -41.87157 1.000 33.71193  ? 204 VAL   A CG2 1 
ATOM   1567 N N   . LEU   A 1 205 ? 11.35589  10.99706 -40.59809 1.000 37.53705  ? 205 LEU   A N   1 
ATOM   1568 C CA  . LEU   A 1 205 ? 12.78259  10.69840 -40.67602 1.000 37.56547  ? 205 LEU   A CA  1 
ATOM   1569 C C   . LEU   A 1 205 ? 13.22833  9.81805  -39.51476 1.000 36.64656  ? 205 LEU   A C   1 
ATOM   1570 O O   . LEU   A 1 205 ? 14.06865  8.92821  -39.69123 1.000 38.64637  ? 205 LEU   A O   1 
ATOM   1571 C CB  . LEU   A 1 205 ? 13.58909  11.99725 -40.70748 1.000 38.16687  ? 205 LEU   A CB  1 
ATOM   1572 C CG  . LEU   A 1 205 ? 13.46944  12.83985 -41.97991 1.000 36.39302  ? 205 LEU   A CG  1 
ATOM   1573 C CD1 . LEU   A 1 205 ? 13.98613  14.25343 -41.74779 1.000 37.34589  ? 205 LEU   A CD1 1 
ATOM   1574 C CD2 . LEU   A 1 205 ? 14.20713  12.17781 -43.13185 1.000 36.50376  ? 205 LEU   A CD2 1 
ATOM   1575 N N   . ALA   A 1 206 ? 12.68014  10.05083 -38.31916 1.000 38.46407  ? 206 ALA   A N   1 
ATOM   1576 C CA  . ALA   A 1 206 ? 13.00495  9.19350  -37.18369 1.000 36.32942  ? 206 ALA   A CA  1 
ATOM   1577 C C   . ALA   A 1 206 ? 12.50058  7.77450  -37.40946 1.000 36.76872  ? 206 ALA   A C   1 
ATOM   1578 O O   . ALA   A 1 206 ? 13.16095  6.80270  -37.02442 1.000 38.82014  ? 206 ALA   A O   1 
ATOM   1579 C CB  . ALA   A 1 206 ? 12.41968  9.77680  -35.89794 1.000 34.84317  ? 206 ALA   A CB  1 
ATOM   1580 N N   . TRP   A 1 207 ? 11.33044  7.63685  -38.03732 1.000 35.98336  ? 207 TRP   A N   1 
ATOM   1581 C CA  . TRP   A 1 207 ? 10.81213  6.31457  -38.36991 1.000 38.28931  ? 207 TRP   A CA  1 
ATOM   1582 C C   . TRP   A 1 207 ? 11.69193  5.61131  -39.39421 1.000 38.46616  ? 207 TRP   A C   1 
ATOM   1583 O O   . TRP   A 1 207 ? 11.80381  4.37992  -39.37312 1.000 40.86052  ? 207 TRP   A O   1 
ATOM   1584 C CB  . TRP   A 1 207 ? 9.37843   6.43684  -38.88556 1.000 39.32404  ? 207 TRP   A CB  1 
ATOM   1585 C CG  . TRP   A 1 207 ? 8.71232   5.12982  -39.19220 1.000 38.81880  ? 207 TRP   A CG  1 
ATOM   1586 C CD1 . TRP   A 1 207 ? 8.31222   4.18156  -38.29532 1.000 40.50827  ? 207 TRP   A CD1 1 
ATOM   1587 C CD2 . TRP   A 1 207 ? 8.34526   4.63769  -40.48676 1.000 39.65262  ? 207 TRP   A CD2 1 
ATOM   1588 N NE1 . TRP   A 1 207 ? 7.72684   3.12614  -38.95236 1.000 42.14145  ? 207 TRP   A NE1 1 
ATOM   1589 C CE2 . TRP   A 1 207 ? 7.73500   3.38151  -40.29835 1.000 39.57009  ? 207 TRP   A CE2 1 
ATOM   1590 C CE3 . TRP   A 1 207 ? 8.47695   5.13561  -41.78698 1.000 41.29554  ? 207 TRP   A CE3 1 
ATOM   1591 C CZ2 . TRP   A 1 207 ? 7.25839   2.61648  -41.35999 1.000 41.12325  ? 207 TRP   A CZ2 1 
ATOM   1592 C CZ3 . TRP   A 1 207 ? 8.00283   4.37366  -42.84039 1.000 43.72593  ? 207 TRP   A CZ3 1 
ATOM   1593 C CH2 . TRP   A 1 207 ? 7.39960   3.12900  -42.61975 1.000 42.58673  ? 207 TRP   A CH2 1 
ATOM   1594 N N   . LEU   A 1 208 ? 12.31981  6.37203  -40.29436 1.000 39.15653  ? 208 LEU   A N   1 
ATOM   1595 C CA  . LEU   A 1 208 ? 13.25614  5.77859  -41.24179 1.000 40.46787  ? 208 LEU   A CA  1 
ATOM   1596 C C   . LEU   A 1 208 ? 14.53559  5.32562  -40.55055 1.000 40.17592  ? 208 LEU   A C   1 
ATOM   1597 O O   . LEU   A 1 208 ? 15.16097  4.35138  -40.98443 1.000 41.06170  ? 208 LEU   A O   1 
ATOM   1598 C CB  . LEU   A 1 208 ? 13.57785  6.77400  -42.35768 1.000 39.62745  ? 208 LEU   A CB  1 
ATOM   1599 C CG  . LEU   A 1 208 ? 12.48439  7.00422  -43.40426 1.000 38.99162  ? 208 LEU   A CG  1 
ATOM   1600 C CD1 . LEU   A 1 208 ? 13.00420  7.85814  -44.54917 1.000 42.51348  ? 208 LEU   A CD1 1 
ATOM   1601 C CD2 . LEU   A 1 208 ? 11.94658  5.68212  -43.92618 1.000 40.92188  ? 208 LEU   A CD2 1 
ATOM   1602 N N   . TYR   A 1 209 ? 14.94199  6.01774  -39.48221 1.000 39.14223  ? 209 TYR   A N   1 
ATOM   1603 C CA  . TYR   A 1 209 ? 16.10815  5.58206  -38.72021 1.000 41.20840  ? 209 TYR   A CA  1 
ATOM   1604 C C   . TYR   A 1 209 ? 15.82466  4.28240  -37.97943 1.000 42.96228  ? 209 TYR   A C   1 
ATOM   1605 O O   . TYR   A 1 209 ? 16.66456  3.37457  -37.96453 1.000 43.46293  ? 209 TYR   A O   1 
ATOM   1606 C CB  . TYR   A 1 209 ? 16.53924  6.67558  -37.74452 1.000 40.71935  ? 209 TYR   A CB  1 
ATOM   1607 C CG  . TYR   A 1 209 ? 17.43364  7.72396  -38.36210 1.000 42.54654  ? 209 TYR   A CG  1 
ATOM   1608 C CD1 . TYR   A 1 209 ? 18.72878  7.41592  -38.75490 1.000 43.17684  ? 209 TYR   A CD1 1 
ATOM   1609 C CD2 . TYR   A 1 209 ? 16.98151  9.02146  -38.55488 1.000 40.05181  ? 209 TYR   A CD2 1 
ATOM   1610 C CE1 . TYR   A 1 209 ? 19.54778  8.37216  -39.32038 1.000 42.95955  ? 209 TYR   A CE1 1 
ATOM   1611 C CE2 . TYR   A 1 209 ? 17.79190  9.98306  -39.11979 1.000 41.41433  ? 209 TYR   A CE2 1 
ATOM   1612 C CZ  . TYR   A 1 209 ? 19.07342  9.65365  -39.50085 1.000 43.28674  ? 209 TYR   A CZ  1 
ATOM   1613 O OH  . TYR   A 1 209 ? 19.88397  10.61067 -40.06419 1.000 43.87455  ? 209 TYR   A OH  1 
ATOM   1614 N N   . ALA   A 1 210 ? 14.64812  4.17641  -37.35562 1.000 39.60602  ? 210 ALA   A N   1 
ATOM   1615 C CA  . ALA   A 1 210 ? 14.23844  2.90523  -36.76936 1.000 42.97967  ? 210 ALA   A CA  1 
ATOM   1616 C C   . ALA   A 1 210 ? 14.18906  1.81240  -37.82744 1.000 42.78130  ? 210 ALA   A C   1 
ATOM   1617 O O   . ALA   A 1 210 ? 14.48067  0.64458  -37.54190 1.000 43.30179  ? 210 ALA   A O   1 
ATOM   1618 C CB  . ALA   A 1 210 ? 12.87943  3.05324  -36.08657 1.000 40.31727  ? 210 ALA   A CB  1 
ATOM   1619 N N   . ALA   A 1 211 ? 13.82898  2.17769  -39.06008 1.000 39.43615  ? 211 ALA   A N   1 
ATOM   1620 C CA  . ALA   A 1 211 ? 13.83254  1.21420  -40.15454 1.000 42.82064  ? 211 ALA   A CA  1 
ATOM   1621 C C   . ALA   A 1 211 ? 15.24126  0.70361  -40.42775 1.000 47.29535  ? 211 ALA   A C   1 
ATOM   1622 O O   . ALA   A 1 211 ? 15.46956  -0.50844 -40.51466 1.000 49.63162  ? 211 ALA   A O   1 
ATOM   1623 C CB  . ALA   A 1 211 ? 13.23428  1.84745  -41.41053 1.000 42.53466  ? 211 ALA   A CB  1 
ATOM   1624 N N   . VAL   A 1 212 ? 16.20251  1.62129  -40.56140 1.000 45.92526  ? 212 VAL   A N   1 
ATOM   1625 C CA  . VAL   A 1 212 ? 17.58792  1.23220  -40.81088 1.000 47.84931  ? 212 VAL   A CA  1 
ATOM   1626 C C   . VAL   A 1 212 ? 18.13154  0.42700  -39.63846 1.000 48.50613  ? 212 VAL   A C   1 
ATOM   1627 O O   . VAL   A 1 212 ? 18.85912  -0.55660 -39.82260 1.000 51.77745  ? 212 VAL   A O   1 
ATOM   1628 C CB  . VAL   A 1 212 ? 18.44458  2.48284  -41.08109 1.000 44.83763  ? 212 VAL   A CB  1 
ATOM   1629 C CG1 . VAL   A 1 212 ? 19.92932  2.15654  -40.95316 1.000 49.83776  ? 212 VAL   A CG1 1 
ATOM   1630 C CG2 . VAL   A 1 212 ? 18.10969  3.07631  -42.44043 1.000 46.04299  ? 212 VAL   A CG2 1 
ATOM   1631 N N   . ILE   A 1 213 ? 17.78337  0.83173  -38.41473 1.000 46.13580  ? 213 ILE   A N   1 
ATOM   1632 C CA  . ILE   A 1 213 ? 18.24895  0.12562  -37.22491 1.000 45.39729  ? 213 ILE   A CA  1 
ATOM   1633 C C   . ILE   A 1 213 ? 17.81012  -1.33307 -37.26477 1.000 48.66236  ? 213 ILE   A C   1 
ATOM   1634 O O   . ILE   A 1 213 ? 18.56106  -2.23479 -36.87261 1.000 51.65300  ? 213 ILE   A O   1 
ATOM   1635 C CB  . ILE   A 1 213 ? 17.74517  0.84355  -35.95768 1.000 46.35637  ? 213 ILE   A CB  1 
ATOM   1636 C CG1 . ILE   A 1 213 ? 18.70611  1.96726  -35.56890 1.000 43.88596  ? 213 ILE   A CG1 1 
ATOM   1637 C CG2 . ILE   A 1 213 ? 17.58081  -0.13286 -34.80098 1.000 43.46330  ? 213 ILE   A CG2 1 
ATOM   1638 C CD1 . ILE   A 1 213 ? 18.06892  3.04823  -34.73096 1.000 46.14937  ? 213 ILE   A CD1 1 
ATOM   1639 N N   . ASN   A 1 214 ? 16.60291  -1.59286 -37.76817 1.000 50.58412  ? 214 ASN   A N   1 
ATOM   1640 C CA  . ASN   A 1 214 ? 16.04138  -2.93663 -37.79976 1.000 50.37519  ? 214 ASN   A CA  1 
ATOM   1641 C C   . ASN   A 1 214 ? 16.21407  -3.62084 -39.15163 1.000 51.01711  ? 214 ASN   A C   1 
ATOM   1642 O O   . ASN   A 1 214 ? 15.48737  -4.57426 -39.45422 1.000 50.82388  ? 214 ASN   A O   1 
ATOM   1643 C CB  . ASN   A 1 214 ? 14.56505  -2.90094 -37.40761 1.000 48.17900  ? 214 ASN   A CB  1 
ATOM   1644 C CG  . ASN   A 1 214 ? 14.36961  -2.84639 -35.90864 1.000 56.92774  ? 214 ASN   A CG  1 
ATOM   1645 O OD1 . ASN   A 1 214 ? 14.42725  -3.86928 -35.22531 1.000 61.04179  ? 214 ASN   A OD1 1 
ATOM   1646 N ND2 . ASN   A 1 214 ? 14.14084  -1.64867 -35.38644 1.000 52.79631  ? 214 ASN   A ND2 1 
ATOM   1647 N N   . GLY   A 1 215 ? 17.15061  -3.15448 -39.97274 1.000 49.04704  ? 215 GLY   A N   1 
ATOM   1648 C CA  . GLY   A 1 215 ? 17.52716  -3.88946 -41.15883 1.000 52.03127  ? 215 GLY   A CA  1 
ATOM   1649 C C   . GLY   A 1 215 ? 16.83076  -3.50446 -42.44681 1.000 52.80926  ? 215 GLY   A C   1 
ATOM   1650 O O   . GLY   A 1 215 ? 17.18506  -4.04672 -43.50130 1.000 54.45735  ? 215 GLY   A O   1 
ATOM   1651 N N   . ASP   A 1 216 ? 15.85273  -2.60314 -42.40918 1.000 51.50306  ? 216 ASP   A N   1 
ATOM   1652 C CA  . ASP   A 1 216 ? 15.16422  -2.16234 -43.62074 1.000 53.15879  ? 216 ASP   A CA  1 
ATOM   1653 C C   . ASP   A 1 216 ? 15.96513  -1.02306 -44.24603 1.000 53.58361  ? 216 ASP   A C   1 
ATOM   1654 O O   . ASP   A 1 216 ? 16.03414  0.07551  -43.68347 1.000 52.22608  ? 216 ASP   A O   1 
ATOM   1655 C CB  . ASP   A 1 216 ? 13.73555  -1.72929 -43.30309 1.000 54.00660  ? 216 ASP   A CB  1 
ATOM   1656 C CG  . ASP   A 1 216 ? 12.70043  -2.73940 -43.76766 1.000 50.66727  ? 216 ASP   A CG  1 
ATOM   1657 O OD1 . ASP   A 1 216 ? 12.92584  -3.40592 -44.80045 1.000 51.17090  ? 216 ASP   A OD1 1 
ATOM   1658 O OD2 . ASP   A 1 216 ? 11.65534  -2.86291 -43.09772 1.000 47.99390  ? 216 ASP   A OD2 1 
ATOM   1659 N N   . ARG   A 1 217 ? 16.57013  -1.28054 -45.41789 1.000 53.27560  ? 217 ARG   A N   1 
ATOM   1660 C CA  . ARG   A 1 217 ? 17.55026  -0.34969 -45.96749 1.000 50.94003  ? 217 ARG   A CA  1 
ATOM   1661 C C   . ARG   A 1 217 ? 17.45519  -0.17602 -47.47639 1.000 48.30127  ? 217 ARG   A C   1 
ATOM   1662 O O   . ARG   A 1 217 ? 18.35766  0.43312  -48.06747 1.000 46.10848  ? 217 ARG   A O   1 
ATOM   1663 C CB  . ARG   A 1 217 ? 18.96650  -0.79705 -45.64068 1.000 57.00889  ? 217 ARG   A CB  1 
ATOM   1664 C CG  . ARG   A 1 217 ? 19.38800  -2.07637 -46.32273 1.000 72.84347  ? 217 ARG   A CG  1 
ATOM   1665 C CD  . ARG   A 1 217 ? 20.02332  -2.97460 -45.28865 1.000 70.76976  ? 217 ARG   A CD  1 
ATOM   1666 N NE  . ARG   A 1 217 ? 20.98636  -2.22469 -44.48901 1.000 72.45580  ? 217 ARG   A NE  1 
ATOM   1667 C CZ  . ARG   A 1 217 ? 21.00676  -2.19324 -43.16378 1.000 71.68592  ? 217 ARG   A CZ  1 
ATOM   1668 N NH1 . ARG   A 1 217 ? 20.14205  -2.87658 -42.44419 1.000 73.38856  ? 217 ARG   A NH1 1 
ATOM   1669 N NH2 . ARG   A 1 217 ? 21.91204  -1.44617 -42.54701 1.000 74.07485  ? 217 ARG   A NH2 1 
ATOM   1670 N N   . TRP   A 1 218 ? 16.41158  -0.69320 -48.12343 1.000 48.05507  ? 218 TRP   A N   1 
ATOM   1671 C CA  . TRP   A 1 218 ? 16.33867  -0.61503 -49.57594 1.000 46.24631  ? 218 TRP   A CA  1 
ATOM   1672 C C   . TRP   A 1 218 ? 16.15007  0.81200  -50.07581 1.000 46.00626  ? 218 TRP   A C   1 
ATOM   1673 O O   . TRP   A 1 218 ? 16.39795  1.07444  -51.25618 1.000 47.31705  ? 218 TRP   A O   1 
ATOM   1674 C CB  . TRP   A 1 218 ? 15.20610  -1.50797 -50.08034 1.000 46.13227  ? 218 TRP   A CB  1 
ATOM   1675 C CG  . TRP   A 1 218 ? 13.87068  -1.08430 -49.57122 1.000 45.35924  ? 218 TRP   A CG  1 
ATOM   1676 C CD1 . TRP   A 1 218 ? 13.21306  -1.58139 -48.48492 1.000 44.69079  ? 218 TRP   A CD1 1 
ATOM   1677 C CD2 . TRP   A 1 218 ? 13.02198  -0.07251 -50.12649 1.000 44.75717  ? 218 TRP   A CD2 1 
ATOM   1678 N NE1 . TRP   A 1 218 ? 12.00984  -0.93972 -48.32581 1.000 46.33328  ? 218 TRP   A NE1 1 
ATOM   1679 C CE2 . TRP   A 1 218 ? 11.86819  -0.00935 -49.32195 1.000 48.82143  ? 218 TRP   A CE2 1 
ATOM   1680 C CE3 . TRP   A 1 218 ? 13.12567  0.78631  -51.22611 1.000 42.36669  ? 218 TRP   A CE3 1 
ATOM   1681 C CZ2 . TRP   A 1 218 ? 10.82569  0.87855  -49.58122 1.000 50.49634  ? 218 TRP   A CZ2 1 
ATOM   1682 C CZ3 . TRP   A 1 218 ? 12.09155  1.66760  -51.48043 1.000 48.09211  ? 218 TRP   A CZ3 1 
ATOM   1683 C CH2 . TRP   A 1 218 ? 10.95644  1.70701  -50.66241 1.000 51.79228  ? 218 TRP   A CH2 1 
ATOM   1684 N N   . PHE   A 1 219 ? 15.72487  1.73558  -49.21260 1.000 45.99468  ? 219 PHE   A N   1 
ATOM   1685 C CA  . PHE   A 1 219 ? 15.41067  3.09937  -49.62249 1.000 45.44507  ? 219 PHE   A CA  1 
ATOM   1686 C C   . PHE   A 1 219 ? 16.59138  4.05565  -49.50793 1.000 45.85271  ? 219 PHE   A C   1 
ATOM   1687 O O   . PHE   A 1 219 ? 16.50294  5.18456  -50.00274 1.000 45.17958  ? 219 PHE   A O   1 
ATOM   1688 C CB  . PHE   A 1 219 ? 14.23880  3.64148  -48.79502 1.000 43.10016  ? 219 PHE   A CB  1 
ATOM   1689 C CG  . PHE   A 1 219 ? 14.38887  3.42476  -47.31592 1.000 41.83004  ? 219 PHE   A CG  1 
ATOM   1690 C CD1 . PHE   A 1 219 ? 15.09556  4.32590  -46.53612 1.000 40.70892  ? 219 PHE   A CD1 1 
ATOM   1691 C CD2 . PHE   A 1 219 ? 13.82822  2.31418  -46.70613 1.000 43.73631  ? 219 PHE   A CD2 1 
ATOM   1692 C CE1 . PHE   A 1 219 ? 15.23580  4.12705  -45.17479 1.000 41.90276  ? 219 PHE   A CE1 1 
ATOM   1693 C CE2 . PHE   A 1 219 ? 13.96597  2.10845  -45.34509 1.000 45.72974  ? 219 PHE   A CE2 1 
ATOM   1694 C CZ  . PHE   A 1 219 ? 14.67069  3.01635  -44.57852 1.000 41.97680  ? 219 PHE   A CZ  1 
ATOM   1695 N N   . LEU   A 1 220 ? 17.68248  3.64009  -48.87246 1.000 44.14768  ? 220 LEU   A N   1 
ATOM   1696 C CA  . LEU   A 1 220 ? 18.85226  4.49705  -48.72620 1.000 45.47832  ? 220 LEU   A CA  1 
ATOM   1697 C C   . LEU   A 1 220 ? 19.58440  4.61169  -50.05786 1.000 48.45398  ? 220 LEU   A C   1 
ATOM   1698 O O   . LEU   A 1 220 ? 20.04192  3.60663  -50.61139 1.000 51.22791  ? 220 LEU   A O   1 
ATOM   1699 C CB  . LEU   A 1 220 ? 19.77348  3.92621  -47.65527 1.000 46.96682  ? 220 LEU   A CB  1 
ATOM   1700 C CG  . LEU   A 1 220 ? 19.07665  3.67166  -46.32211 1.000 50.14027  ? 220 LEU   A CG  1 
ATOM   1701 C CD1 . LEU   A 1 220 ? 19.89367  2.70665  -45.51136 1.000 50.84699  ? 220 LEU   A CD1 1 
ATOM   1702 C CD2 . LEU   A 1 220 ? 18.88579  4.97108  -45.56317 1.000 45.20079  ? 220 LEU   A CD2 1 
ATOM   1703 N N   . ASN   A 1 221 ? 19.69796  5.83028  -50.57487 1.000 50.59611  ? 221 ASN   A N   1 
ATOM   1704 C CA  . ASN   A 1 221 ? 20.41684  6.06971  -51.81480 1.000 54.60286  ? 221 ASN   A CA  1 
ATOM   1705 C C   . ASN   A 1 221 ? 21.79684  6.65273  -51.51736 1.000 55.45737  ? 221 ASN   A C   1 
ATOM   1706 O O   . ASN   A 1 221 ? 22.14355  6.95337  -50.37284 1.000 58.56033  ? 221 ASN   A O   1 
ATOM   1707 C CB  . ASN   A 1 221 ? 19.60977  6.98566  -52.73838 1.000 52.87218  ? 221 ASN   A CB  1 
ATOM   1708 C CG  . ASN   A 1 221 ? 19.16096  8.26112  -52.05341 1.000 55.86929  ? 221 ASN   A CG  1 
ATOM   1709 O OD1 . ASN   A 1 221 ? 19.81754  8.75627  -51.13687 1.000 58.74637  ? 221 ASN   A OD1 1 
ATOM   1710 N ND2 . ASN   A 1 221 ? 18.03216  8.80066  -52.49654 1.000 54.86447  ? 221 ASN   A ND2 1 
ATOM   1711 N N   . ARG   A 1 222 ? 22.59314  6.81414  -52.57218 1.000 58.90810  ? 222 ARG   A N   1 
ATOM   1712 C CA  . ARG   A 1 222 ? 23.94281  7.35013  -52.45305 1.000 59.31645  ? 222 ARG   A CA  1 
ATOM   1713 C C   . ARG   A 1 222 ? 23.97919  8.87183  -52.42612 1.000 58.61880  ? 222 ARG   A C   1 
ATOM   1714 O O   . ARG   A 1 222 ? 25.05749  9.44457  -52.23306 1.000 56.35239  ? 222 ARG   A O   1 
ATOM   1715 C CB  . ARG   A 1 222 ? 24.81015  6.84500  -53.60875 1.000 63.28656  ? 222 ARG   A CB  1 
ATOM   1716 C CG  . ARG   A 1 222 ? 24.33470  7.31166  -54.97658 1.000 62.88717  ? 222 ARG   A CG  1 
ATOM   1717 C CD  . ARG   A 1 222 ? 24.99388  6.52585  -56.09771 1.000 69.07876  ? 222 ARG   A CD  1 
ATOM   1718 N NE  . ARG   A 1 222 ? 24.47628  6.91018  -57.40535 1.000 68.22111  ? 222 ARG   A NE  1 
ATOM   1719 C CZ  . ARG   A 1 222 ? 23.39992  6.37888  -57.96857 1.000 64.99732  ? 222 ARG   A CZ  1 
ATOM   1720 N NH1 . ARG   A 1 222 ? 22.69687  5.43630  -57.36222 1.000 64.78477  ? 222 ARG   A NH1 1 
ATOM   1721 N NH2 . ARG   A 1 222 ? 23.01762  6.80570  -59.16886 1.000 65.41845  ? 222 ARG   A NH2 1 
ATOM   1722 N N   . PHE   A 1 223 ? 22.84220  9.53458  -52.60789 1.000 57.30115  ? 223 PHE   A N   1 
ATOM   1723 C CA  . PHE   A 1 223 ? 22.80671  10.98189 -52.73756 1.000 54.99946  ? 223 PHE   A CA  1 
ATOM   1724 C C   . PHE   A 1 223 ? 22.70093  11.66533 -51.38045 1.000 53.18766  ? 223 PHE   A C   1 
ATOM   1725 O O   . PHE   A 1 223 ? 22.33844  11.05976 -50.36861 1.000 53.94658  ? 223 PHE   A O   1 
ATOM   1726 C CB  . PHE   A 1 223 ? 21.62980  11.42319 -53.60778 1.000 53.15930  ? 223 PHE   A CB  1 
ATOM   1727 C CG  . PHE   A 1 223 ? 21.55214  10.71993 -54.92522 1.000 56.97557  ? 223 PHE   A CG  1 
ATOM   1728 C CD1 . PHE   A 1 223 ? 22.64242  10.69574 -55.77712 1.000 56.50782  ? 223 PHE   A CD1 1 
ATOM   1729 C CD2 . PHE   A 1 223 ? 20.38526  10.08700 -55.31637 1.000 57.49475  ? 223 PHE   A CD2 1 
ATOM   1730 C CE1 . PHE   A 1 223 ? 22.57207  10.04818 -56.99404 1.000 59.57908  ? 223 PHE   A CE1 1 
ATOM   1731 C CE2 . PHE   A 1 223 ? 20.30767  9.43823  -56.53134 1.000 59.64659  ? 223 PHE   A CE2 1 
ATOM   1732 C CZ  . PHE   A 1 223 ? 21.40265  9.41861  -57.37202 1.000 61.72455  ? 223 PHE   A CZ  1 
ATOM   1733 N N   . THR   A 1 224 ? 23.03021  12.95336 -51.38116 1.000 51.21324  ? 224 THR   A N   1 
ATOM   1734 C CA  . THR   A 1 224 ? 22.72844  13.86472 -50.29145 1.000 52.01666  ? 224 THR   A CA  1 
ATOM   1735 C C   . THR   A 1 224 ? 21.97405  15.05231 -50.86892 1.000 51.85616  ? 224 THR   A C   1 
ATOM   1736 O O   . THR   A 1 224 ? 21.85200  15.20645 -52.08707 1.000 54.56175  ? 224 THR   A O   1 
ATOM   1737 C CB  . THR   A 1 224 ? 23.99226  14.34994 -49.57255 1.000 53.02790  ? 224 THR   A CB  1 
ATOM   1738 O OG1 . THR   A 1 224 ? 23.62702  14.93466 -48.31605 1.000 52.59247  ? 224 THR   A OG1 1 
ATOM   1739 C CG2 . THR   A 1 224 ? 24.69519  15.40585 -50.41392 1.000 52.82318  ? 224 THR   A CG2 1 
ATOM   1740 N N   . THR   A 1 225 ? 21.46544  15.90057 -49.98306 1.000 51.78852  ? 225 THR   A N   1 
ATOM   1741 C CA  . THR   A 1 225 ? 20.78014  17.11134 -50.39935 1.000 50.79454  ? 225 THR   A CA  1 
ATOM   1742 C C   . THR   A 1 225 ? 21.05826  18.20649 -49.38403 1.000 47.84648  ? 225 THR   A C   1 
ATOM   1743 O O   . THR   A 1 225 ? 21.60041  17.96152 -48.30362 1.000 45.37043  ? 225 THR   A O   1 
ATOM   1744 C CB  . THR   A 1 225 ? 19.26914  16.88958 -50.54283 1.000 50.55561  ? 225 THR   A CB  1 
ATOM   1745 O OG1 . THR   A 1 225 ? 18.65983  18.06929 -51.08361 1.000 48.07868  ? 225 THR   A OG1 1 
ATOM   1746 C CG2 . THR   A 1 225 ? 18.65004  16.58466 -49.18907 1.000 47.35774  ? 225 THR   A CG2 1 
ATOM   1747 N N   . THR   A 1 226 ? 20.69380  19.42762 -49.75025 1.000 46.96762  ? 226 THR   A N   1 
ATOM   1748 C CA  . THR   A 1 226 ? 20.69635  20.53211 -48.80810 1.000 48.66631  ? 226 THR   A CA  1 
ATOM   1749 C C   . THR   A 1 226 ? 19.32132  20.65533 -48.16424 1.000 48.30758  ? 226 THR   A C   1 
ATOM   1750 O O   . THR   A 1 226 ? 18.31742  20.16611 -48.68777 1.000 48.62533  ? 226 THR   A O   1 
ATOM   1751 C CB  . THR   A 1 226 ? 21.08228  21.84122 -49.49684 1.000 53.05799  ? 226 THR   A CB  1 
ATOM   1752 O OG1 . THR   A 1 226 ? 20.03870  22.23901 -50.39559 1.000 50.57623  ? 226 THR   A OG1 1 
ATOM   1753 C CG2 . THR   A 1 226 ? 22.38492  21.67076 -50.26724 1.000 48.32150  ? 226 THR   A CG2 1 
ATOM   1754 N N   . LEU   A 1 227 ? 19.28851  21.31378 -47.00468 1.000 48.12433  ? 227 LEU   A N   1 
ATOM   1755 C CA  . LEU   A 1 227 ? 18.04406  21.40257 -46.24803 1.000 48.06394  ? 227 LEU   A CA  1 
ATOM   1756 C C   . LEU   A 1 227 ? 16.97707  22.16513 -47.02333 1.000 51.35377  ? 227 LEU   A C   1 
ATOM   1757 O O   . LEU   A 1 227 ? 15.79806  21.79170 -47.00049 1.000 51.63822  ? 227 LEU   A O   1 
ATOM   1758 C CB  . LEU   A 1 227 ? 18.30741  22.04929 -44.88513 1.000 47.79057  ? 227 LEU   A CB  1 
ATOM   1759 C CG  . LEU   A 1 227 ? 17.14871  22.58821 -44.03851 1.000 49.83900  ? 227 LEU   A CG  1 
ATOM   1760 C CD1 . LEU   A 1 227 ? 17.50758  22.45917 -42.57417 1.000 48.82017  ? 227 LEU   A CD1 1 
ATOM   1761 C CD2 . LEU   A 1 227 ? 16.82307  24.04609 -44.35260 1.000 51.94145  ? 227 LEU   A CD2 1 
ATOM   1762 N N   . ASN   A 1 228 ? 17.37086  23.23326 -47.72089 1.000 52.71846  ? 228 ASN   A N   1 
ATOM   1763 C CA  . ASN   A 1 228 ? 16.39439  24.03452 -48.45209 1.000 50.95552  ? 228 ASN   A CA  1 
ATOM   1764 C C   . ASN   A 1 228 ? 15.85261  23.28455 -49.66383 1.000 50.33515  ? 228 ASN   A C   1 
ATOM   1765 O O   . ASN   A 1 228 ? 14.65563  23.36475 -49.96382 1.000 50.42624  ? 228 ASN   A O   1 
ATOM   1766 C CB  . ASN   A 1 228 ? 17.01607  25.36563 -48.87466 1.000 54.28428  ? 228 ASN   A CB  1 
ATOM   1767 C CG  . ASN   A 1 228 ? 16.48054  26.53818 -48.07341 1.000 62.36061  ? 228 ASN   A CG  1 
ATOM   1768 O OD1 . ASN   A 1 228 ? 15.62133  26.37182 -47.20706 1.000 61.70120  ? 228 ASN   A OD1 1 
ATOM   1769 N ND2 . ASN   A 1 228 ? 16.98989  27.73151 -48.35655 1.000 68.36441  ? 228 ASN   A ND2 1 
ATOM   1770 N N   . ASP   A 1 229 ? 16.71402  22.54950 -50.37265 1.000 49.54218  ? 229 ASP   A N   1 
ATOM   1771 C CA  . ASP   A 1 229 ? 16.25253  21.79566 -51.53452 1.000 51.83352  ? 229 ASP   A CA  1 
ATOM   1772 C C   . ASP   A 1 229 ? 15.32293  20.65756 -51.13261 1.000 50.62306  ? 229 ASP   A C   1 
ATOM   1773 O O   . ASP   A 1 229 ? 14.46464  20.25010 -51.92403 1.000 49.17807  ? 229 ASP   A O   1 
ATOM   1774 C CB  . ASP   A 1 229 ? 17.44739  21.25802 -52.32188 1.000 50.57020  ? 229 ASP   A CB  1 
ATOM   1775 C CG  . ASP   A 1 229 ? 17.84770  22.16968 -53.46649 1.000 57.54223  ? 229 ASP   A CG  1 
ATOM   1776 O OD1 . ASP   A 1 229 ? 16.99711  22.43730 -54.34187 1.000 57.82756  ? 229 ASP   A OD1 1 
ATOM   1777 O OD2 . ASP   A 1 229 ? 19.01213  22.62119 -53.48941 1.000 61.16893  ? 229 ASP   A OD2 1 
ATOM   1778 N N   . PHE   A 1 230 ? 15.47643  20.13424 -49.91472 1.000 48.19333  ? 230 PHE   A N   1 
ATOM   1779 C CA  . PHE   A 1 230 ? 14.55473  19.11363 -49.42922 1.000 47.26750  ? 230 PHE   A CA  1 
ATOM   1780 C C   . PHE   A 1 230 ? 13.19700  19.71630 -49.09158 1.000 46.83547  ? 230 PHE   A C   1 
ATOM   1781 O O   . PHE   A 1 230 ? 12.15780  19.08488 -49.31588 1.000 47.22806  ? 230 PHE   A O   1 
ATOM   1782 C CB  . PHE   A 1 230 ? 15.15119  18.40854 -48.20961 1.000 44.33836  ? 230 PHE   A CB  1 
ATOM   1783 C CG  . PHE   A 1 230 ? 14.15562  17.59840 -47.42557 1.000 44.52978  ? 230 PHE   A CG  1 
ATOM   1784 C CD1 . PHE   A 1 230 ? 13.86901  16.29329 -47.78901 1.000 46.99252  ? 230 PHE   A CD1 1 
ATOM   1785 C CD2 . PHE   A 1 230 ? 13.51670  18.13579 -46.31765 1.000 43.37729  ? 230 PHE   A CD2 1 
ATOM   1786 C CE1 . PHE   A 1 230 ? 12.95727  15.54251 -47.07118 1.000 43.69671  ? 230 PHE   A CE1 1 
ATOM   1787 C CE2 . PHE   A 1 230 ? 12.60259  17.39046 -45.59731 1.000 43.82027  ? 230 PHE   A CE2 1 
ATOM   1788 C CZ  . PHE   A 1 230 ? 12.32370  16.09197 -45.97406 1.000 44.16652  ? 230 PHE   A CZ  1 
ATOM   1789 N N   . ASN   A 1 231 ? 13.18617  20.93822 -48.55376 1.000 44.17254  ? 231 ASN   A N   1 
ATOM   1790 C CA  . ASN   A 1 231 ? 11.93194  21.54712 -48.12273 1.000 48.27538  ? 231 ASN   A CA  1 
ATOM   1791 C C   . ASN   A 1 231 ? 11.05080  21.91583 -49.31023 1.000 51.75671  ? 231 ASN   A C   1 
ATOM   1792 O O   . ASN   A 1 231 ? 9.82326   21.78569 -49.24069 1.000 53.22496  ? 231 ASN   A O   1 
ATOM   1793 C CB  . ASN   A 1 231 ? 12.21644  22.77805 -47.26366 1.000 47.20263  ? 231 ASN   A CB  1 
ATOM   1794 C CG  . ASN   A 1 231 ? 12.55018  22.42245 -45.82941 1.000 47.87211  ? 231 ASN   A CG  1 
ATOM   1795 O OD1 . ASN   A 1 231 ? 12.09332  21.40624 -45.30570 1.000 45.22316  ? 231 ASN   A OD1 1 
ATOM   1796 N ND2 . ASN   A 1 231 ? 13.35361  23.26034 -45.18545 1.000 48.16035  ? 231 ASN   A ND2 1 
ATOM   1797 N N   . LEU   A 1 232 ? 11.65416  22.38245 -50.40656 1.000 52.12530  ? 232 LEU   A N   1 
ATOM   1798 C CA  . LEU   A 1 232 ? 10.86495  22.74789 -51.57858 1.000 50.08306  ? 232 LEU   A CA  1 
ATOM   1799 C C   . LEU   A 1 232 ? 10.22865  21.52797 -52.23240 1.000 49.69514  ? 232 LEU   A C   1 
ATOM   1800 O O   . LEU   A 1 232 ? 9.16264   21.64084 -52.84779 1.000 48.95363  ? 232 LEU   A O   1 
ATOM   1801 C CB  . LEU   A 1 232 ? 11.73486  23.50301 -52.58304 1.000 51.68629  ? 232 LEU   A CB  1 
ATOM   1802 C CG  . LEU   A 1 232 ? 12.35560  24.80252 -52.06451 1.000 54.22988  ? 232 LEU   A CG  1 
ATOM   1803 C CD1 . LEU   A 1 232 ? 13.34313  25.37258 -53.07194 1.000 53.08494  ? 232 LEU   A CD1 1 
ATOM   1804 C CD2 . LEU   A 1 232 ? 11.27344  25.82086 -51.72879 1.000 50.51243  ? 232 LEU   A CD2 1 
ATOM   1805 N N   . VAL   A 1 233 ? 10.85894  20.36085 -52.11018 1.000 52.45440  ? 233 VAL   A N   1 
ATOM   1806 C CA  . VAL   A 1 233 ? 10.26255  19.13729 -52.63350 1.000 51.40207  ? 233 VAL   A CA  1 
ATOM   1807 C C   . VAL   A 1 233 ? 9.22071   18.58897 -51.66671 1.000 50.89876  ? 233 VAL   A C   1 
ATOM   1808 O O   . VAL   A 1 233 ? 8.15385   18.12443 -52.08384 1.000 53.07104  ? 233 VAL   A O   1 
ATOM   1809 C CB  . VAL   A 1 233 ? 11.36238  18.10181 -52.93384 1.000 50.99919  ? 233 VAL   A CB  1 
ATOM   1810 C CG1 . VAL   A 1 233 ? 10.75154  16.75560 -53.28654 1.000 53.19861  ? 233 VAL   A CG1 1 
ATOM   1811 C CG2 . VAL   A 1 233 ? 12.25314  18.59070 -54.06177 1.000 50.14208  ? 233 VAL   A CG2 1 
ATOM   1812 N N   . ALA   A 1 234 ? 9.50151   18.65176 -50.36298 1.000 49.49280  ? 234 ALA   A N   1 
ATOM   1813 C CA  . ALA   A 1 234 ? 8.62118   18.02615 -49.38140 1.000 50.35388  ? 234 ALA   A CA  1 
ATOM   1814 C C   . ALA   A 1 234 ? 7.28657   18.75128 -49.25418 1.000 52.74451  ? 234 ALA   A C   1 
ATOM   1815 O O   . ALA   A 1 234 ? 6.27930   18.12895 -48.89857 1.000 51.96315  ? 234 ALA   A O   1 
ATOM   1816 C CB  . ALA   A 1 234 ? 9.31622   17.96157 -48.02070 1.000 48.37399  ? 234 ALA   A CB  1 
ATOM   1817 N N   . MET   A 1 235 ? 7.24951   20.05212 -49.54437 1.000 51.65628  ? 235 MET   A N   1 
ATOM   1818 C CA  . MET   A 1 235 ? 6.04740   20.83118 -49.26768 1.000 49.77039  ? 235 MET   A CA  1 
ATOM   1819 C C   . MET   A 1 235 ? 4.94136   20.59475 -50.28797 1.000 51.00049  ? 235 MET   A C   1 
ATOM   1820 O O   . MET   A 1 235 ? 3.75933   20.71307 -49.94574 1.000 50.78132  ? 235 MET   A O   1 
ATOM   1821 C CB  . MET   A 1 235 ? 6.38874   22.31736 -49.20478 1.000 51.19633  ? 235 MET   A CB  1 
ATOM   1822 C CG  . MET   A 1 235 ? 6.68718   22.81106 -47.80438 1.000 59.93771  ? 235 MET   A CG  1 
ATOM   1823 S SD  . MET   A 1 235 ? 8.02120   24.01872 -47.78688 1.000 87.37280  ? 235 MET   A SD  1 
ATOM   1824 C CE  . MET   A 1 235 ? 8.55980   23.91059 -46.08717 1.000 57.41294  ? 235 MET   A CE  1 
ATOM   1825 N N   . LYS   A 1 236 ? 5.28964   20.27141 -51.53494 1.000 50.31298  ? 236 LYS   A N   1 
ATOM   1826 C CA  . LYS   A 1 236 ? 4.25708   19.95657 -52.51457 1.000 50.58700  ? 236 LYS   A CA  1 
ATOM   1827 C C   . LYS   A 1 236 ? 3.53897   18.65479 -52.17830 1.000 50.62980  ? 236 LYS   A C   1 
ATOM   1828 O O   . LYS   A 1 236 ? 2.46639   18.38844 -52.73168 1.000 53.71970  ? 236 LYS   A O   1 
ATOM   1829 C CB  . LYS   A 1 236 ? 4.86222   19.90896 -53.92261 1.000 48.62512  ? 236 LYS   A CB  1 
ATOM   1830 C CG  . LYS   A 1 236 ? 5.47264   18.58092 -54.33812 1.000 51.45641  ? 236 LYS   A CG  1 
ATOM   1831 C CD  . LYS   A 1 236 ? 5.75225   18.56605 -55.84192 1.000 54.90057  ? 236 LYS   A CD  1 
ATOM   1832 C CE  . LYS   A 1 236 ? 5.27415   17.27915 -56.50022 1.000 59.10697  ? 236 LYS   A CE  1 
ATOM   1833 N NZ  . LYS   A 1 236 ? 6.13356   16.86764 -57.64319 1.000 75.79822  ? 236 LYS   A NZ  1 
ATOM   1834 N N   . TYR   A 1 237 ? 4.09768   17.85327 -51.27210 1.000 48.07518  ? 237 TYR   A N   1 
ATOM   1835 C CA  . TYR   A 1 237 ? 3.43378   16.68025 -50.72340 1.000 47.16987  ? 237 TYR   A CA  1 
ATOM   1836 C C   . TYR   A 1 237 ? 2.87168   16.93688 -49.33077 1.000 44.48481  ? 237 TYR   A C   1 
ATOM   1837 O O   . TYR   A 1 237 ? 2.51754   15.98341 -48.63011 1.000 42.20820  ? 237 TYR   A O   1 
ATOM   1838 C CB  . TYR   A 1 237 ? 4.40211   15.49591 -50.69491 1.000 46.93992  ? 237 TYR   A CB  1 
ATOM   1839 C CG  . TYR   A 1 237 ? 4.84610   15.05159 -52.06982 1.000 46.68289  ? 237 TYR   A CG  1 
ATOM   1840 C CD1 . TYR   A 1 237 ? 4.05440   14.20766 -52.83653 1.000 45.90657  ? 237 TYR   A CD1 1 
ATOM   1841 C CD2 . TYR   A 1 237 ? 6.05168   15.48421 -52.60529 1.000 48.45437  ? 237 TYR   A CD2 1 
ATOM   1842 C CE1 . TYR   A 1 237 ? 4.45271   13.80180 -54.09687 1.000 49.51976  ? 237 TYR   A CE1 1 
ATOM   1843 C CE2 . TYR   A 1 237 ? 6.45892   15.08471 -53.86506 1.000 50.29210  ? 237 TYR   A CE2 1 
ATOM   1844 C CZ  . TYR   A 1 237 ? 5.65544   14.24318 -54.60643 1.000 52.42778  ? 237 TYR   A CZ  1 
ATOM   1845 O OH  . TYR   A 1 237 ? 6.05360   13.84128 -55.86158 1.000 53.86317  ? 237 TYR   A OH  1 
ATOM   1846 N N   . ASN   A 1 238 ? 2.79841   18.20457 -48.91643 1.000 49.23450  ? 238 ASN   A N   1 
ATOM   1847 C CA  . ASN   A 1 238 ? 2.22216   18.60301 -47.62985 1.000 47.25878  ? 238 ASN   A CA  1 
ATOM   1848 C C   . ASN   A 1 238 ? 3.00269   18.01234 -46.45695 1.000 47.47360  ? 238 ASN   A C   1 
ATOM   1849 O O   . ASN   A 1 238 ? 2.42585   17.49368 -45.49907 1.000 45.85464  ? 238 ASN   A O   1 
ATOM   1850 C CB  . ASN   A 1 238 ? 0.74023   18.22833 -47.54360 1.000 45.40186  ? 238 ASN   A CB  1 
ATOM   1851 C CG  . ASN   A 1 238 ? -0.00025  19.01872 -46.48199 1.000 50.33443  ? 238 ASN   A CG  1 
ATOM   1852 O OD1 . ASN   A 1 238 ? 0.35645   20.15676 -46.17872 1.000 52.25078  ? 238 ASN   A OD1 1 
ATOM   1853 N ND2 . ASN   A 1 238 ? -1.04033  18.41857 -45.91353 1.000 52.81851  ? 238 ASN   A ND2 1 
ATOM   1854 N N   . TYR   A 1 239 ? 4.32622   18.08817 -46.53283 1.000 48.55602  ? 239 TYR   A N   1 
ATOM   1855 C CA  . TYR   A 1 239 ? 5.19109   17.71129 -45.42696 1.000 47.41017  ? 239 TYR   A CA  1 
ATOM   1856 C C   . TYR   A 1 239 ? 5.63532   18.96217 -44.67828 1.000 47.75448  ? 239 TYR   A C   1 
ATOM   1857 O O   . TYR   A 1 239 ? 5.82164   20.02953 -45.26855 1.000 48.71588  ? 239 TYR   A O   1 
ATOM   1858 C CB  . TYR   A 1 239 ? 6.41047   16.92467 -45.91894 1.000 46.47521  ? 239 TYR   A CB  1 
ATOM   1859 C CG  . TYR   A 1 239 ? 6.22927   15.42045 -45.89550 1.000 44.64087  ? 239 TYR   A CG  1 
ATOM   1860 C CD1 . TYR   A 1 239 ? 5.13994   14.82052 -46.51567 1.000 44.45999  ? 239 TYR   A CD1 1 
ATOM   1861 C CD2 . TYR   A 1 239 ? 7.14971   14.60130 -45.25490 1.000 42.01753  ? 239 TYR   A CD2 1 
ATOM   1862 C CE1 . TYR   A 1 239 ? 4.97212   13.44731 -46.49564 1.000 39.58949  ? 239 TYR   A CE1 1 
ATOM   1863 C CE2 . TYR   A 1 239 ? 6.98999   13.22795 -45.22946 1.000 40.72471  ? 239 TYR   A CE2 1 
ATOM   1864 C CZ  . TYR   A 1 239 ? 5.90129   12.65650 -45.85113 1.000 40.34548  ? 239 TYR   A CZ  1 
ATOM   1865 O OH  . TYR   A 1 239 ? 5.74269   11.28971 -45.82321 1.000 40.23796  ? 239 TYR   A OH  1 
ATOM   1866 N N   . GLU   A 1 240 ? 5.78980   18.82026 -43.36572 1.000 48.09993  ? 240 GLU   A N   1 
ATOM   1867 C CA  . GLU   A 1 240 ? 6.14543   19.95036 -42.52488 1.000 48.66288  ? 240 GLU   A CA  1 
ATOM   1868 C C   . GLU   A 1 240 ? 7.55298   20.44784 -42.85918 1.000 46.26577  ? 240 GLU   A C   1 
ATOM   1869 O O   . GLU   A 1 240 ? 8.42395   19.66110 -43.23895 1.000 44.45615  ? 240 GLU   A O   1 
ATOM   1870 C CB  . GLU   A 1 240 ? 6.06708   19.55499 -41.05190 1.000 48.39696  ? 240 GLU   A CB  1 
ATOM   1871 C CG  . GLU   A 1 240 ? 6.10164   20.71876 -40.07624 1.000 53.90791  ? 240 GLU   A CG  1 
ATOM   1872 C CD  . GLU   A 1 240 ? 5.30442   20.45136 -38.81826 1.000 63.54423  ? 240 GLU   A CD  1 
ATOM   1873 O OE1 . GLU   A 1 240 ? 4.07679   20.68236 -38.83474 1.000 66.37186  ? 240 GLU   A OE1 1 
ATOM   1874 O OE2 . GLU   A 1 240 ? 5.90577   20.01668 -37.81272 1.000 64.80174  ? 240 GLU   A OE2 1 
ATOM   1875 N N   . PRO   A 1 241 ? 7.78864   21.75666 -42.75229 1.000 50.93193  ? 241 PRO   A N   1 
ATOM   1876 C CA  . PRO   A 1 241 ? 9.14861   22.28055 -42.93578 1.000 49.99129  ? 241 PRO   A CA  1 
ATOM   1877 C C   . PRO   A 1 241 ? 10.14176  21.63358 -41.98388 1.000 48.51096  ? 241 PRO   A C   1 
ATOM   1878 O O   . PRO   A 1 241 ? 9.84437   21.39887 -40.81106 1.000 50.78076  ? 241 PRO   A O   1 
ATOM   1879 C CB  . PRO   A 1 241 ? 8.99450   23.77994 -42.63897 1.000 52.40206  ? 241 PRO   A CB  1 
ATOM   1880 C CG  . PRO   A 1 241 ? 7.59676   23.94704 -42.07389 1.000 54.18039  ? 241 PRO   A CG  1 
ATOM   1881 C CD  . PRO   A 1 241 ? 6.80042   22.84169 -42.67237 1.000 51.85439  ? 241 PRO   A CD  1 
ATOM   1882 N N   . LEU   A 1 242 ? 11.33641  21.35561 -42.50123 1.000 46.41157  ? 242 LEU   A N   1 
ATOM   1883 C CA  . LEU   A 1 242 ? 12.44851  20.86839 -41.69526 1.000 48.43549  ? 242 LEU   A CA  1 
ATOM   1884 C C   . LEU   A 1 242 ? 13.37436  22.03634 -41.37892 1.000 46.71577  ? 242 LEU   A C   1 
ATOM   1885 O O   . LEU   A 1 242 ? 13.95373  22.63818 -42.28953 1.000 45.04009  ? 242 LEU   A O   1 
ATOM   1886 C CB  . LEU   A 1 242 ? 13.21733  19.76192 -42.41460 1.000 46.92114  ? 242 LEU   A CB  1 
ATOM   1887 C CG  . LEU   A 1 242 ? 14.01337  18.86297 -41.46787 1.000 44.56397  ? 242 LEU   A CG  1 
ATOM   1888 C CD1 . LEU   A 1 242 ? 13.07289  18.01393 -40.62674 1.000 43.24455  ? 242 LEU   A CD1 1 
ATOM   1889 C CD2 . LEU   A 1 242 ? 15.00067  17.99957 -42.22806 1.000 43.52355  ? 242 LEU   A CD2 1 
ATOM   1890 N N   . THR   A 1 243 ? 13.51002  22.35251 -40.09615 1.000 45.38184  ? 243 THR   A N   1 
ATOM   1891 C CA  . THR   A 1 243 ? 14.32990  23.46170 -39.63370 1.000 45.64233  ? 243 THR   A CA  1 
ATOM   1892 C C   . THR   A 1 243 ? 15.60386  22.93924 -38.98168 1.000 47.24284  ? 243 THR   A C   1 
ATOM   1893 O O   . THR   A 1 243 ? 15.78696  21.73427 -38.79013 1.000 47.32046  ? 243 THR   A O   1 
ATOM   1894 C CB  . THR   A 1 243 ? 13.54795  24.34115 -38.65181 1.000 49.36551  ? 243 THR   A CB  1 
ATOM   1895 O OG1 . THR   A 1 243 ? 13.24011  23.58512 -37.47399 1.000 51.14570  ? 243 THR   A OG1 1 
ATOM   1896 C CG2 . THR   A 1 243 ? 12.25516  24.82979 -39.29073 1.000 47.92946  ? 243 THR   A CG2 1 
ATOM   1897 N N   . GLN   A 1 244 ? 16.49577  23.87344 -38.64147 1.000 47.97163  ? 244 GLN   A N   1 
ATOM   1898 C CA  . GLN   A 1 244 ? 17.76445  23.48730 -38.03197 1.000 47.84730  ? 244 GLN   A CA  1 
ATOM   1899 C C   . GLN   A 1 244 ? 17.55032  22.87808 -36.65250 1.000 47.89556  ? 244 GLN   A C   1 
ATOM   1900 O O   . GLN   A 1 244 ? 18.25857  21.94145 -36.26394 1.000 47.12290  ? 244 GLN   A O   1 
ATOM   1901 C CB  . GLN   A 1 244 ? 18.70269  24.69059 -37.95112 1.000 46.89179  ? 244 GLN   A CB  1 
ATOM   1902 C CG  . GLN   A 1 244 ? 20.10019  24.33995 -37.46730 1.000 44.38228  ? 244 GLN   A CG  1 
ATOM   1903 C CD  . GLN   A 1 244 ? 20.78481  23.32588 -38.36164 1.000 44.30384  ? 244 GLN   A CD  1 
ATOM   1904 O OE1 . GLN   A 1 244 ? 20.72903  23.42489 -39.58721 1.000 46.02134  ? 244 GLN   A OE1 1 
ATOM   1905 N NE2 . GLN   A 1 244 ? 21.42976  22.33791 -37.75138 1.000 42.12204  ? 244 GLN   A NE2 1 
ATOM   1906 N N   . ASP   A 1 245 ? 16.58001  23.39909 -35.89586 1.000 49.16020  ? 245 ASP   A N   1 
ATOM   1907 C CA  . ASP   A 1 245 ? 16.19918  22.76282 -34.63931 1.000 50.49524  ? 245 ASP   A CA  1 
ATOM   1908 C C   . ASP   A 1 245 ? 15.81924  21.30684 -34.86653 1.000 47.33191  ? 245 ASP   A C   1 
ATOM   1909 O O   . ASP   A 1 245 ? 16.12533  20.43633 -34.04431 1.000 47.92917  ? 245 ASP   A O   1 
ATOM   1910 C CB  . ASP   A 1 245 ? 15.03442  23.52039 -33.99797 1.000 53.05612  ? 245 ASP   A CB  1 
ATOM   1911 C CG  . ASP   A 1 245 ? 15.24339  25.02291 -33.99579 1.000 60.91426  ? 245 ASP   A CG  1 
ATOM   1912 O OD1 . ASP   A 1 245 ? 15.21082  25.63176 -35.08726 1.000 57.90045  ? 245 ASP   A OD1 1 
ATOM   1913 O OD2 . ASP   A 1 245 ? 15.43235  25.59643 -32.90311 1.000 62.52037  ? 245 ASP   A OD2 1 
ATOM   1914 N N   . HIS   A 1 246 ? 15.17082  21.02444 -35.99637 1.000 46.44669  ? 246 HIS   A N   1 
ATOM   1915 C CA  . HIS   A 1 246 ? 14.71565  19.67079 -36.28726 1.000 47.95569  ? 246 HIS   A CA  1 
ATOM   1916 C C   . HIS   A 1 246 ? 15.88683  18.75049 -36.60977 1.000 46.04035  ? 246 HIS   A C   1 
ATOM   1917 O O   . HIS   A 1 246 ? 15.95185  17.61633 -36.11980 1.000 43.65599  ? 246 HIS   A O   1 
ATOM   1918 C CB  . HIS   A 1 246 ? 13.71683  19.71206 -37.43993 1.000 48.33305  ? 246 HIS   A CB  1 
ATOM   1919 C CG  . HIS   A 1 246 ? 12.36633  20.22159 -37.04376 1.000 50.83618  ? 246 HIS   A CG  1 
ATOM   1920 N ND1 . HIS   A 1 246 ? 11.45500  20.70879 -37.95572 1.000 50.29911  ? 246 HIS   A ND1 1 
ATOM   1921 C CD2 . HIS   A 1 246 ? 11.76718  20.30465 -35.83237 1.000 49.97480  ? 246 HIS   A CD2 1 
ATOM   1922 C CE1 . HIS   A 1 246 ? 10.35561  21.07716 -37.32236 1.000 50.09317  ? 246 HIS   A CE1 1 
ATOM   1923 N NE2 . HIS   A 1 246 ? 10.51924  20.84237 -36.03292 1.000 52.08729  ? 246 HIS   A NE2 1 
ATOM   1924 N N   . VAL   A 1 247 ? 16.81987  19.22115 -37.44159 1.000 43.58086  ? 247 VAL   A N   1 
ATOM   1925 C CA  . VAL   A 1 247 ? 18.03021  18.45394 -37.71967 1.000 45.05406  ? 247 VAL   A CA  1 
ATOM   1926 C C   . VAL   A 1 247 ? 18.80425  18.19694 -36.43395 1.000 46.54634  ? 247 VAL   A C   1 
ATOM   1927 O O   . VAL   A 1 247 ? 19.42603  17.13962 -36.27004 1.000 45.66166  ? 247 VAL   A O   1 
ATOM   1928 C CB  . VAL   A 1 247 ? 18.89013  19.19314 -38.76662 1.000 45.64189  ? 247 VAL   A CB  1 
ATOM   1929 C CG1 . VAL   A 1 247 ? 20.25109  18.53088 -38.92250 1.000 42.21768  ? 247 VAL   A CG1 1 
ATOM   1930 C CG2 . VAL   A 1 247 ? 18.16476  19.25356 -40.10319 1.000 43.62944  ? 247 VAL   A CG2 1 
ATOM   1931 N N   . ASP   A 1 248 ? 18.75600  19.14124 -35.49157 1.000 45.11379  ? 248 ASP   A N   1 
ATOM   1932 C CA  . ASP   A 1 248 ? 19.50324  18.99238 -34.24768 1.000 44.66287  ? 248 ASP   A CA  1 
ATOM   1933 C C   . ASP   A 1 248 ? 18.89617  17.91328 -33.35652 1.000 46.39468  ? 248 ASP   A C   1 
ATOM   1934 O O   . ASP   A 1 248 ? 19.62423  17.20736 -32.64842 1.000 47.97177  ? 248 ASP   A O   1 
ATOM   1935 C CB  . ASP   A 1 248 ? 19.55855  20.33291 -33.51528 1.000 48.75951  ? 248 ASP   A CB  1 
ATOM   1936 C CG  . ASP   A 1 248 ? 20.53610  21.30711 -34.15139 1.000 48.45859  ? 248 ASP   A CG  1 
ATOM   1937 O OD1 . ASP   A 1 248 ? 21.17344  20.94324 -35.16296 1.000 45.02343  ? 248 ASP   A OD1 1 
ATOM   1938 O OD2 . ASP   A 1 248 ? 20.65658  22.44351 -33.64557 1.000 48.93096  ? 248 ASP   A OD2 1 
ATOM   1939 N N   . ILE   A 1 249 ? 17.56679  17.77204 -33.37054 1.000 44.38748  ? 249 ILE   A N   1 
ATOM   1940 C CA  . ILE   A 1 249 ? 16.93006  16.72065 -32.58032 1.000 42.85455  ? 249 ILE   A CA  1 
ATOM   1941 C C   . ILE   A 1 249 ? 17.25655  15.34883 -33.15865 1.000 43.84019  ? 249 ILE   A C   1 
ATOM   1942 O O   . ILE   A 1 249 ? 17.49476  14.38782 -32.41737 1.000 45.52158  ? 249 ILE   A O   1 
ATOM   1943 C CB  . ILE   A 1 249 ? 15.40771  16.94662 -32.48853 1.000 48.80373  ? 249 ILE   A CB  1 
ATOM   1944 C CG1 . ILE   A 1 249 ? 15.08451  18.27183 -31.79699 1.000 45.63342  ? 249 ILE   A CG1 1 
ATOM   1945 C CG2 . ILE   A 1 249 ? 14.74019  15.81008 -31.73388 1.000 55.15649  ? 249 ILE   A CG2 1 
ATOM   1946 C CD1 . ILE   A 1 249 ? 13.87922  18.98609 -32.37434 1.000 48.88571  ? 249 ILE   A CD1 1 
ATOM   1947 N N   . LEU   A 1 250 ? 17.28233  15.23565 -34.48810 1.000 45.15597  ? 250 LEU   A N   1 
ATOM   1948 C CA  . LEU   A 1 250 ? 17.64668  13.99069 -35.15628 1.000 46.17170  ? 250 LEU   A CA  1 
ATOM   1949 C C   . LEU   A 1 250 ? 19.13016  13.66371 -35.03668 1.000 43.96378  ? 250 LEU   A C   1 
ATOM   1950 O O   . LEU   A 1 250 ? 19.54910  12.60195 -35.51250 1.000 42.94514  ? 250 LEU   A O   1 
ATOM   1951 C CB  . LEU   A 1 250 ? 17.25711  14.06022 -36.63456 1.000 44.55253  ? 250 LEU   A CB  1 
ATOM   1952 C CG  . LEU   A 1 250 ? 15.76401  14.08558 -36.96771 1.000 43.30689  ? 250 LEU   A CG  1 
ATOM   1953 C CD1 . LEU   A 1 250 ? 15.52787  14.77995 -38.30178 1.000 41.57655  ? 250 LEU   A CD1 1 
ATOM   1954 C CD2 . LEU   A 1 250 ? 15.19753  12.67666 -36.98464 1.000 36.36246  ? 250 LEU   A CD2 1 
ATOM   1955 N N   . GLY   A 1 251 ? 19.91972  14.53736 -34.41496 1.000 42.76473  ? 251 GLY   A N   1 
ATOM   1956 C CA  . GLY   A 1 251 ? 21.35289  14.38105 -34.32907 1.000 45.96290  ? 251 GLY   A CA  1 
ATOM   1957 C C   . GLY   A 1 251 ? 21.81997  13.05772 -33.75470 1.000 45.32258  ? 251 GLY   A C   1 
ATOM   1958 O O   . GLY   A 1 251 ? 22.49298  12.27332 -34.43089 1.000 46.89867  ? 251 GLY   A O   1 
ATOM   1959 N N   . PRO   A 1 252 ? 21.48967  12.78994 -32.48671 1.000 45.68711  ? 252 PRO   A N   1 
ATOM   1960 C CA  . PRO   A 1 252 ? 21.95871  11.54043 -31.86167 1.000 47.68991  ? 252 PRO   A CA  1 
ATOM   1961 C C   . PRO   A 1 252 ? 21.53493  10.28662 -32.60772 1.000 48.84266  ? 252 PRO   A C   1 
ATOM   1962 O O   . PRO   A 1 252 ? 22.30187  9.31527  -32.64944 1.000 46.28565  ? 252 PRO   A O   1 
ATOM   1963 C CB  . PRO   A 1 252 ? 21.34137  11.60091 -30.45741 1.000 47.66344  ? 252 PRO   A CB  1 
ATOM   1964 C CG  . PRO   A 1 252 ? 21.13253  13.05467 -30.20066 1.000 46.71346  ? 252 PRO   A CG  1 
ATOM   1965 C CD  . PRO   A 1 252 ? 20.77714  13.65320 -31.52828 1.000 46.00592  ? 252 PRO   A CD  1 
ATOM   1966 N N   . LEU   A 1 253 ? 20.33686  10.27639 -33.19898 1.000 47.04110  ? 253 LEU   A N   1 
ATOM   1967 C CA  . LEU   A 1 253 ? 19.92622  9.13619  -34.01261 1.000 46.18618  ? 253 LEU   A CA  1 
ATOM   1968 C C   . LEU   A 1 253 ? 20.82521  8.98402  -35.23190 1.000 47.92736  ? 253 LEU   A C   1 
ATOM   1969 O O   . LEU   A 1 253 ? 21.24177  7.87062  -35.57248 1.000 50.42447  ? 253 LEU   A O   1 
ATOM   1970 C CB  . LEU   A 1 253 ? 18.46717  9.29202  -34.44128 1.000 44.42532  ? 253 LEU   A CB  1 
ATOM   1971 C CG  . LEU   A 1 253 ? 17.45856  8.35028  -33.78380 1.000 42.73024  ? 253 LEU   A CG  1 
ATOM   1972 C CD1 . LEU   A 1 253 ? 16.03842  8.80090  -34.08600 1.000 44.53969  ? 253 LEU   A CD1 1 
ATOM   1973 C CD2 . LEU   A 1 253 ? 17.68217  6.91984  -34.24266 1.000 46.47973  ? 253 LEU   A CD2 1 
ATOM   1974 N N   . SER   A 1 254 ? 21.13606  10.09756 -35.89990 1.000 44.09776  ? 254 SER   A N   1 
ATOM   1975 C CA  . SER   A 1 254 ? 22.05717  10.06424 -37.03034 1.000 46.27458  ? 254 SER   A CA  1 
ATOM   1976 C C   . SER   A 1 254 ? 23.44037  9.57819  -36.61829 1.000 47.40101  ? 254 SER   A C   1 
ATOM   1977 O O   . SER   A 1 254 ? 24.17904  9.03072  -37.44557 1.000 45.30621  ? 254 SER   A O   1 
ATOM   1978 C CB  . SER   A 1 254 ? 22.15008  11.45366 -37.65757 1.000 44.46432  ? 254 SER   A CB  1 
ATOM   1979 O OG  . SER   A 1 254 ? 22.99420  11.44884 -38.79409 1.000 48.39208  ? 254 SER   A OG  1 
ATOM   1980 N N   . ALA   A 1 255 ? 23.80912  9.77004  -35.35088 1.000 45.15801  ? 255 ALA   A N   1 
ATOM   1981 C CA  . ALA   A 1 255 ? 25.11604  9.32702  -34.88150 1.000 48.77024  ? 255 ALA   A CA  1 
ATOM   1982 C C   . ALA   A 1 255 ? 25.13775  7.82719  -34.61230 1.000 47.56960  ? 255 ALA   A C   1 
ATOM   1983 O O   . ALA   A 1 255 ? 26.15588  7.16780  -34.84816 1.000 43.19147  ? 255 ALA   A O   1 
ATOM   1984 C CB  . ALA   A 1 255 ? 25.51169  10.10117 -33.62379 1.000 46.94596  ? 255 ALA   A CB  1 
ATOM   1985 N N   . GLN   A 1 256 ? 24.02576  7.27096  -34.12474 1.000 50.20865  ? 256 GLN   A N   1 
ATOM   1986 C CA  . GLN   A 1 256 ? 23.99501  5.84976  -33.79476 1.000 50.94870  ? 256 GLN   A CA  1 
ATOM   1987 C C   . GLN   A 1 256 ? 23.97518  4.97808  -35.04390 1.000 49.74748  ? 256 GLN   A C   1 
ATOM   1988 O O   . GLN   A 1 256 ? 24.53918  3.87784  -35.03968 1.000 50.90033  ? 256 GLN   A O   1 
ATOM   1989 C CB  . GLN   A 1 256 ? 22.78269  5.54086  -32.91611 1.000 50.27295  ? 256 GLN   A CB  1 
ATOM   1990 C CG  . GLN   A 1 256 ? 22.81381  4.16051  -32.27669 1.000 57.77232  ? 256 GLN   A CG  1 
ATOM   1991 C CD  . GLN   A 1 256 ? 21.43106  3.65182  -31.91676 1.000 56.32087  ? 256 GLN   A CD  1 
ATOM   1992 O OE1 . GLN   A 1 256 ? 20.65302  4.34531  -31.26195 1.000 52.65166  ? 256 GLN   A OE1 1 
ATOM   1993 N NE2 . GLN   A 1 256 ? 21.11938  2.43239  -32.34214 1.000 59.85643  ? 256 GLN   A NE2 1 
ATOM   1994 N N   . THR   A 1 257 ? 23.33878  5.44568  -36.11592 1.000 49.71768  ? 257 THR   A N   1 
ATOM   1995 C CA  . THR   A 1 257 ? 23.21889  4.67335  -37.34341 1.000 47.25664  ? 257 THR   A CA  1 
ATOM   1996 C C   . THR   A 1 257 ? 24.28234  5.01648  -38.37740 1.000 47.52370  ? 257 THR   A C   1 
ATOM   1997 O O   . THR   A 1 257 ? 24.41894  4.28706  -39.36538 1.000 50.88998  ? 257 THR   A O   1 
ATOM   1998 C CB  . THR   A 1 257 ? 21.82895  4.87584  -37.95679 1.000 48.08212  ? 257 THR   A CB  1 
ATOM   1999 O OG1 . THR   A 1 257 ? 21.74211  6.19047  -38.52059 1.000 48.35970  ? 257 THR   A OG1 1 
ATOM   2000 C CG2 . THR   A 1 257 ? 20.75228  4.71101  -36.89433 1.000 46.92201  ? 257 THR   A CG2 1 
ATOM   2001 N N   . GLY   A 1 258 ? 25.03282  6.09707  -38.17842 1.000 47.64080  ? 258 GLY   A N   1 
ATOM   2002 C CA  . GLY   A 1 258 ? 26.07266  6.47610  -39.11080 1.000 47.32732  ? 258 GLY   A CA  1 
ATOM   2003 C C   . GLY   A 1 258 ? 25.59452  7.16316  -40.36853 1.000 47.29847  ? 258 GLY   A C   1 
ATOM   2004 O O   . GLY   A 1 258 ? 26.40908  7.41108  -41.26490 1.000 47.39485  ? 258 GLY   A O   1 
ATOM   2005 N N   . ILE   A 1 259 ? 24.30585  7.47630  -40.46942 1.000 46.19014  ? 259 ILE   A N   1 
ATOM   2006 C CA  . ILE   A 1 259 ? 23.74263  8.14224  -41.63770 1.000 47.48319  ? 259 ILE   A CA  1 
ATOM   2007 C C   . ILE   A 1 259 ? 23.55935  9.61232  -41.30014 1.000 48.19975  ? 259 ILE   A C   1 
ATOM   2008 O O   . ILE   A 1 259 ? 22.87345  9.94973  -40.32838 1.000 47.29783  ? 259 ILE   A O   1 
ATOM   2009 C CB  . ILE   A 1 259 ? 22.40323  7.51817  -42.05695 1.000 49.40060  ? 259 ILE   A CB  1 
ATOM   2010 C CG1 . ILE   A 1 259 ? 22.51006  5.99955  -42.14183 1.000 47.78321  ? 259 ILE   A CG1 1 
ATOM   2011 C CG2 . ILE   A 1 259 ? 21.94490  8.09370  -43.38778 1.000 48.64518  ? 259 ILE   A CG2 1 
ATOM   2012 C CD1 . ILE   A 1 259 ? 21.32234  5.30061  -41.55309 1.000 52.44311  ? 259 ILE   A CD1 1 
ATOM   2013 N N   . ALA   A 1 260 ? 24.16146  10.48668 -42.10133 1.000 48.18768  ? 260 ALA   A N   1 
ATOM   2014 C CA  . ALA   A 1 260 ? 23.94198  11.91455 -41.93068 1.000 44.42181  ? 260 ALA   A CA  1 
ATOM   2015 C C   . ALA   A 1 260 ? 22.45886  12.23978 -42.06476 1.000 48.63637  ? 260 ALA   A C   1 
ATOM   2016 O O   . ALA   A 1 260 ? 21.71468  11.56613 -42.78308 1.000 47.43022  ? 260 ALA   A O   1 
ATOM   2017 C CB  . ALA   A 1 260 ? 24.75211  12.70575 -42.95628 1.000 44.73068  ? 260 ALA   A CB  1 
ATOM   2018 N N   . VAL   A 1 261 ? 22.02808  13.28180 -41.34943 1.000 46.98524  ? 261 VAL   A N   1 
ATOM   2019 C CA  . VAL   A 1 261 ? 20.62039  13.67021 -41.38147 1.000 43.29887  ? 261 VAL   A CA  1 
ATOM   2020 C C   . VAL   A 1 261 ? 20.20621  14.05587 -42.79532 1.000 43.94371  ? 261 VAL   A C   1 
ATOM   2021 O O   . VAL   A 1 261 ? 19.13405  13.66544 -43.27312 1.000 42.03411  ? 261 VAL   A O   1 
ATOM   2022 C CB  . VAL   A 1 261 ? 20.35498  14.81275 -40.38284 1.000 40.48386  ? 261 VAL   A CB  1 
ATOM   2023 C CG1 . VAL   A 1 261 ? 18.92893  15.32656 -40.52325 1.000 40.53282  ? 261 VAL   A CG1 1 
ATOM   2024 C CG2 . VAL   A 1 261 ? 20.61213  14.35078 -38.96399 1.000 38.06164  ? 261 VAL   A CG2 1 
ATOM   2025 N N   . LEU   A 1 262 ? 21.05254  14.81594 -43.49252 1.000 47.74196  ? 262 LEU   A N   1 
ATOM   2026 C CA  . LEU   A 1 262 ? 20.71132  15.25746 -44.83913 1.000 47.11180  ? 262 LEU   A CA  1 
ATOM   2027 C C   . LEU   A 1 262 ? 20.80453  14.13031 -45.86121 1.000 48.42646  ? 262 LEU   A C   1 
ATOM   2028 O O   . LEU   A 1 262 ? 20.20278  14.23533 -46.93523 1.000 46.51253  ? 262 LEU   A O   1 
ATOM   2029 C CB  . LEU   A 1 262 ? 21.60741  16.42844 -45.24376 1.000 44.59338  ? 262 LEU   A CB  1 
ATOM   2030 C CG  . LEU   A 1 262 ? 21.21524  17.76101 -44.59901 1.000 44.68523  ? 262 LEU   A CG  1 
ATOM   2031 C CD1 . LEU   A 1 262 ? 21.89848  18.92585 -45.29108 1.000 47.17320  ? 262 LEU   A CD1 1 
ATOM   2032 C CD2 . LEU   A 1 262 ? 19.70291  17.94576 -44.60914 1.000 43.60663  ? 262 LEU   A CD2 1 
ATOM   2033 N N   . ASP   A 1 263 ? 21.54318  13.05954 -45.55736 1.000 47.18757  ? 263 ASP   A N   1 
ATOM   2034 C CA  . ASP   A 1 263 ? 21.49744  11.87373 -46.40716 1.000 45.40952  ? 263 ASP   A CA  1 
ATOM   2035 C C   . ASP   A 1 263 ? 20.14221  11.18502 -46.30655 1.000 45.41899  ? 263 ASP   A C   1 
ATOM   2036 O O   . ASP   A 1 263 ? 19.57281  10.76850 -47.32236 1.000 47.92434  ? 263 ASP   A O   1 
ATOM   2037 C CB  . ASP   A 1 263 ? 22.62049  10.90630 -46.03050 1.000 51.78353  ? 263 ASP   A CB  1 
ATOM   2038 C CG  . ASP   A 1 263 ? 23.98594  11.38729 -46.48563 1.000 64.37681  ? 263 ASP   A CG  1 
ATOM   2039 O OD1 . ASP   A 1 263 ? 24.21069  12.61656 -46.50747 1.000 60.33501  ? 263 ASP   A OD1 1 
ATOM   2040 O OD2 . ASP   A 1 263 ? 24.83444  10.53183 -46.82056 1.000 66.65874  ? 263 ASP   A OD2 1 
ATOM   2041 N N   . MET   A 1 264 ? 19.61008  11.05866 -45.08755 1.000 45.04607  ? 264 MET   A N   1 
ATOM   2042 C CA  . MET   A 1 264 ? 18.27433  10.49845 -44.91523 1.000 45.31926  ? 264 MET   A CA  1 
ATOM   2043 C C   . MET   A 1 264 ? 17.21002  11.39295 -45.53882 1.000 44.72548  ? 264 MET   A C   1 
ATOM   2044 O O   . MET   A 1 264 ? 16.16256  10.90027 -45.97354 1.000 41.73182  ? 264 MET   A O   1 
ATOM   2045 C CB  . MET   A 1 264 ? 17.98609  10.27933 -43.42907 1.000 44.15949  ? 264 MET   A CB  1 
ATOM   2046 C CG  . MET   A 1 264 ? 16.76618  9.41520  -43.14869 1.000 43.69318  ? 264 MET   A CG  1 
ATOM   2047 S SD  . MET   A 1 264 ? 17.01100  7.68879  -43.61234 1.000 44.02675  ? 264 MET   A SD  1 
ATOM   2048 C CE  . MET   A 1 264 ? 18.09981  7.13262  -42.30547 1.000 41.00622  ? 264 MET   A CE  1 
ATOM   2049 N N   . CYS   A 1 265 ? 17.45579  12.70563 -45.58847 1.000 43.16951  ? 265 CYS   A N   1 
ATOM   2050 C CA  . CYS   A 1 265 ? 16.53447  13.60684 -46.27389 1.000 41.92372  ? 265 CYS   A CA  1 
ATOM   2051 C C   . CYS   A 1 265 ? 16.52961  13.34915 -47.77425 1.000 45.54418  ? 265 CYS   A C   1 
ATOM   2052 O O   . CYS   A 1 265 ? 15.46884  13.36830 -48.41061 1.000 44.00745  ? 265 CYS   A O   1 
ATOM   2053 C CB  . CYS   A 1 265 ? 16.90646  15.05953 -45.98380 1.000 39.97390  ? 265 CYS   A CB  1 
ATOM   2054 S SG  . CYS   A 1 265 ? 16.43704  15.62659 -44.33905 1.000 40.73393  ? 265 CYS   A SG  1 
ATOM   2055 N N   . ALA   A 1 266 ? 17.70786  13.11092 -48.35669 1.000 42.17935  ? 266 ALA   A N   1 
ATOM   2056 C CA  . ALA   A 1 266 ? 17.77646  12.76743 -49.77197 1.000 45.02351  ? 266 ALA   A CA  1 
ATOM   2057 C C   . ALA   A 1 266 ? 17.05082  11.46166 -50.06301 1.000 46.22428  ? 266 ALA   A C   1 
ATOM   2058 O O   . ALA   A 1 266 ? 16.51816  11.27891 -51.16358 1.000 48.22841  ? 266 ALA   A O   1 
ATOM   2059 C CB  . ALA   A 1 266 ? 19.23414  12.67816 -50.22212 1.000 47.08569  ? 266 ALA   A CB  1 
ATOM   2060 N N   . SER   A 1 267 ? 17.01667  10.54484 -49.09360 1.000 46.35635  ? 267 SER   A N   1 
ATOM   2061 C CA  . SER   A 1 267 ? 16.26850  9.30677  -49.27886 1.000 46.11016  ? 267 SER   A CA  1 
ATOM   2062 C C   . SER   A 1 267 ? 14.76773  9.55130  -49.17679 1.000 45.07945  ? 267 SER   A C   1 
ATOM   2063 O O   . SER   A 1 267 ? 13.98376  8.95307  -49.92275 1.000 44.59887  ? 267 SER   A O   1 
ATOM   2064 C CB  . SER   A 1 267 ? 16.71908  8.26555  -48.25543 1.000 48.21509  ? 267 SER   A CB  1 
ATOM   2065 O OG  . SER   A 1 267 ? 17.96476  7.69783  -48.62481 1.000 53.36778  ? 267 SER   A OG  1 
ATOM   2066 N N   . LEU   A 1 268 ? 14.34907  10.42925 -48.26107 1.000 44.45305  ? 268 LEU   A N   1 
ATOM   2067 C CA  . LEU   A 1 268 ? 12.93167  10.75822 -48.14711 1.000 43.52974  ? 268 LEU   A CA  1 
ATOM   2068 C C   . LEU   A 1 268 ? 12.45837  11.56709 -49.34818 1.000 44.44354  ? 268 LEU   A C   1 
ATOM   2069 O O   . LEU   A 1 268 ? 11.32107  11.40174 -49.80539 1.000 45.04308  ? 268 LEU   A O   1 
ATOM   2070 C CB  . LEU   A 1 268 ? 12.67122  11.51977 -46.84679 1.000 42.20994  ? 268 LEU   A CB  1 
ATOM   2071 C CG  . LEU   A 1 268 ? 11.24229  12.00822 -46.58477 1.000 39.41733  ? 268 LEU   A CG  1 
ATOM   2072 C CD1 . LEU   A 1 268 ? 10.22619  10.89178 -46.79047 1.000 36.50068  ? 268 LEU   A CD1 1 
ATOM   2073 C CD2 . LEU   A 1 268 ? 11.12402  12.58960 -45.18440 1.000 34.91957  ? 268 LEU   A CD2 1 
ATOM   2074 N N   . LYS   A 1 269 ? 13.31580  12.44983 -49.86830 1.000 46.35781  ? 269 LYS   A N   1 
ATOM   2075 C CA  . LYS   A 1 269 ? 12.97857  13.18439 -51.08340 1.000 46.19685  ? 269 LYS   A CA  1 
ATOM   2076 C C   . LYS   A 1 269 ? 12.69398  12.23041 -52.23599 1.000 48.58783  ? 269 LYS   A C   1 
ATOM   2077 O O   . LYS   A 1 269 ? 11.74699  12.43498 -53.00404 1.000 47.85731  ? 269 LYS   A O   1 
ATOM   2078 C CB  . LYS   A 1 269 ? 14.11317  14.14293 -51.44637 1.000 49.06114  ? 269 LYS   A CB  1 
ATOM   2079 C CG  . LYS   A 1 269 ? 13.97857  14.78253 -52.81756 1.000 53.17939  ? 269 LYS   A CG  1 
ATOM   2080 C CD  . LYS   A 1 269 ? 14.64262  16.15005 -52.85421 1.000 54.26664  ? 269 LYS   A CD  1 
ATOM   2081 C CE  . LYS   A 1 269 ? 16.15668  16.03291 -52.92779 1.000 51.66035  ? 269 LYS   A CE  1 
ATOM   2082 N NZ  . LYS   A 1 269 ? 16.68976  16.55929 -54.21583 1.000 56.34591  ? 269 LYS   A NZ  1 
ATOM   2083 N N   . GLU   A 1 270 ? 13.49894  11.17314 -52.36383 1.000 48.86133  ? 270 GLU   A N   1 
ATOM   2084 C CA  . GLU   A 1 270 ? 13.26067  10.17674 -53.40160 1.000 53.08888  ? 270 GLU   A CA  1 
ATOM   2085 C C   . GLU   A 1 270 ? 11.99491  9.37320  -53.13114 1.000 50.10148  ? 270 GLU   A C   1 
ATOM   2086 O O   . GLU   A 1 270 ? 11.31164  8.96149  -54.07494 1.000 50.19988  ? 270 GLU   A O   1 
ATOM   2087 C CB  . GLU   A 1 270 ? 14.46660  9.24415  -53.51439 1.000 49.26898  ? 270 GLU   A CB  1 
ATOM   2088 C CG  . GLU   A 1 270 ? 14.84969  8.88193  -54.93801 1.000 52.55224  ? 270 GLU   A CG  1 
ATOM   2089 C CD  . GLU   A 1 270 ? 15.74173  7.65815  -55.00238 1.000 61.70759  ? 270 GLU   A CD  1 
ATOM   2090 O OE1 . GLU   A 1 270 ? 16.94648  7.78287  -54.69655 1.000 64.50938  ? 270 GLU   A OE1 1 
ATOM   2091 O OE2 . GLU   A 1 270 ? 15.23969  6.57161  -55.35848 1.000 64.63681  ? 270 GLU   A OE2 1 
ATOM   2092 N N   . LEU   A 1 271 ? 11.66601  9.14381  -51.85745 1.000 48.14825  ? 271 LEU   A N   1 
ATOM   2093 C CA  . LEU   A 1 271 ? 10.48325  8.35560  -51.52486 1.000 47.36080  ? 271 LEU   A CA  1 
ATOM   2094 C C   . LEU   A 1 271 ? 9.20055   9.07358  -51.92775 1.000 50.04572  ? 271 LEU   A C   1 
ATOM   2095 O O   . LEU   A 1 271 ? 8.24333   8.43662  -52.38305 1.000 51.89829  ? 271 LEU   A O   1 
ATOM   2096 C CB  . LEU   A 1 271 ? 10.46702  8.04274  -50.02856 1.000 44.88546  ? 271 LEU   A CB  1 
ATOM   2097 C CG  . LEU   A 1 271 ? 11.36795  6.91436  -49.52595 1.000 43.29325  ? 271 LEU   A CG  1 
ATOM   2098 C CD1 . LEU   A 1 271 ? 11.41193  6.91179  -48.00686 1.000 42.19062  ? 271 LEU   A CD1 1 
ATOM   2099 C CD2 . LEU   A 1 271 ? 10.88777  5.57338  -50.04972 1.000 44.83958  ? 271 LEU   A CD2 1 
ATOM   2100 N N   . LEU   A 1 272 ? 9.16087   10.39772 -51.77101 1.000 45.31080  ? 272 LEU   A N   1 
ATOM   2101 C CA  . LEU   A 1 272 ? 7.92293   11.13314 -52.00171 1.000 48.10500  ? 272 LEU   A CA  1 
ATOM   2102 C C   . LEU   A 1 272 ? 7.62063   11.31775 -53.48385 1.000 47.75442  ? 272 LEU   A C   1 
ATOM   2103 O O   . LEU   A 1 272 ? 6.44841   11.30468 -53.87602 1.000 47.29220  ? 272 LEU   A O   1 
ATOM   2104 C CB  . LEU   A 1 272 ? 7.98452   12.49058 -51.30049 1.000 45.68264  ? 272 LEU   A CB  1 
ATOM   2105 C CG  . LEU   A 1 272 ? 8.02563   12.42314 -49.77285 1.000 41.22617  ? 272 LEU   A CG  1 
ATOM   2106 C CD1 . LEU   A 1 272 ? 8.29493   13.79512 -49.18398 1.000 44.25724  ? 272 LEU   A CD1 1 
ATOM   2107 C CD2 . LEU   A 1 272 ? 6.72826   11.84559 -49.22777 1.000 39.67158  ? 272 LEU   A CD2 1 
ATOM   2108 N N   . GLN   A 1 273 ? 8.64389   11.48525 -54.31727 1.000 51.09686  ? 273 GLN   A N   1 
ATOM   2109 C CA  . GLN   A 1 273 ? 8.44001   11.69181 -55.74464 1.000 52.40107  ? 273 GLN   A CA  1 
ATOM   2110 C C   . GLN   A 1 273 ? 8.47087   10.39742 -56.54714 1.000 51.61481  ? 273 GLN   A C   1 
ATOM   2111 O O   . GLN   A 1 273 ? 8.22065   10.43239 -57.75602 1.000 53.31778  ? 273 GLN   A O   1 
ATOM   2112 C CB  . GLN   A 1 273 ? 9.48806   12.66718 -56.29577 1.000 48.57659  ? 273 GLN   A CB  1 
ATOM   2113 C CG  . GLN   A 1 273 ? 10.93017  12.26363 -56.03259 1.000 51.80006  ? 273 GLN   A CG  1 
ATOM   2114 C CD  . GLN   A 1 273 ? 11.87170  13.45584 -55.98490 1.000 53.41213  ? 273 GLN   A CD  1 
ATOM   2115 O OE1 . GLN   A 1 273 ? 11.46216  14.59465 -56.21098 1.000 53.66565  ? 273 GLN   A OE1 1 
ATOM   2116 N NE2 . GLN   A 1 273 ? 13.14022  13.19771 -55.68577 1.000 52.81671  ? 273 GLN   A NE2 1 
ATOM   2117 N N   . ASN   A 1 274 ? 8.76333   9.26095  -55.91177 1.000 47.69972  ? 274 ASN   A N   1 
ATOM   2118 C CA  . ASN   A 1 274 ? 8.81780   7.98116  -56.60611 1.000 51.56856  ? 274 ASN   A CA  1 
ATOM   2119 C C   . ASN   A 1 274 ? 7.95091   6.89572  -55.98568 1.000 53.69651  ? 274 ASN   A C   1 
ATOM   2120 O O   . ASN   A 1 274 ? 7.79851   5.83483  -56.60160 1.000 56.73903  ? 274 ASN   A O   1 
ATOM   2121 C CB  . ASN   A 1 274 ? 10.26326  7.46165  -56.67297 1.000 54.16656  ? 274 ASN   A CB  1 
ATOM   2122 C CG  . ASN   A 1 274 ? 11.18035  8.37447  -57.46297 1.000 55.23521  ? 274 ASN   A CG  1 
ATOM   2123 O OD1 . ASN   A 1 274 ? 10.72633  9.25382  -58.19449 1.000 56.24943  ? 274 ASN   A OD1 1 
ATOM   2124 N ND2 . ASN   A 1 274 ? 12.48354  8.16872  -57.31623 1.000 54.93927  ? 274 ASN   A ND2 1 
ATOM   2125 N N   . GLY   A 1 275 ? 7.38930   7.11269  -54.80042 1.000 50.99677  ? 275 GLY   A N   1 
ATOM   2126 C CA  . GLY   A 1 275 ? 6.63690   6.06623  -54.14387 1.000 52.89933  ? 275 GLY   A CA  1 
ATOM   2127 C C   . GLY   A 1 275 ? 7.54464   4.95256  -53.64225 1.000 56.13858  ? 275 GLY   A C   1 
ATOM   2128 O O   . GLY   A 1 275 ? 8.77297   5.03799  -53.66879 1.000 57.67950  ? 275 GLY   A O   1 
ATOM   2129 N N   . MET   A 1 276 ? 6.90265   3.88149  -53.17699 1.000 56.23715  ? 276 MET   A N   1 
ATOM   2130 C CA  . MET   A 1 276 ? 7.62892   2.73376  -52.65189 1.000 58.49625  ? 276 MET   A CA  1 
ATOM   2131 C C   . MET   A 1 276 ? 7.83126   1.62472  -53.67516 1.000 60.46266  ? 276 MET   A C   1 
ATOM   2132 O O   . MET   A 1 276 ? 8.67166   0.74667  -53.44964 1.000 63.89466  ? 276 MET   A O   1 
ATOM   2133 C CB  . MET   A 1 276 ? 6.90746   2.16569  -51.42405 1.000 56.41800  ? 276 MET   A CB  1 
ATOM   2134 C CG  . MET   A 1 276 ? 6.71699   3.17488  -50.30083 1.000 55.67178  ? 276 MET   A CG  1 
ATOM   2135 S SD  . MET   A 1 276 ? 6.65887   2.39639  -48.67470 1.000 60.79989  ? 276 MET   A SD  1 
ATOM   2136 C CE  . MET   A 1 276 ? 6.07352   3.75094  -47.65985 1.000 48.63184  ? 276 MET   A CE  1 
ATOM   2137 N N   . ASN   A 1 277 ? 7.08705   1.64536  -54.78313 1.000 59.60182  ? 277 ASN   A N   1 
ATOM   2138 C CA  . ASN   A 1 277 ? 7.24126   0.67457  -55.86898 1.000 63.72964  ? 277 ASN   A CA  1 
ATOM   2139 C C   . ASN   A 1 277 ? 7.04550   -0.75773 -55.36979 1.000 67.51426  ? 277 ASN   A C   1 
ATOM   2140 O O   . ASN   A 1 277 ? 7.87069   -1.64361 -55.60387 1.000 63.64599  ? 277 ASN   A O   1 
ATOM   2141 C CB  . ASN   A 1 277 ? 8.59717   0.83675  -56.56250 1.000 66.72489  ? 277 ASN   A CB  1 
ATOM   2142 C CG  . ASN   A 1 277 ? 8.48741   1.54610  -57.89987 1.000 68.23888  ? 277 ASN   A CG  1 
ATOM   2143 O OD1 . ASN   A 1 277 ? 8.21240   0.92313  -58.92584 1.000 69.36563  ? 277 ASN   A OD1 1 
ATOM   2144 N ND2 . ASN   A 1 277 ? 8.70286   2.85648  -57.89433 1.000 65.27454  ? 277 ASN   A ND2 1 
ATOM   2145 N N   . GLY   A 1 278 ? 5.93260   -0.97957 -54.67002 1.000 67.92422  ? 278 GLY   A N   1 
ATOM   2146 C CA  . GLY   A 1 278 ? 5.56195   -2.30075 -54.21081 1.000 67.60972  ? 278 GLY   A CA  1 
ATOM   2147 C C   . GLY   A 1 278 ? 6.24619   -2.77221 -52.94767 1.000 66.06154  ? 278 GLY   A C   1 
ATOM   2148 O O   . GLY   A 1 278 ? 5.87251   -3.82854 -52.42111 1.000 65.79175  ? 278 GLY   A O   1 
ATOM   2149 N N   . ARG   A 1 279 ? 7.22882   -2.03679 -52.44045 1.000 66.06749  ? 279 ARG   A N   1 
ATOM   2150 C CA  . ARG   A 1 279 ? 7.93603   -2.43285 -51.23361 1.000 59.23070  ? 279 ARG   A CA  1 
ATOM   2151 C C   . ARG   A 1 279 ? 7.29764   -1.79751 -50.00207 1.000 56.51585  ? 279 ARG   A C   1 
ATOM   2152 O O   . ARG   A 1 279 ? 6.56977   -0.80580 -50.08693 1.000 58.36740  ? 279 ARG   A O   1 
ATOM   2153 C CB  . ARG   A 1 279 ? 9.41272   -2.04392 -51.32287 1.000 55.76987  ? 279 ARG   A CB  1 
ATOM   2154 C CG  . ARG   A 1 279 ? 10.04038  -2.31826 -52.67964 1.000 54.58814  ? 279 ARG   A CG  1 
ATOM   2155 C CD  . ARG   A 1 279 ? 11.51748  -2.66252 -52.55603 1.000 50.83997  ? 279 ARG   A CD  1 
ATOM   2156 N NE  . ARG   A 1 279 ? 11.77269  -3.63031 -51.49525 1.000 52.70704  ? 279 ARG   A NE  1 
ATOM   2157 C CZ  . ARG   A 1 279 ? 12.89623  -4.32368 -51.36727 1.000 50.47872  ? 279 ARG   A CZ  1 
ATOM   2158 N NH1 . ARG   A 1 279 ? 13.89313  -4.19044 -52.22748 1.000 50.09439  ? 279 ARG   A NH1 1 
ATOM   2159 N NH2 . ARG   A 1 279 ? 13.02210  -5.17370 -50.35188 1.000 46.04780  ? 279 ARG   A NH2 1 
ATOM   2160 N N   . THR   A 1 280 ? 7.57682   -2.39317 -48.84601 1.000 55.45466  ? 280 THR   A N   1 
ATOM   2161 C CA  . THR   A 1 280 ? 7.10016   -1.89458 -47.56587 1.000 50.61187  ? 280 THR   A CA  1 
ATOM   2162 C C   . THR   A 1 280 ? 8.28540   -1.54355 -46.67672 1.000 49.76259  ? 280 THR   A C   1 
ATOM   2163 O O   . THR   A 1 280 ? 9.37744   -2.09997 -46.82183 1.000 51.14860  ? 280 THR   A O   1 
ATOM   2164 C CB  . THR   A 1 280 ? 6.21332   -2.92596 -46.85242 1.000 51.81648  ? 280 THR   A CB  1 
ATOM   2165 O OG1 . THR   A 1 280 ? 7.00369   -4.06188 -46.48117 1.000 51.70829  ? 280 THR   A OG1 1 
ATOM   2166 C CG2 . THR   A 1 280 ? 5.07813   -3.37929 -47.75982 1.000 57.83860  ? 280 THR   A CG2 1 
ATOM   2167 N N   . ILE   A 1 281 ? 8.06009   -0.61270 -45.75424 1.000 46.88339  ? 281 ILE   A N   1 
ATOM   2168 C CA  . ILE   A 1 281 ? 9.04708   -0.22407 -44.75388 1.000 46.24784  ? 281 ILE   A CA  1 
ATOM   2169 C C   . ILE   A 1 281 ? 8.47332   -0.58083 -43.38993 1.000 45.09827  ? 281 ILE   A C   1 
ATOM   2170 O O   . ILE   A 1 281 ? 7.39556   -0.09529 -43.02307 1.000 44.99455  ? 281 ILE   A O   1 
ATOM   2171 C CB  . ILE   A 1 281 ? 9.38398   1.27304  -44.83490 1.000 46.00032  ? 281 ILE   A CB  1 
ATOM   2172 C CG1 . ILE   A 1 281 ? 9.89372   1.63857  -46.23137 1.000 47.47614  ? 281 ILE   A CG1 1 
ATOM   2173 C CG2 . ILE   A 1 281 ? 10.40818  1.64260  -43.78092 1.000 43.37966  ? 281 ILE   A CG2 1 
ATOM   2174 C CD1 . ILE   A 1 281 ? 10.30523  3.08942  -46.37161 1.000 42.61313  ? 281 ILE   A CD1 1 
ATOM   2175 N N   . LEU   A 1 282 ? 9.18383   -1.43513 -42.64651 1.000 45.64104  ? 282 LEU   A N   1 
ATOM   2176 C CA  . LEU   A 1 282 ? 8.71812   -1.91895 -41.34277 1.000 44.28666  ? 282 LEU   A CA  1 
ATOM   2177 C C   . LEU   A 1 282 ? 7.36638   -2.62287 -41.45670 1.000 47.51559  ? 282 LEU   A C   1 
ATOM   2178 O O   . LEU   A 1 282 ? 6.50510   -2.50985 -40.58153 1.000 43.59003  ? 282 LEU   A O   1 
ATOM   2179 C CB  . LEU   A 1 282 ? 8.67842   -0.78065 -40.31849 1.000 41.56393  ? 282 LEU   A CB  1 
ATOM   2180 C CG  . LEU   A 1 282 ? 9.91339   -0.70241 -39.41584 1.000 41.02915  ? 282 LEU   A CG  1 
ATOM   2181 C CD1 . LEU   A 1 282 ? 11.18061  -1.08294 -40.14496 1.000 48.43228  ? 282 LEU   A CD1 1 
ATOM   2182 C CD2 . LEU   A 1 282 ? 10.06486  0.69611  -38.86156 1.000 44.66843  ? 282 LEU   A CD2 1 
ATOM   2183 N N   . GLY   A 1 283 ? 7.19038   -3.37695 -42.54014 1.000 48.46603  ? 283 GLY   A N   1 
ATOM   2184 C CA  . GLY   A 1 283 ? 5.93141   -4.04800 -42.78349 1.000 46.69322  ? 283 GLY   A CA  1 
ATOM   2185 C C   . GLY   A 1 283 ? 4.77083   -3.11911 -43.04559 1.000 51.74782  ? 283 GLY   A C   1 
ATOM   2186 O O   . GLY   A 1 283 ? 3.61818   -3.50606 -42.83536 1.000 55.26494  ? 283 GLY   A O   1 
ATOM   2187 N N   . SER   A 1 284 ? 5.04012   -1.89719 -43.49982 1.000 50.36856  ? 284 SER   A N   1 
ATOM   2188 C CA  . SER   A 1 284 ? 4.00305   -0.90116 -43.73010 1.000 48.21741  ? 284 SER   A CA  1 
ATOM   2189 C C   . SER   A 1 284 ? 4.12594   -0.34470 -45.13951 1.000 49.36292  ? 284 SER   A C   1 
ATOM   2190 O O   . SER   A 1 284 ? 5.21745   0.04788  -45.56389 1.000 49.33873  ? 284 SER   A O   1 
ATOM   2191 C CB  . SER   A 1 284 ? 4.09316   0.23941  -42.71531 1.000 46.78659  ? 284 SER   A CB  1 
ATOM   2192 O OG  . SER   A 1 284 ? 3.65001   1.45287  -43.29657 1.000 50.28606  ? 284 SER   A OG  1 
ATOM   2193 N N   . ALA   A 1 285 ? 3.00303   -0.29772 -45.85551 1.000 50.21230  ? 285 ALA   A N   1 
ATOM   2194 C CA  . ALA   A 1 285 ? 2.98572   0.25807  -47.20158 1.000 50.56471  ? 285 ALA   A CA  1 
ATOM   2195 C C   . ALA   A 1 285 ? 2.90272   1.77891  -47.21232 1.000 49.59240  ? 285 ALA   A C   1 
ATOM   2196 O O   . ALA   A 1 285 ? 3.03546   2.38365  -48.28184 1.000 49.34777  ? 285 ALA   A O   1 
ATOM   2197 C CB  . ALA   A 1 285 ? 1.81843   -0.33163 -47.99700 1.000 51.54555  ? 285 ALA   A CB  1 
ATOM   2198 N N   . LEU   A 1 286 ? 2.69600   2.40473  -46.05745 1.000 48.89402  ? 286 LEU   A N   1 
ATOM   2199 C CA  . LEU   A 1 286 ? 2.61480   3.85080  -45.93664 1.000 48.10594  ? 286 LEU   A CA  1 
ATOM   2200 C C   . LEU   A 1 286 ? 3.72801   4.35015  -45.02654 1.000 46.99639  ? 286 LEU   A C   1 
ATOM   2201 O O   . LEU   A 1 286 ? 4.19934   3.62756  -44.14394 1.000 49.30882  ? 286 LEU   A O   1 
ATOM   2202 C CB  . LEU   A 1 286 ? 1.25678   4.28263  -45.36822 1.000 45.28417  ? 286 LEU   A CB  1 
ATOM   2203 C CG  . LEU   A 1 286 ? 0.04010   4.20903  -46.29223 1.000 50.74148  ? 286 LEU   A CG  1 
ATOM   2204 C CD1 . LEU   A 1 286 ? -1.08407  5.08829  -45.76462 1.000 49.28527  ? 286 LEU   A CD1 1 
ATOM   2205 C CD2 . LEU   A 1 286 ? 0.41234   4.60370  -47.71295 1.000 47.74639  ? 286 LEU   A CD2 1 
ATOM   2206 N N   . LEU   A 1 287 ? 4.14631   5.59293  -45.24507 1.000 42.19364  ? 287 LEU   A N   1 
ATOM   2207 C CA  . LEU   A 1 287 ? 5.07670   6.22828  -44.32426 1.000 45.16261  ? 287 LEU   A CA  1 
ATOM   2208 C C   . LEU   A 1 287 ? 4.36164   6.58515  -43.02590 1.000 47.88436  ? 287 LEU   A C   1 
ATOM   2209 O O   . LEU   A 1 287 ? 3.14858   6.80646  -43.00200 1.000 51.36647  ? 287 LEU   A O   1 
ATOM   2210 C CB  . LEU   A 1 287 ? 5.68419   7.47915  -44.95447 1.000 42.71943  ? 287 LEU   A CB  1 
ATOM   2211 C CG  . LEU   A 1 287 ? 6.56976   7.22374  -46.17340 1.000 45.22385  ? 287 LEU   A CG  1 
ATOM   2212 C CD1 . LEU   A 1 287 ? 6.96364   8.53117  -46.83999 1.000 36.87340  ? 287 LEU   A CD1 1 
ATOM   2213 C CD2 . LEU   A 1 287 ? 7.80116   6.42985  -45.77214 1.000 45.38671  ? 287 LEU   A CD2 1 
ATOM   2214 N N   . GLU   A 1 288 ? 5.12502   6.64187  -41.93686 1.000 44.00453  ? 288 GLU   A N   1 
ATOM   2215 C CA  . GLU   A 1 288 ? 4.57357   6.84564  -40.60346 1.000 44.10423  ? 288 GLU   A CA  1 
ATOM   2216 C C   . GLU   A 1 288 ? 5.20148   8.07679  -39.96414 1.000 42.31822  ? 288 GLU   A C   1 
ATOM   2217 O O   . GLU   A 1 288 ? 6.42783   8.23279  -39.97470 1.000 37.24375  ? 288 GLU   A O   1 
ATOM   2218 C CB  . GLU   A 1 288 ? 4.79939   5.61050  -39.72596 1.000 44.71101  ? 288 GLU   A CB  1 
ATOM   2219 C CG  . GLU   A 1 288 ? 4.48896   5.79978  -38.24035 1.000 51.33576  ? 288 GLU   A CG  1 
ATOM   2220 C CD  . GLU   A 1 288 ? 2.99970   5.91293  -37.91771 1.000 57.32748  ? 288 GLU   A CD  1 
ATOM   2221 O OE1 . GLU   A 1 288 ? 2.24368   6.55927  -38.67382 1.000 62.11112  ? 288 GLU   A OE1 1 
ATOM   2222 O OE2 . GLU   A 1 288 ? 2.58316   5.34463  -36.88494 1.000 63.43658  ? 288 GLU   A OE2 1 
ATOM   2223 N N   . ASP   A 1 289 ? 4.35508   8.94705  -39.40572 1.000 40.95163  ? 289 ASP   A N   1 
ATOM   2224 C CA  . ASP   A 1 289 ? 4.79471   10.20157 -38.80466 1.000 40.46332  ? 289 ASP   A CA  1 
ATOM   2225 C C   . ASP   A 1 289 ? 4.34277   10.34327 -37.35270 1.000 39.97717  ? 289 ASP   A C   1 
ATOM   2226 O O   . ASP   A 1 289 ? 4.23299   11.46491 -36.84631 1.000 40.25860  ? 289 ASP   A O   1 
ATOM   2227 C CB  . ASP   A 1 289 ? 4.31079   11.38863 -39.64500 1.000 40.77715  ? 289 ASP   A CB  1 
ATOM   2228 C CG  . ASP   A 1 289 ? 2.85946   11.75661 -39.37591 1.000 43.80344  ? 289 ASP   A CG  1 
ATOM   2229 O OD1 . ASP   A 1 289 ? 2.03781   10.84200 -39.14832 1.000 47.21567  ? 289 ASP   A OD1 1 
ATOM   2230 O OD2 . ASP   A 1 289 ? 2.54439   12.96625 -39.38763 1.000 42.12089  ? 289 ASP   A OD2 1 
ATOM   2231 N N   . GLU   A 1 290 ? 4.09377   9.22996  -36.66180 1.000 39.57527  ? 290 GLU   A N   1 
ATOM   2232 C CA  . GLU   A 1 290 ? 3.66662   9.26588  -35.26859 1.000 42.46495  ? 290 GLU   A CA  1 
ATOM   2233 C C   . GLU   A 1 290 ? 4.71688   8.68968  -34.32198 1.000 41.75483  ? 290 GLU   A C   1 
ATOM   2234 O O   . GLU   A 1 290 ? 4.38137   8.27053  -33.20964 1.000 42.35029  ? 290 GLU   A O   1 
ATOM   2235 C CB  . GLU   A 1 290 ? 2.33313   8.53565  -35.10485 1.000 45.09750  ? 290 GLU   A CB  1 
ATOM   2236 C CG  . GLU   A 1 290 ? 1.18592   9.19776  -35.85781 1.000 47.39796  ? 290 GLU   A CG  1 
ATOM   2237 C CD  . GLU   A 1 290 ? -0.12316  9.17565  -35.08891 1.000 51.22016  ? 290 GLU   A CD  1 
ATOM   2238 O OE1 . GLU   A 1 290 ? -0.29099  8.30062  -34.21200 1.000 53.94162  ? 290 GLU   A OE1 1 
ATOM   2239 O OE2 . GLU   A 1 290 ? -0.98549  10.03809 -35.36398 1.000 49.54812  ? 290 GLU   A OE2 1 
ATOM   2240 N N   . PHE   A 1 291 ? 5.98257   8.66620  -34.74068 1.000 43.26850  ? 291 PHE   A N   1 
ATOM   2241 C CA  . PHE   A 1 291 ? 7.10410   8.25636  -33.89850 1.000 40.82735  ? 291 PHE   A CA  1 
ATOM   2242 C C   . PHE   A 1 291 ? 8.08390   9.41902  -33.80849 1.000 40.40108  ? 291 PHE   A C   1 
ATOM   2243 O O   . PHE   A 1 291 ? 8.75995   9.73959  -34.79088 1.000 39.72467  ? 291 PHE   A O   1 
ATOM   2244 C CB  . PHE   A 1 291 ? 7.79900   7.01531  -34.45898 1.000 42.45779  ? 291 PHE   A CB  1 
ATOM   2245 C CG  . PHE   A 1 291 ? 7.03934   5.74029  -34.24242 1.000 44.94895  ? 291 PHE   A CG  1 
ATOM   2246 C CD1 . PHE   A 1 291 ? 7.07002   5.10246  -33.01379 1.000 45.37755  ? 291 PHE   A CD1 1 
ATOM   2247 C CD2 . PHE   A 1 291 ? 6.31001   5.16854  -35.27125 1.000 46.53877  ? 291 PHE   A CD2 1 
ATOM   2248 C CE1 . PHE   A 1 291 ? 6.37526   3.92529  -32.81074 1.000 46.35095  ? 291 PHE   A CE1 1 
ATOM   2249 C CE2 . PHE   A 1 291 ? 5.61440   3.99031  -35.07545 1.000 46.81508  ? 291 PHE   A CE2 1 
ATOM   2250 C CZ  . PHE   A 1 291 ? 5.64700   3.36805  -33.84355 1.000 46.13696  ? 291 PHE   A CZ  1 
ATOM   2251 N N   . THR   A 1 292 ? 8.16795   10.04575 -32.63705 1.000 41.37376  ? 292 THR   A N   1 
ATOM   2252 C CA  . THR   A 1 292 ? 9.13394   11.11255 -32.43357 1.000 42.03156  ? 292 THR   A CA  1 
ATOM   2253 C C   . THR   A 1 292 ? 10.54843  10.53881 -32.37233 1.000 43.44932  ? 292 THR   A C   1 
ATOM   2254 O O   . THR   A 1 292 ? 10.73038  9.33296  -32.19007 1.000 42.06252  ? 292 THR   A O   1 
ATOM   2255 C CB  . THR   A 1 292 ? 8.82678   11.88174 -31.14857 1.000 43.29646  ? 292 THR   A CB  1 
ATOM   2256 O OG1 . THR   A 1 292 ? 9.47965   11.25045 -30.03918 1.000 45.79420  ? 292 THR   A OG1 1 
ATOM   2257 C CG2 . THR   A 1 292 ? 7.33036   11.94076 -30.89976 1.000 42.26565  ? 292 THR   A CG2 1 
ATOM   2258 N N   . PRO   A 1 293 ? 11.57145  11.38417 -32.54649 1.000 43.95683  ? 293 PRO   A N   1 
ATOM   2259 C CA  . PRO   A 1 293 ? 12.94886  10.90251 -32.34434 1.000 48.01182  ? 293 PRO   A CA  1 
ATOM   2260 C C   . PRO   A 1 293 ? 13.17014  10.28924 -30.97215 1.000 51.52761  ? 293 PRO   A C   1 
ATOM   2261 O O   . PRO   A 1 293 ? 13.90334  9.30049  -30.84494 1.000 48.08164  ? 293 PRO   A O   1 
ATOM   2262 C CB  . PRO   A 1 293 ? 13.79047  12.17050 -32.54149 1.000 46.09135  ? 293 PRO   A CB  1 
ATOM   2263 C CG  . PRO   A 1 293 ? 12.97494  13.02685 -33.42936 1.000 45.12901  ? 293 PRO   A CG  1 
ATOM   2264 C CD  . PRO   A 1 293 ? 11.54028  12.75977 -33.07591 1.000 39.80158  ? 293 PRO   A CD  1 
ATOM   2265 N N   . PHE   A 1 294 ? 12.54188  10.85155 -29.93735 1.000 54.35467  ? 294 PHE   A N   1 
ATOM   2266 C CA  . PHE   A 1 294 ? 12.70006  10.31669 -28.58933 1.000 54.31596  ? 294 PHE   A CA  1 
ATOM   2267 C C   . PHE   A 1 294 ? 12.04794  8.94393  -28.46292 1.000 49.58204  ? 294 PHE   A C   1 
ATOM   2268 O O   . PHE   A 1 294 ? 12.54875  8.07533  -27.73825 1.000 51.88515  ? 294 PHE   A O   1 
ATOM   2269 C CB  . PHE   A 1 294 ? 12.11297  11.28970 -27.56041 1.000 56.75876  ? 294 PHE   A CB  1 
ATOM   2270 C CG  . PHE   A 1 294 ? 12.75939  12.66124 -27.55535 1.000 70.47523  ? 294 PHE   A CG  1 
ATOM   2271 C CD1 . PHE   A 1 294 ? 13.49779  13.08185 -26.45940 1.000 72.57715  ? 294 PHE   A CD1 1 
ATOM   2272 C CD2 . PHE   A 1 294 ? 12.59261  13.54329 -28.61695 1.000 72.31630  ? 294 PHE   A CD2 1 
ATOM   2273 C CE1 . PHE   A 1 294 ? 14.08439  14.33711 -26.43613 1.000 72.41601  ? 294 PHE   A CE1 1 
ATOM   2274 C CE2 . PHE   A 1 294 ? 13.18083  14.79965 -28.59935 1.000 80.55038  ? 294 PHE   A CE2 1 
ATOM   2275 C CZ  . PHE   A 1 294 ? 13.92418  15.19623 -27.50696 1.000 72.54824  ? 294 PHE   A CZ  1 
ATOM   2276 N N   . ASP   A 1 295 ? 10.92648  8.73374  -29.15766 1.000 50.18883  ? 295 ASP   A N   1 
ATOM   2277 C CA  . ASP   A 1 295 ? 10.27967  7.42554  -29.15040 1.000 48.99749  ? 295 ASP   A CA  1 
ATOM   2278 C C   . ASP   A 1 295 ? 11.18776  6.35998  -29.75090 1.000 50.10691  ? 295 ASP   A C   1 
ATOM   2279 O O   . ASP   A 1 295 ? 11.24302  5.22803  -29.25551 1.000 51.48296  ? 295 ASP   A O   1 
ATOM   2280 C CB  . ASP   A 1 295 ? 8.95902   7.48972  -29.91999 1.000 48.01213  ? 295 ASP   A CB  1 
ATOM   2281 C CG  . ASP   A 1 295 ? 7.87992   8.25105  -29.17286 1.000 45.95527  ? 295 ASP   A CG  1 
ATOM   2282 O OD1 . ASP   A 1 295 ? 7.97805   8.36419  -27.93264 1.000 50.06528  ? 295 ASP   A OD1 1 
ATOM   2283 O OD2 . ASP   A 1 295 ? 6.93480   8.74015  -29.82938 1.000 43.25714  ? 295 ASP   A OD2 1 
ATOM   2284 N N   . VAL   A 1 296 ? 11.90838  6.70582  -30.81993 1.000 48.86793  ? 296 VAL   A N   1 
ATOM   2285 C CA  . VAL   A 1 296 ? 12.75596  5.73115  -31.50118 1.000 49.42184  ? 296 VAL   A CA  1 
ATOM   2286 C C   . VAL   A 1 296 ? 13.93252  5.33435  -30.61694 1.000 53.28944  ? 296 VAL   A C   1 
ATOM   2287 O O   . VAL   A 1 296 ? 14.25562  4.14809  -30.48219 1.000 54.11418  ? 296 VAL   A O   1 
ATOM   2288 C CB  . VAL   A 1 296 ? 13.22889  6.28924  -32.85589 1.000 44.42359  ? 296 VAL   A CB  1 
ATOM   2289 C CG1 . VAL   A 1 296 ? 14.20026  5.32625  -33.51982 1.000 44.78220  ? 296 VAL   A CG1 1 
ATOM   2290 C CG2 . VAL   A 1 296 ? 12.03900  6.56444  -33.76163 1.000 41.70170  ? 296 VAL   A CG2 1 
ATOM   2291 N N   . VAL   A 1 297 ? 14.59139  6.32071  -30.00303 1.000 51.39305  ? 297 VAL   A N   1 
ATOM   2292 C CA  . VAL   A 1 297 ? 15.72219  6.03070  -29.12426 1.000 53.13324  ? 297 VAL   A CA  1 
ATOM   2293 C C   . VAL   A 1 297 ? 15.27389  5.17464  -27.94676 1.000 57.50643  ? 297 VAL   A C   1 
ATOM   2294 O O   . VAL   A 1 297 ? 15.96881  4.23571  -27.53966 1.000 58.06944  ? 297 VAL   A O   1 
ATOM   2295 C CB  . VAL   A 1 297 ? 16.38132  7.34305  -28.65781 1.000 51.03800  ? 297 VAL   A CB  1 
ATOM   2296 C CG1 . VAL   A 1 297 ? 17.04653  7.16568  -27.29783 1.000 48.63236  ? 297 VAL   A CG1 1 
ATOM   2297 C CG2 . VAL   A 1 297 ? 17.38590  7.82757  -29.69303 1.000 47.44807  ? 297 VAL   A CG2 1 
ATOM   2298 N N   . ARG   A 1 298 ? 14.09765  5.47689  -27.39510 1.000 57.64925  ? 298 ARG   A N   1 
ATOM   2299 C CA  . ARG   A 1 298 ? 13.57303  4.71764  -26.26439 1.000 62.73980  ? 298 ARG   A CA  1 
ATOM   2300 C C   . ARG   A 1 298 ? 13.43748  3.23919  -26.60738 1.000 57.71875  ? 298 ARG   A C   1 
ATOM   2301 O O   . ARG   A 1 298 ? 13.84552  2.36809  -25.83090 1.000 57.73130  ? 298 ARG   A O   1 
ATOM   2302 C CB  . ARG   A 1 298 ? 12.22536  5.30371  -25.84278 1.000 58.87276  ? 298 ARG   A CB  1 
ATOM   2303 C CG  . ARG   A 1 298 ? 11.32573  4.36534  -25.06055 1.000 67.62012  ? 298 ARG   A CG  1 
ATOM   2304 C CD  . ARG   A 1 298 ? 10.33702  5.10936  -24.15307 1.000 68.93279  ? 298 ARG   A CD  1 
ATOM   2305 N NE  . ARG   A 1 298 ? 9.79058   6.33476  -24.73307 1.000 70.06625  ? 298 ARG   A NE  1 
ATOM   2306 C CZ  . ARG   A 1 298 ? 10.30440  7.54825  -24.57254 1.000 70.16705  ? 298 ARG   A CZ  1 
ATOM   2307 N NH1 . ARG   A 1 298 ? 11.38072  7.75063  -23.83104 1.000 66.30139  ? 298 ARG   A NH1 1 
ATOM   2308 N NH2 . ARG   A 1 298 ? 9.71790   8.58533  -25.16469 1.000 65.11614  ? 298 ARG   A NH2 1 
ATOM   2309 N N   . GLN   A 1 299 ? 12.87392  2.93755  -27.77716 1.000 59.87683  ? 299 GLN   A N   1 
ATOM   2310 C CA  . GLN   A 1 299 ? 12.65269  1.54912  -28.16265 1.000 60.17941  ? 299 GLN   A CA  1 
ATOM   2311 C C   . GLN   A 1 299 ? 13.93780  0.86184  -28.60687 1.000 60.78487  ? 299 GLN   A C   1 
ATOM   2312 O O   . GLN   A 1 299 ? 14.05450  -0.36208 -28.48157 1.000 61.85301  ? 299 GLN   A O   1 
ATOM   2313 C CB  . GLN   A 1 299 ? 11.59938  1.48024  -29.27009 1.000 52.51016  ? 299 GLN   A CB  1 
ATOM   2314 C CG  . GLN   A 1 299 ? 11.10614  0.07952  -29.57884 1.000 49.21513  ? 299 GLN   A CG  1 
ATOM   2315 C CD  . GLN   A 1 299 ? 9.73796   0.07737  -30.22222 1.000 47.04547  ? 299 GLN   A CD  1 
ATOM   2316 O OE1 . GLN   A 1 299 ? 9.31815   -0.91571 -30.81422 1.000 48.06125  ? 299 GLN   A OE1 1 
ATOM   2317 N NE2 . GLN   A 1 299 ? 9.02740   1.19137  -30.09985 1.000 47.61714  ? 299 GLN   A NE2 1 
ATOM   2318 N N   . CYS   A 1 300 ? 14.90683  1.62081  -29.11419 1.000 61.16422  ? 300 CYS   A N   1 
ATOM   2319 C CA  . CYS   A 1 300 ? 16.15770  1.06780  -29.61509 1.000 61.42531  ? 300 CYS   A CA  1 
ATOM   2320 C C   . CYS   A 1 300 ? 17.30811  1.20071  -28.62111 1.000 64.99257  ? 300 CYS   A C   1 
ATOM   2321 O O   . CYS   A 1 300 ? 18.44310  0.84226  -28.95211 1.000 65.94848  ? 300 CYS   A O   1 
ATOM   2322 C CB  . CYS   A 1 300 ? 16.52571  1.72780  -30.94657 1.000 57.76794  ? 300 CYS   A CB  1 
ATOM   2323 S SG  . CYS   A 1 300 ? 15.20850  1.66610  -32.18844 1.000 56.71183  ? 300 CYS   A SG  1 
ATOM   2324 N N   . SER   A 1 301 ? 17.04290  1.70125  -27.41245 1.000 62.90143  ? 301 SER   A N   1 
ATOM   2325 C CA  . SER   A 1 301 ? 18.06240  1.75683  -26.36915 1.000 62.44255  ? 301 SER   A CA  1 
ATOM   2326 C C   . SER   A 1 301 ? 17.56507  1.34110  -24.99175 1.000 70.60228  ? 301 SER   A C   1 
ATOM   2327 O O   . SER   A 1 301 ? 18.39902  1.09032  -24.11617 1.000 73.63342  ? 301 SER   A O   1 
ATOM   2328 C CB  . SER   A 1 301 ? 18.66370  3.16770  -26.27316 1.000 61.93920  ? 301 SER   A CB  1 
ATOM   2329 O OG  . SER   A 1 301 ? 19.31490  3.52884  -27.47979 1.000 66.69806  ? 301 SER   A OG  1 
ATOM   2330 N N   . GLY   A 1 302 ? 16.25603  1.25455  -24.76275 1.000 64.42481  ? 302 GLY   A N   1 
ATOM   2331 C CA  . GLY   A 1 302 ? 15.73441  0.81852  -23.48167 1.000 66.94096  ? 302 GLY   A CA  1 
ATOM   2332 C C   . GLY   A 1 302 ? 15.95415  1.82197  -22.36939 1.000 73.56687  ? 302 GLY   A C   1 
ATOM   2333 O O   . GLY   A 1 302 ? 16.85155  1.65147  -21.53846 1.000 75.70416  ? 302 GLY   A O   1 
ATOM   2334 N N   . VAL   A 1 303 ? 15.13585  2.87548  -22.34134 1.000 72.25697  ? 303 VAL   A N   1 
ATOM   2335 C CA  . VAL   A 1 303 ? 15.30112  3.91067  -21.32632 1.000 77.57762  ? 303 VAL   A CA  1 
ATOM   2336 C C   . VAL   A 1 303 ? 14.86265  3.39534  -19.96047 1.000 76.80555  ? 303 VAL   A C   1 
ATOM   2337 O O   . VAL   A 1 303 ? 15.54166  3.62500  -18.95106 1.000 79.83552  ? 303 VAL   A O   1 
ATOM   2338 C CB  . VAL   A 1 303 ? 14.53750  5.18418  -21.73688 1.000 71.44183  ? 303 VAL   A CB  1 
ATOM   2339 C CG1 . VAL   A 1 303 ? 14.09186  5.97254  -20.51257 1.000 65.51016  ? 303 VAL   A CG1 1 
ATOM   2340 C CG2 . VAL   A 1 303 ? 15.40356  6.04747  -22.64271 1.000 65.68709  ? 303 VAL   A CG2 1 
ATOM   2341 N N   . THR   A 1 304 ? 13.73544  2.68558  -19.90859 1.000 71.62760  ? 304 THR   A N   1 
ATOM   2342 C CA  . THR   A 1 304 ? 13.22371  2.09912  -18.66900 1.000 64.52618  ? 304 THR   A CA  1 
ATOM   2343 C C   . THR   A 1 304 ? 12.96961  3.15733  -17.59723 1.000 63.23806  ? 304 THR   A C   1 
ATOM   2344 O O   . THR   A 1 304 ? 11.87133  3.24899  -17.04556 1.000 62.25950  ? 304 THR   A O   1 
ATOM   2345 C CB  . THR   A 1 304 ? 14.19115  1.02794  -18.11213 1.000 61.40469  ? 304 THR   A CB  1 
ATOM   2346 O OG1 . THR   A 1 304 ? 13.94640  -0.22712 -18.76054 1.000 52.09070  ? 304 THR   A OG1 1 
ATOM   2347 C CG2 . THR   A 1 304 ? 14.02925  0.87558  -16.60888 1.000 52.02076  ? 304 THR   A CG2 1 
HETATM 2348 C C13 . A1ALD B 2 .   ? -16.75749 11.63742 -26.96548 1.000 43.17367  ? 401 A1ALD A C13 1 
HETATM 2349 C C17 . A1ALD B 2 .   ? -18.21383 11.25514 -27.14133 1.000 44.33874  ? 401 A1ALD A C17 1 
HETATM 2350 C C22 . A1ALD B 2 .   ? -19.38633 15.58646 -29.79253 1.000 48.08288  ? 401 A1ALD A C22 1 
HETATM 2351 C C24 . A1ALD B 2 .   ? -20.62378 14.90485 -31.80518 1.000 45.96312  ? 401 A1ALD A C24 1 
HETATM 2352 C C26 . A1ALD B 2 .   ? -21.16631 16.49364 -33.78912 1.000 45.45514  ? 401 A1ALD A C26 1 
HETATM 2353 C C28 . A1ALD B 2 .   ? -22.42606 17.93426 -35.39123 1.000 44.91078  ? 401 A1ALD A C28 1 
HETATM 2354 C C02 . A1ALD B 2 .   ? -18.75095 15.33059 -28.43992 1.000 47.18681  ? 401 A1ALD A C02 1 
HETATM 2355 C C04 . A1ALD B 2 .   ? -18.72525 15.68904 -25.92770 1.000 47.11478  ? 401 A1ALD A C04 1 
HETATM 2356 C C05 . A1ALD B 2 .   ? -19.46172 16.52723 -24.85405 1.000 48.19528  ? 401 A1ALD A C05 1 
HETATM 2357 C C06 . A1ALD B 2 .   ? -19.34072 18.04531 -25.13905 1.000 51.00159  ? 401 A1ALD A C06 1 
HETATM 2358 C C07 . A1ALD B 2 .   ? -17.88119 18.49886 -25.00316 1.000 49.30040  ? 401 A1ALD A C07 1 
HETATM 2359 C C08 . A1ALD B 2 .   ? -20.23703 18.84490 -24.18154 1.000 52.34453  ? 401 A1ALD A C08 1 
HETATM 2360 C C09 . A1ALD B 2 .   ? -18.73068 14.22324 -25.45229 1.000 44.59610  ? 401 A1ALD A C09 1 
HETATM 2361 C C11 . A1ALD B 2 .   ? -17.47454 12.26755 -24.63560 1.000 44.10110  ? 401 A1ALD A C11 1 
HETATM 2362 C C12 . A1ALD B 2 .   ? -16.53553 11.39695 -25.49652 1.000 43.22585  ? 401 A1ALD A C12 1 
HETATM 2363 C C14 . A1ALD B 2 .   ? -15.96427 10.75074 -27.90525 1.000 48.85167  ? 401 A1ALD A C14 1 
HETATM 2364 C C16 . A1ALD B 2 .   ? -18.08184 9.73153  -27.57258 1.000 44.98127  ? 401 A1ALD A C16 1 
HETATM 2365 C C19 . A1ALD B 2 .   ? -17.04149 12.27473 -23.16127 1.000 44.11078  ? 401 A1ALD A C19 1 
HETATM 2366 C C23 . A1ALD B 2 .   ? -20.06098 14.61427 -30.54652 1.000 44.89674  ? 401 A1ALD A C23 1 
HETATM 2367 C C25 . A1ALD B 2 .   ? -20.56926 16.17815 -32.42254 1.000 46.66440  ? 401 A1ALD A C25 1 
HETATM 2368 C C27 . A1ALD B 2 .   ? -21.87168 17.64554 -34.08269 1.000 43.22834  ? 401 A1ALD A C27 1 
HETATM 2369 C C29 . A1ALD B 2 .   ? -22.27153 17.06398 -36.44207 1.000 43.17886  ? 401 A1ALD A C29 1 
HETATM 2370 C C30 . A1ALD B 2 .   ? -21.54187 15.84586 -36.21956 1.000 41.26913  ? 401 A1ALD A C30 1 
HETATM 2371 C C33 . A1ALD B 2 .   ? -19.96838 12.58590 -36.86887 1.000 46.27901  ? 401 A1ALD A C33 1 
HETATM 2372 C C34 . A1ALD B 2 .   ? -20.35815 14.32167 -35.04514 1.000 44.53957  ? 401 A1ALD A C34 1 
HETATM 2373 C C35 . A1ALD B 2 .   ? -20.99455 15.57750 -34.89970 1.000 44.31475  ? 401 A1ALD A C35 1 
HETATM 2374 C C36 . A1ALD B 2 .   ? -19.88110 17.13029 -31.64925 1.000 47.61808  ? 401 A1ALD A C36 1 
HETATM 2375 C C37 . A1ALD B 2 .   ? -19.31696 16.85476 -30.39728 1.000 49.01769  ? 401 A1ALD A C37 1 
HETATM 2376 N N03 . A1ALD B 2 .   ? -19.31189 15.87290 -27.26957 1.000 47.45638  ? 401 A1ALD A N03 1 
HETATM 2377 N N10 . A1ALD B 2 .   ? -17.50917 13.65432 -25.10216 1.000 42.46619  ? 401 A1ALD A N10 1 
HETATM 2378 N N15 . A1ALD B 2 .   ? -16.79964 9.62447  -28.24321 1.000 50.77119  ? 401 A1ALD A N15 1 
HETATM 2379 N N20 . A1ALD B 2 .   ? -17.59270 11.62615 -22.22589 1.000 43.60775  ? 401 A1ALD A N20 1 
HETATM 2380 N N31 . A1ALD B 2 .   ? -21.23906 14.80198 -37.09152 1.000 43.89042  ? 401 A1ALD A N31 1 
HETATM 2381 N N32 . A1ALD B 2 .   ? -20.51932 13.89009 -36.35062 1.000 44.20345  ? 401 A1ALD A N32 1 
HETATM 2382 O O01 . A1ALD B 2 .   ? -17.71696 14.66984 -28.31037 1.000 45.33292  ? 401 A1ALD A O01 1 
HETATM 2383 O O18 . A1ALD B 2 .   ? -14.83264 10.90237 -28.33081 1.000 45.52593  ? 401 A1ALD A O18 1 
HETATM 2384 O O21 . A1ALD B 2 .   ? -19.77541 13.58750 -25.38267 1.000 44.64377  ? 401 A1ALD A O21 1 
HETATM 2385 O O   . HOH   C 3 .   ? -16.42480 30.66092 -19.72399 1.000 58.39347  ? 501 HOH   A O   1 
HETATM 2386 O O   . HOH   C 3 .   ? 21.05889  8.50197  -49.04482 1.000 51.42607  ? 502 HOH   A O   1 
HETATM 2387 O O   . HOH   C 3 .   ? -3.66599  0.76558  -8.19204  1.000 56.84057  ? 503 HOH   A O   1 
HETATM 2388 O O   . HOH   C 3 .   ? 22.72700  0.00000  -40.84219 0.50  69.46810  ? 504 HOH   A O   1 
HETATM 2389 O O   . HOH   C 3 .   ? -6.84517  7.85347  -18.26000 1.000 44.37676  ? 505 HOH   A O   1 
HETATM 2390 O O   . HOH   C 3 .   ? -2.31949  22.13219 -40.13749 1.000 50.56274  ? 506 HOH   A O   1 
HETATM 2391 O O   . HOH   C 3 .   ? -20.37240 5.94533  -28.07061 1.000 42.42630  ? 507 HOH   A O   1 
HETATM 2392 O O   . HOH   C 3 .   ? 7.08269   8.32484  -37.38484 1.000 35.62968  ? 508 HOH   A O   1 
HETATM 2393 O O   . HOH   C 3 .   ? -18.94397 12.15558 -39.89440 1.000 45.82793  ? 509 HOH   A O   1 
HETATM 2394 O O   . HOH   C 3 .   ? 0.69287   23.24768 -36.12785 1.000 41.32105  ? 510 HOH   A O   1 
HETATM 2395 O O   . HOH   C 3 .   ? 22.99459  -3.87375 -44.37857 1.000 74.93055  ? 511 HOH   A O   1 
HETATM 2396 O O   . HOH   C 3 .   ? 21.84988  4.65667  -55.02120 1.000 62.29688  ? 512 HOH   A O   1 
HETATM 2397 O O   . HOH   C 3 .   ? -5.78849  1.69270  -8.14184  1.000 50.92840  ? 513 HOH   A O   1 
HETATM 2398 O O   . HOH   C 3 .   ? 5.73571   9.79558  -26.24812 1.000 42.88307  ? 514 HOH   A O   1 
HETATM 2399 O O   . HOH   C 3 .   ? -7.00938  22.97596 -36.41741 1.000 44.40665  ? 515 HOH   A O   1 
HETATM 2400 O O   . HOH   C 3 .   ? -16.96972 17.60062 5.19233   1.000 51.57897  ? 516 HOH   A O   1 
HETATM 2401 O O   . HOH   C 3 .   ? 6.23590   4.54046  -28.87681 1.000 47.53701  ? 517 HOH   A O   1 
HETATM 2402 O O   . HOH   C 3 .   ? 19.73613  18.37517 -53.59723 1.000 57.54197  ? 518 HOH   A O   1 
HETATM 2403 O O   . HOH   C 3 .   ? -1.42608  20.12070 -18.73220 1.000 47.22393  ? 519 HOH   A O   1 
HETATM 2404 O O   . HOH   C 3 .   ? -25.82802 17.04457 -15.00778 1.000 54.82009  ? 520 HOH   A O   1 
HETATM 2405 O O   . HOH   C 3 .   ? 9.58278   1.68212  -61.44233 1.000 48.00823  ? 521 HOH   A O   1 
HETATM 2406 O O   . HOH   C 3 .   ? -24.78200 26.47125 -33.93107 1.000 53.56086  ? 522 HOH   A O   1 
HETATM 2407 O O   . HOH   C 3 .   ? 8.32669   15.89138 -33.10713 1.000 39.80851  ? 523 HOH   A O   1 
HETATM 2408 O O   . HOH   C 3 .   ? 4.70445   27.06534 -27.57227 1.000 48.86486  ? 524 HOH   A O   1 
HETATM 2409 O O   . HOH   C 3 .   ? 20.74829  5.50612  -24.87405 1.000 50.93874  ? 525 HOH   A O   1 
HETATM 2410 O O   . HOH   C 3 .   ? 21.76295  -5.98690 -46.77024 1.000 57.24127  ? 526 HOH   A O   1 
HETATM 2411 O O   . HOH   C 3 .   ? 21.71259  -3.82384 -50.37778 1.000 64.29653  ? 527 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   ? 0.67832 0.62421 0.67102 0.14359  0.03535  0.06998  1   SER   A N   
2    C CA  . SER   A 1   ? 0.68357 0.62135 0.67211 0.13563  0.03553  0.06093  1   SER   A CA  
3    C C   . SER   A 1   ? 0.70336 0.62497 0.68023 0.12754  0.03416  0.05532  1   SER   A C   
4    O O   . SER   A 1   ? 0.68980 0.60832 0.66247 0.12740  0.03247  0.05793  1   SER   A O   
5    C CB  . SER   A 1   ? 0.71431 0.64090 0.70388 0.13938  0.04431  0.06020  1   SER   A CB  
6    O OG  . SER   A 1   ? 0.79169 0.73369 0.79308 0.14778  0.04620  0.06612  1   SER   A OG  
7    N N   . GLY   A 2   ? 0.73300 0.64520 0.70481 0.12083  0.03496  0.04801  2   GLY   A N   
8    C CA  . GLY   A 2   ? 0.69649 0.59719 0.65859 0.11253  0.03248  0.04234  2   GLY   A CA  
9    C C   . GLY   A 2   ? 0.69620 0.60992 0.66019 0.10609  0.02398  0.03834  2   GLY   A C   
10   O O   . GLY   A 2   ? 0.75691 0.68867 0.72876 0.10773  0.01931  0.04030  2   GLY   A O   
11   N N   . PHE   A 3   ? 0.69994 0.60440 0.65671 0.09854  0.02215  0.03249  3   PHE   A N   
12   C CA  . PHE   A 3   ? 0.63848 0.55254 0.59684 0.09250  0.01497  0.02841  3   PHE   A CA  
13   C C   . PHE   A 3   ? 0.62901 0.53394 0.57948 0.08675  0.01256  0.02525  3   PHE   A C   
14   O O   . PHE   A 3   ? 0.62725 0.51748 0.57008 0.08370  0.01586  0.02274  3   PHE   A O   
15   C CB  . PHE   A 3   ? 0.62690 0.54253 0.58722 0.08916  0.01491  0.02452  3   PHE   A CB  
16   C CG  . PHE   A 3   ? 0.63081 0.55907 0.59618 0.08483  0.00829  0.02164  3   PHE   A CG  
17   C CD1 . PHE   A 3   ? 0.63216 0.57763 0.60693 0.08724  0.00549  0.02341  3   PHE   A CD1 
18   C CD2 . PHE   A 3   ? 0.59775 0.52089 0.55878 0.07830  0.00505  0.01715  3   PHE   A CD2 
19   C CE1 . PHE   A 3   ? 0.61372 0.56959 0.59302 0.08267  0.00007  0.01995  3   PHE   A CE1 
20   C CE2 . PHE   A 3   ? 0.57749 0.51063 0.54360 0.07468  -0.00020 0.01446  3   PHE   A CE2 
21   C CZ  . PHE   A 3   ? 0.60635 0.55512 0.58139 0.07658  -0.00244 0.01546  3   PHE   A CZ  
22   N N   . ARG   A 4   ? 0.64895 0.56353 0.60141 0.08501  0.00694  0.02509  4   ARG   A N   
23   C CA  . ARG   A 4   ? 0.64274 0.55131 0.58924 0.08014  0.00456  0.02264  4   ARG   A CA  
24   C C   . ARG   A 4   ? 0.62767 0.54788 0.57800 0.07620  -0.00204 0.01923  4   ARG   A C   
25   O O   . ARG   A 4   ? 0.61646 0.55044 0.57376 0.07779  -0.00483 0.01965  4   ARG   A O   
26   C CB  . ARG   A 4   ? 0.60311 0.50887 0.54685 0.08312  0.00632  0.02707  4   ARG   A CB  
27   C CG  . ARG   A 4   ? 0.63613 0.52880 0.57646 0.08751  0.01365  0.03080  4   ARG   A CG  
28   C CD  . ARG   A 4   ? 0.66489 0.54022 0.59694 0.08243  0.01718  0.02653  4   ARG   A CD  
29   N NE  . ARG   A 4   ? 0.66888 0.54130 0.59617 0.07652  0.01414  0.02391  4   ARG   A NE  
30   C CZ  . ARG   A 4   ? 0.70051 0.56684 0.62415 0.07653  0.01615  0.02644  4   ARG   A CZ  
31   N NH1 . ARG   A 4   ? 0.70865 0.56989 0.63244 0.08242  0.02132  0.03210  4   ARG   A NH1 
32   N NH2 . ARG   A 4   ? 0.73129 0.59681 0.65152 0.07066  0.01317  0.02362  4   ARG   A NH2 
33   N N   . LYS   A 5   ? 0.63961 0.55444 0.58569 0.07091  -0.00427 0.01564  5   LYS   A N   
34   C CA  . LYS   A 5   ? 0.65134 0.57583 0.60081 0.06780  -0.00973 0.01267  5   LYS   A CA  
35   C C   . LYS   A 5   ? 0.63261 0.56602 0.58339 0.07026  -0.01114 0.01534  5   LYS   A C   
36   O O   . LYS   A 5   ? 0.66302 0.59052 0.60895 0.07084  -0.00918 0.01779  5   LYS   A O   
37   C CB  . LYS   A 5   ? 0.66578 0.58294 0.61089 0.06246  -0.01135 0.00911  5   LYS   A CB  
38   C CG  . LYS   A 5   ? 0.65017 0.57524 0.60002 0.05936  -0.01617 0.00529  5   LYS   A CG  
39   C CD  . LYS   A 5   ? 0.68688 0.60626 0.63608 0.05609  -0.01681 0.00285  5   LYS   A CD  
40   C CE  . LYS   A 5   ? 0.74681 0.65961 0.69113 0.05229  -0.01785 0.00137  5   LYS   A CE  
41   N NZ  . LYS   A 5   ? 0.85041 0.75854 0.79341 0.04942  -0.01869 0.00001  5   LYS   A NZ  
42   N N   . MET   A 6   ? 0.60888 0.55672 0.56588 0.07132  -0.01434 0.01487  6   MET   A N   
43   C CA  . MET   A 6   ? 0.60406 0.56293 0.56217 0.07407  -0.01573 0.01795  6   MET   A CA  
44   C C   . MET   A 6   ? 0.56050 0.53032 0.52138 0.07043  -0.02041 0.01330  6   MET   A C   
45   O O   . MET   A 6   ? 0.59025 0.56512 0.55604 0.06790  -0.02268 0.00890  6   MET   A O   
46   C CB  . MET   A 6   ? 0.59096 0.55954 0.55395 0.07939  -0.01482 0.02235  6   MET   A CB  
47   C CG  . MET   A 6   ? 0.59632 0.57122 0.55801 0.08419  -0.01415 0.02874  6   MET   A CG  
48   S SD  . MET   A 6   ? 0.67533 0.66468 0.64427 0.09092  -0.01373 0.03448  6   MET   A SD  
49   C CE  . MET   A 6   ? 0.59443 0.56662 0.56208 0.09489  -0.00680 0.03754  6   MET   A CE  
50   N N   . ALA   A 7   ? 0.49506 0.46794 0.45275 0.07006  -0.02128 0.01418  7   ALA   A N   
51   C CA  . ALA   A 7   ? 0.53208 0.51562 0.49169 0.06696  -0.02494 0.00969  7   ALA   A CA  
52   C C   . ALA   A 7   ? 0.51872 0.51793 0.47950 0.06963  -0.02657 0.01250  7   ALA   A C   
53   O O   . ALA   A 7   ? 0.55015 0.55058 0.50907 0.07426  -0.02473 0.01926  7   ALA   A O   
54   C CB  . ALA   A 7   ? 0.51202 0.48936 0.46718 0.06402  -0.02472 0.00807  7   ALA   A CB  
55   N N   . PHE   A 8   ? 0.52537 0.53679 0.48926 0.06667  -0.02991 0.00727  8   PHE   A N   
56   C CA  . PHE   A 8   ? 0.51914 0.54770 0.48361 0.06814  -0.03211 0.00897  8   PHE   A CA  
57   C C   . PHE   A 8   ? 0.52177 0.55150 0.47970 0.06969  -0.03123 0.01351  8   PHE   A C   
58   O O   . PHE   A 8   ? 0.52081 0.54058 0.47491 0.06768  -0.02970 0.01240  8   PHE   A O   
59   C CB  . PHE   A 8   ? 0.53866 0.57880 0.50718 0.06347  -0.03538 0.00085  8   PHE   A CB  
60   C CG  . PHE   A 8   ? 0.55953 0.60391 0.53508 0.06220  -0.03647 -0.00235 8   PHE   A CG  
61   C CD1 . PHE   A 8   ? 0.59322 0.65288 0.57226 0.06399  -0.03817 -0.00002 8   PHE   A CD1 
62   C CD2 . PHE   A 8   ? 0.55110 0.58492 0.53002 0.05915  -0.03576 -0.00723 8   PHE   A CD2 
63   C CE1 . PHE   A 8   ? 0.62143 0.68565 0.60749 0.06222  -0.03891 -0.00310 8   PHE   A CE1 
64   C CE2 . PHE   A 8   ? 0.60068 0.63791 0.58604 0.05759  -0.03627 -0.00986 8   PHE   A CE2 
65   C CZ  . PHE   A 8   ? 0.60879 0.66117 0.59787 0.05885  -0.03772 -0.00809 8   PHE   A CZ  
66   N N   . PRO   A 9   ? 0.51539 0.55783 0.47209 0.07321  -0.03210 0.01914  9   PRO   A N   
67   C CA  . PRO   A 9   ? 0.54445 0.58993 0.49467 0.07421  -0.03142 0.02353  9   PRO   A CA  
68   C C   . PRO   A 9   ? 0.57355 0.62532 0.52213 0.06881  -0.03334 0.01606  9   PRO   A C   
69   O O   . PRO   A 9   ? 0.57213 0.63656 0.52389 0.06588  -0.03640 0.00984  9   PRO   A O   
70   C CB  . PRO   A 9   ? 0.52614 0.58765 0.47668 0.07897  -0.03295 0.03061  9   PRO   A CB  
71   C CG  . PRO   A 9   ? 0.54123 0.60273 0.49834 0.08190  -0.03286 0.03197  9   PRO   A CG  
72   C CD  . PRO   A 9   ? 0.52730 0.58244 0.48868 0.07671  -0.03362 0.02262  9   PRO   A CD  
73   N N   . SER   A 10  ? 0.51868 0.56147 0.46255 0.06727  -0.03112 0.01635  10  SER   A N   
74   C CA  . SER   A 10  ? 0.54256 0.58824 0.48576 0.06235  -0.03191 0.00885  10  SER   A CA  
75   C C   . SER   A 10  ? 0.55119 0.61079 0.48915 0.06185  -0.03256 0.01021  10  SER   A C   
76   O O   . SER   A 10  ? 0.58067 0.64196 0.51712 0.05821  -0.03216 0.00489  10  SER   A O   
77   C CB  . SER   A 10  ? 0.57060 0.60023 0.51261 0.06040  -0.02921 0.00778  10  SER   A CB  
78   O OG  . SER   A 10  ? 0.58326 0.60625 0.51951 0.06240  -0.02616 0.01537  10  SER   A OG  
79   N N   . GLY   A 11  ? 0.58583 0.65622 0.52110 0.06559  -0.03348 0.01737  11  GLY   A N   
80   C CA  . GLY   A 11  ? 0.57017 0.65361 0.49906 0.06538  -0.03386 0.02019  11  GLY   A CA  
81   C C   . GLY   A 11  ? 0.59027 0.68802 0.51936 0.06034  -0.03641 0.01047  11  GLY   A C   
82   O O   . GLY   A 11  ? 0.57098 0.67197 0.49549 0.05761  -0.03520 0.00799  11  GLY   A O   
83   N N   . LYS   A 12  ? 0.58344 0.68975 0.51792 0.05874  -0.03949 0.00448  12  LYS   A N   
84   C CA  . LYS   A 12  ? 0.56335 0.68311 0.49802 0.05352  -0.04152 -0.00556 12  LYS   A CA  
85   C C   . LYS   A 12  ? 0.57416 0.68380 0.51044 0.04946  -0.03922 -0.01432 12  LYS   A C   
86   O O   . LYS   A 12  ? 0.57420 0.69200 0.50726 0.04606  -0.03874 -0.02015 12  LYS   A O   
87   C CB  . LYS   A 12  ? 0.60995 0.73848 0.55104 0.05195  -0.04470 -0.01059 12  LYS   A CB  
88   C CG  . LYS   A 12  ? 0.61445 0.75777 0.55502 0.05568  -0.04754 -0.00269 12  LYS   A CG  
89   C CD  . LYS   A 12  ? 0.62168 0.76545 0.57076 0.05582  -0.04925 -0.00461 12  LYS   A CD  
90   C CE  . LYS   A 12  ? 0.75365 0.92074 0.70374 0.05574  -0.05341 -0.00322 12  LYS   A CE  
91   N NZ  . LYS   A 12  ? 0.83775 1.00605 0.79232 0.06188  -0.05395 0.00635  12  LYS   A NZ  
92   N N   . VAL   A 13  ? 0.55987 0.65243 0.50118 0.04994  -0.03766 -0.01523 13  VAL   A N   
93   C CA  . VAL   A 13  ? 0.52957 0.61308 0.47359 0.04686  -0.03568 -0.02254 13  VAL   A CA  
94   C C   . VAL   A 13  ? 0.54982 0.63023 0.48835 0.04699  -0.03292 -0.01916 13  VAL   A C   
95   O O   . VAL   A 13  ? 0.52588 0.60655 0.46515 0.04416  -0.03134 -0.02553 13  VAL   A O   
96   C CB  . VAL   A 13  ? 0.52372 0.59135 0.47423 0.04747  -0.03521 -0.02338 13  VAL   A CB  
97   C CG1 . VAL   A 13  ? 0.56239 0.62271 0.51702 0.04472  -0.03368 -0.03083 13  VAL   A CG1 
98   C CG2 . VAL   A 13  ? 0.54641 0.61734 0.50204 0.04743  -0.03750 -0.02535 13  VAL   A CG2 
99   N N   . GLU   A 14  ? 0.56651 0.64385 0.49992 0.05023  -0.03185 -0.00914 14  GLU   A N   
100  C CA  . GLU   A 14  ? 0.56391 0.63763 0.49217 0.04982  -0.02878 -0.00540 14  GLU   A CA  
101  C C   . GLU   A 14  ? 0.59449 0.68312 0.51788 0.04730  -0.02844 -0.00883 14  GLU   A C   
102  O O   . GLU   A 14  ? 0.60100 0.68813 0.52340 0.04492  -0.02585 -0.01175 14  GLU   A O   
103  C CB  . GLU   A 14  ? 0.57830 0.64593 0.50181 0.05375  -0.02725 0.00624  14  GLU   A CB  
104  C CG  . GLU   A 14  ? 0.60228 0.65185 0.52892 0.05520  -0.02575 0.00915  14  GLU   A CG  
105  C CD  . GLU   A 14  ? 0.61077 0.65406 0.53337 0.05954  -0.02382 0.02002  14  GLU   A CD  
106  O OE1 . GLU   A 14  ? 0.58739 0.63056 0.50411 0.05996  -0.02122 0.02606  14  GLU   A OE1 
107  O OE2 . GLU   A 14  ? 0.58693 0.62509 0.51243 0.06264  -0.02444 0.02263  14  GLU   A OE2 
108  N N   . GLY   A 15  ? 0.54208 0.64625 0.46239 0.04758  -0.03097 -0.00868 15  GLY   A N   
109  C CA  . GLY   A 15  ? 0.55607 0.67586 0.47058 0.04480  -0.03076 -0.01232 15  GLY   A CA  
110  C C   . GLY   A 15  ? 0.55809 0.68111 0.47641 0.04024  -0.03014 -0.02535 15  GLY   A C   
111  O O   . GLY   A 15  ? 0.57017 0.70572 0.48349 0.03745  -0.02927 -0.02976 15  GLY   A O   
112  N N   . CYS   A 16  ? 0.53531 0.64718 0.46218 0.03954  -0.03018 -0.03147 16  CYS   A N   
113  C CA  . CYS   A 16  ? 0.53736 0.65006 0.46919 0.03593  -0.02902 -0.04352 16  CYS   A CA  
114  C C   . CYS   A 16  ? 0.53918 0.63967 0.47562 0.03580  -0.02578 -0.04570 16  CYS   A C   
115  O O   . CYS   A 16  ? 0.54673 0.64783 0.48753 0.03353  -0.02395 -0.05504 16  CYS   A O   
116  C CB  . CYS   A 16  ? 0.53175 0.64235 0.47072 0.03500  -0.03139 -0.04945 16  CYS   A CB  
117  S SG  . CYS   A 16  ? 0.57571 0.70147 0.51151 0.03507  -0.03572 -0.04667 16  CYS   A SG  
118  N N   . MET   A 17  ? 0.52173 0.61157 0.45770 0.03807  -0.02486 -0.03755 17  MET   A N   
119  C CA  . MET   A 17  ? 0.52574 0.60531 0.46672 0.03768  -0.02240 -0.03915 17  MET   A CA  
120  C C   . MET   A 17  ? 0.53879 0.62537 0.47605 0.03586  -0.01900 -0.04040 17  MET   A C   
121  O O   . MET   A 17  ? 0.54352 0.63553 0.47287 0.03596  -0.01805 -0.03391 17  MET   A O   
122  C CB  . MET   A 17  ? 0.51956 0.58574 0.46099 0.03979  -0.02263 -0.03076 17  MET   A CB  
123  C CG  . MET   A 17  ? 0.52416 0.58251 0.46959 0.04160  -0.02534 -0.02967 17  MET   A CG  
124  S SD  . MET   A 17  ? 0.60300 0.65947 0.55792 0.04030  -0.02641 -0.04007 17  MET   A SD  
125  C CE  . MET   A 17  ? 0.53452 0.58299 0.49518 0.03968  -0.02402 -0.04249 17  MET   A CE  
126  N N   . VAL   A 18  ? 0.50276 0.58927 0.44608 0.03441  -0.01681 -0.04843 18  VAL   A N   
127  C CA  . VAL   A 18  ? 0.49835 0.59134 0.43993 0.03270  -0.01297 -0.05056 18  VAL   A CA  
128  C C   . VAL   A 18  ? 0.51377 0.59824 0.46424 0.03303  -0.01118 -0.05232 18  VAL   A C   
129  O O   . VAL   A 18  ? 0.52187 0.59729 0.47993 0.03439  -0.01286 -0.05410 18  VAL   A O   
130  C CB  . VAL   A 18  ? 0.50747 0.61326 0.44734 0.03049  -0.01127 -0.06014 18  VAL   A CB  
131  C CG1 . VAL   A 18  ? 0.51367 0.63092 0.44379 0.02967  -0.01336 -0.05776 18  VAL   A CG1 
132  C CG2 . VAL   A 18  ? 0.48362 0.58526 0.43266 0.03043  -0.01150 -0.06989 18  VAL   A CG2 
133  N N   . GLN   A 19  ? 0.54521 0.63370 0.49474 0.03171  -0.00772 -0.05140 19  GLN   A N   
134  C CA  . GLN   A 19  ? 0.52290 0.60676 0.48122 0.03180  -0.00588 -0.05295 19  GLN   A CA  
135  C C   . GLN   A 19  ? 0.52632 0.61709 0.49104 0.03168  -0.00280 -0.06301 19  GLN   A C   
136  O O   . GLN   A 19  ? 0.54876 0.65024 0.50847 0.03008  -0.00002 -0.06712 19  GLN   A O   
137  C CB  . GLN   A 19  ? 0.55279 0.63730 0.50763 0.03001  -0.00350 -0.04622 19  GLN   A CB  
138  C CG  . GLN   A 19  ? 0.58016 0.66315 0.54443 0.02954  -0.00163 -0.04789 19  GLN   A CG  
139  C CD  . GLN   A 19  ? 0.60235 0.68537 0.56345 0.02680  0.00061  -0.04118 19  GLN   A CD  
140  O OE1 . GLN   A 19  ? 0.62451 0.69976 0.58907 0.02606  -0.00061 -0.03718 19  GLN   A OE1 
141  N NE2 . GLN   A 19  ? 0.62160 0.71358 0.57574 0.02481  0.00410  -0.04004 19  GLN   A NE2 
142  N N   . VAL   A 20  ? 0.53051 0.61513 0.50613 0.03353  -0.00301 -0.06682 20  VAL   A N   
143  C CA  . VAL   A 20  ? 0.56595 0.65493 0.54968 0.03436  0.00055  -0.07602 20  VAL   A CA  
144  C C   . VAL   A 20  ? 0.59827 0.68687 0.59093 0.03539  0.00245  -0.07436 20  VAL   A C   
145  O O   . VAL   A 20  ? 0.63091 0.71159 0.62837 0.03657  -0.00039 -0.06925 20  VAL   A O   
146  C CB  . VAL   A 20  ? 0.56147 0.64388 0.55165 0.03620  -0.00084 -0.08214 20  VAL   A CB  
147  C CG1 . VAL   A 20  ? 0.49989 0.58556 0.49871 0.03738  0.00382  -0.09181 20  VAL   A CG1 
148  C CG2 . VAL   A 20  ? 0.53308 0.61725 0.51497 0.03453  -0.00316 -0.08360 20  VAL   A CG2 
149  N N   . THR   A 21  ? 0.57615 0.67436 0.57100 0.03476  0.00729  -0.07875 21  THR   A N   
150  C CA  . THR   A 21  ? 0.55915 0.66005 0.56362 0.03569  0.00957  -0.07778 21  THR   A CA  
151  C C   . THR   A 21  ? 0.59298 0.69966 0.60646 0.03792  0.01449  -0.08721 21  THR   A C   
152  O O   . THR   A 21  ? 0.62059 0.73598 0.62924 0.03634  0.01874  -0.09293 21  THR   A O   
153  C CB  . THR   A 21  ? 0.58691 0.69469 0.58536 0.03228  0.01150  -0.07211 21  THR   A CB  
154  O OG1 . THR   A 21  ? 0.59258 0.69277 0.58418 0.03060  0.00751  -0.06326 21  THR   A OG1 
155  C CG2 . THR   A 21  ? 0.59562 0.70900 0.60507 0.03275  0.01431  -0.07225 21  THR   A CG2 
156  N N   . CYS   A 22  ? 0.56747 0.66933 0.59385 0.04175  0.01420  -0.08870 22  CYS   A N   
157  C CA  . CYS   A 22  ? 0.60035 0.70636 0.63774 0.04497  0.01941  -0.09677 22  CYS   A CA  
158  C C   . CYS   A 22  ? 0.59509 0.70650 0.64360 0.04686  0.02054  -0.09292 22  CYS   A C   
159  O O   . CYS   A 22  ? 0.59062 0.69650 0.64656 0.04915  0.01669  -0.08765 22  CYS   A O   
160  C CB  . CYS   A 22  ? 0.61226 0.70815 0.65661 0.04854  0.01868  -0.10158 22  CYS   A CB  
161  S SG  . CYS   A 22  ? 0.68910 0.78736 0.74796 0.05334  0.02598  -0.11159 22  CYS   A SG  
162  N N   . GLY   A 23  ? 0.56041 0.68370 0.60990 0.04562  0.02576  -0.09545 23  GLY   A N   
163  C CA  . GLY   A 23  ? 0.57782 0.70892 0.63791 0.04666  0.02710  -0.09187 23  GLY   A CA  
164  C C   . GLY   A 23  ? 0.59842 0.72858 0.65397 0.04289  0.02231  -0.08208 23  GLY   A C   
165  O O   . GLY   A 23  ? 0.62538 0.76092 0.67195 0.03813  0.02362  -0.07915 23  GLY   A O   
166  N N   . THR   A 24  ? 0.59952 0.72244 0.66083 0.04474  0.01705  -0.07698 24  THR   A N   
167  C CA  . THR   A 24  ? 0.59958 0.72012 0.65652 0.04085  0.01250  -0.06854 24  THR   A CA  
168  C C   . THR   A 24  ? 0.64246 0.74926 0.69275 0.04077  0.00661  -0.06458 24  THR   A C   
169  O O   . THR   A 24  ? 0.65466 0.75745 0.69690 0.03673  0.00370  -0.05857 24  THR   A O   
170  C CB  . THR   A 24  ? 0.67955 0.80752 0.74981 0.04188  0.01158  -0.06522 24  THR   A CB  
171  O OG1 . THR   A 24  ? 0.68600 0.81273 0.76923 0.04844  0.01125  -0.06785 24  THR   A OG1 
172  C CG2 . THR   A 24  ? 0.73231 0.87500 0.80659 0.03960  0.01701  -0.06673 24  THR   A CG2 
173  N N   . THR   A 25  ? 0.62374 0.72289 0.67726 0.04494  0.00530  -0.06788 25  THR   A N   
174  C CA  . THR   A 25  ? 0.63756 0.72427 0.68482 0.04480  0.00023  -0.06444 25  THR   A CA  
175  C C   . THR   A 25  ? 0.60062 0.68412 0.63375 0.04173  0.00034  -0.06498 25  THR   A C   
176  O O   . THR   A 25  ? 0.59355 0.68124 0.62363 0.04178  0.00384  -0.07097 25  THR   A O   
177  C CB  . THR   A 25  ? 0.62159 0.70129 0.67712 0.04989  -0.00064 -0.06764 25  THR   A CB  
178  O OG1 . THR   A 25  ? 0.65263 0.73831 0.72259 0.05396  0.00120  -0.06863 25  THR   A OG1 
179  C CG2 . THR   A 25  ? 0.62732 0.69580 0.67978 0.04993  -0.00629 -0.06214 25  THR   A CG2 
180  N N   . THR   A 26  ? 0.60627 0.68284 0.63081 0.03912  -0.00340 -0.05873 26  THR   A N   
181  C CA  . THR   A 26  ? 0.58909 0.66293 0.60076 0.03680  -0.00375 -0.05744 26  THR   A CA  
182  C C   . THR   A 26  ? 0.54854 0.61081 0.55646 0.03758  -0.00830 -0.05404 26  THR   A C   
183  O O   . THR   A 26  ? 0.55276 0.60899 0.56289 0.03743  -0.01128 -0.04941 26  THR   A O   
184  C CB  . THR   A 26  ? 0.56266 0.64024 0.56641 0.03259  -0.00232 -0.05221 26  THR   A CB  
185  O OG1 . THR   A 26  ? 0.65610 0.74535 0.66275 0.03158  0.00245  -0.05557 26  THR   A OG1 
186  C CG2 . THR   A 26  ? 0.54769 0.62213 0.53860 0.03115  -0.00294 -0.04941 26  THR   A CG2 
187  N N   . LEU   A 27  ? 0.56306 0.62328 0.56527 0.03810  -0.00873 -0.05661 27  LEU   A N   
188  C CA  . LEU   A 27  ? 0.55909 0.60973 0.55738 0.03874  -0.01249 -0.05372 27  LEU   A CA  
189  C C   . LEU   A 27  ? 0.54011 0.59368 0.52965 0.03792  -0.01223 -0.05538 27  LEU   A C   
190  O O   . LEU   A 27  ? 0.52498 0.58754 0.50995 0.03647  -0.00948 -0.05750 27  LEU   A O   
191  C CB  . LEU   A 27  ? 0.53822 0.58240 0.54556 0.04171  -0.01423 -0.05633 27  LEU   A CB  
192  C CG  . LEU   A 27  ? 0.52375 0.57033 0.53854 0.04391  -0.01172 -0.06452 27  LEU   A CG  
193  C CD1 . LEU   A 27  ? 0.59564 0.63272 0.61688 0.04646  -0.01389 -0.06481 27  LEU   A CD1 
194  C CD2 . LEU   A 27  ? 0.58758 0.64152 0.61069 0.04513  -0.00821 -0.06759 27  LEU   A CD2 
195  N N   . ASN   A 28  ? 0.51495 0.56206 0.50220 0.03875  -0.01513 -0.05427 28  ASN   A N   
196  C CA  . ASN   A 28  ? 0.54459 0.59507 0.52345 0.03797  -0.01587 -0.05398 28  ASN   A CA  
197  C C   . ASN   A 28  ? 0.55343 0.60730 0.53510 0.03816  -0.01555 -0.06215 28  ASN   A C   
198  O O   . ASN   A 28  ? 0.55602 0.60484 0.54606 0.03946  -0.01546 -0.06655 28  ASN   A O   
199  C CB  . ASN   A 28  ? 0.50194 0.54419 0.47632 0.03855  -0.01899 -0.04703 28  ASN   A CB  
200  C CG  . ASN   A 28  ? 0.56790 0.60340 0.54140 0.03804  -0.01921 -0.04036 28  ASN   A CG  
201  O OD1 . ASN   A 28  ? 0.56333 0.60074 0.53070 0.03661  -0.01775 -0.03581 28  ASN   A OD1 
202  N ND2 . ASN   A 28  ? 0.57297 0.60055 0.55232 0.03885  -0.02089 -0.03974 28  ASN   A ND2 
203  N N   . GLY   A 29  ? 0.46966 0.53227 0.44404 0.03663  -0.01526 -0.06399 29  GLY   A N   
204  C CA  . GLY   A 29  ? 0.46535 0.53245 0.44092 0.03558  -0.01498 -0.07226 29  GLY   A CA  
205  C C   . GLY   A 29  ? 0.52155 0.59266 0.49008 0.03469  -0.01799 -0.06971 29  GLY   A C   
206  O O   . GLY   A 29  ? 0.52100 0.59340 0.48265 0.03527  -0.01954 -0.06159 29  GLY   A O   
207  N N   . LEU   A 30  ? 0.52969 0.60290 0.50055 0.03327  -0.01859 -0.07678 30  LEU   A N   
208  C CA  . LEU   A 30  ? 0.53614 0.61538 0.50197 0.03207  -0.02165 -0.07558 30  LEU   A CA  
209  C C   . LEU   A 30  ? 0.55883 0.65251 0.51958 0.02867  -0.02048 -0.08318 30  LEU   A C   
210  O O   . LEU   A 30  ? 0.55686 0.65125 0.52204 0.02642  -0.01829 -0.09343 30  LEU   A O   
211  C CB  . LEU   A 30  ? 0.52339 0.59424 0.49591 0.03220  -0.02352 -0.07745 30  LEU   A CB  
212  C CG  . LEU   A 30  ? 0.55288 0.63034 0.52195 0.03104  -0.02683 -0.07582 30  LEU   A CG  
213  C CD1 . LEU   A 30  ? 0.55781 0.63481 0.52136 0.03392  -0.02914 -0.06430 30  LEU   A CD1 
214  C CD2 . LEU   A 30  ? 0.54812 0.61794 0.52483 0.03014  -0.02764 -0.07974 30  LEU   A CD2 
215  N N   . TRP   A 31  ? 0.51936 0.62436 0.47061 0.02825  -0.02174 -0.07809 31  TRP   A N   
216  C CA  . TRP   A 31  ? 0.51169 0.63249 0.45595 0.02487  -0.02075 -0.08401 31  TRP   A CA  
217  C C   . TRP   A 31  ? 0.54192 0.67289 0.48265 0.02300  -0.02471 -0.08437 31  TRP   A C   
218  O O   . TRP   A 31  ? 0.51149 0.64831 0.44641 0.02481  -0.02769 -0.07504 31  TRP   A O   
219  C CB  . TRP   A 31  ? 0.48876 0.61657 0.42452 0.02562  -0.01925 -0.07740 31  TRP   A CB  
220  C CG  . TRP   A 31  ? 0.52603 0.67060 0.45342 0.02216  -0.01782 -0.08282 31  TRP   A CG  
221  C CD1 . TRP   A 31  ? 0.54806 0.69980 0.47605 0.01818  -0.01607 -0.09539 31  TRP   A CD1 
222  C CD2 . TRP   A 31  ? 0.55585 0.71193 0.47243 0.02211  -0.01760 -0.07586 31  TRP   A CD2 
223  N NE1 . TRP   A 31  ? 0.52456 0.69256 0.44220 0.01541  -0.01503 -0.09710 31  TRP   A NE1 
224  C CE2 . TRP   A 31  ? 0.53034 0.70154 0.44082 0.01793  -0.01606 -0.08473 31  TRP   A CE2 
225  C CE3 . TRP   A 31  ? 0.53962 0.69415 0.45087 0.02504  -0.01819 -0.06294 31  TRP   A CE3 
226  C CZ2 . TRP   A 31  ? 0.59045 0.77625 0.48931 0.01676  -0.01546 -0.08050 31  TRP   A CZ2 
227  C CZ3 . TRP   A 31  ? 0.53458 0.70244 0.43497 0.02412  -0.01733 -0.05837 31  TRP   A CZ3 
228  C CH2 . TRP   A 31  ? 0.60625 0.79010 0.50035 0.02008  -0.01617 -0.06682 31  TRP   A CH2 
229  N N   . LEU   A 32  ? 0.58112 0.71431 0.52591 0.01934  -0.02449 -0.09512 32  LEU   A N   
230  C CA  . LEU   A 32  ? 0.61349 0.75858 0.55578 0.01624  -0.02807 -0.09756 32  LEU   A CA  
231  C C   . LEU   A 32  ? 0.63956 0.79775 0.57771 0.01052  -0.02614 -0.10982 32  LEU   A C   
232  O O   . LEU   A 32  ? 0.62672 0.77820 0.57011 0.00831  -0.02204 -0.12043 32  LEU   A O   
233  C CB  . LEU   A 32  ? 0.57179 0.70688 0.52324 0.01601  -0.02967 -0.09945 32  LEU   A CB  
234  C CG  . LEU   A 32  ? 0.57677 0.69672 0.53315 0.02114  -0.03074 -0.08938 32  LEU   A CG  
235  C CD1 . LEU   A 32  ? 0.53908 0.64774 0.50504 0.02022  -0.03081 -0.09359 32  LEU   A CD1 
236  C CD2 . LEU   A 32  ? 0.56166 0.68816 0.51247 0.02423  -0.03440 -0.07759 32  LEU   A CD2 
237  N N   . ASP   A 33  ? 0.64779 0.82473 0.57657 0.00823  -0.02893 -0.10830 33  ASP   A N   
238  C CA  . ASP   A 33  ? 0.67293 0.86527 0.59485 0.00241  -0.02727 -0.11911 33  ASP   A CA  
239  C C   . ASP   A 33  ? 0.61552 0.80354 0.53542 0.00334  -0.02172 -0.12181 33  ASP   A C   
240  O O   . ASP   A 33  ? 0.60600 0.79014 0.52350 0.00784  -0.02128 -0.11133 33  ASP   A O   
241  C CB  . ASP   A 33  ? 0.68397 0.87657 0.61150 -0.00346 -0.02687 -0.13260 33  ASP   A CB  
242  C CG  . ASP   A 33  ? 0.74650 0.94400 0.67694 -0.00430 -0.03232 -0.12886 33  ASP   A CG  
243  O OD1 . ASP   A 33  ? 0.76630 0.97677 0.69063 -0.00228 -0.03689 -0.11876 33  ASP   A OD1 
244  O OD2 . ASP   A 33  ? 0.76354 0.95205 0.70277 -0.00680 -0.03174 -0.13568 33  ASP   A OD2 
245  N N   . ASP   A 34  ? 0.59341 0.78170 0.51462 -0.00078 -0.01702 -0.13553 34  ASP   A N   
246  C CA  . ASP   A 34  ? 0.64269 0.82799 0.56303 0.00022  -0.01120 -0.13875 34  ASP   A CA  
247  C C   . ASP   A 34  ? 0.63274 0.79851 0.56599 0.00288  -0.00693 -0.14331 34  ASP   A C   
248  O O   . ASP   A 34  ? 0.62444 0.78804 0.56000 0.00218  -0.00110 -0.15188 34  ASP   A O   
249  C CB  . ASP   A 34  ? 0.63856 0.83936 0.55040 -0.00575 -0.00802 -0.15066 34  ASP   A CB  
250  C CG  . ASP   A 34  ? 0.63737 0.83598 0.55432 -0.01122 -0.00588 -0.16630 34  ASP   A CG  
251  O OD1 . ASP   A 34  ? 0.67659 0.86719 0.60104 -0.01144 -0.00876 -0.16642 34  ASP   A OD1 
252  O OD2 . ASP   A 34  ? 0.65923 0.86377 0.57263 -0.01555 -0.00085 -0.17872 34  ASP   A OD2 
253  N N   . VAL   A 35  ? 0.58945 0.74148 0.53124 0.00621  -0.00960 -0.13735 35  VAL   A N   
254  C CA  . VAL   A 35  ? 0.58203 0.71597 0.53612 0.00923  -0.00637 -0.13984 35  VAL   A CA  
255  C C   . VAL   A 35  ? 0.59085 0.71446 0.54834 0.01484  -0.00905 -0.12633 35  VAL   A C   
256  O O   . VAL   A 35  ? 0.59534 0.71972 0.55022 0.01589  -0.01391 -0.11772 35  VAL   A O   
257  C CB  . VAL   A 35  ? 0.59114 0.71714 0.55309 0.00652  -0.00627 -0.14838 35  VAL   A CB  
258  C CG1 . VAL   A 35  ? 0.55853 0.66557 0.53312 0.01055  -0.00323 -0.14873 35  VAL   A CG1 
259  C CG2 . VAL   A 35  ? 0.56658 0.70193 0.52513 0.00008  -0.00295 -0.16316 35  VAL   A CG2 
260  N N   . VAL   A 36  ? 0.52702 0.64158 0.49050 0.01832  -0.00573 -0.12475 36  VAL   A N   
261  C CA  . VAL   A 36  ? 0.53340 0.63783 0.50051 0.02291  -0.00774 -0.11336 36  VAL   A CA  
262  C C   . VAL   A 36  ? 0.52131 0.61035 0.50073 0.02532  -0.00670 -0.11556 36  VAL   A C   
263  O O   . VAL   A 36  ? 0.46768 0.55316 0.45394 0.02536  -0.00224 -0.12417 36  VAL   A O   
264  C CB  . VAL   A 36  ? 0.55734 0.66522 0.52150 0.02462  -0.00527 -0.10847 36  VAL   A CB  
265  C CG1 . VAL   A 36  ? 0.52943 0.62681 0.49732 0.02837  -0.00733 -0.09763 36  VAL   A CG1 
266  C CG2 . VAL   A 36  ? 0.53719 0.66007 0.48863 0.02230  -0.00601 -0.10546 36  VAL   A CG2 
267  N N   . TYR   A 37  ? 0.54936 0.62931 0.53151 0.02754  -0.01049 -0.10757 37  TYR   A N   
268  C CA  . TYR   A 37  ? 0.53959 0.60519 0.53232 0.03000  -0.01019 -0.10760 37  TYR   A CA  
269  C C   . TYR   A 37  ? 0.56379 0.62246 0.55902 0.03388  -0.01126 -0.09803 37  TYR   A C   
270  O O   . TYR   A 37  ? 0.58278 0.64362 0.57150 0.03436  -0.01401 -0.08950 37  TYR   A O   
271  C CB  . TYR   A 37  ? 0.57764 0.63841 0.57159 0.02876  -0.01350 -0.10675 37  TYR   A CB  
272  C CG  . TYR   A 37  ? 0.54941 0.61847 0.54050 0.02391  -0.01328 -0.11573 37  TYR   A CG  
273  C CD1 . TYR   A 37  ? 0.53687 0.62083 0.51796 0.02120  -0.01542 -0.11513 37  TYR   A CD1 
274  C CD2 . TYR   A 37  ? 0.56822 0.63050 0.56664 0.02180  -0.01090 -0.12463 37  TYR   A CD2 
275  C CE1 . TYR   A 37  ? 0.58846 0.68191 0.56674 0.01615  -0.01568 -0.12355 37  TYR   A CE1 
276  C CE2 . TYR   A 37  ? 0.57922 0.64940 0.57504 0.01633  -0.01060 -0.13366 37  TYR   A CE2 
277  C CZ  . TYR   A 37  ? 0.58700 0.67357 0.57264 0.01334  -0.01326 -0.13328 37  TYR   A CZ  
278  O OH  . TYR   A 37  ? 0.60507 0.70140 0.58791 0.00730  -0.01341 -0.14249 37  TYR   A OH  
279  N N   . CYS   A 38  ? 0.60091 0.65143 0.60575 0.03658  -0.00896 -0.09943 38  CYS   A N   
280  C CA  . CYS   A 38  ? 0.57498 0.62033 0.58302 0.03971  -0.01004 -0.09127 38  CYS   A CA  
281  C C   . CYS   A 38  ? 0.57563 0.61086 0.59546 0.04281  -0.00869 -0.09278 38  CYS   A C   
282  O O   . CYS   A 38  ? 0.57298 0.60602 0.59876 0.04285  -0.00538 -0.10096 38  CYS   A O   
283  C CB  . CYS   A 38  ? 0.52346 0.57752 0.52871 0.03969  -0.00768 -0.09020 38  CYS   A CB  
284  S SG  . CYS   A 38  ? 0.60973 0.66742 0.62383 0.04102  -0.00148 -0.09964 38  CYS   A SG  
285  N N   . PRO   A 39  ? 0.53772 0.56657 0.56098 0.04535  -0.01106 -0.08497 39  PRO   A N   
286  C CA  . PRO   A 39  ? 0.55121 0.57186 0.58578 0.04889  -0.01000 -0.08504 39  PRO   A CA  
287  C C   . PRO   A 39  ? 0.56066 0.58589 0.60284 0.05100  -0.00524 -0.09056 39  PRO   A C   
288  O O   . PRO   A 39  ? 0.53259 0.56706 0.57195 0.05030  -0.00376 -0.09070 39  PRO   A O   
289  C CB  . PRO   A 39  ? 0.54513 0.56207 0.57938 0.05034  -0.01383 -0.07515 39  PRO   A CB  
290  C CG  . PRO   A 39  ? 0.56871 0.58742 0.59178 0.04746  -0.01685 -0.07066 39  PRO   A CG  
291  C CD  . PRO   A 39  ? 0.56975 0.59822 0.58648 0.04495  -0.01474 -0.07570 39  PRO   A CD  
292  N N   . ARG   A 40  ? 0.52955 0.54790 0.58183 0.05376  -0.00236 -0.09496 40  ARG   A N   
293  C CA  . ARG   A 40  ? 0.55644 0.57838 0.61692 0.05626  0.00318  -0.10140 40  ARG   A CA  
294  C C   . ARG   A 40  ? 0.55043 0.57660 0.61783 0.06008  0.00305  -0.09552 40  ARG   A C   
295  O O   . ARG   A 40  ? 0.59122 0.62377 0.66439 0.06196  0.00763  -0.10000 40  ARG   A O   
296  C CB  . ARG   A 40  ? 0.56734 0.57915 0.63721 0.05844  0.00698  -0.10763 40  ARG   A CB  
297  C CG  . ARG   A 40  ? 0.56191 0.56344 0.64107 0.06306  0.00518  -0.10059 40  ARG   A CG  
298  C CD  . ARG   A 40  ? 0.53776 0.52799 0.62577 0.06494  0.00968  -0.10667 40  ARG   A CD  
299  N NE  . ARG   A 40  ? 0.53688 0.51617 0.63086 0.06821  0.00718  -0.09899 40  ARG   A NE  
300  C CZ  . ARG   A 40  ? 0.56727 0.53539 0.67161 0.07176  0.01099  -0.10075 40  ARG   A CZ  
301  N NH1 . ARG   A 40  ? 0.60875 0.57403 0.71926 0.07255  0.01787  -0.11063 40  ARG   A NH1 
302  N NH2 . ARG   A 40  ? 0.53214 0.49134 0.64055 0.07457  0.00823  -0.09234 40  ARG   A NH2 
303  N N   . HIS   A 41  ? 0.58815 0.61186 0.65516 0.06096  -0.00188 -0.08600 41  HIS   A N   
304  C CA  . HIS   A 41  ? 0.60385 0.63356 0.67707 0.06361  -0.00256 -0.08047 41  HIS   A CA  
305  C C   . HIS   A 41  ? 0.61195 0.65308 0.67810 0.06027  -0.00238 -0.07956 41  HIS   A C   
306  O O   . HIS   A 41  ? 0.59253 0.63948 0.66206 0.06092  -0.00365 -0.07433 41  HIS   A O   
307  C CB  . HIS   A 41  ? 0.57571 0.59956 0.65044 0.06499  -0.00787 -0.07116 41  HIS   A CB  
308  C CG  . HIS   A 41  ? 0.59289 0.61573 0.65552 0.06065  -0.01249 -0.06577 41  HIS   A CG  
309  N ND1 . HIS   A 41  ? 0.57623 0.60649 0.63348 0.05795  -0.01402 -0.06181 41  HIS   A ND1 
310  C CD2 . HIS   A 41  ? 0.60637 0.62124 0.66182 0.05865  -0.01541 -0.06368 41  HIS   A CD2 
311  C CE1 . HIS   A 41  ? 0.58805 0.61398 0.63519 0.05477  -0.01744 -0.05762 41  HIS   A CE1 
312  N NE2 . HIS   A 41  ? 0.56755 0.58472 0.61356 0.05535  -0.01841 -0.05860 41  HIS   A NE2 
313  N N   . VAL   A 42  ? 0.60256 0.64748 0.65903 0.05647  -0.00079 -0.08433 42  VAL   A N   
314  C CA  . VAL   A 42  ? 0.58752 0.64363 0.63813 0.05368  0.00101  -0.08456 42  VAL   A CA  
315  C C   . VAL   A 42  ? 0.61427 0.67851 0.67485 0.05638  0.00611  -0.08869 42  VAL   A C   
316  O O   . VAL   A 42  ? 0.65801 0.73154 0.71816 0.05510  0.00705  -0.08609 42  VAL   A O   
317  C CB  . VAL   A 42  ? 0.56623 0.62541 0.60509 0.04973  0.00202  -0.08925 42  VAL   A CB  
318  C CG1 . VAL   A 42  ? 0.58098 0.63852 0.62333 0.05042  0.00604  -0.09944 42  VAL   A CG1 
319  C CG2 . VAL   A 42  ? 0.58414 0.65482 0.61631 0.04691  0.00425  -0.08883 42  VAL   A CG2 
320  N N   . ILE   A 43  ? 0.60978 0.67044 0.68004 0.06016  0.00991  -0.09511 43  ILE   A N   
321  C CA  . ILE   A 43  ? 0.64867 0.71681 0.72892 0.06331  0.01590  -0.10030 43  ILE   A CA  
322  C C   . ILE   A 43  ? 0.66242 0.73205 0.75639 0.06844  0.01508  -0.09447 43  ILE   A C   
323  O O   . ILE   A 43  ? 0.70024 0.77685 0.80461 0.07199  0.02004  -0.09780 43  ILE   A O   
324  C CB  . ILE   A 43  ? 0.66596 0.72902 0.75007 0.06490  0.02146  -0.11093 43  ILE   A CB  
325  C CG1 . ILE   A 43  ? 0.62595 0.67587 0.71974 0.06937  0.02048  -0.10960 43  ILE   A CG1 
326  C CG2 . ILE   A 43  ? 0.61296 0.67602 0.68333 0.05927  0.02140  -0.11660 43  ILE   A CG2 
327  C CD1 . ILE   A 43  ? 0.63440 0.67627 0.73058 0.06970  0.02564  -0.11998 43  ILE   A CD1 
328  N N   . CYS   A 44  ? 0.66681 0.73111 0.76121 0.06897  0.00907  -0.08589 44  CYS   A N   
329  C CA  . CYS   A 44  ? 0.66671 0.73386 0.77353 0.07356  0.00738  -0.07964 44  CYS   A CA  
330  C C   . CYS   A 44  ? 0.67956 0.75920 0.78537 0.07076  0.00564  -0.07456 44  CYS   A C   
331  O O   . CYS   A 44  ? 0.69639 0.77821 0.79015 0.06501  0.00388  -0.07303 44  CYS   A O   
332  C CB  . CYS   A 44  ? 0.67868 0.73520 0.78586 0.07499  0.00170  -0.07276 44  CYS   A CB  
333  S SG  . CYS   A 44  ? 0.67636 0.71699 0.78503 0.07752  0.00345  -0.07747 44  CYS   A SG  
334  N N   . THR   A 45  ? 0.64938 0.73740 0.76855 0.07491  0.00636  -0.07175 45  THR   A N   
335  C CA  . THR   A 45  ? 0.67121 0.77050 0.79128 0.07207  0.00341  -0.06555 45  THR   A CA  
336  C C   . THR   A 45  ? 0.70443 0.79825 0.82243 0.07123  -0.00391 -0.05715 45  THR   A C   
337  O O   . THR   A 45  ? 0.69176 0.77329 0.80704 0.07284  -0.00639 -0.05597 45  THR   A O   
338  C CB  . THR   A 45  ? 0.65522 0.76805 0.79119 0.07668  0.00706  -0.06599 45  THR   A CB  
339  O OG1 . THR   A 45  ? 0.64335 0.75147 0.79249 0.08461  0.00788  -0.06555 45  THR   A OG1 
340  C CG2 . THR   A 45  ? 0.61911 0.73955 0.75480 0.07582  0.01447  -0.07405 45  THR   A CG2 
341  N N   . SER   A 46  ? 0.69755 0.80092 0.81661 0.06817  -0.00720 -0.05152 46  SER   A N   
342  C CA  . SER   A 46  ? 0.71471 0.81498 0.83313 0.06752  -0.01389 -0.04395 46  SER   A CA  
343  C C   . SER   A 46  ? 0.75140 0.85197 0.88397 0.07528  -0.01497 -0.04092 46  SER   A C   
344  O O   . SER   A 46  ? 0.76123 0.85358 0.89212 0.07656  -0.01947 -0.03610 46  SER   A O   
345  C CB  . SER   A 46  ? 0.74359 0.85514 0.86050 0.06178  -0.01674 -0.03958 46  SER   A CB  
346  O OG  . SER   A 46  ? 0.78278 0.88757 0.89079 0.05773  -0.02263 -0.03427 46  SER   A OG  
347  N N   . GLU   A 47  ? 0.73306 0.84287 0.87974 0.08083  -0.01045 -0.04344 47  GLU   A N   
348  C CA  . GLU   A 47  ? 0.69612 0.80788 0.85812 0.08911  -0.01095 -0.03955 47  GLU   A CA  
349  C C   . GLU   A 47  ? 0.71902 0.81610 0.88402 0.09499  -0.00732 -0.04328 47  GLU   A C   
350  O O   . GLU   A 47  ? 0.77347 0.86790 0.94917 0.10184  -0.00822 -0.03876 47  GLU   A O   
351  C CB  . GLU   A 47  ? 0.69118 0.82032 0.86869 0.09309  -0.00732 -0.04007 47  GLU   A CB  
352  C CG  . GLU   A 47  ? 0.73787 0.87615 0.93040 0.09949  -0.01093 -0.03200 47  GLU   A CG  
353  C CD  . GLU   A 47  ? 0.83992 0.99849 1.04742 0.10226  -0.00811 -0.03177 47  GLU   A CD  
354  O OE1 . GLU   A 47  ? 0.87337 1.03907 1.07793 0.09783  -0.00385 -0.03746 47  GLU   A OE1 
355  O OE2 . GLU   A 47  ? 0.84136 1.00941 1.06383 0.10903  -0.01003 -0.02553 47  GLU   A OE2 
356  N N   . ASP   A 48  ? 0.73693 0.82486 0.89307 0.09240  -0.00311 -0.05126 48  ASP   A N   
357  C CA  . ASP   A 48  ? 0.72442 0.79807 0.88294 0.09671  0.00055  -0.05570 48  ASP   A CA  
358  C C   . ASP   A 48  ? 0.69307 0.75237 0.84214 0.09458  -0.00423 -0.05208 48  ASP   A C   
359  O O   . ASP   A 48  ? 0.64187 0.68936 0.79544 0.09881  -0.00244 -0.05283 48  ASP   A O   
360  C CB  . ASP   A 48  ? 0.71243 0.78390 0.86588 0.09444  0.00724  -0.06661 48  ASP   A CB  
361  C CG  . ASP   A 48  ? 0.74964 0.82988 0.91641 0.09966  0.01448  -0.07196 48  ASP   A CG  
362  O OD1 . ASP   A 48  ? 0.82096 0.90191 1.00284 0.10736  0.01586  -0.06872 48  ASP   A OD1 
363  O OD2 . ASP   A 48  ? 0.72921 0.81577 0.89139 0.09635  0.01905  -0.07914 48  ASP   A OD2 
364  N N   . MET   A 49  ? 0.72371 0.78346 0.86025 0.08814  -0.00976 -0.04811 49  MET   A N   
365  C CA  . MET   A 49  ? 0.69272 0.73940 0.81876 0.08534  -0.01357 -0.04571 49  MET   A CA  
366  C C   . MET   A 49  ? 0.65368 0.69489 0.78570 0.08972  -0.01737 -0.03785 49  MET   A C   
367  O O   . MET   A 49  ? 0.61551 0.64475 0.74071 0.08841  -0.01941 -0.03628 49  MET   A O   
368  C CB  . MET   A 49  ? 0.72950 0.77855 0.84132 0.07778  -0.01772 -0.04348 49  MET   A CB  
369  C CG  . MET   A 49  ? 0.73049 0.77986 0.83241 0.07303  -0.01447 -0.05040 49  MET   A CG  
370  S SD  . MET   A 49  ? 0.76730 0.82219 0.85600 0.06528  -0.01793 -0.04688 49  MET   A SD  
371  C CE  . MET   A 49  ? 0.70034 0.74705 0.78411 0.06410  -0.02463 -0.03878 49  MET   A CE  
372  N N   . LEU   A 50  ? 0.63967 0.69009 0.78424 0.09490  -0.01838 -0.03250 50  LEU   A N   
373  C CA  . LEU   A 50  ? 0.61934 0.66595 0.76922 0.09929  -0.02232 -0.02391 50  LEU   A CA  
374  C C   . LEU   A 50  ? 0.63487 0.66931 0.79398 0.10625  -0.01788 -0.02508 50  LEU   A C   
375  O O   . LEU   A 50  ? 0.67317 0.69928 0.83278 0.10868  -0.02057 -0.01867 50  LEU   A O   
376  C CB  . LEU   A 50  ? 0.60181 0.66477 0.76160 0.10210  -0.02582 -0.01672 50  LEU   A CB  
377  C CG  . LEU   A 50  ? 0.63199 0.70890 0.78554 0.09521  -0.02958 -0.01564 50  LEU   A CG  
378  C CD1 . LEU   A 50  ? 0.68605 0.77289 0.84246 0.09352  -0.02463 -0.02266 50  LEU   A CD1 
379  C CD2 . LEU   A 50  ? 0.62417 0.71405 0.78490 0.09705  -0.03539 -0.00639 50  LEU   A CD2 
380  N N   . ASN   A 51  ? 0.63953 0.67241 0.80568 0.10923  -0.01079 -0.03316 51  ASN   A N   
381  C CA  . ASN   A 51  ? 0.67680 0.69560 0.85020 0.11443  -0.00524 -0.03657 51  ASN   A CA  
382  C C   . ASN   A 51  ? 0.66314 0.68117 0.83796 0.11378  0.00242  -0.04856 51  ASN   A C   
383  O O   . ASN   A 51  ? 0.62975 0.65119 0.81787 0.12003  0.00805  -0.05131 51  ASN   A O   
384  C CB  . ASN   A 51  ? 0.65302 0.67292 0.84289 0.12402  -0.00451 -0.02897 51  ASN   A CB  
385  C CG  . ASN   A 51  ? 0.66754 0.66904 0.86149 0.12821  -0.00125 -0.02822 51  ASN   A CG  
386  O OD1 . ASN   A 51  ? 0.67188 0.66049 0.85585 0.12320  -0.00045 -0.03286 51  ASN   A OD1 
387  N ND2 . ASN   A 51  ? 0.62456 0.62502 0.83369 0.13744  0.00081  -0.02203 51  ASN   A ND2 
388  N N   . PRO   A 52  ? 0.64932 0.66358 0.81080 0.10652  0.00298  -0.05581 52  PRO   A N   
389  C CA  . PRO   A 52  ? 0.70114 0.71793 0.86188 0.10478  0.00956  -0.06714 52  PRO   A CA  
390  C C   . PRO   A 52  ? 0.67101 0.67391 0.83660 0.10717  0.01641  -0.07515 52  PRO   A C   
391  O O   . PRO   A 52  ? 0.66813 0.65732 0.83282 0.10739  0.01565  -0.07335 52  PRO   A O   
392  C CB  . PRO   A 52  ? 0.66766 0.68685 0.81124 0.09591  0.00628  -0.06989 52  PRO   A CB  
393  C CG  . PRO   A 52  ? 0.63813 0.64760 0.77432 0.09363  0.00054  -0.06349 52  PRO   A CG  
394  C CD  . PRO   A 52  ? 0.63319 0.64242 0.77939 0.09956  -0.00255 -0.05354 52  PRO   A CD  
395  N N   . ASN   A 53  ? 0.61990 0.62654 0.79054 0.10854  0.02360  -0.08449 53  ASN   A N   
396  C CA  . ASN   A 53  ? 0.63834 0.63312 0.81114 0.10870  0.03114  -0.09528 53  ASN   A CA  
397  C C   . ASN   A 53  ? 0.64330 0.64349 0.80245 0.10061  0.03248  -0.10516 53  ASN   A C   
398  O O   . ASN   A 53  ? 0.66242 0.67316 0.82242 0.10036  0.03670  -0.11119 53  ASN   A O   
399  C CB  . ASN   A 53  ? 0.60784 0.60223 0.79747 0.11701  0.03919  -0.09875 53  ASN   A CB  
400  C CG  . ASN   A 53  ? 0.60747 0.58627 0.80046 0.11748  0.04742  -0.10946 53  ASN   A CG  
401  O OD1 . ASN   A 53  ? 0.60411 0.57835 0.78575 0.11012  0.04860  -0.11841 53  ASN   A OD1 
402  N ND2 . ASN   A 53  ? 0.61525 0.58604 0.82421 0.12612  0.05329  -0.10853 53  ASN   A ND2 
403  N N   . TYR   A 54  ? 0.64979 0.64359 0.79637 0.09408  0.02883  -0.10630 54  TYR   A N   
404  C CA  . TYR   A 54  ? 0.63242 0.63290 0.76508 0.08643  0.02869  -0.11359 54  TYR   A CA  
405  C C   . TYR   A 54  ? 0.67203 0.67132 0.80604 0.08526  0.03706  -0.12730 54  TYR   A C   
406  O O   . TYR   A 54  ? 0.68292 0.69287 0.80881 0.08099  0.03868  -0.13344 54  TYR   A O   
407  C CB  . TYR   A 54  ? 0.62819 0.62232 0.74894 0.08058  0.02311  -0.11131 54  TYR   A CB  
408  C CG  . TYR   A 54  ? 0.61381 0.61090 0.72990 0.08020  0.01511  -0.09920 54  TYR   A CG  
409  C CD1 . TYR   A 54  ? 0.61199 0.62125 0.71966 0.07702  0.01154  -0.09587 54  TYR   A CD1 
410  C CD2 . TYR   A 54  ? 0.59244 0.57974 0.71232 0.08281  0.01161  -0.09123 54  TYR   A CD2 
411  C CE1 . TYR   A 54  ? 0.62242 0.63336 0.72559 0.07615  0.00489  -0.08578 54  TYR   A CE1 
412  C CE2 . TYR   A 54  ? 0.60866 0.59873 0.72352 0.08199  0.00469  -0.08103 54  TYR   A CE2 
413  C CZ  . TYR   A 54  ? 0.61791 0.61953 0.72453 0.07856  0.00146  -0.07873 54  TYR   A CZ  
414  O OH  . TYR   A 54  ? 0.61210 0.61552 0.71353 0.07726  -0.00482 -0.06948 54  TYR   A OH  
415  N N   . GLU   A 55  ? 0.66654 0.65276 0.81029 0.08875  0.04278  -0.13231 55  GLU   A N   
416  C CA  . GLU   A 55  ? 0.65867 0.64278 0.80438 0.08762  0.05165  -0.14632 55  GLU   A CA  
417  C C   . GLU   A 55  ? 0.65269 0.64834 0.80581 0.09212  0.05692  -0.14900 55  GLU   A C   
418  O O   . GLU   A 55  ? 0.65868 0.66250 0.80582 0.08832  0.06138  -0.15890 55  GLU   A O   
419  C CB  . GLU   A 55  ? 0.66887 0.63454 0.82462 0.09071  0.05721  -0.15045 55  GLU   A CB  
420  C CG  . GLU   A 55  ? 0.67751 0.63202 0.82548 0.08462  0.05390  -0.15125 55  GLU   A CG  
421  C CD  . GLU   A 55  ? 0.69520 0.64483 0.84400 0.08691  0.04626  -0.13710 55  GLU   A CD  
422  O OE1 . GLU   A 55  ? 0.67873 0.63215 0.83533 0.09363  0.04391  -0.12700 55  GLU   A OE1 
423  O OE2 . GLU   A 55  ? 0.66542 0.60832 0.80703 0.08176  0.04264  -0.13622 55  GLU   A OE2 
424  N N   . ASP   A 56  ? 0.66030 0.65794 0.82648 0.10017  0.05641  -0.13999 56  ASP   A N   
425  C CA  . ASP   A 56  ? 0.68569 0.69618 0.86039 0.10483  0.06095  -0.14114 56  ASP   A CA  
426  C C   . ASP   A 56  ? 0.67000 0.69765 0.83254 0.09891  0.05714  -0.14027 56  ASP   A C   
427  O O   . ASP   A 56  ? 0.67598 0.71315 0.83648 0.09726  0.06274  -0.14853 56  ASP   A O   
428  C CB  . ASP   A 56  ? 0.71038 0.72161 0.90097 0.11415  0.05921  -0.12956 56  ASP   A CB  
429  C CG  . ASP   A 56  ? 0.79609 0.82350 0.99672 0.11912  0.06261  -0.12861 56  ASP   A CG  
430  O OD1 . ASP   A 56  ? 0.86698 0.90488 1.06229 0.11549  0.06671  -0.13668 56  ASP   A OD1 
431  O OD2 . ASP   A 56  ? 0.80390 0.83449 1.01827 0.12683  0.06111  -0.11920 56  ASP   A OD2 
432  N N   . LEU   A 57  ? 0.65594 0.68708 0.80989 0.09549  0.04806  -0.13037 57  LEU   A N   
433  C CA  . LEU   A 57  ? 0.66855 0.71439 0.81135 0.09007  0.04450  -0.12816 57  LEU   A CA  
434  C C   . LEU   A 57  ? 0.68238 0.73114 0.81125 0.08285  0.04730  -0.13854 57  LEU   A C   
435  O O   . LEU   A 57  ? 0.69161 0.75341 0.81509 0.08008  0.04933  -0.14119 57  LEU   A O   
436  C CB  . LEU   A 57  ? 0.62991 0.67560 0.76546 0.08742  0.03487  -0.11655 57  LEU   A CB  
437  C CG  . LEU   A 57  ? 0.62580 0.67576 0.77164 0.09255  0.03066  -0.10517 57  LEU   A CG  
438  C CD1 . LEU   A 57  ? 0.61267 0.66302 0.74810 0.08808  0.02186  -0.09580 57  LEU   A CD1 
439  C CD2 . LEU   A 57  ? 0.59861 0.66404 0.75264 0.09516  0.03418  -0.10528 57  LEU   A CD2 
440  N N   . LEU   A 58  ? 0.68295 0.72056 0.80588 0.07947  0.04753  -0.14439 58  LEU   A N   
441  C CA  . LEU   A 58  ? 0.67488 0.71685 0.78357 0.07200  0.04889  -0.15343 58  LEU   A CA  
442  C C   . LEU   A 58  ? 0.65001 0.69635 0.76149 0.07219  0.05842  -0.16632 58  LEU   A C   
443  O O   . LEU   A 58  ? 0.61574 0.67154 0.71535 0.06639  0.05999  -0.17293 58  LEU   A O   
444  C CB  . LEU   A 58  ? 0.63341 0.66367 0.73578 0.06789  0.04600  -0.15582 58  LEU   A CB  
445  C CG  . LEU   A 58  ? 0.58573 0.62121 0.67306 0.05974  0.04587  -0.16411 58  LEU   A CG  
446  C CD1 . LEU   A 58  ? 0.59148 0.64075 0.66626 0.05598  0.04064  -0.15768 58  LEU   A CD1 
447  C CD2 . LEU   A 58  ? 0.62349 0.64778 0.70730 0.05619  0.04274  -0.16543 58  LEU   A CD2 
448  N N   . ILE   A 59  ? 0.66363 0.70346 0.79047 0.07897  0.06509  -0.16986 59  ILE   A N   
449  C CA  . ILE   A 59  ? 0.66193 0.70513 0.79260 0.07983  0.07521  -0.18258 59  ILE   A CA  
450  C C   . ILE   A 59  ? 0.67864 0.74035 0.80443 0.07830  0.07654  -0.18232 59  ILE   A C   
451  O O   . ILE   A 59  ? 0.71335 0.78314 0.82787 0.07252  0.07991  -0.19128 59  ILE   A O   
452  C CB  . ILE   A 59  ? 0.70074 0.73421 0.85091 0.08906  0.08204  -0.18383 59  ILE   A CB  
453  C CG1 . ILE   A 59  ? 0.65801 0.67173 0.81215 0.08956  0.08344  -0.18736 59  ILE   A CG1 
454  C CG2 . ILE   A 59  ? 0.71628 0.75638 0.87188 0.09119  0.09276  -0.19521 59  ILE   A CG2 
455  C CD1 . ILE   A 59  ? 0.71863 0.72141 0.89011 0.09758  0.09320  -0.19293 59  ILE   A CD1 
456  N N   . ARG   A 60  ? 0.64310 0.71238 0.77724 0.08312  0.07392  -0.17189 60  ARG   A N   
457  C CA  . ARG   A 60  ? 0.70313 0.78982 0.83603 0.08253  0.07545  -0.16994 60  ARG   A CA  
458  C C   . ARG   A 60  ? 0.70134 0.79756 0.81573 0.07424  0.07019  -0.16728 60  ARG   A C   
459  O O   . ARG   A 60  ? 0.74175 0.85178 0.85445 0.07318  0.07056  -0.16360 60  ARG   A O   
460  C CB  . ARG   A 60  ? 0.75052 0.84196 0.89729 0.08901  0.07235  -0.15820 60  ARG   A CB  
461  C CG  . ARG   A 60  ? 0.78326 0.86420 0.94861 0.09813  0.07560  -0.15735 60  ARG   A CG  
462  C CD  . ARG   A 60  ? 0.81474 0.90103 0.99173 0.10363  0.07010  -0.14395 60  ARG   A CD  
463  N NE  . ARG   A 60  ? 0.79511 0.86860 0.98597 0.11133  0.07002  -0.13993 60  ARG   A NE  
464  C CZ  . ARG   A 60  ? 0.87392 0.95206 1.08219 0.11981  0.07088  -0.13319 60  ARG   A CZ  
465  N NH1 . ARG   A 60  ? 0.96263 1.05835 1.17769 0.12160  0.07222  -0.13052 60  ARG   A NH1 
466  N NH2 . ARG   A 60  ? 0.85484 0.92038 1.07421 0.12664  0.07040  -0.12858 60  ARG   A NH2 
467  N N   . LYS   A 61  ? 0.70703 0.79704 0.80821 0.06851  0.06571  -0.16867 61  LYS   A N   
468  C CA  . LYS   A 61  ? 0.68841 0.78715 0.77227 0.06135  0.06084  -0.16550 61  LYS   A CA  
469  C C   . LYS   A 61  ? 0.69621 0.79846 0.76808 0.05558  0.06514  -0.17768 61  LYS   A C   
470  O O   . LYS   A 61  ? 0.69359 0.78605 0.76550 0.05450  0.06683  -0.18577 61  LYS   A O   
471  C CB  . LYS   A 61  ? 0.70029 0.79121 0.77811 0.05944  0.05142  -0.15591 61  LYS   A CB  
472  C CG  . LYS   A 61  ? 0.67638 0.76100 0.76602 0.06493  0.04706  -0.14536 61  LYS   A CG  
473  C CD  . LYS   A 61  ? 0.69985 0.79578 0.79003 0.06506  0.04464  -0.13628 61  LYS   A CD  
474  C CE  . LYS   A 61  ? 0.68215 0.77277 0.78077 0.06881  0.03865  -0.12526 61  LYS   A CE  
475  N NZ  . LYS   A 61  ? 0.65563 0.74680 0.77234 0.07618  0.04241  -0.12503 61  LYS   A NZ  
476  N N   . SER   A 62  ? 0.73541 0.85194 0.79688 0.05149  0.06699  -0.17893 62  SER   A N   
477  C CA  . SER   A 62  ? 0.69675 0.81963 0.74334 0.04486  0.06915  -0.18823 62  SER   A CA  
478  C C   . SER   A 62  ? 0.66086 0.78736 0.69219 0.03961  0.06070  -0.17997 62  SER   A C   
479  O O   . SER   A 62  ? 0.65439 0.77773 0.68672 0.04106  0.05409  -0.16787 62  SER   A O   
480  C CB  . SER   A 62  ? 0.69990 0.83699 0.74361 0.04361  0.07701  -0.19486 62  SER   A CB  
481  O OG  . SER   A 62  ? 0.73521 0.88459 0.76917 0.04066  0.07380  -0.18580 62  SER   A OG  
482  N N   . ASN   A 63  ? 0.69052 0.82411 0.70758 0.03348  0.06115  -0.18675 63  ASN   A N   
483  C CA  . ASN   A 63  ? 0.64753 0.78545 0.65036 0.02900  0.05348  -0.17905 63  ASN   A CA  
484  C C   . ASN   A 63  ? 0.66399 0.81027 0.66187 0.02911  0.05078  -0.16684 63  ASN   A C   
485  O O   . ASN   A 63  ? 0.65230 0.79739 0.64346 0.02793  0.04380  -0.15660 63  ASN   A O   
486  C CB  . ASN   A 63  ? 0.65057 0.79793 0.63916 0.02247  0.05490  -0.18865 63  ASN   A CB  
487  C CG  . ASN   A 63  ? 0.65415 0.79231 0.64529 0.02058  0.05531  -0.19902 63  ASN   A CG  
488  O OD1 . ASN   A 63  ? 0.63098 0.75512 0.63225 0.02379  0.05272  -0.19639 63  ASN   A OD1 
489  N ND2 . ASN   A 63  ? 0.67070 0.81695 0.65241 0.01489  0.05880  -0.21104 63  ASN   A ND2 
490  N N   . HIS   A 64  ? 0.67168 0.82602 0.67337 0.03049  0.05664  -0.16778 64  HIS   A N   
491  C CA  . HIS   A 64  ? 0.66454 0.82769 0.66085 0.02943  0.05524  -0.15730 64  HIS   A CA  
492  C C   . HIS   A 64  ? 0.62865 0.78464 0.63571 0.03341  0.05134  -0.14625 64  HIS   A C   
493  O O   . HIS   A 64  ? 0.66342 0.82367 0.66533 0.03181  0.04868  -0.13626 64  HIS   A O   
494  C CB  . HIS   A 64  ? 0.69583 0.87207 0.69133 0.02844  0.06353  -0.16304 64  HIS   A CB  
495  C CG  . HIS   A 64  ? 0.76499 0.94858 0.75102 0.02457  0.06859  -0.17584 64  HIS   A CG  
496  N ND1 . HIS   A 64  ? 0.73485 0.91219 0.72761 0.02578  0.07300  -0.18879 64  HIS   A ND1 
497  C CD2 . HIS   A 64  ? 0.73111 0.92792 0.70104 0.01918  0.07008  -0.17778 64  HIS   A CD2 
498  C CE1 . HIS   A 64  ? 0.71740 0.90392 0.69839 0.02080  0.07700  -0.19901 64  HIS   A CE1 
499  N NE2 . HIS   A 64  ? 0.72719 0.92637 0.69398 0.01682  0.07506  -0.19235 64  HIS   A NE2 
500  N N   . ASN   A 65  ? 0.63632 0.78164 0.65785 0.03829  0.05107  -0.14770 65  ASN   A N   
501  C CA  . ASN   A 65  ? 0.62469 0.76422 0.65596 0.04175  0.04683  -0.13740 65  ASN   A CA  
502  C C   . ASN   A 65  ? 0.64014 0.77222 0.66385 0.03999  0.03845  -0.12775 65  ASN   A C   
503  O O   . ASN   A 65  ? 0.66395 0.79209 0.69286 0.04161  0.03458  -0.11872 65  ASN   A O   
504  C CB  . ASN   A 65  ? 0.65910 0.78966 0.70740 0.04781  0.04863  -0.14092 65  ASN   A CB  
505  C CG  . ASN   A 65  ? 0.66810 0.80622 0.72756 0.05116  0.05689  -0.14747 65  ASN   A CG  
506  O OD1 . ASN   A 65  ? 0.67341 0.80654 0.74163 0.05463  0.06187  -0.15636 65  ASN   A OD1 
507  N ND2 . ASN   A 65  ? 0.63855 0.78852 0.69822 0.05013  0.05885  -0.14312 65  ASN   A ND2 
508  N N   . PHE   A 66  ? 0.65049 0.78132 0.66234 0.03664  0.03573  -0.12961 66  PHE   A N   
509  C CA  . PHE   A 66  ? 0.61925 0.74333 0.62422 0.03539  0.02836  -0.12106 66  PHE   A CA  
510  C C   . PHE   A 66  ? 0.58652 0.71926 0.57697 0.03133  0.02690  -0.11483 66  PHE   A C   
511  O O   . PHE   A 66  ? 0.58627 0.72889 0.56737 0.02827  0.02980  -0.11996 66  PHE   A O   
512  C CB  . PHE   A 66  ? 0.61063 0.72742 0.61402 0.03488  0.02604  -0.12668 66  PHE   A CB  
513  C CG  . PHE   A 66  ? 0.59513 0.70144 0.61246 0.03889  0.02766  -0.13188 66  PHE   A CG  
514  C CD1 . PHE   A 66  ? 0.58749 0.68379 0.61369 0.04252  0.02386  -0.12447 66  PHE   A CD1 
515  C CD2 . PHE   A 66  ? 0.61199 0.71824 0.63336 0.03899  0.03335  -0.14409 66  PHE   A CD2 
516  C CE1 . PHE   A 66  ? 0.60164 0.68834 0.64059 0.04663  0.02542  -0.12806 66  PHE   A CE1 
517  C CE2 . PHE   A 66  ? 0.61772 0.71300 0.65239 0.04312  0.03545  -0.14821 66  PHE   A CE2 
518  C CZ  . PHE   A 66  ? 0.62839 0.71404 0.67193 0.04718  0.03136  -0.13964 66  PHE   A CZ  
519  N N   . LEU   A 67  ? 0.60132 0.73016 0.58968 0.03126  0.02264  -0.10373 67  LEU   A N   
520  C CA  . LEU   A 67  ? 0.62030 0.75507 0.59605 0.02807  0.02154  -0.09593 67  LEU   A CA  
521  C C   . LEU   A 67  ? 0.61587 0.74319 0.58472 0.02786  0.01525  -0.08928 67  LEU   A C   
522  O O   . LEU   A 67  ? 0.61098 0.72898 0.58306 0.02916  0.01167  -0.08186 67  LEU   A O   
523  C CB  . LEU   A 67  ? 0.62261 0.75892 0.60187 0.02769  0.02306  -0.08876 67  LEU   A CB  
524  C CG  . LEU   A 67  ? 0.71453 0.85577 0.68180 0.02428  0.02323  -0.08015 67  LEU   A CG  
525  C CD1 . LEU   A 67  ? 0.67934 0.83337 0.63612 0.02168  0.02722  -0.08445 67  LEU   A CD1 
526  C CD2 . LEU   A 67  ? 0.65661 0.79851 0.62941 0.02324  0.02519  -0.07436 67  LEU   A CD2 
527  N N   . VAL   A 68  ? 0.60085 0.73316 0.56029 0.02609  0.01404  -0.09216 68  VAL   A N   
528  C CA  . VAL   A 68  ? 0.58003 0.70799 0.53274 0.02604  0.00846  -0.08597 68  VAL   A CA  
529  C C   . VAL   A 68  ? 0.59149 0.72644 0.53182 0.02423  0.00813  -0.07715 68  VAL   A C   
530  O O   . VAL   A 68  ? 0.58654 0.73363 0.51920 0.02190  0.01130  -0.07964 68  VAL   A O   
531  C CB  . VAL   A 68  ? 0.58306 0.71330 0.53403 0.02511  0.00689  -0.09413 68  VAL   A CB  
532  C CG1 . VAL   A 68  ? 0.51984 0.64486 0.46706 0.02576  0.00098  -0.08755 68  VAL   A CG1 
533  C CG2 . VAL   A 68  ? 0.56019 0.68396 0.52327 0.02659  0.00910  -0.10395 68  VAL   A CG2 
534  N N   . GLN   A 69  ? 0.60612 0.73311 0.54426 0.02535  0.00469  -0.06673 69  GLN   A N   
535  C CA  . GLN   A 69  ? 0.63793 0.76867 0.56533 0.02430  0.00476  -0.05681 69  GLN   A CA  
536  C C   . GLN   A 69  ? 0.61325 0.73800 0.53631 0.02611  -0.00021 -0.04935 69  GLN   A C   
537  O O   . GLN   A 69  ? 0.57595 0.68846 0.50501 0.02798  -0.00278 -0.04655 69  GLN   A O   
538  C CB  . GLN   A 69  ? 0.63950 0.76563 0.56944 0.02357  0.00756  -0.05061 69  GLN   A CB  
539  C CG  . GLN   A 69  ? 0.67521 0.80990 0.60868 0.02172  0.01304  -0.05650 69  GLN   A CG  
540  C CD  . GLN   A 69  ? 0.69781 0.82666 0.63947 0.02125  0.01485  -0.05320 69  GLN   A CD  
541  O OE1 . GLN   A 69  ? 0.66084 0.78060 0.61203 0.02301  0.01249  -0.05406 69  GLN   A OE1 
542  N NE2 . GLN   A 69  ? 0.71076 0.84560 0.64864 0.01851  0.01906  -0.04927 69  GLN   A NE2 
543  N N   . ALA   A 70  ? 0.62953 0.76372 0.54223 0.02567  -0.00143 -0.04598 70  ALA   A N   
544  C CA  . ALA   A 70  ? 0.63528 0.76618 0.54335 0.02791  -0.00559 -0.03747 70  ALA   A CA  
545  C C   . ALA   A 70  ? 0.72018 0.85227 0.61931 0.02812  -0.00382 -0.02583 70  ALA   A C   
546  O O   . ALA   A 70  ? 0.73659 0.88153 0.62656 0.02686  -0.00250 -0.02404 70  ALA   A O   
547  C CB  . ALA   A 70  ? 0.58109 0.72307 0.48519 0.02759  -0.00882 -0.04199 70  ALA   A CB  
548  N N   . GLY   A 71  ? 0.71865 0.83715 0.62008 0.02947  -0.00351 -0.01796 71  GLY   A N   
549  C CA  . GLY   A 71  ? 0.77955 0.89656 0.67347 0.02926  -0.00072 -0.00717 71  GLY   A CA  
550  C C   . GLY   A 71  ? 0.85973 0.98163 0.75317 0.02569  0.00440  -0.00943 71  GLY   A C   
551  O O   . GLY   A 71  ? 0.83588 0.95462 0.73788 0.02409  0.00597  -0.01624 71  GLY   A O   
552  N N   . ASN   A 72  ? 0.85184 0.98239 0.73540 0.02457  0.00716  -0.00323 72  ASN   A N   
553  C CA  . ASN   A 72  ? 0.89434 1.03142 0.77630 0.02090  0.01257  -0.00480 72  ASN   A CA  
554  C C   . ASN   A 72  ? 0.89034 1.04494 0.76809 0.01916  0.01379  -0.01327 72  ASN   A C   
555  O O   . ASN   A 72  ? 0.91247 1.07600 0.78490 0.01639  0.01844  -0.01256 72  ASN   A O   
556  C CB  . ASN   A 72  ? 0.93633 1.07060 0.80995 0.02008  0.01602  0.00779  72  ASN   A CB  
557  C CG  . ASN   A 72  ? 1.01524 1.13494 0.89497 0.01818  0.01879  0.01142  72  ASN   A CG  
558  O OD1 . ASN   A 72  ? 1.00327 1.12073 0.89251 0.01622  0.01964  0.00394  72  ASN   A OD1 
559  N ND2 . ASN   A 72  ? 1.06245 1.17241 0.93691 0.01869  0.02034  0.02298  72  ASN   A ND2 
560  N N   . VAL   A 73  ? 0.88021 1.03981 0.76001 0.02029  0.01011  -0.02158 73  VAL   A N   
561  C CA  . VAL   A 73  ? 0.81619 0.99121 0.69270 0.01806  0.01147  -0.03179 73  VAL   A CA  
562  C C   . VAL   A 73  ? 0.76698 0.93801 0.65546 0.01799  0.01145  -0.04467 73  VAL   A C   
563  O O   . VAL   A 73  ? 0.72712 0.88643 0.62391 0.02024  0.00804  -0.04536 73  VAL   A O   
564  C CB  . VAL   A 73  ? 0.81734 1.00432 0.68399 0.01860  0.00751  -0.03045 73  VAL   A CB  
565  C CG1 . VAL   A 73  ? 0.82920 1.01638 0.68634 0.02055  0.00649  -0.01523 73  VAL   A CG1 
566  C CG2 . VAL   A 73  ? 0.76137 0.94413 0.63446 0.02041  0.00220  -0.03610 73  VAL   A CG2 
567  N N   . GLN   A 74  ? 0.79468 0.97505 0.68412 0.01559  0.01576  -0.05453 74  GLN   A N   
568  C CA  . GLN   A 74  ? 0.71370 0.89088 0.61449 0.01590  0.01674  -0.06696 74  GLN   A CA  
569  C C   . GLN   A 74  ? 0.68267 0.86767 0.58024 0.01487  0.01470  -0.07645 74  GLN   A C   
570  O O   . GLN   A 74  ? 0.71471 0.91342 0.60076 0.01252  0.01493  -0.07702 74  GLN   A O   
571  C CB  . GLN   A 74  ? 0.71133 0.89357 0.61669 0.01429  0.02340  -0.07308 74  GLN   A CB  
572  C CG  . GLN   A 74  ? 0.77823 0.94964 0.69595 0.01579  0.02472  -0.07069 74  GLN   A CG  
573  C CD  . GLN   A 74  ? 0.86687 1.04467 0.78408 0.01354  0.03061  -0.06811 74  GLN   A CD  
574  O OE1 . GLN   A 74  ? 0.96503 1.15515 0.87275 0.01100  0.03436  -0.06890 74  GLN   A OE1 
575  N NE2 . GLN   A 74  ? 0.84522 1.01553 0.77257 0.01411  0.03149  -0.06505 74  GLN   A NE2 
576  N N   . LEU   A 75  ? 0.68451 0.86105 0.59210 0.01627  0.01276  -0.08378 75  LEU   A N   
577  C CA  . LEU   A 75  ? 0.68361 0.86564 0.59031 0.01458  0.01150  -0.09450 75  LEU   A CA  
578  C C   . LEU   A 75  ? 0.66229 0.84394 0.57738 0.01382  0.01699  -0.10780 75  LEU   A C   
579  O O   . LEU   A 75  ? 0.65528 0.82588 0.58260 0.01649  0.01852  -0.10891 75  LEU   A O   
580  C CB  . LEU   A 75  ? 0.67878 0.85108 0.59051 0.01648  0.00567  -0.09288 75  LEU   A CB  
581  C CG  . LEU   A 75  ? 0.62691 0.79650 0.53319 0.01850  0.00074  -0.07912 75  LEU   A CG  
582  C CD1 . LEU   A 75  ? 0.55946 0.71967 0.47184 0.02037  -0.00427 -0.07860 75  LEU   A CD1 
583  C CD2 . LEU   A 75  ? 0.61659 0.80201 0.50883 0.01663  -0.00042 -0.07457 75  LEU   A CD2 
584  N N   . ARG   A 76  ? 0.68860 0.88271 0.59707 0.01029  0.02011  -0.11772 76  ARG   A N   
585  C CA  . ARG   A 76  ? 0.67640 0.87102 0.59180 0.00958  0.02661  -0.13084 76  ARG   A CA  
586  C C   . ARG   A 76  ? 0.68939 0.87434 0.61438 0.01011  0.02568  -0.14065 76  ARG   A C   
587  O O   . ARG   A 76  ? 0.70755 0.89555 0.62762 0.00751  0.02209  -0.14430 76  ARG   A O   
588  C CB  . ARG   A 76  ? 0.66989 0.88154 0.57341 0.00509  0.03100  -0.13820 76  ARG   A CB  
589  C CG  . ARG   A 76  ? 0.66267 0.87688 0.57156 0.00509  0.03946  -0.14691 76  ARG   A CG  
590  C CD  . ARG   A 76  ? 0.66570 0.89702 0.56163 0.00015  0.04396  -0.15519 76  ARG   A CD  
591  N NE  . ARG   A 76  ? 0.72649 0.95766 0.62909 -0.00060 0.05145  -0.17085 76  ARG   A NE  
592  C CZ  . ARG   A 76  ? 0.71031 0.94386 0.61806 0.00066  0.05899  -0.17423 76  ARG   A CZ  
593  N NH1 . ARG   A 76  ? 0.69364 0.93026 0.60076 0.00206  0.06000  -0.16336 76  ARG   A NH1 
594  N NH2 . ARG   A 76  ? 0.63971 0.87243 0.55391 0.00043  0.06610  -0.18900 76  ARG   A NH2 
595  N N   . VAL   A 77  ? 0.64776 0.82149 0.58680 0.01345  0.02898  -0.14447 77  VAL   A N   
596  C CA  . VAL   A 77  ? 0.61013 0.77259 0.55953 0.01452  0.02891  -0.15284 77  VAL   A CA  
597  C C   . VAL   A 77  ? 0.65616 0.82443 0.60452 0.01125  0.03514  -0.16865 77  VAL   A C   
598  O O   . VAL   A 77  ? 0.64421 0.81687 0.59482 0.01173  0.04193  -0.17423 77  VAL   A O   
599  C CB  . VAL   A 77  ? 0.58536 0.73382 0.55025 0.01993  0.02984  -0.14950 77  VAL   A CB  
600  C CG1 . VAL   A 77  ? 0.59042 0.72656 0.56574 0.02125  0.03010  -0.15725 77  VAL   A CG1 
601  C CG2 . VAL   A 77  ? 0.59676 0.73982 0.56152 0.02227  0.02403  -0.13479 77  VAL   A CG2 
602  N N   . ILE   A 78  ? 0.68061 0.84913 0.62570 0.00760  0.03315  -0.17627 78  ILE   A N   
603  C CA  . ILE   A 78  ? 0.67778 0.85166 0.62040 0.00324  0.03887  -0.19229 78  ILE   A CA  
604  C C   . ILE   A 78  ? 0.63960 0.79796 0.59617 0.00486  0.04251  -0.20224 78  ILE   A C   
605  O O   . ILE   A 78  ? 0.72725 0.88541 0.68692 0.00369  0.05013  -0.21522 78  ILE   A O   
606  C CB  . ILE   A 78  ? 0.67135 0.85903 0.59935 -0.00339 0.03479  -0.19548 78  ILE   A CB  
607  C CG1 . ILE   A 78  ? 0.71054 0.91706 0.62376 -0.00649 0.03649  -0.19418 78  ILE   A CG1 
608  C CG2 . ILE   A 78  ? 0.65011 0.83570 0.57972 -0.00830 0.03758  -0.21159 78  ILE   A CG2 
609  C CD1 . ILE   A 78  ? 0.70735 0.91564 0.61913 -0.00238 0.03579  -0.17984 78  ILE   A CD1 
610  N N   . GLY   A 79  ? 0.62983 0.77461 0.59509 0.00778  0.03782  -0.19623 79  GLY   A N   
611  C CA  . GLY   A 79  ? 0.60997 0.73853 0.58933 0.01027  0.04132  -0.20318 79  GLY   A CA  
612  C C   . GLY   A 79  ? 0.61950 0.73473 0.60895 0.01602  0.03661  -0.19097 79  GLY   A C   
613  O O   . GLY   A 79  ? 0.59876 0.71698 0.58362 0.01728  0.03057  -0.17836 79  GLY   A O   
614  N N   . HIS   A 80  ? 0.61939 0.71952 0.62251 0.01951  0.03978  -0.19480 80  HIS   A N   
615  C CA  . HIS   A 80  ? 0.60836 0.69574 0.62096 0.02468  0.03544  -0.18389 80  HIS   A CA  
616  C C   . HIS   A 80  ? 0.58878 0.66020 0.61334 0.02623  0.03858  -0.19045 80  HIS   A C   
617  O O   . HIS   A 80  ? 0.59921 0.66711 0.62948 0.02637  0.04609  -0.20181 80  HIS   A O   
618  C CB  . HIS   A 80  ? 0.62672 0.71439 0.64564 0.03061  0.03612  -0.17485 80  HIS   A CB  
619  C CG  . HIS   A 80  ? 0.62558 0.70988 0.65605 0.03469  0.04413  -0.18189 80  HIS   A CG  
620  N ND1 . HIS   A 80  ? 0.64651 0.74195 0.67397 0.03379  0.05021  -0.18841 80  HIS   A ND1 
621  C CD2 . HIS   A 80  ? 0.62981 0.70120 0.67522 0.04015  0.04732  -0.18289 80  HIS   A CD2 
622  C CE1 . HIS   A 80  ? 0.65159 0.74117 0.69223 0.03868  0.05700  -0.19356 80  HIS   A CE1 
623  N NE2 . HIS   A 80  ? 0.62537 0.70033 0.67723 0.04282  0.05528  -0.19003 80  HIS   A NE2 
624  N N   . SER   A 81  ? 0.56547 0.62688 0.59363 0.02736  0.03328  -0.18317 81  SER   A N   
625  C CA  . SER   A 81  ? 0.57960 0.62467 0.61906 0.02901  0.03571  -0.18702 81  SER   A CA  
626  C C   . SER   A 81  ? 0.61240 0.64853 0.65609 0.03254  0.02937  -0.17400 81  SER   A C   
627  O O   . SER   A 81  ? 0.62586 0.66834 0.66168 0.03160  0.02287  -0.16472 81  SER   A O   
628  C CB  . SER   A 81  ? 0.61430 0.65832 0.64969 0.02189  0.03732  -0.19891 81  SER   A CB  
629  O OG  . SER   A 81  ? 0.58244 0.62848 0.61151 0.01828  0.03006  -0.19313 81  SER   A OG  
630  N N   . MET   A 82  ? 0.59850 0.61954 0.65455 0.03671  0.03171  -0.17333 82  MET   A N   
631  C CA  . MET   A 82  ? 0.59121 0.60297 0.65207 0.04043  0.02653  -0.16139 82  MET   A CA  
632  C C   . MET   A 82  ? 0.60969 0.61033 0.67264 0.03728  0.02587  -0.16415 82  MET   A C   
633  O O   . MET   A 82  ? 0.61320 0.60535 0.68223 0.03600  0.03176  -0.17409 82  MET   A O   
634  C CB  . MET   A 82  ? 0.60440 0.60872 0.67805 0.04827  0.02911  -0.15611 82  MET   A CB  
635  C CG  . MET   A 82  ? 0.61728 0.61074 0.69672 0.05199  0.02462  -0.14504 82  MET   A CG  
636  S SD  . MET   A 82  ? 0.70593 0.69212 0.80124 0.06133  0.02768  -0.13914 82  MET   A SD  
637  C CE  . MET   A 82  ? 0.70430 0.67096 0.80941 0.06273  0.03098  -0.14157 82  MET   A CE  
638  N N   . GLN   A 83  ? 0.59300 0.59342 0.65113 0.03587  0.01921  -0.15559 83  GLN   A N   
639  C CA  . GLN   A 83  ? 0.59248 0.58276 0.65305 0.03312  0.01802  -0.15609 83  GLN   A CA  
640  C C   . GLN   A 83  ? 0.59250 0.57351 0.65810 0.03820  0.01413  -0.14328 83  GLN   A C   
641  O O   . GLN   A 83  ? 0.61441 0.60064 0.67349 0.03826  0.00815  -0.13416 83  GLN   A O   
642  C CB  . GLN   A 83  ? 0.58207 0.58241 0.63197 0.02610  0.01387  -0.15842 83  GLN   A CB  
643  C CG  . GLN   A 83  ? 0.58972 0.58127 0.64267 0.02204  0.01353  -0.16099 83  GLN   A CG  
644  C CD  . GLN   A 83  ? 0.62583 0.62970 0.66920 0.01543  0.00897  -0.16253 83  GLN   A CD  
645  O OE1 . GLN   A 83  ? 0.61587 0.63460 0.64987 0.01424  0.00598  -0.16118 83  GLN   A OE1 
646  N NE2 . GLN   A 83  ? 0.62416 0.62243 0.67023 0.01118  0.00853  -0.16488 83  GLN   A NE2 
647  N N   . ASN   A 84  ? 0.56388 0.53113 0.64088 0.04252  0.01782  -0.14259 84  ASN   A N   
648  C CA  . ASN   A 84  ? 0.58329 0.54161 0.66574 0.04766  0.01472  -0.13068 84  ASN   A CA  
649  C C   . ASN   A 84  ? 0.60233 0.56959 0.68217 0.05174  0.01099  -0.12187 84  ASN   A C   
650  O O   . ASN   A 84  ? 0.59042 0.56244 0.67413 0.05486  0.01428  -0.12446 84  ASN   A O   
651  C CB  . ASN   A 84  ? 0.61813 0.57188 0.69664 0.04384  0.01066  -0.12675 84  ASN   A CB  
652  C CG  . ASN   A 84  ? 0.64505 0.58782 0.72884 0.04013  0.01518  -0.13488 84  ASN   A CG  
653  O OD1 . ASN   A 84  ? 0.65938 0.60650 0.73771 0.03338  0.01466  -0.14141 84  ASN   A OD1 
654  N ND2 . ASN   A 84  ? 0.60173 0.53046 0.69653 0.04444  0.01973  -0.13429 84  ASN   A ND2 
655  N N   . CYS   A 85  ? 0.60423 0.57410 0.67797 0.05162  0.00476  -0.11205 85  CYS   A N   
656  C CA  . CYS   A 85  ? 0.58979 0.56700 0.66116 0.05469  0.00144  -0.10389 85  CYS   A CA  
657  C C   . CYS   A 85  ? 0.59621 0.58673 0.65650 0.05109  -0.00066 -0.10489 85  CYS   A C   
658  O O   . CYS   A 85  ? 0.58595 0.58235 0.64306 0.05255  -0.00339 -0.09814 85  CYS   A O   
659  C CB  . CYS   A 85  ? 0.56783 0.53941 0.63869 0.05658  -0.00361 -0.09261 85  CYS   A CB  
660  S SG  . CYS   A 85  ? 0.58686 0.54529 0.67072 0.06250  -0.00190 -0.08764 85  CYS   A SG  
661  N N   . VAL   A 86  ? 0.56274 0.55839 0.61708 0.04625  0.00062  -0.11292 86  VAL   A N   
662  C CA  . VAL   A 86  ? 0.58329 0.59199 0.62662 0.04290  -0.00136 -0.11332 86  VAL   A CA  
663  C C   . VAL   A 86  ? 0.58095 0.59767 0.62397 0.04166  0.00367  -0.12302 86  VAL   A C   
664  O O   . VAL   A 86  ? 0.58176 0.59462 0.62958 0.04039  0.00827  -0.13268 86  VAL   A O   
665  C CB  . VAL   A 86  ? 0.57807 0.58926 0.61367 0.03823  -0.00469 -0.11370 86  VAL   A CB  
666  C CG1 . VAL   A 86  ? 0.59100 0.61654 0.61660 0.03441  -0.00502 -0.11767 86  VAL   A CG1 
667  C CG2 . VAL   A 86  ? 0.57318 0.58066 0.60579 0.03958  -0.00987 -0.10265 86  VAL   A CG2 
668  N N   . LEU   A 87  ? 0.56705 0.59443 0.60438 0.04180  0.00329  -0.12061 87  LEU   A N   
669  C CA  . LEU   A 87  ? 0.57042 0.60765 0.60509 0.04002  0.00784  -0.12914 87  LEU   A CA  
670  C C   . LEU   A 87  ? 0.58014 0.62817 0.60249 0.03448  0.00596  -0.13231 87  LEU   A C   
671  O O   . LEU   A 87  ? 0.58769 0.63854 0.60281 0.03329  0.00082  -0.12487 87  LEU   A O   
672  C CB  . LEU   A 87  ? 0.59415 0.63802 0.62961 0.04291  0.00893  -0.12457 87  LEU   A CB  
673  C CG  . LEU   A 87  ? 0.57554 0.62914 0.61019 0.04202  0.01475  -0.13305 87  LEU   A CG  
674  C CD1 . LEU   A 87  ? 0.60502 0.65199 0.64934 0.04335  0.02099  -0.14376 87  LEU   A CD1 
675  C CD2 . LEU   A 87  ? 0.60136 0.66124 0.63815 0.04485  0.01556  -0.12720 87  LEU   A CD2 
676  N N   . LYS   A 88  ? 0.57628 0.63078 0.59633 0.03120  0.01033  -0.14346 88  LYS   A N   
677  C CA  . LYS   A 88  ? 0.56747 0.63430 0.57587 0.02559  0.00874  -0.14756 88  LYS   A CA  
678  C C   . LYS   A 88  ? 0.56160 0.64066 0.56445 0.02414  0.01296  -0.15332 88  LYS   A C   
679  O O   . LYS   A 88  ? 0.57939 0.65686 0.58745 0.02411  0.01915  -0.16336 88  LYS   A O   
680  C CB  . LYS   A 88  ? 0.54739 0.61097 0.55705 0.02108  0.00959  -0.15713 88  LYS   A CB  
681  C CG  . LYS   A 88  ? 0.58550 0.63823 0.59983 0.02174  0.00560  -0.15149 88  LYS   A CG  
682  C CD  . LYS   A 88  ? 0.54686 0.60092 0.55966 0.01565  0.00532  -0.15990 88  LYS   A CD  
683  C CE  . LYS   A 88  ? 0.56414 0.60751 0.58599 0.01439  0.01182  -0.17163 88  LYS   A CE  
684  N NZ  . LYS   A 88  ? 0.58963 0.62947 0.61287 0.00880  0.01121  -0.17760 88  LYS   A NZ  
685  N N   . LEU   A 89  ? 0.54380 0.63464 0.53612 0.02304  0.01011  -0.14690 89  LEU   A N   
686  C CA  . LEU   A 89  ? 0.56784 0.67150 0.55331 0.02145  0.01381  -0.15060 89  LEU   A CA  
687  C C   . LEU   A 89  ? 0.56713 0.68495 0.53950 0.01588  0.01167  -0.15379 89  LEU   A C   
688  O O   . LEU   A 89  ? 0.57880 0.70085 0.54433 0.01531  0.00596  -0.14511 89  LEU   A O   
689  C CB  . LEU   A 89  ? 0.51409 0.62032 0.49804 0.02467  0.01288  -0.13967 89  LEU   A CB  
690  C CG  . LEU   A 89  ? 0.53986 0.63398 0.53529 0.02990  0.01249  -0.13297 89  LEU   A CG  
691  C CD1 . LEU   A 89  ? 0.48109 0.57818 0.47229 0.03126  0.00976  -0.12106 89  LEU   A CD1 
692  C CD2 . LEU   A 89  ? 0.58314 0.67426 0.58944 0.03258  0.01894  -0.14048 89  LEU   A CD2 
693  N N   . LYS   A 90  ? 0.54865 0.67428 0.51758 0.01190  0.01637  -0.16614 90  LYS   A N   
694  C CA  . LYS   A 90  ? 0.57914 0.72099 0.53483 0.00615  0.01459  -0.16991 90  LYS   A CA  
695  C C   . LYS   A 90  ? 0.63527 0.79024 0.58100 0.00634  0.01549  -0.16436 90  LYS   A C   
696  O O   . LYS   A 90  ? 0.67657 0.83254 0.62446 0.00753  0.02138  -0.16832 90  LYS   A O   
697  C CB  . LYS   A 90  ? 0.61455 0.75917 0.57006 0.00083  0.01942  -0.18657 90  LYS   A CB  
698  C CG  . LYS   A 90  ? 0.63935 0.80248 0.58083 -0.00594 0.01709  -0.19127 90  LYS   A CG  
699  C CD  . LYS   A 90  ? 0.64525 0.80730 0.58810 -0.01114 0.01473  -0.19919 90  LYS   A CD  
700  C CE  . LYS   A 90  ? 0.71826 0.88215 0.66072 -0.01707 0.02137  -0.21744 90  LYS   A CE  
701  N NZ  . LYS   A 90  ? 0.75737 0.92298 0.69952 -0.02378 0.01893  -0.22575 90  LYS   A NZ  
702  N N   . VAL   A 91  ? 0.62524 0.79021 0.56056 0.00538  0.01003  -0.15484 91  VAL   A N   
703  C CA  . VAL   A 91  ? 0.67017 0.84698 0.59530 0.00552  0.01060  -0.14774 91  VAL   A CA  
704  C C   . VAL   A 91  ? 0.68902 0.88473 0.60028 -0.00002 0.00959  -0.15234 91  VAL   A C   
705  O O   . VAL   A 91  ? 0.69330 0.89377 0.60214 -0.00354 0.00612  -0.15700 91  VAL   A O   
706  C CB  . VAL   A 91  ? 0.63262 0.80515 0.55660 0.00959  0.00582  -0.13127 91  VAL   A CB  
707  C CG1 . VAL   A 91  ? 0.61963 0.77739 0.55506 0.01425  0.00790  -0.12702 91  VAL   A CG1 
708  C CG2 . VAL   A 91  ? 0.61618 0.78642 0.53987 0.00973  -0.00079 -0.12619 91  VAL   A CG2 
709  N N   . ASP   A 92  ? 0.69165 0.89926 0.59358 -0.00109 0.01266  -0.15077 92  ASP   A N   
710  C CA  . ASP   A 92  ? 0.69513 0.92250 0.58261 -0.00644 0.01225  -0.15495 92  ASP   A CA  
711  C C   . ASP   A 92  ? 0.70603 0.94357 0.58411 -0.00643 0.00479  -0.14292 92  ASP   A C   
712  O O   . ASP   A 92  ? 0.73977 0.99563 0.60527 -0.01060 0.00340  -0.14456 92  ASP   A O   
713  C CB  . ASP   A 92  ? 0.74038 0.97717 0.62070 -0.00736 0.01835  -0.15615 92  ASP   A CB  
714  C CG  . ASP   A 92  ? 0.81324 1.04732 0.69240 -0.00299 0.01786  -0.14064 92  ASP   A CG  
715  O OD1 . ASP   A 92  ? 0.74185 0.96281 0.62879 0.00134  0.01424  -0.13104 92  ASP   A OD1 
716  O OD2 . ASP   A 92  ? 0.77452 1.01946 0.64472 -0.00431 0.02145  -0.13833 92  ASP   A OD2 
717  N N   . THR   A 93  ? 0.71378 0.94064 0.59748 -0.00176 0.00015  -0.13092 93  THR   A N   
718  C CA  . THR   A 93  ? 0.69976 0.93493 0.57613 -0.00059 -0.00642 -0.11868 93  THR   A CA  
719  C C   . THR   A 93  ? 0.71270 0.93645 0.59856 0.00172  -0.01123 -0.11585 93  THR   A C   
720  O O   . THR   A 93  ? 0.69543 0.90140 0.59227 0.00515  -0.01004 -0.11457 93  THR   A O   
721  C CB  . THR   A 93  ? 0.70393 0.93834 0.57520 0.00349  -0.00619 -0.10346 93  THR   A CB  
722  O OG1 . THR   A 93  ? 0.78931 1.03474 0.65171 0.00102  -0.00124 -0.10595 93  THR   A OG1 
723  C CG2 . THR   A 93  ? 0.70278 0.94539 0.56691 0.00547  -0.01241 -0.09038 93  THR   A CG2 
724  N N   . ALA   A 94  ? 0.68980 0.92484 0.57145 -0.00029 -0.01665 -0.11481 94  ALA   A N   
725  C CA  . ALA   A 94  ? 0.66990 0.89650 0.55963 0.00190  -0.02135 -0.11077 94  ALA   A CA  
726  C C   . ALA   A 94  ? 0.65699 0.88174 0.54436 0.00761  -0.02500 -0.09348 94  ALA   A C   
727  O O   . ALA   A 94  ? 0.70138 0.93924 0.57835 0.00833  -0.02631 -0.08514 94  ALA   A O   
728  C CB  . ALA   A 94  ? 0.67616 0.91652 0.56397 -0.00337 -0.02520 -0.11859 94  ALA   A CB  
729  N N   . ASN   A 95  ? 0.62340 0.83141 0.52027 0.01170  -0.02624 -0.08808 95  ASN   A N   
730  C CA  . ASN   A 95  ? 0.63509 0.83775 0.53095 0.01729  -0.02865 -0.07259 95  ASN   A CA  
731  C C   . ASN   A 95  ? 0.63852 0.85716 0.52832 0.01787  -0.03399 -0.06549 95  ASN   A C   
732  O O   . ASN   A 95  ? 0.63621 0.85860 0.53053 0.01642  -0.03752 -0.06923 95  ASN   A O   
733  C CB  . ASN   A 95  ? 0.60786 0.79028 0.51497 0.02068  -0.02889 -0.07023 95  ASN   A CB  
734  C CG  . ASN   A 95  ? 0.60049 0.77513 0.50668 0.02619  -0.03033 -0.05536 95  ASN   A CG  
735  O OD1 . ASN   A 95  ? 0.60113 0.78288 0.49897 0.02794  -0.03026 -0.04624 95  ASN   A OD1 
736  N ND2 . ASN   A 95  ? 0.60873 0.76818 0.52329 0.02888  -0.03124 -0.05285 95  ASN   A ND2 
737  N N   . PRO   A 96  ? 0.64305 0.87190 0.52306 0.02005  -0.03461 -0.05478 96  PRO   A N   
738  C CA  . PRO   A 96  ? 0.63538 0.88034 0.51028 0.02171  -0.03986 -0.04629 96  PRO   A CA  
739  C C   . PRO   A 96  ? 0.65438 0.88923 0.53653 0.02726  -0.04271 -0.03655 96  PRO   A C   
740  O O   . PRO   A 96  ? 0.65329 0.90135 0.53407 0.02892  -0.04726 -0.03061 96  PRO   A O   
741  C CB  . PRO   A 96  ? 0.62794 0.88263 0.49104 0.02346  -0.03857 -0.03611 96  PRO   A CB  
742  C CG  . PRO   A 96  ? 0.69257 0.92920 0.55758 0.02494  -0.03298 -0.03449 96  PRO   A CG  
743  C CD  . PRO   A 96  ? 0.63026 0.85637 0.50399 0.02131  -0.03035 -0.04918 96  PRO   A CD  
744  N N   . LYS   A 97  ? 0.65277 0.86572 0.54253 0.03015  -0.04013 -0.03474 97  LYS   A N   
745  C CA  . LYS   A 97  ? 0.62508 0.82673 0.52192 0.03494  -0.04204 -0.02712 97  LYS   A CA  
746  C C   . LYS   A 97  ? 0.59552 0.78953 0.50270 0.03259  -0.04308 -0.03691 97  LYS   A C   
747  O O   . LYS   A 97  ? 0.58082 0.76228 0.49469 0.03605  -0.04367 -0.03228 97  LYS   A O   
748  C CB  . LYS   A 97  ? 0.59024 0.77274 0.48794 0.03930  -0.03852 -0.01822 97  LYS   A CB  
749  C CG  . LYS   A 97  ? 0.58745 0.77486 0.47586 0.04253  -0.03730 -0.00579 97  LYS   A CG  
750  C CD  . LYS   A 97  ? 0.64631 0.81675 0.53435 0.04339  -0.03236 -0.00231 97  LYS   A CD  
751  C CE  . LYS   A 97  ? 0.67259 0.83884 0.55531 0.04840  -0.03100 0.01292  97  LYS   A CE  
752  N NZ  . LYS   A 97  ? 0.68939 0.83473 0.57494 0.04935  -0.02674 0.01622  97  LYS   A NZ  
753  N N   . THR   A 98  ? 0.61145 0.81219 0.51981 0.02667  -0.04284 -0.05031 98  THR   A N   
754  C CA  . THR   A 98  ? 0.59712 0.78999 0.51524 0.02393  -0.04318 -0.05991 98  THR   A CA  
755  C C   . THR   A 98  ? 0.58570 0.78531 0.50780 0.02517  -0.04766 -0.05574 98  THR   A C   
756  O O   . THR   A 98  ? 0.58267 0.80248 0.50017 0.02359  -0.05121 -0.05473 98  THR   A O   
757  C CB  . THR   A 98  ? 0.62510 0.82573 0.54278 0.01700  -0.04173 -0.07505 98  THR   A CB  
758  O OG1 . THR   A 98  ? 0.65027 0.84235 0.56676 0.01641  -0.03682 -0.07960 98  THR   A OG1 
759  C CG2 . THR   A 98  ? 0.62599 0.81949 0.55365 0.01384  -0.04212 -0.08429 98  THR   A CG2 
760  N N   . PRO   A 99  ? 0.58234 0.76709 0.51283 0.02788  -0.04766 -0.05313 99  PRO   A N   
761  C CA  . PRO   A 99  ? 0.56057 0.75188 0.49595 0.02889  -0.05136 -0.04983 99  PRO   A CA  
762  C C   . PRO   A 99  ? 0.57696 0.77182 0.51876 0.02243  -0.05215 -0.06257 99  PRO   A C   
763  O O   . PRO   A 99  ? 0.57880 0.76803 0.52192 0.01784  -0.04939 -0.07367 99  PRO   A O   
764  C CB  . PRO   A 99  ? 0.57371 0.74530 0.51442 0.03450  -0.04988 -0.04170 99  PRO   A CB  
765  C CG  . PRO   A 99  ? 0.56746 0.72125 0.51023 0.03322  -0.04588 -0.04749 99  PRO   A CG  
766  C CD  . PRO   A 99  ? 0.56899 0.73102 0.50474 0.03018  -0.04422 -0.05263 99  PRO   A CD  
767  N N   . LYS   A 100 ? 0.59834 0.80277 0.54462 0.02214  -0.05561 -0.06071 100 LYS   A N   
768  C CA  . LYS   A 100 ? 0.59711 0.80109 0.55135 0.01633  -0.05589 -0.07130 100 LYS   A CA  
769  C C   . LYS   A 100 ? 0.59321 0.77256 0.55506 0.01810  -0.05250 -0.07215 100 LYS   A C   
770  O O   . LYS   A 100 ? 0.59063 0.75973 0.55479 0.02387  -0.05238 -0.06245 100 LYS   A O   
771  C CB  . LYS   A 100 ? 0.64107 0.86182 0.59898 0.01598  -0.06033 -0.06771 100 LYS   A CB  
772  C CG  . LYS   A 100 ? 0.61491 0.83476 0.58193 0.00982  -0.06044 -0.07748 100 LYS   A CG  
773  C CD  . LYS   A 100 ? 0.66658 0.90613 0.63744 0.00943  -0.06502 -0.07337 100 LYS   A CD  
774  C CE  . LYS   A 100 ? 0.67087 0.91080 0.65087 0.00218  -0.06490 -0.08354 100 LYS   A CE  
775  N NZ  . LYS   A 100 ? 0.72257 0.98436 0.70702 0.00125  -0.06950 -0.07989 100 LYS   A NZ  
776  N N   . TYR   A 101 ? 0.55014 0.71979 0.51563 0.01334  -0.04948 -0.08348 101 TYR   A N   
777  C CA  . TYR   A 101 ? 0.60185 0.74865 0.57378 0.01539  -0.04622 -0.08366 101 TYR   A CA  
778  C C   . TYR   A 101 ? 0.56903 0.71013 0.54895 0.00960  -0.04461 -0.09461 101 TYR   A C   
779  O O   . TYR   A 101 ? 0.57117 0.72446 0.55111 0.00318  -0.04519 -0.10408 101 TYR   A O   
780  C CB  . TYR   A 101 ? 0.55717 0.69258 0.52568 0.01773  -0.04284 -0.08367 101 TYR   A CB  
781  C CG  . TYR   A 101 ? 0.57527 0.71534 0.54149 0.01279  -0.04036 -0.09525 101 TYR   A CG  
782  C CD1 . TYR   A 101 ? 0.58014 0.70829 0.55305 0.00968  -0.03682 -0.10524 101 TYR   A CD1 
783  C CD2 . TYR   A 101 ? 0.57456 0.73061 0.53181 0.01146  -0.04110 -0.09596 101 TYR   A CD2 
784  C CE1 . TYR   A 101 ? 0.54632 0.67785 0.51749 0.00547  -0.03372 -0.11631 101 TYR   A CE1 
785  C CE2 . TYR   A 101 ? 0.60303 0.76345 0.55768 0.00680  -0.03825 -0.10713 101 TYR   A CE2 
786  C CZ  . TYR   A 101 ? 0.59102 0.73886 0.55287 0.00388  -0.03437 -0.11761 101 TYR   A CZ  
787  O OH  . TYR   A 101 ? 0.64870 0.80009 0.60833 -0.00046 -0.03075 -0.12921 101 TYR   A OH  
788  N N   . LYS   A 102 ? 0.56976 0.69184 0.55623 0.01171  -0.04239 -0.09306 102 LYS   A N   
789  C CA  . LYS   A 102 ? 0.60035 0.71248 0.59496 0.00723  -0.03994 -0.10177 102 LYS   A CA  
790  C C   . LYS   A 102 ? 0.60222 0.69302 0.60042 0.01080  -0.03647 -0.10028 102 LYS   A C   
791  O O   . LYS   A 102 ? 0.61239 0.69613 0.60804 0.01649  -0.03678 -0.09123 102 LYS   A O   
792  C CB  . LYS   A 102 ? 0.64819 0.76297 0.64872 0.00565  -0.04186 -0.09954 102 LYS   A CB  
793  C CG  . LYS   A 102 ? 0.71464 0.82210 0.72328 -0.00054 -0.03929 -0.10930 102 LYS   A CG  
794  C CD  . LYS   A 102 ? 0.78565 0.90889 0.79357 -0.00863 -0.03979 -0.12081 102 LYS   A CD  
795  C CE  . LYS   A 102 ? 0.89429 1.02024 0.90993 -0.01475 -0.03995 -0.12550 102 LYS   A CE  
796  N NZ  . LYS   A 102 ? 0.91352 1.05306 0.92889 -0.02399 -0.03982 -0.13853 102 LYS   A NZ  
797  N N   . PHE   A 103 ? 0.60692 0.68772 0.61118 0.00731  -0.03303 -0.10924 103 PHE   A N   
798  C CA  . PHE   A 103 ? 0.60506 0.66650 0.61418 0.01061  -0.02981 -0.10799 103 PHE   A CA  
799  C C   . PHE   A 103 ? 0.62907 0.67951 0.64595 0.00935  -0.02901 -0.10742 103 PHE   A C   
800  O O   . PHE   A 103 ? 0.63066 0.67960 0.65276 0.00395  -0.02689 -0.11613 103 PHE   A O   
801  C CB  . PHE   A 103 ? 0.59517 0.65244 0.60581 0.00878  -0.02569 -0.11767 103 PHE   A CB  
802  C CG  . PHE   A 103 ? 0.58200 0.64532 0.58590 0.01157  -0.02549 -0.11618 103 PHE   A CG  
803  C CD1 . PHE   A 103 ? 0.59279 0.66286 0.58987 0.01538  -0.02872 -0.10622 103 PHE   A CD1 
804  C CD2 . PHE   A 103 ? 0.57850 0.64028 0.58313 0.01035  -0.02149 -0.12474 103 PHE   A CD2 
805  C CE1 . PHE   A 103 ? 0.57409 0.64938 0.56500 0.01746  -0.02813 -0.10455 103 PHE   A CE1 
806  C CE2 . PHE   A 103 ? 0.57060 0.63859 0.56920 0.01262  -0.02092 -0.12332 103 PHE   A CE2 
807  C CZ  . PHE   A 103 ? 0.58661 0.66141 0.57824 0.01594  -0.02432 -0.11307 103 PHE   A CZ  
808  N N   . VAL   A 104 ? 0.59695 0.63954 0.61429 0.01390  -0.03031 -0.09743 104 VAL   A N   
809  C CA  . VAL   A 104 ? 0.60158 0.63424 0.62527 0.01308  -0.02953 -0.09542 104 VAL   A CA  
810  C C   . VAL   A 104 ? 0.57708 0.59194 0.60358 0.01738  -0.02748 -0.09084 104 VAL   A C   
811  O O   . VAL   A 104 ? 0.60048 0.61254 0.62312 0.02189  -0.02799 -0.08589 104 VAL   A O   
812  C CB  . VAL   A 104 ? 0.59077 0.63098 0.61281 0.01424  -0.03264 -0.08780 104 VAL   A CB  
813  C CG1 . VAL   A 104 ? 0.53088 0.59151 0.54897 0.01172  -0.03553 -0.08996 104 VAL   A CG1 
814  C CG2 . VAL   A 104 ? 0.57762 0.61126 0.59538 0.02077  -0.03371 -0.07705 104 VAL   A CG2 
815  N N   . ARG   A 105 ? 0.53200 0.53536 0.56539 0.01563  -0.02510 -0.09247 105 ARG   A N   
816  C CA  . ARG   A 105 ? 0.56334 0.55069 0.59978 0.01958  -0.02357 -0.08690 105 ARG   A CA  
817  C C   . ARG   A 105 ? 0.58739 0.57139 0.62397 0.02025  -0.02485 -0.07940 105 ARG   A C   
818  O O   . ARG   A 105 ? 0.62645 0.60847 0.66789 0.01640  -0.02350 -0.08174 105 ARG   A O   
819  C CB  . ARG   A 105 ? 0.57218 0.54789 0.61633 0.01777  -0.01933 -0.09334 105 ARG   A CB  
820  C CG  . ARG   A 105 ? 0.54631 0.50624 0.59459 0.02137  -0.01792 -0.08666 105 ARG   A CG  
821  C CD  . ARG   A 105 ? 0.53481 0.48778 0.58512 0.02582  -0.01630 -0.08633 105 ARG   A CD  
822  N NE  . ARG   A 105 ? 0.56604 0.50407 0.62278 0.02818  -0.01391 -0.08255 105 ARG   A NE  
823  C CZ  . ARG   A 105 ? 0.57535 0.50666 0.63504 0.03307  -0.01292 -0.07954 105 ARG   A CZ  
824  N NH1 . ARG   A 105 ? 0.57660 0.51436 0.63377 0.03577  -0.01380 -0.08038 105 ARG   A NH1 
825  N NH2 . ARG   A 105 ? 0.60502 0.52356 0.67059 0.03534  -0.01096 -0.07514 105 ARG   A NH2 
826  N N   . ILE   A 106 ? 0.56188 0.54530 0.59309 0.02475  -0.02700 -0.07079 106 ILE   A N   
827  C CA  . ILE   A 106 ? 0.63583 0.61721 0.66598 0.02568  -0.02790 -0.06382 106 ILE   A CA  
828  C C   . ILE   A 106 ? 0.63679 0.60338 0.67119 0.02618  -0.02579 -0.06088 106 ILE   A C   
829  O O   . ILE   A 106 ? 0.60879 0.56660 0.64638 0.02721  -0.02415 -0.06248 106 ILE   A O   
830  C CB  . ILE   A 106 ? 0.59866 0.58305 0.62130 0.03007  -0.03016 -0.05625 106 ILE   A CB  
831  C CG1 . ILE   A 106 ? 0.58177 0.56004 0.60158 0.03339  -0.03023 -0.05430 106 ILE   A CG1 
832  C CG2 . ILE   A 106 ? 0.55559 0.55542 0.57450 0.02960  -0.03216 -0.05722 106 ILE   A CG2 
833  C CD1 . ILE   A 106 ? 0.57556 0.54128 0.59525 0.03588  -0.02980 -0.04825 106 ILE   A CD1 
834  N N   . GLN   A 107 ? 0.64742 0.61171 0.68204 0.02574  -0.02564 -0.05617 107 GLN   A N   
835  C CA  . GLN   A 107 ? 0.62591 0.57774 0.66339 0.02587  -0.02371 -0.05208 107 GLN   A CA  
836  C C   . GLN   A 107 ? 0.61111 0.55741 0.64240 0.03030  -0.02498 -0.04355 107 GLN   A C   
837  O O   . GLN   A 107 ? 0.60440 0.55679 0.62962 0.03255  -0.02691 -0.04073 107 GLN   A O   
838  C CB  . GLN   A 107 ? 0.64593 0.60025 0.68717 0.02185  -0.02234 -0.05264 107 GLN   A CB  
839  C CG  . GLN   A 107 ? 0.72608 0.67992 0.77504 0.01628  -0.01985 -0.06073 107 GLN   A CG  
840  C CD  . GLN   A 107 ? 0.79971 0.73767 0.85364 0.01609  -0.01657 -0.06015 107 GLN   A CD  
841  O OE1 . GLN   A 107 ? 0.84094 0.77194 0.89766 0.01439  -0.01447 -0.05680 107 GLN   A OE1 
842  N NE2 . GLN   A 107 ? 0.80274 0.73513 0.85810 0.01808  -0.01583 -0.06300 107 GLN   A NE2 
843  N N   . PRO   A 108 ? 0.61696 0.55175 0.64935 0.03148  -0.02381 -0.03926 108 PRO   A N   
844  C CA  . PRO   A 108 ? 0.57884 0.50926 0.60463 0.03467  -0.02503 -0.03162 108 PRO   A CA  
845  C C   . PRO   A 108 ? 0.58909 0.52349 0.61089 0.03417  -0.02490 -0.02839 108 PRO   A C   
846  O O   . PRO   A 108 ? 0.64621 0.58296 0.67190 0.03130  -0.02328 -0.02989 108 PRO   A O   
847  C CB  . PRO   A 108 ? 0.56197 0.48077 0.59075 0.03517  -0.02358 -0.02797 108 PRO   A CB  
848  C CG  . PRO   A 108 ? 0.61873 0.53483 0.65589 0.03171  -0.02076 -0.03299 108 PRO   A CG  
849  C CD  . PRO   A 108 ? 0.64140 0.56653 0.68084 0.03006  -0.02119 -0.04101 108 PRO   A CD  
850  N N   . GLY   A 109 ? 0.56357 0.49879 0.57794 0.03689  -0.02624 -0.02416 109 GLY   A N   
851  C CA  . GLY   A 109 ? 0.52488 0.46344 0.53518 0.03740  -0.02561 -0.02105 109 GLY   A CA  
852  C C   . GLY   A 109 ? 0.53094 0.48044 0.53990 0.03839  -0.02663 -0.02288 109 GLY   A C   
853  O O   . GLY   A 109 ? 0.54139 0.49265 0.54572 0.04041  -0.02615 -0.01931 109 GLY   A O   
854  N N   . GLN   A 110 ? 0.56747 0.52431 0.58018 0.03713  -0.02774 -0.02817 110 GLN   A N   
855  C CA  . GLN   A 110 ? 0.55460 0.52306 0.56560 0.03817  -0.02905 -0.02927 110 GLN   A CA  
856  C C   . GLN   A 110 ? 0.54903 0.51609 0.55324 0.04131  -0.03020 -0.02667 110 GLN   A C   
857  O O   . GLN   A 110 ? 0.54679 0.50634 0.54918 0.04185  -0.03050 -0.02614 110 GLN   A O   
858  C CB  . GLN   A 110 ? 0.53654 0.51412 0.55289 0.03505  -0.02981 -0.03626 110 GLN   A CB  
859  C CG  . GLN   A 110 ? 0.56568 0.54566 0.58916 0.03087  -0.02847 -0.03969 110 GLN   A CG  
860  C CD  . GLN   A 110 ? 0.59803 0.58818 0.62599 0.02695  -0.02918 -0.04751 110 GLN   A CD  
861  O OE1 . GLN   A 110 ? 0.63065 0.61828 0.65934 0.02601  -0.02912 -0.05222 110 GLN   A OE1 
862  N NE2 . GLN   A 110 ? 0.60431 0.60683 0.63543 0.02450  -0.02971 -0.04918 110 GLN   A NE2 
863  N N   . THR   A 111 ? 0.54838 0.52326 0.54927 0.04338  -0.03073 -0.02471 111 THR   A N   
864  C CA  . THR   A 111 ? 0.57025 0.54387 0.56462 0.04605  -0.03123 -0.02184 111 THR   A CA  
865  C C   . THR   A 111 ? 0.56778 0.55209 0.56210 0.04591  -0.03275 -0.02485 111 THR   A C   
866  O O   . THR   A 111 ? 0.56044 0.55454 0.55908 0.04388  -0.03358 -0.02902 111 THR   A O   
867  C CB  . THR   A 111 ? 0.56397 0.53595 0.55357 0.04916  -0.02979 -0.01607 111 THR   A CB  
868  O OG1 . THR   A 111 ? 0.52277 0.50517 0.51584 0.04994  -0.02964 -0.01557 111 THR   A OG1 
869  C CG2 . THR   A 111 ? 0.60016 0.56051 0.58745 0.04913  -0.02799 -0.01327 111 THR   A CG2 
870  N N   . PHE   A 112 ? 0.58013 0.56280 0.56910 0.04761  -0.03296 -0.02281 112 PHE   A N   
871  C CA  . PHE   A 112 ? 0.57154 0.56409 0.55875 0.04781  -0.03401 -0.02442 112 PHE   A CA  
872  C C   . PHE   A 112 ? 0.55517 0.54344 0.53565 0.05007  -0.03332 -0.01982 112 PHE   A C   
873  O O   . PHE   A 112 ? 0.54153 0.51906 0.51929 0.05056  -0.03229 -0.01707 112 PHE   A O   
874  C CB  . PHE   A 112 ? 0.57200 0.56754 0.56300 0.04494  -0.03467 -0.03133 112 PHE   A CB  
875  C CG  . PHE   A 112 ? 0.57168 0.55673 0.56370 0.04455  -0.03409 -0.03223 112 PHE   A CG  
876  C CD1 . PHE   A 112 ? 0.55185 0.53532 0.54028 0.04542  -0.03402 -0.03112 112 PHE   A CD1 
877  C CD2 . PHE   A 112 ? 0.55816 0.53577 0.55517 0.04332  -0.03356 -0.03377 112 PHE   A CD2 
878  C CE1 . PHE   A 112 ? 0.55414 0.53010 0.54442 0.04523  -0.03382 -0.03160 112 PHE   A CE1 
879  C CE2 . PHE   A 112 ? 0.55032 0.51966 0.54872 0.04356  -0.03332 -0.03365 112 PHE   A CE2 
880  C CZ  . PHE   A 112 ? 0.56170 0.53091 0.55700 0.04460  -0.03364 -0.03263 112 PHE   A CZ  
881  N N   . SER   A 113 ? 0.56369 0.56080 0.54121 0.05100  -0.03379 -0.01902 113 SER   A N   
882  C CA  . SER   A 113 ? 0.53675 0.53032 0.50804 0.05262  -0.03271 -0.01477 113 SER   A CA  
883  C C   . SER   A 113 ? 0.57441 0.56837 0.54550 0.05050  -0.03299 -0.01858 113 SER   A C   
884  O O   . SER   A 113 ? 0.57706 0.57894 0.55134 0.04871  -0.03395 -0.02401 113 SER   A O   
885  C CB  . SER   A 113 ? 0.54984 0.55258 0.51773 0.05532  -0.03263 -0.01035 113 SER   A CB  
886  O OG  . SER   A 113 ? 0.56098 0.56410 0.53002 0.05802  -0.03204 -0.00634 113 SER   A OG  
887  N N   . VAL   A 114 ? 0.56016 0.54586 0.52773 0.05046  -0.03186 -0.01608 114 VAL   A N   
888  C CA  . VAL   A 114 ? 0.53314 0.51944 0.50105 0.04867  -0.03180 -0.01894 114 VAL   A CA  
889  C C   . VAL   A 114 ? 0.52996 0.51857 0.49184 0.04921  -0.03045 -0.01515 114 VAL   A C   
890  O O   . VAL   A 114 ? 0.54991 0.53122 0.50722 0.05018  -0.02893 -0.00995 114 VAL   A O   
891  C CB  . VAL   A 114 ? 0.57147 0.54796 0.54110 0.04750  -0.03183 -0.01923 114 VAL   A CB  
892  C CG1 . VAL   A 114 ? 0.50954 0.48746 0.47910 0.04609  -0.03143 -0.02054 114 VAL   A CG1 
893  C CG2 . VAL   A 114 ? 0.54963 0.52454 0.52578 0.04695  -0.03291 -0.02302 114 VAL   A CG2 
894  N N   . LEU   A 115 ? 0.50392 0.50217 0.46557 0.04838  -0.03052 -0.01783 115 LEU   A N   
895  C CA  . LEU   A 115 ? 0.54765 0.54851 0.50373 0.04837  -0.02891 -0.01437 115 LEU   A CA  
896  C C   . LEU   A 115 ? 0.49347 0.49187 0.45117 0.04599  -0.02807 -0.01701 115 LEU   A C   
897  O O   . LEU   A 115 ? 0.50401 0.50929 0.46522 0.04477  -0.02827 -0.02239 115 LEU   A O   
898  C CB  . LEU   A 115 ? 0.49357 0.50795 0.44749 0.04879  -0.02934 -0.01512 115 LEU   A CB  
899  C CG  . LEU   A 115 ? 0.53956 0.55725 0.48725 0.04875  -0.02738 -0.01090 115 LEU   A CG  
900  C CD1 . LEU   A 115 ? 0.56437 0.57342 0.50716 0.05104  -0.02560 -0.00251 115 LEU   A CD1 
901  C CD2 . LEU   A 115 ? 0.55713 0.58990 0.50220 0.04877  -0.02810 -0.01215 115 LEU   A CD2 
902  N N   . ALA   A 116 ? 0.47467 0.46366 0.43011 0.04519  -0.02693 -0.01350 116 ALA   A N   
903  C CA  . ALA   A 116 ? 0.49401 0.48171 0.45150 0.04270  -0.02638 -0.01536 116 ALA   A CA  
904  C C   . ALA   A 116 ? 0.50473 0.49915 0.45886 0.04151  -0.02433 -0.01439 116 ALA   A C   
905  O O   . ALA   A 116 ? 0.55001 0.54223 0.49794 0.04177  -0.02247 -0.00911 116 ALA   A O   
906  C CB  . ALA   A 116 ? 0.52107 0.49764 0.47672 0.04132  -0.02601 -0.01231 116 ALA   A CB  
907  N N   . CYS   A 117 ? 0.50645 0.50870 0.46477 0.04038  -0.02417 -0.01926 117 CYS   A N   
908  C CA  . CYS   A 117 ? 0.52262 0.53290 0.47799 0.03908  -0.02193 -0.01907 117 CYS   A CA  
909  C C   . CYS   A 117 ? 0.50710 0.51863 0.46686 0.03667  -0.02081 -0.02132 117 CYS   A C   
910  O O   . CYS   A 117 ? 0.49667 0.50627 0.46325 0.03674  -0.02223 -0.02452 117 CYS   A O   
911  C CB  . CYS   A 117 ? 0.53914 0.56096 0.49483 0.03990  -0.02212 -0.02356 117 CYS   A CB  
912  S SG  . CYS   A 117 ? 0.58492 0.61028 0.53503 0.04228  -0.02351 -0.02017 117 CYS   A SG  
913  N N   . TYR   A 118 ? 0.52287 0.53826 0.47894 0.03465  -0.01814 -0.01908 118 TYR   A N   
914  C CA  . TYR   A 118 ? 0.55857 0.57809 0.51914 0.03210  -0.01660 -0.02122 118 TYR   A CA  
915  C C   . TYR   A 118 ? 0.54694 0.57612 0.50382 0.03086  -0.01344 -0.02119 118 TYR   A C   
916  O O   . TYR   A 118 ? 0.55134 0.57951 0.50030 0.03051  -0.01185 -0.01596 118 TYR   A O   
917  C CB  . TYR   A 118 ? 0.52955 0.54082 0.48942 0.02917  -0.01630 -0.01736 118 TYR   A CB  
918  C CG  . TYR   A 118 ? 0.53747 0.53959 0.49957 0.02996  -0.01925 -0.01712 118 TYR   A CG  
919  C CD1 . TYR   A 118 ? 0.51820 0.52181 0.48831 0.02997  -0.02137 -0.02035 118 TYR   A CD1 
920  C CD2 . TYR   A 118 ? 0.53796 0.53041 0.49421 0.03098  -0.01967 -0.01327 118 TYR   A CD2 
921  C CE1 . TYR   A 118 ? 0.54286 0.53874 0.51415 0.03056  -0.02404 -0.01960 118 TYR   A CE1 
922  C CE2 . TYR   A 118 ? 0.52950 0.51404 0.48713 0.03146  -0.02195 -0.01321 118 TYR   A CE2 
923  C CZ  . TYR   A 118 ? 0.52792 0.51429 0.49261 0.03104  -0.02424 -0.01630 118 TYR   A CZ  
924  O OH  . TYR   A 118 ? 0.59340 0.57248 0.55865 0.03138  -0.02649 -0.01572 118 TYR   A OH  
925  N N   . ASN   A 119 ? 0.54386 0.58235 0.50651 0.03048  -0.01222 -0.02676 119 ASN   A N   
926  C CA  . ASN   A 119 ? 0.54873 0.59787 0.50813 0.02917  -0.00885 -0.02785 119 ASN   A CA  
927  C C   . ASN   A 119 ? 0.56315 0.61687 0.51501 0.03073  -0.00909 -0.02731 119 ASN   A C   
928  O O   . ASN   A 119 ? 0.56693 0.62590 0.51140 0.02962  -0.00677 -0.02371 119 ASN   A O   
929  C CB  . ASN   A 119 ? 0.52708 0.57541 0.48270 0.02563  -0.00585 -0.02244 119 ASN   A CB  
930  C CG  . ASN   A 119 ? 0.60916 0.65773 0.57301 0.02326  -0.00542 -0.02407 119 ASN   A CG  
931  O OD1 . ASN   A 119 ? 0.62855 0.66875 0.59491 0.02259  -0.00766 -0.02231 119 ASN   A OD1 
932  N ND2 . ASN   A 119 ? 0.61366 0.67291 0.58179 0.02191  -0.00248 -0.02746 119 ASN   A ND2 
933  N N   . GLY   A 120 ? 0.55449 0.60688 0.50825 0.03313  -0.01196 -0.03059 120 GLY   A N   
934  C CA  . GLY   A 120 ? 0.56888 0.62740 0.51655 0.03430  -0.01289 -0.03071 120 GLY   A CA  
935  C C   . GLY   A 120 ? 0.54685 0.60137 0.48645 0.03540  -0.01364 -0.02200 120 GLY   A C   
936  O O   . GLY   A 120 ? 0.58685 0.64915 0.52060 0.03633  -0.01422 -0.02059 120 GLY   A O   
937  N N   . SER   A 121 ? 0.55905 0.60199 0.49819 0.03536  -0.01350 -0.01614 121 SER   A N   
938  C CA  . SER   A 121 ? 0.58861 0.62592 0.52071 0.03688  -0.01325 -0.00761 121 SER   A CA  
939  C C   . SER   A 121 ? 0.58449 0.60936 0.51909 0.03852  -0.01526 -0.00575 121 SER   A C   
940  O O   . SER   A 121 ? 0.55251 0.57016 0.49212 0.03705  -0.01567 -0.00812 121 SER   A O   
941  C CB  . SER   A 121 ? 0.61785 0.65192 0.54502 0.03462  -0.00943 -0.00148 121 SER   A CB  
942  O OG  . SER   A 121 ? 0.67608 0.72050 0.60329 0.03207  -0.00707 -0.00472 121 SER   A OG  
943  N N   . PRO   A 122 ? 0.63728 0.66039 0.56850 0.04161  -0.01648 -0.00134 122 PRO   A N   
944  C CA  . PRO   A 122 ? 0.59170 0.60383 0.52532 0.04332  -0.01801 -0.00012 122 PRO   A CA  
945  C C   . PRO   A 122 ? 0.59746 0.59591 0.52874 0.04204  -0.01553 0.00469  122 PRO   A C   
946  O O   . PRO   A 122 ? 0.65569 0.65172 0.58179 0.04116  -0.01238 0.00998  122 PRO   A O   
947  C CB  . PRO   A 122 ? 0.60442 0.62085 0.53504 0.04714  -0.01931 0.00394  122 PRO   A CB  
948  C CG  . PRO   A 122 ? 0.60397 0.63577 0.53179 0.04694  -0.01969 0.00258  122 PRO   A CG  
949  C CD  . PRO   A 122 ? 0.61356 0.64656 0.53918 0.04386  -0.01674 0.00238  122 PRO   A CD  
950  N N   . SER   A 123 ? 0.56728 0.55651 0.50215 0.04155  -0.01675 0.00265  123 SER   A N   
951  C CA  . SER   A 123 ? 0.59973 0.57566 0.53223 0.03965  -0.01461 0.00583  123 SER   A CA  
952  C C   . SER   A 123 ? 0.58451 0.55040 0.51603 0.04217  -0.01489 0.00813  123 SER   A C   
953  O O   . SER   A 123 ? 0.63880 0.59297 0.56646 0.04121  -0.01208 0.01169  123 SER   A O   
954  C CB  . SER   A 123 ? 0.61417 0.58862 0.55119 0.03552  -0.01538 0.00115  123 SER   A CB  
955  O OG  . SER   A 123 ? 0.71103 0.67359 0.64518 0.03265  -0.01344 0.00348  123 SER   A OG  
956  N N   . GLY   A 124 ? 0.54301 0.51288 0.47792 0.04501  -0.01769 0.00590  124 GLY   A N   
957  C CA  . GLY   A 124 ? 0.58647 0.54795 0.52096 0.04745  -0.01765 0.00792  124 GLY   A CA  
958  C C   . GLY   A 124 ? 0.55831 0.52665 0.49787 0.04951  -0.02093 0.00435  124 GLY   A C   
959  O O   . GLY   A 124 ? 0.56148 0.53913 0.50514 0.04853  -0.02318 -0.00054 124 GLY   A O   
960  N N   . VAL   A 125 ? 0.52289 0.48607 0.46237 0.05221  -0.02067 0.00661  125 VAL   A N   
961  C CA  . VAL   A 125 ? 0.53792 0.50701 0.48227 0.05392  -0.02327 0.00387  125 VAL   A CA  
962  C C   . VAL   A 125 ? 0.53994 0.49857 0.48486 0.05436  -0.02263 0.00423  125 VAL   A C   
963  O O   . VAL   A 125 ? 0.55344 0.50205 0.49412 0.05528  -0.01966 0.00817  125 VAL   A O   
964  C CB  . VAL   A 125 ? 0.54046 0.52011 0.48454 0.05752  -0.02375 0.00705  125 VAL   A CB  
965  C CG1 . VAL   A 125 ? 0.53728 0.51034 0.47749 0.06136  -0.02073 0.01446  125 VAL   A CG1 
966  C CG2 . VAL   A 125 ? 0.54556 0.53326 0.49537 0.05798  -0.02660 0.00304  125 VAL   A CG2 
967  N N   . TYR   A 126 ? 0.54083 0.50121 0.49074 0.05348  -0.02495 -0.00003 126 TYR   A N   
968  C CA  . TYR   A 126 ? 0.55460 0.50656 0.50502 0.05373  -0.02442 0.00018  126 TYR   A CA  
969  C C   . TYR   A 126 ? 0.53628 0.49440 0.49298 0.05380  -0.02680 -0.00342 126 TYR   A C   
970  O O   . TYR   A 126 ? 0.52625 0.49394 0.48678 0.05316  -0.02874 -0.00681 126 TYR   A O   
971  C CB  . TYR   A 126 ? 0.57822 0.52026 0.52626 0.05046  -0.02399 -0.00094 126 TYR   A CB  
972  C CG  . TYR   A 126 ? 0.56827 0.51450 0.51992 0.04764  -0.02644 -0.00500 126 TYR   A CG  
973  C CD1 . TYR   A 126 ? 0.57325 0.52051 0.53009 0.04692  -0.02867 -0.00822 126 TYR   A CD1 
974  C CD2 . TYR   A 126 ? 0.58878 0.53787 0.53911 0.04595  -0.02610 -0.00525 126 TYR   A CD2 
975  C CE1 . TYR   A 126 ? 0.59941 0.55026 0.56047 0.04523  -0.03045 -0.01144 126 TYR   A CE1 
976  C CE2 . TYR   A 126 ? 0.57810 0.53180 0.53272 0.04393  -0.02793 -0.00887 126 TYR   A CE2 
977  C CZ  . TYR   A 126 ? 0.55962 0.51409 0.51981 0.04390  -0.03009 -0.01188 126 TYR   A CZ  
978  O OH  . TYR   A 126 ? 0.57735 0.53615 0.54269 0.04275  -0.03148 -0.01500 126 TYR   A OH  
979  N N   . GLN   A 127 ? 0.57738 0.52954 0.53488 0.05420  -0.02617 -0.00292 127 GLN   A N   
980  C CA  . GLN   A 127 ? 0.56881 0.52531 0.53216 0.05404  -0.02763 -0.00558 127 GLN   A CA  
981  C C   . GLN   A 127 ? 0.58213 0.53246 0.54745 0.05141  -0.02866 -0.00824 127 GLN   A C   
982  O O   . GLN   A 127 ? 0.60967 0.55105 0.57091 0.05039  -0.02777 -0.00671 127 GLN   A O   
983  C CB  . GLN   A 127 ? 0.57218 0.52787 0.53567 0.05670  -0.02579 -0.00245 127 GLN   A CB  
984  C CG  . GLN   A 127 ? 0.56265 0.52644 0.53285 0.05649  -0.02711 -0.00483 127 GLN   A CG  
985  C CD  . GLN   A 127 ? 0.59296 0.57083 0.56613 0.05742  -0.02877 -0.00566 127 GLN   A CD  
986  O OE1 . GLN   A 127 ? 0.64730 0.63353 0.62598 0.05659  -0.02996 -0.00808 127 GLN   A OE1 
987  N NE2 . GLN   A 127 ? 0.56518 0.54626 0.53446 0.05870  -0.02881 -0.00366 127 GLN   A NE2 
988  N N   . CYS   A 128 ? 0.57033 0.52554 0.54183 0.05020  -0.03040 -0.01212 128 CYS   A N   
989  C CA  . CYS   A 128 ? 0.59155 0.54150 0.56597 0.04837  -0.03132 -0.01394 128 CYS   A CA  
990  C C   . CYS   A 128 ? 0.58180 0.53346 0.56211 0.04779  -0.03145 -0.01597 128 CYS   A C   
991  O O   . CYS   A 128 ? 0.58296 0.54277 0.56691 0.04777  -0.03171 -0.01838 128 CYS   A O   
992  C CB  . CYS   A 128 ? 0.59607 0.54860 0.57314 0.04726  -0.03271 -0.01700 128 CYS   A CB  
993  S SG  . CYS   A 128 ? 0.71201 0.66021 0.68359 0.04645  -0.03271 -0.01469 128 CYS   A SG  
994  N N   . ALA   A 129 ? 0.56504 0.50944 0.54609 0.04690  -0.03125 -0.01494 129 ALA   A N   
995  C CA  . ALA   A 129 ? 0.55818 0.50235 0.54504 0.04578  -0.03094 -0.01656 129 ALA   A CA  
996  C C   . ALA   A 129 ? 0.52516 0.46649 0.51688 0.04475  -0.03192 -0.01880 129 ALA   A C   
997  O O   . ALA   A 129 ? 0.55803 0.49495 0.54763 0.04505  -0.03280 -0.01696 129 ALA   A O   
998  C CB  . ALA   A 129 ? 0.57286 0.51076 0.55700 0.04577  -0.02933 -0.01296 129 ALA   A CB  
999  N N   . MET   A 130 ? 0.53556 0.47970 0.53419 0.04350  -0.03159 -0.02281 130 MET   A N   
1000 C CA  . MET   A 130 ? 0.54021 0.48046 0.54458 0.04305  -0.03165 -0.02493 130 MET   A CA  
1001 C C   . MET   A 130 ? 0.55961 0.49132 0.56480 0.04275  -0.03092 -0.02110 130 MET   A C   
1002 O O   . MET   A 130 ? 0.57112 0.50172 0.57865 0.04124  -0.02945 -0.02121 130 MET   A O   
1003 C CB  . MET   A 130 ? 0.51744 0.46282 0.52852 0.04136  -0.03085 -0.03141 130 MET   A CB  
1004 C CG  . MET   A 130 ? 0.54032 0.47938 0.55869 0.04076  -0.02957 -0.03364 130 MET   A CG  
1005 S SD  . MET   A 130 ? 0.57700 0.51502 0.59791 0.04315  -0.03005 -0.03493 130 MET   A SD  
1006 C CE  . MET   A 130 ? 0.49285 0.44240 0.51155 0.04247  -0.03044 -0.04057 130 MET   A CE  
1007 N N   . ARG   A 131 ? 0.53199 0.45863 0.53512 0.04397  -0.03199 -0.01744 131 ARG   A N   
1008 C CA  . ARG   A 131 ? 0.56070 0.48013 0.56235 0.04383  -0.03168 -0.01255 131 ARG   A CA  
1009 C C   . ARG   A 131 ? 0.56260 0.47767 0.57209 0.04315  -0.03005 -0.01346 131 ARG   A C   
1010 O O   . ARG   A 131 ? 0.56324 0.47982 0.57957 0.04303  -0.02932 -0.01819 131 ARG   A O   
1011 C CB  . ARG   A 131 ? 0.57445 0.49170 0.57265 0.04508  -0.03376 -0.00864 131 ARG   A CB  
1012 C CG  . ARG   A 131 ? 0.57355 0.49331 0.56353 0.04486  -0.03487 -0.00762 131 ARG   A CG  
1013 C CD  . ARG   A 131 ? 0.53954 0.45787 0.52322 0.04391  -0.03319 -0.00646 131 ARG   A CD  
1014 N NE  . ARG   A 131 ? 0.58189 0.49454 0.56289 0.04310  -0.03234 -0.00263 131 ARG   A NE  
1015 C CZ  . ARG   A 131 ? 0.61746 0.52808 0.59355 0.04238  -0.03024 -0.00128 131 ARG   A CZ  
1016 N NH1 . ARG   A 131 ? 0.61460 0.52815 0.58844 0.04288  -0.02884 -0.00296 131 ARG   A NH1 
1017 N NH2 . ARG   A 131 ? 0.60479 0.51060 0.57828 0.04143  -0.02927 0.00220  131 ARG   A NH2 
1018 N N   . PRO   A 132 ? 0.60433 0.51349 0.61267 0.04241  -0.02895 -0.00916 132 PRO   A N   
1019 C CA  . PRO   A 132 ? 0.59107 0.49437 0.60685 0.04168  -0.02692 -0.00907 132 PRO   A CA  
1020 C C   . PRO   A 132 ? 0.60922 0.50910 0.63071 0.04412  -0.02750 -0.00846 132 PRO   A C   
1021 O O   . PRO   A 132 ? 0.62368 0.51905 0.65314 0.04379  -0.02520 -0.01065 132 PRO   A O   
1022 C CB  . PRO   A 132 ? 0.61641 0.51442 0.62765 0.04080  -0.02592 -0.00296 132 PRO   A CB  
1023 C CG  . PRO   A 132 ? 0.60887 0.51136 0.61230 0.04012  -0.02617 -0.00280 132 PRO   A CG  
1024 C CD  . PRO   A 132 ? 0.59541 0.50311 0.59578 0.04172  -0.02861 -0.00497 132 PRO   A CD  
1025 N N   . ASN   A 133 ? 0.60005 0.50199 0.61826 0.04650  -0.03019 -0.00563 133 ASN   A N   
1026 C CA  . ASN   A 133 ? 0.59473 0.49553 0.61936 0.04949  -0.03082 -0.00495 133 ASN   A CA  
1027 C C   . ASN   A 133 ? 0.59196 0.49880 0.62044 0.05019  -0.03083 -0.01160 133 ASN   A C   
1028 O O   . ASN   A 133 ? 0.59094 0.49897 0.62403 0.05302  -0.03151 -0.01127 133 ASN   A O   
1029 C CB  . ASN   A 133 ? 0.67372 0.57529 0.69380 0.05148  -0.03390 0.00197  133 ASN   A CB  
1030 C CG  . ASN   A 133 ? 0.63124 0.53932 0.64276 0.05037  -0.03639 0.00149  133 ASN   A CG  
1031 O OD1 . ASN   A 133 ? 0.62667 0.53884 0.63647 0.04910  -0.03587 -0.00354 133 ASN   A OD1 
1032 N ND2 . ASN   A 133 ? 0.62514 0.53429 0.63114 0.05064  -0.03901 0.00690  133 ASN   A ND2 
1033 N N   . PHE   A 134 ? 0.54271 0.45430 0.56934 0.04781  -0.03007 -0.01725 134 PHE   A N   
1034 C CA  . PHE   A 134 ? 0.55071 0.46863 0.58023 0.04780  -0.02965 -0.02402 134 PHE   A CA  
1035 C C   . PHE   A 134 ? 0.54195 0.46585 0.56774 0.04949  -0.03200 -0.02295 134 PHE   A C   
1036 O O   . PHE   A 134 ? 0.57386 0.50174 0.60377 0.05066  -0.03151 -0.02690 134 PHE   A O   
1037 C CB  . PHE   A 134 ? 0.57193 0.48605 0.61134 0.04859  -0.02690 -0.02845 134 PHE   A CB  
1038 C CG  . PHE   A 134 ? 0.57502 0.48376 0.61848 0.04571  -0.02401 -0.03121 134 PHE   A CG  
1039 C CD1 . PHE   A 134 ? 0.57333 0.48759 0.61613 0.04202  -0.02310 -0.03762 134 PHE   A CD1 
1040 C CD2 . PHE   A 134 ? 0.56518 0.46403 0.61312 0.04642  -0.02221 -0.02700 134 PHE   A CD2 
1041 C CE1 . PHE   A 134 ? 0.58507 0.49552 0.63206 0.03853  -0.02047 -0.04056 134 PHE   A CE1 
1042 C CE2 . PHE   A 134 ? 0.59280 0.48633 0.64471 0.04306  -0.01911 -0.02961 134 PHE   A CE2 
1043 C CZ  . PHE   A 134 ? 0.55793 0.45750 0.60956 0.03881  -0.01825 -0.03676 134 PHE   A CZ  
1044 N N   . THR   A 135 ? 0.55021 0.47472 0.56819 0.04922  -0.03412 -0.01804 135 THR   A N   
1045 C CA  . THR   A 135 ? 0.56495 0.49513 0.57810 0.04947  -0.03597 -0.01750 135 THR   A CA  
1046 C C   . THR   A 135 ? 0.55915 0.49181 0.56433 0.04757  -0.03592 -0.01797 135 THR   A C   
1047 O O   . THR   A 135 ? 0.57892 0.50953 0.58242 0.04645  -0.03483 -0.01796 135 THR   A O   
1048 C CB  . THR   A 135 ? 0.54841 0.47725 0.55914 0.05040  -0.03831 -0.01156 135 THR   A CB  
1049 O OG1 . THR   A 135 ? 0.55337 0.47762 0.55712 0.04890  -0.03874 -0.00732 135 THR   A OG1 
1050 C CG2 . THR   A 135 ? 0.54389 0.47053 0.56328 0.05322  -0.03835 -0.00966 135 THR   A CG2 
1051 N N   . ILE   A 136 ? 0.54646 0.48374 0.54730 0.04735  -0.03679 -0.01818 136 ILE   A N   
1052 C CA  . ILE   A 136 ? 0.57010 0.50857 0.56316 0.04620  -0.03645 -0.01740 136 ILE   A CA  
1053 C C   . ILE   A 136 ? 0.57747 0.51531 0.56451 0.04542  -0.03763 -0.01428 136 ILE   A C   
1054 O O   . ILE   A 136 ? 0.58488 0.52565 0.57451 0.04562  -0.03883 -0.01436 136 ILE   A O   
1055 C CB  . ILE   A 136 ? 0.56792 0.51326 0.56146 0.04614  -0.03549 -0.02155 136 ILE   A CB  
1056 C CG1 . ILE   A 136 ? 0.55754 0.50829 0.55266 0.04644  -0.03582 -0.02367 136 ILE   A CG1 
1057 C CG2 . ILE   A 136 ? 0.56094 0.50798 0.56032 0.04586  -0.03443 -0.02560 136 ILE   A CG2 
1058 C CD1 . ILE   A 136 ? 0.58693 0.54392 0.57785 0.04602  -0.03510 -0.02508 136 ILE   A CD1 
1059 N N   . LYS   A 137 ? 0.57093 0.50504 0.55031 0.04435  -0.03700 -0.01178 137 LYS   A N   
1060 C CA  . LYS   A 137 ? 0.57348 0.50592 0.54611 0.04263  -0.03749 -0.00960 137 LYS   A CA  
1061 C C   . LYS   A 137 ? 0.60937 0.54463 0.57872 0.04239  -0.03607 -0.01083 137 LYS   A C   
1062 O O   . LYS   A 137 ? 0.62636 0.55884 0.59072 0.04262  -0.03416 -0.00982 137 LYS   A O   
1063 C CB  . LYS   A 137 ? 0.57921 0.50479 0.54500 0.04138  -0.03685 -0.00666 137 LYS   A CB  
1064 C CG  . LYS   A 137 ? 0.64069 0.56330 0.60937 0.04203  -0.03728 -0.00507 137 LYS   A CG  
1065 C CD  . LYS   A 137 ? 0.67911 0.59831 0.64266 0.04021  -0.03868 -0.00173 137 LYS   A CD  
1066 C CE  . LYS   A 137 ? 0.71532 0.63137 0.68116 0.04093  -0.03879 0.00079  137 LYS   A CE  
1067 N NZ  . LYS   A 137 ? 0.78118 0.69625 0.74291 0.03945  -0.04096 0.00459  137 LYS   A NZ  
1068 N N   . GLY   A 138 ? 0.59651 0.53756 0.56899 0.04224  -0.03668 -0.01263 138 GLY   A N   
1069 C CA  . GLY   A 138 ? 0.57151 0.51605 0.54127 0.04199  -0.03525 -0.01342 138 GLY   A CA  
1070 C C   . GLY   A 138 ? 0.59266 0.53635 0.55798 0.03936  -0.03509 -0.01205 138 GLY   A C   
1071 O O   . GLY   A 138 ? 0.62727 0.56674 0.58946 0.03727  -0.03594 -0.01039 138 GLY   A O   
1072 N N   . SER   A 139 ? 0.58643 0.53474 0.55121 0.03899  -0.03388 -0.01287 139 SER   A N   
1073 C CA  . SER   A 139 ? 0.57676 0.52477 0.53781 0.03587  -0.03314 -0.01184 139 SER   A CA  
1074 C C   . SER   A 139 ? 0.56749 0.52431 0.53246 0.03600  -0.03262 -0.01381 139 SER   A C   
1075 O O   . SER   A 139 ? 0.58158 0.54031 0.54378 0.03667  -0.03063 -0.01346 139 SER   A O   
1076 C CB  . SER   A 139 ? 0.61529 0.55561 0.56791 0.03475  -0.03039 -0.00930 139 SER   A CB  
1077 O OG  . SER   A 139 ? 0.66479 0.60444 0.61409 0.03115  -0.02906 -0.00871 139 SER   A OG  
1078 N N   . PHE   A 140 ? 0.61402 0.57673 0.58551 0.03561  -0.03426 -0.01556 140 PHE   A N   
1079 C CA  . PHE   A 140 ? 0.59849 0.57030 0.57503 0.03615  -0.03346 -0.01818 140 PHE   A CA  
1080 C C   . PHE   A 140 ? 0.61505 0.59157 0.59414 0.03334  -0.03395 -0.01790 140 PHE   A C   
1081 O O   . PHE   A 140 ? 0.60286 0.57940 0.58509 0.03271  -0.03630 -0.01702 140 PHE   A O   
1082 C CB  . PHE   A 140 ? 0.54806 0.52387 0.53260 0.03941  -0.03426 -0.02156 140 PHE   A CB  
1083 C CG  . PHE   A 140 ? 0.58188 0.55547 0.56492 0.04137  -0.03372 -0.02274 140 PHE   A CG  
1084 C CD1 . PHE   A 140 ? 0.55590 0.53410 0.53612 0.04168  -0.03202 -0.02413 140 PHE   A CD1 
1085 C CD2 . PHE   A 140 ? 0.57346 0.54147 0.55799 0.04266  -0.03495 -0.02225 140 PHE   A CD2 
1086 C CE1 . PHE   A 140 ? 0.54673 0.52500 0.52606 0.04312  -0.03196 -0.02524 140 PHE   A CE1 
1087 C CE2 . PHE   A 140 ? 0.54517 0.51241 0.52912 0.04392  -0.03443 -0.02354 140 PHE   A CE2 
1088 C CZ  . PHE   A 140 ? 0.53466 0.50756 0.51624 0.04409  -0.03313 -0.02516 140 PHE   A CZ  
1089 N N   . LEU   A 141 ? 0.59349 0.57498 0.57136 0.03154  -0.03176 -0.01834 141 LEU   A N   
1090 C CA  . LEU   A 141 ? 0.56612 0.55445 0.54774 0.02865  -0.03177 -0.01857 141 LEU   A CA  
1091 C C   . LEU   A 141 ? 0.59148 0.59011 0.58218 0.03127  -0.03127 -0.02197 141 LEU   A C   
1092 O O   . LEU   A 141 ? 0.57053 0.56991 0.56404 0.03484  -0.03091 -0.02456 141 LEU   A O   
1093 C CB  . LEU   A 141 ? 0.53820 0.52517 0.51307 0.02451  -0.02893 -0.01682 141 LEU   A CB  
1094 C CG  . LEU   A 141 ? 0.70695 0.68322 0.67330 0.02101  -0.02839 -0.01396 141 LEU   A CG  
1095 C CD1 . LEU   A 141 ? 0.80350 0.78052 0.76679 0.01556  -0.02585 -0.01296 141 LEU   A CD1 
1096 C CD2 . LEU   A 141 ? 0.69124 0.66411 0.65850 0.02029  -0.03169 -0.01369 141 LEU   A CD2 
1097 N N   . ASN   A 142 ? 0.56849 0.57538 0.56411 0.02922  -0.03090 -0.02237 142 ASN   A N   
1098 C CA  . ASN   A 142 ? 0.54083 0.55790 0.54500 0.03164  -0.02937 -0.02581 142 ASN   A CA  
1099 C C   . ASN   A 142 ? 0.56783 0.58715 0.56749 0.03172  -0.02588 -0.02783 142 ASN   A C   
1100 O O   . ASN   A 142 ? 0.59047 0.60760 0.58225 0.02859  -0.02413 -0.02552 142 ASN   A O   
1101 C CB  . ASN   A 142 ? 0.57027 0.59698 0.58092 0.02919  -0.02948 -0.02537 142 ASN   A CB  
1102 C CG  . ASN   A 142 ? 0.57094 0.60051 0.59007 0.03122  -0.03301 -0.02422 142 ASN   A CG  
1103 O OD1 . ASN   A 142 ? 0.57144 0.60254 0.59022 0.02779  -0.03543 -0.02151 142 ASN   A OD1 
1104 N ND2 . ASN   A 142 ? 0.61449 0.64488 0.64119 0.03665  -0.03322 -0.02617 142 ASN   A ND2 
1105 N N   . GLY   A 143 ? 0.55490 0.57846 0.55934 0.03523  -0.02466 -0.03208 143 GLY   A N   
1106 C CA  . GLY   A 143 ? 0.55094 0.57801 0.55072 0.03533  -0.02177 -0.03450 143 GLY   A CA  
1107 C C   . GLY   A 143 ? 0.52483 0.54548 0.51779 0.03655  -0.02255 -0.03418 143 GLY   A C   
1108 O O   . GLY   A 143 ? 0.52270 0.54765 0.51180 0.03681  -0.02071 -0.03628 143 GLY   A O   
1109 N N   . SER   A 144 ? 0.52180 0.53341 0.51315 0.03718  -0.02522 -0.03157 144 SER   A N   
1110 C CA  . SER   A 144 ? 0.50914 0.51551 0.49542 0.03851  -0.02600 -0.03115 144 SER   A CA  
1111 C C   . SER   A 144 ? 0.52672 0.53571 0.51816 0.04100  -0.02598 -0.03655 144 SER   A C   
1112 O O   . SER   A 144 ? 0.51121 0.51908 0.49891 0.04159  -0.02632 -0.03716 144 SER   A O   
1113 C CB  . SER   A 144 ? 0.51241 0.50874 0.49627 0.03839  -0.02833 -0.02727 144 SER   A CB  
1114 O OG  . SER   A 144 ? 0.52391 0.51865 0.51510 0.03960  -0.03025 -0.02821 144 SER   A OG  
1115 N N   . CYS   A 145 ? 0.53668 0.54914 0.53698 0.04241  -0.02535 -0.04046 145 CYS   A N   
1116 C CA  . CYS   A 145 ? 0.52865 0.54169 0.53438 0.04444  -0.02460 -0.04617 145 CYS   A CA  
1117 C C   . CYS   A 145 ? 0.55515 0.57501 0.55619 0.04344  -0.02259 -0.05039 145 CYS   A C   
1118 O O   . CYS   A 145 ? 0.56332 0.59021 0.56033 0.04199  -0.02080 -0.05022 145 CYS   A O   
1119 C CB  . CYS   A 145 ? 0.55555 0.57128 0.57196 0.04658  -0.02328 -0.04936 145 CYS   A CB  
1120 S SG  . CYS   A 145 ? 0.65123 0.65935 0.67468 0.04883  -0.02620 -0.04504 145 CYS   A SG  
1121 N N   . GLY   A 146 ? 0.53931 0.55770 0.54066 0.04381  -0.02291 -0.05408 146 GLY   A N   
1122 C CA  . GLY   A 146 ? 0.53989 0.56535 0.53566 0.04235  -0.02200 -0.05754 146 GLY   A CA  
1123 C C   . GLY   A 146 ? 0.52941 0.55350 0.51745 0.04175  -0.02427 -0.05268 146 GLY   A C   
1124 O O   . GLY   A 146 ? 0.47961 0.50978 0.46411 0.04079  -0.02441 -0.05536 146 GLY   A O   
1125 N N   . SER   A 147 ? 0.52235 0.53926 0.50784 0.04227  -0.02588 -0.04576 147 SER   A N   
1126 C CA  . SER   A 147 ? 0.49565 0.50977 0.47521 0.04253  -0.02752 -0.04101 147 SER   A CA  
1127 C C   . SER   A 147 ? 0.54648 0.55869 0.52961 0.04288  -0.02881 -0.04417 147 SER   A C   
1128 O O   . SER   A 147 ? 0.52435 0.53179 0.51441 0.04322  -0.02880 -0.04745 147 SER   A O   
1129 C CB  . SER   A 147 ? 0.51097 0.51597 0.48806 0.04283  -0.02830 -0.03432 147 SER   A CB  
1130 O OG  . SER   A 147 ? 0.53522 0.54159 0.51013 0.04164  -0.02688 -0.03207 147 SER   A OG  
1131 N N   . VAL   A 148 ? 0.55080 0.56723 0.52956 0.04281  -0.02977 -0.04282 148 VAL   A N   
1132 C CA  . VAL   A 148 ? 0.55329 0.57085 0.53547 0.04222  -0.03078 -0.04662 148 VAL   A CA  
1133 C C   . VAL   A 148 ? 0.54556 0.55792 0.52586 0.04347  -0.03227 -0.04086 148 VAL   A C   
1134 O O   . VAL   A 148 ? 0.52869 0.54005 0.50334 0.04487  -0.03239 -0.03446 148 VAL   A O   
1135 C CB  . VAL   A 148 ? 0.53572 0.56618 0.51567 0.04044  -0.03070 -0.05162 148 VAL   A CB  
1136 C CG1 . VAL   A 148 ? 0.51379 0.54912 0.49534 0.03913  -0.02845 -0.05806 148 VAL   A CG1 
1137 C CG2 . VAL   A 148 ? 0.55478 0.59260 0.52679 0.04136  -0.03165 -0.04554 148 VAL   A CG2 
1138 N N   . GLY   A 149 ? 0.51227 0.52064 0.49766 0.04297  -0.03286 -0.04321 149 GLY   A N   
1139 C CA  . GLY   A 149 ? 0.54153 0.54726 0.52612 0.04382  -0.03388 -0.03912 149 GLY   A CA  
1140 C C   . GLY   A 149 ? 0.56800 0.58446 0.55359 0.04235  -0.03479 -0.04253 149 GLY   A C   
1141 O O   . GLY   A 149 ? 0.52793 0.55013 0.51665 0.03985  -0.03449 -0.04968 149 GLY   A O   
1142 N N   . PHE   A 150 ? 0.54489 0.56456 0.52805 0.04382  -0.03573 -0.03758 150 PHE   A N   
1143 C CA  . PHE   A 150 ? 0.54267 0.57571 0.52645 0.04249  -0.03712 -0.03991 150 PHE   A CA  
1144 C C   . PHE   A 150 ? 0.57342 0.60720 0.55791 0.04444  -0.03782 -0.03453 150 PHE   A C   
1145 O O   . PHE   A 150 ? 0.55478 0.57925 0.53729 0.04732  -0.03687 -0.02837 150 PHE   A O   
1146 C CB  . PHE   A 150 ? 0.51376 0.55894 0.49171 0.04286  -0.03773 -0.03908 150 PHE   A CB  
1147 C CG  . PHE   A 150 ? 0.51738 0.56099 0.48926 0.04679  -0.03742 -0.02990 150 PHE   A CG  
1148 C CD1 . PHE   A 150 ? 0.52080 0.55442 0.48944 0.04800  -0.03571 -0.02673 150 PHE   A CD1 
1149 C CD2 . PHE   A 150 ? 0.51713 0.56934 0.48707 0.04924  -0.03858 -0.02436 150 PHE   A CD2 
1150 C CE1 . PHE   A 150 ? 0.52917 0.55975 0.49227 0.05107  -0.03472 -0.01871 150 PHE   A CE1 
1151 C CE2 . PHE   A 150 ? 0.53839 0.58751 0.50316 0.05328  -0.03754 -0.01566 150 PHE   A CE2 
1152 C CZ  . PHE   A 150 ? 0.54512 0.58260 0.50624 0.05394  -0.03538 -0.01308 150 PHE   A CZ  
1153 N N   . ASN   A 151 ? 0.50723 0.55289 0.49477 0.04253  -0.03927 -0.03743 151 ASN   A N   
1154 C CA  . ASN   A 151 ? 0.55266 0.60462 0.54136 0.04459  -0.04017 -0.03237 151 ASN   A CA  
1155 C C   . ASN   A 151 ? 0.61739 0.68858 0.60445 0.04404  -0.04251 -0.03279 151 ASN   A C   
1156 O O   . ASN   A 151 ? 0.61503 0.69454 0.60169 0.04025  -0.04340 -0.03963 151 ASN   A O   
1157 C CB  . ASN   A 151 ? 0.56779 0.61661 0.56358 0.04217  -0.03979 -0.03531 151 ASN   A CB  
1158 C CG  . ASN   A 151 ? 0.57257 0.60394 0.56901 0.04356  -0.03769 -0.03257 151 ASN   A CG  
1159 O OD1 . ASN   A 151 ? 0.59750 0.61934 0.59585 0.04147  -0.03675 -0.03655 151 ASN   A OD1 
1160 N ND2 . ASN   A 151 ? 0.54694 0.57440 0.54176 0.04723  -0.03676 -0.02566 151 ASN   A ND2 
1161 N N   . ILE   A 152 ? 0.58306 0.66177 0.56919 0.04796  -0.04336 -0.02541 152 ILE   A N   
1162 C CA  . ILE   A 152 ? 0.66551 0.76400 0.64976 0.04844  -0.04600 -0.02369 152 ILE   A CA  
1163 C C   . ILE   A 152 ? 0.75827 0.86875 0.74912 0.04788  -0.04770 -0.02337 152 ILE   A C   
1164 O O   . ILE   A 152 ? 0.72363 0.82793 0.71783 0.05120  -0.04632 -0.01826 152 ILE   A O   
1165 C CB  . ILE   A 152 ? 0.62785 0.72710 0.60548 0.05433  -0.04551 -0.01388 152 ILE   A CB  
1166 C CG1 . ILE   A 152 ? 0.58370 0.67007 0.55550 0.05435  -0.04336 -0.01407 152 ILE   A CG1 
1167 C CG2 . ILE   A 152 ? 0.69741 0.81832 0.67254 0.05486  -0.04854 -0.01161 152 ILE   A CG2 
1168 C CD1 . ILE   A 152 ? 0.55031 0.63970 0.51491 0.05849  -0.04280 -0.00591 152 ILE   A CD1 
1169 N N   . ASP   A 153 ? 0.77175 0.89995 0.76448 0.04329  -0.05049 -0.02928 153 ASP   A N   
1170 C CA  . ASP   A 153 ? 0.79026 0.93444 0.78955 0.04170  -0.05273 -0.02969 153 ASP   A CA  
1171 C C   . ASP   A 153 ? 0.85332 1.01918 0.84872 0.04388  -0.05613 -0.02495 153 ASP   A C   
1172 O O   . ASP   A 153 ? 0.88330 1.06158 0.87526 0.03934  -0.05827 -0.03093 153 ASP   A O   
1173 C CB  . ASP   A 153 ? 0.85306 0.99951 0.85796 0.03333  -0.05300 -0.04141 153 ASP   A CB  
1174 C CG  . ASP   A 153 ? 1.08207 1.24843 1.09384 0.02993  -0.05568 -0.04331 153 ASP   A CG  
1175 O OD1 . ASP   A 153 ? 1.10200 1.28736 1.11300 0.03272  -0.05873 -0.03767 153 ASP   A OD1 
1176 O OD2 . ASP   A 153 ? 1.32400 1.48725 1.34250 0.02433  -0.05465 -0.05019 153 ASP   A OD2 
1177 N N   . TYR   A 154 ? 0.85095 1.02087 0.84653 0.05108  -0.05627 -0.01398 154 TYR   A N   
1178 C CA  . TYR   A 154 ? 0.85501 1.04593 0.84766 0.05452  -0.05949 -0.00719 154 TYR   A CA  
1179 C C   . TYR   A 154 ? 0.79283 0.98570 0.77567 0.05398  -0.06005 -0.00745 154 TYR   A C   
1180 O O   . TYR   A 154 ? 0.91006 1.09511 0.88715 0.05986  -0.05825 0.00112  154 TYR   A O   
1181 C CB  . TYR   A 154 ? 0.93694 1.15236 0.93560 0.04965  -0.06364 -0.01185 154 TYR   A CB  
1182 C CG  . TYR   A 154 ? 1.06356 1.30411 1.05974 0.05290  -0.06775 -0.00469 154 TYR   A CG  
1183 C CD1 . TYR   A 154 ? 1.01223 1.25330 1.00685 0.06253  -0.06707 0.00886  154 TYR   A CD1 
1184 C CD2 . TYR   A 154 ? 1.11498 1.37887 1.11027 0.04628  -0.07217 -0.01141 154 TYR   A CD2 
1185 C CE1 . TYR   A 154 ? 1.04966 1.31415 1.04224 0.06619  -0.07087 0.01663  154 TYR   A CE1 
1186 C CE2 . TYR   A 154 ? 1.05041 1.33907 1.04299 0.04922  -0.07641 -0.00429 154 TYR   A CE2 
1187 C CZ  . TYR   A 154 ? 1.08312 1.37218 1.07453 0.05954  -0.07586 0.01029  154 TYR   A CZ  
1188 O OH  . TYR   A 154 ? 1.07106 1.38515 1.06000 0.06320  -0.08011 0.01865  154 TYR   A OH  
1189 N N   . ASP   A 155 ? 0.90054 1.10348 0.88138 0.04659  -0.06204 -0.01756 155 ASP   A N   
1190 C CA  . ASP   A 155 ? 0.85680 1.06306 0.82836 0.04515  -0.06225 -0.01923 155 ASP   A CA  
1191 C C   . ASP   A 155 ? 0.76580 0.95926 0.73607 0.03889  -0.05986 -0.03097 155 ASP   A C   
1192 O O   . ASP   A 155 ? 0.67055 0.86300 0.63343 0.03818  -0.05888 -0.03235 155 ASP   A O   
1193 C CB  . ASP   A 155 ? 0.81714 1.05179 0.78551 0.04253  -0.06690 -0.01987 155 ASP   A CB  
1194 C CG  . ASP   A 155 ? 0.80460 1.05198 0.77846 0.03381  -0.06925 -0.03202 155 ASP   A CG  
1195 O OD1 . ASP   A 155 ? 0.83380 1.07350 0.81641 0.03208  -0.06822 -0.03542 155 ASP   A OD1 
1196 O OD2 . ASP   A 155 ? 0.78979 1.05473 0.75885 0.02826  -0.07181 -0.03839 155 ASP   A OD2 
1197 N N   . CYS   A 156 ? 0.81473 0.99852 0.79221 0.03463  -0.05856 -0.03900 156 CYS   A N   
1198 C CA  . CYS   A 156 ? 0.72339 0.89585 0.70113 0.02897  -0.05611 -0.05024 156 CYS   A CA  
1199 C C   . CYS   A 156 ? 0.69124 0.83885 0.66989 0.03246  -0.05235 -0.04753 156 CYS   A C   
1200 O O   . CYS   A 156 ? 0.70699 0.84413 0.69069 0.03510  -0.05138 -0.04340 156 CYS   A O   
1201 C CB  . CYS   A 156 ? 0.71452 0.89135 0.69973 0.02177  -0.05663 -0.06075 156 CYS   A CB  
1202 S SG  . CYS   A 156 ? 0.71468 0.87120 0.70335 0.01658  -0.05233 -0.07269 156 CYS   A SG  
1203 N N   . VAL   A 157 ? 0.66816 0.80752 0.64192 0.03222  -0.05022 -0.04997 157 VAL   A N   
1204 C CA  . VAL   A 157 ? 0.64272 0.76066 0.61718 0.03485  -0.04702 -0.04802 157 VAL   A CA  
1205 C C   . VAL   A 157 ? 0.60832 0.71587 0.58895 0.03027  -0.04509 -0.05801 157 VAL   A C   
1206 O O   . VAL   A 157 ? 0.61574 0.72686 0.59581 0.02598  -0.04420 -0.06694 157 VAL   A O   
1207 C CB  . VAL   A 157 ? 0.61096 0.72618 0.57796 0.03698  -0.04554 -0.04499 157 VAL   A CB  
1208 C CG1 . VAL   A 157 ? 0.59417 0.68900 0.56258 0.03900  -0.04261 -0.04345 157 VAL   A CG1 
1209 C CG2 . VAL   A 157 ? 0.61550 0.74003 0.57635 0.04166  -0.04696 -0.03437 157 VAL   A CG2 
1210 N N   . SER   A 158 ? 0.57422 0.66847 0.56060 0.03132  -0.04401 -0.05635 158 SER   A N   
1211 C CA  . SER   A 158 ? 0.59469 0.67780 0.58753 0.02765  -0.04195 -0.06418 158 SER   A CA  
1212 C C   . SER   A 158 ? 0.57955 0.64572 0.57182 0.03029  -0.03947 -0.06256 158 SER   A C   
1213 O O   . SER   A 158 ? 0.59701 0.65173 0.58985 0.03370  -0.03893 -0.05603 158 SER   A O   
1214 C CB  . SER   A 158 ? 0.57986 0.65988 0.57930 0.02676  -0.04219 -0.06315 158 SER   A CB  
1215 O OG  . SER   A 158 ? 0.68742 0.78445 0.68897 0.02303  -0.04441 -0.06653 158 SER   A OG  
1216 N N   . PHE   A 159 ? 0.53864 0.60416 0.52991 0.02854  -0.03787 -0.06876 159 PHE   A N   
1217 C CA  . PHE   A 159 ? 0.53443 0.58610 0.52656 0.03072  -0.03560 -0.06797 159 PHE   A CA  
1218 C C   . PHE   A 159 ? 0.53998 0.57889 0.54003 0.02938  -0.03383 -0.07190 159 PHE   A C   
1219 O O   . PHE   A 159 ? 0.54674 0.58764 0.55136 0.02531  -0.03285 -0.07986 159 PHE   A O   
1220 C CB  . PHE   A 159 ? 0.53226 0.58896 0.52131 0.02967  -0.03406 -0.07311 159 PHE   A CB  
1221 C CG  . PHE   A 159 ? 0.51471 0.58284 0.49534 0.03115  -0.03534 -0.06824 159 PHE   A CG  
1222 C CD1 . PHE   A 159 ? 0.49904 0.56157 0.47558 0.03504  -0.03511 -0.05981 159 PHE   A CD1 
1223 C CD2 . PHE   A 159 ? 0.53564 0.62023 0.51221 0.02831  -0.03663 -0.07204 159 PHE   A CD2 
1224 C CE1 . PHE   A 159 ? 0.53395 0.60578 0.50284 0.03642  -0.03573 -0.05470 159 PHE   A CE1 
1225 C CE2 . PHE   A 159 ? 0.53996 0.63524 0.50847 0.02998  -0.03772 -0.06653 159 PHE   A CE2 
1226 C CZ  . PHE   A 159 ? 0.51822 0.60645 0.48305 0.03421  -0.03706 -0.05760 159 PHE   A CZ  
1227 N N   . CYS   A 160 ? 0.52308 0.54885 0.52451 0.03255  -0.03325 -0.06625 160 CYS   A N   
1228 C CA  . CYS   A 160 ? 0.54662 0.56000 0.55499 0.03201  -0.03174 -0.06786 160 CYS   A CA  
1229 C C   . CYS   A 160 ? 0.55075 0.55275 0.56089 0.03482  -0.03041 -0.06563 160 CYS   A C   
1230 O O   . CYS   A 160 ? 0.55835 0.55072 0.57472 0.03463  -0.02886 -0.06739 160 CYS   A O   
1231 C CB  . CYS   A 160 ? 0.55717 0.56678 0.56650 0.03256  -0.03282 -0.06231 160 CYS   A CB  
1232 S SG  . CYS   A 160 ? 0.57477 0.57942 0.57778 0.03727  -0.03403 -0.05137 160 CYS   A SG  
1233 N N   . TYR   A 161 ? 0.54931 0.55252 0.55462 0.03729  -0.03089 -0.06155 161 TYR   A N   
1234 C CA  . TYR   A 161 ? 0.56271 0.55682 0.56987 0.03976  -0.03021 -0.05851 161 TYR   A CA  
1235 C C   . TYR   A 161 ? 0.53394 0.53364 0.53801 0.04058  -0.02957 -0.05910 161 TYR   A C   
1236 O O   . TYR   A 161 ? 0.50417 0.51253 0.50202 0.04017  -0.03021 -0.05797 161 TYR   A O   
1237 C CB  . TYR   A 161 ? 0.54486 0.53157 0.54912 0.04170  -0.03167 -0.05023 161 TYR   A CB  
1238 C CG  . TYR   A 161 ? 0.51931 0.49852 0.52475 0.04367  -0.03163 -0.04670 161 TYR   A CG  
1239 C CD1 . TYR   A 161 ? 0.51912 0.48984 0.53058 0.04440  -0.03118 -0.04645 161 TYR   A CD1 
1240 C CD2 . TYR   A 161 ? 0.52472 0.50590 0.52537 0.04461  -0.03206 -0.04322 161 TYR   A CD2 
1241 C CE1 . TYR   A 161 ? 0.51835 0.48431 0.53109 0.04625  -0.03169 -0.04272 161 TYR   A CE1 
1242 C CE2 . TYR   A 161 ? 0.48216 0.45834 0.48426 0.04576  -0.03236 -0.04024 161 TYR   A CE2 
1243 C CZ  . TYR   A 161 ? 0.51334 0.48269 0.52151 0.04671  -0.03244 -0.03993 161 TYR   A CZ  
1244 O OH  . TYR   A 161 ? 0.51001 0.47641 0.51980 0.04793  -0.03327 -0.03648 161 TYR   A OH  
1245 N N   . MET   A 162 ? 0.55906 0.55420 0.56788 0.04193  -0.02815 -0.06040 162 MET   A N   
1246 C CA  . MET   A 162 ? 0.54957 0.54938 0.55662 0.04280  -0.02725 -0.06026 162 MET   A CA  
1247 C C   . MET   A 162 ? 0.52406 0.51663 0.53513 0.04509  -0.02747 -0.05612 162 MET   A C   
1248 O O   . MET   A 162 ? 0.51652 0.50285 0.53496 0.04633  -0.02668 -0.05760 162 MET   A O   
1249 C CB  . MET   A 162 ? 0.53217 0.53868 0.54212 0.04162  -0.02451 -0.06880 162 MET   A CB  
1250 C CG  . MET   A 162 ? 0.59093 0.60769 0.59461 0.04094  -0.02387 -0.06899 162 MET   A CG  
1251 S SD  . MET   A 162 ? 0.62034 0.64340 0.62819 0.04052  -0.01974 -0.07789 162 MET   A SD  
1252 C CE  . MET   A 162 ? 0.54260 0.57898 0.53966 0.03864  -0.01984 -0.07658 162 MET   A CE  
1253 N N   . HIS   A 163 ? 0.51270 0.50637 0.51907 0.04549  -0.02846 -0.05076 163 HIS   A N   
1254 C CA  . HIS   A 163 ? 0.52833 0.51657 0.53739 0.04689  -0.02944 -0.04618 163 HIS   A CA  
1255 C C   . HIS   A 163 ? 0.52202 0.51332 0.53871 0.04838  -0.02772 -0.04930 163 HIS   A C   
1256 O O   . HIS   A 163 ? 0.48759 0.48647 0.50420 0.04788  -0.02567 -0.05319 163 HIS   A O   
1257 C CB  . HIS   A 163 ? 0.48665 0.47501 0.48821 0.04592  -0.03065 -0.04027 163 HIS   A CB  
1258 C CG  . HIS   A 163 ? 0.50230 0.48616 0.50561 0.04632  -0.03209 -0.03587 163 HIS   A CG  
1259 N ND1 . HIS   A 163 ? 0.45633 0.43279 0.46164 0.04716  -0.03370 -0.03317 163 HIS   A ND1 
1260 C CD2 . HIS   A 163 ? 0.50226 0.48904 0.50550 0.04556  -0.03225 -0.03372 163 HIS   A CD2 
1261 C CE1 . HIS   A 163 ? 0.53406 0.50961 0.54000 0.04698  -0.03511 -0.02951 163 HIS   A CE1 
1262 N NE2 . HIS   A 163 ? 0.54111 0.52302 0.54618 0.04585  -0.03432 -0.02997 163 HIS   A NE2 
1263 N N   . HIS   A 164 ? 0.53600 0.52192 0.55931 0.05046  -0.02840 -0.04716 164 HIS   A N   
1264 C CA  . HIS   A 164 ? 0.55296 0.54114 0.58560 0.05302  -0.02671 -0.04929 164 HIS   A CA  
1265 C C   . HIS   A 164 ? 0.57388 0.56151 0.60951 0.05450  -0.02896 -0.04313 164 HIS   A C   
1266 O O   . HIS   A 164 ? 0.55685 0.55097 0.59751 0.05571  -0.02810 -0.04344 164 HIS   A O   
1267 C CB  . HIS   A 164 ? 0.52536 0.50780 0.56597 0.05494  -0.02462 -0.05361 164 HIS   A CB  
1268 C CG  . HIS   A 164 ? 0.56170 0.54815 0.60392 0.05402  -0.02098 -0.06228 164 HIS   A CG  
1269 N ND1 . HIS   A 164 ? 0.55995 0.54744 0.59648 0.05091  -0.02073 -0.06628 164 HIS   A ND1 
1270 C CD2 . HIS   A 164 ? 0.53457 0.52483 0.58352 0.05566  -0.01729 -0.06805 164 HIS   A CD2 
1271 C CE1 . HIS   A 164 ? 0.51677 0.50875 0.55559 0.05011  -0.01729 -0.07443 164 HIS   A CE1 
1272 N NE2 . HIS   A 164 ? 0.54550 0.53859 0.59174 0.05302  -0.01483 -0.07588 164 HIS   A NE2 
1273 N N   . MET   A 165 ? 0.52150 0.50264 0.55414 0.05420  -0.03178 -0.03766 165 MET   A N   
1274 C CA  . MET   A 165 ? 0.55789 0.53840 0.59486 0.05595  -0.03405 -0.03229 165 MET   A CA  
1275 C C   . MET   A 165 ? 0.60502 0.58108 0.63366 0.05357  -0.03717 -0.02661 165 MET   A C   
1276 O O   . MET   A 165 ? 0.59174 0.56232 0.61373 0.05193  -0.03721 -0.02653 165 MET   A O   
1277 C CB  . MET   A 165 ? 0.56551 0.54087 0.61203 0.05985  -0.03314 -0.03231 165 MET   A CB  
1278 C CG  . MET   A 165 ? 0.62416 0.60311 0.67923 0.06331  -0.03438 -0.02811 165 MET   A CG  
1279 S SD  . MET   A 165 ? 0.78299 0.75541 0.85073 0.06883  -0.03152 -0.02914 165 MET   A SD  
1280 C CE  . MET   A 165 ? 0.55716 0.51832 0.61930 0.06627  -0.03015 -0.03211 165 MET   A CE  
1281 N N   . GLU   A 166 ? 0.56470 0.54386 0.59402 0.05331  -0.03965 -0.02209 166 GLU   A N   
1282 C CA  . GLU   A 166 ? 0.57076 0.54562 0.59313 0.05116  -0.04256 -0.01692 166 GLU   A CA  
1283 C C   . GLU   A 166 ? 0.56394 0.53859 0.59266 0.05394  -0.04483 -0.01239 166 GLU   A C   
1284 O O   . GLU   A 166 ? 0.56580 0.54776 0.60276 0.05623  -0.04543 -0.01147 166 GLU   A O   
1285 C CB  . GLU   A 166 ? 0.56254 0.54169 0.57815 0.04707  -0.04370 -0.01552 166 GLU   A CB  
1286 C CG  . GLU   A 166 ? 0.59594 0.57023 0.60346 0.04420  -0.04616 -0.01126 166 GLU   A CG  
1287 C CD  . GLU   A 166 ? 0.66231 0.63964 0.66321 0.03942  -0.04667 -0.01068 166 GLU   A CD  
1288 O OE1 . GLU   A 166 ? 0.65632 0.63431 0.65392 0.03775  -0.04426 -0.01321 166 GLU   A OE1 
1289 O OE2 . GLU   A 166 ? 0.68771 0.66684 0.68648 0.03704  -0.04936 -0.00765 166 GLU   A OE2 
1290 N N   . LEU   A 167 ? 0.53947 0.50647 0.56465 0.05399  -0.04593 -0.00916 167 LEU   A N   
1291 C CA  . LEU   A 167 ? 0.53923 0.50549 0.56950 0.05681  -0.04804 -0.00382 167 LEU   A CA  
1292 C C   . LEU   A 167 ? 0.53291 0.50507 0.55884 0.05434  -0.05194 0.00097  167 LEU   A C   
1293 O O   . LEU   A 167 ? 0.57293 0.54602 0.59001 0.04973  -0.05255 -0.00002 167 LEU   A O   
1294 C CB  . LEU   A 167 ? 0.57883 0.53489 0.60646 0.05732  -0.04735 -0.00202 167 LEU   A CB  
1295 C CG  . LEU   A 167 ? 0.56171 0.51203 0.59618 0.05992  -0.04377 -0.00597 167 LEU   A CG  
1296 C CD1 . LEU   A 167 ? 0.53178 0.48638 0.57823 0.06418  -0.04225 -0.00774 167 LEU   A CD1 
1297 C CD2 . LEU   A 167 ? 0.55343 0.50218 0.58280 0.05716  -0.04145 -0.01199 167 LEU   A CD2 
1298 N N   . PRO   A 168 ? 0.57079 0.54728 0.60296 0.05723  -0.05453 0.00624  168 PRO   A N   
1299 C CA  . PRO   A 168 ? 0.55975 0.54382 0.58772 0.05431  -0.05879 0.01072  168 PRO   A CA  
1300 C C   . PRO   A 168 ? 0.58437 0.56263 0.59865 0.04911  -0.05998 0.01179  168 PRO   A C   
1301 O O   . PRO   A 168 ? 0.58806 0.57189 0.59625 0.04456  -0.06250 0.01266  168 PRO   A O   
1302 C CB  . PRO   A 168 ? 0.52289 0.51068 0.55971 0.05942  -0.06113 0.01726  168 PRO   A CB  
1303 C CG  . PRO   A 168 ? 0.56317 0.54928 0.61216 0.06516  -0.05756 0.01468  168 PRO   A CG  
1304 C CD  . PRO   A 168 ? 0.54059 0.51712 0.58523 0.06345  -0.05342 0.00796  168 PRO   A CD  
1305 N N   . THR   A 169 ? 0.54843 0.51585 0.55789 0.04934  -0.05790 0.01135  169 THR   A N   
1306 C CA  . THR   A 169 ? 0.58410 0.54559 0.58101 0.04496  -0.05824 0.01217  169 THR   A CA  
1307 C C   . THR   A 169 ? 0.61288 0.57109 0.60211 0.04103  -0.05577 0.00707  169 THR   A C   
1308 O O   . THR   A 169 ? 0.64837 0.60123 0.62729 0.03747  -0.05530 0.00716  169 THR   A O   
1309 C CB  . THR   A 169 ? 0.62679 0.57887 0.62240 0.04695  -0.05676 0.01442  169 THR   A CB  
1310 O OG1 . THR   A 169 ? 0.62770 0.57414 0.62697 0.04872  -0.05303 0.00987  169 THR   A OG1 
1311 C CG2 . THR   A 169 ? 0.66162 0.61567 0.66479 0.05118  -0.05875 0.02047  169 THR   A CG2 
1312 N N   . GLY   A 170 ? 0.58265 0.54382 0.57648 0.04177  -0.05385 0.00290  170 GLY   A N   
1313 C CA  . GLY   A 170 ? 0.58400 0.54255 0.57114 0.03865  -0.05141 -0.00090 170 GLY   A CA  
1314 C C   . GLY   A 170 ? 0.59903 0.55163 0.58622 0.04062  -0.04814 -0.00392 170 GLY   A C   
1315 O O   . GLY   A 170 ? 0.62352 0.57591 0.60743 0.03927  -0.04605 -0.00675 170 GLY   A O   
1316 N N   . VAL   A 171 ? 0.58815 0.53643 0.57902 0.04353  -0.04764 -0.00313 171 VAL   A N   
1317 C CA  . VAL   A 171 ? 0.56976 0.51418 0.56175 0.04492  -0.04486 -0.00635 171 VAL   A CA  
1318 C C   . VAL   A 171 ? 0.54972 0.49970 0.54982 0.04700  -0.04366 -0.01037 171 VAL   A C   
1319 O O   . VAL   A 171 ? 0.54021 0.49640 0.54558 0.04784  -0.04470 -0.01027 171 VAL   A O   
1320 C CB  . VAL   A 171 ? 0.56985 0.50801 0.56356 0.04649  -0.04437 -0.00453 171 VAL   A CB  
1321 C CG1 . VAL   A 171 ? 0.59484 0.52834 0.58008 0.04433  -0.04532 -0.00051 171 VAL   A CG1 
1322 C CG2 . VAL   A 171 ? 0.54108 0.48046 0.54475 0.04976  -0.04508 -0.00323 171 VAL   A CG2 
1323 N N   . HIS   A 172 ? 0.53032 0.47908 0.53158 0.04769  -0.04139 -0.01411 172 HIS   A N   
1324 C CA  . HIS   A 172 ? 0.53330 0.48767 0.54021 0.04886  -0.03979 -0.01886 172 HIS   A CA  
1325 C C   . HIS   A 172 ? 0.52601 0.47778 0.53912 0.05053  -0.03801 -0.02225 172 HIS   A C   
1326 O O   . HIS   A 172 ? 0.56940 0.51575 0.58070 0.05002  -0.03762 -0.02151 172 HIS   A O   
1327 C CB  . HIS   A 172 ? 0.53189 0.48965 0.53252 0.04693  -0.03863 -0.02089 172 HIS   A CB  
1328 C CG  . HIS   A 172 ? 0.58618 0.54479 0.58042 0.04456  -0.03957 -0.01799 172 HIS   A CG  
1329 N ND1 . HIS   A 172 ? 0.58317 0.53633 0.56878 0.04260  -0.03952 -0.01535 172 HIS   A ND1 
1330 C CD2 . HIS   A 172 ? 0.60014 0.56426 0.59567 0.04346  -0.04019 -0.01765 172 HIS   A CD2 
1331 C CE1 . HIS   A 172 ? 0.59013 0.54446 0.57158 0.04006  -0.03994 -0.01387 172 HIS   A CE1 
1332 N NE2 . HIS   A 172 ? 0.61978 0.58127 0.60721 0.04030  -0.04055 -0.01511 172 HIS   A NE2 
1333 N N   . ALA   A 173 ? 0.51734 0.47305 0.53799 0.05222  -0.03652 -0.02636 173 ALA   A N   
1334 C CA  . ALA   A 173 ? 0.49473 0.44773 0.52192 0.05328  -0.03417 -0.03085 173 ALA   A CA  
1335 C C   . ALA   A 173 ? 0.49220 0.45187 0.52095 0.05275  -0.03196 -0.03763 173 ALA   A C   
1336 O O   . ALA   A 173 ? 0.50882 0.47505 0.53746 0.05302  -0.03187 -0.03837 173 ALA   A O   
1337 C CB  . ALA   A 173 ? 0.47824 0.42722 0.51471 0.05652  -0.03369 -0.02914 173 ALA   A CB  
1338 N N   . GLY   A 174 ? 0.51522 0.47385 0.54527 0.05155  -0.03007 -0.04274 174 GLY   A N   
1339 C CA  . GLY   A 174 ? 0.52644 0.49201 0.55696 0.05045  -0.02797 -0.04973 174 GLY   A CA  
1340 C C   . GLY   A 174 ? 0.51538 0.47817 0.55075 0.04925  -0.02546 -0.05614 174 GLY   A C   
1341 O O   . GLY   A 174 ? 0.48072 0.43524 0.52052 0.04968  -0.02488 -0.05497 174 GLY   A O   
1342 N N   . THR   A 175 ? 0.49473 0.46471 0.52881 0.04727  -0.02378 -0.06304 175 THR   A N   
1343 C CA  . THR   A 175 ? 0.51201 0.48096 0.55023 0.04503  -0.02104 -0.07095 175 THR   A CA  
1344 C C   . THR   A 175 ? 0.55515 0.53179 0.58663 0.04119  -0.02225 -0.07362 175 THR   A C   
1345 O O   . THR   A 175 ? 0.52951 0.51245 0.55349 0.04104  -0.02469 -0.06946 175 THR   A O   
1346 C CB  . THR   A 175 ? 0.52605 0.49781 0.56956 0.04580  -0.01734 -0.07840 175 THR   A CB  
1347 O OG1 . THR   A 175 ? 0.50236 0.48573 0.53934 0.04419  -0.01758 -0.08124 175 THR   A OG1 
1348 C CG2 . THR   A 175 ? 0.51089 0.47842 0.56112 0.05044  -0.01654 -0.07458 175 THR   A CG2 
1349 N N   . ASP   A 176 ? 0.57141 0.54767 0.60603 0.03801  -0.02037 -0.08055 176 ASP   A N   
1350 C CA  . ASP   A 176 ? 0.57477 0.56153 0.60415 0.03402  -0.02132 -0.08482 176 ASP   A CA  
1351 C C   . ASP   A 176 ? 0.58583 0.58240 0.61258 0.03311  -0.01978 -0.09118 176 ASP   A C   
1352 O O   . ASP   A 176 ? 0.54033 0.53548 0.56927 0.03577  -0.01799 -0.09157 176 ASP   A O   
1353 C CB  . ASP   A 176 ? 0.57622 0.55994 0.61001 0.03002  -0.01998 -0.09018 176 ASP   A CB  
1354 C CG  . ASP   A 176 ? 0.59226 0.56749 0.63446 0.02933  -0.01543 -0.09769 176 ASP   A CG  
1355 O OD1 . ASP   A 176 ? 0.60735 0.58584 0.65041 0.02961  -0.01292 -0.10379 176 ASP   A OD1 
1356 O OD2 . ASP   A 176 ? 0.59049 0.55533 0.63858 0.02855  -0.01387 -0.09743 176 ASP   A OD2 
1357 N N   . LEU   A 177 ? 0.56428 0.57205 0.58635 0.02924  -0.02040 -0.09619 177 LEU   A N   
1358 C CA  . LEU   A 177 ? 0.58737 0.60580 0.60541 0.02791  -0.01897 -0.10207 177 LEU   A CA  
1359 C C   . LEU   A 177 ? 0.60212 0.61846 0.62579 0.02534  -0.01437 -0.11356 177 LEU   A C   
1360 O O   . LEU   A 177 ? 0.58482 0.61095 0.60473 0.02305  -0.01271 -0.12041 177 LEU   A O   
1361 C CB  . LEU   A 177 ? 0.60235 0.63543 0.61192 0.02510  -0.02194 -0.10160 177 LEU   A CB  
1362 C CG  . LEU   A 177 ? 0.56925 0.60738 0.57134 0.02823  -0.02479 -0.09181 177 LEU   A CG  
1363 C CD1 . LEU   A 177 ? 0.52846 0.56800 0.52873 0.03027  -0.02275 -0.09181 177 LEU   A CD1 
1364 C CD2 . LEU   A 177 ? 0.55411 0.58251 0.55733 0.03138  -0.02691 -0.08230 177 LEU   A CD2 
1365 N N   . GLU   A 178 ? 0.60517 0.60858 0.63751 0.02567  -0.01186 -0.11576 178 GLU   A N   
1366 C CA  . GLU   A 178 ? 0.60178 0.59969 0.64082 0.02423  -0.00642 -0.12610 178 GLU   A CA  
1367 C C   . GLU   A 178 ? 0.59894 0.58578 0.64584 0.03000  -0.00345 -0.12336 178 GLU   A C   
1368 O O   . GLU   A 178 ? 0.62213 0.60126 0.67653 0.03016  0.00170  -0.13059 178 GLU   A O   
1369 C CB  . GLU   A 178 ? 0.64643 0.63776 0.69027 0.01960  -0.00483 -0.13179 178 GLU   A CB  
1370 C CG  . GLU   A 178 ? 0.67962 0.68410 0.71743 0.01283  -0.00679 -0.13774 178 GLU   A CG  
1371 C CD  . GLU   A 178 ? 0.72095 0.71901 0.76433 0.00754  -0.00504 -0.14342 178 GLU   A CD  
1372 O OE1 . GLU   A 178 ? 0.73744 0.71962 0.78897 0.00949  -0.00216 -0.14188 178 GLU   A OE1 
1373 O OE2 . GLU   A 178 ? 0.71624 0.72567 0.75598 0.00125  -0.00653 -0.14917 178 GLU   A OE2 
1374 N N   . GLY   A 179 ? 0.60440 0.59048 0.65009 0.03468  -0.00640 -0.11314 179 GLY   A N   
1375 C CA  . GLY   A 179 ? 0.58401 0.56218 0.63727 0.04023  -0.00448 -0.10941 179 GLY   A CA  
1376 C C   . GLY   A 179 ? 0.56921 0.53356 0.62976 0.04280  -0.00451 -0.10398 179 GLY   A C   
1377 O O   . GLY   A 179 ? 0.62481 0.58286 0.69270 0.04775  -0.00287 -0.10064 179 GLY   A O   
1378 N N   . ASN   A 180 ? 0.54068 0.50099 0.59965 0.03972  -0.00627 -0.10252 180 ASN   A N   
1379 C CA  . ASN   A 180 ? 0.54943 0.49648 0.61473 0.04145  -0.00581 -0.09757 180 ASN   A CA  
1380 C C   . ASN   A 180 ? 0.54549 0.49220 0.60645 0.04395  -0.01073 -0.08591 180 ASN   A C   
1381 O O   . ASN   A 180 ? 0.52886 0.48149 0.58221 0.04143  -0.01418 -0.08316 180 ASN   A O   
1382 C CB  . ASN   A 180 ? 0.58292 0.52567 0.64947 0.03603  -0.00423 -0.10306 180 ASN   A CB  
1383 C CG  . ASN   A 180 ? 0.60995 0.55056 0.68148 0.03297  0.00140  -0.11536 180 ASN   A CG  
1384 O OD1 . ASN   A 180 ? 0.60256 0.53672 0.68111 0.03654  0.00568  -0.11808 180 ASN   A OD1 
1385 N ND2 . ASN   A 180 ? 0.67357 0.62006 0.74170 0.02625  0.00161  -0.12309 180 ASN   A ND2 
1386 N N   . PHE   A 181 ? 0.53413 0.47426 0.60006 0.04892  -0.01088 -0.07919 181 PHE   A N   
1387 C CA  . PHE   A 181 ? 0.51895 0.45871 0.58053 0.05093  -0.01529 -0.06876 181 PHE   A CA  
1388 C C   . PHE   A 181 ? 0.55760 0.49127 0.61688 0.04849  -0.01662 -0.06512 181 PHE   A C   
1389 O O   . PHE   A 181 ? 0.52862 0.45485 0.59288 0.04662  -0.01377 -0.06856 181 PHE   A O   
1390 C CB  . PHE   A 181 ? 0.52004 0.45504 0.58823 0.05643  -0.01519 -0.06266 181 PHE   A CB  
1391 C CG  . PHE   A 181 ? 0.54570 0.48986 0.61201 0.05877  -0.01702 -0.06034 181 PHE   A CG  
1392 C CD1 . PHE   A 181 ? 0.54749 0.49633 0.60596 0.05820  -0.02139 -0.05367 181 PHE   A CD1 
1393 C CD2 . PHE   A 181 ? 0.51770 0.46550 0.59041 0.06131  -0.01386 -0.06508 181 PHE   A CD2 
1394 C CE1 . PHE   A 181 ? 0.56384 0.52088 0.62086 0.05952  -0.02276 -0.05175 181 PHE   A CE1 
1395 C CE2 . PHE   A 181 ? 0.54864 0.50564 0.62020 0.06301  -0.01528 -0.06289 181 PHE   A CE2 
1396 C CZ  . PHE   A 181 ? 0.56254 0.52416 0.62627 0.06183  -0.01983 -0.05619 181 PHE   A CZ  
1397 N N   . TYR   A 182 ? 0.53145 0.46809 0.58321 0.04827  -0.02053 -0.05831 182 TYR   A N   
1398 C CA  . TYR   A 182 ? 0.49942 0.43010 0.54905 0.04701  -0.02176 -0.05303 182 TYR   A CA  
1399 C C   . TYR   A 182 ? 0.50740 0.43012 0.56034 0.05081  -0.02237 -0.04525 182 TYR   A C   
1400 O O   . TYR   A 182 ? 0.54597 0.47183 0.59580 0.05323  -0.02503 -0.03992 182 TYR   A O   
1401 C CB  . TYR   A 182 ? 0.51747 0.45464 0.55759 0.04534  -0.02497 -0.04962 182 TYR   A CB  
1402 C CG  . TYR   A 182 ? 0.50859 0.45424 0.54546 0.04175  -0.02482 -0.05557 182 TYR   A CG  
1403 C CD1 . TYR   A 182 ? 0.50320 0.44812 0.54114 0.03835  -0.02401 -0.05779 182 TYR   A CD1 
1404 C CD2 . TYR   A 182 ? 0.48168 0.43712 0.51437 0.04164  -0.02560 -0.05844 182 TYR   A CD2 
1405 C CE1 . TYR   A 182 ? 0.51684 0.47166 0.55214 0.03506  -0.02441 -0.06280 182 TYR   A CE1 
1406 C CE2 . TYR   A 182 ? 0.49710 0.46173 0.52642 0.03859  -0.02588 -0.06301 182 TYR   A CE2 
1407 C CZ  . TYR   A 182 ? 0.49686 0.46170 0.52763 0.03537  -0.02551 -0.06517 182 TYR   A CZ  
1408 O OH  . TYR   A 182 ? 0.50623 0.48227 0.53404 0.03231  -0.02628 -0.06937 182 TYR   A OH  
1409 N N   . GLY   A 183 ? 0.50056 0.41342 0.55984 0.05111  -0.01985 -0.04448 183 GLY   A N   
1410 C CA  . GLY   A 183 ? 0.54879 0.45441 0.61137 0.05492  -0.02036 -0.03637 183 GLY   A CA  
1411 C C   . GLY   A 183 ? 0.58723 0.49006 0.65928 0.05946  -0.01798 -0.03726 183 GLY   A C   
1412 O O   . GLY   A 183 ? 0.53739 0.44274 0.61363 0.05935  -0.01522 -0.04514 183 GLY   A O   
1413 N N   . PRO   A 184 ? 0.57947 0.47764 0.65505 0.06375  -0.01892 -0.02889 184 PRO   A N   
1414 C CA  . PRO   A 184 ? 0.63990 0.53512 0.72608 0.06924  -0.01643 -0.02822 184 PRO   A CA  
1415 C C   . PRO   A 184 ? 0.64124 0.54718 0.72771 0.07260  -0.01920 -0.02632 184 PRO   A C   
1416 O O   . PRO   A 184 ? 0.72633 0.63307 0.81742 0.07743  -0.02072 -0.01899 184 PRO   A O   
1417 C CB  . PRO   A 184 ? 0.59586 0.48151 0.68525 0.07207  -0.01640 -0.01877 184 PRO   A CB  
1418 C CG  . PRO   A 184 ? 0.58400 0.47345 0.66232 0.06935  -0.02120 -0.01246 184 PRO   A CG  
1419 C CD  . PRO   A 184 ? 0.56489 0.46041 0.63505 0.06385  -0.02202 -0.01947 184 PRO   A CD  
1420 N N   . PHE   A 185 ? 0.62744 0.54254 0.70920 0.06996  -0.01985 -0.03262 185 PHE   A N   
1421 C CA  . PHE   A 185 ? 0.60687 0.53281 0.68830 0.07198  -0.02211 -0.03152 185 PHE   A CA  
1422 C C   . PHE   A 185 ? 0.60971 0.53954 0.69757 0.07324  -0.01805 -0.04003 185 PHE   A C   
1423 O O   . PHE   A 185 ? 0.62240 0.54886 0.71103 0.07069  -0.01433 -0.04830 185 PHE   A O   
1424 C CB  . PHE   A 185 ? 0.59854 0.53217 0.66809 0.06782  -0.02612 -0.03056 185 PHE   A CB  
1425 C CG  . PHE   A 185 ? 0.60448 0.53396 0.66654 0.06584  -0.02924 -0.02389 185 PHE   A CG  
1426 C CD1 . PHE   A 185 ? 0.56298 0.49185 0.62541 0.06830  -0.03212 -0.01526 185 PHE   A CD1 
1427 C CD2 . PHE   A 185 ? 0.54669 0.47388 0.60138 0.06155  -0.02919 -0.02624 185 PHE   A CD2 
1428 C CE1 . PHE   A 185 ? 0.59949 0.52475 0.65418 0.06617  -0.03456 -0.00963 185 PHE   A CE1 
1429 C CE2 . PHE   A 185 ? 0.53947 0.46295 0.58748 0.05990  -0.03137 -0.02046 185 PHE   A CE2 
1430 C CZ  . PHE   A 185 ? 0.57911 0.50122 0.62668 0.06204  -0.03389 -0.01241 185 PHE   A CZ  
1431 N N   . VAL   A 186 ? 0.59635 0.53418 0.68883 0.07688  -0.01869 -0.03817 186 VAL   A N   
1432 C CA  . VAL   A 186 ? 0.57316 0.51626 0.67182 0.07854  -0.01467 -0.04565 186 VAL   A CA  
1433 C C   . VAL   A 186 ? 0.58739 0.54387 0.68116 0.07726  -0.01741 -0.04515 186 VAL   A C   
1434 O O   . VAL   A 186 ? 0.59308 0.55427 0.68311 0.07716  -0.02203 -0.03778 186 VAL   A O   
1435 C CB  . VAL   A 186 ? 0.58704 0.52611 0.69984 0.08545  -0.01100 -0.04414 186 VAL   A CB  
1436 C CG1 . VAL   A 186 ? 0.54306 0.46715 0.66090 0.08633  -0.00727 -0.04504 186 VAL   A CG1 
1437 C CG2 . VAL   A 186 ? 0.56117 0.50593 0.67760 0.08988  -0.01526 -0.03352 186 VAL   A CG2 
1438 N N   . ASP   A 187 ? 0.54634 0.50893 0.63980 0.07580  -0.01426 -0.05328 187 ASP   A N   
1439 C CA  . ASP   A 187 ? 0.55056 0.52557 0.63941 0.07411  -0.01587 -0.05347 187 ASP   A CA  
1440 C C   . ASP   A 187 ? 0.55852 0.54044 0.65796 0.07926  -0.01514 -0.05050 187 ASP   A C   
1441 O O   . ASP   A 187 ? 0.56802 0.55407 0.67458 0.08161  -0.01059 -0.05627 187 ASP   A O   
1442 C CB  . ASP   A 187 ? 0.54126 0.52084 0.62514 0.07050  -0.01267 -0.06275 187 ASP   A CB  
1443 C CG  . ASP   A 187 ? 0.57071 0.54539 0.66225 0.07214  -0.00669 -0.07138 187 ASP   A CG  
1444 O OD1 . ASP   A 187 ? 0.58493 0.55106 0.68604 0.07634  -0.00470 -0.06983 187 ASP   A OD1 
1445 O OD2 . ASP   A 187 ? 0.57314 0.55239 0.66084 0.06910  -0.00376 -0.07969 187 ASP   A OD2 
1446 N N   . ARG   A 188 ? 0.55975 0.54393 0.66027 0.08093  -0.01962 -0.04148 188 ARG   A N   
1447 C CA  . ARG   A 188 ? 0.57047 0.56298 0.68172 0.08594  -0.01988 -0.03724 188 ARG   A CA  
1448 C C   . ARG   A 188 ? 0.58432 0.58270 0.69105 0.08436  -0.02620 -0.02838 188 ARG   A C   
1449 O O   . ARG   A 188 ? 0.59827 0.58966 0.69894 0.08286  -0.02956 -0.02343 188 ARG   A O   
1450 C CB  . ARG   A 188 ? 0.58068 0.56574 0.70493 0.09285  -0.01676 -0.03565 188 ARG   A CB  
1451 C CG  . ARG   A 188 ? 0.62370 0.61800 0.76052 0.09918  -0.01726 -0.02993 188 ARG   A CG  
1452 C CD  . ARG   A 188 ? 0.64913 0.63403 0.79777 0.10642  -0.01478 -0.02595 188 ARG   A CD  
1453 N NE  . ARG   A 188 ? 0.65012 0.64343 0.80742 0.11189  -0.01845 -0.01576 188 ARG   A NE  
1454 C CZ  . ARG   A 188 ? 0.68319 0.67211 0.85323 0.11982  -0.01642 -0.01044 188 ARG   A CZ  
1455 N NH1 . ARG   A 188 ? 0.66650 0.64102 0.84244 0.12308  -0.01016 -0.01470 188 ARG   A NH1 
1456 N NH2 . ARG   A 188 ? 0.66203 0.66140 0.83919 0.12448  -0.02068 -0.00045 188 ARG   A NH2 
1457 N N   . GLN   A 189 ? 0.58988 0.60143 0.69941 0.08420  -0.02754 -0.02680 189 GLN   A N   
1458 C CA  . GLN   A 189 ? 0.57662 0.59525 0.68198 0.08172  -0.03338 -0.01941 189 GLN   A CA  
1459 C C   . GLN   A 189 ? 0.56587 0.58457 0.68005 0.08724  -0.03602 -0.01134 189 GLN   A C   
1460 O O   . GLN   A 189 ? 0.53300 0.56241 0.65815 0.09147  -0.03660 -0.00788 189 GLN   A O   
1461 C CB  . GLN   A 189 ? 0.57936 0.61255 0.68602 0.07933  -0.03361 -0.02053 189 GLN   A CB  
1462 C CG  . GLN   A 189 ? 0.54688 0.58752 0.64809 0.07509  -0.03935 -0.01429 189 GLN   A CG  
1463 C CD  . GLN   A 189 ? 0.54553 0.60072 0.64901 0.07213  -0.03912 -0.01558 189 GLN   A CD  
1464 O OE1 . GLN   A 189 ? 0.57283 0.63026 0.67534 0.07059  -0.03499 -0.02161 189 GLN   A OE1 
1465 N NE2 . GLN   A 189 ? 0.47742 0.54333 0.58378 0.07090  -0.04355 -0.00988 189 GLN   A NE2 
1466 N N   . THR   A 190 ? 0.59437 0.60155 0.70386 0.08732  -0.03757 -0.00785 190 THR   A N   
1467 C CA  . THR   A 190 ? 0.58835 0.59445 0.70403 0.09214  -0.04033 0.00090  190 THR   A CA  
1468 C C   . THR   A 190 ? 0.57274 0.57002 0.67648 0.08824  -0.04382 0.00505  190 THR   A C   
1469 O O   . THR   A 190 ? 0.55266 0.54166 0.64642 0.08358  -0.04263 0.00042  190 THR   A O   
1470 C CB  . THR   A 190 ? 0.60429 0.60280 0.73295 0.09971  -0.03544 0.00045  190 THR   A CB  
1471 O OG1 . THR   A 190 ? 0.57248 0.57250 0.70849 0.10529  -0.03828 0.01048  190 THR   A OG1 
1472 C CG2 . THR   A 190 ? 0.58444 0.56657 0.70808 0.09797  -0.03172 -0.00464 190 THR   A CG2 
1473 N N   . ALA   A 191 ? 0.57262 0.57281 0.67757 0.09029  -0.04813 0.01409  191 ALA   A N   
1474 C CA  . ALA   A 191 ? 0.56851 0.56191 0.66183 0.08651  -0.05149 0.01856  191 ALA   A CA  
1475 C C   . ALA   A 191 ? 0.57990 0.55718 0.67256 0.08795  -0.04782 0.01732  191 ALA   A C   
1476 O O   . ALA   A 191 ? 0.58750 0.55940 0.69061 0.09403  -0.04510 0.01975  191 ALA   A O   
1477 C CB  . ALA   A 191 ? 0.54585 0.54744 0.64094 0.08860  -0.05684 0.02870  191 ALA   A CB  
1478 N N   . GLN   A 192 ? 0.56556 0.53516 0.64650 0.08233  -0.04740 0.01357  192 GLN   A N   
1479 C CA  . GLN   A 192 ? 0.61042 0.56598 0.68974 0.08230  -0.04425 0.01221  192 GLN   A CA  
1480 C C   . GLN   A 192 ? 0.62760 0.57886 0.69376 0.07730  -0.04697 0.01523  192 GLN   A C   
1481 O O   . GLN   A 192 ? 0.59272 0.54941 0.64943 0.07259  -0.04960 0.01422  192 GLN   A O   
1482 C CB  . GLN   A 192 ? 0.57922 0.53002 0.65952 0.08074  -0.03938 0.00218  192 GLN   A CB  
1483 C CG  . GLN   A 192 ? 0.52044 0.47465 0.61305 0.08529  -0.03562 -0.00228 192 GLN   A CG  
1484 C CD  . GLN   A 192 ? 0.58255 0.53344 0.67424 0.08275  -0.03110 -0.01268 192 GLN   A CD  
1485 O OE1 . GLN   A 192 ? 0.61097 0.55199 0.70022 0.08077  -0.02869 -0.01595 192 GLN   A OE1 
1486 N NE2 . GLN   A 192 ? 0.56012 0.52020 0.65363 0.08243  -0.02994 -0.01790 192 GLN   A NE2 
1487 N N   . ALA   A 193 ? 0.60831 0.54925 0.67409 0.07829  -0.04574 0.01882  193 ALA   A N   
1488 C CA  . ALA   A 193 ? 0.62142 0.55769 0.67556 0.07409  -0.04753 0.02201  193 ALA   A CA  
1489 C C   . ALA   A 193 ? 0.63619 0.56154 0.68814 0.07176  -0.04347 0.01698  193 ALA   A C   
1490 O O   . ALA   A 193 ? 0.65368 0.57182 0.71414 0.07439  -0.03962 0.01497  193 ALA   A O   
1491 C CB  . ALA   A 193 ? 0.60711 0.54251 0.66154 0.07674  -0.05011 0.03226  193 ALA   A CB  
1492 N N   . ALA   A 194 ? 0.58294 0.50734 0.62391 0.06672  -0.04410 0.01479  194 ALA   A N   
1493 C CA  . ALA   A 194 ? 0.66028 0.57629 0.69869 0.06415  -0.04087 0.01107  194 ALA   A CA  
1494 C C   . ALA   A 194 ? 0.68187 0.59050 0.71742 0.06397  -0.04076 0.01781  194 ALA   A C   
1495 O O   . ALA   A 194 ? 0.68036 0.59138 0.71203 0.06467  -0.04384 0.02509  194 ALA   A O   
1496 C CB  . ALA   A 194 ? 0.60379 0.52268 0.63268 0.05961  -0.04120 0.00623  194 ALA   A CB  
1497 N N   . GLY   A 195 ? 0.67682 0.57715 0.71421 0.06263  -0.03710 0.01530  195 GLY   A N   
1498 C CA  . GLY   A 195 ? 0.70387 0.59703 0.73798 0.06168  -0.03627 0.02125  195 GLY   A CA  
1499 C C   . GLY   A 195 ? 0.71078 0.60663 0.73219 0.05799  -0.03845 0.02347  195 GLY   A C   
1500 O O   . GLY   A 195 ? 0.68618 0.58746 0.70158 0.05565  -0.03968 0.01921  195 GLY   A O   
1501 N N   . THR   A 196 ? 0.76465 0.65617 0.78178 0.05753  -0.03850 0.03043  196 THR   A N   
1502 C CA  . THR   A 196 ? 0.71311 0.60621 0.71787 0.05391  -0.03972 0.03229  196 THR   A CA  
1503 C C   . THR   A 196 ? 0.73761 0.62885 0.73944 0.05051  -0.03678 0.02577  196 THR   A C   
1504 O O   . THR   A 196 ? 0.77477 0.66094 0.78248 0.04997  -0.03337 0.02317  196 THR   A O   
1505 C CB  . THR   A 196 ? 0.72305 0.61180 0.72392 0.05398  -0.03965 0.04093  196 THR   A CB  
1506 O OG1 . THR   A 196 ? 0.74873 0.63729 0.73803 0.04996  -0.03913 0.04109  196 THR   A OG1 
1507 C CG2 . THR   A 196 ? 0.73900 0.61851 0.74861 0.05534  -0.03561 0.04260  196 THR   A CG2 
1508 N N   . ASP   A 197 ? 0.74428 0.63996 0.73752 0.04819  -0.03797 0.02312  197 ASP   A N   
1509 C CA  . ASP   A 197 ? 0.68162 0.57737 0.67279 0.04592  -0.03554 0.01732  197 ASP   A CA  
1510 C C   . ASP   A 197 ? 0.69220 0.58400 0.67703 0.04352  -0.03313 0.01972  197 ASP   A C   
1511 O O   . ASP   A 197 ? 0.73493 0.62495 0.71327 0.04287  -0.03382 0.02531  197 ASP   A O   
1512 C CB  . ASP   A 197 ? 0.63288 0.53432 0.61858 0.04511  -0.03719 0.01365  197 ASP   A CB  
1513 C CG  . ASP   A 197 ? 0.64985 0.55331 0.63774 0.04449  -0.03518 0.00738  197 ASP   A CG  
1514 O OD1 . ASP   A 197 ? 0.65286 0.55554 0.64882 0.04497  -0.03351 0.00441  197 ASP   A OD1 
1515 O OD2 . ASP   A 197 ? 0.64074 0.54662 0.62225 0.04342  -0.03516 0.00550  197 ASP   A OD2 
1516 N N   . THR   A 198 ? 0.66754 0.55904 0.65437 0.04212  -0.03024 0.01542  198 THR   A N   
1517 C CA  . THR   A 198 ? 0.66811 0.55710 0.65050 0.03994  -0.02727 0.01684  198 THR   A CA  
1518 C C   . THR   A 198 ? 0.66104 0.55410 0.63971 0.03913  -0.02611 0.01240  198 THR   A C   
1519 O O   . THR   A 198 ? 0.63874 0.53614 0.61942 0.04007  -0.02735 0.00819  198 THR   A O   
1520 C CB  . THR   A 198 ? 0.63845 0.52344 0.62894 0.03896  -0.02419 0.01691  198 THR   A CB  
1521 O OG1 . THR   A 198 ? 0.64923 0.53746 0.64760 0.03866  -0.02337 0.01031  198 THR   A OG1 
1522 C CG2 . THR   A 198 ? 0.67149 0.55112 0.66655 0.04047  -0.02475 0.02189  198 THR   A CG2 
1523 N N   . THR   A 199 ? 0.61305 0.50482 0.58639 0.03766  -0.02338 0.01378  199 THR   A N   
1524 C CA  . THR   A 199 ? 0.59689 0.49206 0.56721 0.03763  -0.02157 0.01060  199 THR   A CA  
1525 C C   . THR   A 199 ? 0.59894 0.49766 0.57770 0.03711  -0.01930 0.00748  199 THR   A C   
1526 O O   . THR   A 199 ? 0.59559 0.49221 0.57823 0.03545  -0.01709 0.00897  199 THR   A O   
1527 C CB  . THR   A 199 ? 0.62350 0.51585 0.58390 0.03659  -0.01921 0.01328  199 THR   A CB  
1528 O OG1 . THR   A 199 ? 0.63544 0.52591 0.58732 0.03629  -0.02158 0.01503  199 THR   A OG1 
1529 C CG2 . THR   A 199 ? 0.53991 0.43518 0.49888 0.03738  -0.01641 0.01042  199 THR   A CG2 
1530 N N   . ILE   A 200 ? 0.52734 0.43205 0.50885 0.03819  -0.01984 0.00335  200 ILE   A N   
1531 C CA  . ILE   A 200 ? 0.53496 0.44571 0.52450 0.03740  -0.01844 -0.00011 200 ILE   A CA  
1532 C C   . ILE   A 200 ? 0.51151 0.42420 0.49895 0.03715  -0.01501 0.00133  200 ILE   A C   
1533 O O   . ILE   A 200 ? 0.52800 0.44321 0.51096 0.03914  -0.01425 0.00137  200 ILE   A O   
1534 C CB  . ILE   A 200 ? 0.53604 0.45394 0.52841 0.03876  -0.02048 -0.00436 200 ILE   A CB  
1535 C CG1 . ILE   A 200 ? 0.56143 0.47721 0.55456 0.03941  -0.02338 -0.00549 200 ILE   A CG1 
1536 C CG2 . ILE   A 200 ? 0.50466 0.43009 0.50565 0.03713  -0.01968 -0.00829 200 ILE   A CG2 
1537 C CD1 . ILE   A 200 ? 0.54991 0.47051 0.54047 0.04120  -0.02528 -0.00757 200 ILE   A CD1 
1538 N N   . THR   A 201 ? 0.48342 0.39473 0.47463 0.03479  -0.01245 0.00263  201 THR   A N   
1539 C CA  . THR   A 201 ? 0.53473 0.44743 0.52382 0.03444  -0.00861 0.00456  201 THR   A CA  
1540 C C   . THR   A 201 ? 0.49436 0.41727 0.48827 0.03574  -0.00764 0.00182  201 THR   A C   
1541 O O   . THR   A 201 ? 0.44718 0.37177 0.43712 0.03786  -0.00520 0.00321  201 THR   A O   
1542 C CB  . THR   A 201 ? 0.53591 0.44534 0.52877 0.03115  -0.00592 0.00668  201 THR   A CB  
1543 O OG1 . THR   A 201 ? 0.54129 0.44178 0.52950 0.03064  -0.00702 0.01039  201 THR   A OG1 
1544 C CG2 . THR   A 201 ? 0.52830 0.43954 0.51876 0.03070  -0.00144 0.00879  201 THR   A CG2 
1545 N N   . VAL   A 202 ? 0.40320 0.33339 0.40570 0.03457  -0.00936 -0.00204 202 VAL   A N   
1546 C CA  . VAL   A 202 ? 0.46157 0.40382 0.46925 0.03566  -0.00902 -0.00414 202 VAL   A CA  
1547 C C   . VAL   A 202 ? 0.52491 0.46906 0.52677 0.04016  -0.01006 -0.00325 202 VAL   A C   
1548 O O   . VAL   A 202 ? 0.47108 0.42113 0.47322 0.04282  -0.00802 -0.00188 202 VAL   A O   
1549 C CB  . VAL   A 202 ? 0.51678 0.46685 0.53348 0.03283  -0.01122 -0.00910 202 VAL   A CB  
1550 C CG1 . VAL   A 202 ? 0.44216 0.40708 0.46399 0.03390  -0.01159 -0.01082 202 VAL   A CG1 
1551 C CG2 . VAL   A 202 ? 0.53231 0.47873 0.55491 0.02805  -0.00935 -0.01003 202 VAL   A CG2 
1552 N N   . ASN   A 203 ? 0.48624 0.42534 0.48328 0.04119  -0.01287 -0.00377 203 ASN   A N   
1553 C CA  . ASN   A 203 ? 0.41089 0.35041 0.40218 0.04488  -0.01350 -0.00281 203 ASN   A CA  
1554 C C   . ASN   A 203 ? 0.42055 0.35301 0.40397 0.04675  -0.01008 0.00055  203 ASN   A C   
1555 O O   . ASN   A 203 ? 0.61319 0.54708 0.59379 0.05014  -0.00861 0.00171  203 ASN   A O   
1556 C CB  . ASN   A 203 ? 0.53918 0.47479 0.52735 0.04478  -0.01688 -0.00418 203 ASN   A CB  
1557 C CG  . ASN   A 203 ? 0.50962 0.45243 0.50493 0.04328  -0.01964 -0.00829 203 ASN   A CG  
1558 O OD1 . ASN   A 203 ? 0.52073 0.47224 0.52291 0.04204  -0.01939 -0.01041 203 ASN   A OD1 
1559 N ND2 . ASN   A 203 ? 0.51700 0.45681 0.51082 0.04309  -0.02210 -0.00978 203 ASN   A ND2 
1560 N N   . VAL   A 204 ? 0.53126 0.45591 0.51085 0.04458  -0.00845 0.00219  204 VAL   A N   
1561 C CA  . VAL   A 204 ? 0.47153 0.38976 0.44298 0.04563  -0.00469 0.00457  204 VAL   A CA  
1562 C C   . VAL   A 204 ? 0.42142 0.34566 0.39691 0.04756  -0.00044 0.00537  204 VAL   A C   
1563 O O   . VAL   A 204 ? 0.58383 0.50654 0.55525 0.05077  0.00271  0.00637  204 VAL   A O   
1564 C CB  . VAL   A 204 ? 0.50426 0.41428 0.47019 0.04251  -0.00423 0.00641  204 VAL   A CB  
1565 C CG1 . VAL   A 204 ? 0.47131 0.37543 0.42804 0.04294  0.00008  0.00806  204 VAL   A CG1 
1566 C CG2 . VAL   A 204 ? 0.47094 0.37643 0.43353 0.04134  -0.00852 0.00625  204 VAL   A CG2 
1567 N N   . LEU   A 205 ? 0.50364 0.43484 0.48776 0.04560  0.00007  0.00488  205 LEU   A N   
1568 C CA  . LEU   A 205 ? 0.49956 0.43866 0.48910 0.04722  0.00403  0.00574  205 LEU   A CA  
1569 C C   . LEU   A 205 ? 0.48328 0.43197 0.47715 0.05163  0.00329  0.00552  205 LEU   A C   
1570 O O   . LEU   A 205 ? 0.50733 0.45919 0.50187 0.05543  0.00715  0.00740  205 LEU   A O   
1571 C CB  . LEU   A 205 ? 0.50206 0.44743 0.50068 0.04318  0.00439  0.00487  205 LEU   A CB  
1572 C CG  . LEU   A 205 ? 0.48365 0.42034 0.47878 0.03928  0.00655  0.00655  205 LEU   A CG  
1573 C CD1 . LEU   A 205 ? 0.49104 0.43223 0.49571 0.03465  0.00614  0.00519  205 LEU   A CD1 
1574 C CD2 . LEU   A 205 ? 0.48744 0.42177 0.47776 0.04050  0.01224  0.00905  205 LEU   A CD2 
1575 N N   . ALA   A 206 ? 0.50364 0.45730 0.50052 0.05147  -0.00135 0.00355  206 ALA   A N   
1576 C CA  . ALA   A 206 ? 0.47249 0.43553 0.47233 0.05575  -0.00243 0.00417  206 ALA   A CA  
1577 C C   . ALA   A 206 ? 0.48374 0.43826 0.47504 0.06016  -0.00028 0.00660  206 ALA   A C   
1578 O O   . ALA   A 206 ? 0.50745 0.46701 0.50053 0.06507  0.00189  0.00904  206 ALA   A O   
1579 C CB  . ALA   A 206 ? 0.45033 0.41991 0.45364 0.05401  -0.00766 0.00123  206 ALA   A CB  
1580 N N   . TRP   A 207 ? 0.48106 0.42276 0.46338 0.05841  -0.00069 0.00608  207 TRP   A N   
1581 C CA  . TRP   A 207 ? 0.51635 0.44850 0.48996 0.06129  0.00189  0.00759  207 TRP   A CA  
1582 C C   . TRP   A 207 ? 0.52081 0.44876 0.49196 0.06359  0.00814  0.00930  207 TRP   A C   
1583 O O   . TRP   A 207 ? 0.55373 0.47740 0.52138 0.06770  0.01165  0.01084  207 TRP   A O   
1584 C CB  . TRP   A 207 ? 0.53595 0.45714 0.50104 0.05782  -0.00024 0.00621  207 TRP   A CB  
1585 C CG  . TRP   A 207 ? 0.53597 0.44712 0.49185 0.05931  0.00213  0.00680  207 TRP   A CG  
1586 C CD1 . TRP   A 207 ? 0.55791 0.46874 0.51248 0.06211  0.00181  0.00756  207 TRP   A CD1 
1587 C CD2 . TRP   A 207 ? 0.55353 0.45326 0.49983 0.05742  0.00539  0.00644  207 TRP   A CD2 
1588 N NE1 . TRP   A 207 ? 0.58563 0.48464 0.53092 0.06190  0.00500  0.00747  207 TRP   A NE1 
1589 C CE2 . TRP   A 207 ? 0.55706 0.44947 0.49695 0.05885  0.00712  0.00639  207 TRP   A CE2 
1590 C CE3 . TRP   A 207 ? 0.57725 0.47245 0.51934 0.05430  0.00718  0.00616  207 TRP   A CE3 
1591 C CZ2 . TRP   A 207 ? 0.58405 0.46485 0.51360 0.05679  0.01054  0.00519  207 TRP   A CZ2 
1592 C CZ3 . TRP   A 207 ? 0.61515 0.49982 0.54642 0.05256  0.01027  0.00534  207 TRP   A CZ3 
1593 C CH2 . TRP   A 207 ? 0.60512 0.48271 0.53027 0.05357  0.01191  0.00443  207 TRP   A CH2 
1594 N N   . LEU   A 208 ? 0.52874 0.45733 0.50171 0.06101  0.01014  0.00906  208 LEU   A N   
1595 C CA  . LEU   A 208 ? 0.54666 0.47282 0.51811 0.06316  0.01662  0.01038  208 LEU   A CA  
1596 C C   . LEU   A 208 ? 0.53574 0.47389 0.51688 0.06838  0.01898  0.01239  208 LEU   A C   
1597 O O   . LEU   A 208 ? 0.54824 0.48378 0.52813 0.07269  0.02474  0.01396  208 LEU   A O   
1598 C CB  . LEU   A 208 ? 0.53674 0.46133 0.50759 0.05866  0.01818  0.01001  208 LEU   A CB  
1599 C CG  . LEU   A 208 ? 0.53649 0.44886 0.49616 0.05441  0.01748  0.00928  208 LEU   A CG  
1600 C CD1 . LEU   A 208 ? 0.58166 0.49313 0.54053 0.05081  0.02014  0.01011  208 LEU   A CD1 
1601 C CD2 . LEU   A 208 ? 0.56812 0.46979 0.51694 0.05607  0.02073  0.00872  208 LEU   A CD2 
1602 N N   . TYR   A 209 ? 0.51481 0.46662 0.50580 0.06808  0.01478  0.01228  209 TYR   A N   
1603 C CA  . TYR   A 209 ? 0.53308 0.49894 0.53371 0.07310  0.01600  0.01467  209 TYR   A CA  
1604 C C   . TYR   A 209 ? 0.55675 0.52081 0.55481 0.07921  0.01647  0.01730  209 TYR   A C   
1605 O O   . TYR   A 209 ? 0.56084 0.52829 0.56227 0.08529  0.02089  0.02054  209 TYR   A O   
1606 C CB  . TYR   A 209 ? 0.51822 0.49985 0.52909 0.07013  0.01092  0.01321  209 TYR   A CB  
1607 C CG  . TYR   A 209 ? 0.53702 0.52488 0.55467 0.06589  0.01254  0.01197  209 TYR   A CG  
1608 C CD1 . TYR   A 209 ? 0.53992 0.53631 0.56429 0.06878  0.01733  0.01414  209 TYR   A CD1 
1609 C CD2 . TYR   A 209 ? 0.50632 0.49134 0.52412 0.05910  0.00974  0.00887  209 TYR   A CD2 
1610 C CE1 . TYR   A 209 ? 0.53303 0.53542 0.56382 0.06436  0.01918  0.01309  209 TYR   A CE1 
1611 C CE2 . TYR   A 209 ? 0.51998 0.50964 0.54394 0.05481  0.01172  0.00805  209 TYR   A CE2 
1612 C CZ  . TYR   A 209 ? 0.53861 0.53718 0.56891 0.05714  0.01639  0.01008  209 TYR   A CZ  
1613 O OH  . TYR   A 209 ? 0.54227 0.54581 0.57895 0.05235  0.01871  0.00933  209 TYR   A OH  
1614 N N   . ALA   A 210 ? 0.51787 0.47658 0.51040 0.07790  0.01233  0.01630  210 ALA   A N   
1615 C CA  . ALA   A 210 ? 0.56350 0.51754 0.55199 0.08299  0.01344  0.01902  210 ALA   A CA  
1616 C C   . ALA   A 210 ? 0.56857 0.50755 0.54937 0.08555  0.02034  0.01983  210 ALA   A C   
1617 O O   . ALA   A 210 ? 0.57601 0.51255 0.55672 0.09165  0.02418  0.02314  210 ALA   A O   
1618 C CB  . ALA   A 210 ? 0.53305 0.48272 0.51611 0.07994  0.00835  0.01725  210 ALA   A CB  
1619 N N   . ALA   A 211 ? 0.53188 0.46053 0.50598 0.08092  0.02226  0.01687  211 ALA   A N   
1620 C CA  . ALA   A 211 ? 0.58205 0.49685 0.54809 0.08232  0.02919  0.01651  211 ALA   A CA  
1621 C C   . ALA   A 211 ? 0.63475 0.55485 0.60741 0.08814  0.03559  0.01902  211 ALA   A C   
1622 O O   . ALA   A 211 ? 0.66741 0.58038 0.63799 0.09352  0.04136  0.02077  211 ALA   A O   
1623 C CB  . ALA   A 211 ? 0.58426 0.48996 0.54191 0.07570  0.02930  0.01307  211 ALA   A CB  
1624 N N   . VAL   A 212 ? 0.61036 0.54295 0.59164 0.08716  0.03506  0.01925  212 VAL   A N   
1625 C CA  . VAL   A 212 ? 0.62952 0.56978 0.61876 0.09259  0.04102  0.02173  212 VAL   A CA  
1626 C C   . VAL   A 212 ? 0.63192 0.58178 0.62931 0.10045  0.04095  0.02637  212 VAL   A C   
1627 O O   . VAL   A 212 ? 0.67287 0.62147 0.67297 0.10737  0.04751  0.02925  212 VAL   A O   
1628 C CB  . VAL   A 212 ? 0.58420 0.53755 0.58187 0.08883  0.03971  0.02096  212 VAL   A CB  
1629 C CG1 . VAL   A 212 ? 0.63899 0.60613 0.64849 0.09487  0.04424  0.02418  212 VAL   A CG1 
1630 C CG2 . VAL   A 212 ? 0.60577 0.54862 0.59503 0.08257  0.04197  0.01783  212 VAL   A CG2 
1631 N N   . ILE   A 213 ? 0.59729 0.55704 0.59862 0.09972  0.03377  0.02738  213 ILE   A N   
1632 C CA  . ILE   A 213 ? 0.58195 0.55253 0.59041 0.10692  0.03280  0.03250  213 ILE   A CA  
1633 C C   . ILE   A 213 ? 0.63063 0.58611 0.63221 0.11267  0.03801  0.03519  213 ILE   A C   
1634 O O   . ILE   A 213 ? 0.66505 0.62500 0.67252 0.12096  0.04189  0.04044  213 ILE   A O   
1635 C CB  . ILE   A 213 ? 0.58944 0.57141 0.60047 0.10375  0.02412  0.03211  213 ILE   A CB  
1636 C CG1 . ILE   A 213 ? 0.54746 0.55001 0.56999 0.10122  0.02036  0.03134  213 ILE   A CG1 
1637 C CG2 . ILE   A 213 ? 0.55153 0.53672 0.56315 0.11012  0.02299  0.03722  213 ILE   A CG2 
1638 C CD1 . ILE   A 213 ? 0.57365 0.58329 0.59652 0.09477  0.01255  0.02782  213 ILE   A CD1 
1639 N N   . ASN   A 214 ? 0.66506 0.60243 0.65447 0.10835  0.03851  0.03176  214 ASN   A N   
1640 C CA  . ASN   A 214 ? 0.67025 0.59156 0.65222 0.11214  0.04341  0.03333  214 ASN   A CA  
1641 C C   . ASN   A 214 ? 0.68585 0.59124 0.66133 0.11267  0.05224  0.03081  214 ASN   A C   
1642 O O   . ASN   A 214 ? 0.69221 0.58036 0.65851 0.11265  0.05635  0.02962  214 ASN   A O   
1643 C CB  . ASN   A 214 ? 0.64845 0.56077 0.62136 0.10675  0.03859  0.03099  214 ASN   A CB  
1644 C CG  . ASN   A 214 ? 0.75370 0.67787 0.73143 0.10899  0.03264  0.03482  214 ASN   A CG  
1645 O OD1 . ASN   A 214 ? 0.80625 0.72844 0.78463 0.11508  0.03501  0.03978  214 ASN   A OD1 
1646 N ND2 . ASN   A 214 ? 0.69627 0.63256 0.67719 0.10405  0.02523  0.03260  214 ASN   A ND2 
1647 N N   . GLY   A 215 ? 0.65768 0.56848 0.63741 0.11261  0.05555  0.02959  215 GLY   A N   
1648 C CA  . GLY   A 215 ? 0.70139 0.59932 0.67623 0.11446  0.06498  0.02763  215 GLY   A CA  
1649 C C   . GLY   A 215 ? 0.71952 0.60479 0.68221 0.10616  0.06621  0.02132  215 GLY   A C   
1650 O O   . GLY   A 215 ? 0.74531 0.62071 0.70312 0.10693  0.07429  0.01894  215 GLY   A O   
1651 N N   . ASP   A 216 ? 0.70461 0.59013 0.66215 0.09848  0.05874  0.01865  216 ASP   A N   
1652 C CA  . ASP   A 216 ? 0.73267 0.60823 0.67890 0.09067  0.05901  0.01361  216 ASP   A CA  
1653 C C   . ASP   A 216 ? 0.73290 0.61897 0.68406 0.08802  0.05858  0.01324  216 ASP   A C   
1654 O O   . ASP   A 216 ? 0.70925 0.60766 0.66744 0.08568  0.05196  0.01438  216 ASP   A O   
1655 C CB  . ASP   A 216 ? 0.74700 0.61859 0.68642 0.08435  0.05146  0.01169  216 ASP   A CB  
1656 C CG  . ASP   A 216 ? 0.71473 0.56886 0.64154 0.08182  0.05450  0.00856  216 ASP   A CG  
1657 O OD1 . ASP   A 216 ? 0.72708 0.57045 0.64673 0.08154  0.06191  0.00581  216 ASP   A OD1 
1658 O OD2 . ASP   A 216 ? 0.68269 0.53415 0.60671 0.07968  0.04972  0.00847  216 ASP   A OD2 
1659 N N   . ARG   A 217 ? 0.73208 0.61283 0.67932 0.08803  0.06614  0.01139  217 ARG   A N   
1660 C CA  . ARG   A 217 ? 0.69681 0.58838 0.65030 0.08668  0.06739  0.01190  217 ARG   A CA  
1661 C C   . ARG   A 217 ? 0.67010 0.55266 0.61247 0.08139  0.07215  0.00836  217 ARG   A C   
1662 O O   . ARG   A 217 ? 0.63838 0.52844 0.58509 0.08063  0.07516  0.00889  217 ARG   A O   
1663 C CB  . ARG   A 217 ? 0.76602 0.66803 0.73203 0.09466  0.07299  0.01517  217 ARG   A CB  
1664 C CG  . ARG   A 217 ? 0.97174 0.86251 0.93347 0.09987  0.08344  0.01410  217 ARG   A CG  
1665 C CD  . ARG   A 217 ? 0.94004 0.83636 0.91253 0.10964  0.08566  0.01874  217 ARG   A CD  
1666 N NE  . ARG   A 217 ? 0.94895 0.86700 0.93704 0.11241  0.08152  0.02297  217 ARG   A NE  
1667 C CZ  . ARG   A 217 ? 0.93257 0.86186 0.92931 0.11591  0.07540  0.02707  217 ARG   A CZ  
1668 N NH1 . ARG   A 217 ? 0.95856 0.87941 0.95047 0.11766  0.07289  0.02818  217 ARG   A NH1 
1669 N NH2 . ARG   A 217 ? 0.95139 0.90144 0.96168 0.11712  0.07172  0.02997  217 ARG   A NH2 
1670 N N   . TRP   A 218 ? 0.67671 0.54436 0.60480 0.07738  0.07304  0.00478  218 TRP   A N   
1671 C CA  . TRP   A 218 ? 0.66033 0.52018 0.57664 0.07231  0.07781  0.00134  218 TRP   A CA  
1672 C C   . TRP   A 218 ? 0.65546 0.52197 0.57060 0.06570  0.07242  0.00222  218 TRP   A C   
1673 O O   . TRP   A 218 ? 0.67531 0.53939 0.58314 0.06208  0.07661  0.00080  218 TRP   A O   
1674 C CB  . TRP   A 218 ? 0.66930 0.51298 0.57054 0.06880  0.07928  -0.00302 218 TRP   A CB  
1675 C CG  . TRP   A 218 ? 0.66115 0.50369 0.55861 0.06407  0.06997  -0.00299 218 TRP   A CG  
1676 C CD1 . TRP   A 218 ? 0.65243 0.49296 0.55265 0.06624  0.06612  -0.00214 218 TRP   A CD1 
1677 C CD2 . TRP   A 218 ? 0.65534 0.49922 0.54601 0.05669  0.06362  -0.00343 218 TRP   A CD2 
1678 N NE1 . TRP   A 218 ? 0.67454 0.51546 0.57046 0.06055  0.05793  -0.00252 218 TRP   A NE1 
1679 C CE2 . TRP   A 218 ? 0.70722 0.55021 0.59757 0.05494  0.05617  -0.00314 218 TRP   A CE2 
1680 C CE3 . TRP   A 218 ? 0.62627 0.47225 0.51122 0.05166  0.06371  -0.00349 218 TRP   A CE3 
1681 C CZ2 . TRP   A 218 ? 0.72957 0.57405 0.61500 0.04886  0.04890  -0.00299 218 TRP   A CZ2 
1682 C CZ3 . TRP   A 218 ? 0.70020 0.54724 0.57984 0.04569  0.05629  -0.00276 218 TRP   A CZ3 
1683 C CH2 . TRP   A 218 ? 0.74704 0.59348 0.62735 0.04457  0.04899  -0.00256 218 TRP   A CH2 
1684 N N   . PHE   A 219 ? 0.65041 0.52481 0.57237 0.06411  0.06374  0.00460  219 PHE   A N   
1685 C CA  . PHE   A 219 ? 0.64234 0.52105 0.56332 0.05803  0.05856  0.00573  219 PHE   A CA  
1686 C C   . PHE   A 219 ? 0.63914 0.53069 0.57236 0.05863  0.05934  0.00841  219 PHE   A C   
1687 O O   . PHE   A 219 ? 0.63006 0.52403 0.56252 0.05359  0.05685  0.00964  219 PHE   A O   
1688 C CB  . PHE   A 219 ? 0.61226 0.49145 0.53389 0.05558  0.04928  0.00630  219 PHE   A CB  
1689 C CG  . PHE   A 219 ? 0.59008 0.47633 0.52294 0.06040  0.04590  0.00760  219 PHE   A CG  
1690 C CD1 . PHE   A 219 ? 0.56716 0.46647 0.51312 0.06138  0.04279  0.00973  219 PHE   A CD1 
1691 C CD2 . PHE   A 219 ? 0.61727 0.49731 0.54720 0.06351  0.04601  0.00666  219 PHE   A CD2 
1692 C CE1 . PHE   A 219 ? 0.57653 0.48370 0.53188 0.06544  0.03944  0.01086  219 PHE   A CE1 
1693 C CE2 . PHE   A 219 ? 0.63697 0.52413 0.57642 0.06798  0.04292  0.00852  219 PHE   A CE2 
1694 C CZ  . PHE   A 219 ? 0.58057 0.48189 0.53246 0.06898  0.03944  0.01060  219 PHE   A CZ  
1695 N N   . LEU   A 220 ? 0.61085 0.51096 0.55560 0.06452  0.06279  0.00962  220 LEU   A N   
1696 C CA  . LEU   A 220 ? 0.61887 0.53285 0.57625 0.06468  0.06367  0.01182  220 LEU   A CA  
1697 C C   . LEU   A 220 ? 0.65846 0.57106 0.61151 0.06270  0.07136  0.01147  220 LEU   A C   
1698 O O   . LEU   A 220 ? 0.69643 0.60436 0.64565 0.06637  0.07914  0.01008  220 LEU   A O   
1699 C CB  . LEU   A 220 ? 0.62945 0.55466 0.60042 0.07187  0.06488  0.01353  220 LEU   A CB  
1700 C CG  . LEU   A 220 ? 0.66809 0.59480 0.64221 0.07426  0.05798  0.01413  220 LEU   A CG  
1701 C CD1 . LEU   A 220 ? 0.67139 0.60563 0.65493 0.08257  0.06099  0.01637  220 LEU   A CD1 
1702 C CD2 . LEU   A 220 ? 0.59982 0.53626 0.58134 0.06992  0.05003  0.01463  220 LEU   A CD2 
1703 N N   . ASN   A 221 ? 0.68424 0.60038 0.63780 0.05692  0.06975  0.01276  221 ASN   A N   
1704 C CA  . ASN   A 221 ? 0.73628 0.65240 0.68598 0.05440  0.07692  0.01305  221 ASN   A CA  
1705 C C   . ASN   A 221 ? 0.73674 0.66819 0.70220 0.05548  0.07967  0.01508  221 ASN   A C   
1706 O O   . ASN   A 221 ? 0.76798 0.71033 0.74672 0.05744  0.07531  0.01609  221 ASN   A O   
1707 C CB  . ASN   A 221 ? 0.72051 0.62955 0.65884 0.04704  0.07416  0.01391  221 ASN   A CB  
1708 C CG  . ASN   A 221 ? 0.75472 0.66808 0.69997 0.04339  0.06593  0.01616  221 ASN   A CG  
1709 O OD1 . ASN   A 221 ? 0.78278 0.70697 0.74235 0.04453  0.06392  0.01698  221 ASN   A OD1 
1710 N ND2 . ASN   A 221 ? 0.74804 0.65330 0.68326 0.03893  0.06126  0.01703  221 ASN   A ND2 
1711 N N   . ARG   A 222 ? 0.78046 0.71359 0.74418 0.05373  0.08710  0.01551  222 ARG   A N   
1712 C CA  . ARG   A 222 ? 0.77574 0.72391 0.75411 0.05401  0.09079  0.01731  222 ARG   A CA  
1713 C C   . ARG   A 222 ? 0.76346 0.71683 0.74696 0.04684  0.08644  0.01948  222 ARG   A C   
1714 O O   . ARG   A 222 ? 0.72593 0.69258 0.72262 0.04577  0.08868  0.02074  222 ARG   A O   
1715 C CB  . ARG   A 222 ? 0.82733 0.77531 0.80197 0.05522  0.10159  0.01673  222 ARG   A CB  
1716 C CG  . ARG   A 222 ? 0.83094 0.76867 0.78981 0.04861  0.10423  0.01677  222 ARG   A CG  
1717 C CD  . ARG   A 222 ? 0.91262 0.84761 0.86444 0.05046  0.11530  0.01489  222 ARG   A CD  
1718 N NE  . ARG   A 222 ? 0.91053 0.83615 0.84542 0.04396  0.11750  0.01494  222 ARG   A NE  
1719 C CZ  . ARG   A 222 ? 0.88000 0.79207 0.79753 0.04227  0.11634  0.01248  222 ARG   A CZ  
1720 N NH1 . ARG   A 222 ? 0.88069 0.78554 0.79529 0.04625  0.11342  0.00953  222 ARG   A NH1 
1721 N NH2 . ARG   A 222 ? 0.89224 0.79847 0.79489 0.03611  0.11813  0.01320  222 ARG   A NH2 
1722 N N   . PHE   A 223 ? 0.75319 0.69667 0.72732 0.04195  0.08060  0.02001  223 PHE   A N   
1723 C CA  . PHE   A 223 ? 0.72231 0.66760 0.69983 0.03520  0.07760  0.02244  223 PHE   A CA  
1724 C C   . PHE   A 223 ? 0.69260 0.64534 0.68294 0.03456  0.07013  0.02202  223 PHE   A C   
1725 O O   . PHE   A 223 ? 0.70060 0.65510 0.69402 0.03887  0.06573  0.02021  223 PHE   A O   
1726 C CB  . PHE   A 223 ? 0.70879 0.64036 0.67067 0.03072  0.07505  0.02398  223 PHE   A CB  
1727 C CG  . PHE   A 223 ? 0.76476 0.68856 0.71150 0.03060  0.08147  0.02370  223 PHE   A CG  
1728 C CD1 . PHE   A 223 ? 0.75700 0.68559 0.70445 0.02974  0.09016  0.02445  223 PHE   A CD1 
1729 C CD2 . PHE   A 223 ? 0.78018 0.69252 0.71184 0.03084  0.07902  0.02230  223 PHE   A CD2 
1730 C CE1 . PHE   A 223 ? 0.80318 0.72473 0.73582 0.02927  0.09650  0.02352  223 PHE   A CE1 
1731 C CE2 . PHE   A 223 ? 0.81461 0.72021 0.73149 0.02992  0.08497  0.02120  223 PHE   A CE2 
1732 C CZ  . PHE   A 223 ? 0.83945 0.74938 0.75643 0.02918  0.09383  0.02167  223 PHE   A CZ  
1733 N N   . THR   A 224 ? 0.66386 0.62068 0.66133 0.02874  0.06918  0.02362  224 THR   A N   
1734 C CA  . THR   A 224 ? 0.66970 0.63018 0.67651 0.02604  0.06222  0.02277  224 THR   A CA  
1735 C C   . THR   A 224 ? 0.67325 0.62306 0.67399 0.01996  0.06012  0.02525  224 THR   A C   
1736 O O   . THR   A 224 ? 0.71343 0.65561 0.70405 0.01768  0.06411  0.02822  224 THR   A O   
1737 C CB  . THR   A 224 ? 0.67108 0.64836 0.69538 0.02443  0.06344  0.02177  224 THR   A CB  
1738 O OG1 . THR   A 224 ? 0.66151 0.64290 0.69387 0.02290  0.05627  0.01947  224 THR   A OG1 
1739 C CG2 . THR   A 224 ? 0.66699 0.64556 0.69449 0.01773  0.06846  0.02407  224 THR   A CG2 
1740 N N   . THR   A 225 ? 0.67046 0.61989 0.67738 0.01751  0.05405  0.02420  225 THR   A N   
1741 C CA  . THR   A 225 ? 0.66231 0.60177 0.66588 0.01235  0.05217  0.02689  225 THR   A CA  
1742 C C   . THR   A 225 ? 0.61849 0.56352 0.63594 0.00828  0.04924  0.02470  225 THR   A C   
1743 O O   . THR   A 225 ? 0.57971 0.53651 0.60765 0.00954  0.04735  0.02083  225 THR   A O   
1744 C CB  . THR   A 225 ? 0.66751 0.59460 0.65878 0.01440  0.04702  0.02784  225 THR   A CB  
1745 O OG1 . THR   A 225 ? 0.64026 0.55804 0.62847 0.01011  0.04594  0.03172  225 THR   A OG1 
1746 C CG2 . THR   A 225 ? 0.62455 0.55423 0.62060 0.01749  0.04049  0.02389  225 THR   A CG2 
1747 N N   . THR   A 226 ? 0.61024 0.54677 0.62754 0.00324  0.04911  0.02730  226 THR   A N   
1748 C CA  . THR   A 226 ? 0.62750 0.56543 0.65616 -0.00098 0.04623  0.02463  226 THR   A CA  
1749 C C   . THR   A 226 ? 0.62711 0.55652 0.65184 0.00135  0.03953  0.02333  226 THR   A C   
1750 O O   . THR   A 226 ? 0.63801 0.55862 0.65092 0.00485  0.03749  0.02596  226 THR   A O   
1751 C CB  . THR   A 226 ? 0.68389 0.61615 0.71593 -0.00776 0.05058  0.02814  226 THR   A CB  
1752 O OG1 . THR   A 226 ? 0.66132 0.57847 0.68188 -0.00745 0.05000  0.03370  226 THR   A OG1 
1753 C CG2 . THR   A 226 ? 0.62025 0.56080 0.65495 -0.01009 0.05782  0.02998  226 THR   A CG2 
1754 N N   . LEU   A 227 ? 0.62021 0.55315 0.65515 -0.00096 0.03624  0.01882  227 LEU   A N   
1755 C CA  . LEU   A 227 ? 0.62230 0.54898 0.65493 0.00144  0.03022  0.01672  227 LEU   A CA  
1756 C C   . LEU   A 227 ? 0.67156 0.58262 0.69703 0.00083  0.02975  0.02164  227 LEU   A C   
1757 O O   . LEU   A 227 ? 0.67981 0.58460 0.69761 0.00480  0.02564  0.02263  227 LEU   A O   
1758 C CB  . LEU   A 227 ? 0.61232 0.54623 0.65728 -0.00175 0.02768  0.01037  227 LEU   A CB  
1759 C CG  . LEU   A 227 ? 0.64039 0.56729 0.68598 -0.00128 0.02280  0.00739  227 LEU   A CG  
1760 C CD1 . LEU   A 227 ? 0.62030 0.56001 0.67464 -0.00206 0.01961  0.00014  227 LEU   A CD1 
1761 C CD2 . LEU   A 227 ? 0.66996 0.58459 0.71899 -0.00605 0.02480  0.00890  227 LEU   A CD2 
1762 N N   . ASN   A 228 ? 0.68992 0.59505 0.71809 -0.00406 0.03402  0.02525  228 ASN   A N   
1763 C CA  . ASN   A 228 ? 0.67437 0.56505 0.69667 -0.00424 0.03372  0.03107  228 ASN   A CA  
1764 C C   . ASN   A 228 ? 0.67290 0.55910 0.68050 -0.00070 0.03387  0.03715  228 ASN   A C   
1765 O O   . ASN   A 228 ? 0.67921 0.55719 0.67956 0.00206  0.03039  0.04060  228 ASN   A O   
1766 C CB  . ASN   A 228 ? 0.71610 0.60114 0.74532 -0.01050 0.03886  0.03392  228 ASN   A CB  
1767 C CG  . ASN   A 228 ? 0.81810 0.69536 0.85596 -0.01279 0.03731  0.03137  228 ASN   A CG  
1768 O OD1 . ASN   A 228 ? 0.80971 0.68641 0.84824 -0.00952 0.03231  0.02747  228 ASN   A OD1 
1769 N ND2 . ASN   A 228 ? 0.89404 0.76482 0.93868 -0.01857 0.04216  0.03339  228 ASN   A ND2 
1770 N N   . ASP   A 229 ? 0.66234 0.55454 0.66550 -0.00086 0.03799  0.03826  229 ASP   A N   
1771 C CA  . ASP   A 229 ? 0.69757 0.58597 0.68590 0.00176  0.03864  0.04294  229 ASP   A CA  
1772 C C   . ASP   A 229 ? 0.68435 0.57359 0.66551 0.00702  0.03342  0.04001  229 ASP   A C   
1773 O O   . ASP   A 229 ? 0.67198 0.55575 0.64082 0.00886  0.03182  0.04354  229 ASP   A O   
1774 C CB  . ASP   A 229 ? 0.68026 0.57505 0.66613 0.00033  0.04514  0.04377  229 ASP   A CB  
1775 C CG  . ASP   A 229 ? 0.77127 0.66066 0.75441 -0.00420 0.05046  0.05049  229 ASP   A CG  
1776 O OD1 . ASP   A 229 ? 0.78140 0.66196 0.75383 -0.00382 0.04940  0.05656  229 ASP   A OD1 
1777 O OD2 . ASP   A 229 ? 0.81253 0.70725 0.80436 -0.00827 0.05568  0.05002  229 ASP   A OD2 
1778 N N   . PHE   A 230 ? 0.64871 0.54523 0.63719 0.00911  0.03076  0.03374  230 PHE   A N   
1779 C CA  . PHE   A 230 ? 0.63892 0.53555 0.62148 0.01375  0.02596  0.03110  230 PHE   A CA  
1780 C C   . PHE   A 230 ? 0.63618 0.52549 0.61787 0.01461  0.02051  0.03218  230 PHE   A C   
1781 O O   . PHE   A 230 ? 0.64531 0.53125 0.61789 0.01740  0.01711  0.03310  230 PHE   A O   
1782 C CB  . PHE   A 230 ? 0.59562 0.50266 0.58637 0.01588  0.02494  0.02503  230 PHE   A CB  
1783 C CG  . PHE   A 230 ? 0.59927 0.50606 0.58660 0.02002  0.01967  0.02215  230 PHE   A CG  
1784 C CD1 . PHE   A 230 ? 0.63399 0.54001 0.61151 0.02351  0.01993  0.02203  230 PHE   A CD1 
1785 C CD2 . PHE   A 230 ? 0.58239 0.48945 0.57630 0.02010  0.01500  0.01923  230 PHE   A CD2 
1786 C CE1 . PHE   A 230 ? 0.59343 0.49887 0.56797 0.02678  0.01553  0.01958  230 PHE   A CE1 
1787 C CE2 . PHE   A 230 ? 0.58898 0.49627 0.57972 0.02364  0.01055  0.01681  230 PHE   A CE2 
1788 C CZ  . PHE   A 230 ? 0.59682 0.50331 0.57800 0.02689  0.01076  0.01722  230 PHE   A CZ  
1789 N N   . ASN   A 231 ? 0.60000 0.48687 0.59148 0.01210  0.01996  0.03183  231 ASN   A N   
1790 C CA  . ASN   A 231 ? 0.65380 0.53412 0.64633 0.01352  0.01536  0.03238  231 ASN   A CA  
1791 C C   . ASN   A 231 ? 0.70395 0.57539 0.68717 0.01413  0.01481  0.04001  231 ASN   A C   
1792 O O   . ASN   A 231 ? 0.72497 0.59333 0.70401 0.01706  0.01027  0.04124  231 ASN   A O   
1793 C CB  . ASN   A 231 ? 0.63627 0.51535 0.64186 0.01044  0.01599  0.02947  231 ASN   A CB  
1794 C CG  . ASN   A 231 ? 0.63895 0.52727 0.65270 0.01070  0.01387  0.02143  231 ASN   A CG  
1795 O OD1 . ASN   A 231 ? 0.60513 0.49812 0.61502 0.01438  0.01042  0.01875  231 ASN   A OD1 
1796 N ND2 . ASN   A 231 ? 0.63789 0.52922 0.66277 0.00640  0.01601  0.01760  231 ASN   A ND2 
1797 N N   . LEU   A 232 ? 0.71077 0.57903 0.69073 0.01132  0.01933  0.04552  232 LEU   A N   
1798 C CA  . LEU   A 232 ? 0.69046 0.55156 0.66091 0.01184  0.01872  0.05369  232 LEU   A CA  
1799 C C   . LEU   A 232 ? 0.68941 0.55291 0.64588 0.01428  0.01623  0.05451  232 LEU   A C   
1800 O O   . LEU   A 232 ? 0.68373 0.54363 0.63266 0.01576  0.01293  0.05965  232 LEU   A O   
1801 C CB  . LEU   A 232 ? 0.71214 0.56986 0.68184 0.00791  0.02465  0.05959  232 LEU   A CB  
1802 C CG  . LEU   A 232 ? 0.74115 0.59494 0.72440 0.00439  0.02788  0.05922  232 LEU   A CG  
1803 C CD1 . LEU   A 232 ? 0.72776 0.57939 0.70984 -0.00005 0.03449  0.06472  232 LEU   A CD1 
1804 C CD2 . LEU   A 232 ? 0.69545 0.54028 0.68352 0.00618  0.02479  0.06217  232 LEU   A CD2 
1805 N N   . VAL   A 233 ? 0.72338 0.59310 0.67654 0.01466  0.01789  0.04952  233 VAL   A N   
1806 C CA  . VAL   A 233 ? 0.71393 0.58493 0.65418 0.01649  0.01606  0.04889  233 VAL   A CA  
1807 C C   . VAL   A 233 ? 0.70668 0.57889 0.64834 0.01965  0.01022  0.04471  233 VAL   A C   
1808 O O   . VAL   A 233 ? 0.73767 0.60855 0.67024 0.02075  0.00659  0.04628  233 VAL   A O   
1809 C CB  . VAL   A 233 ? 0.70857 0.58426 0.64490 0.01601  0.02122  0.04544  233 VAL   A CB  
1810 C CG1 . VAL   A 233 ? 0.74046 0.61636 0.66448 0.01775  0.01980  0.04308  233 VAL   A CG1 
1811 C CG2 . VAL   A 233 ? 0.69921 0.57393 0.63204 0.01270  0.02721  0.05015  233 VAL   A CG2 
1812 N N   . ALA   A 234 ? 0.68400 0.55955 0.63695 0.02074  0.00922  0.03936  234 ALA   A N   
1813 C CA  . ALA   A 234 ? 0.69385 0.57142 0.64795 0.02361  0.00439  0.03504  234 ALA   A CA  
1814 C C   . ALA   A 234 ? 0.72506 0.59870 0.68029 0.02478  -0.00047 0.03787  234 ALA   A C   
1815 O O   . ALA   A 234 ? 0.71590 0.59067 0.66780 0.02684  -0.00460 0.03615  234 ALA   A O   
1816 C CB  . ALA   A 234 ? 0.66306 0.54640 0.62853 0.02425  0.00468  0.02900  234 ALA   A CB  
1817 N N   . MET   A 235 ? 0.71115 0.58011 0.67144 0.02364  0.00027  0.04242  235 MET   A N   
1818 C CA  . MET   A 235 ? 0.68718 0.55256 0.65131 0.02563  -0.00378 0.04495  235 MET   A CA  
1819 C C   . MET   A 235 ? 0.70669 0.57095 0.66014 0.02686  -0.00706 0.05098  235 MET   A C   
1820 O O   . MET   A 235 ? 0.70327 0.56787 0.65831 0.02939  -0.01155 0.05166  235 MET   A O   
1821 C CB  . MET   A 235 ? 0.70393 0.56344 0.67785 0.02429  -0.00121 0.04790  235 MET   A CB  
1822 C CG  . MET   A 235 ? 0.81003 0.67049 0.79683 0.02395  -0.00092 0.04106  235 MET   A CG  
1823 S SD  . MET   A 235 ? 1.15549 1.01209 1.15219 0.01932  0.00513  0.04102  235 MET   A SD  
1824 C CE  . MET   A 235 ? 0.77002 0.63359 0.77782 0.01814  0.00465  0.03027  235 MET   A CE  
1825 N N   . LYS   A 236 ? 0.70170 0.56565 0.64432 0.02494  -0.00491 0.05528  236 LYS   A N   
1826 C CA  . LYS   A 236 ? 0.70865 0.57349 0.63994 0.02540  -0.00841 0.06045  236 LYS   A CA  
1827 C C   . LYS   A 236 ? 0.70966 0.57920 0.63484 0.02618  -0.01195 0.05516  236 LYS   A C   
1828 O O   . LYS   A 236 ? 0.75051 0.62229 0.66830 0.02647  -0.01605 0.05818  236 LYS   A O   
1829 C CB  . LYS   A 236 ? 0.68782 0.55174 0.60797 0.02253  -0.00483 0.06572  236 LYS   A CB  
1830 C CG  . LYS   A 236 ? 0.72615 0.59313 0.63583 0.02049  -0.00202 0.06091  236 LYS   A CG  
1831 C CD  . LYS   A 236 ? 0.77427 0.64087 0.67083 0.01762  0.00074  0.06663  236 LYS   A CD  
1832 C CE  . LYS   A 236 ? 0.83139 0.70124 0.71317 0.01611  -0.00049 0.06381  236 LYS   A CE  
1833 N NZ  . LYS   A 236 ? 1.04670 0.91649 0.91680 0.01285  0.00516  0.06460  236 LYS   A NZ  
1834 N N   . TYR   A 237 ? 0.67556 0.54706 0.60402 0.02640  -0.01045 0.04766  237 TYR   A N   
1835 C CA  . TYR   A 237 ? 0.66420 0.53895 0.58908 0.02732  -0.01331 0.04243  237 TYR   A CA  
1836 C C   . TYR   A 237 ? 0.62595 0.50232 0.56195 0.02990  -0.01643 0.03876  237 TYR   A C   
1837 O O   . TYR   A 237 ? 0.59653 0.47559 0.53160 0.03069  -0.01796 0.03384  237 TYR   A O   
1838 C CB  . TYR   A 237 ? 0.66263 0.53822 0.58265 0.02636  -0.00912 0.03727  237 TYR   A CB  
1839 C CG  . TYR   A 237 ? 0.66403 0.53821 0.57149 0.02371  -0.00567 0.03964  237 TYR   A CG  
1840 C CD1 . TYR   A 237 ? 0.65832 0.53288 0.55304 0.02205  -0.00748 0.03957  237 TYR   A CD1 
1841 C CD2 . TYR   A 237 ? 0.68663 0.55962 0.59480 0.02237  -0.00037 0.04158  237 TYR   A CD2 
1842 C CE1 . TYR   A 237 ? 0.70858 0.58209 0.59086 0.01917  -0.00403 0.04101  237 TYR   A CE1 
1843 C CE2 . TYR   A 237 ? 0.71421 0.58624 0.61042 0.01985  0.00330  0.04351  237 TYR   A CE2 
1844 C CZ  . TYR   A 237 ? 0.74566 0.61780 0.62856 0.01829  0.00147  0.04305  237 TYR   A CZ  
1845 O OH  . TYR   A 237 ? 0.76837 0.63977 0.63841 0.01533  0.00539  0.04426  237 TYR   A OH  
1846 N N   . ASN   A 238 ? 0.68337 0.55765 0.62967 0.03105  -0.01685 0.04096  238 ASN   A N   
1847 C CA  . ASN   A 238 ? 0.65441 0.52993 0.61128 0.03333  -0.01935 0.03737  238 ASN   A CA  
1848 C C   . ASN   A 238 ? 0.65441 0.53315 0.61622 0.03329  -0.01767 0.03002  238 ASN   A C   
1849 O O   . ASN   A 238 ? 0.63204 0.51415 0.59608 0.03478  -0.02013 0.02579  238 ASN   A O   
1850 C CB  . ASN   A 238 ? 0.63082 0.50925 0.58500 0.03514  -0.02443 0.03809  238 ASN   A CB  
1851 C CG  . ASN   A 238 ? 0.68936 0.56816 0.65496 0.03784  -0.02658 0.03651  238 ASN   A CG  
1852 O OD1 . ASN   A 238 ? 0.71196 0.58682 0.68651 0.03840  -0.02463 0.03727  238 ASN   A OD1 
1853 N ND2 . ASN   A 238 ? 0.71941 0.60266 0.68480 0.03923  -0.03013 0.03398  238 ASN   A ND2 
1854 N N   . TYR   A 239 ? 0.66753 0.54619 0.63119 0.03157  -0.01343 0.02889  239 TYR   A N   
1855 C CA  . TYR   A 239 ? 0.64940 0.53267 0.61930 0.03162  -0.01188 0.02287  239 TYR   A CA  
1856 C C   . TYR   A 239 ? 0.64989 0.53272 0.63185 0.03060  -0.01081 0.02106  239 TYR   A C   
1857 O O   . TYR   A 239 ? 0.66279 0.54056 0.64763 0.02909  -0.00897 0.02486  239 TYR   A O   
1858 C CB  . TYR   A 239 ? 0.63838 0.52372 0.60375 0.03051  -0.00774 0.02233  239 TYR   A CB  
1859 C CG  . TYR   A 239 ? 0.61720 0.50455 0.57440 0.03199  -0.00806 0.02009  239 TYR   A CG  
1860 C CD1 . TYR   A 239 ? 0.61903 0.50367 0.56658 0.03217  -0.01050 0.02178  239 TYR   A CD1 
1861 C CD2 . TYR   A 239 ? 0.58163 0.47375 0.54110 0.03312  -0.00574 0.01644  239 TYR   A CD2 
1862 C CE1 . TYR   A 239 ? 0.55967 0.44474 0.49981 0.03288  -0.01013 0.01926  239 TYR   A CE1 
1863 C CE2 . TYR   A 239 ? 0.56756 0.45985 0.51994 0.03477  -0.00528 0.01475  239 TYR   A CE2 
1864 C CZ  . TYR   A 239 ? 0.56745 0.45543 0.51006 0.03436  -0.00722 0.01586  239 TYR   A CZ  
1865 O OH  . TYR   A 239 ? 0.56880 0.45563 0.50442 0.03538  -0.00614 0.01370  239 TYR   A OH  
1866 N N   . GLU   A 240 ? 0.65031 0.53832 0.63895 0.03114  -0.01179 0.01518  240 GLU   A N   
1867 C CA  . GLU   A 240 ? 0.65368 0.54187 0.65342 0.02952  -0.01088 0.01187  240 GLU   A CA  
1868 C C   . GLU   A 240 ? 0.62168 0.51062 0.62559 0.02608  -0.00654 0.01206  240 GLU   A C   
1869 O O   . GLU   A 240 ? 0.59861 0.49179 0.59873 0.02571  -0.00452 0.01247  240 GLU   A O   
1870 C CB  . GLU   A 240 ? 0.64634 0.54181 0.65071 0.03040  -0.01292 0.00523  240 GLU   A CB  
1871 C CG  . GLU   A 240 ? 0.71266 0.60809 0.72750 0.02860  -0.01258 0.00060  240 GLU   A CG  
1872 C CD  . GLU   A 240 ? 0.83251 0.73253 0.84935 0.03043  -0.01562 -0.00445 240 GLU   A CD  
1873 O OE1 . GLU   A 240 ? 0.86995 0.76572 0.88616 0.03269  -0.01757 -0.00317 240 GLU   A OE1 
1874 O OE2 . GLU   A 240 ? 0.84474 0.75348 0.86395 0.02966  -0.01600 -0.00940 240 GLU   A OE2 
1875 N N   . PRO   A 241 ? 0.67953 0.56408 0.69156 0.02347  -0.00459 0.01179  241 PRO   A N   
1876 C CA  . PRO   A 241 ? 0.66526 0.55149 0.68269 0.01929  -0.00029 0.01115  241 PRO   A CA  
1877 C C   . PRO   A 241 ? 0.64118 0.53928 0.66274 0.01822  -0.00017 0.00518  241 PRO   A C   
1878 O O   . PRO   A 241 ? 0.66701 0.57073 0.69170 0.01924  -0.00296 -0.00010 241 PRO   A O   
1879 C CB  . PRO   A 241 ? 0.69518 0.57415 0.72172 0.01664  0.00132  0.01013  241 PRO   A CB  
1880 C CG  . PRO   A 241 ? 0.71882 0.59411 0.74568 0.02017  -0.00231 0.00905  241 PRO   A CG  
1881 C CD  . PRO   A 241 ? 0.69249 0.56900 0.70874 0.02423  -0.00550 0.01319  241 PRO   A CD  
1882 N N   . LEU   A 242 ? 0.61300 0.51574 0.63470 0.01629  0.00320  0.00640  242 LEU   A N   
1883 C CA  . LEU   A 242 ? 0.63252 0.54798 0.65983 0.01517  0.00378  0.00176  242 LEU   A CA  
1884 C C   . LEU   A 242 ? 0.60633 0.52421 0.64444 0.00930  0.00662  -0.00131 242 LEU   A C   
1885 O O   . LEU   A 242 ? 0.58620 0.49965 0.62547 0.00616  0.01068  0.00217  242 LEU   A O   
1886 C CB  . LEU   A 242 ? 0.61350 0.53395 0.63534 0.01712  0.00613  0.00472  242 LEU   A CB  
1887 C CG  . LEU   A 242 ? 0.57768 0.51202 0.60352 0.01881  0.00533  0.00095  242 LEU   A CG  
1888 C CD1 . LEU   A 242 ? 0.56196 0.49762 0.58351 0.02313  0.00090  -0.00094 242 LEU   A CD1 
1889 C CD2 . LEU   A 242 ? 0.56377 0.50291 0.58702 0.02035  0.00920  0.00383  242 LEU   A CD2 
1890 N N   . THR   A 243 ? 0.58454 0.50961 0.63016 0.00735  0.00468  -0.00797 243 THR   A N   
1891 C CA  . THR   A 243 ? 0.58332 0.51139 0.63949 0.00082  0.00708  -0.01252 243 THR   A CA  
1892 C C   . THR   A 243 ? 0.59582 0.54141 0.65778 -0.00110 0.00710  -0.01623 243 THR   A C   
1893 O O   . THR   A 243 ? 0.59504 0.54972 0.65321 0.00340  0.00520  -0.01515 243 THR   A O   
1894 C CB  . THR   A 243 ? 0.63048 0.55398 0.69121 -0.00093 0.00527  -0.01826 243 THR   A CB  
1895 O OG1 . THR   A 243 ? 0.64993 0.58369 0.70968 0.00173  0.00095  -0.02298 243 THR   A OG1 
1896 C CG2 . THR   A 243 ? 0.61924 0.52658 0.67528 0.00201  0.00518  -0.01381 243 THR   A CG2 
1897 N N   . GLN   A 244 ? 0.60016 0.55065 0.67190 -0.00797 0.00948  -0.02049 244 GLN   A N   
1898 C CA  . GLN   A 244 ? 0.59000 0.55929 0.66869 -0.01045 0.00936  -0.02389 244 GLN   A CA  
1899 C C   . GLN   A 244 ? 0.58628 0.56804 0.66549 -0.00820 0.00425  -0.02904 244 GLN   A C   
1900 O O   . GLN   A 244 ? 0.57094 0.56817 0.65134 -0.00565 0.00271  -0.02865 244 GLN   A O   
1901 C CB  . GLN   A 244 ? 0.57344 0.54548 0.66276 -0.01943 0.01293  -0.02794 244 GLN   A CB  
1902 C CG  . GLN   A 244 ? 0.53183 0.52513 0.62936 -0.02252 0.01304  -0.03073 244 GLN   A CG  
1903 C CD  . GLN   A 244 ? 0.52974 0.52910 0.62451 -0.01790 0.01514  -0.02404 244 GLN   A CD  
1904 O OE1 . GLN   A 244 ? 0.55676 0.54471 0.64714 -0.01718 0.01912  -0.01830 244 GLN   A OE1 
1905 N NE2 . GLN   A 244 ? 0.49526 0.51275 0.59244 -0.01452 0.01272  -0.02459 244 GLN   A NE2 
1906 N N   . ASP   A 245 ? 0.60463 0.58015 0.68308 -0.00883 0.00186  -0.03356 245 ASP   A N   
1907 C CA  . ASP   A 245 ? 0.61858 0.60456 0.69545 -0.00612 -0.00292 -0.03768 245 ASP   A CA  
1908 C C   . ASP   A 245 ? 0.58074 0.56861 0.64904 0.00212  -0.00512 -0.03191 245 ASP   A C   
1909 O O   . ASP   A 245 ? 0.58369 0.58557 0.65184 0.00485  -0.00804 -0.03280 245 ASP   A O   
1910 C CB  . ASP   A 245 ? 0.65465 0.63061 0.73063 -0.00719 -0.00424 -0.04256 245 ASP   A CB  
1911 C CG  . ASP   A 245 ? 0.75415 0.72253 0.83779 -0.01489 -0.00072 -0.04758 245 ASP   A CG  
1912 O OD1 . ASP   A 245 ? 0.72036 0.67525 0.80435 -0.01598 0.00313  -0.04315 245 ASP   A OD1 
1913 O OD2 . ASP   A 245 ? 0.77031 0.74590 0.85928 -0.02005 -0.00156 -0.05597 245 ASP   A OD2 
1914 N N   . HIS   A 246 ? 0.57661 0.55054 0.63762 0.00593  -0.00356 -0.02579 246 HIS   A N   
1915 C CA  . HIS   A 246 ? 0.59886 0.57216 0.65108 0.01300  -0.00505 -0.02093 246 HIS   A CA  
1916 C C   . HIS   A 246 ? 0.57052 0.55489 0.62391 0.01517  -0.00326 -0.01776 246 HIS   A C   
1917 O O   . HIS   A 246 ? 0.53855 0.53093 0.58925 0.02008  -0.00514 -0.01655 246 HIS   A O   
1918 C CB  . HIS   A 246 ? 0.61200 0.56827 0.65617 0.01535  -0.00388 -0.01593 246 HIS   A CB  
1919 C CG  . HIS   A 246 ? 0.64751 0.59455 0.68948 0.01589  -0.00636 -0.01788 246 HIS   A CG  
1920 N ND1 . HIS   A 246 ? 0.64692 0.57956 0.68466 0.01661  -0.00553 -0.01411 246 HIS   A ND1 
1921 C CD2 . HIS   A 246 ? 0.63473 0.58579 0.67830 0.01610  -0.00951 -0.02296 246 HIS   A CD2 
1922 C CE1 . HIS   A 246 ? 0.64575 0.57403 0.68353 0.01755  -0.00797 -0.01676 246 HIS   A CE1 
1923 N NE2 . HIS   A 246 ? 0.66638 0.60527 0.70743 0.01711  -0.01018 -0.02243 246 HIS   A NE2 
1924 N N   . VAL   A 247 ? 0.53782 0.52254 0.59552 0.01180  0.00083  -0.01605 247 VAL   A N   
1925 C CA  . VAL   A 247 ? 0.55146 0.54819 0.61220 0.01365  0.00318  -0.01347 247 VAL   A CA  
1926 C C   . VAL   A 247 ? 0.56109 0.57766 0.62980 0.01323  0.00033  -0.01722 247 VAL   A C   
1927 O O   . VAL   A 247 ? 0.54594 0.57365 0.61535 0.01807  0.00034  -0.01455 247 VAL   A O   
1928 C CB  . VAL   A 247 ? 0.55822 0.55263 0.62333 0.00891  0.00836  -0.01162 247 VAL   A CB  
1929 C CG1 . VAL   A 247 ? 0.50787 0.51750 0.57871 0.01024  0.01108  -0.00983 247 VAL   A CG1 
1930 C CG2 . VAL   A 247 ? 0.54184 0.51840 0.59748 0.01027  0.01104  -0.00660 247 VAL   A CG2 
1931 N N   . ASP   A 248 ? 0.53938 0.56077 0.61397 0.00762  -0.00206 -0.02340 248 ASP   A N   
1932 C CA  . ASP   A 248 ? 0.52438 0.56637 0.60624 0.00617  -0.00517 -0.02739 248 ASP   A CA  
1933 C C   . ASP   A 248 ? 0.54651 0.59368 0.62260 0.01268  -0.00945 -0.02641 248 ASP   A C   
1934 O O   . ASP   A 248 ? 0.55936 0.62420 0.63915 0.01526  -0.01142 -0.02559 248 ASP   A O   
1935 C CB  . ASP   A 248 ? 0.57316 0.61769 0.66179 -0.00251 -0.00612 -0.03523 248 ASP   A CB  
1936 C CG  . ASP   A 248 ? 0.56614 0.61177 0.66330 -0.00987 -0.00183 -0.03654 248 ASP   A CG  
1937 O OD1 . ASP   A 248 ? 0.52257 0.56783 0.62029 -0.00802 0.00181  -0.03111 248 ASP   A OD1 
1938 O OD2 . ASP   A 248 ? 0.56988 0.61621 0.67306 -0.01779 -0.00164 -0.04324 248 ASP   A OD2 
1939 N N   . ILE   A 249 ? 0.52885 0.56145 0.59622 0.01545  -0.01086 -0.02604 249 ILE   A N   
1940 C CA  . ILE   A 249 ? 0.51026 0.54637 0.57164 0.02138  -0.01434 -0.02466 249 ILE   A CA  
1941 C C   . ILE   A 249 ? 0.52385 0.56067 0.58121 0.02871  -0.01258 -0.01772 249 ILE   A C   
1942 O O   . ILE   A 249 ? 0.54152 0.58950 0.59859 0.03343  -0.01457 -0.01565 249 ILE   A O   
1943 C CB  . ILE   A 249 ? 0.59322 0.61401 0.64709 0.02203  -0.01589 -0.02616 249 ILE   A CB  
1944 C CG1 . ILE   A 249 ? 0.55176 0.57195 0.61015 0.01541  -0.01706 -0.03356 249 ILE   A CG1 
1945 C CG2 . ILE   A 249 ? 0.67482 0.69865 0.72223 0.02786  -0.01889 -0.02426 249 ILE   A CG2 
1946 C CD1 . ILE   A 249 ? 0.60064 0.60171 0.65508 0.01462  -0.01595 -0.03404 249 ILE   A CD1 
1947 N N   . LEU   A 250 ? 0.54563 0.57041 0.59967 0.02979  -0.00849 -0.01395 250 LEU   A N   
1948 C CA  . LEU   A 250 ? 0.56005 0.58396 0.61030 0.03619  -0.00562 -0.00820 250 LEU   A CA  
1949 C C   . LEU   A 250 ? 0.52326 0.56459 0.58258 0.03740  -0.00379 -0.00653 250 LEU   A C   
1950 O O   . LEU   A 250 ? 0.51076 0.55266 0.56830 0.04333  -0.00081 -0.00186 250 LEU   A O   
1951 C CB  . LEU   A 250 ? 0.54750 0.55427 0.59103 0.03603  -0.00159 -0.00543 250 LEU   A CB  
1952 C CG  . LEU   A 250 ? 0.54066 0.53057 0.57423 0.03647  -0.00310 -0.00531 250 LEU   A CG  
1953 C CD1 . LEU   A 250 ? 0.52435 0.50098 0.55439 0.03335  -0.00001 -0.00374 250 LEU   A CD1 
1954 C CD2 . LEU   A 250 ? 0.45703 0.44240 0.48218 0.04280  -0.00317 -0.00220 250 LEU   A CD2 
1955 N N   . GLY   A 251 ? 0.49998 0.55567 0.56922 0.03189  -0.00526 -0.01041 251 GLY   A N   
1956 C CA  . GLY   A 251 ? 0.53092 0.60514 0.61033 0.03202  -0.00370 -0.00910 251 GLY   A CA  
1957 C C   . GLY   A 251 ? 0.51811 0.60528 0.59867 0.04016  -0.00465 -0.00449 251 GLY   A C   
1958 O O   . GLY   A 251 ? 0.53699 0.62591 0.61903 0.04533  -0.00050 0.00030  251 GLY   A O   
1959 N N   . PRO   A 252 ? 0.51975 0.61636 0.59979 0.04162  -0.00976 -0.00564 252 PRO   A N   
1960 C CA  . PRO   A 252 ? 0.54021 0.64999 0.62180 0.04977  -0.01077 -0.00024 252 PRO   A CA  
1961 C C   . PRO   A 252 ? 0.56245 0.65742 0.63593 0.05807  -0.00683 0.00568  252 PRO   A C   
1962 O O   . PRO   A 252 ? 0.52598 0.62943 0.60323 0.06502  -0.00446 0.01108  252 PRO   A O   
1963 C CB  . PRO   A 252 ? 0.53812 0.65560 0.61727 0.04885  -0.01688 -0.00288 252 PRO   A CB  
1964 C CG  . PRO   A 252 ? 0.52525 0.64264 0.60700 0.03892  -0.01895 -0.01089 252 PRO   A CG  
1965 C CD  . PRO   A 252 ? 0.52395 0.62129 0.60278 0.03580  -0.01448 -0.01186 252 PRO   A CD  
1966 N N   . LEU   A 253 ? 0.55041 0.62375 0.61319 0.05747  -0.00585 0.00472  253 LEU   A N   
1967 C CA  . LEU   A 253 ? 0.54734 0.60565 0.60188 0.06393  -0.00164 0.00926  253 LEU   A CA  
1968 C C   . LEU   A 253 ? 0.56900 0.62540 0.62662 0.06517  0.00462  0.01149  253 LEU   A C   
1969 O O   . LEU   A 253 ? 0.60108 0.65670 0.65812 0.07221  0.00871  0.01601  253 LEU   A O   
1970 C CB  . LEU   A 253 ? 0.53578 0.57332 0.57886 0.06166  -0.00230 0.00716  253 LEU   A CB  
1971 C CG  . LEU   A 253 ? 0.51906 0.55032 0.55417 0.06609  -0.00443 0.00895  253 LEU   A CG  
1972 C CD1 . LEU   A 253 ? 0.55045 0.56519 0.57667 0.06222  -0.00606 0.00585  253 LEU   A CD1 
1973 C CD2 . LEU   A 253 ? 0.56968 0.59525 0.60109 0.07373  0.00020  0.01434  253 LEU   A CD2 
1974 N N   . SER   A 254 ? 0.51978 0.57499 0.58075 0.05840  0.00597  0.00839  254 SER   A N   
1975 C CA  . SER   A 254 ? 0.54619 0.60141 0.61062 0.05873  0.01214  0.01029  254 SER   A CA  
1976 C C   . SER   A 254 ? 0.54948 0.62575 0.62578 0.06304  0.01363  0.01326  254 SER   A C   
1977 O O   . SER   A 254 ? 0.52212 0.59869 0.60062 0.06688  0.01961  0.01630  254 SER   A O   
1978 C CB  . SER   A 254 ? 0.52370 0.57534 0.59040 0.04999  0.01289  0.00671  254 SER   A CB  
1979 O OG  . SER   A 254 ? 0.57278 0.62394 0.64196 0.04983  0.01922  0.00868  254 SER   A OG  
1980 N N   . ALA   A 255 ? 0.51226 0.60714 0.59640 0.06251  0.00839  0.01244  255 ALA   A N   
1981 C CA  . ALA   A 255 ? 0.54633 0.66408 0.64264 0.06677  0.00896  0.01581  255 ALA   A CA  
1982 C C   . ALA   A 255 ? 0.53176 0.64981 0.62586 0.07777  0.01055  0.02214  255 ALA   A C   
1983 O O   . ALA   A 255 ? 0.47018 0.59884 0.57206 0.08386  0.01461  0.02660  255 ALA   A O   
1984 C CB  . ALA   A 255 ? 0.51318 0.65228 0.61826 0.06155  0.00244  0.01250  255 ALA   A CB  
1985 N N   . GLN   A 256 ? 0.57248 0.67872 0.65650 0.08053  0.00788  0.02280  256 GLN   A N   
1986 C CA  . GLN   A 256 ? 0.58296 0.68815 0.66471 0.09069  0.00959  0.02905  256 GLN   A CA  
1987 C C   . GLN   A 256 ? 0.57548 0.66305 0.65165 0.09583  0.01764  0.03155  256 GLN   A C   
1988 O O   . GLN   A 256 ? 0.58791 0.67870 0.66737 0.10473  0.02170  0.03709  256 GLN   A O   
1989 C CB  . GLN   A 256 ? 0.58014 0.67743 0.65257 0.09123  0.00479  0.02881  256 GLN   A CB  
1990 C CG  . GLN   A 256 ? 0.67462 0.77431 0.74616 0.10122  0.00558  0.03584  256 GLN   A CG  
1991 C CD  . GLN   A 256 ? 0.66597 0.74885 0.72511 0.10187  0.00385  0.03576  256 GLN   A CD  
1992 O OE1 . GLN   A 256 ? 0.62066 0.70388 0.67598 0.09608  -0.00165 0.03166  256 GLN   A OE1 
1993 N NE2 . GLN   A 256 ? 0.71773 0.78572 0.77082 0.10873  0.00899  0.04001  256 GLN   A NE2 
1994 N N   . THR   A 257 ? 0.58409 0.65319 0.65176 0.09050  0.02024  0.02764  257 THR   A N   
1995 C CA  . THR   A 257 ? 0.56118 0.61279 0.62157 0.09403  0.02777  0.02887  257 THR   A CA  
1996 C C   . THR   A 257 ? 0.56089 0.61718 0.62762 0.09282  0.03374  0.02861  257 THR   A C   
1997 O O   . THR   A 257 ? 0.60883 0.65378 0.67098 0.09663  0.04094  0.02980  257 THR   A O   
1998 C CB  . THR   A 257 ? 0.58394 0.61301 0.62995 0.08914  0.02711  0.02526  257 THR   A CB  
1999 O OG1 . THR   A 257 ? 0.58793 0.61556 0.63396 0.08051  0.02576  0.02114  257 THR   A OG1 
2000 C CG2 . THR   A 257 ? 0.57203 0.59808 0.61272 0.08911  0.02094  0.02492  257 THR   A CG2 
2001 N N   . GLY   A 258 ? 0.55356 0.62607 0.63050 0.08723  0.03136  0.02675  258 GLY   A N   
2002 C CA  . GLY   A 258 ? 0.54531 0.62378 0.62914 0.08545  0.03711  0.02664  258 GLY   A CA  
2003 C C   . GLY   A 258 ? 0.55362 0.61505 0.62846 0.07865  0.04036  0.02335  258 GLY   A C   
2004 O O   . GLY   A 258 ? 0.55251 0.61688 0.63140 0.07720  0.04611  0.02354  258 GLY   A O   
2005 N N   . ILE   A 259 ? 0.54916 0.59374 0.61211 0.07458  0.03696  0.02078  259 ILE   A N   
2006 C CA  . ILE   A 259 ? 0.57395 0.60259 0.62761 0.06838  0.03927  0.01851  259 ILE   A CA  
2007 C C   . ILE   A 259 ? 0.58037 0.61304 0.63797 0.05965  0.03420  0.01537  259 ILE   A C   
2008 O O   . ILE   A 259 ? 0.56868 0.60244 0.62599 0.05790  0.02774  0.01349  259 ILE   A O   
2009 C CB  . ILE   A 259 ? 0.61043 0.61802 0.64855 0.06966  0.03908  0.01802  259 ILE   A CB  
2010 C CG1 . ILE   A 259 ? 0.59263 0.59562 0.62729 0.07830  0.04374  0.02056  259 ILE   A CG1 
2011 C CG2 . ILE   A 259 ? 0.60890 0.60204 0.63735 0.06408  0.04205  0.01668  259 ILE   A CG2 
2012 C CD1 . ILE   A 259 ? 0.65821 0.65036 0.68403 0.08073  0.04005  0.02047  259 ILE   A CD1 
2013 N N   . ALA   A 260 ? 0.57851 0.61273 0.63967 0.05408  0.03763  0.01473  260 ALA   A N   
2014 C CA  . ALA   A 260 ? 0.52976 0.56420 0.59387 0.04542  0.03405  0.01179  260 ALA   A CA  
2015 C C   . ALA   A 260 ? 0.59329 0.60937 0.64530 0.04305  0.03038  0.01044  260 ALA   A C   
2016 O O   . ALA   A 260 ? 0.58678 0.58837 0.62698 0.04595  0.03225  0.01187  260 ALA   A O   
2017 C CB  . ALA   A 260 ? 0.53192 0.56765 0.59999 0.04002  0.03956  0.01221  260 ALA   A CB  
2018 N N   . VAL   A 261 ? 0.57084 0.58818 0.62620 0.03759  0.02525  0.00738  261 VAL   A N   
2019 C CA  . VAL   A 261 ? 0.53257 0.53425 0.57834 0.03566  0.02161  0.00619  261 VAL   A CA  
2020 C C   . VAL   A 261 ? 0.54881 0.53510 0.58575 0.03297  0.02536  0.00826  261 VAL   A C   
2021 O O   . VAL   A 261 ? 0.53299 0.50566 0.55845 0.03473  0.02452  0.00936  261 VAL   A O   
2022 C CB  . VAL   A 261 ? 0.49322 0.49942 0.54556 0.03013  0.01656  0.00208  261 VAL   A CB  
2023 C CG1 . VAL   A 261 ? 0.50215 0.49208 0.54583 0.02830  0.01361  0.00122  261 VAL   A CG1 
2024 C CG2 . VAL   A 261 ? 0.45535 0.47680 0.51402 0.03284  0.01224  0.00010  261 VAL   A CG2 
2025 N N   . LEU   A 262 ? 0.59431 0.58336 0.63631 0.02842  0.02957  0.00906  262 LEU   A N   
2026 C CA  . LEU   A 262 ? 0.59370 0.56920 0.62714 0.02554  0.03321  0.01174  262 LEU   A CA  
2027 C C   . LEU   A 262 ? 0.61530 0.58552 0.63917 0.03009  0.03817  0.01440  262 LEU   A C   
2028 O O   . LEU   A 262 ? 0.59888 0.55652 0.61186 0.02869  0.04003  0.01655  262 LEU   A O   
2029 C CB  . LEU   A 262 ? 0.55753 0.53745 0.59936 0.01889  0.03669  0.01206  262 LEU   A CB  
2030 C CG  . LEU   A 262 ? 0.55746 0.53525 0.60513 0.01288  0.03288  0.00948  262 LEU   A CG  
2031 C CD1 . LEU   A 262 ? 0.58755 0.56426 0.64055 0.00585  0.03739  0.01077  262 LEU   A CD1 
2032 C CD2 . LEU   A 262 ? 0.55206 0.51479 0.59000 0.01385  0.02861  0.00989  262 LEU   A CD2 
2033 N N   . ASP   A 263 ? 0.59521 0.57486 0.62284 0.03554  0.04054  0.01434  263 ASP   A N   
2034 C CA  . ASP   A 263 ? 0.57824 0.55097 0.59614 0.04042  0.04539  0.01589  263 ASP   A CA  
2035 C C   . ASP   A 263 ? 0.58661 0.54661 0.59250 0.04311  0.04172  0.01533  263 ASP   A C   
2036 O O   . ASP   A 263 ? 0.62649 0.57449 0.61993 0.04311  0.04431  0.01612  263 ASP   A O   
2037 C CB  . ASP   A 263 ? 0.65186 0.63754 0.67814 0.04637  0.04918  0.01627  263 ASP   A CB  
2038 C CG  . ASP   A 263 ? 0.80403 0.80159 0.84040 0.04402  0.05469  0.01723  263 ASP   A CG  
2039 O OD1 . ASP   A 263 ? 0.74991 0.75072 0.79183 0.03726  0.05352  0.01681  263 ASP   A OD1 
2040 O OD2 . ASP   A 263 ? 0.83005 0.83350 0.86918 0.04894  0.06062  0.01837  263 ASP   A OD2 
2041 N N   . MET   A 264 ? 0.57969 0.54290 0.58896 0.04494  0.03576  0.01379  264 MET   A N   
2042 C CA  . MET   A 264 ? 0.59035 0.54232 0.58925 0.04672  0.03202  0.01316  264 MET   A CA  
2043 C C   . MET   A 264 ? 0.58922 0.52983 0.58032 0.04165  0.02931  0.01344  264 MET   A C   
2044 O O   . MET   A 264 ? 0.55865 0.48845 0.53851 0.04224  0.02817  0.01361  264 MET   A O   
2045 C CB  . MET   A 264 ? 0.57123 0.53048 0.57614 0.04931  0.02644  0.01168  264 MET   A CB  
2046 C CG  . MET   A 264 ? 0.57175 0.52129 0.56710 0.05218  0.02366  0.01127  264 MET   A CG  
2047 S SD  . MET   A 264 ? 0.58005 0.52419 0.56857 0.05873  0.02961  0.01258  264 MET   A SD  
2048 C CE  . MET   A 264 ? 0.53178 0.49275 0.53351 0.06471  0.02943  0.01388  264 MET   A CE  
2049 N N   . CYS   A 265 ? 0.56663 0.50973 0.56389 0.03660  0.02838  0.01368  265 CYS   A N   
2050 C CA  . CYS   A 265 ? 0.55664 0.48897 0.54731 0.03242  0.02656  0.01516  265 CYS   A CA  
2051 C C   . CYS   A 265 ? 0.60888 0.53310 0.58849 0.03149  0.03138  0.01801  265 CYS   A C   
2052 O O   . CYS   A 265 ? 0.59627 0.51056 0.56525 0.03051  0.02951  0.01947  265 CYS   A O   
2053 C CB  . CYS   A 265 ? 0.52744 0.46337 0.52801 0.02735  0.02559  0.01495  265 CYS   A CB  
2054 S SG  . CYS   A 265 ? 0.53210 0.47358 0.54202 0.02680  0.01901  0.01084  265 CYS   A SG  
2055 N N   . ALA   A 266 ? 0.56376 0.49313 0.54573 0.03163  0.03763  0.01880  266 ALA   A N   
2056 C CA  . ALA   A 266 ? 0.60583 0.52835 0.57651 0.03078  0.04296  0.02092  266 ALA   A CA  
2057 C C   . ALA   A 266 ? 0.62750 0.54266 0.58614 0.03437  0.04325  0.01953  266 ALA   A C   
2058 O O   . ALA   A 266 ? 0.65998 0.56668 0.60580 0.03257  0.04497  0.02070  266 ALA   A O   
2059 C CB  . ALA   A 266 ? 0.62716 0.55796 0.60392 0.03078  0.05020  0.02146  266 ALA   A CB  
2060 N N   . SER   A 267 ? 0.62691 0.54526 0.58917 0.03908  0.04170  0.01710  267 SER   A N   
2061 C CA  . SER   A 267 ? 0.63015 0.54031 0.58152 0.04200  0.04209  0.01549  267 SER   A CA  
2062 C C   . SER   A 267 ? 0.62219 0.52458 0.56604 0.03980  0.03557  0.01540  267 SER   A C   
2063 O O   . SER   A 267 ? 0.62321 0.51692 0.55442 0.03890  0.03606  0.01485  267 SER   A O   
2064 C CB  . SER   A 267 ? 0.65276 0.56836 0.61084 0.04797  0.04288  0.01387  267 SER   A CB  
2065 O OG  . SER   A 267 ? 0.71504 0.63570 0.67699 0.05108  0.05019  0.01408  267 SER   A OG  
2066 N N   . LEU   A 268 ? 0.61046 0.51642 0.56213 0.03870  0.02961  0.01563  268 LEU   A N   
2067 C CA  . LEU   A 268 ? 0.60268 0.50242 0.54883 0.03695  0.02362  0.01583  268 LEU   A CA  
2068 C C   . LEU   A 268 ? 0.61880 0.51262 0.55723 0.03271  0.02355  0.01898  268 LEU   A C   
2069 O O   . LEU   A 268 ? 0.63167 0.51929 0.56048 0.03154  0.02060  0.01961  268 LEU   A O   
2070 C CB  . LEU   A 268 ? 0.58051 0.48573 0.53754 0.03707  0.01816  0.01486  268 LEU   A CB  
2071 C CG  . LEU   A 268 ? 0.54777 0.44806 0.50185 0.03572  0.01210  0.01505  268 LEU   A CG  
2072 C CD1 . LEU   A 268 ? 0.51642 0.41069 0.45975 0.03706  0.01082  0.01410  268 LEU   A CD1 
2073 C CD2 . LEU   A 268 ? 0.48514 0.39151 0.45014 0.03633  0.00789  0.01292  268 LEU   A CD2 
2074 N N   . LYS   A 269 ? 0.64079 0.53715 0.58344 0.03026  0.02675  0.02136  269 LYS   A N   
2075 C CA  . LYS   A 269 ? 0.64320 0.53414 0.57793 0.02650  0.02746  0.02543  269 LYS   A CA  
2076 C C   . LYS   A 269 ? 0.68030 0.56594 0.59988 0.02608  0.03055  0.02540  269 LYS   A C   
2077 O O   . LYS   A 269 ? 0.67610 0.55671 0.58555 0.02378  0.02802  0.02784  269 LYS   A O   
2078 C CB  . LYS   A 269 ? 0.67585 0.57051 0.61774 0.02385  0.03175  0.02792  269 LYS   A CB  
2079 C CG  . LYS   A 269 ? 0.73278 0.62223 0.66557 0.02017  0.03403  0.03296  269 LYS   A CG  
2080 C CD  . LYS   A 269 ? 0.74284 0.63395 0.68510 0.01688  0.03570  0.03627  269 LYS   A CD  
2081 C CE  . LYS   A 269 ? 0.70504 0.60347 0.65434 0.01618  0.04238  0.03502  269 LYS   A CE  
2082 N NZ  . LYS   A 269 ? 0.76698 0.66333 0.71058 0.01246  0.04796  0.03973  269 LYS   A NZ  
2083 N N   . GLU   A 270 ? 0.68383 0.57091 0.60176 0.02830  0.03613  0.02252  270 GLU   A N   
2084 C CA  . GLU   A 270 ? 0.74416 0.62548 0.64749 0.02768  0.03989  0.02109  270 GLU   A CA  
2085 C C   . GLU   A 270 ? 0.71064 0.58668 0.60631 0.02826  0.03541  0.01854  270 GLU   A C   
2086 O O   . GLU   A 270 ? 0.71819 0.58899 0.60019 0.02555  0.03566  0.01815  270 GLU   A O   
2087 C CB  . GLU   A 270 ? 0.69443 0.57803 0.59953 0.03063  0.04774  0.01835  270 GLU   A CB  
2088 C CG  . GLU   A 270 ? 0.74133 0.62130 0.63412 0.02828  0.05462  0.01827  270 GLU   A CG  
2089 C CD  . GLU   A 270 ? 0.85733 0.73717 0.75010 0.03215  0.06244  0.01440  270 GLU   A CD  
2090 O OE1 . GLU   A 270 ? 0.88659 0.77380 0.79067 0.03473  0.06675  0.01494  270 GLU   A OE1 
2091 O OE2 . GLU   A 270 ? 0.90051 0.77300 0.78240 0.03258  0.06451  0.01075  270 GLU   A OE2 
2092 N N   . LEU   A 271 ? 0.68246 0.56049 0.58646 0.03126  0.03136  0.01670  271 LEU   A N   
2093 C CA  . LEU   A 271 ? 0.67612 0.54956 0.57382 0.03159  0.02750  0.01426  271 LEU   A CA  
2094 C C   . LEU   A 271 ? 0.71270 0.58421 0.60461 0.02806  0.02129  0.01678  271 LEU   A C   
2095 O O   . LEU   A 271 ? 0.74112 0.60844 0.62234 0.02610  0.01963  0.01532  271 LEU   A O   
2096 C CB  . LEU   A 271 ? 0.64001 0.51702 0.54841 0.03558  0.02473  0.01244  271 LEU   A CB  
2097 C CG  . LEU   A 271 ? 0.61833 0.49630 0.53031 0.04010  0.02997  0.00999  271 LEU   A CG  
2098 C CD1 . LEU   A 271 ? 0.59845 0.48253 0.52207 0.04370  0.02629  0.00964  271 LEU   A CD1 
2099 C CD2 . LEU   A 271 ? 0.64485 0.51401 0.54484 0.04010  0.03330  0.00694  271 LEU   A CD2 
2100 N N   . LEU   A 272 ? 0.64922 0.52394 0.54845 0.02717  0.01800  0.02060  272 LEU   A N   
2101 C CA  . LEU   A 272 ? 0.68600 0.55959 0.58218 0.02508  0.01190  0.02372  272 LEU   A CA  
2102 C C   . LEU   A 272 ? 0.68668 0.55780 0.56997 0.02140  0.01283  0.02712  272 LEU   A C   
2103 O O   . LEU   A 272 ? 0.68352 0.55387 0.55949 0.01963  0.00826  0.02849  272 LEU   A O   
2104 C CB  . LEU   A 272 ? 0.65010 0.52664 0.55899 0.02575  0.00880  0.02655  272 LEU   A CB  
2105 C CG  . LEU   A 272 ? 0.58855 0.46864 0.50922 0.02871  0.00645  0.02309  272 LEU   A CG  
2106 C CD1 . LEU   A 272 ? 0.62209 0.50464 0.55484 0.02847  0.00487  0.02489  272 LEU   A CD1 
2107 C CD2 . LEU   A 272 ? 0.57017 0.44928 0.48789 0.02961  0.00148  0.02112  272 LEU   A CD2 
2108 N N   . GLN   A 273 ? 0.73005 0.60105 0.61035 0.02008  0.01860  0.02867  273 GLN   A N   
2109 C CA  . GLN   A 273 ? 0.75142 0.62090 0.61868 0.01636  0.01990  0.03226  273 GLN   A CA  
2110 C C   . GLN   A 273 ? 0.74714 0.61377 0.60021 0.01453  0.02413  0.02783  273 GLN   A C   
2111 O O   . GLN   A 273 ? 0.77322 0.63925 0.61336 0.01085  0.02505  0.02994  273 GLN   A O   
2112 C CB  . GLN   A 273 ? 0.70137 0.57212 0.57220 0.01521  0.02428  0.03682  273 GLN   A CB  
2113 C CG  . GLN   A 273 ? 0.73941 0.61203 0.61672 0.01680  0.03139  0.03353  273 GLN   A CG  
2114 C CD  . GLN   A 273 ? 0.75540 0.63084 0.64317 0.01605  0.03386  0.03758  273 GLN   A CD  
2115 O OE1 . GLN   A 273 ? 0.75842 0.63277 0.64786 0.01431  0.03086  0.04307  273 GLN   A OE1 
2116 N NE2 . GLN   A 273 ? 0.74405 0.62326 0.63948 0.01735  0.03957  0.03503  273 GLN   A NE2 
2117 N N   . ASN   A 274 ? 0.69762 0.56230 0.55246 0.01691  0.02696  0.02182  274 ASN   A N   
2118 C CA  . ASN   A 274 ? 0.75237 0.61256 0.59444 0.01531  0.03198  0.01675  274 ASN   A CA  
2119 C C   . ASN   A 274 ? 0.78136 0.63792 0.62094 0.01584  0.02956  0.01170  274 ASN   A C   
2120 O O   . ASN   A 274 ? 0.82547 0.67704 0.65331 0.01356  0.03336  0.00703  274 ASN   A O   
2121 C CB  . ASN   A 274 ? 0.78440 0.64396 0.62973 0.01785  0.04086  0.01417  274 ASN   A CB  
2122 C CG  . ASN   A 274 ? 0.79663 0.65958 0.64247 0.01636  0.04477  0.01852  274 ASN   A CG  
2123 O OD1 . ASN   A 274 ? 0.81094 0.67513 0.65115 0.01288  0.04179  0.02339  274 ASN   A OD1 
2124 N ND2 . ASN   A 274 ? 0.78981 0.65479 0.64284 0.01910  0.05166  0.01725  274 ASN   A ND2 
2125 N N   . GLY   A 275 ? 0.74308 0.60160 0.59296 0.01839  0.02392  0.01216  275 GLY   A N   
2126 C CA  . GLY   A 275 ? 0.76885 0.62393 0.61716 0.01891  0.02229  0.00768  275 GLY   A CA  
2127 C C   . GLY   A 275 ? 0.81026 0.66120 0.66156 0.02266  0.02910  0.00340  275 GLY   A C   
2128 O O   . GLY   A 275 ? 0.82753 0.67988 0.68415 0.02550  0.03451  0.00398  275 GLY   A O   
2129 N N   . MET   A 276 ? 0.81420 0.66016 0.66239 0.02273  0.02894  -0.00063 276 MET   A N   
2130 C CA  . MET   A 276 ? 0.84361 0.68444 0.69454 0.02683  0.03538  -0.00409 276 MET   A CA  
2131 C C   . MET   A 276 ? 0.87583 0.70786 0.71361 0.02438  0.04298  -0.00904 276 MET   A C   
2132 O O   . MET   A 276 ? 0.92009 0.74734 0.76028 0.02846  0.05012  -0.01137 276 MET   A O   
2133 C CB  . MET   A 276 ? 0.81597 0.65542 0.67224 0.02889  0.03182  -0.00525 276 MET   A CB  
2134 C CG  . MET   A 276 ? 0.79938 0.64731 0.66859 0.03146  0.02499  -0.00139 276 MET   A CG  
2135 S SD  . MET   A 276 ? 0.86123 0.70905 0.73984 0.03658  0.02435  -0.00216 276 MET   A SD  
2136 C CE  . MET   A 276 ? 0.70012 0.55787 0.58979 0.03699  0.01547  0.00117  276 MET   A CE  
2137 N N   . ASN   A 277 ? 0.87012 0.70028 0.69420 0.01791  0.04176  -0.01070 277 ASN   A N   
2138 C CA  . ASN   A 277 ? 0.92983 0.75194 0.73966 0.01429  0.04907  -0.01627 277 ASN   A CA  
2139 C C   . ASN   A 277 ? 0.98180 0.79367 0.78977 0.01541  0.05365  -0.02191 277 ASN   A C   
2140 O O   . ASN   A 277 ? 0.93603 0.74035 0.74187 0.01785  0.06271  -0.02556 277 ASN   A O   
2141 C CB  . ASN   A 277 ? 0.96765 0.79028 0.77731 0.01644  0.05685  -0.01576 277 ASN   A CB  
2142 C CG  . ASN   A 277 ? 0.98947 0.81573 0.78756 0.01070  0.05628  -0.01428 277 ASN   A CG  
2143 O OD1 . ASN   A 277 ? 1.01043 0.83178 0.79337 0.00550  0.05999  -0.01901 277 ASN   A OD1 
2144 N ND2 . ASN   A 277 ? 0.94684 0.78162 0.75168 0.01139  0.05184  -0.00769 277 ASN   A ND2 
2145 N N   . GLY   A 278 ? 0.98676 0.79812 0.79594 0.01373  0.04770  -0.02241 278 GLY   A N   
2146 C CA  . GLY   A 278 ? 0.98705 0.78814 0.79368 0.01363  0.05149  -0.02737 278 GLY   A CA  
2147 C C   . GLY   A 278 ? 0.96389 0.76259 0.78355 0.02173  0.05445  -0.02550 278 GLY   A C   
2148 O O   . GLY   A 278 ? 0.96367 0.75369 0.78243 0.02215  0.05712  -0.02842 278 GLY   A O   
2149 N N   . ARG   A 279 ? 0.95738 0.76385 0.78904 0.02790  0.05410  -0.02056 279 ARG   A N   
2150 C CA  . ARG   A 279 ? 0.86647 0.67325 0.71078 0.03575  0.05634  -0.01812 279 ARG   A CA  
2151 C C   . ARG   A 279 ? 0.82612 0.64096 0.68026 0.03718  0.04756  -0.01419 279 ARG   A C   
2152 O O   . ARG   A 279 ? 0.84731 0.66907 0.70132 0.03343  0.04010  -0.01246 279 ARG   A O   
2153 C CB  . ARG   A 279 ? 0.81803 0.63040 0.67058 0.04141  0.06109  -0.01537 279 ARG   A CB  
2154 C CG  . ARG   A 279 ? 0.80799 0.61530 0.65082 0.03923  0.06900  -0.01878 279 ARG   A CG  
2155 C CD  . ARG   A 279 ? 0.75730 0.56568 0.60871 0.04661  0.07721  -0.01759 279 ARG   A CD  
2156 N NE  . ARG   A 279 ? 0.77973 0.58380 0.63909 0.05338  0.08022  -0.01685 279 ARG   A NE  
2157 C CZ  . ARG   A 279 ? 0.75009 0.55214 0.61572 0.06046  0.08861  -0.01637 279 ARG   A CZ  
2158 N NH1 . ARG   A 279 ? 0.74475 0.54872 0.60989 0.06161  0.09530  -0.01722 279 ARG   A NH1 
2159 N NH2 . ARG   A 279 ? 0.69279 0.49123 0.56559 0.06680  0.09054  -0.01456 279 ARG   A NH2 
2160 N N   . THR   A 280 ? 0.81015 0.62407 0.67281 0.04292  0.04884  -0.01261 280 THR   A N   
2161 C CA  . THR   A 280 ? 0.74304 0.56478 0.61520 0.04491  0.04160  -0.00918 280 THR   A CA  
2162 C C   . THR   A 280 ? 0.72482 0.55547 0.61047 0.05224  0.04222  -0.00497 280 THR   A C   
2163 O O   . THR   A 280 ? 0.74215 0.57082 0.63044 0.05701  0.04916  -0.00457 280 THR   A O   
2164 C CB  . THR   A 280 ? 0.76164 0.57582 0.63133 0.04441  0.04162  -0.01065 280 THR   A CB  
2165 O OG1 . THR   A 280 ? 0.76198 0.56871 0.63399 0.05025  0.04935  -0.01039 280 THR   A OG1 
2166 C CG2 . THR   A 280 ? 0.84513 0.65099 0.70149 0.03643  0.04154  -0.01554 280 THR   A CG2 
2167 N N   . ILE   A 281 ? 0.68194 0.52308 0.57633 0.05298  0.03505  -0.00206 281 ILE   A N   
2168 C CA  . ILE   A 281 ? 0.66607 0.51772 0.57342 0.05889  0.03426  0.00155  281 ILE   A CA  
2169 C C   . ILE   A 281 ? 0.64925 0.50313 0.56115 0.06122  0.03054  0.00308  281 ILE   A C   
2170 O O   . ILE   A 281 ? 0.64772 0.50339 0.55847 0.05755  0.02442  0.00248  281 ILE   A O   
2171 C CB  . ILE   A 281 ? 0.65711 0.51975 0.57094 0.05714  0.02958  0.00310  281 ILE   A CB  
2172 C CG1 . ILE   A 281 ? 0.67843 0.53867 0.58677 0.05434  0.03344  0.00215  281 ILE   A CG1 
2173 C CG2 . ILE   A 281 ? 0.61555 0.49005 0.54263 0.06229  0.02871  0.00600  281 ILE   A CG2 
2174 C CD1 . ILE   A 281 ? 0.61155 0.48120 0.52636 0.05251  0.02993  0.00415  281 ILE   A CD1 
2175 N N   . LEU   A 282 ? 0.65432 0.50843 0.57140 0.06756  0.03445  0.00542  282 LEU   A N   
2176 C CA  . LEU   A 282 ? 0.63542 0.49128 0.55599 0.07027  0.03186  0.00763  282 LEU   A CA  
2177 C C   . LEU   A 282 ? 0.68335 0.52773 0.59429 0.06579  0.03154  0.00506  282 LEU   A C   
2178 O O   . LEU   A 282 ? 0.63225 0.47961 0.54437 0.06447  0.02666  0.00571  282 LEU   A O   
2179 C CB  . LEU   A 282 ? 0.59307 0.46356 0.52261 0.07031  0.02434  0.00942  282 LEU   A CB  
2180 C CG  . LEU   A 282 ? 0.57849 0.46125 0.51919 0.07674  0.02476  0.01327  282 LEU   A CG  
2181 C CD1 . LEU   A 282 ? 0.67171 0.55377 0.61473 0.08071  0.03153  0.01428  282 LEU   A CD1 
2182 C CD2 . LEU   A 282 ? 0.61727 0.51411 0.56582 0.07472  0.01826  0.01312  282 LEU   A CD2 
2183 N N   . GLY   A 283 ? 0.70286 0.53442 0.60420 0.06310  0.03713  0.00176  283 GLY   A N   
2184 C CA  . GLY   A 283 ? 0.68712 0.50808 0.57893 0.05761  0.03716  -0.00149 283 GLY   A CA  
2185 C C   . GLY   A 283 ? 0.75063 0.57634 0.63921 0.05071  0.02970  -0.00349 283 GLY   A C   
2186 O O   . GLY   A 283 ? 0.79802 0.61971 0.68208 0.04658  0.02761  -0.00514 283 GLY   A O   
2187 N N   . SER   A 284 ? 0.72937 0.56372 0.62068 0.04945  0.02585  -0.00305 284 SER   A N   
2188 C CA  . SER   A 284 ? 0.70083 0.54055 0.59066 0.04407  0.01877  -0.00387 284 SER   A CA  
2189 C C   . SER   A 284 ? 0.71785 0.55651 0.60120 0.04011  0.01932  -0.00538 284 SER   A C   
2190 O O   . SER   A 284 ? 0.71586 0.55691 0.60188 0.04257  0.02216  -0.00422 284 SER   A O   
2191 C CB  . SER   A 284 ? 0.67491 0.52708 0.57568 0.04653  0.01271  -0.00099 284 SER   A CB  
2192 O OG  . SER   A 284 ? 0.71754 0.57478 0.61832 0.04285  0.00785  -0.00106 284 SER   A OG  
2193 N N   . ALA   A 285 ? 0.73222 0.56841 0.60720 0.03385  0.01649  -0.00765 285 ALA   A N   
2194 C CA  . ALA   A 285 ? 0.73906 0.57540 0.60676 0.02964  0.01623  -0.00846 285 ALA   A CA  
2195 C C   . ALA   A 285 ? 0.72129 0.56773 0.59527 0.02960  0.01007  -0.00497 285 ALA   A C   
2196 O O   . ALA   A 285 ? 0.71945 0.56696 0.58858 0.02695  0.00989  -0.00424 285 ALA   A O   
2197 C CB  . ALA   A 285 ? 0.75720 0.58825 0.61304 0.02263  0.01546  -0.01214 285 ALA   A CB  
2198 N N   . LEU   A 286 ? 0.70669 0.56005 0.59100 0.03239  0.00549  -0.00281 286 LEU   A N   
2199 C CA  . LEU   A 286 ? 0.69159 0.55320 0.58302 0.03265  0.00032  0.00010  286 LEU   A CA  
2200 C C   . LEU   A 286 ? 0.67198 0.53899 0.57467 0.03761  0.00124  0.00176  286 LEU   A C   
2201 O O   . LEU   A 286 ? 0.70004 0.56694 0.60653 0.04120  0.00359  0.00128  286 LEU   A O   
2202 C CB  . LEU   A 286 ? 0.65352 0.51948 0.54758 0.03085  -0.00616 0.00041  286 LEU   A CB  
2203 C CG  . LEU   A 286 ? 0.72590 0.59090 0.61114 0.02547  -0.00914 -0.00023 286 LEU   A CG  
2204 C CD1 . LEU   A 286 ? 0.70295 0.57521 0.59445 0.02506  -0.01581 0.00150  286 LEU   A CD1 
2205 C CD2 . LEU   A 286 ? 0.69091 0.55455 0.56868 0.02290  -0.00777 0.00096  286 LEU   A CD2 
2206 N N   . LEU   A 287 ? 0.60767 0.47976 0.51573 0.03761  -0.00060 0.00394  287 LEU   A N   
2207 C CA  . LEU   A 287 ? 0.63922 0.51806 0.55869 0.04108  -0.00070 0.00495  287 LEU   A CA  
2208 C C   . LEU   A 287 ? 0.66958 0.55363 0.59617 0.04213  -0.00560 0.00447  287 LEU   A C   
2209 O O   . LEU   A 287 ? 0.71453 0.59809 0.63907 0.03998  -0.00957 0.00422  287 LEU   A O   
2210 C CB  . LEU   A 287 ? 0.60611 0.48785 0.52918 0.03985  -0.00078 0.00706  287 LEU   A CB  
2211 C CG  . LEU   A 287 ? 0.64106 0.51919 0.55805 0.03899  0.00470  0.00770  287 LEU   A CG  
2212 C CD1 . LEU   A 287 ? 0.53362 0.41404 0.45336 0.03698  0.00425  0.01047  287 LEU   A CD1 
2213 C CD2 . LEU   A 287 ? 0.64138 0.52095 0.56216 0.04286  0.01000  0.00681  287 LEU   A CD2 
2214 N N   . GLU   A 288 ? 0.61558 0.50571 0.55068 0.04541  -0.00524 0.00431  288 GLU   A N   
2215 C CA  . GLU   A 288 ? 0.61296 0.50867 0.55412 0.04655  -0.00908 0.00339  288 GLU   A CA  
2216 C C   . GLU   A 288 ? 0.58421 0.48805 0.53564 0.04697  -0.01096 0.00317  288 GLU   A C   
2217 O O   . GLU   A 288 ? 0.51714 0.42491 0.47305 0.04826  -0.00839 0.00368  288 GLU   A O   
2218 C CB  . GLU   A 288 ? 0.62066 0.51678 0.56138 0.04982  -0.00705 0.00325  288 GLU   A CB  
2219 C CG  . GLU   A 288 ? 0.69986 0.60366 0.64700 0.05137  -0.01042 0.00263  288 GLU   A CG  
2220 C CD  . GLU   A 288 ? 0.77692 0.67942 0.72183 0.04902  -0.01418 0.00139  288 GLU   A CD  
2221 O OE1 . GLU   A 288 ? 0.83910 0.73888 0.78196 0.04604  -0.01625 0.00106  288 GLU   A OE1 
2222 O OE2 . GLU   A 288 ? 0.85328 0.75826 0.79876 0.05033  -0.01498 0.00116  288 GLU   A OE2 
2223 N N   . ASP   A 289 ? 0.56466 0.47117 0.52014 0.04567  -0.01511 0.00208  289 ASP   A N   
2224 C CA  . ASP   A 289 ? 0.55326 0.46601 0.51815 0.04518  -0.01671 0.00090  289 ASP   A CA  
2225 C C   . ASP   A 289 ? 0.54318 0.46252 0.51326 0.04608  -0.01959 -0.00167 289 ASP   A C   
2226 O O   . ASP   A 289 ? 0.54335 0.46616 0.52013 0.04484  -0.02147 -0.00368 289 ASP   A O   
2227 C CB  . ASP   A 289 ? 0.55834 0.46704 0.52397 0.04262  -0.01802 0.00198  289 ASP   A CB  
2228 C CG  . ASP   A 289 ? 0.59710 0.50457 0.56266 0.04206  -0.02177 0.00146  289 ASP   A CG  
2229 O OD1 . ASP   A 289 ? 0.64224 0.54889 0.60285 0.04256  -0.02285 0.00109  289 ASP   A OD1 
2230 O OD2 . ASP   A 289 ? 0.57405 0.48130 0.54505 0.04116  -0.02326 0.00149  289 ASP   A OD2 
2231 N N   . GLU   A 290 ? 0.53865 0.45944 0.50559 0.04808  -0.01952 -0.00171 290 GLU   A N   
2232 C CA  . GLU   A 290 ? 0.57172 0.49938 0.54237 0.04888  -0.02195 -0.00382 290 GLU   A CA  
2233 C C   . GLU   A 290 ? 0.55898 0.49496 0.53256 0.05154  -0.02086 -0.00350 290 GLU   A C   
2234 O O   . GLU   A 290 ? 0.56470 0.50591 0.53851 0.05279  -0.02222 -0.00408 290 GLU   A O   
2235 C CB  . GLU   A 290 ? 0.60824 0.53201 0.57325 0.04871  -0.02319 -0.00365 290 GLU   A CB  
2236 C CG  . GLU   A 290 ? 0.63947 0.55829 0.60314 0.04630  -0.02520 -0.00385 290 GLU   A CG  
2237 C CD  . GLU   A 290 ? 0.68693 0.60805 0.65115 0.04586  -0.02774 -0.00538 290 GLU   A CD  
2238 O OE1 . GLU   A 290 ? 0.72112 0.64491 0.68351 0.04693  -0.02737 -0.00567 290 GLU   A OE1 
2239 O OE2 . GLU   A 290 ? 0.66511 0.58559 0.63191 0.04468  -0.02984 -0.00591 290 GLU   A OE2 
2240 N N   . PHE   A 291 ? 0.57658 0.51483 0.55259 0.05252  -0.01841 -0.00220 291 PHE   A N   
2241 C CA  . PHE   A 291 ? 0.54076 0.48927 0.52122 0.05527  -0.01765 -0.00135 291 PHE   A CA  
2242 C C   . PHE   A 291 ? 0.52987 0.48648 0.51871 0.05312  -0.01813 -0.00344 291 PHE   A C   
2243 O O   . PHE   A 291 ? 0.52188 0.47559 0.51189 0.05216  -0.01572 -0.00252 291 PHE   A O   
2244 C CB  . PHE   A 291 ? 0.56384 0.50880 0.54056 0.05894  -0.01356 0.00240  291 PHE   A CB  
2245 C CG  . PHE   A 291 ? 0.59990 0.53843 0.56953 0.06122  -0.01253 0.00434  291 PHE   A CG  
2246 C CD1 . PHE   A 291 ? 0.60266 0.54811 0.57338 0.06418  -0.01345 0.00587  291 PHE   A CD1 
2247 C CD2 . PHE   A 291 ? 0.62694 0.55277 0.58856 0.06002  -0.01048 0.00471  291 PHE   A CD2 
2248 C CE1 . PHE   A 291 ? 0.61941 0.55797 0.58374 0.06599  -0.01194 0.00802  291 PHE   A CE1 
2249 C CE2 . PHE   A 291 ? 0.63472 0.55401 0.59003 0.06128  -0.00907 0.00602  291 PHE   A CE2 
2250 C CZ  . PHE   A 291 ? 0.62370 0.54873 0.58056 0.06433  -0.00958 0.00783  291 PHE   A CZ  
2251 N N   . THR   A 292 ? 0.53692 0.50377 0.53132 0.05187  -0.02093 -0.00651 292 THR   A N   
2252 C CA  . THR   A 292 ? 0.53963 0.51506 0.54231 0.04900  -0.02126 -0.00927 292 THR   A CA  
2253 C C   . THR   A 292 ? 0.55302 0.53832 0.55954 0.05152  -0.01943 -0.00663 292 THR   A C   
2254 O O   . THR   A 292 ? 0.53604 0.52277 0.53937 0.05613  -0.01833 -0.00284 292 THR   A O   
2255 C CB  . THR   A 292 ? 0.55135 0.53549 0.55823 0.04647  -0.02449 -0.01417 292 THR   A CB  
2256 O OG1 . THR   A 292 ? 0.57779 0.57581 0.58637 0.04868  -0.02580 -0.01349 292 THR   A OG1 
2257 C CG2 . THR   A 292 ? 0.54230 0.51901 0.54459 0.04620  -0.02613 -0.01567 292 THR   A CG2 
2258 N N   . PRO   A 293 ? 0.55470 0.54683 0.56863 0.04864  -0.01870 -0.00834 293 PRO   A N   
2259 C CA  . PRO   A 293 ? 0.59997 0.60490 0.61936 0.05103  -0.01737 -0.00599 293 PRO   A CA  
2260 C C   . PRO   A 293 ? 0.63927 0.65830 0.66025 0.05390  -0.02017 -0.00530 293 PRO   A C   
2261 O O   . PRO   A 293 ? 0.59303 0.61886 0.61499 0.05894  -0.01881 -0.00072 293 PRO   A O   
2262 C CB  . PRO   A 293 ? 0.57081 0.58182 0.59864 0.04560  -0.01697 -0.00947 293 PRO   A CB  
2263 C CG  . PRO   A 293 ? 0.56465 0.56060 0.58945 0.04201  -0.01605 -0.01112 293 PRO   A CG  
2264 C CD  . PRO   A 293 ? 0.50231 0.48985 0.52012 0.04330  -0.01837 -0.01173 293 PRO   A CD  
2265 N N   . PHE   A 294 ? 0.67348 0.69715 0.69460 0.05107  -0.02380 -0.00951 294 PHE   A N   
2266 C CA  . PHE   A 294 ? 0.66807 0.70604 0.68964 0.05334  -0.02671 -0.00878 294 PHE   A CA  
2267 C C   . PHE   A 294 ? 0.61281 0.64439 0.62668 0.05926  -0.02592 -0.00337 294 PHE   A C   
2268 O O   . PHE   A 294 ? 0.63835 0.68041 0.65265 0.06371  -0.02652 0.00086  294 PHE   A O   
2269 C CB  . PHE   A 294 ? 0.69686 0.74029 0.71943 0.04829  -0.03016 -0.01541 294 PHE   A CB  
2270 C CG  . PHE   A 294 ? 0.86595 0.91543 0.89635 0.04175  -0.03057 -0.02153 294 PHE   A CG  
2271 C CD1 . PHE   A 294 ? 0.88456 0.95269 0.92035 0.03866  -0.03330 -0.02524 294 PHE   A CD1 
2272 C CD2 . PHE   A 294 ? 0.89300 0.92961 0.92508 0.03827  -0.02817 -0.02363 294 PHE   A CD2 
2273 C CE1 . PHE   A 294 ? 0.87842 0.95161 0.92145 0.03175  -0.03329 -0.03158 294 PHE   A CE1 
2274 C CE2 . PHE   A 294 ? 0.99343 1.03426 1.03287 0.03195  -0.02792 -0.02911 294 PHE   A CE2 
2275 C CZ  . PHE   A 294 ? 0.88425 0.94297 0.92929 0.02840  -0.03032 -0.03349 294 PHE   A CZ  
2276 N N   . ASP   A 295 ? 0.62841 0.64314 0.63540 0.05924  -0.02452 -0.00320 295 ASP   A N   
2277 C CA  . ASP   A 295 ? 0.61842 0.62526 0.61800 0.06389  -0.02310 0.00145  295 ASP   A CA  
2278 C C   . ASP   A 295 ? 0.63280 0.63845 0.63258 0.06924  -0.01925 0.00721  295 ASP   A C   
2279 O O   . ASP   A 295 ? 0.65058 0.65774 0.64780 0.07430  -0.01826 0.01202  295 ASP   A O   
2280 C CB  . ASP   A 295 ? 0.61375 0.60380 0.60669 0.06183  -0.02234 -0.00004 295 ASP   A CB  
2281 C CG  . ASP   A 295 ? 0.58764 0.57854 0.57991 0.05825  -0.02560 -0.00465 295 ASP   A CG  
2282 O OD1 . ASP   A 295 ? 0.63503 0.63798 0.62924 0.05812  -0.02805 -0.00606 295 ASP   A OD1 
2283 O OD2 . ASP   A 295 ? 0.55784 0.53804 0.54770 0.05568  -0.02559 -0.00679 295 ASP   A OD2 
2284 N N   . VAL   A 296 ? 0.61709 0.61968 0.62000 0.06838  -0.01656 0.00698  296 VAL   A N   
2285 C CA  . VAL   A 296 ? 0.62472 0.62511 0.62797 0.07350  -0.01199 0.01183  296 VAL   A CA  
2286 C C   . VAL   A 296 ? 0.66528 0.68359 0.67589 0.07791  -0.01261 0.01547  296 VAL   A C   
2287 O O   . VAL   A 296 ? 0.67612 0.69428 0.68569 0.08434  -0.00996 0.02104  296 VAL   A O   
2288 C CB  . VAL   A 296 ? 0.56316 0.55694 0.56780 0.07095  -0.00878 0.01037  296 VAL   A CB  
2289 C CG1 . VAL   A 296 ? 0.56758 0.56053 0.57341 0.07635  -0.00345 0.01479  296 VAL   A CG1 
2290 C CG2 . VAL   A 296 ? 0.53698 0.51389 0.53361 0.06729  -0.00837 0.00799  296 VAL   A CG2 
2291 N N   . VAL   A 297 ? 0.63335 0.66759 0.65176 0.07446  -0.01600 0.01247  297 VAL   A N   
2292 C CA  . VAL   A 297 ? 0.64613 0.70056 0.67214 0.07801  -0.01746 0.01582  297 VAL   A CA  
2293 C C   . VAL   A 297 ? 0.70110 0.76069 0.72319 0.08226  -0.01978 0.01971  297 VAL   A C   
2294 O O   . VAL   A 297 ? 0.70442 0.77279 0.72917 0.08893  -0.01874 0.02622  297 VAL   A O   
2295 C CB  . VAL   A 297 ? 0.61145 0.68196 0.64580 0.07173  -0.02104 0.01049  297 VAL   A CB  
2296 C CG1 . VAL   A 297 ? 0.57169 0.66496 0.61116 0.07358  -0.02507 0.01243  297 VAL   A CG1 
2297 C CG2 . VAL   A 297 ? 0.56328 0.63502 0.60451 0.07004  -0.01774 0.00985  297 VAL   A CG2 
2298 N N   . ARG   A 298 ? 0.70677 0.76096 0.72268 0.07875  -0.02260 0.01626  298 ARG   A N   
2299 C CA  . ARG   A 298 ? 0.77131 0.82988 0.78263 0.08202  -0.02459 0.01980  298 ARG   A CA  
2300 C C   . ARG   A 298 ? 0.71308 0.76033 0.71963 0.08927  -0.02018 0.02719  298 ARG   A C   
2301 O O   . ARG   A 298 ? 0.71002 0.76620 0.71731 0.09512  -0.02025 0.03371  298 ARG   A O   
2302 C CB  . ARG   A 298 ? 0.72664 0.77836 0.73190 0.07673  -0.02718 0.01431  298 ARG   A CB  
2303 C CG  . ARG   A 298 ? 0.84105 0.88930 0.83891 0.07974  -0.02745 0.01808  298 ARG   A CG  
2304 C CD  . ARG   A 298 ? 0.85756 0.90927 0.85230 0.07455  -0.03115 0.01243  298 ARG   A CD  
2305 N NE  . ARG   A 298 ? 0.87398 0.91829 0.86993 0.06822  -0.03177 0.00464  298 ARG   A NE  
2306 C CZ  . ARG   A 298 ? 0.87013 0.92373 0.87217 0.06341  -0.03393 -0.00128 298 ARG   A CZ  
2307 N NH1 . ARG   A 298 ? 0.81309 0.88546 0.82061 0.06334  -0.03620 -0.00115 298 ARG   A NH1 
2308 N NH2 . ARG   A 298 ? 0.80906 0.85313 0.81193 0.05843  -0.03372 -0.00734 298 ARG   A NH2 
2309 N N   . GLN   A 299 ? 0.74868 0.77616 0.75020 0.08887  -0.01608 0.02637  299 GLN   A N   
2310 C CA  . GLN   A 299 ? 0.75871 0.77288 0.75495 0.09467  -0.01116 0.03207  299 GLN   A CA  
2311 C C   . GLN   A 299 ? 0.76313 0.78118 0.76523 0.10130  -0.00688 0.03746  299 GLN   A C   
2312 O O   . GLN   A 299 ? 0.77897 0.79196 0.77920 0.10795  -0.00314 0.04382  299 GLN   A O   
2313 C CB  . GLN   A 299 ? 0.67127 0.66416 0.65972 0.09109  -0.00839 0.02853  299 GLN   A CB  
2314 C CG  . GLN   A 299 ? 0.63707 0.61438 0.61851 0.09522  -0.00342 0.03282  299 GLN   A CG  
2315 C CD  . GLN   A 299 ? 0.61809 0.57849 0.59093 0.09010  -0.00285 0.02872  299 GLN   A CD  
2316 O OE1 . GLN   A 299 ? 0.63802 0.58335 0.60474 0.09148  0.00176  0.03027  299 GLN   A OE1 
2317 N NE2 . GLN   A 299 ? 0.62447 0.58763 0.59713 0.08406  -0.00738 0.02335  299 GLN   A NE2 
2318 N N   . CYS   A 300 ? 0.76251 0.78931 0.77214 0.09973  -0.00691 0.03520  300 CYS   A N   
2319 C CA  . CYS   A 300 ? 0.76198 0.79357 0.77833 0.10578  -0.00247 0.03977  300 CYS   A CA  
2320 C C   . CYS   A 300 ? 0.79538 0.85208 0.82196 0.10919  -0.00575 0.04362  300 CYS   A C   
2321 O O   . CYS   A 300 ? 0.80234 0.86681 0.83659 0.11438  -0.00254 0.04760  300 CYS   A O   
2322 C CB  . CYS   A 300 ? 0.71731 0.74222 0.73539 0.10194  0.00057  0.03531  300 CYS   A CB  
2323 S SG  . CYS   A 300 ? 0.71693 0.71504 0.72283 0.09726  0.00369  0.03079  300 CYS   A SG  
2324 N N   . SER   A 301 ? 0.76420 0.83467 0.79110 0.10632  -0.01197 0.04244  301 SER   A N   
2325 C CA  . SER   A 301 ? 0.74701 0.84304 0.78249 0.10927  -0.01574 0.04635  301 SER   A CA  
2326 C C   . SER   A 301 ? 0.84885 0.95357 0.88015 0.11119  -0.01990 0.05005  301 SER   A C   
2327 O O   . SER   A 301 ? 0.87825 1.00391 0.91557 0.11545  -0.02257 0.05550  301 SER   A O   
2328 C CB  . SER   A 301 ? 0.73284 0.84480 0.77577 0.10165  -0.01989 0.03949  301 SER   A CB  
2329 O OG  . SER   A 301 ? 0.79300 0.90018 0.84104 0.10035  -0.01587 0.03734  301 SER   A OG  
2330 N N   . GLY   A 302 ? 0.77857 0.86930 0.79999 0.10824  -0.02053 0.04766  302 GLY   A N   
2331 C CA  . GLY   A 302 ? 0.80960 0.90765 0.82621 0.10993  -0.02379 0.05142  302 GLY   A CA  
2332 C C   . GLY   A 302 ? 0.88506 1.00560 0.90455 0.10453  -0.03063 0.04715  302 GLY   A C   
2333 O O   . GLY   A 302 ? 0.90305 1.04541 0.92796 0.10798  -0.03358 0.05207  302 GLY   A O   
2334 N N   . VAL   A 303 ? 0.87122 0.98702 0.88719 0.09602  -0.03307 0.03791  303 VAL   A N   
2335 C CA  . VAL   A 303 ? 0.93132 1.06671 0.94957 0.08984  -0.03887 0.03212  303 VAL   A CA  
2336 C C   . VAL   A 303 ? 0.91999 1.06593 0.93234 0.09182  -0.04198 0.03616  303 VAL   A C   
2337 O O   . VAL   A 303 ? 0.94946 1.11893 0.96500 0.09131  -0.04642 0.03710  303 VAL   A O   
2338 C CB  . VAL   A 303 ? 0.85751 0.98279 0.87417 0.08077  -0.03958 0.02115  303 VAL   A CB  
2339 C CG1 . VAL   A 303 ? 0.77896 0.91701 0.79312 0.07479  -0.04436 0.01501  303 VAL   A CG1 
2340 C CG2 . VAL   A 303 ? 0.78126 0.90818 0.80637 0.07717  -0.03862 0.01672  303 VAL   A CG2 
2341 N N   . THR   A 304 ? 0.86278 0.99243 0.86631 0.09374  -0.03966 0.03873  304 THR   A N   
2342 C CA  . THR   A 304 ? 0.77249 0.90981 0.76940 0.09580  -0.04170 0.04343  304 THR   A CA  
2343 C C   . THR   A 304 ? 0.75132 0.90485 0.74659 0.08842  -0.04700 0.03570  304 THR   A C   
2344 O O   . THR   A 304 ? 0.74318 0.89146 0.73094 0.08532  -0.04743 0.03273  304 THR   A O   
2345 C CB  . THR   A 304 ? 0.72725 0.87879 0.72706 0.10476  -0.04180 0.05535  304 THR   A CB  
2346 O OG1 . THR   A 304 ? 0.61656 0.74893 0.61372 0.11201  -0.03593 0.06333  304 THR   A OG1 
2347 C CG2 . THR   A 304 ? 0.60390 0.77381 0.59884 0.10490  -0.04615 0.05876  304 THR   A CG2 
2348 C C13 . A1ALD B .   ? 0.54076 0.53952 0.56013 0.04553  -0.03569 -0.02727 401 A1ALD A C13 
2349 C C17 . A1ALD B .   ? 0.55119 0.55858 0.57490 0.04417  -0.03640 -0.02567 401 A1ALD A C17 
2350 C C22 . A1ALD B .   ? 0.58761 0.59405 0.64527 0.06039  -0.04121 -0.01819 401 A1ALD A C22 
2351 C C24 . A1ALD B .   ? 0.55774 0.57353 0.61512 0.05820  -0.04866 -0.00792 401 A1ALD A C24 
2352 C C26 . A1ALD B .   ? 0.54706 0.56434 0.61569 0.06567  -0.05382 0.00324  401 A1ALD A C26 
2353 C C28 . A1ALD B .   ? 0.53157 0.55905 0.61579 0.07429  -0.05889 0.01563  401 A1ALD A C28 
2354 C C02 . A1ALD B .   ? 0.57829 0.58294 0.63165 0.05871  -0.03742 -0.02472 401 A1ALD A C02 
2355 C C04 . A1ALD B .   ? 0.57460 0.58484 0.63071 0.05924  -0.03003 -0.03638 401 A1ALD A C04 
2356 C C05 . A1ALD B .   ? 0.58303 0.59949 0.64868 0.06240  -0.02560 -0.04216 401 A1ALD A C05 
2357 C C06 . A1ALD B .   ? 0.61729 0.62745 0.69309 0.06763  -0.02383 -0.04359 401 A1ALD A C06 
2358 C C07 . A1ALD B .   ? 0.60107 0.60059 0.67153 0.06638  -0.02301 -0.04680 401 A1ALD A C07 
2359 C C08 . A1ALD B .   ? 0.62874 0.64505 0.71506 0.07123  -0.01887 -0.04921 401 A1ALD A C08 
2360 C C09 . A1ALD B .   ? 0.54470 0.55902 0.59073 0.05417  -0.03039 -0.03596 401 A1ALD A C09 
2361 C C11 . A1ALD B .   ? 0.54603 0.55714 0.57247 0.04736  -0.03001 -0.03581 401 A1ALD A C11 
2362 C C12 . A1ALD B .   ? 0.54092 0.54362 0.55784 0.04494  -0.03247 -0.03148 401 A1ALD A C12 
2363 C C14 . A1ALD B .   ? 0.61849 0.60925 0.62841 0.04287  -0.03762 -0.02342 401 A1ALD A C14 
2364 C C16 . A1ALD B .   ? 0.56393 0.56814 0.57701 0.03891  -0.03733 -0.02260 401 A1ALD A C16 
2365 C C19 . A1ALD B .   ? 0.54598 0.56071 0.56932 0.04690  -0.02669 -0.04093 401 A1ALD A C19 
2366 C C23 . A1ALD B .   ? 0.54652 0.55904 0.60031 0.05684  -0.04472 -0.01402 401 A1ALD A C23 
2367 C C25 . A1ALD B .   ? 0.56505 0.57764 0.63035 0.06388  -0.04925 -0.00447 401 A1ALD A C25 
2368 C C27 . A1ALD B .   ? 0.51315 0.53475 0.59458 0.07233  -0.05411 0.00724  401 A1ALD A C27 
2369 C C29 . A1ALD B .   ? 0.51274 0.54184 0.58601 0.06877  -0.06343 0.01921  401 A1ALD A C29 
2370 C C30 . A1ALD B .   ? 0.49498 0.51841 0.55465 0.06147  -0.06281 0.01447  401 A1ALD A C30 
2371 C C33 . A1ALD B .   ? 0.57475 0.58510 0.59854 0.04324  -0.06364 0.00879  401 A1ALD A C33 
2372 C C34 . A1ALD B .   ? 0.54504 0.55790 0.58936 0.05362  -0.05850 0.00506  401 A1ALD A C34 
2373 C C35 . A1ALD B .   ? 0.53611 0.55361 0.59404 0.06040  -0.05805 0.00707  401 A1ALD A C35 
2374 C C36 . A1ALD B .   ? 0.57839 0.58307 0.64781 0.06744  -0.04511 -0.00874 401 A1ALD A C36 
2375 C C37 . A1ALD B .   ? 0.59821 0.60031 0.66392 0.06548  -0.04137 -0.01572 401 A1ALD A C37 
2376 N N03 . A1ALD B .   ? 0.57733 0.58772 0.63808 0.06102  -0.03358 -0.02997 401 A1ALD A N03 
2377 N N10 . A1ALD B .   ? 0.52305 0.53162 0.55885 0.05152  -0.03022 -0.03700 401 A1ALD A N10 
2378 N N15 . A1ALD B .   ? 0.64306 0.63679 0.64923 0.03898  -0.03839 -0.02097 401 A1ALD A N15 
2379 N N20 . A1ALD B .   ? 0.53804 0.55997 0.55888 0.04497  -0.02451 -0.04211 401 A1ALD A N20 
2380 N N31 . A1ALD B .   ? 0.53273 0.55519 0.57972 0.05494  -0.06584 0.01584  401 A1ALD A N31 
2381 N N32 . A1ALD B .   ? 0.54203 0.55725 0.58025 0.05047  -0.06282 0.00992  401 A1ALD A N32 
2382 O O01 . A1ALD B .   ? 0.56011 0.55885 0.60348 0.05550  -0.03743 -0.02560 401 A1ALD A O01 
2383 O O18 . A1ALD B .   ? 0.58017 0.56337 0.58624 0.04346  -0.03809 -0.02267 401 A1ALD A O18 
2384 O O21 . A1ALD B .   ? 0.54208 0.56459 0.58958 0.05260  -0.03060 -0.03449 401 A1ALD A O21 
2385 O O   . HOH   C .   ? 0.71668 0.64414 0.85787 0.08169  0.03535  -0.12235 501 HOH   A O   
2386 O O   . HOH   C .   ? 0.67449 0.62008 0.65938 0.05153  0.06128  0.01670  502 HOH   A O   
2387 O O   . HOH   C .   ? 0.71528 0.83307 0.61133 0.05490  -0.02662 0.02261  503 HOH   A O   
2388 O O   . HOH   C .   ? 0.87466 0.85989 0.90493 0.11578  0.00000  -0.00000 504 HOH   A O   
2389 O O   . HOH   C .   ? 0.56632 0.59084 0.52895 0.04377  -0.02861 -0.03089 505 HOH   A O   
2390 O O   . HOH   C .   ? 0.67353 0.55547 0.69215 0.04728  -0.02759 0.01278  506 HOH   A O   
2391 O O   . HOH   C .   ? 0.53337 0.54533 0.53331 0.02198  -0.03673 -0.01789 507 HOH   A O   
2392 O O   . HOH   C .   ? 0.48637 0.41160 0.45580 0.05200  -0.01162 0.00162  508 HOH   A O   
2393 O O   . HOH   C .   ? 0.57862 0.58079 0.58184 0.03730  -0.06981 0.01728  509 HOH   A O   
2394 O O   . HOH   C .   ? 0.54779 0.43688 0.58534 0.03760  -0.01932 -0.01491 510 HOH   A O   
2395 O O   . HOH   C .   ? 0.97217 0.89786 0.97698 0.13008  0.09607  0.02933  511 HOH   A O   
2396 O O   . HOH   C .   ? 0.84465 0.74953 0.77281 0.05437  0.10186  0.00887  512 HOH   A O   
2397 O O   . HOH   C .   ? 0.64167 0.75376 0.53962 0.04746  -0.02249 0.00930  513 HOH   A O   
2398 O O   . HOH   C .   ? 0.54373 0.54924 0.53639 0.05162  -0.03274 -0.01654 514 HOH   A O   
2399 O O   . HOH   C .   ? 0.58176 0.47873 0.62677 0.05938  -0.03073 -0.00079 515 HOH   A O   
2400 O O   . HOH   C .   ? 0.60889 0.84878 0.50210 -0.00924 0.05327  -0.19729 516 HOH   A O   
2401 O O   . HOH   C .   ? 0.62021 0.59247 0.59351 0.06757  -0.02078 0.00718  517 HOH   A O   
2402 O O   . HOH   C .   ? 0.76547 0.67946 0.74141 0.00495  0.05831  0.03982  518 HOH   A O   
2403 O O   . HOH   C .   ? 0.58588 0.60238 0.60603 0.02261  -0.02421 -0.09685 519 HOH   A O   
2404 O O   . HOH   C .   ? 0.63099 0.72944 0.72248 0.06302  0.01664  -0.08798 520 HOH   A O   
2405 O O   . HOH   C .   ? 0.74475 0.57054 0.50880 -0.00018 0.07045  -0.01767 521 HOH   A O   
2406 O O   . HOH   C .   ? 0.61661 0.62482 0.79364 0.12907  -0.03417 0.02571  522 HOH   A O   
2407 O O   . HOH   C .   ? 0.51075 0.47273 0.52906 0.03441  -0.02189 -0.02136 523 HOH   A O   
2408 O O   . HOH   C .   ? 0.61941 0.54626 0.69097 0.00501  -0.00773 -0.08358 524 HOH   A O   
2409 O O   . HOH   C .   ? 0.56769 0.73571 0.63204 0.08957  -0.03076 0.03068  525 HOH   A O   
2410 O O   . HOH   C .   ? 0.77658 0.64957 0.74876 0.12748  0.11549  0.01783  526 HOH   A O   
2411 O O   . HOH   C .   ? 0.87579 0.74429 0.82289 0.10452  0.12012  0.00450  527 HOH   A O   
# 
