data_9HAK
# 
_entry.id   9HAK 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.399 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9HAK         pdb_00009hak 10.2210/pdb9hak/pdb 
WWPDB D_1292142948 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2024-12-04 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9HAK 
_pdbx_database_status.recvd_initial_deposition_date   2024-11-04 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_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                 2 
_pdbx_contact_author.email              aengus.mac-sweeney@idorsia.com 
_pdbx_contact_author.name_first         Aengus 
_pdbx_contact_author.name_last          'Mac Sweeney' 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-7250-9541 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Mac Sweeney, A.' 1 ? 
'Hazemann, J.'    2 ? 
# 
_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                     
;Accelerating the hit-to-lead optimization of a SARS-CoV-2 Mpro inhibitor series by combining high throughput medicinal chemistry and computational simulations
;
_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 'Hazemann, J.'    1 ? 
primary 'Mac Sweeney, A.' 2 ? 
primary 'Lange, R.'       3 ? 
primary 'Bourquin, G.'    4 ? 
primary 'Ritz, D.'        5 ? 
primary 'Richard, S.'     6 ? 
primary 'Regeon, S.'      7 ? 
primary 'Czodrowski, P.'  8 ? 
# 
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 2   3.4.22.69 ? ? ? 
2 non-polymer syn 
'(5~{R})-4-[(4-bromanyl-2-ethyl-phenyl)methyl]-~{N}-ethyl-1-thieno[2,3-c]pyridin-4-ylcarbonyl-1,4-diazepane-5-carboxamide' 529.492 
2   ?         ? ? ? 
3 non-polymer syn 'CHLORIDE ION' 35.453    1   ?         ? ? ? 
4 non-polymer syn 'SODIUM ION' 22.990    1   ?         ? ? ? 
5 water       nat water 18.015    604 ?         ? ? ? 
# 
_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,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 '(5~{R})-4-[(4-bromanyl-2-ethyl-phenyl)methyl]-~{N}-ethyl-1-thieno[2,3-c]pyridin-4-ylcarbonyl-1,4-diazepane-5-carboxamide' A1ITI 
3 'CHLORIDE ION'                                                                                                             CL    
4 'SODIUM ION'                                                                                                               NA    
5 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                 ? 
_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' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1ITI non-polymer         . 
'(5~{R})-4-[(4-bromanyl-2-ethyl-phenyl)methyl]-~{N}-ethyl-1-thieno[2,3-c]pyridin-4-ylcarbonyl-1,4-diazepane-5-carboxamide' ? 
'C25 H29 Br N4 O2 S' 529.492 
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 
CL    non-polymer         . 'CHLORIDE ION' ? 'Cl -1'              35.453  
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 
NA    non-polymer         . 'SODIUM ION' ? 'Na 1'               22.990  
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 305 305 305 PHE PHE A . n 
A 1 306 GLN 306 306 306 GLN GLN A . n 
B 1 1   SER 1   1   1   SER SER B . n 
B 1 2   GLY 2   2   2   GLY GLY B . n 
B 1 3   PHE 3   3   3   PHE PHE B . n 
B 1 4   ARG 4   4   4   ARG ARG B . n 
B 1 5   LYS 5   5   5   LYS LYS B . n 
B 1 6   MET 6   6   6   MET MET B . n 
B 1 7   ALA 7   7   7   ALA ALA B . n 
B 1 8   PHE 8   8   8   PHE PHE B . n 
B 1 9   PRO 9   9   9   PRO PRO B . n 
B 1 10  SER 10  10  10  SER SER B . n 
B 1 11  GLY 11  11  11  GLY GLY B . n 
B 1 12  LYS 12  12  12  LYS LYS B . n 
B 1 13  VAL 13  13  13  VAL VAL B . n 
B 1 14  GLU 14  14  14  GLU GLU B . n 
B 1 15  GLY 15  15  15  GLY GLY B . n 
B 1 16  CYS 16  16  16  CYS CYS B . n 
B 1 17  MET 17  17  17  MET MET B . n 
B 1 18  VAL 18  18  18  VAL VAL B . n 
B 1 19  GLN 19  19  19  GLN GLN B . n 
B 1 20  VAL 20  20  20  VAL VAL B . n 
B 1 21  THR 21  21  21  THR THR B . n 
B 1 22  CYS 22  22  22  CYS CYS B . n 
B 1 23  GLY 23  23  23  GLY GLY B . n 
B 1 24  THR 24  24  24  THR THR B . n 
B 1 25  THR 25  25  25  THR THR B . n 
B 1 26  THR 26  26  26  THR THR B . n 
B 1 27  LEU 27  27  27  LEU LEU B . n 
B 1 28  ASN 28  28  28  ASN ASN B . n 
B 1 29  GLY 29  29  29  GLY GLY B . n 
B 1 30  LEU 30  30  30  LEU LEU B . n 
B 1 31  TRP 31  31  31  TRP TRP B . n 
B 1 32  LEU 32  32  32  LEU LEU B . n 
B 1 33  ASP 33  33  33  ASP ASP B . n 
B 1 34  ASP 34  34  34  ASP ASP B . n 
B 1 35  VAL 35  35  35  VAL VAL B . n 
B 1 36  VAL 36  36  36  VAL VAL B . n 
B 1 37  TYR 37  37  37  TYR TYR B . n 
B 1 38  CYS 38  38  38  CYS CYS B . n 
B 1 39  PRO 39  39  39  PRO PRO B . n 
B 1 40  ARG 40  40  40  ARG ARG B . n 
B 1 41  HIS 41  41  41  HIS HIS B . n 
B 1 42  VAL 42  42  42  VAL VAL B . n 
B 1 43  ILE 43  43  43  ILE ILE B . n 
B 1 44  CYS 44  44  44  CYS CYS B . n 
B 1 45  THR 45  45  45  THR THR B . n 
B 1 46  SER 46  46  46  SER SER B . n 
B 1 47  GLU 47  47  47  GLU GLU B . n 
B 1 48  ASP 48  48  48  ASP ASP B . n 
B 1 49  MET 49  49  49  MET MET B . n 
B 1 50  LEU 50  50  50  LEU LEU B . n 
B 1 51  ASN 51  51  51  ASN ASN B . n 
B 1 52  PRO 52  52  52  PRO PRO B . n 
B 1 53  ASN 53  53  53  ASN ASN B . n 
B 1 54  TYR 54  54  54  TYR TYR B . n 
B 1 55  GLU 55  55  55  GLU GLU B . n 
B 1 56  ASP 56  56  56  ASP ASP B . n 
B 1 57  LEU 57  57  57  LEU LEU B . n 
B 1 58  LEU 58  58  58  LEU LEU B . n 
B 1 59  ILE 59  59  59  ILE ILE B . n 
B 1 60  ARG 60  60  60  ARG ARG B . n 
B 1 61  LYS 61  61  61  LYS LYS B . n 
B 1 62  SER 62  62  62  SER SER B . n 
B 1 63  ASN 63  63  63  ASN ASN B . n 
B 1 64  HIS 64  64  64  HIS HIS B . n 
B 1 65  ASN 65  65  65  ASN ASN B . n 
B 1 66  PHE 66  66  66  PHE PHE B . n 
B 1 67  LEU 67  67  67  LEU LEU B . n 
B 1 68  VAL 68  68  68  VAL VAL B . n 
B 1 69  GLN 69  69  69  GLN GLN B . n 
B 1 70  ALA 70  70  70  ALA ALA B . n 
B 1 71  GLY 71  71  71  GLY GLY B . n 
B 1 72  ASN 72  72  72  ASN ASN B . n 
B 1 73  VAL 73  73  73  VAL VAL B . n 
B 1 74  GLN 74  74  74  GLN GLN B . n 
B 1 75  LEU 75  75  75  LEU LEU B . n 
B 1 76  ARG 76  76  76  ARG ARG B . n 
B 1 77  VAL 77  77  77  VAL VAL B . n 
B 1 78  ILE 78  78  78  ILE ILE B . n 
B 1 79  GLY 79  79  79  GLY GLY B . n 
B 1 80  HIS 80  80  80  HIS HIS B . n 
B 1 81  SER 81  81  81  SER SER B . n 
B 1 82  MET 82  82  82  MET MET B . n 
B 1 83  GLN 83  83  83  GLN GLN B . n 
B 1 84  ASN 84  84  84  ASN ASN B . n 
B 1 85  CYS 85  85  85  CYS CYS B . n 
B 1 86  VAL 86  86  86  VAL VAL B . n 
B 1 87  LEU 87  87  87  LEU LEU B . n 
B 1 88  LYS 88  88  88  LYS LYS B . n 
B 1 89  LEU 89  89  89  LEU LEU B . n 
B 1 90  LYS 90  90  90  LYS LYS B . n 
B 1 91  VAL 91  91  91  VAL VAL B . n 
B 1 92  ASP 92  92  92  ASP ASP B . n 
B 1 93  THR 93  93  93  THR THR B . n 
B 1 94  ALA 94  94  94  ALA ALA B . n 
B 1 95  ASN 95  95  95  ASN ASN B . n 
B 1 96  PRO 96  96  96  PRO PRO B . n 
B 1 97  LYS 97  97  97  LYS LYS B . n 
B 1 98  THR 98  98  98  THR THR B . n 
B 1 99  PRO 99  99  99  PRO PRO B . n 
B 1 100 LYS 100 100 100 LYS LYS B . n 
B 1 101 TYR 101 101 101 TYR TYR B . n 
B 1 102 LYS 102 102 102 LYS LYS B . n 
B 1 103 PHE 103 103 103 PHE PHE B . n 
B 1 104 VAL 104 104 104 VAL VAL B . n 
B 1 105 ARG 105 105 105 ARG ARG B . n 
B 1 106 ILE 106 106 106 ILE ILE B . n 
B 1 107 GLN 107 107 107 GLN GLN B . n 
B 1 108 PRO 108 108 108 PRO PRO B . n 
B 1 109 GLY 109 109 109 GLY GLY B . n 
B 1 110 GLN 110 110 110 GLN GLN B . n 
B 1 111 THR 111 111 111 THR THR B . n 
B 1 112 PHE 112 112 112 PHE PHE B . n 
B 1 113 SER 113 113 113 SER SER B . n 
B 1 114 VAL 114 114 114 VAL VAL B . n 
B 1 115 LEU 115 115 115 LEU LEU B . n 
B 1 116 ALA 116 116 116 ALA ALA B . n 
B 1 117 CYS 117 117 117 CYS CYS B . n 
B 1 118 TYR 118 118 118 TYR TYR B . n 
B 1 119 ASN 119 119 119 ASN ASN B . n 
B 1 120 GLY 120 120 120 GLY GLY B . n 
B 1 121 SER 121 121 121 SER SER B . n 
B 1 122 PRO 122 122 122 PRO PRO B . n 
B 1 123 SER 123 123 123 SER SER B . n 
B 1 124 GLY 124 124 124 GLY GLY B . n 
B 1 125 VAL 125 125 125 VAL VAL B . n 
B 1 126 TYR 126 126 126 TYR TYR B . n 
B 1 127 GLN 127 127 127 GLN GLN B . n 
B 1 128 CYS 128 128 128 CYS CYS B . n 
B 1 129 ALA 129 129 129 ALA ALA B . n 
B 1 130 MET 130 130 130 MET MET B . n 
B 1 131 ARG 131 131 131 ARG ARG B . n 
B 1 132 PRO 132 132 132 PRO PRO B . n 
B 1 133 ASN 133 133 133 ASN ASN B . n 
B 1 134 PHE 134 134 134 PHE PHE B . n 
B 1 135 THR 135 135 135 THR THR B . n 
B 1 136 ILE 136 136 136 ILE ILE B . n 
B 1 137 LYS 137 137 137 LYS LYS B . n 
B 1 138 GLY 138 138 138 GLY GLY B . n 
B 1 139 SER 139 139 139 SER SER B . n 
B 1 140 PHE 140 140 140 PHE PHE B . n 
B 1 141 LEU 141 141 141 LEU LEU B . n 
B 1 142 ASN 142 142 142 ASN ASN B . n 
B 1 143 GLY 143 143 143 GLY GLY B . n 
B 1 144 SER 144 144 144 SER SER B . n 
B 1 145 CYS 145 145 145 CYS CYS B . n 
B 1 146 GLY 146 146 146 GLY GLY B . n 
B 1 147 SER 147 147 147 SER SER B . n 
B 1 148 VAL 148 148 148 VAL VAL B . n 
B 1 149 GLY 149 149 149 GLY GLY B . n 
B 1 150 PHE 150 150 150 PHE PHE B . n 
B 1 151 ASN 151 151 151 ASN ASN B . n 
B 1 152 ILE 152 152 152 ILE ILE B . n 
B 1 153 ASP 153 153 153 ASP ASP B . n 
B 1 154 TYR 154 154 154 TYR TYR B . n 
B 1 155 ASP 155 155 155 ASP ASP B . n 
B 1 156 CYS 156 156 156 CYS CYS B . n 
B 1 157 VAL 157 157 157 VAL VAL B . n 
B 1 158 SER 158 158 158 SER SER B . n 
B 1 159 PHE 159 159 159 PHE PHE B . n 
B 1 160 CYS 160 160 160 CYS CYS B . n 
B 1 161 TYR 161 161 161 TYR TYR B . n 
B 1 162 MET 162 162 162 MET MET B . n 
B 1 163 HIS 163 163 163 HIS HIS B . n 
B 1 164 HIS 164 164 164 HIS HIS B . n 
B 1 165 MET 165 165 165 MET MET B . n 
B 1 166 GLU 166 166 166 GLU GLU B . n 
B 1 167 LEU 167 167 167 LEU LEU B . n 
B 1 168 PRO 168 168 168 PRO PRO B . n 
B 1 169 THR 169 169 169 THR THR B . n 
B 1 170 GLY 170 170 170 GLY GLY B . n 
B 1 171 VAL 171 171 171 VAL VAL B . n 
B 1 172 HIS 172 172 172 HIS HIS B . n 
B 1 173 ALA 173 173 173 ALA ALA B . n 
B 1 174 GLY 174 174 174 GLY GLY B . n 
B 1 175 THR 175 175 175 THR THR B . n 
B 1 176 ASP 176 176 176 ASP ASP B . n 
B 1 177 LEU 177 177 177 LEU LEU B . n 
B 1 178 GLU 178 178 178 GLU GLU B . n 
B 1 179 GLY 179 179 179 GLY GLY B . n 
B 1 180 ASN 180 180 180 ASN ASN B . n 
B 1 181 PHE 181 181 181 PHE PHE B . n 
B 1 182 TYR 182 182 182 TYR TYR B . n 
B 1 183 GLY 183 183 183 GLY GLY B . n 
B 1 184 PRO 184 184 184 PRO PRO B . n 
B 1 185 PHE 185 185 185 PHE PHE B . n 
B 1 186 VAL 186 186 186 VAL VAL B . n 
B 1 187 ASP 187 187 187 ASP ASP B . n 
B 1 188 ARG 188 188 188 ARG ARG B . n 
B 1 189 GLN 189 189 189 GLN GLN B . n 
B 1 190 THR 190 190 190 THR THR B . n 
B 1 191 ALA 191 191 191 ALA ALA B . n 
B 1 192 GLN 192 192 192 GLN GLN B . n 
B 1 193 ALA 193 193 193 ALA ALA B . n 
B 1 194 ALA 194 194 194 ALA ALA B . n 
B 1 195 GLY 195 195 195 GLY GLY B . n 
B 1 196 THR 196 196 196 THR THR B . n 
B 1 197 ASP 197 197 197 ASP ASP B . n 
B 1 198 THR 198 198 198 THR THR B . n 
B 1 199 THR 199 199 199 THR THR B . n 
B 1 200 ILE 200 200 200 ILE ILE B . n 
B 1 201 THR 201 201 201 THR THR B . n 
B 1 202 VAL 202 202 202 VAL VAL B . n 
B 1 203 ASN 203 203 203 ASN ASN B . n 
B 1 204 VAL 204 204 204 VAL VAL B . n 
B 1 205 LEU 205 205 205 LEU LEU B . n 
B 1 206 ALA 206 206 206 ALA ALA B . n 
B 1 207 TRP 207 207 207 TRP TRP B . n 
B 1 208 LEU 208 208 208 LEU LEU B . n 
B 1 209 TYR 209 209 209 TYR TYR B . n 
B 1 210 ALA 210 210 210 ALA ALA B . n 
B 1 211 ALA 211 211 211 ALA ALA B . n 
B 1 212 VAL 212 212 212 VAL VAL B . n 
B 1 213 ILE 213 213 213 ILE ILE B . n 
B 1 214 ASN 214 214 214 ASN ASN B . n 
B 1 215 GLY 215 215 215 GLY GLY B . n 
B 1 216 ASP 216 216 216 ASP ASP B . n 
B 1 217 ARG 217 217 217 ARG ARG B . n 
B 1 218 TRP 218 218 218 TRP TRP B . n 
B 1 219 PHE 219 219 219 PHE PHE B . n 
B 1 220 LEU 220 220 220 LEU LEU B . n 
B 1 221 ASN 221 221 221 ASN ASN B . n 
B 1 222 ARG 222 222 222 ARG ARG B . n 
B 1 223 PHE 223 223 223 PHE PHE B . n 
B 1 224 THR 224 224 224 THR THR B . n 
B 1 225 THR 225 225 225 THR THR B . n 
B 1 226 THR 226 226 226 THR THR B . n 
B 1 227 LEU 227 227 227 LEU LEU B . n 
B 1 228 ASN 228 228 228 ASN ASN B . n 
B 1 229 ASP 229 229 229 ASP ASP B . n 
B 1 230 PHE 230 230 230 PHE PHE B . n 
B 1 231 ASN 231 231 231 ASN ASN B . n 
B 1 232 LEU 232 232 232 LEU LEU B . n 
B 1 233 VAL 233 233 233 VAL VAL B . n 
B 1 234 ALA 234 234 234 ALA ALA B . n 
B 1 235 MET 235 235 235 MET MET B . n 
B 1 236 LYS 236 236 236 LYS LYS B . n 
B 1 237 TYR 237 237 237 TYR TYR B . n 
B 1 238 ASN 238 238 238 ASN ASN B . n 
B 1 239 TYR 239 239 239 TYR TYR B . n 
B 1 240 GLU 240 240 240 GLU GLU B . n 
B 1 241 PRO 241 241 241 PRO PRO B . n 
B 1 242 LEU 242 242 242 LEU LEU B . n 
B 1 243 THR 243 243 243 THR THR B . n 
B 1 244 GLN 244 244 244 GLN GLN B . n 
B 1 245 ASP 245 245 245 ASP ASP B . n 
B 1 246 HIS 246 246 246 HIS HIS B . n 
B 1 247 VAL 247 247 247 VAL VAL B . n 
B 1 248 ASP 248 248 248 ASP ASP B . n 
B 1 249 ILE 249 249 249 ILE ILE B . n 
B 1 250 LEU 250 250 250 LEU LEU B . n 
B 1 251 GLY 251 251 251 GLY GLY B . n 
B 1 252 PRO 252 252 252 PRO PRO B . n 
B 1 253 LEU 253 253 253 LEU LEU B . n 
B 1 254 SER 254 254 254 SER SER B . n 
B 1 255 ALA 255 255 255 ALA ALA B . n 
B 1 256 GLN 256 256 256 GLN GLN B . n 
B 1 257 THR 257 257 257 THR THR B . n 
B 1 258 GLY 258 258 258 GLY GLY B . n 
B 1 259 ILE 259 259 259 ILE ILE B . n 
B 1 260 ALA 260 260 260 ALA ALA B . n 
B 1 261 VAL 261 261 261 VAL VAL B . n 
B 1 262 LEU 262 262 262 LEU LEU B . n 
B 1 263 ASP 263 263 263 ASP ASP B . n 
B 1 264 MET 264 264 264 MET MET B . n 
B 1 265 CYS 265 265 265 CYS CYS B . n 
B 1 266 ALA 266 266 266 ALA ALA B . n 
B 1 267 SER 267 267 267 SER SER B . n 
B 1 268 LEU 268 268 268 LEU LEU B . n 
B 1 269 LYS 269 269 269 LYS LYS B . n 
B 1 270 GLU 270 270 270 GLU GLU B . n 
B 1 271 LEU 271 271 271 LEU LEU B . n 
B 1 272 LEU 272 272 272 LEU LEU B . n 
B 1 273 GLN 273 273 273 GLN GLN B . n 
B 1 274 ASN 274 274 274 ASN ASN B . n 
B 1 275 GLY 275 275 275 GLY GLY B . n 
B 1 276 MET 276 276 276 MET MET B . n 
B 1 277 ASN 277 277 277 ASN ASN B . n 
B 1 278 GLY 278 278 278 GLY GLY B . n 
B 1 279 ARG 279 279 279 ARG ARG B . n 
B 1 280 THR 280 280 280 THR THR B . n 
B 1 281 ILE 281 281 281 ILE ILE B . n 
B 1 282 LEU 282 282 282 LEU LEU B . n 
B 1 283 GLY 283 283 283 GLY GLY B . n 
B 1 284 SER 284 284 284 SER SER B . n 
B 1 285 ALA 285 285 285 ALA ALA B . n 
B 1 286 LEU 286 286 286 LEU LEU B . n 
B 1 287 LEU 287 287 287 LEU LEU B . n 
B 1 288 GLU 288 288 288 GLU GLU B . n 
B 1 289 ASP 289 289 289 ASP ASP B . n 
B 1 290 GLU 290 290 290 GLU GLU B . n 
B 1 291 PHE 291 291 291 PHE PHE B . n 
B 1 292 THR 292 292 292 THR THR B . n 
B 1 293 PRO 293 293 293 PRO PRO B . n 
B 1 294 PHE 294 294 294 PHE PHE B . n 
B 1 295 ASP 295 295 295 ASP ASP B . n 
B 1 296 VAL 296 296 296 VAL VAL B . n 
B 1 297 VAL 297 297 297 VAL VAL B . n 
B 1 298 ARG 298 298 298 ARG ARG B . n 
B 1 299 GLN 299 299 299 GLN GLN B . n 
B 1 300 CYS 300 300 300 CYS CYS B . n 
B 1 301 SER 301 301 301 SER SER B . n 
B 1 302 GLY 302 302 302 GLY GLY B . n 
B 1 303 VAL 303 303 303 VAL VAL B . n 
B 1 304 THR 304 304 304 THR THR B . n 
B 1 305 PHE 305 305 305 PHE PHE B . n 
B 1 306 GLN 306 306 ?   ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1ITI 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1ITI 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 A1ITI 1   401 401 A1ITI LIG A . 
D 3 CL    1   402 1   CL    CL  A . 
E 2 A1ITI 1   401 401 A1ITI LIG B . 
F 4 NA    1   402 1   NA    NA  B . 
G 5 HOH   1   501 646 HOH   HOH A . 
G 5 HOH   2   502 597 HOH   HOH A . 
G 5 HOH   3   503 381 HOH   HOH A . 
G 5 HOH   4   504 296 HOH   HOH A . 
G 5 HOH   5   505 516 HOH   HOH A . 
G 5 HOH   6   506 178 HOH   HOH A . 
G 5 HOH   7   507 368 HOH   HOH A . 
G 5 HOH   8   508 506 HOH   HOH A . 
G 5 HOH   9   509 267 HOH   HOH A . 
G 5 HOH   10  510 231 HOH   HOH A . 
G 5 HOH   11  511 34  HOH   HOH A . 
G 5 HOH   12  512 599 HOH   HOH A . 
G 5 HOH   13  513 647 HOH   HOH A . 
G 5 HOH   14  514 147 HOH   HOH A . 
G 5 HOH   15  515 592 HOH   HOH A . 
G 5 HOH   16  516 275 HOH   HOH A . 
G 5 HOH   17  517 285 HOH   HOH A . 
G 5 HOH   18  518 612 HOH   HOH A . 
G 5 HOH   19  519 622 HOH   HOH A . 
G 5 HOH   20  520 277 HOH   HOH A . 
G 5 HOH   21  521 372 HOH   HOH A . 
G 5 HOH   22  522 515 HOH   HOH A . 
G 5 HOH   23  523 138 HOH   HOH A . 
G 5 HOH   24  524 217 HOH   HOH A . 
G 5 HOH   25  525 295 HOH   HOH A . 
G 5 HOH   26  526 550 HOH   HOH A . 
G 5 HOH   27  527 230 HOH   HOH A . 
G 5 HOH   28  528 214 HOH   HOH A . 
G 5 HOH   29  529 442 HOH   HOH A . 
G 5 HOH   30  530 73  HOH   HOH A . 
G 5 HOH   31  531 239 HOH   HOH A . 
G 5 HOH   32  532 637 HOH   HOH A . 
G 5 HOH   33  533 370 HOH   HOH A . 
G 5 HOH   34  534 406 HOH   HOH A . 
G 5 HOH   35  535 38  HOH   HOH A . 
G 5 HOH   36  536 315 HOH   HOH A . 
G 5 HOH   37  537 133 HOH   HOH A . 
G 5 HOH   38  538 455 HOH   HOH A . 
G 5 HOH   39  539 321 HOH   HOH A . 
G 5 HOH   40  540 611 HOH   HOH A . 
G 5 HOH   41  541 547 HOH   HOH A . 
G 5 HOH   42  542 208 HOH   HOH A . 
G 5 HOH   43  543 312 HOH   HOH A . 
G 5 HOH   44  544 431 HOH   HOH A . 
G 5 HOH   45  545 40  HOH   HOH A . 
G 5 HOH   46  546 472 HOH   HOH A . 
G 5 HOH   47  547 297 HOH   HOH A . 
G 5 HOH   48  548 402 HOH   HOH A . 
G 5 HOH   49  549 107 HOH   HOH A . 
G 5 HOH   50  550 207 HOH   HOH A . 
G 5 HOH   51  551 67  HOH   HOH A . 
G 5 HOH   52  552 301 HOH   HOH A . 
G 5 HOH   53  553 47  HOH   HOH A . 
G 5 HOH   54  554 156 HOH   HOH A . 
G 5 HOH   55  555 61  HOH   HOH A . 
G 5 HOH   56  556 441 HOH   HOH A . 
G 5 HOH   57  557 18  HOH   HOH A . 
G 5 HOH   58  558 59  HOH   HOH A . 
G 5 HOH   59  559 10  HOH   HOH A . 
G 5 HOH   60  560 24  HOH   HOH A . 
G 5 HOH   61  561 366 HOH   HOH A . 
G 5 HOH   62  562 541 HOH   HOH A . 
G 5 HOH   63  563 346 HOH   HOH A . 
G 5 HOH   64  564 195 HOH   HOH A . 
G 5 HOH   65  565 567 HOH   HOH A . 
G 5 HOH   66  566 403 HOH   HOH A . 
G 5 HOH   67  567 31  HOH   HOH A . 
G 5 HOH   68  568 263 HOH   HOH A . 
G 5 HOH   69  569 291 HOH   HOH A . 
G 5 HOH   70  570 56  HOH   HOH A . 
G 5 HOH   71  571 176 HOH   HOH A . 
G 5 HOH   72  572 245 HOH   HOH A . 
G 5 HOH   73  573 427 HOH   HOH A . 
G 5 HOH   74  574 222 HOH   HOH A . 
G 5 HOH   75  575 65  HOH   HOH A . 
G 5 HOH   76  576 159 HOH   HOH A . 
G 5 HOH   77  577 125 HOH   HOH A . 
G 5 HOH   78  578 434 HOH   HOH A . 
G 5 HOH   79  579 51  HOH   HOH A . 
G 5 HOH   80  580 164 HOH   HOH A . 
G 5 HOH   81  581 255 HOH   HOH A . 
G 5 HOH   82  582 117 HOH   HOH A . 
G 5 HOH   83  583 422 HOH   HOH A . 
G 5 HOH   84  584 2   HOH   HOH A . 
G 5 HOH   85  585 135 HOH   HOH A . 
G 5 HOH   86  586 3   HOH   HOH A . 
G 5 HOH   87  587 37  HOH   HOH A . 
G 5 HOH   88  588 451 HOH   HOH A . 
G 5 HOH   89  589 54  HOH   HOH A . 
G 5 HOH   90  590 26  HOH   HOH A . 
G 5 HOH   91  591 123 HOH   HOH A . 
G 5 HOH   92  592 158 HOH   HOH A . 
G 5 HOH   93  593 332 HOH   HOH A . 
G 5 HOH   94  594 68  HOH   HOH A . 
G 5 HOH   95  595 342 HOH   HOH A . 
G 5 HOH   96  596 134 HOH   HOH A . 
G 5 HOH   97  597 260 HOH   HOH A . 
G 5 HOH   98  598 378 HOH   HOH A . 
G 5 HOH   99  599 358 HOH   HOH A . 
G 5 HOH   100 600 446 HOH   HOH A . 
G 5 HOH   101 601 531 HOH   HOH A . 
G 5 HOH   102 602 525 HOH   HOH A . 
G 5 HOH   103 603 32  HOH   HOH A . 
G 5 HOH   104 604 143 HOH   HOH A . 
G 5 HOH   105 605 91  HOH   HOH A . 
G 5 HOH   106 606 113 HOH   HOH A . 
G 5 HOH   107 607 82  HOH   HOH A . 
G 5 HOH   108 608 170 HOH   HOH A . 
G 5 HOH   109 609 205 HOH   HOH A . 
G 5 HOH   110 610 254 HOH   HOH A . 
G 5 HOH   111 611 546 HOH   HOH A . 
G 5 HOH   112 612 607 HOH   HOH A . 
G 5 HOH   113 613 105 HOH   HOH A . 
G 5 HOH   114 614 46  HOH   HOH A . 
G 5 HOH   115 615 120 HOH   HOH A . 
G 5 HOH   116 616 89  HOH   HOH A . 
G 5 HOH   117 617 90  HOH   HOH A . 
G 5 HOH   118 618 216 HOH   HOH A . 
G 5 HOH   119 619 470 HOH   HOH A . 
G 5 HOH   120 620 103 HOH   HOH A . 
G 5 HOH   121 621 44  HOH   HOH A . 
G 5 HOH   122 622 16  HOH   HOH A . 
G 5 HOH   123 623 140 HOH   HOH A . 
G 5 HOH   124 624 235 HOH   HOH A . 
G 5 HOH   125 625 328 HOH   HOH A . 
G 5 HOH   126 626 394 HOH   HOH A . 
G 5 HOH   127 627 174 HOH   HOH A . 
G 5 HOH   128 628 84  HOH   HOH A . 
G 5 HOH   129 629 294 HOH   HOH A . 
G 5 HOH   130 630 110 HOH   HOH A . 
G 5 HOH   131 631 126 HOH   HOH A . 
G 5 HOH   132 632 116 HOH   HOH A . 
G 5 HOH   133 633 98  HOH   HOH A . 
G 5 HOH   134 634 63  HOH   HOH A . 
G 5 HOH   135 635 212 HOH   HOH A . 
G 5 HOH   136 636 259 HOH   HOH A . 
G 5 HOH   137 637 78  HOH   HOH A . 
G 5 HOH   138 638 99  HOH   HOH A . 
G 5 HOH   139 639 237 HOH   HOH A . 
G 5 HOH   140 640 5   HOH   HOH A . 
G 5 HOH   141 641 538 HOH   HOH A . 
G 5 HOH   142 642 613 HOH   HOH A . 
G 5 HOH   143 643 22  HOH   HOH A . 
G 5 HOH   144 644 15  HOH   HOH A . 
G 5 HOH   145 645 173 HOH   HOH A . 
G 5 HOH   146 646 130 HOH   HOH A . 
G 5 HOH   147 647 375 HOH   HOH A . 
G 5 HOH   148 648 307 HOH   HOH A . 
G 5 HOH   149 649 171 HOH   HOH A . 
G 5 HOH   150 650 602 HOH   HOH A . 
G 5 HOH   151 651 429 HOH   HOH A . 
G 5 HOH   152 652 641 HOH   HOH A . 
G 5 HOH   153 653 6   HOH   HOH A . 
G 5 HOH   154 654 21  HOH   HOH A . 
G 5 HOH   155 655 88  HOH   HOH A . 
G 5 HOH   156 656 182 HOH   HOH A . 
G 5 HOH   157 657 302 HOH   HOH A . 
G 5 HOH   158 658 310 HOH   HOH A . 
G 5 HOH   159 659 534 HOH   HOH A . 
G 5 HOH   160 660 430 HOH   HOH A . 
G 5 HOH   161 661 96  HOH   HOH A . 
G 5 HOH   162 662 151 HOH   HOH A . 
G 5 HOH   163 663 219 HOH   HOH A . 
G 5 HOH   164 664 210 HOH   HOH A . 
G 5 HOH   165 665 118 HOH   HOH A . 
G 5 HOH   166 666 425 HOH   HOH A . 
G 5 HOH   167 667 387 HOH   HOH A . 
G 5 HOH   168 668 303 HOH   HOH A . 
G 5 HOH   169 669 274 HOH   HOH A . 
G 5 HOH   170 670 594 HOH   HOH A . 
G 5 HOH   171 671 326 HOH   HOH A . 
G 5 HOH   172 672 17  HOH   HOH A . 
G 5 HOH   173 673 640 HOH   HOH A . 
G 5 HOH   174 674 48  HOH   HOH A . 
G 5 HOH   175 675 243 HOH   HOH A . 
G 5 HOH   176 676 545 HOH   HOH A . 
G 5 HOH   177 677 53  HOH   HOH A . 
G 5 HOH   178 678 198 HOH   HOH A . 
G 5 HOH   179 679 196 HOH   HOH A . 
G 5 HOH   180 680 52  HOH   HOH A . 
G 5 HOH   181 681 461 HOH   HOH A . 
G 5 HOH   182 682 393 HOH   HOH A . 
G 5 HOH   183 683 571 HOH   HOH A . 
G 5 HOH   184 684 181 HOH   HOH A . 
G 5 HOH   185 685 228 HOH   HOH A . 
G 5 HOH   186 686 33  HOH   HOH A . 
G 5 HOH   187 687 95  HOH   HOH A . 
G 5 HOH   188 688 30  HOH   HOH A . 
G 5 HOH   189 689 186 HOH   HOH A . 
G 5 HOH   190 690 279 HOH   HOH A . 
G 5 HOH   191 691 194 HOH   HOH A . 
G 5 HOH   192 692 7   HOH   HOH A . 
G 5 HOH   193 693 166 HOH   HOH A . 
G 5 HOH   194 694 153 HOH   HOH A . 
G 5 HOH   195 695 526 HOH   HOH A . 
G 5 HOH   196 696 57  HOH   HOH A . 
G 5 HOH   197 697 92  HOH   HOH A . 
G 5 HOH   198 698 203 HOH   HOH A . 
G 5 HOH   199 699 413 HOH   HOH A . 
G 5 HOH   200 700 511 HOH   HOH A . 
G 5 HOH   201 701 249 HOH   HOH A . 
G 5 HOH   202 702 437 HOH   HOH A . 
G 5 HOH   203 703 386 HOH   HOH A . 
G 5 HOH   204 704 23  HOH   HOH A . 
G 5 HOH   205 705 128 HOH   HOH A . 
G 5 HOH   206 706 522 HOH   HOH A . 
G 5 HOH   207 707 14  HOH   HOH A . 
G 5 HOH   208 708 227 HOH   HOH A . 
G 5 HOH   209 709 20  HOH   HOH A . 
G 5 HOH   210 710 236 HOH   HOH A . 
G 5 HOH   211 711 36  HOH   HOH A . 
G 5 HOH   212 712 131 HOH   HOH A . 
G 5 HOH   213 713 144 HOH   HOH A . 
G 5 HOH   214 714 139 HOH   HOH A . 
G 5 HOH   215 715 456 HOH   HOH A . 
G 5 HOH   216 716 41  HOH   HOH A . 
G 5 HOH   217 717 537 HOH   HOH A . 
G 5 HOH   218 718 266 HOH   HOH A . 
G 5 HOH   219 719 163 HOH   HOH A . 
G 5 HOH   220 720 39  HOH   HOH A . 
G 5 HOH   221 721 85  HOH   HOH A . 
G 5 HOH   222 722 124 HOH   HOH A . 
G 5 HOH   223 723 79  HOH   HOH A . 
G 5 HOH   224 724 323 HOH   HOH A . 
G 5 HOH   225 725 114 HOH   HOH A . 
G 5 HOH   226 726 248 HOH   HOH A . 
G 5 HOH   227 727 384 HOH   HOH A . 
G 5 HOH   228 728 410 HOH   HOH A . 
G 5 HOH   229 729 177 HOH   HOH A . 
G 5 HOH   230 730 284 HOH   HOH A . 
G 5 HOH   231 731 415 HOH   HOH A . 
G 5 HOH   232 732 244 HOH   HOH A . 
G 5 HOH   233 733 411 HOH   HOH A . 
G 5 HOH   234 734 270 HOH   HOH A . 
G 5 HOH   235 735 353 HOH   HOH A . 
G 5 HOH   236 736 341 HOH   HOH A . 
G 5 HOH   237 737 102 HOH   HOH A . 
G 5 HOH   238 738 389 HOH   HOH A . 
G 5 HOH   239 739 224 HOH   HOH A . 
G 5 HOH   240 740 385 HOH   HOH A . 
G 5 HOH   241 741 333 HOH   HOH A . 
G 5 HOH   242 742 215 HOH   HOH A . 
G 5 HOH   243 743 201 HOH   HOH A . 
G 5 HOH   244 744 396 HOH   HOH A . 
G 5 HOH   245 745 369 HOH   HOH A . 
G 5 HOH   246 746 367 HOH   HOH A . 
G 5 HOH   247 747 335 HOH   HOH A . 
G 5 HOH   248 748 501 HOH   HOH A . 
G 5 HOH   249 749 213 HOH   HOH A . 
G 5 HOH   250 750 202 HOH   HOH A . 
G 5 HOH   251 751 444 HOH   HOH A . 
G 5 HOH   252 752 401 HOH   HOH A . 
G 5 HOH   253 753 463 HOH   HOH A . 
G 5 HOH   254 754 465 HOH   HOH A . 
G 5 HOH   255 755 552 HOH   HOH A . 
G 5 HOH   256 756 344 HOH   HOH A . 
G 5 HOH   257 757 330 HOH   HOH A . 
G 5 HOH   258 758 566 HOH   HOH A . 
G 5 HOH   259 759 121 HOH   HOH A . 
G 5 HOH   260 760 183 HOH   HOH A . 
G 5 HOH   261 761 271 HOH   HOH A . 
G 5 HOH   262 762 83  HOH   HOH A . 
G 5 HOH   263 763 190 HOH   HOH A . 
G 5 HOH   264 764 345 HOH   HOH A . 
G 5 HOH   265 765 447 HOH   HOH A . 
G 5 HOH   266 766 132 HOH   HOH A . 
G 5 HOH   267 767 257 HOH   HOH A . 
G 5 HOH   268 768 137 HOH   HOH A . 
G 5 HOH   269 769 313 HOH   HOH A . 
G 5 HOH   270 770 435 HOH   HOH A . 
G 5 HOH   271 771 485 HOH   HOH A . 
G 5 HOH   272 772 503 HOH   HOH A . 
G 5 HOH   273 773 407 HOH   HOH A . 
G 5 HOH   274 774 486 HOH   HOH A . 
G 5 HOH   275 775 564 HOH   HOH A . 
G 5 HOH   276 776 317 HOH   HOH A . 
G 5 HOH   277 777 119 HOH   HOH A . 
G 5 HOH   278 778 621 HOH   HOH A . 
G 5 HOH   279 779 600 HOH   HOH A . 
G 5 HOH   280 780 615 HOH   HOH A . 
G 5 HOH   281 781 287 HOH   HOH A . 
G 5 HOH   282 782 492 HOH   HOH A . 
G 5 HOH   283 783 242 HOH   HOH A . 
G 5 HOH   284 784 498 HOH   HOH A . 
G 5 HOH   285 785 519 HOH   HOH A . 
G 5 HOH   286 786 337 HOH   HOH A . 
G 5 HOH   287 787 218 HOH   HOH A . 
G 5 HOH   288 788 475 HOH   HOH A . 
G 5 HOH   289 789 283 HOH   HOH A . 
G 5 HOH   290 790 596 HOH   HOH A . 
G 5 HOH   291 791 471 HOH   HOH A . 
G 5 HOH   292 792 423 HOH   HOH A . 
G 5 HOH   293 793 169 HOH   HOH A . 
G 5 HOH   294 794 433 HOH   HOH A . 
G 5 HOH   295 795 391 HOH   HOH A . 
G 5 HOH   296 796 81  HOH   HOH A . 
G 5 HOH   297 797 349 HOH   HOH A . 
G 5 HOH   298 798 234 HOH   HOH A . 
G 5 HOH   299 799 488 HOH   HOH A . 
G 5 HOH   300 800 648 HOH   HOH A . 
G 5 HOH   301 801 238 HOH   HOH A . 
G 5 HOH   302 802 468 HOH   HOH A . 
G 5 HOH   303 803 80  HOH   HOH A . 
G 5 HOH   304 804 493 HOH   HOH A . 
G 5 HOH   305 805 340 HOH   HOH A . 
G 5 HOH   306 806 399 HOH   HOH A . 
G 5 HOH   307 807 211 HOH   HOH A . 
G 5 HOH   308 808 327 HOH   HOH A . 
G 5 HOH   309 809 610 HOH   HOH A . 
G 5 HOH   310 810 204 HOH   HOH A . 
G 5 HOH   311 811 298 HOH   HOH A . 
G 5 HOH   312 812 500 HOH   HOH A . 
G 5 HOH   313 813 414 HOH   HOH A . 
G 5 HOH   314 814 432 HOH   HOH A . 
G 5 HOH   315 815 421 HOH   HOH A . 
G 5 HOH   316 816 365 HOH   HOH A . 
G 5 HOH   317 817 268 HOH   HOH A . 
G 5 HOH   318 818 281 HOH   HOH A . 
G 5 HOH   319 819 553 HOH   HOH A . 
G 5 HOH   320 820 643 HOH   HOH A . 
G 5 HOH   321 821 376 HOH   HOH A . 
G 5 HOH   322 822 362 HOH   HOH A . 
G 5 HOH   323 823 262 HOH   HOH A . 
G 5 HOH   324 824 145 HOH   HOH A . 
G 5 HOH   325 825 495 HOH   HOH A . 
G 5 HOH   326 826 502 HOH   HOH A . 
G 5 HOH   327 827 490 HOH   HOH A . 
G 5 HOH   328 828 445 HOH   HOH A . 
G 5 HOH   329 829 339 HOH   HOH A . 
G 5 HOH   330 830 576 HOH   HOH A . 
G 5 HOH   331 831 364 HOH   HOH A . 
H 5 HOH   1   501 443 HOH   HOH B . 
H 5 HOH   2   502 521 HOH   HOH B . 
H 5 HOH   3   503 390 HOH   HOH B . 
H 5 HOH   4   504 188 HOH   HOH B . 
H 5 HOH   5   505 568 HOH   HOH B . 
H 5 HOH   6   506 625 HOH   HOH B . 
H 5 HOH   7   507 278 HOH   HOH B . 
H 5 HOH   8   508 347 HOH   HOH B . 
H 5 HOH   9   509 74  HOH   HOH B . 
H 5 HOH   10  510 383 HOH   HOH B . 
H 5 HOH   11  511 590 HOH   HOH B . 
H 5 HOH   12  512 614 HOH   HOH B . 
H 5 HOH   13  513 416 HOH   HOH B . 
H 5 HOH   14  514 355 HOH   HOH B . 
H 5 HOH   15  515 247 HOH   HOH B . 
H 5 HOH   16  516 578 HOH   HOH B . 
H 5 HOH   17  517 87  HOH   HOH B . 
H 5 HOH   18  518 351 HOH   HOH B . 
H 5 HOH   19  519 240 HOH   HOH B . 
H 5 HOH   20  520 629 HOH   HOH B . 
H 5 HOH   21  521 112 HOH   HOH B . 
H 5 HOH   22  522 167 HOH   HOH B . 
H 5 HOH   23  523 388 HOH   HOH B . 
H 5 HOH   24  524 168 HOH   HOH B . 
H 5 HOH   25  525 191 HOH   HOH B . 
H 5 HOH   26  526 272 HOH   HOH B . 
H 5 HOH   27  527 570 HOH   HOH B . 
H 5 HOH   28  528 264 HOH   HOH B . 
H 5 HOH   29  529 152 HOH   HOH B . 
H 5 HOH   30  530 412 HOH   HOH B . 
H 5 HOH   31  531 530 HOH   HOH B . 
H 5 HOH   32  532 223 HOH   HOH B . 
H 5 HOH   33  533 72  HOH   HOH B . 
H 5 HOH   34  534 452 HOH   HOH B . 
H 5 HOH   35  535 161 HOH   HOH B . 
H 5 HOH   36  536 12  HOH   HOH B . 
H 5 HOH   37  537 93  HOH   HOH B . 
H 5 HOH   38  538 251 HOH   HOH B . 
H 5 HOH   39  539 76  HOH   HOH B . 
H 5 HOH   40  540 354 HOH   HOH B . 
H 5 HOH   41  541 392 HOH   HOH B . 
H 5 HOH   42  542 64  HOH   HOH B . 
H 5 HOH   43  543 282 HOH   HOH B . 
H 5 HOH   44  544 300 HOH   HOH B . 
H 5 HOH   45  545 350 HOH   HOH B . 
H 5 HOH   46  546 642 HOH   HOH B . 
H 5 HOH   47  547 304 HOH   HOH B . 
H 5 HOH   48  548 160 HOH   HOH B . 
H 5 HOH   49  549 122 HOH   HOH B . 
H 5 HOH   50  550 273 HOH   HOH B . 
H 5 HOH   51  551 404 HOH   HOH B . 
H 5 HOH   52  552 630 HOH   HOH B . 
H 5 HOH   53  553 62  HOH   HOH B . 
H 5 HOH   54  554 408 HOH   HOH B . 
H 5 HOH   55  555 192 HOH   HOH B . 
H 5 HOH   56  556 35  HOH   HOH B . 
H 5 HOH   57  557 380 HOH   HOH B . 
H 5 HOH   58  558 288 HOH   HOH B . 
H 5 HOH   59  559 580 HOH   HOH B . 
H 5 HOH   60  560 290 HOH   HOH B . 
H 5 HOH   61  561 77  HOH   HOH B . 
H 5 HOH   62  562 603 HOH   HOH B . 
H 5 HOH   63  563 633 HOH   HOH B . 
H 5 HOH   64  564 175 HOH   HOH B . 
H 5 HOH   65  565 572 HOH   HOH B . 
H 5 HOH   66  566 71  HOH   HOH B . 
H 5 HOH   67  567 97  HOH   HOH B . 
H 5 HOH   68  568 100 HOH   HOH B . 
H 5 HOH   69  569 373 HOH   HOH B . 
H 5 HOH   70  570 252 HOH   HOH B . 
H 5 HOH   71  571 320 HOH   HOH B . 
H 5 HOH   72  572 157 HOH   HOH B . 
H 5 HOH   73  573 9   HOH   HOH B . 
H 5 HOH   74  574 316 HOH   HOH B . 
H 5 HOH   75  575 13  HOH   HOH B . 
H 5 HOH   76  576 636 HOH   HOH B . 
H 5 HOH   77  577 512 HOH   HOH B . 
H 5 HOH   78  578 398 HOH   HOH B . 
H 5 HOH   79  579 360 HOH   HOH B . 
H 5 HOH   80  580 518 HOH   HOH B . 
H 5 HOH   81  581 305 HOH   HOH B . 
H 5 HOH   82  582 209 HOH   HOH B . 
H 5 HOH   83  583 582 HOH   HOH B . 
H 5 HOH   84  584 25  HOH   HOH B . 
H 5 HOH   85  585 129 HOH   HOH B . 
H 5 HOH   86  586 104 HOH   HOH B . 
H 5 HOH   87  587 311 HOH   HOH B . 
H 5 HOH   88  588 363 HOH   HOH B . 
H 5 HOH   89  589 233 HOH   HOH B . 
H 5 HOH   90  590 324 HOH   HOH B . 
H 5 HOH   91  591 109 HOH   HOH B . 
H 5 HOH   92  592 528 HOH   HOH B . 
H 5 HOH   93  593 184 HOH   HOH B . 
H 5 HOH   94  594 477 HOH   HOH B . 
H 5 HOH   95  595 638 HOH   HOH B . 
H 5 HOH   96  596 635 HOH   HOH B . 
H 5 HOH   97  597 448 HOH   HOH B . 
H 5 HOH   98  598 165 HOH   HOH B . 
H 5 HOH   99  599 206 HOH   HOH B . 
H 5 HOH   100 600 60  HOH   HOH B . 
H 5 HOH   101 601 106 HOH   HOH B . 
H 5 HOH   102 602 334 HOH   HOH B . 
H 5 HOH   103 603 142 HOH   HOH B . 
H 5 HOH   104 604 29  HOH   HOH B . 
H 5 HOH   105 605 617 HOH   HOH B . 
H 5 HOH   106 606 309 HOH   HOH B . 
H 5 HOH   107 607 397 HOH   HOH B . 
H 5 HOH   108 608 299 HOH   HOH B . 
H 5 HOH   109 609 286 HOH   HOH B . 
H 5 HOH   110 610 127 HOH   HOH B . 
H 5 HOH   111 611 374 HOH   HOH B . 
H 5 HOH   112 612 276 HOH   HOH B . 
H 5 HOH   113 613 336 HOH   HOH B . 
H 5 HOH   114 614 322 HOH   HOH B . 
H 5 HOH   115 615 101 HOH   HOH B . 
H 5 HOH   116 616 11  HOH   HOH B . 
H 5 HOH   117 617 66  HOH   HOH B . 
H 5 HOH   118 618 265 HOH   HOH B . 
H 5 HOH   119 619 549 HOH   HOH B . 
H 5 HOH   120 620 1   HOH   HOH B . 
H 5 HOH   121 621 608 HOH   HOH B . 
H 5 HOH   122 622 292 HOH   HOH B . 
H 5 HOH   123 623 146 HOH   HOH B . 
H 5 HOH   124 624 49  HOH   HOH B . 
H 5 HOH   125 625 197 HOH   HOH B . 
H 5 HOH   126 626 474 HOH   HOH B . 
H 5 HOH   127 627 226 HOH   HOH B . 
H 5 HOH   128 628 331 HOH   HOH B . 
H 5 HOH   129 629 632 HOH   HOH B . 
H 5 HOH   130 630 69  HOH   HOH B . 
H 5 HOH   131 631 382 HOH   HOH B . 
H 5 HOH   132 632 141 HOH   HOH B . 
H 5 HOH   133 633 466 HOH   HOH B . 
H 5 HOH   134 634 634 HOH   HOH B . 
H 5 HOH   135 635 189 HOH   HOH B . 
H 5 HOH   136 636 314 HOH   HOH B . 
H 5 HOH   137 637 150 HOH   HOH B . 
H 5 HOH   138 638 28  HOH   HOH B . 
H 5 HOH   139 639 55  HOH   HOH B . 
H 5 HOH   140 640 449 HOH   HOH B . 
H 5 HOH   141 641 50  HOH   HOH B . 
H 5 HOH   142 642 589 HOH   HOH B . 
H 5 HOH   143 643 356 HOH   HOH B . 
H 5 HOH   144 644 627 HOH   HOH B . 
H 5 HOH   145 645 246 HOH   HOH B . 
H 5 HOH   146 646 514 HOH   HOH B . 
H 5 HOH   147 647 229 HOH   HOH B . 
H 5 HOH   148 648 58  HOH   HOH B . 
H 5 HOH   149 649 454 HOH   HOH B . 
H 5 HOH   150 650 86  HOH   HOH B . 
H 5 HOH   151 651 172 HOH   HOH B . 
H 5 HOH   152 652 155 HOH   HOH B . 
H 5 HOH   153 653 42  HOH   HOH B . 
H 5 HOH   154 654 8   HOH   HOH B . 
H 5 HOH   155 655 108 HOH   HOH B . 
H 5 HOH   156 656 293 HOH   HOH B . 
H 5 HOH   157 657 561 HOH   HOH B . 
H 5 HOH   158 658 111 HOH   HOH B . 
H 5 HOH   159 659 221 HOH   HOH B . 
H 5 HOH   160 660 289 HOH   HOH B . 
H 5 HOH   161 661 542 HOH   HOH B . 
H 5 HOH   162 662 187 HOH   HOH B . 
H 5 HOH   163 663 43  HOH   HOH B . 
H 5 HOH   164 664 27  HOH   HOH B . 
H 5 HOH   165 665 559 HOH   HOH B . 
H 5 HOH   166 666 306 HOH   HOH B . 
H 5 HOH   167 667 329 HOH   HOH B . 
H 5 HOH   168 668 250 HOH   HOH B . 
H 5 HOH   169 669 554 HOH   HOH B . 
H 5 HOH   170 670 45  HOH   HOH B . 
H 5 HOH   171 671 556 HOH   HOH B . 
H 5 HOH   172 672 162 HOH   HOH B . 
H 5 HOH   173 673 94  HOH   HOH B . 
H 5 HOH   174 674 261 HOH   HOH B . 
H 5 HOH   175 675 19  HOH   HOH B . 
H 5 HOH   176 676 529 HOH   HOH B . 
H 5 HOH   177 677 551 HOH   HOH B . 
H 5 HOH   178 678 241 HOH   HOH B . 
H 5 HOH   179 679 75  HOH   HOH B . 
H 5 HOH   180 680 359 HOH   HOH B . 
H 5 HOH   181 681 154 HOH   HOH B . 
H 5 HOH   182 682 70  HOH   HOH B . 
H 5 HOH   183 683 535 HOH   HOH B . 
H 5 HOH   184 684 318 HOH   HOH B . 
H 5 HOH   185 685 149 HOH   HOH B . 
H 5 HOH   186 686 258 HOH   HOH B . 
H 5 HOH   187 687 193 HOH   HOH B . 
H 5 HOH   188 688 524 HOH   HOH B . 
H 5 HOH   189 689 505 HOH   HOH B . 
H 5 HOH   190 690 185 HOH   HOH B . 
H 5 HOH   191 691 624 HOH   HOH B . 
H 5 HOH   192 692 507 HOH   HOH B . 
H 5 HOH   193 693 179 HOH   HOH B . 
H 5 HOH   194 694 583 HOH   HOH B . 
H 5 HOH   195 695 459 HOH   HOH B . 
H 5 HOH   196 696 639 HOH   HOH B . 
H 5 HOH   197 697 540 HOH   HOH B . 
H 5 HOH   198 698 436 HOH   HOH B . 
H 5 HOH   199 699 426 HOH   HOH B . 
H 5 HOH   200 700 269 HOH   HOH B . 
H 5 HOH   201 701 527 HOH   HOH B . 
H 5 HOH   202 702 462 HOH   HOH B . 
H 5 HOH   203 703 581 HOH   HOH B . 
H 5 HOH   204 704 491 HOH   HOH B . 
H 5 HOH   205 705 115 HOH   HOH B . 
H 5 HOH   206 706 419 HOH   HOH B . 
H 5 HOH   207 707 473 HOH   HOH B . 
H 5 HOH   208 708 232 HOH   HOH B . 
H 5 HOH   209 709 361 HOH   HOH B . 
H 5 HOH   210 710 487 HOH   HOH B . 
H 5 HOH   211 711 481 HOH   HOH B . 
H 5 HOH   212 712 357 HOH   HOH B . 
H 5 HOH   213 713 644 HOH   HOH B . 
H 5 HOH   214 714 220 HOH   HOH B . 
H 5 HOH   215 715 458 HOH   HOH B . 
H 5 HOH   216 716 645 HOH   HOH B . 
H 5 HOH   217 717 424 HOH   HOH B . 
H 5 HOH   218 718 476 HOH   HOH B . 
H 5 HOH   219 719 628 HOH   HOH B . 
H 5 HOH   220 720 348 HOH   HOH B . 
H 5 HOH   221 721 377 HOH   HOH B . 
H 5 HOH   222 722 440 HOH   HOH B . 
H 5 HOH   223 723 343 HOH   HOH B . 
H 5 HOH   224 724 605 HOH   HOH B . 
H 5 HOH   225 725 338 HOH   HOH B . 
H 5 HOH   226 726 199 HOH   HOH B . 
H 5 HOH   227 727 417 HOH   HOH B . 
H 5 HOH   228 728 148 HOH   HOH B . 
H 5 HOH   229 729 574 HOH   HOH B . 
H 5 HOH   230 730 631 HOH   HOH B . 
H 5 HOH   231 731 280 HOH   HOH B . 
H 5 HOH   232 732 587 HOH   HOH B . 
H 5 HOH   233 733 225 HOH   HOH B . 
H 5 HOH   234 734 563 HOH   HOH B . 
H 5 HOH   235 735 180 HOH   HOH B . 
H 5 HOH   236 736 453 HOH   HOH B . 
H 5 HOH   237 737 616 HOH   HOH B . 
H 5 HOH   238 738 601 HOH   HOH B . 
H 5 HOH   239 739 395 HOH   HOH B . 
H 5 HOH   240 740 484 HOH   HOH B . 
H 5 HOH   241 741 136 HOH   HOH B . 
H 5 HOH   242 742 482 HOH   HOH B . 
H 5 HOH   243 743 532 HOH   HOH B . 
H 5 HOH   244 744 319 HOH   HOH B . 
H 5 HOH   245 745 548 HOH   HOH B . 
H 5 HOH   246 746 623 HOH   HOH B . 
H 5 HOH   247 747 565 HOH   HOH B . 
H 5 HOH   248 748 489 HOH   HOH B . 
H 5 HOH   249 749 499 HOH   HOH B . 
H 5 HOH   250 750 409 HOH   HOH B . 
H 5 HOH   251 751 483 HOH   HOH B . 
H 5 HOH   252 752 595 HOH   HOH B . 
H 5 HOH   253 753 478 HOH   HOH B . 
H 5 HOH   254 754 405 HOH   HOH B . 
H 5 HOH   255 755 626 HOH   HOH B . 
H 5 HOH   256 756 586 HOH   HOH B . 
H 5 HOH   257 757 557 HOH   HOH B . 
H 5 HOH   258 758 593 HOH   HOH B . 
H 5 HOH   259 759 598 HOH   HOH B . 
H 5 HOH   260 760 467 HOH   HOH B . 
H 5 HOH   261 761 418 HOH   HOH B . 
H 5 HOH   262 762 496 HOH   HOH B . 
H 5 HOH   263 763 609 HOH   HOH B . 
H 5 HOH   264 764 606 HOH   HOH B . 
H 5 HOH   265 765 428 HOH   HOH B . 
H 5 HOH   266 766 618 HOH   HOH B . 
H 5 HOH   267 767 604 HOH   HOH B . 
H 5 HOH   268 768 379 HOH   HOH B . 
H 5 HOH   269 769 513 HOH   HOH B . 
H 5 HOH   270 770 584 HOH   HOH B . 
H 5 HOH   271 771 588 HOH   HOH B . 
H 5 HOH   272 772 619 HOH   HOH B . 
H 5 HOH   273 773 620 HOH   HOH B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A ASN 72  ? CG  ? A ASN 72  CG  
2  1 Y 1 A ASN 72  ? OD1 ? A ASN 72  OD1 
3  1 Y 1 A ASN 72  ? ND2 ? A ASN 72  ND2 
4  1 Y 1 A ASP 155 ? CG  ? A ASP 155 CG  
5  1 Y 1 A ASP 155 ? OD1 ? A ASP 155 OD1 
6  1 Y 1 A ASP 155 ? OD2 ? A ASP 155 OD2 
7  1 Y 1 B LYS 5   ? NZ  ? B LYS 5   NZ  
8  1 Y 1 B GLU 55  ? CG  ? B GLU 55  CG  
9  1 Y 1 B GLU 55  ? CD  ? B GLU 55  CD  
10 1 Y 1 B GLU 55  ? OE1 ? B GLU 55  OE1 
11 1 Y 1 B GLU 55  ? OE2 ? B GLU 55  OE2 
12 1 Y 1 B ILE 59  ? CG1 ? B ILE 59  CG1 
13 1 Y 1 B ILE 59  ? CG2 ? B ILE 59  CG2 
14 1 Y 1 B ILE 59  ? CD1 ? B ILE 59  CD1 
15 1 Y 1 B ARG 60  ? CG  ? B ARG 60  CG  
16 1 Y 1 B ARG 60  ? CD  ? B ARG 60  CD  
17 1 Y 1 B ARG 60  ? NE  ? B ARG 60  NE  
18 1 Y 1 B ARG 60  ? CZ  ? B ARG 60  CZ  
19 1 Y 1 B ARG 60  ? NH1 ? B ARG 60  NH1 
20 1 Y 1 B ARG 60  ? NH2 ? B ARG 60  NH2 
21 1 Y 1 B SER 62  ? OG  ? B SER 62  OG  
22 1 Y 1 B ASN 65  ? CG  ? B ASN 65  CG  
23 1 Y 1 B ASN 65  ? OD1 ? B ASN 65  OD1 
24 1 Y 1 B ASN 65  ? ND2 ? B ASN 65  ND2 
25 1 Y 1 B GLN 74  ? CG  ? B GLN 74  CG  
26 1 Y 1 B GLN 74  ? CD  ? B GLN 74  CD  
27 1 Y 1 B GLN 74  ? OE1 ? B GLN 74  OE1 
28 1 Y 1 B GLN 74  ? NE2 ? B GLN 74  NE2 
29 1 Y 1 B ASP 153 ? CG  ? B ASP 153 CG  
30 1 Y 1 B ASP 153 ? OD1 ? B ASP 153 OD1 
31 1 Y 1 B ASP 153 ? OD2 ? B ASP 153 OD2 
32 1 Y 1 B TYR 154 ? CG  ? B TYR 154 CG  
33 1 Y 1 B TYR 154 ? CD1 ? B TYR 154 CD1 
34 1 Y 1 B TYR 154 ? CD2 ? B TYR 154 CD2 
35 1 Y 1 B TYR 154 ? CE1 ? B TYR 154 CE1 
36 1 Y 1 B TYR 154 ? CE2 ? B TYR 154 CE2 
37 1 Y 1 B TYR 154 ? CZ  ? B TYR 154 CZ  
38 1 Y 1 B TYR 154 ? OH  ? B TYR 154 OH  
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC   ? ? ? 5.8.0425 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? .        2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER   ? ? ? .        4 
# 
_cell.angle_alpha                  90 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9HAK 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     67.833 
_cell.length_a_esd                 ? 
_cell.length_b                     100.163 
_cell.length_b_esd                 ? 
_cell.length_c                     104.285 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9HAK 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_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                   9HAK 
_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             2.62 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          53.02 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    'Morpheus screen, condition A4' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_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 CdTe 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         2024-04-10 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.00 
_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                        'ESRF BEAMLINE ID23-1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.00 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   ID23-1 
_diffrn_source.pdbx_synchrotron_site       ESRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9HAK 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.250 
_reflns.d_resolution_low                               56.87 
_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                                     192867 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           98.3 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                10.3 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          8.4 
_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                                0.036 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.996 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.111 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.250 
_reflns_shell.d_res_low                                     1.271 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           0.9 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             9375 
_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                               0.688 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.532 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  2.13 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            0.638 
_refine.aniso_B[1][2]                            0.000 
_refine.aniso_B[1][3]                            0.000 
_refine.aniso_B[2][2]                            -0.242 
_refine.aniso_B[2][3]                            -0.000 
_refine.aniso_B[3][3]                            -0.396 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               20.668 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.975 
_refine.correlation_coeff_Fo_to_Fc_free          0.971 
_refine.details                                  'Hydrogens have been added in their riding positions' 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9HAK 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.250 
_refine.ls_d_res_low                             56.87 
_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                     192726 
_refine.ls_number_reflns_R_free                  9585 
_refine.ls_number_reflns_R_work                  183141 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.201 
_refine.ls_percent_reflns_R_free                 4.973 
_refine.ls_R_factor_all                          0.161 
_refine.ls_R_factor_obs                          ? 
_refine.ls_R_factor_R_free                       0.1757 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1598 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'MASK BULK SOLVENT' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.041 
_refine.pdbx_overall_ESU_R_Free                  0.039 
_refine.pdbx_solvent_vdw_probe_radii             1.200 
_refine.pdbx_solvent_ion_probe_radii             0.800 
_refine.pdbx_solvent_shrinkage_radii             0.800 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             1.691 
_refine.overall_SU_ML                            0.031 
_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.pdbx_number_atoms_protein        4688 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         68 
_refine_hist.number_atoms_solvent             604 
_refine_hist.number_atoms_total               5360 
_refine_hist.d_res_high                       1.250 
_refine_hist.d_res_low                        56.87 
# 
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' ? 0.005  0.012  4989  ? r_bond_refined_d               ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.016  4612  ? r_bond_other_d                 ? ? 
'X-RAY DIFFRACTION' ? 1.375  1.800  6809  ? r_angle_refined_deg            ? ? 
'X-RAY DIFFRACTION' ? 0.508  1.748  10597 ? r_angle_other_deg              ? ? 
'X-RAY DIFFRACTION' ? 6.939  5.000  640   ? r_dihedral_angle_1_deg         ? ? 
'X-RAY DIFFRACTION' ? 6.689  5.000  22    ? r_dihedral_angle_2_deg         ? ? 
'X-RAY DIFFRACTION' ? 11.070 10.000 786   ? r_dihedral_angle_3_deg         ? ? 
'X-RAY DIFFRACTION' ? 15.197 10.000 215   ? r_dihedral_angle_6_deg         ? ? 
'X-RAY DIFFRACTION' ? 0.071  0.200  761   ? r_chiral_restr                 ? ? 
'X-RAY DIFFRACTION' ? 0.006  0.020  6001  ? r_gen_planes_refined           ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  1191  ? r_gen_planes_other             ? ? 
'X-RAY DIFFRACTION' ? 0.213  0.200  911   ? r_nbd_refined                  ? ? 
'X-RAY DIFFRACTION' ? 0.193  0.200  4256  ? r_symmetry_nbd_other           ? ? 
'X-RAY DIFFRACTION' ? 0.181  0.200  2477  ? r_nbtor_refined                ? ? 
'X-RAY DIFFRACTION' ? 0.081  0.200  2491  ? r_symmetry_nbtor_other         ? ? 
'X-RAY DIFFRACTION' ? 0.101  0.200  389   ? r_xyhbond_nbd_refined          ? ? 
'X-RAY DIFFRACTION' ? 0.193  0.200  3     ? r_metal_ion_refined            ? ? 
'X-RAY DIFFRACTION' ? 0.166  0.200  13    ? r_symmetry_nbd_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.192  0.200  72    ? r_nbd_other                    ? ? 
'X-RAY DIFFRACTION' ? 0.126  0.200  27    ? r_symmetry_xyhbond_nbd_refined ? ? 
'X-RAY DIFFRACTION' ? 3.473  1.908  2510  ? r_mcbond_it                    ? ? 
'X-RAY DIFFRACTION' ? 3.468  1.908  2510  ? r_mcbond_other                 ? ? 
'X-RAY DIFFRACTION' ? 5.438  3.435  3156  ? r_mcangle_it                   ? ? 
'X-RAY DIFFRACTION' ? 5.438  3.436  3157  ? r_mcangle_other                ? ? 
'X-RAY DIFFRACTION' ? 3.966  2.055  2479  ? r_scbond_it                    ? ? 
'X-RAY DIFFRACTION' ? 3.966  2.055  2480  ? r_scbond_other                 ? ? 
'X-RAY DIFFRACTION' ? 6.091  3.712  3649  ? r_scangle_it                   ? ? 
'X-RAY DIFFRACTION' ? 6.090  3.712  3650  ? r_scangle_other                ? ? 
'X-RAY DIFFRACTION' ? 11.647 22.110 5669  ? r_lrange_it                    ? ? 
'X-RAY DIFFRACTION' ? 10.422 20.634 5516  ? r_lrange_other                 ? ? 
'X-RAY DIFFRACTION' ? 1.987  3.000  9601  ? r_rigid_bond_restr             ? ? 
'X-RAY DIFFRACTION' ? 0.117  0.050  9480  ? r_ncsr_local_group_1           ? ? 
# 
loop_
_refine_ls_restr_ncs.pdbx_refine_id 
_refine_ls_restr_ncs.dom_id 
_refine_ls_restr_ncs.ncs_model_details 
_refine_ls_restr_ncs.rms_dev_B_iso 
_refine_ls_restr_ncs.rms_dev_position 
_refine_ls_restr_ncs.weight_B_iso 
_refine_ls_restr_ncs.weight_position 
_refine_ls_restr_ncs.pdbx_ordinal 
_refine_ls_restr_ncs.pdbx_type 
_refine_ls_restr_ncs.pdbx_asym_id 
_refine_ls_restr_ncs.pdbx_auth_asym_id 
_refine_ls_restr_ncs.pdbx_number 
_refine_ls_restr_ncs.pdbx_rms 
_refine_ls_restr_ncs.pdbx_weight 
_refine_ls_restr_ncs.pdbx_ens_id 
'X-RAY DIFFRACTION' 1 ? ? 0.11679 ? 0.05008 1 'Local ncs' ? A ? ? ? 1 
'X-RAY DIFFRACTION' 2 ? ? 0.11679 ? 0.05008 2 'Local ncs' ? A ? ? ? 1 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.250 1.282 . . 667 13166 96.0959 . . . . 0.344 . . . . . . . . . . . 0.330 
'X-RAY DIFFRACTION' 1.282 1.317 . . 678 12828 96.4576 . . . . 0.308 . . . . . . . . . . . 0.302 
'X-RAY DIFFRACTION' 1.317 1.355 . . 711 12571 97.0835 . . . . 0.276 . . . . . . . . . . . 0.300 
'X-RAY DIFFRACTION' 1.355 1.397 . . 658 12228 97.4146 . . . . 0.230 . . . . . . . . . . . 0.254 
'X-RAY DIFFRACTION' 1.397 1.443 . . 622 11930 97.6126 . . . . 0.201 . . . . . . . . . . . 0.213 
'X-RAY DIFFRACTION' 1.443 1.493 . . 570 11627 97.7872 . . . . 0.161 . . . . . . . . . . . 0.172 
'X-RAY DIFFRACTION' 1.493 1.550 . . 636 11130 98.0663 . . . . 0.142 . . . . . . . . . . . 0.178 
'X-RAY DIFFRACTION' 1.550 1.613 . . 568 10831 98.2588 . . . . 0.128 . . . . . . . . . . . 0.155 
'X-RAY DIFFRACTION' 1.613 1.684 . . 549 10370 98.4226 . . . . 0.122 . . . . . . . . . . . 0.158 
'X-RAY DIFFRACTION' 1.684 1.767 . . 552 9915  98.6615 . . . . 0.120 . . . . . . . . . . . 0.153 
'X-RAY DIFFRACTION' 1.767 1.862 . . 493 9523  98.8356 . . . . 0.126 . . . . . . . . . . . 0.157 
'X-RAY DIFFRACTION' 1.862 1.975 . . 477 9042  99.0737 . . . . 0.136 . . . . . . . . . . . 0.152 
'X-RAY DIFFRACTION' 1.975 2.111 . . 438 8538  99.3140 . . . . 0.146 . . . . . . . . . . . 0.162 
'X-RAY DIFFRACTION' 2.111 2.280 . . 373 8000  99.3592 . . . . 0.137 . . . . . . . . . . . 0.154 
'X-RAY DIFFRACTION' 2.280 2.497 . . 371 7366  99.5881 . . . . 0.140 . . . . . . . . . . . 0.161 
'X-RAY DIFFRACTION' 2.497 2.791 . . 359 6703  99.7880 . . . . 0.150 . . . . . . . . . . . 0.161 
'X-RAY DIFFRACTION' 2.791 3.222 . . 298 5957  99.8404 . . . . 0.159 . . . . . . . . . . . 0.181 
'X-RAY DIFFRACTION' 3.222 3.943 . . 222 5116  99.9813 . . . . 0.158 . . . . . . . . . . . 0.161 
'X-RAY DIFFRACTION' 3.943 5.563 . . 217 3985  99.9049 . . . . 0.162 . . . . . . . . . . . 0.162 
'X-RAY DIFFRACTION' 5.563 56.87 . . 126 2316  99.5516 . . . . 0.214 . . . . . . . . . . . 0.229 
# 
loop_
_struct_ncs_dom.id 
_struct_ncs_dom.pdbx_ens_id 
_struct_ncs_dom.details 
1 1 A 
2 1 A 
# 
loop_
_struct_ncs_dom_lim.pdbx_ens_id 
_struct_ncs_dom_lim.dom_id 
_struct_ncs_dom_lim.pdbx_component_id 
_struct_ncs_dom_lim.beg_label_asym_id 
_struct_ncs_dom_lim.beg_label_comp_id 
_struct_ncs_dom_lim.beg_label_seq_id 
_struct_ncs_dom_lim.beg_label_alt_id 
_struct_ncs_dom_lim.end_label_asym_id 
_struct_ncs_dom_lim.end_label_comp_id 
_struct_ncs_dom_lim.end_label_seq_id 
_struct_ncs_dom_lim.end_label_alt_id 
_struct_ncs_dom_lim.beg_auth_asym_id 
_struct_ncs_dom_lim.beg_auth_comp_id 
_struct_ncs_dom_lim.beg_auth_seq_id 
_struct_ncs_dom_lim.end_auth_asym_id 
_struct_ncs_dom_lim.end_auth_comp_id 
_struct_ncs_dom_lim.end_auth_seq_id 
_struct_ncs_dom_lim.pdbx_refine_code 
_struct_ncs_dom_lim.selection_details 
1 1 1 A SER 1 . A THR 304 . A SER 1 A THR 304 ? ? 
1 2 1 A SER 1 . A THR 304 . A SER 1 A THR 304 ? ? 
# 
_struct_ncs_ens.id        1 
_struct_ncs_ens.details   'Local NCS retraints between domains:       1       2' 
# 
_struct.entry_id                     9HAK 
_struct.title                        'Structure of compound 119 bound to SARS-CoV-2 main protease' 
_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        9HAK 
_struct_keywords.text            'Inhibitor, docking, HYDROLASE' 
_struct_keywords.pdbx_keywords   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 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 2 ? 
F N N 4 ? 
G N N 5 ? 
H N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    R1A_SARS2 
_struct_ref.pdbx_db_accession          P0DTC1 
_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 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9HAK A 1 ? 306 ? P0DTC1 3264 ? 3569 ? 1 306 
2 1 9HAK B 1 ? 306 ? P0DTC1 3264 ? 3569 ? 1 306 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
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)' 3040  ? 
1 MORE         -33   ? 
1 'SSA (A^2)'  25240 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 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 SER A 46  ? LEU A 50  ? SER A 46  LEU A 50  5 ? 5  
HELX_P HELX_P4  AA4 ASN A 53  ? ARG A 60  ? ASN A 53  ARG A 60  1 ? 8  
HELX_P HELX_P5  AA5 LYS A 61  ? HIS A 64  ? LYS A 61  HIS A 64  5 ? 4  
HELX_P HELX_P6  AA6 ILE A 152 ? CYS A 156 ? ILE A 152 CYS A 156 5 ? 5  
HELX_P HELX_P7  AA7 ILE A 200 ? ASN A 214 ? ILE A 200 ASN A 214 1 ? 15 
HELX_P HELX_P8  AA8 THR A 226 ? LYS A 236 ? THR A 226 LYS A 236 1 ? 11 
HELX_P HELX_P9  AA9 THR A 243 ? LEU A 250 ? THR A 243 LEU A 250 1 ? 8  
HELX_P HELX_P10 AB1 LEU A 250 ? GLY A 258 ? LEU A 250 GLY A 258 1 ? 9  
HELX_P HELX_P11 AB2 ALA A 260 ? GLY A 275 ? ALA A 260 GLY A 275 1 ? 16 
HELX_P HELX_P12 AB3 THR A 292 ? CYS A 300 ? THR A 292 CYS A 300 1 ? 9  
HELX_P HELX_P13 AB4 SER B 10  ? GLY B 15  ? SER B 10  GLY B 15  1 ? 6  
HELX_P HELX_P14 AB5 HIS B 41  ? CYS B 44  ? HIS B 41  CYS B 44  5 ? 4  
HELX_P HELX_P15 AB6 THR B 45  ? LEU B 50  ? THR B 45  LEU B 50  1 ? 6  
HELX_P HELX_P16 AB7 ASN B 53  ? ARG B 60  ? ASN B 53  ARG B 60  1 ? 8  
HELX_P HELX_P17 AB8 SER B 62  ? HIS B 64  ? SER B 62  HIS B 64  5 ? 3  
HELX_P HELX_P18 AB9 ILE B 200 ? ASN B 214 ? ILE B 200 ASN B 214 1 ? 15 
HELX_P HELX_P19 AC1 THR B 226 ? TYR B 237 ? THR B 226 TYR B 237 1 ? 12 
HELX_P HELX_P20 AC2 THR B 243 ? LEU B 250 ? THR B 243 LEU B 250 1 ? 8  
HELX_P HELX_P21 AC3 LEU B 250 ? GLY B 258 ? LEU B 250 GLY B 258 1 ? 9  
HELX_P HELX_P22 AC4 ALA B 260 ? GLY B 275 ? ALA B 260 GLY B 275 1 ? 16 
HELX_P HELX_P23 AC5 THR B 292 ? GLY B 302 ? THR B 292 GLY B 302 1 ? 11 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_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 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_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 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? B ASN 221 O   ? ? ? 1_555 F NA  . NA ? ? B ASN 221 B NA  402 1_555 ? ? ? ? ? ? ? 2.641 ? ? 
metalc2 metalc ? ? B ASN 221 OD1 ? ? ? 1_555 F NA  . NA ? ? B ASN 221 B NA  402 1_555 ? ? ? ? ? ? ? 2.467 ? ? 
metalc3 metalc ? ? B PHE 223 O   ? ? ? 1_555 F NA  . NA ? ? B PHE 223 B NA  402 1_555 ? ? ? ? ? ? ? 2.256 ? ? 
metalc4 metalc ? ? B ASP 263 O   ? ? ? 1_555 F NA  . NA ? ? B ASP 263 B NA  402 1_555 ? ? ? ? ? ? ? 3.071 ? ? 
metalc5 metalc ? ? B ASP 263 OD1 ? ? ? 1_555 F NA  . NA ? ? B ASP 263 B NA  402 1_555 ? ? ? ? ? ? ? 2.124 ? ? 
metalc6 metalc ? ? F NA  .   NA  ? ? ? 1_555 H HOH . O  ? ? B NA  402 B HOH 577 1_555 ? ? ? ? ? ? ? 2.333 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  O   ? B ASN 221 ? B ASN 221 ? 1_555 NA ? F NA . ? B NA 402 ? 1_555 OD1 ? B ASN 221 ? B ASN 221 ? 1_555 73.9  ? 
2  O   ? B ASN 221 ? B ASN 221 ? 1_555 NA ? F NA . ? B NA 402 ? 1_555 O   ? B PHE 223 ? B PHE 223 ? 1_555 114.9 ? 
3  OD1 ? B ASN 221 ? B ASN 221 ? 1_555 NA ? F NA . ? B NA 402 ? 1_555 O   ? B PHE 223 ? B PHE 223 ? 1_555 90.7  ? 
4  O   ? B ASN 221 ? B ASN 221 ? 1_555 NA ? F NA . ? B NA 402 ? 1_555 O   ? B ASP 263 ? B ASP 263 ? 1_555 153.6 ? 
5  OD1 ? B ASN 221 ? B ASN 221 ? 1_555 NA ? F NA . ? B NA 402 ? 1_555 O   ? B ASP 263 ? B ASP 263 ? 1_555 109.7 ? 
6  O   ? B PHE 223 ? B PHE 223 ? 1_555 NA ? F NA . ? B NA 402 ? 1_555 O   ? B ASP 263 ? B ASP 263 ? 1_555 91.3  ? 
7  O   ? B ASN 221 ? B ASN 221 ? 1_555 NA ? F NA . ? B NA 402 ? 1_555 OD1 ? B ASP 263 ? B ASP 263 ? 1_555 99.5  ? 
8  OD1 ? B ASN 221 ? B ASN 221 ? 1_555 NA ? F NA . ? B NA 402 ? 1_555 OD1 ? B ASP 263 ? B ASP 263 ? 1_555 170.2 ? 
9  O   ? B PHE 223 ? B PHE 223 ? 1_555 NA ? F NA . ? B NA 402 ? 1_555 OD1 ? B ASP 263 ? B ASP 263 ? 1_555 98.7  ? 
10 O   ? B ASP 263 ? B ASP 263 ? 1_555 NA ? F NA . ? B NA 402 ? 1_555 OD1 ? B ASP 263 ? B ASP 263 ? 1_555 73.0  ? 
11 O   ? B ASN 221 ? B ASN 221 ? 1_555 NA ? F NA . ? B NA 402 ? 1_555 O   ? H HOH .   ? B HOH 577 ? 1_555 80.0  ? 
12 OD1 ? B ASN 221 ? B ASN 221 ? 1_555 NA ? F NA . ? B NA 402 ? 1_555 O   ? H HOH .   ? B HOH 577 ? 1_555 93.5  ? 
13 O   ? B PHE 223 ? B PHE 223 ? 1_555 NA ? F NA . ? B NA 402 ? 1_555 O   ? H HOH .   ? B HOH 577 ? 1_555 165.1 ? 
14 O   ? B ASP 263 ? B ASP 263 ? 1_555 NA ? F NA . ? B NA 402 ? 1_555 O   ? H HOH .   ? B HOH 577 ? 1_555 73.8  ? 
15 OD1 ? B ASP 263 ? B ASP 263 ? 1_555 NA ? F NA . ? B NA 402 ? 1_555 O   ? H HOH .   ? B HOH 577 ? 1_555 78.1  ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 7 ? 
AA2 ? 5 ? 
AA3 ? 3 ? 
AA4 ? 7 ? 
AA5 ? 5 ? 
AA6 ? 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 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA4 5 6 ? anti-parallel 
AA4 6 7 ? anti-parallel 
AA5 1 2 ? parallel      
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA5 4 5 ? anti-parallel 
AA6 1 2 ? parallel      
AA6 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 TYR A 101 ? PHE A 103 ? TYR A 101 PHE A 103 
AA2 2 VAL A 157 ? GLU A 166 ? VAL A 157 GLU A 166 
AA2 3 VAL A 148 ? ASN A 151 ? VAL A 148 ASN A 151 
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 TYR A 101 ? PHE A 103 ? TYR A 101 PHE A 103 
AA3 2 VAL A 157 ? GLU A 166 ? VAL A 157 GLU A 166 
AA3 3 HIS A 172 ? THR A 175 ? HIS A 172 THR A 175 
AA4 1 VAL B 73  ? LEU B 75  ? VAL B 73  LEU B 75  
AA4 2 PHE B 66  ? ALA B 70  ? PHE B 66  ALA B 70  
AA4 3 MET B 17  ? CYS B 22  ? MET B 17  CYS B 22  
AA4 4 THR B 25  ? LEU B 32  ? THR B 25  LEU B 32  
AA4 5 VAL B 35  ? PRO B 39  ? VAL B 35  PRO B 39  
AA4 6 VAL B 86  ? VAL B 91  ? VAL B 86  VAL B 91  
AA4 7 VAL B 77  ? GLN B 83  ? VAL B 77  GLN B 83  
AA5 1 LYS B 100 ? PHE B 103 ? LYS B 100 PHE B 103 
AA5 2 CYS B 156 ? GLU B 166 ? CYS B 156 GLU B 166 
AA5 3 VAL B 148 ? ASP B 153 ? VAL B 148 ASP B 153 
AA5 4 THR B 111 ? TYR B 118 ? THR B 111 TYR B 118 
AA5 5 SER B 121 ? ALA B 129 ? SER B 121 ALA B 129 
AA6 1 LYS B 100 ? PHE B 103 ? LYS B 100 PHE B 103 
AA6 2 CYS B 156 ? GLU B 166 ? CYS B 156 GLU B 166 
AA6 3 HIS B 172 ? THR B 175 ? HIS B 172 THR B 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 VAL A 73  ? O VAL A 73  N ALA A 70  ? N ALA A 70  
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 VAL A 36  ? N VAL A 36  O LEU A 89  ? O LEU A 89  
AA1 6 7 O LYS A 88  ? O LYS A 88  N SER A 81  ? N SER A 81  
AA2 1 2 N LYS A 102 ? N LYS A 102 O PHE A 159 ? O PHE A 159 
AA2 2 3 O SER A 158 ? O SER A 158 N ASN A 151 ? N ASN A 151 
AA2 3 4 O PHE A 150 ? O PHE A 150 N SER A 113 ? N SER A 113 
AA2 4 5 N ALA A 116 ? N ALA A 116 O SER A 123 ? O SER A 123 
AA3 1 2 N LYS A 102 ? N LYS A 102 O PHE A 159 ? O PHE A 159 
AA3 2 3 N MET A 165 ? N MET A 165 O ALA A 173 ? O ALA A 173 
AA4 1 2 O VAL B 73  ? O VAL B 73  N ALA B 70  ? N ALA B 70  
AA4 2 3 O LEU B 67  ? O LEU B 67  N THR B 21  ? N THR B 21  
AA4 3 4 N VAL B 20  ? N VAL B 20  O LEU B 27  ? O LEU B 27  
AA4 4 5 N LEU B 30  ? N LEU B 30  O TYR B 37  ? O TYR B 37  
AA4 5 6 N VAL B 36  ? N VAL B 36  O LEU B 89  ? O LEU B 89  
AA4 6 7 O LYS B 88  ? O LYS B 88  N SER B 81  ? N SER B 81  
AA5 1 2 N LYS B 100 ? N LYS B 100 O VAL B 157 ? O VAL B 157 
AA5 2 3 O CYS B 156 ? O CYS B 156 N ASP B 153 ? N ASP B 153 
AA5 3 4 O PHE B 150 ? O PHE B 150 N SER B 113 ? N SER B 113 
AA5 4 5 N ALA B 116 ? N ALA B 116 O SER B 123 ? O SER B 123 
AA6 1 2 N LYS B 100 ? N LYS B 100 O VAL B 157 ? O VAL B 157 
AA6 2 3 N MET B 165 ? N MET B 165 O ALA B 173 ? O ALA B 173 
# 
_pdbx_entry_details.entry_id                   9HAK 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
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  ? ? 53.42   -131.29 
2 1 ASN A 51  ? ? -141.03 57.11   
3 1 ASN A 84  ? ? 52.81   -124.86 
4 1 ASP A 155 ? ? 83.72   -8.12   
5 1 GLN A 189 ? ? -86.07  48.16   
6 1 ASP B 33  ? ? 52.24   -134.26 
7 1 ASN B 51  ? ? -166.45 71.77   
8 1 ASN B 84  ? ? 51.66   -126.14 
9 1 TYR B 154 ? ? 51.65   -101.89 
# 
_pdbx_validate_planes.id              1 
_pdbx_validate_planes.PDB_model_num   1 
_pdbx_validate_planes.auth_comp_id    ARG 
_pdbx_validate_planes.auth_asym_id    B 
_pdbx_validate_planes.auth_seq_id     4 
_pdbx_validate_planes.PDB_ins_code    ? 
_pdbx_validate_planes.label_alt_id    ? 
_pdbx_validate_planes.rmsd            0.087 
_pdbx_validate_planes.type            'SIDE CHAIN' 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 829 ? 5.95 . 
2 1 O ? A HOH 830 ? 5.96 . 
3 1 O ? A HOH 831 ? 6.50 . 
4 1 O ? B HOH 771 ? 5.91 . 
5 1 O ? B HOH 772 ? 7.47 . 
6 1 O ? B HOH 773 ? 8.32 . 
# 
_pdbx_unobs_or_zero_occ_residues.id               1 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num    1 
_pdbx_unobs_or_zero_occ_residues.polymer_flag     Y 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag   1 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id     B 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id     GLN 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id      306 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code     ? 
_pdbx_unobs_or_zero_occ_residues.label_asym_id    B 
_pdbx_unobs_or_zero_occ_residues.label_comp_id    GLN 
_pdbx_unobs_or_zero_occ_residues.label_seq_id     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 
A1ITI C4   C  Y N 1   
A1ITI C5   C  N N 2   
A1ITI C7   C  N N 3   
A1ITI C8   C  N N 4   
A1ITI C10  C  N N 5   
A1ITI C13  C  Y N 6   
A1ITI C15  C  Y N 7   
A1ITI C21  C  Y N 8   
A1ITI C24  C  N N 9   
A1ITI C26  C  N N 10  
A1ITI C1   C  N N 11  
A1ITI C2   C  N N 12  
A1ITI C3   C  Y N 13  
A1ITI N6   N  N N 14  
A1ITI N9   N  N N 15  
A1ITI C11  C  N N 16  
A1ITI C12  C  N N 17  
A1ITI C14  C  Y N 18  
A1ITI C16  C  Y N 19  
A1ITI S17  S  Y N 20  
A1ITI C18  C  Y N 21  
A1ITI C19  C  Y N 22  
A1ITI N20  N  Y N 23  
A1ITI O22  O  N N 24  
A1ITI C23  C  N R 25  
A1ITI N25  N  N N 26  
A1ITI C27  C  N N 27  
A1ITI O28  O  N N 28  
A1ITI C29  C  Y N 29  
A1ITI C30  C  Y N 30  
A1ITI C31  C  Y N 31  
A1ITI BR32 BR N N 32  
A1ITI C33  C  Y N 33  
A1ITI H1   H  N N 34  
A1ITI H2   H  N N 35  
A1ITI H3   H  N N 36  
A1ITI H4   H  N N 37  
A1ITI H5   H  N N 38  
A1ITI H6   H  N N 39  
A1ITI H7   H  N N 40  
A1ITI H8   H  N N 41  
A1ITI H9   H  N N 42  
A1ITI H10  H  N N 43  
A1ITI H11  H  N N 44  
A1ITI H12  H  N N 45  
A1ITI H13  H  N N 46  
A1ITI H14  H  N N 47  
A1ITI H15  H  N N 48  
A1ITI H16  H  N N 49  
A1ITI H17  H  N N 50  
A1ITI H19  H  N N 51  
A1ITI H20  H  N N 52  
A1ITI H21  H  N N 53  
A1ITI H22  H  N N 54  
A1ITI H23  H  N N 55  
A1ITI H24  H  N N 56  
A1ITI H25  H  N N 57  
A1ITI H26  H  N N 58  
A1ITI H27  H  N N 59  
A1ITI H28  H  N N 60  
A1ITI H29  H  N N 61  
A1ITI H30  H  N N 62  
ALA   N    N  N N 63  
ALA   CA   C  N S 64  
ALA   C    C  N N 65  
ALA   O    O  N N 66  
ALA   CB   C  N N 67  
ALA   OXT  O  N N 68  
ALA   H    H  N N 69  
ALA   H2   H  N N 70  
ALA   HA   H  N N 71  
ALA   HB1  H  N N 72  
ALA   HB2  H  N N 73  
ALA   HB3  H  N N 74  
ALA   HXT  H  N N 75  
ARG   N    N  N N 76  
ARG   CA   C  N S 77  
ARG   C    C  N N 78  
ARG   O    O  N N 79  
ARG   CB   C  N N 80  
ARG   CG   C  N N 81  
ARG   CD   C  N N 82  
ARG   NE   N  N N 83  
ARG   CZ   C  N N 84  
ARG   NH1  N  N N 85  
ARG   NH2  N  N N 86  
ARG   OXT  O  N N 87  
ARG   H    H  N N 88  
ARG   H2   H  N N 89  
ARG   HA   H  N N 90  
ARG   HB2  H  N N 91  
ARG   HB3  H  N N 92  
ARG   HG2  H  N N 93  
ARG   HG3  H  N N 94  
ARG   HD2  H  N N 95  
ARG   HD3  H  N N 96  
ARG   HE   H  N N 97  
ARG   HH11 H  N N 98  
ARG   HH12 H  N N 99  
ARG   HH21 H  N N 100 
ARG   HH22 H  N N 101 
ARG   HXT  H  N N 102 
ASN   N    N  N N 103 
ASN   CA   C  N S 104 
ASN   C    C  N N 105 
ASN   O    O  N N 106 
ASN   CB   C  N N 107 
ASN   CG   C  N N 108 
ASN   OD1  O  N N 109 
ASN   ND2  N  N N 110 
ASN   OXT  O  N N 111 
ASN   H    H  N N 112 
ASN   H2   H  N N 113 
ASN   HA   H  N N 114 
ASN   HB2  H  N N 115 
ASN   HB3  H  N N 116 
ASN   HD21 H  N N 117 
ASN   HD22 H  N N 118 
ASN   HXT  H  N N 119 
ASP   N    N  N N 120 
ASP   CA   C  N S 121 
ASP   C    C  N N 122 
ASP   O    O  N N 123 
ASP   CB   C  N N 124 
ASP   CG   C  N N 125 
ASP   OD1  O  N N 126 
ASP   OD2  O  N N 127 
ASP   OXT  O  N N 128 
ASP   H    H  N N 129 
ASP   H2   H  N N 130 
ASP   HA   H  N N 131 
ASP   HB2  H  N N 132 
ASP   HB3  H  N N 133 
ASP   HD2  H  N N 134 
ASP   HXT  H  N N 135 
CL    CL   CL N N 136 
CYS   N    N  N N 137 
CYS   CA   C  N R 138 
CYS   C    C  N N 139 
CYS   O    O  N N 140 
CYS   CB   C  N N 141 
CYS   SG   S  N N 142 
CYS   OXT  O  N N 143 
CYS   H    H  N N 144 
CYS   H2   H  N N 145 
CYS   HA   H  N N 146 
CYS   HB2  H  N N 147 
CYS   HB3  H  N N 148 
CYS   HG   H  N N 149 
CYS   HXT  H  N N 150 
GLN   N    N  N N 151 
GLN   CA   C  N S 152 
GLN   C    C  N N 153 
GLN   O    O  N N 154 
GLN   CB   C  N N 155 
GLN   CG   C  N N 156 
GLN   CD   C  N N 157 
GLN   OE1  O  N N 158 
GLN   NE2  N  N N 159 
GLN   OXT  O  N N 160 
GLN   H    H  N N 161 
GLN   H2   H  N N 162 
GLN   HA   H  N N 163 
GLN   HB2  H  N N 164 
GLN   HB3  H  N N 165 
GLN   HG2  H  N N 166 
GLN   HG3  H  N N 167 
GLN   HE21 H  N N 168 
GLN   HE22 H  N N 169 
GLN   HXT  H  N N 170 
GLU   N    N  N N 171 
GLU   CA   C  N S 172 
GLU   C    C  N N 173 
GLU   O    O  N N 174 
GLU   CB   C  N N 175 
GLU   CG   C  N N 176 
GLU   CD   C  N N 177 
GLU   OE1  O  N N 178 
GLU   OE2  O  N N 179 
GLU   OXT  O  N N 180 
GLU   H    H  N N 181 
GLU   H2   H  N N 182 
GLU   HA   H  N N 183 
GLU   HB2  H  N N 184 
GLU   HB3  H  N N 185 
GLU   HG2  H  N N 186 
GLU   HG3  H  N N 187 
GLU   HE2  H  N N 188 
GLU   HXT  H  N N 189 
GLY   N    N  N N 190 
GLY   CA   C  N N 191 
GLY   C    C  N N 192 
GLY   O    O  N N 193 
GLY   OXT  O  N N 194 
GLY   H    H  N N 195 
GLY   H2   H  N N 196 
GLY   HA2  H  N N 197 
GLY   HA3  H  N N 198 
GLY   HXT  H  N N 199 
HIS   N    N  N N 200 
HIS   CA   C  N S 201 
HIS   C    C  N N 202 
HIS   O    O  N N 203 
HIS   CB   C  N N 204 
HIS   CG   C  Y N 205 
HIS   ND1  N  Y N 206 
HIS   CD2  C  Y N 207 
HIS   CE1  C  Y N 208 
HIS   NE2  N  Y N 209 
HIS   OXT  O  N N 210 
HIS   H    H  N N 211 
HIS   H2   H  N N 212 
HIS   HA   H  N N 213 
HIS   HB2  H  N N 214 
HIS   HB3  H  N N 215 
HIS   HD1  H  N N 216 
HIS   HD2  H  N N 217 
HIS   HE1  H  N N 218 
HIS   HE2  H  N N 219 
HIS   HXT  H  N N 220 
HOH   O    O  N N 221 
HOH   H1   H  N N 222 
HOH   H2   H  N N 223 
ILE   N    N  N N 224 
ILE   CA   C  N S 225 
ILE   C    C  N N 226 
ILE   O    O  N N 227 
ILE   CB   C  N S 228 
ILE   CG1  C  N N 229 
ILE   CG2  C  N N 230 
ILE   CD1  C  N N 231 
ILE   OXT  O  N N 232 
ILE   H    H  N N 233 
ILE   H2   H  N N 234 
ILE   HA   H  N N 235 
ILE   HB   H  N N 236 
ILE   HG12 H  N N 237 
ILE   HG13 H  N N 238 
ILE   HG21 H  N N 239 
ILE   HG22 H  N N 240 
ILE   HG23 H  N N 241 
ILE   HD11 H  N N 242 
ILE   HD12 H  N N 243 
ILE   HD13 H  N N 244 
ILE   HXT  H  N N 245 
LEU   N    N  N N 246 
LEU   CA   C  N S 247 
LEU   C    C  N N 248 
LEU   O    O  N N 249 
LEU   CB   C  N N 250 
LEU   CG   C  N N 251 
LEU   CD1  C  N N 252 
LEU   CD2  C  N N 253 
LEU   OXT  O  N N 254 
LEU   H    H  N N 255 
LEU   H2   H  N N 256 
LEU   HA   H  N N 257 
LEU   HB2  H  N N 258 
LEU   HB3  H  N N 259 
LEU   HG   H  N N 260 
LEU   HD11 H  N N 261 
LEU   HD12 H  N N 262 
LEU   HD13 H  N N 263 
LEU   HD21 H  N N 264 
LEU   HD22 H  N N 265 
LEU   HD23 H  N N 266 
LEU   HXT  H  N N 267 
LYS   N    N  N N 268 
LYS   CA   C  N S 269 
LYS   C    C  N N 270 
LYS   O    O  N N 271 
LYS   CB   C  N N 272 
LYS   CG   C  N N 273 
LYS   CD   C  N N 274 
LYS   CE   C  N N 275 
LYS   NZ   N  N N 276 
LYS   OXT  O  N N 277 
LYS   H    H  N N 278 
LYS   H2   H  N N 279 
LYS   HA   H  N N 280 
LYS   HB2  H  N N 281 
LYS   HB3  H  N N 282 
LYS   HG2  H  N N 283 
LYS   HG3  H  N N 284 
LYS   HD2  H  N N 285 
LYS   HD3  H  N N 286 
LYS   HE2  H  N N 287 
LYS   HE3  H  N N 288 
LYS   HZ1  H  N N 289 
LYS   HZ2  H  N N 290 
LYS   HZ3  H  N N 291 
LYS   HXT  H  N N 292 
MET   N    N  N N 293 
MET   CA   C  N S 294 
MET   C    C  N N 295 
MET   O    O  N N 296 
MET   CB   C  N N 297 
MET   CG   C  N N 298 
MET   SD   S  N N 299 
MET   CE   C  N N 300 
MET   OXT  O  N N 301 
MET   H    H  N N 302 
MET   H2   H  N N 303 
MET   HA   H  N N 304 
MET   HB2  H  N N 305 
MET   HB3  H  N N 306 
MET   HG2  H  N N 307 
MET   HG3  H  N N 308 
MET   HE1  H  N N 309 
MET   HE2  H  N N 310 
MET   HE3  H  N N 311 
MET   HXT  H  N N 312 
NA    NA   NA N N 313 
PHE   N    N  N N 314 
PHE   CA   C  N S 315 
PHE   C    C  N N 316 
PHE   O    O  N N 317 
PHE   CB   C  N N 318 
PHE   CG   C  Y N 319 
PHE   CD1  C  Y N 320 
PHE   CD2  C  Y N 321 
PHE   CE1  C  Y N 322 
PHE   CE2  C  Y N 323 
PHE   CZ   C  Y N 324 
PHE   OXT  O  N N 325 
PHE   H    H  N N 326 
PHE   H2   H  N N 327 
PHE   HA   H  N N 328 
PHE   HB2  H  N N 329 
PHE   HB3  H  N N 330 
PHE   HD1  H  N N 331 
PHE   HD2  H  N N 332 
PHE   HE1  H  N N 333 
PHE   HE2  H  N N 334 
PHE   HZ   H  N N 335 
PHE   HXT  H  N N 336 
PRO   N    N  N N 337 
PRO   CA   C  N S 338 
PRO   C    C  N N 339 
PRO   O    O  N N 340 
PRO   CB   C  N N 341 
PRO   CG   C  N N 342 
PRO   CD   C  N N 343 
PRO   OXT  O  N N 344 
PRO   H    H  N N 345 
PRO   HA   H  N N 346 
PRO   HB2  H  N N 347 
PRO   HB3  H  N N 348 
PRO   HG2  H  N N 349 
PRO   HG3  H  N N 350 
PRO   HD2  H  N N 351 
PRO   HD3  H  N N 352 
PRO   HXT  H  N N 353 
SER   N    N  N N 354 
SER   CA   C  N S 355 
SER   C    C  N N 356 
SER   O    O  N N 357 
SER   CB   C  N N 358 
SER   OG   O  N N 359 
SER   OXT  O  N N 360 
SER   H    H  N N 361 
SER   H2   H  N N 362 
SER   HA   H  N N 363 
SER   HB2  H  N N 364 
SER   HB3  H  N N 365 
SER   HG   H  N N 366 
SER   HXT  H  N N 367 
THR   N    N  N N 368 
THR   CA   C  N S 369 
THR   C    C  N N 370 
THR   O    O  N N 371 
THR   CB   C  N R 372 
THR   OG1  O  N N 373 
THR   CG2  C  N N 374 
THR   OXT  O  N N 375 
THR   H    H  N N 376 
THR   H2   H  N N 377 
THR   HA   H  N N 378 
THR   HB   H  N N 379 
THR   HG1  H  N N 380 
THR   HG21 H  N N 381 
THR   HG22 H  N N 382 
THR   HG23 H  N N 383 
THR   HXT  H  N N 384 
TRP   N    N  N N 385 
TRP   CA   C  N S 386 
TRP   C    C  N N 387 
TRP   O    O  N N 388 
TRP   CB   C  N N 389 
TRP   CG   C  Y N 390 
TRP   CD1  C  Y N 391 
TRP   CD2  C  Y N 392 
TRP   NE1  N  Y N 393 
TRP   CE2  C  Y N 394 
TRP   CE3  C  Y N 395 
TRP   CZ2  C  Y N 396 
TRP   CZ3  C  Y N 397 
TRP   CH2  C  Y N 398 
TRP   OXT  O  N N 399 
TRP   H    H  N N 400 
TRP   H2   H  N N 401 
TRP   HA   H  N N 402 
TRP   HB2  H  N N 403 
TRP   HB3  H  N N 404 
TRP   HD1  H  N N 405 
TRP   HE1  H  N N 406 
TRP   HE3  H  N N 407 
TRP   HZ2  H  N N 408 
TRP   HZ3  H  N N 409 
TRP   HH2  H  N N 410 
TRP   HXT  H  N N 411 
TYR   N    N  N N 412 
TYR   CA   C  N S 413 
TYR   C    C  N N 414 
TYR   O    O  N N 415 
TYR   CB   C  N N 416 
TYR   CG   C  Y N 417 
TYR   CD1  C  Y N 418 
TYR   CD2  C  Y N 419 
TYR   CE1  C  Y N 420 
TYR   CE2  C  Y N 421 
TYR   CZ   C  Y N 422 
TYR   OH   O  N N 423 
TYR   OXT  O  N N 424 
TYR   H    H  N N 425 
TYR   H2   H  N N 426 
TYR   HA   H  N N 427 
TYR   HB2  H  N N 428 
TYR   HB3  H  N N 429 
TYR   HD1  H  N N 430 
TYR   HD2  H  N N 431 
TYR   HE1  H  N N 432 
TYR   HE2  H  N N 433 
TYR   HH   H  N N 434 
TYR   HXT  H  N N 435 
VAL   N    N  N N 436 
VAL   CA   C  N S 437 
VAL   C    C  N N 438 
VAL   O    O  N N 439 
VAL   CB   C  N N 440 
VAL   CG1  C  N N 441 
VAL   CG2  C  N N 442 
VAL   OXT  O  N N 443 
VAL   H    H  N N 444 
VAL   H2   H  N N 445 
VAL   HA   H  N N 446 
VAL   HB   H  N N 447 
VAL   HG11 H  N N 448 
VAL   HG12 H  N N 449 
VAL   HG13 H  N N 450 
VAL   HG21 H  N N 451 
VAL   HG22 H  N N 452 
VAL   HG23 H  N N 453 
VAL   HXT  H  N N 454 
# 
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 
A1ITI BR32 C31  sing N N 1   
A1ITI C31  C33  doub Y N 2   
A1ITI C31  C30  sing Y N 3   
A1ITI C33  C3   sing Y N 4   
A1ITI C30  C29  doub Y N 5   
A1ITI C3   C2   sing N N 6   
A1ITI C3   C4   doub Y N 7   
A1ITI C2   C1   sing N N 8   
A1ITI C29  C4   sing Y N 9   
A1ITI C4   C5   sing N N 10  
A1ITI C5   N6   sing N N 11  
A1ITI O28  C24  doub N N 12  
A1ITI N6   C7   sing N N 13  
A1ITI N6   C23  sing N N 14  
A1ITI C24  N25  sing N N 15  
A1ITI C24  C23  sing N N 16  
A1ITI C26  N25  sing N N 17  
A1ITI C26  C27  sing N N 18  
A1ITI C7   C8   sing N N 19  
A1ITI C23  C11  sing N N 20  
A1ITI C8   N9   sing N N 21  
A1ITI C11  C10  sing N N 22  
A1ITI N9   C10  sing N N 23  
A1ITI N9   C12  sing N N 24  
A1ITI S17  C16  sing Y N 25  
A1ITI S17  C18  sing Y N 26  
A1ITI C16  C15  doub Y N 27  
A1ITI C19  C18  doub Y N 28  
A1ITI C19  N20  sing Y N 29  
A1ITI C18  C14  sing Y N 30  
A1ITI N20  C21  doub Y N 31  
A1ITI C15  C14  sing Y N 32  
A1ITI C14  C13  doub Y N 33  
A1ITI C21  C13  sing Y N 34  
A1ITI C13  C12  sing N N 35  
A1ITI C12  O22  doub N N 36  
A1ITI C5   H1   sing N N 37  
A1ITI C5   H2   sing N N 38  
A1ITI C7   H3   sing N N 39  
A1ITI C7   H4   sing N N 40  
A1ITI C8   H5   sing N N 41  
A1ITI C8   H6   sing N N 42  
A1ITI C10  H7   sing N N 43  
A1ITI C10  H8   sing N N 44  
A1ITI C15  H9   sing N N 45  
A1ITI C21  H10  sing N N 46  
A1ITI C26  H11  sing N N 47  
A1ITI C26  H12  sing N N 48  
A1ITI C1   H13  sing N N 49  
A1ITI C1   H14  sing N N 50  
A1ITI C1   H15  sing N N 51  
A1ITI C2   H16  sing N N 52  
A1ITI C2   H17  sing N N 53  
A1ITI C11  H19  sing N N 54  
A1ITI C11  H20  sing N N 55  
A1ITI C16  H21  sing N N 56  
A1ITI C19  H22  sing N N 57  
A1ITI C23  H23  sing N N 58  
A1ITI N25  H24  sing N N 59  
A1ITI C27  H25  sing N N 60  
A1ITI C27  H26  sing N N 61  
A1ITI C27  H27  sing N N 62  
A1ITI C29  H28  sing N N 63  
A1ITI C30  H29  sing N N 64  
A1ITI C33  H30  sing N N 65  
ALA   N    CA   sing N N 66  
ALA   N    H    sing N N 67  
ALA   N    H2   sing N N 68  
ALA   CA   C    sing N N 69  
ALA   CA   CB   sing N N 70  
ALA   CA   HA   sing N N 71  
ALA   C    O    doub N N 72  
ALA   C    OXT  sing N N 73  
ALA   CB   HB1  sing N N 74  
ALA   CB   HB2  sing N N 75  
ALA   CB   HB3  sing N N 76  
ALA   OXT  HXT  sing N N 77  
ARG   N    CA   sing N N 78  
ARG   N    H    sing N N 79  
ARG   N    H2   sing N N 80  
ARG   CA   C    sing N N 81  
ARG   CA   CB   sing N N 82  
ARG   CA   HA   sing N N 83  
ARG   C    O    doub N N 84  
ARG   C    OXT  sing N N 85  
ARG   CB   CG   sing N N 86  
ARG   CB   HB2  sing N N 87  
ARG   CB   HB3  sing N N 88  
ARG   CG   CD   sing N N 89  
ARG   CG   HG2  sing N N 90  
ARG   CG   HG3  sing N N 91  
ARG   CD   NE   sing N N 92  
ARG   CD   HD2  sing N N 93  
ARG   CD   HD3  sing N N 94  
ARG   NE   CZ   sing N N 95  
ARG   NE   HE   sing N N 96  
ARG   CZ   NH1  sing N N 97  
ARG   CZ   NH2  doub N N 98  
ARG   NH1  HH11 sing N N 99  
ARG   NH1  HH12 sing N N 100 
ARG   NH2  HH21 sing N N 101 
ARG   NH2  HH22 sing N N 102 
ARG   OXT  HXT  sing N N 103 
ASN   N    CA   sing N N 104 
ASN   N    H    sing N N 105 
ASN   N    H2   sing N N 106 
ASN   CA   C    sing N N 107 
ASN   CA   CB   sing N N 108 
ASN   CA   HA   sing N N 109 
ASN   C    O    doub N N 110 
ASN   C    OXT  sing N N 111 
ASN   CB   CG   sing N N 112 
ASN   CB   HB2  sing N N 113 
ASN   CB   HB3  sing N N 114 
ASN   CG   OD1  doub N N 115 
ASN   CG   ND2  sing N N 116 
ASN   ND2  HD21 sing N N 117 
ASN   ND2  HD22 sing N N 118 
ASN   OXT  HXT  sing N N 119 
ASP   N    CA   sing N N 120 
ASP   N    H    sing N N 121 
ASP   N    H2   sing N N 122 
ASP   CA   C    sing N N 123 
ASP   CA   CB   sing N N 124 
ASP   CA   HA   sing N N 125 
ASP   C    O    doub N N 126 
ASP   C    OXT  sing N N 127 
ASP   CB   CG   sing N N 128 
ASP   CB   HB2  sing N N 129 
ASP   CB   HB3  sing N N 130 
ASP   CG   OD1  doub N N 131 
ASP   CG   OD2  sing N N 132 
ASP   OD2  HD2  sing N N 133 
ASP   OXT  HXT  sing N N 134 
CYS   N    CA   sing N N 135 
CYS   N    H    sing N N 136 
CYS   N    H2   sing N N 137 
CYS   CA   C    sing N N 138 
CYS   CA   CB   sing N N 139 
CYS   CA   HA   sing N N 140 
CYS   C    O    doub N N 141 
CYS   C    OXT  sing N N 142 
CYS   CB   SG   sing N N 143 
CYS   CB   HB2  sing N N 144 
CYS   CB   HB3  sing N N 145 
CYS   SG   HG   sing N N 146 
CYS   OXT  HXT  sing N N 147 
GLN   N    CA   sing N N 148 
GLN   N    H    sing N N 149 
GLN   N    H2   sing N N 150 
GLN   CA   C    sing N N 151 
GLN   CA   CB   sing N N 152 
GLN   CA   HA   sing N N 153 
GLN   C    O    doub N N 154 
GLN   C    OXT  sing N N 155 
GLN   CB   CG   sing N N 156 
GLN   CB   HB2  sing N N 157 
GLN   CB   HB3  sing N N 158 
GLN   CG   CD   sing N N 159 
GLN   CG   HG2  sing N N 160 
GLN   CG   HG3  sing N N 161 
GLN   CD   OE1  doub N N 162 
GLN   CD   NE2  sing N N 163 
GLN   NE2  HE21 sing N N 164 
GLN   NE2  HE22 sing N N 165 
GLN   OXT  HXT  sing N N 166 
GLU   N    CA   sing N N 167 
GLU   N    H    sing N N 168 
GLU   N    H2   sing N N 169 
GLU   CA   C    sing N N 170 
GLU   CA   CB   sing N N 171 
GLU   CA   HA   sing N N 172 
GLU   C    O    doub N N 173 
GLU   C    OXT  sing N N 174 
GLU   CB   CG   sing N N 175 
GLU   CB   HB2  sing N N 176 
GLU   CB   HB3  sing N N 177 
GLU   CG   CD   sing N N 178 
GLU   CG   HG2  sing N N 179 
GLU   CG   HG3  sing N N 180 
GLU   CD   OE1  doub N N 181 
GLU   CD   OE2  sing N N 182 
GLU   OE2  HE2  sing N N 183 
GLU   OXT  HXT  sing N N 184 
GLY   N    CA   sing N N 185 
GLY   N    H    sing N N 186 
GLY   N    H2   sing N N 187 
GLY   CA   C    sing N N 188 
GLY   CA   HA2  sing N N 189 
GLY   CA   HA3  sing N N 190 
GLY   C    O    doub N N 191 
GLY   C    OXT  sing N N 192 
GLY   OXT  HXT  sing N N 193 
HIS   N    CA   sing N N 194 
HIS   N    H    sing N N 195 
HIS   N    H2   sing N N 196 
HIS   CA   C    sing N N 197 
HIS   CA   CB   sing N N 198 
HIS   CA   HA   sing N N 199 
HIS   C    O    doub N N 200 
HIS   C    OXT  sing N N 201 
HIS   CB   CG   sing N N 202 
HIS   CB   HB2  sing N N 203 
HIS   CB   HB3  sing N N 204 
HIS   CG   ND1  sing Y N 205 
HIS   CG   CD2  doub Y N 206 
HIS   ND1  CE1  doub Y N 207 
HIS   ND1  HD1  sing N N 208 
HIS   CD2  NE2  sing Y N 209 
HIS   CD2  HD2  sing N N 210 
HIS   CE1  NE2  sing Y N 211 
HIS   CE1  HE1  sing N N 212 
HIS   NE2  HE2  sing N N 213 
HIS   OXT  HXT  sing N N 214 
HOH   O    H1   sing N N 215 
HOH   O    H2   sing N N 216 
ILE   N    CA   sing N N 217 
ILE   N    H    sing N N 218 
ILE   N    H2   sing N N 219 
ILE   CA   C    sing N N 220 
ILE   CA   CB   sing N N 221 
ILE   CA   HA   sing N N 222 
ILE   C    O    doub N N 223 
ILE   C    OXT  sing N N 224 
ILE   CB   CG1  sing N N 225 
ILE   CB   CG2  sing N N 226 
ILE   CB   HB   sing N N 227 
ILE   CG1  CD1  sing N N 228 
ILE   CG1  HG12 sing N N 229 
ILE   CG1  HG13 sing N N 230 
ILE   CG2  HG21 sing N N 231 
ILE   CG2  HG22 sing N N 232 
ILE   CG2  HG23 sing N N 233 
ILE   CD1  HD11 sing N N 234 
ILE   CD1  HD12 sing N N 235 
ILE   CD1  HD13 sing N N 236 
ILE   OXT  HXT  sing N N 237 
LEU   N    CA   sing N N 238 
LEU   N    H    sing N N 239 
LEU   N    H2   sing N N 240 
LEU   CA   C    sing N N 241 
LEU   CA   CB   sing N N 242 
LEU   CA   HA   sing N N 243 
LEU   C    O    doub N N 244 
LEU   C    OXT  sing N N 245 
LEU   CB   CG   sing N N 246 
LEU   CB   HB2  sing N N 247 
LEU   CB   HB3  sing N N 248 
LEU   CG   CD1  sing N N 249 
LEU   CG   CD2  sing N N 250 
LEU   CG   HG   sing N N 251 
LEU   CD1  HD11 sing N N 252 
LEU   CD1  HD12 sing N N 253 
LEU   CD1  HD13 sing N N 254 
LEU   CD2  HD21 sing N N 255 
LEU   CD2  HD22 sing N N 256 
LEU   CD2  HD23 sing N N 257 
LEU   OXT  HXT  sing N N 258 
LYS   N    CA   sing N N 259 
LYS   N    H    sing N N 260 
LYS   N    H2   sing N N 261 
LYS   CA   C    sing N N 262 
LYS   CA   CB   sing N N 263 
LYS   CA   HA   sing N N 264 
LYS   C    O    doub N N 265 
LYS   C    OXT  sing N N 266 
LYS   CB   CG   sing N N 267 
LYS   CB   HB2  sing N N 268 
LYS   CB   HB3  sing N N 269 
LYS   CG   CD   sing N N 270 
LYS   CG   HG2  sing N N 271 
LYS   CG   HG3  sing N N 272 
LYS   CD   CE   sing N N 273 
LYS   CD   HD2  sing N N 274 
LYS   CD   HD3  sing N N 275 
LYS   CE   NZ   sing N N 276 
LYS   CE   HE2  sing N N 277 
LYS   CE   HE3  sing N N 278 
LYS   NZ   HZ1  sing N N 279 
LYS   NZ   HZ2  sing N N 280 
LYS   NZ   HZ3  sing N N 281 
LYS   OXT  HXT  sing N N 282 
MET   N    CA   sing N N 283 
MET   N    H    sing N N 284 
MET   N    H2   sing N N 285 
MET   CA   C    sing N N 286 
MET   CA   CB   sing N N 287 
MET   CA   HA   sing N N 288 
MET   C    O    doub N N 289 
MET   C    OXT  sing N N 290 
MET   CB   CG   sing N N 291 
MET   CB   HB2  sing N N 292 
MET   CB   HB3  sing N N 293 
MET   CG   SD   sing N N 294 
MET   CG   HG2  sing N N 295 
MET   CG   HG3  sing N N 296 
MET   SD   CE   sing N N 297 
MET   CE   HE1  sing N N 298 
MET   CE   HE2  sing N N 299 
MET   CE   HE3  sing N N 300 
MET   OXT  HXT  sing N N 301 
PHE   N    CA   sing N N 302 
PHE   N    H    sing N N 303 
PHE   N    H2   sing N N 304 
PHE   CA   C    sing N N 305 
PHE   CA   CB   sing N N 306 
PHE   CA   HA   sing N N 307 
PHE   C    O    doub N N 308 
PHE   C    OXT  sing N N 309 
PHE   CB   CG   sing N N 310 
PHE   CB   HB2  sing N N 311 
PHE   CB   HB3  sing N N 312 
PHE   CG   CD1  doub Y N 313 
PHE   CG   CD2  sing Y N 314 
PHE   CD1  CE1  sing Y N 315 
PHE   CD1  HD1  sing N N 316 
PHE   CD2  CE2  doub Y N 317 
PHE   CD2  HD2  sing N N 318 
PHE   CE1  CZ   doub Y N 319 
PHE   CE1  HE1  sing N N 320 
PHE   CE2  CZ   sing Y N 321 
PHE   CE2  HE2  sing N N 322 
PHE   CZ   HZ   sing N N 323 
PHE   OXT  HXT  sing N N 324 
PRO   N    CA   sing N N 325 
PRO   N    CD   sing N N 326 
PRO   N    H    sing N N 327 
PRO   CA   C    sing N N 328 
PRO   CA   CB   sing N N 329 
PRO   CA   HA   sing N N 330 
PRO   C    O    doub N N 331 
PRO   C    OXT  sing N N 332 
PRO   CB   CG   sing N N 333 
PRO   CB   HB2  sing N N 334 
PRO   CB   HB3  sing N N 335 
PRO   CG   CD   sing N N 336 
PRO   CG   HG2  sing N N 337 
PRO   CG   HG3  sing N N 338 
PRO   CD   HD2  sing N N 339 
PRO   CD   HD3  sing N N 340 
PRO   OXT  HXT  sing N N 341 
SER   N    CA   sing N N 342 
SER   N    H    sing N N 343 
SER   N    H2   sing N N 344 
SER   CA   C    sing N N 345 
SER   CA   CB   sing N N 346 
SER   CA   HA   sing N N 347 
SER   C    O    doub N N 348 
SER   C    OXT  sing N N 349 
SER   CB   OG   sing N N 350 
SER   CB   HB2  sing N N 351 
SER   CB   HB3  sing N N 352 
SER   OG   HG   sing N N 353 
SER   OXT  HXT  sing N N 354 
THR   N    CA   sing N N 355 
THR   N    H    sing N N 356 
THR   N    H2   sing N N 357 
THR   CA   C    sing N N 358 
THR   CA   CB   sing N N 359 
THR   CA   HA   sing N N 360 
THR   C    O    doub N N 361 
THR   C    OXT  sing N N 362 
THR   CB   OG1  sing N N 363 
THR   CB   CG2  sing N N 364 
THR   CB   HB   sing N N 365 
THR   OG1  HG1  sing N N 366 
THR   CG2  HG21 sing N N 367 
THR   CG2  HG22 sing N N 368 
THR   CG2  HG23 sing N N 369 
THR   OXT  HXT  sing N N 370 
TRP   N    CA   sing N N 371 
TRP   N    H    sing N N 372 
TRP   N    H2   sing N N 373 
TRP   CA   C    sing N N 374 
TRP   CA   CB   sing N N 375 
TRP   CA   HA   sing N N 376 
TRP   C    O    doub N N 377 
TRP   C    OXT  sing N N 378 
TRP   CB   CG   sing N N 379 
TRP   CB   HB2  sing N N 380 
TRP   CB   HB3  sing N N 381 
TRP   CG   CD1  doub Y N 382 
TRP   CG   CD2  sing Y N 383 
TRP   CD1  NE1  sing Y N 384 
TRP   CD1  HD1  sing N N 385 
TRP   CD2  CE2  doub Y N 386 
TRP   CD2  CE3  sing Y N 387 
TRP   NE1  CE2  sing Y N 388 
TRP   NE1  HE1  sing N N 389 
TRP   CE2  CZ2  sing Y N 390 
TRP   CE3  CZ3  doub Y N 391 
TRP   CE3  HE3  sing N N 392 
TRP   CZ2  CH2  doub Y N 393 
TRP   CZ2  HZ2  sing N N 394 
TRP   CZ3  CH2  sing Y N 395 
TRP   CZ3  HZ3  sing N N 396 
TRP   CH2  HH2  sing N N 397 
TRP   OXT  HXT  sing N N 398 
TYR   N    CA   sing N N 399 
TYR   N    H    sing N N 400 
TYR   N    H2   sing N N 401 
TYR   CA   C    sing N N 402 
TYR   CA   CB   sing N N 403 
TYR   CA   HA   sing N N 404 
TYR   C    O    doub N N 405 
TYR   C    OXT  sing N N 406 
TYR   CB   CG   sing N N 407 
TYR   CB   HB2  sing N N 408 
TYR   CB   HB3  sing N N 409 
TYR   CG   CD1  doub Y N 410 
TYR   CG   CD2  sing Y N 411 
TYR   CD1  CE1  sing Y N 412 
TYR   CD1  HD1  sing N N 413 
TYR   CD2  CE2  doub Y N 414 
TYR   CD2  HD2  sing N N 415 
TYR   CE1  CZ   doub Y N 416 
TYR   CE1  HE1  sing N N 417 
TYR   CE2  CZ   sing Y N 418 
TYR   CE2  HE2  sing N N 419 
TYR   CZ   OH   sing N N 420 
TYR   OH   HH   sing N N 421 
TYR   OXT  HXT  sing N N 422 
VAL   N    CA   sing N N 423 
VAL   N    H    sing N N 424 
VAL   N    H2   sing N N 425 
VAL   CA   C    sing N N 426 
VAL   CA   CB   sing N N 427 
VAL   CA   HA   sing N N 428 
VAL   C    O    doub N N 429 
VAL   C    OXT  sing N N 430 
VAL   CB   CG1  sing N N 431 
VAL   CB   CG2  sing N N 432 
VAL   CB   HB   sing N N 433 
VAL   CG1  HG11 sing N N 434 
VAL   CG1  HG12 sing N N 435 
VAL   CG1  HG13 sing N N 436 
VAL   CG2  HG21 sing N N 437 
VAL   CG2  HG22 sing N N 438 
VAL   CG2  HG23 sing N N 439 
VAL   OXT  HXT  sing N N 440 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      Other 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          'internal structure' 
# 
_atom_sites.entry_id                    9HAK 
_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]   0.014742 
_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]   0.009984 
_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]   0.009589 
_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.pdbx_scat_Z 
_atom_type.pdbx_N_electrons 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
BR 35 35 17.1822 2.1723  5.2368 16.5796 5.6388 0.2609  3.9859 41.4328  0.4668   
C  6  6  2.3103  20.8439 1.0201 10.2075 1.5888 0.5687  0.8651 51.6512  0.2156   
CL 17 17 11.4601 0.0104  7.1962 1.1662  6.2554 18.5194 1.6455 47.7784  -9.3746  
H  1  1  0.4930  10.5109 0.3229 26.1257 0.1402 3.1424  0.0408 57.7997  0.0030   
N  7  7  12.2220 0.0057  3.1346 9.8933  2.0141 28.9975 1.1672 0.5826   -11.5379 
NA 11 11 4.7659  3.2850  3.1758 8.8422  1.2683 0.3136  1.1136 129.4240 0.7218   
O  8  8  3.0487  13.2771 2.2870 5.7011  1.5464 0.3239  0.8671 32.9089  0.2508   
S  16 16 6.9054  1.4679  5.2035 22.2151 1.4379 0.2536  1.5863 56.1720  1.0220   
# 
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   ? 13.733  9.326   -12.885 1   19.081 ? 1   SER   A N    1 
ATOM   2    C  CA   . SER   A 1 1   ? 13.97   8.304   -13.944 1   19.764 ? 1   SER   A CA   1 
ATOM   3    C  C    . SER   A 1 1   ? 12.81   7.317   -13.962 1   18.74  ? 1   SER   A C    1 
ATOM   4    O  O    . SER   A 1 1   ? 11.919  7.384   -13.125 1   16.436 ? 1   SER   A O    1 
ATOM   5    C  CB   . SER   A 1 1   ? 15.32   7.591   -13.776 1   19.131 ? 1   SER   A CB   1 
ATOM   6    O  OG   . SER   A 1 1   ? 15.613  6.706   -14.853 1   24.128 ? 1   SER   A OG   1 
ATOM   7    N  N    . GLY   A 1 2   ? 12.829  6.434   -14.964 1   18.786 ? 2   GLY   A N    1 
ATOM   8    C  CA   . GLY   A 1 2   ? 11.761  5.495   -15.229 1   18.013 ? 2   GLY   A CA   1 
ATOM   9    C  C    . GLY   A 1 2   ? 10.908  5.981   -16.395 1   17.411 ? 2   GLY   A C    1 
ATOM   10   O  O    . GLY   A 1 2   ? 10.942  7.144   -16.768 1   18.178 ? 2   GLY   A O    1 
ATOM   11   N  N    . PHE   A 1 3   ? 10.148  5.065   -16.974 1   16.67  ? 3   PHE   A N    1 
ATOM   12   C  CA   . PHE   A 1 3   ? 9.253   5.432   -18.053 1   16.569 ? 3   PHE   A CA   1 
ATOM   13   C  C    . PHE   A 1 3   ? 8.166   4.376   -18.119 1   16.548 ? 3   PHE   A C    1 
ATOM   14   O  O    . PHE   A 1 3   ? 8.438   3.214   -18.393 1   18.284 ? 3   PHE   A O    1 
ATOM   15   C  CB   . PHE   A 1 3   ? 10.017  5.572   -19.376 1   17.191 ? 3   PHE   A CB   1 
ATOM   16   C  CG   . PHE   A 1 3   ? 9.256   6.424   -20.379 1   17.87  ? 3   PHE   A CG   1 
ATOM   17   C  CD1  . PHE   A 1 3   ? 9.202   7.806   -20.236 1   18.721 ? 3   PHE   A CD1  1 
ATOM   18   C  CD2  . PHE   A 1 3   ? 8.542   5.842   -21.422 1   19.163 ? 3   PHE   A CD2  1 
ATOM   19   C  CE1  . PHE   A 1 3   ? 8.474   8.587   -21.121 1   19.612 ? 3   PHE   A CE1  1 
ATOM   20   C  CE2  . PHE   A 1 3   ? 7.842   6.632   -22.32  1   19.005 ? 3   PHE   A CE2  1 
ATOM   21   C  CZ   . PHE   A 1 3   ? 7.792   7.999   -22.156 1   19.705 ? 3   PHE   A CZ   1 
ATOM   22   N  N    . ARG   A 1 4   ? 6.928   4.806   -17.852 1   15.504 ? 4   ARG   A N    1 
ATOM   23   C  CA   . ARG   A 1 4   ? 5.794   3.906   -17.774 1   15.922 ? 4   ARG   A CA   1 
ATOM   24   C  C    . ARG   A 1 4   ? 4.647   4.465   -18.602 1   14.38  ? 4   ARG   A C    1 
ATOM   25   O  O    . ARG   A 1 4   ? 4.548   5.671   -18.798 1   14.08  ? 4   ARG   A O    1 
ATOM   26   C  CB   . ARG   A 1 4   ? 5.32    3.854   -16.318 1   17.424 ? 4   ARG   A CB   1 
ATOM   27   C  CG   . ARG   A 1 4   ? 6.236   3.074   -15.391 1   20.02  ? 4   ARG   A CG   1 
ATOM   28   C  CD   . ARG   A 1 4   ? 5.926   1.572   -15.516 1   21.676 ? 4   ARG   A CD   1 
ATOM   29   N  NE   . ARG   A 1 4   ? 6.448   0.787   -14.384 1   23.326 ? 4   ARG   A NE   1 
ATOM   30   C  CZ   . ARG   A 1 4   ? 6.311   -0.53   -14.304 1   22.321 ? 4   ARG   A CZ   1 
ATOM   31   N  NH1  . ARG   A 1 4   ? 5.472   -1.155  -15.115 1   24.308 ? 4   ARG   A NH1  1 
ATOM   32   N  NH2  . ARG   A 1 4   ? 6.997   -1.229  -13.415 1   19.929 ? 4   ARG   A NH2  1 
ATOM   33   N  N    A LYS   A 1 5   ? 3.758   3.583   -19.068 0.5 15.191 ? 5   LYS   A N    1 
ATOM   34   N  N    B LYS   A 1 5   ? 3.774   3.565   -19.061 0.5 14.266 ? 5   LYS   A N    1 
ATOM   35   C  CA   A LYS   A 1 5   ? 2.492   4.038   -19.624 0.5 15.821 ? 5   LYS   A CA   1 
ATOM   36   C  CA   B LYS   A 1 5   ? 2.463   3.974   -19.53  0.5 14.606 ? 5   LYS   A CA   1 
ATOM   37   C  C    A LYS   A 1 5   ? 1.675   4.613   -18.47  0.5 15.291 ? 5   LYS   A C    1 
ATOM   38   C  C    B LYS   A 1 5   ? 1.762   4.624   -18.345 0.5 14.356 ? 5   LYS   A C    1 
ATOM   39   O  O    A LYS   A 1 5   ? 1.202   3.88    -17.615 0.5 16.966 ? 5   LYS   A O    1 
ATOM   40   O  O    B LYS   A 1 5   ? 1.534   3.969   -17.328 0.5 15.223 ? 5   LYS   A O    1 
ATOM   41   C  CB   A LYS   A 1 5   ? 1.743   2.92    -20.359 0.5 18.308 ? 5   LYS   A CB   1 
ATOM   42   C  CB   B LYS   A 1 5   ? 1.671   2.767   -20.046 0.5 15.91  ? 5   LYS   A CB   1 
ATOM   43   C  CG   A LYS   A 1 5   ? 1.921   2.83    -21.875 0.5 20.121 ? 5   LYS   A CG   1 
ATOM   44   C  CG   B LYS   A 1 5   ? 2.122   2.258   -21.402 0.5 16.649 ? 5   LYS   A CG   1 
ATOM   45   C  CD   A LYS   A 1 5   ? 1.568   1.46    -22.443 0.5 21.857 ? 5   LYS   A CD   1 
ATOM   46   C  CD   B LYS   A 1 5   ? 1.058   1.5     -22.188 0.5 17.885 ? 5   LYS   A CD   1 
ATOM   47   C  CE   A LYS   A 1 5   ? 1.532   1.377   -23.941 0.5 22.35  ? 5   LYS   A CE   1 
ATOM   48   C  CE   B LYS   A 1 5   ? 1.587   1.273   -23.564 0.5 18.906 ? 5   LYS   A CE   1 
ATOM   49   N  NZ   A LYS   A 1 5   ? 0.571   0.327   -24.297 0.5 22.677 ? 5   LYS   A NZ   1 
ATOM   50   N  NZ   B LYS   A 1 5   ? 2.158   2.539   -24.031 0.5 19.471 ? 5   LYS   A NZ   1 
ATOM   51   N  N    . MET   A 1 6   ? 1.535   5.935   -18.452 1   14.356 ? 6   MET   A N    1 
ATOM   52   C  CA   A MET   A 1 6   ? 1.02    6.668   -17.313 0.6 14.755 ? 6   MET   A CA   1 
ATOM   53   C  CA   B MET   A 1 6   ? 1.046   6.712   -17.329 0.4 14.25  ? 6   MET   A CA   1 
ATOM   54   C  C    . MET   A 1 6   ? -0.296  7.328   -17.703 1   13.992 ? 6   MET   A C    1 
ATOM   55   O  O    . MET   A 1 6   ? -0.363  8.133   -18.631 1   14.681 ? 6   MET   A O    1 
ATOM   56   C  CB   A MET   A 1 6   ? 2.034   7.723   -16.872 0.6 16.768 ? 6   MET   A CB   1 
ATOM   57   C  CB   B MET   A 1 6   ? 2.062   7.806   -16.986 0.4 15.099 ? 6   MET   A CB   1 
ATOM   58   C  CG   A MET   A 1 6   ? 1.649   8.407   -15.592 0.6 18.941 ? 6   MET   A CG   1 
ATOM   59   C  CG   B MET   A 1 6   ? 1.641   8.722   -15.873 0.4 15.787 ? 6   MET   A CG   1 
ATOM   60   S  SD   A MET   A 1 6   ? 3.058   9.287   -14.899 0.6 22.305 ? 6   MET   A SD   1 
ATOM   61   S  SD   B MET   A 1 6   ? 2.968   9.845   -15.404 0.4 17.605 ? 6   MET   A SD   1 
ATOM   62   C  CE   A MET   A 1 6   ? 3.185   10.514  -16.212 0.6 20.249 ? 6   MET   A CE   1 
ATOM   63   C  CE   B MET   A 1 6   ? 4.292   8.641   -15.231 0.4 15.15  ? 6   MET   A CE   1 
ATOM   64   N  N    . ALA   A 1 7   ? -1.341  6.951   -16.971 1   12.928 ? 7   ALA   A N    1 
ATOM   65   C  CA   . ALA   A 1 7   ? -2.665  7.523   -17.171 1   12.939 ? 7   ALA   A CA   1 
ATOM   66   C  C    . ALA   A 1 7   ? -2.811  8.797   -16.354 1   12.48  ? 7   ALA   A C    1 
ATOM   67   O  O    . ALA   A 1 7   ? -2.03   9.085   -15.443 1   13.285 ? 7   ALA   A O    1 
ATOM   68   C  CB   . ALA   A 1 7   ? -3.75   6.537   -16.8   1   13.158 ? 7   ALA   A CB   1 
ATOM   69   N  N    . PHE   A 1 8   ? -3.811  9.593   -16.709 1   11.982 ? 8   PHE   A N    1 
ATOM   70   C  CA   . PHE   A 1 8   ? -4.208  10.692  -15.851 1   12.449 ? 8   PHE   A CA   1 
ATOM   71   C  C    . PHE   A 1 8   ? -4.942  10.149  -14.633 1   13.165 ? 8   PHE   A C    1 
ATOM   72   O  O    . PHE   A 1 8   ? -5.675  9.164   -14.718 1   13.908 ? 8   PHE   A O    1 
ATOM   73   C  CB   . PHE   A 1 8   ? -5.083  11.694  -16.595 1   12.7   ? 8   PHE   A CB   1 
ATOM   74   C  CG   . PHE   A 1 8   ? -4.266  12.549  -17.545 1   13.655 ? 8   PHE   A CG   1 
ATOM   75   C  CD1  . PHE   A 1 8   ? -3.522  13.617  -17.053 1   15.399 ? 8   PHE   A CD1  1 
ATOM   76   C  CD2  . PHE   A 1 8   ? -4.162  12.221  -18.893 1   14.643 ? 8   PHE   A CD2  1 
ATOM   77   C  CE1  . PHE   A 1 8   ? -2.745  14.368  -17.908 1   16.138 ? 8   PHE   A CE1  1 
ATOM   78   C  CE2  . PHE   A 1 8   ? -3.375  12.982  -19.738 1   14.989 ? 8   PHE   A CE2  1 
ATOM   79   C  CZ   . PHE   A 1 8   ? -2.673  14.049  -19.241 1   15.993 ? 8   PHE   A CZ   1 
ATOM   80   N  N    . PRO   A 1 9   ? -4.821  10.834  -13.474 1   13.961 ? 9   PRO   A N    1 
ATOM   81   C  CA   . PRO   A 1 9   ? -5.625  10.488  -12.301 1   14.543 ? 9   PRO   A CA   1 
ATOM   82   C  C    . PRO   A 1 9   ? -7.098  10.551  -12.704 1   14.211 ? 9   PRO   A C    1 
ATOM   83   O  O    . PRO   A 1 9   ? -7.505  11.505  -13.358 1   14.839 ? 9   PRO   A O    1 
ATOM   84   C  CB   . PRO   A 1 9   ? -5.224  11.572  -11.286 1   15.364 ? 9   PRO   A CB   1 
ATOM   85   C  CG   . PRO   A 1 9   ? -3.851  12.033  -11.753 1   15.968 ? 9   PRO   A CG   1 
ATOM   86   C  CD   . PRO   A 1 9   ? -3.978  12.019  -13.264 1   15.47  ? 9   PRO   A CD   1 
ATOM   87   N  N    . SER   A 1 10  ? -7.89   9.54    -12.308 1   13.391 ? 10  SER   A N    1 
ATOM   88   C  CA   . SER   A 1 10  ? -9.216  9.317   -12.872 1   13.515 ? 10  SER   A CA   1 
ATOM   89   C  C    . SER   A 1 10  ? -10.343 9.939   -12.049 1   13.261 ? 10  SER   A C    1 
ATOM   90   O  O    . SER   A 1 10  ? -11.494 9.883   -12.487 1   13.274 ? 10  SER   A O    1 
ATOM   91   C  CB   . SER   A 1 10  ? -9.456  7.845   -13.051 1   14.186 ? 10  SER   A CB   1 
ATOM   92   O  OG   . SER   A 1 10  ? -9.29   7.128   -11.832 1   14.369 ? 10  SER   A OG   1 
ATOM   93   N  N    . GLY   A 1 11  ? -10.04  10.521  -10.882 1   13.326 ? 11  GLY   A N    1 
ATOM   94   C  CA   . GLY   A 1 11  ? -11.082 10.963  -9.958  1   13.747 ? 11  GLY   A CA   1 
ATOM   95   C  C    . GLY   A 1 11  ? -12.1   11.906  -10.594 1   14.167 ? 11  GLY   A C    1 
ATOM   96   O  O    . GLY   A 1 11  ? -13.297 11.771  -10.348 1   14.988 ? 11  GLY   A O    1 
ATOM   97   N  N    . LYS   A 1 12  ? -11.647 12.867  -11.404 1   13.402 ? 12  LYS   A N    1 
ATOM   98   C  CA   . LYS   A 1 12  ? -12.569 13.833  -11.986 1   14.13  ? 12  LYS   A CA   1 
ATOM   99   C  C    . LYS   A 1 12  ? -13.585 13.156  -12.903 1   13.697 ? 12  LYS   A C    1 
ATOM   100  O  O    . LYS   A 1 12  ? -14.691 13.66   -13.05  1   15.401 ? 12  LYS   A O    1 
ATOM   101  C  CB   . LYS   A 1 12  ? -11.82  14.94   -12.726 1   15.378 ? 12  LYS   A CB   1 
ATOM   102  C  CG   . LYS   A 1 12  ? -11.108 15.915  -11.811 1   17.591 ? 12  LYS   A CG   1 
ATOM   103  C  CD   . LYS   A 1 12  ? -10.221 16.879  -12.592 1   20.532 ? 12  LYS   A CD   1 
ATOM   104  C  CE   . LYS   A 1 12  ? -9.671  17.973  -11.737 1   23.6   ? 12  LYS   A CE   1 
ATOM   105  N  NZ   . LYS   A 1 12  ? -8.822  17.459  -10.664 1   25.886 ? 12  LYS   A NZ   1 
ATOM   106  N  N    . VAL   A 1 13  ? -13.204 12.042  -13.531 1   13.19  ? 13  VAL   A N    1 
ATOM   107  C  CA   . VAL   A 1 13  ? -14.097 11.295  -14.409 1   12.899 ? 13  VAL   A CA   1 
ATOM   108  C  C    . VAL   A 1 13  ? -14.947 10.307  -13.607 1   13.063 ? 13  VAL   A C    1 
ATOM   109  O  O    . VAL   A 1 13  ? -16.128 10.118  -13.915 1   13.492 ? 13  VAL   A O    1 
ATOM   110  C  CB   . VAL   A 1 13  ? -13.31  10.615  -15.54  1   13.062 ? 13  VAL   A CB   1 
ATOM   111  C  CG1  . VAL   A 1 13  ? -14.224 9.797   -16.449 1   14.183 ? 13  VAL   A CG1  1 
ATOM   112  C  CG2  . VAL   A 1 13  ? -12.552 11.663  -16.351 1   14.431 ? 13  VAL   A CG2  1 
ATOM   113  N  N    . GLU   A 1 14  ? -14.383 9.692   -12.564 1   13.222 ? 14  GLU   A N    1 
ATOM   114  C  CA   . GLU   A 1 14  ? -15.144 8.766   -11.732 1   13.534 ? 14  GLU   A CA   1 
ATOM   115  C  C    . GLU   A 1 14  ? -16.433 9.411   -11.223 1   14.228 ? 14  GLU   A C    1 
ATOM   116  O  O    . GLU   A 1 14  ? -17.48  8.761   -11.19  1   15.11  ? 14  GLU   A O    1 
ATOM   117  C  CB   . GLU   A 1 14  ? -14.336 8.311   -10.516 1   14.211 ? 14  GLU   A CB   1 
ATOM   118  C  CG   . GLU   A 1 14  ? -13.177 7.38    -10.846 1   14.95  ? 14  GLU   A CG   1 
ATOM   119  C  CD   . GLU   A 1 14  ? -12.237 7.192   -9.67   1   16.1   ? 14  GLU   A CD   1 
ATOM   120  O  OE1  . GLU   A 1 14  ? -11.024 7.407   -9.841  1   15.604 ? 14  GLU   A OE1  1 
ATOM   121  O  OE2  . GLU   A 1 14  ? -12.718 6.843   -8.576  1   17.861 ? 14  GLU   A OE2  1 
ATOM   122  N  N    . GLY   A 1 15  ? -16.353 10.693  -10.845 1   14.104 ? 15  GLY   A N    1 
ATOM   123  C  CA   . GLY   A 1 15  ? -17.485 11.402  -10.276 1   15.001 ? 15  GLY   A CA   1 
ATOM   124  C  C    . GLY   A 1 15  ? -18.574 11.705  -11.303 1   14.755 ? 15  GLY   A C    1 
ATOM   125  O  O    . GLY   A 1 15  ? -19.62  12.238  -10.935 1   16.218 ? 15  GLY   A O    1 
ATOM   126  N  N    . CYS   A 1 16  ? -18.331 11.349  -12.57  1   13.828 ? 16  CYS   A N    1 
ATOM   127  C  CA   . CYS   A 1 16  ? -19.278 11.585  -13.647 1   13.86  ? 16  CYS   A CA   1 
ATOM   128  C  C    . CYS   A 1 16  ? -19.908 10.294  -14.162 1   13.619 ? 16  CYS   A C    1 
ATOM   129  O  O    . CYS   A 1 16  ? -20.801 10.36   -15.001 1   14.171 ? 16  CYS   A O    1 
ATOM   130  C  CB   . CYS   A 1 16  ? -18.622 12.307  -14.817 1   14.446 ? 16  CYS   A CB   1 
ATOM   131  S  SG   . CYS   A 1 16  ? -17.914 13.914  -14.393 1   17.7   ? 16  CYS   A SG   1 
ATOM   132  N  N    . MET   A 1 17  ? -19.488 9.124   -13.672 1   13.565 ? 17  MET   A N    1 
ATOM   133  C  CA   . MET   A 1 17  ? -19.981 7.884   -14.243 1   13.798 ? 17  MET   A CA   1 
ATOM   134  C  C    . MET   A 1 17  ? -21.293 7.479   -13.58  1   14.018 ? 17  MET   A C    1 
ATOM   135  O  O    . MET   A 1 17  ? -21.415 7.481   -12.36  1   15.452 ? 17  MET   A O    1 
ATOM   136  C  CB   . MET   A 1 17  ? -18.942 6.768   -14.11  1   14.374 ? 17  MET   A CB   1 
ATOM   137  C  CG   . MET   A 1 17  ? -17.634 7.067   -14.815 1   14.846 ? 17  MET   A CG   1 
ATOM   138  S  SD   . MET   A 1 17  ? -17.781 7.57    -16.544 1   15.228 ? 17  MET   A SD   1 
ATOM   139  C  CE   . MET   A 1 17  ? -18.737 6.215   -17.247 1   15.229 ? 17  MET   A CE   1 
ATOM   140  N  N    . VAL   A 1 18  ? -22.265 7.131   -14.431 1   13.787 ? 18  VAL   A N    1 
ATOM   141  C  CA   . VAL   A 1 18  ? -23.571 6.679   -13.987 1   14.239 ? 18  VAL   A CA   1 
ATOM   142  C  C    . VAL   A 1 18  ? -23.957 5.425   -14.763 1   14.073 ? 18  VAL   A C    1 
ATOM   143  O  O    . VAL   A 1 18  ? -23.328 5.066   -15.755 1   13.994 ? 18  VAL   A O    1 
ATOM   144  C  CB   . VAL   A 1 18  ? -24.636 7.781   -14.149 1   14.788 ? 18  VAL   A CB   1 
ATOM   145  C  CG1  . VAL   A 1 18  ? -24.329 9.005   -13.297 1   15.403 ? 18  VAL   A CG1  1 
ATOM   146  C  CG2  . VAL   A 1 18  ? -24.854 8.198   -15.599 1   14.46  ? 18  VAL   A CG2  1 
ATOM   147  N  N    . GLN   A 1 19  ? -25.033 4.781   -14.307 1   14.997 ? 19  GLN   A N    1 
ATOM   148  C  CA   . GLN   A 1 19  ? -25.613 3.645   -14.989 1   16.106 ? 19  GLN   A CA   1 
ATOM   149  C  C    . GLN   A 1 19  ? -26.879 4.098   -15.718 1   15.703 ? 19  GLN   A C    1 
ATOM   150  O  O    . GLN   A 1 19  ? -27.688 4.817   -15.142 1   16.556 ? 19  GLN   A O    1 
ATOM   151  C  CB   . GLN   A 1 19  ? -25.945 2.598   -13.931 1   19.523 ? 19  GLN   A CB   1 
ATOM   152  C  CG   . GLN   A 1 19  ? -26.469 1.304   -14.524 1   22.385 ? 19  GLN   A CG   1 
ATOM   153  C  CD   . GLN   A 1 19  ? -26.864 0.305   -13.469 1   25.234 ? 19  GLN   A CD   1 
ATOM   154  O  OE1  . GLN   A 1 19  ? -26.133 -0.647  -13.191 1   28.811 ? 19  GLN   A OE1  1 
ATOM   155  N  NE2  . GLN   A 1 19  ? -28.037 0.513   -12.889 1   26.875 ? 19  GLN   A NE2  1 
ATOM   156  N  N    . VAL   A 1 20  ? -27.034 3.665   -16.976 1   15.026 ? 20  VAL   A N    1 
ATOM   157  C  CA   . VAL   A 1 20  ? -28.211 3.964   -17.776 1   15.698 ? 20  VAL   A CA   1 
ATOM   158  C  C    . VAL   A 1 20  ? -28.872 2.646   -18.161 1   15.622 ? 20  VAL   A C    1 
ATOM   159  O  O    . VAL   A 1 20  ? -28.215 1.759   -18.693 1   16.492 ? 20  VAL   A O    1 
ATOM   160  C  CB   . VAL   A 1 20  ? -27.88  4.789   -19.032 1   15.942 ? 20  VAL   A CB   1 
ATOM   161  C  CG1  . VAL   A 1 20  ? -29.123 5.079   -19.867 1   16.207 ? 20  VAL   A CG1  1 
ATOM   162  C  CG2  . VAL   A 1 20  ? -27.152 6.081   -18.681 1   16.363 ? 20  VAL   A CG2  1 
ATOM   163  N  N    . THR   A 1 21  ? -30.18  2.536   -17.892 1   16.623 ? 21  THR   A N    1 
ATOM   164  C  CA   . THR   A 1 21  ? -30.946 1.358   -18.255 1   18.054 ? 21  THR   A CA   1 
ATOM   165  C  C    . THR   A 1 21  ? -32.112 1.755   -19.158 1   18.358 ? 21  THR   A C    1 
ATOM   166  O  O    . THR   A 1 21  ? -32.855 2.69    -18.868 1   20.16  ? 21  THR   A O    1 
ATOM   167  C  CB   . THR   A 1 21  ? -31.464 0.651   -17.003 1   19.613 ? 21  THR   A CB   1 
ATOM   168  O  OG1  . THR   A 1 21  ? -30.325 0.29    -16.23  1   21.189 ? 21  THR   A OG1  1 
ATOM   169  C  CG2  . THR   A 1 21  ? -32.238 -0.614  -17.329 1   20.592 ? 21  THR   A CG2  1 
ATOM   170  N  N    . CYS   A 1 22  ? -32.279 0.998   -20.243 1   18.865 ? 22  CYS   A N    1 
ATOM   171  C  CA   . CYS   A 1 22  ? -33.435 1.111   -21.117 1   19.952 ? 22  CYS   A CA   1 
ATOM   172  C  C    . CYS   A 1 22  ? -33.899 -0.315  -21.396 1   20.678 ? 22  CYS   A C    1 
ATOM   173  O  O    . CYS   A 1 22  ? -33.15  -1.108  -21.962 1   20.597 ? 22  CYS   A O    1 
ATOM   174  C  CB   . CYS   A 1 22  ? -33.071 1.878   -22.39  1   20.867 ? 22  CYS   A CB   1 
ATOM   175  S  SG   . CYS   A 1 22  ? -34.485 2.199   -23.47  1   25.205 ? 22  CYS   A SG   1 
ATOM   176  N  N    . GLY   A 1 23  ? -35.11  -0.659  -20.952 1   23.085 ? 23  GLY   A N    1 
ATOM   177  C  CA   . GLY   A 1 23  ? -35.58  -2.03   -21.059 1   24.442 ? 23  GLY   A CA   1 
ATOM   178  C  C    . GLY   A 1 23  ? -34.647 -2.988  -20.319 1   24.756 ? 23  GLY   A C    1 
ATOM   179  O  O    . GLY   A 1 23  ? -34.34  -2.776  -19.145 1   25.902 ? 23  GLY   A O    1 
ATOM   180  N  N    . THR   A 1 24  ? -34.165 -4.017  -21.026 1   24.235 ? 24  THR   A N    1 
ATOM   181  C  CA   . THR   A 1 24  ? -33.296 -5.025  -20.43  1   26.005 ? 24  THR   A CA   1 
ATOM   182  C  C    . THR   A 1 24  ? -31.818 -4.645  -20.548 1   24.403 ? 24  THR   A C    1 
ATOM   183  O  O    . THR   A 1 24  ? -30.959 -5.398  -20.078 1   26.129 ? 24  THR   A O    1 
ATOM   184  C  CB   . THR   A 1 24  ? -33.557 -6.389  -21.072 1   28.271 ? 24  THR   A CB   1 
ATOM   185  O  OG1  . THR   A 1 24  ? -33.329 -6.243  -22.472 1   31.408 ? 24  THR   A OG1  1 
ATOM   186  C  CG2  . THR   A 1 24  ? -34.964 -6.891  -20.806 1   29.141 ? 24  THR   A CG2  1 
ATOM   187  N  N    . THR   A 1 25  ? -31.499 -3.494  -21.155 1   22.23  ? 25  THR   A N    1 
ATOM   188  C  CA   . THR   A 1 25  ? -30.103 -3.131  -21.381 1   21.943 ? 25  THR   A CA   1 
ATOM   189  C  C    . THR   A 1 25  ? -29.636 -2.12   -20.341 1   20.829 ? 25  THR   A C    1 
ATOM   190  O  O    . THR   A 1 25  ? -30.248 -1.069  -20.177 1   21.819 ? 25  THR   A O    1 
ATOM   191  C  CB   . THR   A 1 25  ? -29.888 -2.54   -22.769 1   23.567 ? 25  THR   A CB   1 
ATOM   192  O  OG1  . THR   A 1 25  ? -30.208 -3.597  -23.664 1   26.165 ? 25  THR   A OG1  1 
ATOM   193  C  CG2  . THR   A 1 25  ? -28.457 -2.056  -22.947 1   24.076 ? 25  THR   A CG2  1 
ATOM   194  N  N    . THR   A 1 26  ? -28.492 -2.426  -19.719 1   20.816 ? 26  THR   A N    1 
ATOM   195  C  CA   . THR   A 1 26  ? -27.798 -1.506  -18.838 1   19.794 ? 26  THR   A CA   1 
ATOM   196  C  C    . THR   A 1 26  ? -26.397 -1.267  -19.394 1   17.605 ? 26  THR   A C    1 
ATOM   197  O  O    . THR   A 1 26  ? -25.688 -2.217  -19.739 1   18.735 ? 26  THR   A O    1 
ATOM   198  C  CB   . THR   A 1 26  ? -27.742 -2.086  -17.427 1   22.623 ? 26  THR   A CB   1 
ATOM   199  O  OG1  . THR   A 1 26  ? -29.081 -2.161  -16.948 1   25.56  ? 26  THR   A OG1  1 
ATOM   200  C  CG2  . THR   A 1 26  ? -26.947 -1.208  -16.489 1   23.136 ? 26  THR   A CG2  1 
ATOM   201  N  N    . LEU   A 1 27  ? -26.004 0.01    -19.459 1   15.261 ? 27  LEU   A N    1 
ATOM   202  C  CA   . LEU   A 1 27  ? -24.627 0.358   -19.778 1   14.037 ? 27  LEU   A CA   1 
ATOM   203  C  C    . LEU   A 1 27  ? -24.245 1.626   -19.011 1   13.244 ? 27  LEU   A C    1 
ATOM   204  O  O    . LEU   A 1 27  ? -24.973 2.055   -18.12  1   14.653 ? 27  LEU   A O    1 
ATOM   205  C  CB   . LEU   A 1 27  ? -24.385 0.431   -21.291 1   14.013 ? 27  LEU   A CB   1 
ATOM   206  C  CG   . LEU   A 1 27  ? -25.414 1.181   -22.141 1   14.092 ? 27  LEU   A CG   1 
ATOM   207  C  CD1  . LEU   A 1 27  ? -25.51  2.649   -21.792 1   14.051 ? 27  LEU   A CD1  1 
ATOM   208  C  CD2  . LEU   A 1 27  ? -25.068 0.987   -23.597 1   15.273 ? 27  LEU   A CD2  1 
ATOM   209  N  N    . ASN   A 1 28  ? -23.081 2.205   -19.323 1   12.453 ? 28  ASN   A N    1 
ATOM   210  C  CA   . ASN   A 1 28  ? -22.579 3.365   -18.613 1   12.303 ? 28  ASN   A CA   1 
ATOM   211  C  C    . ASN   A 1 28  ? -22.938 4.665   -19.336 1   12.42  ? 28  ASN   A C    1 
ATOM   212  O  O    . ASN   A 1 28  ? -23.017 4.716   -20.563 1   13.408 ? 28  ASN   A O    1 
ATOM   213  C  CB   . ASN   A 1 28  ? -21.062 3.303   -18.468 1   12.159 ? 28  ASN   A CB   1 
ATOM   214  C  CG   . ASN   A 1 28  ? -20.594 2.003   -17.867 1   12.523 ? 28  ASN   A CG   1 
ATOM   215  O  OD1  . ASN   A 1 28  ? -20.664 1.812   -16.649 1   13.53  ? 28  ASN   A OD1  1 
ATOM   216  N  ND2  . ASN   A 1 28  ? -20.115 1.105   -18.712 1   13.152 ? 28  ASN   A ND2  1 
ATOM   217  N  N    . GLY   A 1 29  ? -23.154 5.716   -18.54  1   12.612 ? 29  GLY   A N    1 
ATOM   218  C  CA   . GLY   A 1 29  ? -23.297 7.067   -19.043 1   12.742 ? 29  GLY   A CA   1 
ATOM   219  C  C    . GLY   A 1 29  ? -22.34  8.034   -18.352 1   12.362 ? 29  GLY   A C    1 
ATOM   220  O  O    . GLY   A 1 29  ? -21.792 7.737   -17.284 1   12.908 ? 29  GLY   A O    1 
ATOM   221  N  N    . LEU   A 1 30  ? -22.173 9.196   -18.991 1   12.747 ? 30  LEU   A N    1 
ATOM   222  C  CA   . LEU   A 1 30  ? -21.329 10.265  -18.495 1   12.769 ? 30  LEU   A CA   1 
ATOM   223  C  C    . LEU   A 1 30  ? -22.218 11.452  -18.14  1   13.315 ? 30  LEU   A C    1 
ATOM   224  O  O    . LEU   A 1 30  ? -22.904 12.004  -19.005 1   13.31  ? 30  LEU   A O    1 
ATOM   225  C  CB   . LEU   A 1 30  ? -20.311 10.611  -19.583 1   12.899 ? 30  LEU   A CB   1 
ATOM   226  C  CG   . LEU   A 1 30  ? -19.291 11.69   -19.23  1   13.479 ? 30  LEU   A CG   1 
ATOM   227  C  CD1  . LEU   A 1 30  ? -18.298 11.153  -18.204 1   14.198 ? 30  LEU   A CD1  1 
ATOM   228  C  CD2  . LEU   A 1 30  ? -18.589 12.209  -20.481 1   13.921 ? 30  LEU   A CD2  1 
ATOM   229  N  N    . TRP   A 1 31  ? -22.209 11.82   -16.854 1   13.049 ? 31  TRP   A N    1 
ATOM   230  C  CA   . TRP   A 1 31  ? -23.083 12.84   -16.294 1   13.902 ? 31  TRP   A CA   1 
ATOM   231  C  C    . TRP   A 1 31  ? -22.297 14.135  -16.1   1   14.433 ? 31  TRP   A C    1 
ATOM   232  O  O    . TRP   A 1 31  ? -21.434 14.212  -15.232 1   14.457 ? 31  TRP   A O    1 
ATOM   233  C  CB   . TRP   A 1 31  ? -23.658 12.315  -14.973 1   14.549 ? 31  TRP   A CB   1 
ATOM   234  C  CG   . TRP   A 1 31  ? -24.608 13.232  -14.25  1   15.5   ? 31  TRP   A CG   1 
ATOM   235  C  CD1  . TRP   A 1 31  ? -25.419 14.199  -14.768 1   16.057 ? 31  TRP   A CD1  1 
ATOM   236  C  CD2  . TRP   A 1 31  ? -24.882 13.197  -12.834 1   16.547 ? 31  TRP   A CD2  1 
ATOM   237  N  NE1  . TRP   A 1 31  ? -26.161 14.778  -13.771 1   16.919 ? 31  TRP   A NE1  1 
ATOM   238  C  CE2  . TRP   A 1 31  ? -25.849 14.19   -12.574 1   16.906 ? 31  TRP   A CE2  1 
ATOM   239  C  CE3  . TRP   A 1 31  ? -24.376 12.446  -11.769 1   17.482 ? 31  TRP   A CE3  1 
ATOM   240  C  CZ2  . TRP   A 1 31  ? -26.336 14.433  -11.287 1   17.627 ? 31  TRP   A CZ2  1 
ATOM   241  C  CZ3  . TRP   A 1 31  ? -24.85  12.694  -10.499 1   18.698 ? 31  TRP   A CZ3  1 
ATOM   242  C  CH2  . TRP   A 1 31  ? -25.822 13.667  -10.266 1   18.658 ? 31  TRP   A CH2  1 
ATOM   243  N  N    . LEU   A 1 32  ? -22.592 15.138  -16.928 1   14.164 ? 32  LEU   A N    1 
ATOM   244  C  CA   . LEU   A 1 32  ? -21.914 16.428  -16.887 1   14.481 ? 32  LEU   A CA   1 
ATOM   245  C  C    . LEU   A 1 32  ? -22.987 17.504  -16.831 1   15.876 ? 32  LEU   A C    1 
ATOM   246  O  O    . LEU   A 1 32  ? -23.862 17.518  -17.681 1   16.67  ? 32  LEU   A O    1 
ATOM   247  C  CB   . LEU   A 1 32  ? -21.058 16.619  -18.134 1   15.024 ? 32  LEU   A CB   1 
ATOM   248  C  CG   . LEU   A 1 32  ? -19.939 15.604  -18.353 1   15.564 ? 32  LEU   A CG   1 
ATOM   249  C  CD1  . LEU   A 1 32  ? -19.377 15.754  -19.753 1   16.454 ? 32  LEU   A CD1  1 
ATOM   250  C  CD2  . LEU   A 1 32  ? -18.858 15.803  -17.303 1   16.292 ? 32  LEU   A CD2  1 
ATOM   251  N  N    . ASP   A 1 33  ? -22.915 18.401  -15.848 1   16.709 ? 33  ASP   A N    1 
ATOM   252  C  CA   . ASP   A 1 33  ? -23.995 19.357  -15.659 1   18.111 ? 33  ASP   A CA   1 
ATOM   253  C  C    . ASP   A 1 33  ? -25.293 18.555  -15.552 1   17.266 ? 33  ASP   A C    1 
ATOM   254  O  O    . ASP   A 1 33  ? -25.323 17.572  -14.831 1   17.98  ? 33  ASP   A O    1 
ATOM   255  C  CB   . ASP   A 1 33  ? -23.903 20.454  -16.71  1   20.476 ? 33  ASP   A CB   1 
ATOM   256  C  CG   . ASP   A 1 33  ? -22.582 21.215  -16.712 1   23.614 ? 33  ASP   A CG   1 
ATOM   257  O  OD1  . ASP   A 1 33  ? -22.133 21.604  -15.619 1   28.327 ? 33  ASP   A OD1  1 
ATOM   258  O  OD2  . ASP   A 1 33  ? -21.999 21.386  -17.803 1   27.943 ? 33  ASP   A OD2  1 
ATOM   259  N  N    . ASP   A 1 34  ? -26.341 18.93   -16.292 1   17.828 ? 34  ASP   A N    1 
ATOM   260  C  CA   . ASP   A 1 34  ? -27.626 18.246  -16.193 1   18.507 ? 34  ASP   A CA   1 
ATOM   261  C  C    . ASP   A 1 34  ? -27.882 17.334  -17.398 1   17.424 ? 34  ASP   A C    1 
ATOM   262  O  O    . ASP   A 1 34  ? -29.041 17.095  -17.739 1   18.669 ? 34  ASP   A O    1 
ATOM   263  C  CB   . ASP   A 1 34  ? -28.773 19.237  -16.048 1   20.613 ? 34  ASP   A CB   1 
ATOM   264  C  CG   . ASP   A 1 34  ? -28.911 20.244  -17.181 1   22.62  ? 34  ASP   A CG   1 
ATOM   265  O  OD1  . ASP   A 1 34  ? -27.991 20.327  -18.026 1   23.948 ? 34  ASP   A OD1  1 
ATOM   266  O  OD2  . ASP   A 1 34  ? -29.943 20.934  -17.222 1   27.398 ? 34  ASP   A OD2  1 
ATOM   267  N  N    . VAL   A 1 35  ? -26.816 16.821  -18.033 1   16.254 ? 35  VAL   A N    1 
ATOM   268  C  CA   . VAL   A 1 35  ? -26.933 15.938  -19.185 1   15.821 ? 35  VAL   A CA   1 
ATOM   269  C  C    . VAL   A 1 35  ? -26.163 14.648  -18.918 1   14.642 ? 35  VAL   A C    1 
ATOM   270  O  O    . VAL   A 1 35  ? -25.053 14.675  -18.393 1   15.165 ? 35  VAL   A O    1 
ATOM   271  C  CB   . VAL   A 1 35  ? -26.46  16.608  -20.492 1   17.241 ? 35  VAL   A CB   1 
ATOM   272  C  CG1  . VAL   A 1 35  ? -26.582 15.662  -21.682 1   17.93  ? 35  VAL   A CG1  1 
ATOM   273  C  CG2  . VAL   A 1 35  ? -27.224 17.907  -20.74  1   18.949 ? 35  VAL   A CG2  1 
ATOM   274  N  N    . VAL   A 1 36  ? -26.769 13.519  -19.304 1   14.167 ? 36  VAL   A N    1 
ATOM   275  C  CA   . VAL   A 1 36  ? -26.106 12.224  -19.324 1   14.341 ? 36  VAL   A CA   1 
ATOM   276  C  C    . VAL   A 1 36  ? -25.93  11.799  -20.776 1   14.101 ? 36  VAL   A C    1 
ATOM   277  O  O    . VAL   A 1 36  ? -26.904 11.71   -21.516 1   14.999 ? 36  VAL   A O    1 
ATOM   278  C  CB   . VAL   A 1 36  ? -26.878 11.161  -18.519 1   14.823 ? 36  VAL   A CB   1 
ATOM   279  C  CG1  . VAL   A 1 36  ? -26.254 9.775   -18.652 1   15.432 ? 36  VAL   A CG1  1 
ATOM   280  C  CG2  . VAL   A 1 36  ? -26.985 11.57   -17.052 1   15.286 ? 36  VAL   A CG2  1 
ATOM   281  N  N    . TYR   A 1 37  ? -24.68  11.503  -21.143 1   13.451 ? 37  TYR   A N    1 
ATOM   282  C  CA   . TYR   A 1 37  ? -24.315 11.057  -22.475 1   13.755 ? 37  TYR   A CA   1 
ATOM   283  C  C    . TYR   A 1 37  ? -24.089 9.554   -22.456 1   12.973 ? 37  TYR   A C    1 
ATOM   284  O  O    . TYR   A 1 37  ? -23.378 9.054   -21.586 1   13.448 ? 37  TYR   A O    1 
ATOM   285  C  CB   . TYR   A 1 37  ? -23.014 11.743  -22.905 1   13.945 ? 37  TYR   A CB   1 
ATOM   286  C  CG   . TYR   A 1 37  ? -23.067 13.262  -22.889 1   14.782 ? 37  TYR   A CG   1 
ATOM   287  C  CD1  . TYR   A 1 37  ? -22.914 13.982  -21.707 1   15.238 ? 37  TYR   A CD1  1 
ATOM   288  C  CD2  . TYR   A 1 37  ? -23.292 13.976  -24.059 1   15.742 ? 37  TYR   A CD2  1 
ATOM   289  C  CE1  . TYR   A 1 37  ? -22.993 15.365  -21.69  1   16.334 ? 37  TYR   A CE1  1 
ATOM   290  C  CE2  . TYR   A 1 37  ? -23.379 15.358  -24.049 1   16.517 ? 37  TYR   A CE2  1 
ATOM   291  C  CZ   . TYR   A 1 37  ? -23.247 16.055  -22.86  1   16.681 ? 37  TYR   A CZ   1 
ATOM   292  O  OH   . TYR   A 1 37  ? -23.342 17.418  -22.848 1   18.87  ? 37  TYR   A OH   1 
ATOM   293  N  N    . CYS   A 1 38  ? -24.621 8.835   -23.445 1   13.172 ? 38  CYS   A N    1 
ATOM   294  C  CA   . CYS   A 1 38  ? -24.355 7.413   -23.543 1   13.306 ? 38  CYS   A CA   1 
ATOM   295  C  C    . CYS   A 1 38  ? -24.513 6.962   -24.991 1   12.923 ? 38  CYS   A C    1 
ATOM   296  O  O    . CYS   A 1 38  ? -25.039 7.698   -25.829 1   13.578 ? 38  CYS   A O    1 
ATOM   297  C  CB   . CYS   A 1 38  ? -25.254 6.607   -22.604 1   13.95  ? 38  CYS   A CB   1 
ATOM   298  S  SG   . CYS   A 1 38  ? -26.994 6.522   -23.101 1   15.797 ? 38  CYS   A SG   1 
ATOM   299  N  N    . PRO   A 1 39  ? -24.069 5.74    -25.344 1   12.193 ? 39  PRO   A N    1 
ATOM   300  C  CA   . PRO   A 1 39  ? -24.272 5.241   -26.704 1   12.1   ? 39  PRO   A CA   1 
ATOM   301  C  C    . PRO   A 1 39  ? -25.761 5.101   -27.004 1   12.515 ? 39  PRO   A C    1 
ATOM   302  O  O    . PRO   A 1 39  ? -26.517 4.571   -26.187 1   12.887 ? 39  PRO   A O    1 
ATOM   303  C  CB   . PRO   A 1 39  ? -23.548 3.883   -26.698 1   12.491 ? 39  PRO   A CB   1 
ATOM   304  C  CG   . PRO   A 1 39  ? -22.549 4.005   -25.576 1   12.82  ? 39  PRO   A CG   1 
ATOM   305  C  CD   . PRO   A 1 39  ? -23.263 4.822   -24.522 1   12.626 ? 39  PRO   A CD   1 
ATOM   306  N  N    . ARG   A 1 40  ? -26.162 5.502   -28.21  1   12.707 ? 40  ARG   A N    1 
ATOM   307  C  CA   . ARG   A 1 40  ? -27.572 5.415   -28.556 1   12.94  ? 40  ARG   A CA   1 
ATOM   308  C  C    . ARG   A 1 40  ? -28.011 3.955   -28.676 1   13.221 ? 40  ARG   A C    1 
ATOM   309  O  O    . ARG   A 1 40  ? -29.208 3.691   -28.576 1   14.069 ? 40  ARG   A O    1 
ATOM   310  C  CB   . ARG   A 1 40  ? -27.942 6.202   -29.815 1   13.561 ? 40  ARG   A CB   1 
ATOM   311  C  CG   . ARG   A 1 40  ? -27.322 5.68    -31.098 1   13.943 ? 40  ARG   A CG   1 
ATOM   312  C  CD   . ARG   A 1 40  ? -27.835 6.462   -32.289 1   14.567 ? 40  ARG   A CD   1 
ATOM   313  N  NE   . ARG   A 1 40  ? -27.149 6.006   -33.497 1   15.056 ? 40  ARG   A NE   1 
ATOM   314  C  CZ   . ARG   A 1 40  ? -27.508 6.338   -34.728 1   15.853 ? 40  ARG   A CZ   1 
ATOM   315  N  NH1  . ARG   A 1 40  ? -28.493 7.219   -34.919 1   16.351 ? 40  ARG   A NH1  1 
ATOM   316  N  NH2  . ARG   A 1 40  ? -26.88  5.785   -35.75  1   15.869 ? 40  ARG   A NH2  1 
ATOM   317  N  N    . HIS   A 1 41  ? -27.085 3.002   -28.853 1   13.144 ? 41  HIS   A N    1 
ATOM   318  C  CA   . HIS   A 1 41  ? -27.478 1.608   -28.953 1   13.666 ? 41  HIS   A CA   1 
ATOM   319  C  C    . HIS   A 1 41  ? -28.098 1.079   -27.661 1   13.966 ? 41  HIS   A C    1 
ATOM   320  O  O    . HIS   A 1 41  ? -28.644 -0.018  -27.665 1   14.72  ? 41  HIS   A O    1 
ATOM   321  C  CB   . HIS   A 1 41  ? -26.371 0.72    -29.527 1   13.696 ? 41  HIS   A CB   1 
ATOM   322  C  CG   . HIS   A 1 41  ? -25.191 0.438   -28.657 1   13.917 ? 41  HIS   A CG   1 
ATOM   323  N  ND1  . HIS   A 1 41  ? -25.27  -0.288  -27.494 1   14.603 ? 41  HIS   A ND1  1 
ATOM   324  C  CD2  . HIS   A 1 41  ? -23.891 0.731   -28.834 1   14.317 ? 41  HIS   A CD2  1 
ATOM   325  C  CE1  . HIS   A 1 41  ? -24.044 -0.435  -26.999 1   14.625 ? 41  HIS   A CE1  1 
ATOM   326  N  NE2  . HIS   A 1 41  ? -23.195 0.179   -27.799 1   15.101 ? 41  HIS   A NE2  1 
ATOM   327  N  N    . VAL   A 1 42  ? -28.075 1.852   -26.57  1   14.091 ? 42  VAL   A N    1 
ATOM   328  C  CA   . VAL   A 1 42  ? -28.818 1.469   -25.375 1   14.658 ? 42  VAL   A CA   1 
ATOM   329  C  C    . VAL   A 1 42  ? -30.295 1.19    -25.685 1   14.759 ? 42  VAL   A C    1 
ATOM   330  O  O    . VAL   A 1 42  ? -30.917 0.401   -24.984 1   15.91  ? 42  VAL   A O    1 
ATOM   331  C  CB   . VAL   A 1 42  ? -28.659 2.531   -24.269 1   15.046 ? 42  VAL   A CB   1 
ATOM   332  C  CG1  . VAL   A 1 42  ? -29.43  3.817   -24.558 1   15.229 ? 42  VAL   A CG1  1 
ATOM   333  C  CG2  . VAL   A 1 42  ? -29.05  1.964   -22.905 1   15.894 ? 42  VAL   A CG2  1 
ATOM   334  N  N    . ILE   A 1 43  ? -30.867 1.821   -26.72  1   14.668 ? 43  ILE   A N    1 
ATOM   335  C  CA   . ILE   A 1 43  ? -32.291 1.647   -27.027 1   15.643 ? 43  ILE   A CA   1 
ATOM   336  C  C    . ILE   A 1 43  ? -32.559 0.418   -27.896 1   17.316 ? 43  ILE   A C    1 
ATOM   337  O  O    . ILE   A 1 43  ? -33.712 0.159   -28.24  1   20.002 ? 43  ILE   A O    1 
ATOM   338  C  CB   . ILE   A 1 43  ? -32.914 2.912   -27.654 1   15.207 ? 43  ILE   A CB   1 
ATOM   339  C  CG1  . ILE   A 1 43  ? -32.448 3.179   -29.092 1   15.601 ? 43  ILE   A CG1  1 
ATOM   340  C  CG2  . ILE   A 1 43  ? -32.689 4.12    -26.742 1   15.801 ? 43  ILE   A CG2  1 
ATOM   341  C  CD1  . ILE   A 1 43  ? -33.065 4.417   -29.717 1   15.834 ? 43  ILE   A CD1  1 
ATOM   342  N  N    . CYS   A 1 44  ? -31.519 -0.335  -28.263 1   17.721 ? 44  CYS   A N    1 
ATOM   343  C  CA   . CYS   A 1 44  ? -31.677 -1.513  -29.104 1   19.819 ? 44  CYS   A CA   1 
ATOM   344  C  C    . CYS   A 1 44  ? -31.757 -2.801  -28.3   1   24.248 ? 44  CYS   A C    1 
ATOM   345  O  O    . CYS   A 1 44  ? -30.968 -3.024  -27.387 1   26.6   ? 44  CYS   A O    1 
ATOM   346  C  CB   . CYS   A 1 44  ? -30.475 -1.709  -30.007 1   20.083 ? 44  CYS   A CB   1 
ATOM   347  S  SG   . CYS   A 1 44  ? -30.301 -0.334  -31.156 1   21.185 ? 44  CYS   A SG   1 
ATOM   348  N  N    . THR   A 1 45  ? -32.675 -3.671  -28.731 1   26.786 ? 45  THR   A N    1 
ATOM   349  C  CA   . THR   A 1 45  ? -32.686 -5.073  -28.339 1   30.204 ? 45  THR   A CA   1 
ATOM   350  C  C    . THR   A 1 45  ? -31.721 -5.833  -29.245 1   29.45  ? 45  THR   A C    1 
ATOM   351  O  O    . THR   A 1 45  ? -31.265 -5.303  -30.25  1   28.928 ? 45  THR   A O    1 
ATOM   352  C  CB   . THR   A 1 45  ? -34.099 -5.655  -28.45  1   32.233 ? 45  THR   A CB   1 
ATOM   353  O  OG1  . THR   A 1 45  ? -34.401 -5.682  -29.844 1   35.007 ? 45  THR   A OG1  1 
ATOM   354  C  CG2  . THR   A 1 45  ? -35.141 -4.847  -27.698 1   33.687 ? 45  THR   A CG2  1 
ATOM   355  N  N    . SER   A 1 46  ? -31.449 -7.097  -28.91  1   31.156 ? 46  SER   A N    1 
ATOM   356  C  CA   . SER   A 1 46  ? -30.638 -7.949  -29.767 1   32.691 ? 46  SER   A CA   1 
ATOM   357  C  C    . SER   A 1 46  ? -31.253 -8.058  -31.165 1   34.874 ? 46  SER   A C    1 
ATOM   358  O  O    . SER   A 1 46  ? -30.528 -8.103  -32.153 1   33.701 ? 46  SER   A O    1 
ATOM   359  C  CB   . SER   A 1 46  ? -30.402 -9.306  -29.141 1   34.185 ? 46  SER   A CB   1 
ATOM   360  O  OG   . SER   A 1 46  ? -31.611 -9.979  -28.815 1   36.853 ? 46  SER   A OG   1 
ATOM   361  N  N    . GLU   A 1 47  ? -32.588 -8.072  -31.251 1   36.684 ? 47  GLU   A N    1 
ATOM   362  C  CA   . GLU   A 1 47  ? -33.265 -8.16   -32.539 1   40.193 ? 47  GLU   A CA   1 
ATOM   363  C  C    . GLU   A 1 47  ? -33.036 -6.875  -33.343 1   37.862 ? 47  GLU   A C    1 
ATOM   364  O  O    . GLU   A 1 47  ? -32.896 -6.924  -34.557 1   44.671 ? 47  GLU   A O    1 
ATOM   365  C  CB   . GLU   A 1 47  ? -34.763 -8.456  -32.396 1   44.019 ? 47  GLU   A CB   1 
ATOM   366  C  CG   . GLU   A 1 47  ? -35.157 -9.321  -31.197 1   46.905 ? 47  GLU   A CG   1 
ATOM   367  C  CD   . GLU   A 1 47  ? -34.533 -10.703 -31.085 1   50.401 ? 47  GLU   A CD   1 
ATOM   368  O  OE1  . GLU   A 1 47  ? -34.053 -11.24  -32.106 1   53.039 ? 47  GLU   A OE1  1 
ATOM   369  O  OE2  . GLU   A 1 47  ? -34.513 -11.234 -29.951 1   54.818 ? 47  GLU   A OE2  1 
ATOM   370  N  N    . ASP   A 1 48  ? -32.944 -5.729  -32.662 1   32.129 ? 48  ASP   A N    1 
ATOM   371  C  CA   . ASP   A 1 48  ? -32.815 -4.437  -33.315 1   30.604 ? 48  ASP   A CA   1 
ATOM   372  C  C    . ASP   A 1 48  ? -31.418 -4.233  -33.908 1   29.011 ? 48  ASP   A C    1 
ATOM   373  O  O    . ASP   A 1 48  ? -31.239 -3.331  -34.714 1   29.228 ? 48  ASP   A O    1 
ATOM   374  C  CB   . ASP   A 1 48  ? -33.14  -3.289  -32.361 1   31.222 ? 48  ASP   A CB   1 
ATOM   375  C  CG   . ASP   A 1 48  ? -34.56  -3.257  -31.81  1   32.829 ? 48  ASP   A CG   1 
ATOM   376  O  OD1  . ASP   A 1 48  ? -35.502 -3.574  -32.561 1   35.868 ? 48  ASP   A OD1  1 
ATOM   377  O  OD2  . ASP   A 1 48  ? -34.73  -2.897  -30.633 1   35.415 ? 48  ASP   A OD2  1 
ATOM   378  N  N    . MET   A 1 49  ? -30.411 -5.036  -33.535 1   28.957 ? 49  MET   A N    1 
ATOM   379  C  CA   . MET   A 1 49  ? -29.025 -4.586  -33.632 1   26.898 ? 49  MET   A CA   1 
ATOM   380  C  C    . MET   A 1 49  ? -28.423 -4.697  -35.045 1   25.892 ? 49  MET   A C    1 
ATOM   381  O  O    . MET   A 1 49  ? -27.43  -4.036  -35.294 1   24.138 ? 49  MET   A O    1 
ATOM   382  C  CB   . MET   A 1 49  ? -28.167 -5.282  -32.564 1   26.601 ? 49  MET   A CB   1 
ATOM   383  C  CG   . MET   A 1 49  ? -26.912 -4.52   -32.122 1   26.335 ? 49  MET   A CG   1 
ATOM   384  S  SD   . MET   A 1 49  ? -27.153 -2.972  -31.22  1   24.94  ? 49  MET   A SD   1 
ATOM   385  C  CE   . MET   A 1 49  ? -26.996 -1.785  -32.562 1   25.694 ? 49  MET   A CE   1 
ATOM   386  N  N    . LEU   A 1 50  ? -28.983 -5.474  -35.987 1   26.41  ? 50  LEU   A N    1 
ATOM   387  C  CA   . LEU   A 1 50  ? -28.454 -5.572  -37.352 1   26.201 ? 50  LEU   A CA   1 
ATOM   388  C  C    . LEU   A 1 50  ? -28.732 -4.326  -38.202 1   24.216 ? 50  LEU   A C    1 
ATOM   389  O  O    . LEU   A 1 50  ? -27.883 -3.898  -38.982 1   25.359 ? 50  LEU   A O    1 
ATOM   390  C  CB   . LEU   A 1 50  ? -28.996 -6.787  -38.105 1   29.131 ? 50  LEU   A CB   1 
ATOM   391  C  CG   . LEU   A 1 50  ? -28.231 -8.106  -38.001 1   31.73  ? 50  LEU   A CG   1 
ATOM   392  C  CD1  . LEU   A 1 50  ? -29.001 -9.204  -38.717 1   32.046 ? 50  LEU   A CD1  1 
ATOM   393  C  CD2  . LEU   A 1 50  ? -26.851 -7.979  -38.599 1   32.493 ? 50  LEU   A CD2  1 
ATOM   394  N  N    . ASN   A 1 51  ? -29.979 -3.835  -38.183 1   23.802 ? 51  ASN   A N    1 
ATOM   395  C  CA   . ASN   A 1 51  ? -30.383 -2.713  -39.023 1   22.914 ? 51  ASN   A CA   1 
ATOM   396  C  C    . ASN   A 1 51  ? -31.319 -1.817  -38.217 1   22.758 ? 51  ASN   A C    1 
ATOM   397  O  O    . ASN   A 1 51  ? -32.45  -1.543  -38.62  1   26.683 ? 51  ASN   A O    1 
ATOM   398  C  CB   . ASN   A 1 51  ? -31.042 -3.157  -40.328 1   23.144 ? 51  ASN   A CB   1 
ATOM   399  C  CG   . ASN   A 1 51  ? -30.062 -3.741  -41.322 1   23.494 ? 51  ASN   A CG   1 
ATOM   400  O  OD1  . ASN   A 1 51  ? -29.275 -3.011  -41.943 1   23.328 ? 51  ASN   A OD1  1 
ATOM   401  N  ND2  . ASN   A 1 51  ? -30.126 -5.048  -41.523 1   22.884 ? 51  ASN   A ND2  1 
ATOM   402  N  N    . PRO   A 1 52  ? -30.864 -1.316  -37.048 1   21.114 ? 52  PRO   A N    1 
ATOM   403  C  CA   . PRO   A 1 52  ? -31.695 -0.469  -36.201 1   21.17  ? 52  PRO   A CA   1 
ATOM   404  C  C    . PRO   A 1 52  ? -32.104 0.791   -36.952 1   20.296 ? 52  PRO   A C    1 
ATOM   405  O  O    . PRO   A 1 52  ? -31.298 1.414   -37.644 1   22.335 ? 52  PRO   A O    1 
ATOM   406  C  CB   . PRO   A 1 52  ? -30.779 -0.128  -35.019 1   21.975 ? 52  PRO   A CB   1 
ATOM   407  C  CG   . PRO   A 1 52  ? -29.388 -0.211  -35.606 1   21.457 ? 52  PRO   A CG   1 
ATOM   408  C  CD   . PRO   A 1 52  ? -29.478 -1.39   -36.562 1   21.356 ? 52  PRO   A CD   1 
ATOM   409  N  N    . ASN   A 1 53  ? -33.366 1.168   -36.784 1   19.264 ? 53  ASN   A N    1 
ATOM   410  C  CA   . ASN   A 1 53  ? -33.839 2.461   -37.212 1   18.94  ? 53  ASN   A CA   1 
ATOM   411  C  C    . ASN   A 1 53  ? -33.963 3.323   -35.961 1   17.154 ? 53  ASN   A C    1 
ATOM   412  O  O    . ASN   A 1 53  ? -34.974 3.284   -35.261 1   17.024 ? 53  ASN   A O    1 
ATOM   413  C  CB   . ASN   A 1 53  ? -35.164 2.307   -37.943 1   19.907 ? 53  ASN   A CB   1 
ATOM   414  C  CG   . ASN   A 1 53  ? -35.631 3.598   -38.556 1   21.96  ? 53  ASN   A CG   1 
ATOM   415  O  OD1  . ASN   A 1 53  ? -35.416 4.682   -37.995 1   20.771 ? 53  ASN   A OD1  1 
ATOM   416  N  ND2  . ASN   A 1 53  ? -36.241 3.483   -39.729 1   25.005 ? 53  ASN   A ND2  1 
ATOM   417  N  N    . TYR   A 1 54  ? -32.897 4.066   -35.65  1   17.06  ? 54  TYR   A N    1 
ATOM   418  C  CA   . TYR   A 1 54  ? -32.794 4.707   -34.351 1   16.229 ? 54  TYR   A CA   1 
ATOM   419  C  C    . TYR   A 1 54  ? -33.893 5.752   -34.158 1   16.091 ? 54  TYR   A C    1 
ATOM   420  O  O    . TYR   A 1 54  ? -34.423 5.875   -33.06  1   16.382 ? 54  TYR   A O    1 
ATOM   421  C  CB   . TYR   A 1 54  ? -31.411 5.312   -34.147 1   16.115 ? 54  TYR   A CB   1 
ATOM   422  C  CG   . TYR   A 1 54  ? -30.358 4.273   -33.81  1   15.447 ? 54  TYR   A CG   1 
ATOM   423  C  CD1  . TYR   A 1 54  ? -30.262 3.766   -32.523 1   15.498 ? 54  TYR   A CD1  1 
ATOM   424  C  CD2  . TYR   A 1 54  ? -29.462 3.81    -34.769 1   15.255 ? 54  TYR   A CD2  1 
ATOM   425  C  CE1  . TYR   A 1 54  ? -29.291 2.833   -32.198 1   15.472 ? 54  TYR   A CE1  1 
ATOM   426  C  CE2  . TYR   A 1 54  ? -28.501 2.872   -34.456 1   15.495 ? 54  TYR   A CE2  1 
ATOM   427  C  CZ   . TYR   A 1 54  ? -28.402 2.394   -33.163 1   15.411 ? 54  TYR   A CZ   1 
ATOM   428  O  OH   . TYR   A 1 54  ? -27.449 1.481   -32.816 1   16.826 ? 54  TYR   A OH   1 
ATOM   429  N  N    . GLU   A 1 55  ? -34.253 6.487   -35.216 1   16.275 ? 55  GLU   A N    1 
ATOM   430  C  CA   . GLU   A 1 55  ? -35.326 7.472   -35.107 1   17.014 ? 55  GLU   A CA   1 
ATOM   431  C  C    . GLU   A 1 55  ? -36.647 6.803   -34.716 1   16.074 ? 55  GLU   A C    1 
ATOM   432  O  O    . GLU   A 1 55  ? -37.391 7.296   -33.862 1   15.916 ? 55  GLU   A O    1 
ATOM   433  C  CB   . GLU   A 1 55  ? -35.48  8.221   -36.427 1   18.762 ? 55  GLU   A CB   1 
ATOM   434  C  CG   . GLU   A 1 55  ? -34.288 9.109   -36.752 1   21.621 ? 55  GLU   A CG   1 
ATOM   435  C  CD   . GLU   A 1 55  ? -33.031 8.439   -37.307 1   25.069 ? 55  GLU   A CD   1 
ATOM   436  O  OE1  . GLU   A 1 55  ? -32.934 7.207   -37.619 1   25.904 ? 55  GLU   A OE1  1 
ATOM   437  O  OE2  . GLU   A 1 55  ? -32.084 9.242   -37.423 1   29.809 ? 55  GLU   A OE2  1 
ATOM   438  N  N    . ASP   A 1 56  ? -36.927 5.661   -35.345 1   15.406 ? 56  ASP   A N    1 
ATOM   439  C  CA   . ASP   A 1 56  ? -38.155 4.92    -35.112 1   15.585 ? 56  ASP   A CA   1 
ATOM   440  C  C    . ASP   A 1 56  ? -38.137 4.289   -33.72  1   15.541 ? 56  ASP   A C    1 
ATOM   441  O  O    . ASP   A 1 56  ? -39.161 4.222   -33.053 1   16.746 ? 56  ASP   A O    1 
ATOM   442  C  CB   . ASP   A 1 56  ? -38.383 3.871   -36.185 1   16.154 ? 56  ASP   A CB   1 
ATOM   443  C  CG   . ASP   A 1 56  ? -39.776 3.267   -36.163 1   16.713 ? 56  ASP   A CG   1 
ATOM   444  O  OD1  . ASP   A 1 56  ? -40.707 3.942   -36.627 1   18.046 ? 56  ASP   A OD1  1 
ATOM   445  O  OD2  . ASP   A 1 56  ? -39.914 2.151   -35.65  1   19.905 ? 56  ASP   A OD2  1 
ATOM   446  N  N    . LEU   A 1 57  ? -36.971 3.798   -33.278 1   15.088 ? 57  LEU   A N    1 
ATOM   447  C  CA   . LEU   A 1 57  ? -36.872 3.203   -31.951 1   15.484 ? 57  LEU   A CA   1 
ATOM   448  C  C    . LEU   A 1 57  ? -37.05  4.27    -30.867 1   14.673 ? 57  LEU   A C    1 
ATOM   449  O  O    . LEU   A 1 57  ? -37.714 4.031   -29.857 1   15.751 ? 57  LEU   A O    1 
ATOM   450  C  CB   . LEU   A 1 57  ? -35.541 2.475   -31.78  1   15.897 ? 57  LEU   A CB   1 
ATOM   451  C  CG   . LEU   A 1 57  ? -35.33  1.224   -32.636 1   17.897 ? 57  LEU   A CG   1 
ATOM   452  C  CD1  . LEU   A 1 57  ? -33.889 0.769   -32.571 1   19.117 ? 57  LEU   A CD1  1 
ATOM   453  C  CD2  . LEU   A 1 57  ? -36.255 0.098   -32.2   1   19.628 ? 57  LEU   A CD2  1 
ATOM   454  N  N    . LEU   A 1 58  ? -36.468 5.449   -31.089 1   14.546 ? 58  LEU   A N    1 
ATOM   455  C  CA   . LEU   A 1 58  ? -36.427 6.482   -30.068 1   14.656 ? 58  LEU   A CA   1 
ATOM   456  C  C    . LEU   A 1 58  ? -37.796 7.151   -29.887 1   14.78  ? 58  LEU   A C    1 
ATOM   457  O  O    . LEU   A 1 58  ? -38.163 7.507   -28.763 1   15.301 ? 58  LEU   A O    1 
ATOM   458  C  CB   . LEU   A 1 58  ? -35.342 7.516   -30.362 1   15.606 ? 58  LEU   A CB   1 
ATOM   459  C  CG   . LEU   A 1 58  ? -35.093 8.554   -29.265 1   16.099 ? 58  LEU   A CG   1 
ATOM   460  C  CD1  . LEU   A 1 58  ? -34.699 7.898   -27.946 1   16.026 ? 58  LEU   A CD1  1 
ATOM   461  C  CD2  . LEU   A 1 58  ? -33.995 9.502   -29.725 1   17.594 ? 58  LEU   A CD2  1 
ATOM   462  N  N    A ILE   A 1 59  ? -38.549 7.328   -30.986 0.5 14.702 ? 59  ILE   A N    1 
ATOM   463  N  N    B ILE   A 1 59  ? -38.552 7.333   -30.977 0.5 14.642 ? 59  ILE   A N    1 
ATOM   464  C  CA   A ILE   A 1 59  ? -39.824 8.033   -30.918 0.5 14.717 ? 59  ILE   A CA   1 
ATOM   465  C  CA   B ILE   A 1 59  ? -39.803 8.071   -30.863 0.5 14.579 ? 59  ILE   A CA   1 
ATOM   466  C  C    A ILE   A 1 59  ? -40.791 7.29    -29.992 0.5 14.555 ? 59  ILE   A C    1 
ATOM   467  C  C    B ILE   A 1 59  ? -40.8   7.291   -29.997 0.5 14.45  ? 59  ILE   A C    1 
ATOM   468  O  O    A ILE   A 1 59  ? -41.711 7.894   -29.434 0.5 15.501 ? 59  ILE   A O    1 
ATOM   469  O  O    B ILE   A 1 59  ? -41.736 7.878   -29.452 0.5 15.261 ? 59  ILE   A O    1 
ATOM   470  C  CB   A ILE   A 1 59  ? -40.425 8.224   -32.324 0.5 15.097 ? 59  ILE   A CB   1 
ATOM   471  C  CB   B ILE   A 1 59  ? -40.354 8.432   -32.254 0.5 14.904 ? 59  ILE   A CB   1 
ATOM   472  C  CG1  A ILE   A 1 59  ? -41.501 9.321   -32.351 0.5 15.745 ? 59  ILE   A CG1  1 
ATOM   473  C  CG1  B ILE   A 1 59  ? -41.39  9.558   -32.19  0.5 15.451 ? 59  ILE   A CG1  1 
ATOM   474  C  CG2  A ILE   A 1 59  ? -40.951 6.898   -32.871 0.5 15.094 ? 59  ILE   A CG2  1 
ATOM   475  C  CG2  B ILE   A 1 59  ? -40.891 7.2     -32.976 0.5 14.761 ? 59  ILE   A CG2  1 
ATOM   476  C  CD1  A ILE   A 1 59  ? -40.981 10.716  -32.045 0.5 16.14  ? 59  ILE   A CD1  1 
ATOM   477  C  CD1  B ILE   A 1 59  ? -41.664 10.2    -33.538 0.5 15.934 ? 59  ILE   A CD1  1 
ATOM   478  N  N    . ARG   A 1 60  ? -40.571 5.98    -29.839 1   14.496 ? 60  ARG   A N    1 
ATOM   479  C  CA   . ARG   A 1 60  ? -41.428 5.102   -29.056 1   15.016 ? 60  ARG   A CA   1 
ATOM   480  C  C    . ARG   A 1 60  ? -41.099 5.146   -27.566 1   15.514 ? 60  ARG   A C    1 
ATOM   481  O  O    . ARG   A 1 60  ? -41.785 4.495   -26.774 1   16.211 ? 60  ARG   A O    1 
ATOM   482  C  CB   . ARG   A 1 60  ? -41.268 3.659   -29.544 1   14.614 ? 60  ARG   A CB   1 
ATOM   483  C  CG   . ARG   A 1 60  ? -41.631 3.506   -31.01  1   15.088 ? 60  ARG   A CG   1 
ATOM   484  C  CD   . ARG   A 1 60  ? -41.241 2.143   -31.509 1   15.593 ? 60  ARG   A CD   1 
ATOM   485  N  NE   . ARG   A 1 60  ? -41.465 2.044   -32.953 1   15.634 ? 60  ARG   A NE   1 
ATOM   486  C  CZ   . ARG   A 1 60  ? -42.55  1.574   -33.552 1   15.668 ? 60  ARG   A CZ   1 
ATOM   487  N  NH1  . ARG   A 1 60  ? -43.578 1.171   -32.827 1   15.72  ? 60  ARG   A NH1  1 
ATOM   488  N  NH2  . ARG   A 1 60  ? -42.577 1.499   -34.877 1   16.483 ? 60  ARG   A NH2  1 
ATOM   489  N  N    . LYS   A 1 61  ? -40.052 5.894   -27.192 1   16.156 ? 61  LYS   A N    1 
ATOM   490  C  CA   . LYS   A 1 61  ? -39.613 5.975   -25.81  1   16.581 ? 61  LYS   A CA   1 
ATOM   491  C  C    . LYS   A 1 61  ? -40.123 7.265   -25.175 1   17.678 ? 61  LYS   A C    1 
ATOM   492  O  O    . LYS   A 1 61  ? -40.148 8.32    -25.805 1   18.881 ? 61  LYS   A O    1 
ATOM   493  C  CB   . LYS   A 1 61  ? -38.083 5.971   -25.724 1   17.286 ? 61  LYS   A CB   1 
ATOM   494  C  CG   . LYS   A 1 61  ? -37.392 4.739   -26.274 1   19.4   ? 61  LYS   A CG   1 
ATOM   495  C  CD   . LYS   A 1 61  ? -37.736 3.443   -25.559 1   21.734 ? 61  LYS   A CD   1 
ATOM   496  C  CE   . LYS   A 1 61  ? -36.963 2.313   -26.156 1   23.509 ? 61  LYS   A CE   1 
ATOM   497  N  NZ   . LYS   A 1 61  ? -37.361 1.036   -25.565 1   27.531 ? 61  LYS   A NZ   1 
ATOM   498  N  N    . SER   A 1 62  ? -40.5   7.156   -23.898 1   18.424 ? 62  SER   A N    1 
ATOM   499  C  CA   . SER   A 1 62  ? -40.743 8.307   -23.047 1   19.184 ? 62  SER   A CA   1 
ATOM   500  C  C    . SER   A 1 62  ? -39.504 8.556   -22.186 1   19.009 ? 62  SER   A C    1 
ATOM   501  O  O    . SER   A 1 62  ? -38.633 7.69    -22.062 1   19.552 ? 62  SER   A O    1 
ATOM   502  C  CB   . SER   A 1 62  ? -41.946 8.087   -22.188 1   21.47  ? 62  SER   A CB   1 
ATOM   503  O  OG   . SER   A 1 62  ? -41.681 7.046   -21.263 1   24.003 ? 62  SER   A OG   1 
ATOM   504  N  N    . ASN   A 1 63  ? -39.459 9.724   -21.54  1   18.414 ? 63  ASN   A N    1 
ATOM   505  C  CA   . ASN   A 1 63  ? -38.4   10.025  -20.594 1   18.219 ? 63  ASN   A CA   1 
ATOM   506  C  C    . ASN   A 1 63  ? -38.303 8.939   -19.521 1   18.271 ? 63  ASN   A C    1 
ATOM   507  O  O    . ASN   A 1 63  ? -37.206 8.558   -19.105 1   18.388 ? 63  ASN   A O    1 
ATOM   508  C  CB   . ASN   A 1 63  ? -38.597 11.382  -19.941 1   19.349 ? 63  ASN   A CB   1 
ATOM   509  C  CG   . ASN   A 1 63  ? -38.395 12.539  -20.89  1   21.002 ? 63  ASN   A CG   1 
ATOM   510  O  OD1  . ASN   A 1 63  ? -37.517 12.495  -21.765 1   23.417 ? 63  ASN   A OD1  1 
ATOM   511  N  ND2  . ASN   A 1 63  ? -39.183 13.592  -20.718 1   21.401 ? 63  ASN   A ND2  1 
ATOM   512  N  N    . HIS   A 1 64  ? -39.457 8.449   -19.052 1   18.497 ? 64  HIS   A N    1 
ATOM   513  C  CA   . HIS   A 1 64  ? -39.489 7.522   -17.928 1   19.189 ? 64  HIS   A CA   1 
ATOM   514  C  C    . HIS   A 1 64  ? -39.104 6.097   -18.339 1   19.927 ? 64  HIS   A C    1 
ATOM   515  O  O    . HIS   A 1 64  ? -38.922 5.238   -17.472 1   22.538 ? 64  HIS   A O    1 
ATOM   516  C  CB   . HIS   A 1 64  ? -40.809 7.625   -17.159 1   20.196 ? 64  HIS   A CB   1 
ATOM   517  C  CG   . HIS   A 1 64  ? -42.034 7.349   -17.951 1   21.74  ? 64  HIS   A CG   1 
ATOM   518  N  ND1  . HIS   A 1 64  ? -42.721 8.322   -18.646 1   23.282 ? 64  HIS   A ND1  1 
ATOM   519  C  CD2  . HIS   A 1 64  ? -42.718 6.219   -18.117 1   23.647 ? 64  HIS   A CD2  1 
ATOM   520  C  CE1  . HIS   A 1 64  ? -43.787 7.774   -19.218 1   24.222 ? 64  HIS   A CE1  1 
ATOM   521  N  NE2  . HIS   A 1 64  ? -43.791 6.491   -18.923 1   24.432 ? 64  HIS   A NE2  1 
ATOM   522  N  N    . ASN   A 1 65  ? -38.877 5.852   -19.637 1   18.87  ? 65  ASN   A N    1 
ATOM   523  C  CA   . ASN   A 1 65  ? -38.31  4.589   -20.097 1   19.455 ? 65  ASN   A CA   1 
ATOM   524  C  C    . ASN   A 1 65  ? -36.795 4.515   -19.863 1   19.299 ? 65  ASN   A C    1 
ATOM   525  O  O    . ASN   A 1 65  ? -36.193 3.458   -20.062 1   21.508 ? 65  ASN   A O    1 
ATOM   526  C  CB   . ASN   A 1 65  ? -38.576 4.336   -21.577 1   20.442 ? 65  ASN   A CB   1 
ATOM   527  C  CG   . ASN   A 1 65  ? -40.024 4.04    -21.882 1   21.697 ? 65  ASN   A CG   1 
ATOM   528  O  OD1  . ASN   A 1 65  ? -40.555 4.523   -22.889 1   22.366 ? 65  ASN   A OD1  1 
ATOM   529  N  ND2  . ASN   A 1 65  ? -40.683 3.249   -21.044 1   24.165 ? 65  ASN   A ND2  1 
ATOM   530  N  N    . PHE   A 1 66  ? -36.17  5.631   -19.475 1   18.17  ? 66  PHE   A N    1 
ATOM   531  C  CA   . PHE   A 1 66  ? -34.747 5.657   -19.175 1   18.517 ? 66  PHE   A CA   1 
ATOM   532  C  C    . PHE   A 1 66  ? -34.547 5.762   -17.671 1   19.17  ? 66  PHE   A C    1 
ATOM   533  O  O    . PHE   A 1 66  ? -35.047 6.701   -17.055 1   21.571 ? 66  PHE   A O    1 
ATOM   534  C  CB   . PHE   A 1 66  ? -34.078 6.86    -19.839 1   18.411 ? 66  PHE   A CB   1 
ATOM   535  C  CG   . PHE   A 1 66  ? -34.143 6.788   -21.35  1   18.245 ? 66  PHE   A CG   1 
ATOM   536  C  CD1  . PHE   A 1 66  ? -33.226 6.014   -22.049 1   18.541 ? 66  PHE   A CD1  1 
ATOM   537  C  CD2  . PHE   A 1 66  ? -35.13  7.461   -22.061 1   18.252 ? 66  PHE   A CD2  1 
ATOM   538  C  CE1  . PHE   A 1 66  ? -33.296 5.911   -23.425 1   18.69  ? 66  PHE   A CE1  1 
ATOM   539  C  CE2  . PHE   A 1 66  ? -35.184 7.374   -23.439 1   18.537 ? 66  PHE   A CE2  1 
ATOM   540  C  CZ   . PHE   A 1 66  ? -34.268 6.596   -24.118 1   18.591 ? 66  PHE   A CZ   1 
ATOM   541  N  N    . LEU   A 1 67  ? -33.82  4.793   -17.106 1   19.376 ? 67  LEU   A N    1 
ATOM   542  C  CA   . LEU   A 1 67  ? -33.457 4.835   -15.7   1   20.201 ? 67  LEU   A CA   1 
ATOM   543  C  C    . LEU   A 1 67  ? -31.981 5.19    -15.591 1   18.887 ? 67  LEU   A C    1 
ATOM   544  O  O    . LEU   A 1 67  ? -31.146 4.548   -16.218 1   21.076 ? 67  LEU   A O    1 
ATOM   545  C  CB   . LEU   A 1 67  ? -33.74  3.487   -15.048 1   23.491 ? 67  LEU   A CB   1 
ATOM   546  C  CG   . LEU   A 1 67  ? -35.193 3.014   -15.097 1   27.859 ? 67  LEU   A CG   1 
ATOM   547  C  CD1  . LEU   A 1 67  ? -35.27  1.689   -14.35  1   29.582 ? 67  LEU   A CD1  1 
ATOM   548  C  CD2  . LEU   A 1 67  ? -36.185 4.01    -14.517 1   30.558 ? 67  LEU   A CD2  1 
ATOM   549  N  N    . VAL   A 1 68  ? -31.686 6.226   -14.809 1   18.408 ? 68  VAL   A N    1 
ATOM   550  C  CA   . VAL   A 1 68  ? -30.325 6.677   -14.601 1   17.702 ? 68  VAL   A CA   1 
ATOM   551  C  C    . VAL   A 1 68  ? -30.042 6.619   -13.108 1   17.509 ? 68  VAL   A C    1 
ATOM   552  O  O    . VAL   A 1 68  ? -30.784 7.188   -12.319 1   19.195 ? 68  VAL   A O    1 
ATOM   553  C  CB   . VAL   A 1 68  ? -30.104 8.093   -15.145 1   19.476 ? 68  VAL   A CB   1 
ATOM   554  C  CG1  . VAL   A 1 68  ? -28.669 8.545   -14.901 1   19.921 ? 68  VAL   A CG1  1 
ATOM   555  C  CG2  . VAL   A 1 68  ? -30.463 8.188   -16.622 1   20.204 ? 68  VAL   A CG2  1 
ATOM   556  N  N    . GLN   A 1 69  ? -28.971 5.919   -12.74  1   17.815 ? 69  GLN   A N    1 
ATOM   557  C  CA   . GLN   A 1 69  ? -28.584 5.761   -11.352 1   19.911 ? 69  GLN   A CA   1 
ATOM   558  C  C    . GLN   A 1 69  ? -27.157 6.273   -11.167 1   19.617 ? 69  GLN   A C    1 
ATOM   559  O  O    . GLN   A 1 69  ? -26.248 5.831   -11.866 1   18.16  ? 69  GLN   A O    1 
ATOM   560  C  CB   . GLN   A 1 69  ? -28.731 4.279   -11.01  1   23.504 ? 69  GLN   A CB   1 
ATOM   561  C  CG   . GLN   A 1 69  ? -28.613 3.952   -9.525  1   28.367 ? 69  GLN   A CG   1 
ATOM   562  C  CD   . GLN   A 1 69  ? -28.883 2.492   -9.224  1   33.053 ? 69  GLN   A CD   1 
ATOM   563  O  OE1  . GLN   A 1 69  ? -29.786 1.871   -9.797  1   37.158 ? 69  GLN   A OE1  1 
ATOM   564  N  NE2  . GLN   A 1 69  ? -28.095 1.921   -8.325  1   35.754 ? 69  GLN   A NE2  1 
ATOM   565  N  N    . ALA   A 1 70  ? -27     7.21    -10.226 1   20.749 ? 70  ALA   A N    1 
ATOM   566  C  CA   . ALA   A 1 70  ? -25.704 7.712   -9.813  1   22.539 ? 70  ALA   A CA   1 
ATOM   567  C  C    . ALA   A 1 70  ? -25.426 7.193   -8.409  1   24.858 ? 70  ALA   A C    1 
ATOM   568  O  O    . ALA   A 1 70  ? -26.028 7.668   -7.448  1   26.68  ? 70  ALA   A O    1 
ATOM   569  C  CB   . ALA   A 1 70  ? -25.708 9.224   -9.858  1   23.315 ? 70  ALA   A CB   1 
ATOM   570  N  N    . GLY   A 1 71  ? -24.543 6.198   -8.303  1   25.486 ? 71  GLY   A N    1 
ATOM   571  C  CA   . GLY   A 1 71  ? -24.394 5.462   -7.06   1   28.305 ? 71  GLY   A CA   1 
ATOM   572  C  C    . GLY   A 1 71  ? -25.729 4.845   -6.645  1   31.355 ? 71  GLY   A C    1 
ATOM   573  O  O    . GLY   A 1 71  ? -26.278 4.026   -7.377  1   34.645 ? 71  GLY   A O    1 
ATOM   574  N  N    . ASN   A 1 72  ? -26.263 5.295   -5.5    1   33.821 ? 72  ASN   A N    1 
ATOM   575  C  CA   . ASN   A 1 72  ? -27.503 4.77    -4.941  1   35.64  ? 72  ASN   A CA   1 
ATOM   576  C  C    . ASN   A 1 72  ? -28.704 5.663   -5.271  1   36.21  ? 72  ASN   A C    1 
ATOM   577  O  O    . ASN   A 1 72  ? -29.81  5.379   -4.819  1   39.044 ? 72  ASN   A O    1 
ATOM   578  C  CB   . ASN   A 1 72  ? -27.395 4.592   -3.428  1   37.165 ? 72  ASN   A CB   1 
ATOM   579  N  N    . VAL   A 1 73  ? -28.492 6.728   -6.059  1   33.014 ? 73  VAL   A N    1 
ATOM   580  C  CA   . VAL   A 1 73  ? -29.486 7.773   -6.265  1   32.213 ? 73  VAL   A CA   1 
ATOM   581  C  C    . VAL   A 1 73  ? -30.039 7.668   -7.684  1   28.611 ? 73  VAL   A C    1 
ATOM   582  O  O    . VAL   A 1 73  ? -29.28  7.669   -8.641  1   27.641 ? 73  VAL   A O    1 
ATOM   583  C  CB   . VAL   A 1 73  ? -28.865 9.167   -6.034  1   33.857 ? 73  VAL   A CB   1 
ATOM   584  C  CG1  . VAL   A 1 73  ? -29.853 10.292  -6.305  1   35.127 ? 73  VAL   A CG1  1 
ATOM   585  C  CG2  . VAL   A 1 73  ? -28.291 9.319   -4.631  1   35.027 ? 73  VAL   A CG2  1 
ATOM   586  N  N    . GLN   A 1 74  ? -31.367 7.607   -7.816  1   29.081 ? 74  GLN   A N    1 
ATOM   587  C  CA   . GLN   A 1 74  ? -32.018 7.676   -9.116  1   27.845 ? 74  GLN   A CA   1 
ATOM   588  C  C    . GLN   A 1 74  ? -32.11  9.134   -9.563  1   26.174 ? 74  GLN   A C    1 
ATOM   589  O  O    . GLN   A 1 74  ? -32.576 9.982   -8.808  1   29.837 ? 74  GLN   A O    1 
ATOM   590  C  CB   . GLN   A 1 74  ? -33.421 7.065   -9.065  1   31.15  ? 74  GLN   A CB   1 
ATOM   591  C  CG   . GLN   A 1 74  ? -33.447 5.583   -8.71   1   35.041 ? 74  GLN   A CG   1 
ATOM   592  C  CD   . GLN   A 1 74  ? -32.66  4.727   -9.678  1   38.83  ? 74  GLN   A CD   1 
ATOM   593  O  OE1  . GLN   A 1 74  ? -32.82  4.823   -10.901 1   41.557 ? 74  GLN   A OE1  1 
ATOM   594  N  NE2  . GLN   A 1 74  ? -31.779 3.894   -9.143  1   41.171 ? 74  GLN   A NE2  1 
ATOM   595  N  N    . LEU   A 1 75  ? -31.68  9.408   -10.799 1   22.458 ? 75  LEU   A N    1 
ATOM   596  C  CA   . LEU   A 1 75  ? -31.854 10.703  -11.437 1   22.526 ? 75  LEU   A CA   1 
ATOM   597  C  C    . LEU   A 1 75  ? -33.064 10.64   -12.361 1   23.737 ? 75  LEU   A C    1 
ATOM   598  O  O    . LEU   A 1 75  ? -33.202 9.697   -13.137 1   28.151 ? 75  LEU   A O    1 
ATOM   599  C  CB   . LEU   A 1 75  ? -30.626 11.105  -12.248 1   23.341 ? 75  LEU   A CB   1 
ATOM   600  C  CG   . LEU   A 1 75  ? -29.293 11.059  -11.504 1   23.673 ? 75  LEU   A CG   1 
ATOM   601  C  CD1  . LEU   A 1 75  ? -28.192 11.523  -12.436 1   25.058 ? 75  LEU   A CD1  1 
ATOM   602  C  CD2  . LEU   A 1 75  ? -29.32  11.909  -10.244 1   25.256 ? 75  LEU   A CD2  1 
ATOM   603  N  N    . ARG   A 1 76  ? -33.881 11.69   -12.337 1   22.115 ? 76  ARG   A N    1 
ATOM   604  C  CA   . ARG   A 1 76  ? -35.081 11.712  -13.156 1   22.935 ? 76  ARG   A CA   1 
ATOM   605  C  C    . ARG   A 1 76  ? -34.767 12.32   -14.517 1   20.865 ? 76  ARG   A C    1 
ATOM   606  O  O    . ARG   A 1 76  ? -34.278 13.438  -14.61  1   20.076 ? 76  ARG   A O    1 
ATOM   607  C  CB   . ARG   A 1 76  ? -36.189 12.495  -12.453 1   26.177 ? 76  ARG   A CB   1 
ATOM   608  C  CG   . ARG   A 1 76  ? -37.532 12.337  -13.147 1   28.747 ? 76  ARG   A CG   1 
ATOM   609  C  CD   . ARG   A 1 76  ? -38.672 12.801  -12.241 1   32.084 ? 76  ARG   A CD   1 
ATOM   610  N  NE   . ARG   A 1 76  ? -38.996 14.218  -12.433 1   37.549 ? 76  ARG   A NE   1 
ATOM   611  C  CZ   . ARG   A 1 76  ? -39.775 14.701  -13.401 1   40.689 ? 76  ARG   A CZ   1 
ATOM   612  N  NH1  . ARG   A 1 76  ? -40.265 13.894  -14.326 1   43.198 ? 76  ARG   A NH1  1 
ATOM   613  N  NH2  . ARG   A 1 76  ? -40.042 15.996  -13.456 1   42.985 ? 76  ARG   A NH2  1 
ATOM   614  N  N    . VAL   A 1 77  ? -35.096 11.575  -15.577 1   20.295 ? 77  VAL   A N    1 
ATOM   615  C  CA   . VAL   A 1 77  ? -34.907 12.042  -16.939 1   19.272 ? 77  VAL   A CA   1 
ATOM   616  C  C    . VAL   A 1 77  ? -36.086 12.943  -17.304 1   19.212 ? 77  VAL   A C    1 
ATOM   617  O  O    . VAL   A 1 77  ? -37.245 12.564  -17.125 1   20.934 ? 77  VAL   A O    1 
ATOM   618  C  CB   . VAL   A 1 77  ? -34.753 10.854  -17.912 1   19.322 ? 77  VAL   A CB   1 
ATOM   619  C  CG1  . VAL   A 1 77  ? -34.736 11.31   -19.366 1   19.132 ? 77  VAL   A CG1  1 
ATOM   620  C  CG2  . VAL   A 1 77  ? -33.522 10.012  -17.587 1   20.39  ? 77  VAL   A CG2  1 
ATOM   621  N  N    . ILE   A 1 78  ? -35.773 14.146  -17.802 1   20.088 ? 78  ILE   A N    1 
ATOM   622  C  CA   . ILE   A 1 78  ? -36.784 15.138  -18.13  1   21.327 ? 78  ILE   A CA   1 
ATOM   623  C  C    . ILE   A 1 78  ? -36.718 15.552  -19.599 1   21.465 ? 78  ILE   A C    1 
ATOM   624  O  O    . ILE   A 1 78  ? -37.486 16.403  -20.039 1   23.704 ? 78  ILE   A O    1 
ATOM   625  C  CB   . ILE   A 1 78  ? -36.678 16.353  -17.19  1   23.29  ? 78  ILE   A CB   1 
ATOM   626  C  CG1  . ILE   A 1 78  ? -35.318 17.049  -17.278 1   24.36  ? 78  ILE   A CG1  1 
ATOM   627  C  CG2  . ILE   A 1 78  ? -37.016 15.941  -15.757 1   23.846 ? 78  ILE   A CG2  1 
ATOM   628  C  CD1  . ILE   A 1 78  ? -35.278 18.41   -16.605 1   25.7   ? 78  ILE   A CD1  1 
ATOM   629  N  N    . GLY   A 1 79  ? -35.839 14.923  -20.376 1   19.868 ? 79  GLY   A N    1 
ATOM   630  C  CA   . GLY   A 1 79  ? -35.771 15.18   -21.799 1   20.463 ? 79  GLY   A CA   1 
ATOM   631  C  C    . GLY   A 1 79  ? -34.757 14.241  -22.43  1   19.657 ? 79  GLY   A C    1 
ATOM   632  O  O    . GLY   A 1 79  ? -33.921 13.677  -21.73  1   19.897 ? 79  GLY   A O    1 
ATOM   633  N  N    . HIS   A 1 80  ? -34.867 14.038  -23.741 1   19.476 ? 80  HIS   A N    1 
ATOM   634  C  CA   . HIS   A 1 80  ? -33.888 13.219  -24.433 1   20.071 ? 80  HIS   A CA   1 
ATOM   635  C  C    . HIS   A 1 80  ? -33.75  13.702  -25.868 1   20.553 ? 80  HIS   A C    1 
ATOM   636  O  O    . HIS   A 1 80  ? -34.707 14.162  -26.477 1   21.93  ? 80  HIS   A O    1 
ATOM   637  C  CB   . HIS   A 1 80  ? -34.252 11.732  -24.373 1   20.2   ? 80  HIS   A CB   1 
ATOM   638  C  CG   . HIS   A 1 80  ? -35.585 11.422  -24.948 1   21.444 ? 80  HIS   A CG   1 
ATOM   639  N  ND1  . HIS   A 1 80  ? -36.737 11.543  -24.206 1   22.349 ? 80  HIS   A ND1  1 
ATOM   640  C  CD2  . HIS   A 1 80  ? -35.963 11.024  -26.173 1   22.187 ? 80  HIS   A CD2  1 
ATOM   641  C  CE1  . HIS   A 1 80  ? -37.776 11.212  -24.963 1   23.351 ? 80  HIS   A CE1  1 
ATOM   642  N  NE2  . HIS   A 1 80  ? -37.327 10.905  -26.161 1   23.563 ? 80  HIS   A NE2  1 
ATOM   643  N  N    . SER   A 1 81  ? -32.544 13.542  -26.405 1   20.389 ? 81  SER   A N    1 
ATOM   644  C  CA   . SER   A 1 81  ? -32.302 13.794  -27.807 1   21.1   ? 81  SER   A CA   1 
ATOM   645  C  C    . SER   A 1 81  ? -31.125 12.939  -28.238 1   19.338 ? 81  SER   A C    1 
ATOM   646  O  O    . SER   A 1 81  ? -30.343 12.471  -27.414 1   20.524 ? 81  SER   A O    1 
ATOM   647  C  CB   . SER   A 1 81  ? -32.052 15.237  -28.071 1   23.191 ? 81  SER   A CB   1 
ATOM   648  O  OG   . SER   A 1 81  ? -30.865 15.68   -27.434 1   25.224 ? 81  SER   A OG   1 
ATOM   649  N  N    . MET   A 1 82  ? -31.039 12.746  -29.545 1   18.759 ? 82  MET   A N    1 
ATOM   650  C  CA   . MET   A 1 82  ? -29.982 11.975  -30.161 1   19.505 ? 82  MET   A CA   1 
ATOM   651  C  C    . MET   A 1 82  ? -29.136 12.945  -30.976 1   19.504 ? 82  MET   A C    1 
ATOM   652  O  O    . MET   A 1 82  ? -29.665 13.794  -31.691 1   21.264 ? 82  MET   A O    1 
ATOM   653  C  CB   . MET   A 1 82  ? -30.663 10.9    -31.019 1   21.543 ? 82  MET   A CB   1 
ATOM   654  C  CG   . MET   A 1 82  ? -29.753 10.054  -31.84  1   21.692 ? 82  MET   A CG   1 
ATOM   655  S  SD   . MET   A 1 82  ? -30.646 8.613   -32.449 1   21.434 ? 82  MET   A SD   1 
ATOM   656  C  CE   . MET   A 1 82  ? -31.822 9.27    -33.638 1   21.462 ? 82  MET   A CE   1 
ATOM   657  N  N    . GLN   A 1 83  ? -27.82  12.839  -30.813 1   18.169 ? 83  GLN   A N    1 
ATOM   658  C  CA   . GLN   A 1 83  ? -26.877 13.59   -31.618 1   18.523 ? 83  GLN   A CA   1 
ATOM   659  C  C    . GLN   A 1 83  ? -25.917 12.579  -32.225 1   17.937 ? 83  GLN   A C    1 
ATOM   660  O  O    . GLN   A 1 83  ? -25.141 11.957  -31.502 1   17.903 ? 83  GLN   A O    1 
ATOM   661  C  CB   . GLN   A 1 83  ? -26.103 14.599  -30.777 1   19.487 ? 83  GLN   A CB   1 
ATOM   662  C  CG   . GLN   A 1 83  ? -25.055 15.376  -31.564 1   20.653 ? 83  GLN   A CG   1 
ATOM   663  C  CD   . GLN   A 1 83  ? -24.276 16.348  -30.704 1   22.263 ? 83  GLN   A CD   1 
ATOM   664  O  OE1  . GLN   A 1 83  ? -24.317 16.302  -29.47  1   24.554 ? 83  GLN   A OE1  1 
ATOM   665  N  NE2  . GLN   A 1 83  ? -23.56  17.247  -31.357 1   25.134 ? 83  GLN   A NE2  1 
ATOM   666  N  N    . ASN   A 1 84  ? -26.009 12.387  -33.542 1   17.709 ? 84  ASN   A N    1 
ATOM   667  C  CA   . ASN   A 1 84  ? -25.207 11.364  -34.19  1   17.111 ? 84  ASN   A CA   1 
ATOM   668  C  C    . ASN   A 1 84  ? -25.449 10.053  -33.444 1   15.754 ? 84  ASN   A C    1 
ATOM   669  O  O    . ASN   A 1 84  ? -26.606 9.658   -33.305 1   16.841 ? 84  ASN   A O    1 
ATOM   670  C  CB   . ASN   A 1 84  ? -23.763 11.837  -34.326 1   17.554 ? 84  ASN   A CB   1 
ATOM   671  C  CG   . ASN   A 1 84  ? -23.685 13.145  -35.077 1   18.681 ? 84  ASN   A CG   1 
ATOM   672  O  OD1  . ASN   A 1 84  ? -24.242 13.252  -36.177 1   20.429 ? 84  ASN   A OD1  1 
ATOM   673  N  ND2  . ASN   A 1 84  ? -23.039 14.15   -34.501 1   19.44  ? 84  ASN   A ND2  1 
ATOM   674  N  N    . CYS   A 1 85  ? -24.39  9.389   -32.956 1   14.747 ? 85  CYS   A N    1 
ATOM   675  C  CA   . CYS   A 1 85  ? -24.542 8.085   -32.33  1   14.645 ? 85  CYS   A CA   1 
ATOM   676  C  C    . CYS   A 1 85  ? -24.575 8.143   -30.8   1   14.114 ? 85  CYS   A C    1 
ATOM   677  O  O    . CYS   A 1 85  ? -24.439 7.101   -30.154 1   14.146 ? 85  CYS   A O    1 
ATOM   678  C  CB   . CYS   A 1 85  ? -23.462 7.118   -32.786 1   15.4   ? 85  CYS   A CB   1 
ATOM   679  S  SG   . CYS   A 1 85  ? -23.463 6.855   -34.577 1   17.494 ? 85  CYS   A SG   1 
ATOM   680  N  N    A VAL   A 1 86  ? -24.77  9.34    -30.232 0.5 14.963 ? 86  VAL   A N    1 
ATOM   681  N  N    B VAL   A 1 86  ? -24.784 9.338   -30.236 0.5 14.772 ? 86  VAL   A N    1 
ATOM   682  C  CA   A VAL   A 1 86  ? -24.902 9.459   -28.789 0.5 15.767 ? 86  VAL   A CA   1 
ATOM   683  C  CA   B VAL   A 1 86  ? -24.886 9.504   -28.794 0.5 15.388 ? 86  VAL   A CA   1 
ATOM   684  C  C    A VAL   A 1 86  ? -26.311 9.914   -28.43  0.5 15.855 ? 86  VAL   A C    1 
ATOM   685  C  C    B VAL   A 1 86  ? -26.302 9.929   -28.422 0.5 15.653 ? 86  VAL   A C    1 
ATOM   686  O  O    A VAL   A 1 86  ? -26.948 10.706  -29.13  0.5 17.103 ? 86  VAL   A O    1 
ATOM   687  O  O    B VAL   A 1 86  ? -26.947 10.714  -29.123 0.5 16.875 ? 86  VAL   A O    1 
ATOM   688  C  CB   A VAL   A 1 86  ? -23.839 10.341  -28.109 0.5 17.107 ? 86  VAL   A CB   1 
ATOM   689  C  CB   B VAL   A 1 86  ? -23.811 10.493  -28.303 0.5 16.189 ? 86  VAL   A CB   1 
ATOM   690  C  CG1  A VAL   A 1 86  ? -22.462 9.722   -28.255 0.5 17.814 ? 86  VAL   A CG1  1 
ATOM   691  C  CG1  B VAL   A 1 86  ? -24.133 11.158  -26.969 0.5 16.375 ? 86  VAL   A CG1  1 
ATOM   692  C  CG2  A VAL   A 1 86  ? -23.878 11.79   -28.567 0.5 17.11  ? 86  VAL   A CG2  1 
ATOM   693  C  CG2  B VAL   A 1 86  ? -22.474 9.786   -28.202 0.5 16.863 ? 86  VAL   A CG2  1 
ATOM   694  N  N    . LEU   A 1 87  ? -26.796 9.33    -27.335 1   15.48  ? 87  LEU   A N    1 
ATOM   695  C  CA   . LEU   A 1 87  ? -28.024 9.759   -26.706 1   16.6   ? 87  LEU   A CA   1 
ATOM   696  C  C    . LEU   A 1 87  ? -27.674 10.734  -25.589 1   16.308 ? 87  LEU   A C    1 
ATOM   697  O  O    . LEU   A 1 87  ? -26.755 10.478  -24.806 1   15.66  ? 87  LEU   A O    1 
ATOM   698  C  CB   . LEU   A 1 87  ? -28.71  8.494   -26.196 1   18.231 ? 87  LEU   A CB   1 
ATOM   699  C  CG   . LEU   A 1 87  ? -30.065 8.678   -25.524 1   20.333 ? 87  LEU   A CG   1 
ATOM   700  C  CD1  . LEU   A 1 87  ? -31.135 9.178   -26.494 1   20.531 ? 87  LEU   A CD1  1 
ATOM   701  C  CD2  . LEU   A 1 87  ? -30.459 7.347   -24.898 1   21.209 ? 87  LEU   A CD2  1 
ATOM   702  N  N    . LYS   A 1 88  ? -28.428 11.836  -25.525 1   16.718 ? 88  LYS   A N    1 
ATOM   703  C  CA   . LYS   A 1 88  ? -28.293 12.828  -24.473 1   17.128 ? 88  LYS   A CA   1 
ATOM   704  C  C    . LYS   A 1 88  ? -29.565 12.853  -23.637 1   17.19  ? 88  LYS   A C    1 
ATOM   705  O  O    . LYS   A 1 88  ? -30.627 13.213  -24.128 1   19.095 ? 88  LYS   A O    1 
ATOM   706  C  CB   . LYS   A 1 88  ? -27.996 14.202  -25.073 1   18.327 ? 88  LYS   A CB   1 
ATOM   707  C  CG   . LYS   A 1 88  ? -26.701 14.242  -25.864 1   19.801 ? 88  LYS   A CG   1 
ATOM   708  C  CD   . LYS   A 1 88  ? -26.305 15.613  -26.387 1   23.271 ? 88  LYS   A CD   1 
ATOM   709  C  CE   . LYS   A 1 88  ? -27.215 16.147  -27.433 1   24.972 ? 88  LYS   A CE   1 
ATOM   710  N  NZ   . LYS   A 1 88  ? -26.631 17.349  -28.028 1   27.112 ? 88  LYS   A NZ   1 
ATOM   711  N  N    . LEU   A 1 89  ? -29.45  12.462  -22.371 1   15.932 ? 89  LEU   A N    1 
ATOM   712  C  CA   . LEU   A 1 89  ? -30.586 12.458  -21.464 1   16.149 ? 89  LEU   A CA   1 
ATOM   713  C  C    . LEU   A 1 89  ? -30.468 13.67   -20.554 1   17.228 ? 89  LEU   A C    1 
ATOM   714  O  O    . LEU   A 1 89  ? -29.536 13.753  -19.765 1   17.809 ? 89  LEU   A O    1 
ATOM   715  C  CB   . LEU   A 1 89  ? -30.599 11.167  -20.653 1   16.719 ? 89  LEU   A CB   1 
ATOM   716  C  CG   . LEU   A 1 89  ? -30.607 9.865   -21.459 1   17.27  ? 89  LEU   A CG   1 
ATOM   717  C  CD1  . LEU   A 1 89  ? -30.436 8.657   -20.557 1   18.583 ? 89  LEU   A CD1  1 
ATOM   718  C  CD2  . LEU   A 1 89  ? -31.883 9.744   -22.269 1   17.72  ? 89  LEU   A CD2  1 
ATOM   719  N  N    . LYS   A 1 90  ? -31.422 14.597  -20.666 1   18.047 ? 90  LYS   A N    1 
ATOM   720  C  CA   . LYS   A 1 90  ? -31.495 15.703  -19.73  1   19.173 ? 90  LYS   A CA   1 
ATOM   721  C  C    . LYS   A 1 90  ? -32.077 15.18   -18.419 1   19.115 ? 90  LYS   A C    1 
ATOM   722  O  O    . LYS   A 1 90  ? -33.098 14.498  -18.431 1   19.054 ? 90  LYS   A O    1 
ATOM   723  C  CB   . LYS   A 1 90  ? -32.358 16.827  -20.308 1   21.47  ? 90  LYS   A CB   1 
ATOM   724  C  CG   . LYS   A 1 90  ? -32.298 18.125  -19.541 1   24.594 ? 90  LYS   A CG   1 
ATOM   725  C  CD   . LYS   A 1 90  ? -33.08  19.236  -20.216 1   28.502 ? 90  LYS   A CD   1 
ATOM   726  C  CE   . LYS   A 1 90  ? -33.248 20.419  -19.324 1   32.208 ? 90  LYS   A CE   1 
ATOM   727  N  NZ   . LYS   A 1 90  ? -33.908 21.525  -20.019 1   35.489 ? 90  LYS   A NZ   1 
ATOM   728  N  N    . VAL   A 1 91  ? -31.417 15.506  -17.304 1   18.397 ? 91  VAL   A N    1 
ATOM   729  C  CA   . VAL   A 1 91  ? -31.845 15.056  -15.99  1   19.17  ? 91  VAL   A CA   1 
ATOM   730  C  C    . VAL   A 1 91  ? -32.152 16.276  -15.122 1   20.44  ? 91  VAL   A C    1 
ATOM   731  O  O    . VAL   A 1 91  ? -31.756 17.399  -15.441 1   20.909 ? 91  VAL   A O    1 
ATOM   732  C  CB   . VAL   A 1 91  ? -30.837 14.09   -15.328 1   19.138 ? 91  VAL   A CB   1 
ATOM   733  C  CG1  . VAL   A 1 91  ? -30.785 12.752  -16.062 1   18.976 ? 91  VAL   A CG1  1 
ATOM   734  C  CG2  . VAL   A 1 91  ? -29.438 14.689  -15.2   1   19.436 ? 91  VAL   A CG2  1 
ATOM   735  N  N    . ASP   A 1 92  ? -32.868 16.03   -14.018 1   22.492 ? 92  ASP   A N    1 
ATOM   736  C  CA   . ASP   A 1 92  ? -33.397 17.081  -13.162 1   24.352 ? 92  ASP   A CA   1 
ATOM   737  C  C    . ASP   A 1 92  ? -32.364 17.62   -12.172 1   25.38  ? 92  ASP   A C    1 
ATOM   738  O  O    . ASP   A 1 92  ? -32.681 18.546  -11.424 1   28.469 ? 92  ASP   A O    1 
ATOM   739  C  CB   . ASP   A 1 92  ? -34.616 16.596  -12.391 1   27.196 ? 92  ASP   A CB   1 
ATOM   740  C  CG   . ASP   A 1 92  ? -34.374 15.514  -11.339 1   32.415 ? 92  ASP   A CG   1 
ATOM   741  O  OD1  . ASP   A 1 92  ? -33.252 14.95   -11.287 1   36.539 ? 92  ASP   A OD1  1 
ATOM   742  O  OD2  . ASP   A 1 92  ? -35.321 15.244  -10.566 1   38.806 ? 92  ASP   A OD2  1 
ATOM   743  N  N    . THR   A 1 93  ? -31.165 17.024  -12.141 1   24.103 ? 93  THR   A N    1 
ATOM   744  C  CA   . THR   A 1 93  ? -30.116 17.379  -11.194 1   23.79  ? 93  THR   A CA   1 
ATOM   745  C  C    . THR   A 1 93  ? -28.821 17.627  -11.967 1   22.173 ? 93  THR   A C    1 
ATOM   746  O  O    . THR   A 1 93  ? -28.409 16.779  -12.755 1   23.255 ? 93  THR   A O    1 
ATOM   747  C  CB   . THR   A 1 93  ? -29.92  16.233  -10.2   1   25.913 ? 93  THR   A CB   1 
ATOM   748  O  OG1  . THR   A 1 93  ? -31.175 15.926  -9.603  1   28.744 ? 93  THR   A OG1  1 
ATOM   749  C  CG2  . THR   A 1 93  ? -28.903 16.573  -9.12   1   26.533 ? 93  THR   A CG2  1 
ATOM   750  N  N    . ALA   A 1 94  ? -28.163 18.766  -11.717 1   20.962 ? 94  ALA   A N    1 
ATOM   751  C  CA   . ALA   A 1 94  ? -26.817 18.988  -12.228 1   20.353 ? 94  ALA   A CA   1 
ATOM   752  C  C    . ALA   A 1 94  ? -25.829 18.2    -11.374 1   20.061 ? 94  ALA   A C    1 
ATOM   753  O  O    . ALA   A 1 94  ? -25.939 18.182  -10.151 1   21.276 ? 94  ALA   A O    1 
ATOM   754  C  CB   . ALA   A 1 94  ? -26.471 20.459  -12.207 1   21.987 ? 94  ALA   A CB   1 
ATOM   755  N  N    . ASN   A 1 95  ? -24.849 17.567  -12.022 1   17.924 ? 95  ASN   A N    1 
ATOM   756  C  CA   . ASN   A 1 95  ? -23.845 16.814  -11.293 1   16.894 ? 95  ASN   A CA   1 
ATOM   757  C  C    . ASN   A 1 95  ? -22.989 17.78   -10.476 1   17.053 ? 95  ASN   A C    1 
ATOM   758  O  O    . ASN   A 1 95  ? -22.255 18.586  -11.042 1   17.346 ? 95  ASN   A O    1 
ATOM   759  C  CB   . ASN   A 1 95  ? -22.996 15.997  -12.255 1   16.214 ? 95  ASN   A CB   1 
ATOM   760  C  CG   . ASN   A 1 95  ? -21.999 15.124  -11.543 1   16.458 ? 95  ASN   A CG   1 
ATOM   761  O  OD1  . ASN   A 1 95  ? -21.881 15.178  -10.313 1   17.653 ? 95  ASN   A OD1  1 
ATOM   762  N  ND2  . ASN   A 1 95  ? -21.264 14.332  -12.3   1   16.718 ? 95  ASN   A ND2  1 
ATOM   763  N  N    . PRO   A 1 96  ? -23.013 17.713  -9.126  1   17.97  ? 96  PRO   A N    1 
ATOM   764  C  CA   . PRO   A 1 96  ? -22.217 18.635  -8.315  1   18.804 ? 96  PRO   A CA   1 
ATOM   765  C  C    . PRO   A 1 96  ? -20.716 18.38   -8.441  1   18.729 ? 96  PRO   A C    1 
ATOM   766  O  O    . PRO   A 1 96  ? -19.915 19.229  -8.057  1   21.283 ? 96  PRO   A O    1 
ATOM   767  C  CB   . PRO   A 1 96  ? -22.723 18.399  -6.886  1   20.003 ? 96  PRO   A CB   1 
ATOM   768  C  CG   . PRO   A 1 96  ? -23.259 16.992  -6.901  1   20.645 ? 96  PRO   A CG   1 
ATOM   769  C  CD   . PRO   A 1 96  ? -23.778 16.749  -8.313  1   18.697 ? 96  PRO   A CD   1 
ATOM   770  N  N    . LYS   A 1 97  ? -20.342 17.21   -8.978  1   17.912 ? 97  LYS   A N    1 
ATOM   771  C  CA   . LYS   A 1 97  ? -18.943 16.845  -9.146  1   18.4   ? 97  LYS   A CA   1 
ATOM   772  C  C    . LYS   A 1 97  ? -18.475 17.088  -10.58  1   17.355 ? 97  LYS   A C    1 
ATOM   773  O  O    . LYS   A 1 97  ? -17.399 16.623  -10.944 1   18     ? 97  LYS   A O    1 
ATOM   774  C  CB   . LYS   A 1 97  ? -18.723 15.377  -8.761  1   20.084 ? 97  LYS   A CB   1 
ATOM   775  C  CG   . LYS   A 1 97  ? -19.112 15      -7.335  1   22.614 ? 97  LYS   A CG   1 
ATOM   776  C  CD   . LYS   A 1 97  ? -18.732 13.58   -6.929  1   25.371 ? 97  LYS   A CD   1 
ATOM   777  C  CE   . LYS   A 1 97  ? -19.255 13.238  -5.567  1   29.213 ? 97  LYS   A CE   1 
ATOM   778  N  NZ   . LYS   A 1 97  ? -18.765 11.958  -5.056  1   32.873 ? 97  LYS   A NZ   1 
ATOM   779  N  N    . THR   A 1 98  ? -19.244 17.826  -11.389 1   16.924 ? 98  THR   A N    1 
ATOM   780  C  CA   . THR   A 1 98  ? -18.816 18.137  -12.747 1   16.949 ? 98  THR   A CA   1 
ATOM   781  C  C    . THR   A 1 98  ? -17.485 18.88   -12.71  1   16.718 ? 98  THR   A C    1 
ATOM   782  O  O    . THR   A 1 98  ? -17.396 19.959  -12.137 1   17.988 ? 98  THR   A O    1 
ATOM   783  C  CB   . THR   A 1 98  ? -19.85  19.003  -13.469 1   17.251 ? 98  THR   A CB   1 
ATOM   784  O  OG1  . THR   A 1 98  ? -21.099 18.324  -13.501 1   17.056 ? 98  THR   A OG1  1 
ATOM   785  C  CG2  . THR   A 1 98  ? -19.46  19.3    -14.904 1   17.5   ? 98  THR   A CG2  1 
ATOM   786  N  N    . PRO   A 1 99  ? -16.421 18.353  -13.354 1   16.07  ? 99  PRO   A N    1 
ATOM   787  C  CA   . PRO   A 1 99  ? -15.152 19.073  -13.441 1   16.286 ? 99  PRO   A CA   1 
ATOM   788  C  C    . PRO   A 1 99  ? -15.204 20.122  -14.541 1   16.381 ? 99  PRO   A C    1 
ATOM   789  O  O    . PRO   A 1 99  ? -16.128 20.125  -15.347 1   17.473 ? 99  PRO   A O    1 
ATOM   790  C  CB   . PRO   A 1 99  ? -14.185 17.937  -13.788 1   16.522 ? 99  PRO   A CB   1 
ATOM   791  C  CG   . PRO   A 1 99  ? -15.004 17.048  -14.702 1   16.117 ? 99  PRO   A CG   1 
ATOM   792  C  CD   . PRO   A 1 99  ? -16.388 17.066  -14.067 1   16.279 ? 99  PRO   A CD   1 
ATOM   793  N  N    . LYS   A 1 100 ? -14.186 20.989  -14.593 1   17.324 ? 100 LYS   A N    1 
ATOM   794  C  CA   . LYS   A 1 100 ? -13.952 21.775  -15.795 1   18.534 ? 100 LYS   A CA   1 
ATOM   795  C  C    . LYS   A 1 100 ? -13.715 20.783  -16.928 1   17.495 ? 100 LYS   A C    1 
ATOM   796  O  O    . LYS   A 1 100 ? -12.914 19.872  -16.769 1   17.632 ? 100 LYS   A O    1 
ATOM   797  C  CB   . LYS   A 1 100 ? -12.736 22.698  -15.664 1   21.264 ? 100 LYS   A CB   1 
ATOM   798  C  CG   . LYS   A 1 100 ? -12.878 23.817  -14.647 1   25.32  ? 100 LYS   A CG   1 
ATOM   799  C  CD   . LYS   A 1 100 ? -11.69  24.767  -14.596 1   28.895 ? 100 LYS   A CD   1 
ATOM   800  C  CE   . LYS   A 1 100 ? -11.954 25.98   -13.758 1   32.693 ? 100 LYS   A CE   1 
ATOM   801  N  NZ   . LYS   A 1 100 ? -10.74  26.785  -13.596 1   35.119 ? 100 LYS   A NZ   1 
ATOM   802  N  N    . TYR   A 1 101 ? -14.409 20.943  -18.061 1   16.696 ? 101 TYR   A N    1 
ATOM   803  C  CA   . TYR   A 1 101 ? -14.296 19.958  -19.128 1   16.358 ? 101 TYR   A CA   1 
ATOM   804  C  C    . TYR   A 1 101 ? -14.538 20.582  -20.497 1   16.559 ? 101 TYR   A C    1 
ATOM   805  O  O    . TYR   A 1 101 ? -15.131 21.649  -20.625 1   18.018 ? 101 TYR   A O    1 
ATOM   806  C  CB   . TYR   A 1 101 ? -15.265 18.786  -18.931 1   16.837 ? 101 TYR   A CB   1 
ATOM   807  C  CG   . TYR   A 1 101 ? -16.713 19.118  -19.266 1   17.345 ? 101 TYR   A CG   1 
ATOM   808  C  CD1  . TYR   A 1 101 ? -17.55  19.701  -18.323 1   17.888 ? 101 TYR   A CD1  1 
ATOM   809  C  CD2  . TYR   A 1 101 ? -17.245 18.862  -20.527 1   18.327 ? 101 TYR   A CD2  1 
ATOM   810  C  CE1  . TYR   A 1 101 ? -18.862 20.028  -18.623 1   19.215 ? 101 TYR   A CE1  1 
ATOM   811  C  CE2  . TYR   A 1 101 ? -18.56  19.171  -20.837 1   19.234 ? 101 TYR   A CE2  1 
ATOM   812  C  CZ   . TYR   A 1 101 ? -19.371 19.757  -19.88  1   19.327 ? 101 TYR   A CZ   1 
ATOM   813  O  OH   . TYR   A 1 101 ? -20.672 20.093  -20.14  1   22.434 ? 101 TYR   A OH   1 
ATOM   814  N  N    . LYS   A 1 102 ? -14.106 19.841  -21.523 1   16.17  ? 102 LYS   A N    1 
ATOM   815  C  CA   . LYS   A 1 102 ? -14.385 20.142  -22.912 1   16.543 ? 102 LYS   A CA   1 
ATOM   816  C  C    . LYS   A 1 102 ? -14.449 18.834  -23.685 1   16.074 ? 102 LYS   A C    1 
ATOM   817  O  O    . LYS   A 1 102 ? -14.002 17.793  -23.192 1   15.563 ? 102 LYS   A O    1 
ATOM   818  C  CB   . LYS   A 1 102 ? -13.316 21.021  -23.563 1   19.915 ? 102 LYS   A CB   1 
ATOM   819  C  CG   . LYS   A 1 102 ? -11.924 20.437  -23.539 1   22.264 ? 102 LYS   A CG   1 
ATOM   820  C  CD   . LYS   A 1 102 ? -10.933 21.247  -24.357 1   26.012 ? 102 LYS   A CD   1 
ATOM   821  C  CE   . LYS   A 1 102 ? -10.793 22.634  -23.853 1   27.74  ? 102 LYS   A CE   1 
ATOM   822  N  NZ   . LYS   A 1 102 ? -9.748  23.324  -24.615 1   29.581 ? 102 LYS   A NZ   1 
ATOM   823  N  N    . PHE   A 1 103 ? -15.037 18.905  -24.88  1   15.452 ? 103 PHE   A N    1 
ATOM   824  C  CA   . PHE   A 1 103 ? -15.064 17.785  -25.801 1   15.731 ? 103 PHE   A CA   1 
ATOM   825  C  C    . PHE   A 1 103 ? -14.065 18.056  -26.92  1   16.326 ? 103 PHE   A C    1 
ATOM   826  O  O    . PHE   A 1 103 ? -14.098 19.13   -27.516 1   17.901 ? 103 PHE   A O    1 
ATOM   827  C  CB   . PHE   A 1 103 ? -16.47  17.587  -26.379 1   15.993 ? 103 PHE   A CB   1 
ATOM   828  C  CG   . PHE   A 1 103 ? -17.558 17.183  -25.392 1   15.507 ? 103 PHE   A CG   1 
ATOM   829  C  CD1  . PHE   A 1 103 ? -17.259 16.653  -24.139 1   15.851 ? 103 PHE   A CD1  1 
ATOM   830  C  CD2  . PHE   A 1 103 ? -18.897 17.275  -25.756 1   16.683 ? 103 PHE   A CD2  1 
ATOM   831  C  CE1  . PHE   A 1 103 ? -18.256 16.262  -23.263 1   16.062 ? 103 PHE   A CE1  1 
ATOM   832  C  CE2  . PHE   A 1 103 ? -19.893 16.878  -24.872 1   16.991 ? 103 PHE   A CE2  1 
ATOM   833  C  CZ   . PHE   A 1 103 ? -19.567 16.363  -23.634 1   16.963 ? 103 PHE   A CZ   1 
ATOM   834  N  N    . VAL   A 1 104 ? -13.202 17.077  -27.208 1   15.878 ? 104 VAL   A N    1 
ATOM   835  C  CA   . VAL   A 1 104 ? -12.226 17.211  -28.278 1   17.187 ? 104 VAL   A CA   1 
ATOM   836  C  C    . VAL   A 1 104 ? -12.246 15.932  -29.104 1   16.474 ? 104 VAL   A C    1 
ATOM   837  O  O    . VAL   A 1 104 ? -12.155 14.844  -28.548 1   18.129 ? 104 VAL   A O    1 
ATOM   838  C  CB   . VAL   A 1 104 ? -10.808 17.501  -27.746 1   18.949 ? 104 VAL   A CB   1 
ATOM   839  C  CG1  . VAL   A 1 104 ? -9.786  17.702  -28.865 1   20.669 ? 104 VAL   A CG1  1 
ATOM   840  C  CG2  . VAL   A 1 104 ? -10.775 18.692  -26.796 1   20.654 ? 104 VAL   A CG2  1 
ATOM   841  N  N    . ARG   A 1 105 ? -12.279 16.08   -30.432 1   16.144 ? 105 ARG   A N    1 
ATOM   842  C  CA   . ARG   A 1 105 ? -12.09  14.966  -31.344 1   16.736 ? 105 ARG   A CA   1 
ATOM   843  C  C    . ARG   A 1 105 ? -10.608 14.864  -31.688 1   16.42  ? 105 ARG   A C    1 
ATOM   844  O  O    . ARG   A 1 105 ? -10.007 15.843  -32.121 1   20.002 ? 105 ARG   A O    1 
ATOM   845  C  CB   . ARG   A 1 105 ? -12.907 15.165  -32.624 1   18.011 ? 105 ARG   A CB   1 
ATOM   846  C  CG   . ARG   A 1 105 ? -12.847 13.965  -33.558 1   18.397 ? 105 ARG   A CG   1 
ATOM   847  C  CD   . ARG   A 1 105 ? -13.608 14.178  -34.842 1   18.765 ? 105 ARG   A CD   1 
ATOM   848  N  NE   . ARG   A 1 105 ? -13.51  13.009  -35.722 1   19.194 ? 105 ARG   A NE   1 
ATOM   849  C  CZ   . ARG   A 1 105 ? -14.188 11.879  -35.587 1   19.371 ? 105 ARG   A CZ   1 
ATOM   850  N  NH1  . ARG   A 1 105 ? -15.084 11.741  -34.627 1   19.734 ? 105 ARG   A NH1  1 
ATOM   851  N  NH2  . ARG   A 1 105 ? -14.01  10.89   -36.44  1   20.165 ? 105 ARG   A NH2  1 
ATOM   852  N  N    . ILE   A 1 106 ? -10.025 13.688  -31.452 1   14.772 ? 106 ILE   A N    1 
ATOM   853  C  CA   . ILE   A 1 106 ? -8.592  13.514  -31.618 1   14.1   ? 106 ILE   A CA   1 
ATOM   854  C  C    . ILE   A 1 106 ? -8.272  12.903  -32.974 1   14.479 ? 106 ILE   A C    1 
ATOM   855  O  O    . ILE   A 1 106 ? -9.157  12.41   -33.674 1   15.395 ? 106 ILE   A O    1 
ATOM   856  C  CB   . ILE   A 1 106 ? -8.007  12.67   -30.47  1   14.04  ? 106 ILE   A CB   1 
ATOM   857  C  CG1  . ILE   A 1 106 ? -8.631  11.27   -30.397 1   15.117 ? 106 ILE   A CG1  1 
ATOM   858  C  CG2  . ILE   A 1 106 ? -8.12   13.426  -29.148 1   14.975 ? 106 ILE   A CG2  1 
ATOM   859  C  CD1  . ILE   A 1 106 ? -7.943  10.303  -29.453 1   15.687 ? 106 ILE   A CD1  1 
ATOM   860  N  N    . GLN   A 1 107 ? -6.986  12.968  -33.34  1   14.061 ? 107 GLN   A N    1 
ATOM   861  C  CA   . GLN   A 1 107 ? -6.487  12.373  -34.561 1   14.861 ? 107 GLN   A CA   1 
ATOM   862  C  C    . GLN   A 1 107 ? -5.788  11.053  -34.272 1   14.812 ? 107 GLN   A C    1 
ATOM   863  O  O    . GLN   A 1 107 ? -5.295  10.819  -33.17  1   15.64  ? 107 GLN   A O    1 
ATOM   864  C  CB   . GLN   A 1 107 ? -5.483  13.322  -35.214 1   16.696 ? 107 GLN   A CB   1 
ATOM   865  C  CG   . GLN   A 1 107 ? -6.122  14.601  -35.733 1   19.169 ? 107 GLN   A CG   1 
ATOM   866  C  CD   . GLN   A 1 107 ? -7.263  14.33   -36.69  1   22.631 ? 107 GLN   A CD   1 
ATOM   867  O  OE1  . GLN   A 1 107 ? -7.112  13.613  -37.686 1   26.287 ? 107 GLN   A OE1  1 
ATOM   868  N  NE2  . GLN   A 1 107 ? -8.43   14.877  -36.388 1   25.436 ? 107 GLN   A NE2  1 
ATOM   869  N  N    . PRO   A 1 108 ? -5.654  10.172  -35.28  1   15.71  ? 108 PRO   A N    1 
ATOM   870  C  CA   . PRO   A 1 108 ? -4.859  8.962   -35.105 1   16.917 ? 108 PRO   A CA   1 
ATOM   871  C  C    . PRO   A 1 108 ? -3.461  9.31    -34.613 1   16.162 ? 108 PRO   A C    1 
ATOM   872  O  O    . PRO   A 1 108 ? -2.854  10.278  -35.071 1   17.44  ? 108 PRO   A O    1 
ATOM   873  C  CB   . PRO   A 1 108 ? -4.833  8.311   -36.486 1   18.608 ? 108 PRO   A CB   1 
ATOM   874  C  CG   . PRO   A 1 108 ? -5.985  8.914   -37.206 1   20.289 ? 108 PRO   A CG   1 
ATOM   875  C  CD   . PRO   A 1 108 ? -6.21   10.302  -36.633 1   17.387 ? 108 PRO   A CD   1 
ATOM   876  N  N    . GLY   A 1 109 ? -2.969  8.496   -33.676 1   15.386 ? 109 GLY   A N    1 
ATOM   877  C  CA   . GLY   A 1 109 ? -1.668  8.685   -33.058 1   16.293 ? 109 GLY   A CA   1 
ATOM   878  C  C    . GLY   A 1 109 ? -1.757  9.323   -31.677 1   15.139 ? 109 GLY   A C    1 
ATOM   879  O  O    . GLY   A 1 109 ? -0.855  9.143   -30.856 1   16.096 ? 109 GLY   A O    1 
ATOM   880  N  N    . GLN   A 1 110 ? -2.864  10.026  -31.401 1   14.123 ? 110 GLN   A N    1 
ATOM   881  C  CA   . GLN   A 1 110 ? -3.056  10.663  -30.11  1   13.436 ? 110 GLN   A CA   1 
ATOM   882  C  C    . GLN   A 1 110 ? -3.377  9.616   -29.044 1   12.762 ? 110 GLN   A C    1 
ATOM   883  O  O    . GLN   A 1 110 ? -3.978  8.592   -29.346 1   13.287 ? 110 GLN   A O    1 
ATOM   884  C  CB   . GLN   A 1 110 ? -4.207  11.663  -30.218 1   13.095 ? 110 GLN   A CB   1 
ATOM   885  C  CG   . GLN   A 1 110 ? -4.475  12.455  -28.946 1   13.71  ? 110 GLN   A CG   1 
ATOM   886  C  CD   . GLN   A 1 110 ? -3.292  13.298  -28.537 1   14.403 ? 110 GLN   A CD   1 
ATOM   887  O  OE1  . GLN   A 1 110 ? -2.422  12.852  -27.781 1   15.772 ? 110 GLN   A OE1  1 
ATOM   888  N  NE2  . GLN   A 1 110 ? -3.197  14.484  -29.111 1   15.181 ? 110 GLN   A NE2  1 
ATOM   889  N  N    . THR   A 1 111 ? -2.963  9.902   -27.806 1   12.448 ? 111 THR   A N    1 
ATOM   890  C  CA   . THR   A 1 111 ? -3.212  9.026   -26.673 1   12.333 ? 111 THR   A CA   1 
ATOM   891  C  C    . THR   A 1 111 ? -4.228  9.653   -25.725 1   12.056 ? 111 THR   A C    1 
ATOM   892  O  O    . THR   A 1 111 ? -4.509  10.85   -25.773 1   13.003 ? 111 THR   A O    1 
ATOM   893  C  CB   . THR   A 1 111 ? -1.906  8.717   -25.936 1   12.913 ? 111 THR   A CB   1 
ATOM   894  O  OG1  . THR   A 1 111 ? -1.383  9.956   -25.468 1   13.362 ? 111 THR   A OG1  1 
ATOM   895  C  CG2  . THR   A 1 111 ? -0.926  7.97    -26.822 1   13.32  ? 111 THR   A CG2  1 
ATOM   896  N  N    . PHE   A 1 112 ? -4.767  8.803   -24.853 1   11.678 ? 112 PHE   A N    1 
ATOM   897  C  CA   . PHE   A 1 112 ? -5.726  9.206   -23.843 1   11.301 ? 112 PHE   A CA   1 
ATOM   898  C  C    . PHE   A 1 112 ? -5.825  8.097   -22.802 1   11.014 ? 112 PHE   A C    1 
ATOM   899  O  O    . PHE   A 1 112 ? -5.446  6.959   -23.045 1   11.287 ? 112 PHE   A O    1 
ATOM   900  C  CB   . PHE   A 1 112 ? -7.089  9.528   -24.467 1   11.743 ? 112 PHE   A CB   1 
ATOM   901  C  CG   . PHE   A 1 112 ? -7.671  8.413   -25.32  1   12.831 ? 112 PHE   A CG   1 
ATOM   902  C  CD1  . PHE   A 1 112 ? -7.365  8.32    -26.676 1   14.369 ? 112 PHE   A CD1  1 
ATOM   903  C  CD2  . PHE   A 1 112 ? -8.525  7.469   -24.777 1   13.231 ? 112 PHE   A CD2  1 
ATOM   904  C  CE1  . PHE   A 1 112 ? -7.912  7.319   -27.46  1   15.943 ? 112 PHE   A CE1  1 
ATOM   905  C  CE2  . PHE   A 1 112 ? -9.121  6.503   -25.581 1   14.829 ? 112 PHE   A CE2  1 
ATOM   906  C  CZ   . PHE   A 1 112 ? -8.804  6.426   -26.912 1   16.057 ? 112 PHE   A CZ   1 
ATOM   907  N  N    . SER   A 1 113 ? -6.373  8.471   -21.642 1   10.866 ? 113 SER   A N    1 
ATOM   908  C  CA   . SER   A 1 113 ? -6.671  7.547   -20.566 1   11.1   ? 113 SER   A CA   1 
ATOM   909  C  C    . SER   A 1 113 ? -8.087  7.024   -20.732 1   11.259 ? 113 SER   A C    1 
ATOM   910  O  O    . SER   A 1 113 ? -8.976  7.791   -21.072 1   12.507 ? 113 SER   A O    1 
ATOM   911  C  CB   . SER   A 1 113 ? -6.537  8.23    -19.226 1   11.667 ? 113 SER   A CB   1 
ATOM   912  O  OG   . SER   A 1 113 ? -5.255  8.828   -19.054 1   12.569 ? 113 SER   A OG   1 
ATOM   913  N  N    . VAL   A 1 114 ? -8.267  5.74    -20.467 1   10.852 ? 114 VAL   A N    1 
ATOM   914  C  CA   . VAL   A 1 114 ? -9.575  5.106   -20.465 1   11.066 ? 114 VAL   A CA   1 
ATOM   915  C  C    . VAL   A 1 114 ? -9.918  4.729   -19.032 1   11.001 ? 114 VAL   A C    1 
ATOM   916  O  O    . VAL   A 1 114 ? -9.116  4.092   -18.359 1   11.411 ? 114 VAL   A O    1 
ATOM   917  C  CB   . VAL   A 1 114 ? -9.579  3.855   -21.362 1   12.552 ? 114 VAL   A CB   1 
ATOM   918  C  CG1  . VAL   A 1 114 ? -10.829 3.012   -21.17  1   12.977 ? 114 VAL   A CG1  1 
ATOM   919  C  CG2  . VAL   A 1 114 ? -9.403  4.231   -22.824 1   13.931 ? 114 VAL   A CG2  1 
ATOM   920  N  N    . LEU   A 1 115 ? -11.133 5.088   -18.598 1   11.431 ? 115 LEU   A N    1 
ATOM   921  C  CA   . LEU   A 1 115 ? -11.663 4.591   -17.342 1   11.502 ? 115 LEU   A CA   1 
ATOM   922  C  C    . LEU   A 1 115 ? -12.709 3.525   -17.651 1   11.194 ? 115 LEU   A C    1 
ATOM   923  O  O    . LEU   A 1 115 ? -13.838 3.845   -18.041 1   11.957 ? 115 LEU   A O    1 
ATOM   924  C  CB   . LEU   A 1 115 ? -12.23  5.734   -16.504 1   12.047 ? 115 LEU   A CB   1 
ATOM   925  C  CG   . LEU   A 1 115 ? -12.826 5.34    -15.153 1   12.64  ? 115 LEU   A CG   1 
ATOM   926  C  CD1  . LEU   A 1 115 ? -11.719 4.881   -14.221 1   12.988 ? 115 LEU   A CD1  1 
ATOM   927  C  CD2  . LEU   A 1 115 ? -13.625 6.477   -14.547 1   13.282 ? 115 LEU   A CD2  1 
ATOM   928  N  N    . ALA   A 1 116 ? -12.304 2.254   -17.557 1   11.591 ? 116 ALA   A N    1 
ATOM   929  C  CA   . ALA   A 1 116 ? -13.193 1.147   -17.857 1   12.252 ? 116 ALA   A CA   1 
ATOM   930  C  C    . ALA   A 1 116 ? -14.197 1.025   -16.72  1   12.76  ? 116 ALA   A C    1 
ATOM   931  O  O    . ALA   A 1 116 ? -13.792 0.985   -15.567 1   14.265 ? 116 ALA   A O    1 
ATOM   932  C  CB   . ALA   A 1 116 ? -12.409 -0.131  -18.048 1   13.892 ? 116 ALA   A CB   1 
ATOM   933  N  N    . CYS   A 1 117 ? -15.486 0.981   -17.08  1   12.676 ? 117 CYS   A N    1 
ATOM   934  C  CA   A CYS   A 1 117 ? -16.556 0.944   -16.1   0.6 12.326 ? 117 CYS   A CA   1 
ATOM   935  C  CA   B CYS   A 1 117 ? -16.612 1.041   -16.159 0.4 13.861 ? 117 CYS   A CA   1 
ATOM   936  C  C    . CYS   A 1 117 ? -17.59  -0.104  -16.465 1   13.036 ? 117 CYS   A C    1 
ATOM   937  O  O    . CYS   A 1 117 ? -17.766 -0.453  -17.625 1   13.044 ? 117 CYS   A O    1 
ATOM   938  C  CB   A CYS   A 1 117 ? -17.346 2.239   -16.03  0.6 11.477 ? 117 CYS   A CB   1 
ATOM   939  C  CB   B CYS   A 1 117 ? -17.258 2.407   -16.381 0.4 16.103 ? 117 CYS   A CB   1 
ATOM   940  S  SG   A CYS   A 1 117 ? -16.34  3.634   -15.497 0.6 10.785 ? 117 CYS   A SG   1 
ATOM   941  S  SG   B CYS   A 1 117 ? -18.151 3.132   -14.984 0.4 21.218 ? 117 CYS   A SG   1 
ATOM   942  N  N    . TYR   A 1 118 ? -18.253 -0.61   -15.422 1   13.212 ? 118 TYR   A N    1 
ATOM   943  C  CA   . TYR   A 1 118 ? -19.329 -1.585  -15.532 1   13.837 ? 118 TYR   A CA   1 
ATOM   944  C  C    . TYR   A 1 118 ? -20.421 -1.149  -14.558 1   14.937 ? 118 TYR   A C    1 
ATOM   945  O  O    . TYR   A 1 118 ? -20.128 -0.858  -13.4   1   15.372 ? 118 TYR   A O    1 
ATOM   946  C  CB   . TYR   A 1 118 ? -18.845 -3.01   -15.213 1   14.289 ? 118 TYR   A CB   1 
ATOM   947  C  CG   . TYR   A 1 118 ? -17.747 -3.416  -16.176 1   14.125 ? 118 TYR   A CG   1 
ATOM   948  C  CD1  . TYR   A 1 118 ? -18.048 -3.987  -17.4   1   13.966 ? 118 TYR   A CD1  1 
ATOM   949  C  CD2  . TYR   A 1 118 ? -16.419 -3.13   -15.897 1   14.387 ? 118 TYR   A CD2  1 
ATOM   950  C  CE1  . TYR   A 1 118 ? -17.066 -4.243  -18.335 1   13.983 ? 118 TYR   A CE1  1 
ATOM   951  C  CE2  . TYR   A 1 118 ? -15.423 -3.397  -16.819 1   14.062 ? 118 TYR   A CE2  1 
ATOM   952  C  CZ   . TYR   A 1 118 ? -15.747 -3.958  -18.042 1   13.93  ? 118 TYR   A CZ   1 
ATOM   953  O  OH   . TYR   A 1 118 ? -14.799 -4.206  -18.987 1   14.24  ? 118 TYR   A OH   1 
ATOM   954  N  N    . ASN   A 1 119 ? -21.67  -1.088  -15.034 1   15.868 ? 119 ASN   A N    1 
ATOM   955  C  CA   . ASN   A 1 119 ? -22.796 -0.747  -14.177 1   17.047 ? 119 ASN   A CA   1 
ATOM   956  C  C    . ASN   A 1 119 ? -22.58  0.591   -13.477 1   16.751 ? 119 ASN   A C    1 
ATOM   957  O  O    . ASN   A 1 119 ? -23.023 0.787   -12.345 1   18.652 ? 119 ASN   A O    1 
ATOM   958  C  CB   . ASN   A 1 119 ? -23.074 -1.858  -13.175 1   19.243 ? 119 ASN   A CB   1 
ATOM   959  C  CG   . ASN   A 1 119 ? -23.549 -3.098  -13.886 1   21.909 ? 119 ASN   A CG   1 
ATOM   960  O  OD1  . ASN   A 1 119 ? -22.828 -4.095  -13.966 1   25.712 ? 119 ASN   A OD1  1 
ATOM   961  N  ND2  . ASN   A 1 119 ? -24.755 -3.038  -14.428 1   24.811 ? 119 ASN   A ND2  1 
ATOM   962  N  N    . GLY   A 1 120 ? -21.955 1.536   -14.181 1   15.955 ? 120 GLY   A N    1 
ATOM   963  C  CA   . GLY   A 1 120 ? -21.732 2.879   -13.668 1   16.645 ? 120 GLY   A CA   1 
ATOM   964  C  C    . GLY   A 1 120 ? -20.566 2.985   -12.681 1   16.819 ? 120 GLY   A C    1 
ATOM   965  O  O    . GLY   A 1 120 ? -20.347 4.064   -12.128 1   18.67  ? 120 GLY   A O    1 
ATOM   966  N  N    . SER   A 1 121 ? -19.848 1.879   -12.438 1   16.573 ? 121 SER   A N    1 
ATOM   967  C  CA   . SER   A 1 121 ? -18.805 1.815   -11.428 1   17.928 ? 121 SER   A CA   1 
ATOM   968  C  C    . SER   A 1 121 ? -17.449 1.601   -12.087 1   17.741 ? 121 SER   A C    1 
ATOM   969  O  O    . SER   A 1 121 ? -17.293 0.719   -12.92  1   16.673 ? 121 SER   A O    1 
ATOM   970  C  CB   . SER   A 1 121 ? -19.089 0.718   -10.431 1   19.724 ? 121 SER   A CB   1 
ATOM   971  O  OG   . SER   A 1 121 ? -20.18  1.09    -9.601  1   23.397 ? 121 SER   A OG   1 
ATOM   972  N  N    . PRO   A 1 122 ? -16.432 2.416   -11.742 1   19.185 ? 122 PRO   A N    1 
ATOM   973  C  CA   . PRO   A 1 122 ? -15.113 2.258   -12.347 1   19.229 ? 122 PRO   A CA   1 
ATOM   974  C  C    . PRO   A 1 122 ? -14.393 0.975   -11.928 1   18.978 ? 122 PRO   A C    1 
ATOM   975  O  O    . PRO   A 1 122 ? -14.389 0.601   -10.76  1   20.612 ? 122 PRO   A O    1 
ATOM   976  C  CB   . PRO   A 1 122 ? -14.423 3.569   -11.904 1   21.245 ? 122 PRO   A CB   1 
ATOM   977  C  CG   . PRO   A 1 122 ? -15.585 4.537   -11.663 1   24.004 ? 122 PRO   A CG   1 
ATOM   978  C  CD   . PRO   A 1 122 ? -16.547 3.642   -10.929 1   21.913 ? 122 PRO   A CD   1 
ATOM   979  N  N    . SER   A 1 123 ? -13.748 0.323   -12.906 1   17.435 ? 123 SER   A N    1 
ATOM   980  C  CA   . SER   A 1 123 ? -12.97  -0.899  -12.71  1   18.229 ? 123 SER   A CA   1 
ATOM   981  C  C    . SER   A 1 123 ? -11.466 -0.606  -12.728 1   15.885 ? 123 SER   A C    1 
ATOM   982  O  O    . SER   A 1 123 ? -10.704 -1.162  -11.938 1   16.983 ? 123 SER   A O    1 
ATOM   983  C  CB   . SER   A 1 123 ? -13.336 -1.939  -13.768 1   21.083 ? 123 SER   A CB   1 
ATOM   984  O  OG   . SER   A 1 123 ? -12.526 -3.112  -13.729 1   24.891 ? 123 SER   A OG   1 
ATOM   985  N  N    . GLY   A 1 124 ? -11.027 0.265   -13.63  1   13.996 ? 124 GLY   A N    1 
ATOM   986  C  CA   . GLY   A 1 124 ? -9.602  0.491   -13.782 1   13.5   ? 124 GLY   A CA   1 
ATOM   987  C  C    . GLY   A 1 124 ? -9.32   1.564   -14.822 1   12.589 ? 124 GLY   A C    1 
ATOM   988  O  O    . GLY   A 1 124 ? -10.208 1.94    -15.583 1   12.853 ? 124 GLY   A O    1 
ATOM   989  N  N    . VAL   A 1 125 ? -8.071  2.034   -14.831 1   12.416 ? 125 VAL   A N    1 
ATOM   990  C  CA   . VAL   A 1 125 ? -7.656  3.102   -15.722 1   12.641 ? 125 VAL   A CA   1 
ATOM   991  C  C    . VAL   A 1 125 ? -6.373  2.674   -16.429 1   12.5   ? 125 VAL   A C    1 
ATOM   992  O  O    . VAL   A 1 125 ? -5.473  2.103   -15.808 1   13.62  ? 125 VAL   A O    1 
ATOM   993  C  CB   . VAL   A 1 125 ? -7.508  4.446   -14.974 1   15.036 ? 125 VAL   A CB   1 
ATOM   994  C  CG1  . VAL   A 1 125 ? -6.428  4.44    -13.913 1   16.823 ? 125 VAL   A CG1  1 
ATOM   995  C  CG2  . VAL   A 1 125 ? -7.303  5.62    -15.919 1   15.506 ? 125 VAL   A CG2  1 
ATOM   996  N  N    . TYR   A 1 126 ? -6.305  2.964   -17.728 1   11.893 ? 126 TYR   A N    1 
ATOM   997  C  CA   . TYR   A 1 126 ? -5.125  2.638   -18.515 1   11.876 ? 126 TYR   A CA   1 
ATOM   998  C  C    . TYR   A 1 126 ? -5.033  3.569   -19.714 1   12.16  ? 126 TYR   A C    1 
ATOM   999  O  O    . TYR   A 1 126 ? -6.006  4.198   -20.088 1   12.777 ? 126 TYR   A O    1 
ATOM   1000 C  CB   . TYR   A 1 126 ? -5.167  1.183   -18.982 1   12.886 ? 126 TYR   A CB   1 
ATOM   1001 C  CG   . TYR   A 1 126 ? -6.422  0.767   -19.734 1   13.429 ? 126 TYR   A CG   1 
ATOM   1002 C  CD1  . TYR   A 1 126 ? -6.552  0.932   -21.108 1   14.074 ? 126 TYR   A CD1  1 
ATOM   1003 C  CD2  . TYR   A 1 126 ? -7.502  0.233   -19.05  1   14.82  ? 126 TYR   A CD2  1 
ATOM   1004 C  CE1  . TYR   A 1 126 ? -7.709  0.565   -21.772 1   14.723 ? 126 TYR   A CE1  1 
ATOM   1005 C  CE2  . TYR   A 1 126 ? -8.649  -0.16   -19.708 1   15.317 ? 126 TYR   A CE2  1 
ATOM   1006 C  CZ   . TYR   A 1 126 ? -8.754  0       -21.071 1   15.366 ? 126 TYR   A CZ   1 
ATOM   1007 O  OH   . TYR   A 1 126 ? -9.893  -0.383  -21.718 1   17.469 ? 126 TYR   A OH   1 
ATOM   1008 N  N    . GLN   A 1 127 ? -3.853  3.622   -20.337 1   12.815 ? 127 GLN   A N    1 
ATOM   1009 C  CA   . GLN   A 1 127 ? -3.614  4.436   -21.52  1   13.349 ? 127 GLN   A CA   1 
ATOM   1010 C  C    . GLN   A 1 127 ? -3.915  3.662   -22.801 1   13.744 ? 127 GLN   A C    1 
ATOM   1011 O  O    . GLN   A 1 127 ? -3.594  2.487   -22.911 1   15.483 ? 127 GLN   A O    1 
ATOM   1012 C  CB   . GLN   A 1 127 ? -2.144  4.814   -21.689 1   14.491 ? 127 GLN   A CB   1 
ATOM   1013 C  CG   . GLN   A 1 127 ? -1.659  5.918   -20.767 1   14.826 ? 127 GLN   A CG   1 
ATOM   1014 C  CD   . GLN   A 1 127 ? -2.396  7.21    -21.004 1   14.391 ? 127 GLN   A CD   1 
ATOM   1015 O  OE1  . GLN   A 1 127 ? -3.417  7.458   -20.368 1   14.565 ? 127 GLN   A OE1  1 
ATOM   1016 N  NE2  . GLN   A 1 127 ? -1.872  8.045   -21.891 1   15.668 ? 127 GLN   A NE2  1 
ATOM   1017 N  N    . CYS   A 1 128 ? -4.443  4.376   -23.797 1   13.63  ? 128 CYS   A N    1 
ATOM   1018 C  CA   . CYS   A 1 128 ? -4.687  3.875   -25.145 1   14.702 ? 128 CYS   A CA   1 
ATOM   1019 C  C    . CYS   A 1 128 ? -4.231  4.925   -26.155 1   14.842 ? 128 CYS   A C    1 
ATOM   1020 O  O    . CYS   A 1 128 ? -4.115  6.097   -25.819 1   17.906 ? 128 CYS   A O    1 
ATOM   1021 C  CB   . CYS   A 1 128 ? -6.184  3.66    -25.378 1   17.521 ? 128 CYS   A CB   1 
ATOM   1022 S  SG   . CYS   A 1 128 ? -6.758  2.058   -24.785 1   22.495 ? 128 CYS   A SG   1 
ATOM   1023 N  N    . ALA   A 1 129 ? -3.926  4.48    -27.375 1   15.803 ? 129 ALA   A N    1 
ATOM   1024 C  CA   . ALA   A 1 129 ? -3.735  5.37    -28.51  1   15.665 ? 129 ALA   A CA   1 
ATOM   1025 C  C    . ALA   A 1 129 ? -4.834  5.126   -29.538 1   14.752 ? 129 ALA   A C    1 
ATOM   1026 O  O    . ALA   A 1 129 ? -5.272  3.999   -29.744 1   16.289 ? 129 ALA   A O    1 
ATOM   1027 C  CB   . ALA   A 1 129 ? -2.383  5.162   -29.155 1   16.702 ? 129 ALA   A CB   1 
ATOM   1028 N  N    . MET   A 1 130 ? -5.238  6.186   -30.225 1   13.379 ? 130 MET   A N    1 
ATOM   1029 C  CA   . MET   A 1 130 ? -6.04   6.04    -31.423 1   13.549 ? 130 MET   A CA   1 
ATOM   1030 C  C    . MET   A 1 130 ? -5.131  5.497   -32.521 1   13.055 ? 130 MET   A C    1 
ATOM   1031 O  O    . MET   A 1 130 ? -4.175  6.155   -32.93  1   13.49  ? 130 MET   A O    1 
ATOM   1032 C  CB   . MET   A 1 130 ? -6.675  7.376   -31.811 1   14.86  ? 130 MET   A CB   1 
ATOM   1033 C  CG   . MET   A 1 130 ? -7.58   7.275   -33.031 1   16.487 ? 130 MET   A CG   1 
ATOM   1034 S  SD   . MET   A 1 130 ? -9.021  6.209   -32.854 1   18.028 ? 130 MET   A SD   1 
ATOM   1035 C  CE   . MET   A 1 130 ? -9.849  6.99    -31.467 1   16.989 ? 130 MET   A CE   1 
ATOM   1036 N  N    . ARG   A 1 131 ? -5.398  4.27    -32.966 1   12.968 ? 131 ARG   A N    1 
ATOM   1037 C  CA   . ARG   A 1 131 ? -4.566  3.641   -33.976 1   13.215 ? 131 ARG   A CA   1 
ATOM   1038 C  C    . ARG   A 1 131 ? -4.793  4.322   -35.327 1   13.908 ? 131 ARG   A C    1 
ATOM   1039 O  O    . ARG   A 1 131 ? -5.821  4.944   -35.577 1   14.467 ? 131 ARG   A O    1 
ATOM   1040 C  CB   . ARG   A 1 131 ? -4.904  2.154   -34.114 1   13.754 ? 131 ARG   A CB   1 
ATOM   1041 C  CG   . ARG   A 1 131 ? -4.744  1.298   -32.873 1   14.085 ? 131 ARG   A CG   1 
ATOM   1042 C  CD   . ARG   A 1 131 ? -3.383  1.414   -32.232 1   13.799 ? 131 ARG   A CD   1 
ATOM   1043 N  NE   . ARG   A 1 131 ? -2.333  1.052   -33.187 1   14.471 ? 131 ARG   A NE   1 
ATOM   1044 C  CZ   . ARG   A 1 131 ? -1.034  1.196   -32.936 1   14.618 ? 131 ARG   A CZ   1 
ATOM   1045 N  NH1  . ARG   A 1 131 ? -0.616  1.55    -31.734 1   14.21  ? 131 ARG   A NH1  1 
ATOM   1046 N  NH2  . ARG   A 1 131 ? -0.151  0.974   -33.894 1   14.939 ? 131 ARG   A NH2  1 
ATOM   1047 N  N    . PRO   A 1 132 ? -3.841  4.197   -36.272 1   14.361 ? 132 PRO   A N    1 
ATOM   1048 C  CA   . PRO   A 1 132 ? -4.041  4.718   -37.622 1   14.727 ? 132 PRO   A CA   1 
ATOM   1049 C  C    . PRO   A 1 132 ? -5.307  4.239   -38.314 1   15.263 ? 132 PRO   A C    1 
ATOM   1050 O  O    . PRO   A 1 132 ? -5.828  4.944   -39.169 1   17.206 ? 132 PRO   A O    1 
ATOM   1051 C  CB   . PRO   A 1 132 ? -2.762  4.253   -38.34  1   15.09  ? 132 PRO   A CB   1 
ATOM   1052 C  CG   . PRO   A 1 132 ? -1.718  4.267   -37.249 1   15.147 ? 132 PRO   A CG   1 
ATOM   1053 C  CD   . PRO   A 1 132 ? -2.471  3.706   -36.044 1   14.76  ? 132 PRO   A CD   1 
ATOM   1054 N  N    . ASN   A 1 133 ? -5.781  3.048   -37.956 1   15.159 ? 133 ASN   A N    1 
ATOM   1055 C  CA   . ASN   A 1 133 ? -7.007  2.509   -38.533 1   16.007 ? 133 ASN   A CA   1 
ATOM   1056 C  C    . ASN   A 1 133 ? -8.247  2.852   -37.698 1   16.179 ? 133 ASN   A C    1 
ATOM   1057 O  O    . ASN   A 1 133 ? -9.315  2.282   -37.936 1   17.182 ? 133 ASN   A O    1 
ATOM   1058 C  CB   . ASN   A 1 133 ? -6.888  1.006   -38.744 1   16.27  ? 133 ASN   A CB   1 
ATOM   1059 C  CG   . ASN   A 1 133 ? -6.892  0.219   -37.458 1   16.884 ? 133 ASN   A CG   1 
ATOM   1060 O  OD1  . ASN   A 1 133 ? -6.95   0.794   -36.361 1   16.365 ? 133 ASN   A OD1  1 
ATOM   1061 N  ND2  . ASN   A 1 133 ? -6.866  -1.097  -37.581 1   18.078 ? 133 ASN   A ND2  1 
ATOM   1062 N  N    . PHE   A 1 134 ? -8.111  3.804   -36.763 1   15.796 ? 134 PHE   A N    1 
ATOM   1063 C  CA   . PHE   A 1 134 ? -9.229  4.398   -36.029 1   15.877 ? 134 PHE   A CA   1 
ATOM   1064 C  C    . PHE   A 1 134 ? -9.88   3.413   -35.053 1   16.362 ? 134 PHE   A C    1 
ATOM   1065 O  O    . PHE   A 1 134 ? -11.034 3.598   -34.662 1   19.756 ? 134 PHE   A O    1 
ATOM   1066 C  CB   . PHE   A 1 134 ? -10.29  4.991   -36.965 1   17.182 ? 134 PHE   A CB   1 
ATOM   1067 C  CG   . PHE   A 1 134 ? -9.782  6.188   -37.752 1   19.688 ? 134 PHE   A CG   1 
ATOM   1068 C  CD1  . PHE   A 1 134 ? -9.65   7.429   -37.143 1   21.925 ? 134 PHE   A CD1  1 
ATOM   1069 C  CD2  . PHE   A 1 134 ? -9.449  6.064   -39.094 1   20.572 ? 134 PHE   A CD2  1 
ATOM   1070 C  CE1  . PHE   A 1 134 ? -9.192  8.516   -37.867 1   24.514 ? 134 PHE   A CE1  1 
ATOM   1071 C  CE2  . PHE   A 1 134 ? -8.985  7.153   -39.808 1   22.23  ? 134 PHE   A CE2  1 
ATOM   1072 C  CZ   . PHE   A 1 134 ? -8.84   8.372   -39.186 1   23.749 ? 134 PHE   A CZ   1 
ATOM   1073 N  N    . THR   A 1 135 ? -9.139  2.392   -34.635 1   15.466 ? 135 THR   A N    1 
ATOM   1074 C  CA   . THR   A 1 135 ? -9.526  1.535   -33.534 1   14.971 ? 135 THR   A CA   1 
ATOM   1075 C  C    . THR   A 1 135 ? -8.641  1.846   -32.338 1   14.236 ? 135 THR   A C    1 
ATOM   1076 O  O    . THR   A 1 135 ? -7.635  2.54    -32.475 1   14.736 ? 135 THR   A O    1 
ATOM   1077 C  CB   . THR   A 1 135 ? -9.427  0.061   -33.92  1   15.601 ? 135 THR   A CB   1 
ATOM   1078 O  OG1  . THR   A 1 135 ? -8.073  -0.306  -34.155 1   16.571 ? 135 THR   A OG1  1 
ATOM   1079 C  CG2  . THR   A 1 135 ? -10.269 -0.281  -35.131 1   16.917 ? 135 THR   A CG2  1 
ATOM   1080 N  N    . ILE   A 1 136 ? -9.008  1.3     -31.174 1   13.852 ? 136 ILE   A N    1 
ATOM   1081 C  CA   . ILE   A 1 136 ? -8.111  1.324   -30.03  1   14.053 ? 136 ILE   A CA   1 
ATOM   1082 C  C    . ILE   A 1 136 ? -7.934  -0.097  -29.522 1   14.026 ? 136 ILE   A C    1 
ATOM   1083 O  O    . ILE   A 1 136 ? -8.805  -0.944  -29.686 1   14.662 ? 136 ILE   A O    1 
ATOM   1084 C  CB   . ILE   A 1 136 ? -8.575  2.296   -28.931 1   15.712 ? 136 ILE   A CB   1 
ATOM   1085 C  CG1  . ILE   A 1 136 ? -9.792  1.793   -28.155 1   14.979 ? 136 ILE   A CG1  1 
ATOM   1086 C  CG2  . ILE   A 1 136 ? -8.796  3.691   -29.515 1   17.362 ? 136 ILE   A CG2  1 
ATOM   1087 C  CD1  . ILE   A 1 136 ? -10.19  2.702   -27.002 1   15.128 ? 136 ILE   A CD1  1 
ATOM   1088 N  N    . LYS   A 1 137 ? -6.776  -0.35   -28.91  1   14.463 ? 137 LYS   A N    1 
ATOM   1089 C  CA   . LYS   A 1 137 ? -6.477  -1.661  -28.359 1   16.052 ? 137 LYS   A CA   1 
ATOM   1090 C  C    . LYS   A 1 137 ? -6.649  -1.578  -26.85  1   15.553 ? 137 LYS   A C    1 
ATOM   1091 O  O    . LYS   A 1 137 ? -5.704  -1.3    -26.103 1   15.934 ? 137 LYS   A O    1 
ATOM   1092 C  CB   . LYS   A 1 137 ? -5.067  -2.105  -28.763 1   17.655 ? 137 LYS   A CB   1 
ATOM   1093 C  CG   . LYS   A 1 137 ? -4.845  -2.236  -30.262 1   20.691 ? 137 LYS   A CG   1 
ATOM   1094 C  CD   . LYS   A 1 137 ? -3.395  -2.546  -30.615 1   24.552 ? 137 LYS   A CD   1 
ATOM   1095 C  CE   . LYS   A 1 137 ? -3.207  -2.801  -32.068 1   29.121 ? 137 LYS   A CE   1 
ATOM   1096 N  NZ   . LYS   A 1 137 ? -1.847  -3.27   -32.338 1   32.295 ? 137 LYS   A NZ   1 
ATOM   1097 N  N    . GLY   A 1 138 ? -7.884  -1.769  -26.404 1   16.846 ? 138 GLY   A N    1 
ATOM   1098 C  CA   . GLY   A 1 138 ? -8.202  -1.603  -25.003 1   17.056 ? 138 GLY   A CA   1 
ATOM   1099 C  C    . GLY   A 1 138 ? -8.411  -2.931  -24.291 1   15.813 ? 138 GLY   A C    1 
ATOM   1100 O  O    . GLY   A 1 138 ? -7.982  -3.996  -24.734 1   17.106 ? 138 GLY   A O    1 
ATOM   1101 N  N    . SER   A 1 139 ? -9.074  -2.815  -23.142 1   13.592 ? 139 SER   A N    1 
ATOM   1102 C  CA   . SER   A 1 139 ? -9.469  -3.935  -22.321 1   14.873 ? 139 SER   A CA   1 
ATOM   1103 C  C    . SER   A 1 139 ? -10.892 -3.661  -21.86  1   13.689 ? 139 SER   A C    1 
ATOM   1104 O  O    . SER   A 1 139 ? -11.128 -2.815  -20.995 1   13.409 ? 139 SER   A O    1 
ATOM   1105 C  CB   . SER   A 1 139 ? -8.527  -4.109  -21.16  1   15.73  ? 139 SER   A CB   1 
ATOM   1106 O  OG   . SER   A 1 139 ? -8.965  -5.154  -20.313 1   18.212 ? 139 SER   A OG   1 
ATOM   1107 N  N    . PHE   A 1 140 ? -11.826 -4.296  -22.569 1   13.219 ? 140 PHE   A N    1 
ATOM   1108 C  CA   . PHE   A 1 140 ? -13.237 -4.003  -22.423 1   13.268 ? 140 PHE   A CA   1 
ATOM   1109 C  C    . PHE   A 1 140 ? -14.023 -5.3    -22.522 1   13.811 ? 140 PHE   A C    1 
ATOM   1110 O  O    . PHE   A 1 140 ? -13.861 -6.044  -23.478 1   14.575 ? 140 PHE   A O    1 
ATOM   1111 C  CB   . PHE   A 1 140 ? -13.736 -3.078  -23.536 1   13.525 ? 140 PHE   A CB   1 
ATOM   1112 C  CG   . PHE   A 1 140 ? -13.242 -1.641  -23.547 1   14.001 ? 140 PHE   A CG   1 
ATOM   1113 C  CD1  . PHE   A 1 140 ? -13.657 -0.721  -22.598 1   15.897 ? 140 PHE   A CD1  1 
ATOM   1114 C  CD2  . PHE   A 1 140 ? -12.382 -1.2    -24.539 1   15.837 ? 140 PHE   A CD2  1 
ATOM   1115 C  CE1  . PHE   A 1 140 ? -13.241 0.603   -22.663 1   17.185 ? 140 PHE   A CE1  1 
ATOM   1116 C  CE2  . PHE   A 1 140 ? -11.949 0.106   -24.579 1   17.486 ? 140 PHE   A CE2  1 
ATOM   1117 C  CZ   . PHE   A 1 140 ? -12.407 1.011   -23.671 1   17.035 ? 140 PHE   A CZ   1 
ATOM   1118 N  N    . LEU   A 1 141 ? -14.914 -5.522  -21.554 1   14.165 ? 141 LEU   A N    1 
ATOM   1119 C  CA   . LEU   A 1 141 ? -15.777 -6.688  -21.527 1   14.434 ? 141 LEU   A CA   1 
ATOM   1120 C  C    . LEU   A 1 141 ? -17.218 -6.262  -21.762 1   14.156 ? 141 LEU   A C    1 
ATOM   1121 O  O    . LEU   A 1 141 ? -17.524 -5.078  -21.787 1   13.862 ? 141 LEU   A O    1 
ATOM   1122 C  CB   . LEU   A 1 141 ? -15.664 -7.364  -20.166 1   15.921 ? 141 LEU   A CB   1 
ATOM   1123 C  CG   . LEU   A 1 141 ? -14.269 -7.784  -19.714 1   17.732 ? 141 LEU   A CG   1 
ATOM   1124 C  CD1  . LEU   A 1 141 ? -14.313 -8.142  -18.233 1   18.373 ? 141 LEU   A CD1  1 
ATOM   1125 C  CD2  . LEU   A 1 141 ? -13.79  -8.924  -20.576 1   18.492 ? 141 LEU   A CD2  1 
ATOM   1126 N  N    . ASN   A 1 142 ? -18.087 -7.256  -21.912 1   14.983 ? 142 ASN   A N    1 
ATOM   1127 C  CA   . ASN   A 1 142 ? -19.517 -7.023  -21.909 1   15.534 ? 142 ASN   A CA   1 
ATOM   1128 C  C    . ASN   A 1 142 ? -19.896 -6.137  -20.721 1   14.966 ? 142 ASN   A C    1 
ATOM   1129 O  O    . ASN   A 1 142 ? -19.518 -6.423  -19.581 1   15.627 ? 142 ASN   A O    1 
ATOM   1130 C  CB   . ASN   A 1 142 ? -20.24  -8.361  -21.892 1   17.074 ? 142 ASN   A CB   1 
ATOM   1131 C  CG   . ASN   A 1 142 ? -21.724 -8.213  -22.092 1   19.655 ? 142 ASN   A CG   1 
ATOM   1132 O  OD1  . ASN   A 1 142 ? -22.158 -7.397  -22.908 1   21.137 ? 142 ASN   A OD1  1 
ATOM   1133 N  ND2  . ASN   A 1 142 ? -22.502 -8.989  -21.359 1   23.614 ? 142 ASN   A ND2  1 
ATOM   1134 N  N    . GLY   A 1 143 ? -20.646 -5.064  -21.012 1   13.859 ? 143 GLY   A N    1 
ATOM   1135 C  CA   . GLY   A 1 143 ? -21.081 -4.117  -19.996 1   13.624 ? 143 GLY   A CA   1 
ATOM   1136 C  C    . GLY   A 1 143 ? -20.273 -2.82   -19.969 1   12.765 ? 143 GLY   A C    1 
ATOM   1137 O  O    . GLY   A 1 143 ? -20.606 -1.913  -19.219 1   13.335 ? 143 GLY   A O    1 
ATOM   1138 N  N    . SER   A 1 144 ? -19.207 -2.72   -20.782 1   12.062 ? 144 SER   A N    1 
ATOM   1139 C  CA   . SER   A 1 144 ? -18.302 -1.573  -20.716 1   12.387 ? 144 SER   A CA   1 
ATOM   1140 C  C    . SER   A 1 144 ? -18.704 -0.417  -21.627 1   11.795 ? 144 SER   A C    1 
ATOM   1141 O  O    . SER   A 1 144 ? -18.057 0.625   -21.624 1   11.578 ? 144 SER   A O    1 
ATOM   1142 C  CB   . SER   A 1 144 ? -16.896 -1.982  -21.064 1   12.623 ? 144 SER   A CB   1 
ATOM   1143 O  OG   . SER   A 1 144 ? -16.829 -2.494  -22.385 1   12.945 ? 144 SER   A OG   1 
ATOM   1144 N  N    . CYS   A 1 145 ? -19.762 -0.581  -22.431 1   12.207 ? 145 CYS   A N    1 
ATOM   1145 C  CA   . CYS   A 1 145 ? -20.157 0.485   -23.337 1   12.281 ? 145 CYS   A CA   1 
ATOM   1146 C  C    . CYS   A 1 145 ? -20.477 1.752   -22.553 1   11.732 ? 145 CYS   A C    1 
ATOM   1147 O  O    . CYS   A 1 145 ? -21.048 1.688   -21.465 1   12.299 ? 145 CYS   A O    1 
ATOM   1148 C  CB   . CYS   A 1 145 ? -21.354 0.082   -24.181 1   13.142 ? 145 CYS   A CB   1 
ATOM   1149 S  SG   . CYS   A 1 145 ? -21.031 -1.323  -25.269 1   15.089 ? 145 CYS   A SG   1 
ATOM   1150 N  N    . GLY   A 1 146 ? -20.072 2.9     -23.101 1   11.581 ? 146 GLY   A N    1 
ATOM   1151 C  CA   . GLY   A 1 146 ? -20.248 4.173   -22.436 1   11.979 ? 146 GLY   A CA   1 
ATOM   1152 C  C    . GLY   A 1 146 ? -19.068 4.57    -21.553 1   11.704 ? 146 GLY   A C    1 
ATOM   1153 O  O    . GLY   A 1 146 ? -19.035 5.699   -21.084 1   12.824 ? 146 GLY   A O    1 
ATOM   1154 N  N    . SER   A 1 147 ? -18.12  3.647   -21.328 1   11.582 ? 147 SER   A N    1 
ATOM   1155 C  CA   . SER   A 1 147 ? -16.835 4.025   -20.756 1   11.374 ? 147 SER   A CA   1 
ATOM   1156 C  C    . SER   A 1 147 ? -16.191 5.093   -21.639 1   11.289 ? 147 SER   A C    1 
ATOM   1157 O  O    . SER   A 1 147 ? -16.368 5.073   -22.855 1   12.275 ? 147 SER   A O    1 
ATOM   1158 C  CB   . SER   A 1 147 ? -15.897 2.842   -20.623 1   11.73  ? 147 SER   A CB   1 
ATOM   1159 O  OG   . SER   A 1 147 ? -16.379 1.826   -19.759 1   12.128 ? 147 SER   A OG   1 
ATOM   1160 N  N    . VAL   A 1 148 ? -15.433 6.015   -21.031 1   11.203 ? 148 VAL   A N    1 
ATOM   1161 C  CA   . VAL   A 1 148 ? -14.875 7.126   -21.781 1   11.698 ? 148 VAL   A CA   1 
ATOM   1162 C  C    . VAL   A 1 148 ? -13.352 7.183   -21.691 1   11.154 ? 148 VAL   A C    1 
ATOM   1163 O  O    . VAL   A 1 148 ? -12.717 6.661   -20.772 1   11.694 ? 148 VAL   A O    1 
ATOM   1164 C  CB   . VAL   A 1 148 ? -15.488 8.477   -21.374 1   12.749 ? 148 VAL   A CB   1 
ATOM   1165 C  CG1  . VAL   A 1 148 ? -16.98  8.498   -21.682 1   13.022 ? 148 VAL   A CG1  1 
ATOM   1166 C  CG2  . VAL   A 1 148 ? -15.217 8.835   -19.92  1   13.576 ? 148 VAL   A CG2  1 
ATOM   1167 N  N    . GLY   A 1 149 ? -12.816 7.88    -22.695 1   11.31  ? 149 GLY   A N    1 
ATOM   1168 C  CA   . GLY   A 1 149 ? -11.415 8.237   -22.792 1   11.287 ? 149 GLY   A CA   1 
ATOM   1169 C  C    . GLY   A 1 149 ? -11.238 9.746   -22.704 1   11.638 ? 149 GLY   A C    1 
ATOM   1170 O  O    . GLY   A 1 149 ? -12.088 10.51   -23.148 1   12.625 ? 149 GLY   A O    1 
ATOM   1171 N  N    . PHE   A 1 150 ? -10.122 10.17   -22.111 1   11.682 ? 150 PHE   A N    1 
ATOM   1172 C  CA   . PHE   A 1 150 ? -9.927  11.564  -21.762 1   12.269 ? 150 PHE   A CA   1 
ATOM   1173 C  C    . PHE   A 1 150 ? -8.452  11.874  -21.53  1   11.998 ? 150 PHE   A C    1 
ATOM   1174 O  O    . PHE   A 1 150 ? -7.634  10.987  -21.272 1   11.706 ? 150 PHE   A O    1 
ATOM   1175 C  CB   . PHE   A 1 150 ? -10.706 11.906  -20.485 1   13.113 ? 150 PHE   A CB   1 
ATOM   1176 C  CG   . PHE   A 1 150 ? -10.309 11.056  -19.289 1   13.576 ? 150 PHE   A CG   1 
ATOM   1177 C  CD1  . PHE   A 1 150 ? -10.853 9.792   -19.112 1   14.785 ? 150 PHE   A CD1  1 
ATOM   1178 C  CD2  . PHE   A 1 150 ? -9.369  11.497  -18.365 1   13.853 ? 150 PHE   A CD2  1 
ATOM   1179 C  CE1  . PHE   A 1 150 ? -10.466 8.992   -18.044 1   15.69  ? 150 PHE   A CE1  1 
ATOM   1180 C  CE2  . PHE   A 1 150 ? -8.979  10.682  -17.309 1   14.564 ? 150 PHE   A CE2  1 
ATOM   1181 C  CZ   . PHE   A 1 150 ? -9.529  9.438   -17.152 1   15.485 ? 150 PHE   A CZ   1 
ATOM   1182 N  N    . ASN   A 1 151 ? -8.142  13.171  -21.606 1   12.543 ? 151 ASN   A N    1 
ATOM   1183 C  CA   . ASN   A 1 151 ? -6.884  13.72   -21.118 1   12.926 ? 151 ASN   A CA   1 
ATOM   1184 C  C    . ASN   A 1 151 ? -7.206  14.787  -20.077 1   13.999 ? 151 ASN   A C    1 
ATOM   1185 O  O    . ASN   A 1 151 ? -8.324  15.288  -20.041 1   15.237 ? 151 ASN   A O    1 
ATOM   1186 C  CB   . ASN   A 1 151 ? -6.02   14.268  -22.254 1   13.356 ? 151 ASN   A CB   1 
ATOM   1187 C  CG   . ASN   A 1 151 ? -5.417  13.167  -23.096 1   14.063 ? 151 ASN   A CG   1 
ATOM   1188 O  OD1  . ASN   A 1 151 ? -4.567  12.398  -22.645 1   15.233 ? 151 ASN   A OD1  1 
ATOM   1189 N  ND2  . ASN   A 1 151 ? -5.924  12.996  -24.295 1   14.386 ? 151 ASN   A ND2  1 
ATOM   1190 N  N    . ILE   A 1 152 ? -6.248  15.113  -19.208 1   14.267 ? 152 ILE   A N    1 
ATOM   1191 C  CA   . ILE   A 1 152 ? -6.443  16.163  -18.218 1   16.176 ? 152 ILE   A CA   1 
ATOM   1192 C  C    . ILE   A 1 152 ? -5.177  17.003  -18.184 1   19.456 ? 152 ILE   A C    1 
ATOM   1193 O  O    . ILE   A 1 152 ? -4.495  17.089  -17.16  1   22.835 ? 152 ILE   A O    1 
ATOM   1194 C  CB   . ILE   A 1 152 ? -6.782  15.634  -16.811 1   17.008 ? 152 ILE   A CB   1 
ATOM   1195 C  CG1  . ILE   A 1 152 ? -7.809  14.507  -16.829 1   17.161 ? 152 ILE   A CG1  1 
ATOM   1196 C  CG2  . ILE   A 1 152 ? -7.225  16.799  -15.928 1   17.623 ? 152 ILE   A CG2  1 
ATOM   1197 C  CD1  . ILE   A 1 152 ? -8.18   13.986  -15.452 1   17.741 ? 152 ILE   A CD1  1 
ATOM   1198 N  N    . ASP   A 1 153 ? -4.848  17.59   -19.33  1   21.997 ? 153 ASP   A N    1 
ATOM   1199 C  CA   . ASP   A 1 153 ? -3.795  18.583  -19.391 1   23.972 ? 153 ASP   A CA   1 
ATOM   1200 C  C    . ASP   A 1 153 ? -4.331  19.841  -18.709 1   27.41  ? 153 ASP   A C    1 
ATOM   1201 O  O    . ASP   A 1 153 ? -5.4    20.336  -19.06  1   30.76  ? 153 ASP   A O    1 
ATOM   1202 C  CB   . ASP   A 1 153 ? -3.326  18.813  -20.821 1   23.437 ? 153 ASP   A CB   1 
ATOM   1203 C  CG   . ASP   A 1 153 ? -2.988  17.555  -21.61  1   22.809 ? 153 ASP   A CG   1 
ATOM   1204 O  OD1  . ASP   A 1 153 ? -2.194  16.729  -21.106 1   22.995 ? 153 ASP   A OD1  1 
ATOM   1205 O  OD2  . ASP   A 1 153 ? -3.523  17.405  -22.72  1   22.952 ? 153 ASP   A OD2  1 
ATOM   1206 N  N    . TYR   A 1 154 ? -3.597  20.32   -17.703 1   30.787 ? 154 TYR   A N    1 
ATOM   1207 C  CA   . TYR   A 1 154 ? -3.816  21.628  -17.106 1   32.546 ? 154 TYR   A CA   1 
ATOM   1208 C  C    . TYR   A 1 154 ? -5.202  21.731  -16.459 1   32.609 ? 154 TYR   A C    1 
ATOM   1209 O  O    . TYR   A 1 154 ? -5.844  22.773  -16.57  1   33.83  ? 154 TYR   A O    1 
ATOM   1210 C  CB   . TYR   A 1 154 ? -3.615  22.738  -18.153 1   35.1   ? 154 TYR   A CB   1 
ATOM   1211 C  CG   . TYR   A 1 154 ? -2.555  22.481  -19.223 1   39.171 ? 154 TYR   A CG   1 
ATOM   1212 C  CD1  . TYR   A 1 154 ? -1.199  22.54   -18.926 1   40.677 ? 154 TYR   A CD1  1 
ATOM   1213 C  CD2  . TYR   A 1 154 ? -2.914  22.203  -20.541 1   40.925 ? 154 TYR   A CD2  1 
ATOM   1214 C  CE1  . TYR   A 1 154 ? -0.234  22.311  -19.896 1   43.278 ? 154 TYR   A CE1  1 
ATOM   1215 C  CE2  . TYR   A 1 154 ? -1.96   21.976  -21.522 1   42.68  ? 154 TYR   A CE2  1 
ATOM   1216 C  CZ   . TYR   A 1 154 ? -0.614  22.032  -21.198 1   43.539 ? 154 TYR   A CZ   1 
ATOM   1217 O  OH   . TYR   A 1 154 ? 0.337   21.809  -22.151 1   46.889 ? 154 TYR   A OH   1 
ATOM   1218 N  N    . ASP   A 1 155 ? -5.659  20.679  -15.758 1   32.435 ? 155 ASP   A N    1 
ATOM   1219 C  CA   . ASP   A 1 155 ? -6.761  20.77   -14.798 1   31.642 ? 155 ASP   A CA   1 
ATOM   1220 C  C    . ASP   A 1 155 ? -8.15   20.675  -15.445 1   31.3   ? 155 ASP   A C    1 
ATOM   1221 O  O    . ASP   A 1 155 ? -9.154  20.597  -14.744 1   33.884 ? 155 ASP   A O    1 
ATOM   1222 C  CB   . ASP   A 1 155 ? -6.664  22.02   -13.936 1   34.435 ? 155 ASP   A CB   1 
ATOM   1223 N  N    . CYS   A 1 156 ? -8.21   20.692  -16.78  1   25.55  ? 156 CYS   A N    1 
ATOM   1224 C  CA   . CYS   A 1 156 ? -9.457  20.598  -17.522 1   22.389 ? 156 CYS   A CA   1 
ATOM   1225 C  C    . CYS   A 1 156 ? -9.531  19.213  -18.15  1   19.125 ? 156 CYS   A C    1 
ATOM   1226 O  O    . CYS   A 1 156 ? -8.568  18.778  -18.781 1   19.357 ? 156 CYS   A O    1 
ATOM   1227 C  CB   . CYS   A 1 156 ? -9.48   21.668  -18.603 1   24.142 ? 156 CYS   A CB   1 
ATOM   1228 S  SG   . CYS   A 1 156 ? -10.915 21.597  -19.702 1   25.544 ? 156 CYS   A SG   1 
ATOM   1229 N  N    . VAL   A 1 157 ? -10.673 18.535  -17.998 1   16.476 ? 157 VAL   A N    1 
ATOM   1230 C  CA   . VAL   A 1 157 ? -10.848 17.22   -18.594 1   15.314 ? 157 VAL   A CA   1 
ATOM   1231 C  C    . VAL   A 1 157 ? -11.283 17.367  -20.047 1   15.392 ? 157 VAL   A C    1 
ATOM   1232 O  O    . VAL   A 1 157 ? -12.349 17.908  -20.294 1   16.924 ? 157 VAL   A O    1 
ATOM   1233 C  CB   . VAL   A 1 157 ? -11.853 16.339  -17.832 1   15.078 ? 157 VAL   A CB   1 
ATOM   1234 C  CG1  . VAL   A 1 157 ? -11.942 14.96   -18.453 1   15.33  ? 157 VAL   A CG1  1 
ATOM   1235 C  CG2  . VAL   A 1 157 ? -11.492 16.219  -16.36  1   15.78  ? 157 VAL   A CG2  1 
ATOM   1236 N  N    . SER   A 1 158 ? -10.478 16.85   -20.982 1   15.053 ? 158 SER   A N    1 
ATOM   1237 C  CA   . SER   A 1 158 ? -10.832 16.818  -22.391 1   15.307 ? 158 SER   A CA   1 
ATOM   1238 C  C    . SER   A 1 158 ? -11.322 15.415  -22.726 1   14.759 ? 158 SER   A C    1 
ATOM   1239 O  O    . SER   A 1 158 ? -10.531 14.491  -22.831 1   16.043 ? 158 SER   A O    1 
ATOM   1240 C  CB   . SER   A 1 158 ? -9.686  17.234  -23.297 1   17.006 ? 158 SER   A CB   1 
ATOM   1241 O  OG   . SER   A 1 158 ? -8.495  16.487  -23.094 1   20.658 ? 158 SER   A OG   1 
ATOM   1242 N  N    . PHE   A 1 159 ? -12.643 15.25   -22.864 1   13.586 ? 159 PHE   A N    1 
ATOM   1243 C  CA   . PHE   A 1 159 ? -13.218 13.967  -23.234 1   13.499 ? 159 PHE   A CA   1 
ATOM   1244 C  C    . PHE   A 1 159 ? -13.104 13.771  -24.741 1   13.431 ? 159 PHE   A C    1 
ATOM   1245 O  O    . PHE   A 1 159 ? -13.518 14.645  -25.499 1   14.174 ? 159 PHE   A O    1 
ATOM   1246 C  CB   . PHE   A 1 159 ? -14.691 13.904  -22.834 1   13.638 ? 159 PHE   A CB   1 
ATOM   1247 C  CG   . PHE   A 1 159 ? -14.93  13.902  -21.335 1   13.76  ? 159 PHE   A CG   1 
ATOM   1248 C  CD1  . PHE   A 1 159 ? -14.704 12.754  -20.592 1   13.603 ? 159 PHE   A CD1  1 
ATOM   1249 C  CD2  . PHE   A 1 159 ? -15.363 15.041  -20.673 1   13.91  ? 159 PHE   A CD2  1 
ATOM   1250 C  CE1  . PHE   A 1 159 ? -14.928 12.734  -19.233 1   13.562 ? 159 PHE   A CE1  1 
ATOM   1251 C  CE2  . PHE   A 1 159 ? -15.587 15.022  -19.308 1   13.647 ? 159 PHE   A CE2  1 
ATOM   1252 C  CZ   . PHE   A 1 159 ? -15.367 13.87   -18.589 1   13.582 ? 159 PHE   A CZ   1 
ATOM   1253 N  N    . CYS   A 1 160 ? -12.551 12.628  -25.158 1   12.944 ? 160 CYS   A N    1 
ATOM   1254 C  CA   . CYS   A 1 160 ? -12.289 12.382  -26.565 1   13.414 ? 160 CYS   A CA   1 
ATOM   1255 C  C    . CYS   A 1 160 ? -12.856 11.065  -27.083 1   12.859 ? 160 CYS   A C    1 
ATOM   1256 O  O    . CYS   A 1 160 ? -12.875 10.872  -28.292 1   14.911 ? 160 CYS   A O    1 
ATOM   1257 C  CB   . CYS   A 1 160 ? -10.798 12.446  -26.886 1   13.669 ? 160 CYS   A CB   1 
ATOM   1258 S  SG   . CYS   A 1 160 ? -9.766  11.332  -25.91  1   15.34  ? 160 CYS   A SG   1 
ATOM   1259 N  N    . TYR   A 1 161 ? -13.307 10.154  -26.213 1   11.898 ? 161 TYR   A N    1 
ATOM   1260 C  CA   . TYR   A 1 161 ? -13.735 8.84    -26.667 1   11.754 ? 161 TYR   A CA   1 
ATOM   1261 C  C    . TYR   A 1 161 ? -14.874 8.343   -25.789 1   12.089 ? 161 TYR   A C    1 
ATOM   1262 O  O    . TYR   A 1 161 ? -14.84  8.528   -24.576 1   12.129 ? 161 TYR   A O    1 
ATOM   1263 C  CB   . TYR   A 1 161 ? -12.565 7.843   -26.622 1   11.697 ? 161 TYR   A CB   1 
ATOM   1264 C  CG   . TYR   A 1 161 ? -12.89  6.416   -27.04  1   11.69  ? 161 TYR   A CG   1 
ATOM   1265 C  CD1  . TYR   A 1 161 ? -12.902 6.033   -28.374 1   12.115 ? 161 TYR   A CD1  1 
ATOM   1266 C  CD2  . TYR   A 1 161 ? -13.199 5.441   -26.099 1   11.796 ? 161 TYR   A CD2  1 
ATOM   1267 C  CE1  . TYR   A 1 161 ? -13.216 4.741   -28.756 1   12.169 ? 161 TYR   A CE1  1 
ATOM   1268 C  CE2  . TYR   A 1 161 ? -13.496 4.138   -26.465 1   11.968 ? 161 TYR   A CE2  1 
ATOM   1269 C  CZ   . TYR   A 1 161 ? -13.513 3.785   -27.801 1   12.363 ? 161 TYR   A CZ   1 
ATOM   1270 O  OH   . TYR   A 1 161 ? -13.81  2.512   -28.198 1   13.321 ? 161 TYR   A OH   1 
ATOM   1271 N  N    . MET   A 1 162 ? -15.877 7.731   -26.43  1   11.622 ? 162 MET   A N    1 
ATOM   1272 C  CA   . MET   A 1 162 ? -16.887 6.955   -25.737 1   11.834 ? 162 MET   A CA   1 
ATOM   1273 C  C    . MET   A 1 162 ? -16.955 5.583   -26.4   1   11.373 ? 162 MET   A C    1 
ATOM   1274 O  O    . MET   A 1 162 ? -17.03  5.487   -27.624 1   11.958 ? 162 MET   A O    1 
ATOM   1275 C  CB   . MET   A 1 162 ? -18.258 7.641   -25.8   1   12.986 ? 162 MET   A CB   1 
ATOM   1276 C  CG   . MET   A 1 162 ? -19.357 6.804   -25.149 1   13.87  ? 162 MET   A CG   1 
ATOM   1277 S  SD   . MET   A 1 162 ? -20.859 7.647   -24.635 1   18.681 ? 162 MET   A SD   1 
ATOM   1278 C  CE   . MET   A 1 162 ? -20.398 8.371   -23.049 1   18.439 ? 162 MET   A CE   1 
ATOM   1279 N  N    . HIS   A 1 163 ? -16.927 4.531   -25.583 1   11.411 ? 163 HIS   A N    1 
ATOM   1280 C  CA   . HIS   A 1 163 ? -16.816 3.172   -26.089 1   11.65  ? 163 HIS   A CA   1 
ATOM   1281 C  C    . HIS   A 1 163 ? -18.163 2.636   -26.579 1   12.205 ? 163 HIS   A C    1 
ATOM   1282 O  O    . HIS   A 1 163 ? -19.151 2.662   -25.837 1   12.431 ? 163 HIS   A O    1 
ATOM   1283 C  CB   . HIS   A 1 163 ? -16.278 2.271   -24.974 1   11.642 ? 163 HIS   A CB   1 
ATOM   1284 C  CG   . HIS   A 1 163 ? -16.039 0.886   -25.44  1   11.942 ? 163 HIS   A CG   1 
ATOM   1285 N  ND1  . HIS   A 1 163 ? -15.282 0.62    -26.551 1   12.572 ? 163 HIS   A ND1  1 
ATOM   1286 C  CD2  . HIS   A 1 163 ? -16.476 -0.297  -24.978 1   12.008 ? 163 HIS   A CD2  1 
ATOM   1287 C  CE1  . HIS   A 1 163 ? -15.265 -0.689  -26.745 1   12.635 ? 163 HIS   A CE1  1 
ATOM   1288 N  NE2  . HIS   A 1 163 ? -15.992 -1.27   -25.804 1   12.446 ? 163 HIS   A NE2  1 
ATOM   1289 N  N    . HIS   A 1 164 ? -18.191 2.115   -27.814 1   12.117 ? 164 HIS   A N    1 
ATOM   1290 C  CA   . HIS   A 1 164 ? -19.418 1.561   -28.379 1   12.353 ? 164 HIS   A CA   1 
ATOM   1291 C  C    . HIS   A 1 164 ? -19.379 0.05    -28.619 1   12.428 ? 164 HIS   A C    1 
ATOM   1292 O  O    . HIS   A 1 164 ? -20.394 -0.609  -28.398 1   13.575 ? 164 HIS   A O    1 
ATOM   1293 C  CB   . HIS   A 1 164 ? -19.831 2.249   -29.682 1   12.913 ? 164 HIS   A CB   1 
ATOM   1294 C  CG   . HIS   A 1 164 ? -20.422 3.592   -29.492 1   12.732 ? 164 HIS   A CG   1 
ATOM   1295 N  ND1  . HIS   A 1 164 ? -19.817 4.721   -28.986 1   14.78  ? 164 HIS   A ND1  1 
ATOM   1296 C  CD2  . HIS   A 1 164 ? -21.675 3.963   -29.877 1   11.39  ? 164 HIS   A CD2  1 
ATOM   1297 C  CE1  . HIS   A 1 164 ? -20.702 5.724   -29.018 1   11.893 ? 164 HIS   A CE1  1 
ATOM   1298 N  NE2  . HIS   A 1 164 ? -21.826 5.276   -29.571 1   14.657 ? 164 HIS   A NE2  1 
ATOM   1299 N  N    . MET   A 1 165 ? -18.286 -0.518  -29.138 1   13.025 ? 165 MET   A N    1 
ATOM   1300 C  CA   . MET   A 1 165 ? -18.296 -1.95   -29.396 1   13.621 ? 165 MET   A CA   1 
ATOM   1301 C  C    . MET   A 1 165 ? -16.887 -2.513  -29.564 1   13.539 ? 165 MET   A C    1 
ATOM   1302 O  O    . MET   A 1 165 ? -15.927 -1.784  -29.789 1   13.548 ? 165 MET   A O    1 
ATOM   1303 C  CB   . MET   A 1 165 ? -19.124 -2.345  -30.629 1   15.047 ? 165 MET   A CB   1 
ATOM   1304 C  CG   . MET   A 1 165 ? -18.512 -1.97   -31.945 1   16.542 ? 165 MET   A CG   1 
ATOM   1305 S  SD   . MET   A 1 165 ? -18.83  -0.258  -32.393 1   18.463 ? 165 MET   A SD   1 
ATOM   1306 C  CE   . MET   A 1 165 ? -18.641 -0.397  -34.174 1   18.073 ? 165 MET   A CE   1 
ATOM   1307 N  N    . GLU   A 1 166 ? -16.811 -3.842  -29.463 1   13.74  ? 166 GLU   A N    1 
ATOM   1308 C  CA   . GLU   A 1 166 ? -15.645 -4.614  -29.858 1   13.923 ? 166 GLU   A CA   1 
ATOM   1309 C  C    . GLU   A 1 166 ? -15.899 -5.198  -31.245 1   15.079 ? 166 GLU   A C    1 
ATOM   1310 O  O    . GLU   A 1 166 ? -16.963 -5.762  -31.515 1   15.731 ? 166 GLU   A O    1 
ATOM   1311 C  CB   . GLU   A 1 166 ? -15.356 -5.708  -28.835 1   14.263 ? 166 GLU   A CB   1 
ATOM   1312 C  CG   . GLU   A 1 166 ? -14.106 -6.523  -29.168 1   14.88  ? 166 GLU   A CG   1 
ATOM   1313 C  CD   . GLU   A 1 166 ? -13.635 -7.41   -28.036 1   15.963 ? 166 GLU   A CD   1 
ATOM   1314 O  OE1  . GLU   A 1 166 ? -13.532 -6.881  -26.902 1   15.009 ? 166 GLU   A OE1  1 
ATOM   1315 O  OE2  . GLU   A 1 166 ? -13.334 -8.597  -28.295 1   18.148 ? 166 GLU   A OE2  1 
ATOM   1316 N  N    . LEU   A 1 167 ? -14.891 -5.044  -32.11  1   15.618 ? 167 LEU   A N    1 
ATOM   1317 C  CA   . LEU   A 1 167 ? -14.907 -5.58   -33.455 1   17.672 ? 167 LEU   A CA   1 
ATOM   1318 C  C    . LEU   A 1 167 ? -14.445 -7.032  -33.429 1   18.59  ? 167 LEU   A C    1 
ATOM   1319 O  O    . LEU   A 1 167 ? -13.831 -7.49   -32.467 1   18.885 ? 167 LEU   A O    1 
ATOM   1320 C  CB   . LEU   A 1 167 ? -14.028 -4.719  -34.357 1   18.623 ? 167 LEU   A CB   1 
ATOM   1321 C  CG   . LEU   A 1 167 ? -14.543 -3.296  -34.6   1   20.373 ? 167 LEU   A CG   1 
ATOM   1322 C  CD1  . LEU   A 1 167 ? -13.492 -2.478  -35.315 1   21.015 ? 167 LEU   A CD1  1 
ATOM   1323 C  CD2  . LEU   A 1 167 ? -15.847 -3.31   -35.385 1   22.329 ? 167 LEU   A CD2  1 
ATOM   1324 N  N    . PRO   A 1 168 ? -14.747 -7.812  -34.488 1   21.695 ? 168 PRO   A N    1 
ATOM   1325 C  CA   . PRO   A 1 168 ? -14.362 -9.224  -34.515 1   23.457 ? 168 PRO   A CA   1 
ATOM   1326 C  C    . PRO   A 1 168 ? -12.886 -9.564  -34.307 1   23.751 ? 168 PRO   A C    1 
ATOM   1327 O  O    . PRO   A 1 168 ? -12.575 -10.679 -33.897 1   26.281 ? 168 PRO   A O    1 
ATOM   1328 C  CB   . PRO   A 1 168 ? -14.86  -9.675  -35.901 1   25.154 ? 168 PRO   A CB   1 
ATOM   1329 C  CG   . PRO   A 1 168 ? -15.989 -8.733  -36.228 1   25.085 ? 168 PRO   A CG   1 
ATOM   1330 C  CD   . PRO   A 1 168 ? -15.576 -7.408  -35.64  1   22.834 ? 168 PRO   A CD   1 
ATOM   1331 N  N    . THR   A 1 169 ? -11.983 -8.616  -34.597 1   24.614 ? 169 THR   A N    1 
ATOM   1332 C  CA   . THR   A 1 169 ? -10.554 -8.826  -34.414 1   25.273 ? 169 THR   A CA   1 
ATOM   1333 C  C    . THR   A 1 169 ? -10.115 -8.541  -32.976 1   23.027 ? 169 THR   A C    1 
ATOM   1334 O  O    . THR   A 1 169 ? -8.93   -8.643  -32.675 1   24.761 ? 169 THR   A O    1 
ATOM   1335 C  CB   . THR   A 1 169 ? -9.768  -7.97   -35.409 1   27.437 ? 169 THR   A CB   1 
ATOM   1336 O  OG1  . THR   A 1 169 ? -10.246 -6.634  -35.3   1   29.296 ? 169 THR   A OG1  1 
ATOM   1337 C  CG2  . THR   A 1 169 ? -9.916  -8.459  -36.839 1   28.778 ? 169 THR   A CG2  1 
ATOM   1338 N  N    . GLY   A 1 170 ? -11.043 -8.175  -32.086 1   20.325 ? 170 GLY   A N    1 
ATOM   1339 C  CA   . GLY   A 1 170 ? -10.735 -8.01   -30.676 1   19.017 ? 170 GLY   A CA   1 
ATOM   1340 C  C    . GLY   A 1 170 ? -10.237 -6.607  -30.329 1   18.406 ? 170 GLY   A C    1 
ATOM   1341 O  O    . GLY   A 1 170 ? -9.722  -6.401  -29.237 1   22.036 ? 170 GLY   A O    1 
ATOM   1342 N  N    . VAL   A 1 171 ? -10.375 -5.661  -31.26  1   16.65  ? 171 VAL   A N    1 
ATOM   1343 C  CA   . VAL   A 1 171 ? -10.058 -4.268  -31.006 1   15.766 ? 171 VAL   A CA   1 
ATOM   1344 C  C    . VAL   A 1 171 ? -11.373 -3.511  -30.836 1   14.669 ? 171 VAL   A C    1 
ATOM   1345 O  O    . VAL   A 1 171 ? -12.457 -4.057  -31.062 1   15.049 ? 171 VAL   A O    1 
ATOM   1346 C  CB   . VAL   A 1 171 ? -9.188  -3.672  -32.127 1   17.18  ? 171 VAL   A CB   1 
ATOM   1347 C  CG1  . VAL   A 1 171 ? -7.875  -4.433  -32.268 1   18.592 ? 171 VAL   A CG1  1 
ATOM   1348 C  CG2  . VAL   A 1 171 ? -9.933  -3.616  -33.457 1   18.006 ? 171 VAL   A CG2  1 
ATOM   1349 N  N    . HIS   A 1 172 ? -11.257 -2.236  -30.469 1   13.458 ? 172 HIS   A N    1 
ATOM   1350 C  CA   . HIS   A 1 172 ? -12.381 -1.497  -29.913 1   13.851 ? 172 HIS   A CA   1 
ATOM   1351 C  C    . HIS   A 1 172 ? -12.673 -0.255  -30.74  1   13.89  ? 172 HIS   A C    1 
ATOM   1352 O  O    . HIS   A 1 172 ? -11.763 0.378   -31.273 1   15.008 ? 172 HIS   A O    1 
ATOM   1353 C  CB   . HIS   A 1 172 ? -12.079 -1.187  -28.452 1   14.409 ? 172 HIS   A CB   1 
ATOM   1354 C  CG   . HIS   A 1 172 ? -11.837 -2.448  -27.71  1   14.488 ? 172 HIS   A CG   1 
ATOM   1355 N  ND1  . HIS   A 1 172 ? -10.621 -2.836  -27.186 1   14.797 ? 172 HIS   A ND1  1 
ATOM   1356 C  CD2  . HIS   A 1 172 ? -12.705 -3.437  -27.449 1   14.508 ? 172 HIS   A CD2  1 
ATOM   1357 C  CE1  . HIS   A 1 172 ? -10.769 -4.024  -26.609 1   14.804 ? 172 HIS   A CE1  1 
ATOM   1358 N  NE2  . HIS   A 1 172 ? -12.038 -4.408  -26.765 1   15.822 ? 172 HIS   A NE2  1 
ATOM   1359 N  N    . ALA   A 1 173 ? -13.968 0.074   -30.838 1   13.648 ? 173 ALA   A N    1 
ATOM   1360 C  CA   . ALA   A 1 173 ? -14.419 1.184   -31.648 1   13.79  ? 173 ALA   A CA   1 
ATOM   1361 C  C    . ALA   A 1 173 ? -15.405 2.038   -30.86  1   12.787 ? 173 ALA   A C    1 
ATOM   1362 O  O    . ALA   A 1 173 ? -16.169 1.539   -30.024 1   13.643 ? 173 ALA   A O    1 
ATOM   1363 C  CB   . ALA   A 1 173 ? -15.063 0.664   -32.914 1   14.829 ? 173 ALA   A CB   1 
ATOM   1364 N  N    . GLY   A 1 174 ? -15.398 3.326   -31.173 1   12.685 ? 174 GLY   A N    1 
ATOM   1365 C  CA   . GLY   A 1 174 ? -16.277 4.25    -30.486 1   12.482 ? 174 GLY   A CA   1 
ATOM   1366 C  C    . GLY   A 1 174 ? -16.31  5.612   -31.158 1   12.441 ? 174 GLY   A C    1 
ATOM   1367 O  O    . GLY   A 1 174 ? -15.835 5.784   -32.282 1   13.887 ? 174 GLY   A O    1 
ATOM   1368 N  N    . THR   A 1 175 ? -16.882 6.569   -30.425 1   12.72  ? 175 THR   A N    1 
ATOM   1369 C  CA   . THR   A 1 175 ? -17.189 7.885   -30.954 1   12.983 ? 175 THR   A CA   1 
ATOM   1370 C  C    . THR   A 1 175 ? -16.465 8.957   -30.155 1   13.265 ? 175 THR   A C    1 
ATOM   1371 O  O    . THR   A 1 175 ? -15.988 8.721   -29.044 1   14.002 ? 175 THR   A O    1 
ATOM   1372 C  CB   . THR   A 1 175 ? -18.691 8.166   -30.931 1   13.549 ? 175 THR   A CB   1 
ATOM   1373 O  OG1  . THR   A 1 175 ? -19.151 8.221   -29.581 1   13.671 ? 175 THR   A OG1  1 
ATOM   1374 C  CG2  . THR   A 1 175 ? -19.486 7.13    -31.702 1   13.742 ? 175 THR   A CG2  1 
ATOM   1375 N  N    . ASP   A 1 176 ? -16.451 10.165  -30.724 1   13.636 ? 176 ASP   A N    1 
ATOM   1376 C  CA   . ASP   A 1 176 ? -16.226 11.357  -29.927 1   14.651 ? 176 ASP   A CA   1 
ATOM   1377 C  C    . ASP   A 1 176 ? -17.482 11.636  -29.092 1   14.538 ? 176 ASP   A C    1 
ATOM   1378 O  O    . ASP   A 1 176 ? -18.482 10.912  -29.171 1   14.267 ? 176 ASP   A O    1 
ATOM   1379 C  CB   . ASP   A 1 176 ? -15.739 12.493  -30.809 1   15.002 ? 176 ASP   A CB   1 
ATOM   1380 C  CG   . ASP   A 1 176 ? -16.745 13.028  -31.817 1   16.048 ? 176 ASP   A CG   1 
ATOM   1381 O  OD1  . ASP   A 1 176 ? -17.959 12.843  -31.573 1   16.32  ? 176 ASP   A OD1  1 
ATOM   1382 O  OD2  . ASP   A 1 176 ? -16.302 13.619  -32.822 1   18.023 ? 176 ASP   A OD2  1 
ATOM   1383 N  N    . LEU   A 1 177 ? -17.437 12.686  -28.265 1   14.736 ? 177 LEU   A N    1 
ATOM   1384 C  CA   . LEU   A 1 177 ? -18.553 12.969  -27.371 1   14.747 ? 177 LEU   A CA   1 
ATOM   1385 C  C    . LEU   A 1 177 ? -19.669 13.723  -28.096 1   15.742 ? 177 LEU   A C    1 
ATOM   1386 O  O    . LEU   A 1 177 ? -20.71  13.967  -27.497 1   16.803 ? 177 LEU   A O    1 
ATOM   1387 C  CB   . LEU   A 1 177 ? -18.11  13.661  -26.081 1   15.197 ? 177 LEU   A CB   1 
ATOM   1388 C  CG   . LEU   A 1 177 ? -17.781 12.721  -24.917 1   16.11  ? 177 LEU   A CG   1 
ATOM   1389 C  CD1  . LEU   A 1 177 ? -19.03  12.041  -24.387 1   16.886 ? 177 LEU   A CD1  1 
ATOM   1390 C  CD2  . LEU   A 1 177 ? -16.706 11.696  -25.307 1   16.48  ? 177 LEU   A CD2  1 
ATOM   1391 N  N    . GLU   A 1 178 ? -19.478 14.041  -29.384 1   15.817 ? 178 GLU   A N    1 
ATOM   1392 C  CA   . GLU   A 1 178 ? -20.55  14.519  -30.251 1   17.058 ? 178 GLU   A CA   1 
ATOM   1393 C  C    . GLU   A 1 178 ? -21.202 13.353  -31.002 1   16.057 ? 178 GLU   A C    1 
ATOM   1394 O  O    . GLU   A 1 178 ? -22.084 13.559  -31.84  1   17.699 ? 178 GLU   A O    1 
ATOM   1395 C  CB   . GLU   A 1 178 ? -20.009 15.582  -31.21  1   19.588 ? 178 GLU   A CB   1 
ATOM   1396 C  CG   . GLU   A 1 178 ? -19.667 16.885  -30.496 1   22.757 ? 178 GLU   A CG   1 
ATOM   1397 C  CD   . GLU   A 1 178 ? -19.247 18.05   -31.369 1   26.439 ? 178 GLU   A CD   1 
ATOM   1398 O  OE1  . GLU   A 1 178 ? -18.78  17.831  -32.497 1   29.805 ? 178 GLU   A OE1  1 
ATOM   1399 O  OE2  . GLU   A 1 178 ? -19.431 19.195  -30.919 1   31.643 ? 178 GLU   A OE2  1 
ATOM   1400 N  N    . GLY   A 1 179 ? -20.768 12.119  -30.719 1   15.645 ? 179 GLY   A N    1 
ATOM   1401 C  CA   . GLY   A 1 179 ? -21.393 10.93   -31.277 1   15.274 ? 179 GLY   A CA   1 
ATOM   1402 C  C    . GLY   A 1 179 ? -20.931 10.573  -32.688 1   15.348 ? 179 GLY   A C    1 
ATOM   1403 O  O    . GLY   A 1 179 ? -21.556 9.723   -33.32  1   15.939 ? 179 GLY   A O    1 
ATOM   1404 N  N    . ASN   A 1 180 ? -19.822 11.166  -33.161 1   15.613 ? 180 ASN   A N    1 
ATOM   1405 C  CA   . ASN   A 1 180 ? -19.257 10.814  -34.454 1   16.619 ? 180 ASN   A CA   1 
ATOM   1406 C  C    . ASN   A 1 180 ? -18.231 9.701   -34.273 1   15.112 ? 180 ASN   A C    1 
ATOM   1407 O  O    . ASN   A 1 180 ? -17.266 9.871   -33.534 1   15.136 ? 180 ASN   A O    1 
ATOM   1408 C  CB   . ASN   A 1 180 ? -18.616 12.028  -35.107 1   18.192 ? 180 ASN   A CB   1 
ATOM   1409 C  CG   . ASN   A 1 180 ? -19.634 13.086  -35.438 1   21.676 ? 180 ASN   A CG   1 
ATOM   1410 O  OD1  . ASN   A 1 180 ? -20.587 12.83   -36.184 1   25.108 ? 180 ASN   A OD1  1 
ATOM   1411 N  ND2  . ASN   A 1 180 ? -19.481 14.257  -34.842 1   24.086 ? 180 ASN   A ND2  1 
ATOM   1412 N  N    . PHE   A 1 181 ? -18.438 8.569   -34.957 1   15.069 ? 181 PHE   A N    1 
ATOM   1413 C  CA   . PHE   A 1 181 ? -17.482 7.474   -34.903 1   15.303 ? 181 PHE   A CA   1 
ATOM   1414 C  C    . PHE   A 1 181 ? -16.099 7.947   -35.338 1   15.217 ? 181 PHE   A C    1 
ATOM   1415 O  O    . PHE   A 1 181 ? -15.951 8.768   -36.241 1   16.525 ? 181 PHE   A O    1 
ATOM   1416 C  CB   . PHE   A 1 181 ? -17.887 6.261   -35.748 1   15.436 ? 181 PHE   A CB   1 
ATOM   1417 C  CG   . PHE   A 1 181 ? -18.633 5.238   -34.91  1   15.377 ? 181 PHE   A CG   1 
ATOM   1418 C  CD1  . PHE   A 1 181 ? -20.014 5.297   -34.775 1   15.836 ? 181 PHE   A CD1  1 
ATOM   1419 C  CD2  . PHE   A 1 181 ? -17.945 4.251   -34.215 1   15.399 ? 181 PHE   A CD2  1 
ATOM   1420 C  CE1  . PHE   A 1 181 ? -20.685 4.384   -33.977 1   15.732 ? 181 PHE   A CE1  1 
ATOM   1421 C  CE2  . PHE   A 1 181 ? -18.619 3.345   -33.416 1   15.745 ? 181 PHE   A CE2  1 
ATOM   1422 C  CZ   . PHE   A 1 181 ? -19.985 3.405   -33.311 1   15.599 ? 181 PHE   A CZ   1 
ATOM   1423 N  N    . TYR   A 1 182 ? -15.089 7.385   -34.668 1   14.439 ? 182 TYR   A N    1 
ATOM   1424 C  CA   . TYR   A 1 182 ? -13.746 7.318   -35.211 1   15.136 ? 182 TYR   A CA   1 
ATOM   1425 C  C    . TYR   A 1 182 ? -13.726 6.197   -36.243 1   16.627 ? 182 TYR   A C    1 
ATOM   1426 O  O    . TYR   A 1 182 ? -14.127 5.078   -35.953 1   18.189 ? 182 TYR   A O    1 
ATOM   1427 C  CB   . TYR   A 1 182 ? -12.735 7.082   -34.085 1   14.652 ? 182 TYR   A CB   1 
ATOM   1428 C  CG   . TYR   A 1 182 ? -12.585 8.286   -33.169 1   14.188 ? 182 TYR   A CG   1 
ATOM   1429 C  CD1  . TYR   A 1 182 ? -11.864 9.402   -33.578 1   14.496 ? 182 TYR   A CD1  1 
ATOM   1430 C  CD2  . TYR   A 1 182 ? -13.189 8.329   -31.914 1   13.717 ? 182 TYR   A CD2  1 
ATOM   1431 C  CE1  . TYR   A 1 182 ? -11.699 10.497  -32.747 1   14.986 ? 182 TYR   A CE1  1 
ATOM   1432 C  CE2  . TYR   A 1 182 ? -13.049 9.432   -31.083 1   13.678 ? 182 TYR   A CE2  1 
ATOM   1433 C  CZ   . TYR   A 1 182 ? -12.297 10.518  -31.499 1   14.017 ? 182 TYR   A CZ   1 
ATOM   1434 O  OH   . TYR   A 1 182 ? -12.134 11.612  -30.696 1   14.387 ? 182 TYR   A OH   1 
ATOM   1435 N  N    . GLY   A 1 183 ? -13.236 6.498   -37.445 1   18.293 ? 183 GLY   A N    1 
ATOM   1436 C  CA   . GLY   A 1 183 ? -13.132 5.477   -38.469 1   18.893 ? 183 GLY   A CA   1 
ATOM   1437 C  C    . GLY   A 1 183 ? -14.438 5.261   -39.223 1   20.353 ? 183 GLY   A C    1 
ATOM   1438 O  O    . GLY   A 1 183 ? -15.445 5.937   -38.983 1   22.823 ? 183 GLY   A O    1 
ATOM   1439 N  N    . PRO   A 1 184 ? -14.456 4.258   -40.12  1   22.015 ? 184 PRO   A N    1 
ATOM   1440 C  CA   . PRO   A 1 184 ? -15.616 4.007   -40.978 1   22.772 ? 184 PRO   A CA   1 
ATOM   1441 C  C    . PRO   A 1 184 ? -16.781 3.254   -40.334 1   23.972 ? 184 PRO   A C    1 
ATOM   1442 O  O    . PRO   A 1 184 ? -17.765 2.944   -41.001 1   26.815 ? 184 PRO   A O    1 
ATOM   1443 C  CB   . PRO   A 1 184 ? -14.939 3.238   -42.147 1   23.813 ? 184 PRO   A CB   1 
ATOM   1444 C  CG   . PRO   A 1 184 ? -13.843 2.45    -41.489 1   24.566 ? 184 PRO   A CG   1 
ATOM   1445 C  CD   . PRO   A 1 184 ? -13.316 3.382   -40.416 1   23.253 ? 184 PRO   A CD   1 
ATOM   1446 N  N    . PHE   A 1 185 ? -16.756 3.118   -39.009 1   20.862 ? 185 PHE   A N    1 
ATOM   1447 C  CA   . PHE   A 1 185 ? -17.612 2.167   -38.322 1   20.084 ? 185 PHE   A CA   1 
ATOM   1448 C  C    . PHE   A 1 185 ? -18.994 2.759   -38.082 1   20.201 ? 185 PHE   A C    1 
ATOM   1449 O  O    . PHE   A 1 185 ? -19.179 3.973   -38.116 1   21.305 ? 185 PHE   A O    1 
ATOM   1450 C  CB   . PHE   A 1 185 ? -16.946 1.741   -37.016 1   19.668 ? 185 PHE   A CB   1 
ATOM   1451 C  CG   . PHE   A 1 185 ? -15.525 1.253   -37.249 1   19.192 ? 185 PHE   A CG   1 
ATOM   1452 C  CD1  . PHE   A 1 185 ? -15.277 0.121   -38.019 1   19.469 ? 185 PHE   A CD1  1 
ATOM   1453 C  CD2  . PHE   A 1 185 ? -14.446 1.941   -36.721 1   18.641 ? 185 PHE   A CD2  1 
ATOM   1454 C  CE1  . PHE   A 1 185 ? -13.979 -0.288  -38.272 1   19.584 ? 185 PHE   A CE1  1 
ATOM   1455 C  CE2  . PHE   A 1 185 ? -13.15  1.52    -36.968 1   18.907 ? 185 PHE   A CE2  1 
ATOM   1456 C  CZ   . PHE   A 1 185 ? -12.921 0.403   -37.73  1   19.506 ? 185 PHE   A CZ   1 
ATOM   1457 N  N    . VAL   A 1 186 ? -19.948 1.847   -37.881 1   20.151 ? 186 VAL   A N    1 
ATOM   1458 C  CA   . VAL   A 1 186 ? -21.342 2.185   -37.648 1   19.687 ? 186 VAL   A CA   1 
ATOM   1459 C  C    . VAL   A 1 186 ? -21.848 1.39    -36.446 1   17.668 ? 186 VAL   A C    1 
ATOM   1460 O  O    . VAL   A 1 186 ? -21.358 0.302   -36.158 1   17.715 ? 186 VAL   A O    1 
ATOM   1461 C  CB   . VAL   A 1 186 ? -22.2   1.909   -38.898 1   21.12  ? 186 VAL   A CB   1 
ATOM   1462 C  CG1  . VAL   A 1 186 ? -21.814 2.837   -40.04  1   21.392 ? 186 VAL   A CG1  1 
ATOM   1463 C  CG2  . VAL   A 1 186 ? -22.127 0.452   -39.342 1   22.364 ? 186 VAL   A CG2  1 
ATOM   1464 N  N    . ASP   A 1 187 ? -22.867 1.929   -35.767 1   16.979 ? 187 ASP   A N    1 
ATOM   1465 C  CA   . ASP   A 1 187 ? -23.457 1.265   -34.607 1   16.634 ? 187 ASP   A CA   1 
ATOM   1466 C  C    . ASP   A 1 187 ? -24.563 0.302   -35.052 1   17.271 ? 187 ASP   A C    1 
ATOM   1467 O  O    . ASP   A 1 187 ? -25.745 0.459   -34.704 1   18.573 ? 187 ASP   A O    1 
ATOM   1468 C  CB   . ASP   A 1 187 ? -23.875 2.259   -33.536 1   16.917 ? 187 ASP   A CB   1 
ATOM   1469 C  CG   . ASP   A 1 187 ? -24.762 3.419   -33.953 1   16.24  ? 187 ASP   A CG   1 
ATOM   1470 O  OD1  . ASP   A 1 187 ? -25.05  3.572   -35.167 1   17.125 ? 187 ASP   A OD1  1 
ATOM   1471 O  OD2  . ASP   A 1 187 ? -25.135 4.178   -33.045 1   16.119 ? 187 ASP   A OD2  1 
ATOM   1472 N  N    . ARG   A 1 188 ? -24.134 -0.698  -35.834 1   18.438 ? 188 ARG   A N    1 
ATOM   1473 C  CA   . ARG   A 1 188 ? -24.95  -1.793  -36.337 1   21.374 ? 188 ARG   A CA   1 
ATOM   1474 C  C    . ARG   A 1 188 ? -24.079 -3.045  -36.277 1   20.464 ? 188 ARG   A C    1 
ATOM   1475 O  O    . ARG   A 1 188 ? -22.878 -2.964  -36.534 1   20.458 ? 188 ARG   A O    1 
ATOM   1476 C  CB   . ARG   A 1 188 ? -25.382 -1.756  -37.82  1   24.487 ? 188 ARG   A CB   1 
ATOM   1477 C  CG   . ARG   A 1 188 ? -25.999 -0.503  -38.412 1   26.988 ? 188 ARG   A CG   1 
ATOM   1478 C  CD   . ARG   A 1 188 ? -25.957 -0.422  -39.943 1   25.233 ? 188 ARG   A CD   1 
ATOM   1479 N  NE   . ARG   A 1 188 ? -26.366 -1.568  -40.768 1   23.708 ? 188 ARG   A NE   1 
ATOM   1480 C  CZ   . ARG   A 1 188 ? -26.112 -1.688  -42.079 1   24.979 ? 188 ARG   A CZ   1 
ATOM   1481 N  NH1  . ARG   A 1 188 ? -25.386 -0.776  -42.708 1   24.754 ? 188 ARG   A NH1  1 
ATOM   1482 N  NH2  . ARG   A 1 188 ? -26.546 -2.737  -42.758 1   25.299 ? 188 ARG   A NH2  1 
ATOM   1483 N  N    . GLN   A 1 189 ? -24.688 -4.205  -36.007 1   21.559 ? 189 GLN   A N    1 
ATOM   1484 C  CA   . GLN   A 1 189 ? -23.968 -5.473  -35.927 1   24.325 ? 189 GLN   A CA   1 
ATOM   1485 C  C    . GLN   A 1 189 ? -23.823 -6.125  -37.307 1   28.675 ? 189 GLN   A C    1 
ATOM   1486 O  O    . GLN   A 1 189 ? -24.024 -7.334  -37.462 1   34.186 ? 189 GLN   A O    1 
ATOM   1487 C  CB   . GLN   A 1 189 ? -24.7   -6.321  -34.886 1   28.974 ? 189 GLN   A CB   1 
ATOM   1488 C  CG   . GLN   A 1 189 ? -23.938 -7.517  -34.33  1   32.803 ? 189 GLN   A CG   1 
ATOM   1489 C  CD   . GLN   A 1 189 ? -24.663 -8.124  -33.148 1   35.065 ? 189 GLN   A CD   1 
ATOM   1490 O  OE1  . GLN   A 1 189 ? -25.896 -8.23   -33.138 1   36.883 ? 189 GLN   A OE1  1 
ATOM   1491 N  NE2  . GLN   A 1 189 ? -23.912 -8.49   -32.12  1   34.753 ? 189 GLN   A NE2  1 
ATOM   1492 N  N    . THR   A 1 190 ? -23.387 -5.331  -38.296 1   28.243 ? 190 THR   A N    1 
ATOM   1493 C  CA   . THR   A 1 190 ? -23.14  -5.768  -39.661 1   30.566 ? 190 THR   A CA   1 
ATOM   1494 C  C    . THR   A 1 190 ? -21.644 -6.013  -39.812 1   31.05  ? 190 THR   A C    1 
ATOM   1495 O  O    . THR   A 1 190 ? -20.848 -5.552  -38.992 1   31.823 ? 190 THR   A O    1 
ATOM   1496 C  CB   . THR   A 1 190 ? -23.653 -4.686  -40.615 1   31.688 ? 190 THR   A CB   1 
ATOM   1497 O  OG1  . THR   A 1 190 ? -23.695 -5.22   -41.935 1   34.497 ? 190 THR   A OG1  1 
ATOM   1498 C  CG2  . THR   A 1 190 ? -22.818 -3.419  -40.584 1   31.003 ? 190 THR   A CG2  1 
ATOM   1499 N  N    . ALA   A 1 191 ? -21.266 -6.751  -40.855 1   33.197 ? 191 ALA   A N    1 
ATOM   1500 C  CA   . ALA   A 1 191 ? -19.864 -6.995  -41.144 1   35.095 ? 191 ALA   A CA   1 
ATOM   1501 C  C    . ALA   A 1 191 ? -19.179 -5.656  -41.374 1   33.807 ? 191 ALA   A C    1 
ATOM   1502 O  O    . ALA   A 1 191 ? -19.571 -4.861  -42.224 1   38.592 ? 191 ALA   A O    1 
ATOM   1503 C  CB   . ALA   A 1 191 ? -19.688 -7.904  -42.337 1   37.145 ? 191 ALA   A CB   1 
ATOM   1504 N  N    . GLN   A 1 192 ? -18.202 -5.385  -40.519 1   35.437 ? 192 GLN   A N    1 
ATOM   1505 C  CA   . GLN   A 1 192 ? -17.307 -4.268  -40.69  1   32.617 ? 192 GLN   A CA   1 
ATOM   1506 C  C    . GLN   A 1 192 ? -15.977 -4.812  -40.202 1   37.064 ? 192 GLN   A C    1 
ATOM   1507 O  O    . GLN   A 1 192 ? -15.933 -5.652  -39.296 1   38.55  ? 192 GLN   A O    1 
ATOM   1508 C  CB   . GLN   A 1 192 ? -17.725 -2.973  -39.988 1   34.074 ? 192 GLN   A CB   1 
ATOM   1509 C  CG   . GLN   A 1 192 ? -18.35  -3.138  -38.606 1   32.033 ? 192 GLN   A CG   1 
ATOM   1510 C  CD   . GLN   A 1 192 ? -19.129 -1.916  -38.148 1   29.44  ? 192 GLN   A CD   1 
ATOM   1511 O  OE1  . GLN   A 1 192 ? -18.812 -0.783  -38.504 1   29.976 ? 192 GLN   A OE1  1 
ATOM   1512 N  NE2  . GLN   A 1 192 ? -20.18  -2.126  -37.375 1   26.634 ? 192 GLN   A NE2  1 
ATOM   1513 N  N    . ALA   A 1 193 ? -14.924 -4.383  -40.892 1   37.978 ? 193 ALA   A N    1 
ATOM   1514 C  CA   . ALA   A 1 193 ? -13.574 -4.715  -40.502 1   37.471 ? 193 ALA   A CA   1 
ATOM   1515 C  C    . ALA   A 1 193 ? -12.727 -3.449  -40.554 1   37.572 ? 193 ALA   A C    1 
ATOM   1516 O  O    . ALA   A 1 193 ? -12.886 -2.607  -41.438 1   38.435 ? 193 ALA   A O    1 
ATOM   1517 C  CB   . ALA   A 1 193 ? -13.029 -5.8    -41.39  1   38.633 ? 193 ALA   A CB   1 
ATOM   1518 N  N    . ALA   A 1 194 ? -11.852 -3.335  -39.56  1   36.653 ? 194 ALA   A N    1 
ATOM   1519 C  CA   . ALA   A 1 194 ? -10.859 -2.284  -39.536 1   35.42  ? 194 ALA   A CA   1 
ATOM   1520 C  C    . ALA   A 1 194 ? -9.884  -2.509  -40.685 1   36.072 ? 194 ALA   A C    1 
ATOM   1521 O  O    . ALA   A 1 194 ? -9.615  -3.651  -41.067 1   35.877 ? 194 ALA   A O    1 
ATOM   1522 C  CB   . ALA   A 1 194 ? -10.16  -2.291  -38.199 1   36.612 ? 194 ALA   A CB   1 
ATOM   1523 N  N    . GLY   A 1 195 ? -9.372  -1.401  -41.232 1   34.332 ? 195 GLY   A N    1 
ATOM   1524 C  CA   . GLY   A 1 195 ? -8.25   -1.45   -42.15  1   34.016 ? 195 GLY   A CA   1 
ATOM   1525 C  C    . GLY   A 1 195 ? -7.022  -2.048  -41.472 1   31.73  ? 195 GLY   A C    1 
ATOM   1526 O  O    . GLY   A 1 195 ? -6.934  -2.088  -40.249 1   31.225 ? 195 GLY   A O    1 
ATOM   1527 N  N    . THR   A 1 196 ? -6.083  -2.544  -42.281 1   31.064 ? 196 THR   A N    1 
ATOM   1528 C  CA   . THR   A 1 196 ? -4.831  -3.053  -41.754 1   30.071 ? 196 THR   A CA   1 
ATOM   1529 C  C    . THR   A 1 196 ? -4.168  -1.926  -40.973 1   27.461 ? 196 THR   A C    1 
ATOM   1530 O  O    . THR   A 1 196 ? -4.059  -0.804  -41.457 1   30.419 ? 196 THR   A O    1 
ATOM   1531 C  CB   . THR   A 1 196 ? -3.952  -3.55   -42.898 1   32.891 ? 196 THR   A CB   1 
ATOM   1532 O  OG1  . THR   A 1 196 ? -3.809  -2.416  -43.751 1   39.413 ? 196 THR   A OG1  1 
ATOM   1533 C  CG2  . THR   A 1 196 ? -4.58   -4.717  -43.64  1   32.733 ? 196 THR   A CG2  1 
ATOM   1534 N  N    . ASP   A 1 197 ? -3.752  -2.226  -39.749 1   24.798 ? 197 ASP   A N    1 
ATOM   1535 C  CA   . ASP   A 1 197 ? -3.165  -1.201  -38.924 1   23.568 ? 197 ASP   A CA   1 
ATOM   1536 C  C    . ASP   A 1 197 ? -1.684  -1.056  -39.255 1   22.369 ? 197 ASP   A C    1 
ATOM   1537 O  O    . ASP   A 1 197 ? -1.07   -1.946  -39.846 1   24.13  ? 197 ASP   A O    1 
ATOM   1538 C  CB   . ASP   A 1 197 ? -3.342  -1.503  -37.456 1   23.453 ? 197 ASP   A CB   1 
ATOM   1539 C  CG   . ASP   A 1 197 ? -3.236  -0.269  -36.58  1   23.296 ? 197 ASP   A CG   1 
ATOM   1540 O  OD1  . ASP   A 1 197 ? -3.513  0.86    -37.103 1   23.316 ? 197 ASP   A OD1  1 
ATOM   1541 O  OD2  . ASP   A 1 197 ? -2.882  -0.456  -35.414 1   23.709 ? 197 ASP   A OD2  1 
ATOM   1542 N  N    . THR   A 1 198 ? -1.154  0.107   -38.875 1   18.906 ? 198 THR   A N    1 
ATOM   1543 C  CA   . THR   A 1 198 ? 0.232   0.451   -39.097 1   17.113 ? 198 THR   A CA   1 
ATOM   1544 C  C    . THR   A 1 198 ? 0.811   0.997   -37.797 1   15.364 ? 198 THR   A C    1 
ATOM   1545 O  O    . THR   A 1 198 ? 0.095   1.311   -36.859 1   15.609 ? 198 THR   A O    1 
ATOM   1546 C  CB   . THR   A 1 198 ? 0.335   1.456   -40.244 1   18.802 ? 198 THR   A CB   1 
ATOM   1547 O  OG1  . THR   A 1 198 ? -0.558  2.518   -39.924 1   20.474 ? 198 THR   A OG1  1 
ATOM   1548 C  CG2  . THR   A 1 198 ? -0.009  0.836   -41.588 1   20.249 ? 198 THR   A CG2  1 
ATOM   1549 N  N    . THR   A 1 199 ? 2.14    1.117   -37.769 1   14.279 ? 199 THR   A N    1 
ATOM   1550 C  CA   . THR   A 1 199 ? 2.857   1.611   -36.603 1   14.414 ? 199 THR   A CA   1 
ATOM   1551 C  C    . THR   A 1 199 ? 2.95    3.135   -36.655 1   13.97  ? 199 THR   A C    1 
ATOM   1552 O  O    . THR   A 1 199 ? 3.182   3.715   -37.716 1   14.518 ? 199 THR   A O    1 
ATOM   1553 C  CB   . THR   A 1 199 ? 4.237   0.955   -36.528 1   14.831 ? 199 THR   A CB   1 
ATOM   1554 O  OG1  . THR   A 1 199 ? 4.026   -0.447  -36.41  1   16.384 ? 199 THR   A OG1  1 
ATOM   1555 C  CG2  . THR   A 1 199 ? 5.046   1.437   -35.337 1   15.083 ? 199 THR   A CG2  1 
ATOM   1556 N  N    . ILE   A 1 200 ? 2.762   3.774   -35.491 1   13.576 ? 200 ILE   A N    1 
ATOM   1557 C  CA   . ILE   A 1 200 ? 2.734   5.225   -35.4   1   13.279 ? 200 ILE   A CA   1 
ATOM   1558 C  C    . ILE   A 1 200 ? 4.165   5.755   -35.287 1   13.024 ? 200 ILE   A C    1 
ATOM   1559 O  O    . ILE   A 1 200 ? 4.733   5.844   -34.191 1   13.002 ? 200 ILE   A O    1 
ATOM   1560 C  CB   . ILE   A 1 200 ? 1.867   5.698   -34.225 1   13.565 ? 200 ILE   A CB   1 
ATOM   1561 C  CG1  . ILE   A 1 200 ? 0.478   5.063   -34.241 1   14.207 ? 200 ILE   A CG1  1 
ATOM   1562 C  CG2  . ILE   A 1 200 ? 1.782   7.221   -34.221 1   13.607 ? 200 ILE   A CG2  1 
ATOM   1563 C  CD1  . ILE   A 1 200 ? -0.208  5.055   -32.891 1   14.161 ? 200 ILE   A CD1  1 
ATOM   1564 N  N    . THR   A 1 201 ? 4.746   6.103   -36.441 1   12.917 ? 201 THR   A N    1 
ATOM   1565 C  CA   . THR   A 1 201 ? 6.171   6.378   -36.556 1   12.911 ? 201 THR   A CA   1 
ATOM   1566 C  C    . THR   A 1 201 ? 6.598   7.526   -35.639 1   12.729 ? 201 THR   A C    1 
ATOM   1567 O  O    . THR   A 1 201 ? 7.624   7.439   -34.96  1   13.11  ? 201 THR   A O    1 
ATOM   1568 C  CB   . THR   A 1 201 ? 6.478   6.702   -38.017 1   13.508 ? 201 THR   A CB   1 
ATOM   1569 O  OG1  . THR   A 1 201 ? 5.947   5.619   -38.777 1   14.284 ? 201 THR   A OG1  1 
ATOM   1570 C  CG2  . THR   A 1 201 ? 7.967   6.879   -38.26  1   14.017 ? 201 THR   A CG2  1 
ATOM   1571 N  N    . VAL   A 1 202 ? 5.85    8.632   -35.642 1   12.668 ? 202 VAL   A N    1 
ATOM   1572 C  CA   . VAL   A 1 202 ? 6.222   9.783   -34.843 1   13.186 ? 202 VAL   A CA   1 
ATOM   1573 C  C    . VAL   A 1 202 ? 6.326   9.407   -33.365 1   13.031 ? 202 VAL   A C    1 
ATOM   1574 O  O    . VAL   A 1 202 ? 7.164   9.94    -32.644 1   13.307 ? 202 VAL   A O    1 
ATOM   1575 C  CB   . VAL   A 1 202 ? 5.27    10.97   -35.072 1   13.838 ? 202 VAL   A CB   1 
ATOM   1576 C  CG1  . VAL   A 1 202 ? 3.826   10.687  -34.671 1   14.713 ? 202 VAL   A CG1  1 
ATOM   1577 C  CG2  . VAL   A 1 202 ? 5.795   12.234  -34.397 1   14.627 ? 202 VAL   A CG2  1 
ATOM   1578 N  N    . ASN   A 1 203 ? 5.448   8.515   -32.903 1   12.701 ? 203 ASN   A N    1 
ATOM   1579 C  CA   . ASN   A 1 203 ? 5.45    8.084   -31.517 1   12.477 ? 203 ASN   A CA   1 
ATOM   1580 C  C    . ASN   A 1 203 ? 6.67    7.211   -31.212 1   12.52  ? 203 ASN   A C    1 
ATOM   1581 O  O    . ASN   A 1 203 ? 7.272   7.31    -30.137 1   13.197 ? 203 ASN   A O    1 
ATOM   1582 C  CB   . ASN   A 1 203 ? 4.158   7.349   -31.169 1   12.389 ? 203 ASN   A CB   1 
ATOM   1583 C  CG   . ASN   A 1 203 ? 2.963   8.268   -31.07  1   12.482 ? 203 ASN   A CG   1 
ATOM   1584 O  OD1  . ASN   A 1 203 ? 3.069   9.477   -31.293 1   12.814 ? 203 ASN   A OD1  1 
ATOM   1585 N  ND2  . ASN   A 1 203 ? 1.822   7.699   -30.711 1   12.891 ? 203 ASN   A ND2  1 
ATOM   1586 N  N    . VAL   A 1 204 ? 7.044   6.325   -32.139 1   12.376 ? 204 VAL   A N    1 
ATOM   1587 C  CA   . VAL   A 1 204 ? 8.251   5.527   -31.932 1   12.278 ? 204 VAL   A CA   1 
ATOM   1588 C  C    . VAL   A 1 204 ? 9.46    6.455   -31.77  1   12.212 ? 204 VAL   A C    1 
ATOM   1589 O  O    . VAL   A 1 204 ? 10.3    6.265   -30.883 1   12.185 ? 204 VAL   A O    1 
ATOM   1590 C  CB   . VAL   A 1 204 ? 8.494   4.504   -33.056 1   12.652 ? 204 VAL   A CB   1 
ATOM   1591 C  CG1  . VAL   A 1 204 ? 9.806   3.766   -32.832 1   12.86  ? 204 VAL   A CG1  1 
ATOM   1592 C  CG2  . VAL   A 1 204 ? 7.351   3.507   -33.183 1   13.052 ? 204 VAL   A CG2  1 
ATOM   1593 N  N    . LEU   A 1 205 ? 9.558   7.467   -32.63  1   12.124 ? 205 LEU   A N    1 
ATOM   1594 C  CA   . LEU   A 1 205 ? 10.654  8.42    -32.539 1   12.512 ? 205 LEU   A CA   1 
ATOM   1595 C  C    . LEU   A 1 205 ? 10.63   9.133   -31.189 1   12.623 ? 205 LEU   A C    1 
ATOM   1596 O  O    . LEU   A 1 205 ? 11.665  9.278   -30.547 1   13.257 ? 205 LEU   A O    1 
ATOM   1597 C  CB   . LEU   A 1 205 ? 10.603  9.395   -33.711 1   12.851 ? 205 LEU   A CB   1 
ATOM   1598 C  CG   . LEU   A 1 205 ? 10.897  8.76    -35.076 1   13.146 ? 205 LEU   A CG   1 
ATOM   1599 C  CD1  . LEU   A 1 205 ? 10.5    9.705   -36.186 1   13.706 ? 205 LEU   A CD1  1 
ATOM   1600 C  CD2  . LEU   A 1 205 ? 12.364  8.372   -35.204 1   13.656 ? 205 LEU   A CD2  1 
ATOM   1601 N  N    . ALA   A 1 206 ? 9.441   9.546   -30.724 1   12.717 ? 206 ALA   A N    1 
ATOM   1602 C  CA   . ALA   A 1 206 ? 9.32    10.209  -29.433 1   13.011 ? 206 ALA   A CA   1 
ATOM   1603 C  C    . ALA   A 1 206 ? 9.874   9.324   -28.317 1   12.714 ? 206 ALA   A C    1 
ATOM   1604 O  O    . ALA   A 1 206 ? 10.574  9.791   -27.421 1   12.956 ? 206 ALA   A O    1 
ATOM   1605 C  CB   . ALA   A 1 206 ? 7.877   10.554  -29.161 1   13.27  ? 206 ALA   A CB   1 
ATOM   1606 N  N    . TRP   A 1 207 ? 9.542   8.038   -28.365 1   12.89  ? 207 TRP   A N    1 
ATOM   1607 C  CA   . TRP   A 1 207 ? 9.955   7.085   -27.345 1   12.895 ? 207 TRP   A CA   1 
ATOM   1608 C  C    . TRP   A 1 207 ? 11.466  6.832   -27.401 1   12.513 ? 207 TRP   A C    1 
ATOM   1609 O  O    . TRP   A 1 207 ? 12.099  6.671   -26.355 1   12.799 ? 207 TRP   A O    1 
ATOM   1610 C  CB   . TRP   A 1 207 ? 9.091   5.832   -27.525 1   13.532 ? 207 TRP   A CB   1 
ATOM   1611 C  CG   . TRP   A 1 207 ? 9.481   4.616   -26.747 1   14.212 ? 207 TRP   A CG   1 
ATOM   1612 C  CD1  . TRP   A 1 207 ? 9.148   4.255   -25.472 1   15.221 ? 207 TRP   A CD1  1 
ATOM   1613 C  CD2  . TRP   A 1 207 ? 10.198  3.515   -27.312 1   15.338 ? 207 TRP   A CD2  1 
ATOM   1614 N  NE1  . TRP   A 1 207 ? 9.659   3.016   -25.194 1   15.977 ? 207 TRP   A NE1  1 
ATOM   1615 C  CE2  . TRP   A 1 207 ? 10.304  2.534   -26.305 1   16.009 ? 207 TRP   A CE2  1 
ATOM   1616 C  CE3  . TRP   A 1 207 ? 10.757  3.286   -28.57  1   15.816 ? 207 TRP   A CE3  1 
ATOM   1617 C  CZ2  . TRP   A 1 207 ? 10.952  1.324   -26.543 1   16.653 ? 207 TRP   A CZ2  1 
ATOM   1618 C  CZ3  . TRP   A 1 207 ? 11.385  2.087   -28.797 1   17.324 ? 207 TRP   A CZ3  1 
ATOM   1619 C  CH2  . TRP   A 1 207 ? 11.478  1.125   -27.798 1   16.699 ? 207 TRP   A CH2  1 
ATOM   1620 N  N    . LEU   A 1 208 ? 12.062  6.828   -28.602 1   12.571 ? 208 LEU   A N    1 
ATOM   1621 C  CA   . LEU   A 1 208 ? 13.515  6.766   -28.702 1   12.842 ? 208 LEU   A CA   1 
ATOM   1622 C  C    . LEU   A 1 208 ? 14.153  7.988   -28.042 1   13.091 ? 208 LEU   A C    1 
ATOM   1623 O  O    . LEU   A 1 208 ? 15.178  7.866   -27.362 1   13.477 ? 208 LEU   A O    1 
ATOM   1624 C  CB   . LEU   A 1 208 ? 13.941  6.621   -30.164 1   13.237 ? 208 LEU   A CB   1 
ATOM   1625 C  CG   . LEU   A 1 208 ? 13.605  5.273   -30.811 1   13.416 ? 208 LEU   A CG   1 
ATOM   1626 C  CD1  . LEU   A 1 208 ? 13.988  5.305   -32.291 1   14.114 ? 208 LEU   A CD1  1 
ATOM   1627 C  CD2  . LEU   A 1 208 ? 14.282  4.101   -30.11  1   14.338 ? 208 LEU   A CD2  1 
ATOM   1628 N  N    . TYR   A 1 209 ? 13.565  9.17    -28.249 1   12.636 ? 209 TYR   A N    1 
ATOM   1629 C  CA   . TYR   A 1 209 ? 14.04   10.361  -27.557 1   13.026 ? 209 TYR   A CA   1 
ATOM   1630 C  C    . TYR   A 1 209 ? 13.916  10.191  -26.041 1   13.443 ? 209 TYR   A C    1 
ATOM   1631 O  O    . TYR   A 1 209 ? 14.818  10.599  -25.301 1   14.36  ? 209 TYR   A O    1 
ATOM   1632 C  CB   . TYR   A 1 209 ? 13.313  11.624  -28.027 1   13.259 ? 209 TYR   A CB   1 
ATOM   1633 C  CG   . TYR   A 1 209 ? 13.845  12.196  -29.335 1   13.708 ? 209 TYR   A CG   1 
ATOM   1634 C  CD1  . TYR   A 1 209 ? 15.091  12.801  -29.384 1   13.907 ? 209 TYR   A CD1  1 
ATOM   1635 C  CD2  . TYR   A 1 209 ? 13.104  12.149  -30.506 1   13.983 ? 209 TYR   A CD2  1 
ATOM   1636 C  CE1  . TYR   A 1 209 ? 15.595  13.331  -30.559 1   14.31  ? 209 TYR   A CE1  1 
ATOM   1637 C  CE2  . TYR   A 1 209 ? 13.585  12.697  -31.683 1   14.437 ? 209 TYR   A CE2  1 
ATOM   1638 C  CZ   . TYR   A 1 209 ? 14.84   13.289  -31.715 1   14.426 ? 209 TYR   A CZ   1 
ATOM   1639 O  OH   . TYR   A 1 209 ? 15.327  13.834  -32.874 1   15.089 ? 209 TYR   A OH   1 
ATOM   1640 N  N    . ALA   A 1 210 ? 12.804  9.61    -25.568 1   13.235 ? 210 ALA   A N    1 
ATOM   1641 C  CA   . ALA   A 1 210 ? 12.642  9.348   -24.144 1   13.452 ? 210 ALA   A CA   1 
ATOM   1642 C  C    . ALA   A 1 210 ? 13.774  8.47    -23.627 1   13.421 ? 210 ALA   A C    1 
ATOM   1643 O  O    . ALA   A 1 210 ? 14.3    8.708   -22.542 1   13.739 ? 210 ALA   A O    1 
ATOM   1644 C  CB   . ALA   A 1 210 ? 11.307  8.693   -23.85  1   13.321 ? 210 ALA   A CB   1 
ATOM   1645 N  N    . ALA   A 1 211 ? 14.161  7.465   -24.421 1   12.752 ? 211 ALA   A N    1 
ATOM   1646 C  CA   . ALA   A 1 211 ? 15.231  6.568   -24.012 1   13.232 ? 211 ALA   A CA   1 
ATOM   1647 C  C    . ALA   A 1 211 ? 16.554  7.33    -23.874 1   13.35  ? 211 ALA   A C    1 
ATOM   1648 O  O    . ALA   A 1 211 ? 17.301  7.111   -22.918 1   13.94  ? 211 ALA   A O    1 
ATOM   1649 C  CB   . ALA   A 1 211 ? 15.342  5.427   -24.987 1   13.27  ? 211 ALA   A CB   1 
ATOM   1650 N  N    . VAL   A 1 212 ? 16.831  8.249   -24.802 1   13.468 ? 212 VAL   A N    1 
ATOM   1651 C  CA   . VAL   A 1 212 ? 18.041  9.054   -24.716 1   13.938 ? 212 VAL   A CA   1 
ATOM   1652 C  C    . VAL   A 1 212 ? 17.981  9.948   -23.474 1   14.271 ? 212 VAL   A C    1 
ATOM   1653 O  O    . VAL   A 1 212 ? 18.958  10.075  -22.732 1   14.269 ? 212 VAL   A O    1 
ATOM   1654 C  CB   . VAL   A 1 212 ? 18.294  9.867   -26     1   13.886 ? 212 VAL   A CB   1 
ATOM   1655 C  CG1  . VAL   A 1 212 ? 19.474  10.813  -25.827 1   14.615 ? 212 VAL   A CG1  1 
ATOM   1656 C  CG2  . VAL   A 1 212 ? 18.506  8.961   -27.209 1   14.057 ? 212 VAL   A CG2  1 
ATOM   1657 N  N    . ILE   A 1 213 ? 16.842  10.606  -23.244 1   14.436 ? 213 ILE   A N    1 
ATOM   1658 C  CA   . ILE   A 1 213 ? 16.694  11.489  -22.093 1   15.123 ? 213 ILE   A CA   1 
ATOM   1659 C  C    . ILE   A 1 213 ? 17.001  10.712  -20.814 1   15.533 ? 213 ILE   A C    1 
ATOM   1660 O  O    . ILE   A 1 213 ? 17.643  11.238  -19.901 1   16.889 ? 213 ILE   A O    1 
ATOM   1661 C  CB   . ILE   A 1 213 ? 15.289  12.126  -22.06  1   15.676 ? 213 ILE   A CB   1 
ATOM   1662 C  CG1  . ILE   A 1 213 ? 15.129  13.135  -23.19  1   16.517 ? 213 ILE   A CG1  1 
ATOM   1663 C  CG2  . ILE   A 1 213 ? 15.009  12.756  -20.693 1   16.498 ? 213 ILE   A CG2  1 
ATOM   1664 C  CD1  . ILE   A 1 213 ? 13.697  13.551  -23.453 1   17.462 ? 213 ILE   A CD1  1 
ATOM   1665 N  N    . ASN   A 1 214 ? 16.57   9.446   -20.769 1   15.26  ? 214 ASN   A N    1 
ATOM   1666 C  CA   . ASN   A 1 214 ? 16.741  8.618   -19.591 1   16.586 ? 214 ASN   A CA   1 
ATOM   1667 C  C    . ASN   A 1 214 ? 18.095  7.916   -19.547 1   16.751 ? 214 ASN   A C    1 
ATOM   1668 O  O    . ASN   A 1 214 ? 18.353  7.202   -18.587 1   18.825 ? 214 ASN   A O    1 
ATOM   1669 C  CB   . ASN   A 1 214 ? 15.579  7.652   -19.449 1   17.571 ? 214 ASN   A CB   1 
ATOM   1670 C  CG   . ASN   A 1 214 ? 14.352  8.361   -18.932 1   20.005 ? 214 ASN   A CG   1 
ATOM   1671 O  OD1  . ASN   A 1 214 ? 14.25   9.594   -18.989 1   21.381 ? 214 ASN   A OD1  1 
ATOM   1672 N  ND2  . ASN   A 1 214 ? 13.409  7.586   -18.436 1   22.49  ? 214 ASN   A ND2  1 
ATOM   1673 N  N    . GLY   A 1 215 ? 18.966  8.149   -20.534 1   16.163 ? 215 GLY   A N    1 
ATOM   1674 C  CA   . GLY   A 1 215 ? 20.371  7.822   -20.372 1   16.026 ? 215 GLY   A CA   1 
ATOM   1675 C  C    . GLY   A 1 215 ? 20.906  6.777   -21.348 1   16.638 ? 215 GLY   A C    1 
ATOM   1676 O  O    . GLY   A 1 215 ? 22.047  6.369   -21.178 1   19.482 ? 215 GLY   A O    1 
ATOM   1677 N  N    . ASP   A 1 216 ? 20.138  6.361   -22.365 1   15.032 ? 216 ASP   A N    1 
ATOM   1678 C  CA   . ASP   A 1 216 ? 20.545  5.258   -23.225 1   16.831 ? 216 ASP   A CA   1 
ATOM   1679 C  C    . ASP   A 1 216 ? 20.73   5.749   -24.659 1   16.317 ? 216 ASP   A C    1 
ATOM   1680 O  O    . ASP   A 1 216 ? 19.838  6.382   -25.206 1   17.763 ? 216 ASP   A O    1 
ATOM   1681 C  CB   . ASP   A 1 216 ? 19.5    4.157   -23.138 1   19.794 ? 216 ASP   A CB   1 
ATOM   1682 C  CG   . ASP   A 1 216 ? 19.907  2.757   -23.546 1   23.426 ? 216 ASP   A CG   1 
ATOM   1683 O  OD1  . ASP   A 1 216 ? 21.082  2.582   -23.911 1   26.902 ? 216 ASP   A OD1  1 
ATOM   1684 O  OD2  . ASP   A 1 216 ? 19.031  1.856   -23.488 1   28.376 ? 216 ASP   A OD2  1 
ATOM   1685 N  N    . ARG   A 1 217 ? 21.862  5.368   -25.284 1   15.749 ? 217 ARG   A N    1 
ATOM   1686 C  CA   . ARG   A 1 217 ? 22.239  5.815   -26.619 1   16.057 ? 217 ARG   A CA   1 
ATOM   1687 C  C    . ARG   A 1 217 ? 22.657  4.666   -27.533 1   15.704 ? 217 ARG   A C    1 
ATOM   1688 O  O    . ARG   A 1 217 ? 23.126  4.932   -28.645 1   15.926 ? 217 ARG   A O    1 
ATOM   1689 C  CB   . ARG   A 1 217 ? 23.456  6.752   -26.526 1   16.896 ? 217 ARG   A CB   1 
ATOM   1690 C  CG   . ARG   A 1 217 ? 23.143  8.085   -25.872 1   17.712 ? 217 ARG   A CG   1 
ATOM   1691 C  CD   . ARG   A 1 217 ? 24.339  9.012   -25.831 1   17.466 ? 217 ARG   A CD   1 
ATOM   1692 N  NE   . ARG   A 1 217 ? 24.826  9.353   -27.169 1   16.472 ? 217 ARG   A NE   1 
ATOM   1693 C  CZ   . ARG   A 1 217 ? 24.569  10.47   -27.838 1   16.048 ? 217 ARG   A CZ   1 
ATOM   1694 N  NH1  . ARG   A 1 217 ? 23.765  11.405  -27.34  1   16.45  ? 217 ARG   A NH1  1 
ATOM   1695 N  NH2  . ARG   A 1 217 ? 25.075  10.626  -29.048 1   16.723 ? 217 ARG   A NH2  1 
ATOM   1696 N  N    . TRP   A 1 218 ? 22.524  3.409   -27.081 1   15.154 ? 218 TRP   A N    1 
ATOM   1697 C  CA   . TRP   A 1 218 ? 23.184  2.293   -27.755 1   15.535 ? 218 TRP   A CA   1 
ATOM   1698 C  C    . TRP   A 1 218 ? 22.744  2.157   -29.214 1   14.707 ? 218 TRP   A C    1 
ATOM   1699 O  O    . TRP   A 1 218 ? 23.501  1.636   -30.036 1   14.85  ? 218 TRP   A O    1 
ATOM   1700 C  CB   . TRP   A 1 218 ? 22.983  0.963   -27.004 1   16.265 ? 218 TRP   A CB   1 
ATOM   1701 C  CG   . TRP   A 1 218 ? 21.586  0.388   -26.971 1   16.969 ? 218 TRP   A CG   1 
ATOM   1702 C  CD1  . TRP   A 1 218 ? 20.707  0.429   -25.924 1   18.225 ? 218 TRP   A CD1  1 
ATOM   1703 C  CD2  . TRP   A 1 218 ? 20.92   -0.364  -28.009 1   16.813 ? 218 TRP   A CD2  1 
ATOM   1704 N  NE1  . TRP   A 1 218 ? 19.554  -0.241  -26.234 1   18.751 ? 218 TRP   A NE1  1 
ATOM   1705 C  CE2  . TRP   A 1 218 ? 19.64   -0.721  -27.512 1   17.938 ? 218 TRP   A CE2  1 
ATOM   1706 C  CE3  . TRP   A 1 218 ? 21.256  -0.747  -29.31  1   17.838 ? 218 TRP   A CE3  1 
ATOM   1707 C  CZ2  . TRP   A 1 218 ? 18.728  -1.453  -28.269 1   18.422 ? 218 TRP   A CZ2  1 
ATOM   1708 C  CZ3  . TRP   A 1 218 ? 20.344  -1.46   -30.061 1   18.397 ? 218 TRP   A CZ3  1 
ATOM   1709 C  CH2  . TRP   A 1 218 ? 19.105  -1.815  -29.541 1   18.469 ? 218 TRP   A CH2  1 
ATOM   1710 N  N    . PHE   A 1 219 ? 21.506  2.579   -29.503 1   14.523 ? 219 PHE   A N    1 
ATOM   1711 C  CA   . PHE   A 1 219 ? 20.849  2.35    -30.785 1   14.511 ? 219 PHE   A CA   1 
ATOM   1712 C  C    . PHE   A 1 219 ? 21.116  3.466   -31.792 1   13.996 ? 219 PHE   A C    1 
ATOM   1713 O  O    . PHE   A 1 219 ? 20.689  3.364   -32.944 1   15.581 ? 219 PHE   A O    1 
ATOM   1714 C  CB   . PHE   A 1 219 ? 19.334  2.204   -30.557 1   14.592 ? 219 PHE   A CB   1 
ATOM   1715 C  CG   . PHE   A 1 219 ? 18.76   3.261   -29.625 1   14.37  ? 219 PHE   A CG   1 
ATOM   1716 C  CD1  . PHE   A 1 219 ? 18.428  4.526   -30.088 1   14.542 ? 219 PHE   A CD1  1 
ATOM   1717 C  CD2  . PHE   A 1 219 ? 18.632  2.997   -28.265 1   14.802 ? 219 PHE   A CD2  1 
ATOM   1718 C  CE1  . PHE   A 1 219 ? 17.962  5.497   -29.212 1   14.203 ? 219 PHE   A CE1  1 
ATOM   1719 C  CE2  . PHE   A 1 219 ? 18.212  3.982   -27.389 1   14.605 ? 219 PHE   A CE2  1 
ATOM   1720 C  CZ   . PHE   A 1 219 ? 17.859  5.225   -27.863 1   14.748 ? 219 PHE   A CZ   1 
ATOM   1721 N  N    . LEU   A 1 220 ? 21.781  4.549   -31.386 1   14.016 ? 220 LEU   A N    1 
ATOM   1722 C  CA   . LEU   A 1 220 ? 22.136  5.619   -32.308 1   14.744 ? 220 LEU   A CA   1 
ATOM   1723 C  C    . LEU   A 1 220 ? 23.199  5.137   -33.3   1   14.648 ? 220 LEU   A C    1 
ATOM   1724 O  O    . LEU   A 1 220 ? 23.879  4.142   -33.07  1   15.586 ? 220 LEU   A O    1 
ATOM   1725 C  CB   . LEU   A 1 220 ? 22.615  6.853   -31.547 1   15.242 ? 220 LEU   A CB   1 
ATOM   1726 C  CG   . LEU   A 1 220 ? 21.614  7.469   -30.566 1   16.11  ? 220 LEU   A CG   1 
ATOM   1727 C  CD1  . LEU   A 1 220 ? 22.244  8.638   -29.853 1   17.402 ? 220 LEU   A CD1  1 
ATOM   1728 C  CD2  . LEU   A 1 220 ? 20.334  7.906   -31.263 1   17.044 ? 220 LEU   A CD2  1 
ATOM   1729 N  N    . ASN   A 1 221 ? 23.364  5.878   -34.405 1   15.513 ? 221 ASN   A N    1 
ATOM   1730 C  CA   . ASN   A 1 221 ? 24.409  5.569   -35.372 1   15.635 ? 221 ASN   A CA   1 
ATOM   1731 C  C    . ASN   A 1 221 ? 24.951  6.865   -35.967 1   15.828 ? 221 ASN   A C    1 
ATOM   1732 O  O    . ASN   A 1 221 ? 24.482  7.945   -35.652 1   16.032 ? 221 ASN   A O    1 
ATOM   1733 C  CB   . ASN   A 1 221 ? 23.94   4.556   -36.413 1   16.166 ? 221 ASN   A CB   1 
ATOM   1734 C  CG   . ASN   A 1 221 ? 22.847  5.061   -37.321 1   17.909 ? 221 ASN   A CG   1 
ATOM   1735 O  OD1  . ASN   A 1 221 ? 22.767  6.248   -37.641 1   17.014 ? 221 ASN   A OD1  1 
ATOM   1736 N  ND2  . ASN   A 1 221 ? 21.982  4.158   -37.738 1   22.521 ? 221 ASN   A ND2  1 
ATOM   1737 N  N    . ARG   A 1 222 ? 25.955  6.74    -36.837 1   16.291 ? 222 ARG   A N    1 
ATOM   1738 C  CA   . ARG   A 1 222 ? 26.631  7.89    -37.412 1   17.326 ? 222 ARG   A CA   1 
ATOM   1739 C  C    . ARG   A 1 222 ? 25.936  8.427   -38.661 1   17.504 ? 222 ARG   A C    1 
ATOM   1740 O  O    . ARG   A 1 222 ? 26.43   9.369   -39.287 1   19.639 ? 222 ARG   A O    1 
ATOM   1741 C  CB   . ARG   A 1 222 ? 28.072  7.526   -37.786 1   17.667 ? 222 ARG   A CB   1 
ATOM   1742 C  CG   . ARG   A 1 222 ? 28.201  6.528   -38.93  1   19.614 ? 222 ARG   A CG   1 
ATOM   1743 C  CD   . ARG   A 1 222 ? 29.643  6.252   -39.277 1   20.772 ? 222 ARG   A CD   1 
ATOM   1744 N  NE   . ARG   A 1 222 ? 30.238  7.433   -39.901 1   23.874 ? 222 ARG   A NE   1 
ATOM   1745 C  CZ   . ARG   A 1 222 ? 31.514  7.598   -40.217 1   25.315 ? 222 ARG   A CZ   1 
ATOM   1746 N  NH1  . ARG   A 1 222 ? 32.446  6.746   -39.824 1   26.192 ? 222 ARG   A NH1  1 
ATOM   1747 N  NH2  . ARG   A 1 222 ? 31.867  8.667   -40.904 1   28.252 ? 222 ARG   A NH2  1 
ATOM   1748 N  N    . PHE   A 1 223 ? 24.807  7.823   -39.053 1   17.566 ? 223 PHE   A N    1 
ATOM   1749 C  CA   . PHE   A 1 223 ? 24.209  8.105   -40.346 1   18.785 ? 223 PHE   A CA   1 
ATOM   1750 C  C    . PHE   A 1 223 ? 23.044  9.086   -40.229 1   18.758 ? 223 PHE   A C    1 
ATOM   1751 O  O    . PHE   A 1 223 ? 22.541  9.385   -39.141 1   18.396 ? 223 PHE   A O    1 
ATOM   1752 C  CB   . PHE   A 1 223 ? 23.765  6.774   -40.956 1   20.054 ? 223 PHE   A CB   1 
ATOM   1753 C  CG   . PHE   A 1 223 ? 24.917  5.809   -41.166 1   22.276 ? 223 PHE   A CG   1 
ATOM   1754 C  CD1  . PHE   A 1 223 ? 25.91   6.106   -42.094 1   24.73  ? 223 PHE   A CD1  1 
ATOM   1755 C  CD2  . PHE   A 1 223 ? 25.032  4.647   -40.411 1   24.015 ? 223 PHE   A CD2  1 
ATOM   1756 C  CE1  . PHE   A 1 223 ? 26.978  5.244   -42.297 1   26.485 ? 223 PHE   A CE1  1 
ATOM   1757 C  CE2  . PHE   A 1 223 ? 26.108  3.785   -40.621 1   26.206 ? 223 PHE   A CE2  1 
ATOM   1758 C  CZ   . PHE   A 1 223 ? 27.079  4.091   -41.554 1   27.068 ? 223 PHE   A CZ   1 
ATOM   1759 N  N    . THR   A 1 224 ? 22.622  9.592   -41.392 1   20.069 ? 224 THR   A N    1 
ATOM   1760 C  CA   . THR   A 1 224 ? 21.392  10.357  -41.493 1   20.318 ? 224 THR   A CA   1 
ATOM   1761 C  C    . THR   A 1 224 ? 20.581  9.826   -42.672 1   19.582 ? 224 THR   A C    1 
ATOM   1762 O  O    . THR   A 1 224 ? 20.926  8.833   -43.303 1   19.962 ? 224 THR   A O    1 
ATOM   1763 C  CB   . THR   A 1 224 ? 21.719  11.85   -41.598 1   22.385 ? 224 THR   A CB   1 
ATOM   1764 O  OG1  . THR   A 1 224 ? 20.508  12.554  -41.322 1   23.668 ? 224 THR   A OG1  1 
ATOM   1765 C  CG2  . THR   A 1 224 ? 22.312  12.24   -42.941 1   23.595 ? 224 THR   A CG2  1 
ATOM   1766 N  N    . THR   A 1 225 ? 19.458  10.475  -42.929 1   17.87  ? 225 THR   A N    1 
ATOM   1767 C  CA   . THR   A 1 225 ? 18.581  10.081  -44.015 1   16.907 ? 225 THR   A CA   1 
ATOM   1768 C  C    . THR   A 1 225 ? 17.841  11.327  -44.464 1   16.78  ? 225 THR   A C    1 
ATOM   1769 O  O    . THR   A 1 225 ? 17.669  12.251  -43.671 1   17.581 ? 225 THR   A O    1 
ATOM   1770 C  CB   . THR   A 1 225 ? 17.632  8.98    -43.542 1   17.158 ? 225 THR   A CB   1 
ATOM   1771 O  OG1  . THR   A 1 225 ? 16.806  8.577   -44.628 1   16.568 ? 225 THR   A OG1  1 
ATOM   1772 C  CG2  . THR   A 1 225 ? 16.731  9.427   -42.405 1   17.611 ? 225 THR   A CG2  1 
ATOM   1773 N  N    . THR   A 1 226 ? 17.404  11.333  -45.725 1   16.09  ? 226 THR   A N    1 
ATOM   1774 C  CA   . THR   A 1 226 ? 16.387  12.292  -46.115 1   16.099 ? 226 THR   A CA   1 
ATOM   1775 C  C    . THR   A 1 226 ? 15.041  11.795  -45.589 1   15.814 ? 226 THR   A C    1 
ATOM   1776 O  O    . THR   A 1 226 ? 14.851  10.605  -45.324 1   15.141 ? 226 THR   A O    1 
ATOM   1777 C  CB   . THR   A 1 226 ? 16.339  12.506  -47.624 1   17.127 ? 226 THR   A CB   1 
ATOM   1778 O  OG1  . THR   A 1 226 ? 15.892  11.283  -48.189 1   16.607 ? 226 THR   A OG1  1 
ATOM   1779 C  CG2  . THR   A 1 226 ? 17.675  12.918  -48.215 1   17.562 ? 226 THR   A CG2  1 
ATOM   1780 N  N    . LEU   A 1 227 ? 14.085  12.72   -45.494 1   16.075 ? 227 LEU   A N    1 
ATOM   1781 C  CA   . LEU   A 1 227 ? 12.738  12.356  -45.082 1   16.387 ? 227 LEU   A CA   1 
ATOM   1782 C  C    . LEU   A 1 227 ? 12.136  11.37   -46.087 1   16.036 ? 227 LEU   A C    1 
ATOM   1783 O  O    . LEU   A 1 227 ? 11.506  10.389  -45.701 1   16.033 ? 227 LEU   A O    1 
ATOM   1784 C  CB   . LEU   A 1 227 ? 11.89   13.617  -44.919 1   17.371 ? 227 LEU   A CB   1 
ATOM   1785 C  CG   . LEU   A 1 227 ? 10.472  13.419  -44.368 1   18.074 ? 227 LEU   A CG   1 
ATOM   1786 C  CD1  . LEU   A 1 227 ? 10.466  12.757  -43.002 1   18.193 ? 227 LEU   A CD1  1 
ATOM   1787 C  CD2  . LEU   A 1 227 ? 9.738   14.749  -44.329 1   18.655 ? 227 LEU   A CD2  1 
ATOM   1788 N  N    A ASN   A 1 228 ? 12.344  11.608  -47.386 0.5 16.396 ? 228 ASN   A N    1 
ATOM   1789 N  N    B ASN   A 1 228 ? 12.347  11.65   -47.381 0.5 16.134 ? 228 ASN   A N    1 
ATOM   1790 C  CA   A ASN   A 1 228 ? 11.72   10.746  -48.378 0.5 16.92  ? 228 ASN   A CA   1 
ATOM   1791 C  CA   B ASN   A 1 228 ? 11.858  10.824  -48.476 0.5 16.586 ? 228 ASN   A CA   1 
ATOM   1792 C  C    A ASN   A 1 228 ? 12.339  9.35    -48.329 0.5 16.159 ? 228 ASN   A C    1 
ATOM   1793 C  C    B ASN   A 1 228 ? 12.354  9.386   -48.332 0.5 16.059 ? 228 ASN   A C    1 
ATOM   1794 O  O    A ASN   A 1 228 ? 11.605  8.377   -48.408 0.5 15.872 ? 228 ASN   A O    1 
ATOM   1795 O  O    B ASN   A 1 228 ? 11.581  8.44    -48.391 0.5 16.055 ? 228 ASN   A O    1 
ATOM   1796 C  CB   A ASN   A 1 228 ? 11.723  11.332  -49.785 0.5 18.299 ? 228 ASN   A CB   1 
ATOM   1797 C  CB   B ASN   A 1 228 ? 12.313  11.383  -49.823 0.5 17.257 ? 228 ASN   A CB   1 
ATOM   1798 C  CG   A ASN   A 1 228 ? 10.64   10.708  -50.638 0.5 19.893 ? 228 ASN   A CG   1 
ATOM   1799 C  CG   B ASN   A 1 228 ? 12.117  10.393  -50.95  0.5 18.808 ? 228 ASN   A CG   1 
ATOM   1800 O  OD1  A ASN   A 1 228 ? 10.935  10.094  -51.67  0.5 21.624 ? 228 ASN   A OD1  1 
ATOM   1801 O  OD1  B ASN   A 1 228 ? 10.993  9.921   -51.154 0.5 20.335 ? 228 ASN   A OD1  1 
ATOM   1802 N  ND2  A ASN   A 1 228 ? 9.385   10.84   -50.232 0.5 20.63  ? 228 ASN   A ND2  1 
ATOM   1803 N  ND2  B ASN   A 1 228 ? 13.18   10.049  -51.676 0.5 19.178 ? 228 ASN   A ND2  1 
ATOM   1804 N  N    . ASP   A 1 229 ? 13.668  9.23    -48.178 1   15.69  ? 229 ASP   A N    1 
ATOM   1805 C  CA   . ASP   A 1 229 ? 14.271  7.909   -48.095 1   15.454 ? 229 ASP   A CA   1 
ATOM   1806 C  C    . ASP   A 1 229 ? 13.821  7.192   -46.827 1   14.661 ? 229 ASP   A C    1 
ATOM   1807 O  O    . ASP   A 1 229 ? 13.597  5.987   -46.839 1   15.636 ? 229 ASP   A O    1 
ATOM   1808 C  CB   . ASP   A 1 229 ? 15.787  7.977   -48.185 1   16.008 ? 229 ASP   A CB   1 
ATOM   1809 C  CG   . ASP   A 1 229 ? 16.348  8.217   -49.58  1   17.149 ? 229 ASP   A CG   1 
ATOM   1810 O  OD1  . ASP   A 1 229 ? 15.575  8.072   -50.56  1   18.145 ? 229 ASP   A OD1  1 
ATOM   1811 O  OD2  . ASP   A 1 229 ? 17.552  8.528   -49.677 1   17.371 ? 229 ASP   A OD2  1 
ATOM   1812 N  N    . PHE   A 1 230 ? 13.69   7.932   -45.726 1   14.369 ? 230 PHE   A N    1 
ATOM   1813 C  CA   . PHE   A 1 230 ? 13.194  7.337   -44.498 1   14.883 ? 230 PHE   A CA   1 
ATOM   1814 C  C    . PHE   A 1 230 ? 11.808  6.726   -44.736 1   14.917 ? 230 PHE   A C    1 
ATOM   1815 O  O    . PHE   A 1 230 ? 11.551  5.592   -44.353 1   15.114 ? 230 PHE   A O    1 
ATOM   1816 C  CB   . PHE   A 1 230 ? 13.155  8.382   -43.385 1   14.979 ? 230 PHE   A CB   1 
ATOM   1817 C  CG   . PHE   A 1 230 ? 12.442  7.811   -42.173 1   15.313 ? 230 PHE   A CG   1 
ATOM   1818 C  CD1  . PHE   A 1 230 ? 13.063  6.877   -41.353 1   15.829 ? 230 PHE   A CD1  1 
ATOM   1819 C  CD2  . PHE   A 1 230 ? 11.114  8.127   -41.938 1   16.261 ? 230 PHE   A CD2  1 
ATOM   1820 C  CE1  . PHE   A 1 230 ? 12.388  6.321   -40.282 1   16.094 ? 230 PHE   A CE1  1 
ATOM   1821 C  CE2  . PHE   A 1 230 ? 10.444  7.555   -40.879 1   16.542 ? 230 PHE   A CE2  1 
ATOM   1822 C  CZ   . PHE   A 1 230 ? 11.084  6.653   -40.056 1   16.534 ? 230 PHE   A CZ   1 
ATOM   1823 N  N    . ASN   A 1 231 ? 10.906  7.491   -45.367 1   14.761 ? 231 ASN   A N    1 
ATOM   1824 C  CA   . ASN   A 1 231 ? 9.542   7.03    -45.58  1   15.779 ? 231 ASN   A CA   1 
ATOM   1825 C  C    . ASN   A 1 231 ? 9.512   5.823   -46.517 1   15.39  ? 231 ASN   A C    1 
ATOM   1826 O  O    . ASN   A 1 231 ? 8.728   4.904   -46.319 1   16.72  ? 231 ASN   A O    1 
ATOM   1827 C  CB   . ASN   A 1 231 ? 8.654   8.167   -46.062 1   16.44  ? 231 ASN   A CB   1 
ATOM   1828 C  CG   . ASN   A 1 231 ? 8.247   9.064   -44.924 1   17.377 ? 231 ASN   A CG   1 
ATOM   1829 O  OD1  . ASN   A 1 231 ? 7.978   8.566   -43.822 1   18.577 ? 231 ASN   A OD1  1 
ATOM   1830 N  ND2  . ASN   A 1 231 ? 8.213   10.366  -45.156 1   19.14  ? 231 ASN   A ND2  1 
ATOM   1831 N  N    . LEU   A 1 232 ? 10.378  5.808   -47.542 1   15.259 ? 232 LEU   A N    1 
ATOM   1832 C  CA   . LEU   A 1 232 ? 10.406  4.685   -48.458 1   15.831 ? 232 LEU   A CA   1 
ATOM   1833 C  C    . LEU   A 1 232 ? 10.771  3.402   -47.715 1   16.022 ? 232 LEU   A C    1 
ATOM   1834 O  O    . LEU   A 1 232 ? 10.212  2.342   -47.985 1   17.698 ? 232 LEU   A O    1 
ATOM   1835 C  CB   . LEU   A 1 232 ? 11.373  4.968   -49.607 1   15.952 ? 232 LEU   A CB   1 
ATOM   1836 C  CG   . LEU   A 1 232 ? 10.88   5.979   -50.644 1   16.968 ? 232 LEU   A CG   1 
ATOM   1837 C  CD1  . LEU   A 1 232 ? 12.013  6.355   -51.575 1   16.831 ? 232 LEU   A CD1  1 
ATOM   1838 C  CD2  . LEU   A 1 232 ? 9.722   5.439   -51.443 1   18.327 ? 232 LEU   A CD2  1 
ATOM   1839 N  N    . VAL   A 1 233 ? 11.73   3.491   -46.789 1   15.447 ? 233 VAL   A N    1 
ATOM   1840 C  CA   . VAL   A 1 233 ? 12.135  2.325   -46.017 1   16.155 ? 233 VAL   A CA   1 
ATOM   1841 C  C    . VAL   A 1 233 ? 11.064  1.966   -44.985 1   15.828 ? 233 VAL   A C    1 
ATOM   1842 O  O    . VAL   A 1 233 ? 10.685  0.807   -44.859 1   15.913 ? 233 VAL   A O    1 
ATOM   1843 C  CB   . VAL   A 1 233 ? 13.509  2.542   -45.359 1   16.652 ? 233 VAL   A CB   1 
ATOM   1844 C  CG1  . VAL   A 1 233 ? 13.868  1.439   -44.369 1   16.882 ? 233 VAL   A CG1  1 
ATOM   1845 C  CG2  . VAL   A 1 233 ? 14.584  2.669   -46.42  1   17.074 ? 233 VAL   A CG2  1 
ATOM   1846 N  N    . ALA   A 1 234 ? 10.615  2.952   -44.208 1   16.698 ? 234 ALA   A N    1 
ATOM   1847 C  CA   . ALA   A 1 234 ? 9.762   2.648   -43.071 1   18.129 ? 234 ALA   A CA   1 
ATOM   1848 C  C    . ALA   A 1 234 ? 8.451   2.03    -43.546 1   17.538 ? 234 ALA   A C    1 
ATOM   1849 O  O    . ALA   A 1 234 ? 7.899   1.164   -42.878 1   17.268 ? 234 ALA   A O    1 
ATOM   1850 C  CB   . ALA   A 1 234 ? 9.534   3.871   -42.226 1   19.311 ? 234 ALA   A CB   1 
ATOM   1851 N  N    . MET   A 1 235 ? 7.955   2.448   -44.706 1   17.976 ? 235 MET   A N    1 
ATOM   1852 C  CA   . MET   A 1 235 ? 6.699   1.916   -45.208 1   19.228 ? 235 MET   A CA   1 
ATOM   1853 C  C    . MET   A 1 235 ? 6.813   0.419   -45.502 1   17.667 ? 235 MET   A C    1 
ATOM   1854 O  O    . MET   A 1 235 ? 5.816   -0.296  -45.417 1   18.087 ? 235 MET   A O    1 
ATOM   1855 C  CB   . MET   A 1 235 ? 6.209   2.803   -46.357 1   22.282 ? 235 MET   A CB   1 
ATOM   1856 C  CG   . MET   A 1 235 ? 5.797   4.161   -45.794 1   26.802 ? 235 MET   A CG   1 
ATOM   1857 S  SD   . MET   A 1 235 ? 5.16    5.389   -46.947 1   35.559 ? 235 MET   A SD   1 
ATOM   1858 C  CE   . MET   A 1 235 ? 3.497   4.727   -47.118 1   35.692 ? 235 MET   A CE   1 
ATOM   1859 N  N    . LYS   A 1 236 ? 8.025   -0.073  -45.782 1   17.328 ? 236 LYS   A N    1 
ATOM   1860 C  CA   . LYS   A 1 236 ? 8.234   -1.488  -46.039 1   17.874 ? 236 LYS   A CA   1 
ATOM   1861 C  C    . LYS   A 1 236 ? 8.059   -2.311  -44.76  1   17.417 ? 236 LYS   A C    1 
ATOM   1862 O  O    . LYS   A 1 236 ? 7.898   -3.522  -44.827 1   20.599 ? 236 LYS   A O    1 
ATOM   1863 C  CB   . LYS   A 1 236 ? 9.607   -1.683  -46.701 1   18.854 ? 236 LYS   A CB   1 
ATOM   1864 C  CG   . LYS   A 1 236 ? 9.744   -1.003  -48.071 1   19.945 ? 236 LYS   A CG   1 
ATOM   1865 C  CD   . LYS   A 1 236 ? 11.117  -1.024  -48.739 1   20.852 ? 236 LYS   A CD   1 
ATOM   1866 C  CE   . LYS   A 1 236 ? 11.134  -0.212  -50.014 1   21.719 ? 236 LYS   A CE   1 
ATOM   1867 N  NZ   . LYS   A 1 236 ? 12.464  -0.134  -50.633 1   22.36  ? 236 LYS   A NZ   1 
ATOM   1868 N  N    . TYR   A 1 237 ? 8.073   -1.664  -43.591 1   16.658 ? 237 TYR   A N    1 
ATOM   1869 C  CA   . TYR   A 1 237 ? 7.83    -2.334  -42.321 1   16.552 ? 237 TYR   A CA   1 
ATOM   1870 C  C    . TYR   A 1 237 ? 6.454   -1.962  -41.762 1   16.981 ? 237 TYR   A C    1 
ATOM   1871 O  O    . TYR   A 1 237 ? 6.185   -2.168  -40.578 1   17.316 ? 237 TYR   A O    1 
ATOM   1872 C  CB   . TYR   A 1 237 ? 8.889   -1.932  -41.299 1   16.322 ? 237 TYR   A CB   1 
ATOM   1873 C  CG   . TYR   A 1 237 ? 10.319  -2.27   -41.663 1   16.078 ? 237 TYR   A CG   1 
ATOM   1874 C  CD1  . TYR   A 1 237 ? 10.86   -3.495  -41.308 1   16.38  ? 237 TYR   A CD1  1 
ATOM   1875 C  CD2  . TYR   A 1 237 ? 11.12   -1.362  -42.344 1   16.421 ? 237 TYR   A CD2  1 
ATOM   1876 C  CE1  . TYR   A 1 237 ? 12.18   -3.803  -41.592 1   16.613 ? 237 TYR   A CE1  1 
ATOM   1877 C  CE2  . TYR   A 1 237 ? 12.439  -1.657  -42.634 1   16.247 ? 237 TYR   A CE2  1 
ATOM   1878 C  CZ   . TYR   A 1 237 ? 12.967  -2.878  -42.254 1   16.928 ? 237 TYR   A CZ   1 
ATOM   1879 O  OH   . TYR   A 1 237 ? 14.282  -3.154  -42.499 1   18.387 ? 237 TYR   A OH   1 
ATOM   1880 N  N    . ASN   A 1 238 ? 5.568   -1.411  -42.602 1   17.026 ? 238 ASN   A N    1 
ATOM   1881 C  CA   . ASN   A 1 238 ? 4.2     -1.133  -42.2   1   17.519 ? 238 ASN   A CA   1 
ATOM   1882 C  C    . ASN   A 1 238 ? 4.16    0.011   -41.189 1   15.394 ? 238 ASN   A C    1 
ATOM   1883 O  O    . ASN   A 1 238 ? 3.298   0.032   -40.317 1   15.98  ? 238 ASN   A O    1 
ATOM   1884 C  CB   . ASN   A 1 238 ? 3.534   -2.398  -41.663 1   20.678 ? 238 ASN   A CB   1 
ATOM   1885 C  CG   . ASN   A 1 238 ? 2.039   -2.357  -41.797 1   25.159 ? 238 ASN   A CG   1 
ATOM   1886 O  OD1  . ASN   A 1 238 ? 1.522   -2.01   -42.864 1   30.723 ? 238 ASN   A OD1  1 
ATOM   1887 N  ND2  . ASN   A 1 238 ? 1.339   -2.707  -40.732 1   27.79  ? 238 ASN   A ND2  1 
ATOM   1888 N  N    . TYR   A 1 239 ? 5.097   0.955   -41.304 1   14.371 ? 239 TYR   A N    1 
ATOM   1889 C  CA   . TYR   A 1 239 ? 5.084   2.189   -40.528 1   14.374 ? 239 TYR   A CA   1 
ATOM   1890 C  C    . TYR   A 1 239 ? 4.341   3.285   -41.291 1   15.644 ? 239 TYR   A C    1 
ATOM   1891 O  O    . TYR   A 1 239 ? 4.426   3.361   -42.514 1   16.642 ? 239 TYR   A O    1 
ATOM   1892 C  CB   . TYR   A 1 239 ? 6.508   2.673   -40.234 1   14.309 ? 239 TYR   A CB   1 
ATOM   1893 C  CG   . TYR   A 1 239 ? 7.137   2.046   -39.002 1   14.132 ? 239 TYR   A CG   1 
ATOM   1894 C  CD1  . TYR   A 1 239 ? 7.156   0.67    -38.795 1   14.651 ? 239 TYR   A CD1  1 
ATOM   1895 C  CD2  . TYR   A 1 239 ? 7.655   2.856   -37.997 1   15.124 ? 239 TYR   A CD2  1 
ATOM   1896 C  CE1  . TYR   A 1 239 ? 7.687   0.123   -37.631 1   15.009 ? 239 TYR   A CE1  1 
ATOM   1897 C  CE2  . TYR   A 1 239 ? 8.196   2.321   -36.84  1   14.941 ? 239 TYR   A CE2  1 
ATOM   1898 C  CZ   . TYR   A 1 239 ? 8.195   0.952   -36.643 1   14.661 ? 239 TYR   A CZ   1 
ATOM   1899 O  OH   . TYR   A 1 239 ? 8.718   0.467   -35.473 1   15.876 ? 239 TYR   A OH   1 
ATOM   1900 N  N    . GLU   A 1 240 ? 3.626   4.141   -40.551 1   15.806 ? 240 GLU   A N    1 
ATOM   1901 C  CA   . GLU   A 1 240 ? 2.956   5.295   -41.122 1   17.282 ? 240 GLU   A CA   1 
ATOM   1902 C  C    . GLU   A 1 240 ? 3.973   6.266   -41.692 1   17.591 ? 240 GLU   A C    1 
ATOM   1903 O  O    . GLU   A 1 240 ? 5.082   6.378   -41.176 1   16.991 ? 240 GLU   A O    1 
ATOM   1904 C  CB   . GLU   A 1 240 ? 2.146   6.026   -40.053 1   19.755 ? 240 GLU   A CB   1 
ATOM   1905 C  CG   . GLU   A 1 240 ? 0.825   5.331   -39.761 1   23.168 ? 240 GLU   A CG   1 
ATOM   1906 C  CD   . GLU   A 1 240 ? -0.179  5.535   -40.881 1   25.384 ? 240 GLU   A CD   1 
ATOM   1907 O  OE1  . GLU   A 1 240 ? -0.566  6.701   -41.113 1   31.821 ? 240 GLU   A OE1  1 
ATOM   1908 O  OE2  . GLU   A 1 240 ? -0.57   4.537   -41.526 1   30.015 ? 240 GLU   A OE2  1 
ATOM   1909 N  N    . PRO   A 1 241 ? 3.618   7.023   -42.753 1   18.034 ? 241 PRO   A N    1 
ATOM   1910 C  CA   . PRO   A 1 241 ? 4.486   8.097   -43.216 1   18.521 ? 241 PRO   A CA   1 
ATOM   1911 C  C    . PRO   A 1 241 ? 4.77    9.108   -42.112 1   17.385 ? 241 PRO   A C    1 
ATOM   1912 O  O    . PRO   A 1 241 ? 3.899   9.452   -41.313 1   18.731 ? 241 PRO   A O    1 
ATOM   1913 C  CB   . PRO   A 1 241 ? 3.694   8.728   -44.371 1   19.968 ? 241 PRO   A CB   1 
ATOM   1914 C  CG   . PRO   A 1 241 ? 2.734   7.647   -44.804 1   20.044 ? 241 PRO   A CG   1 
ATOM   1915 C  CD   . PRO   A 1 241 ? 2.392   6.889   -43.548 1   19.539 ? 241 PRO   A CD   1 
ATOM   1916 N  N    . LEU   A 1 242 ? 6.012   9.584   -42.088 1   16.059 ? 242 LEU   A N    1 
ATOM   1917 C  CA   . LEU   A 1 242 ? 6.403   10.7    -41.255 1   15.839 ? 242 LEU   A CA   1 
ATOM   1918 C  C    . LEU   A 1 242 ? 6.301   11.966  -42.095 1   16.778 ? 242 LEU   A C    1 
ATOM   1919 O  O    . LEU   A 1 242 ? 6.884   12.035  -43.176 1   17.73  ? 242 LEU   A O    1 
ATOM   1920 C  CB   . LEU   A 1 242 ? 7.829   10.486  -40.749 1   16.385 ? 242 LEU   A CB   1 
ATOM   1921 C  CG   . LEU   A 1 242 ? 8.282   11.406  -39.615 1   16.533 ? 242 LEU   A CG   1 
ATOM   1922 C  CD1  . LEU   A 1 242 ? 7.578   11.025  -38.332 1   16.926 ? 242 LEU   A CD1  1 
ATOM   1923 C  CD2  . LEU   A 1 242 ? 9.785   11.347  -39.458 1   17.154 ? 242 LEU   A CD2  1 
ATOM   1924 N  N    . THR   A 1 243 ? 5.546   12.949  -41.587 1   17.165 ? 243 THR   A N    1 
ATOM   1925 C  CA   . THR   A 1 243 ? 5.326   14.204  -42.286 1   17.603 ? 243 THR   A CA   1 
ATOM   1926 C  C    . THR   A 1 243 ? 6.234   15.283  -41.709 1   17.994 ? 243 THR   A C    1 
ATOM   1927 O  O    . THR   A 1 243 ? 6.796   15.133  -40.632 1   16.986 ? 243 THR   A O    1 
ATOM   1928 C  CB   . THR   A 1 243 ? 3.86    14.626  -42.17  1   18.141 ? 243 THR   A CB   1 
ATOM   1929 O  OG1  . THR   A 1 243 ? 3.636   14.961  -40.8   1   18.592 ? 243 THR   A OG1  1 
ATOM   1930 C  CG2  . THR   A 1 243 ? 2.915   13.535  -42.631 1   18.719 ? 243 THR   A CG2  1 
ATOM   1931 N  N    . GLN   A 1 244 ? 6.32    16.408  -42.416 1   18.407 ? 244 GLN   A N    1 
ATOM   1932 C  CA   . GLN   A 1 244 ? 7.042   17.555  -41.899 1   19.635 ? 244 GLN   A CA   1 
ATOM   1933 C  C    . GLN   A 1 244 ? 6.393   18.048  -40.604 1   19.045 ? 244 GLN   A C    1 
ATOM   1934 O  O    . GLN   A 1 244 ? 7.09    18.513  -39.715 1   19.669 ? 244 GLN   A O    1 
ATOM   1935 C  CB   . GLN   A 1 244 ? 7.148   18.654  -42.956 1   21.243 ? 244 GLN   A CB   1 
ATOM   1936 C  CG   . GLN   A 1 244 ? 8.03    19.825  -42.54  1   23.345 ? 244 GLN   A CG   1 
ATOM   1937 C  CD   . GLN   A 1 244 ? 9.449   19.411  -42.212 1   23.902 ? 244 GLN   A CD   1 
ATOM   1938 O  OE1  . GLN   A 1 244 ? 10.068  18.597  -42.909 1   25.359 ? 244 GLN   A OE1  1 
ATOM   1939 N  NE2  . GLN   A 1 244 ? 9.966   19.943  -41.117 1   25.168 ? 244 GLN   A NE2  1 
ATOM   1940 N  N    . ASP   A 1 245 ? 5.067   17.926  -40.466 1   19.349 ? 245 ASP   A N    1 
ATOM   1941 C  CA   . ASP   A 1 245 ? 4.423   18.275  -39.205 1   19.942 ? 245 ASP   A CA   1 
ATOM   1942 C  C    . ASP   A 1 245 ? 4.997   17.438  -38.065 1   18.7   ? 245 ASP   A C    1 
ATOM   1943 O  O    . ASP   A 1 245 ? 5.269   17.952  -36.988 1   20.409 ? 245 ASP   A O    1 
ATOM   1944 C  CB   . ASP   A 1 245 ? 2.916   18.078  -39.233 1   20.247 ? 245 ASP   A CB   1 
ATOM   1945 C  CG   . ASP   A 1 245 ? 2.128   19.148  -39.966 1   21.967 ? 245 ASP   A CG   1 
ATOM   1946 O  OD1  . ASP   A 1 245 ? 2.763   20.025  -40.576 1   22.969 ? 245 ASP   A OD1  1 
ATOM   1947 O  OD2  . ASP   A 1 245 ? 0.885   19.107  -39.891 1   24.977 ? 245 ASP   A OD2  1 
ATOM   1948 N  N    . HIS   A 1 246 ? 5.171   16.14   -38.307 1   17.97  ? 246 HIS   A N    1 
ATOM   1949 C  CA   . HIS   A 1 246 ? 5.756   15.262  -37.309 1   17.668 ? 246 HIS   A CA   1 
ATOM   1950 C  C    . HIS   A 1 246 ? 7.178   15.693  -36.967 1   18.235 ? 246 HIS   A C    1 
ATOM   1951 O  O    . HIS   A 1 246 ? 7.569   15.679  -35.806 1   18.587 ? 246 HIS   A O    1 
ATOM   1952 C  CB   . HIS   A 1 246 ? 5.732   13.809  -37.776 1   17.178 ? 246 HIS   A CB   1 
ATOM   1953 C  CG   . HIS   A 1 246 ? 4.376   13.239  -37.98  1   17.616 ? 246 HIS   A CG   1 
ATOM   1954 N  ND1  . HIS   A 1 246 ? 4.124   12.316  -38.97  1   18.347 ? 246 HIS   A ND1  1 
ATOM   1955 C  CD2  . HIS   A 1 246 ? 3.215   13.44   -37.341 1   18.604 ? 246 HIS   A CD2  1 
ATOM   1956 C  CE1  . HIS   A 1 246 ? 2.84    11.977  -38.922 1   19.128 ? 246 HIS   A CE1  1 
ATOM   1957 N  NE2  . HIS   A 1 246 ? 2.274   12.649  -37.941 1   18.918 ? 246 HIS   A NE2  1 
ATOM   1958 N  N    . VAL   A 1 247 ? 7.966   16.039  -37.99  1   18.003 ? 247 VAL   A N    1 
ATOM   1959 C  CA   . VAL   A 1 247 ? 9.332   16.475  -37.753 1   18.587 ? 247 VAL   A CA   1 
ATOM   1960 C  C    . VAL   A 1 247 ? 9.332   17.73   -36.88  1   19.621 ? 247 VAL   A C    1 
ATOM   1961 O  O    . VAL   A 1 247 ? 10.116  17.834  -35.938 1   20.867 ? 247 VAL   A O    1 
ATOM   1962 C  CB   . VAL   A 1 247 ? 10.086  16.694  -39.076 1   19.173 ? 247 VAL   A CB   1 
ATOM   1963 C  CG1  . VAL   A 1 247 ? 11.453  17.33   -38.855 1   19.889 ? 247 VAL   A CG1  1 
ATOM   1964 C  CG2  . VAL   A 1 247 ? 10.223  15.394  -39.858 1   18.909 ? 247 VAL   A CG2  1 
ATOM   1965 N  N    . ASP   A 1 248 ? 8.427   18.666  -37.178 1   20.312 ? 248 ASP   A N    1 
ATOM   1966 C  CA   . ASP   A 1 248 ? 8.33    19.909  -36.427 1   20.931 ? 248 ASP   A CA   1 
ATOM   1967 C  C    . ASP   A 1 248 ? 7.988   19.622  -34.965 1   20.971 ? 248 ASP   A C    1 
ATOM   1968 O  O    . ASP   A 1 248 ? 8.569   20.216  -34.06  1   22.535 ? 248 ASP   A O    1 
ATOM   1969 C  CB   . ASP   A 1 248 ? 7.322   20.854  -37.063 1   22.703 ? 248 ASP   A CB   1 
ATOM   1970 C  CG   . ASP   A 1 248 ? 7.726   21.438  -38.41  1   24.547 ? 248 ASP   A CG   1 
ATOM   1971 O  OD1  . ASP   A 1 248 ? 8.907   21.298  -38.783 1   26.254 ? 248 ASP   A OD1  1 
ATOM   1972 O  OD2  . ASP   A 1 248 ? 6.849   22.02   -39.084 1   26.889 ? 248 ASP   A OD2  1 
ATOM   1973 N  N    . ILE   A 1 249 ? 7.026   18.72   -34.741 1   21.44  ? 249 ILE   A N    1 
ATOM   1974 C  CA   . ILE   A 1 249 ? 6.541   18.401  -33.405 1   22.221 ? 249 ILE   A CA   1 
ATOM   1975 C  C    . ILE   A 1 249 ? 7.642   17.76   -32.562 1   21.063 ? 249 ILE   A C    1 
ATOM   1976 O  O    . ILE   A 1 249 ? 7.627   17.896  -31.339 1   22.285 ? 249 ILE   A O    1 
ATOM   1977 C  CB   . ILE   A 1 249 ? 5.283   17.514  -33.503 1   24.443 ? 249 ILE   A CB   1 
ATOM   1978 C  CG1  . ILE   A 1 249 ? 4.108   18.303  -34.109 1   27.167 ? 249 ILE   A CG1  1 
ATOM   1979 C  CG2  . ILE   A 1 249 ? 4.901   16.918  -32.147 1   27.911 ? 249 ILE   A CG2  1 
ATOM   1980 C  CD1  . ILE   A 1 249 ? 2.987   17.439  -34.661 1   29.364 ? 249 ILE   A CD1  1 
ATOM   1981 N  N    . LEU   A 1 250 ? 8.592   17.069  -33.211 1   19.559 ? 250 LEU   A N    1 
ATOM   1982 C  CA   . LEU   A 1 250 ? 9.712   16.437  -32.52  1   18.28  ? 250 LEU   A CA   1 
ATOM   1983 C  C    . LEU   A 1 250 ? 10.834  17.429  -32.204 1   19.122 ? 250 LEU   A C    1 
ATOM   1984 O  O    . LEU   A 1 250 ? 11.793  17.049  -31.541 1   18.972 ? 250 LEU   A O    1 
ATOM   1985 C  CB   . LEU   A 1 250 ? 10.242  15.256  -33.335 1   17.373 ? 250 LEU   A CB   1 
ATOM   1986 C  CG   . LEU   A 1 250 ? 9.338   14.018  -33.38  1   16.933 ? 250 LEU   A CG   1 
ATOM   1987 C  CD1  . LEU   A 1 250 ? 9.768   13.1    -34.507 1   16.91  ? 250 LEU   A CD1  1 
ATOM   1988 C  CD2  . LEU   A 1 250 ? 9.336   13.261  -32.063 1   17.69  ? 250 LEU   A CD2  1 
ATOM   1989 N  N    . GLY   A 1 251 ? 10.726  18.684  -32.657 1   19.888 ? 251 GLY   A N    1 
ATOM   1990 C  CA   . GLY   A 1 251 ? 11.772  19.682  -32.467 1   20.641 ? 251 GLY   A CA   1 
ATOM   1991 C  C    . GLY   A 1 251 ? 12.221  19.829  -31.013 1   20.84  ? 251 GLY   A C    1 
ATOM   1992 O  O    . GLY   A 1 251 ? 13.417  19.832  -30.727 1   19.921 ? 251 GLY   A O    1 
ATOM   1993 N  N    . PRO   A 1 252 ? 11.306  20.024  -30.045 1   21.033 ? 252 PRO   A N    1 
ATOM   1994 C  CA   . PRO   A 1 252 ? 11.718  20.152  -28.645 1   20.789 ? 252 PRO   A CA   1 
ATOM   1995 C  C    . PRO   A 1 252 ? 12.532  18.978  -28.105 1   19.172 ? 252 PRO   A C    1 
ATOM   1996 O  O    . PRO   A 1 252 ? 13.525  19.198  -27.413 1   19.699 ? 252 PRO   A O    1 
ATOM   1997 C  CB   . PRO   A 1 252 ? 10.37   20.369  -27.933 1   21.981 ? 252 PRO   A CB   1 
ATOM   1998 C  CG   . PRO   A 1 252 ? 9.549   21.099  -28.973 1   22.55  ? 252 PRO   A CG   1 
ATOM   1999 C  CD   . PRO   A 1 252 ? 9.883   20.343  -30.245 1   22.149 ? 252 PRO   A CD   1 
ATOM   2000 N  N    . LEU   A 1 253 ? 12.137  17.745  -28.43  1   17.527 ? 253 LEU   A N    1 
ATOM   2001 C  CA   . LEU   A 1 253 ? 12.879  16.576  -27.977 1   16.445 ? 253 LEU   A CA   1 
ATOM   2002 C  C    . LEU   A 1 253 ? 14.254  16.518  -28.644 1   16.078 ? 253 LEU   A C    1 
ATOM   2003 O  O    . LEU   A 1 253 ? 15.245  16.164  -28.011 1   16.437 ? 253 LEU   A O    1 
ATOM   2004 C  CB   . LEU   A 1 253 ? 12.07   15.303  -28.232 1   16.671 ? 253 LEU   A CB   1 
ATOM   2005 C  CG   . LEU   A 1 253 ? 10.84   15.132  -27.328 1   17.326 ? 253 LEU   A CG   1 
ATOM   2006 C  CD1  . LEU   A 1 253 ? 9.999   13.954  -27.793 1   17.75  ? 253 LEU   A CD1  1 
ATOM   2007 C  CD2  . LEU   A 1 253 ? 11.249  14.919  -25.888 1   17.866 ? 253 LEU   A CD2  1 
ATOM   2008 N  N    . SER   A 1 254 ? 14.305  16.888  -29.923 1   15.871 ? 254 SER   A N    1 
ATOM   2009 C  CA   . SER   A 1 254 ? 15.559  16.995  -30.653 1   16.622 ? 254 SER   A CA   1 
ATOM   2010 C  C    . SER   A 1 254 ? 16.49   17.996  -29.973 1   16.792 ? 254 SER   A C    1 
ATOM   2011 O  O    . SER   A 1 254 ? 17.677  17.725  -29.803 1   17.759 ? 254 SER   A O    1 
ATOM   2012 C  CB   . SER   A 1 254 ? 15.292  17.372  -32.083 1   17.708 ? 254 SER   A CB   1 
ATOM   2013 O  OG   . SER   A 1 254 ? 16.497  17.531  -32.81  1   19.215 ? 254 SER   A OG   1 
ATOM   2014 N  N    . ALA   A 1 255 ? 15.947  19.153  -29.575 1   17.815 ? 255 ALA   A N    1 
ATOM   2015 C  CA   . ALA   A 1 255 ? 16.753  20.198  -28.958 1   19.257 ? 255 ALA   A CA   1 
ATOM   2016 C  C    . ALA   A 1 255 ? 17.272  19.754  -27.592 1   19.063 ? 255 ALA   A C    1 
ATOM   2017 O  O    . ALA   A 1 255 ? 18.415  20.041  -27.244 1   20.217 ? 255 ALA   A O    1 
ATOM   2018 C  CB   . ALA   A 1 255 ? 15.965  21.481  -28.854 1   20.589 ? 255 ALA   A CB   1 
ATOM   2019 N  N    . GLN   A 1 256 ? 16.442  19.047  -26.827 1   18.532 ? 256 GLN   A N    1 
ATOM   2020 C  CA   . GLN   A 1 256 ? 16.82   18.638  -25.485 1   18.72  ? 256 GLN   A CA   1 
ATOM   2021 C  C    . GLN   A 1 256 ? 17.952  17.611  -25.522 1   18.037 ? 256 GLN   A C    1 
ATOM   2022 O  O    . GLN   A 1 256 ? 18.79   17.576  -24.618 1   20.63  ? 256 GLN   A O    1 
ATOM   2023 C  CB   . GLN   A 1 256 ? 15.626  18.098  -24.699 1   20.156 ? 256 GLN   A CB   1 
ATOM   2024 C  CG   . GLN   A 1 256 ? 15.981  17.833  -23.238 1   21.151 ? 256 GLN   A CG   1 
ATOM   2025 C  CD   . GLN   A 1 256 ? 14.847  17.303  -22.392 1   22.425 ? 256 GLN   A CD   1 
ATOM   2026 O  OE1  . GLN   A 1 256 ? 13.701  17.726  -22.53  1   25.58  ? 256 GLN   A OE1  1 
ATOM   2027 N  NE2  . GLN   A 1 256 ? 15.161  16.374  -21.5   1   22.601 ? 256 GLN   A NE2  1 
ATOM   2028 N  N    . THR   A 1 257 ? 17.978  16.778  -26.562 1   16.831 ? 257 THR   A N    1 
ATOM   2029 C  CA   . THR   A 1 257 ? 18.919  15.666  -26.631 1   16.703 ? 257 THR   A CA   1 
ATOM   2030 C  C    . THR   A 1 257 ? 20.115  15.942  -27.541 1   16.528 ? 257 THR   A C    1 
ATOM   2031 O  O    . THR   A 1 257 ? 21.09   15.207  -27.475 1   17.314 ? 257 THR   A O    1 
ATOM   2032 C  CB   . THR   A 1 257 ? 18.194  14.408  -27.108 1   16.038 ? 257 THR   A CB   1 
ATOM   2033 O  OG1  . THR   A 1 257 ? 17.664  14.626  -28.415 1   15.243 ? 257 THR   A OG1  1 
ATOM   2034 C  CG2  . THR   A 1 257 ? 17.109  13.986  -26.139 1   16.276 ? 257 THR   A CG2  1 
ATOM   2035 N  N    . GLY   A 1 258 ? 20.025  16.942  -28.423 1   16.313 ? 258 GLY   A N    1 
ATOM   2036 C  CA   . GLY   A 1 258 ? 21.088  17.218  -29.376 1   17.122 ? 258 GLY   A CA   1 
ATOM   2037 C  C    . GLY   A 1 258 ? 21.111  16.244  -30.555 1   17.774 ? 258 GLY   A C    1 
ATOM   2038 O  O    . GLY   A 1 258 ? 22.122  16.15   -31.248 1   20.241 ? 258 GLY   A O    1 
ATOM   2039 N  N    . ILE   A 1 259 ? 20.016  15.509  -30.776 1   15.827 ? 259 ILE   A N    1 
ATOM   2040 C  CA   . ILE   A 1 259 ? 19.927  14.545  -31.862 1   15.51  ? 259 ILE   A CA   1 
ATOM   2041 C  C    . ILE   A 1 259 ? 18.907  15.059  -32.871 1   15.085 ? 259 ILE   A C    1 
ATOM   2042 O  O    . ILE   A 1 259 ? 17.723  15.156  -32.551 1   15.625 ? 259 ILE   A O    1 
ATOM   2043 C  CB   . ILE   A 1 259 ? 19.544  13.149  -31.35  1   15.543 ? 259 ILE   A CB   1 
ATOM   2044 C  CG1  . ILE   A 1 259 ? 20.546  12.671  -30.318 1   16.541 ? 259 ILE   A CG1  1 
ATOM   2045 C  CG2  . ILE   A 1 259 ? 19.4    12.151  -32.503 1   15.597 ? 259 ILE   A CG2  1 
ATOM   2046 C  CD1  . ILE   A 1 259 ? 20.07   11.486  -29.512 1   17.314 ? 259 ILE   A CD1  1 
ATOM   2047 N  N    . ALA   A 1 260 ? 19.389  15.382  -34.072 1   15.328 ? 260 ALA   A N    1 
ATOM   2048 C  CA   . ALA   A 1 260 ? 18.521  15.873  -35.128 1   15.156 ? 260 ALA   A CA   1 
ATOM   2049 C  C    . ALA   A 1 260 ? 17.46   14.819  -35.443 1   14.989 ? 260 ALA   A C    1 
ATOM   2050 O  O    . ALA   A 1 260 ? 17.714  13.621  -35.388 1   14.692 ? 260 ALA   A O    1 
ATOM   2051 C  CB   . ALA   A 1 260 ? 19.356  16.214  -36.356 1   15.993 ? 260 ALA   A CB   1 
ATOM   2052 N  N    . VAL   A 1 261 ? 16.276  15.286  -35.835 1   15.659 ? 261 VAL   A N    1 
ATOM   2053 C  CA   . VAL   A 1 261 ? 15.165  14.38   -36.086 1   15.84  ? 261 VAL   A CA   1 
ATOM   2054 C  C    . VAL   A 1 261 ? 15.546  13.357  -37.162 1   15.053 ? 261 VAL   A C    1 
ATOM   2055 O  O    . VAL   A 1 261 ? 15.3    12.163  -36.995 1   14.491 ? 261 VAL   A O    1 
ATOM   2056 C  CB   . VAL   A 1 261 ? 13.869  15.129  -36.439 1   16.78  ? 261 VAL   A CB   1 
ATOM   2057 C  CG1  . VAL   A 1 261 ? 12.777  14.14   -36.813 1   17.158 ? 261 VAL   A CG1  1 
ATOM   2058 C  CG2  . VAL   A 1 261 ? 13.42   16.043  -35.301 1   17.624 ? 261 VAL   A CG2  1 
ATOM   2059 N  N    . LEU   A 1 262 ? 16.156  13.804  -38.268 1   14.802 ? 262 LEU   A N    1 
ATOM   2060 C  CA   . LEU   A 1 262 ? 16.494  12.867  -39.333 1   15.296 ? 262 LEU   A CA   1 
ATOM   2061 C  C    . LEU   A 1 262 ? 17.613  11.906  -38.918 1   14.98  ? 262 LEU   A C    1 
ATOM   2062 O  O    . LEU   A 1 262 ? 17.712  10.813  -39.467 1   15.55  ? 262 LEU   A O    1 
ATOM   2063 C  CB   . LEU   A 1 262 ? 16.822  13.616  -40.623 1   16.523 ? 262 LEU   A CB   1 
ATOM   2064 C  CG   . LEU   A 1 262 ? 15.624  14.319  -41.268 1   17.562 ? 262 LEU   A CG   1 
ATOM   2065 C  CD1  . LEU   A 1 262 ? 16.086  15.169  -42.435 1   18.871 ? 262 LEU   A CD1  1 
ATOM   2066 C  CD2  . LEU   A 1 262 ? 14.565  13.323  -41.713 1   18.351 ? 262 LEU   A CD2  1 
ATOM   2067 N  N    . ASP   A 1 263 ? 18.449  12.301  -37.955 1   14.803 ? 263 ASP   A N    1 
ATOM   2068 C  CA   . ASP   A 1 263 ? 19.426  11.387  -37.387 1   15.323 ? 263 ASP   A CA   1 
ATOM   2069 C  C    . ASP   A 1 263 ? 18.73   10.327  -36.545 1   14.768 ? 263 ASP   A C    1 
ATOM   2070 O  O    . ASP   A 1 263 ? 19.103  9.166   -36.615 1   14.983 ? 263 ASP   A O    1 
ATOM   2071 C  CB   . ASP   A 1 263 ? 20.52   12.137  -36.648 1   16.639 ? 263 ASP   A CB   1 
ATOM   2072 C  CG   . ASP   A 1 263 ? 21.433  12.988  -37.522 1   18.341 ? 263 ASP   A CG   1 
ATOM   2073 O  OD1  . ASP   A 1 263 ? 21.352  12.878  -38.767 1   21.495 ? 263 ASP   A OD1  1 
ATOM   2074 O  OD2  . ASP   A 1 263 ? 22.197  13.786  -36.951 1   21.267 ? 263 ASP   A OD2  1 
ATOM   2075 N  N    . MET   A 1 264 ? 17.701  10.7    -35.772 1   14.214 ? 264 MET   A N    1 
ATOM   2076 C  CA   . MET   A 1 264 ? 16.935  9.698   -35.051 1   13.897 ? 264 MET   A CA   1 
ATOM   2077 C  C    . MET   A 1 264 ? 16.197  8.781   -36.029 1   13.83  ? 264 MET   A C    1 
ATOM   2078 O  O    . MET   A 1 264 ? 16.061  7.582   -35.781 1   14.09  ? 264 MET   A O    1 
ATOM   2079 C  CB   . MET   A 1 264 ? 15.962  10.324  -34.049 1   13.829 ? 264 MET   A CB   1 
ATOM   2080 C  CG   . MET   A 1 264 ? 15.385  9.311   -33.076 1   14.096 ? 264 MET   A CG   1 
ATOM   2081 S  SD   . MET   A 1 264 ? 16.636  8.571   -31.999 1   14.476 ? 264 MET   A SD   1 
ATOM   2082 C  CE   . MET   A 1 264 ? 16.597  9.765   -30.657 1   14.963 ? 264 MET   A CE   1 
ATOM   2083 N  N    . CYS   A 1 265 ? 15.731  9.338   -37.153 1   13.858 ? 265 CYS   A N    1 
ATOM   2084 C  CA   . CYS   A 1 265 ? 15.141  8.516   -38.201 1   14.481 ? 265 CYS   A CA   1 
ATOM   2085 C  C    . CYS   A 1 265 ? 16.122  7.451   -38.705 1   14.538 ? 265 CYS   A C    1 
ATOM   2086 O  O    . CYS   A 1 265 ? 15.746  6.302   -38.952 1   14.547 ? 265 CYS   A O    1 
ATOM   2087 C  CB   . CYS   A 1 265 ? 14.64   9.378   -39.35  1   14.798 ? 265 CYS   A CB   1 
ATOM   2088 S  SG   . CYS   A 1 265 ? 13.158  10.35   -38.966 1   16.582 ? 265 CYS   A SG   1 
ATOM   2089 N  N    . ALA   A 1 266 ? 17.401  7.827   -38.852 1   14.863 ? 266 ALA   A N    1 
ATOM   2090 C  CA   . ALA   A 1 266 ? 18.419  6.876   -39.28  1   14.811 ? 266 ALA   A CA   1 
ATOM   2091 C  C    . ALA   A 1 266 ? 18.607  5.775   -38.233 1   14.772 ? 266 ALA   A C    1 
ATOM   2092 O  O    . ALA   A 1 266 ? 18.858  4.62    -38.579 1   15.563 ? 266 ALA   A O    1 
ATOM   2093 C  CB   . ALA   A 1 266 ? 19.722  7.593   -39.589 1   15.598 ? 266 ALA   A CB   1 
ATOM   2094 N  N    . SER   A 1 267 ? 18.511  6.13    -36.946 1   14.275 ? 267 SER   A N    1 
ATOM   2095 C  CA   . SER   A 1 267 ? 18.569  5.139   -35.884 1   14.873 ? 267 SER   A CA   1 
ATOM   2096 C  C    . SER   A 1 267 ? 17.403  4.163   -36.02  1   14.567 ? 267 SER   A C    1 
ATOM   2097 O  O    . SER   A 1 267 ? 17.585  2.955   -35.918 1   15.032 ? 267 SER   A O    1 
ATOM   2098 C  CB   . SER   A 1 267 ? 18.577  5.799   -34.532 1   16.055 ? 267 SER   A CB   1 
ATOM   2099 O  OG   . SER   A 1 267 ? 18.467  4.861   -33.47  1   17.646 ? 267 SER   A OG   1 
ATOM   2100 N  N    . LEU   A 1 268 ? 16.191  4.691   -36.215 1   14.303 ? 268 LEU   A N    1 
ATOM   2101 C  CA   . LEU   A 1 268 ? 15.025  3.833   -36.34  1   13.866 ? 268 LEU   A CA   1 
ATOM   2102 C  C    . LEU   A 1 268 ? 15.145  2.902   -37.552 1   13.69  ? 268 LEU   A C    1 
ATOM   2103 O  O    . LEU   A 1 268 ? 14.819  1.719   -37.453 1   13.835 ? 268 LEU   A O    1 
ATOM   2104 C  CB   . LEU   A 1 268 ? 13.766  4.695   -36.377 1   13.837 ? 268 LEU   A CB   1 
ATOM   2105 C  CG   . LEU   A 1 268 ? 12.447  3.955   -36.63  1   14.051 ? 268 LEU   A CG   1 
ATOM   2106 C  CD1  . LEU   A 1 268 ? 12.241  2.821   -35.655 1   14.204 ? 268 LEU   A CD1  1 
ATOM   2107 C  CD2  . LEU   A 1 268 ? 11.286  4.924   -36.563 1   14.416 ? 268 LEU   A CD2  1 
ATOM   2108 N  N    . LYS   A 1 269 ? 15.625  3.421   -38.684 1   14.084 ? 269 LYS   A N    1 
ATOM   2109 C  CA   . LYS   A 1 269 ? 15.844  2.571   -39.853 1   14.838 ? 269 LYS   A CA   1 
ATOM   2110 C  C    . LYS   A 1 269 ? 16.733  1.373   -39.486 1   15.136 ? 269 LYS   A C    1 
ATOM   2111 O  O    . LYS   A 1 269 ? 16.488  0.23    -39.884 1   15.317 ? 269 LYS   A O    1 
ATOM   2112 C  CB   . LYS   A 1 269 ? 16.469  3.392   -40.986 1   16.935 ? 269 LYS   A CB   1 
ATOM   2113 C  CG   . LYS   A 1 269 ? 15.597  4.417   -41.659 1   19.302 ? 269 LYS   A CG   1 
ATOM   2114 C  CD   . LYS   A 1 269 ? 16.347  5.394   -42.559 1   21.449 ? 269 LYS   A CD   1 
ATOM   2115 C  CE   . LYS   A 1 269 ? 16.673  4.86    -43.897 1   22.339 ? 269 LYS   A CE   1 
ATOM   2116 N  NZ   . LYS   A 1 269 ? 17.522  5.804   -44.628 1   22.288 ? 269 LYS   A NZ   1 
ATOM   2117 N  N    . GLU   A 1 270 ? 17.804  1.639   -38.732 1   14.906 ? 270 GLU   A N    1 
ATOM   2118 C  CA   . GLU   A 1 270 ? 18.738  0.58    -38.392 1   15.565 ? 270 GLU   A CA   1 
ATOM   2119 C  C    . GLU   A 1 270 ? 18.12   -0.409  -37.401 1   14.806 ? 270 GLU   A C    1 
ATOM   2120 O  O    . GLU   A 1 270 ? 18.376  -1.602  -37.497 1   15.485 ? 270 GLU   A O    1 
ATOM   2121 C  CB   . GLU   A 1 270 ? 20.034  1.202   -37.888 1   16.522 ? 270 GLU   A CB   1 
ATOM   2122 C  CG   . GLU   A 1 270 ? 21.122  0.184   -37.573 1   17.724 ? 270 GLU   A CG   1 
ATOM   2123 C  CD   . GLU   A 1 270 ? 22.442  0.894   -37.371 1   19.008 ? 270 GLU   A CD   1 
ATOM   2124 O  OE1  . GLU   A 1 270 ? 23.11   1.254   -38.356 1   21.425 ? 270 GLU   A OE1  1 
ATOM   2125 O  OE2  . GLU   A 1 270 ? 22.744  1.173   -36.218 1   20.511 ? 270 GLU   A OE2  1 
ATOM   2126 N  N    . LEU   A 1 271 ? 17.309  0.075   -36.451 1   14.824 ? 271 LEU   A N    1 
ATOM   2127 C  CA   . LEU   A 1 271 ? 16.614  -0.814  -35.526 1   14.837 ? 271 LEU   A CA   1 
ATOM   2128 C  C    . LEU   A 1 271 ? 15.661  -1.749  -36.266 1   15.334 ? 271 LEU   A C    1 
ATOM   2129 O  O    . LEU   A 1 271 ? 15.536  -2.918  -35.907 1   15.943 ? 271 LEU   A O    1 
ATOM   2130 C  CB   . LEU   A 1 271 ? 15.884  0.009   -34.47  1   15.407 ? 271 LEU   A CB   1 
ATOM   2131 C  CG   . LEU   A 1 271 ? 16.769  0.594   -33.37  1   15.519 ? 271 LEU   A CG   1 
ATOM   2132 C  CD1  . LEU   A 1 271 ? 16.032  1.665   -32.599 1   15.874 ? 271 LEU   A CD1  1 
ATOM   2133 C  CD2  . LEU   A 1 271 ? 17.281  -0.516  -32.445 1   16.743 ? 271 LEU   A CD2  1 
ATOM   2134 N  N    . LEU   A 1 272 ? 14.97   -1.222  -37.286 1   14.297 ? 272 LEU   A N    1 
ATOM   2135 C  CA   . LEU   A 1 272 ? 14.054  -2.041  -38.071 1   14.845 ? 272 LEU   A CA   1 
ATOM   2136 C  C    . LEU   A 1 272 ? 14.813  -3.121  -38.836 1   15.077 ? 272 LEU   A C    1 
ATOM   2137 O  O    . LEU   A 1 272 ? 14.313  -4.231  -39.007 1   15.772 ? 272 LEU   A O    1 
ATOM   2138 C  CB   . LEU   A 1 272 ? 13.213  -1.17   -39.001 1   15.149 ? 272 LEU   A CB   1 
ATOM   2139 C  CG   . LEU   A 1 272 ? 12.181  -0.296  -38.286 1   15.877 ? 272 LEU   A CG   1 
ATOM   2140 C  CD1  . LEU   A 1 272 ? 11.59   0.729   -39.226 1   16.541 ? 272 LEU   A CD1  1 
ATOM   2141 C  CD2  . LEU   A 1 272 ? 11.072  -1.139  -37.672 1   16.494 ? 272 LEU   A CD2  1 
ATOM   2142 N  N    . GLN   A 1 273 ? 16.013  -2.779  -39.316 1   15.232 ? 273 GLN   A N    1 
ATOM   2143 C  CA   . GLN   A 1 273 ? 16.851  -3.705  -40.058 1   16.092 ? 273 GLN   A CA   1 
ATOM   2144 C  C    . GLN   A 1 273 ? 17.468  -4.784  -39.171 1   15.884 ? 273 GLN   A C    1 
ATOM   2145 O  O    . GLN   A 1 273 ? 17.636  -5.922  -39.611 1   16.576 ? 273 GLN   A O    1 
ATOM   2146 C  CB   . GLN   A 1 273 ? 17.927  -2.839  -40.7   1   16.698 ? 273 GLN   A CB   1 
ATOM   2147 C  CG   . GLN   A 1 273 ? 19.091  -3.576  -41.344 1   17.743 ? 273 GLN   A CG   1 
ATOM   2148 C  CD   . GLN   A 1 273 ? 20.137  -2.576  -41.763 1   18.704 ? 273 GLN   A CD   1 
ATOM   2149 O  OE1  . GLN   A 1 273 ? 19.988  -1.9    -42.785 1   20.919 ? 273 GLN   A OE1  1 
ATOM   2150 N  NE2  . GLN   A 1 273 ? 21.136  -2.393  -40.916 1   18.928 ? 273 GLN   A NE2  1 
ATOM   2151 N  N    . ASN   A 1 274 ? 17.855  -4.406  -37.945 1   16.156 ? 274 ASN   A N    1 
ATOM   2152 C  CA   . ASN   A 1 274 ? 18.744  -5.224  -37.129 1   16.842 ? 274 ASN   A CA   1 
ATOM   2153 C  C    . ASN   A 1 274 ? 18.016  -5.944  -35.993 1   18.125 ? 274 ASN   A C    1 
ATOM   2154 O  O    . ASN   A 1 274 ? 18.513  -6.958  -35.513 1   20.251 ? 274 ASN   A O    1 
ATOM   2155 C  CB   . ASN   A 1 274 ? 19.866  -4.395  -36.513 1   17.037 ? 274 ASN   A CB   1 
ATOM   2156 C  CG   . ASN   A 1 274 ? 20.879  -3.916  -37.527 1   17.25  ? 274 ASN   A CG   1 
ATOM   2157 O  OD1  . ASN   A 1 274 ? 20.874  -4.356  -38.68  1   18.542 ? 274 ASN   A OD1  1 
ATOM   2158 N  ND2  . ASN   A 1 274 ? 21.777  -3.027  -37.12  1   17.484 ? 274 ASN   A ND2  1 
ATOM   2159 N  N    . GLY   A 1 275 ? 16.899  -5.385  -35.507 1   18.537 ? 275 GLY   A N    1 
ATOM   2160 C  CA   . GLY   A 1 275 ? 16.358  -5.819  -34.228 1   19.575 ? 275 GLY   A CA   1 
ATOM   2161 C  C    . GLY   A 1 275 ? 17.206  -5.265  -33.084 1   20.226 ? 275 GLY   A C    1 
ATOM   2162 O  O    . GLY   A 1 275 ? 18.012  -4.361  -33.29  1   21.239 ? 275 GLY   A O    1 
ATOM   2163 N  N    . MET   A 1 276 ? 17.018  -5.813  -31.876 1   20.645 ? 276 MET   A N    1 
ATOM   2164 C  CA   A MET   A 1 276 ? 17.604  -5.319  -30.642 0.6 21.776 ? 276 MET   A CA   1 
ATOM   2165 C  CA   B MET   A 1 276 ? 17.689  -5.237  -30.718 0.4 19.757 ? 276 MET   A CA   1 
ATOM   2166 C  C    . MET   A 1 276 ? 18.9    -6.05   -30.276 1   21.483 ? 276 MET   A C    1 
ATOM   2167 O  O    . MET   A 1 276 ? 19.612  -5.614  -29.373 1   22.392 ? 276 MET   A O    1 
ATOM   2168 C  CB   A MET   A 1 276 ? 16.625  -5.588  -29.495 0.6 22.387 ? 276 MET   A CB   1 
ATOM   2169 C  CB   B MET   A 1 276 ? 16.742  -5.078  -29.529 0.4 17.736 ? 276 MET   A CB   1 
ATOM   2170 C  CG   A MET   A 1 276 ? 15.251  -4.979  -29.656 0.6 23.61  ? 276 MET   A CG   1 
ATOM   2171 C  CG   B MET   A 1 276 ? 15.718  -4.004  -29.755 0.4 16.098 ? 276 MET   A CG   1 
ATOM   2172 S  SD   A MET   A 1 276 ? 15.348  -3.183  -29.606 0.6 25.41  ? 276 MET   A SD   1 
ATOM   2173 S  SD   B MET   A 1 276 ? 14.904  -3.581  -28.212 0.4 14.263 ? 276 MET   A SD   1 
ATOM   2174 C  CE   A MET   A 1 276 ? 13.676  -2.752  -29.103 0.6 25.325 ? 276 MET   A CE   1 
ATOM   2175 C  CE   B MET   A 1 276 ? 13.603  -2.53   -28.863 0.4 14.841 ? 276 MET   A CE   1 
ATOM   2176 N  N    . ASN   A 1 277 ? 19.149  -7.208  -30.904 1   22.918 ? 277 ASN   A N    1 
ATOM   2177 C  CA   . ASN   A 1 277 ? 20.3    -8.031  -30.554 1   24.927 ? 277 ASN   A CA   1 
ATOM   2178 C  C    . ASN   A 1 277 ? 20.364  -8.287  -29.047 1   24.705 ? 277 ASN   A C    1 
ATOM   2179 O  O    . ASN   A 1 277 ? 21.427  -8.184  -28.427 1   26.665 ? 277 ASN   A O    1 
ATOM   2180 C  CB   . ASN   A 1 277 ? 21.585  -7.401  -31.078 1   26.407 ? 277 ASN   A CB   1 
ATOM   2181 C  CG   . ASN   A 1 277 ? 21.774  -7.687  -32.546 1   30.193 ? 277 ASN   A CG   1 
ATOM   2182 O  OD1  . ASN   A 1 277 ? 22.156  -8.811  -32.896 1   34.654 ? 277 ASN   A OD1  1 
ATOM   2183 N  ND2  . ASN   A 1 277 ? 21.539  -6.703  -33.406 1   30.469 ? 277 ASN   A ND2  1 
ATOM   2184 N  N    . GLY   A 1 278 ? 19.21   -8.613  -28.46  1   24.131 ? 278 GLY   A N    1 
ATOM   2185 C  CA   . GLY   A 1 278 ? 19.153  -9.069  -27.083 1   23.966 ? 278 GLY   A CA   1 
ATOM   2186 C  C    . GLY   A 1 278 ? 19.091  -7.928  -26.068 1   23.542 ? 278 GLY   A C    1 
ATOM   2187 O  O    . GLY   A 1 278 ? 19.035  -8.178  -24.867 1   25.65  ? 278 GLY   A O    1 
ATOM   2188 N  N    . ARG   A 1 279 ? 19.083  -6.681  -26.548 1   22.449 ? 279 ARG   A N    1 
ATOM   2189 C  CA   . ARG   A 1 279 ? 18.999  -5.518  -25.683 1   22.393 ? 279 ARG   A CA   1 
ATOM   2190 C  C    . ARG   A 1 279 ? 17.543  -5.097  -25.559 1   20.244 ? 279 ARG   A C    1 
ATOM   2191 O  O    . ARG   A 1 279 ? 16.669  -5.622  -26.243 1   20.498 ? 279 ARG   A O    1 
ATOM   2192 C  CB   . ARG   A 1 279 ? 19.856  -4.376  -26.238 1   24.509 ? 279 ARG   A CB   1 
ATOM   2193 C  CG   . ARG   A 1 279 ? 21.332  -4.722  -26.114 1   26.813 ? 279 ARG   A CG   1 
ATOM   2194 C  CD   . ARG   A 1 279 ? 22.221  -3.756  -26.842 1   29.33  ? 279 ARG   A CD   1 
ATOM   2195 N  NE   . ARG   A 1 279 ? 22.116  -3.973  -28.289 1   31.349 ? 279 ARG   A NE   1 
ATOM   2196 C  CZ   . ARG   A 1 279 ? 22.961  -3.505  -29.201 1   32.404 ? 279 ARG   A CZ   1 
ATOM   2197 N  NH1  . ARG   A 1 279 ? 24.052  -2.857  -28.825 1   33.577 ? 279 ARG   A NH1  1 
ATOM   2198 N  NH2  . ARG   A 1 279 ? 22.716  -3.705  -30.487 1   32.289 ? 279 ARG   A NH2  1 
ATOM   2199 N  N    . THR   A 1 280 ? 17.294  -4.149  -24.659 1   19.379 ? 280 THR   A N    1 
ATOM   2200 C  CA   . THR   A 1 280 ? 15.983  -3.543  -24.539 1   18.249 ? 280 THR   A CA   1 
ATOM   2201 C  C    . THR   A 1 280 ? 16.147  -2.029  -24.596 1   17.989 ? 280 THR   A C    1 
ATOM   2202 O  O    . THR   A 1 280 ? 17.253  -1.495  -24.46  1   18.884 ? 280 THR   A O    1 
ATOM   2203 C  CB   . THR   A 1 280 ? 15.274  -3.979  -23.257 1   19.726 ? 280 THR   A CB   1 
ATOM   2204 O  OG1  . THR   A 1 280 ? 16.127  -3.663  -22.163 1   21.814 ? 280 THR   A OG1  1 
ATOM   2205 C  CG2  . THR   A 1 280 ? 14.921  -5.455  -23.242 1   20.66  ? 280 THR   A CG2  1 
ATOM   2206 N  N    . ILE   A 1 281 ? 15.013  -1.365  -24.829 1   16.487 ? 281 ILE   A N    1 
ATOM   2207 C  CA   . ILE   A 1 281 ? 14.912  0.082   -24.79  1   15.768 ? 281 ILE   A CA   1 
ATOM   2208 C  C    . ILE   A 1 281 ? 13.786  0.409   -23.821 1   16.058 ? 281 ILE   A C    1 
ATOM   2209 O  O    . ILE   A 1 281 ? 12.652  -0.021  -24.021 1   15.821 ? 281 ILE   A O    1 
ATOM   2210 C  CB   . ILE   A 1 281 ? 14.662  0.676   -26.187 1   15.363 ? 281 ILE   A CB   1 
ATOM   2211 C  CG1  . ILE   A 1 281 ? 15.778  0.303   -27.169 1   15.628 ? 281 ILE   A CG1  1 
ATOM   2212 C  CG2  . ILE   A 1 281 ? 14.456  2.189   -26.106 1   15.715 ? 281 ILE   A CG2  1 
ATOM   2213 C  CD1  . ILE   A 1 281 ? 15.556  0.798   -28.59  1   15.53  ? 281 ILE   A CD1  1 
ATOM   2214 N  N    . LEU   A 1 282 ? 14.124  1.121   -22.748 1   16.434 ? 282 LEU   A N    1 
ATOM   2215 C  CA   . LEU   A 1 282 ? 13.155  1.445   -21.711 1   16.845 ? 282 LEU   A CA   1 
ATOM   2216 C  C    . LEU   A 1 282 ? 12.366  0.197   -21.311 1   18.019 ? 282 LEU   A C    1 
ATOM   2217 O  O    . LEU   A 1 282 ? 11.148  0.237   -21.114 1   19.265 ? 282 LEU   A O    1 
ATOM   2218 C  CB   . LEU   A 1 282 ? 12.255  2.587   -22.176 1   16.159 ? 282 LEU   A CB   1 
ATOM   2219 C  CG   . LEU   A 1 282 ? 12.946  3.95    -22.293 1   15.783 ? 282 LEU   A CG   1 
ATOM   2220 C  CD1  . LEU   A 1 282 ? 12.044  4.95    -22.963 1   15.72  ? 282 LEU   A CD1  1 
ATOM   2221 C  CD2  . LEU   A 1 282 ? 13.388  4.46    -20.925 1   16.017 ? 282 LEU   A CD2  1 
ATOM   2222 N  N    . GLY   A 1 283 ? 13.093  -0.912  -21.164 1   18.868 ? 283 GLY   A N    1 
ATOM   2223 C  CA   . GLY   A 1 283 ? 12.518  -2.152  -20.675 1   19.655 ? 283 GLY   A CA   1 
ATOM   2224 C  C    . GLY   A 1 283 ? 11.711  -2.95   -21.701 1   19.793 ? 283 GLY   A C    1 
ATOM   2225 O  O    . GLY   A 1 283 ? 11.167  -3.983  -21.337 1   23.689 ? 283 GLY   A O    1 
ATOM   2226 N  N    A SER   A 1 284 ? 11.647  -2.486  -22.96  0.5 18.117 ? 284 SER   A N    1 
ATOM   2227 N  N    B SER   A 1 284 ? 11.662  -2.489  -22.958 0.5 18.185 ? 284 SER   A N    1 
ATOM   2228 C  CA   A SER   A 1 284 ? 10.885  -3.151  -24.011 0.5 17.717 ? 284 SER   A CA   1 
ATOM   2229 C  CA   B SER   A 1 284 ? 10.901  -3.146  -24.011 0.5 17.726 ? 284 SER   A CA   1 
ATOM   2230 C  C    A SER   A 1 284 ? 11.813  -3.814  -25.029 0.5 16.975 ? 284 SER   A C    1 
ATOM   2231 C  C    B SER   A 1 284 ? 11.822  -3.818  -25.028 0.5 17.007 ? 284 SER   A C    1 
ATOM   2232 O  O    A SER   A 1 284 ? 12.855  -3.261  -25.374 0.5 17.515 ? 284 SER   A O    1 
ATOM   2233 O  O    B SER   A 1 284 ? 12.862  -3.266  -25.378 0.5 17.542 ? 284 SER   A O    1 
ATOM   2234 C  CB   A SER   A 1 284 ? 9.963   -2.171  -24.713 0.5 17.73  ? 284 SER   A CB   1 
ATOM   2235 C  CB   B SER   A 1 284 ? 10.027  -2.153  -24.722 0.5 17.792 ? 284 SER   A CB   1 
ATOM   2236 O  OG   A SER   A 1 284 ? 9.195   -2.791  -25.746 0.5 18.336 ? 284 SER   A OG   1 
ATOM   2237 O  OG   B SER   A 1 284 ? 9.105   -1.541  -23.834 0.5 18.551 ? 284 SER   A OG   1 
ATOM   2238 N  N    . ALA   A 1 285 ? 11.395  -4.986  -25.525 1   17.178 ? 285 ALA   A N    1 
ATOM   2239 C  CA   . ALA   A 1 285 ? 12.094  -5.697  -26.584 1   17.934 ? 285 ALA   A CA   1 
ATOM   2240 C  C    . ALA   A 1 285 ? 11.456  -5.437  -27.951 1   18.035 ? 285 ALA   A C    1 
ATOM   2241 O  O    . ALA   A 1 285 ? 11.888  -6.012  -28.947 1   20.82  ? 285 ALA   A O    1 
ATOM   2242 C  CB   . ALA   A 1 285 ? 12.148  -7.179  -26.273 1   19.263 ? 285 ALA   A CB   1 
ATOM   2243 N  N    . LEU   A 1 286 ? 10.439  -4.57   -27.995 1   17.462 ? 286 LEU   A N    1 
ATOM   2244 C  CA   . LEU   A 1 286 ? 9.794   -4.146  -29.229 1   17.978 ? 286 LEU   A CA   1 
ATOM   2245 C  C    . LEU   A 1 286 ? 9.804   -2.622  -29.268 1   16.301 ? 286 LEU   A C    1 
ATOM   2246 O  O    . LEU   A 1 286 ? 9.971   -1.97   -28.245 1   17.219 ? 286 LEU   A O    1 
ATOM   2247 C  CB   . LEU   A 1 286 ? 8.359   -4.653  -29.315 1   20.95  ? 286 LEU   A CB   1 
ATOM   2248 C  CG   . LEU   A 1 286 ? 8.165   -6.167  -29.405 1   24.687 ? 286 LEU   A CG   1 
ATOM   2249 C  CD1  . LEU   A 1 286 ? 6.688   -6.473  -29.215 1   25.988 ? 286 LEU   A CD1  1 
ATOM   2250 C  CD2  . LEU   A 1 286 ? 8.669   -6.742  -30.714 1   27.533 ? 286 LEU   A CD2  1 
ATOM   2251 N  N    . LEU   A 1 287 ? 9.556   -2.057  -30.449 1   15.169 ? 287 LEU   A N    1 
ATOM   2252 C  CA   . LEU   A 1 287 ? 9.498   -0.613  -30.595 1   15.015 ? 287 LEU   A CA   1 
ATOM   2253 C  C    . LEU   A 1 287 ? 8.102   -0.119  -30.214 1   15.375 ? 287 LEU   A C    1 
ATOM   2254 O  O    . LEU   A 1 287 ? 7.099   -0.479  -30.833 1   18.749 ? 287 LEU   A O    1 
ATOM   2255 C  CB   . LEU   A 1 287 ? 9.893   -0.245  -32.023 1   15.865 ? 287 LEU   A CB   1 
ATOM   2256 C  CG   . LEU   A 1 287 ? 11.272  -0.756  -32.462 1   16.942 ? 287 LEU   A CG   1 
ATOM   2257 C  CD1  . LEU   A 1 287 ? 11.556  -0.44   -33.92  1   17.92  ? 287 LEU   A CD1  1 
ATOM   2258 C  CD2  . LEU   A 1 287 ? 12.391  -0.219  -31.58  1   18.603 ? 287 LEU   A CD2  1 
ATOM   2259 N  N    . GLU   A 1 288 ? 8.044   0.726   -29.191 1   14.686 ? 288 GLU   A N    1 
ATOM   2260 C  CA   . GLU   A 1 288 ? 6.785   1.168   -28.615 1   14.927 ? 288 GLU   A CA   1 
ATOM   2261 C  C    . GLU   A 1 288 ? 6.25    2.371   -29.382 1   13.488 ? 288 GLU   A C    1 
ATOM   2262 O  O    . GLU   A 1 288 ? 6.99    3.335   -29.586 1   13.242 ? 288 GLU   A O    1 
ATOM   2263 C  CB   . GLU   A 1 288 ? 7.035   1.585   -27.166 1   16.344 ? 288 GLU   A CB   1 
ATOM   2264 C  CG   . GLU   A 1 288 ? 7.401   0.428   -26.244 1   20.064 ? 288 GLU   A CG   1 
ATOM   2265 C  CD   . GLU   A 1 288 ? 6.266   -0.485  -25.834 1   22.599 ? 288 GLU   A CD   1 
ATOM   2266 O  OE1  . GLU   A 1 288 ? 5.056   -0.233  -26.116 1   24.629 ? 288 GLU   A OE1  1 
ATOM   2267 O  OE2  . GLU   A 1 288 ? 6.644   -1.476  -25.146 1   27.837 ? 288 GLU   A OE2  1 
ATOM   2268 N  N    . ASP   A 1 289 ? 4.941   2.353   -29.709 1   12.919 ? 289 ASP   A N    1 
ATOM   2269 C  CA   . ASP   A 1 289 ? 4.367   3.429   -30.511 1   13.266 ? 289 ASP   A CA   1 
ATOM   2270 C  C    . ASP   A 1 289 ? 3.149   4.1     -29.87  1   13.279 ? 289 ASP   A C    1 
ATOM   2271 O  O    . ASP   A 1 289 ? 2.438   4.822   -30.568 1   13.566 ? 289 ASP   A O    1 
ATOM   2272 C  CB   . ASP   A 1 289 ? 4.043   2.981   -31.928 1   14.332 ? 289 ASP   A CB   1 
ATOM   2273 C  CG   . ASP   A 1 289 ? 2.781   2.154   -32.108 1   14.009 ? 289 ASP   A CG   1 
ATOM   2274 O  OD1  . ASP   A 1 289 ? 2.258   1.619   -31.102 1   14.734 ? 289 ASP   A OD1  1 
ATOM   2275 O  OD2  . ASP   A 1 289 ? 2.329   2.058   -33.263 1   14.662 ? 289 ASP   A OD2  1 
ATOM   2276 N  N    . GLU   A 1 290 ? 2.922   3.928   -28.561 1   12.928 ? 290 GLU   A N    1 
ATOM   2277 C  CA   . GLU   A 1 290 ? 1.771   4.554   -27.914 1   13.039 ? 290 GLU   A CA   1 
ATOM   2278 C  C    . GLU   A 1 290 ? 2.186   5.617   -26.894 1   12.919 ? 290 GLU   A C    1 
ATOM   2279 O  O    . GLU   A 1 290 ? 1.435   5.915   -25.969 1   13.716 ? 290 GLU   A O    1 
ATOM   2280 C  CB   . GLU   A 1 290 ? 0.773   3.514   -27.389 1   13.813 ? 290 GLU   A CB   1 
ATOM   2281 C  CG   . GLU   A 1 290 ? 0.128   2.707   -28.519 1   14.764 ? 290 GLU   A CG   1 
ATOM   2282 C  CD   . GLU   A 1 290 ? -1.214  2.061   -28.217 1   14.832 ? 290 GLU   A CD   1 
ATOM   2283 O  OE1  . GLU   A 1 290 ? -1.681  2.171   -27.052 1   16.141 ? 290 GLU   A OE1  1 
ATOM   2284 O  OE2  . GLU   A 1 290 ? -1.805  1.45    -29.155 1   15.373 ? 290 GLU   A OE2  1 
ATOM   2285 N  N    . PHE   A 1 291 ? 3.349   6.246   -27.112 1   13.002 ? 291 PHE   A N    1 
ATOM   2286 C  CA   . PHE   A 1 291 ? 3.713   7.473   -26.425 1   13.333 ? 291 PHE   A CA   1 
ATOM   2287 C  C    . PHE   A 1 291 ? 3.905   8.591   -27.442 1   12.898 ? 291 PHE   A C    1 
ATOM   2288 O  O    . PHE   A 1 291 ? 4.723   8.465   -28.354 1   13.296 ? 291 PHE   A O    1 
ATOM   2289 C  CB   . PHE   A 1 291 ? 5.021   7.359   -25.647 1   14.648 ? 291 PHE   A CB   1 
ATOM   2290 C  CG   . PHE   A 1 291 ? 4.993   6.344   -24.527 1   16.018 ? 291 PHE   A CG   1 
ATOM   2291 C  CD1  . PHE   A 1 291 ? 4.501   6.712   -23.281 1   16.695 ? 291 PHE   A CD1  1 
ATOM   2292 C  CD2  . PHE   A 1 291 ? 5.485   5.057   -24.706 1   17.195 ? 291 PHE   A CD2  1 
ATOM   2293 C  CE1  . PHE   A 1 291 ? 4.532   5.823   -22.236 1   18.787 ? 291 PHE   A CE1  1 
ATOM   2294 C  CE2  . PHE   A 1 291 ? 5.503   4.161   -23.645 1   18.886 ? 291 PHE   A CE2  1 
ATOM   2295 C  CZ   . PHE   A 1 291 ? 5       4.543   -22.419 1   18.836 ? 291 PHE   A CZ   1 
ATOM   2296 N  N    . THR   A 1 292 ? 3.163   9.687   -27.285 1   13.381 ? 292 THR   A N    1 
ATOM   2297 C  CA   . THR   A 1 292 ? 3.311   10.823  -28.176 1   13.781 ? 292 THR   A CA   1 
ATOM   2298 C  C    . THR   A 1 292 ? 4.487   11.684  -27.751 1   14.026 ? 292 THR   A C    1 
ATOM   2299 O  O    . THR   A 1 292 ? 4.962   11.598  -26.628 1   13.96  ? 292 THR   A O    1 
ATOM   2300 C  CB   . THR   A 1 292 ? 2.048   11.676  -28.221 1   14.115 ? 292 THR   A CB   1 
ATOM   2301 O  OG1  . THR   A 1 292 ? 1.97    12.327  -26.962 1   14.352 ? 292 THR   A OG1  1 
ATOM   2302 C  CG2  . THR   A 1 292 ? 0.784   10.876  -28.467 1   14.595 ? 292 THR   A CG2  1 
ATOM   2303 N  N    . PRO   A 1 293 ? 4.962   12.59   -28.622 1   14.281 ? 293 PRO   A N    1 
ATOM   2304 C  CA   . PRO   A 1 293 ? 5.932   13.594  -28.195 1   14.901 ? 293 PRO   A CA   1 
ATOM   2305 C  C    . PRO   A 1 293 ? 5.507   14.362  -26.946 1   15.01  ? 293 PRO   A C    1 
ATOM   2306 O  O    . PRO   A 1 293 ? 6.321   14.6    -26.049 1   15.553 ? 293 PRO   A O    1 
ATOM   2307 C  CB   . PRO   A 1 293 ? 6.06    14.488  -29.438 1   15.464 ? 293 PRO   A CB   1 
ATOM   2308 C  CG   . PRO   A 1 293 ? 5.786   13.542  -30.594 1   15.756 ? 293 PRO   A CG   1 
ATOM   2309 C  CD   . PRO   A 1 293 ? 4.685   12.633  -30.067 1   15.418 ? 293 PRO   A CD   1 
ATOM   2310 N  N    . PHE   A 1 294 ? 4.219   14.725  -26.877 1   15.258 ? 294 PHE   A N    1 
ATOM   2311 C  CA   . PHE   A 1 294 ? 3.705   15.454  -25.729 1   15.738 ? 294 PHE   A CA   1 
ATOM   2312 C  C    . PHE   A 1 294 ? 3.771   14.582  -24.469 1   15.157 ? 294 PHE   A C    1 
ATOM   2313 O  O    . PHE   A 1 294 ? 4.102   15.06   -23.388 1   16.511 ? 294 PHE   A O    1 
ATOM   2314 C  CB   . PHE   A 1 294 ? 2.29    15.929  -26.071 1   16.832 ? 294 PHE   A CB   1 
ATOM   2315 C  CG   . PHE   A 1 294 ? 1.648   16.877  -25.078 1   19.316 ? 294 PHE   A CG   1 
ATOM   2316 C  CD1  . PHE   A 1 294 ? 1.079   16.39   -23.912 1   20.125 ? 294 PHE   A CD1  1 
ATOM   2317 C  CD2  . PHE   A 1 294 ? 1.574   18.244  -25.335 1   20.591 ? 294 PHE   A CD2  1 
ATOM   2318 C  CE1  . PHE   A 1 294 ? 0.475   17.246  -23.009 1   21.2   ? 294 PHE   A CE1  1 
ATOM   2319 C  CE2  . PHE   A 1 294 ? 0.971   19.097  -24.425 1   21.357 ? 294 PHE   A CE2  1 
ATOM   2320 C  CZ   . PHE   A 1 294 ? 0.424   18.596  -23.267 1   21.844 ? 294 PHE   A CZ   1 
ATOM   2321 N  N    . ASP   A 1 295 ? 3.452   13.293  -24.606 1   14.47  ? 295 ASP   A N    1 
ATOM   2322 C  CA   . ASP   A 1 295 ? 3.5     12.353  -23.496 1   14.221 ? 295 ASP   A CA   1 
ATOM   2323 C  C    . ASP   A 1 295 ? 4.916   12.244  -22.93  1   14.457 ? 295 ASP   A C    1 
ATOM   2324 O  O    . ASP   A 1 295 ? 5.105   12.087  -21.729 1   15.156 ? 295 ASP   A O    1 
ATOM   2325 C  CB   . ASP   A 1 295 ? 3.039   10.968  -23.912 1   14.628 ? 295 ASP   A CB   1 
ATOM   2326 C  CG   . ASP   A 1 295 ? 1.575   10.827  -24.277 1   15.116 ? 295 ASP   A CG   1 
ATOM   2327 O  OD1  . ASP   A 1 295 ? 0.795   11.734  -23.896 1   15.719 ? 295 ASP   A OD1  1 
ATOM   2328 O  OD2  . ASP   A 1 295 ? 1.257   9.808   -24.937 1   14.799 ? 295 ASP   A OD2  1 
ATOM   2329 N  N    . VAL   A 1 296 ? 5.918   12.281  -23.81  1   13.877 ? 296 VAL   A N    1 
ATOM   2330 C  CA   . VAL   A 1 296 ? 7.294   12.151  -23.366 1   14.064 ? 296 VAL   A CA   1 
ATOM   2331 C  C    . VAL   A 1 296 ? 7.686   13.391  -22.571 1   14.448 ? 296 VAL   A C    1 
ATOM   2332 O  O    . VAL   A 1 296 ? 8.275   13.273  -21.502 1   14.563 ? 296 VAL   A O    1 
ATOM   2333 C  CB   . VAL   A 1 296 ? 8.234   11.905  -24.556 1   14.411 ? 296 VAL   A CB   1 
ATOM   2334 C  CG1  . VAL   A 1 296 ? 9.697   12.028  -24.139 1   14.668 ? 296 VAL   A CG1  1 
ATOM   2335 C  CG2  . VAL   A 1 296 ? 7.951   10.559  -25.207 1   14.246 ? 296 VAL   A CG2  1 
ATOM   2336 N  N    . VAL   A 1 297 ? 7.359   14.576  -23.084 1   14.968 ? 297 VAL   A N    1 
ATOM   2337 C  CA   . VAL   A 1 297 ? 7.656   15.807  -22.371 1   16.508 ? 297 VAL   A CA   1 
ATOM   2338 C  C    . VAL   A 1 297 ? 6.901   15.843  -21.039 1   16.81  ? 297 VAL   A C    1 
ATOM   2339 O  O    . VAL   A 1 297 ? 7.436   16.318  -20.039 1   18.477 ? 297 VAL   A O    1 
ATOM   2340 C  CB   . VAL   A 1 297 ? 7.345   17.022  -23.263 1   17.471 ? 297 VAL   A CB   1 
ATOM   2341 C  CG1  . VAL   A 1 297 ? 7.394   18.33   -22.487 1   18.507 ? 297 VAL   A CG1  1 
ATOM   2342 C  CG2  . VAL   A 1 297 ? 8.283   17.057  -24.473 1   18.17  ? 297 VAL   A CG2  1 
ATOM   2343 N  N    . ARG   A 1 298 ? 5.659   15.339  -21.016 1   16.534 ? 298 ARG   A N    1 
ATOM   2344 C  CA   . ARG   A 1 298 ? 4.852   15.283  -19.8   1   17.442 ? 298 ARG   A CA   1 
ATOM   2345 C  C    . ARG   A 1 298 ? 5.584   14.51   -18.701 1   17.007 ? 298 ARG   A C    1 
ATOM   2346 O  O    . ARG   A 1 298 ? 5.613   14.928  -17.549 1   18.701 ? 298 ARG   A O    1 
ATOM   2347 C  CB   . ARG   A 1 298 ? 3.496   14.629  -20.097 1   17.86  ? 298 ARG   A CB   1 
ATOM   2348 C  CG   . ARG   A 1 298 ? 2.657   14.259  -18.879 1   18.954 ? 298 ARG   A CG   1 
ATOM   2349 C  CD   . ARG   A 1 298 ? 1.325   13.591  -19.205 1   19.009 ? 298 ARG   A CD   1 
ATOM   2350 N  NE   . ARG   A 1 298 ? 0.657   13.134  -17.978 1   18.458 ? 298 ARG   A NE   1 
ATOM   2351 C  CZ   . ARG   A 1 298 ? 0.081   11.952  -17.799 1   18.291 ? 298 ARG   A CZ   1 
ATOM   2352 N  NH1  . ARG   A 1 298 ? -0.082  11.129  -18.819 1   19.226 ? 298 ARG   A NH1  1 
ATOM   2353 N  NH2  . ARG   A 1 298 ? -0.365  11.621  -16.599 1   17.709 ? 298 ARG   A NH2  1 
ATOM   2354 N  N    . GLN   A 1 299 ? 6.167   13.368  -19.07  1   16.141 ? 299 GLN   A N    1 
ATOM   2355 C  CA   . GLN   A 1 299 ? 6.649   12.385  -18.116 1   16.36  ? 299 GLN   A CA   1 
ATOM   2356 C  C    . GLN   A 1 299 ? 8.141   12.509  -17.797 1   17.766 ? 299 GLN   A C    1 
ATOM   2357 O  O    . GLN   A 1 299 ? 8.546   12.293  -16.657 1   18.769 ? 299 GLN   A O    1 
ATOM   2358 C  CB   . GLN   A 1 299 ? 6.342   10.981  -18.639 1   15.87  ? 299 GLN   A CB   1 
ATOM   2359 C  CG   . GLN   A 1 299 ? 6.793   9.905   -17.663 1   15.893 ? 299 GLN   A CG   1 
ATOM   2360 C  CD   . GLN   A 1 299 ? 6.342   8.497   -17.967 1   14.844 ? 299 GLN   A CD   1 
ATOM   2361 O  OE1  . GLN   A 1 299 ? 6.798   7.558   -17.317 1   14.816 ? 299 GLN   A OE1  1 
ATOM   2362 N  NE2  . GLN   A 1 299 ? 5.44    8.301   -18.918 1   15.357 ? 299 GLN   A NE2  1 
ATOM   2363 N  N    . CYS   A 1 300 ? 8.97    12.794  -18.803 1   18.431 ? 300 CYS   A N    1 
ATOM   2364 C  CA   . CYS   A 1 300 ? 10.416  12.721  -18.643 1   19.663 ? 300 CYS   A CA   1 
ATOM   2365 C  C    . CYS   A 1 300 ? 10.969  13.983  -17.992 1   20.598 ? 300 CYS   A C    1 
ATOM   2366 O  O    . CYS   A 1 300 ? 10.358  15.041  -18.058 1   20.572 ? 300 CYS   A O    1 
ATOM   2367 C  CB   . CYS   A 1 300 ? 11.108  12.593  -19.993 1   19.409 ? 300 CYS   A CB   1 
ATOM   2368 S  SG   . CYS   A 1 300 ? 11.105  10.923  -20.685 1   24.346 ? 300 CYS   A SG   1 
ATOM   2369 N  N    . SER   A 1 301 ? 12.186  13.859  -17.443 1   20.467 ? 301 SER   A N    1 
ATOM   2370 C  CA   . SER   A 1 301 ? 12.979  15.001  -17.018 1   20.673 ? 301 SER   A CA   1 
ATOM   2371 C  C    . SER   A 1 301 ? 13.21   15.964  -18.184 1   21.266 ? 301 SER   A C    1 
ATOM   2372 O  O    . SER   A 1 301 ? 13.391  15.552  -19.337 1   21.486 ? 301 SER   A O    1 
ATOM   2373 C  CB   . SER   A 1 301 ? 14.293  14.55   -16.441 1   21.036 ? 301 SER   A CB   1 
ATOM   2374 O  OG   . SER   A 1 301 ? 15.044  15.663  -15.97  1   22.987 ? 301 SER   A OG   1 
ATOM   2375 N  N    . GLY   A 1 302 ? 13.25   17.257  -17.85  1   21.683 ? 302 GLY   A N    1 
ATOM   2376 C  CA   . GLY   A 1 302 ? 13.687  18.288  -18.78  1   22.765 ? 302 GLY   A CA   1 
ATOM   2377 C  C    . GLY   A 1 302 ? 15.208  18.344  -18.928 1   23.872 ? 302 GLY   A C    1 
ATOM   2378 O  O    . GLY   A 1 302 ? 15.701  19.138  -19.728 1   25.984 ? 302 GLY   A O    1 
ATOM   2379 N  N    . VAL   A 1 303 ? 15.941  17.545  -18.13  1   23.962 ? 303 VAL   A N    1 
ATOM   2380 C  CA   . VAL   A 1 303 ? 17.397  17.464  -18.194 1   25.252 ? 303 VAL   A CA   1 
ATOM   2381 C  C    . VAL   A 1 303 ? 17.788  16.062  -18.669 1   24.564 ? 303 VAL   A C    1 
ATOM   2382 O  O    . VAL   A 1 303 ? 17.401  15.066  -18.064 1   26.295 ? 303 VAL   A O    1 
ATOM   2383 C  CB   . VAL   A 1 303 ? 18.014  17.779  -16.814 1   27.696 ? 303 VAL   A CB   1 
ATOM   2384 C  CG1  . VAL   A 1 303 ? 19.531  17.673  -16.825 1   28.716 ? 303 VAL   A CG1  1 
ATOM   2385 C  CG2  . VAL   A 1 303 ? 17.599  19.148  -16.294 1   29     ? 303 VAL   A CG2  1 
ATOM   2386 N  N    . THR   A 1 304 ? 18.543  15.984  -19.772 1   23.681 ? 304 THR   A N    1 
ATOM   2387 C  CA   . THR   A 1 304 ? 19.001  14.715  -20.321 1   23.196 ? 304 THR   A CA   1 
ATOM   2388 C  C    . THR   A 1 304 ? 20.1    14.143  -19.424 1   22.946 ? 304 THR   A C    1 
ATOM   2389 O  O    . THR   A 1 304 ? 20.974  14.876  -18.965 1   23.814 ? 304 THR   A O    1 
ATOM   2390 C  CB   . THR   A 1 304 ? 19.502  14.936  -21.751 1   23.504 ? 304 THR   A CB   1 
ATOM   2391 O  OG1  . THR   A 1 304 ? 18.38   15.348  -22.53  1   24.859 ? 304 THR   A OG1  1 
ATOM   2392 C  CG2  . THR   A 1 304 ? 20.078  13.68   -22.376 1   24.479 ? 304 THR   A CG2  1 
ATOM   2393 N  N    . PHE   A 1 305 ? 20.066  12.826  -19.19  1   22.217 ? 305 PHE   A N    1 
ATOM   2394 C  CA   . PHE   A 1 305 ? 21.149  12.141  -18.496 1   22.26  ? 305 PHE   A CA   1 
ATOM   2395 C  C    . PHE   A 1 305 ? 22.256  11.839  -19.503 1   22.827 ? 305 PHE   A C    1 
ATOM   2396 O  O    . PHE   A 1 305 ? 22.162  10.861  -20.24  1   23.427 ? 305 PHE   A O    1 
ATOM   2397 C  CB   . PHE   A 1 305 ? 20.597  10.874  -17.828 1   22.749 ? 305 PHE   A CB   1 
ATOM   2398 C  CG   . PHE   A 1 305 ? 21.579  10.027  -17.02  1   23.131 ? 305 PHE   A CG   1 
ATOM   2399 C  CD1  . PHE   A 1 305 ? 22.749  10.565  -16.485 1   24.189 ? 305 PHE   A CD1  1 
ATOM   2400 C  CD2  . PHE   A 1 305 ? 21.3    8.688   -16.764 1   24.429 ? 305 PHE   A CD2  1 
ATOM   2401 C  CE1  . PHE   A 1 305 ? 23.624  9.773   -15.75  1   25.066 ? 305 PHE   A CE1  1 
ATOM   2402 C  CE2  . PHE   A 1 305 ? 22.175  7.903   -16.024 1   25.357 ? 305 PHE   A CE2  1 
ATOM   2403 C  CZ   . PHE   A 1 305 ? 23.336  8.447   -15.517 1   25.294 ? 305 PHE   A CZ   1 
ATOM   2404 N  N    . GLN   A 1 306 ? 23.305  12.674  -19.518 1   24.106 ? 306 GLN   A N    1 
ATOM   2405 C  CA   . GLN   A 1 306 ? 24.284  12.672  -20.596 1   24.764 ? 306 GLN   A CA   1 
ATOM   2406 C  C    . GLN   A 1 306 ? 25.374  11.59   -20.434 1   24.397 ? 306 GLN   A C    1 
ATOM   2407 O  O    . GLN   A 1 306 ? 25.965  11.254  -21.481 1   23.999 ? 306 GLN   A O    1 
ATOM   2408 C  CB   . GLN   A 1 306 ? 24.935  14.049  -20.716 1   26.526 ? 306 GLN   A CB   1 
ATOM   2409 C  CG   . GLN   A 1 306 ? 24      15.116  -21.271 1   28.573 ? 306 GLN   A CG   1 
ATOM   2410 C  CD   . GLN   A 1 306 ? 24.706  16.434  -21.485 1   32.625 ? 306 GLN   A CD   1 
ATOM   2411 O  OE1  . GLN   A 1 306 ? 25.657  16.528  -22.269 1   36.295 ? 306 GLN   A OE1  1 
ATOM   2412 N  NE2  . GLN   A 1 306 ? 24.266  17.461  -20.774 1   35.155 ? 306 GLN   A NE2  1 
ATOM   2413 O  OXT  . GLN   A 1 306 ? 25.606  11.123  -19.306 1   25.038 ? 306 GLN   A OXT  1 
ATOM   2414 N  N    . SER   B 1 1   ? -12.905 -8.256  -24.65  1   17.162 ? 1   SER   B N    1 
ATOM   2415 C  CA   . SER   B 1 1   ? -11.567 -8.88   -24.539 1   17.534 ? 1   SER   B CA   1 
ATOM   2416 C  C    . SER   B 1 1   ? -10.479 -7.8    -24.546 1   17.074 ? 1   SER   B C    1 
ATOM   2417 O  O    . SER   B 1 1   ? -10.769 -6.605  -24.571 1   16.57  ? 1   SER   B O    1 
ATOM   2418 C  CB   . SER   B 1 1   ? -11.38  -9.924  -25.612 1   19.387 ? 1   SER   B CB   1 
ATOM   2419 O  OG   . SER   B 1 1   ? -11.189 -9.338  -26.886 1   20.425 ? 1   SER   B OG   1 
ATOM   2420 N  N    . GLY   B 1 2   ? -9.227  -8.255  -24.483 1   17.852 ? 2   GLY   B N    1 
ATOM   2421 C  CA   . GLY   B 1 2   ? -8.078  -7.376  -24.41  1   17.911 ? 2   GLY   B CA   1 
ATOM   2422 C  C    . GLY   B 1 2   ? -7.462  -7.473  -23.021 1   18.566 ? 2   GLY   B C    1 
ATOM   2423 O  O    . GLY   B 1 2   ? -8.15   -7.776  -22.051 1   20.748 ? 2   GLY   B O    1 
ATOM   2424 N  N    . PHE   B 1 3   ? -6.172  -7.168  -22.921 1   19.511 ? 3   PHE   B N    1 
ATOM   2425 C  CA   . PHE   B 1 3   ? -5.475  -7.289  -21.654 1   20.205 ? 3   PHE   B CA   1 
ATOM   2426 C  C    . PHE   B 1 3   ? -4.429  -6.188  -21.586 1   19.821 ? 3   PHE   B C    1 
ATOM   2427 O  O    . PHE   B 1 3   ? -3.508  -6.166  -22.396 1   24.094 ? 3   PHE   B O    1 
ATOM   2428 C  CB   . PHE   B 1 3   ? -4.861  -8.683  -21.484 1   21.197 ? 3   PHE   B CB   1 
ATOM   2429 C  CG   . PHE   B 1 3   ? -4.56   -9.003  -20.022 1   21.789 ? 3   PHE   B CG   1 
ATOM   2430 C  CD1  . PHE   B 1 3   ? -5.596  -9.357  -19.162 1   22.577 ? 3   PHE   B CD1  1 
ATOM   2431 C  CD2  . PHE   B 1 3   ? -3.269  -8.911  -19.5   1   22.93  ? 3   PHE   B CD2  1 
ATOM   2432 C  CE1  . PHE   B 1 3   ? -5.35   -9.624  -17.826 1   22.992 ? 3   PHE   B CE1  1 
ATOM   2433 C  CE2  . PHE   B 1 3   ? -3.026  -9.178  -18.163 1   22.466 ? 3   PHE   B CE2  1 
ATOM   2434 C  CZ   . PHE   B 1 3   ? -4.072  -9.511  -17.323 1   22.46  ? 3   PHE   B CZ   1 
ATOM   2435 N  N    . ARG   B 1 4   ? -4.578  -5.304  -20.594 1   18.852 ? 4   ARG   B N    1 
ATOM   2436 C  CA   . ARG   B 1 4   ? -3.749  -4.127  -20.457 1   18.205 ? 4   ARG   B CA   1 
ATOM   2437 C  C    . ARG   B 1 4   ? -3.249  -4.002  -19.022 1   17.55  ? 4   ARG   B C    1 
ATOM   2438 O  O    . ARG   B 1 4   ? -3.892  -4.458  -18.089 1   17.32  ? 4   ARG   B O    1 
ATOM   2439 C  CB   . ARG   B 1 4   ? -4.583  -2.892  -20.795 1   18.788 ? 4   ARG   B CB   1 
ATOM   2440 C  CG   . ARG   B 1 4   ? -5.089  -2.878  -22.232 1   19.832 ? 4   ARG   B CG   1 
ATOM   2441 C  CD   . ARG   B 1 4   ? -3.966  -3.03   -23.244 1   20.325 ? 4   ARG   B CD   1 
ATOM   2442 N  NE   . ARG   B 1 4   ? -2.989  -2.01   -22.861 1   20.54  ? 4   ARG   B NE   1 
ATOM   2443 C  CZ   . ARG   B 1 4   ? -3.24   -0.719  -22.903 1   20.887 ? 4   ARG   B CZ   1 
ATOM   2444 N  NH1  . ARG   B 1 4   ? -4.22   -0.285  -23.677 1   20.793 ? 4   ARG   B NH1  1 
ATOM   2445 N  NH2  . ARG   B 1 4   ? -2.453  0.133   -22.256 1   21.255 ? 4   ARG   B NH2  1 
ATOM   2446 N  N    . LYS   B 1 5   ? -2.101  -3.345  -18.859 1   17.29  ? 5   LYS   B N    1 
ATOM   2447 C  CA   . LYS   B 1 5   ? -1.647  -2.949  -17.538 1   17.56  ? 5   LYS   B CA   1 
ATOM   2448 C  C    . LYS   B 1 5   ? -2.597  -1.873  -17.017 1   16.593 ? 5   LYS   B C    1 
ATOM   2449 O  O    . LYS   B 1 5   ? -2.667  -0.767  -17.534 1   18.786 ? 5   LYS   B O    1 
ATOM   2450 C  CB   . LYS   B 1 5   ? -0.171  -2.536  -17.555 1   20.295 ? 5   LYS   B CB   1 
ATOM   2451 C  CG   . LYS   B 1 5   ? 0.489   -2.591  -16.189 1   21.913 ? 5   LYS   B CG   1 
ATOM   2452 C  CD   . LYS   B 1 5   ? 0.924   -3.976  -15.718 1   24.361 ? 5   LYS   B CD   1 
ATOM   2453 C  CE   . LYS   B 1 5   ? 2.261   -4.465  -16.277 1   25.312 ? 5   LYS   B CE   1 
ATOM   2454 N  N    . MET   B 1 6   ? -3.389  -2.246  -16.023 1   14.739 ? 6   MET   B N    1 
ATOM   2455 C  CA   . MET   B 1 6   ? -4.497  -1.437  -15.55  1   15.272 ? 6   MET   B CA   1 
ATOM   2456 C  C    . MET   B 1 6   ? -4.29   -1.042  -14.087 1   14.604 ? 6   MET   B C    1 
ATOM   2457 O  O    . MET   B 1 6   ? -4.049  -1.906  -13.239 1   16.704 ? 6   MET   B O    1 
ATOM   2458 C  CB   . MET   B 1 6   ? -5.763  -2.288  -15.682 1   18.361 ? 6   MET   B CB   1 
ATOM   2459 C  CG   . MET   B 1 6   ? -7.034  -1.625  -15.307 1   21.668 ? 6   MET   B CG   1 
ATOM   2460 S  SD   . MET   B 1 6   ? -8.404  -2.735  -15.665 1   28.077 ? 6   MET   B SD   1 
ATOM   2461 C  CE   . MET   B 1 6   ? -8.15   -3.065  -17.405 1   22.358 ? 6   MET   B CE   1 
ATOM   2462 N  N    . ALA   B 1 7   ? -4.384  0.261   -13.798 1   13.533 ? 7   ALA   B N    1 
ATOM   2463 C  CA   . ALA   B 1 7   ? -4.334  0.754   -12.43  1   13.614 ? 7   ALA   B CA   1 
ATOM   2464 C  C    . ALA   B 1 7   ? -5.734  0.783   -11.838 1   13.275 ? 7   ALA   B C    1 
ATOM   2465 O  O    . ALA   B 1 7   ? -6.733  0.81    -12.548 1   13.689 ? 7   ALA   B O    1 
ATOM   2466 C  CB   . ALA   B 1 7   ? -3.729  2.139   -12.371 1   14.321 ? 7   ALA   B CB   1 
ATOM   2467 N  N    . PHE   B 1 8   ? -5.802  0.839   -10.51  1   13.718 ? 8   PHE   B N    1 
ATOM   2468 C  CA   . PHE   B 1 8   ? -7.067  1.091   -9.84   1   14.542 ? 8   PHE   B CA   1 
ATOM   2469 C  C    . PHE   B 1 8   ? -7.504  2.527   -10.105 1   14.302 ? 8   PHE   B C    1 
ATOM   2470 O  O    . PHE   B 1 8   ? -6.679  3.429   -10.234 1   14.498 ? 8   PHE   B O    1 
ATOM   2471 C  CB   . PHE   B 1 8   ? -6.959  0.872   -8.329  1   15.726 ? 8   PHE   B CB   1 
ATOM   2472 C  CG   . PHE   B 1 8   ? -6.875  -0.588  -7.938  1   17.093 ? 8   PHE   B CG   1 
ATOM   2473 C  CD1  . PHE   B 1 8   ? -8.015  -1.379  -7.898  1   18.818 ? 8   PHE   B CD1  1 
ATOM   2474 C  CD2  . PHE   B 1 8   ? -5.651  -1.168  -7.65   1   18.851 ? 8   PHE   B CD2  1 
ATOM   2475 C  CE1  . PHE   B 1 8   ? -7.923  -2.719  -7.563  1   20.468 ? 8   PHE   B CE1  1 
ATOM   2476 C  CE2  . PHE   B 1 8   ? -5.571  -2.511  -7.33   1   20.265 ? 8   PHE   B CE2  1 
ATOM   2477 C  CZ   . PHE   B 1 8   ? -6.706  -3.273  -7.261  1   20.937 ? 8   PHE   B CZ   1 
ATOM   2478 N  N    . PRO   B 1 9   ? -8.825  2.81    -10.114 1   15.145 ? 9   PRO   B N    1 
ATOM   2479 C  CA   . PRO   B 1 9   ? -9.286  4.195   -10.131 1   14.939 ? 9   PRO   B CA   1 
ATOM   2480 C  C    . PRO   B 1 9   ? -8.695  4.938   -8.931  1   14.758 ? 9   PRO   B C    1 
ATOM   2481 O  O    . PRO   B 1 9   ? -8.738  4.42    -7.82   1   16.973 ? 9   PRO   B O    1 
ATOM   2482 C  CB   . PRO   B 1 9   ? -10.826 4.059   -10.066 1   15.981 ? 9   PRO   B CB   1 
ATOM   2483 C  CG   . PRO   B 1 9   ? -11.109 2.625   -10.469 1   16.842 ? 9   PRO   B CG   1 
ATOM   2484 C  CD   . PRO   B 1 9   ? -9.912  1.836   -9.965  1   15.693 ? 9   PRO   B CD   1 
ATOM   2485 N  N    . SER   B 1 10  ? -8.164  6.145   -9.161  1   14.44  ? 10  SER   B N    1 
ATOM   2486 C  CA   . SER   B 1 10  ? -7.337  6.832   -8.172  1   13.671 ? 10  SER   B CA   1 
ATOM   2487 C  C    . SER   B 1 10  ? -8.097  7.894   -7.373  1   14.165 ? 10  SER   B C    1 
ATOM   2488 O  O    . SER   B 1 10  ? -7.522  8.514   -6.482  1   14.441 ? 10  SER   B O    1 
ATOM   2489 C  CB   . SER   B 1 10  ? -6.128  7.449   -8.835  1   14.13  ? 10  SER   B CB   1 
ATOM   2490 O  OG   . SER   B 1 10  ? -6.511  8.331   -9.878  1   14.551 ? 10  SER   B OG   1 
ATOM   2491 N  N    . GLY   B 1 11  ? -9.381  8.116   -7.673  1   15.124 ? 11  GLY   B N    1 
ATOM   2492 C  CA   . GLY   B 1 11  ? -10.13  9.218   -7.079  1   15.715 ? 11  GLY   B CA   1 
ATOM   2493 C  C    . GLY   B 1 11  ? -10.088 9.252   -5.549  1   15.97  ? 11  GLY   B C    1 
ATOM   2494 O  O    . GLY   B 1 11  ? -9.896  10.317  -4.955  1   16.948 ? 11  GLY   B O    1 
ATOM   2495 N  N    . LYS   B 1 12  ? -10.253 8.088   -4.909  1   15.887 ? 12  LYS   B N    1 
ATOM   2496 C  CA   . LYS   B 1 12  ? -10.3   8.033   -3.456  1   16.77  ? 12  LYS   B CA   1 
ATOM   2497 C  C    . LYS   B 1 12  ? -8.97   8.48    -2.845  1   16.251 ? 12  LYS   B C    1 
ATOM   2498 O  O    . LYS   B 1 12  ? -8.955  9.007   -1.736  1   17.975 ? 12  LYS   B O    1 
ATOM   2499 C  CB   . LYS   B 1 12  ? -10.664 6.63    -2.972  1   18.834 ? 12  LYS   B CB   1 
ATOM   2500 C  CG   . LYS   B 1 12  ? -12.11  6.228   -3.206  1   21.913 ? 12  LYS   B CG   1 
ATOM   2501 C  CD   . LYS   B 1 12  ? -12.451 4.883   -2.583  1   25.95  ? 12  LYS   B CD   1 
ATOM   2502 C  CE   . LYS   B 1 12  ? -13.919 4.698   -2.386  1   29.126 ? 12  LYS   B CE   1 
ATOM   2503 N  NZ   . LYS   B 1 12  ? -14.587 4.568   -3.677  1   31.844 ? 12  LYS   B NZ   1 
ATOM   2504 N  N    . VAL   B 1 13  ? -7.864  8.267   -3.567  1   14.702 ? 13  VAL   B N    1 
ATOM   2505 C  CA   . VAL   B 1 13  ? -6.547  8.653   -3.085  1   14.937 ? 13  VAL   B CA   1 
ATOM   2506 C  C    . VAL   B 1 13  ? -6.244  10.112  -3.439  1   14.704 ? 13  VAL   B C    1 
ATOM   2507 O  O    . VAL   B 1 13  ? -5.6    10.818  -2.66   1   14.681 ? 13  VAL   B O    1 
ATOM   2508 C  CB   . VAL   B 1 13  ? -5.475  7.695   -3.643  1   15.135 ? 13  VAL   B CB   1 
ATOM   2509 C  CG1  . VAL   B 1 13  ? -4.071  8.108   -3.215  1   15.56  ? 13  VAL   B CG1  1 
ATOM   2510 C  CG2  . VAL   B 1 13  ? -5.766  6.246   -3.262  1   15.797 ? 13  VAL   B CG2  1 
ATOM   2511 N  N    . GLU   B 1 14  ? -6.698  10.584  -4.61   1   14.723 ? 14  GLU   B N    1 
ATOM   2512 C  CA   . GLU   B 1 14  ? -6.461  11.964  -5.004  1   14.623 ? 14  GLU   B CA   1 
ATOM   2513 C  C    . GLU   B 1 14  ? -6.916  12.927  -3.903  1   15.261 ? 14  GLU   B C    1 
ATOM   2514 O  O    . GLU   B 1 14  ? -6.253  13.926  -3.638  1   16.804 ? 14  GLU   B O    1 
ATOM   2515 C  CB   . GLU   B 1 14  ? -7.173  12.307  -6.313  1   14.384 ? 14  GLU   B CB   1 
ATOM   2516 C  CG   . GLU   B 1 14  ? -6.559  11.627  -7.535  1   14.559 ? 14  GLU   B CG   1 
ATOM   2517 C  CD   . GLU   B 1 14  ? -7.462  11.697  -8.756  1   14.663 ? 14  GLU   B CD   1 
ATOM   2518 O  OE1  . GLU   B 1 14  ? -7.752  10.634  -9.336  1   14.809 ? 14  GLU   B OE1  1 
ATOM   2519 O  OE2  . GLU   B 1 14  ? -7.876  12.823  -9.117  1   16.424 ? 14  GLU   B OE2  1 
ATOM   2520 N  N    . GLY   B 1 15  ? -8.07   12.635  -3.292  1   15.965 ? 15  GLY   B N    1 
ATOM   2521 C  CA   . GLY   B 1 15  ? -8.652  13.494  -2.277  1   16.861 ? 15  GLY   B CA   1 
ATOM   2522 C  C    . GLY   B 1 15  ? -7.876  13.512  -0.961  1   16.851 ? 15  GLY   B C    1 
ATOM   2523 O  O    . GLY   B 1 15  ? -8.257  14.221  -0.028  1   18.92  ? 15  GLY   B O    1 
ATOM   2524 N  N    . CYS   B 1 16  ? -6.793  12.732  -0.887  1   15.133 ? 16  CYS   B N    1 
ATOM   2525 C  CA   . CYS   B 1 16  ? -5.972  12.656  0.309   1   15.709 ? 16  CYS   B CA   1 
ATOM   2526 C  C    . CYS   B 1 16  ? -4.598  13.293  0.106   1   14.869 ? 16  CYS   B C    1 
ATOM   2527 O  O    . CYS   B 1 16  ? -3.825  13.38   1.055   1   15.785 ? 16  CYS   B O    1 
ATOM   2528 C  CB   . CYS   B 1 16  ? -5.757  11.213  0.743   1   15.949 ? 16  CYS   B CB   1 
ATOM   2529 S  SG   . CYS   B 1 16  ? -7.289  10.318  1.07    1   18.122 ? 16  CYS   B SG   1 
ATOM   2530 N  N    . MET   B 1 17  ? -4.264  13.731  -1.114  1   14.801 ? 17  MET   B N    1 
ATOM   2531 C  CA   . MET   B 1 17  ? -2.916  14.228  -1.354  1   14.887 ? 17  MET   B CA   1 
ATOM   2532 C  C    . MET   B 1 17  ? -2.831  15.71   -1.005  1   15.016 ? 17  MET   B C    1 
ATOM   2533 O  O    . MET   B 1 17  ? -3.69   16.507  -1.387  1   17.156 ? 17  MET   B O    1 
ATOM   2534 C  CB   . MET   B 1 17  ? -2.479  13.978  -2.799  1   15.327 ? 17  MET   B CB   1 
ATOM   2535 C  CG   . MET   B 1 17  ? -2.529  12.51   -3.192  1   15.35  ? 17  MET   B CG   1 
ATOM   2536 S  SD   . MET   B 1 17  ? -1.617  11.409  -2.091  1   15.991 ? 17  MET   B SD   1 
ATOM   2537 C  CE   . MET   B 1 17  ? 0.032   12.125  -2.02   1   16.369 ? 17  MET   B CE   1 
ATOM   2538 N  N    . VAL   B 1 18  ? -1.778  16.05   -0.256  1   14.971 ? 18  VAL   B N    1 
ATOM   2539 C  CA   . VAL   B 1 18  ? -1.524  17.416  0.163   1   15.795 ? 18  VAL   B CA   1 
ATOM   2540 C  C    . VAL   B 1 18  ? -0.06   17.765  -0.085  1   16.291 ? 18  VAL   B C    1 
ATOM   2541 O  O    . VAL   B 1 18  ? 0.767   16.896  -0.351  1   15.654 ? 18  VAL   B O    1 
ATOM   2542 C  CB   . VAL   B 1 18  ? -1.895  17.648  1.642   1   15.771 ? 18  VAL   B CB   1 
ATOM   2543 C  CG1  . VAL   B 1 18  ? -3.375  17.399  1.905   1   16.796 ? 18  VAL   B CG1  1 
ATOM   2544 C  CG2  . VAL   B 1 18  ? -1.055  16.809  2.596   1   15.63  ? 18  VAL   B CG2  1 
ATOM   2545 N  N    . GLN   B 1 19  ? 0.235   19.063  0.007   1   18.583 ? 19  GLN   B N    1 
ATOM   2546 C  CA   . GLN   B 1 19  ? 1.588   19.575  -0.108  1   19.648 ? 19  GLN   B CA   1 
ATOM   2547 C  C    . GLN   B 1 19  ? 2.14    19.852  1.285   1   20.218 ? 19  GLN   B C    1 
ATOM   2548 O  O    . GLN   B 1 19  ? 1.455   20.473  2.096   1   20.942 ? 19  GLN   B O    1 
ATOM   2549 C  CB   . GLN   B 1 19  ? 1.55    20.885  -0.891  1   23.116 ? 19  GLN   B CB   1 
ATOM   2550 C  CG   . GLN   B 1 19  ? 2.934   21.443  -1.196  1   25.827 ? 19  GLN   B CG   1 
ATOM   2551 C  CD   . GLN   B 1 19  ? 2.886   22.717  -2.005  1   30.862 ? 19  GLN   B CD   1 
ATOM   2552 O  OE1  . GLN   B 1 19  ? 3.197   22.735  -3.202  1   35.145 ? 19  GLN   B OE1  1 
ATOM   2553 N  NE2  . GLN   B 1 19  ? 2.476   23.799  -1.362  1   33.196 ? 19  GLN   B NE2  1 
ATOM   2554 N  N    . VAL   B 1 20  ? 3.364   19.381  1.544   1   19.068 ? 20  VAL   B N    1 
ATOM   2555 C  CA   . VAL   B 1 20  ? 4.033   19.594  2.815   1   19.273 ? 20  VAL   B CA   1 
ATOM   2556 C  C    . VAL   B 1 20  ? 5.321   20.36   2.543   1   20.993 ? 20  VAL   B C    1 
ATOM   2557 O  O    . VAL   B 1 20  ? 6.126   19.937  1.723   1   20.68  ? 20  VAL   B O    1 
ATOM   2558 C  CB   . VAL   B 1 20  ? 4.333   18.268  3.537   1   19.197 ? 20  VAL   B CB   1 
ATOM   2559 C  CG1  . VAL   B 1 20  ? 5.093   18.49   4.847   1   19.946 ? 20  VAL   B CG1  1 
ATOM   2560 C  CG2  . VAL   B 1 20  ? 3.063   17.472  3.779   1   19.117 ? 20  VAL   B CG2  1 
ATOM   2561 N  N    . THR   B 1 21  ? 5.509   21.477  3.253   1   23.678 ? 21  THR   B N    1 
ATOM   2562 C  CA   . THR   B 1 21  ? 6.717   22.275  3.121   1   25.321 ? 21  THR   B CA   1 
ATOM   2563 C  C    . THR   B 1 21  ? 7.388   22.378  4.486   1   26.742 ? 21  THR   B C    1 
ATOM   2564 O  O    . THR   B 1 21  ? 6.743   22.705  5.478   1   27.93  ? 21  THR   B O    1 
ATOM   2565 C  CB   . THR   B 1 21  ? 6.402   23.662  2.562   1   27.35  ? 21  THR   B CB   1 
ATOM   2566 O  OG1  . THR   B 1 21  ? 5.778   23.459  1.299   1   29.508 ? 21  THR   B OG1  1 
ATOM   2567 C  CG2  . THR   B 1 21  ? 7.644   24.522  2.402   1   29.053 ? 21  THR   B CG2  1 
ATOM   2568 N  N    . CYS   B 1 22  ? 8.694   22.11   4.506   1   26.719 ? 22  CYS   B N    1 
ATOM   2569 C  CA   . CYS   B 1 22  ? 9.526   22.356  5.67    1   27.534 ? 22  CYS   B CA   1 
ATOM   2570 C  C    . CYS   B 1 22  ? 10.748  23.128  5.19    1   28.116 ? 22  CYS   B C    1 
ATOM   2571 O  O    . CYS   B 1 22  ? 11.528  22.6    4.402   1   29.082 ? 22  CYS   B O    1 
ATOM   2572 C  CB   . CYS   B 1 22  ? 9.898   21.043  6.348   1   28.442 ? 22  CYS   B CB   1 
ATOM   2573 S  SG   . CYS   B 1 22  ? 10.855  21.244  7.874   1   31.043 ? 22  CYS   B SG   1 
ATOM   2574 N  N    . GLY   B 1 23  ? 10.874  24.39   5.622   1   29.397 ? 23  GLY   B N    1 
ATOM   2575 C  CA   . GLY   B 1 23  ? 11.942  25.243  5.131   1   30.045 ? 23  GLY   B CA   1 
ATOM   2576 C  C    . GLY   B 1 23  ? 11.895  25.364  3.61    1   30.249 ? 23  GLY   B C    1 
ATOM   2577 O  O    . GLY   B 1 23  ? 10.863  25.738  3.053   1   33.014 ? 23  GLY   B O    1 
ATOM   2578 N  N    . THR   B 1 24  ? 12.997  24.992  2.943   1   29.621 ? 24  THR   B N    1 
ATOM   2579 C  CA   . THR   B 1 24  ? 13.113  25.131  1.501   1   29.677 ? 24  THR   B CA   1 
ATOM   2580 C  C    . THR   B 1 24  ? 12.582  23.903  0.755   1   27.316 ? 24  THR   B C    1 
ATOM   2581 O  O    . THR   B 1 24  ? 12.571  23.912  -0.472  1   27.815 ? 24  THR   B O    1 
ATOM   2582 C  CB   . THR   B 1 24  ? 14.573  25.408  1.135   1   30.605 ? 24  THR   B CB   1 
ATOM   2583 O  OG1  . THR   B 1 24  ? 15.348  24.313  1.615   1   32.125 ? 24  THR   B OG1  1 
ATOM   2584 C  CG2  . THR   B 1 24  ? 15.085  26.712  1.718   1   31.801 ? 24  THR   B CG2  1 
ATOM   2585 N  N    . THR   B 1 25  ? 12.126  22.864  1.469   1   25.269 ? 25  THR   B N    1 
ATOM   2586 C  CA   . THR   B 1 25  ? 11.695  21.63   0.826   1   24.211 ? 25  THR   B CA   1 
ATOM   2587 C  C    . THR   B 1 25  ? 10.175  21.567  0.746   1   23.52  ? 25  THR   B C    1 
ATOM   2588 O  O    . THR   B 1 25  ? 9.506   21.681  1.765   1   24.463 ? 25  THR   B O    1 
ATOM   2589 C  CB   . THR   B 1 25  ? 12.208  20.412  1.587   1   24.257 ? 25  THR   B CB   1 
ATOM   2590 O  OG1  . THR   B 1 25  ? 13.616  20.444  1.397   1   25.236 ? 25  THR   B OG1  1 
ATOM   2591 C  CG2  . THR   B 1 25  ? 11.652  19.116  1.021   1   24.184 ? 25  THR   B CG2  1 
ATOM   2592 N  N    . THR   B 1 26  ? 9.659   21.277  -0.455  1   22.028 ? 26  THR   B N    1 
ATOM   2593 C  CA   . THR   B 1 26  ? 8.259   20.923  -0.644  1   21.573 ? 26  THR   B CA   1 
ATOM   2594 C  C    . THR   B 1 26  ? 8.181   19.511  -1.216  1   19.679 ? 26  THR   B C    1 
ATOM   2595 O  O    . THR   B 1 26  ? 8.887   19.179  -2.168  1   20.531 ? 26  THR   B O    1 
ATOM   2596 C  CB   . THR   B 1 26  ? 7.572   21.928  -1.568  1   23.941 ? 26  THR   B CB   1 
ATOM   2597 O  OG1  . THR   B 1 26  ? 7.596   23.18   -0.891  1   27.259 ? 26  THR   B OG1  1 
ATOM   2598 C  CG2  . THR   B 1 26  ? 6.133   21.556  -1.866  1   24.993 ? 26  THR   B CG2  1 
ATOM   2599 N  N    . LEU   B 1 27  ? 7.332   18.68   -0.603  1   18.258 ? 27  LEU   B N    1 
ATOM   2600 C  CA   . LEU   B 1 27  ? 7.026   17.367  -1.145  1   17.496 ? 27  LEU   B CA   1 
ATOM   2601 C  C    . LEU   B 1 27  ? 5.571   17.024  -0.816  1   16.242 ? 27  LEU   B C    1 
ATOM   2602 O  O    . LEU   B 1 27  ? 4.793   17.913  -0.464  1   18.013 ? 27  LEU   B O    1 
ATOM   2603 C  CB   . LEU   B 1 27  ? 8.041   16.312  -0.697  1   17.095 ? 27  LEU   B CB   1 
ATOM   2604 C  CG   . LEU   B 1 27  ? 8.413   16.261  0.785   1   17.365 ? 27  LEU   B CG   1 
ATOM   2605 C  CD1  . LEU   B 1 27  ? 7.241   15.896  1.674   1   16.955 ? 27  LEU   B CD1  1 
ATOM   2606 C  CD2  . LEU   B 1 27  ? 9.569   15.287  0.985   1   17.481 ? 27  LEU   B CD2  1 
ATOM   2607 N  N    . ASN   B 1 28  ? 5.178   15.762  -1.02   1   15.015 ? 28  ASN   B N    1 
ATOM   2608 C  CA   . ASN   B 1 28  ? 3.784   15.361  -0.913  1   14.347 ? 28  ASN   B CA   1 
ATOM   2609 C  C    . ASN   B 1 28  ? 3.535   14.667  0.417   1   14.399 ? 28  ASN   B C    1 
ATOM   2610 O  O    . ASN   B 1 28  ? 4.407   13.988  0.96    1   14.718 ? 28  ASN   B O    1 
ATOM   2611 C  CB   . ASN   B 1 28  ? 3.39    14.428  -2.053  1   13.618 ? 28  ASN   B CB   1 
ATOM   2612 C  CG   . ASN   B 1 28  ? 3.789   14.997  -3.393  1   13.99  ? 28  ASN   B CG   1 
ATOM   2613 O  OD1  . ASN   B 1 28  ? 3.103   15.88   -3.921  1   14.87  ? 28  ASN   B OD1  1 
ATOM   2614 N  ND2  . ASN   B 1 28  ? 4.879   14.499  -3.961  1   14.908 ? 28  ASN   B ND2  1 
ATOM   2615 N  N    . GLY   B 1 29  ? 2.302   14.818  0.903   1   14.159 ? 29  GLY   B N    1 
ATOM   2616 C  CA   . GLY   B 1 29  ? 1.827   14.099  2.069   1   14.044 ? 29  GLY   B CA   1 
ATOM   2617 C  C    . GLY   B 1 29  ? 0.469   13.457  1.818   1   13.432 ? 29  GLY   B C    1 
ATOM   2618 O  O    . GLY   B 1 29  ? -0.252  13.829  0.896   1   13.415 ? 29  GLY   B O    1 
ATOM   2619 N  N    . LEU   B 1 30  ? 0.141   12.5    2.688   1   12.866 ? 30  LEU   B N    1 
ATOM   2620 C  CA   . LEU   B 1 30  ? -1.107  11.757  2.65    1   12.57  ? 30  LEU   B CA   1 
ATOM   2621 C  C    . LEU   B 1 30  ? -1.922  12.152  3.88    1   13.2   ? 30  LEU   B C    1 
ATOM   2622 O  O    . LEU   B 1 30  ? -1.488  11.913  5       1   13.808 ? 30  LEU   B O    1 
ATOM   2623 C  CB   . LEU   B 1 30  ? -0.788  10.263  2.613   1   12.8   ? 30  LEU   B CB   1 
ATOM   2624 C  CG   . LEU   B 1 30  ? -1.991  9.322   2.515   1   13.216 ? 30  LEU   B CG   1 
ATOM   2625 C  CD1  . LEU   B 1 30  ? -2.668  9.431   1.165   1   13.868 ? 30  LEU   B CD1  1 
ATOM   2626 C  CD2  . LEU   B 1 30  ? -1.629  7.884   2.78    1   13.265 ? 30  LEU   B CD2  1 
ATOM   2627 N  N    . TRP   B 1 31  ? -3.107  12.724  3.64    1   13.407 ? 31  TRP   B N    1 
ATOM   2628 C  CA   . TRP   B 1 31  ? -3.975  13.273  4.673   1   13.534 ? 31  TRP   B CA   1 
ATOM   2629 C  C    . TRP   B 1 31  ? -5.138  12.318  4.905   1   13.403 ? 31  TRP   B C    1 
ATOM   2630 O  O    . TRP   B 1 31  ? -6.013  12.185  4.044   1   13.529 ? 31  TRP   B O    1 
ATOM   2631 C  CB   . TRP   B 1 31  ? -4.467  14.653  4.219   1   14.822 ? 31  TRP   B CB   1 
ATOM   2632 C  CG   . TRP   B 1 31  ? -5.358  15.389  5.185   1   16.365 ? 31  TRP   B CG   1 
ATOM   2633 C  CD1  . TRP   B 1 31  ? -5.42   15.275  6.542   1   17.035 ? 31  TRP   B CD1  1 
ATOM   2634 C  CD2  . TRP   B 1 31  ? -6.311  16.407  4.821   1   18.074 ? 31  TRP   B CD2  1 
ATOM   2635 N  NE1  . TRP   B 1 31  ? -6.349  16.143  7.05    1   18.399 ? 31  TRP   B NE1  1 
ATOM   2636 C  CE2  . TRP   B 1 31  ? -6.91   16.854  6.02    1   18.469 ? 31  TRP   B CE2  1 
ATOM   2637 C  CE3  . TRP   B 1 31  ? -6.716  16.971  3.605   1   18.888 ? 31  TRP   B CE3  1 
ATOM   2638 C  CZ2  . TRP   B 1 31  ? -7.893  17.843  6.031   1   19.694 ? 31  TRP   B CZ2  1 
ATOM   2639 C  CZ3  . TRP   B 1 31  ? -7.688  17.944  3.62    1   20.309 ? 31  TRP   B CZ3  1 
ATOM   2640 C  CH2  . TRP   B 1 31  ? -8.26   18.374  4.815   1   20.12  ? 31  TRP   B CH2  1 
ATOM   2641 N  N    . LEU   B 1 32  ? -5.132  11.651  6.064   1   14.05  ? 32  LEU   B N    1 
ATOM   2642 C  CA   . LEU   B 1 32  ? -6.162  10.698  6.436   1   14.457 ? 32  LEU   B CA   1 
ATOM   2643 C  C    . LEU   B 1 32  ? -6.606  11.044  7.849   1   15.655 ? 32  LEU   B C    1 
ATOM   2644 O  O    . LEU   B 1 32  ? -5.77   11.18   8.738   1   15.396 ? 32  LEU   B O    1 
ATOM   2645 C  CB   . LEU   B 1 32  ? -5.631  9.269   6.398   1   14.575 ? 32  LEU   B CB   1 
ATOM   2646 C  CG   . LEU   B 1 32  ? -5.154  8.774   5.03    1   15.08  ? 32  LEU   B CG   1 
ATOM   2647 C  CD1  . LEU   B 1 32  ? -4.37   7.5     5.222   1   15.183 ? 32  LEU   B CD1  1 
ATOM   2648 C  CD2  . LEU   B 1 32  ? -6.291  8.564   4.057   1   16.088 ? 32  LEU   B CD2  1 
ATOM   2649 N  N    . ASP   B 1 33  ? -7.921  11.143  8.079   1   17.623 ? 33  ASP   B N    1 
ATOM   2650 C  CA   . ASP   B 1 33  ? -8.392  11.623  9.369   1   19.059 ? 33  ASP   B CA   1 
ATOM   2651 C  C    . ASP   B 1 33  ? -7.668  12.952  9.63    1   18.65  ? 33  ASP   B C    1 
ATOM   2652 O  O    . ASP   B 1 33  ? -7.553  13.789  8.725   1   20.015 ? 33  ASP   B O    1 
ATOM   2653 C  CB   . ASP   B 1 33  ? -8.255  10.515  10.412  1   21.634 ? 33  ASP   B CB   1 
ATOM   2654 C  CG   . ASP   B 1 33  ? -9.026  9.238   10.094  1   24.441 ? 33  ASP   B CG   1 
ATOM   2655 O  OD1  . ASP   B 1 33  ? -10.226 9.367   9.847   1   28.94  ? 33  ASP   B OD1  1 
ATOM   2656 O  OD2  . ASP   B 1 33  ? -8.428  8.127   10.079  1   30.093 ? 33  ASP   B OD2  1 
ATOM   2657 N  N    . ASP   B 1 34  ? -7.139  13.145  10.846  1   18.616 ? 34  ASP   B N    1 
ATOM   2658 C  CA   . ASP   B 1 34  ? -6.476  14.398  11.188  1   17.695 ? 34  ASP   B CA   1 
ATOM   2659 C  C    . ASP   B 1 34  ? -4.952  14.26   11.214  1   16.399 ? 34  ASP   B C    1 
ATOM   2660 O  O    . ASP   B 1 34  ? -4.285  14.987  11.953  1   16.582 ? 34  ASP   B O    1 
ATOM   2661 C  CB   . ASP   B 1 34  ? -6.983  14.945  12.511  1   19.097 ? 34  ASP   B CB   1 
ATOM   2662 C  CG   . ASP   B 1 34  ? -6.769  14.051  13.719  1   20.74  ? 34  ASP   B CG   1 
ATOM   2663 O  OD1  . ASP   B 1 34  ? -6.374  12.878  13.53   1   21.825 ? 34  ASP   B OD1  1 
ATOM   2664 O  OD2  . ASP   B 1 34  ? -6.977  14.552  14.847  1   24.653 ? 34  ASP   B OD2  1 
ATOM   2665 N  N    . VAL   B 1 35  ? -4.396  13.363  10.389  1   15.225 ? 35  VAL   B N    1 
ATOM   2666 C  CA   . VAL   B 1 35  ? -2.954  13.18   10.303  1   15.027 ? 35  VAL   B CA   1 
ATOM   2667 C  C    . VAL   B 1 35  ? -2.506  13.267  8.844   1   14.337 ? 35  VAL   B C    1 
ATOM   2668 O  O    . VAL   B 1 35  ? -3.157  12.732  7.948   1   14.979 ? 35  VAL   B O    1 
ATOM   2669 C  CB   . VAL   B 1 35  ? -2.494  11.862  10.95   1   16.066 ? 35  VAL   B CB   1 
ATOM   2670 C  CG1  . VAL   B 1 35  ? -0.987  11.654  10.837  1   15.945 ? 35  VAL   B CG1  1 
ATOM   2671 C  CG2  . VAL   B 1 35  ? -2.898  11.8    12.418  1   17.116 ? 35  VAL   B CG2  1 
ATOM   2672 N  N    . VAL   B 1 36  ? -1.365  13.938  8.635   1   14.265 ? 36  VAL   B N    1 
ATOM   2673 C  CA   . VAL   B 1 36  ? -0.665  13.94   7.358   1   14.259 ? 36  VAL   B CA   1 
ATOM   2674 C  C    . VAL   B 1 36  ? 0.632   13.156  7.502   1   13.655 ? 36  VAL   B C    1 
ATOM   2675 O  O    . VAL   B 1 36  ? 1.439   13.431  8.385   1   14.323 ? 36  VAL   B O    1 
ATOM   2676 C  CB   . VAL   B 1 36  ? -0.394  15.375  6.872   1   15.093 ? 36  VAL   B CB   1 
ATOM   2677 C  CG1  . VAL   B 1 36  ? 0.472   15.401  5.614   1   15.599 ? 36  VAL   B CG1  1 
ATOM   2678 C  CG2  . VAL   B 1 36  ? -1.697  16.14   6.667   1   15.837 ? 36  VAL   B CG2  1 
ATOM   2679 N  N    . TYR   B 1 37  ? 0.806   12.177  6.617   1   12.95  ? 37  TYR   B N    1 
ATOM   2680 C  CA   . TYR   B 1 37  ? 1.971   11.308  6.611   1   12.492 ? 37  TYR   B CA   1 
ATOM   2681 C  C    . TYR   B 1 37  ? 2.891   11.716  5.467   1   12.755 ? 37  TYR   B C    1 
ATOM   2682 O  O    . TYR   B 1 37  ? 2.423   11.917  4.349   1   13.545 ? 37  TYR   B O    1 
ATOM   2683 C  CB   . TYR   B 1 37  ? 1.536   9.854   6.392   1   12.678 ? 37  TYR   B CB   1 
ATOM   2684 C  CG   . TYR   B 1 37  ? 0.537   9.338   7.42    1   13.62  ? 37  TYR   B CG   1 
ATOM   2685 C  CD1  . TYR   B 1 37  ? -0.819  9.607   7.289   1   14.235 ? 37  TYR   B CD1  1 
ATOM   2686 C  CD2  . TYR   B 1 37  ? 0.945   8.619   8.531   1   14.762 ? 37  TYR   B CD2  1 
ATOM   2687 C  CE1  . TYR   B 1 37  ? -1.738  9.167   8.225   1   14.771 ? 37  TYR   B CE1  1 
ATOM   2688 C  CE2  . TYR   B 1 37  ? 0.036   8.168   9.474   1   14.742 ? 37  TYR   B CE2  1 
ATOM   2689 C  CZ   . TYR   B 1 37  ? -1.309  8.461   9.331   1   15.362 ? 37  TYR   B CZ   1 
ATOM   2690 O  OH   . TYR   B 1 37  ? -2.194  8.039   10.28   1   17.257 ? 37  TYR   B OH   1 
ATOM   2691 N  N    . CYS   B 1 38  ? 4.199   11.807  5.738   1   12.881 ? 38  CYS   B N    1 
ATOM   2692 C  CA   . CYS   B 1 38  ? 5.146   12.102  4.674   1   13.042 ? 38  CYS   B CA   1 
ATOM   2693 C  C    . CYS   B 1 38  ? 6.514   11.534  5.037   1   12.905 ? 38  CYS   B C    1 
ATOM   2694 O  O    . CYS   B 1 38  ? 6.738   11.093  6.162   1   13.77  ? 38  CYS   B O    1 
ATOM   2695 C  CB   . CYS   B 1 38  ? 5.207   13.6    4.388   1   13.801 ? 38  CYS   B CB   1 
ATOM   2696 S  SG   . CYS   B 1 38  ? 6.063   14.579  5.65    1   16.915 ? 38  CYS   B SG   1 
ATOM   2697 N  N    . PRO   B 1 39  ? 7.488   11.504  4.1     1   13.208 ? 39  PRO   B N    1 
ATOM   2698 C  CA   . PRO   B 1 39  ? 8.823   11.017  4.445   1   12.999 ? 39  PRO   B CA   1 
ATOM   2699 C  C    . PRO   B 1 39  ? 9.49    11.895  5.495   1   13.708 ? 39  PRO   B C    1 
ATOM   2700 O  O    . PRO   B 1 39  ? 9.442   13.117  5.399   1   14.124 ? 39  PRO   B O    1 
ATOM   2701 C  CB   . PRO   B 1 39  ? 9.563   11.098  3.104   1   13.581 ? 39  PRO   B CB   1 
ATOM   2702 C  CG   . PRO   B 1 39  ? 8.459   10.956  2.084   1   13.245 ? 39  PRO   B CG   1 
ATOM   2703 C  CD   . PRO   B 1 39  ? 7.355   11.824  2.667   1   13.5   ? 39  PRO   B CD   1 
ATOM   2704 N  N    . ARG   B 1 40  ? 10.155  11.277  6.472   1   13.511 ? 40  ARG   B N    1 
ATOM   2705 C  CA   . ARG   B 1 40  ? 10.816  12.065  7.501   1   14.299 ? 40  ARG   B CA   1 
ATOM   2706 C  C    . ARG   B 1 40  ? 11.97   12.887  6.921   1   14.739 ? 40  ARG   B C    1 
ATOM   2707 O  O    . ARG   B 1 40  ? 12.345  13.889  7.528   1   15.891 ? 40  ARG   B O    1 
ATOM   2708 C  CB   . ARG   B 1 40  ? 11.268  11.246  8.712   1   14.338 ? 40  ARG   B CB   1 
ATOM   2709 C  CG   . ARG   B 1 40  ? 12.364  10.236  8.435   1   14.215 ? 40  ARG   B CG   1 
ATOM   2710 C  CD   . ARG   B 1 40  ? 12.809  9.558   9.716   1   14.275 ? 40  ARG   B CD   1 
ATOM   2711 N  NE   . ARG   B 1 40  ? 13.783  8.515   9.391   1   14.627 ? 40  ARG   B NE   1 
ATOM   2712 C  CZ   . ARG   B 1 40  ? 14.515  7.846   10.276  1   15.596 ? 40  ARG   B CZ   1 
ATOM   2713 N  NH1  . ARG   B 1 40  ? 14.27   7.951   11.564  1   15.75  ? 40  ARG   B NH1  1 
ATOM   2714 N  NH2  . ARG   B 1 40  ? 15.495  7.053   9.86    1   15.815 ? 40  ARG   B NH2  1 
ATOM   2715 N  N    . HIS   B 1 41  ? 12.519  12.497  5.758   1   14.979 ? 41  HIS   B N    1 
ATOM   2716 C  CA   . HIS   B 1 41  ? 13.61   13.249  5.163   1   16.129 ? 41  HIS   B CA   1 
ATOM   2717 C  C    . HIS   B 1 41  ? 13.214  14.676  4.785   1   16.802 ? 41  HIS   B C    1 
ATOM   2718 O  O    . HIS   B 1 41  ? 14.091  15.483  4.476   1   17.482 ? 41  HIS   B O    1 
ATOM   2719 C  CB   . HIS   B 1 41  ? 14.295  12.453  4.047   1   16.02  ? 41  HIS   B CB   1 
ATOM   2720 C  CG   . HIS   B 1 41  ? 13.571  12.315  2.746   1   15.921 ? 41  HIS   B CG   1 
ATOM   2721 N  ND1  . HIS   B 1 41  ? 13.207  13.373  1.939   1   16.6   ? 41  HIS   B ND1  1 
ATOM   2722 C  CD2  . HIS   B 1 41  ? 13.23   11.205  2.075   1   16.503 ? 41  HIS   B CD2  1 
ATOM   2723 C  CE1  . HIS   B 1 41  ? 12.648  12.903  0.831   1   16.586 ? 41  HIS   B CE1  1 
ATOM   2724 N  NE2  . HIS   B 1 41  ? 12.666  11.588  0.886   1   16.552 ? 41  HIS   B NE2  1 
ATOM   2725 N  N    . VAL   B 1 42  ? 11.916  15.004  4.833   1   16.919 ? 42  VAL   B N    1 
ATOM   2726 C  CA   . VAL   B 1 42  ? 11.48   16.367  4.583   1   17.743 ? 42  VAL   B CA   1 
ATOM   2727 C  C    . VAL   B 1 42  ? 12.215  17.359  5.491   1   19.431 ? 42  VAL   B C    1 
ATOM   2728 O  O    . VAL   B 1 42  ? 12.366  18.517  5.099   1   21.482 ? 42  VAL   B O    1 
ATOM   2729 C  CB   . VAL   B 1 42  ? 9.951   16.495  4.733   1   17.556 ? 42  VAL   B CB   1 
ATOM   2730 C  CG1  . VAL   B 1 42  ? 9.493   16.392  6.186   1   17.434 ? 42  VAL   B CG1  1 
ATOM   2731 C  CG2  . VAL   B 1 42  ? 9.433   17.779  4.097   1   18.02  ? 42  VAL   B CG2  1 
ATOM   2732 N  N    . ILE   B 1 43  ? 12.667  16.925  6.684   1   19.896 ? 43  ILE   B N    1 
ATOM   2733 C  CA   . ILE   B 1 43  ? 13.276  17.845  7.64    1   21.274 ? 43  ILE   B CA   1 
ATOM   2734 C  C    . ILE   B 1 43  ? 14.758  18.094  7.357   1   22.712 ? 43  ILE   B C    1 
ATOM   2735 O  O    . ILE   B 1 43  ? 15.351  18.916  8.047   1   24.786 ? 43  ILE   B O    1 
ATOM   2736 C  CB   . ILE   B 1 43  ? 13.074  17.388  9.098   1   22.557 ? 43  ILE   B CB   1 
ATOM   2737 C  CG1  . ILE   B 1 43  ? 13.871  16.125  9.467   1   23.455 ? 43  ILE   B CG1  1 
ATOM   2738 C  CG2  . ILE   B 1 43  ? 11.585  17.246  9.403   1   23.211 ? 43  ILE   B CG2  1 
ATOM   2739 C  CD1  . ILE   B 1 43  ? 13.736  15.714  10.924  1   24.181 ? 43  ILE   B CD1  1 
ATOM   2740 N  N    . CYS   B 1 44  ? 15.342  17.432  6.35    1   22.036 ? 44  CYS   B N    1 
ATOM   2741 C  CA   . CYS   B 1 44  ? 16.781  17.49   6.14    1   22.488 ? 44  CYS   B CA   1 
ATOM   2742 C  C    . CYS   B 1 44  ? 17.185  18.559  5.128   1   23.759 ? 44  CYS   B C    1 
ATOM   2743 O  O    . CYS   B 1 44  ? 16.611  18.624  4.046   1   25.651 ? 44  CYS   B O    1 
ATOM   2744 C  CB   . CYS   B 1 44  ? 17.286  16.166  5.592   1   22.633 ? 44  CYS   B CB   1 
ATOM   2745 S  SG   . CYS   B 1 44  ? 17.156  14.818  6.79    1   24.259 ? 44  CYS   B SG   1 
ATOM   2746 N  N    . THR   B 1 45  ? 18.222  19.343  5.464   1   25.193 ? 45  THR   B N    1 
ATOM   2747 C  CA   . THR   B 1 45  ? 18.959  20.1    4.464   1   26.171 ? 45  THR   B CA   1 
ATOM   2748 C  C    . THR   B 1 45  ? 19.766  19.106  3.634   1   25.878 ? 45  THR   B C    1 
ATOM   2749 O  O    . THR   B 1 45  ? 19.912  17.95   4.029   1   24.867 ? 45  THR   B O    1 
ATOM   2750 C  CB   . THR   B 1 45  ? 19.878  21.149  5.091   1   27.467 ? 45  THR   B CB   1 
ATOM   2751 O  OG1  . THR   B 1 45  ? 20.918  20.425  5.736   1   28.029 ? 45  THR   B OG1  1 
ATOM   2752 C  CG2  . THR   B 1 45  ? 19.168  22.068  6.069   1   28.425 ? 45  THR   B CG2  1 
ATOM   2753 N  N    . SER   B 1 46  ? 20.308  19.568  2.502   1   26.872 ? 46  SER   B N    1 
ATOM   2754 C  CA   . SER   B 1 46  ? 21.168  18.726  1.686   1   27.571 ? 46  SER   B CA   1 
ATOM   2755 C  C    . SER   B 1 46  ? 22.347  18.214  2.514   1   26.932 ? 46  SER   B C    1 
ATOM   2756 O  O    . SER   B 1 46  ? 22.759  17.067  2.36    1   26.623 ? 46  SER   B O    1 
ATOM   2757 C  CB   . SER   B 1 46  ? 21.632  19.449  0.444   1   29.711 ? 46  SER   B CB   1 
ATOM   2758 O  OG   . SER   B 1 46  ? 20.538  19.676  -0.433  1   34.589 ? 46  SER   B OG   1 
ATOM   2759 N  N    . GLU   B 1 47  ? 22.882  19.051  3.414   1   27.752 ? 47  GLU   B N    1 
ATOM   2760 C  CA   . GLU   B 1 47  ? 24.014  18.643  4.229   1   28.068 ? 47  GLU   B CA   1 
ATOM   2761 C  C    . GLU   B 1 47  ? 23.574  17.603  5.26    1   26.148 ? 47  GLU   B C    1 
ATOM   2762 O  O    . GLU   B 1 47  ? 24.286  16.623  5.489   1   27.681 ? 47  GLU   B O    1 
ATOM   2763 C  CB   . GLU   B 1 47  ? 24.688  19.843  4.892   1   31.176 ? 47  GLU   B CB   1 
ATOM   2764 C  CG   . GLU   B 1 47  ? 26.037  19.493  5.512   1   34.322 ? 47  GLU   B CG   1 
ATOM   2765 C  CD   . GLU   B 1 47  ? 27.181  19.21   4.549   1   37.458 ? 47  GLU   B CD   1 
ATOM   2766 O  OE1  . GLU   B 1 47  ? 27.033  19.348  3.312   1   39.437 ? 47  GLU   B OE1  1 
ATOM   2767 O  OE2  . GLU   B 1 47  ? 28.262  18.85   5.068   1   43.19  ? 47  GLU   B OE2  1 
ATOM   2768 N  N    . ASP   B 1 48  ? 22.394  17.803  5.869   1   25.022 ? 48  ASP   B N    1 
ATOM   2769 C  CA   . ASP   B 1 48  ? 21.885  16.85   6.848   1   24.972 ? 48  ASP   B CA   1 
ATOM   2770 C  C    . ASP   B 1 48  ? 21.679  15.469  6.227   1   22.881 ? 48  ASP   B C    1 
ATOM   2771 O  O    . ASP   B 1 48  ? 21.871  14.451  6.884   1   23.671 ? 48  ASP   B O    1 
ATOM   2772 C  CB   . ASP   B 1 48  ? 20.533  17.243  7.41    1   26.268 ? 48  ASP   B CB   1 
ATOM   2773 C  CG   . ASP   B 1 48  ? 20.47   18.539  8.201   1   28.595 ? 48  ASP   B CG   1 
ATOM   2774 O  OD1  . ASP   B 1 48  ? 21.446  18.837  8.925   1   31.085 ? 48  ASP   B OD1  1 
ATOM   2775 O  OD2  . ASP   B 1 48  ? 19.408  19.199  8.126   1   29.598 ? 48  ASP   B OD2  1 
ATOM   2776 N  N    . MET   B 1 49  ? 21.24   15.469  4.964   1   21.743 ? 49  MET   B N    1 
ATOM   2777 C  CA   . MET   B 1 49  ? 20.841  14.265  4.259   1   20.212 ? 49  MET   B CA   1 
ATOM   2778 C  C    . MET   B 1 49  ? 21.989  13.259  4.13    1   21.186 ? 49  MET   B C    1 
ATOM   2779 O  O    . MET   B 1 49  ? 21.729  12.064  4.003   1   20.771 ? 49  MET   B O    1 
ATOM   2780 C  CB   . MET   B 1 49  ? 20.333  14.652  2.865   1   19.924 ? 49  MET   B CB   1 
ATOM   2781 C  CG   . MET   B 1 49  ? 19.447  13.631  2.167   1   19.466 ? 49  MET   B CG   1 
ATOM   2782 S  SD   . MET   B 1 49  ? 17.839  13.389  2.944   1   19.543 ? 49  MET   B SD   1 
ATOM   2783 C  CE   . MET   B 1 49  ? 18.171  11.939  3.948   1   18.941 ? 49  MET   B CE   1 
ATOM   2784 N  N    . LEU   B 1 50  ? 23.241  13.75   4.151   1   22.101 ? 50  LEU   B N    1 
ATOM   2785 C  CA   . LEU   B 1 50  ? 24.427  12.911  4.052   1   23.732 ? 50  LEU   B CA   1 
ATOM   2786 C  C    . LEU   B 1 50  ? 24.607  12.038  5.292   1   23.66  ? 50  LEU   B C    1 
ATOM   2787 O  O    . LEU   B 1 50  ? 25.186  10.962  5.19    1   25.524 ? 50  LEU   B O    1 
ATOM   2788 C  CB   . LEU   B 1 50  ? 25.661  13.788  3.839   1   24.934 ? 50  LEU   B CB   1 
ATOM   2789 C  CG   . LEU   B 1 50  ? 25.661  14.668  2.587   1   26.257 ? 50  LEU   B CG   1 
ATOM   2790 C  CD1  . LEU   B 1 50  ? 26.837  15.634  2.608   1   27.481 ? 50  LEU   B CD1  1 
ATOM   2791 C  CD2  . LEU   B 1 50  ? 25.693  13.824  1.326   1   26.846 ? 50  LEU   B CD2  1 
ATOM   2792 N  N    . ASN   B 1 51  ? 24.09   12.475  6.447   1   24.987 ? 51  ASN   B N    1 
ATOM   2793 C  CA   . ASN   B 1 51  ? 24.233  11.711  7.679   1   26.353 ? 51  ASN   B CA   1 
ATOM   2794 C  C    . ASN   B 1 51  ? 23.281  12.259  8.739   1   25.605 ? 51  ASN   B C    1 
ATOM   2795 O  O    . ASN   B 1 51  ? 23.696  12.91   9.697   1   27.561 ? 51  ASN   B O    1 
ATOM   2796 C  CB   . ASN   B 1 51  ? 25.67   11.725  8.185   1   28.466 ? 51  ASN   B CB   1 
ATOM   2797 C  CG   . ASN   B 1 51  ? 25.873  10.773  9.338   1   31.541 ? 51  ASN   B CG   1 
ATOM   2798 O  OD1  . ASN   B 1 51  ? 25.065  9.862   9.551   1   33.454 ? 51  ASN   B OD1  1 
ATOM   2799 N  ND2  . ASN   B 1 51  ? 26.961  10.949  10.069  1   33.242 ? 51  ASN   B ND2  1 
ATOM   2800 N  N    . PRO   B 1 52  ? 21.961  12.028  8.589   1   24.459 ? 52  PRO   B N    1 
ATOM   2801 C  CA   . PRO   B 1 52  ? 20.98   12.667  9.461   1   24.103 ? 52  PRO   B CA   1 
ATOM   2802 C  C    . PRO   B 1 52  ? 20.84   11.996  10.821  1   25.682 ? 52  PRO   B C    1 
ATOM   2803 O  O    . PRO   B 1 52  ? 20.797  10.779  10.925  1   28.283 ? 52  PRO   B O    1 
ATOM   2804 C  CB   . PRO   B 1 52  ? 19.705  12.557  8.627   1   23.797 ? 52  PRO   B CB   1 
ATOM   2805 C  CG   . PRO   B 1 52  ? 19.894  11.261  7.879   1   24.126 ? 52  PRO   B CG   1 
ATOM   2806 C  CD   . PRO   B 1 52  ? 21.354  11.251  7.498   1   24.76  ? 52  PRO   B CD   1 
ATOM   2807 N  N    . ASN   B 1 53  ? 20.734  12.825  11.852  1   28.304 ? 53  ASN   B N    1 
ATOM   2808 C  CA   . ASN   B 1 53  ? 20.287  12.369  13.156  1   29.421 ? 53  ASN   B CA   1 
ATOM   2809 C  C    . ASN   B 1 53  ? 18.85   12.848  13.31   1   29.646 ? 53  ASN   B C    1 
ATOM   2810 O  O    . ASN   B 1 53  ? 18.62   13.967  13.748  1   30.759 ? 53  ASN   B O    1 
ATOM   2811 C  CB   . ASN   B 1 53  ? 21.202  12.863  14.271  1   32.06  ? 53  ASN   B CB   1 
ATOM   2812 C  CG   . ASN   B 1 53  ? 20.818  12.313  15.625  1   34.471 ? 53  ASN   B CG   1 
ATOM   2813 O  OD1  . ASN   B 1 53  ? 19.648  11.99   15.871  1   36.418 ? 53  ASN   B OD1  1 
ATOM   2814 N  ND2  . ASN   B 1 53  ? 21.773  12.258  16.538  1   36.514 ? 53  ASN   B ND2  1 
ATOM   2815 N  N    . TYR   B 1 54  ? 17.885  12.022  12.898  1   30.198 ? 54  TYR   B N    1 
ATOM   2816 C  CA   . TYR   B 1 54  ? 16.518  12.484  12.746  1   30.278 ? 54  TYR   B CA   1 
ATOM   2817 C  C    . TYR   B 1 54  ? 15.921  12.93   14.075  1   32.588 ? 54  TYR   B C    1 
ATOM   2818 O  O    . TYR   B 1 54  ? 15.218  13.934  14.102  1   32.739 ? 54  TYR   B O    1 
ATOM   2819 C  CB   . TYR   B 1 54  ? 15.638  11.405  12.119  1   27.383 ? 54  TYR   B CB   1 
ATOM   2820 C  CG   . TYR   B 1 54  ? 15.86   11.282  10.624  1   22.868 ? 54  TYR   B CG   1 
ATOM   2821 C  CD1  . TYR   B 1 54  ? 15.303  12.211  9.754   1   22.728 ? 54  TYR   B CD1  1 
ATOM   2822 C  CD2  . TYR   B 1 54  ? 16.612  10.247  10.093  1   21.426 ? 54  TYR   B CD2  1 
ATOM   2823 C  CE1  . TYR   B 1 54  ? 15.491  12.113  8.39    1   21.095 ? 54  TYR   B CE1  1 
ATOM   2824 C  CE2  . TYR   B 1 54  ? 16.805  10.138  8.726   1   20.611 ? 54  TYR   B CE2  1 
ATOM   2825 C  CZ   . TYR   B 1 54  ? 16.228  11.065  7.874   1   20.024 ? 54  TYR   B CZ   1 
ATOM   2826 O  OH   . TYR   B 1 54  ? 16.386  10.98   6.528   1   18.234 ? 54  TYR   B OH   1 
ATOM   2827 N  N    . GLU   B 1 55  ? 16.209  12.202  15.16   1   36.924 ? 55  GLU   B N    1 
ATOM   2828 C  CA   . GLU   B 1 55  ? 15.703  12.556  16.478  1   40.231 ? 55  GLU   B CA   1 
ATOM   2829 C  C    . GLU   B 1 55  ? 16.171  13.962  16.851  1   39.594 ? 55  GLU   B C    1 
ATOM   2830 O  O    . GLU   B 1 55  ? 15.391  14.786  17.329  1   43.019 ? 55  GLU   B O    1 
ATOM   2831 C  CB   . GLU   B 1 55  ? 16.166  11.541  17.524  1   43.31  ? 55  GLU   B CB   1 
ATOM   2832 N  N    . ASP   B 1 56  ? 17.457  14.226  16.605  1   40.308 ? 56  ASP   B N    1 
ATOM   2833 C  CA   . ASP   B 1 56  ? 18.066  15.494  16.953  1   41.942 ? 56  ASP   B CA   1 
ATOM   2834 C  C    . ASP   B 1 56  ? 17.574  16.605  16.027  1   40.195 ? 56  ASP   B C    1 
ATOM   2835 O  O    . ASP   B 1 56  ? 17.355  17.726  16.462  1   44.411 ? 56  ASP   B O    1 
ATOM   2836 C  CB   . ASP   B 1 56  ? 19.578  15.39   16.932  1   43.245 ? 56  ASP   B CB   1 
ATOM   2837 C  CG   . ASP   B 1 56  ? 20.284  16.571  17.568  1   45.399 ? 56  ASP   B CG   1 
ATOM   2838 O  OD1  . ASP   B 1 56  ? 20.23   16.68   18.811  1   45.892 ? 56  ASP   B OD1  1 
ATOM   2839 O  OD2  . ASP   B 1 56  ? 20.824  17.387  16.802  1   47.716 ? 56  ASP   B OD2  1 
ATOM   2840 N  N    . LEU   B 1 57  ? 17.396  16.3    14.74   1   40.512 ? 57  LEU   B N    1 
ATOM   2841 C  CA   . LEU   B 1 57  ? 16.92   17.294  13.79   1   41.232 ? 57  LEU   B CA   1 
ATOM   2842 C  C    . LEU   B 1 57  ? 15.468  17.65   14.091  1   44.085 ? 57  LEU   B C    1 
ATOM   2843 O  O    . LEU   B 1 57  ? 15.09   18.806  13.96   1   45.149 ? 57  LEU   B O    1 
ATOM   2844 C  CB   . LEU   B 1 57  ? 17.051  16.803  12.348  1   40.507 ? 57  LEU   B CB   1 
ATOM   2845 C  CG   . LEU   B 1 57  ? 18.475  16.672  11.8    1   41.757 ? 57  LEU   B CG   1 
ATOM   2846 C  CD1  . LEU   B 1 57  ? 18.426  15.965  10.455  1   41.636 ? 57  LEU   B CD1  1 
ATOM   2847 C  CD2  . LEU   B 1 57  ? 19.188  18.019  11.704  1   42.751 ? 57  LEU   B CD2  1 
ATOM   2848 N  N    . LEU   B 1 58  ? 14.656  16.66   14.488  1   44.533 ? 58  LEU   B N    1 
ATOM   2849 C  CA   . LEU   B 1 58  ? 13.234  16.885  14.696  1   46.95  ? 58  LEU   B CA   1 
ATOM   2850 C  C    . LEU   B 1 58  ? 12.98   17.662  15.988  1   48.868 ? 58  LEU   B C    1 
ATOM   2851 O  O    . LEU   B 1 58  ? 12.066  18.471  16.035  1   48.891 ? 58  LEU   B O    1 
ATOM   2852 C  CB   . LEU   B 1 58  ? 12.43   15.587  14.677  1   46.965 ? 58  LEU   B CB   1 
ATOM   2853 C  CG   . LEU   B 1 58  ? 10.909  15.781  14.698  1   47.07  ? 58  LEU   B CG   1 
ATOM   2854 C  CD1  . LEU   B 1 58  ? 10.449  16.55   13.461  1   47.531 ? 58  LEU   B CD1  1 
ATOM   2855 C  CD2  . LEU   B 1 58  ? 10.165  14.473  14.831  1   47.609 ? 58  LEU   B CD2  1 
ATOM   2856 N  N    . ILE   B 1 59  ? 13.787  17.44   17.03   1   52.716 ? 59  ILE   B N    1 
ATOM   2857 C  CA   . ILE   B 1 59  ? 13.625  18.131  18.302  1   55.329 ? 59  ILE   B CA   1 
ATOM   2858 C  C    . ILE   B 1 59  ? 13.746  19.646  18.107  1   56.524 ? 59  ILE   B C    1 
ATOM   2859 O  O    . ILE   B 1 59  ? 13.179  20.416  18.878  1   61.034 ? 59  ILE   B O    1 
ATOM   2860 C  CB   . ILE   B 1 59  ? 14.635  17.605  19.341  1   54.999 ? 59  ILE   B CB   1 
ATOM   2861 N  N    . ARG   B 1 60  ? 14.477  20.064  17.067  1   58.173 ? 60  ARG   B N    1 
ATOM   2862 C  CA   . ARG   B 1 60  ? 14.726  21.468  16.776  1   58.978 ? 60  ARG   B CA   1 
ATOM   2863 C  C    . ARG   B 1 60  ? 13.584  22.099  15.978  1   58.69  ? 60  ARG   B C    1 
ATOM   2864 O  O    . ARG   B 1 60  ? 13.597  23.304  15.74   1   58.235 ? 60  ARG   B O    1 
ATOM   2865 C  CB   . ARG   B 1 60  ? 16.032  21.618  15.984  1   61.703 ? 60  ARG   B CB   1 
ATOM   2866 N  N    . LYS   B 1 61  ? 12.604  21.286  15.563  1   56.678 ? 61  LYS   B N    1 
ATOM   2867 C  CA   . LYS   B 1 61  ? 11.468  21.749  14.782  1   55.353 ? 61  LYS   B CA   1 
ATOM   2868 C  C    . LYS   B 1 61  ? 10.244  21.893  15.68   1   53.37  ? 61  LYS   B C    1 
ATOM   2869 O  O    . LYS   B 1 61  ? 10.027  21.083  16.58   1   55.326 ? 61  LYS   B O    1 
ATOM   2870 C  CB   . LYS   B 1 61  ? 11.108  20.731  13.691  1   55.215 ? 61  LYS   B CB   1 
ATOM   2871 C  CG   . LYS   B 1 61  ? 12.168  20.5    12.632  1   56.077 ? 61  LYS   B CG   1 
ATOM   2872 C  CD   . LYS   B 1 61  ? 12.409  21.742  11.784  1   56.091 ? 61  LYS   B CD   1 
ATOM   2873 C  CE   . LYS   B 1 61  ? 13.291  21.516  10.605  1   56.881 ? 61  LYS   B CE   1 
ATOM   2874 N  NZ   . LYS   B 1 61  ? 14.692  21.396  11.012  1   58.39  ? 61  LYS   B NZ   1 
ATOM   2875 N  N    . SER   B 1 62  ? 9.434   22.917  15.406  1   50.189 ? 62  SER   B N    1 
ATOM   2876 C  CA   . SER   B 1 62  ? 8.129   23.044  16.03   1   47.915 ? 62  SER   B CA   1 
ATOM   2877 C  C    . SER   B 1 62  ? 7.046   22.854  14.97   1   42.841 ? 62  SER   B C    1 
ATOM   2878 O  O    . SER   B 1 62  ? 7.338   22.754  13.784  1   42.112 ? 62  SER   B O    1 
ATOM   2879 C  CB   . SER   B 1 62  ? 7.992   24.36   16.75   1   49.242 ? 62  SER   B CB   1 
ATOM   2880 N  N    . ASN   B 1 63  ? 5.789   22.806  15.419  1   39.058 ? 63  ASN   B N    1 
ATOM   2881 C  CA   . ASN   B 1 63  ? 4.647   22.627  14.538  1   35.431 ? 63  ASN   B CA   1 
ATOM   2882 C  C    . ASN   B 1 63  ? 4.648   23.652  13.408  1   36.825 ? 63  ASN   B C    1 
ATOM   2883 O  O    . ASN   B 1 63  ? 4.307   23.322  12.276  1   35.598 ? 63  ASN   B O    1 
ATOM   2884 C  CB   . ASN   B 1 63  ? 3.326   22.716  15.298  1   33.283 ? 63  ASN   B CB   1 
ATOM   2885 C  CG   . ASN   B 1 63  ? 3.149   21.577  16.273  1   33.06  ? 63  ASN   B CG   1 
ATOM   2886 O  OD1  . ASN   B 1 63  ? 3.577   20.456  15.99   1   32.028 ? 63  ASN   B OD1  1 
ATOM   2887 N  ND2  . ASN   B 1 63  ? 2.521   21.827  17.41   1   33.135 ? 63  ASN   B ND2  1 
ATOM   2888 N  N    . HIS   B 1 64  ? 5.032   24.887  13.748  1   40.61  ? 64  HIS   B N    1 
ATOM   2889 C  CA   . HIS   B 1 64  ? 4.981   26.045  12.873  1   43.308 ? 64  HIS   B CA   1 
ATOM   2890 C  C    . HIS   B 1 64  ? 5.967   25.949  11.704  1   42.59  ? 64  HIS   B C    1 
ATOM   2891 O  O    . HIS   B 1 64  ? 5.844   26.699  10.737  1   42.382 ? 64  HIS   B O    1 
ATOM   2892 C  CB   . HIS   B 1 64  ? 5.239   27.283  13.74   1   46.785 ? 64  HIS   B CB   1 
ATOM   2893 C  CG   . HIS   B 1 64  ? 6.452   27.165  14.61   1   52     ? 64  HIS   B CG   1 
ATOM   2894 N  ND1  . HIS   B 1 64  ? 7.712   26.864  14.138  1   55.024 ? 64  HIS   B ND1  1 
ATOM   2895 C  CD2  . HIS   B 1 64  ? 6.579   27.3    15.935  1   55.214 ? 64  HIS   B CD2  1 
ATOM   2896 C  CE1  . HIS   B 1 64  ? 8.565   26.838  15.151  1   56.143 ? 64  HIS   B CE1  1 
ATOM   2897 N  NE2  . HIS   B 1 64  ? 7.897   27.095  16.253  1   56.54  ? 64  HIS   B NE2  1 
ATOM   2898 N  N    . ASN   B 1 65  ? 6.941   25.03   11.8    1   38.765 ? 65  ASN   B N    1 
ATOM   2899 C  CA   . ASN   B 1 65  ? 7.925   24.828  10.747  1   36.628 ? 65  ASN   B CA   1 
ATOM   2900 C  C    . ASN   B 1 65  ? 7.343   24.033  9.578   1   34.091 ? 65  ASN   B C    1 
ATOM   2901 O  O    . ASN   B 1 65  ? 7.984   23.918  8.537   1   35.463 ? 65  ASN   B O    1 
ATOM   2902 C  CB   . ASN   B 1 65  ? 9.158   24.092  11.259  1   35.42  ? 65  ASN   B CB   1 
ATOM   2903 N  N    . PHE   B 1 66  ? 6.16    23.437  9.766   1   29.854 ? 66  PHE   B N    1 
ATOM   2904 C  CA   . PHE   B 1 66  ? 5.544   22.598  8.753   1   28.609 ? 66  PHE   B CA   1 
ATOM   2905 C  C    . PHE   B 1 66  ? 4.33    23.314  8.185   1   29.653 ? 66  PHE   B C    1 
ATOM   2906 O  O    . PHE   B 1 66  ? 3.408   23.633  8.926   1   33.588 ? 66  PHE   B O    1 
ATOM   2907 C  CB   . PHE   B 1 66  ? 5.118   21.254  9.348   1   27.55  ? 66  PHE   B CB   1 
ATOM   2908 C  CG   . PHE   B 1 66  ? 6.292   20.465  9.902   1   26.434 ? 66  PHE   B CG   1 
ATOM   2909 C  CD1  . PHE   B 1 66  ? 7.107   19.73   9.054   1   26.261 ? 66  PHE   B CD1  1 
ATOM   2910 C  CD2  . PHE   B 1 66  ? 6.61    20.506  11.255  1   26.738 ? 66  PHE   B CD2  1 
ATOM   2911 C  CE1  . PHE   B 1 66  ? 8.191   19.026  9.552   1   26.481 ? 66  PHE   B CE1  1 
ATOM   2912 C  CE2  . PHE   B 1 66  ? 7.695   19.795  11.748  1   26.537 ? 66  PHE   B CE2  1 
ATOM   2913 C  CZ   . PHE   B 1 66  ? 8.48    19.059  10.897  1   26.659 ? 66  PHE   B CZ   1 
ATOM   2914 N  N    . LEU   B 1 67  ? 4.362   23.587  6.88    1   28.416 ? 67  LEU   B N    1 
ATOM   2915 C  CA   . LEU   B 1 67  ? 3.245   24.196  6.181   1   28.566 ? 67  LEU   B CA   1 
ATOM   2916 C  C    . LEU   B 1 67  ? 2.574   23.122  5.334   1   27.083 ? 67  LEU   B C    1 
ATOM   2917 O  O    . LEU   B 1 67  ? 3.231   22.452  4.54    1   29.348 ? 67  LEU   B O    1 
ATOM   2918 C  CB   . LEU   B 1 67  ? 3.74    25.366  5.335   1   30.174 ? 67  LEU   B CB   1 
ATOM   2919 C  CG   . LEU   B 1 67  ? 4.471   26.472  6.103   1   33.093 ? 67  LEU   B CG   1 
ATOM   2920 C  CD1  . LEU   B 1 67  ? 4.989   27.526  5.15    1   33.477 ? 67  LEU   B CD1  1 
ATOM   2921 C  CD2  . LEU   B 1 67  ? 3.575   27.088  7.165   1   34.861 ? 67  LEU   B CD2  1 
ATOM   2922 N  N    . VAL   B 1 68  ? 1.265   22.958  5.531   1   25.141 ? 68  VAL   B N    1 
ATOM   2923 C  CA   . VAL   B 1 68  ? 0.504   21.93   4.85    1   23.475 ? 68  VAL   B CA   1 
ATOM   2924 C  C    . VAL   B 1 68  ? -0.636  22.605  4.098   1   23.996 ? 68  VAL   B C    1 
ATOM   2925 O  O    . VAL   B 1 68  ? -1.399  23.374  4.679   1   24.517 ? 68  VAL   B O    1 
ATOM   2926 C  CB   . VAL   B 1 68  ? -0.025  20.856  5.815   1   23.18  ? 68  VAL   B CB   1 
ATOM   2927 C  CG1  . VAL   B 1 68  ? -0.839  19.806  5.08    1   23.598 ? 68  VAL   B CG1  1 
ATOM   2928 C  CG2  . VAL   B 1 68  ? 1.105   20.193  6.59    1   23.319 ? 68  VAL   B CG2  1 
ATOM   2929 N  N    . GLN   B 1 69  ? -0.74   22.288  2.807   1   24.72  ? 69  GLN   B N    1 
ATOM   2930 C  CA   . GLN   B 1 69  ? -1.736  22.886  1.94    1   26.381 ? 69  GLN   B CA   1 
ATOM   2931 C  C    . GLN   B 1 69  ? -2.517  21.776  1.245   1   24.039 ? 69  GLN   B C    1 
ATOM   2932 O  O    . GLN   B 1 69  ? -1.925  20.907  0.615   1   23.071 ? 69  GLN   B O    1 
ATOM   2933 C  CB   . GLN   B 1 69  ? -0.98   23.775  0.953   1   30.555 ? 69  GLN   B CB   1 
ATOM   2934 C  CG   . GLN   B 1 69  ? -1.868  24.78   0.242   1   34.938 ? 69  GLN   B CG   1 
ATOM   2935 C  CD   . GLN   B 1 69  ? -1.089  25.783  -0.585  1   38.244 ? 69  GLN   B CD   1 
ATOM   2936 O  OE1  . GLN   B 1 69  ? -0.077  26.335  -0.135  1   39.566 ? 69  GLN   B OE1  1 
ATOM   2937 N  NE2  . GLN   B 1 69  ? -1.544  26.021  -1.808  1   40.806 ? 69  GLN   B NE2  1 
ATOM   2938 N  N    . ALA   B 1 70  ? -3.845  21.806  1.385   1   24.961 ? 70  ALA   B N    1 
ATOM   2939 C  CA   . ALA   B 1 70  ? -4.744  20.914  0.669   1   25.658 ? 70  ALA   B CA   1 
ATOM   2940 C  C    . ALA   B 1 70  ? -5.472  21.733  -0.393  1   27.883 ? 70  ALA   B C    1 
ATOM   2941 O  O    . ALA   B 1 70  ? -6.356  22.517  -0.064  1   29.828 ? 70  ALA   B O    1 
ATOM   2942 C  CB   . ALA   B 1 70  ? -5.715  20.275  1.638   1   26.656 ? 70  ALA   B CB   1 
ATOM   2943 N  N    . GLY   B 1 71  ? -5.069  21.575  -1.66   1   30.029 ? 71  GLY   B N    1 
ATOM   2944 C  CA   . GLY   B 1 71  ? -5.461  22.518  -2.692  1   32.667 ? 71  GLY   B CA   1 
ATOM   2945 C  C    . GLY   B 1 71  ? -5.052  23.935  -2.292  1   34.936 ? 71  GLY   B C    1 
ATOM   2946 O  O    . GLY   B 1 71  ? -3.867  24.204  -2.122  1   36.299 ? 71  GLY   B O    1 
ATOM   2947 N  N    . ASN   B 1 72  ? -6.048  24.811  -2.099  1   37.645 ? 72  ASN   B N    1 
ATOM   2948 C  CA   . ASN   B 1 72  ? -5.825  26.211  -1.766  1   40.449 ? 72  ASN   B CA   1 
ATOM   2949 C  C    . ASN   B 1 72  ? -6.027  26.484  -0.273  1   40.225 ? 72  ASN   B C    1 
ATOM   2950 O  O    . ASN   B 1 72  ? -5.972  27.639  0.141   1   41.394 ? 72  ASN   B O    1 
ATOM   2951 C  CB   . ASN   B 1 72  ? -6.747  27.112  -2.585  1   43.605 ? 72  ASN   B CB   1 
ATOM   2952 C  CG   . ASN   B 1 72  ? -6.442  27.057  -4.063  1   47.148 ? 72  ASN   B CG   1 
ATOM   2953 O  OD1  . ASN   B 1 72  ? -5.32   26.721  -4.459  1   48.767 ? 72  ASN   B OD1  1 
ATOM   2954 N  ND2  . ASN   B 1 72  ? -7.41   27.413  -4.896  1   50.878 ? 72  ASN   B ND2  1 
ATOM   2955 N  N    . VAL   B 1 73  ? -6.234  25.434  0.538   1   39.806 ? 73  VAL   B N    1 
ATOM   2956 C  CA   . VAL   B 1 73  ? -6.579  25.565  1.947   1   38.167 ? 73  VAL   B CA   1 
ATOM   2957 C  C    . VAL   B 1 73  ? -5.369  25.19   2.796   1   35.363 ? 73  VAL   B C    1 
ATOM   2958 O  O    . VAL   B 1 73  ? -4.827  24.099  2.645   1   35.225 ? 73  VAL   B O    1 
ATOM   2959 C  CB   . VAL   B 1 73  ? -7.781  24.672  2.316   1   39.607 ? 73  VAL   B CB   1 
ATOM   2960 C  CG1  . VAL   B 1 73  ? -8.109  24.728  3.807   1   40.013 ? 73  VAL   B CG1  1 
ATOM   2961 C  CG2  . VAL   B 1 73  ? -9.016  25.013  1.492   1   41.129 ? 73  VAL   B CG2  1 
ATOM   2962 N  N    . GLN   B 1 74  ? -4.97   26.084  3.706   1   34.945 ? 74  GLN   B N    1 
ATOM   2963 C  CA   . GLN   B 1 74  ? -3.904  25.8    4.652   1   34.651 ? 74  GLN   B CA   1 
ATOM   2964 C  C    . GLN   B 1 74  ? -4.47   24.984  5.812   1   33.231 ? 74  GLN   B C    1 
ATOM   2965 O  O    . GLN   B 1 74  ? -5.491  25.353  6.392   1   36.485 ? 74  GLN   B O    1 
ATOM   2966 C  CB   . GLN   B 1 74  ? -3.282  27.094  5.181   1   36.503 ? 74  GLN   B CB   1 
ATOM   2967 N  N    . LEU   B 1 75  ? -3.797  23.873  6.136   1   30.008 ? 75  LEU   B N    1 
ATOM   2968 C  CA   . LEU   B 1 75  ? -4.1    23.079  7.317   1   31     ? 75  LEU   B CA   1 
ATOM   2969 C  C    . LEU   B 1 75  ? -3.095  23.428  8.404   1   32.886 ? 75  LEU   B C    1 
ATOM   2970 O  O    . LEU   B 1 75  ? -1.893  23.416  8.151   1   36.153 ? 75  LEU   B O    1 
ATOM   2971 C  CB   . LEU   B 1 75  ? -4.017  21.586  7.014   1   29.999 ? 75  LEU   B CB   1 
ATOM   2972 C  CG   . LEU   B 1 75  ? -4.834  21.087  5.823   1   29.802 ? 75  LEU   B CG   1 
ATOM   2973 C  CD1  . LEU   B 1 75  ? -4.671  19.586  5.722   1   29.064 ? 75  LEU   B CD1  1 
ATOM   2974 C  CD2  . LEU   B 1 75  ? -6.294  21.469  5.948   1   30.908 ? 75  LEU   B CD2  1 
ATOM   2975 N  N    . ARG   B 1 76  ? -3.582  23.66   9.625   1   31.384 ? 76  ARG   B N    1 
ATOM   2976 C  CA   . ARG   B 1 76  ? -2.71   24.042  10.721  1   31.928 ? 76  ARG   B CA   1 
ATOM   2977 C  C    . ARG   B 1 76  ? -2.167  22.789  11.405  1   27.979 ? 76  ARG   B C    1 
ATOM   2978 O  O    . ARG   B 1 76  ? -2.936  21.928  11.833  1   26.522 ? 76  ARG   B O    1 
ATOM   2979 C  CB   . ARG   B 1 76  ? -3.462  24.916  11.728  1   35.227 ? 76  ARG   B CB   1 
ATOM   2980 C  CG   . ARG   B 1 76  ? -2.535  25.508  12.78   1   39.308 ? 76  ARG   B CG   1 
ATOM   2981 C  CD   . ARG   B 1 76  ? -3.189  26.508  13.709  1   43.045 ? 76  ARG   B CD   1 
ATOM   2982 N  NE   . ARG   B 1 76  ? -3.765  25.848  14.886  1   47.038 ? 76  ARG   B NE   1 
ATOM   2983 C  CZ   . ARG   B 1 76  ? -5.055  25.589  15.078  1   49.753 ? 76  ARG   B CZ   1 
ATOM   2984 N  NH1  . ARG   B 1 76  ? -5.942  25.873  14.139  1   50.85  ? 76  ARG   B NH1  1 
ATOM   2985 N  NH2  . ARG   B 1 76  ? -5.466  25.049  16.214  1   50.044 ? 76  ARG   B NH2  1 
ATOM   2986 N  N    . VAL   B 1 77  ? -0.834  22.706  11.507  1   26.294 ? 77  VAL   B N    1 
ATOM   2987 C  CA   . VAL   B 1 77  ? -0.179  21.595  12.18   1   24.587 ? 77  VAL   B CA   1 
ATOM   2988 C  C    . VAL   B 1 77  ? -0.225  21.851  13.688  1   24.183 ? 77  VAL   B C    1 
ATOM   2989 O  O    . VAL   B 1 77  ? 0.162   22.924  14.147  1   25.798 ? 77  VAL   B O    1 
ATOM   2990 C  CB   . VAL   B 1 77  ? 1.258   21.395  11.66   1   24.487 ? 77  VAL   B CB   1 
ATOM   2991 C  CG1  . VAL   B 1 77  ? 2.02    20.361  12.473  1   23.782 ? 77  VAL   B CG1  1 
ATOM   2992 C  CG2  . VAL   B 1 77  ? 1.263   21.001  10.189  1   24.661 ? 77  VAL   B CG2  1 
ATOM   2993 N  N    . ILE   B 1 78  ? -0.714  20.856  14.443  1   22.647 ? 78  ILE   B N    1 
ATOM   2994 C  CA   . ILE   B 1 78  ? -0.878  20.982  15.884  1   23.072 ? 78  ILE   B CA   1 
ATOM   2995 C  C    . ILE   B 1 78  ? -0.087  19.912  16.638  1   21.838 ? 78  ILE   B C    1 
ATOM   2996 O  O    . ILE   B 1 78  ? -0.123  19.856  17.864  1   23.56  ? 78  ILE   B O    1 
ATOM   2997 C  CB   . ILE   B 1 78  ? -2.37   20.967  16.271  1   23.661 ? 78  ILE   B CB   1 
ATOM   2998 C  CG1  . ILE   B 1 78  ? -3.062  19.656  15.893  1   24.302 ? 78  ILE   B CG1  1 
ATOM   2999 C  CG2  . ILE   B 1 78  ? -3.089  22.174  15.67   1   24.583 ? 78  ILE   B CG2  1 
ATOM   3000 C  CD1  . ILE   B 1 78  ? -4.432  19.468  16.518  1   25.015 ? 78  ILE   B CD1  1 
ATOM   3001 N  N    . GLY   B 1 79  ? 0.662   19.078  15.919  1   21.06  ? 79  GLY   B N    1 
ATOM   3002 C  CA   . GLY   B 1 79  ? 1.536   18.108  16.555  1   21.039 ? 79  GLY   B CA   1 
ATOM   3003 C  C    . GLY   B 1 79  ? 2.414   17.45   15.502  1   21.455 ? 79  GLY   B C    1 
ATOM   3004 O  O    . GLY   B 1 79  ? 2.061   17.454  14.328  1   20.257 ? 79  GLY   B O    1 
ATOM   3005 N  N    . HIS   B 1 80  ? 3.567   16.925  15.925  1   23.466 ? 80  HIS   B N    1 
ATOM   3006 C  CA   . HIS   B 1 80  ? 4.441   16.232  14.998  1   25.177 ? 80  HIS   B CA   1 
ATOM   3007 C  C    . HIS   B 1 80  ? 5.187   15.136  15.74   1   24.715 ? 80  HIS   B C    1 
ATOM   3008 O  O    . HIS   B 1 80  ? 5.541   15.284  16.907  1   26.689 ? 80  HIS   B O    1 
ATOM   3009 C  CB   . HIS   B 1 80  ? 5.404   17.206  14.315  1   27.15  ? 80  HIS   B CB   1 
ATOM   3010 C  CG   . HIS   B 1 80  ? 6.275   17.952  15.267  1   30.554 ? 80  HIS   B CG   1 
ATOM   3011 N  ND1  . HIS   B 1 80  ? 5.842   19.088  15.919  1   32.855 ? 80  HIS   B ND1  1 
ATOM   3012 C  CD2  . HIS   B 1 80  ? 7.524   17.738  15.694  1   33.29  ? 80  HIS   B CD2  1 
ATOM   3013 C  CE1  . HIS   B 1 80  ? 6.81    19.54   16.703  1   34.709 ? 80  HIS   B CE1  1 
ATOM   3014 N  NE2  . HIS   B 1 80  ? 7.842   18.738  16.58   1   35.51  ? 80  HIS   B NE2  1 
ATOM   3015 N  N    . SER   B 1 81  ? 5.407   14.026  15.04   1   22.118 ? 81  SER   B N    1 
ATOM   3016 C  CA   . SER   B 1 81  ? 6.137   12.904  15.599  1   21.745 ? 81  SER   B CA   1 
ATOM   3017 C  C    . SER   B 1 81  ? 6.586   12.016  14.457  1   20.377 ? 81  SER   B C    1 
ATOM   3018 O  O    . SER   B 1 81  ? 6.062   12.131  13.358  1   20.556 ? 81  SER   B O    1 
ATOM   3019 C  CB   . SER   B 1 81  ? 5.309   12.108  16.582  1   23.782 ? 81  SER   B CB   1 
ATOM   3020 O  OG   . SER   B 1 81  ? 4.179   11.523  15.95   1   25.57  ? 81  SER   B OG   1 
ATOM   3021 N  N    . MET   B 1 82  ? 7.524   11.12   14.748  1   20.541 ? 82  MET   B N    1 
ATOM   3022 C  CA   . MET   B 1 82  ? 8.008   10.183  13.762  1   19.958 ? 82  MET   B CA   1 
ATOM   3023 C  C    . MET   B 1 82  ? 7.568   8.776   14.146  1   18.954 ? 82  MET   B C    1 
ATOM   3024 O  O    . MET   B 1 82  ? 7.536   8.417   15.319  1   20.86  ? 82  MET   B O    1 
ATOM   3025 C  CB   . MET   B 1 82  ? 9.528   10.252  13.642  1   23.568 ? 82  MET   B CB   1 
ATOM   3026 C  CG   . MET   B 1 82  ? 10.027  11.343  12.712  1   26.128 ? 82  MET   B CG   1 
ATOM   3027 S  SD   . MET   B 1 82  ? 11.827  11.456  12.67   1   30.632 ? 82  MET   B SD   1 
ATOM   3028 C  CE   . MET   B 1 82  ? 12.211  9.834   13.322  1   25.068 ? 82  MET   B CE   1 
ATOM   3029 N  N    . GLN   B 1 83  ? 7.231   7.993   13.125  1   16.584 ? 83  GLN   B N    1 
ATOM   3030 C  CA   . GLN   B 1 83  ? 7.131   6.556   13.255  1   16.612 ? 83  GLN   B CA   1 
ATOM   3031 C  C    . GLN   B 1 83  ? 8.055   5.937   12.214  1   15.759 ? 83  GLN   B C    1 
ATOM   3032 O  O    . GLN   B 1 83  ? 7.801   6.062   11.019  1   16.041 ? 83  GLN   B O    1 
ATOM   3033 C  CB   . GLN   B 1 83  ? 5.703   6.072   13.034  1   17.618 ? 83  GLN   B CB   1 
ATOM   3034 C  CG   . GLN   B 1 83  ? 5.576   4.558   13.156  1   18.676 ? 83  GLN   B CG   1 
ATOM   3035 C  CD   . GLN   B 1 83  ? 4.156   4.081   12.985  1   20.289 ? 83  GLN   B CD   1 
ATOM   3036 O  OE1  . GLN   B 1 83  ? 3.331   4.755   12.363  1   22.648 ? 83  GLN   B OE1  1 
ATOM   3037 N  NE2  . GLN   B 1 83  ? 3.87    2.901   13.512  1   21.7   ? 83  GLN   B NE2  1 
ATOM   3038 N  N    . ASN   B 1 84  ? 9.136   5.304   12.676  1   15.156 ? 84  ASN   B N    1 
ATOM   3039 C  CA   . ASN   B 1 84  ? 10.128  4.786   11.755  1   14.425 ? 84  ASN   B CA   1 
ATOM   3040 C  C    . ASN   B 1 84  ? 10.526  5.92    10.805  1   13.999 ? 84  ASN   B C    1 
ATOM   3041 O  O    . ASN   B 1 84  ? 10.899  7.001   11.266  1   14.236 ? 84  ASN   B O    1 
ATOM   3042 C  CB   . ASN   B 1 84  ? 9.628   3.491   11.128  1   14.945 ? 84  ASN   B CB   1 
ATOM   3043 C  CG   . ASN   B 1 84  ? 9.282   2.466   12.178  1   16.733 ? 84  ASN   B CG   1 
ATOM   3044 O  OD1  . ASN   B 1 84  ? 10.077  2.214   13.088  1   18.125 ? 84  ASN   B OD1  1 
ATOM   3045 N  ND2  . ASN   B 1 84  ? 8.108   1.871   12.084  1   17.598 ? 84  ASN   B ND2  1 
ATOM   3046 N  N    . CYS   B 1 85  ? 10.435  5.688   9.492   1   13.498 ? 85  CYS   B N    1 
ATOM   3047 C  CA   . CYS   B 1 85  ? 10.891  6.67    8.52    1   13.473 ? 85  CYS   B CA   1 
ATOM   3048 C  C    . CYS   B 1 85  ? 9.79    7.59    7.996   1   13.169 ? 85  CYS   B C    1 
ATOM   3049 O  O    . CYS   B 1 85  ? 10.007  8.293   7.012   1   13.412 ? 85  CYS   B O    1 
ATOM   3050 C  CB   . CYS   B 1 85  ? 11.607  6.006   7.353   1   13.878 ? 85  CYS   B CB   1 
ATOM   3051 S  SG   . CYS   B 1 85  ? 13.032  5.015   7.857   1   15.656 ? 85  CYS   B SG   1 
ATOM   3052 N  N    . VAL   B 1 86  ? 8.622   7.603   8.655   1   13.98  ? 86  VAL   B N    1 
ATOM   3053 C  CA   . VAL   B 1 86  ? 7.551   8.517   8.302   1   15.163 ? 86  VAL   B CA   1 
ATOM   3054 C  C    . VAL   B 1 86  ? 7.369   9.566   9.392   1   15.162 ? 86  VAL   B C    1 
ATOM   3055 O  O    . VAL   B 1 86  ? 7.423   9.266   10.578  1   17.384 ? 86  VAL   B O    1 
ATOM   3056 C  CB   . VAL   B 1 86  ? 6.278   7.693   8.033   1   16.216 ? 86  VAL   B CB   1 
ATOM   3057 C  CG1  . VAL   B 1 86  ? 4.981   8.482   8.174   1   18.024 ? 86  VAL   B CG1  1 
ATOM   3058 C  CG2  . VAL   B 1 86  ? 6.376   7.048   6.658   1   16.599 ? 86  VAL   B CG2  1 
ATOM   3059 N  N    . LEU   B 1 87  ? 7.147   10.799  8.945   1   14.76  ? 87  LEU   B N    1 
ATOM   3060 C  CA   . LEU   B 1 87  ? 6.72    11.886  9.8     1   15.706 ? 87  LEU   B CA   1 
ATOM   3061 C  C    . LEU   B 1 87  ? 5.194   11.948  9.786   1   15.595 ? 87  LEU   B C    1 
ATOM   3062 O  O    . LEU   B 1 87  ? 4.572   11.86   8.728   1   15.889 ? 87  LEU   B O    1 
ATOM   3063 C  CB   . LEU   B 1 87  ? 7.366   13.16   9.256   1   17.739 ? 87  LEU   B CB   1 
ATOM   3064 C  CG   . LEU   B 1 87  ? 7.065   14.463  9.999   1   19.32  ? 87  LEU   B CG   1 
ATOM   3065 C  CD1  . LEU   B 1 87  ? 7.715   14.479  11.361  1   20.702 ? 87  LEU   B CD1  1 
ATOM   3066 C  CD2  . LEU   B 1 87  ? 7.543   15.63   9.165   1   20.212 ? 87  LEU   B CD2  1 
ATOM   3067 N  N    . LYS   B 1 88  ? 4.623   12.105  10.983  1   14.981 ? 88  LYS   B N    1 
ATOM   3068 C  CA   . LYS   B 1 88  ? 3.191   12.252  11.175  1   15.409 ? 88  LYS   B CA   1 
ATOM   3069 C  C    . LYS   B 1 88  ? 2.924   13.659  11.693  1   16.154 ? 88  LYS   B C    1 
ATOM   3070 O  O    . LYS   B 1 88  ? 3.381   14.036  12.778  1   18.612 ? 88  LYS   B O    1 
ATOM   3071 C  CB   . LYS   B 1 88  ? 2.703   11.201  12.173  1   16.829 ? 88  LYS   B CB   1 
ATOM   3072 C  CG   . LYS   B 1 88  ? 2.902   9.792   11.669  1   18.579 ? 88  LYS   B CG   1 
ATOM   3073 C  CD   . LYS   B 1 88  ? 2.713   8.699   12.71   1   23.006 ? 88  LYS   B CD   1 
ATOM   3074 C  CE   . LYS   B 1 88  ? 1.383   8.547   13.321  1   27.495 ? 88  LYS   B CE   1 
ATOM   3075 N  NZ   . LYS   B 1 88  ? 1.457   7.311   14.112  1   30.249 ? 88  LYS   B NZ   1 
ATOM   3076 N  N    . LEU   B 1 89  ? 2.201   14.435  10.885  1   15.62  ? 89  LEU   B N    1 
ATOM   3077 C  CA   . LEU   B 1 89  ? 1.82    15.781  11.26   1   15.985 ? 89  LEU   B CA   1 
ATOM   3078 C  C    . LEU   B 1 89  ? 0.35    15.743  11.637  1   16.827 ? 89  LEU   B C    1 
ATOM   3079 O  O    . LEU   B 1 89  ? -0.5    15.524  10.776  1   17.279 ? 89  LEU   B O    1 
ATOM   3080 C  CB   . LEU   B 1 89  ? 2.076   16.73   10.092  1   17.148 ? 89  LEU   B CB   1 
ATOM   3081 C  CG   . LEU   B 1 89  ? 3.518   16.779  9.581   1   18.397 ? 89  LEU   B CG   1 
ATOM   3082 C  CD1  . LEU   B 1 89  ? 3.617   17.631  8.328   1   19.783 ? 89  LEU   B CD1  1 
ATOM   3083 C  CD2  . LEU   B 1 89  ? 4.441   17.298  10.667  1   18.908 ? 89  LEU   B CD2  1 
ATOM   3084 N  N    . LYS   B 1 90  ? 0.063   15.964  12.92   1   17.311 ? 90  LYS   B N    1 
ATOM   3085 C  CA   . LYS   B 1 90  ? -1.313  16.096  13.357  1   17.901 ? 90  LYS   B CA   1 
ATOM   3086 C  C    . LYS   B 1 90  ? -1.808  17.474  12.93   1   18.705 ? 90  LYS   B C    1 
ATOM   3087 O  O    . LYS   B 1 90  ? -1.112  18.461  13.142  1   19.231 ? 90  LYS   B O    1 
ATOM   3088 C  CB   . LYS   B 1 90  ? -1.401  15.938  14.875  1   19.607 ? 90  LYS   B CB   1 
ATOM   3089 C  CG   . LYS   B 1 90  ? -2.804  15.752  15.418  1   22.818 ? 90  LYS   B CG   1 
ATOM   3090 C  CD   . LYS   B 1 90  ? -3.304  14.328  15.212  1   26.268 ? 90  LYS   B CD   1 
ATOM   3091 C  CE   . LYS   B 1 90  ? -4.255  13.827  16.247  1   29.241 ? 90  LYS   B CE   1 
ATOM   3092 N  NZ   . LYS   B 1 90  ? -4.733  12.494  15.867  1   30.857 ? 90  LYS   B NZ   1 
ATOM   3093 N  N    . VAL   B 1 91  ? -2.989  17.523  12.303  1   19.303 ? 91  VAL   B N    1 
ATOM   3094 C  CA   . VAL   B 1 91  ? -3.551  18.771  11.813  1   20.445 ? 91  VAL   B CA   1 
ATOM   3095 C  C    . VAL   B 1 91  ? -4.886  19.027  12.514  1   21.88  ? 91  VAL   B C    1 
ATOM   3096 O  O    . VAL   B 1 91  ? -5.467  18.128  13.123  1   21.823 ? 91  VAL   B O    1 
ATOM   3097 C  CB   . VAL   B 1 91  ? -3.665  18.819  10.273  1   20.711 ? 91  VAL   B CB   1 
ATOM   3098 C  CG1  . VAL   B 1 91  ? -2.289  18.893  9.621   1   21.053 ? 91  VAL   B CG1  1 
ATOM   3099 C  CG2  . VAL   B 1 91  ? -4.467  17.658  9.706   1   20.59  ? 91  VAL   B CG2  1 
ATOM   3100 N  N    . ASP   B 1 92  ? -5.368  20.267  12.399  1   25.145 ? 92  ASP   B N    1 
ATOM   3101 C  CA   . ASP   B 1 92  ? -6.53   20.721  13.143  1   27.453 ? 92  ASP   B CA   1 
ATOM   3102 C  C    . ASP   B 1 92  ? -7.845  20.317  12.477  1   28.144 ? 92  ASP   B C    1 
ATOM   3103 O  O    . ASP   B 1 92  ? -8.897  20.576  13.051  1   30.881 ? 92  ASP   B O    1 
ATOM   3104 C  CB   . ASP   B 1 92  ? -6.512  22.23   13.334  1   31.984 ? 92  ASP   B CB   1 
ATOM   3105 C  CG   . ASP   B 1 92  ? -6.653  23.083  12.079  1   36.249 ? 92  ASP   B CG   1 
ATOM   3106 O  OD1  . ASP   B 1 92  ? -6.597  22.53   10.962  1   40.015 ? 92  ASP   B OD1  1 
ATOM   3107 O  OD2  . ASP   B 1 92  ? -6.822  24.311  12.233  1   41.476 ? 92  ASP   B OD2  1 
ATOM   3108 N  N    . THR   B 1 93  ? -7.776  19.717  11.28   1   28.84  ? 93  THR   B N    1 
ATOM   3109 C  CA   . THR   B 1 93  ? -8.947  19.371  10.489  1   30.184 ? 93  THR   B CA   1 
ATOM   3110 C  C    . THR   B 1 93  ? -8.831  17.916  10.042  1   27.425 ? 93  THR   B C    1 
ATOM   3111 O  O    . THR   B 1 93  ? -7.811  17.53   9.478   1   28.061 ? 93  THR   B O    1 
ATOM   3112 C  CB   . THR   B 1 93  ? -9.028  20.296  9.272   1   33.564 ? 93  THR   B CB   1 
ATOM   3113 O  OG1  . THR   B 1 93  ? -9.044  21.642  9.738   1   36.552 ? 93  THR   B OG1  1 
ATOM   3114 C  CG2  . THR   B 1 93  ? -10.264 20.052  8.425   1   34.72  ? 93  THR   B CG2  1 
ATOM   3115 N  N    . ALA   B 1 94  ? -9.887  17.125  10.277  1   26.801 ? 94  ALA   B N    1 
ATOM   3116 C  CA   . ALA   B 1 94  ? -9.993  15.8    9.695   1   25.262 ? 94  ALA   B CA   1 
ATOM   3117 C  C    . ALA   B 1 94  ? -10.347 15.918  8.215   1   23.613 ? 94  ALA   B C    1 
ATOM   3118 O  O    . ALA   B 1 94  ? -11.198 16.716  7.838   1   25.402 ? 94  ALA   B O    1 
ATOM   3119 C  CB   . ALA   B 1 94  ? -11.016 14.969  10.433  1   26.239 ? 94  ALA   B CB   1 
ATOM   3120 N  N    . ASN   B 1 95  ? -9.694  15.109  7.375   1   21.08  ? 95  ASN   B N    1 
ATOM   3121 C  CA   . ASN   B 1 95  ? -9.985  15.122  5.952   1   19.848 ? 95  ASN   B CA   1 
ATOM   3122 C  C    . ASN   B 1 95  ? -11.412 14.626  5.725   1   19.641 ? 95  ASN   B C    1 
ATOM   3123 O  O    . ASN   B 1 95  ? -11.708 13.459  5.973   1   19.648 ? 95  ASN   B O    1 
ATOM   3124 C  CB   . ASN   B 1 95  ? -8.969  14.275  5.198   1   18.513 ? 95  ASN   B CB   1 
ATOM   3125 C  CG   . ASN   B 1 95  ? -9.153  14.337  3.702   1   18.746 ? 95  ASN   B CG   1 
ATOM   3126 O  OD1  . ASN   B 1 95  ? -10.109 14.948  3.214   1   18.904 ? 95  ASN   B OD1  1 
ATOM   3127 N  ND2  . ASN   B 1 95  ? -8.268  13.69   2.958   1   18.703 ? 95  ASN   B ND2  1 
ATOM   3128 N  N    . PRO   B 1 96  ? -12.337 15.462  5.2     1   20.699 ? 96  PRO   B N    1 
ATOM   3129 C  CA   . PRO   B 1 96  ? -13.708 15.008  4.967   1   21.415 ? 96  PRO   B CA   1 
ATOM   3130 C  C    . PRO   B 1 96  ? -13.814 13.966  3.857   1   21.576 ? 96  PRO   B C    1 
ATOM   3131 O  O    . PRO   B 1 96  ? -14.831 13.286  3.734   1   24.019 ? 96  PRO   B O    1 
ATOM   3132 C  CB   . PRO   B 1 96  ? -14.465 16.3    4.621   1   22.38  ? 96  PRO   B CB   1 
ATOM   3133 C  CG   . PRO   B 1 96  ? -13.406 17.224  4.064   1   23.203 ? 96  PRO   B CG   1 
ATOM   3134 C  CD   . PRO   B 1 96  ? -12.117 16.854  4.781   1   21.866 ? 96  PRO   B CD   1 
ATOM   3135 N  N    . LYS   B 1 97  ? -12.758 13.853  3.046   1   20.256 ? 97  LYS   B N    1 
ATOM   3136 C  CA   . LYS   B 1 97  ? -12.717 12.898  1.951   1   20.556 ? 97  LYS   B CA   1 
ATOM   3137 C  C    . LYS   B 1 97  ? -11.927 11.645  2.329   1   18.818 ? 97  LYS   B C    1 
ATOM   3138 O  O    . LYS   B 1 97  ? -11.548 10.888  1.442   1   19.606 ? 97  LYS   B O    1 
ATOM   3139 C  CB   . LYS   B 1 97  ? -12.091 13.53   0.698   1   22.754 ? 97  LYS   B CB   1 
ATOM   3140 C  CG   . LYS   B 1 97  ? -12.818 14.75   0.156   1   26.025 ? 97  LYS   B CG   1 
ATOM   3141 C  CD   . LYS   B 1 97  ? -12.297 15.249  -1.187  1   30.207 ? 97  LYS   B CD   1 
ATOM   3142 C  CE   . LYS   B 1 97  ? -13.095 16.417  -1.678  1   32.905 ? 97  LYS   B CE   1 
ATOM   3143 N  NZ   . LYS   B 1 97  ? -12.772 16.774  -3.061  1   36.275 ? 97  LYS   B NZ   1 
ATOM   3144 N  N    . THR   B 1 98  ? -11.677 11.411  3.623   1   17.896 ? 98  THR   B N    1 
ATOM   3145 C  CA   . THR   B 1 98  ? -10.949 10.216  4.032   1   17.323 ? 98  THR   B CA   1 
ATOM   3146 C  C    . THR   B 1 98  ? -11.748 8.996   3.59    1   17.226 ? 98  THR   B C    1 
ATOM   3147 O  O    . THR   B 1 98  ? -12.891 8.829   4.025   1   18.528 ? 98  THR   B O    1 
ATOM   3148 C  CB   . THR   B 1 98  ? -10.741 10.159  5.546   1   17.486 ? 98  THR   B CB   1 
ATOM   3149 O  OG1  . THR   B 1 98  ? -10.026 11.312  5.976   1   17.821 ? 98  THR   B OG1  1 
ATOM   3150 C  CG2  . THR   B 1 98  ? -9.992  8.914   5.984   1   17.89  ? 98  THR   B CG2  1 
ATOM   3151 N  N    . PRO   B 1 99  ? -11.187 8.09    2.759   1   16.354 ? 99  PRO   B N    1 
ATOM   3152 C  CA   . PRO   B 1 99  ? -11.903 6.871   2.384   1   16.863 ? 99  PRO   B CA   1 
ATOM   3153 C  C    . PRO   B 1 99  ? -11.778 5.855   3.509   1   16.465 ? 99  PRO   B C    1 
ATOM   3154 O  O    . PRO   B 1 99  ? -10.949 6.016   4.398   1   17.146 ? 99  PRO   B O    1 
ATOM   3155 C  CB   . PRO   B 1 99  ? -11.169 6.428   1.12    1   17.222 ? 99  PRO   B CB   1 
ATOM   3156 C  CG   . PRO   B 1 99  ? -9.75   6.845   1.388   1   17.335 ? 99  PRO   B CG   1 
ATOM   3157 C  CD   . PRO   B 1 99  ? -9.855  8.171   2.136   1   16.981 ? 99  PRO   B CD   1 
ATOM   3158 N  N    . LYS   B 1 100 ? -12.575 4.786   3.453   1   16.82  ? 100 LYS   B N    1 
ATOM   3159 C  CA   . LYS   B 1 100 ? -12.277 3.605   4.249   1   17.027 ? 100 LYS   B CA   1 
ATOM   3160 C  C    . LYS   B 1 100 ? -10.89  3.126   3.825   1   16.118 ? 100 LYS   B C    1 
ATOM   3161 O  O    . LYS   B 1 100 ? -10.622 3.016   2.626   1   16.52  ? 100 LYS   B O    1 
ATOM   3162 C  CB   . LYS   B 1 100 ? -13.297 2.493   3.986   1   19.473 ? 100 LYS   B CB   1 
ATOM   3163 C  CG   . LYS   B 1 100 ? -13.154 1.275   4.883   1   23.12  ? 100 LYS   B CG   1 
ATOM   3164 C  CD   . LYS   B 1 100 ? -14.133 0.149   4.572   1   26.632 ? 100 LYS   B CD   1 
ATOM   3165 C  CE   . LYS   B 1 100 ? -13.867 -1.086  5.375   1   30.264 ? 100 LYS   B CE   1 
ATOM   3166 N  NZ   . LYS   B 1 100 ? -15     -2.014  5.307   1   33.745 ? 100 LYS   B NZ   1 
ATOM   3167 N  N    . TYR   B 1 101 ? -10.003 2.889   4.795   1   14.878 ? 101 TYR   B N    1 
ATOM   3168 C  CA   . TYR   B 1 101 ? -8.63   2.567   4.44    1   14.859 ? 101 TYR   B CA   1 
ATOM   3169 C  C    . TYR   B 1 101 ? -7.986  1.678   5.498   1   15.721 ? 101 TYR   B C    1 
ATOM   3170 O  O    . TYR   B 1 101 ? -8.433  1.612   6.64    1   16.246 ? 101 TYR   B O    1 
ATOM   3171 C  CB   . TYR   B 1 101 ? -7.768  3.819   4.244   1   15.011 ? 101 TYR   B CB   1 
ATOM   3172 C  CG   . TYR   B 1 101 ? -7.345  4.494   5.541   1   14.935 ? 101 TYR   B CG   1 
ATOM   3173 C  CD1  . TYR   B 1 101 ? -8.172  5.423   6.158   1   15.246 ? 101 TYR   B CD1  1 
ATOM   3174 C  CD2  . TYR   B 1 101 ? -6.129  4.204   6.155   1   15.565 ? 101 TYR   B CD2  1 
ATOM   3175 C  CE1  . TYR   B 1 101 ? -7.824  6.027   7.354   1   16.033 ? 101 TYR   B CE1  1 
ATOM   3176 C  CE2  . TYR   B 1 101 ? -5.769  4.804   7.35    1   15.717 ? 101 TYR   B CE2  1 
ATOM   3177 C  CZ   . TYR   B 1 101 ? -6.611  5.718   7.951   1   16.494 ? 101 TYR   B CZ   1 
ATOM   3178 O  OH   . TYR   B 1 101 ? -6.235  6.302   9.131   1   18.45  ? 101 TYR   B OH   1 
ATOM   3179 N  N    . LYS   B 1 102 ? -6.9    1.029   5.066   1   15.635 ? 102 LYS   B N    1 
ATOM   3180 C  CA   . LYS   B 1 102 ? -5.999  0.294   5.931   1   16.411 ? 102 LYS   B CA   1 
ATOM   3181 C  C    . LYS   B 1 102 ? -4.583  0.566   5.444   1   15.285 ? 102 LYS   B C    1 
ATOM   3182 O  O    . LYS   B 1 102 ? -4.377  0.899   4.276   1   14.838 ? 102 LYS   B O    1 
ATOM   3183 C  CB   . LYS   B 1 102 ? -6.25   -1.215  5.837   1   19.917 ? 102 LYS   B CB   1 
ATOM   3184 C  CG   . LYS   B 1 102 ? -7.625  -1.718  6.215   1   24.466 ? 102 LYS   B CG   1 
ATOM   3185 C  CD   . LYS   B 1 102 ? -7.826  -3.171  5.799   1   29.337 ? 102 LYS   B CD   1 
ATOM   3186 C  CE   . LYS   B 1 102 ? -9.236  -3.635  6.014   1   32.897 ? 102 LYS   B CE   1 
ATOM   3187 N  NZ   . LYS   B 1 102 ? -9.567  -4.811  5.204   1   36.383 ? 102 LYS   B NZ   1 
ATOM   3188 N  N    . PHE   B 1 103 ? -3.625  0.379   6.356   1   14.441 ? 103 PHE   B N    1 
ATOM   3189 C  CA   . PHE   B 1 103 ? -2.219  0.303   5.998   1   14.415 ? 103 PHE   B CA   1 
ATOM   3190 C  C    . PHE   B 1 103 ? -1.807  -1.163  5.953   1   15.525 ? 103 PHE   B C    1 
ATOM   3191 O  O    . PHE   B 1 103 ? -2.046  -1.91   6.906   1   16.69  ? 103 PHE   B O    1 
ATOM   3192 C  CB   . PHE   B 1 103 ? -1.38   1.061   7.025   1   14.726 ? 103 PHE   B CB   1 
ATOM   3193 C  CG   . PHE   B 1 103 ? -1.555  2.571   7.081   1   14.696 ? 103 PHE   B CG   1 
ATOM   3194 C  CD1  . PHE   B 1 103 ? -2.18   3.288   6.064   1   14.467 ? 103 PHE   B CD1  1 
ATOM   3195 C  CD2  . PHE   B 1 103 ? -1.032  3.288   8.155   1   15.598 ? 103 PHE   B CD2  1 
ATOM   3196 C  CE1  . PHE   B 1 103 ? -2.262  4.67    6.123   1   14.6   ? 103 PHE   B CE1  1 
ATOM   3197 C  CE2  . PHE   B 1 103 ? -1.133  4.667   8.212   1   15.797 ? 103 PHE   B CE2  1 
ATOM   3198 C  CZ   . PHE   B 1 103 ? -1.751  5.355   7.205   1   15.252 ? 103 PHE   B CZ   1 
ATOM   3199 N  N    . VAL   B 1 104 ? -1.191  -1.562  4.836   1   14.248 ? 104 VAL   B N    1 
ATOM   3200 C  CA   . VAL   B 1 104 ? -0.779  -2.943  4.652   1   15.443 ? 104 VAL   B CA   1 
ATOM   3201 C  C    . VAL   B 1 104 ? 0.654   -2.948  4.132   1   15.481 ? 104 VAL   B C    1 
ATOM   3202 O  O    . VAL   B 1 104 ? 1.07    -2.061  3.386   1   17.852 ? 104 VAL   B O    1 
ATOM   3203 C  CB   . VAL   B 1 104 ? -1.687  -3.714  3.68    1   18.202 ? 104 VAL   B CB   1 
ATOM   3204 C  CG1  . VAL   B 1 104 ? -3.143  -3.683  4.11    1   18.612 ? 104 VAL   B CG1  1 
ATOM   3205 C  CG2  . VAL   B 1 104 ? -1.522  -3.234  2.254   1   20.334 ? 104 VAL   B CG2  1 
ATOM   3206 N  N    . ARG   B 1 105 ? 1.421   -3.937  4.57    1   14.857 ? 105 ARG   B N    1 
ATOM   3207 C  CA   . ARG   B 1 105 ? 2.754   -4.141  4.046   1   15.175 ? 105 ARG   B CA   1 
ATOM   3208 C  C    . ARG   B 1 105 ? 2.679   -5.293  3.062   1   15.327 ? 105 ARG   B C    1 
ATOM   3209 O  O    . ARG   B 1 105 ? 2.247   -6.384  3.429   1   17.975 ? 105 ARG   B O    1 
ATOM   3210 C  CB   . ARG   B 1 105 ? 3.714   -4.45   5.194   1   15.803 ? 105 ARG   B CB   1 
ATOM   3211 C  CG   . ARG   B 1 105 ? 5.157   -4.569  4.721   1   15.922 ? 105 ARG   B CG   1 
ATOM   3212 C  CD   . ARG   B 1 105 ? 6.1     -4.828  5.879   1   16.225 ? 105 ARG   B CD   1 
ATOM   3213 N  NE   . ARG   B 1 105 ? 7.479   -4.948  5.396   1   16.394 ? 105 ARG   B NE   1 
ATOM   3214 C  CZ   . ARG   B 1 105 ? 8.26    -3.946  5.01    1   15.704 ? 105 ARG   B CZ   1 
ATOM   3215 N  NH1  . ARG   B 1 105 ? 7.855   -2.692  5.115   1   14.372 ? 105 ARG   B NH1  1 
ATOM   3216 N  NH2  . ARG   B 1 105 ? 9.465   -4.217  4.538   1   16.624 ? 105 ARG   B NH2  1 
ATOM   3217 N  N    . ILE   B 1 106 ? 3.114   -5.045  1.825   1   15.361 ? 106 ILE   B N    1 
ATOM   3218 C  CA   . ILE   B 1 106 ? 3.012   -6.061  0.787   1   16.486 ? 106 ILE   B CA   1 
ATOM   3219 C  C    . ILE   B 1 106 ? 4.291   -6.881  0.686   1   16.897 ? 106 ILE   B C    1 
ATOM   3220 O  O    . ILE   B 1 106 ? 5.322   -6.537  1.255   1   17.645 ? 106 ILE   B O    1 
ATOM   3221 C  CB   . ILE   B 1 106 ? 2.642   -5.455  -0.569  1   17.363 ? 106 ILE   B CB   1 
ATOM   3222 C  CG1  . ILE   B 1 106 ? 3.653   -4.413  -1.04   1   17.343 ? 106 ILE   B CG1  1 
ATOM   3223 C  CG2  . ILE   B 1 106 ? 1.209   -4.938  -0.511  1   18.282 ? 106 ILE   B CG2  1 
ATOM   3224 C  CD1  . ILE   B 1 106 ? 3.489   -4.045  -2.5    1   18.53  ? 106 ILE   B CD1  1 
ATOM   3225 N  N    . GLN   B 1 107 ? 4.159   -8.002  -0.022  1   18.401 ? 107 GLN   B N    1 
ATOM   3226 C  CA   . GLN   B 1 107 ? 5.256   -8.924  -0.235  1   19.733 ? 107 GLN   B CA   1 
ATOM   3227 C  C    . GLN   B 1 107 ? 5.795   -8.757  -1.647  1   18.173 ? 107 GLN   B C    1 
ATOM   3228 O  O    . GLN   B 1 107 ? 5.078   -8.331  -2.557  1   16.786 ? 107 GLN   B O    1 
ATOM   3229 C  CB   . GLN   B 1 107 ? 4.812   -10.373 -0.055  1   23.249 ? 107 GLN   B CB   1 
ATOM   3230 C  CG   . GLN   B 1 107 ? 4.1     -10.637 1.269   1   28.231 ? 107 GLN   B CG   1 
ATOM   3231 C  CD   . GLN   B 1 107 ? 4.346   -12.026 1.804   1   33.292 ? 107 GLN   B CD   1 
ATOM   3232 O  OE1  . GLN   B 1 107 ? 5.483   -12.378 2.128   1   39.618 ? 107 GLN   B OE1  1 
ATOM   3233 N  NE2  . GLN   B 1 107 ? 3.293   -12.827 1.903   1   37.463 ? 107 GLN   B NE2  1 
ATOM   3234 N  N    . PRO   B 1 108 ? 7.068   -9.125  -1.886  1   18.638 ? 108 PRO   B N    1 
ATOM   3235 C  CA   . PRO   B 1 108 ? 7.612   -9.098  -3.24   1   18.27  ? 108 PRO   B CA   1 
ATOM   3236 C  C    . PRO   B 1 108 ? 6.725   -9.92   -4.164  1   16.952 ? 108 PRO   B C    1 
ATOM   3237 O  O    . PRO   B 1 108 ? 6.241   -10.99  -3.79   1   18.061 ? 108 PRO   B O    1 
ATOM   3238 C  CB   . PRO   B 1 108 ? 9.008   -9.7    -3.108  1   19.834 ? 108 PRO   B CB   1 
ATOM   3239 C  CG   . PRO   B 1 108 ? 9.34    -9.465  -1.673  1   21.799 ? 108 PRO   B CG   1 
ATOM   3240 C  CD   . PRO   B 1 108 ? 8.044   -9.604  -0.888  1   20.541 ? 108 PRO   B CD   1 
ATOM   3241 N  N    . GLY   B 1 109 ? 6.522   -9.381  -5.366  1   15.853 ? 109 GLY   B N    1 
ATOM   3242 C  CA   . GLY   B 1 109 ? 5.681   -10.004 -6.373  1   16.261 ? 109 GLY   B CA   1 
ATOM   3243 C  C    . GLY   B 1 109 ? 4.291   -9.387  -6.441  1   15.695 ? 109 GLY   B C    1 
ATOM   3244 O  O    . GLY   B 1 109 ? 3.612   -9.49   -7.459  1   18.376 ? 109 GLY   B O    1 
ATOM   3245 N  N    . GLN   B 1 110 ? 3.845   -8.763  -5.35   1   14.519 ? 110 GLN   B N    1 
ATOM   3246 C  CA   . GLN   B 1 110 ? 2.537   -8.14   -5.327  1   15.456 ? 110 GLN   B CA   1 
ATOM   3247 C  C    . GLN   B 1 110 ? 2.598   -6.826  -6.095  1   14.647 ? 110 GLN   B C    1 
ATOM   3248 O  O    . GLN   B 1 110 ? 3.616   -6.147  -6.115  1   14.903 ? 110 GLN   B O    1 
ATOM   3249 C  CB   . GLN   B 1 110 ? 2.073   -7.954  -3.883  1   17.272 ? 110 GLN   B CB   1 
ATOM   3250 C  CG   . GLN   B 1 110 ? 1.758   -9.259  -3.151  1   21.523 ? 110 GLN   B CG   1 
ATOM   3251 C  CD   . GLN   B 1 110 ? 1.068   -9.071  -1.813  1   25.301 ? 110 GLN   B CD   1 
ATOM   3252 O  OE1  . GLN   B 1 110 ? 1.692   -8.822  -0.773  1   27.899 ? 110 GLN   B OE1  1 
ATOM   3253 N  NE2  . GLN   B 1 110 ? -0.247  -9.226  -1.819  1   30.039 ? 110 GLN   B NE2  1 
ATOM   3254 N  N    . THR   B 1 111 ? 1.464   -6.471  -6.708  1   14.402 ? 111 THR   B N    1 
ATOM   3255 C  CA   . THR   B 1 111 ? 1.331   -5.262  -7.494  1   14.142 ? 111 THR   B CA   1 
ATOM   3256 C  C    . THR   B 1 111 ? 0.511   -4.217  -6.741  1   13.624 ? 111 THR   B C    1 
ATOM   3257 O  O    . THR   B 1 111 ? -0.192  -4.516  -5.78   1   14.612 ? 111 THR   B O    1 
ATOM   3258 C  CB   . THR   B 1 111 ? 0.699   -5.596  -8.838  1   15.272 ? 111 THR   B CB   1 
ATOM   3259 O  OG1  . THR   B 1 111 ? -0.561  -6.2    -8.563  1   15.437 ? 111 THR   B OG1  1 
ATOM   3260 C  CG2  . THR   B 1 111 ? 1.573   -6.522  -9.657  1   15.603 ? 111 THR   B CG2  1 
ATOM   3261 N  N    . PHE   B 1 112 ? 0.627   -2.981  -7.205  1   13.16  ? 112 PHE   B N    1 
ATOM   3262 C  CA   . PHE   B 1 112 ? -0.143  -1.88   -6.666  1   12.902 ? 112 PHE   B CA   1 
ATOM   3263 C  C    . PHE   B 1 112 ? -0.112  -0.726  -7.655  1   12.066 ? 112 PHE   B C    1 
ATOM   3264 O  O    . PHE   B 1 112 ? 0.726   -0.678  -8.559  1   12.726 ? 112 PHE   B O    1 
ATOM   3265 C  CB   . PHE   B 1 112 ? 0.405   -1.446  -5.307  1   13.357 ? 112 PHE   B CB   1 
ATOM   3266 C  CG   . PHE   B 1 112 ? 1.874   -1.063  -5.288  1   13.503 ? 112 PHE   B CG   1 
ATOM   3267 C  CD1  . PHE   B 1 112 ? 2.869   -2.018  -5.111  1   14.915 ? 112 PHE   B CD1  1 
ATOM   3268 C  CD2  . PHE   B 1 112 ? 2.251   0.263   -5.432  1   14.067 ? 112 PHE   B CD2  1 
ATOM   3269 C  CE1  . PHE   B 1 112 ? 4.206   -1.633  -5.059  1   15.87  ? 112 PHE   B CE1  1 
ATOM   3270 C  CE2  . PHE   B 1 112 ? 3.576   0.642   -5.365  1   14.888 ? 112 PHE   B CE2  1 
ATOM   3271 C  CZ   . PHE   B 1 112 ? 4.548   -0.306  -5.178  1   15.449 ? 112 PHE   B CZ   1 
ATOM   3272 N  N    . SER   B 1 113 ? -1.057  0.196   -7.465  1   11.957 ? 113 SER   B N    1 
ATOM   3273 C  CA   . SER   B 1 113 ? -1.127  1.395   -8.272  1   12.212 ? 113 SER   B CA   1 
ATOM   3274 C  C    . SER   B 1 113 ? -0.357  2.5     -7.57   1   11.861 ? 113 SER   B C    1 
ATOM   3275 O  O    . SER   B 1 113 ? -0.512  2.685   -6.362  1   12.935 ? 113 SER   B O    1 
ATOM   3276 C  CB   . SER   B 1 113 ? -2.555  1.825   -8.467  1   13.287 ? 113 SER   B CB   1 
ATOM   3277 O  OG   . SER   B 1 113 ? -3.286  0.823   -9.149  1   15.79  ? 113 SER   B OG   1 
ATOM   3278 N  N    . VAL   B 1 114 ? 0.394   3.275   -8.35   1   12.134 ? 114 VAL   B N    1 
ATOM   3279 C  CA   . VAL   B 1 114 ? 1.104   4.447   -7.867  1   11.858 ? 114 VAL   B CA   1 
ATOM   3280 C  C    . VAL   B 1 114 ? 0.394   5.689   -8.381  1   11.811 ? 114 VAL   B C    1 
ATOM   3281 O  O    . VAL   B 1 114 ? 0.126   5.807   -9.575  1   13.065 ? 114 VAL   B O    1 
ATOM   3282 C  CB   . VAL   B 1 114 ? 2.56    4.449   -8.364  1   13.196 ? 114 VAL   B CB   1 
ATOM   3283 C  CG1  . VAL   B 1 114 ? 3.262   5.782   -8.111  1   13.274 ? 114 VAL   B CG1  1 
ATOM   3284 C  CG2  . VAL   B 1 114 ? 3.335   3.283   -7.765  1   14.162 ? 114 VAL   B CG2  1 
ATOM   3285 N  N    . LEU   B 1 115 ? 0.119   6.611   -7.462  1   11.912 ? 115 LEU   B N    1 
ATOM   3286 C  CA   . LEU   B 1 115 ? -0.346  7.935   -7.819  1   12.194 ? 115 LEU   B CA   1 
ATOM   3287 C  C    . LEU   B 1 115 ? 0.825   8.899   -7.678  1   12.294 ? 115 LEU   B C    1 
ATOM   3288 O  O    . LEU   B 1 115 ? 1.188   9.295   -6.57   1   12.955 ? 115 LEU   B O    1 
ATOM   3289 C  CB   . LEU   B 1 115 ? -1.513  8.345   -6.932  1   12.758 ? 115 LEU   B CB   1 
ATOM   3290 C  CG   . LEU   B 1 115 ? -2.162  9.682   -7.296  1   13.61  ? 115 LEU   B CG   1 
ATOM   3291 C  CD1  . LEU   B 1 115 ? -2.823  9.608   -8.666  1   14.245 ? 115 LEU   B CD1  1 
ATOM   3292 C  CD2  . LEU   B 1 115 ? -3.179  10.108  -6.247  1   14.265 ? 115 LEU   B CD2  1 
ATOM   3293 N  N    . ALA   B 1 116 ? 1.458   9.212   -8.813  1   12.693 ? 116 ALA   B N    1 
ATOM   3294 C  CA   . ALA   B 1 116 ? 2.591   10.116  -8.837  1   13.551 ? 116 ALA   B CA   1 
ATOM   3295 C  C    . ALA   B 1 116 ? 2.068   11.531  -8.632  1   13.704 ? 116 ALA   B C    1 
ATOM   3296 O  O    . ALA   B 1 116 ? 1.124   11.947  -9.302  1   16.332 ? 116 ALA   B O    1 
ATOM   3297 C  CB   . ALA   B 1 116 ? 3.356   9.979   -10.125 1   14.076 ? 116 ALA   B CB   1 
ATOM   3298 N  N    A CYS   B 1 117 ? 2.661   12.234  -7.662  0.5 13.269 ? 117 CYS   B N    1 
ATOM   3299 N  N    B CYS   B 1 117 ? 2.748   12.274  -7.757  0.5 15.077 ? 117 CYS   B N    1 
ATOM   3300 C  CA   A CYS   B 1 117 ? 2.256   13.582  -7.319  0.5 12.982 ? 117 CYS   B CA   1 
ATOM   3301 C  CA   B CYS   B 1 117 ? 2.265   13.541  -7.247  0.5 16.002 ? 117 CYS   B CA   1 
ATOM   3302 C  C    A CYS   B 1 117 ? 3.458   14.515  -7.245  0.5 13.552 ? 117 CYS   B C    1 
ATOM   3303 C  C    B CYS   B 1 117 ? 3.438   14.522  -7.174  0.5 15.351 ? 117 CYS   B C    1 
ATOM   3304 O  O    A CYS   B 1 117 ? 4.57    14.09   -6.93   0.5 13.442 ? 117 CYS   B O    1 
ATOM   3305 O  O    B CYS   B 1 117 ? 4.551   14.12   -6.845  0.5 15.125 ? 117 CYS   B O    1 
ATOM   3306 C  CB   A CYS   B 1 117 ? 1.58    13.632  -5.961  0.5 12.46  ? 117 CYS   B CB   1 
ATOM   3307 C  CB   B CYS   B 1 117 ? 1.626   13.261  -5.893  0.5 17.914 ? 117 CYS   B CB   1 
ATOM   3308 S  SG   A CYS   B 1 117 ? 0.121   12.575  -5.819  0.5 11.632 ? 117 CYS   B SG   1 
ATOM   3309 S  SG   B CYS   B 1 117 ? 0.499   14.552  -5.32   0.5 22.71  ? 117 CYS   B SG   1 
ATOM   3310 N  N    . TYR   B 1 118 ? 3.18    15.796  -7.501  1   15.208 ? 118 TYR   B N    1 
ATOM   3311 C  CA   . TYR   B 1 118 ? 4.156   16.871  -7.402  1   15.425 ? 118 TYR   B CA   1 
ATOM   3312 C  C    . TYR   B 1 118 ? 3.452   18.067  -6.769  1   16.644 ? 118 TYR   B C    1 
ATOM   3313 O  O    . TYR   B 1 118 ? 2.348   18.416  -7.188  1   17.577 ? 118 TYR   B O    1 
ATOM   3314 C  CB   . TYR   B 1 118 ? 4.745   17.252  -8.772  1   15.962 ? 118 TYR   B CB   1 
ATOM   3315 C  CG   . TYR   B 1 118 ? 5.471   16.071  -9.389  1   15.758 ? 118 TYR   B CG   1 
ATOM   3316 C  CD1  . TYR   B 1 118 ? 6.805   15.828  -9.093  1   15.794 ? 118 TYR   B CD1  1 
ATOM   3317 C  CD2  . TYR   B 1 118 ? 4.789   15.131  -10.156 1   15.609 ? 118 TYR   B CD2  1 
ATOM   3318 C  CE1  . TYR   B 1 118 ? 7.453   14.708  -9.584  1   15.774 ? 118 TYR   B CE1  1 
ATOM   3319 C  CE2  . TYR   B 1 118 ? 5.416   13.998  -10.641 1   15.858 ? 118 TYR   B CE2  1 
ATOM   3320 C  CZ   . TYR   B 1 118 ? 6.759   13.796  -10.361 1   15.277 ? 118 TYR   B CZ   1 
ATOM   3321 O  OH   . TYR   B 1 118 ? 7.399   12.684  -10.807 1   15.511 ? 118 TYR   B OH   1 
ATOM   3322 N  N    . ASN   B 1 119 ? 4.081   18.679  -5.756  1   18.366 ? 119 ASN   B N    1 
ATOM   3323 C  CA   . ASN   B 1 119 ? 3.533   19.864  -5.116  1   20.344 ? 119 ASN   B CA   1 
ATOM   3324 C  C    . ASN   B 1 119 ? 2.13    19.601  -4.57   1   19.235 ? 119 ASN   B C    1 
ATOM   3325 O  O    . ASN   B 1 119 ? 1.291   20.5    -4.567  1   21.152 ? 119 ASN   B O    1 
ATOM   3326 C  CB   . ASN   B 1 119 ? 3.537   21.054  -6.072  1   23.31  ? 119 ASN   B CB   1 
ATOM   3327 C  CG   . ASN   B 1 119 ? 4.946   21.45   -6.432  1   28.172 ? 119 ASN   B CG   1 
ATOM   3328 O  OD1  . ASN   B 1 119 ? 5.75    21.736  -5.539  1   35.819 ? 119 ASN   B OD1  1 
ATOM   3329 N  ND2  . ASN   B 1 119 ? 5.279   21.42   -7.713  1   32.146 ? 119 ASN   B ND2  1 
ATOM   3330 N  N    . GLY   B 1 120 ? 1.875   18.373  -4.108  1   17.822 ? 120 GLY   B N    1 
ATOM   3331 C  CA   . GLY   B 1 120 ? 0.582   18.008  -3.547  1   17.796 ? 120 GLY   B CA   1 
ATOM   3332 C  C    . GLY   B 1 120 ? -0.507  17.721  -4.583  1   18.673 ? 120 GLY   B C    1 
ATOM   3333 O  O    . GLY   B 1 120 ? -1.636  17.419  -4.201  1   20.101 ? 120 GLY   B O    1 
ATOM   3334 N  N    A SER   B 1 121 ? -0.165  17.825  -5.87   0.5 18.353 ? 121 SER   B N    1 
ATOM   3335 N  N    B SER   B 1 121 ? -0.136  17.739  -5.87   0.5 18.079 ? 121 SER   B N    1 
ATOM   3336 C  CA   A SER   B 1 121 ? -1.123  17.651  -6.948  0.5 19.024 ? 121 SER   B CA   1 
ATOM   3337 C  CA   B SER   B 1 121 ? -1.075  17.668  -6.98   0.5 18.418 ? 121 SER   B CA   1 
ATOM   3338 C  C    A SER   B 1 121 ? -0.852  16.331  -7.658  0.5 18.042 ? 121 SER   B C    1 
ATOM   3339 C  C    B SER   B 1 121 ? -0.88   16.376  -7.769  0.5 17.204 ? 121 SER   B C    1 
ATOM   3340 O  O    A SER   B 1 121 ? 0.27    16.07   -8.094  0.5 18.167 ? 121 SER   B O    1 
ATOM   3341 O  O    B SER   B 1 121 ? 0.144   16.201  -8.437  0.5 16.221 ? 121 SER   B O    1 
ATOM   3342 C  CB   A SER   B 1 121 ? -1.068  18.796  -7.908  0.5 20.399 ? 121 SER   B CB   1 
ATOM   3343 C  CB   B SER   B 1 121 ? -0.927  18.869  -7.88   0.5 19.452 ? 121 SER   B CB   1 
ATOM   3344 O  OG   A SER   B 1 121 ? -2.087  18.684  -8.89   0.5 22.054 ? 121 SER   B OG   1 
ATOM   3345 O  OG   B SER   B 1 121 ? -1.484  20.02   -7.26   0.5 21.043 ? 121 SER   B OG   1 
ATOM   3346 N  N    . PRO   B 1 122 ? -1.852  15.43   -7.754  1   17.26  ? 122 PRO   B N    1 
ATOM   3347 C  CA   . PRO   B 1 122 ? -1.702  14.211  -8.548  1   17.561 ? 122 PRO   B CA   1 
ATOM   3348 C  C    . PRO   B 1 122 ? -1.459  14.483  -10.032 1   17.359 ? 122 PRO   B C    1 
ATOM   3349 O  O    . PRO   B 1 122 ? -2.138  15.318  -10.631 1   18.664 ? 122 PRO   B O    1 
ATOM   3350 C  CB   . PRO   B 1 122 ? -3.017  13.483  -8.292  1   18.001 ? 122 PRO   B CB   1 
ATOM   3351 C  CG   . PRO   B 1 122 ? -3.489  14.015  -6.958  1   18.767 ? 122 PRO   B CG   1 
ATOM   3352 C  CD   . PRO   B 1 122 ? -3.106  15.474  -6.985  1   18.333 ? 122 PRO   B CD   1 
ATOM   3353 N  N    . SER   B 1 123 ? -0.492  13.757  -10.607 1   16.751 ? 123 SER   B N    1 
ATOM   3354 C  CA   . SER   B 1 123 ? -0.018  14.006  -11.957 1   17.025 ? 123 SER   B CA   1 
ATOM   3355 C  C    . SER   B 1 123 ? -0.266  12.802  -12.859 1   14.951 ? 123 SER   B C    1 
ATOM   3356 O  O    . SER   B 1 123 ? -0.492  12.966  -14.049 1   16.321 ? 123 SER   B O    1 
ATOM   3357 C  CB   . SER   B 1 123 ? 1.44    14.402  -11.956 1   20.423 ? 123 SER   B CB   1 
ATOM   3358 O  OG   . SER   B 1 123 ? 2.249   13.342  -11.497 1   25.526 ? 123 SER   B OG   1 
ATOM   3359 N  N    . GLY   B 1 124 ? -0.181  11.589  -12.322 1   13.427 ? 124 GLY   B N    1 
ATOM   3360 C  CA   . GLY   B 1 124 ? -0.324  10.404  -13.145 1   13.357 ? 124 GLY   B CA   1 
ATOM   3361 C  C    . GLY   B 1 124 ? -0.531  9.156   -12.306 1   13.062 ? 124 GLY   B C    1 
ATOM   3362 O  O    . GLY   B 1 124 ? -0.25   9.159   -11.118 1   13.783 ? 124 GLY   B O    1 
ATOM   3363 N  N    . VAL   B 1 125 ? -1.04   8.094   -12.936 1   12.412 ? 125 VAL   B N    1 
ATOM   3364 C  CA   . VAL   B 1 125 ? -1.267  6.832   -12.25  1   13.093 ? 125 VAL   B CA   1 
ATOM   3365 C  C    . VAL   B 1 125 ? -0.738  5.706   -13.127 1   13.19  ? 125 VAL   B C    1 
ATOM   3366 O  O    . VAL   B 1 125 ? -0.921  5.726   -14.341 1   15.166 ? 125 VAL   B O    1 
ATOM   3367 C  CB   . VAL   B 1 125 ? -2.75   6.65    -11.849 1   15.867 ? 125 VAL   B CB   1 
ATOM   3368 C  CG1  . VAL   B 1 125 ? -3.685  6.563   -13.04  1   17.629 ? 125 VAL   B CG1  1 
ATOM   3369 C  CG2  . VAL   B 1 125 ? -2.958  5.476   -10.911 1   16.849 ? 125 VAL   B CG2  1 
ATOM   3370 N  N    . TYR   B 1 126 ? -0.093  4.724   -12.492 1   12.395 ? 126 TYR   B N    1 
ATOM   3371 C  CA   . TYR   B 1 126 ? 0.393   3.553   -13.2   1   12.89  ? 126 TYR   B CA   1 
ATOM   3372 C  C    . TYR   B 1 126 ? 0.542   2.39    -12.222 1   12.975 ? 126 TYR   B C    1 
ATOM   3373 O  O    . TYR   B 1 126 ? 0.629   2.588   -11.021 1   14.09  ? 126 TYR   B O    1 
ATOM   3374 C  CB   . TYR   B 1 126 ? 1.723   3.809   -13.92  1   13.762 ? 126 TYR   B CB   1 
ATOM   3375 C  CG   . TYR   B 1 126 ? 2.813   4.415   -13.058 1   14.417 ? 126 TYR   B CG   1 
ATOM   3376 C  CD1  . TYR   B 1 126 ? 3.657   3.634   -12.277 1   14.769 ? 126 TYR   B CD1  1 
ATOM   3377 C  CD2  . TYR   B 1 126 ? 2.998   5.786   -13.039 1   16.46  ? 126 TYR   B CD2  1 
ATOM   3378 C  CE1  . TYR   B 1 126 ? 4.632   4.217   -11.489 1   15.566 ? 126 TYR   B CE1  1 
ATOM   3379 C  CE2  . TYR   B 1 126 ? 3.971   6.374   -12.258 1   16.853 ? 126 TYR   B CE2  1 
ATOM   3380 C  CZ   . TYR   B 1 126 ? 4.776   5.588   -11.468 1   15.781 ? 126 TYR   B CZ   1 
ATOM   3381 O  OH   . TYR   B 1 126 ? 5.756   6.143   -10.7   1   18.105 ? 126 TYR   B OH   1 
ATOM   3382 N  N    . GLN   B 1 127 ? 0.623   1.172   -12.759 1   14.886 ? 127 GLN   B N    1 
ATOM   3383 C  CA   . GLN   B 1 127 ? 0.832   -0.03   -11.971 1   15.917 ? 127 GLN   B CA   1 
ATOM   3384 C  C    . GLN   B 1 127 ? 2.321   -0.345  -11.827 1   16.679 ? 127 GLN   B C    1 
ATOM   3385 O  O    . GLN   B 1 127 ? 3.084   -0.219  -12.784 1   17.473 ? 127 GLN   B O    1 
ATOM   3386 C  CB   . GLN   B 1 127 ? 0.342   -1.286  -12.687 1   19.187 ? 127 GLN   B CB   1 
ATOM   3387 C  CG   . GLN   B 1 127 ? -1.133  -1.583  -12.592 1   21.124 ? 127 GLN   B CG   1 
ATOM   3388 C  CD   . GLN   B 1 127 ? -1.603  -1.734  -11.17  1   20.54  ? 127 GLN   B CD   1 
ATOM   3389 O  OE1  . GLN   B 1 127 ? -1.982  -0.75   -10.553 1   20.397 ? 127 GLN   B OE1  1 
ATOM   3390 N  NE2  . GLN   B 1 127 ? -1.653  -2.955  -10.658 1   19.541 ? 127 GLN   B NE2  1 
ATOM   3391 N  N    . CYS   B 1 128 ? 2.682   -0.846  -10.64  1   16.095 ? 128 CYS   B N    1 
ATOM   3392 C  CA   . CYS   B 1 128 ? 4.024   -1.301  -10.295 1   16.727 ? 128 CYS   B CA   1 
ATOM   3393 C  C    . CYS   B 1 128 ? 3.911   -2.659  -9.609  1   15.81  ? 128 CYS   B C    1 
ATOM   3394 O  O    . CYS   B 1 128 ? 2.878   -2.992  -9.059  1   18.94  ? 128 CYS   B O    1 
ATOM   3395 C  CB   . CYS   B 1 128 ? 4.718   -0.316  -9.34   1   17.425 ? 128 CYS   B CB   1 
ATOM   3396 S  SG   . CYS   B 1 128 ? 5.46    1.082   -10.216 1   23.206 ? 128 CYS   B SG   1 
ATOM   3397 N  N    . ALA   B 1 129 ? 4.975   -3.452  -9.644  1   15.834 ? 129 ALA   B N    1 
ATOM   3398 C  CA   . ALA   B 1 129 ? 5.149   -4.588  -8.751  1   15.123 ? 129 ALA   B CA   1 
ATOM   3399 C  C    . ALA   B 1 129 ? 6.277   -4.291  -7.769  1   14.735 ? 129 ALA   B C    1 
ATOM   3400 O  O    . ALA   B 1 129 ? 7.268   -3.644  -8.104  1   15.528 ? 129 ALA   B O    1 
ATOM   3401 C  CB   . ALA   B 1 129 ? 5.467   -5.841  -9.521  1   16.142 ? 129 ALA   B CB   1 
ATOM   3402 N  N    . MET   B 1 130 ? 6.132   -4.812  -6.556  1   13.572 ? 130 MET   B N    1 
ATOM   3403 C  CA   . MET   B 1 130 ? 7.263   -4.881  -5.648  1   13.73  ? 130 MET   B CA   1 
ATOM   3404 C  C    . MET   B 1 130 ? 8.198   -5.964  -6.177  1   13.423 ? 130 MET   B C    1 
ATOM   3405 O  O    . MET   B 1 130 ? 7.824   -7.128  -6.258  1   13.938 ? 130 MET   B O    1 
ATOM   3406 C  CB   . MET   B 1 130 ? 6.788   -5.204  -4.23   1   14.485 ? 130 MET   B CB   1 
ATOM   3407 C  CG   . MET   B 1 130 ? 7.901   -5.271  -3.202  1   15.456 ? 130 MET   B CG   1 
ATOM   3408 S  SD   . MET   B 1 130 ? 8.856   -3.759  -2.995  1   16.622 ? 130 MET   B SD   1 
ATOM   3409 C  CE   . MET   B 1 130 ? 7.579   -2.592  -2.521  1   15.952 ? 130 MET   B CE   1 
ATOM   3410 N  N    . ARG   B 1 131 ? 9.4     -5.565  -6.603  1   13.022 ? 131 ARG   B N    1 
ATOM   3411 C  CA   . ARG   B 1 131 ? 10.333  -6.519  -7.18   1   12.923 ? 131 ARG   B CA   1 
ATOM   3412 C  C    . ARG   B 1 131 ? 10.866  -7.451  -6.094  1   12.89  ? 131 ARG   B C    1 
ATOM   3413 O  O    . ARG   B 1 131 ? 10.877  -7.12   -4.904  1   12.98  ? 131 ARG   B O    1 
ATOM   3414 C  CB   . ARG   B 1 131 ? 11.512  -5.804  -7.851  1   13.335 ? 131 ARG   B CB   1 
ATOM   3415 C  CG   . ARG   B 1 131 ? 11.164  -4.834  -8.971  1   13.852 ? 131 ARG   B CG   1 
ATOM   3416 C  CD   . ARG   B 1 131 ? 10.331  -5.449  -10.053 1   13.924 ? 131 ARG   B CD   1 
ATOM   3417 N  NE   . ARG   B 1 131 ? 10.946  -6.669  -10.584 1   13.86  ? 131 ARG   B NE   1 
ATOM   3418 C  CZ   . ARG   B 1 131 ? 10.349  -7.507  -11.411 1   13.832 ? 131 ARG   B CZ   1 
ATOM   3419 N  NH1  . ARG   B 1 131 ? 9.183   -7.182  -11.952 1   13.872 ? 131 ARG   B NH1  1 
ATOM   3420 N  NH2  . ARG   B 1 131 ? 10.932  -8.648  -11.727 1   14.792 ? 131 ARG   B NH2  1 
ATOM   3421 N  N    . PRO   B 1 132 ? 11.367  -8.645  -6.464  1   12.911 ? 132 PRO   B N    1 
ATOM   3422 C  CA   . PRO   B 1 132 ? 12.054  -9.501  -5.494  1   13.39  ? 132 PRO   B CA   1 
ATOM   3423 C  C    . PRO   B 1 132 ? 13.192  -8.819  -4.737  1   13.323 ? 132 PRO   B C    1 
ATOM   3424 O  O    . PRO   B 1 132 ? 13.443  -9.172  -3.587  1   14.489 ? 132 PRO   B O    1 
ATOM   3425 C  CB   . PRO   B 1 132 ? 12.536  -10.656 -6.369  1   14.088 ? 132 PRO   B CB   1 
ATOM   3426 C  CG   . PRO   B 1 132 ? 11.481  -10.749 -7.448  1   14.273 ? 132 PRO   B CG   1 
ATOM   3427 C  CD   . PRO   B 1 132 ? 11.178  -9.303  -7.767  1   13.796 ? 132 PRO   B CD   1 
ATOM   3428 N  N    . ASN   B 1 133 ? 13.833  -7.819  -5.361  1   13.088 ? 133 ASN   B N    1 
ATOM   3429 C  CA   . ASN   B 1 133 ? 14.907  -7.074  -4.707  1   13.431 ? 133 ASN   B CA   1 
ATOM   3430 C  C    . ASN   B 1 133 ? 14.39   -5.857  -3.937  1   13.778 ? 133 ASN   B C    1 
ATOM   3431 O  O    . ASN   B 1 133 ? 15.184  -5.032  -3.496  1   14.34  ? 133 ASN   B O    1 
ATOM   3432 C  CB   . ASN   B 1 133 ? 16.014  -6.715  -5.695  1   14.022 ? 133 ASN   B CB   1 
ATOM   3433 C  CG   . ASN   B 1 133 ? 15.615  -5.628  -6.664  1   13.828 ? 133 ASN   B CG   1 
ATOM   3434 O  OD1  . ASN   B 1 133 ? 14.478  -5.142  -6.643  1   13.881 ? 133 ASN   B OD1  1 
ATOM   3435 N  ND2  . ASN   B 1 133 ? 16.531  -5.235  -7.542  1   14.344 ? 133 ASN   B ND2  1 
ATOM   3436 N  N    . PHE   B 1 134 ? 13.065  -5.763  -3.764  1   13.169 ? 134 PHE   B N    1 
ATOM   3437 C  CA   . PHE   B 1 134 ? 12.389  -4.772  -2.934  1   13.812 ? 134 PHE   B CA   1 
ATOM   3438 C  C    . PHE   B 1 134 ? 12.507  -3.351  -3.476  1   14.35  ? 134 PHE   B C    1 
ATOM   3439 O  O    . PHE   B 1 134 ? 12.353  -2.39   -2.734  1   17.616 ? 134 PHE   B O    1 
ATOM   3440 C  CB   . PHE   B 1 134 ? 12.899  -4.813  -1.492  1   14.141 ? 134 PHE   B CB   1 
ATOM   3441 C  CG   . PHE   B 1 134 ? 12.423  -6.027  -0.725  1   14.933 ? 134 PHE   B CG   1 
ATOM   3442 C  CD1  . PHE   B 1 134 ? 11.093  -6.128  -0.322  1   16.459 ? 134 PHE   B CD1  1 
ATOM   3443 C  CD2  . PHE   B 1 134 ? 13.298  -7.042  -0.372  1   15.951 ? 134 PHE   B CD2  1 
ATOM   3444 C  CE1  . PHE   B 1 134 ? 10.648  -7.228  0.393   1   17.778 ? 134 PHE   B CE1  1 
ATOM   3445 C  CE2  . PHE   B 1 134 ? 12.85   -8.133  0.357   1   17.525 ? 134 PHE   B CE2  1 
ATOM   3446 C  CZ   . PHE   B 1 134 ? 11.534  -8.214  0.751   1   18.191 ? 134 PHE   B CZ   1 
ATOM   3447 N  N    . THR   B 1 135 ? 12.777  -3.202  -4.767  1   13.922 ? 135 THR   B N    1 
ATOM   3448 C  CA   . THR   B 1 135 ? 12.642  -1.927  -5.446  1   13.746 ? 135 THR   B CA   1 
ATOM   3449 C  C    . THR   B 1 135 ? 11.353  -1.95   -6.261  1   13.053 ? 135 THR   B C    1 
ATOM   3450 O  O    . THR   B 1 135 ? 10.735  -3.005  -6.438  1   13.974 ? 135 THR   B O    1 
ATOM   3451 C  CB   . THR   B 1 135 ? 13.865  -1.653  -6.327  1   14.013 ? 135 THR   B CB   1 
ATOM   3452 O  OG1  . THR   B 1 135 ? 13.911  -2.587  -7.407  1   14.473 ? 135 THR   B OG1  1 
ATOM   3453 C  CG2  . THR   B 1 135 ? 15.152  -1.677  -5.516  1   14.954 ? 135 THR   B CG2  1 
ATOM   3454 N  N    . ILE   B 1 136 ? 10.991  -0.78   -6.787  1   13.056 ? 136 ILE   B N    1 
ATOM   3455 C  CA   . ILE   B 1 136 ? 9.949   -0.73   -7.798  1   13.498 ? 136 ILE   B CA   1 
ATOM   3456 C  C    . ILE   B 1 136 ? 10.508  0.003   -9.007  1   13.269 ? 136 ILE   B C    1 
ATOM   3457 O  O    . ILE   B 1 136 ? 11.345  0.893   -8.891  1   13.827 ? 136 ILE   B O    1 
ATOM   3458 C  CB   . ILE   B 1 136 ? 8.629   -0.119  -7.288  1   15.536 ? 136 ILE   B CB   1 
ATOM   3459 C  CG1  . ILE   B 1 136 ? 8.72    1.381   -7.035  1   15.332 ? 136 ILE   B CG1  1 
ATOM   3460 C  CG2  . ILE   B 1 136 ? 8.14    -0.888  -6.063  1   17.112 ? 136 ILE   B CG2  1 
ATOM   3461 C  CD1  . ILE   B 1 136 ? 7.397   2.04    -6.656  1   15.524 ? 136 ILE   B CD1  1 
ATOM   3462 N  N    . LYS   B 1 137 ? 10.051  -0.43   -10.178 1   13.913 ? 137 LYS   B N    1 
ATOM   3463 C  CA   . LYS   B 1 137 ? 10.416  0.23    -11.413 1   14.698 ? 137 LYS   B CA   1 
ATOM   3464 C  C    . LYS   B 1 137 ? 9.348   1.265   -11.722 1   14.882 ? 137 LYS   B C    1 
ATOM   3465 O  O    . LYS   B 1 137 ? 8.416   1.02    -12.478 1   15.401 ? 137 LYS   B O    1 
ATOM   3466 C  CB   . LYS   B 1 137 ? 10.599  -0.796  -12.526 1   17.031 ? 137 LYS   B CB   1 
ATOM   3467 C  CG   . LYS   B 1 137 ? 11.715  -1.802  -12.295 1   19.485 ? 137 LYS   B CG   1 
ATOM   3468 C  CD   . LYS   B 1 137 ? 11.867  -2.739  -13.488 1   23.333 ? 137 LYS   B CD   1 
ATOM   3469 C  CE   . LYS   B 1 137 ? 12.634  -3.974  -13.183 1   27.462 ? 137 LYS   B CE   1 
ATOM   3470 N  NZ   . LYS   B 1 137 ? 12.703  -4.822  -14.372 1   30.237 ? 137 LYS   B NZ   1 
ATOM   3471 N  N    . GLY   B 1 138 ? 9.466   2.401   -11.044 1   14.988 ? 138 GLY   B N    1 
ATOM   3472 C  CA   . GLY   B 1 138 ? 8.48    3.454   -11.168 1   15.407 ? 138 GLY   B CA   1 
ATOM   3473 C  C    . GLY   B 1 138 ? 8.907   4.482   -12.209 1   14.522 ? 138 GLY   B C    1 
ATOM   3474 O  O    . GLY   B 1 138 ? 9.834   4.264   -12.992 1   16.256 ? 138 GLY   B O    1 
ATOM   3475 N  N    . SER   B 1 139 ? 8.198   5.601   -12.195 1   13.769 ? 139 SER   B N    1 
ATOM   3476 C  CA   . SER   B 1 139 ? 8.494   6.754   -13.019 1   13.513 ? 139 SER   B CA   1 
ATOM   3477 C  C    . SER   B 1 139 ? 8.29    7.972   -12.129 1   13.447 ? 139 SER   B C    1 
ATOM   3478 O  O    . SER   B 1 139 ? 7.156   8.344   -11.832 1   14.357 ? 139 SER   B O    1 
ATOM   3479 C  CB   . SER   B 1 139 ? 7.626   6.796   -14.241 1   14.613 ? 139 SER   B CB   1 
ATOM   3480 O  OG   . SER   B 1 139 ? 7.98    7.944   -14.992 1   16.187 ? 139 SER   B OG   1 
ATOM   3481 N  N    . PHE   B 1 140 ? 9.398   8.516   -11.628 1   13.209 ? 140 PHE   B N    1 
ATOM   3482 C  CA   . PHE   B 1 140 ? 9.384   9.547   -10.609 1   13.551 ? 140 PHE   B CA   1 
ATOM   3483 C  C    . PHE   B 1 140 ? 10.499  10.553  -10.867 1   14.123 ? 140 PHE   B C    1 
ATOM   3484 O  O    . PHE   B 1 140 ? 11.628  10.167  -11.179 1   15.119 ? 140 PHE   B O    1 
ATOM   3485 C  CB   . PHE   B 1 140 ? 9.64    8.964   -9.221  1   14.013 ? 140 PHE   B CB   1 
ATOM   3486 C  CG   . PHE   B 1 140 ? 8.545   8.099   -8.617  1   14.057 ? 140 PHE   B CG   1 
ATOM   3487 C  CD1  . PHE   B 1 140 ? 7.321   8.644   -8.233  1   15.383 ? 140 PHE   B CD1  1 
ATOM   3488 C  CD2  . PHE   B 1 140 ? 8.769   6.752   -8.393  1   15.622 ? 140 PHE   B CD2  1 
ATOM   3489 C  CE1  . PHE   B 1 140 ? 6.356   7.857   -7.642  1   16.239 ? 140 PHE   B CE1  1 
ATOM   3490 C  CE2  . PHE   B 1 140 ? 7.809   5.983   -7.751  1   16.912 ? 140 PHE   B CE2  1 
ATOM   3491 C  CZ   . PHE   B 1 140 ? 6.618   6.547   -7.371  1   16.705 ? 140 PHE   B CZ   1 
ATOM   3492 N  N    . LEU   B 1 141 ? 10.162  11.834  -10.705 1   15.143 ? 141 LEU   B N    1 
ATOM   3493 C  CA   . LEU   B 1 141 ? 11.098  12.929  -10.871 1   15.646 ? 141 LEU   B CA   1 
ATOM   3494 C  C    . LEU   B 1 141 ? 11.283  13.624  -9.528  1   15.918 ? 141 LEU   B C    1 
ATOM   3495 O  O    . LEU   B 1 141 ? 10.58   13.349  -8.553  1   15.516 ? 141 LEU   B O    1 
ATOM   3496 C  CB   . LEU   B 1 141 ? 10.571  13.924  -11.906 1   16.602 ? 141 LEU   B CB   1 
ATOM   3497 C  CG   . LEU   B 1 141 ? 10.371  13.362  -13.319 1   18.411 ? 141 LEU   B CG   1 
ATOM   3498 C  CD1  . LEU   B 1 141 ? 9.799   14.44   -14.216 1   19.677 ? 141 LEU   B CD1  1 
ATOM   3499 C  CD2  . LEU   B 1 141 ? 11.654  12.789  -13.911 1   19.861 ? 141 LEU   B CD2  1 
ATOM   3500 N  N    . ASN   B 1 142 ? 12.222  14.57   -9.5    1   16.413 ? 142 ASN   B N    1 
ATOM   3501 C  CA   . ASN   B 1 142 ? 12.377  15.464  -8.374  1   17.188 ? 142 ASN   B CA   1 
ATOM   3502 C  C    . ASN   B 1 142 ? 11.022  16.055  -7.997  1   16.531 ? 142 ASN   B C    1 
ATOM   3503 O  O    . ASN   B 1 142 ? 10.306  16.575  -8.854  1   17.399 ? 142 ASN   B O    1 
ATOM   3504 C  CB   . ASN   B 1 142 ? 13.402  16.539  -8.714  1   18.805 ? 142 ASN   B CB   1 
ATOM   3505 C  CG   . ASN   B 1 142 ? 13.749  17.41   -7.535  1   21.785 ? 142 ASN   B CG   1 
ATOM   3506 O  OD1  . ASN   B 1 142 ? 13.896  16.91   -6.417  1   23.682 ? 142 ASN   B OD1  1 
ATOM   3507 N  ND2  . ASN   B 1 142 ? 13.906  18.702  -7.778  1   25.622 ? 142 ASN   B ND2  1 
ATOM   3508 N  N    . GLY   B 1 143 ? 10.692  15.969  -6.7    1   16.025 ? 143 GLY   B N    1 
ATOM   3509 C  CA   . GLY   B 1 143 ? 9.458   16.508  -6.156  1   15.645 ? 143 GLY   B CA   1 
ATOM   3510 C  C    . GLY   B 1 143 ? 8.39    15.442  -5.898  1   15.05  ? 143 GLY   B C    1 
ATOM   3511 O  O    . GLY   B 1 143 ? 7.332   15.762  -5.36   1   15.682 ? 143 GLY   B O    1 
ATOM   3512 N  N    . SER   B 1 144 ? 8.667   14.181  -6.245  1   13.972 ? 144 SER   B N    1 
ATOM   3513 C  CA   . SER   B 1 144 ? 7.677   13.116  -6.154  1   13.483 ? 144 SER   B CA   1 
ATOM   3514 C  C    . SER   B 1 144 ? 7.649   12.406  -4.801  1   13.283 ? 144 SER   B C    1 
ATOM   3515 O  O    . SER   B 1 144 ? 6.822   11.527  -4.597  1   12.591 ? 144 SER   B O    1 
ATOM   3516 C  CB   . SER   B 1 144 ? 7.909   12.095  -7.229  1   13.808 ? 144 SER   B CB   1 
ATOM   3517 O  OG   . SER   B 1 144 ? 9.2     11.505  -7.094  1   13.96  ? 144 SER   B OG   1 
ATOM   3518 N  N    . CYS   B 1 145 ? 8.563   12.733  -3.887  1   13.374 ? 145 CYS   B N    1 
ATOM   3519 C  CA   . CYS   B 1 145 ? 8.586   12.039  -2.611  1   13.339 ? 145 CYS   B CA   1 
ATOM   3520 C  C    . CYS   B 1 145 ? 7.255   12.225  -1.883  1   12.711 ? 145 CYS   B C    1 
ATOM   3521 O  O    . CYS   B 1 145 ? 6.644   13.293  -1.928  1   13.651 ? 145 CYS   B O    1 
ATOM   3522 C  CB   . CYS   B 1 145 ? 9.733   12.516  -1.731  1   14.009 ? 145 CYS   B CB   1 
ATOM   3523 S  SG   . CYS   B 1 145 ? 11.359  12.219  -2.461  1   16.099 ? 145 CYS   B SG   1 
ATOM   3524 N  N    . GLY   B 1 146 ? 6.804   11.156  -1.222  1   12.314 ? 146 GLY   B N    1 
ATOM   3525 C  CA   . GLY   B 1 146 ? 5.514   11.161  -0.546  1   12.283 ? 146 GLY   B CA   1 
ATOM   3526 C  C    . GLY   B 1 146 ? 4.358   10.724  -1.448  1   12.601 ? 146 GLY   B C    1 
ATOM   3527 O  O    . GLY   B 1 146 ? 3.25    10.544  -0.945  1   13.422 ? 146 GLY   B O    1 
ATOM   3528 N  N    . SER   B 1 147 ? 4.614   10.54   -2.752  1   12.111 ? 147 SER   B N    1 
ATOM   3529 C  CA   . SER   B 1 147 ? 3.67    9.828   -3.603  1   11.982 ? 147 SER   B CA   1 
ATOM   3530 C  C    . SER   B 1 147 ? 3.398   8.452   -3.007  1   12.1   ? 147 SER   B C    1 
ATOM   3531 O  O    . SER   B 1 147 ? 4.272   7.868   -2.381  1   12.517 ? 147 SER   B O    1 
ATOM   3532 C  CB   . SER   B 1 147 ? 4.201   9.68    -5.021  1   12.027 ? 147 SER   B CB   1 
ATOM   3533 O  OG   . SER   B 1 147 ? 4.368   10.928  -5.674  1   12.931 ? 147 SER   B OG   1 
ATOM   3534 N  N    . VAL   B 1 148 ? 2.19    7.922   -3.214  1   11.734 ? 148 VAL   B N    1 
ATOM   3535 C  CA   . VAL   B 1 148 ? 1.801   6.682   -2.567  1   12.112 ? 148 VAL   B CA   1 
ATOM   3536 C  C    . VAL   B 1 148 ? 1.364   5.626   -3.57   1   11.943 ? 148 VAL   B C    1 
ATOM   3537 O  O    . VAL   B 1 148 ? 0.938   5.923   -4.683  1   12.782 ? 148 VAL   B O    1 
ATOM   3538 C  CB   . VAL   B 1 148 ? 0.718   6.867   -1.49   1   13.818 ? 148 VAL   B CB   1 
ATOM   3539 C  CG1  . VAL   B 1 148 ? 1.247   7.738   -0.367  1   14.787 ? 148 VAL   B CG1  1 
ATOM   3540 C  CG2  . VAL   B 1 148 ? -0.605  7.376   -2.047  1   15.576 ? 148 VAL   B CG2  1 
ATOM   3541 N  N    . GLY   B 1 149 ? 1.457   4.387   -3.089  1   12.147 ? 149 GLY   B N    1 
ATOM   3542 C  CA   . GLY   B 1 149 ? 0.972   3.22    -3.786  1   11.659 ? 149 GLY   B CA   1 
ATOM   3543 C  C    . GLY   B 1 149 ? -0.12   2.542   -2.97   1   11.844 ? 149 GLY   B C    1 
ATOM   3544 O  O    . GLY   B 1 149 ? -0.1    2.575   -1.735  1   12.085 ? 149 GLY   B O    1 
ATOM   3545 N  N    . PHE   B 1 150 ? -1.07   1.925   -3.683  1   11.994 ? 150 PHE   B N    1 
ATOM   3546 C  CA   . PHE   B 1 150 ? -2.256  1.386   -3.037  1   12.368 ? 150 PHE   B CA   1 
ATOM   3547 C  C    . PHE   B 1 150 ? -2.91   0.317   -3.906  1   12.447 ? 150 PHE   B C    1 
ATOM   3548 O  O    . PHE   B 1 150 ? -2.673  0.234   -5.112  1   12.368 ? 150 PHE   B O    1 
ATOM   3549 C  CB   . PHE   B 1 150 ? -3.258  2.516   -2.771  1   13.167 ? 150 PHE   B CB   1 
ATOM   3550 C  CG   . PHE   B 1 150 ? -3.779  3.161   -4.047  1   14.706 ? 150 PHE   B CG   1 
ATOM   3551 C  CD1  . PHE   B 1 150 ? -3.047  4.13    -4.722  1   15.732 ? 150 PHE   B CD1  1 
ATOM   3552 C  CD2  . PHE   B 1 150 ? -5.003  2.766   -4.577  1   15.363 ? 150 PHE   B CD2  1 
ATOM   3553 C  CE1  . PHE   B 1 150 ? -3.511  4.66    -5.914  1   16.911 ? 150 PHE   B CE1  1 
ATOM   3554 C  CE2  . PHE   B 1 150 ? -5.473  3.323   -5.756  1   16.411 ? 150 PHE   B CE2  1 
ATOM   3555 C  CZ   . PHE   B 1 150 ? -4.725  4.261   -6.417  1   16.938 ? 150 PHE   B CZ   1 
ATOM   3556 N  N    . ASN   B 1 151 ? -3.757  -0.471  -3.241  1   12.79  ? 151 ASN   B N    1 
ATOM   3557 C  CA   . ASN   B 1 151 ? -4.732  -1.337  -3.879  1   13.688 ? 151 ASN   B CA   1 
ATOM   3558 C  C    . ASN   B 1 151 ? -6.118  -0.964  -3.354  1   14.524 ? 151 ASN   B C    1 
ATOM   3559 O  O    . ASN   B 1 151 ? -6.24   -0.33   -2.311  1   15.213 ? 151 ASN   B O    1 
ATOM   3560 C  CB   . ASN   B 1 151 ? -4.427  -2.799  -3.572  1   15.105 ? 151 ASN   B CB   1 
ATOM   3561 C  CG   . ASN   B 1 151 ? -3.234  -3.32   -4.331  1   16.448 ? 151 ASN   B CG   1 
ATOM   3562 O  OD1  . ASN   B 1 151 ? -3.382  -3.747  -5.469  1   20.657 ? 151 ASN   B OD1  1 
ATOM   3563 N  ND2  . ASN   B 1 151 ? -2.064  -3.366  -3.723  1   16.531 ? 151 ASN   B ND2  1 
ATOM   3564 N  N    . ILE   B 1 152 ? -7.163  -1.361  -4.08   1   14.997 ? 152 ILE   B N    1 
ATOM   3565 C  CA   . ILE   B 1 152 ? -8.519  -1.24   -3.566  1   17.927 ? 152 ILE   B CA   1 
ATOM   3566 C  C    . ILE   B 1 152 ? -9.152  -2.626  -3.503  1   20.94  ? 152 ILE   B C    1 
ATOM   3567 O  O    . ILE   B 1 152 ? -8.93   -3.456  -4.377  1   22.175 ? 152 ILE   B O    1 
ATOM   3568 C  CB   . ILE   B 1 152 ? -9.357  -0.283  -4.427  1   19.647 ? 152 ILE   B CB   1 
ATOM   3569 C  CG1  . ILE   B 1 152 ? -8.651  1.052   -4.678  1   20.706 ? 152 ILE   B CG1  1 
ATOM   3570 C  CG2  . ILE   B 1 152 ? -10.737 -0.084  -3.798  1   20.917 ? 152 ILE   B CG2  1 
ATOM   3571 C  CD1  . ILE   B 1 152 ? -9.447  2.02    -5.543  1   23.208 ? 152 ILE   B CD1  1 
ATOM   3572 N  N    . ASP   B 1 153 ? -9.958  -2.839  -2.458  1   25.466 ? 153 ASP   B N    1 
ATOM   3573 C  CA   . ASP   B 1 153 ? -10.862 -3.977  -2.392  1   29.65  ? 153 ASP   B CA   1 
ATOM   3574 C  C    . ASP   B 1 153 ? -12.234 -3.454  -1.977  1   31.953 ? 153 ASP   B C    1 
ATOM   3575 O  O    . ASP   B 1 153 ? -12.369 -2.862  -0.91   1   33.845 ? 153 ASP   B O    1 
ATOM   3576 C  CB   . ASP   B 1 153 ? -10.325 -5.049  -1.458  1   32.568 ? 153 ASP   B CB   1 
ATOM   3577 N  N    . TYR   B 1 154 ? -13.228 -3.65   -2.853  1   35.772 ? 154 TYR   B N    1 
ATOM   3578 C  CA   . TYR   B 1 154 ? -14.553 -3.066  -2.722  1   37.803 ? 154 TYR   B CA   1 
ATOM   3579 C  C    . TYR   B 1 154 ? -14.432 -1.556  -2.504  1   39.03  ? 154 TYR   B C    1 
ATOM   3580 O  O    . TYR   B 1 154 ? -14.159 -0.807  -3.443  1   39.845 ? 154 TYR   B O    1 
ATOM   3581 C  CB   . TYR   B 1 154 ? -15.311 -3.826  -1.626  1   36.796 ? 154 TYR   B CB   1 
ATOM   3582 N  N    . ASP   B 1 155 ? -14.593 -1.133  -1.247  1   38.496 ? 155 ASP   B N    1 
ATOM   3583 C  CA   . ASP   B 1 155 ? -14.622 0.276   -0.889  1   37.19  ? 155 ASP   B CA   1 
ATOM   3584 C  C    . ASP   B 1 155 ? -13.402 0.668   -0.048  1   33.158 ? 155 ASP   B C    1 
ATOM   3585 O  O    . ASP   B 1 155 ? -13.304 1.831   0.362   1   34.36  ? 155 ASP   B O    1 
ATOM   3586 C  CB   . ASP   B 1 155 ? -15.896 0.599   -0.128  1   40.272 ? 155 ASP   B CB   1 
ATOM   3587 C  CG   . ASP   B 1 155 ? -16.162 -0.287  1.08    1   43.117 ? 155 ASP   B CG   1 
ATOM   3588 O  OD1  . ASP   B 1 155 ? -15.483 -1.331  1.205   1   44.805 ? 155 ASP   B OD1  1 
ATOM   3589 O  OD2  . ASP   B 1 155 ? -17.048 0.071   1.879   1   47.479 ? 155 ASP   B OD2  1 
ATOM   3590 N  N    . CYS   B 1 156 ? -12.476 -0.277  0.202   1   27.56  ? 156 CYS   B N    1 
ATOM   3591 C  CA   . CYS   B 1 156 ? -11.389 -0.038  1.147   1   22.659 ? 156 CYS   B CA   1 
ATOM   3592 C  C    . CYS   B 1 156 ? -10.062 0.141   0.415   1   19.768 ? 156 CYS   B C    1 
ATOM   3593 O  O    . CYS   B 1 156 ? -9.631  -0.72   -0.346  1   20.575 ? 156 CYS   B O    1 
ATOM   3594 C  CB   . CYS   B 1 156 ? -11.245 -1.158  2.169   1   25.594 ? 156 CYS   B CB   1 
ATOM   3595 S  SG   . CYS   B 1 156 ? -9.969  -0.822  3.411   1   27.631 ? 156 CYS   B SG   1 
ATOM   3596 N  N    . VAL   B 1 157 ? -9.423  1.287   0.662   1   16.687 ? 157 VAL   B N    1 
ATOM   3597 C  CA   . VAL   B 1 157 ? -8.118  1.567   0.089   1   15.652 ? 157 VAL   B CA   1 
ATOM   3598 C  C    . VAL   B 1 157 ? -7.056  0.99    1.019   1   14.813 ? 157 VAL   B C    1 
ATOM   3599 O  O    . VAL   B 1 157 ? -6.96   1.396   2.175   1   16.521 ? 157 VAL   B O    1 
ATOM   3600 C  CB   . VAL   B 1 157 ? -7.877  3.073   -0.11   1   16.588 ? 157 VAL   B CB   1 
ATOM   3601 C  CG1  . VAL   B 1 157 ? -6.496  3.325   -0.709  1   16.645 ? 157 VAL   B CG1  1 
ATOM   3602 C  CG2  . VAL   B 1 157 ? -8.961  3.711   -0.969  1   17.368 ? 157 VAL   B CG2  1 
ATOM   3603 N  N    . SER   B 1 158 ? -6.24   0.073   0.493   1   13.792 ? 158 SER   B N    1 
ATOM   3604 C  CA   . SER   B 1 158 ? -5.115  -0.47   1.239   1   13.924 ? 158 SER   B CA   1 
ATOM   3605 C  C    . SER   B 1 158 ? -3.847  0.234   0.764   1   13.135 ? 158 SER   B C    1 
ATOM   3606 O  O    . SER   B 1 158 ? -3.353  -0.053  -0.32   1   14.171 ? 158 SER   B O    1 
ATOM   3607 C  CB   . SER   B 1 158 ? -5.017  -1.963  1.064   1   15.334 ? 158 SER   B CB   1 
ATOM   3608 O  OG   . SER   B 1 158 ? -6.089  -2.607  1.732   1   18.425 ? 158 SER   B OG   1 
ATOM   3609 N  N    . PHE   B 1 159 ? -3.327  1.163   1.576   1   12.845 ? 159 PHE   B N    1 
ATOM   3610 C  CA   . PHE   B 1 159 ? -2.1    1.871   1.25    1   12.926 ? 159 PHE   B CA   1 
ATOM   3611 C  C    . PHE   B 1 159 ? -0.908  0.991   1.591   1   12.584 ? 159 PHE   B C    1 
ATOM   3612 O  O    . PHE   B 1 159 ? -0.827  0.485   2.709   1   13.447 ? 159 PHE   B O    1 
ATOM   3613 C  CB   . PHE   B 1 159 ? -1.996  3.174   2.044   1   12.753 ? 159 PHE   B CB   1 
ATOM   3614 C  CG   . PHE   B 1 159 ? -3.033  4.203   1.65    1   12.936 ? 159 PHE   B CG   1 
ATOM   3615 C  CD1  . PHE   B 1 159 ? -2.869  4.959   0.501   1   13.3   ? 159 PHE   B CD1  1 
ATOM   3616 C  CD2  . PHE   B 1 159 ? -4.146  4.436   2.447   1   13.607 ? 159 PHE   B CD2  1 
ATOM   3617 C  CE1  . PHE   B 1 159 ? -3.802  5.908   0.148   1   14.065 ? 159 PHE   B CE1  1 
ATOM   3618 C  CE2  . PHE   B 1 159 ? -5.089  5.385   2.081   1   14.095 ? 159 PHE   B CE2  1 
ATOM   3619 C  CZ   . PHE   B 1 159 ? -4.91   6.12    0.938   1   14.245 ? 159 PHE   B CZ   1 
ATOM   3620 N  N    . CYS   B 1 160 ? 0.015   0.834   0.63    1   11.865 ? 160 CYS   B N    1 
ATOM   3621 C  CA   . CYS   B 1 160 ? 1.133   -0.082  0.821   1   12.449 ? 160 CYS   B CA   1 
ATOM   3622 C  C    . CYS   B 1 160 ? 2.499   0.552   0.568   1   12.322 ? 160 CYS   B C    1 
ATOM   3623 O  O    . CYS   B 1 160 ? 3.485   -0.077  0.923   1   13.124 ? 160 CYS   B O    1 
ATOM   3624 C  CB   . CYS   B 1 160 ? 0.974   -1.333  -0.033  1   13.374 ? 160 CYS   B CB   1 
ATOM   3625 S  SG   . CYS   B 1 160 ? 0.849   -1.014  -1.814  1   14.56  ? 160 CYS   B SG   1 
ATOM   3626 N  N    . TYR   B 1 161 ? 2.587   1.738   -0.029  1   11.46  ? 161 TYR   B N    1 
ATOM   3627 C  CA   . TYR   B 1 161 ? 3.881   2.293   -0.404  1   11.503 ? 161 TYR   B CA   1 
ATOM   3628 C  C    . TYR   B 1 161 ? 3.851   3.808   -0.272  1   11.418 ? 161 TYR   B C    1 
ATOM   3629 O  O    . TYR   B 1 161 ? 2.867   4.45    -0.633  1   11.792 ? 161 TYR   B O    1 
ATOM   3630 C  CB   . TYR   B 1 161 ? 4.236   1.908   -1.847  1   11.537 ? 161 TYR   B CB   1 
ATOM   3631 C  CG   . TYR   B 1 161 ? 5.558   2.448   -2.383  1   11.963 ? 161 TYR   B CG   1 
ATOM   3632 C  CD1  . TYR   B 1 161 ? 6.768   1.809   -2.121  1   12.152 ? 161 TYR   B CD1  1 
ATOM   3633 C  CD2  . TYR   B 1 161 ? 5.603   3.595   -3.158  1   11.735 ? 161 TYR   B CD2  1 
ATOM   3634 C  CE1  . TYR   B 1 161 ? 7.961   2.301   -2.618  1   12.628 ? 161 TYR   B CE1  1 
ATOM   3635 C  CE2  . TYR   B 1 161 ? 6.793   4.086   -3.673  1   12.131 ? 161 TYR   B CE2  1 
ATOM   3636 C  CZ   . TYR   B 1 161 ? 7.988   3.443   -3.39   1   12.479 ? 161 TYR   B CZ   1 
ATOM   3637 O  OH   . TYR   B 1 161 ? 9.194   3.911   -3.852  1   13.413 ? 161 TYR   B OH   1 
ATOM   3638 N  N    . MET   B 1 162 ? 4.949   4.364   0.247   1   11.537 ? 162 MET   B N    1 
ATOM   3639 C  CA   A MET   B 1 162 ? 5.229   5.786   0.186   0.6 12.115 ? 162 MET   B CA   1 
ATOM   3640 C  CA   B MET   B 1 162 ? 5.217   5.786   0.155   0.4 11.066 ? 162 MET   B CA   1 
ATOM   3641 C  C    . MET   B 1 162 ? 6.619   5.961   -0.415  1   11.408 ? 162 MET   B C    1 
ATOM   3642 O  O    . MET   B 1 162 ? 7.566   5.299   0.014   1   11.594 ? 162 MET   B O    1 
ATOM   3643 C  CB   A MET   B 1 162 ? 5.183   6.425   1.579   0.6 13.889 ? 162 MET   B CB   1 
ATOM   3644 C  CB   B MET   B 1 162 ? 5.095   6.497   1.509   0.4 10.934 ? 162 MET   B CB   1 
ATOM   3645 C  CG   A MET   B 1 162 ? 5.557   7.895   1.601   0.6 15.525 ? 162 MET   B CG   1 
ATOM   3646 C  CG   B MET   B 1 162 ? 5.449   7.968   1.434   0.4 10.416 ? 162 MET   B CG   1 
ATOM   3647 S  SD   A MET   B 1 162 ? 5.822   8.544   3.268   0.6 19.181 ? 162 MET   B SD   1 
ATOM   3648 S  SD   B MET   B 1 162 ? 4.852   8.981   2.803   0.4 9.792  ? 162 MET   B SD   1 
ATOM   3649 C  CE   A MET   B 1 162 ? 4.249   8.242   4.084   0.6 18.964 ? 162 MET   B CE   1 
ATOM   3650 C  CE   B MET   B 1 162 ? 3.101   9.215   2.478   0.4 9.805  ? 162 MET   B CE   1 
ATOM   3651 N  N    . HIS   B 1 163 ? 6.737   6.849   -1.399  1   11.208 ? 163 HIS   B N    1 
ATOM   3652 C  CA   . HIS   B 1 163 ? 7.97    7       -2.159  1   11.217 ? 163 HIS   B CA   1 
ATOM   3653 C  C    . HIS   B 1 163 ? 8.993   7.851   -1.405  1   11.8   ? 163 HIS   B C    1 
ATOM   3654 O  O    . HIS   B 1 163 ? 8.685   8.971   -0.995  1   12.524 ? 163 HIS   B O    1 
ATOM   3655 C  CB   . HIS   B 1 163 ? 7.642   7.665   -3.499  1   11.661 ? 163 HIS   B CB   1 
ATOM   3656 C  CG   . HIS   B 1 163 ? 8.832   7.767   -4.372  1   12.251 ? 163 HIS   B CG   1 
ATOM   3657 N  ND1  . HIS   B 1 163 ? 9.64    6.679   -4.609  1   12.463 ? 163 HIS   B ND1  1 
ATOM   3658 C  CD2  . HIS   B 1 163 ? 9.364   8.802   -5.026  1   12.261 ? 163 HIS   B CD2  1 
ATOM   3659 C  CE1  . HIS   B 1 163 ? 10.635  7.069   -5.388  1   12.596 ? 163 HIS   B CE1  1 
ATOM   3660 N  NE2  . HIS   B 1 163 ? 10.511  8.354   -5.643  1   12.791 ? 163 HIS   B NE2  1 
ATOM   3661 N  N    . HIS   B 1 164 ? 10.23   7.327   -1.267  1   11.809 ? 164 HIS   B N    1 
ATOM   3662 C  CA   . HIS   B 1 164 ? 11.294  8.071   -0.602  1   12.331 ? 164 HIS   B CA   1 
ATOM   3663 C  C    . HIS   B 1 164 ? 12.446  8.5     -1.516  1   13.068 ? 164 HIS   B C    1 
ATOM   3664 O  O    . HIS   B 1 164 ? 12.965  9.595   -1.315  1   14.798 ? 164 HIS   B O    1 
ATOM   3665 C  CB   . HIS   B 1 164 ? 11.865  7.313   0.603   1   12.334 ? 164 HIS   B CB   1 
ATOM   3666 C  CG   . HIS   B 1 164 ? 10.954  7.23    1.778   1   12.727 ? 164 HIS   B CG   1 
ATOM   3667 N  ND1  . HIS   B 1 164 ? 11.253  7.778   3.009   1   12.895 ? 164 HIS   B ND1  1 
ATOM   3668 C  CD2  . HIS   B 1 164 ? 9.72    6.705   1.884   1   12.948 ? 164 HIS   B CD2  1 
ATOM   3669 C  CE1  . HIS   B 1 164 ? 10.248  7.553   3.837   1   12.738 ? 164 HIS   B CE1  1 
ATOM   3670 N  NE2  . HIS   B 1 164 ? 9.296   6.914   3.173   1   13.276 ? 164 HIS   B NE2  1 
ATOM   3671 N  N    . MET   B 1 165 ? 12.928  7.646   -2.426  1   13.497 ? 165 MET   B N    1 
ATOM   3672 C  CA   . MET   B 1 165 ? 14.083  8.056   -3.224  1   13.901 ? 165 MET   B CA   1 
ATOM   3673 C  C    . MET   B 1 165 ? 14.262  7.194   -4.473  1   13.915 ? 165 MET   B C    1 
ATOM   3674 O  O    . MET   B 1 165 ? 13.692  6.113   -4.606  1   13.724 ? 165 MET   B O    1 
ATOM   3675 C  CB   . MET   B 1 165 ? 15.394  8.056   -2.427  1   16.082 ? 165 MET   B CB   1 
ATOM   3676 C  CG   . MET   B 1 165 ? 15.944  6.703   -2.148  1   17.329 ? 165 MET   B CG   1 
ATOM   3677 S  SD   . MET   B 1 165 ? 15.17   5.937   -0.719  1   20.376 ? 165 MET   B SD   1 
ATOM   3678 C  CE   . MET   B 1 165 ? 16.563  4.856   -0.394  1   19.23  ? 165 MET   B CE   1 
ATOM   3679 N  N    . GLU   B 1 166 ? 15.12   7.704   -5.364  1   14.552 ? 166 GLU   B N    1 
ATOM   3680 C  CA   . GLU   B 1 166 ? 15.613  6.958   -6.506  1   14.552 ? 166 GLU   B CA   1 
ATOM   3681 C  C    . GLU   B 1 166 ? 17.044  6.499   -6.236  1   15.417 ? 166 GLU   B C    1 
ATOM   3682 O  O    . GLU   B 1 166 ? 17.876  7.268   -5.751  1   16.956 ? 166 GLU   B O    1 
ATOM   3683 C  CB   . GLU   B 1 166 ? 15.549  7.844   -7.746  1   14.277 ? 166 GLU   B CB   1 
ATOM   3684 C  CG   . GLU   B 1 166 ? 15.97   7.122   -9.017  1   14.788 ? 166 GLU   B CG   1 
ATOM   3685 C  CD   . GLU   B 1 166 ? 15.642  7.947   -10.242 1   15.699 ? 166 GLU   B CD   1 
ATOM   3686 O  OE1  . GLU   B 1 166 ? 16.602  8.297   -10.959 1   18.613 ? 166 GLU   B OE1  1 
ATOM   3687 O  OE2  . GLU   B 1 166 ? 14.462  8.245   -10.496 1   15.386 ? 166 GLU   B OE2  1 
ATOM   3688 N  N    . LEU   B 1 167 ? 17.3    5.231   -6.552  1   15.46  ? 167 LEU   B N    1 
ATOM   3689 C  CA   . LEU   B 1 167 ? 18.62   4.632   -6.449  1   17.099 ? 167 LEU   B CA   1 
ATOM   3690 C  C    . LEU   B 1 167 ? 19.421  4.901   -7.721  1   18.97  ? 167 LEU   B C    1 
ATOM   3691 O  O    . LEU   B 1 167 ? 18.871  5.273   -8.757  1   18.129 ? 167 LEU   B O    1 
ATOM   3692 C  CB   . LEU   B 1 167 ? 18.453  3.135   -6.199  1   17.604 ? 167 LEU   B CB   1 
ATOM   3693 C  CG   . LEU   B 1 167 ? 17.87   2.755   -4.838  1   19.124 ? 167 LEU   B CG   1 
ATOM   3694 C  CD1  . LEU   B 1 167 ? 17.456  1.3     -4.817  1   20.201 ? 167 LEU   B CD1  1 
ATOM   3695 C  CD2  . LEU   B 1 167 ? 18.856  3.038   -3.723  1   21.314 ? 167 LEU   B CD2  1 
ATOM   3696 N  N    . PRO   B 1 168 ? 20.76   4.738   -7.68   1   20.959 ? 168 PRO   B N    1 
ATOM   3697 C  CA   . PRO   B 1 168 ? 21.597  5.022   -8.845  1   22.231 ? 168 PRO   B CA   1 
ATOM   3698 C  C    . PRO   B 1 168 ? 21.246  4.351   -10.172 1   22.573 ? 168 PRO   B C    1 
ATOM   3699 O  O    . PRO   B 1 168 ? 21.586  4.89    -11.225 1   25.633 ? 168 PRO   B O    1 
ATOM   3700 C  CB   . PRO   B 1 168 ? 22.99   4.576   -8.344  1   23.393 ? 168 PRO   B CB   1 
ATOM   3701 C  CG   . PRO   B 1 168 ? 22.951  4.843   -6.864  1   23.929 ? 168 PRO   B CG   1 
ATOM   3702 C  CD   . PRO   B 1 168 ? 21.552  4.411   -6.482  1   22.67  ? 168 PRO   B CD   1 
ATOM   3703 N  N    . THR   B 1 169 ? 20.604  3.173   -10.129 1   21.862 ? 169 THR   B N    1 
ATOM   3704 C  CA   . THR   B 1 169 ? 20.23   2.461   -11.344 1   21.99  ? 169 THR   B CA   1 
ATOM   3705 C  C    . THR   B 1 169 ? 18.898  2.967   -11.909 1   20.123 ? 169 THR   B C    1 
ATOM   3706 O  O    . THR   B 1 169 ? 18.42   2.442   -12.915 1   22.807 ? 169 THR   B O    1 
ATOM   3707 C  CB   . THR   B 1 169 ? 20.166  0.956   -11.084 1   24.359 ? 169 THR   B CB   1 
ATOM   3708 O  OG1  . THR   B 1 169 ? 19.331  0.744   -9.949  1   24.341 ? 169 THR   B OG1  1 
ATOM   3709 C  CG2  . THR   B 1 169 ? 21.54   0.352   -10.852 1   26.465 ? 169 THR   B CG2  1 
ATOM   3710 N  N    . GLY   B 1 170 ? 18.269  3.955   -11.262 1   17.453 ? 170 GLY   B N    1 
ATOM   3711 C  CA   . GLY   B 1 170 ? 17.052  4.546   -11.801 1   16.555 ? 170 GLY   B CA   1 
ATOM   3712 C  C    . GLY   B 1 170 ? 15.779  3.846   -11.338 1   16.131 ? 170 GLY   B C    1 
ATOM   3713 O  O    . GLY   B 1 170 ? 14.706  4.179   -11.821 1   19.134 ? 170 GLY   B O    1 
ATOM   3714 N  N    . VAL   B 1 171 ? 15.897  2.92    -10.394 1   14.814 ? 171 VAL   B N    1 
ATOM   3715 C  CA   . VAL   B 1 171 ? 14.737  2.314   -9.758  1   14.591 ? 171 VAL   B CA   1 
ATOM   3716 C  C    . VAL   B 1 171 ? 14.49   2.994   -8.41   1   13.417 ? 171 VAL   B C    1 
ATOM   3717 O  O    . VAL   B 1 171 ? 15.27   3.826   -7.953  1   14.476 ? 171 VAL   B O    1 
ATOM   3718 C  CB   . VAL   B 1 171 ? 14.897  0.793   -9.622  1   15.186 ? 171 VAL   B CB   1 
ATOM   3719 C  CG1  . VAL   B 1 171 ? 15.135  0.143   -10.984 1   16.467 ? 171 VAL   B CG1  1 
ATOM   3720 C  CG2  . VAL   B 1 171 ? 16.002  0.421   -8.642  1   15.247 ? 171 VAL   B CG2  1 
ATOM   3721 N  N    . HIS   B 1 172 ? 13.366  2.636   -7.79   1   13.123 ? 172 HIS   B N    1 
ATOM   3722 C  CA   . HIS   B 1 172 ? 12.775  3.437   -6.733  1   13.09  ? 172 HIS   B CA   1 
ATOM   3723 C  C    . HIS   B 1 172 ? 12.629  2.64    -5.445  1   13.155 ? 172 HIS   B C    1 
ATOM   3724 O  O    . HIS   B 1 172 ? 12.375  1.437   -5.474  1   14.262 ? 172 HIS   B O    1 
ATOM   3725 C  CB   . HIS   B 1 172 ? 11.444  4.004   -7.233  1   13.378 ? 172 HIS   B CB   1 
ATOM   3726 C  CG   . HIS   B 1 172 ? 11.689  4.84    -8.422  1   13.96  ? 172 HIS   B CG   1 
ATOM   3727 N  ND1  . HIS   B 1 172 ? 11.295  4.509   -9.696  1   13.834 ? 172 HIS   B ND1  1 
ATOM   3728 C  CD2  . HIS   B 1 172 ? 12.386  5.984   -8.523  1   14.558 ? 172 HIS   B CD2  1 
ATOM   3729 C  CE1  . HIS   B 1 172 ? 11.728  5.449   -10.524 1   14.361 ? 172 HIS   B CE1  1 
ATOM   3730 N  NE2  . HIS   B 1 172 ? 12.385  6.36    -9.835  1   14.652 ? 172 HIS   B NE2  1 
ATOM   3731 N  N    . ALA   B 1 173 ? 12.771  3.357   -4.321  1   13.166 ? 173 ALA   B N    1 
ATOM   3732 C  CA   . ALA   B 1 173 ? 12.675  2.746   -3.009  1   13.233 ? 173 ALA   B CA   1 
ATOM   3733 C  C    . ALA   B 1 173 ? 11.799  3.594   -2.1    1   12.702 ? 173 ALA   B C    1 
ATOM   3734 O  O    . ALA   B 1 173 ? 11.747  4.822   -2.197  1   12.62  ? 173 ALA   B O    1 
ATOM   3735 C  CB   . ALA   B 1 173 ? 14.048  2.575   -2.407  1   13.94  ? 173 ALA   B CB   1 
ATOM   3736 N  N    . GLY   B 1 174 ? 11.144  2.901   -1.175  1   11.878 ? 174 GLY   B N    1 
ATOM   3737 C  CA   . GLY   B 1 174 ? 10.261  3.568   -0.243  1   11.918 ? 174 GLY   B CA   1 
ATOM   3738 C  C    . GLY   B 1 174 ? 9.833   2.641   0.882   1   11.558 ? 174 GLY   B C    1 
ATOM   3739 O  O    . GLY   B 1 174 ? 10.399  1.565   1.075   1   12.381 ? 174 GLY   B O    1 
ATOM   3740 N  N    . THR   B 1 175 ? 8.822   3.102   1.627   1   11.507 ? 175 THR   B N    1 
ATOM   3741 C  CA   . THR   B 1 175 ? 8.397   2.46    2.857   1   11.847 ? 175 THR   B CA   1 
ATOM   3742 C  C    . THR   B 1 175 ? 6.943   2.029   2.749   1   11.419 ? 175 THR   B C    1 
ATOM   3743 O  O    . THR   B 1 175 ? 6.207   2.479   1.875   1   12.209 ? 175 THR   B O    1 
ATOM   3744 C  CB   . THR   B 1 175 ? 8.566   3.409   4.05    1   11.961 ? 175 THR   B CB   1 
ATOM   3745 O  OG1  . THR   B 1 175 ? 7.694   4.533   3.912   1   12.311 ? 175 THR   B OG1  1 
ATOM   3746 C  CG2  . THR   B 1 175 ? 9.993   3.896   4.214   1   12.895 ? 175 THR   B CG2  1 
ATOM   3747 N  N    . ASP   B 1 176 ? 6.527   1.207   3.712   1   11.322 ? 176 ASP   B N    1 
ATOM   3748 C  CA   . ASP   B 1 176 ? 5.11    1.093   4.025   1   12.022 ? 176 ASP   B CA   1 
ATOM   3749 C  C    . ASP   B 1 176 ? 4.659   2.369   4.742   1   12.349 ? 176 ASP   B C    1 
ATOM   3750 O  O    . ASP   B 1 176 ? 5.445   3.289   4.989   1   12.871 ? 176 ASP   B O    1 
ATOM   3751 C  CB   . ASP   B 1 176 ? 4.841   -0.223  4.735   1   13.007 ? 176 ASP   B CB   1 
ATOM   3752 C  CG   . ASP   B 1 176 ? 5.42    -0.354  6.13    1   13.837 ? 176 ASP   B CG   1 
ATOM   3753 O  OD1  . ASP   B 1 176 ? 5.655   0.703   6.762   1   14.392 ? 176 ASP   B OD1  1 
ATOM   3754 O  OD2  . ASP   B 1 176 ? 5.652   -1.516  6.545   1   15.32  ? 176 ASP   B OD2  1 
ATOM   3755 N  N    . LEU   B 1 177 ? 3.363   2.456   5.054   1   12.494 ? 177 LEU   B N    1 
ATOM   3756 C  CA   . LEU   B 1 177 ? 2.827   3.671   5.647   1   13.435 ? 177 LEU   B CA   1 
ATOM   3757 C  C    . LEU   B 1 177 ? 3.114   3.755   7.144   1   14.181 ? 177 LEU   B C    1 
ATOM   3758 O  O    . LEU   B 1 177 ? 2.844   4.794   7.749   1   16.056 ? 177 LEU   B O    1 
ATOM   3759 C  CB   . LEU   B 1 177 ? 1.34    3.846   5.335   1   13.609 ? 177 LEU   B CB   1 
ATOM   3760 C  CG   . LEU   B 1 177 ? 1.023   4.655   4.073   1   14.676 ? 177 LEU   B CG   1 
ATOM   3761 C  CD1  . LEU   B 1 177 ? 1.438   6.109   4.218   1   16.34  ? 177 LEU   B CD1  1 
ATOM   3762 C  CD2  . LEU   B 1 177 ? 1.675   4.034   2.858   1   15.475 ? 177 LEU   B CD2  1 
ATOM   3763 N  N    . GLU   B 1 178 ? 3.715   2.698   7.71    1   14.209 ? 178 GLU   B N    1 
ATOM   3764 C  CA   . GLU   B 1 178 ? 4.261   2.757   9.057   1   15.875 ? 178 GLU   B CA   1 
ATOM   3765 C  C    . GLU   B 1 178 ? 5.748   3.114   9.043   1   15.538 ? 178 GLU   B C    1 
ATOM   3766 O  O    . GLU   B 1 178 ? 6.4     3.086   10.084  1   17.262 ? 178 GLU   B O    1 
ATOM   3767 C  CB   . GLU   B 1 178 ? 4.032   1.424   9.763   1   18.232 ? 178 GLU   B CB   1 
ATOM   3768 C  CG   . GLU   B 1 178 ? 2.572   1.18    10.126  1   21.644 ? 178 GLU   B CG   1 
ATOM   3769 C  CD   . GLU   B 1 178 ? 2.364   -0.087  10.942  1   26.363 ? 178 GLU   B CD   1 
ATOM   3770 O  OE1  . GLU   B 1 178 ? 3.203   -1.015  10.881  1   30.082 ? 178 GLU   B OE1  1 
ATOM   3771 O  OE2  . GLU   B 1 178 ? 1.371   -0.115  11.687  1   31.739 ? 178 GLU   B OE2  1 
ATOM   3772 N  N    . GLY   B 1 179 ? 6.291   3.438   7.866   1   14.918 ? 179 GLY   B N    1 
ATOM   3773 C  CA   . GLY   B 1 179 ? 7.64    3.971   7.749   1   14.941 ? 179 GLY   B CA   1 
ATOM   3774 C  C    . GLY   B 1 179 ? 8.742   2.915   7.739   1   14.13  ? 179 GLY   B C    1 
ATOM   3775 O  O    . GLY   B 1 179 ? 9.905   3.267   7.944   1   14.787 ? 179 GLY   B O    1 
ATOM   3776 N  N    . ASN   B 1 180 ? 8.389   1.643   7.501   1   13.325 ? 180 ASN   B N    1 
ATOM   3777 C  CA   . ASN   B 1 180 ? 9.379   0.585   7.375   1   13.781 ? 180 ASN   B CA   1 
ATOM   3778 C  C    . ASN   B 1 180 ? 9.771   0.432   5.908   1   13.252 ? 180 ASN   B C    1 
ATOM   3779 O  O    . ASN   B 1 180 ? 8.906   0.171   5.071   1   12.994 ? 180 ASN   B O    1 
ATOM   3780 C  CB   . ASN   B 1 180 ? 8.844   -0.748  7.878   1   14.827 ? 180 ASN   B CB   1 
ATOM   3781 C  CG   . ASN   B 1 180 ? 8.352   -0.684  9.3     1   17.339 ? 180 ASN   B CG   1 
ATOM   3782 O  OD1  . ASN   B 1 180 ? 9.154   -0.6    10.226  1   20.01  ? 180 ASN   B OD1  1 
ATOM   3783 N  ND2  . ASN   B 1 180 ? 7.044   -0.75   9.496   1   18.667 ? 180 ASN   B ND2  1 
ATOM   3784 N  N    . PHE   B 1 181 ? 11.062  0.607   5.592   1   13.595 ? 181 PHE   B N    1 
ATOM   3785 C  CA   . PHE   B 1 181 ? 11.535  0.423   4.229   1   13.406 ? 181 PHE   B CA   1 
ATOM   3786 C  C    . PHE   B 1 181 ? 11.207  -0.978  3.723   1   13.163 ? 181 PHE   B C    1 
ATOM   3787 O  O    . PHE   B 1 181 ? 11.279  -1.966  4.451   1   13.682 ? 181 PHE   B O    1 
ATOM   3788 C  CB   . PHE   B 1 181 ? 13.039  0.67    4.071   1   14.108 ? 181 PHE   B CB   1 
ATOM   3789 C  CG   . PHE   B 1 181 ? 13.337  2.09    3.625   1   14.311 ? 181 PHE   B CG   1 
ATOM   3790 C  CD1  . PHE   B 1 181 ? 13.312  2.425   2.272   1   14.763 ? 181 PHE   B CD1  1 
ATOM   3791 C  CD2  . PHE   B 1 181 ? 13.559  3.104   4.549   1   14.602 ? 181 PHE   B CD2  1 
ATOM   3792 C  CE1  . PHE   B 1 181 ? 13.523  3.73    1.861   1   14.993 ? 181 PHE   B CE1  1 
ATOM   3793 C  CE2  . PHE   B 1 181 ? 13.786  4.406   4.132   1   15.456 ? 181 PHE   B CE2  1 
ATOM   3794 C  CZ   . PHE   B 1 181 ? 13.768  4.72    2.794   1   15.452 ? 181 PHE   B CZ   1 
ATOM   3795 N  N    . TYR   B 1 182 ? 10.849  -1.029  2.437   1   12.653 ? 182 TYR   B N    1 
ATOM   3796 C  CA   . TYR   B 1 182 ? 10.97   -2.238  1.653   1   12.897 ? 182 TYR   B CA   1 
ATOM   3797 C  C    . TYR   B 1 182 ? 12.427  -2.333  1.224   1   13.251 ? 182 TYR   B C    1 
ATOM   3798 O  O    . TYR   B 1 182 ? 12.965  -1.406  0.622   1   14.403 ? 182 TYR   B O    1 
ATOM   3799 C  CB   . TYR   B 1 182 ? 10.042  -2.193  0.44    1   12.848 ? 182 TYR   B CB   1 
ATOM   3800 C  CG   . TYR   B 1 182 ? 8.57    -2.228  0.793   1   12.461 ? 182 TYR   B CG   1 
ATOM   3801 C  CD1  . TYR   B 1 182 ? 7.95    -3.425  1.119   1   12.708 ? 182 TYR   B CD1  1 
ATOM   3802 C  CD2  . TYR   B 1 182 ? 7.808   -1.071  0.785   1   12.043 ? 182 TYR   B CD2  1 
ATOM   3803 C  CE1  . TYR   B 1 182 ? 6.598   -3.471  1.423   1   12.933 ? 182 TYR   B CE1  1 
ATOM   3804 C  CE2  . TYR   B 1 182 ? 6.451   -1.1    1.091   1   12.636 ? 182 TYR   B CE2  1 
ATOM   3805 C  CZ   . TYR   B 1 182 ? 5.852   -2.303  1.408   1   12.42  ? 182 TYR   B CZ   1 
ATOM   3806 O  OH   . TYR   B 1 182 ? 4.522   -2.367  1.709   1   13.215 ? 182 TYR   B OH   1 
ATOM   3807 N  N    . GLY   B 1 183 ? 13.063  -3.449  1.551   1   13.337 ? 183 GLY   B N    1 
ATOM   3808 C  CA   . GLY   B 1 183 ? 14.419  -3.688  1.105   1   14.133 ? 183 GLY   B CA   1 
ATOM   3809 C  C    . GLY   B 1 183 ? 15.454  -3.091  2.052   1   14.911 ? 183 GLY   B C    1 
ATOM   3810 O  O    . GLY   B 1 183 ? 15.151  -2.339  2.983   1   15.032 ? 183 GLY   B O    1 
ATOM   3811 N  N    . PRO   B 1 184 ? 16.734  -3.441  1.802   1   15.23  ? 184 PRO   B N    1 
ATOM   3812 C  CA   . PRO   B 1 184 ? 17.844  -3.079  2.687   1   15.878 ? 184 PRO   B CA   1 
ATOM   3813 C  C    . PRO   B 1 184 ? 18.371  -1.666  2.463   1   16.329 ? 184 PRO   B C    1 
ATOM   3814 O  O    . PRO   B 1 184 ? 19.56   -1.46   2.216   1   19.837 ? 184 PRO   B O    1 
ATOM   3815 C  CB   . PRO   B 1 184 ? 18.867  -4.162  2.319   1   16.903 ? 184 PRO   B CB   1 
ATOM   3816 C  CG   . PRO   B 1 184 ? 18.659  -4.38   0.841   1   16.936 ? 184 PRO   B CG   1 
ATOM   3817 C  CD   . PRO   B 1 184 ? 17.163  -4.294  0.679   1   16.16  ? 184 PRO   B CD   1 
ATOM   3818 N  N    . PHE   B 1 185 ? 17.456  -0.701  2.53    1   15.017 ? 185 PHE   B N    1 
ATOM   3819 C  CA   . PHE   B 1 185 ? 17.752  0.686   2.22    1   15.088 ? 185 PHE   B CA   1 
ATOM   3820 C  C    . PHE   B 1 185 ? 17.521  1.545   3.456   1   15.17  ? 185 PHE   B C    1 
ATOM   3821 O  O    . PHE   B 1 185 ? 16.749  1.177   4.347   1   16.823 ? 185 PHE   B O    1 
ATOM   3822 C  CB   . PHE   B 1 185 ? 16.893  1.192   1.055   1   15.496 ? 185 PHE   B CB   1 
ATOM   3823 C  CG   . PHE   B 1 185 ? 16.997  0.261   -0.136  1   15.77  ? 185 PHE   B CG   1 
ATOM   3824 C  CD1  . PHE   B 1 185 ? 18.211  0.085   -0.782  1   15.901 ? 185 PHE   B CD1  1 
ATOM   3825 C  CD2  . PHE   B 1 185 ? 15.906  -0.47   -0.583  1   16.2   ? 185 PHE   B CD2  1 
ATOM   3826 C  CE1  . PHE   B 1 185 ? 18.321  -0.799  -1.84   1   16.25  ? 185 PHE   B CE1  1 
ATOM   3827 C  CE2  . PHE   B 1 185 ? 16.021  -1.334  -1.657  1   16.864 ? 185 PHE   B CE2  1 
ATOM   3828 C  CZ   . PHE   B 1 185 ? 17.228  -1.505  -2.27   1   16.691 ? 185 PHE   B CZ   1 
ATOM   3829 N  N    . VAL   B 1 186 ? 18.195  2.697   3.464   1   14.624 ? 186 VAL   B N    1 
ATOM   3830 C  CA   . VAL   B 1 186 ? 18.072  3.677   4.527   1   15.305 ? 186 VAL   B CA   1 
ATOM   3831 C  C    . VAL   B 1 186 ? 17.824  5.058   3.929   1   15.207 ? 186 VAL   B C    1 
ATOM   3832 O  O    . VAL   B 1 186 ? 18.215  5.334   2.794   1   15.689 ? 186 VAL   B O    1 
ATOM   3833 C  CB   . VAL   B 1 186 ? 19.317  3.684   5.433   1   16.505 ? 186 VAL   B CB   1 
ATOM   3834 C  CG1  . VAL   B 1 186 ? 19.461  2.361   6.171   1   17.796 ? 186 VAL   B CG1  1 
ATOM   3835 C  CG2  . VAL   B 1 186 ? 20.588  4.008   4.653   1   16.822 ? 186 VAL   B CG2  1 
ATOM   3836 N  N    . ASP   B 1 187 ? 17.179  5.927   4.717   1   15.431 ? 187 ASP   B N    1 
ATOM   3837 C  CA   . ASP   B 1 187 ? 16.913  7.295   4.293   1   15.527 ? 187 ASP   B CA   1 
ATOM   3838 C  C    . ASP   B 1 187 ? 18.114  8.174   4.634   1   15.84  ? 187 ASP   B C    1 
ATOM   3839 O  O    . ASP   B 1 187 ? 18.059  9.053   5.495   1   16.136 ? 187 ASP   B O    1 
ATOM   3840 C  CB   . ASP   B 1 187 ? 15.574  7.805   4.798   1   15.436 ? 187 ASP   B CB   1 
ATOM   3841 C  CG   . ASP   B 1 187 ? 15.265  7.666   6.28    1   15.738 ? 187 ASP   B CG   1 
ATOM   3842 O  OD1  . ASP   B 1 187 ? 16.07   7.05    7.011   1   16.228 ? 187 ASP   B OD1  1 
ATOM   3843 O  OD2  . ASP   B 1 187 ? 14.195  8.153   6.686   1   15.441 ? 187 ASP   B OD2  1 
ATOM   3844 N  N    . ARG   B 1 188 ? 19.193  7.931   3.883   1   16.857 ? 188 ARG   B N    1 
ATOM   3845 C  CA   . ARG   B 1 188 ? 20.425  8.701   3.943   1   18.613 ? 188 ARG   B CA   1 
ATOM   3846 C  C    . ARG   B 1 188 ? 21.011  8.747   2.54    1   19.232 ? 188 ARG   B C    1 
ATOM   3847 O  O    . ARG   B 1 188 ? 20.966  7.733   1.841   1   19.647 ? 188 ARG   B O    1 
ATOM   3848 C  CB   . ARG   B 1 188 ? 21.416  8.003   4.879   1   20.585 ? 188 ARG   B CB   1 
ATOM   3849 C  CG   . ARG   B 1 188 ? 22.754  8.705   5.051   1   22.335 ? 188 ARG   B CG   1 
ATOM   3850 C  CD   . ARG   B 1 188 ? 23.641  7.903   6.008   1   25.22  ? 188 ARG   B CD   1 
ATOM   3851 N  NE   . ARG   B 1 188 ? 25.025  8.382   5.994   1   28.754 ? 188 ARG   B NE   1 
ATOM   3852 C  CZ   . ARG   B 1 188 ? 26.07   7.637   6.328   1   32.386 ? 188 ARG   B CZ   1 
ATOM   3853 N  NH1  . ARG   B 1 188 ? 27.28   8.167   6.352   1   35.49  ? 188 ARG   B NH1  1 
ATOM   3854 N  NH2  . ARG   B 1 188 ? 25.893  6.362   6.642   1   35.316 ? 188 ARG   B NH2  1 
ATOM   3855 N  N    . GLN   B 1 189 ? 21.572  9.904   2.162   1   20.408 ? 189 GLN   B N    1 
ATOM   3856 C  CA   . GLN   B 1 189 ? 22.317  10.033  0.92    1   21.866 ? 189 GLN   B CA   1 
ATOM   3857 C  C    . GLN   B 1 189 ? 23.711  9.441   1.142   1   23.048 ? 189 GLN   B C    1 
ATOM   3858 O  O    . GLN   B 1 189 ? 24.609  10.125  1.612   1   25.402 ? 189 GLN   B O    1 
ATOM   3859 C  CB   . GLN   B 1 189 ? 22.33   11.502  0.5     1   23.24  ? 189 GLN   B CB   1 
ATOM   3860 C  CG   . GLN   B 1 189 ? 23.161  11.799  -0.744  1   25.718 ? 189 GLN   B CG   1 
ATOM   3861 C  CD   . GLN   B 1 189 ? 22.602  11.171  -2.002  1   28.897 ? 189 GLN   B CD   1 
ATOM   3862 O  OE1  . GLN   B 1 189 ? 21.86   11.804  -2.763  1   33.441 ? 189 GLN   B OE1  1 
ATOM   3863 N  NE2  . GLN   B 1 189 ? 22.946  9.912   -2.228  1   29.9   ? 189 GLN   B NE2  1 
ATOM   3864 N  N    . THR   B 1 190 ? 23.801  8.128   0.907   1   24.977 ? 190 THR   B N    1 
ATOM   3865 C  CA   . THR   B 1 190 ? 25.016  7.336   0.972   1   26.02  ? 190 THR   B CA   1 
ATOM   3866 C  C    . THR   B 1 190 ? 24.916  6.304   -0.15   1   26.105 ? 190 THR   B C    1 
ATOM   3867 O  O    . THR   B 1 190 ? 23.823  6.086   -0.681  1   26.302 ? 190 THR   B O    1 
ATOM   3868 C  CB   . THR   B 1 190 ? 25.132  6.683   2.354   1   27.101 ? 190 THR   B CB   1 
ATOM   3869 O  OG1  . THR   B 1 190 ? 26.458  6.183   2.489   1   29.929 ? 190 THR   B OG1  1 
ATOM   3870 C  CG2  . THR   B 1 190 ? 24.156  5.538   2.566   1   29.032 ? 190 THR   B CG2  1 
ATOM   3871 N  N    . ALA   B 1 191 ? 26.041  5.669   -0.497  1   26.451 ? 191 ALA   B N    1 
ATOM   3872 C  CA   . ALA   B 1 191 ? 26.041  4.681   -1.562  1   25.717 ? 191 ALA   B CA   1 
ATOM   3873 C  C    . ALA   B 1 191 ? 25.111  3.529   -1.196  1   23.134 ? 191 ALA   B C    1 
ATOM   3874 O  O    . ALA   B 1 191 ? 25.256  2.91    -0.146  1   24.625 ? 191 ALA   B O    1 
ATOM   3875 C  CB   . ALA   B 1 191 ? 27.44   4.183   -1.831  1   27.039 ? 191 ALA   B CB   1 
ATOM   3876 N  N    . GLN   B 1 192 ? 24.122  3.291   -2.056  1   21.318 ? 192 GLN   B N    1 
ATOM   3877 C  CA   . GLN   B 1 192 ? 23.187  2.191   -1.887  1   19.444 ? 192 GLN   B CA   1 
ATOM   3878 C  C    . GLN   B 1 192 ? 22.924  1.614   -3.265  1   20.623 ? 192 GLN   B C    1 
ATOM   3879 O  O    . GLN   B 1 192 ? 23.068  2.328   -4.254  1   23.76  ? 192 GLN   B O    1 
ATOM   3880 C  CB   . GLN   B 1 192 ? 21.873  2.639   -1.251  1   18.658 ? 192 GLN   B CB   1 
ATOM   3881 C  CG   . GLN   B 1 192 ? 22.08   3.371   0.063   1   18.044 ? 192 GLN   B CG   1 
ATOM   3882 C  CD   . GLN   B 1 192 ? 20.78   3.605   0.788   1   16.979 ? 192 GLN   B CD   1 
ATOM   3883 O  OE1  . GLN   B 1 192 ? 20.127  2.649   1.225   1   17.136 ? 192 GLN   B OE1  1 
ATOM   3884 N  NE2  . GLN   B 1 192 ? 20.41   4.869   0.941   1   17.706 ? 192 GLN   B NE2  1 
ATOM   3885 N  N    . ALA   B 1 193 ? 22.634  0.318   -3.32   1   20.417 ? 193 ALA   B N    1 
ATOM   3886 C  CA   . ALA   B 1 193 ? 22.413  -0.346  -4.593  1   22.852 ? 193 ALA   B CA   1 
ATOM   3887 C  C    . ALA   B 1 193 ? 21.384  -1.443  -4.405  1   25.698 ? 193 ALA   B C    1 
ATOM   3888 O  O    . ALA   B 1 193 ? 21.408  -2.149  -3.402  1   27.151 ? 193 ALA   B O    1 
ATOM   3889 C  CB   . ALA   B 1 193 ? 23.714  -0.907  -5.135  1   23.218 ? 193 ALA   B CB   1 
ATOM   3890 N  N    . ALA   B 1 194 ? 20.507  -1.579  -5.398  1   28.674 ? 194 ALA   B N    1 
ATOM   3891 C  CA   . ALA   B 1 194 ? 19.593  -2.704  -5.455  1   30.237 ? 194 ALA   B CA   1 
ATOM   3892 C  C    . ALA   B 1 194 ? 20.396  -3.979  -5.682  1   27.02  ? 194 ALA   B C    1 
ATOM   3893 O  O    . ALA   B 1 194 ? 21.384  -3.959  -6.41   1   27.706 ? 194 ALA   B O    1 
ATOM   3894 C  CB   . ALA   B 1 194 ? 18.59   -2.493  -6.559  1   32.863 ? 194 ALA   B CB   1 
ATOM   3895 N  N    . GLY   B 1 195 ? 19.981  -5.072  -5.032  1   25.165 ? 195 GLY   B N    1 
ATOM   3896 C  CA   . GLY   B 1 195 ? 20.531  -6.376  -5.345  1   23.273 ? 195 GLY   B CA   1 
ATOM   3897 C  C    . GLY   B 1 195 ? 20.09   -6.805  -6.739  1   21.475 ? 195 GLY   B C    1 
ATOM   3898 O  O    . GLY   B 1 195 ? 19.178  -6.224  -7.326  1   21.613 ? 195 GLY   B O    1 
ATOM   3899 N  N    A THR   B 1 196 ? 20.749  -7.837  -7.265  0.5 21.696 ? 196 THR   B N    1 
ATOM   3900 N  N    B THR   B 1 196 ? 20.741  -7.842  -7.268  0.5 20.862 ? 196 THR   B N    1 
ATOM   3901 C  CA   A THR   B 1 196 ? 20.368  -8.415  -8.542  0.5 22.172 ? 196 THR   B CA   1 
ATOM   3902 C  CA   B THR   B 1 196 ? 20.366  -8.358  -8.573  0.5 20.84  ? 196 THR   B CA   1 
ATOM   3903 C  C    A THR   B 1 196 ? 18.908  -8.849  -8.462  0.5 21.673 ? 196 THR   B C    1 
ATOM   3904 C  C    B THR   B 1 196 ? 18.937  -8.88   -8.502  0.5 20.933 ? 196 THR   B C    1 
ATOM   3905 O  O    A THR   B 1 196 ? 18.499  -9.527  -7.525  0.5 23.902 ? 196 THR   B O    1 
ATOM   3906 O  O    B THR   B 1 196 ? 18.594  -9.669  -7.627  0.5 23.886 ? 196 THR   B O    1 
ATOM   3907 C  CB   A THR   B 1 196 ? 21.282  -9.595  -8.866  0.5 23.974 ? 196 THR   B CB   1 
ATOM   3908 C  CB   B THR   B 1 196 ? 21.319  -9.459  -9.021  0.5 21.501 ? 196 THR   B CB   1 
ATOM   3909 O  OG1  A THR   B 1 196 ? 21.129  -10.482 -7.763  0.5 26.355 ? 196 THR   B OG1  1 
ATOM   3910 O  OG1  B THR   B 1 196 ? 22.614  -8.874  -8.94   0.5 22.294 ? 196 THR   B OG1  1 
ATOM   3911 C  CG2  A THR   B 1 196 ? 22.739  -9.195  -8.998  0.5 24.362 ? 196 THR   B CG2  1 
ATOM   3912 C  CG2  B THR   B 1 196 ? 20.988  -9.932  -10.424 0.5 21.465 ? 196 THR   B CG2  1 
ATOM   3913 N  N    . ASP   B 1 197 ? 18.104  -8.421  -9.43   1   20.236 ? 197 ASP   B N    1 
ATOM   3914 C  CA   . ASP   B 1 197 ? 16.704  -8.771  -9.409  1   19.067 ? 197 ASP   B CA   1 
ATOM   3915 C  C    . ASP   B 1 197 ? 16.487  -10.132 -10.068 1   19.428 ? 197 ASP   B C    1 
ATOM   3916 O  O    . ASP   B 1 197 ? 17.36   -10.659 -10.768 1   21.506 ? 197 ASP   B O    1 
ATOM   3917 C  CB   . ASP   B 1 197 ? 15.885  -7.683  -10.062 1   18.589 ? 197 ASP   B CB   1 
ATOM   3918 C  CG   . ASP   B 1 197 ? 14.439  -7.648  -9.607  1   18.065 ? 197 ASP   B CG   1 
ATOM   3919 O  OD1  . ASP   B 1 197 ? 14.139  -8.174  -8.509  1   17.152 ? 197 ASP   B OD1  1 
ATOM   3920 O  OD2  . ASP   B 1 197 ? 13.64   -7.115  -10.368 1   19.231 ? 197 ASP   B OD2  1 
ATOM   3921 N  N    . THR   B 1 198 ? 15.3    -10.688 -9.807  1   17.404 ? 198 THR   B N    1 
ATOM   3922 C  CA   . THR   B 1 198 ? 14.867  -11.938 -10.406 1   17.097 ? 198 THR   B CA   1 
ATOM   3923 C  C    . THR   B 1 198 ? 13.458  -11.749 -10.962 1   15.776 ? 198 THR   B C    1 
ATOM   3924 O  O    . THR   B 1 198 ? 12.798  -10.759 -10.675 1   16.158 ? 198 THR   B O    1 
ATOM   3925 C  CB   . THR   B 1 198 ? 14.919  -13.065 -9.379  1   19.331 ? 198 THR   B CB   1 
ATOM   3926 O  OG1  . THR   B 1 198 ? 14.179  -12.604 -8.259  1   20.733 ? 198 THR   B OG1  1 
ATOM   3927 C  CG2  . THR   B 1 198 ? 16.329  -13.401 -8.934  1   20.81  ? 198 THR   B CG2  1 
ATOM   3928 N  N    . THR   B 1 199 ? 13.023  -12.717 -11.771 1   14.993 ? 199 THR   B N    1 
ATOM   3929 C  CA   . THR   B 1 199 ? 11.72   -12.649 -12.416 1   14.63  ? 199 THR   B CA   1 
ATOM   3930 C  C    . THR   B 1 199 ? 10.682  -13.359 -11.54  1   14.328 ? 199 THR   B C    1 
ATOM   3931 O  O    . THR   B 1 199 ? 10.953  -14.402 -10.949 1   14.989 ? 199 THR   B O    1 
ATOM   3932 C  CB   . THR   B 1 199 ? 11.809  -13.258 -13.814 1   15.418 ? 199 THR   B CB   1 
ATOM   3933 O  OG1  . THR   B 1 199 ? 12.753  -12.478 -14.55  1   16.623 ? 199 THR   B OG1  1 
ATOM   3934 C  CG2  . THR   B 1 199 ? 10.469  -13.241 -14.527 1   16.005 ? 199 THR   B CG2  1 
ATOM   3935 N  N    . ILE   B 1 200 ? 9.479   -12.774 -11.466 1   14.013 ? 200 ILE   B N    1 
ATOM   3936 C  CA   . ILE   B 1 200 ? 8.429   -13.278 -10.592 1   13.413 ? 200 ILE   B CA   1 
ATOM   3937 C  C    . ILE   B 1 200 ? 7.647   -14.382 -11.312 1   13.366 ? 200 ILE   B C    1 
ATOM   3938 O  O    . ILE   B 1 200 ? 6.704   -14.115 -12.051 1   13.224 ? 200 ILE   B O    1 
ATOM   3939 C  CB   . ILE   B 1 200 ? 7.506   -12.131 -10.131 1   13.547 ? 200 ILE   B CB   1 
ATOM   3940 C  CG1  . ILE   B 1 200 ? 8.28    -10.955 -9.527  1   14.03  ? 200 ILE   B CG1  1 
ATOM   3941 C  CG2  . ILE   B 1 200 ? 6.458   -12.664 -9.159  1   13.992 ? 200 ILE   B CG2  1 
ATOM   3942 C  CD1  . ILE   B 1 200 ? 7.559   -9.626  -9.646  1   13.846 ? 200 ILE   B CD1  1 
ATOM   3943 N  N    . THR   B 1 201 ? 8.029   -15.634 -11.069 1   13.805 ? 201 THR   B N    1 
ATOM   3944 C  CA   . THR   B 1 201 ? 7.546   -16.781 -11.833 1   13.977 ? 201 THR   B CA   1 
ATOM   3945 C  C    . THR   B 1 201 ? 6.02    -16.905 -11.794 1   14.078 ? 201 THR   B C    1 
ATOM   3946 O  O    . THR   B 1 201 ? 5.385   -17.136 -12.823 1   13.824 ? 201 THR   B O    1 
ATOM   3947 C  CB   . THR   B 1 201 ? 8.191   -18.048 -11.278 1   14.475 ? 201 THR   B CB   1 
ATOM   3948 O  OG1  . THR   B 1 201 ? 9.593   -17.789 -11.258 1   15.346 ? 201 THR   B OG1  1 
ATOM   3949 C  CG2  . THR   B 1 201 ? 7.89    -19.269 -12.121 1   15.363 ? 201 THR   B CG2  1 
ATOM   3950 N  N    . VAL   B 1 202 ? 5.426   -16.824 -10.599 1   13.93  ? 202 VAL   B N    1 
ATOM   3951 C  CA   . VAL   B 1 202 ? 3.989   -17.027 -10.487 1   14.039 ? 202 VAL   B CA   1 
ATOM   3952 C  C    . VAL   B 1 202 ? 3.24    -15.994 -11.337 1   13.862 ? 202 VAL   B C    1 
ATOM   3953 O  O    . VAL   B 1 202 ? 2.179   -16.297 -11.894 1   13.992 ? 202 VAL   B O    1 
ATOM   3954 C  CB   . VAL   B 1 202 ? 3.526   -17.014 -9.017  1   15.911 ? 202 VAL   B CB   1 
ATOM   3955 C  CG1  . VAL   B 1 202 ? 3.823   -15.693 -8.318  1   16.449 ? 202 VAL   B CG1  1 
ATOM   3956 C  CG2  . VAL   B 1 202 ? 2.046   -17.367 -8.899  1   16.626 ? 202 VAL   B CG2  1 
ATOM   3957 N  N    . ASN   B 1 203 ? 3.773   -14.776 -11.428 1   12.533 ? 203 ASN   B N    1 
ATOM   3958 C  CA   . ASN   B 1 203 ? 3.152   -13.724 -12.215 1   12.38  ? 203 ASN   B CA   1 
ATOM   3959 C  C    . ASN   B 1 203 ? 3.294   -14.001 -13.717 1   12.3   ? 203 ASN   B C    1 
ATOM   3960 O  O    . ASN   B 1 203 ? 2.369   -13.757 -14.498 1   12.593 ? 203 ASN   B O    1 
ATOM   3961 C  CB   . ASN   B 1 203 ? 3.749   -12.363 -11.883 1   12.797 ? 203 ASN   B CB   1 
ATOM   3962 C  CG   . ASN   B 1 203 ? 3.324   -11.85  -10.525 1   13.068 ? 203 ASN   B CG   1 
ATOM   3963 O  OD1  . ASN   B 1 203 ? 2.635   -12.539 -9.764  1   13.752 ? 203 ASN   B OD1  1 
ATOM   3964 N  ND2  . ASN   B 1 203 ? 3.736   -10.631 -10.211 1   13.332 ? 203 ASN   B ND2  1 
ATOM   3965 N  N    . VAL   B 1 204 ? 4.448   -14.513 -14.16  1   12.241 ? 204 VAL   B N    1 
ATOM   3966 C  CA   . VAL   B 1 204 ? 4.59    -14.888 -15.561 1   12.342 ? 204 VAL   B CA   1 
ATOM   3967 C  C    . VAL   B 1 204 ? 3.543   -15.946 -15.915 1   12.321 ? 204 VAL   B C    1 
ATOM   3968 O  O    . VAL   B 1 204 ? 2.891   -15.867 -16.959 1   12.527 ? 204 VAL   B O    1 
ATOM   3969 C  CB   . VAL   B 1 204 ? 6.005   -15.37  -15.914 1   12.626 ? 204 VAL   B CB   1 
ATOM   3970 C  CG1  . VAL   B 1 204 ? 6.076   -15.88  -17.348 1   13.58  ? 204 VAL   B CG1  1 
ATOM   3971 C  CG2  . VAL   B 1 204 ? 7.047   -14.278 -15.682 1   12.825 ? 204 VAL   B CG2  1 
ATOM   3972 N  N    . LEU   B 1 205 ? 3.375   -16.952 -15.054 1   12.758 ? 205 LEU   B N    1 
ATOM   3973 C  CA   . LEU   B 1 205 ? 2.363   -17.974 -15.293 1   13.464 ? 205 LEU   B CA   1 
ATOM   3974 C  C    . LEU   B 1 205 ? 0.97    -17.345 -15.372 1   14.042 ? 205 LEU   B C    1 
ATOM   3975 O  O    . LEU   B 1 205 ? 0.2     -17.667 -16.269 1   13.871 ? 205 LEU   B O    1 
ATOM   3976 C  CB   . LEU   B 1 205 ? 2.446   -19.052 -14.213 1   14.228 ? 205 LEU   B CB   1 
ATOM   3977 C  CG   . LEU   B 1 205 ? 3.694   -19.933 -14.281 1   14.844 ? 205 LEU   B CG   1 
ATOM   3978 C  CD1  . LEU   B 1 205 ? 3.843   -20.737 -13.014 1   15.077 ? 205 LEU   B CD1  1 
ATOM   3979 C  CD2  . LEU   B 1 205 ? 3.685   -20.864 -15.498 1   15.457 ? 205 LEU   B CD2  1 
ATOM   3980 N  N    . ALA   B 1 206 ? 0.647   -16.428 -14.457 1   13.763 ? 206 ALA   B N    1 
ATOM   3981 C  CA   . ALA   B 1 206 ? -0.646  -15.752 -14.49  1   14.381 ? 206 ALA   B CA   1 
ATOM   3982 C  C    . ALA   B 1 206 ? -0.88   -15.067 -15.837 1   13.91  ? 206 ALA   B C    1 
ATOM   3983 O  O    . ALA   B 1 206 ? -1.969  -15.133 -16.407 1   14.693 ? 206 ALA   B O    1 
ATOM   3984 C  CB   . ALA   B 1 206 ? -0.736  -14.765 -13.343 1   14.656 ? 206 ALA   B CB   1 
ATOM   3985 N  N    . TRP   B 1 207 ? 0.154   -14.395 -16.344 1   13.121 ? 207 TRP   B N    1 
ATOM   3986 C  CA   . TRP   B 1 207 ? 0.062   -13.663 -17.594 1   12.876 ? 207 TRP   B CA   1 
ATOM   3987 C  C    . TRP   B 1 207 ? -0.082  -14.616 -18.782 1   12.364 ? 207 TRP   B C    1 
ATOM   3988 O  O    . TRP   B 1 207 ? -0.803  -14.306 -19.727 1   12.95  ? 207 TRP   B O    1 
ATOM   3989 C  CB   . TRP   B 1 207 ? 1.262   -12.725 -17.698 1   13.552 ? 207 TRP   B CB   1 
ATOM   3990 C  CG   . TRP   B 1 207 ? 1.491   -12.041 -19.013 1   14.119 ? 207 TRP   B CG   1 
ATOM   3991 C  CD1  . TRP   B 1 207 ? 0.943   -10.896 -19.521 1   15.517 ? 207 TRP   B CD1  1 
ATOM   3992 C  CD2  . TRP   B 1 207 ? 2.46    -12.483 -19.975 1   15.692 ? 207 TRP   B CD2  1 
ATOM   3993 N  NE1  . TRP   B 1 207 ? 1.492   -10.618 -20.743 1   16.428 ? 207 TRP   B NE1  1 
ATOM   3994 C  CE2  . TRP   B 1 207 ? 2.436   -11.566 -21.042 1   16.633 ? 207 TRP   B CE2  1 
ATOM   3995 C  CE3  . TRP   B 1 207 ? 3.345   -13.564 -19.998 1   16.876 ? 207 TRP   B CE3  1 
ATOM   3996 C  CZ2  . TRP   B 1 207 ? 3.287   -11.712 -22.136 1   17.72  ? 207 TRP   B CZ2  1 
ATOM   3997 C  CZ3  . TRP   B 1 207 ? 4.199   -13.687 -21.064 1   18.495 ? 207 TRP   B CZ3  1 
ATOM   3998 C  CH2  . TRP   B 1 207 ? 4.166   -12.773 -22.11  1   18.401 ? 207 TRP   B CH2  1 
ATOM   3999 N  N    . LEU   B 1 208 ? 0.572   -15.781 -18.738 1   12.459 ? 208 LEU   B N    1 
ATOM   4000 C  CA   . LEU   B 1 208 ? 0.343   -16.785 -19.767 1   13.284 ? 208 LEU   B CA   1 
ATOM   4001 C  C    . LEU   B 1 208 ? -1.118  -17.23  -19.753 1   14.07  ? 208 LEU   B C    1 
ATOM   4002 O  O    . LEU   B 1 208 ? -1.709  -17.433 -20.811 1   14.402 ? 208 LEU   B O    1 
ATOM   4003 C  CB   . LEU   B 1 208 ? 1.298   -17.963 -19.592 1   13.701 ? 208 LEU   B CB   1 
ATOM   4004 C  CG   . LEU   B 1 208 ? 2.776   -17.676 -19.87  1   13.798 ? 208 LEU   B CG   1 
ATOM   4005 C  CD1  . LEU   B 1 208 ? 3.64    -18.89  -19.553 1   14.647 ? 208 LEU   B CD1  1 
ATOM   4006 C  CD2  . LEU   B 1 208 ? 3.045   -17.24  -21.288 1   14.63  ? 208 LEU   B CD2  1 
ATOM   4007 N  N    . TYR   B 1 209 ? -1.722  -17.386 -18.572 1   14.952 ? 209 TYR   B N    1 
ATOM   4008 C  CA   . TYR   B 1 209 ? -3.142  -17.698 -18.506 1   16.002 ? 209 TYR   B CA   1 
ATOM   4009 C  C    . TYR   B 1 209 ? -3.975  -16.568 -19.114 1   15.652 ? 209 TYR   B C    1 
ATOM   4010 O  O    . TYR   B 1 209 ? -4.936  -16.831 -19.837 1   16.361 ? 209 TYR   B O    1 
ATOM   4011 C  CB   . TYR   B 1 209 ? -3.583  -17.986 -17.073 1   16.799 ? 209 TYR   B CB   1 
ATOM   4012 C  CG   . TYR   B 1 209 ? -3.231  -19.382 -16.584 1   17.963 ? 209 TYR   B CG   1 
ATOM   4013 C  CD1  . TYR   B 1 209 ? -3.913  -20.494 -17.068 1   19.938 ? 209 TYR   B CD1  1 
ATOM   4014 C  CD2  . TYR   B 1 209 ? -2.243  -19.584 -15.626 1   17.87  ? 209 TYR   B CD2  1 
ATOM   4015 C  CE1  . TYR   B 1 209 ? -3.606  -21.768 -16.624 1   20.42  ? 209 TYR   B CE1  1 
ATOM   4016 C  CE2  . TYR   B 1 209 ? -1.934  -20.853 -15.169 1   19.548 ? 209 TYR   B CE2  1 
ATOM   4017 C  CZ   . TYR   B 1 209 ? -2.606  -21.947 -15.681 1   20.421 ? 209 TYR   B CZ   1 
ATOM   4018 O  OH   . TYR   B 1 209 ? -2.3    -23.201 -15.233 1   22.355 ? 209 TYR   B OH   1 
ATOM   4019 N  N    . ALA   B 1 210 ? -3.618  -15.309 -18.833 1   14.843 ? 210 ALA   B N    1 
ATOM   4020 C  CA   . ALA   B 1 210 ? -4.309  -14.168 -19.422 1   14.671 ? 210 ALA   B CA   1 
ATOM   4021 C  C    . ALA   B 1 210 ? -4.255  -14.25  -20.945 1   14.922 ? 210 ALA   B C    1 
ATOM   4022 O  O    . ALA   B 1 210 ? -5.237  -13.975 -21.634 1   15.573 ? 210 ALA   B O    1 
ATOM   4023 C  CB   . ALA   B 1 210 ? -3.708  -12.873 -18.939 1   14.52  ? 210 ALA   B CB   1 
ATOM   4024 N  N    . ALA   B 1 211 ? -3.087  -14.643 -21.464 1   14.507 ? 211 ALA   B N    1 
ATOM   4025 C  CA   . ALA   B 1 211 ? -2.891  -14.769 -22.897 1   15.04  ? 211 ALA   B CA   1 
ATOM   4026 C  C    . ALA   B 1 211 ? -3.821  -15.828 -23.464 1   15.532 ? 211 ALA   B C    1 
ATOM   4027 O  O    . ALA   B 1 211 ? -4.441  -15.596 -24.493 1   16.487 ? 211 ALA   B O    1 
ATOM   4028 C  CB   . ALA   B 1 211 ? -1.447  -15.091 -23.214 1   15.191 ? 211 ALA   B CB   1 
ATOM   4029 N  N    . VAL   B 1 212 ? -3.941  -16.972 -22.785 1   16.096 ? 212 VAL   B N    1 
ATOM   4030 C  CA   . VAL   B 1 212 ? -4.829  -18.022 -23.265 1   18.263 ? 212 VAL   B CA   1 
ATOM   4031 C  C    . VAL   B 1 212 ? -6.278  -17.527 -23.253 1   19.85  ? 212 VAL   B C    1 
ATOM   4032 O  O    . VAL   B 1 212 ? -7.027  -17.754 -24.206 1   20.727 ? 212 VAL   B O    1 
ATOM   4033 C  CB   . VAL   B 1 212 ? -4.654  -19.304 -22.428 1   19.046 ? 212 VAL   B CB   1 
ATOM   4034 C  CG1  . VAL   B 1 212 ? -5.716  -20.348 -22.727 1   20.003 ? 212 VAL   B CG1  1 
ATOM   4035 C  CG2  . VAL   B 1 212 ? -3.271  -19.908 -22.623 1   17.948 ? 212 VAL   B CG2  1 
ATOM   4036 N  N    . ILE   B 1 213 ? -6.681  -16.859 -22.168 1   19.558 ? 213 ILE   B N    1 
ATOM   4037 C  CA   . ILE   B 1 213 ? -8.043  -16.36  -22.058 1   20.876 ? 213 ILE   B CA   1 
ATOM   4038 C  C    . ILE   B 1 213 ? -8.36   -15.428 -23.231 1   20.57  ? 213 ILE   B C    1 
ATOM   4039 O  O    . ILE   B 1 213 ? -9.487  -15.399 -23.733 1   21.702 ? 213 ILE   B O    1 
ATOM   4040 C  CB   . ILE   B 1 213 ? -8.251  -15.696 -20.685 1   21.479 ? 213 ILE   B CB   1 
ATOM   4041 C  CG1  . ILE   B 1 213 ? -8.244  -16.752 -19.566 1   22.733 ? 213 ILE   B CG1  1 
ATOM   4042 C  CG2  . ILE   B 1 213 ? -9.54   -14.876 -20.661 1   22.862 ? 213 ILE   B CG2  1 
ATOM   4043 C  CD1  . ILE   B 1 213 ? -8.078  -16.195 -18.163 1   23.752 ? 213 ILE   B CD1  1 
ATOM   4044 N  N    . ASN   B 1 214 ? -7.358  -14.66  -23.668 1   19.561 ? 214 ASN   B N    1 
ATOM   4045 C  CA   . ASN   B 1 214 ? -7.503  -13.704 -24.757 1   21.105 ? 214 ASN   B CA   1 
ATOM   4046 C  C    . ASN   B 1 214 ? -7.132  -14.302 -26.118 1   21.348 ? 214 ASN   B C    1 
ATOM   4047 O  O    . ASN   B 1 214 ? -6.939  -13.57  -27.09  1   23.286 ? 214 ASN   B O    1 
ATOM   4048 C  CB   . ASN   B 1 214 ? -6.692  -12.451 -24.454 1   22.28  ? 214 ASN   B CB   1 
ATOM   4049 C  CG   . ASN   B 1 214 ? -7.417  -11.586 -23.458 1   24.553 ? 214 ASN   B CG   1 
ATOM   4050 O  OD1  . ASN   B 1 214 ? -8.331  -10.844 -23.842 1   28.979 ? 214 ASN   B OD1  1 
ATOM   4051 N  ND2  . ASN   B 1 214 ? -7.093  -11.732 -22.184 1   25.345 ? 214 ASN   B ND2  1 
ATOM   4052 N  N    . GLY   B 1 215 ? -7.026  -15.629 -26.205 1   21.346 ? 215 GLY   B N    1 
ATOM   4053 C  CA   . GLY   B 1 215 ? -6.979  -16.313 -27.489 1   23.163 ? 215 GLY   B CA   1 
ATOM   4054 C  C    . GLY   B 1 215 ? -5.566  -16.544 -28.035 1   23.908 ? 215 GLY   B C    1 
ATOM   4055 O  O    . GLY   B 1 215 ? -5.413  -16.997 -29.164 1   26.794 ? 215 GLY   B O    1 
ATOM   4056 N  N    . ASP   B 1 216 ? -4.535  -16.286 -27.225 1   23.395 ? 216 ASP   B N    1 
ATOM   4057 C  CA   . ASP   B 1 216 ? -3.154  -16.394 -27.673 1   24.217 ? 216 ASP   B CA   1 
ATOM   4058 C  C    . ASP   B 1 216 ? -2.583  -17.676 -27.066 1   24.448 ? 216 ASP   B C    1 
ATOM   4059 O  O    . ASP   B 1 216 ? -2.376  -17.713 -25.858 1   25.731 ? 216 ASP   B O    1 
ATOM   4060 C  CB   . ASP   B 1 216 ? -2.434  -15.109 -27.293 1   27.082 ? 216 ASP   B CB   1 
ATOM   4061 C  CG   . ASP   B 1 216 ? -1.3    -14.659 -28.197 1   28.207 ? 216 ASP   B CG   1 
ATOM   4062 O  OD1  . ASP   B 1 216 ? -0.959  -15.422 -29.129 1   30.584 ? 216 ASP   B OD1  1 
ATOM   4063 O  OD2  . ASP   B 1 216 ? -0.805  -13.526 -27.978 1   28.761 ? 216 ASP   B OD2  1 
ATOM   4064 N  N    . ARG   B 1 217 ? -2.381  -18.729 -27.879 1   24.406 ? 217 ARG   B N    1 
ATOM   4065 C  CA   . ARG   B 1 217 ? -2.247  -20.094 -27.375 1   25.94  ? 217 ARG   B CA   1 
ATOM   4066 C  C    . ARG   B 1 217 ? -1.079  -20.859 -27.998 1   24.09  ? 217 ARG   B C    1 
ATOM   4067 O  O    . ARG   B 1 217 ? -0.898  -22.043 -27.719 1   25.015 ? 217 ARG   B O    1 
ATOM   4068 C  CB   . ARG   B 1 217 ? -3.467  -20.944 -27.754 1   29.356 ? 217 ARG   B CB   1 
ATOM   4069 C  CG   . ARG   B 1 217 ? -4.824  -20.433 -27.302 1   30.807 ? 217 ARG   B CG   1 
ATOM   4070 C  CD   . ARG   B 1 217 ? -5.92   -21.403 -27.691 1   32.662 ? 217 ARG   B CD   1 
ATOM   4071 N  NE   . ARG   B 1 217 ? -5.725  -22.733 -27.107 1   32.714 ? 217 ARG   B NE   1 
ATOM   4072 C  CZ   . ARG   B 1 217 ? -6.336  -23.22  -26.029 1   31.62  ? 217 ARG   B CZ   1 
ATOM   4073 N  NH1  . ARG   B 1 217 ? -7.135  -22.46  -25.299 1   30.581 ? 217 ARG   B NH1  1 
ATOM   4074 N  NH2  . ARG   B 1 217 ? -6.128  -24.475 -25.677 1   32.221 ? 217 ARG   B NH2  1 
ATOM   4075 N  N    . TRP   B 1 218 ? -0.278  -20.2   -28.838 1   22.318 ? 218 TRP   B N    1 
ATOM   4076 C  CA   . TRP   B 1 218 ? 0.695   -20.913 -29.651 1   21.942 ? 218 TRP   B CA   1 
ATOM   4077 C  C    . TRP   B 1 218 ? 1.746   -21.622 -28.799 1   21.987 ? 218 TRP   B C    1 
ATOM   4078 O  O    . TRP   B 1 218 ? 2.383   -22.556 -29.287 1   24.823 ? 218 TRP   B O    1 
ATOM   4079 C  CB   . TRP   B 1 218 ? 1.375   -19.96  -30.644 1   22.088 ? 218 TRP   B CB   1 
ATOM   4080 C  CG   . TRP   B 1 218 ? 2.145   -18.829 -30.015 1   22.072 ? 218 TRP   B CG   1 
ATOM   4081 C  CD1  . TRP   B 1 218 ? 1.726   -17.538 -29.879 1   22.173 ? 218 TRP   B CD1  1 
ATOM   4082 C  CD2  . TRP   B 1 218 ? 3.483   -18.878 -29.466 1   22.315 ? 218 TRP   B CD2  1 
ATOM   4083 N  NE1  . TRP   B 1 218 ? 2.692   -16.79  -29.267 1   22.392 ? 218 TRP   B NE1  1 
ATOM   4084 C  CE2  . TRP   B 1 218 ? 3.784   -17.575 -29.014 1   22.608 ? 218 TRP   B CE2  1 
ATOM   4085 C  CE3  . TRP   B 1 218 ? 4.45    -19.879 -29.324 1   23.532 ? 218 TRP   B CE3  1 
ATOM   4086 C  CZ2  . TRP   B 1 218 ? 5.009   -17.25  -28.432 1   22.826 ? 218 TRP   B CZ2  1 
ATOM   4087 C  CZ3  . TRP   B 1 218 ? 5.659   -19.554 -28.749 1   23.699 ? 218 TRP   B CZ3  1 
ATOM   4088 C  CH2  . TRP   B 1 218 ? 5.937   -18.256 -28.329 1   23.399 ? 218 TRP   B CH2  1 
ATOM   4089 N  N    . PHE   B 1 219 ? 1.948   -21.159 -27.556 1   20.596 ? 219 PHE   B N    1 
ATOM   4090 C  CA   . PHE   B 1 219 ? 3.01    -21.671 -26.695 1   19.71  ? 219 PHE   B CA   1 
ATOM   4091 C  C    . PHE   B 1 219 ? 2.56    -22.899 -25.886 1   19.827 ? 219 PHE   B C    1 
ATOM   4092 O  O    . PHE   B 1 219 ? 3.367   -23.491 -25.17  1   20.853 ? 219 PHE   B O    1 
ATOM   4093 C  CB   . PHE   B 1 219 ? 3.48    -20.553 -25.757 1   19.041 ? 219 PHE   B CB   1 
ATOM   4094 C  CG   . PHE   B 1 219 ? 2.336   -19.849 -25.04  1   18.176 ? 219 PHE   B CG   1 
ATOM   4095 C  CD1  . PHE   B 1 219 ? 1.764   -20.398 -23.894 1   18.232 ? 219 PHE   B CD1  1 
ATOM   4096 C  CD2  . PHE   B 1 219 ? 1.788   -18.68  -25.552 1   17.734 ? 219 PHE   B CD2  1 
ATOM   4097 C  CE1  . PHE   B 1 219 ? 0.7     -19.772 -23.264 1   17.735 ? 219 PHE   B CE1  1 
ATOM   4098 C  CE2  . PHE   B 1 219 ? 0.737   -18.054 -24.902 1   17.636 ? 219 PHE   B CE2  1 
ATOM   4099 C  CZ   . PHE   B 1 219 ? 0.184   -18.62  -23.777 1   17.887 ? 219 PHE   B CZ   1 
ATOM   4100 N  N    . LEU   B 1 220 ? 1.277   -23.276 -25.959 1   20.38  ? 220 LEU   B N    1 
ATOM   4101 C  CA   . LEU   B 1 220 ? 0.801   -24.479 -25.291 1   20.934 ? 220 LEU   B CA   1 
ATOM   4102 C  C    . LEU   B 1 220 ? 1.402   -25.709 -25.967 1   21.748 ? 220 LEU   B C    1 
ATOM   4103 O  O    . LEU   B 1 220 ? 1.717   -25.683 -27.154 1   23.83  ? 220 LEU   B O    1 
ATOM   4104 C  CB   . LEU   B 1 220 ? -0.724  -24.547 -25.267 1   21.673 ? 220 LEU   B CB   1 
ATOM   4105 C  CG   . LEU   B 1 220 ? -1.417  -23.402 -24.523 1   21.854 ? 220 LEU   B CG   1 
ATOM   4106 C  CD1  . LEU   B 1 220 ? -2.934  -23.518 -24.637 1   22.592 ? 220 LEU   B CD1  1 
ATOM   4107 C  CD2  . LEU   B 1 220 ? -0.971  -23.343 -23.063 1   21.309 ? 220 LEU   B CD2  1 
ATOM   4108 N  N    . ASN   B 1 221 ? 1.581   -26.781 -25.188 1   21.241 ? 221 ASN   B N    1 
ATOM   4109 C  CA   . ASN   B 1 221 ? 2.202   -27.992 -25.702 1   19.953 ? 221 ASN   B CA   1 
ATOM   4110 C  C    . ASN   B 1 221 ? 1.618   -29.202 -24.977 1   18.614 ? 221 ASN   B C    1 
ATOM   4111 O  O    . ASN   B 1 221 ? 0.849   -29.056 -24.025 1   20.623 ? 221 ASN   B O    1 
ATOM   4112 C  CB   . ASN   B 1 221 ? 3.729   -27.927 -25.644 1   20.097 ? 221 ASN   B CB   1 
ATOM   4113 C  CG   . ASN   B 1 221 ? 4.301   -27.838 -24.247 1   20.647 ? 221 ASN   B CG   1 
ATOM   4114 O  OD1  . ASN   B 1 221 ? 3.766   -28.415 -23.295 1   20.635 ? 221 ASN   B OD1  1 
ATOM   4115 N  ND2  . ASN   B 1 221 ? 5.406   -27.13  -24.107 1   21.775 ? 221 ASN   B ND2  1 
ATOM   4116 N  N    . ARG   B 1 222 ? 2.013   -30.402 -25.415 1   17.731 ? 222 ARG   B N    1 
ATOM   4117 C  CA   . ARG   B 1 222 ? 1.46    -31.639 -24.873 1   17.225 ? 222 ARG   B CA   1 
ATOM   4118 C  C    . ARG   B 1 222 ? 2.118   -32.046 -23.553 1   16.974 ? 222 ARG   B C    1 
ATOM   4119 O  O    . ARG   B 1 222 ? 1.679   -33.015 -22.933 1   17.909 ? 222 ARG   B O    1 
ATOM   4120 C  CB   . ARG   B 1 222 ? 1.665   -32.807 -25.844 1   17.275 ? 222 ARG   B CB   1 
ATOM   4121 C  CG   . ARG   B 1 222 ? 3.117   -33.232 -26.017 1   17.979 ? 222 ARG   B CG   1 
ATOM   4122 C  CD   . ARG   B 1 222 ? 3.259   -34.683 -26.447 1   18.997 ? 222 ARG   B CD   1 
ATOM   4123 N  NE   . ARG   B 1 222 ? 2.751   -34.88  -27.801 1   19.403 ? 222 ARG   B NE   1 
ATOM   4124 C  CZ   . ARG   B 1 222 ? 1.943   -35.857 -28.217 1   18.421 ? 222 ARG   B CZ   1 
ATOM   4125 N  NH1  . ARG   B 1 222 ? 1.592   -36.863 -27.421 1   17.506 ? 222 ARG   B NH1  1 
ATOM   4126 N  NH2  . ARG   B 1 222 ? 1.492   -35.807 -29.453 1   19.673 ? 222 ARG   B NH2  1 
ATOM   4127 N  N    . PHE   B 1 223 ? 3.162   -31.329 -23.125 1   16.321 ? 223 PHE   B N    1 
ATOM   4128 C  CA   . PHE   B 1 223 ? 3.993   -31.811 -22.04  1   16.536 ? 223 PHE   B CA   1 
ATOM   4129 C  C    . PHE   B 1 223 ? 3.529   -31.251 -20.695 1   17.623 ? 223 PHE   B C    1 
ATOM   4130 O  O    . PHE   B 1 223 ? 2.859   -30.215 -20.604 1   17.964 ? 223 PHE   B O    1 
ATOM   4131 C  CB   . PHE   B 1 223 ? 5.444   -31.408 -22.308 1   17.731 ? 223 PHE   B CB   1 
ATOM   4132 C  CG   . PHE   B 1 223 ? 5.958   -31.915 -23.642 1   18.23  ? 223 PHE   B CG   1 
ATOM   4133 C  CD1  . PHE   B 1 223 ? 6.183   -33.27  -23.84  1   18.199 ? 223 PHE   B CD1  1 
ATOM   4134 C  CD2  . PHE   B 1 223 ? 6.201   -31.046 -24.696 1   19.116 ? 223 PHE   B CD2  1 
ATOM   4135 C  CE1  . PHE   B 1 223 ? 6.62    -33.739 -25.069 1   19.17  ? 223 PHE   B CE1  1 
ATOM   4136 C  CE2  . PHE   B 1 223 ? 6.618   -31.521 -25.924 1   19.839 ? 223 PHE   B CE2  1 
ATOM   4137 C  CZ   . PHE   B 1 223 ? 6.836   -32.861 -26.105 1   19.37  ? 223 PHE   B CZ   1 
ATOM   4138 N  N    . THR   B 1 224 ? 3.929   -31.958 -19.639 1   19.18  ? 224 THR   B N    1 
ATOM   4139 C  CA   . THR   B 1 224 ? 3.849   -31.419 -18.297 1   21.302 ? 224 THR   B CA   1 
ATOM   4140 C  C    . THR   B 1 224 ? 5.201   -31.624 -17.615 1   22.72  ? 224 THR   B C    1 
ATOM   4141 O  O    . THR   B 1 224 ? 6.161   -32.119 -18.21  1   25.199 ? 224 THR   B O    1 
ATOM   4142 C  CB   . THR   B 1 224 ? 2.675   -32.06  -17.556 1   22.729 ? 224 THR   B CB   1 
ATOM   4143 O  OG1  . THR   B 1 224 ? 2.469   -31.291 -16.381 1   25.141 ? 224 THR   B OG1  1 
ATOM   4144 C  CG2  . THR   B 1 224 ? 2.918   -33.504 -17.166 1   22.356 ? 224 THR   B CG2  1 
ATOM   4145 N  N    . THR   B 1 225 ? 5.281   -31.186 -16.366 1   22.179 ? 225 THR   B N    1 
ATOM   4146 C  CA   . THR   B 1 225 ? 6.506   -31.349 -15.608 1   22.866 ? 225 THR   B CA   1 
ATOM   4147 C  C    . THR   B 1 225 ? 6.134   -31.51  -14.143 1   23.154 ? 225 THR   B C    1 
ATOM   4148 O  O    . THR   B 1 225 ? 4.959   -31.585 -13.795 1   25.199 ? 225 THR   B O    1 
ATOM   4149 C  CB   . THR   B 1 225 ? 7.43    -30.159 -15.873 1   23.129 ? 225 THR   B CB   1 
ATOM   4150 O  OG1  . THR   B 1 225 ? 8.69    -30.468 -15.275 1   26.404 ? 225 THR   B OG1  1 
ATOM   4151 C  CG2  . THR   B 1 225 ? 6.88    -28.852 -15.325 1   23.671 ? 225 THR   B CG2  1 
ATOM   4152 N  N    . THR   B 1 226 ? 7.158   -31.597 -13.299 1   24.363 ? 226 THR   B N    1 
ATOM   4153 C  CA   . THR   B 1 226 ? 6.959   -31.639 -11.864 1   24.392 ? 226 THR   B CA   1 
ATOM   4154 C  C    . THR   B 1 226 ? 7.421   -30.308 -11.294 1   23.921 ? 226 THR   B C    1 
ATOM   4155 O  O    . THR   B 1 226 ? 8.185   -29.572 -11.923 1   24.174 ? 226 THR   B O    1 
ATOM   4156 C  CB   . THR   B 1 226 ? 7.734   -32.793 -11.227 1   25.063 ? 226 THR   B CB   1 
ATOM   4157 O  OG1  . THR   B 1 226 ? 9.117   -32.5   -11.409 1   25.336 ? 226 THR   B OG1  1 
ATOM   4158 C  CG2  . THR   B 1 226 ? 7.344   -34.137 -11.819 1   26.387 ? 226 THR   B CG2  1 
ATOM   4159 N  N    . LEU   B 1 227 ? 6.97    -30.024 -10.077 1   24.34  ? 227 LEU   B N    1 
ATOM   4160 C  CA   . LEU   B 1 227 ? 7.388   -28.813 -9.405  1   25.557 ? 227 LEU   B CA   1 
ATOM   4161 C  C    . LEU   B 1 227 ? 8.907   -28.811 -9.216  1   26.585 ? 227 LEU   B C    1 
ATOM   4162 O  O    . LEU   B 1 227 ? 9.549   -27.795 -9.438  1   27.401 ? 227 LEU   B O    1 
ATOM   4163 C  CB   . LEU   B 1 227 ? 6.623   -28.711 -8.088  1   27.564 ? 227 LEU   B CB   1 
ATOM   4164 C  CG   . LEU   B 1 227 ? 6.645   -27.34  -7.423  1   28.354 ? 227 LEU   B CG   1 
ATOM   4165 C  CD1  . LEU   B 1 227 ? 6.139   -26.27  -8.381  1   28.984 ? 227 LEU   B CD1  1 
ATOM   4166 C  CD2  . LEU   B 1 227 ? 5.81    -27.347 -6.148  1   29.944 ? 227 LEU   B CD2  1 
ATOM   4167 N  N    A ASN   B 1 228 ? 9.483   -29.951 -8.823  0.5 26.36  ? 228 ASN   B N    1 
ATOM   4168 N  N    B ASN   B 1 228 ? 9.459   -29.976 -8.843  0.5 26.762 ? 228 ASN   B N    1 
ATOM   4169 C  CA   A ASN   B 1 228 ? 10.923  -30.04  -8.618  0.5 27.235 ? 228 ASN   B CA   1 
ATOM   4170 C  CA   B ASN   B 1 228 ? 10.886  -30.157 -8.612  0.5 28.211 ? 228 ASN   B CA   1 
ATOM   4171 C  C    A ASN   B 1 228 ? 11.698  -29.754 -9.905  0.5 26.63  ? 228 ASN   B C    1 
ATOM   4172 C  C    B ASN   B 1 228 ? 11.695  -29.833 -9.868  0.5 27.063 ? 228 ASN   B C    1 
ATOM   4173 O  O    A ASN   B 1 228 ? 12.65   -28.957 -9.908  0.5 27.844 ? 228 ASN   B O    1 
ATOM   4174 O  O    B ASN   B 1 228 ? 12.676  -29.1   -9.804  0.5 28.287 ? 228 ASN   B O    1 
ATOM   4175 C  CB   A ASN   B 1 228 ? 11.325  -31.391 -8.042  0.5 27.974 ? 228 ASN   B CB   1 
ATOM   4176 C  CB   B ASN   B 1 228 ? 11.176  -31.577 -8.132  0.5 29.423 ? 228 ASN   B CB   1 
ATOM   4177 C  CG   A ASN   B 1 228 ? 11.054  -31.476 -6.56   0.5 29.402 ? 228 ASN   B CG   1 
ATOM   4178 C  CG   B ASN   B 1 228 ? 12.644  -31.83  -7.881  0.5 31.824 ? 228 ASN   B CG   1 
ATOM   4179 O  OD1  A ASN   B 1 228 ? 10.824  -30.452 -5.907  0.5 30.485 ? 228 ASN   B OD1  1 
ATOM   4180 O  OD1  B ASN   B 1 228 ? 13.07   -31.901 -6.724  0.5 33.585 ? 228 ASN   B OD1  1 
ATOM   4181 N  ND2  A ASN   B 1 228 ? 11.092  -32.68  -6.011  0.5 30.254 ? 228 ASN   B ND2  1 
ATOM   4182 N  ND2  B ASN   B 1 228 ? 13.43   -31.978 -8.937  0.5 32.396 ? 228 ASN   B ND2  1 
ATOM   4183 N  N    . ASP   B 1 229 ? 11.29   -30.404 -11.006 1   27.348 ? 229 ASP   B N    1 
ATOM   4184 C  CA   . ASP   B 1 229 ? 12.017  -30.253 -12.263 1   27.837 ? 229 ASP   B CA   1 
ATOM   4185 C  C    . ASP   B 1 229 ? 11.899  -28.814 -12.772 1   27.61  ? 229 ASP   B C    1 
ATOM   4186 O  O    . ASP   B 1 229 ? 12.861  -28.222 -13.277 1   27.683 ? 229 ASP   B O    1 
ATOM   4187 C  CB   . ASP   B 1 229 ? 11.538  -31.233 -13.32  1   30.613 ? 229 ASP   B CB   1 
ATOM   4188 C  CG   . ASP   B 1 229 ? 11.995  -32.679 -13.182 1   33.785 ? 229 ASP   B CG   1 
ATOM   4189 O  OD1  . ASP   B 1 229 ? 12.764  -32.992 -12.244 1   37.957 ? 229 ASP   B OD1  1 
ATOM   4190 O  OD2  . ASP   B 1 229 ? 11.59   -33.487 -14.037 1   37.393 ? 229 ASP   B OD2  1 
ATOM   4191 N  N    . PHE   B 1 230 ? 10.702  -28.243 -12.626 1   25.373 ? 230 PHE   B N    1 
ATOM   4192 C  CA   . PHE   B 1 230 ? 10.491  -26.886 -13.084 1   24.796 ? 230 PHE   B CA   1 
ATOM   4193 C  C    . PHE   B 1 230 ? 11.39   -25.931 -12.298 1   24.275 ? 230 PHE   B C    1 
ATOM   4194 O  O    . PHE   B 1 230 ? 12.004  -25.034 -12.88  1   24.307 ? 230 PHE   B O    1 
ATOM   4195 C  CB   . PHE   B 1 230 ? 9.019   -26.494 -12.987 1   24.472 ? 230 PHE   B CB   1 
ATOM   4196 C  CG   . PHE   B 1 230 ? 8.89    -25.038 -13.386 1   24.777 ? 230 PHE   B CG   1 
ATOM   4197 C  CD1  . PHE   B 1 230 ? 8.937   -24.66  -14.723 1   26.315 ? 230 PHE   B CD1  1 
ATOM   4198 C  CD2  . PHE   B 1 230 ? 8.791   -24.055 -12.417 1   26.295 ? 230 PHE   B CD2  1 
ATOM   4199 C  CE1  . PHE   B 1 230 ? 8.844   -23.325 -15.076 1   26.542 ? 230 PHE   B CE1  1 
ATOM   4200 C  CE2  . PHE   B 1 230 ? 8.737   -22.725 -12.773 1   26.701 ? 230 PHE   B CE2  1 
ATOM   4201 C  CZ   . PHE   B 1 230 ? 8.754   -22.362 -14.097 1   27.313 ? 230 PHE   B CZ   1 
ATOM   4202 N  N    . ASN   B 1 231 ? 11.482  -26.127 -10.979 1   23.302 ? 231 ASN   B N    1 
ATOM   4203 C  CA   . ASN   B 1 231 ? 12.268  -25.235 -10.142 1   23.886 ? 231 ASN   B CA   1 
ATOM   4204 C  C    . ASN   B 1 231 ? 13.755  -25.309 -10.475 1   25.057 ? 231 ASN   B C    1 
ATOM   4205 O  O    . ASN   B 1 231 ? 14.442  -24.3   -10.345 1   26.001 ? 231 ASN   B O    1 
ATOM   4206 C  CB   . ASN   B 1 231 ? 11.973  -25.443 -8.661  1   24.897 ? 231 ASN   B CB   1 
ATOM   4207 C  CG   . ASN   B 1 231 ? 10.716  -24.703 -8.272  1   25.949 ? 231 ASN   B CG   1 
ATOM   4208 O  OD1  . ASN   B 1 231 ? 10.461  -23.606 -8.779  1   30.011 ? 231 ASN   B OD1  1 
ATOM   4209 N  ND2  . ASN   B 1 231 ? 9.873   -25.31  -7.455  1   25.783 ? 231 ASN   B ND2  1 
ATOM   4210 N  N    . LEU   B 1 232 ? 14.254  -26.451 -10.946 1   26.217 ? 232 LEU   B N    1 
ATOM   4211 C  CA   . LEU   B 1 232 ? 15.627  -26.491 -11.437 1   27.497 ? 232 LEU   B CA   1 
ATOM   4212 C  C    . LEU   B 1 232 ? 15.786  -25.535 -12.622 1   25.977 ? 232 LEU   B C    1 
ATOM   4213 O  O    . LEU   B 1 232 ? 16.784  -24.824 -12.723 1   26.699 ? 232 LEU   B O    1 
ATOM   4214 C  CB   . LEU   B 1 232 ? 16.053  -27.909 -11.806 1   29.639 ? 232 LEU   B CB   1 
ATOM   4215 C  CG   . LEU   B 1 232 ? 16.025  -28.927 -10.661 1   32.048 ? 232 LEU   B CG   1 
ATOM   4216 C  CD1  . LEU   B 1 232 ? 16.145  -30.337 -11.211 1   33.077 ? 232 LEU   B CD1  1 
ATOM   4217 C  CD2  . LEU   B 1 232 ? 17.128  -28.637 -9.654  1   33.509 ? 232 LEU   B CD2  1 
ATOM   4218 N  N    . VAL   B 1 233 ? 14.787  -25.499 -13.512 1   25.524 ? 233 VAL   B N    1 
ATOM   4219 C  CA   . VAL   B 1 233 ? 14.808  -24.607 -14.664 1   24.224 ? 233 VAL   B CA   1 
ATOM   4220 C  C    . VAL   B 1 233 ? 14.69   -23.147 -14.228 1   23.069 ? 233 VAL   B C    1 
ATOM   4221 O  O    . VAL   B 1 233 ? 15.429  -22.291 -14.706 1   22.389 ? 233 VAL   B O    1 
ATOM   4222 C  CB   . VAL   B 1 233 ? 13.689  -24.975 -15.66  1   25.152 ? 233 VAL   B CB   1 
ATOM   4223 C  CG1  . VAL   B 1 233 ? 13.592  -23.983 -16.814 1   25.407 ? 233 VAL   B CG1  1 
ATOM   4224 C  CG2  . VAL   B 1 233 ? 13.854  -26.397 -16.182 1   24.869 ? 233 VAL   B CG2  1 
ATOM   4225 N  N    . ALA   B 1 234 ? 13.76   -22.846 -13.322 1   23.545 ? 234 ALA   B N    1 
ATOM   4226 C  CA   . ALA   B 1 234 ? 13.585  -21.486 -12.836 1   23.694 ? 234 ALA   B CA   1 
ATOM   4227 C  C    . ALA   B 1 234 ? 14.912  -20.933 -12.315 1   23.916 ? 234 ALA   B C    1 
ATOM   4228 O  O    . ALA   B 1 234 ? 15.301  -19.805 -12.615 1   23.283 ? 234 ALA   B O    1 
ATOM   4229 C  CB   . ALA   B 1 234 ? 12.517  -21.461 -11.76  1   24.408 ? 234 ALA   B CB   1 
ATOM   4230 N  N    . MET   B 1 235 ? 15.618  -21.756 -11.539 1   24.731 ? 235 MET   B N    1 
ATOM   4231 C  CA   . MET   B 1 235 ? 16.842  -21.299 -10.908 1   26.913 ? 235 MET   B CA   1 
ATOM   4232 C  C    . MET   B 1 235 ? 17.875  -20.957 -11.981 1   25.531 ? 235 MET   B C    1 
ATOM   4233 O  O    . MET   B 1 235 ? 18.575  -19.954 -11.884 1   25.389 ? 235 MET   B O    1 
ATOM   4234 C  CB   . MET   B 1 235 ? 17.39   -22.365 -9.958  1   30.463 ? 235 MET   B CB   1 
ATOM   4235 C  CG   . MET   B 1 235 ? 18.599  -21.919 -9.164  1   33.74  ? 235 MET   B CG   1 
ATOM   4236 S  SD   . MET   B 1 235 ? 19.003  -23.069 -7.836  1   40.608 ? 235 MET   B SD   1 
ATOM   4237 C  CE   . MET   B 1 235 ? 17.725  -22.709 -6.621  1   40.694 ? 235 MET   B CE   1 
ATOM   4238 N  N    . LYS   B 1 236 ? 17.918  -21.774 -13.039 1   25.067 ? 236 LYS   B N    1 
ATOM   4239 C  CA   . LYS   B 1 236 ? 18.884  -21.586 -14.107 1   25.289 ? 236 LYS   B CA   1 
ATOM   4240 C  C    . LYS   B 1 236 ? 18.674  -20.241 -14.809 1   23.235 ? 236 LYS   B C    1 
ATOM   4241 O  O    . LYS   B 1 236 ? 19.643  -19.631 -15.272 1   25.023 ? 236 LYS   B O    1 
ATOM   4242 C  CB   . LYS   B 1 236 ? 18.801  -22.761 -15.087 1   27.344 ? 236 LYS   B CB   1 
ATOM   4243 C  CG   . LYS   B 1 236 ? 19.673  -22.618 -16.329 1   30.744 ? 236 LYS   B CG   1 
ATOM   4244 C  CD   . LYS   B 1 236 ? 19.698  -23.826 -17.265 1   34.079 ? 236 LYS   B CD   1 
ATOM   4245 C  CE   . LYS   B 1 236 ? 20.319  -23.5   -18.594 1   36.764 ? 236 LYS   B CE   1 
ATOM   4246 N  NZ   . LYS   B 1 236 ? 20.488  -24.687 -19.434 1   39.527 ? 236 LYS   B NZ   1 
ATOM   4247 N  N    . TYR   B 1 237 ? 17.409  -19.796 -14.897 1   20.726 ? 237 TYR   B N    1 
ATOM   4248 C  CA   . TYR   B 1 237 ? 17.063  -18.603 -15.662 1   20.533 ? 237 TYR   B CA   1 
ATOM   4249 C  C    . TYR   B 1 237 ? 16.772  -17.389 -14.775 1   19.716 ? 237 TYR   B C    1 
ATOM   4250 O  O    . TYR   B 1 237 ? 16.203  -16.405 -15.251 1   19.928 ? 237 TYR   B O    1 
ATOM   4251 C  CB   . TYR   B 1 237 ? 15.883  -18.928 -16.585 1   20.856 ? 237 TYR   B CB   1 
ATOM   4252 C  CG   . TYR   B 1 237 ? 16.3    -19.813 -17.751 1   21.748 ? 237 TYR   B CG   1 
ATOM   4253 C  CD1  . TYR   B 1 237 ? 16.87   -19.262 -18.89  1   23.235 ? 237 TYR   B CD1  1 
ATOM   4254 C  CD2  . TYR   B 1 237 ? 16.16   -21.194 -17.699 1   22.473 ? 237 TYR   B CD2  1 
ATOM   4255 C  CE1  . TYR   B 1 237 ? 17.285  -20.054 -19.944 1   24.198 ? 237 TYR   B CE1  1 
ATOM   4256 C  CE2  . TYR   B 1 237 ? 16.579  -22     -18.742 1   23.468 ? 237 TYR   B CE2  1 
ATOM   4257 C  CZ   . TYR   B 1 237 ? 17.139  -21.428 -19.871 1   24.044 ? 237 TYR   B CZ   1 
ATOM   4258 O  OH   . TYR   B 1 237 ? 17.556  -22.22  -20.903 1   26.38  ? 237 TYR   B OH   1 
ATOM   4259 N  N    A ASN   B 1 238 ? 17.149  -17.444 -13.494 0.5 19.322 ? 238 ASN   B N    1 
ATOM   4260 N  N    B ASN   B 1 238 ? 17.188  -17.477 -13.503 0.5 19.746 ? 238 ASN   B N    1 
ATOM   4261 C  CA   A ASN   B 1 238 ? 17.036  -16.276 -12.626 0.5 19.001 ? 238 ASN   B CA   1 
ATOM   4262 C  CA   B ASN   B 1 238 ? 17.054  -16.399 -12.531 0.5 19.659 ? 238 ASN   B CA   1 
ATOM   4263 C  C    A ASN   B 1 238 ? 15.565  -15.971 -12.324 0.5 17.815 ? 238 ASN   B C    1 
ATOM   4264 C  C    B ASN   B 1 238 ? 15.588  -15.997 -12.389 0.5 18.239 ? 238 ASN   B C    1 
ATOM   4265 O  O    A ASN   B 1 238 ? 15.186  -14.816 -12.112 0.5 17.527 ? 238 ASN   B O    1 
ATOM   4266 O  O    B ASN   B 1 238 ? 15.254  -14.814 -12.359 0.5 17.955 ? 238 ASN   B O    1 
ATOM   4267 C  CB   A ASN   B 1 238 ? 17.745  -15.07  -13.238 0.5 20.063 ? 238 ASN   B CB   1 
ATOM   4268 C  CB   B ASN   B 1 238 ? 17.976  -15.229 -12.853 0.5 21.453 ? 238 ASN   B CB   1 
ATOM   4269 C  CG   A ASN   B 1 238 ? 18.158  -14.062 -12.195 0.5 21.329 ? 238 ASN   B CG   1 
ATOM   4270 C  CG   B ASN   B 1 238 ? 19.43   -15.629 -12.787 0.5 23.353 ? 238 ASN   B CG   1 
ATOM   4271 O  OD1  A ASN   B 1 238 ? 18.763  -14.444 -11.188 0.5 24.531 ? 238 ASN   B OD1  1 
ATOM   4272 O  OD1  B ASN   B 1 238 ? 19.87   -16.233 -11.8   0.5 25.162 ? 238 ASN   B OD1  1 
ATOM   4273 N  ND2  A ASN   B 1 238 ? 17.869  -12.789 -12.419 0.5 21.868 ? 238 ASN   B ND2  1 
ATOM   4274 N  ND2  B ASN   B 1 238 ? 20.185  -15.317 -13.83  0.5 24.898 ? 238 ASN   B ND2  1 
ATOM   4275 N  N    . TYR   B 1 239 ? 14.744  -17.026 -12.311 1   17.174 ? 239 TYR   B N    1 
ATOM   4276 C  CA   . TYR   B 1 239 ? 13.348  -16.924 -11.934 1   16.877 ? 239 TYR   B CA   1 
ATOM   4277 C  C    . TYR   B 1 239 ? 13.231  -17.335 -10.469 1   17.507 ? 239 TYR   B C    1 
ATOM   4278 O  O    . TYR   B 1 239 ? 13.955  -18.211 -10.004 1   18.755 ? 239 TYR   B O    1 
ATOM   4279 C  CB   . TYR   B 1 239 ? 12.502  -17.862 -12.8   1   16.356 ? 239 TYR   B CB   1 
ATOM   4280 C  CG   . TYR   B 1 239 ? 11.991  -17.236 -14.09  1   15.797 ? 239 TYR   B CG   1 
ATOM   4281 C  CD1  . TYR   B 1 239 ? 12.828  -16.593 -14.995 1   15.899 ? 239 TYR   B CD1  1 
ATOM   4282 C  CD2  . TYR   B 1 239 ? 10.636  -17.269 -14.385 1   16.45  ? 239 TYR   B CD2  1 
ATOM   4283 C  CE1  . TYR   B 1 239 ? 12.335  -16.016 -16.154 1   16.059 ? 239 TYR   B CE1  1 
ATOM   4284 C  CE2  . TYR   B 1 239 ? 10.13   -16.696 -15.539 1   16.632 ? 239 TYR   B CE2  1 
ATOM   4285 C  CZ   . TYR   B 1 239 ? 10.976  -16.059 -16.424 1   16.361 ? 239 TYR   B CZ   1 
ATOM   4286 O  OH   . TYR   B 1 239 ? 10.45   -15.488 -17.546 1   18.184 ? 239 TYR   B OH   1 
ATOM   4287 N  N    . GLU   B 1 240 ? 12.283  -16.714 -9.763  1   17.578 ? 240 GLU   B N    1 
ATOM   4288 C  CA   . GLU   B 1 240 ? 11.968  -17.087 -8.396  1   18.948 ? 240 GLU   B CA   1 
ATOM   4289 C  C    . GLU   B 1 240 ? 11.452  -18.524 -8.332  1   18.754 ? 240 GLU   B C    1 
ATOM   4290 O  O    . GLU   B 1 240 ? 10.823  -19.025 -9.266  1   17.854 ? 240 GLU   B O    1 
ATOM   4291 C  CB   . GLU   B 1 240 ? 10.916  -16.141 -7.818  1   19.585 ? 240 GLU   B CB   1 
ATOM   4292 C  CG   . GLU   B 1 240 ? 11.478  -14.762 -7.489  1   22.43  ? 240 GLU   B CG   1 
ATOM   4293 C  CD   . GLU   B 1 240 ? 12.441  -14.758 -6.31   1   25.176 ? 240 GLU   B CD   1 
ATOM   4294 O  OE1  . GLU   B 1 240 ? 11.998  -15.109 -5.194  1   30.132 ? 240 GLU   B OE1  1 
ATOM   4295 O  OE2  . GLU   B 1 240 ? 13.626  -14.425 -6.503  1   26.896 ? 240 GLU   B OE2  1 
ATOM   4296 N  N    . PRO   B 1 241 ? 11.669  -19.24  -7.209  1   20.54  ? 241 PRO   B N    1 
ATOM   4297 C  CA   . PRO   B 1 241 ? 11.046  -20.55  -7.03   1   21.378 ? 241 PRO   B CA   1 
ATOM   4298 C  C    . PRO   B 1 241 ? 9.525   -20.482 -7.107  1   21.063 ? 241 PRO   B C    1 
ATOM   4299 O  O    . PRO   B 1 241 ? 8.916   -19.502 -6.679  1   21.57  ? 241 PRO   B O    1 
ATOM   4300 C  CB   . PRO   B 1 241 ? 11.52   -20.972 -5.636  1   22.695 ? 241 PRO   B CB   1 
ATOM   4301 C  CG   . PRO   B 1 241 ? 12.798  -20.204 -5.442  1   23.008 ? 241 PRO   B CG   1 
ATOM   4302 C  CD   . PRO   B 1 241 ? 12.529  -18.85  -6.079  1   22.273 ? 241 PRO   B CD   1 
ATOM   4303 N  N    . LEU   B 1 242 ? 8.928   -21.527 -7.685  1   21.091 ? 242 LEU   B N    1 
ATOM   4304 C  CA   . LEU   B 1 242 ? 7.486   -21.703 -7.638  1   21.065 ? 242 LEU   B CA   1 
ATOM   4305 C  C    . LEU   B 1 242 ? 7.16    -22.631 -6.473  1   21.381 ? 242 LEU   B C    1 
ATOM   4306 O  O    . LEU   B 1 242 ? 7.723   -23.713 -6.372  1   23.135 ? 242 LEU   B O    1 
ATOM   4307 C  CB   . LEU   B 1 242 ? 6.973   -22.275 -8.957  1   21.128 ? 242 LEU   B CB   1 
ATOM   4308 C  CG   . LEU   B 1 242 ? 5.455   -22.199 -9.163  1   21.447 ? 242 LEU   B CG   1 
ATOM   4309 C  CD1  . LEU   B 1 242 ? 5.002   -20.754 -9.368  1   20.67  ? 242 LEU   B CD1  1 
ATOM   4310 C  CD2  . LEU   B 1 242 ? 5.032   -23.091 -10.316 1   21.724 ? 242 LEU   B CD2  1 
ATOM   4311 N  N    . THR   B 1 243 ? 6.261   -22.196 -5.587  1   22.112 ? 243 THR   B N    1 
ATOM   4312 C  CA   . THR   B 1 243 ? 5.864   -22.986 -4.431  1   23.223 ? 243 THR   B CA   1 
ATOM   4313 C  C    . THR   B 1 243 ? 4.507   -23.632 -4.684  1   23.349 ? 243 THR   B C    1 
ATOM   4314 O  O    . THR   B 1 243 ? 3.766   -23.24  -5.582  1   23.185 ? 243 THR   B O    1 
ATOM   4315 C  CB   . THR   B 1 243 ? 5.812   -22.109 -3.179  1   23.986 ? 243 THR   B CB   1 
ATOM   4316 O  OG1  . THR   B 1 243 ? 4.717   -21.216 -3.365  1   23.903 ? 243 THR   B OG1  1 
ATOM   4317 C  CG2  . THR   B 1 243 ? 7.113   -21.36  -2.948  1   24.915 ? 243 THR   B CG2  1 
ATOM   4318 N  N    . GLN   B 1 244 ? 4.151   -24.574 -3.805  1   24.844 ? 244 GLN   B N    1 
ATOM   4319 C  CA   . GLN   B 1 244 ? 2.829   -25.171 -3.841  1   26.645 ? 244 GLN   B CA   1 
ATOM   4320 C  C    . GLN   B 1 244 ? 1.768   -24.095 -3.606  1   26.797 ? 244 GLN   B C    1 
ATOM   4321 O  O    . GLN   B 1 244 ? 0.686   -24.168 -4.182  1   27.125 ? 244 GLN   B O    1 
ATOM   4322 C  CB   . GLN   B 1 244 ? 2.71    -26.308 -2.825  1   28.793 ? 244 GLN   B CB   1 
ATOM   4323 C  CG   . GLN   B 1 244 ? 1.39    -27.069 -2.896  1   30.691 ? 244 GLN   B CG   1 
ATOM   4324 C  CD   . GLN   B 1 244 ? 1.144   -27.694 -4.252  1   31.896 ? 244 GLN   B CD   1 
ATOM   4325 O  OE1  . GLN   B 1 244 ? 2.039   -28.318 -4.827  1   34.005 ? 244 GLN   B OE1  1 
ATOM   4326 N  NE2  . GLN   B 1 244 ? -0.056  -27.52  -4.79   1   33.952 ? 244 GLN   B NE2  1 
ATOM   4327 N  N    . ASP   B 1 245 ? 2.056   -23.092 -2.768  1   27.124 ? 245 ASP   B N    1 
ATOM   4328 C  CA   . ASP   B 1 245 ? 1.075   -22.04  -2.555  1   28.556 ? 245 ASP   B CA   1 
ATOM   4329 C  C    . ASP   B 1 245 ? 0.816   -21.302 -3.868  1   26.471 ? 245 ASP   B C    1 
ATOM   4330 O  O    . ASP   B 1 245 ? -0.331  -20.968 -4.161  1   27.443 ? 245 ASP   B O    1 
ATOM   4331 C  CB   . ASP   B 1 245 ? 1.439   -21.094 -1.423  1   31.373 ? 245 ASP   B CB   1 
ATOM   4332 C  CG   . ASP   B 1 245 ? 0.319   -20.143 -1.019  1   35.909 ? 245 ASP   B CG   1 
ATOM   4333 O  OD1  . ASP   B 1 245 ? -0.833  -20.616 -0.911  1   40.752 ? 245 ASP   B OD1  1 
ATOM   4334 O  OD2  . ASP   B 1 245 ? 0.601   -18.94  -0.811  1   39.6   ? 245 ASP   B OD2  1 
ATOM   4335 N  N    . HIS   B 1 246 ? 1.87    -21.061 -4.66   1   24.237 ? 246 HIS   B N    1 
ATOM   4336 C  CA   . HIS   B 1 246 ? 1.702   -20.432 -5.963  1   23.785 ? 246 HIS   B CA   1 
ATOM   4337 C  C    . HIS   B 1 246 ? 0.811   -21.286 -6.866  1   23.749 ? 246 HIS   B C    1 
ATOM   4338 O  O    . HIS   B 1 246 ? -0.061  -20.764 -7.564  1   25.08  ? 246 HIS   B O    1 
ATOM   4339 C  CB   . HIS   B 1 246 ? 3.049   -20.185 -6.649  1   22.076 ? 246 HIS   B CB   1 
ATOM   4340 C  CG   . HIS   B 1 246 ? 3.928   -19.205 -5.945  1   22.358 ? 246 HIS   B CG   1 
ATOM   4341 N  ND1  . HIS   B 1 246 ? 5.301   -19.321 -5.938  1   22.743 ? 246 HIS   B ND1  1 
ATOM   4342 C  CD2  . HIS   B 1 246 ? 3.641   -18.094 -5.25   1   22.199 ? 246 HIS   B CD2  1 
ATOM   4343 C  CE1  . HIS   B 1 246 ? 5.814   -18.313 -5.247  1   22.815 ? 246 HIS   B CE1  1 
ATOM   4344 N  NE2  . HIS   B 1 246 ? 4.824   -17.544 -4.836  1   22.092 ? 246 HIS   B NE2  1 
ATOM   4345 N  N    . VAL   B 1 247 ? 1.049   -22.601 -6.861  1   25.294 ? 247 VAL   B N    1 
ATOM   4346 C  CA   . VAL   B 1 247 ? 0.263   -23.513 -7.676  1   26.579 ? 247 VAL   B CA   1 
ATOM   4347 C  C    . VAL   B 1 247 ? -1.204  -23.423 -7.264  1   28.836 ? 247 VAL   B C    1 
ATOM   4348 O  O    . VAL   B 1 247 ? -2.08   -23.373 -8.118  1   28.616 ? 247 VAL   B O    1 
ATOM   4349 C  CB   . VAL   B 1 247 ? 0.785   -24.96  -7.577  1   27.598 ? 247 VAL   B CB   1 
ATOM   4350 C  CG1  . VAL   B 1 247 ? -0.141  -25.951 -8.271  1   27.754 ? 247 VAL   B CG1  1 
ATOM   4351 C  CG2  . VAL   B 1 247 ? 2.197   -25.084 -8.133  1   27.368 ? 247 VAL   B CG2  1 
ATOM   4352 N  N    . ASP   B 1 248 ? -1.458  -23.405 -5.952  1   30.408 ? 248 ASP   B N    1 
ATOM   4353 C  CA   . ASP   B 1 248 ? -2.81   -23.363 -5.419  1   32.787 ? 248 ASP   B CA   1 
ATOM   4354 C  C    . ASP   B 1 248 ? -3.518  -22.09  -5.875  1   31.971 ? 248 ASP   B C    1 
ATOM   4355 O  O    . ASP   B 1 248 ? -4.673  -22.143 -6.301  1   34.376 ? 248 ASP   B O    1 
ATOM   4356 C  CB   . ASP   B 1 248 ? -2.798  -23.493 -3.904  1   34.202 ? 248 ASP   B CB   1 
ATOM   4357 C  CG   . ASP   B 1 248 ? -2.389  -24.86  -3.373  1   35.98  ? 248 ASP   B CG   1 
ATOM   4358 O  OD1  . ASP   B 1 248 ? -2.326  -25.81  -4.186  1   37.067 ? 248 ASP   B OD1  1 
ATOM   4359 O  OD2  . ASP   B 1 248 ? -2.126  -24.964 -2.151  1   37.899 ? 248 ASP   B OD2  1 
ATOM   4360 N  N    . ILE   B 1 249 ? -2.806  -20.956 -5.797  1   31.719 ? 249 ILE   B N    1 
ATOM   4361 C  CA   . ILE   B 1 249 ? -3.361  -19.652 -6.134  1   31.743 ? 249 ILE   B CA   1 
ATOM   4362 C  C    . ILE   B 1 249 ? -3.756  -19.597 -7.615  1   30.83  ? 249 ILE   B C    1 
ATOM   4363 O  O    . ILE   B 1 249 ? -4.701  -18.895 -7.976  1   32.514 ? 249 ILE   B O    1 
ATOM   4364 C  CB   . ILE   B 1 249 ? -2.362  -18.542 -5.75   1   33.539 ? 249 ILE   B CB   1 
ATOM   4365 C  CG1  . ILE   B 1 249 ? -2.172  -18.448 -4.232  1   35.22  ? 249 ILE   B CG1  1 
ATOM   4366 C  CG2  . ILE   B 1 249 ? -2.769  -17.19  -6.337  1   35.204 ? 249 ILE   B CG2  1 
ATOM   4367 C  CD1  . ILE   B 1 249 ? -0.9    -17.733 -3.808  1   35.778 ? 249 ILE   B CD1  1 
ATOM   4368 N  N    . LEU   B 1 250 ? -3.036  -20.338 -8.47   1   28.007 ? 250 LEU   B N    1 
ATOM   4369 C  CA   . LEU   B 1 250 ? -3.309  -20.358 -9.898  1   27.421 ? 250 LEU   B CA   1 
ATOM   4370 C  C    . LEU   B 1 250 ? -4.414  -21.357 -10.267 1   29.131 ? 250 LEU   B C    1 
ATOM   4371 O  O    . LEU   B 1 250 ? -4.775  -21.45  -11.435 1   30.636 ? 250 LEU   B O    1 
ATOM   4372 C  CB   . LEU   B 1 250 ? -2.016  -20.694 -10.641 1   23.613 ? 250 LEU   B CB   1 
ATOM   4373 C  CG   . LEU   B 1 250 ? -0.933  -19.609 -10.707 1   22.436 ? 250 LEU   B CG   1 
ATOM   4374 C  CD1  . LEU   B 1 250 ? 0.382   -20.241 -11.127 1   21.844 ? 250 LEU   B CD1  1 
ATOM   4375 C  CD2  . LEU   B 1 250 ? -1.306  -18.51  -11.68  1   22.34  ? 250 LEU   B CD2  1 
ATOM   4376 N  N    . GLY   B 1 251 ? -4.943  -22.119 -9.3    1   30.363 ? 251 GLY   B N    1 
ATOM   4377 C  CA   . GLY   B 1 251 ? -5.857  -23.227 -9.575  1   29.958 ? 251 GLY   B CA   1 
ATOM   4378 C  C    . GLY   B 1 251 ? -7.07   -22.846 -10.432 1   28.576 ? 251 GLY   B C    1 
ATOM   4379 O  O    . GLY   B 1 251 ? -7.44   -23.573 -11.362 1   29.762 ? 251 GLY   B O    1 
ATOM   4380 N  N    . PRO   B 1 252 ? -7.756  -21.719 -10.132 1   26.929 ? 252 PRO   B N    1 
ATOM   4381 C  CA   . PRO   B 1 252 ? -8.855  -21.229 -10.961 1   29.499 ? 252 PRO   B CA   1 
ATOM   4382 C  C    . PRO   B 1 252 ? -8.554  -21.13  -12.453 1   28.844 ? 252 PRO   B C    1 
ATOM   4383 O  O    . PRO   B 1 252 ? -9.351  -21.561 -13.271 1   32.522 ? 252 PRO   B O    1 
ATOM   4384 C  CB   . PRO   B 1 252 ? -9.092  -19.836 -10.328 1   29.95  ? 252 PRO   B CB   1 
ATOM   4385 C  CG   . PRO   B 1 252 ? -8.78   -20.054 -8.876  1   31.647 ? 252 PRO   B CG   1 
ATOM   4386 C  CD   . PRO   B 1 252 ? -7.51   -20.86  -8.957  1   28.413 ? 252 PRO   B CD   1 
ATOM   4387 N  N    . LEU   B 1 253 ? -7.386  -20.57  -12.789 1   27.267 ? 253 LEU   B N    1 
ATOM   4388 C  CA   . LEU   B 1 253 ? -7.014  -20.336 -14.17  1   24.752 ? 253 LEU   B CA   1 
ATOM   4389 C  C    . LEU   B 1 253 ? -6.752  -21.681 -14.84  1   26.76  ? 253 LEU   B C    1 
ATOM   4390 O  O    . LEU   B 1 253 ? -7.106  -21.848 -16.005 1   27.625 ? 253 LEU   B O    1 
ATOM   4391 C  CB   . LEU   B 1 253 ? -5.814  -19.389 -14.231 1   24.963 ? 253 LEU   B CB   1 
ATOM   4392 C  CG   . LEU   B 1 253 ? -6.069  -17.964 -13.72  1   24.785 ? 253 LEU   B CG   1 
ATOM   4393 C  CD1  . LEU   B 1 253 ? -4.835  -17.128 -13.46  1   27.238 ? 253 LEU   B CD1  1 
ATOM   4394 C  CD2  . LEU   B 1 253 ? -6.971  -17.23  -14.71  1   27.044 ? 253 LEU   B CD2  1 
ATOM   4395 N  N    . SER   B 1 254 ? -6.172  -22.642 -14.105 1   24.272 ? 254 SER   B N    1 
ATOM   4396 C  CA   . SER   B 1 254 ? -5.967  -23.988 -14.62  1   25.656 ? 254 SER   B CA   1 
ATOM   4397 C  C    . SER   B 1 254 ? -7.296  -24.604 -15.043 1   26.912 ? 254 SER   B C    1 
ATOM   4398 O  O    . SER   B 1 254 ? -7.422  -25.178 -16.13  1   27.434 ? 254 SER   B O    1 
ATOM   4399 C  CB   . SER   B 1 254 ? -5.278  -24.861 -13.585 1   24.529 ? 254 SER   B CB   1 
ATOM   4400 O  OG   . SER   B 1 254 ? -5.177  -26.219 -14.011 1   27.272 ? 254 SER   B OG   1 
ATOM   4401 N  N    . ALA   B 1 255 ? -8.288  -24.48  -14.156 1   27.853 ? 255 ALA   B N    1 
ATOM   4402 C  CA   . ALA   B 1 255 ? -9.58   -25.114 -14.356 1   28.771 ? 255 ALA   B CA   1 
ATOM   4403 C  C    . ALA   B 1 255 ? -10.302 -24.469 -15.537 1   29.506 ? 255 ALA   B C    1 
ATOM   4404 O  O    . ALA   B 1 255 ? -10.933 -25.159 -16.341 1   29.996 ? 255 ALA   B O    1 
ATOM   4405 C  CB   . ALA   B 1 255 ? -10.394 -25.022 -13.085 1   30.392 ? 255 ALA   B CB   1 
ATOM   4406 N  N    . GLN   B 1 256 ? -10.2   -23.139 -15.64  1   29.657 ? 256 GLN   B N    1 
ATOM   4407 C  CA   . GLN   B 1 256 ? -10.945 -22.396 -16.642 1   31.067 ? 256 GLN   B CA   1 
ATOM   4408 C  C    . GLN   B 1 256 ? -10.421 -22.716 -18.039 1   30.571 ? 256 GLN   B C    1 
ATOM   4409 O  O    . GLN   B 1 256 ? -11.18  -22.71  -19.002 1   32.045 ? 256 GLN   B O    1 
ATOM   4410 C  CB   . GLN   B 1 256 ? -10.853 -20.901 -16.339 1   30.611 ? 256 GLN   B CB   1 
ATOM   4411 C  CG   . GLN   B 1 256 ? -11.502 -19.988 -17.373 1   32.793 ? 256 GLN   B CG   1 
ATOM   4412 C  CD   . GLN   B 1 256 ? -11.276 -18.525 -17.056 1   35.05  ? 256 GLN   B CD   1 
ATOM   4413 O  OE1  . GLN   B 1 256 ? -10.894 -18.154 -15.94  1   37.199 ? 256 GLN   B OE1  1 
ATOM   4414 N  NE2  . GLN   B 1 256 ? -11.504 -17.673 -18.044 1   37.202 ? 256 GLN   B NE2  1 
ATOM   4415 N  N    . THR   B 1 257 ? -9.114  -22.979 -18.146 1   28.254 ? 257 THR   B N    1 
ATOM   4416 C  CA   . THR   B 1 257 ? -8.445  -23.038 -19.435 1   28.418 ? 257 THR   B CA   1 
ATOM   4417 C  C    . THR   B 1 257 ? -8.137  -24.479 -19.826 1   29.05  ? 257 THR   B C    1 
ATOM   4418 O  O    . THR   B 1 257 ? -7.79   -24.732 -20.981 1   29.431 ? 257 THR   B O    1 
ATOM   4419 C  CB   . THR   B 1 257 ? -7.16   -22.203 -19.379 1   28.531 ? 257 THR   B CB   1 
ATOM   4420 O  OG1  . THR   B 1 257 ? -6.282  -22.722 -18.378 1   28.584 ? 257 THR   B OG1  1 
ATOM   4421 C  CG2  . THR   B 1 257 ? -7.423  -20.737 -19.079 1   27.219 ? 257 THR   B CG2  1 
ATOM   4422 N  N    . GLY   B 1 258 ? -8.19   -25.408 -18.862 1   28.697 ? 258 GLY   B N    1 
ATOM   4423 C  CA   . GLY   B 1 258 ? -7.861  -26.797 -19.129 1   30.73  ? 258 GLY   B CA   1 
ATOM   4424 C  C    . GLY   B 1 258 ? -6.355  -27.047 -19.172 1   31.502 ? 258 GLY   B C    1 
ATOM   4425 O  O    . GLY   B 1 258 ? -5.933  -28.109 -19.622 1   33.31  ? 258 GLY   B O    1 
ATOM   4426 N  N    . ILE   B 1 259 ? -5.561  -26.08  -18.684 1   32.301 ? 259 ILE   B N    1 
ATOM   4427 C  CA   . ILE   B 1 259 ? -4.115  -26.185 -18.633 1   33.002 ? 259 ILE   B CA   1 
ATOM   4428 C  C    . ILE   B 1 259 ? -3.732  -26.17  -17.159 1   33.341 ? 259 ILE   B C    1 
ATOM   4429 O  O    . ILE   B 1 259 ? -3.778  -25.129 -16.513 1   33.317 ? 259 ILE   B O    1 
ATOM   4430 C  CB   . ILE   B 1 259 ? -3.461  -25.024 -19.41  1   33.427 ? 259 ILE   B CB   1 
ATOM   4431 C  CG1  . ILE   B 1 259 ? -3.979  -24.953 -20.851 1   35.537 ? 259 ILE   B CG1  1 
ATOM   4432 C  CG2  . ILE   B 1 259 ? -1.938  -25.13  -19.374 1   33.885 ? 259 ILE   B CG2  1 
ATOM   4433 C  CD1  . ILE   B 1 259 ? -4.416  -23.574 -21.294 1   35.885 ? 259 ILE   B CD1  1 
ATOM   4434 N  N    . ALA   B 1 260 ? -3.392  -27.343 -16.622 1   32.525 ? 260 ALA   B N    1 
ATOM   4435 C  CA   . ALA   B 1 260 ? -2.928  -27.448 -15.25  1   31.435 ? 260 ALA   B CA   1 
ATOM   4436 C  C    . ALA   B 1 260 ? -1.705  -26.56  -15.077 1   29.687 ? 260 ALA   B C    1 
ATOM   4437 O  O    . ALA   B 1 260 ? -1.008  -26.278 -16.043 1   28.609 ? 260 ALA   B O    1 
ATOM   4438 C  CB   . ALA   B 1 260 ? -2.62   -28.883 -14.93  1   31.006 ? 260 ALA   B CB   1 
ATOM   4439 N  N    . VAL   B 1 261 ? -1.45   -26.095 -13.856 1   28.267 ? 261 VAL   B N    1 
ATOM   4440 C  CA   . VAL   B 1 261 ? -0.306  -25.232 -13.618 1   27.563 ? 261 VAL   B CA   1 
ATOM   4441 C  C    . VAL   B 1 261 ? 0.98    -25.905 -14.104 1   26.791 ? 261 VAL   B C    1 
ATOM   4442 O  O    . VAL   B 1 261 ? 1.777   -25.256 -14.76  1   24.463 ? 261 VAL   B O    1 
ATOM   4443 C  CB   . VAL   B 1 261 ? -0.201  -24.769 -12.154 1   26.334 ? 261 VAL   B CB   1 
ATOM   4444 C  CG1  . VAL   B 1 261 ? 1.098   -24.02  -11.899 1   26.695 ? 261 VAL   B CG1  1 
ATOM   4445 C  CG2  . VAL   B 1 261 ? -1.389  -23.899 -11.767 1   26.304 ? 261 VAL   B CG2  1 
ATOM   4446 N  N    . LEU   B 1 262 ? 1.197   -27.191 -13.809 1   27.477 ? 262 LEU   B N    1 
ATOM   4447 C  CA   . LEU   B 1 262 ? 2.424   -27.853 -14.241 1   28.388 ? 262 LEU   B CA   1 
ATOM   4448 C  C    . LEU   B 1 262 ? 2.491   -28.032 -15.763 1   29.503 ? 262 LEU   B C    1 
ATOM   4449 O  O    . LEU   B 1 262 ? 3.581   -28.098 -16.33  1   29.136 ? 262 LEU   B O    1 
ATOM   4450 C  CB   . LEU   B 1 262 ? 2.585   -29.166 -13.476 1   29.393 ? 262 LEU   B CB   1 
ATOM   4451 C  CG   . LEU   B 1 262 ? 2.906   -29     -11.988 1   30.283 ? 262 LEU   B CG   1 
ATOM   4452 C  CD1  . LEU   B 1 262 ? 2.863   -30.316 -11.245 1   30.73  ? 262 LEU   B CD1  1 
ATOM   4453 C  CD2  . LEU   B 1 262 ? 4.266   -28.347 -11.812 1   30.181 ? 262 LEU   B CD2  1 
ATOM   4454 N  N    . ASP   B 1 263 ? 1.326   -28.069 -16.424 1   27.564 ? 263 ASP   B N    1 
ATOM   4455 C  CA   . ASP   B 1 263 ? 1.199   -28.037 -17.876 1   27.676 ? 263 ASP   B CA   1 
ATOM   4456 C  C    . ASP   B 1 263 ? 1.717   -26.683 -18.389 1   25.361 ? 263 ASP   B C    1 
ATOM   4457 O  O    . ASP   B 1 263 ? 2.522   -26.596 -19.325 1   25.794 ? 263 ASP   B O    1 
ATOM   4458 C  CB   . ASP   B 1 263 ? -0.249  -28.419 -18.184 1   29.947 ? 263 ASP   B CB   1 
ATOM   4459 C  CG   . ASP   B 1 263 ? -0.7    -28.565 -19.628 1   31.447 ? 263 ASP   B CG   1 
ATOM   4460 O  OD1  . ASP   B 1 263 ? 0.129   -28.319 -20.522 1   33.833 ? 263 ASP   B OD1  1 
ATOM   4461 O  OD2  . ASP   B 1 263 ? -1.886  -28.935 -19.838 1   35.073 ? 263 ASP   B OD2  1 
ATOM   4462 N  N    . MET   B 1 264 ? 1.246   -25.6   -17.765 1   24.115 ? 264 MET   B N    1 
ATOM   4463 C  CA   . MET   B 1 264 ? 1.685   -24.267 -18.142 1   22.282 ? 264 MET   B CA   1 
ATOM   4464 C  C    . MET   B 1 264 ? 3.165   -24.094 -17.802 1   22.169 ? 264 MET   B C    1 
ATOM   4465 O  O    . MET   B 1 264 ? 3.874   -23.41  -18.522 1   22.252 ? 264 MET   B O    1 
ATOM   4466 C  CB   . MET   B 1 264 ? 0.842   -23.184 -17.457 1   21.735 ? 264 MET   B CB   1 
ATOM   4467 C  CG   . MET   B 1 264 ? 1.065   -21.805 -18.044 1   21.324 ? 264 MET   B CG   1 
ATOM   4468 S  SD   . MET   B 1 264 ? 0.462   -21.661 -19.74  1   20.356 ? 264 MET   B SD   1 
ATOM   4469 C  CE   . MET   B 1 264 ? -1.245  -21.185 -19.421 1   21.555 ? 264 MET   B CE   1 
ATOM   4470 N  N    . CYS   B 1 265 ? 3.635   -24.725 -16.72  1   22.841 ? 265 CYS   B N    1 
ATOM   4471 C  CA   . CYS   B 1 265 ? 5.054   -24.693 -16.391 1   23.281 ? 265 CYS   B CA   1 
ATOM   4472 C  C    . CYS   B 1 265 ? 5.881   -25.321 -17.51  1   23.246 ? 265 CYS   B C    1 
ATOM   4473 O  O    . CYS   B 1 265 ? 6.962   -24.831 -17.802 1   23.336 ? 265 CYS   B O    1 
ATOM   4474 C  CB   . CYS   B 1 265 ? 5.373   -25.414 -15.089 1   24.419 ? 265 CYS   B CB   1 
ATOM   4475 S  SG   . CYS   B 1 265 ? 4.884   -24.458 -13.631 1   25.558 ? 265 CYS   B SG   1 
ATOM   4476 N  N    . ALA   B 1 266 ? 5.38    -26.394 -18.135 1   23.476 ? 266 ALA   B N    1 
ATOM   4477 C  CA   . ALA   B 1 266 ? 6.076   -26.993 -19.262 1   23.739 ? 266 ALA   B CA   1 
ATOM   4478 C  C    . ALA   B 1 266 ? 6.13    -26.022 -20.445 1   22.671 ? 266 ALA   B C    1 
ATOM   4479 O  O    . ALA   B 1 266 ? 7.132   -25.98  -21.147 1   25.197 ? 266 ALA   B O    1 
ATOM   4480 C  CB   . ALA   B 1 266 ? 5.444   -28.311 -19.644 1   24.752 ? 266 ALA   B CB   1 
ATOM   4481 N  N    . SER   B 1 267 ? 5.071   -25.228 -20.655 1   21.594 ? 267 SER   B N    1 
ATOM   4482 C  CA   . SER   B 1 267 ? 5.119   -24.175 -21.661 1   20.767 ? 267 SER   B CA   1 
ATOM   4483 C  C    . SER   B 1 267 ? 6.204   -23.151 -21.331 1   19.445 ? 267 SER   B C    1 
ATOM   4484 O  O    . SER   B 1 267 ? 6.996   -22.758 -22.19  1   19.931 ? 267 SER   B O    1 
ATOM   4485 C  CB   . SER   B 1 267 ? 3.781   -23.494 -21.823 1   21.158 ? 267 SER   B CB   1 
ATOM   4486 O  OG   . SER   B 1 267 ? 2.86    -24.291 -22.55  1   21.394 ? 267 SER   B OG   1 
ATOM   4487 N  N    . LEU   B 1 268 ? 6.214   -22.696 -20.076 1   19.216 ? 268 LEU   B N    1 
ATOM   4488 C  CA   . LEU   B 1 268 ? 7.165   -21.682 -19.657 1   19.329 ? 268 LEU   B CA   1 
ATOM   4489 C  C    . LEU   B 1 268 ? 8.588   -22.226 -19.771 1   21.089 ? 268 LEU   B C    1 
ATOM   4490 O  O    . LEU   B 1 268 ? 9.479   -21.524 -20.223 1   20.026 ? 268 LEU   B O    1 
ATOM   4491 C  CB   . LEU   B 1 268 ? 6.827   -21.199 -18.246 1   18.395 ? 268 LEU   B CB   1 
ATOM   4492 C  CG   . LEU   B 1 268 ? 7.805   -20.192 -17.634 1   18.131 ? 268 LEU   B CG   1 
ATOM   4493 C  CD1  . LEU   B 1 268 ? 8.019   -19.005 -18.542 1   17.732 ? 268 LEU   B CD1  1 
ATOM   4494 C  CD2  . LEU   B 1 268 ? 7.288   -19.725 -16.29  1   18.396 ? 268 LEU   B CD2  1 
ATOM   4495 N  N    . LYS   B 1 269 ? 8.804   -23.482 -19.366 1   22.751 ? 269 LYS   B N    1 
ATOM   4496 C  CA   . LYS   B 1 269 ? 10.101  -24.119 -19.495 1   24.802 ? 269 LYS   B CA   1 
ATOM   4497 C  C    . LYS   B 1 269 ? 10.585  -24.036 -20.938 1   24.284 ? 269 LYS   B C    1 
ATOM   4498 O  O    . LYS   B 1 269 ? 11.737  -23.71  -21.183 1   25.184 ? 269 LYS   B O    1 
ATOM   4499 C  CB   . LYS   B 1 269 ? 9.969   -25.553 -18.968 1   26.813 ? 269 LYS   B CB   1 
ATOM   4500 C  CG   . LYS   B 1 269 ? 11.111  -26.511 -19.21  1   29.755 ? 269 LYS   B CG   1 
ATOM   4501 C  CD   . LYS   B 1 269 ? 10.844  -27.843 -18.517 1   32.872 ? 269 LYS   B CD   1 
ATOM   4502 C  CE   . LYS   B 1 269 ? 11.56   -28.988 -19.129 1   35.703 ? 269 LYS   B CE   1 
ATOM   4503 N  NZ   . LYS   B 1 269 ? 11.116  -30.25  -18.529 1   36.869 ? 269 LYS   B NZ   1 
ATOM   4504 N  N    . GLU   B 1 270 ? 9.699   -24.33  -21.895 1   23.05  ? 270 GLU   B N    1 
ATOM   4505 C  CA   . GLU   B 1 270 ? 10.084  -24.333 -23.295 1   22.924 ? 270 GLU   B CA   1 
ATOM   4506 C  C    . GLU   B 1 270 ? 10.397  -22.917 -23.78  1   22.306 ? 270 GLU   B C    1 
ATOM   4507 O  O    . GLU   B 1 270 ? 11.344  -22.731 -24.542 1   24.26  ? 270 GLU   B O    1 
ATOM   4508 C  CB   . GLU   B 1 270 ? 9.033   -25.052 -24.143 1   24.055 ? 270 GLU   B CB   1 
ATOM   4509 C  CG   . GLU   B 1 270 ? 8.927   -26.549 -23.838 1   26.088 ? 270 GLU   B CG   1 
ATOM   4510 C  CD   . GLU   B 1 270 ? 10.209  -27.371 -23.898 1   27.536 ? 270 GLU   B CD   1 
ATOM   4511 O  OE1  . GLU   B 1 270 ? 10.943  -27.204 -24.891 1   30.454 ? 270 GLU   B OE1  1 
ATOM   4512 O  OE2  . GLU   B 1 270 ? 10.475  -28.183 -22.976 1   28.799 ? 270 GLU   B OE2  1 
ATOM   4513 N  N    . LEU   B 1 271 ? 9.616   -21.924 -23.339 1   21.157 ? 271 LEU   B N    1 
ATOM   4514 C  CA   . LEU   B 1 271 ? 9.876   -20.535 -23.696 1   20.45  ? 271 LEU   B CA   1 
ATOM   4515 C  C    . LEU   B 1 271 ? 11.249  -20.089 -23.185 1   22.272 ? 271 LEU   B C    1 
ATOM   4516 O  O    . LEU   B 1 271 ? 11.967  -19.366 -23.87  1   24.014 ? 271 LEU   B O    1 
ATOM   4517 C  CB   . LEU   B 1 271 ? 8.773   -19.629 -23.15  1   19.55  ? 271 LEU   B CB   1 
ATOM   4518 C  CG   . LEU   B 1 271 ? 7.409   -19.747 -23.83  1   20.002 ? 271 LEU   B CG   1 
ATOM   4519 C  CD1  . LEU   B 1 271 ? 6.305   -19.121 -23.016 1   19.706 ? 271 LEU   B CD1  1 
ATOM   4520 C  CD2  . LEU   B 1 271 ? 7.452   -19.115 -25.193 1   21.031 ? 271 LEU   B CD2  1 
ATOM   4521 N  N    . LEU   B 1 272 ? 11.597  -20.486 -21.959 1   22.485 ? 272 LEU   B N    1 
ATOM   4522 C  CA   . LEU   B 1 272 ? 12.876  -20.105 -21.374 1   23.009 ? 272 LEU   B CA   1 
ATOM   4523 C  C    . LEU   B 1 272 ? 14.03   -20.741 -22.145 1   24.734 ? 272 LEU   B C    1 
ATOM   4524 O  O    . LEU   B 1 272 ? 15.054  -20.096 -22.363 1   26.986 ? 272 LEU   B O    1 
ATOM   4525 C  CB   . LEU   B 1 272 ? 12.931  -20.472 -19.893 1   22.892 ? 272 LEU   B CB   1 
ATOM   4526 C  CG   . LEU   B 1 272 ? 12.007  -19.654 -18.989 1   22.584 ? 272 LEU   B CG   1 
ATOM   4527 C  CD1  . LEU   B 1 272 ? 11.957  -20.229 -17.589 1   22.925 ? 272 LEU   B CD1  1 
ATOM   4528 C  CD2  . LEU   B 1 272 ? 12.407  -18.189 -18.975 1   22.827 ? 272 LEU   B CD2  1 
ATOM   4529 N  N    . GLN   B 1 273 ? 13.828  -21.989 -22.578 1   26.599 ? 273 GLN   B N    1 
ATOM   4530 C  CA   . GLN   B 1 273 ? 14.885  -22.75  -23.221 1   28.264 ? 273 GLN   B CA   1 
ATOM   4531 C  C    . GLN   B 1 273 ? 15.048  -22.335 -24.684 1   29.9   ? 273 GLN   B C    1 
ATOM   4532 O  O    . GLN   B 1 273 ? 16.16   -22.418 -25.204 1   32.563 ? 273 GLN   B O    1 
ATOM   4533 C  CB   . GLN   B 1 273 ? 14.645  -24.25  -23.022 1   28.79  ? 273 GLN   B CB   1 
ATOM   4534 C  CG   . GLN   B 1 273 ? 14.833  -24.71  -21.58  1   29.061 ? 273 GLN   B CG   1 
ATOM   4535 C  CD   . GLN   B 1 273 ? 14.523  -26.172 -21.331 1   30.186 ? 273 GLN   B CD   1 
ATOM   4536 O  OE1  . GLN   B 1 273 ? 14.059  -26.919 -22.204 1   31.229 ? 273 GLN   B OE1  1 
ATOM   4537 N  NE2  . GLN   B 1 273 ? 14.753  -26.593 -20.097 1   31.08  ? 273 GLN   B NE2  1 
ATOM   4538 N  N    . ASN   B 1 274 ? 13.962  -21.908 -25.347 1   29.368 ? 274 ASN   B N    1 
ATOM   4539 C  CA   . ASN   B 1 274 ? 13.952  -21.786 -26.801 1   30.116 ? 274 ASN   B CA   1 
ATOM   4540 C  C    . ASN   B 1 274 ? 13.664  -20.36  -27.275 1   30.304 ? 274 ASN   B C    1 
ATOM   4541 O  O    . ASN   B 1 274 ? 13.873  -20.061 -28.447 1   32.749 ? 274 ASN   B O    1 
ATOM   4542 C  CB   . ASN   B 1 274 ? 12.95   -22.754 -27.428 1   31.854 ? 274 ASN   B CB   1 
ATOM   4543 C  CG   . ASN   B 1 274 ? 13.352  -24.196 -27.221 1   32.379 ? 274 ASN   B CG   1 
ATOM   4544 O  OD1  . ASN   B 1 274 ? 14.228  -24.701 -27.932 1   36.823 ? 274 ASN   B OD1  1 
ATOM   4545 N  ND2  . ASN   B 1 274 ? 12.734  -24.881 -26.27  1   34.066 ? 274 ASN   B ND2  1 
ATOM   4546 N  N    . GLY   B 1 275 ? 13.166  -19.481 -26.4   1   28.699 ? 275 GLY   B N    1 
ATOM   4547 C  CA   . GLY   B 1 275 ? 12.717  -18.165 -26.829 1   28.315 ? 275 GLY   B CA   1 
ATOM   4548 C  C    . GLY   B 1 275 ? 11.341  -18.238 -27.494 1   27.94  ? 275 GLY   B C    1 
ATOM   4549 O  O    . GLY   B 1 275 ? 10.692  -19.279 -27.451 1   27.867 ? 275 GLY   B O    1 
ATOM   4550 N  N    . MET   B 1 276 ? 10.923  -17.137 -28.131 1   28.433 ? 276 MET   B N    1 
ATOM   4551 C  CA   . MET   B 1 276 ? 9.607   -17.035 -28.749 1   29.251 ? 276 MET   B CA   1 
ATOM   4552 C  C    . MET   B 1 276 ? 9.637   -17.29  -30.256 1   30.47  ? 276 MET   B C    1 
ATOM   4553 O  O    . MET   B 1 276 ? 8.584   -17.301 -30.896 1   30.025 ? 276 MET   B O    1 
ATOM   4554 C  CB   . MET   B 1 276 ? 8.998   -15.644 -28.539 1   29.993 ? 276 MET   B CB   1 
ATOM   4555 C  CG   . MET   B 1 276 ? 8.572   -15.391 -27.122 1   29.323 ? 276 MET   B CG   1 
ATOM   4556 S  SD   . MET   B 1 276 ? 7.501   -13.939 -27.038 1   27.158 ? 276 MET   B SD   1 
ATOM   4557 C  CE   . MET   B 1 276 ? 7.498   -13.701 -25.257 1   27.183 ? 276 MET   B CE   1 
ATOM   4558 N  N    . ASN   B 1 277 ? 10.831  -17.484 -30.829 1   31.885 ? 277 ASN   B N    1 
ATOM   4559 C  CA   . ASN   B 1 277 ? 10.973  -17.779 -32.25  1   34.178 ? 277 ASN   B CA   1 
ATOM   4560 C  C    . ASN   B 1 277 ? 10.26   -16.708 -33.079 1   32.558 ? 277 ASN   B C    1 
ATOM   4561 O  O    . ASN   B 1 277 ? 9.569   -17.019 -34.046 1   34.993 ? 277 ASN   B O    1 
ATOM   4562 C  CB   . ASN   B 1 277 ? 10.473  -19.179 -32.597 1   38.266 ? 277 ASN   B CB   1 
ATOM   4563 C  CG   . ASN   B 1 277 ? 11.392  -20.269 -32.095 1   42.538 ? 277 ASN   B CG   1 
ATOM   4564 O  OD1  . ASN   B 1 277 ? 12.477  -20.474 -32.652 1   47.436 ? 277 ASN   B OD1  1 
ATOM   4565 N  ND2  . ASN   B 1 277 ? 10.975  -20.986 -31.06  1   44.258 ? 277 ASN   B ND2  1 
ATOM   4566 N  N    . GLY   B 1 278 ? 10.422  -15.438 -32.69  1   31.711 ? 278 GLY   B N    1 
ATOM   4567 C  CA   . GLY   B 1 278 ? 9.936   -14.316 -33.476 1   32.317 ? 278 GLY   B CA   1 
ATOM   4568 C  C    . GLY   B 1 278 ? 8.468   -13.975 -33.217 1   31.55  ? 278 GLY   B C    1 
ATOM   4569 O  O    . GLY   B 1 278 ? 7.946   -13.048 -33.832 1   33.26  ? 278 GLY   B O    1 
ATOM   4570 N  N    . ARG   B 1 279 ? 7.806   -14.708 -32.311 1   29.688 ? 279 ARG   B N    1 
ATOM   4571 C  CA   . ARG   B 1 279 ? 6.399   -14.476 -32.026 1   27.539 ? 279 ARG   B CA   1 
ATOM   4572 C  C    . ARG   B 1 279 ? 6.254   -13.568 -30.81  1   24.896 ? 279 ARG   B C    1 
ATOM   4573 O  O    . ARG   B 1 279 ? 7.238   -13.241 -30.157 1   26.284 ? 279 ARG   B O    1 
ATOM   4574 C  CB   . ARG   B 1 279 ? 5.695   -15.816 -31.805 1   28.957 ? 279 ARG   B CB   1 
ATOM   4575 C  CG   . ARG   B 1 279 ? 5.573   -16.618 -33.09  1   31.491 ? 279 ARG   B CG   1 
ATOM   4576 C  CD   . ARG   B 1 279 ? 5.083   -18.021 -32.84  1   33.018 ? 279 ARG   B CD   1 
ATOM   4577 N  NE   . ARG   B 1 279 ? 6.127   -18.832 -32.205 1   35.842 ? 279 ARG   B NE   1 
ATOM   4578 C  CZ   . ARG   B 1 279 ? 6.112   -20.157 -32.102 1   38.988 ? 279 ARG   B CZ   1 
ATOM   4579 N  NH1  . ARG   B 1 279 ? 5.13    -20.862 -32.642 1   39.613 ? 279 ARG   B NH1  1 
ATOM   4580 N  NH2  . ARG   B 1 279 ? 7.089   -20.778 -31.461 1   40.209 ? 279 ARG   B NH2  1 
ATOM   4581 N  N    . THR   B 1 280 ? 5.012   -13.16  -30.524 1   21.677 ? 280 THR   B N    1 
ATOM   4582 C  CA   . THR   B 1 280 ? 4.709   -12.368 -29.344 1   20.493 ? 280 THR   B CA   1 
ATOM   4583 C  C    . THR   B 1 280 ? 3.593   -13.047 -28.559 1   18.777 ? 280 THR   B C    1 
ATOM   4584 O  O    . THR   B 1 280 ? 2.899   -13.919 -29.081 1   19.714 ? 280 THR   B O    1 
ATOM   4585 C  CB   . THR   B 1 280 ? 4.309   -10.937 -29.713 1   21.899 ? 280 THR   B CB   1 
ATOM   4586 O  OG1  . THR   B 1 280 ? 3.2     -11.02  -30.611 1   23.045 ? 280 THR   B OG1  1 
ATOM   4587 C  CG2  . THR   B 1 280 ? 5.454   -10.161 -30.335 1   23.168 ? 280 THR   B CG2  1 
ATOM   4588 N  N    . ILE   B 1 281 ? 3.45    -12.619 -27.3   1   17.012 ? 281 ILE   B N    1 
ATOM   4589 C  CA   . ILE   B 1 281 ? 2.376   -13.049 -26.421 1   16.399 ? 281 ILE   B CA   1 
ATOM   4590 C  C    . ILE   B 1 281 ? 1.716   -11.789 -25.876 1   16.468 ? 281 ILE   B C    1 
ATOM   4591 O  O    . ILE   B 1 281 ? 2.394   -10.966 -25.274 1   16.32  ? 281 ILE   B O    1 
ATOM   4592 C  CB   . ILE   B 1 281 ? 2.913   -13.939 -25.282 1   16.172 ? 281 ILE   B CB   1 
ATOM   4593 C  CG1  . ILE   B 1 281 ? 3.592   -15.193 -25.827 1   16.998 ? 281 ILE   B CG1  1 
ATOM   4594 C  CG2  . ILE   B 1 281 ? 1.804   -14.29  -24.286 1   16.262 ? 281 ILE   B CG2  1 
ATOM   4595 C  CD1  . ILE   B 1 281 ? 4.276   -16.046 -24.776 1   17.073 ? 281 ILE   B CD1  1 
ATOM   4596 N  N    . LEU   B 1 282 ? 0.41    -11.621 -26.113 1   17.054 ? 282 LEU   B N    1 
ATOM   4597 C  CA   . LEU   B 1 282 ? -0.287  -10.406 -25.708 1   17.368 ? 282 LEU   B CA   1 
ATOM   4598 C  C    . LEU   B 1 282 ? 0.507   -9.167  -26.112 1   19.006 ? 282 LEU   B C    1 
ATOM   4599 O  O    . LEU   B 1 282 ? 0.613   -8.202  -25.352 1   21.308 ? 282 LEU   B O    1 
ATOM   4600 C  CB   . LEU   B 1 282 ? -0.573  -10.411 -24.208 1   17.389 ? 282 LEU   B CB   1 
ATOM   4601 C  CG   . LEU   B 1 282 ? -1.724  -11.303 -23.752 1   17.503 ? 282 LEU   B CG   1 
ATOM   4602 C  CD1  . LEU   B 1 282 ? -1.805  -11.372 -22.238 1   17.895 ? 282 LEU   B CD1  1 
ATOM   4603 C  CD2  . LEU   B 1 282 ? -3.024  -10.804 -24.331 1   17.632 ? 282 LEU   B CD2  1 
ATOM   4604 N  N    . GLY   B 1 283 ? 1.041   -9.204  -27.335 1   19.691 ? 283 GLY   B N    1 
ATOM   4605 C  CA   . GLY   B 1 283 ? 1.743   -8.069  -27.91  1   20.773 ? 283 GLY   B CA   1 
ATOM   4606 C  C    . GLY   B 1 283 ? 3.131   -7.79   -27.325 1   21.107 ? 283 GLY   B C    1 
ATOM   4607 O  O    . GLY   B 1 283 ? 3.691   -6.739  -27.614 1   24.127 ? 283 GLY   B O    1 
ATOM   4608 N  N    A SER   B 1 284 ? 3.668   -8.718  -26.522 0.5 19.425 ? 284 SER   B N    1 
ATOM   4609 N  N    B SER   B 1 284 ? 3.668   -8.733  -26.533 0.5 20.352 ? 284 SER   B N    1 
ATOM   4610 C  CA   A SER   B 1 284 ? 4.963   -8.553  -25.88  0.5 18.874 ? 284 SER   B CA   1 
ATOM   4611 C  CA   B SER   B 1 284 ? 4.96    -8.586  -25.878 0.5 20.293 ? 284 SER   B CA   1 
ATOM   4612 C  C    A SER   B 1 284 ? 5.954   -9.556  -26.461 0.5 18.593 ? 284 SER   B C    1 
ATOM   4613 C  C    B SER   B 1 284 ? 5.968   -9.578  -26.453 0.5 19.271 ? 284 SER   B C    1 
ATOM   4614 O  O    A SER   B 1 284 ? 5.598   -10.708 -26.702 0.5 18.844 ? 284 SER   B O    1 
ATOM   4615 O  O    B SER   B 1 284 ? 5.646   -10.739 -26.693 0.5 19.247 ? 284 SER   B O    1 
ATOM   4616 C  CB   A SER   B 1 284 ? 4.847   -8.724  -24.381 0.5 18.13  ? 284 SER   B CB   1 
ATOM   4617 C  CB   B SER   B 1 284 ? 4.845   -8.784  -24.386 0.5 20.5   ? 284 SER   B CB   1 
ATOM   4618 O  OG   A SER   B 1 284 ? 6.098   -8.527  -23.742 0.5 17.472 ? 284 SER   B OG   1 
ATOM   4619 O  OG   B SER   B 1 284 ? 4.001   -7.81   -23.788 0.5 21.914 ? 284 SER   B OG   1 
ATOM   4620 N  N    . ALA   B 1 285 ? 7.216   -9.122  -26.601 1   19     ? 285 ALA   B N    1 
ATOM   4621 C  CA   . ALA   B 1 285 ? 8.319   -9.998  -26.986 1   19.136 ? 285 ALA   B CA   1 
ATOM   4622 C  C    . ALA   B 1 285 ? 9.123   -10.446 -25.763 1   19.198 ? 285 ALA   B C    1 
ATOM   4623 O  O    . ALA   B 1 285 ? 10.116  -11.154 -25.893 1   22.388 ? 285 ALA   B O    1 
ATOM   4624 C  CB   . ALA   B 1 285 ? 9.207   -9.29   -27.988 1   20.34  ? 285 ALA   B CB   1 
ATOM   4625 N  N    . LEU   B 1 286 ? 8.679   -10.055 -24.567 1   17.672 ? 286 LEU   B N    1 
ATOM   4626 C  CA   . LEU   B 1 286 ? 9.278   -10.471 -23.311 1   18.422 ? 286 LEU   B CA   1 
ATOM   4627 C  C    . LEU   B 1 286 ? 8.197   -11.137 -22.473 1   16.929 ? 286 LEU   B C    1 
ATOM   4628 O  O    . LEU   B 1 286 ? 7.006   -10.907 -22.679 1   16.993 ? 286 LEU   B O    1 
ATOM   4629 C  CB   . LEU   B 1 286 ? 9.827   -9.283  -22.523 1   20.355 ? 286 LEU   B CB   1 
ATOM   4630 C  CG   . LEU   B 1 286 ? 10.898  -8.413  -23.168 1   22.903 ? 286 LEU   B CG   1 
ATOM   4631 C  CD1  . LEU   B 1 286 ? 11.016  -7.15   -22.316 1   23.66  ? 286 LEU   B CD1  1 
ATOM   4632 C  CD2  . LEU   B 1 286 ? 12.195  -9.195  -23.237 1   24.368 ? 286 LEU   B CD2  1 
ATOM   4633 N  N    . LEU   B 1 287 ? 8.629   -11.923 -21.493 1   15.213 ? 287 LEU   B N    1 
ATOM   4634 C  CA   . LEU   B 1 287 ? 7.696   -12.55  -20.577 1   15.941 ? 287 LEU   B CA   1 
ATOM   4635 C  C    . LEU   B 1 287 ? 7.391   -11.565 -19.454 1   16.05  ? 287 LEU   B C    1 
ATOM   4636 O  O    . LEU   B 1 287 ? 8.265   -11.188 -18.687 1   19.388 ? 287 LEU   B O    1 
ATOM   4637 C  CB   . LEU   B 1 287 ? 8.281   -13.872 -20.085 1   16.462 ? 287 LEU   B CB   1 
ATOM   4638 C  CG   . LEU   B 1 287 ? 8.635   -14.882 -21.182 1   17.561 ? 287 LEU   B CG   1 
ATOM   4639 C  CD1  . LEU   B 1 287 ? 9.248   -16.139 -20.596 1   19.27  ? 287 LEU   B CD1  1 
ATOM   4640 C  CD2  . LEU   B 1 287 ? 7.444   -15.257 -22.033 1   18.858 ? 287 LEU   B CD2  1 
ATOM   4641 N  N    . GLU   B 1 288 ? 6.129   -11.148 -19.366 1   14.683 ? 288 GLU   B N    1 
ATOM   4642 C  CA   . GLU   B 1 288 ? 5.715   -10.119 -18.433 1   14.978 ? 288 GLU   B CA   1 
ATOM   4643 C  C    . GLU   B 1 288 ? 5.464   -10.705 -17.048 1   13.399 ? 288 GLU   B C    1 
ATOM   4644 O  O    . GLU   B 1 288 ? 4.766   -11.703 -16.924 1   13.155 ? 288 GLU   B O    1 
ATOM   4645 C  CB   . GLU   B 1 288 ? 4.421   -9.523  -18.978 1   16.839 ? 288 GLU   B CB   1 
ATOM   4646 C  CG   . GLU   B 1 288 ? 3.732   -8.543  -18.042 1   20.024 ? 288 GLU   B CG   1 
ATOM   4647 C  CD   . GLU   B 1 288 ? 4.495   -7.254  -17.866 1   23.236 ? 288 GLU   B CD   1 
ATOM   4648 O  OE1  . GLU   B 1 288 ? 4.663   -6.866  -16.682 1   23.727 ? 288 GLU   B OE1  1 
ATOM   4649 O  OE2  . GLU   B 1 288 ? 4.935   -6.68   -18.901 1   27.391 ? 288 GLU   B OE2  1 
ATOM   4650 N  N    . ASP   B 1 289 ? 5.976   -10.032 -16.005 1   12.748 ? 289 ASP   B N    1 
ATOM   4651 C  CA   . ASP   B 1 289 ? 5.885   -10.559 -14.652 1   12.688 ? 289 ASP   B CA   1 
ATOM   4652 C  C    . ASP   B 1 289 ? 5.292   -9.56   -13.659 1   12.491 ? 289 ASP   B C    1 
ATOM   4653 O  O    . ASP   B 1 289 ? 5.423   -9.787  -12.467 1   13.475 ? 289 ASP   B O    1 
ATOM   4654 C  CB   . ASP   B 1 289 ? 7.234   -11.064 -14.143 1   13.032 ? 289 ASP   B CB   1 
ATOM   4655 C  CG   . ASP   B 1 289 ? 8.241   -10.009 -13.712 1   13.683 ? 289 ASP   B CG   1 
ATOM   4656 O  OD1  . ASP   B 1 289 ? 8.073   -8.829  -14.085 1   14.082 ? 289 ASP   B OD1  1 
ATOM   4657 O  OD2  . ASP   B 1 289 ? 9.195   -10.393 -12.999 1   14.872 ? 289 ASP   B OD2  1 
ATOM   4658 N  N    . GLU   B 1 290 ? 4.56    -8.538  -14.121 1   13.057 ? 290 GLU   B N    1 
ATOM   4659 C  CA   . GLU   B 1 290 ? 3.945   -7.582  -13.204 1   13.859 ? 290 GLU   B CA   1 
ATOM   4660 C  C    . GLU   B 1 290 ? 2.411   -7.633  -13.253 1   14.356 ? 290 GLU   B C    1 
ATOM   4661 O  O    . GLU   B 1 290 ? 1.751   -6.638  -12.938 1   16.117 ? 290 GLU   B O    1 
ATOM   4662 C  CB   . GLU   B 1 290 ? 4.53    -6.172  -13.351 1   15.387 ? 290 GLU   B CB   1 
ATOM   4663 C  CG   . GLU   B 1 290 ? 6.021   -6.116  -13.02  1   16.094 ? 290 GLU   B CG   1 
ATOM   4664 C  CD   . GLU   B 1 290 ? 6.593   -4.766  -12.631 1   15.826 ? 290 GLU   B CD   1 
ATOM   4665 O  OE1  . GLU   B 1 290 ? 5.855   -3.763  -12.702 1   16.147 ? 290 GLU   B OE1  1 
ATOM   4666 O  OE2  . GLU   B 1 290 ? 7.79    -4.702  -12.24  1   16.241 ? 290 GLU   B OE2  1 
ATOM   4667 N  N    . PHE   B 1 291 ? 1.853   -8.816  -13.531 1   13.862 ? 291 PHE   B N    1 
ATOM   4668 C  CA   . PHE   B 1 291 ? 0.456   -9.121  -13.24  1   14.364 ? 291 PHE   B CA   1 
ATOM   4669 C  C    . PHE   B 1 291 ? 0.394   -10.3   -12.278 1   14.074 ? 291 PHE   B C    1 
ATOM   4670 O  O    . PHE   B 1 291 ? 0.919   -11.37  -12.582 1   14.643 ? 291 PHE   B O    1 
ATOM   4671 C  CB   . PHE   B 1 291 ? -0.337  -9.543  -14.476 1   15.416 ? 291 PHE   B CB   1 
ATOM   4672 C  CG   . PHE   B 1 291 ? -0.476  -8.479  -15.542 1   16.184 ? 291 PHE   B CG   1 
ATOM   4673 C  CD1  . PHE   B 1 291 ? -1.499  -7.542  -15.479 1   17.039 ? 291 PHE   B CD1  1 
ATOM   4674 C  CD2  . PHE   B 1 291 ? 0.39    -8.442  -16.622 1   16.876 ? 291 PHE   B CD2  1 
ATOM   4675 C  CE1  . PHE   B 1 291 ? -1.652  -6.593  -16.474 1   18.328 ? 291 PHE   B CE1  1 
ATOM   4676 C  CE2  . PHE   B 1 291 ? 0.226   -7.492  -17.617 1   18.342 ? 291 PHE   B CE2  1 
ATOM   4677 C  CZ   . PHE   B 1 291 ? -0.793  -6.58   -17.543 1   18.432 ? 291 PHE   B CZ   1 
ATOM   4678 N  N    . THR   B 1 292 ? -0.29   -10.111 -11.144 1   14.455 ? 292 THR   B N    1 
ATOM   4679 C  CA   . THR   B 1 292 ? -0.533  -11.217 -10.233 1   15.069 ? 292 THR   B CA   1 
ATOM   4680 C  C    . THR   B 1 292 ? -1.69   -12.069 -10.75  1   15.368 ? 292 THR   B C    1 
ATOM   4681 O  O    . THR   B 1 292 ? -2.487  -11.649 -11.596 1   15.706 ? 292 THR   B O    1 
ATOM   4682 C  CB   . THR   B 1 292 ? -0.858  -10.717 -8.83   1   16.272 ? 292 THR   B CB   1 
ATOM   4683 O  OG1  . THR   B 1 292 ? -2.151  -10.12  -8.91   1   17.55  ? 292 THR   B OG1  1 
ATOM   4684 C  CG2  . THR   B 1 292 ? 0.208   -9.783  -8.289  1   16.094 ? 292 THR   B CG2  1 
ATOM   4685 N  N    . PRO   B 1 293 ? -1.845  -13.294 -10.214 1   16.227 ? 293 PRO   B N    1 
ATOM   4686 C  CA   . PRO   B 1 293 ? -3.045  -14.079 -10.505 1   16.868 ? 293 PRO   B CA   1 
ATOM   4687 C  C    . PRO   B 1 293 ? -4.34   -13.311 -10.248 1   18.405 ? 293 PRO   B C    1 
ATOM   4688 O  O    . PRO   B 1 293 ? -5.265  -13.398 -11.052 1   19.474 ? 293 PRO   B O    1 
ATOM   4689 C  CB   . PRO   B 1 293 ? -2.878  -15.298 -9.601  1   17.651 ? 293 PRO   B CB   1 
ATOM   4690 C  CG   . PRO   B 1 293 ? -1.379  -15.432 -9.449  1   17.353 ? 293 PRO   B CG   1 
ATOM   4691 C  CD   . PRO   B 1 293 ? -0.847  -14.014 -9.402  1   16.783 ? 293 PRO   B CD   1 
ATOM   4692 N  N    . PHE   B 1 294 ? -4.39   -12.554 -9.147  1   19.672 ? 294 PHE   B N    1 
ATOM   4693 C  CA   . PHE   B 1 294 ? -5.578  -11.797 -8.805  1   21.698 ? 294 PHE   B CA   1 
ATOM   4694 C  C    . PHE   B 1 294 ? -5.823  -10.707 -9.847  1   20.909 ? 294 PHE   B C    1 
ATOM   4695 O  O    . PHE   B 1 294 ? -6.968  -10.468 -10.222 1   22.871 ? 294 PHE   B O    1 
ATOM   4696 C  CB   . PHE   B 1 294 ? -5.526  -11.191 -7.399  1   25.075 ? 294 PHE   B CB   1 
ATOM   4697 C  CG   . PHE   B 1 294 ? -6.744  -10.311 -7.139  1   30.185 ? 294 PHE   B CG   1 
ATOM   4698 C  CD1  . PHE   B 1 294 ? -8.015  -10.869 -7.043  1   32.448 ? 294 PHE   B CD1  1 
ATOM   4699 C  CD2  . PHE   B 1 294 ? -6.631  -8.922  -7.07   1   32.746 ? 294 PHE   B CD2  1 
ATOM   4700 C  CE1  . PHE   B 1 294 ? -9.129  -10.067 -6.839  1   35.435 ? 294 PHE   B CE1  1 
ATOM   4701 C  CE2  . PHE   B 1 294 ? -7.75   -8.126  -6.866  1   34.268 ? 294 PHE   B CE2  1 
ATOM   4702 C  CZ   . PHE   B 1 294 ? -8.993  -8.698  -6.745  1   35.53  ? 294 PHE   B CZ   1 
ATOM   4703 N  N    . ASP   B 1 295 ? -4.748  -10.058 -10.323 1   19.425 ? 295 ASP   B N    1 
ATOM   4704 C  CA   . ASP   B 1 295 ? -4.852  -9.025  -11.343 1   19.842 ? 295 ASP   B CA   1 
ATOM   4705 C  C    . ASP   B 1 295 ? -5.5    -9.577  -12.61  1   19.849 ? 295 ASP   B C    1 
ATOM   4706 O  O    . ASP   B 1 295 ? -6.308  -8.898  -13.244 1   21.005 ? 295 ASP   B O    1 
ATOM   4707 C  CB   . ASP   B 1 295 ? -3.493  -8.441  -11.697 1   19.179 ? 295 ASP   B CB   1 
ATOM   4708 C  CG   . ASP   B 1 295 ? -2.826  -7.618  -10.609 1   18.894 ? 295 ASP   B CG   1 
ATOM   4709 O  OD1  . ASP   B 1 295 ? -3.548  -7.207  -9.666  1   21.218 ? 295 ASP   B OD1  1 
ATOM   4710 O  OD2  . ASP   B 1 295 ? -1.587  -7.433  -10.704 1   18.354 ? 295 ASP   B OD2  1 
ATOM   4711 N  N    . VAL   B 1 296 ? -5.141  -10.809 -12.98  1   18.943 ? 296 VAL   B N    1 
ATOM   4712 C  CA   . VAL   B 1 296 ? -5.68   -11.396 -14.191 1   19.879 ? 296 VAL   B CA   1 
ATOM   4713 C  C    . VAL   B 1 296 ? -7.179  -11.66  -14.013 1   22.144 ? 296 VAL   B C    1 
ATOM   4714 O  O    . VAL   B 1 296 ? -7.987  -11.296 -14.866 1   24.237 ? 296 VAL   B O    1 
ATOM   4715 C  CB   . VAL   B 1 296 ? -4.914  -12.669 -14.581 1   19.438 ? 296 VAL   B CB   1 
ATOM   4716 C  CG1  . VAL   B 1 296 ? -5.587  -13.36  -15.756 1   20.086 ? 296 VAL   B CG1  1 
ATOM   4717 C  CG2  . VAL   B 1 296 ? -3.448  -12.378 -14.88  1   18.263 ? 296 VAL   B CG2  1 
ATOM   4718 N  N    . VAL   B 1 297 ? -7.54   -12.285 -12.887 1   23.551 ? 297 VAL   B N    1 
ATOM   4719 C  CA   . VAL   B 1 297 ? -8.927  -12.63  -12.625 1   26.104 ? 297 VAL   B CA   1 
ATOM   4720 C  C    . VAL   B 1 297 ? -9.778  -11.36  -12.553 1   25.753 ? 297 VAL   B C    1 
ATOM   4721 O  O    . VAL   B 1 297 ? -10.889 -11.347 -13.089 1   26.473 ? 297 VAL   B O    1 
ATOM   4722 C  CB   . VAL   B 1 297 ? -9.072  -13.488 -11.351 1   27.466 ? 297 VAL   B CB   1 
ATOM   4723 C  CG1  . VAL   B 1 297 ? -10.538 -13.715 -10.986 1   29.339 ? 297 VAL   B CG1  1 
ATOM   4724 C  CG2  . VAL   B 1 297 ? -8.355  -14.826 -11.485 1   28.034 ? 297 VAL   B CG2  1 
ATOM   4725 N  N    A ARG   B 1 298 ? -9.25   -10.317 -11.894 0.5 26.245 ? 298 ARG   B N    1 
ATOM   4726 N  N    B ARG   B 1 298 ? -9.256  -10.291 -11.94  0.5 27.236 ? 298 ARG   B N    1 
ATOM   4727 C  CA   A ARG   B 1 298 ? -9.957  -9.054  -11.712 0.5 26.097 ? 298 ARG   B CA   1 
ATOM   4728 C  CA   B ARG   B 1 298 ? -10.047 -9.094  -11.69  0.5 27.717 ? 298 ARG   B CA   1 
ATOM   4729 C  C    A ARG   B 1 298 ? -10.306 -8.463  -13.072 0.5 25.328 ? 298 ARG   B C    1 
ATOM   4730 C  C    B ARG   B 1 298 ? -10.231 -8.283  -12.977 0.5 27.369 ? 298 ARG   B C    1 
ATOM   4731 O  O    A ARG   B 1 298 ? -11.45  -8.071  -13.328 0.5 24.869 ? 298 ARG   B O    1 
ATOM   4732 O  O    B ARG   B 1 298 ? -11.236 -7.586  -13.125 0.5 29.251 ? 298 ARG   B O    1 
ATOM   4733 C  CB   A ARG   B 1 298 ? -9.082  -8.036  -10.963 0.5 27.512 ? 298 ARG   B CB   1 
ATOM   4734 C  CB   B ARG   B 1 298 ? -9.454  -8.265  -10.542 0.5 29.513 ? 298 ARG   B CB   1 
ATOM   4735 C  CG   A ARG   B 1 298 ? -9.42   -6.554  -11.101 0.5 27.349 ? 298 ARG   B CG   1 
ATOM   4736 C  CG   B ARG   B 1 298 ? -8.334  -7.312  -10.939 0.5 30.361 ? 298 ARG   B CG   1 
ATOM   4737 C  CD   A ARG   B 1 298 ? -8.262  -5.647  -10.674 0.5 26.686 ? 298 ARG   B CD   1 
ATOM   4738 C  CD   B ARG   B 1 298 ? -7.779  -6.473  -9.789  0.5 32.137 ? 298 ARG   B CD   1 
ATOM   4739 N  NE   A ARG   B 1 298 ? -8.519  -4.215  -10.872 0.5 25.709 ? 298 ARG   B NE   1 
ATOM   4740 N  NE   B ARG   B 1 298 ? -7.42   -5.139  -10.289 0.5 31.967 ? 298 ARG   B NE   1 
ATOM   4741 C  CZ   A ARG   B 1 298 ? -7.68   -3.353  -11.443 0.5 24.372 ? 298 ARG   B CZ   1 
ATOM   4742 C  CZ   B ARG   B 1 298 ? -6.204  -4.61   -10.331 0.5 31.543 ? 298 ARG   B CZ   1 
ATOM   4743 N  NH1  A ARG   B 1 298 ? -6.448  -3.713  -11.736 0.5 23.398 ? 298 ARG   B NH1  1 
ATOM   4744 N  NH1  B ARG   B 1 298 ? -5.189  -5.215  -9.742  0.5 31.357 ? 298 ARG   B NH1  1 
ATOM   4745 N  NH2  A ARG   B 1 298 ? -8.079  -2.13   -11.742 0.5 22.634 ? 298 ARG   B NH2  1 
ATOM   4746 N  NH2  B ARG   B 1 298 ? -6.017  -3.447  -10.934 0.5 31.685 ? 298 ARG   B NH2  1 
ATOM   4747 N  N    . GLN   B 1 299 ? -9.281  -8.381  -13.92  1   24.995 ? 299 GLN   B N    1 
ATOM   4748 C  CA   . GLN   B 1 299 ? -9.402  -7.678  -15.186 1   24.003 ? 299 GLN   B CA   1 
ATOM   4749 C  C    . GLN   B 1 299 ? -10.282 -8.474  -16.141 1   25.413 ? 299 GLN   B C    1 
ATOM   4750 O  O    . GLN   B 1 299 ? -11.108 -7.889  -16.838 1   27.605 ? 299 GLN   B O    1 
ATOM   4751 C  CB   . GLN   B 1 299 ? -8.045  -7.382  -15.814 1   21.73  ? 299 GLN   B CB   1 
ATOM   4752 C  CG   . GLN   B 1 299 ? -8.149  -6.768  -17.202 1   20.21  ? 299 GLN   B CG   1 
ATOM   4753 C  CD   . GLN   B 1 299 ? -6.863  -6.198  -17.764 1   18.722 ? 299 GLN   B CD   1 
ATOM   4754 O  OE1  . GLN   B 1 299 ? -6.809  -5.824  -18.941 1   18.578 ? 299 GLN   B OE1  1 
ATOM   4755 N  NE2  . GLN   B 1 299 ? -5.824  -6.085  -16.947 1   18.556 ? 299 GLN   B NE2  1 
ATOM   4756 N  N    . CYS   B 1 300 ? -10.134 -9.801  -16.127 1   26.005 ? 300 CYS   B N    1 
ATOM   4757 C  CA   . CYS   B 1 300 ? -10.862 -10.662 -17.043 1   27.758 ? 300 CYS   B CA   1 
ATOM   4758 C  C    . CYS   B 1 300 ? -12.328 -10.825 -16.632 1   28.088 ? 300 CYS   B C    1 
ATOM   4759 O  O    . CYS   B 1 300 ? -13.126 -11.273 -17.45  1   27.477 ? 300 CYS   B O    1 
ATOM   4760 C  CB   . CYS   B 1 300 ? -10.139 -11.994 -17.214 1   28.973 ? 300 CYS   B CB   1 
ATOM   4761 S  SG   . CYS   B 1 300 ? -8.545  -11.826 -18.059 1   33.816 ? 300 CYS   B SG   1 
ATOM   4762 N  N    . SER   B 1 301 ? -12.701 -10.397 -15.41  1   27.794 ? 301 SER   B N    1 
ATOM   4763 C  CA   . SER   B 1 301 ? -14.064 -10.553 -14.909 1   28.223 ? 301 SER   B CA   1 
ATOM   4764 C  C    . SER   B 1 301 ? -14.756 -9.216  -14.604 1   27.934 ? 301 SER   B C    1 
ATOM   4765 O  O    . SER   B 1 301 ? -15.918 -9.203  -14.194 1   28.135 ? 301 SER   B O    1 
ATOM   4766 C  CB   . SER   B 1 301 ? -14.086 -11.466 -13.706 1   29.976 ? 301 SER   B CB   1 
ATOM   4767 O  OG   . SER   B 1 301 ? -13.508 -10.851 -12.563 1   31.715 ? 301 SER   B OG   1 
ATOM   4768 N  N    . GLY   B 1 302 ? -14.066 -8.086  -14.81  1   27.438 ? 302 GLY   B N    1 
ATOM   4769 C  CA   . GLY   B 1 302 ? -14.7   -6.771  -14.777 1   26.93  ? 302 GLY   B CA   1 
ATOM   4770 C  C    . GLY   B 1 302 ? -15.107 -6.319  -13.371 1   26.552 ? 302 GLY   B C    1 
ATOM   4771 O  O    . GLY   B 1 302 ? -16.13  -5.655  -13.199 1   25.248 ? 302 GLY   B O    1 
ATOM   4772 N  N    . VAL   B 1 303 ? -14.284 -6.659  -12.372 1   25.855 ? 303 VAL   B N    1 
ATOM   4773 C  CA   . VAL   B 1 303 ? -14.516 -6.245  -10.99  1   25.476 ? 303 VAL   B CA   1 
ATOM   4774 C  C    . VAL   B 1 303 ? -14.479 -4.716  -10.895 1   24.258 ? 303 VAL   B C    1 
ATOM   4775 O  O    . VAL   B 1 303 ? -13.581 -4.094  -11.458 1   24.425 ? 303 VAL   B O    1 
ATOM   4776 C  CB   . VAL   B 1 303 ? -13.444 -6.889  -10.084 1   26.418 ? 303 VAL   B CB   1 
ATOM   4777 C  CG1  . VAL   B 1 303 ? -13.505 -6.374  -8.648  1   27.909 ? 303 VAL   B CG1  1 
ATOM   4778 C  CG2  . VAL   B 1 303 ? -13.529 -8.412  -10.096 1   26.334 ? 303 VAL   B CG2  1 
ATOM   4779 N  N    . THR   B 1 304 ? -15.427 -4.116  -10.157 1   23.128 ? 304 THR   B N    1 
ATOM   4780 C  CA   . THR   B 1 304 ? -15.471 -2.668  -9.975  1   24.233 ? 304 THR   B CA   1 
ATOM   4781 C  C    . THR   B 1 304 ? -15.264 -2.277  -8.511  1   24.89  ? 304 THR   B C    1 
ATOM   4782 O  O    . THR   B 1 304 ? -15.315 -3.116  -7.614  1   26.333 ? 304 THR   B O    1 
ATOM   4783 C  CB   . THR   B 1 304 ? -16.797 -2.09   -10.474 1   23.908 ? 304 THR   B CB   1 
ATOM   4784 O  OG1  . THR   B 1 304 ? -17.818 -2.725  -9.711  1   24.772 ? 304 THR   B OG1  1 
ATOM   4785 C  CG2  . THR   B 1 304 ? -17.034 -2.327  -11.951 1   23.066 ? 304 THR   B CG2  1 
ATOM   4786 N  N    . PHE   B 1 305 ? -15.07  -0.964  -8.3    1   26.277 ? 305 PHE   B N    1 
ATOM   4787 C  CA   . PHE   B 1 305 ? -14.78  -0.388  -6.993  1   27.516 ? 305 PHE   B CA   1 
ATOM   4788 C  C    . PHE   B 1 305 ? -15.719 0.791   -6.711  1   30.725 ? 305 PHE   B C    1 
ATOM   4789 O  O    . PHE   B 1 305 ? -16.449 1.233   -7.621  1   35.019 ? 305 PHE   B O    1 
ATOM   4790 C  CB   . PHE   B 1 305 ? -13.303 0.017   -6.973  1   28.013 ? 305 PHE   B CB   1 
ATOM   4791 C  CG   . PHE   B 1 305 ? -12.429 -1.162  -7.365  1   27.617 ? 305 PHE   B CG   1 
ATOM   4792 C  CD1  . PHE   B 1 305 ? -12.128 -2.15   -6.437  1   27.533 ? 305 PHE   B CD1  1 
ATOM   4793 C  CD2  . PHE   B 1 305 ? -11.995 -1.322  -8.677  1   28.575 ? 305 PHE   B CD2  1 
ATOM   4794 C  CE1  . PHE   B 1 305 ? -11.373 -3.253  -6.799  1   28.646 ? 305 PHE   B CE1  1 
ATOM   4795 C  CE2  . PHE   B 1 305 ? -11.24  -2.428  -9.035  1   30.9   ? 305 PHE   B CE2  1 
ATOM   4796 C  CZ   . PHE   B 1 305 ? -10.934 -3.391  -8.097  1   30.754 ? 305 PHE   B CZ   1 
HETATM 4797 C  C4   . A1ITI C 2 .   ? -22.635 -3.993  -31.151 1   19.118 ? 401 A1ITI A C4   1 
HETATM 4798 C  C5   . A1ITI C 2 .   ? -23.496 -3.749  -29.941 1   19.025 ? 401 A1ITI A C5   1 
HETATM 4799 C  C7   . A1ITI C 2 .   ? -21.734 -4.1    -28.224 1   16.533 ? 401 A1ITI A C7   1 
HETATM 4800 C  C8   . A1ITI C 2 .   ? -21.068 -5.116  -27.324 1   16.326 ? 401 A1ITI A C8   1 
HETATM 4801 C  C10  . A1ITI C 2 .   ? -22.792 -4.773  -25.491 1   16.58  ? 401 A1ITI A C10  1 
HETATM 4802 C  C13  . A1ITI C 2 .   ? -19.024 -4.964  -25.155 1   14.373 ? 401 A1ITI A C13  1 
HETATM 4803 C  C15  . A1ITI C 2 .   ? -19.077 -7.558  -25.346 1   16.184 ? 401 A1ITI A C15  1 
HETATM 4804 C  C21  . A1ITI C 2 .   ? -18.166 -3.866  -25.177 1   14.224 ? 401 A1ITI A C21  1 
HETATM 4805 C  C24  . A1ITI C 2 .   ? -25.435 -5.141  -28.272 1   19.566 ? 401 A1ITI A C24  1 
HETATM 4806 C  C26  . A1ITI C 2 .   ? -27.883 -4.992  -28.251 1   22.152 ? 401 A1ITI A C26  1 
HETATM 4807 C  C1   . A1ITI C 2 .   ? -22.479 -0.61   -31.654 1   22.543 ? 401 A1ITI A C1   1 
HETATM 4808 C  C2   . A1ITI C 2 .   ? -23.308 -1.752  -32.165 1   22.342 ? 401 A1ITI A C2   1 
HETATM 4809 C  C3   . A1ITI C 2 .   ? -22.55  -3.058  -32.192 1   20.88  ? 401 A1ITI A C3   1 
HETATM 4810 N  N6   . A1ITI C 2 .   ? -23.073 -4.494  -28.701 1   17.735 ? 401 A1ITI A N6   1 
HETATM 4811 N  N9   . A1ITI C 2 .   ? -21.385 -4.892  -25.912 1   15.512 ? 401 A1ITI A N9   1 
HETATM 4812 C  C11  . A1ITI C 2 .   ? -23.784 -5.394  -26.465 1   17.256 ? 401 A1ITI A C11  1 
HETATM 4813 C  C12  . A1ITI C 2 .   ? -20.485 -4.722  -24.929 1   15.125 ? 401 A1ITI A C12  1 
HETATM 4814 C  C14  . A1ITI C 2 .   ? -18.479 -6.249  -25.322 1   14.964 ? 401 A1ITI A C14  1 
HETATM 4815 C  C16  . A1ITI C 2 .   ? -18.16  -8.533  -25.541 1   16.829 ? 401 A1ITI A C16  1 
HETATM 4816 S  S17  . A1ITI C 2 .   ? -16.542 -7.944  -25.704 1   16.871 ? 401 A1ITI A S17  1 
HETATM 4817 C  C18  . A1ITI C 2 .   ? -17.083 -6.309  -25.508 1   14.561 ? 401 A1ITI A C18  1 
HETATM 4818 C  C19  . A1ITI C 2 .   ? -16.309 -5.153  -25.52  1   14.42  ? 401 A1ITI A C19  1 
HETATM 4819 N  N20  . A1ITI C 2 .   ? -16.841 -3.939  -25.355 1   14.367 ? 401 A1ITI A N20  1 
HETATM 4820 O  O22  . A1ITI C 2 .   ? -20.803 -4.441  -23.787 1   15.481 ? 401 A1ITI A O22  1 
HETATM 4821 C  C23  . A1ITI C 2 .   ? -24.151 -4.568  -27.689 1   18.005 ? 401 A1ITI A C23  1 
HETATM 4822 N  N25  . A1ITI C 2 .   ? -26.547 -4.472  -27.973 1   20.778 ? 401 A1ITI A N25  1 
HETATM 4823 C  C27  . A1ITI C 2 .   ? -28.392 -5.764  -27.077 1   22.913 ? 401 A1ITI A C27  1 
HETATM 4824 O  O28  . A1ITI C 2 .   ? -25.402 -6.179  -28.925 1   22.016 ? 401 A1ITI A O28  1 
HETATM 4825 C  C29  . A1ITI C 2 .   ? -21.908 -5.18   -31.238 1   19.787 ? 401 A1ITI A C29  1 
HETATM 4826 C  C30  . A1ITI C 2 .   ? -21.103 -5.449  -32.327 1   20.981 ? 401 A1ITI A C30  1 
HETATM 4827 C  C31  . A1ITI C 2 .   ? -21.028 -4.522  -33.341 1   21.274 ? 401 A1ITI A C31  1 
HETATM 4828 BR BR32 . A1ITI C 2 .   ? -19.923 -4.881  -34.843 0.8 23.44  ? 401 A1ITI A BR32 1 
HETATM 4829 C  C33  . A1ITI C 2 .   ? -21.736 -3.336  -33.289 1   20.78  ? 401 A1ITI A C33  1 
HETATM 4830 CL CL   . CL    D 3 .   ? -5.218  15.123  -31.644 1   15.203 ? 402 CL    A CL   1 
HETATM 4831 C  C4   . A1ITI E 2 .   ? 17.634  10.883  -0.833  1   19.055 ? 401 A1ITI B C4   1 
HETATM 4832 C  C5   . A1ITI E 2 .   ? 16.786  12.097  -0.569  1   18.858 ? 401 A1ITI B C5   1 
HETATM 4833 C  C7   . A1ITI E 2 .   ? 15.426  12.053  -2.664  1   17.202 ? 401 A1ITI B C7   1 
HETATM 4834 C  C8   . A1ITI E 2 .   ? 15.348  12.532  -4.097  1   17.101 ? 401 A1ITI B C8   1 
HETATM 4835 C  C10  . A1ITI E 2 .   ? 14.225  14.697  -3.414  1   17.1   ? 401 A1ITI B C10  1 
HETATM 4836 C  C13  . A1ITI E 2 .   ? 13.225  12.362  -6.208  1   15.347 ? 401 A1ITI B C13  1 
HETATM 4837 C  C15  . A1ITI E 2 .   ? 15.012  13.364  -7.8    1   17.26  ? 401 A1ITI B C15  1 
HETATM 4838 C  C21  . A1ITI E 2 .   ? 12.347  11.289  -6.057  1   15.326 ? 401 A1ITI B C21  1 
HETATM 4839 C  C24  . A1ITI E 2 .   ? 16.967  14.982  -0.717  1   20.043 ? 401 A1ITI B C24  1 
HETATM 4840 C  C26  . A1ITI E 2 .   ? 17.345  16.589  1.105   1   22.331 ? 401 A1ITI B C26  1 
HETATM 4841 C  C1   . A1ITI E 2 .   ? 15.665  8.947   1.298   1   20.901 ? 401 A1ITI B C1   1 
HETATM 4842 C  C2   . A1ITI E 2 .   ? 16.947  9.753   1.369   1   20.974 ? 401 A1ITI B C2   1 
HETATM 4843 C  C3   . A1ITI E 2 .   ? 17.712  9.802   0.061   1   20.097 ? 401 A1ITI B C3   1 
HETATM 4844 N  N6   . A1ITI E 2 .   ? 16.338  12.845  -1.806  1   18.028 ? 401 A1ITI B N6   1 
HETATM 4845 N  N9   . A1ITI E 2 .   ? 14.271  13.509  -4.276  1   16.58  ? 401 A1ITI B N9   1 
HETATM 4846 C  C11  . A1ITI E 2 .   ? 15.555  15.035  -2.754  1   17.893 ? 401 A1ITI B C11  1 
HETATM 4847 C  C12  . A1ITI E 2 .   ? 13.249  13.416  -5.141  1   15.751 ? 401 A1ITI B C12  1 
HETATM 4848 C  C14  . A1ITI E 2 .   ? 14.032  12.415  -7.357  1   16.278 ? 401 A1ITI B C14  1 
HETATM 4849 C  C16  . A1ITI E 2 .   ? 15.56   13.019  -8.985  1   17.809 ? 401 A1ITI B C16  1 
HETATM 4850 S  S17  . A1ITI E 2 .   ? 14.933  11.55   -9.633  1   17.59  ? 401 A1ITI B S17  1 
HETATM 4851 C  C18  . A1ITI E 2 .   ? 13.884  11.357  -8.27   1   15.48  ? 401 A1ITI B C18  1 
HETATM 4852 C  C19  . A1ITI E 2 .   ? 12.98   10.327  -8.03   1   14.844 ? 401 A1ITI B C19  1 
HETATM 4853 N  N20  . A1ITI E 2 .   ? 12.218  10.29   -6.934  1   14.875 ? 401 A1ITI B N20  1 
HETATM 4854 O  O22  . A1ITI E 2 .   ? 12.308  14.199  -5.137  1   17.104 ? 401 A1ITI B O22  1 
HETATM 4855 C  C23  . A1ITI E 2 .   ? 15.921  14.221  -1.519  1   18.549 ? 401 A1ITI B C23  1 
HETATM 4856 N  N25  . A1ITI E 2 .   ? 16.503  15.697  0.312   1   21.409 ? 401 A1ITI B N25  1 
HETATM 4857 C  C27  . A1ITI E 2 .   ? 17.163  18.005  0.673   1   22.674 ? 401 A1ITI B C27  1 
HETATM 4858 O  O28  . A1ITI E 2 .   ? 18.141  14.964  -1.068  1   22.218 ? 401 A1ITI B O28  1 
HETATM 4859 C  C29  . A1ITI E 2 .   ? 18.375  10.843  -2.018  1   20.34  ? 401 A1ITI B C29  1 
HETATM 4860 C  C30  . A1ITI E 2 .   ? 19.176  9.762   -2.328  1   21.281 ? 401 A1ITI B C30  1 
HETATM 4861 C  C31  . A1ITI E 2 .   ? 19.24   8.714   -1.444  1   21.563 ? 401 A1ITI B C31  1 
HETATM 4862 BR BR32 . A1ITI E 2 .   ? 20.333  7.221   -1.864  0.8 24.636 ? 401 A1ITI B BR32 1 
HETATM 4863 C  C33  . A1ITI E 2 .   ? 18.525  8.718   -0.263  1   20.797 ? 401 A1ITI B C33  1 
HETATM 4864 NA NA   . NA    F 4 .   ? 1.906   -28.474 -21.676 1   25.611 ? 402 NA    B NA   1 
HETATM 4865 O  O    . HOH   G 5 .   ? -29.731 -2.154  -25.76  1   28.35  ? 501 HOH   A O    1 
HETATM 4866 O  O    . HOH   G 5 .   ? -35.57  -3.017  -34.898 1   40.025 ? 502 HOH   A O    1 
HETATM 4867 O  O    . HOH   G 5 .   ? -8.401  16.601  -33.82  1   47.674 ? 503 HOH   A O    1 
HETATM 4868 O  O    . HOH   G 5 .   ? -20.923 -4.66   -12.461 1   32.195 ? 504 HOH   A O    1 
HETATM 4869 O  O    . HOH   G 5 .   ? -33.974 7.337   -13.413 1   31.399 ? 505 HOH   A O    1 
HETATM 4870 O  O    . HOH   G 5 .   ? -36.208 -0.22   -28.328 1   29.39  ? 506 HOH   A O    1 
HETATM 4871 O  O    . HOH   G 5 .   ? -1.048  -2.163  -35.023 1   48.81  ? 507 HOH   A O    1 
HETATM 4872 O  O    . HOH   G 5 .   ? 3.534   1.694   -26.769 1   23.896 ? 508 HOH   A O    1 
HETATM 4873 O  O    . HOH   G 5 .   ? -29.629 8.549   -37.276 1   33.896 ? 509 HOH   A O    1 
HETATM 4874 O  O    . HOH   G 5 .   ? 9.442   9.018   -53.468 1   32.055 ? 510 HOH   A O    1 
HETATM 4875 O  O    . HOH   G 5 .   ? 22.189  14.724  -34.549 1   21.211 ? 511 HOH   A O    1 
HETATM 4876 O  O    . HOH   G 5 .   ? 26.011  14.94   -24.271 1   38.622 ? 512 HOH   A O    1 
HETATM 4877 O  O    . HOH   G 5 .   ? -30.854 -6.098  -23.598 1   34.037 ? 513 HOH   A O    1 
HETATM 4878 O  O    . HOH   G 5 .   ? 4.985   21.291  -41.004 1   24.632 ? 514 HOH   A O    1 
HETATM 4879 O  O    . HOH   G 5 .   ? -32.443 12.15   -7.389  1   46.087 ? 515 HOH   A O    1 
HETATM 4880 O  O    . HOH   G 5 .   ? -17.978 6.358   -39.387 1   33.971 ? 516 HOH   A O    1 
HETATM 4881 O  O    . HOH   G 5 .   ? -15.073 5.763   -8.285  1   35.889 ? 517 HOH   A O    1 
HETATM 4882 O  O    . HOH   G 5 .   ? 0.589   4.865   -23.734 1   29.54  ? 518 HOH   A O    1 
HETATM 4883 O  O    . HOH   G 5 .   ? -3.519  1.635   -40.698 1   36.878 ? 519 HOH   A O    1 
HETATM 4884 O  O    . HOH   G 5 .   ? -1.322  19.117  -17.25  1   43.055 ? 520 HOH   A O    1 
HETATM 4885 O  O    . HOH   G 5 .   ? 11.117  17.358  -22.294 1   36.941 ? 521 HOH   A O    1 
HETATM 4886 O  O    . HOH   G 5 .   ? -43.426 5.197   -21.907 1   36.899 ? 522 HOH   A O    1 
HETATM 4887 O  O    . HOH   G 5 .   ? -1.066  2.68    -24.553 1   18.869 ? 523 HOH   A O    1 
HETATM 4888 O  O    . HOH   G 5 .   ? -21.554 10.735  -37.436 1   55.879 ? 524 HOH   A O    1 
HETATM 4889 O  O    . HOH   G 5 .   ? -2.018  12.719  -34.569 1   25.175 ? 525 HOH   A O    1 
HETATM 4890 O  O    . HOH   G 5 .   ? 3.808   -1.216  -33.905 1   44.023 ? 526 HOH   A O    1 
HETATM 4891 O  O    . HOH   G 5 .   ? 21.864  17.339  -19.222 1   37.257 ? 527 HOH   A O    1 
HETATM 4892 O  O    . HOH   G 5 .   ? -38.416 0.078   -35.016 1   29.022 ? 528 HOH   A O    1 
HETATM 4893 O  O    . HOH   G 5 .   ? 17.353  8.225   -16.122 1   35.658 ? 529 HOH   A O    1 
HETATM 4894 O  O    . HOH   G 5 .   ? -12.299 -3.617  -18.392 1   18.585 ? 530 HOH   A O    1 
HETATM 4895 O  O    . HOH   G 5 .   ? 4.854   -2.31   -38.087 1   29.499 ? 531 HOH   A O    1 
HETATM 4896 O  O    . HOH   G 5 .   ? -30.224 -4.532  -17.187 1   41.322 ? 532 HOH   A O    1 
HETATM 4897 O  O    . HOH   G 5 .   ? -16.545 16.416  -32.597 1   41.614 ? 533 HOH   A O    1 
HETATM 4898 O  O    . HOH   G 5 .   ? 25.751  12.386  -16.984 1   31.264 ? 534 HOH   A O    1 
HETATM 4899 O  O    . HOH   G 5 .   ? -11.168 -6.357  -19.458 1   24.776 ? 535 HOH   A O    1 
HETATM 4900 O  O    . HOH   G 5 .   ? 25.521  12.162  -23.934 1   23.832 ? 536 HOH   A O    1 
HETATM 4901 O  O    . HOH   G 5 .   ? 21.388  0.726   -33.974 1   20.528 ? 537 HOH   A O    1 
HETATM 4902 O  O    . HOH   G 5 .   ? -24.93  9.808   -6.312  1   50.367 ? 538 HOH   A O    1 
HETATM 4903 O  O    . HOH   G 5 .   ? 19.9    -8.817  -36.817 1   26.197 ? 539 HOH   A O    1 
HETATM 4904 O  O    . HOH   G 5 .   ? 7.306   6.107   -42.613 1   35.237 ? 540 HOH   A O    1 
HETATM 4905 O  O    . HOH   G 5 .   ? -22.28  -0.481  -10.062 1   36.404 ? 541 HOH   A O    1 
HETATM 4906 O  O    . HOH   G 5 .   ? 9.99    17.06   -19.902 1   26.312 ? 542 HOH   A O    1 
HETATM 4907 O  O    . HOH   G 5 .   ? 13.867  -7.785  -29.129 1   33.134 ? 543 HOH   A O    1 
HETATM 4908 O  O    . HOH   G 5 .   ? -32.14  20.034  -15.33  1   46.187 ? 544 HOH   A O    1 
HETATM 4909 O  O    . HOH   G 5 .   ? -15.458 5.965   -18.195 1   14.64  ? 545 HOH   A O    1 
HETATM 4910 O  O    . HOH   G 5 .   ? -37.97  0.437   -23.028 1   42.9   ? 546 HOH   A O    1 
HETATM 4911 O  O    . HOH   G 5 .   ? 15.87   -7.999  -27.19  1   32.303 ? 547 HOH   A O    1 
HETATM 4912 O  O    . HOH   G 5 .   ? 17.861  -1.51   -44.372 1   34.034 ? 548 HOH   A O    1 
HETATM 4913 O  O    . HOH   G 5 .   ? -0.473  11.742  -21.524 1   17.218 ? 549 HOH   A O    1 
HETATM 4914 O  O    . HOH   G 5 .   ? -28.795 1.346   -38.628 1   35.115 ? 550 HOH   A O    1 
HETATM 4915 O  O    . HOH   G 5 .   ? -24.577 -3.283  -21.95  1   19.397 ? 551 HOH   A O    1 
HETATM 4916 O  O    . HOH   G 5 .   ? 25.229  -0.594  -29.699 1   38.841 ? 552 HOH   A O    1 
HETATM 4917 O  O    . HOH   G 5 .   ? -22.719 -1.74   -17.55  1   17.745 ? 553 HOH   A O    1 
HETATM 4918 O  O    . HOH   G 5 .   ? -38.434 10.287  -16.298 1   26.968 ? 554 HOH   A O    1 
HETATM 4919 O  O    . HOH   G 5 .   ? 23.784  10.316  -36.932 1   22.36  ? 555 HOH   A O    1 
HETATM 4920 O  O    . HOH   G 5 .   ? -29.434 16.485  -31.715 1   49.58  ? 556 HOH   A O    1 
HETATM 4921 O  O    . HOH   G 5 .   ? -2.533  10.649  -22.962 1   14.509 ? 557 HOH   A O    1 
HETATM 4922 O  O    . HOH   G 5 .   ? 8.441   -2.205  -35.183 1   23.334 ? 558 HOH   A O    1 
HETATM 4923 O  O    . HOH   G 5 .   ? 18.132  10.363  -51.575 1   17.733 ? 559 HOH   A O    1 
HETATM 4924 O  O    . HOH   G 5 .   ? -22.034 -2.402  -22.509 1   15.158 ? 560 HOH   A O    1 
HETATM 4925 O  O    . HOH   G 5 .   ? -37.311 1.048   -20.563 1   34.244 ? 561 HOH   A O    1 
HETATM 4926 O  O    . HOH   G 5 .   ? -3.809  16.47   -14.616 1   40.014 ? 562 HOH   A O    1 
HETATM 4927 O  O    . HOH   G 5 .   ? -17.427 9.926   -38.194 1   33.847 ? 563 HOH   A O    1 
HETATM 4928 O  O    . HOH   G 5 .   ? -17.352 22.865  -21.588 1   39.131 ? 564 HOH   A O    1 
HETATM 4929 O  O    . HOH   G 5 .   ? -0.374  16.927  -38.887 1   47.435 ? 565 HOH   A O    1 
HETATM 4930 O  O    . HOH   G 5 .   ? 2.501   2.848   -44.355 1   35.782 ? 566 HOH   A O    1 
HETATM 4931 O  O    . HOH   G 5 .   ? -15.944 14.35   -10.668 1   21.992 ? 567 HOH   A O    1 
HETATM 4932 O  O    . HOH   G 5 .   ? -38.896 10.083  -28.216 1   25.264 ? 568 HOH   A O    1 
HETATM 4933 O  O    . HOH   G 5 .   ? 17.226  14.849  -14.578 1   29.345 ? 569 HOH   A O    1 
HETATM 4934 O  O    . HOH   G 5 .   ? -22.466 16.185  -27.487 1   25.204 ? 570 HOH   A O    1 
HETATM 4935 O  O    . HOH   G 5 .   ? -17.795 -7.931  -32.922 1   28.713 ? 571 HOH   A O    1 
HETATM 4936 O  O    . HOH   G 5 .   ? -26.872 19.829  -8.2    1   28.441 ? 572 HOH   A O    1 
HETATM 4937 O  O    . HOH   G 5 .   ? 9.517   18.626  -45.571 1   36.459 ? 573 HOH   A O    1 
HETATM 4938 O  O    . HOH   G 5 .   ? -5.997  -4.983  -26.311 1   26.226 ? 574 HOH   A O    1 
HETATM 4939 O  O    . HOH   G 5 .   ? 0.004   14.099  -27.598 1   19.31  ? 575 HOH   A O    1 
HETATM 4940 O  O    . HOH   G 5 .   ? 11.922  19.866  -35.758 1   29.758 ? 576 HOH   A O    1 
HETATM 4941 O  O    . HOH   G 5 .   ? 20.642  -4.075  -32.635 1   24.141 ? 577 HOH   A O    1 
HETATM 4942 O  O    . HOH   G 5 .   ? 24.449  17.519  -30.869 1   39.764 ? 578 HOH   A O    1 
HETATM 4943 O  O    . HOH   G 5 .   ? 1.248   11.316  -32.157 1   20.73  ? 579 HOH   A O    1 
HETATM 4944 O  O    . HOH   G 5 .   ? 11.45   9.558   -15.599 1   22.649 ? 580 HOH   A O    1 
HETATM 4945 O  O    . HOH   G 5 .   ? 17.053  12.36   -17.482 1   26.843 ? 581 HOH   A O    1 
HETATM 4946 O  O    . HOH   G 5 .   ? -6.38   17.692  -21.855 1   33.24  ? 582 HOH   A O    1 
HETATM 4947 O  O    . HOH   G 5 .   ? -0.117  17.257  -19.412 1   37.22  ? 583 HOH   A O    1 
HETATM 4948 O  O    . HOH   G 5 .   ? 13.194  11.118  -16.982 1   19.01  ? 584 HOH   A O    1 
HETATM 4949 O  O    . HOH   G 5 .   ? 9.234   17.31   -29.206 1   22.076 ? 585 HOH   A O    1 
HETATM 4950 O  O    . HOH   G 5 .   ? -4.614  1.553   -28.712 1   14.6   ? 586 HOH   A O    1 
HETATM 4951 O  O    . HOH   G 5 .   ? 20.34   4.226   -40.847 1   22.419 ? 587 HOH   A O    1 
HETATM 4952 O  O    . HOH   G 5 .   ? 14.217  20.89   -21.22  1   42.094 ? 588 HOH   A O    1 
HETATM 4953 O  O    . HOH   G 5 .   ? -26.985 -2.069  -26.317 1   21.938 ? 589 HOH   A O    1 
HETATM 4954 O  O    . HOH   G 5 .   ? 16.604  2.314   -22.303 1   23.847 ? 590 HOH   A O    1 
HETATM 4955 O  O    . HOH   G 5 .   ? 16.029  -1.133  -21.115 1   27.648 ? 591 HOH   A O    1 
HETATM 4956 O  O    . HOH   G 5 .   ? 11.901  -5.168  -38.095 1   25.376 ? 592 HOH   A O    1 
HETATM 4957 O  O    . HOH   G 5 .   ? 1.435   1.354   -16.502 1   33.326 ? 593 HOH   A O    1 
HETATM 4958 O  O    . HOH   G 5 .   ? 15.612  -0.753  -42.453 1   19.133 ? 594 HOH   A O    1 
HETATM 4959 O  O    . HOH   G 5 .   ? 20.36   15.189  -42.078 1   38.241 ? 595 HOH   A O    1 
HETATM 4960 O  O    . HOH   G 5 .   ? 7.718   23.695  -41.081 1   31.382 ? 596 HOH   A O    1 
HETATM 4961 O  O    . HOH   G 5 .   ? 0.028   3.907   -44.134 1   38.244 ? 597 HOH   A O    1 
HETATM 4962 O  O    . HOH   G 5 .   ? -27.167 -8.23   -29.424 1   41.293 ? 598 HOH   A O    1 
HETATM 4963 O  O    . HOH   G 5 .   ? -9.846  11.723  -36.248 1   31.086 ? 599 HOH   A O    1 
HETATM 4964 O  O    . HOH   G 5 .   ? 11.611  21.33   -38.272 1   33.608 ? 600 HOH   A O    1 
HETATM 4965 O  O    . HOH   G 5 .   ? 18.003  20.447  -20.49  1   40.555 ? 601 HOH   A O    1 
HETATM 4966 O  O    . HOH   G 5 .   ? -18.597 -8.732  -18.388 1   45.622 ? 602 HOH   A O    1 
HETATM 4967 O  O    . HOH   G 5 .   ? 18.831  9.381   -47.384 1   18.217 ? 603 HOH   A O    1 
HETATM 4968 O  O    . HOH   G 5 .   ? 8.174   2.147   -49.838 1   27.513 ? 604 HOH   A O    1 
HETATM 4969 O  O    . HOH   G 5 .   ? 10.683  1.614   -18.569 1   21.396 ? 605 HOH   A O    1 
HETATM 4970 O  O    . HOH   G 5 .   ? -38.277 1.44    -29.081 1   25.103 ? 606 HOH   A O    1 
HETATM 4971 O  O    . HOH   G 5 .   ? 23.485  14.158  -28.369 1   19.873 ? 607 HOH   A O    1 
HETATM 4972 O  O    . HOH   G 5 .   ? 19.153  14.461  -44.414 1   26.726 ? 608 HOH   A O    1 
HETATM 4973 O  O    . HOH   G 5 .   ? 13.612  21.409  -25.756 1   34.266 ? 609 HOH   A O    1 
HETATM 4974 O  O    . HOH   G 5 .   ? -12.703 8.769   -38.929 1   29.006 ? 610 HOH   A O    1 
HETATM 4975 O  O    . HOH   G 5 .   ? 25.444  11.512  -40.734 1   35.711 ? 611 HOH   A O    1 
HETATM 4976 O  O    . HOH   G 5 .   ? 20.404  20.989  -28.921 1   43.729 ? 612 HOH   A O    1 
HETATM 4977 O  O    . HOH   G 5 .   ? -3.38   19.777  -24.143 1   23.431 ? 613 HOH   A O    1 
HETATM 4978 O  O    . HOH   G 5 .   ? 0.907   15.075  -40.336 1   26.193 ? 614 HOH   A O    1 
HETATM 4979 O  O    . HOH   G 5 .   ? 25.837  1.582   -37.992 1   26.604 ? 615 HOH   A O    1 
HETATM 4980 O  O    . HOH   G 5 .   ? 21.85   14.335  -24.957 1   25.397 ? 616 HOH   A O    1 
HETATM 4981 O  O    . HOH   G 5 .   ? -10.227 1.253   -40.342 1   28.013 ? 617 HOH   A O    1 
HETATM 4982 O  O    . HOH   G 5 .   ? 17.907  4.774   -47.174 1   24.222 ? 618 HOH   A O    1 
HETATM 4983 O  O    . HOH   G 5 .   ? 7.071   -4.22   -38.936 1   38.43  ? 619 HOH   A O    1 
HETATM 4984 O  O    . HOH   G 5 .   ? -23.327 -8.014  -29.063 1   31.572 ? 620 HOH   A O    1 
HETATM 4985 O  O    . HOH   G 5 .   ? 15.705  11.514  -50.949 1   19.675 ? 621 HOH   A O    1 
HETATM 4986 O  O    . HOH   G 5 .   ? 21.725  10.147  -22.948 1   21.081 ? 622 HOH   A O    1 
HETATM 4987 O  O    . HOH   G 5 .   ? -22.015 13.336  -8.239  1   29.553 ? 623 HOH   A O    1 
HETATM 4988 O  O    . HOH   G 5 .   ? 1.338   -0.37   -26.88  1   30.575 ? 624 HOH   A O    1 
HETATM 4989 O  O    . HOH   G 5 .   ? 12.457  -5.613  -19.486 1   51.316 ? 625 HOH   A O    1 
HETATM 4990 O  O    . HOH   G 5 .   ? -40.598 11.187  -14.882 1   35.244 ? 626 HOH   A O    1 
HETATM 4991 O  O    . HOH   G 5 .   ? -4.646  7.204   -40.286 1   26.586 ? 627 HOH   A O    1 
HETATM 4992 O  O    . HOH   G 5 .   ? 18.94   6.171   -49.14  1   19.972 ? 628 HOH   A O    1 
HETATM 4993 O  O    . HOH   G 5 .   ? 0.505   21.773  -40.612 1   42.64  ? 629 HOH   A O    1 
HETATM 4994 O  O    . HOH   G 5 .   ? -23.264 18.631  -20.338 1   23.837 ? 630 HOH   A O    1 
HETATM 4995 O  O    . HOH   G 5 .   ? -28.522 10.649  -35.073 1   24.844 ? 631 HOH   A O    1 
HETATM 4996 O  O    . HOH   G 5 .   ? 16.899  4.912   -21.249 1   20.794 ? 632 HOH   A O    1 
HETATM 4997 O  O    . HOH   G 5 .   ? 21.428  8.04    -35.559 1   20.942 ? 633 HOH   A O    1 
HETATM 4998 O  O    . HOH   G 5 .   ? -8.452  14.422  -24.972 1   19.263 ? 634 HOH   A O    1 
HETATM 4999 O  O    . HOH   G 5 .   ? -36.093 8.774   -15.502 1   25.679 ? 635 HOH   A O    1 
HETATM 5000 O  O    . HOH   G 5 .   ? 1.226   10.151  -41.729 1   30.763 ? 636 HOH   A O    1 
HETATM 5001 O  O    . HOH   G 5 .   ? -13.559 3.758   -33.475 1   17.419 ? 637 HOH   A O    1 
HETATM 5002 O  O    . HOH   G 5 .   ? -24.344 -5.978  -21.899 1   23.047 ? 638 HOH   A O    1 
HETATM 5003 O  O    . HOH   G 5 .   ? -11.971 -5.873  -37.366 1   38.026 ? 639 HOH   A O    1 
HETATM 5004 O  O    . HOH   G 5 .   ? 5.799   5.582   -28.414 1   12.98  ? 640 HOH   A O    1 
HETATM 5005 O  O    . HOH   G 5 .   ? -35.707 -1.224  -25.633 1   35.621 ? 641 HOH   A O    1 
HETATM 5006 O  O    . HOH   G 5 .   ? -26.079 -5.913  -40.628 1   38.524 ? 642 HOH   A O    1 
HETATM 5007 O  O    . HOH   G 5 .   ? 0.768   7.585   -23.293 1   16.621 ? 643 HOH   A O    1 
HETATM 5008 O  O    . HOH   G 5 .   ? -15.278 14.472  -28.078 1   19.413 ? 644 HOH   A O    1 
HETATM 5009 O  O    . HOH   G 5 .   ? -6.734  -2.583  -35.111 1   33.283 ? 645 HOH   A O    1 
HETATM 5010 O  O    . HOH   G 5 .   ? -29.838 2.401   -14.433 1   22.899 ? 646 HOH   A O    1 
HETATM 5011 O  O    . HOH   G 5 .   ? -0.63   -1.071  -28.714 1   27.705 ? 647 HOH   A O    1 
HETATM 5012 O  O    . HOH   G 5 .   ? -6.981  4.404   -41.681 1   35.585 ? 648 HOH   A O    1 
HETATM 5013 O  O    . HOH   G 5 .   ? -20.925 21.561  -6.841  1   36.16  ? 649 HOH   A O    1 
HETATM 5014 O  O    . HOH   G 5 .   ? 7.273   1.978   -20.641 1   38.647 ? 650 HOH   A O    1 
HETATM 5015 O  O    . HOH   G 5 .   ? 2.242   -1.092  -31.873 1   34.45  ? 651 HOH   A O    1 
HETATM 5016 O  O    . HOH   G 5 .   ? 5.76    -2.236  -35.089 1   36.889 ? 652 HOH   A O    1 
HETATM 5017 O  O    . HOH   G 5 .   ? -18.894 -5.918  -29.459 1   17.062 ? 653 HOH   A O    1 
HETATM 5018 O  O    . HOH   G 5 .   ? -24.558 3.496   -30.365 1   15.042 ? 654 HOH   A O    1 
HETATM 5019 O  O    . HOH   G 5 .   ? -37.004 9.953   -32.97  1   21.281 ? 655 HOH   A O    1 
HETATM 5020 O  O    . HOH   G 5 .   ? 11.693  1.395   -52.892 1   32.18  ? 656 HOH   A O    1 
HETATM 5021 O  O    . HOH   G 5 .   ? -24.916 1.919   -41.957 1   56.348 ? 657 HOH   A O    1 
HETATM 5022 O  O    . HOH   G 5 .   ? -18.661 -6.528  -37.471 1   39.344 ? 658 HOH   A O    1 
HETATM 5023 O  O    . HOH   G 5 .   ? 12.182  18.162  -15.38  1   36.294 ? 659 HOH   A O    1 
HETATM 5024 O  O    . HOH   G 5 .   ? 14.981  -7.776  -31.572 1   34.27  ? 660 HOH   A O    1 
HETATM 5025 O  O    . HOH   G 5 .   ? 8.407   11.704  -47.703 1   34.782 ? 661 HOH   A O    1 
HETATM 5026 O  O    . HOH   G 5 .   ? -8.079  -5.016  -36.189 1   52.887 ? 662 HOH   A O    1 
HETATM 5027 O  O    . HOH   G 5 .   ? -7.418  -4.912  -28.476 1   31.065 ? 663 HOH   A O    1 
HETATM 5028 O  O    . HOH   G 5 .   ? 12.423  17.032  -42.565 1   28.091 ? 664 HOH   A O    1 
HETATM 5029 O  O    . HOH   G 5 .   ? -24.435 -4      -17.901 1   28.247 ? 665 HOH   A O    1 
HETATM 5030 O  O    . HOH   G 5 .   ? -33.18  7.692   -5.615  1   48.967 ? 666 HOH   A O    1 
HETATM 5031 O  O    . HOH   G 5 .   ? -12.741 20.546  -29.595 1   26.748 ? 667 HOH   A O    1 
HETATM 5032 O  O    . HOH   G 5 .   ? -31.254 15.969  -24.615 1   33.674 ? 668 HOH   A O    1 
HETATM 5033 O  O    . HOH   G 5 .   ? -15.852 21.446  -25.914 1   28.084 ? 669 HOH   A O    1 
HETATM 5034 O  O    . HOH   G 5 .   ? -22.601 -8.492  -25.515 1   38.738 ? 670 HOH   A O    1 
HETATM 5035 O  O    . HOH   G 5 .   ? -27.643 14.137  -35.111 1   43.211 ? 671 HOH   A O    1 
HETATM 5036 O  O    . HOH   G 5 .   ? -20.632 8.333   -36.784 1   23.119 ? 672 HOH   A O    1 
HETATM 5037 O  O    . HOH   G 5 .   ? -0.572  12.337  -38.054 1   38.707 ? 673 HOH   A O    1 
HETATM 5038 O  O    . HOH   G 5 .   ? -21.232 5.973   -38.089 1   22.171 ? 674 HOH   A O    1 
HETATM 5039 O  O    . HOH   G 5 .   ? 0.732   14.963  -15.768 1   33.224 ? 675 HOH   A O    1 
HETATM 5040 O  O    . HOH   G 5 .   ? 6.478   12.192  -14.669 1   32.501 ? 676 HOH   A O    1 
HETATM 5041 O  O    . HOH   G 5 .   ? -23.475 4.702   -37.29  1   22.308 ? 677 HOH   A O    1 
HETATM 5042 O  O    . HOH   G 5 .   ? -33.149 -1.413  -24.974 1   28.115 ? 678 HOH   A O    1 
HETATM 5043 O  O    . HOH   G 5 .   ? -12.671 18.687  -31.6   1   25.639 ? 679 HOH   A O    1 
HETATM 5044 O  O    . HOH   G 5 .   ? -26.368 2.442   -37.472 1   23.943 ? 680 HOH   A O    1 
HETATM 5045 O  O    . HOH   G 5 .   ? -31.576 2.617   -12.293 1   40.212 ? 681 HOH   A O    1 
HETATM 5046 O  O    . HOH   G 5 .   ? -22.939 2.787   -10.26  1   39.692 ? 682 HOH   A O    1 
HETATM 5047 O  O    . HOH   G 5 .   ? -22.894 21.285  -12.844 1   43.047 ? 683 HOH   A O    1 
HETATM 5048 O  O    . HOH   G 5 .   ? -11.035 5.725   -6.498  1   25.582 ? 684 HOH   A O    1 
HETATM 5049 O  O    . HOH   G 5 .   ? 5.298   16.349  -45.13  1   36.157 ? 685 HOH   A O    1 
HETATM 5050 O  O    . HOH   G 5 .   ? 14.874  15.415  -46.23  1   21.45  ? 686 HOH   A O    1 
HETATM 5051 O  O    . HOH   G 5 .   ? 3.758   17.78   -22.432 1   23.593 ? 687 HOH   A O    1 
HETATM 5052 O  O    . HOH   G 5 .   ? 9.119   1.274   -22.928 1   26.103 ? 688 HOH   A O    1 
HETATM 5053 O  O    . HOH   G 5 .   ? -23.088 5.35    -10.678 1   32.296 ? 689 HOH   A O    1 
HETATM 5054 O  O    . HOH   G 5 .   ? 3.31    -0.012  -28.929 1   36.203 ? 690 HOH   A O    1 
HETATM 5055 O  O    . HOH   G 5 .   ? 10.719  22.084  -34.676 1   27.773 ? 691 HOH   A O    1 
HETATM 5056 O  O    . HOH   G 5 .   ? 22.839  11.853  -24.613 1   18.11  ? 692 HOH   A O    1 
HETATM 5057 O  O    . HOH   G 5 .   ? -12.091 20.646  -12.595 1   26.948 ? 693 HOH   A O    1 
HETATM 5058 O  O    . HOH   G 5 .   ? 14.16   4.973   -17.383 1   24.305 ? 694 HOH   A O    1 
HETATM 5059 O  O    . HOH   G 5 .   ? 16.916  -9.648  -29.933 1   34.865 ? 695 HOH   A O    1 
HETATM 5060 O  O    . HOH   G 5 .   ? -37.249 15.194  -24.972 1   27.936 ? 696 HOH   A O    1 
HETATM 5061 O  O    . HOH   G 5 .   ? 9.197   -3.646  -32.874 1   22.732 ? 697 HOH   A O    1 
HETATM 5062 O  O    . HOH   G 5 .   ? -17.581 22.658  -15.554 1   29.1   ? 698 HOH   A O    1 
HETATM 5063 O  O    . HOH   G 5 .   ? -13.641 24.16   -20.386 1   45.814 ? 699 HOH   A O    1 
HETATM 5064 O  O    . HOH   G 5 .   ? 24.492  12.959  -30.727 1   23.199 ? 700 HOH   A O    1 
HETATM 5065 O  O    . HOH   G 5 .   ? -33.572 13.264  -30.932 1   28.306 ? 701 HOH   A O    1 
HETATM 5066 O  O    . HOH   G 5 .   ? 8.824   -1.477  -20.574 1   47.837 ? 702 HOH   A O    1 
HETATM 5067 O  O    . HOH   G 5 .   ? 24.097  8.846   -43.826 1   38.296 ? 703 HOH   A O    1 
HETATM 5068 O  O    . HOH   G 5 .   ? 1.768   8.012   -20.657 1   16.917 ? 704 HOH   A O    1 
HETATM 5069 O  O    . HOH   G 5 .   ? 3.457   10.204  -20.175 1   19.881 ? 705 HOH   A O    1 
HETATM 5070 O  O    . HOH   G 5 .   ? -20.935 16.819  -34.933 1   49.274 ? 706 HOH   A O    1 
HETATM 5071 O  O    . HOH   G 5 .   ? -17.016 -9.973  -22.33  1   20.447 ? 707 HOH   A O    1 
HETATM 5072 O  O    . HOH   G 5 .   ? -29.293 20.44   -9.565  1   26.48  ? 708 HOH   A O    1 
HETATM 5073 O  O    . HOH   G 5 .   ? 3.928   9.019   -37.855 1   17.69  ? 709 HOH   A O    1 
HETATM 5074 O  O    . HOH   G 5 .   ? -40.712 11.222  -25.87  1   28.351 ? 710 HOH   A O    1 
HETATM 5075 O  O    . HOH   G 5 .   ? 13.248  14.276  -48.402 1   21.819 ? 711 HOH   A O    1 
HETATM 5076 O  O    . HOH   G 5 .   ? 22.987  -6.866  -35.982 1   25.694 ? 712 HOH   A O    1 
HETATM 5077 O  O    . HOH   G 5 .   ? 16.266  18.189  -36.412 1   24.11  ? 713 HOH   A O    1 
HETATM 5078 O  O    . HOH   G 5 .   ? -27.589 -5.238  -19.982 1   30.159 ? 714 HOH   A O    1 
HETATM 5079 O  O    . HOH   G 5 .   ? 24.214  13.406  -39.392 1   38.658 ? 715 HOH   A O    1 
HETATM 5080 O  O    . HOH   G 5 .   ? -35.676 -0.521  -35.96  1   24.417 ? 716 HOH   A O    1 
HETATM 5081 O  O    . HOH   G 5 .   ? -19.161 5.947   -10.149 1   46.999 ? 717 HOH   A O    1 
HETATM 5082 O  O    . HOH   G 5 .   ? -11.388 14.029  -37.547 1   30.434 ? 718 HOH   A O    1 
HETATM 5083 O  O    . HOH   G 5 .   ? -28.614 5.828   -38.173 1   35.273 ? 719 HOH   A O    1 
HETATM 5084 O  O    . HOH   G 5 .   ? 16.338  16.723  -38.853 1   21.579 ? 720 HOH   A O    1 
HETATM 5085 O  O    . HOH   G 5 .   ? -31.047 4.772   -37.882 1   26.853 ? 721 HOH   A O    1 
HETATM 5086 O  O    . HOH   G 5 .   ? 19.941  7.447   -45.756 1   24.043 ? 722 HOH   A O    1 
HETATM 5087 O  O    . HOH   G 5 .   ? -43.407 4.424   -24.269 1   26.615 ? 723 HOH   A O    1 
HETATM 5088 O  O    . HOH   G 5 .   ? 19.688  -3.357  -23.059 1   35.509 ? 724 HOH   A O    1 
HETATM 5089 O  O    . HOH   G 5 .   ? 19.903  6.057   -42.798 1   22.651 ? 725 HOH   A O    1 
HETATM 5090 O  O    . HOH   G 5 .   ? -16.396 23.198  -17.911 1   30.056 ? 726 HOH   A O    1 
HETATM 5091 O  O    . HOH   G 5 .   ? 23.798  14.51   -17.18  1   34.945 ? 727 HOH   A O    1 
HETATM 5092 O  O    . HOH   G 5 .   ? -16.295 19.511  -29.546 1   34.977 ? 728 HOH   A O    1 
HETATM 5093 O  O    . HOH   G 5 .   ? 21.687  -2.025  -34.268 1   24.082 ? 729 HOH   A O    1 
HETATM 5094 O  O    . HOH   G 5 .   ? -6.948  15.451  -11.959 1   29.672 ? 730 HOH   A O    1 
HETATM 5095 O  O    . HOH   G 5 .   ? 12.913  20.089  -40.377 1   33.538 ? 731 HOH   A O    1 
HETATM 5096 O  O    . HOH   G 5 .   ? -39.949 13.829  -17.734 1   30.593 ? 732 HOH   A O    1 
HETATM 5097 O  O    . HOH   G 5 .   ? -25.301 -9.656  -22.409 1   41.213 ? 733 HOH   A O    1 
HETATM 5098 O  O    . HOH   G 5 .   ? 15.238  21.166  -32.818 1   44.976 ? 734 HOH   A O    1 
HETATM 5099 O  O    . HOH   G 5 .   ? -2.561  3.091   -15.605 1   26.606 ? 735 HOH   A O    1 
HETATM 5100 O  O    . HOH   G 5 .   ? -39.289 15.464  -23.189 1   33.227 ? 736 HOH   A O    1 
HETATM 5101 O  O    . HOH   G 5 .   ? 3.223   17.997  -42.96  1   26.433 ? 737 HOH   A O    1 
HETATM 5102 O  O    . HOH   G 5 .   ? -40.256 16.412  -18.634 1   46.787 ? 738 HOH   A O    1 
HETATM 5103 O  O    . HOH   G 5 .   ? 2.457   15.072  -29.415 1   24.15  ? 739 HOH   A O    1 
HETATM 5104 O  O    . HOH   G 5 .   ? -37.639 13.977  -27.497 1   30.836 ? 740 HOH   A O    1 
HETATM 5105 O  O    . HOH   G 5 .   ? 10.596  -5.07   -44.473 1   31.622 ? 741 HOH   A O    1 
HETATM 5106 O  O    . HOH   G 5 .   ? 22.727  9.954   -33.995 1   27.18  ? 742 HOH   A O    1 
HETATM 5107 O  O    . HOH   G 5 .   ? -31.649 3.321   -40.162 1   31.873 ? 743 HOH   A O    1 
HETATM 5108 O  O    . HOH   G 5 .   ? -30.151 12.835  -34.726 1   41.059 ? 744 HOH   A O    1 
HETATM 5109 O  O    . HOH   G 5 .   ? 7.037   17.45   -27.414 1   29.05  ? 745 HOH   A O    1 
HETATM 5110 O  O    . HOH   G 5 .   ? -11.923 13.501  -7.962  1   41.286 ? 746 HOH   A O    1 
HETATM 5111 O  O    . HOH   G 5 .   ? 16.607  4.403   -18.541 1   32.639 ? 747 HOH   A O    1 
HETATM 5112 O  O    . HOH   G 5 .   ? -42.331 -1.853  -32.189 1   50.743 ? 748 HOH   A O    1 
HETATM 5113 O  O    . HOH   G 5 .   ? -35.788 12.45   -29.137 1   26.378 ? 749 HOH   A O    1 
HETATM 5114 O  O    . HOH   G 5 .   ? -14.785 13.998  -8.316  1   34.79  ? 750 HOH   A O    1 
HETATM 5115 O  O    . HOH   G 5 .   ? 13.176  16.723  -13.378 1   43.763 ? 751 HOH   A O    1 
HETATM 5116 O  O    . HOH   G 5 .   ? -24.294 10.433  -38.043 1   59.004 ? 752 HOH   A O    1 
HETATM 5117 O  O    . HOH   G 5 .   ? 12.857  -4.95   -35.525 1   60.764 ? 753 HOH   A O    1 
HETATM 5118 O  O    . HOH   G 5 .   ? 19.864  1.344   -41.455 1   32.923 ? 754 HOH   A O    1 
HETATM 5119 O  O    . HOH   G 5 .   ? -20.493 -8.945  -31.924 1   45.065 ? 755 HOH   A O    1 
HETATM 5120 O  O    . HOH   G 5 .   ? -0.58   13.038  -30.863 1   31.807 ? 756 HOH   A O    1 
HETATM 5121 O  O    . HOH   G 5 .   ? -28.729 -6.536  -22.524 1   44.82  ? 757 HOH   A O    1 
HETATM 5122 O  O    . HOH   G 5 .   ? -16.325 9.765   -7.469  1   45.623 ? 758 HOH   A O    1 
HETATM 5123 O  O    . HOH   G 5 .   ? -15.758 16.603  -29.925 1   28.786 ? 759 HOH   A O    1 
HETATM 5124 O  O    . HOH   G 5 .   ? 0.48    11.566  -34.708 1   29.755 ? 760 HOH   A O    1 
HETATM 5125 O  O    . HOH   G 5 .   ? -14.963 9.83    -39.768 1   38.52  ? 761 HOH   A O    1 
HETATM 5126 O  O    . HOH   G 5 .   ? 15.412  12.552  -12.977 1   39.496 ? 762 HOH   A O    1 
HETATM 5127 O  O    . HOH   G 5 .   ? 25.429  -1.192  -36.972 1   30.196 ? 763 HOH   A O    1 
HETATM 5128 O  O    . HOH   G 5 .   ? -2.397  14.42   -32.675 1   31.737 ? 764 HOH   A O    1 
HETATM 5129 O  O    . HOH   G 5 .   ? -33.417 17.353  -24.279 1   47.862 ? 765 HOH   A O    1 
HETATM 5130 O  O    . HOH   G 5 .   ? -25.716 -3.502  -24.457 1   22.478 ? 766 HOH   A O    1 
HETATM 5131 O  O    . HOH   G 5 .   ? -0.178  12.46   -40.817 1   30.471 ? 767 HOH   A O    1 
HETATM 5132 O  O    . HOH   G 5 .   ? 12.954  2.554   -17.406 1   28.07  ? 768 HOH   A O    1 
HETATM 5133 O  O    . HOH   G 5 .   ? -13.503 22.867  -27.059 1   29.598 ? 769 HOH   A O    1 
HETATM 5134 O  O    . HOH   G 5 .   ? 23.144  17.278  -34.773 1   46.15  ? 770 HOH   A O    1 
HETATM 5135 O  O    . HOH   G 5 .   ? -40.166 13.008  -27.675 1   28.944 ? 771 HOH   A O    1 
HETATM 5136 O  O    . HOH   G 5 .   ? -43.4   -2.273  -34.925 1   36.207 ? 772 HOH   A O    1 
HETATM 5137 O  O    . HOH   G 5 .   ? 22.621  16.693  -39.458 1   82.983 ? 773 HOH   A O    1 
HETATM 5138 O  O    . HOH   G 5 .   ? -39.473 -1.261  -32.786 1   32.681 ? 774 HOH   A O    1 
HETATM 5139 O  O    . HOH   G 5 .   ? -0.299  20.701  -43.214 1   38.525 ? 775 HOH   A O    1 
HETATM 5140 O  O    . HOH   G 5 .   ? -14.999 18.587  -32.901 1   35.067 ? 776 HOH   A O    1 
HETATM 5141 O  O    . HOH   G 5 .   ? -37.695 11.121  -30.57  1   25.135 ? 777 HOH   A O    1 
HETATM 5142 O  O    . HOH   G 5 .   ? 14.867  14.157  -50.639 1   36.553 ? 778 HOH   A O    1 
HETATM 5143 O  O    . HOH   G 5 .   ? 6.645   4.175   -49.553 1   48.729 ? 779 HOH   A O    1 
HETATM 5144 O  O    . HOH   G 5 .   ? 23.271  9.076   -46.434 1   31.062 ? 780 HOH   A O    1 
HETATM 5145 O  O    . HOH   G 5 .   ? -24.685 21.06   -20.65  1   41.619 ? 781 HOH   A O    1 
HETATM 5146 O  O    . HOH   G 5 .   ? -12.26  7.215   -41.5   1   41.6   ? 782 HOH   A O    1 
HETATM 5147 O  O    . HOH   G 5 .   ? 10.687  15.12   -48.441 1   44.384 ? 783 HOH   A O    1 
HETATM 5148 O  O    . HOH   G 5 .   ? 10.535  19.951  -23.65  1   36.646 ? 784 HOH   A O    1 
HETATM 5149 O  O    . HOH   G 5 .   ? 23.387  12.598  -33.241 1   26.752 ? 785 HOH   A O    1 
HETATM 5150 O  O    . HOH   G 5 .   ? 25.633  15.012  -26.937 1   37.22  ? 786 HOH   A O    1 
HETATM 5151 O  O    . HOH   G 5 .   ? -21.969 18.809  -27.253 1   36.578 ? 787 HOH   A O    1 
HETATM 5152 O  O    . HOH   G 5 .   ? -31.65  21.948  -13.647 1   55.416 ? 788 HOH   A O    1 
HETATM 5153 O  O    . HOH   G 5 .   ? -3.259  -4.543  -26.607 1   27.601 ? 789 HOH   A O    1 
HETATM 5154 O  O    . HOH   G 5 .   ? -21.069 -10.559 -25.27  1   41.926 ? 790 HOH   A O    1 
HETATM 5155 O  O    . HOH   G 5 .   ? 2.927   22.111  -25.336 1   40.404 ? 791 HOH   A O    1 
HETATM 5156 O  O    . HOH   G 5 .   ? 21.004  13.314  -46.302 1   31.509 ? 792 HOH   A O    1 
HETATM 5157 O  O    . HOH   G 5 .   ? 13.363  17.29   -45.088 1   29.274 ? 793 HOH   A O    1 
HETATM 5158 O  O    . HOH   G 5 .   ? -2.24   13.937  -37.05  1   40.036 ? 794 HOH   A O    1 
HETATM 5159 O  O    . HOH   G 5 .   ? -15.615 -11.452 -26.199 1   37.578 ? 795 HOH   A O    1 
HETATM 5160 O  O    . HOH   G 5 .   ? 21.088  10.881  -47.741 1   28.133 ? 796 HOH   A O    1 
HETATM 5161 O  O    . HOH   G 5 .   ? 1.387   8.463   -37.671 1   46.716 ? 797 HOH   A O    1 
HETATM 5162 O  O    . HOH   G 5 .   ? 10.512  0.216   -16.14  1   27.198 ? 798 HOH   A O    1 
HETATM 5163 O  O    . HOH   G 5 .   ? -16.855 -10.312 -31.275 1   52.729 ? 799 HOH   A O    1 
HETATM 5164 O  O    . HOH   G 5 .   ? -25.72  -8.363  -25.139 1   36.537 ? 800 HOH   A O    1 
HETATM 5165 O  O    . HOH   G 5 .   ? 8.977   1.738   -52.399 1   30.817 ? 801 HOH   A O    1 
HETATM 5166 O  O    . HOH   G 5 .   ? -25.248 4.034   -39.478 1   39.032 ? 802 HOH   A O    1 
HETATM 5167 O  O    . HOH   G 5 .   ? -20.57  -8.211  -29.313 1   25.816 ? 803 HOH   A O    1 
HETATM 5168 O  O    . HOH   G 5 .   ? 12.443  -6.976  -43.648 1   38.885 ? 804 HOH   A O    1 
HETATM 5169 O  O    . HOH   G 5 .   ? -9.759  3.537   -42.127 1   42.078 ? 805 HOH   A O    1 
HETATM 5170 O  O    . HOH   G 5 .   ? -17.363 -11.018 -19.742 1   40.926 ? 806 HOH   A O    1 
HETATM 5171 O  O    . HOH   G 5 .   ? -26.371 -6.072  -23.858 1   25.821 ? 807 HOH   A O    1 
HETATM 5172 O  O    . HOH   G 5 .   ? -5.46   21.334  -23.4   1   46.36  ? 808 HOH   A O    1 
HETATM 5173 O  O    . HOH   G 5 .   ? -27.273 17.224  -33.781 1   55.303 ? 809 HOH   A O    1 
HETATM 5174 O  O    . HOH   G 5 .   ? 17.465  16.104  -45.897 1   30.835 ? 810 HOH   A O    1 
HETATM 5175 O  O    . HOH   G 5 .   ? 20.295  11.929  -50.601 1   32.936 ? 811 HOH   A O    1 
HETATM 5176 O  O    . HOH   G 5 .   ? -16.834 -11.964 -33.4   1   46.489 ? 812 HOH   A O    1 
HETATM 5177 O  O    . HOH   G 5 .   ? 11.534  17.69   -47.072 1   47.364 ? 813 HOH   A O    1 
HETATM 5178 O  O    . HOH   G 5 .   ? -0.43   5.977   -45.806 1   43.697 ? 814 HOH   A O    1 
HETATM 5179 O  O    . HOH   G 5 .   ? 18.596  19.728  -36.171 1   36.609 ? 815 HOH   A O    1 
HETATM 5180 O  O    . HOH   G 5 .   ? -16.407 23.676  -24.534 1   38.404 ? 816 HOH   A O    1 
HETATM 5181 O  O    . HOH   G 5 .   ? 18.802  17.128  -40.084 1   35.133 ? 817 HOH   A O    1 
HETATM 5182 O  O    . HOH   G 5 .   ? -19.001 -11.476 -23.697 1   30.223 ? 818 HOH   A O    1 
HETATM 5183 O  O    . HOH   G 5 .   ? -19.386 -8.364  -35.098 1   50.573 ? 819 HOH   A O    1 
HETATM 5184 O  O    . HOH   G 5 .   ? -6.08   8.945   -41.759 1   40.767 ? 820 HOH   A O    1 
HETATM 5185 O  O    . HOH   G 5 .   ? 4.514   20.088  -23.926 1   39.546 ? 821 HOH   A O    1 
HETATM 5186 O  O    . HOH   G 5 .   ? 9.331   -4.192  -37.446 1   32.692 ? 822 HOH   A O    1 
HETATM 5187 O  O    . HOH   G 5 .   ? -34.499 11.263  -33.096 1   29.702 ? 823 HOH   A O    1 
HETATM 5188 O  O    . HOH   G 5 .   ? 14.522  17.94   -40.779 1   24.12  ? 824 HOH   A O    1 
HETATM 5189 O  O    . HOH   G 5 .   ? 17.175  15.547  -50.603 1   46.804 ? 825 HOH   A O    1 
HETATM 5190 O  O    . HOH   G 5 .   ? 5.761   21.827  -28.077 1   34.181 ? 826 HOH   A O    1 
HETATM 5191 O  O    . HOH   G 5 .   ? 6.73    20.044  -26.151 1   32.237 ? 827 HOH   A O    1 
HETATM 5192 O  O    . HOH   G 5 .   ? 19.655  14.493  -51.065 1   40.464 ? 828 HOH   A O    1 
HETATM 5193 O  O    . HOH   G 5 .   ? -19.917 -10.503 -28.191 1   49.049 ? 829 HOH   A O    1 
HETATM 5194 O  O    . HOH   G 5 .   ? 8.491   21.284  -24.94  1   33.243 ? 830 HOH   A O    1 
HETATM 5195 O  O    . HOH   G 5 .   ? 16.765  18.926  -42.219 1   36.134 ? 831 HOH   A O    1 
HETATM 5196 O  O    . HOH   H 5 .   ? -11.215 7.212   9.291   1   37.01  ? 501 HOH   B O    1 
HETATM 5197 O  O    . HOH   H 5 .   ? 0.166   24.672  7.583   1   34.483 ? 502 HOH   B O    1 
HETATM 5198 O  O    . HOH   H 5 .   ? -1.856  6.943   12.515  1   61.514 ? 503 HOH   B O    1 
HETATM 5199 O  O    . HOH   H 5 .   ? 11.416  -0.265  11.268  1   24.931 ? 504 HOH   B O    1 
HETATM 5200 O  O    . HOH   H 5 .   ? 10.02   -9.492  -17.991 1   46.255 ? 505 HOH   B O    1 
HETATM 5201 O  O    . HOH   H 5 .   ? 22.527  9.032   10.23   1   38.761 ? 506 HOH   B O    1 
HETATM 5202 O  O    . HOH   H 5 .   ? 23.011  17.404  10.351  1   39.66  ? 507 HOH   B O    1 
HETATM 5203 O  O    . HOH   H 5 .   ? 0.634   -14.355 -30.839 1   36.725 ? 508 HOH   B O    1 
HETATM 5204 O  O    . HOH   H 5 .   ? 14.277  18.334  3.006   1   21.722 ? 509 HOH   B O    1 
HETATM 5205 O  O    . HOH   H 5 .   ? -13.453 17.812  8.411   1   66.815 ? 510 HOH   B O    1 
HETATM 5206 O  O    . HOH   H 5 .   ? 2.409   -28.759 -7.347  1   40.683 ? 511 HOH   B O    1 
HETATM 5207 O  O    . HOH   H 5 .   ? -8.294  -2.844  0.277   1   31.278 ? 512 HOH   B O    1 
HETATM 5208 O  O    . HOH   H 5 .   ? 26.113  15.718  7.1     1   39.548 ? 513 HOH   B O    1 
HETATM 5209 O  O    . HOH   H 5 .   ? 0.287   9.802   -4.173  1   22.23  ? 514 HOH   B O    1 
HETATM 5210 O  O    . HOH   H 5 .   ? -10.701 -8.072  -21.57  1   27.495 ? 515 HOH   B O    1 
HETATM 5211 O  O    . HOH   H 5 .   ? 10.042  -27.968 -5.654  1   46.339 ? 516 HOH   B O    1 
HETATM 5212 O  O    . HOH   H 5 .   ? 6.148   10.979  -12.353 1   19.146 ? 517 HOH   B O    1 
HETATM 5213 O  O    . HOH   H 5 .   ? 2.203   5.751   10.217  1   50.566 ? 518 HOH   B O    1 
HETATM 5214 O  O    . HOH   H 5 .   ? 10.583  17.557  -11.272 1   38.278 ? 519 HOH   B O    1 
HETATM 5215 O  O    . HOH   H 5 .   ? -0.42   -1.973  8.966   1   32.2   ? 520 HOH   B O    1 
HETATM 5216 O  O    . HOH   H 5 .   ? -10.934 10.716  -1.105  1   31.607 ? 521 HOH   B O    1 
HETATM 5217 O  O    . HOH   H 5 .   ? 19.09   7.479   -10.748 1   27.855 ? 522 HOH   B O    1 
HETATM 5218 O  O    . HOH   H 5 .   ? 15.278  22.084  0.181   1   40.308 ? 523 HOH   B O    1 
HETATM 5219 O  O    . HOH   H 5 .   ? 15.347  -12.903 -14.388 1   34.493 ? 524 HOH   B O    1 
HETATM 5220 O  O    . HOH   H 5 .   ? -7.951  -19.599 -25.855 1   40.911 ? 525 HOH   B O    1 
HETATM 5221 O  O    . HOH   H 5 .   ? 20.24   16.563  -0.895  1   39.18  ? 526 HOH   B O    1 
HETATM 5222 O  O    . HOH   H 5 .   ? 3.863   -12.02  -3.254  1   39.829 ? 527 HOH   B O    1 
HETATM 5223 O  O    . HOH   H 5 .   ? 11.267  -12.488 -27.874 1   28.397 ? 528 HOH   B O    1 
HETATM 5224 O  O    . HOH   H 5 .   ? 9.373   -18.244 -4.389  1   31.724 ? 529 HOH   B O    1 
HETATM 5225 O  O    . HOH   H 5 .   ? -2.816  10.698  16.241  1   37.327 ? 530 HOH   B O    1 
HETATM 5226 O  O    . HOH   H 5 .   ? 28.375  7.985   2.846   1   34.873 ? 531 HOH   B O    1 
HETATM 5227 O  O    . HOH   H 5 .   ? 7.267   -7.384  -16.539 1   28.623 ? 532 HOH   B O    1 
HETATM 5228 O  O    . HOH   H 5 .   ? 3.565   -2.936  -13.78  1   19.293 ? 533 HOH   B O    1 
HETATM 5229 O  O    . HOH   H 5 .   ? -11.549 -16.949 -23.071 1   53.631 ? 534 HOH   B O    1 
HETATM 5230 O  O    . HOH   H 5 .   ? 4.872   -19.14  -1.7    1   32.063 ? 535 HOH   B O    1 
HETATM 5231 O  O    . HOH   H 5 .   ? 10.36   14.998  -3.495  1   17.251 ? 536 HOH   B O    1 
HETATM 5232 O  O    . HOH   H 5 .   ? -3.193  0.058   -26.127 1   24.041 ? 537 HOH   B O    1 
HETATM 5233 O  O    . HOH   H 5 .   ? -4.73   8.777   9.825   1   23.32  ? 538 HOH   B O    1 
HETATM 5234 O  O    . HOH   H 5 .   ? -2.945  -8.307  -7.097  1   29.088 ? 539 HOH   B O    1 
HETATM 5235 O  O    . HOH   H 5 .   ? 5.294   7.929   16.716  1   47.387 ? 540 HOH   B O    1 
HETATM 5236 O  O    . HOH   H 5 .   ? 16.463  16.27   -5.942  1   37.214 ? 541 HOH   B O    1 
HETATM 5237 O  O    . HOH   H 5 .   ? 17.826  -5.193  -3.022  1   28.285 ? 542 HOH   B O    1 
HETATM 5238 O  O    . HOH   H 5 .   ? -7.293  17.353  14.939  1   36.33  ? 543 HOH   B O    1 
HETATM 5239 O  O    . HOH   H 5 .   ? 9.837   -12.55  -30.239 1   27.5   ? 544 HOH   B O    1 
HETATM 5240 O  O    . HOH   H 5 .   ? 19.233  -25.287 -11.704 1   36.551 ? 545 HOH   B O    1 
HETATM 5241 O  O    . HOH   H 5 .   ? -15.689 -11.967 -17.912 1   44.412 ? 546 HOH   B O    1 
HETATM 5242 O  O    . HOH   H 5 .   ? 14.092  -2.654  5.443   1   29.248 ? 547 HOH   B O    1 
HETATM 5243 O  O    . HOH   H 5 .   ? 12.835  18.432  -4.458  1   25.895 ? 548 HOH   B O    1 
HETATM 5244 O  O    . HOH   H 5 .   ? 10.982  17.528  -2.582  1   20.297 ? 549 HOH   B O    1 
HETATM 5245 O  O    . HOH   H 5 .   ? 1.245   24.659  10.173  1   35.45  ? 550 HOH   B O    1 
HETATM 5246 O  O    . HOH   H 5 .   ? 23.937  -4.629  -5.831  1   33.5   ? 551 HOH   B O    1 
HETATM 5247 O  O    . HOH   H 5 .   ? 10.63   -34.577 -10.572 1   41.841 ? 552 HOH   B O    1 
HETATM 5248 O  O    . HOH   H 5 .   ? 6.505   18.21   -4.566  1   20.963 ? 553 HOH   B O    1 
HETATM 5249 O  O    . HOH   H 5 .   ? 6.541   -13.06  -2.073  1   34.005 ? 554 HOH   B O    1 
HETATM 5250 O  O    . HOH   H 5 .   ? -4.507  16.545  -10.172 1   32.274 ? 555 HOH   B O    1 
HETATM 5251 O  O    . HOH   H 5 .   ? -2.678  -4.353  -8.013  1   23.19  ? 556 HOH   B O    1 
HETATM 5252 O  O    . HOH   H 5 .   ? -1.347  20.959  -4.153  1   40.392 ? 557 HOH   B O    1 
HETATM 5253 O  O    . HOH   H 5 .   ? 25.499  2.542   -5.435  1   40.221 ? 558 HOH   B O    1 
HETATM 5254 O  O    . HOH   H 5 .   ? 9.362   -15.383 -4.616  1   42.626 ? 559 HOH   B O    1 
HETATM 5255 O  O    . HOH   H 5 .   ? -8.743  -8.639  -27.829 1   28.386 ? 560 HOH   B O    1 
HETATM 5256 O  O    . HOH   H 5 .   ? 12.239  -14.105 -19.046 1   24.086 ? 561 HOH   B O    1 
HETATM 5257 O  O    . HOH   H 5 .   ? 22.723  15.608  0.072   1   38.36  ? 562 HOH   B O    1 
HETATM 5258 O  O    . HOH   H 5 .   ? 7.976   25.59   6.398   1   41.934 ? 563 HOH   B O    1 
HETATM 5259 O  O    . HOH   H 5 .   ? 3.113   23.428  1.817   1   35.861 ? 564 HOH   B O    1 
HETATM 5260 O  O    . HOH   H 5 .   ? 0.202   -8.06   2.81    1   37.922 ? 565 HOH   B O    1 
HETATM 5261 O  O    . HOH   H 5 .   ? -6.318  15.001  -8.666  1   24.598 ? 566 HOH   B O    1 
HETATM 5262 O  O    . HOH   H 5 .   ? 12.142  7.036   13.683  1   21.01  ? 567 HOH   B O    1 
HETATM 5263 O  O    . HOH   H 5 .   ? 9.121   10.381  -14.575 1   27.528 ? 568 HOH   B O    1 
HETATM 5264 O  O    . HOH   H 5 .   ? 10.42   -8.409  -15.403 1   30.674 ? 569 HOH   B O    1 
HETATM 5265 O  O    . HOH   H 5 .   ? -1.264  -0.615  11.206  1   41.031 ? 570 HOH   B O    1 
HETATM 5266 O  O    . HOH   H 5 .   ? 15.354  -17.459 -21.744 1   33.052 ? 571 HOH   B O    1 
HETATM 5267 O  O    . HOH   H 5 .   ? 20.936  0.8     -7.746  1   29.989 ? 572 HOH   B O    1 
HETATM 5268 O  O    . HOH   H 5 .   ? -8.747  13.379  -11.64  1   15.56  ? 573 HOH   B O    1 
HETATM 5269 O  O    . HOH   H 5 .   ? 15.86   -0.77   6.037   1   27.476 ? 574 HOH   B O    1 
HETATM 5270 O  O    . HOH   H 5 .   ? 8.067   -2.512  -10.453 1   14.904 ? 575 HOH   B O    1 
HETATM 5271 O  O    . HOH   H 5 .   ? -12.418 -12.355 -19.854 1   38.791 ? 576 HOH   B O    1 
HETATM 5272 O  O    . HOH   H 5 .   ? 1.11    -26.371 -22.296 1   22.528 ? 577 HOH   B O    1 
HETATM 5273 O  O    . HOH   H 5 .   ? 19.478  22.054  1.732   1   38.879 ? 578 HOH   B O    1 
HETATM 5274 O  O    . HOH   H 5 .   ? 16.439  -15.377 -17.778 1   32.179 ? 579 HOH   B O    1 
HETATM 5275 O  O    . HOH   H 5 .   ? 13.973  -28.28  -7.532  1   31.43  ? 580 HOH   B O    1 
HETATM 5276 O  O    . HOH   H 5 .   ? 18.906  -18.209 -9.795  1   38.752 ? 581 HOH   B O    1 
HETATM 5277 O  O    . HOH   H 5 .   ? 11.943  -14.462 -30.624 1   39.509 ? 582 HOH   B O    1 
HETATM 5278 O  O    . HOH   H 5 .   ? 4.005   -29.771 -3.568  1   45.813 ? 583 HOH   B O    1 
HETATM 5279 O  O    . HOH   H 5 .   ? 2.687   -12.589 -7.015  1   23.347 ? 584 HOH   B O    1 
HETATM 5280 O  O    . HOH   H 5 .   ? -0.989  -5.384  -12.438 1   18.805 ? 585 HOH   B O    1 
HETATM 5281 O  O    . HOH   H 5 .   ? 12.441  -11.486 -2.487  1   21.951 ? 586 HOH   B O    1 
HETATM 5282 O  O    . HOH   H 5 .   ? 1.254   1.752   13.706  1   36.647 ? 587 HOH   B O    1 
HETATM 5283 O  O    . HOH   H 5 .   ? -3.61   -25.358 -9.259  1   41.107 ? 588 HOH   B O    1 
HETATM 5284 O  O    . HOH   H 5 .   ? 20.532  7.929   -6.071  1   33.428 ? 589 HOH   B O    1 
HETATM 5285 O  O    . HOH   H 5 .   ? 13.871  -7.82   -13.022 1   50.985 ? 590 HOH   B O    1 
HETATM 5286 O  O    . HOH   H 5 .   ? 4.034   -2.376  8.632   1   23.835 ? 591 HOH   B O    1 
HETATM 5287 O  O    . HOH   H 5 .   ? 4.929   -15.156 -3.462  1   38.806 ? 592 HOH   B O    1 
HETATM 5288 O  O    . HOH   H 5 .   ? -8.633  -22.841 -22.804 1   42.83  ? 593 HOH   B O    1 
HETATM 5289 O  O    . HOH   H 5 .   ? 24.408  12.685  15.828  1   50.423 ? 594 HOH   B O    1 
HETATM 5290 O  O    . HOH   H 5 .   ? -3.908  -3.762  7.771   1   43.816 ? 595 HOH   B O    1 
HETATM 5291 O  O    . HOH   H 5 .   ? 9.847   24.58   -1.678  1   42.002 ? 596 HOH   B O    1 
HETATM 5292 O  O    . HOH   H 5 .   ? -7.176  -18.934 -30.058 1   47.517 ? 597 HOH   B O    1 
HETATM 5293 O  O    . HOH   H 5 .   ? 14.969  -20.132 -8.282  1   25.593 ? 598 HOH   B O    1 
HETATM 5294 O  O    . HOH   H 5 .   ? 2.154   13.453  15.195  1   31.088 ? 599 HOH   B O    1 
HETATM 5295 O  O    . HOH   H 5 .   ? 15.724  -9.368  -2.014  1   17.593 ? 600 HOH   B O    1 
HETATM 5296 O  O    . HOH   H 5 .   ? 13.85   16.032  1.437   1   20.66  ? 601 HOH   B O    1 
HETATM 5297 O  O    . HOH   H 5 .   ? -10.416 17.044  1.411   1   36.54  ? 602 HOH   B O    1 
HETATM 5298 O  O    . HOH   H 5 .   ? 7.53    -7.672  2.514   1   25.603 ? 603 HOH   B O    1 
HETATM 5299 O  O    . HOH   H 5 .   ? 11.859  0.075   -1.461  1   15.134 ? 604 HOH   B O    1 
HETATM 5300 O  O    . HOH   H 5 .   ? 26.399  0.534   -1.046  1   43.454 ? 605 HOH   B O    1 
HETATM 5301 O  O    . HOH   H 5 .   ? -0.611  22.075  19.478  1   35.397 ? 606 HOH   B O    1 
HETATM 5302 O  O    . HOH   H 5 .   ? 16.849  -25.553 -18.579 1   57.348 ? 607 HOH   B O    1 
HETATM 5303 O  O    . HOH   H 5 .   ? 1.352   17.769  -10.404 1   31.697 ? 608 HOH   B O    1 
HETATM 5304 O  O    . HOH   H 5 .   ? 15.724  -16.265 -6.408  1   38.558 ? 609 HOH   B O    1 
HETATM 5305 O  O    . HOH   H 5 .   ? 12.899  0.317   7.676   1   25.409 ? 610 HOH   B O    1 
HETATM 5306 O  O    . HOH   H 5 .   ? -13.471 7.598   6.469   1   47.554 ? 611 HOH   B O    1 
HETATM 5307 O  O    . HOH   H 5 .   ? 17.485  10.792  -11.878 1   30.426 ? 612 HOH   B O    1 
HETATM 5308 O  O    . HOH   H 5 .   ? 13.539  -17.874 -30.197 1   38.372 ? 613 HOH   B O    1 
HETATM 5309 O  O    . HOH   H 5 .   ? 27.075  3.02    1.991   1   43.124 ? 614 HOH   B O    1 
HETATM 5310 O  O    . HOH   H 5 .   ? -1.214  -7.072  -5.219  1   24.03  ? 615 HOH   B O    1 
HETATM 5311 O  O    . HOH   H 5 .   ? 2.691   -11.034 -15.139 1   13.358 ? 616 HOH   B O    1 
HETATM 5312 O  O    . HOH   H 5 .   ? 1.495   0.348   4.93    1   18.056 ? 617 HOH   B O    1 
HETATM 5313 O  O    . HOH   H 5 .   ? 19.053  14.118  -3.6    1   32.361 ? 618 HOH   B O    1 
HETATM 5314 O  O    . HOH   H 5 .   ? 14.95   -4.833  -11.388 1   37.209 ? 619 HOH   B O    1 
HETATM 5315 O  O    . HOH   H 5 .   ? 12.632  9.663   4.885   1   14.788 ? 620 HOH   B O    1 
HETATM 5316 O  O    . HOH   H 5 .   ? 16.341  -17.115 -8.965  1   37.656 ? 621 HOH   B O    1 
HETATM 5317 O  O    . HOH   H 5 .   ? -10.943 12.873  -5.545  1   35.691 ? 622 HOH   B O    1 
HETATM 5318 O  O    . HOH   H 5 .   ? 9.744   2.603   -15.276 1   24.074 ? 623 HOH   B O    1 
HETATM 5319 O  O    . HOH   H 5 .   ? 12.403  2.751   -12.622 1   20.242 ? 624 HOH   B O    1 
HETATM 5320 O  O    . HOH   H 5 .   ? 9.837   -6.959  3.948   1   24.041 ? 625 HOH   B O    1 
HETATM 5321 O  O    . HOH   H 5 .   ? -5.324  -5.337  1.759   1   49.739 ? 626 HOH   B O    1 
HETATM 5322 O  O    . HOH   H 5 .   ? -4.994  -7.406  -25.49  1   25.159 ? 627 HOH   B O    1 
HETATM 5323 O  O    . HOH   H 5 .   ? 12.91   -12.037 -17.35  1   33.765 ? 628 HOH   B O    1 
HETATM 5324 O  O    . HOH   H 5 .   ? 3.669   -8.448  4.764   1   40.661 ? 629 HOH   B O    1 
HETATM 5325 O  O    . HOH   H 5 .   ? -3.131  -4.49   -13.981 1   16.388 ? 630 HOH   B O    1 
HETATM 5326 O  O    . HOH   H 5 .   ? 8.795   -4.612  -14.901 1   42.682 ? 631 HOH   B O    1 
HETATM 5327 O  O    . HOH   H 5 .   ? 27.119  10.279  2.955   1   35.324 ? 632 HOH   B O    1 
HETATM 5328 O  O    . HOH   H 5 .   ? 9.888   26.709  0.554   1   56     ? 633 HOH   B O    1 
HETATM 5329 O  O    . HOH   H 5 .   ? 8.708   27.246  4.158   1   47.258 ? 634 HOH   B O    1 
HETATM 5330 O  O    . HOH   H 5 .   ? 8.827   11.389  17.273  1   47.854 ? 635 HOH   B O    1 
HETATM 5331 O  O    . HOH   H 5 .   ? 22.652  8.255   -4.538  1   33.494 ? 636 HOH   B O    1 
HETATM 5332 O  O    . HOH   H 5 .   ? 0.645   -11.37  -29.367 1   26.639 ? 637 HOH   B O    1 
HETATM 5333 O  O    . HOH   H 5 .   ? 12.246  -5.617  3.237   1   18.085 ? 638 HOH   B O    1 
HETATM 5334 O  O    . HOH   H 5 .   ? 16.881  9.964   -5.179  1   19.29  ? 639 HOH   B O    1 
HETATM 5335 O  O    . HOH   H 5 .   ? 21.768  15.505  11.868  1   35.928 ? 640 HOH   B O    1 
HETATM 5336 O  O    . HOH   H 5 .   ? -4.346  0.302   9.137   1   23.213 ? 641 HOH   B O    1 
HETATM 5337 O  O    . HOH   H 5 .   ? 23.454  -6.223  -9.672  1   48.83  ? 642 HOH   B O    1 
HETATM 5338 O  O    . HOH   H 5 .   ? 12.622  -9.605  -14.629 1   38.593 ? 643 HOH   B O    1 
HETATM 5339 O  O    . HOH   H 5 .   ? 24.756  15.581  9.537   1   38.836 ? 644 HOH   B O    1 
HETATM 5340 O  O    . HOH   H 5 .   ? -7.324  -26.026 -23.512 1   32.061 ? 645 HOH   B O    1 
HETATM 5341 O  O    . HOH   H 5 .   ? 5.252   -31.865 -8.675  1   31.128 ? 646 HOH   B O    1 
HETATM 5342 O  O    . HOH   H 5 .   ? 13.625  -22.565 -8.193  1   27.874 ? 647 HOH   B O    1 
HETATM 5343 O  O    . HOH   H 5 .   ? 22.878  -8.675  -5.51   1   31.269 ? 648 HOH   B O    1 
HETATM 5344 O  O    . HOH   H 5 .   ? -2.936  -26.881 -11.512 1   34.76  ? 649 HOH   B O    1 
HETATM 5345 O  O    . HOH   H 5 .   ? 11.458  -12.314 -21.056 1   21.884 ? 650 HOH   B O    1 
HETATM 5346 O  O    . HOH   H 5 .   ? 0.314   -5.737  6.543   1   27.058 ? 651 HOH   B O    1 
HETATM 5347 O  O    . HOH   H 5 .   ? 1.295   -8.118  -22.186 1   30.912 ? 652 HOH   B O    1 
HETATM 5348 O  O    . HOH   H 5 .   ? -2.019  -2.653  -0.914  1   18.206 ? 653 HOH   B O    1 
HETATM 5349 O  O    . HOH   H 5 .   ? -14.71  -10.393 -23.888 1   22.043 ? 654 HOH   B O    1 
HETATM 5350 O  O    . HOH   H 5 .   ? 15.858  -3.115  -9.49   1   23.741 ? 655 HOH   B O    1 
HETATM 5351 O  O    . HOH   H 5 .   ? 6.241   -23.064 -25.043 1   25.844 ? 656 HOH   B O    1 
HETATM 5352 O  O    . HOH   H 5 .   ? 6.383   -25.624 -26.399 1   35.632 ? 657 HOH   B O    1 
HETATM 5353 O  O    . HOH   H 5 .   ? 11.443  21.674  -2.724  1   32.202 ? 658 HOH   B O    1 
HETATM 5354 O  O    . HOH   H 5 .   ? 28.707  6.702   0.073   1   42.538 ? 659 HOH   B O    1 
HETATM 5355 O  O    . HOH   H 5 .   ? 8.605   20.053  -4.937  1   31.993 ? 660 HOH   B O    1 
HETATM 5356 O  O    . HOH   H 5 .   ? -14.077 -4.709  -5.506  1   42.383 ? 661 HOH   B O    1 
HETATM 5357 O  O    . HOH   H 5 .   ? -2.797  -12.915 -6.729  1   27.595 ? 662 HOH   B O    1 
HETATM 5358 O  O    . HOH   H 5 .   ? -5.404  -6.236  -14.063 1   22.691 ? 663 HOH   B O    1 
HETATM 5359 O  O    . HOH   H 5 .   ? 16.287  4.149   7.269   1   19.032 ? 664 HOH   B O    1 
HETATM 5360 O  O    . HOH   H 5 .   ? 3.088   -33.608 -12.824 1   34.542 ? 665 HOH   B O    1 
HETATM 5361 O  O    . HOH   H 5 .   ? 12.687  -14.866 -27.601 1   35.728 ? 666 HOH   B O    1 
HETATM 5362 O  O    . HOH   H 5 .   ? -2.869  19.722  -2.244  1   30.459 ? 667 HOH   B O    1 
HETATM 5363 O  O    . HOH   H 5 .   ? -5.071  16.516  -4.363  1   31.122 ? 668 HOH   B O    1 
HETATM 5364 O  O    . HOH   H 5 .   ? 8.348   -30.767 -19.636 1   46.62  ? 669 HOH   B O    1 
HETATM 5365 O  O    . HOH   H 5 .   ? -14.318 4.594   1.089   1   27.857 ? 670 HOH   B O    1 
HETATM 5366 O  O    . HOH   H 5 .   ? 6.381   -25.814 -2.333  1   33.692 ? 671 HOH   B O    1 
HETATM 5367 O  O    . HOH   H 5 .   ? 16.107  -10.748 -6.29   1   33.217 ? 672 HOH   B O    1 
HETATM 5368 O  O    . HOH   H 5 .   ? 9.127   4.868   15.604  1   21.925 ? 673 HOH   B O    1 
HETATM 5369 O  O    . HOH   H 5 .   ? 18.967  7.513   7.862   1   26.906 ? 674 HOH   B O    1 
HETATM 5370 O  O    . HOH   H 5 .   ? 14.179  14.866  -11.717 1   24.264 ? 675 HOH   B O    1 
HETATM 5371 O  O    . HOH   H 5 .   ? 9.644   8.925   17.353  1   41.681 ? 676 HOH   B O    1 
HETATM 5372 O  O    . HOH   H 5 .   ? -12.808 3.575   -5.844  1   38.596 ? 677 HOH   B O    1 
HETATM 5373 O  O    . HOH   H 5 .   ? 5.809   1.946   15.556  1   28.931 ? 678 HOH   B O    1 
HETATM 5374 O  O    . HOH   H 5 .   ? -0.728  0.916   -15.397 1   24.313 ? 679 HOH   B O    1 
HETATM 5375 O  O    . HOH   H 5 .   ? -1.639  -18.036 -30.676 1   34.915 ? 680 HOH   B O    1 
HETATM 5376 O  O    . HOH   H 5 .   ? -11.674 -5.046  -16.164 1   30.723 ? 681 HOH   B O    1 
HETATM 5377 O  O    . HOH   H 5 .   ? 7.126   -17.079 -8.153  1   19.891 ? 682 HOH   B O    1 
HETATM 5378 O  O    . HOH   H 5 .   ? 20.851  10.967  -5.455  1   35.389 ? 683 HOH   B O    1 
HETATM 5379 O  O    . HOH   H 5 .   ? -16.396 2.185   -3.826  1   62.722 ? 684 HOH   B O    1 
HETATM 5380 O  O    . HOH   H 5 .   ? 6.063   -0.557  12.322  1   26.511 ? 685 HOH   B O    1 
HETATM 5381 O  O    . HOH   H 5 .   ? 9.763   -24.009 -4.195  1   40.051 ? 686 HOH   B O    1 
HETATM 5382 O  O    . HOH   H 5 .   ? 22.959  5.788   -3.537  1   39.685 ? 687 HOH   B O    1 
HETATM 5383 O  O    . HOH   H 5 .   ? 0.36    4.806   11.947  1   85.645 ? 688 HOH   B O    1 
HETATM 5384 O  O    . HOH   H 5 .   ? 7.848   -32.204 -7.611  1   29.528 ? 689 HOH   B O    1 
HETATM 5385 O  O    . HOH   H 5 .   ? 3.922   -23.35  -0.415  1   32.551 ? 690 HOH   B O    1 
HETATM 5386 O  O    . HOH   H 5 .   ? 28.272  10.859  5.423   1   41.819 ? 691 HOH   B O    1 
HETATM 5387 O  O    . HOH   H 5 .   ? -10.956 3.395   7.611   1   24.428 ? 692 HOH   B O    1 
HETATM 5388 O  O    . HOH   H 5 .   ? -5.279  -6.104  -5.499  1   36.74  ? 693 HOH   B O    1 
HETATM 5389 O  O    . HOH   H 5 .   ? 10.921  -32.881 -16.998 1   36.746 ? 694 HOH   B O    1 
HETATM 5390 O  O    . HOH   H 5 .   ? 6.911   -7.955  5.577   1   40.998 ? 695 HOH   B O    1 
HETATM 5391 O  O    . HOH   H 5 .   ? -17.327 -6.188  -8.917  1   40.239 ? 696 HOH   B O    1 
HETATM 5392 O  O    . HOH   H 5 .   ? 10.44   -12.784 -3.918  1   35.166 ? 697 HOH   B O    1 
HETATM 5393 O  O    . HOH   H 5 .   ? 13.428  19.387  -10.746 1   48.266 ? 698 HOH   B O    1 
HETATM 5394 O  O    . HOH   H 5 .   ? 18.926  -5.786  -10.815 1   57.629 ? 699 HOH   B O    1 
HETATM 5395 O  O    . HOH   H 5 .   ? 17.994  -1.948  -10.668 1   31.072 ? 700 HOH   B O    1 
HETATM 5396 O  O    . HOH   H 5 .   ? -2.741  -11.113 -28.243 1   41.209 ? 701 HOH   B O    1 
HETATM 5397 O  O    . HOH   H 5 .   ? 6.336   -4.277  -16.23  1   32.728 ? 702 HOH   B O    1 
HETATM 5398 O  O    . HOH   H 5 .   ? -4.574  15.251  -12.675 1   42.338 ? 703 HOH   B O    1 
HETATM 5399 O  O    . HOH   H 5 .   ? -2.31   -6.894  -25.508 1   45.558 ? 704 HOH   B O    1 
HETATM 5400 O  O    . HOH   H 5 .   ? 18.108  5.359   8.997   1   20.306 ? 705 HOH   B O    1 
HETATM 5401 O  O    . HOH   H 5 .   ? 8.384   -12.49  -5.699  1   34.404 ? 706 HOH   B O    1 
HETATM 5402 O  O    . HOH   H 5 .   ? 17.917  21.572  -0.621  1   35.618 ? 707 HOH   B O    1 
HETATM 5403 O  O    . HOH   H 5 .   ? 14.094  21.631  -2.308  1   37.725 ? 708 HOH   B O    1 
HETATM 5404 O  O    . HOH   H 5 .   ? -0.504  17.666  -12.312 1   51.585 ? 709 HOH   B O    1 
HETATM 5405 O  O    . HOH   H 5 .   ? -10.391 -10.761 -21.241 1   36.959 ? 710 HOH   B O    1 
HETATM 5406 O  O    . HOH   H 5 .   ? 23.406  -4.814  -3.061  1   24.352 ? 711 HOH   B O    1 
HETATM 5407 O  O    . HOH   H 5 .   ? 5.013   -13.505 -5.639  1   34.84  ? 712 HOH   B O    1 
HETATM 5408 O  O    . HOH   H 5 .   ? -2.613  -6.944  -2.686  1   42.706 ? 713 HOH   B O    1 
HETATM 5409 O  O    . HOH   H 5 .   ? 12.432  -5.149  5.978   1   31.054 ? 714 HOH   B O    1 
HETATM 5410 O  O    . HOH   H 5 .   ? -9.404  15.144  -5.224  1   40.073 ? 715 HOH   B O    1 
HETATM 5411 O  O    . HOH   H 5 .   ? 1.371   14.743  17.423  1   43.697 ? 716 HOH   B O    1 
HETATM 5412 O  O    . HOH   H 5 .   ? 8.147   19.509  -8.247  1   55.077 ? 717 HOH   B O    1 
HETATM 5413 O  O    . HOH   H 5 .   ? -6.738  -4.415  -1.281  1   44.987 ? 718 HOH   B O    1 
HETATM 5414 O  O    . HOH   H 5 .   ? 15.605  -26.048 -7.408  1   37.672 ? 719 HOH   B O    1 
HETATM 5415 O  O    . HOH   H 5 .   ? -6.473  -9.581  -26.704 1   32.395 ? 720 HOH   B O    1 
HETATM 5416 O  O    . HOH   H 5 .   ? 15.957  -9.521  -13.94  1   49.78  ? 721 HOH   B O    1 
HETATM 5417 O  O    . HOH   H 5 .   ? 12.467  -25.229 -4.873  1   39.683 ? 722 HOH   B O    1 
HETATM 5418 O  O    . HOH   H 5 .   ? -9.218  -26.496 -25.631 1   35.989 ? 723 HOH   B O    1 
HETATM 5419 O  O    . HOH   H 5 .   ? 7.011   -17.642 -1.86   1   39.895 ? 724 HOH   B O    1 
HETATM 5420 O  O    . HOH   H 5 .   ? 4.349   18.021  19.384  1   73.979 ? 725 HOH   B O    1 
HETATM 5421 O  O    . HOH   H 5 .   ? 13.236  16.812  -1.092  1   22.134 ? 726 HOH   B O    1 
HETATM 5422 O  O    . HOH   H 5 .   ? 4.717   -20.792 0.354   1   39.007 ? 727 HOH   B O    1 
HETATM 5423 O  O    . HOH   H 5 .   ? 1.704   -1.187  7.192   1   26.711 ? 728 HOH   B O    1 
HETATM 5424 O  O    . HOH   H 5 .   ? 3.635   -31.126 -6.819  1   40.063 ? 729 HOH   B O    1 
HETATM 5425 O  O    . HOH   H 5 .   ? 2.412   -7.723  6.987   1   41.953 ? 730 HOH   B O    1 
HETATM 5426 O  O    . HOH   H 5 .   ? -3.323  -5.018  -0.505  1   37.323 ? 731 HOH   B O    1 
HETATM 5427 O  O    . HOH   H 5 .   ? 1.059   -11.383 -5.004  1   38.074 ? 732 HOH   B O    1 
HETATM 5428 O  O    . HOH   H 5 .   ? 7.401   -15.041 -6.412  1   28.185 ? 733 HOH   B O    1 
HETATM 5429 O  O    . HOH   H 5 .   ? -6.821  16.492  -6.595  1   43.838 ? 734 HOH   B O    1 
HETATM 5430 O  O    . HOH   H 5 .   ? 16.969  -11.078 -3.757  1   36.609 ? 735 HOH   B O    1 
HETATM 5431 O  O    . HOH   H 5 .   ? -4.908  -14.241 -5.465  1   55.228 ? 736 HOH   B O    1 
HETATM 5432 O  O    . HOH   H 5 .   ? 26.892  0.827   -3.904  1   41.828 ? 737 HOH   B O    1 
HETATM 5433 O  O    . HOH   H 5 .   ? 24.043  -1.771  -8.912  1   44.671 ? 738 HOH   B O    1 
HETATM 5434 O  O    . HOH   H 5 .   ? 23.918  1.026   -8.238  1   39.624 ? 739 HOH   B O    1 
HETATM 5435 O  O    . HOH   H 5 .   ? 14.665  18.726  -2.393  1   27.45  ? 740 HOH   B O    1 
HETATM 5436 O  O    . HOH   H 5 .   ? 22.851  -7.468  -2.912  1   25.318 ? 741 HOH   B O    1 
HETATM 5437 O  O    . HOH   H 5 .   ? 17.633  -7.483  -0.946  1   24.521 ? 742 HOH   B O    1 
HETATM 5438 O  O    . HOH   H 5 .   ? 0.608   -4.548  9.058   1   33.874 ? 743 HOH   B O    1 
HETATM 5439 O  O    . HOH   H 5 .   ? 12.391  -10.144 -19.409 1   35.924 ? 744 HOH   B O    1 
HETATM 5440 O  O    . HOH   H 5 .   ? 8.944   -14.203 -2.278  1   41.824 ? 745 HOH   B O    1 
HETATM 5441 O  O    . HOH   H 5 .   ? 28.19   13.843  6.525   1   38.609 ? 746 HOH   B O    1 
HETATM 5442 O  O    . HOH   H 5 .   ? 13.127  10.202  17.445  1   42.308 ? 747 HOH   B O    1 
HETATM 5443 O  O    . HOH   H 5 .   ? 14.489  -23.938 -6.016  1   35.146 ? 748 HOH   B O    1 
HETATM 5444 O  O    . HOH   H 5 .   ? 16.95   18.441  -3.709  1   37.587 ? 749 HOH   B O    1 
HETATM 5445 O  O    . HOH   H 5 .   ? -13.005 -12.065 -22.48  1   39.482 ? 750 HOH   B O    1 
HETATM 5446 O  O    . HOH   H 5 .   ? 20.434  -8.45   -2.206  1   24.842 ? 751 HOH   B O    1 
HETATM 5447 O  O    . HOH   H 5 .   ? 13.108  -10.66  -29.124 1   38.06  ? 752 HOH   B O    1 
HETATM 5448 O  O    . HOH   H 5 .   ? 10.551  -10.205 -31.58  1   46.899 ? 753 HOH   B O    1 
HETATM 5449 O  O    . HOH   H 5 .   ? 18.542  12.206  -5.731  1   34.325 ? 754 HOH   B O    1 
HETATM 5450 O  O    . HOH   H 5 .   ? 23.21   6.975   12.459  1   42.423 ? 755 HOH   B O    1 
HETATM 5451 O  O    . HOH   H 5 .   ? 10.586  -19.562 -2.387  1   39.545 ? 756 HOH   B O    1 
HETATM 5452 O  O    . HOH   H 5 .   ? 3.439   -33.689 -9.987  1   33.655 ? 757 HOH   B O    1 
HETATM 5453 O  O    . HOH   H 5 .   ? 25.875  -3.132  -7.054  1   43.82  ? 758 HOH   B O    1 
HETATM 5454 O  O    . HOH   H 5 .   ? 16.376  -19.596 -6.242  1   49.531 ? 759 HOH   B O    1 
HETATM 5455 O  O    . HOH   H 5 .   ? 1.017   -14.981 -5.85   1   45.726 ? 760 HOH   B O    1 
HETATM 5456 O  O    . HOH   H 5 .   ? 16.536  16.042  -10.76  1   38.443 ? 761 HOH   B O    1 
HETATM 5457 O  O    . HOH   H 5 .   ? 25.736  -3.632  -2.038  1   29.213 ? 762 HOH   B O    1 
HETATM 5458 O  O    . HOH   H 5 .   ? 14.71   -15.426 -19.801 1   33.509 ? 763 HOH   B O    1 
HETATM 5459 O  O    . HOH   H 5 .   ? -10.631 19.795  2.481   1   53.489 ? 764 HOH   B O    1 
HETATM 5460 O  O    . HOH   H 5 .   ? 11.426  -11.997 0.081   1   29.256 ? 765 HOH   B O    1 
HETATM 5461 O  O    . HOH   H 5 .   ? 27.016  -2.044  -4.267  1   40.724 ? 766 HOH   B O    1 
HETATM 5462 O  O    . HOH   H 5 .   ? 6.789   17.426  -12.541 1   65.427 ? 767 HOH   B O    1 
HETATM 5463 O  O    . HOH   H 5 .   ? 10.613  -22.268 -2.258  1   42.371 ? 768 HOH   B O    1 
HETATM 5464 O  O    . HOH   H 5 .   ? 15.786  8.678   19.032  1   33.502 ? 769 HOH   B O    1 
HETATM 5465 O  O    . HOH   H 5 .   ? 8.921   -18.791 -0.4    1   40.778 ? 770 HOH   B O    1 
HETATM 5466 O  O    . HOH   H 5 .   ? 15.75   -22.25  -4.168  1   50.312 ? 771 HOH   B O    1 
HETATM 5467 O  O    . HOH   H 5 .   ? 27.56   -5.154  -0.426  1   59.733 ? 772 HOH   B O    1 
HETATM 5468 O  O    . HOH   H 5 .   ? 26.944  -7.848  -0.921  1   51.813 ? 773 HOH   B 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   ? 0.132567  0.382181 0.210233 -0.0210193  0.028065    0.00683566  1   SER   A N    
2    C  CA   . SER   A 1   ? 0.160581  0.391297 0.199046 -0.012884   0.0169012   -0.00671409 1   SER   A CA   
3    C  C    . SER   A 1   ? 0.150384  0.371354 0.190311 0.00275568  0.0238241   -0.0167186  1   SER   A C    
4    O  O    . SER   A 1   ? 0.149572  0.309387 0.165544 0.0125579   0.0145718   0.00567647  1   SER   A O    
5    C  CB   . SER   A 1   ? 0.156727  0.401182 0.168975 -0.00226948 0.0367813   -0.0302858  1   SER   A CB   
6    O  OG   . SER   A 1   ? 0.232534  0.438522 0.24568  0.00347431  0.0299016   -0.0578367  1   SER   A OG   
7    N  N    . GLY   A 2   ? 0.140929  0.37562  0.197216 0.00417567  0.0355788   -0.030663   2   GLY   A N    
8    C  CA   . GLY   A 2   ? 0.13346   0.361672 0.189274 0.0219515   0.0166818   -0.0331949  2   GLY   A CA   
9    C  C    . GLY   A 2   ? 0.119631  0.336888 0.20502  0.0278346   0.0153976   -0.0280891  2   GLY   A C    
10   O  O    . GLY   A 2   ? 0.149935  0.331865 0.208879 -0.00776803 -0.011415   -0.0147231  2   GLY   A O    
11   N  N    . PHE   A 3   ? 0.113475  0.325736 0.19416  0.0372569   0.00383232  -0.0323019  3   PHE   A N    
12   C  CA   . PHE   A 3   ? 0.106974  0.328325 0.194255 0.0357618   0.0123556   -0.0249254  3   PHE   A CA   
13   C  C    . PHE   A 3   ? 0.124187  0.300147 0.204403 0.0421471   0.00030242  -0.0230711  3   PHE   A C    
14   O  O    . PHE   A 3   ? 0.137476  0.315538 0.241706 0.048372    -0.00468997 -0.0367582  3   PHE   A O    
15   C  CB   . PHE   A 3   ? 0.103615  0.349238 0.200331 0.0174263   0.0210972   -0.026293   3   PHE   A CB   
16   C  CG   . PHE   A 3   ? 0.122492  0.359269 0.197205 0.0105776   0.0177738   -0.0196612  3   PHE   A CG   
17   C  CD1  . PHE   A 3   ? 0.145214  0.362172 0.203944 -0.00390667 0.0132613   -0.00235054 3   PHE   A CD1  
18   C  CD2  . PHE   A 3   ? 0.144688  0.376237 0.207187 0.00389835  0.00786423  -0.00974552 3   PHE   A CD2  
19   C  CE1  . PHE   A 3   ? 0.157817  0.374018 0.21334  -0.00786413 0.0166855   0.00528545  3   PHE   A CE1  
20   C  CE2  . PHE   A 3   ? 0.142517  0.382881 0.19671  -0.00705223 0.0145214   -0.00125065 3   PHE   A CE2  
21   C  CZ   . PHE   A 3   ? 0.159907  0.382304 0.206508 -0.0082874  0.0223992   0.00586625  3   PHE   A CZ   
22   N  N    . ARG   A 4   ? 0.126548  0.278725 0.183804 0.0400853   -0.00019883 -0.0142429  4   ARG   A N    
23   C  CA   . ARG   A 4   ? 0.146773  0.265507 0.192698 0.0358868   -0.00383534 -0.00067815 4   ARG   A CA   
24   C  C    . ARG   A 4   ? 0.130187  0.242755 0.173441 0.0237643   0.00884837  0.00601022  4   ARG   A C    
25   O  O    . ARG   A 4   ? 0.111972  0.248383 0.17461  0.0135792   0.0116228   0.0109856   4   ARG   A O    
26   C  CB   . ARG   A 4   ? 0.184656  0.277823 0.199537 0.0385017   -0.0127873  0.0161472   4   ARG   A CB   
27   C  CG   . ARG   A 4   ? 0.243473  0.286285 0.2309   0.0337849   -0.0472502  0.0277839   4   ARG   A CG   
28   C  CD   . ARG   A 4   ? 0.280087  0.273652 0.269865 0.0432911   -0.0777747  0.0370029   4   ARG   A CD   
29   N  NE   . ARG   A 4   ? 0.330685  0.272954 0.282655 0.00669895  -0.0975132  0.0420174   4   ARG   A NE   
30   C  CZ   . ARG   A 4   ? 0.291784  0.264059 0.292264 0.00070598  -0.0903447  0.0262742   4   ARG   A CZ   
31   N  NH1  . ARG   A 4   ? 0.304722  0.291191 0.327699 -0.0312889  -0.0918813  0.0201828   4   ARG   A NH1  
32   N  NH2  . ARG   A 4   ? 0.245829  0.22328  0.288094 -0.00426959 -0.0930684  0.0102993   4   ARG   A NH2  
33   N  N    A LYS   A 5   ? 0.144364  0.249502 0.183338 0.0189824   0.00750862  -0.00240093 5   LYS   A N    
34   N  N    B LYS   A 5   ? 0.12013   0.245305 0.176606 0.0315067   -0.00120334 0.00259907  5   LYS   A N    
35   C  CA   A LYS   A 5   ? 0.157092  0.254657 0.189382 0.0144942   0.00555997  0.00514859  5   LYS   A CA   
36   C  CA   B LYS   A 5   ? 0.126648  0.24852  0.179796 0.029575    -0.00560706 0.0108038   5   LYS   A CA   
37   C  C    A LYS   A 5   ? 0.15738   0.239504 0.184103 0.0122799   0.00526601  0.0102021   5   LYS   A C    
38   C  C    B LYS   A 5   ? 0.129755  0.237106 0.178587 0.0171395   -0.00249698 0.0106486   5   LYS   A C    
39   O  O    A LYS   A 5   ? 0.205234  0.242682 0.196719 0.0131416   0.0223377   0.0156661   5   LYS   A O    
40   O  O    B LYS   A 5   ? 0.154688  0.236477 0.187222 0.0044344   0.00538534  0.00927244  5   LYS   A O    
41   C  CB   A LYS   A 5   ? 0.203362  0.273944 0.218305 -0.0022516  0.0128934   -0.00852307 5   LYS   A CB   
42   C  CB   B LYS   A 5   ? 0.147316  0.26074  0.196437 0.0297974   -0.00590705 0.006117    5   LYS   A CB   
43   C  CG   A LYS   A 5   ? 0.230432  0.300811 0.23327  -0.00729553 0.0146901   -0.0183956  5   LYS   A CG   
44   C  CG   B LYS   A 5   ? 0.159168  0.271839 0.201564 0.0443719   -0.00515016 0.0112513   5   LYS   A CG   
45   C  CD   A LYS   A 5   ? 0.258307  0.318602 0.253561 -0.00955692 0.0116765   -0.0244532  5   LYS   A CD   
46   C  CD   B LYS   A 5   ? 0.163567  0.294115 0.221882 0.0461776   -0.00907496 0.0132455   5   LYS   A CD   
47   C  CE   A LYS   A 5   ? 0.265558  0.322865 0.260762 -0.0158721  0.00465663  -0.0275105  5   LYS   A CE   
48   C  CE   B LYS   A 5   ? 0.177317  0.31554  0.225469 0.0564567   -0.0125848  0.0148482   5   LYS   A CE   
49   N  NZ   A LYS   A 5   ? 0.265456  0.325049 0.271122 -0.0236502  0.0104557   -0.0202329  5   LYS   A NZ   
50   N  NZ   B LYS   A 5   ? 0.176078  0.32855  0.235167 0.0586833   -0.00663434 0.0246541   5   LYS   A NZ   
51   N  N    . MET   A 6   ? 0.134837  0.232766 0.177856 0.0169174   -0.00156299 0.0104018   6   MET   A N    
52   C  CA   A MET   A 6   ? 0.145977  0.226299 0.188341 0.0246776   -0.00849006 0.00769045  6   MET   A CA   
53   C  CA   B MET   A 6   ? 0.130814  0.22424  0.186384 0.0170993   -0.00957153 0.0079209   6   MET   A CA   
54   C  C    . MET   A 6   ? 0.14068   0.217384 0.173562 0.0198083   -0.013157   0.012546    6   MET   A C    
55   O  O    . MET   A 6   ? 0.141103  0.223807 0.192902 0.0120211   -0.0165096  0.0246894   6   MET   A O    
56   C  CB   A MET   A 6   ? 0.180585  0.242568 0.213938 0.0241907   -0.0212316  -1.466e-05  6   MET   A CB   
57   C  CB   B MET   A 6   ? 0.133522  0.234706 0.20546  0.0164333   -0.0181339  0.00480233  6   MET   A CB   
58   C  CG   A MET   A 6   ? 0.225871  0.254905 0.238899 0.0363543   -0.0105839  -0.00709118 6   MET   A CG   
59   C  CG   B MET   A 6   ? 0.139728  0.240236 0.219879 0.018536    -0.0144397  0.00101553  6   MET   A CG   
60   S  SD   A MET   A 6   ? 0.301886  0.284049 0.261544 0.032781    -0.0512072  -0.00477374 6   MET   A SD   
61   S  SD   B MET   A 6   ? 0.157896  0.254884 0.256132 0.0145757   -0.0259184  -0.00573781 6   MET   A SD   
62   C  CE   A MET   A 6   ? 0.251428  0.287    0.230953 0.0153193   -0.0478179  -0.014006   6   MET   A CE   
63   C  CE   B MET   A 6   ? 0.0950304 0.250684 0.229898 -0.00420117 -0.0166585  -0.00992785 6   MET   A CE   
64   N  N    . ALA   A 7   ? 0.123215  0.202237 0.165762 0.0229195   -0.018712   0.0114738   7   ALA   A N    
65   C  CA   . ALA   A 7   ? 0.121404  0.198503 0.171698 0.0216381   -0.0204619  0.00670106  7   ALA   A CA   
66   C  C    . ALA   A 7   ? 0.115897  0.200368 0.157902 0.0285679   -0.014428   0.00294408  7   ALA   A C    
67   O  O    . ALA   A 7   ? 0.129251  0.2041   0.171421 0.0323505   -0.0277896  -0.00903303 7   ALA   A O    
68   C  CB   . ALA   A 7   ? 0.121438  0.201382 0.177112 0.020072    -0.0190027  0.00901082  7   ALA   A CB   
69   N  N    . PHE   A 8   ? 0.110376  0.196991 0.147877 0.0274957   -0.0203149  -0.00734396 8   PHE   A N    
70   C  CA   . PHE   A 8   ? 0.10946   0.202094 0.161436 0.0248667   -0.0153241  -0.00982424 8   PHE   A CA   
71   C  C    . PHE   A 8   ? 0.11303   0.21999  0.167202 0.017493    -0.0116226  -0.0136096  8   PHE   A C    
72   O  O    . PHE   A 8   ? 0.128422  0.232528 0.167489 0.0119237   -0.00562135 -0.0109064  8   PHE   A O    
73   C  CB   . PHE   A 8   ? 0.111252  0.198609 0.172699 0.0310451   -0.0115432  -0.00549895 8   PHE   A CB   
74   C  CG   . PHE   A 8   ? 0.121529  0.199404 0.197894 0.0273984   -0.00884932 0.0020222   8   PHE   A CG   
75   C  CD1  . PHE   A 8   ? 0.156605  0.214345 0.214157 0.0169601   -0.00930559 0.00197981  8   PHE   A CD1  
76   C  CD2  . PHE   A 8   ? 0.13254   0.217699 0.206109 0.0280621   -0.0106725  0.0143647   8   PHE   A CD2  
77   C  CE1  . PHE   A 8   ? 0.155147  0.228649 0.229386 0.0011018   -0.0132007  0.00502157  8   PHE   A CE1  
78   C  CE2  . PHE   A 8   ? 0.149679  0.212828 0.207006 0.0246929   -0.00597761 0.0167696   8   PHE   A CE2  
79   C  CZ   . PHE   A 8   ? 0.150533  0.232958 0.224156 0.0155523   -0.00677876 0.0138305   8   PHE   A CZ   
80   N  N    . PRO   A 9   ? 0.110437  0.250287 0.169723 0.0123791   -0.0200331  -0.0177071  9   PRO   A N    
81   C  CA   . PRO   A 9   ? 0.122643  0.259089 0.170854 0.0215604   -0.0197647  -0.0135609  9   PRO   A CA   
82   C  C    . PRO   A 9   ? 0.12311   0.248166 0.168683 0.0300853   -0.0168563  -0.00568205 9   PRO   A C    
83   O  O    . PRO   A 9   ? 0.134159  0.257999 0.171671 0.0261926   -0.0106422  0.00861267  9   PRO   A O    
84   C  CB   . PRO   A 9   ? 0.121682  0.276165 0.185932 0.0165975   -0.0218006  -0.0202023  9   PRO   A CB   
85   C  CG   . PRO   A 9   ? 0.136622  0.280453 0.189635 0.00524722  -0.0172637  -0.0256445  9   PRO   A CG   
86   C  CD   . PRO   A 9   ? 0.127849  0.272983 0.18694  0.00289951  -0.0223696  -0.0284256  9   PRO   A CD   
87   N  N    . SER   A 10  ? 0.112608  0.241109 0.155085 0.0341838   -0.020487   -0.00695404 10  SER   A N    
88   C  CA   . SER   A 10  ? 0.113937  0.235172 0.164406 0.0344865   -0.0181504  -0.014011   10  SER   A CA   
89   C  C    . SER   A 10  ? 0.107933  0.231705 0.164202 0.034736    -0.0200658  -0.0147393  10  SER   A C    
90   O  O    . SER   A 10  ? 0.0994614 0.229583 0.175297 0.0335401   -0.0185255  -0.0123238  10  SER   A O    
91   C  CB   . SER   A 10  ? 0.126828  0.233694 0.178487 0.0407137   -0.0198718  -0.015761   10  SER   A CB   
92   O  OG   . SER   A 10  ? 0.138951  0.21829  0.188701 0.0408132   -0.0265769  -0.0150628  10  SER   A OG   
93   N  N    . GLY   A 11  ? 0.110922  0.23044  0.164971 0.0345826   -0.0120132  -0.0148183  11  GLY   A N    
94   C  CA   . GLY   A 11  ? 0.124764  0.237827 0.15975  0.0338353   -0.00823166 -0.0135013  11  GLY   A CA   
95   C  C    . GLY   A 11  ? 0.135501  0.233367 0.169426 0.0324285   -0.0129018  -0.0146738  11  GLY   A C    
96   O  O    . GLY   A 11  ? 0.13425   0.240989 0.194251 0.0330167   -0.00571474 -0.0207739  11  GLY   A O    
97   N  N    . LYS   A 12  ? 0.120266  0.224317 0.164616 0.0360526   -0.018752   -0.0117194  12  LYS   A N    
98   C  CA   . LYS   A 12  ? 0.133658  0.221892 0.181312 0.0417792   -0.0254087  -0.0143422  12  LYS   A CA   
99   C  C    . LYS   A 12  ? 0.124693  0.214947 0.180795 0.0480509   -0.0255804  -0.0149624  12  LYS   A C    
100  O  O    . LYS   A 12  ? 0.133506  0.241133 0.210537 0.0668826   -0.0321033  -0.0360589  12  LYS   A O    
101  C  CB   . LYS   A 12  ? 0.150446  0.228751 0.205086 0.0385086   -0.0342297  -0.00711216 12  LYS   A CB   
102  C  CG   . LYS   A 12  ? 0.19364   0.247124 0.227633 0.0322259   -0.0427422  -0.015453   12  LYS   A CG   
103  C  CD   . LYS   A 12  ? 0.22914   0.282489 0.268506 0.0128991   -0.035672   -0.0110375  12  LYS   A CD   
104  C  CE   . LYS   A 12  ? 0.275157  0.299498 0.322028 0.0103372   -0.0333757  -0.0310521  12  LYS   A CE   
105  N  NZ   . LYS   A 12  ? 0.30702   0.33795  0.338598 0.00923248  -0.0363373  -0.0416179  12  LYS   A NZ   
106  N  N    . VAL   A 13  ? 0.120666  0.206076 0.17442  0.0401509   -0.0214959  -0.0145687  13  VAL   A N    
107  C  CA   . VAL   A 13  ? 0.115012  0.207302 0.167796 0.0397545   -0.018976   -0.0105438  13  VAL   A CA   
108  C  C    . VAL   A 13  ? 0.118705  0.211451 0.166164 0.0372387   -0.0176164  -0.00885027 13  VAL   A C    
109  O  O    . VAL   A 13  ? 0.113601  0.230005 0.169015 0.0318844   -0.00742923 -0.00820255 13  VAL   A O    
110  C  CB   . VAL   A 13  ? 0.122114  0.202755 0.171418 0.0348077   -0.0155717  -0.00920628 13  VAL   A CB   
111  C  CG1  . VAL   A 13  ? 0.142543  0.218709 0.177632 0.0274262   -0.0119403  -0.0159893  13  VAL   A CG1  
112  C  CG2  . VAL   A 13  ? 0.146894  0.214603 0.186814 0.0279836   -0.0109955  -0.00606729 13  VAL   A CG2  
113  N  N    . GLU   A 14  ? 0.118824  0.216152 0.167407 0.0388185   -0.014261   -0.00631091 14  GLU   A N    
114  C  CA   . GLU   A 14  ? 0.123787  0.218174 0.172278 0.0359328   -0.00897561 -0.00767758 14  GLU   A CA   
115  C  C    . GLU   A 14  ? 0.127204  0.235475 0.177921 0.036381    -0.010608   -0.0185624  14  GLU   A C    
116  O  O    . GLU   A 14  ? 0.115215  0.257128 0.201757 0.0371793   -0.00044468 -0.0114474  14  GLU   A O    
117  C  CB   . GLU   A 14  ? 0.13143   0.227901 0.180636 0.0375582   -0.0116333  -0.00599372 14  GLU   A CB   
118  C  CG   . GLU   A 14  ? 0.141709  0.235737 0.19057  0.044139    -0.0133003  0.00185218  14  GLU   A CG   
119  C  CD   . GLU   A 14  ? 0.149519  0.267318 0.1949   0.0407036   -0.0183655  -0.00053545 14  GLU   A CD   
120  O  OE1  . GLU   A 14  ? 0.138018  0.265397 0.189471 0.0583143   -0.0259279  -0.0165517  14  GLU   A OE1  
121  O  OE2  . GLU   A 14  ? 0.171601  0.312435 0.194587 0.0562648   -0.0122611  0.00603413  14  GLU   A OE2  
122  N  N    . GLY   A 15  ? 0.114447  0.242782 0.178669 0.0397633   -0.0158651  -0.0254931  15  GLY   A N    
123  C  CA   . GLY   A 15  ? 0.127604  0.250956 0.191426 0.046839    -0.0140579  -0.0342583  15  GLY   A CA   
124  C  C    . GLY   A 15  ? 0.113868  0.250478 0.196266 0.0507189   -0.0078131  -0.0294911  15  GLY   A C    
125  O  O    . GLY   A 15  ? 0.128394  0.27904  0.208764 0.0708243   -0.00693928 -0.0379494  15  GLY   A O    
126  N  N    . CYS   A 16  ? 0.104694  0.231789 0.188906 0.0497075   -0.0187862  -0.0302973  16  CYS   A N    
127  C  CA   . CYS   A 16  ? 0.10402   0.230746 0.191834 0.0438916   -0.020422   -0.0226909  16  CYS   A CA   
128  C  C    . CYS   A 16  ? 0.101     0.230131 0.186332 0.0321124   -0.0119844  -0.0203081  16  CYS   A C    
129  O  O    . CYS   A 16  ? 0.116158  0.232433 0.18985  0.0349165   -0.0226396  -0.0191307  16  CYS   A O    
130  C  CB   . CYS   A 16  ? 0.104428  0.234463 0.209973 0.0336126   -0.0347473  -0.0111432  16  CYS   A CB   
131  S  SG   . CYS   A 16  ? 0.162358  0.238714 0.271464 0.0270602   -0.0624896  -0.008959   16  CYS   A SG   
132  N  N    . MET   A 17  ? 0.107536  0.228045 0.179817 0.0207823   -0.0127771  -0.021554   17  MET   A N    
133  C  CA   . MET   A 17  ? 0.107455  0.228571 0.188227 0.0149717   -0.00664139 -0.0129739  17  MET   A CA   
134  C  C    . MET   A 17  ? 0.112114  0.239162 0.181332 0.0110756   -0.00160936 -0.0143042  17  MET   A C    
135  O  O    . MET   A 17  ? 0.123101  0.280268 0.183749 0.00073955  0.00154125  -0.0127281  17  MET   A O    
136  C  CB   . MET   A 17  ? 0.111784  0.23584  0.198526 0.0186314   -0.0136002  -0.0111396  17  MET   A CB   
137  C  CG   . MET   A 17  ? 0.11693   0.242616 0.20452  0.0164037   -0.00641184 -0.0147287  17  MET   A CG   
138  S  SD   . MET   A 17  ? 0.116188  0.254946 0.207459 0.02715     0.0125913   -0.017903   17  MET   A SD   
139  C  CE   . MET   A 17  ? 0.111607  0.250337 0.216691 0.0281065   0.011503    -0.0252837  17  MET   A CE   
140  N  N    . VAL   A 18  ? 0.0987647 0.241758 0.183337 0.00927881  0.00304398  -0.0173551  18  VAL   A N    
141  C  CA   . VAL   A 18  ? 0.104078  0.253794 0.183156 0.0130563   0.00897019  -0.0122071  18  VAL   A CA   
142  C  C    . VAL   A 18  ? 0.0982683 0.248733 0.187703 0.0108868   0.0074038   -0.00771811 18  VAL   A C    
143  O  O    . VAL   A 18  ? 0.104387  0.251591 0.175718 0.00180025  0.0042985   -0.00306272 18  VAL   A O    
144  C  CB   . VAL   A 18  ? 0.10449   0.261636 0.195736 0.0230014   0.00760739  -0.0176659  18  VAL   A CB   
145  C  CG1  . VAL   A 18  ? 0.113813  0.266195 0.205243 0.0299169   0.0114284   -0.0240077  18  VAL   A CG1  
146  C  CG2  . VAL   A 18  ? 0.103296  0.254861 0.191263 0.0292377   0.00325514  -0.0172121  18  VAL   A CG2  
147  N  N    . GLN   A 19  ? 0.1044    0.267641 0.19778  0.00058095  0.010097    -0.00937954 19  GLN   A N    
148  C  CA   . GLN   A 19  ? 0.106556  0.281922 0.22346  0.0029801   0.00816457  -0.0136296  19  GLN   A CA   
149  C  C    . GLN   A 19  ? 0.109315  0.274213 0.213119 0.0091689   0.0110913   -0.0156474  19  GLN   A C    
150  O  O    . GLN   A 19  ? 0.105405  0.308688 0.214943 0.0198798   0.00408582  -0.0326184  19  GLN   A O    
151  C  CB   . GLN   A 19  ? 0.148977  0.316794 0.276028 -0.00573889 -0.00637884 0.00427578  19  GLN   A CB   
152  C  CG   . GLN   A 19  ? 0.18501   0.346523 0.318979 -0.0135742  -0.0011746  0.00448197  19  GLN   A CG   
153  C  CD   . GLN   A 19  ? 0.207703  0.396182 0.354891 -0.0231253  0.0118775   0.0320576   19  GLN   A CD   
154  O  OE1  . GLN   A 19  ? 0.242275  0.438791 0.41363  -0.00402525 -0.00244185 0.0469328   19  GLN   A OE1  
155  N  NE2  . GLN   A 19  ? 0.21118   0.435841 0.374122 -0.018076   0.0202489   0.0341347   19  GLN   A NE2  
156  N  N    . VAL   A 20  ? 0.0959708 0.267266 0.207676 0.00628242  0.0273297   -0.00593294 20  VAL   A N    
157  C  CA   . VAL   A 20  ? 0.103076  0.276672 0.216693 0.00375637  0.0290459   -0.012091   20  VAL   A CA   
158  C  C    . VAL   A 20  ? 0.0972487 0.281522 0.214803 -0.00685984 0.0278538   -0.0111288  20  VAL   A C    
159  O  O    . VAL   A 20  ? 0.102411  0.286547 0.237646 -0.00445631 0.0191178   -0.00912871 20  VAL   A O    
160  C  CB   . VAL   A 20  ? 0.115151  0.275965 0.214614 0.0103753   0.0384771   -0.0149974  20  VAL   A CB   
161  C  CG1  . VAL   A 20  ? 0.122158  0.282156 0.211475 0.00434388  0.0387337   -0.016925   20  VAL   A CG1  
162  C  CG2  . VAL   A 20  ? 0.126924  0.272211 0.222571 0.0144119   0.0350671   -0.0156148  20  VAL   A CG2  
163  N  N    . THR   A 21  ? 0.0987228 0.302563 0.230301 -0.0054661  0.0322979   -0.00853989 21  THR   A N    
164  C  CA   . THR   A 21  ? 0.120162  0.318863 0.246955 -0.0152602  0.0186806   -0.00665714 21  THR   A CA   
165  C  C    . THR   A 21  ? 0.120582  0.340699 0.236255 -0.0149995  0.0239366   -0.0138453  21  THR   A C    
166  O  O    . THR   A 21  ? 0.141168  0.357664 0.267165 0.00300518  0.0115935   -0.0330288  21  THR   A O    
167  C  CB   . THR   A 21  ? 0.138022  0.34139  0.265778 -0.0246827  0.010384    0.0127222   21  THR   A CB   
168  O  OG1  . THR   A 21  ? 0.156271  0.370379 0.278422 -0.0311169  -0.00354603 0.0241939   21  THR   A OG1  
169  C  CG2  . THR   A 21  ? 0.132264  0.360065 0.290071 -0.034155   0.00921043  0.0120535   21  THR   A CG2  
170  N  N    . CYS   A 22  ? 0.122987  0.35422  0.239566 -0.0197585  0.0295411   -0.0190261  22  CYS   A N    
171  C  CA   . CYS   A 22  ? 0.139726  0.379069 0.239303 -0.0290434  0.0259937   -0.0233345  22  CYS   A CA   
172  C  C    . CYS   A 22  ? 0.142248  0.374205 0.26922  -0.0332361  0.0211568   -0.0163899  22  CYS   A C    
173  O  O    . CYS   A 22  ? 0.165957  0.365792 0.250844 -0.0225057  0.0108386   -0.0294567  22  CYS   A O    
174  C  CB   . CYS   A 22  ? 0.153249  0.410339 0.229259 -0.0345693  0.0338189   -0.0224108  22  CYS   A CB   
175  S  SG   . CYS   A 22  ? 0.231478  0.456828 0.269362 -0.0366168  -0.00659168 -0.00980534 22  CYS   A SG   
176  N  N    . GLY   A 23  ? 0.156107  0.392753 0.328261 -0.0553834  0.0269208   -0.0206725  23  GLY   A N    
177  C  CA   . GLY   A 23  ? 0.162546  0.398615 0.367537 -0.0689589  0.0315829   -0.0149742  23  GLY   A CA   
178  C  C    . GLY   A 23  ? 0.176443  0.388459 0.375705 -0.079835   0.0358175   -0.00804771 23  GLY   A C    
179  O  O    . GLY   A 23  ? 0.222312  0.395733 0.366111 -0.0791361  0.0543329   -0.00136255 23  GLY   A O    
180  N  N    . THR   A 24  ? 0.166288  0.367298 0.387249 -0.093282   0.0432181   -0.0108737  24  THR   A N    
181  C  CA   . THR   A 24  ? 0.214899  0.364102 0.409076 -0.088948   0.0421391   -0.00533414 24  THR   A CA   
182  C  C    . THR   A 24  ? 0.202337  0.331911 0.392942 -0.0681729  0.0499741   -0.00752349 24  THR   A C    
183  O  O    . THR   A 24  ? 0.199226  0.353586 0.439955 -0.068829   0.0397431   0.0088599   24  THR   A O    
184  C  CB   . THR   A 24  ? 0.26225   0.377181 0.43472  -0.100058   0.028869    -0.0107226  24  THR   A CB   
185  O  OG1  . THR   A 24  ? 0.325181  0.410434 0.457744 -0.0991903  0.0446508   -0.0387526  24  THR   A OG1  
186  C  CG2  . THR   A 24  ? 0.270422  0.388685 0.448127 -0.103355   0.0285314   -0.00465839 24  THR   A CG2  
187  N  N    . THR   A 25  ? 0.177302  0.318203 0.349133 -0.0657664  0.053472    -0.0227157  25  THR   A N    
188  C  CA   . THR   A 25  ? 0.180563  0.300372 0.352783 -0.0600999  0.0720987   -0.0278056  25  THR   A CA   
189  C  C    . THR   A 25  ? 0.160547  0.289875 0.340967 -0.0458983  0.0549706   -0.0251114  25  THR   A C    
190  O  O    . THR   A 25  ? 0.160497  0.302481 0.36603  -0.0393834  0.039335    -0.0284451  25  THR   A O    
191  C  CB   . THR   A 25  ? 0.2223    0.313342 0.359778 -0.0523301  0.0817908   -0.0292649  25  THR   A CB   
192  O  OG1  . THR   A 25  ? 0.285468  0.331325 0.377351 -0.0600467  0.105074    -0.0334796  25  THR   A OG1  
193  C  CG2  . THR   A 25  ? 0.225768  0.316535 0.372469 -0.0451916  0.105478    -0.0414111  25  THR   A CG2  
194  N  N    . THR   A 26  ? 0.156683  0.28003  0.354185 -0.0312692  0.0533119   -0.022918   26  THR   A N    
195  C  CA   . THR   A 26  ? 0.138019  0.287497 0.32655  -0.023837   0.045246    -0.0127332  26  THR   A CA   
196  C  C    . THR   A 26  ? 0.133612  0.257955 0.277349 -0.0119884  0.0323764   -0.0145091  26  THR   A C    
197  O  O    . THR   A 26  ? 0.135333  0.267214 0.309283 -0.014828   0.0282313   -0.033223   26  THR   A O    
198  C  CB   . THR   A 26  ? 0.189705  0.329724 0.340129 -0.0265901  0.0690123   -0.00302783 26  THR   A CB   
199  O  OG1  . THR   A 26  ? 0.207611  0.379508 0.38406  -0.0397284  0.0795617   0.0124914   26  THR   A OG1  
200  C  CG2  . THR   A 26  ? 0.205553  0.342124 0.331398 -0.0249314  0.0793998   -0.00348224 26  THR   A CG2  
201  N  N    . LEU   A 27  ? 0.109523  0.23987  0.230451 0.00212718  0.0202972   -0.0110306  27  LEU   A N    
202  C  CA   . LEU   A 27  ? 0.0984018 0.226745 0.208189 0.00907697  0.0142655   -0.0135368  27  LEU   A CA   
203  C  C    . LEU   A 27  ? 0.0940666 0.2206   0.188531 0.00566148  0.0195253   -0.00906411 27  LEU   A C    
204  O  O    . LEU   A 27  ? 0.107552  0.252357 0.196838 0.00890097  0.0297849   -0.0121271  27  LEU   A O    
205  C  CB   . LEU   A 27  ? 0.0911787 0.231273 0.209996 0.00843438  0.00561757  -0.017506   27  LEU   A CB   
206  C  CG   . LEU   A 27  ? 0.08752   0.237454 0.210471 0.00870256  0.00048192  -0.0220855  27  LEU   A CG   
207  C  CD1  . LEU   A 27  ? 0.0880965 0.238307 0.207475 0.0149249   -0.00092934 -0.0209248  27  LEU   A CD1  
208  C  CD2  . LEU   A 27  ? 0.105428  0.256805 0.218073 0.00979722  -0.00928064 -0.0250122  27  LEU   A CD2  
209  N  N    . ASN   A 28  ? 0.0942567 0.212096 0.166819 0.00810936  0.0171027   0.0003011   28  ASN   A N    
210  C  CA   . ASN   A 28  ? 0.0908661 0.22005  0.156525 0.0107958   0.00644923  -0.00290182 28  ASN   A CA   
211  C  C    . ASN   A 28  ? 0.0937293 0.219765 0.158414 0.0119464   0.00534903  -0.00230024 28  ASN   A C    
212  O  O    . ASN   A 28  ? 0.114889  0.234336 0.160206 0.0202595   -9.243e-05  -0.00018523 28  ASN   A O    
213  C  CB   . ASN   A 28  ? 0.0885955 0.222018 0.151376 0.00793842  0.00524705  -0.0026636  28  ASN   A CB   
214  C  CG   . ASN   A 28  ? 0.0927564 0.231151 0.151925 0.00806217  0.00896311  0.00352581  28  ASN   A CG   
215  O  OD1  . ASN   A 28  ? 0.106031  0.256418 0.151637 0.0168421   0.0112191   0.00845324  28  ASN   A OD1  
216  N  ND2  . ASN   A 28  ? 0.108996  0.233712 0.157021 0.0183349   0.00926292  0.00538594  28  ASN   A ND2  
217  N  N    . GLY   A 29  ? 0.0956571 0.220783 0.162757 0.0173793   0.00532775  -0.00420171 29  GLY   A N    
218  C  CA   . GLY   A 29  ? 0.102975  0.216577 0.164591 0.0199963   0.00669158  -0.0142705  29  GLY   A CA   
219  C  C    . GLY   A 29  ? 0.100534  0.211475 0.157674 0.0215728   0.00411622  -0.0142575  29  GLY   A C    
220  O  O    . GLY   A 29  ? 0.103435  0.229077 0.157944 0.0208026   0.00278923  -0.0135114  29  GLY   A O    
221  N  N    . LEU   A 30  ? 0.106632  0.215715 0.161996 0.0210616   -0.0059987  -0.0149126  30  LEU   A N    
222  C  CA   . LEU   A 30  ? 0.091458  0.221841 0.171873 0.0182859   -0.00301421 -0.0104296  30  LEU   A CA   
223  C  C    . LEU   A 30  ? 0.0977704 0.223194 0.184962 0.0240029   -0.0113646  -0.0125509  30  LEU   A C    
224  O  O    . LEU   A 30  ? 0.0991463 0.218113 0.188478 0.0303258   -0.0145741  -0.00964398 30  LEU   A O    
225  C  CB   . LEU   A 30  ? 0.0875967 0.222127 0.180384 0.0223247   -0.00376373 -0.005176   30  LEU   A CB   
226  C  CG   . LEU   A 30  ? 0.0914567 0.220201 0.200499 0.0230162   -1.796e-05  -0.0062649  30  LEU   A CG   
227  C  CD1  . LEU   A 30  ? 0.0932587 0.240322 0.205865 0.0181994   -0.00183972 -0.00658235 30  LEU   A CD1  
228  C  CD2  . LEU   A 30  ? 0.0993849 0.224186 0.205362 0.0209357   -0.00066104 -0.00114373 30  LEU   A CD2  
229  N  N    . TRP   A 31  ? 0.0845753 0.224509 0.186714 0.0354302   -0.014373   -0.0232679  31  TRP   A N    
230  C  CA   . TRP   A 31  ? 0.0953381 0.22899  0.203895 0.0388136   -0.0131027  -0.0263011  31  TRP   A CA   
231  C  C    . TRP   A 31  ? 0.110341  0.227347 0.210683 0.0342784   -0.00518202 -0.026564   31  TRP   A C    
232  O  O    . TRP   A 31  ? 0.114752  0.222518 0.212012 0.0265252   -0.0165825  -0.0352483  31  TRP   A O    
233  C  CB   . TRP   A 31  ? 0.108909  0.235539 0.208352 0.0422553   -0.00483261 -0.0333282  31  TRP   A CB   
234  C  CG   . TRP   A 31  ? 0.116759  0.256561 0.215621 0.0387483   0.00911351  -0.0409647  31  TRP   A CG   
235  C  CD1  . TRP   A 31  ? 0.131225  0.256632 0.222244 0.0401386   0.0140159   -0.0467557  31  TRP   A CD1  
236  C  CD2  . TRP   A 31  ? 0.141251  0.265467 0.222011 0.0268721   0.0266984   -0.0514095  31  TRP   A CD2  
237  N  NE1  . TRP   A 31  ? 0.130352  0.273065 0.239423 0.0445135   0.0229808   -0.0542538  31  TRP   A NE1  
238  C  CE2  . TRP   A 31  ? 0.142866  0.277029 0.222465 0.0316713   0.0330274   -0.0513893  31  TRP   A CE2  
239  C  CE3  . TRP   A 31  ? 0.168311  0.275344 0.220566 0.0137211   0.0272284   -0.0501407  31  TRP   A CE3  
240  C  CZ2  . TRP   A 31  ? 0.163276  0.282498 0.223983 0.0251867   0.0364337   -0.0585027  31  TRP   A CZ2  
241  C  CZ3  . TRP   A 31  ? 0.190251  0.294388 0.225815 0.0174589   0.0336809   -0.0564433  31  TRP   A CZ3  
242  C  CH2  . TRP   A 31  ? 0.186462  0.297113 0.225339 0.0176127   0.036331    -0.0533336  31  TRP   A CH2  
243  N  N    . LEU   A 32  ? 0.108121  0.217467 0.212562 0.0325049   -0.00983685 -0.0283261  32  LEU   A N    
244  C  CA   . LEU   A 32  ? 0.102952  0.2236   0.223645 0.0319544   -0.00345243 -0.0235988  32  LEU   A CA   
245  C  C    . LEU   A 32  ? 0.118509  0.230962 0.25374  0.0421981   -0.00995317 -0.0268166  32  LEU   A C    
246  O  O    . LEU   A 32  ? 0.127788  0.243698 0.261899 0.0437522   -0.0237003  -0.0243957  32  LEU   A O    
247  C  CB   . LEU   A 32  ? 0.114444  0.23263  0.22378  0.0360137   0.00039403  -0.0160697  32  LEU   A CB   
248  C  CG   . LEU   A 32  ? 0.117711  0.240078 0.233578 0.0389436   0.0100336   -0.0088157  32  LEU   A CG   
249  C  CD1  . LEU   A 32  ? 0.12831   0.258813 0.238072 0.0293578   0.0110339   -0.0147979  32  LEU   A CD1  
250  C  CD2  . LEU   A 32  ? 0.133779  0.253616 0.231643 0.0448947   0.0085582   -0.00301252 32  LEU   A CD2  
251  N  N    . ASP   A 33  ? 0.113409  0.242863 0.27861  0.0420605   -0.00400906 -0.0431882  33  ASP   A N    
252  C  CA   . ASP   A 33  ? 0.129887  0.243558 0.314676 0.0498164   -0.00129794 -0.0433577  33  ASP   A CA   
253  C  C    . ASP   A 33  ? 0.125002  0.238469 0.292568 0.0564239   0.00160737  -0.048516   33  ASP   A C    
254  O  O    . ASP   A 33  ? 0.136097  0.264448 0.282612 0.0662568   0.0111691   -0.0385677  33  ASP   A O    
255  C  CB   . ASP   A 33  ? 0.159234  0.261812 0.356952 0.0470503   -0.00221423 -0.0325479  33  ASP   A CB   
256  C  CG   . ASP   A 33  ? 0.204031  0.282029 0.41116  0.0192993   0.0101691   -0.0411321  33  ASP   A CG   
257  O  OD1  . ASP   A 33  ? 0.254277  0.356933 0.465094 -0.00237831 -0.0188359  -0.036341   33  ASP   A OD1  
258  O  OD2  . ASP   A 33  ? 0.244799  0.339799 0.477114 0.00977399  0.0369367   -0.021393   33  ASP   A OD2  
259  N  N    . ASP   A 34  ? 0.124389  0.25243  0.300564 0.0574124   -0.0056407  -0.0460605  34  ASP   A N    
260  C  CA   . ASP   A 34  ? 0.118375  0.269879 0.314944 0.0586863   -0.0077433  -0.0482208  34  ASP   A CA   
261  C  C    . ASP   A 34  ? 0.112133  0.264329 0.285577 0.0565986   -0.0109148  -0.0414244  34  ASP   A C    
262  O  O    . ASP   A 34  ? 0.123765  0.29115  0.294433 0.0487098   -0.0139609  -0.0476441  34  ASP   A O    
263  C  CB   . ASP   A 34  ? 0.133601  0.291941 0.357663 0.0742663   -0.0162223  -0.0506021  34  ASP   A CB   
264  C  CG   . ASP   A 34  ? 0.158171  0.301587 0.399695 0.0880643   -0.0188865  -0.0393296  34  ASP   A CG   
265  O  OD1  . ASP   A 34  ? 0.194907  0.307977 0.407042 0.0750046   -0.0326286  -0.0239819  34  ASP   A OD1  
266  O  OD2  . ASP   A 34  ? 0.209814  0.348639 0.482529 0.138778    -0.0317551  -0.0222906  34  ASP   A OD2  
267  N  N    . VAL   A 35  ? 0.107326  0.250685 0.259557 0.0517053   -0.0176295  -0.0381119  35  VAL   A N    
268  C  CA   . VAL   A 35  ? 0.112088  0.251661 0.237367 0.0462658   -0.0162663  -0.0260553  35  VAL   A CA   
269  C  C    . VAL   A 35  ? 0.0948613 0.248459 0.212998 0.041175    -0.0132607  -0.0359844  35  VAL   A C    
270  O  O    . VAL   A 35  ? 0.101244  0.248858 0.226101 0.0450315   -0.0270838  -0.0262741  35  VAL   A O    
271  C  CB   . VAL   A 35  ? 0.147281  0.265767 0.242016 0.0480756   -0.0194307  -0.0189329  35  VAL   A CB   
272  C  CG1  . VAL   A 35  ? 0.167217  0.280128 0.23391  0.0487564   -0.0226082  -0.0182404  35  VAL   A CG1  
273  C  CG2  . VAL   A 35  ? 0.184352  0.275013 0.260594 0.0506091   -0.00920608 -0.0108502  35  VAL   A CG2  
274  N  N    . VAL   A 36  ? 0.0911788 0.235238 0.211883 0.0299445   -0.00924469 -0.0312926  36  VAL   A N    
275  C  CA   . VAL   A 36  ? 0.10323   0.239575 0.202077 0.0262166   -0.0076659  -0.0258144  36  VAL   A CA   
276  C  C    . VAL   A 36  ? 0.101079  0.240983 0.193711 0.0250842   -0.0151458  -0.0241437  36  VAL   A C    
277  O  O    . VAL   A 36  ? 0.0991123 0.263418 0.207357 0.0376508   -0.0179055  -0.0314209  36  VAL   A O    
278  C  CB   . VAL   A 36  ? 0.103339  0.248405 0.211476 0.0208468   -0.00125983 -0.0254044  36  VAL   A CB   
279  C  CG1  . VAL   A 36  ? 0.127073  0.245506 0.213783 0.0137776   0.00399678  -0.0263378  36  VAL   A CG1  
280  C  CG2  . VAL   A 36  ? 0.110384  0.253981 0.216452 0.0274132   0.01059     -0.0264951  36  VAL   A CG2  
281  N  N    . TYR   A 37  ? 0.0975046 0.223076 0.190508 0.0224601   -0.0161944  -0.0212958  37  TYR   A N    
282  C  CA   . TYR   A 37  ? 0.10495   0.230627 0.187036 0.0223659   -0.0180569  -0.0143237  37  TYR   A CA   
283  C  C    . TYR   A 37  ? 0.0906679 0.231915 0.170328 0.0203332   -0.0148591  -0.0134401  37  TYR   A C    
284  O  O    . TYR   A 37  ? 0.10974   0.236383 0.164838 0.026       -0.0225196  -0.0143799  37  TYR   A O    
285  C  CB   . TYR   A 37  ? 0.106764  0.225028 0.198066 0.0236116   -0.0151455  -0.00937179 37  TYR   A CB   
286  C  CG   . TYR   A 37  ? 0.11782   0.223402 0.220413 0.030939    -0.0205532  -0.004008   37  TYR   A CG   
287  C  CD1  . TYR   A 37  ? 0.136666  0.215539 0.226785 0.0240355   -0.0353494  -0.00024397 37  TYR   A CD1  
288  C  CD2  . TYR   A 37  ? 0.135491  0.230159 0.232463 0.0252425   -0.018001   -0.00205199 37  TYR   A CD2  
289  C  CE1  . TYR   A 37  ? 0.15111   0.226376 0.243146 0.0187694   -0.0291835  -0.00581872 37  TYR   A CE1  
290  C  CE2  . TYR   A 37  ? 0.147318  0.230105 0.250141 0.0198325   -0.0249595  0.0079918   37  TYR   A CE2  
291  C  CZ   . TYR   A 37  ? 0.146679  0.225483 0.261642 0.0171063   -0.0339483  0.00420777  37  TYR   A CZ   
292  O  OH   . TYR   A 37  ? 0.178643  0.231479 0.306859 0.0114088   -0.042659   0.0126258   37  TYR   A OH   
293  N  N    . CYS   A 38  ? 0.09579   0.238673 0.16603  0.012713    -0.0110756  -0.0107326  38  CYS   A N    
294  C  CA   . CYS   A 38  ? 0.0978361 0.239457 0.168281 0.00348006  -0.0102563  -0.0145918  38  CYS   A CA   
295  C  C    . CYS   A 38  ? 0.0980499 0.23251  0.160467 0.0102233   -0.003424   -0.00734687 38  CYS   A C    
296  O  O    . CYS   A 38  ? 0.120737  0.232539 0.162632 0.0273279   -0.00844721 -0.00844468 38  CYS   A O    
297  C  CB   . CYS   A 38  ? 0.110726  0.249393 0.169924 -0.00100157 -0.00408483 -0.0137851  38  CYS   A CB   
298  S  SG   . CYS   A 38  ? 0.111195  0.300923 0.18811  -0.0109906  0.00524512  -0.0170649  38  CYS   A SG   
299  N  N    . PRO   A 39  ? 0.0882575 0.221376 0.153662 0.00692525  -0.0105984  -0.00407766 39  PRO   A N    
300  C  CA   . PRO   A 39  ? 0.0849778 0.222957 0.151824 0.00620266  -0.00653424 -0.00467163 39  PRO   A CA   
301  C  C    . PRO   A 39  ? 0.0866875 0.231613 0.157227 0.00444711  -0.00999132 -0.00632    39  PRO   A C    
302  O  O    . PRO   A 39  ? 0.0850141 0.246089 0.158529 0.0096765   -0.00648494 -0.0053969  39  PRO   A O    
303  C  CB   . PRO   A 39  ? 0.08277   0.225505 0.166331 0.0061235   -0.00053182 -0.00875613 39  PRO   A CB   
304  C  CG   . PRO   A 39  ? 0.0996021 0.221915 0.165585 0.00720407  -0.00615106 -0.00485842 39  PRO   A CG   
305  C  CD   . PRO   A 39  ? 0.0904518 0.226445 0.162851 0.00494326  -0.00865663 -0.00237284 39  PRO   A CD   
306  N  N    . ARG   A 40  ? 0.0827843 0.2386   0.161432 0.0139382   -0.00632284 -0.00011331 40  ARG   A N    
307  C  CA   . ARG   A 40  ? 0.0827051 0.251769 0.157183 0.0159192   -0.00654026 0.00035506  40  ARG   A CA   
308  C  C    . ARG   A 40  ? 0.0848638 0.251312 0.166176 0.0188633   -0.00949858 -0.00632878 40  ARG   A C    
309  O  O    . ARG   A 40  ? 0.0865051 0.265657 0.182391 0.0122156   -0.00790091 -0.0143627  40  ARG   A O    
310  C  CB   . ARG   A 40  ? 0.0901444 0.264521 0.160572 0.0135234   -0.00987104 0.00893007  40  ARG   A CB   
311  C  CG   . ARG   A 40  ? 0.0891165 0.280979 0.159675 0.0216903   -0.0108557  0.00657353  40  ARG   A CG   
312  C  CD   . ARG   A 40  ? 0.0935733 0.298049 0.161846 0.0215842   -0.012038   0.0113743   40  ARG   A CD   
313  N  NE   . ARG   A 40  ? 0.0871845 0.31795  0.16693  0.0312393   -0.00076107 0.0159941   40  ARG   A NE   
314  C  CZ   . ARG   A 40  ? 0.0908739 0.337228 0.174241 0.0441421   -0.012823   0.0150139   40  ARG   A CZ   
315  N  NH1  . ARG   A 40  ? 0.101644  0.347866 0.171748 0.0476797   -0.00091323 0.0188665   40  ARG   A NH1  
316  N  NH2  . ARG   A 40  ? 0.0861807 0.341894 0.174876 0.055924    -0.012369   0.0139792   40  ARG   A NH2  
317  N  N    . HIS   A 41  ? 0.0807849 0.251546 0.167068 0.0157333   -0.00807378 -0.00685735 41  HIS   A N    
318  C  CA   . HIS   A 41  ? 0.0902122 0.254533 0.174508 0.0203099   -0.0145406  -0.00715885 41  HIS   A CA   
319  C  C    . HIS   A 41  ? 0.0913976 0.252473 0.186756 0.0211511   -0.00842542 -0.0050489  41  HIS   A C    
320  O  O    . HIS   A 41  ? 0.0946974 0.250761 0.213822 0.0156015   0.00040821  -0.0127106  41  HIS   A O    
321  C  CB   . HIS   A 41  ? 0.0897241 0.261242 0.169436 0.0123058   -0.00519134 -0.00858608 41  HIS   A CB   
322  C  CG   . HIS   A 41  ? 0.0978697 0.262809 0.168106 0.015949    -0.00887777 -0.0100577  41  HIS   A CG   
323  N  ND1  . HIS   A 41  ? 0.105615  0.27317  0.176078 0.0259688   -0.00966693 -0.0054838  41  HIS   A ND1  
324  C  CD2  . HIS   A 41  ? 0.105752  0.263017 0.175207 0.00917067  0.0002736   -0.0091611  41  HIS   A CD2  
325  C  CE1  . HIS   A 41  ? 0.108906  0.270857 0.175906 0.0232085   -0.0105047  0.00153548  41  HIS   A CE1  
326  N  NE2  . HIS   A 41  ? 0.120512  0.2675   0.185743 0.0208158   -0.0061356  -0.003319   41  HIS   A NE2  
327  N  N    . VAL   A 42  ? 0.0942563 0.260017 0.18111  0.00945499  0.00077816  -0.00339785 42  VAL   A N    
328  C  CA   . VAL   A 42  ? 0.0959693 0.27546  0.185499 0.00462095  -0.00206525 0.00300182  42  VAL   A CA   
329  C  C    . VAL   A 42  ? 0.0952523 0.270364 0.195159 -0.00087185 0.00495795  0.00351255  42  VAL   A C    
330  O  O    . VAL   A 42  ? 0.106812  0.283012 0.214674 -0.0199941  0.00156475  0.0163571   42  VAL   A O    
331  C  CB   . VAL   A 42  ? 0.101543  0.284376 0.185769 0.0033668   0.00488161  -0.00051267 42  VAL   A CB   
332  C  CG1  . VAL   A 42  ? 0.101898  0.284435 0.192282 0.00384735  0.00170443  -0.00196797 42  VAL   A CG1  
333  C  CG2  . VAL   A 42  ? 0.113216  0.308548 0.182118 0.00184096  -4.489e-05  -0.00039409 42  VAL   A CG2  
334  N  N    . ILE   A 43  ? 0.0956746 0.264328 0.197329 -0.00179033 -0.00706926 -0.00646761 43  ILE   A N    
335  C  CA   . ILE   A 43  ? 0.0969044 0.283574 0.213879 0.00084975  -0.00862107 -0.0220428  43  ILE   A CA   
336  C  C    . ILE   A 43  ? 0.118269  0.295103 0.244545 0.00347014  -0.00599269 -0.036151   43  ILE   A C    
337  O  O    . ILE   A 43  ? 0.130432  0.33061  0.29894  -0.00106473 -0.017545   -0.0474218  43  ILE   A O    
338  C  CB   . ILE   A 43  ? 0.0898068 0.289212 0.198774 0.00771768  -0.0201296  -0.0259944  43  ILE   A CB   
339  C  CG1  . ILE   A 43  ? 0.0882406 0.305799 0.19872  0.01387     -0.0236982  -0.0238761  43  ILE   A CG1  
340  C  CG2  . ILE   A 43  ? 0.118451  0.281476 0.20045  0.0229068   -0.0230199  -0.025731   43  ILE   A CG2  
341  C  CD1  . ILE   A 43  ? 0.0922675 0.311249 0.198094 0.0108182   -0.0215484  -0.0255729  43  ILE   A CD1  
342  N  N    . CYS   A 44  ? 0.113765  0.30236  0.257182 0.00947568  -0.0194101  -0.0538142  44  CYS   A N    
343  C  CA   . CYS   A 44  ? 0.14071   0.318494 0.293824 0.00587351  -0.0146862  -0.0659153  44  CYS   A CA   
344  C  C    . CYS   A 44  ? 0.198838  0.345837 0.376637 0.00751021  -0.00021213 -0.058904   44  CYS   A C    
345  O  O    . CYS   A 44  ? 0.235768  0.360294 0.414604 0.00047009  0.00265298  -0.00656046 44  CYS   A O    
346  C  CB   . CYS   A 44  ? 0.155386  0.32682  0.280875 0.0111889   -0.0176021  -0.0614337  44  CYS   A CB   
347  S  SG   . CYS   A 44  ? 0.187831  0.352231 0.264869 0.00399048  -0.0353278  -0.0569589  44  CYS   A SG   
348  N  N    . THR   A 45  ? 0.186135  0.376787 0.454811 -0.00908925 0.0086033   -0.0620198  45  THR   A N    
349  C  CA   . THR   A 45  ? 0.256128  0.376841 0.514654 -0.0078249  0.01672     -0.0702765  45  THR   A CA   
350  C  C    . THR   A 45  ? 0.224007  0.375007 0.519944 -0.0208088  -0.00197597 -0.0878296  45  THR   A C    
351  O  O    . THR   A 45  ? 0.208942  0.376913 0.513276 0.00735227  -0.00251563 -0.0954696  45  THR   A O    
352  C  CB   . THR   A 45  ? 0.269151  0.402006 0.553535 -0.0219178  0.0134735   -0.0610206  45  THR   A CB   
353  O  OG1  . THR   A 45  ? 0.323762  0.415317 0.591025 -0.0266152  0.00054597  -0.0485772  45  THR   A OG1  
354  C  CG2  . THR   A 45  ? 0.270928  0.432295 0.576713 -0.0121896  0.0173536   -0.0581651  45  THR   A CG2  
355  N  N    . SER   A 46  ? 0.278392  0.380497 0.524904 -0.034876   -0.0167426  -0.101246   46  SER   A N    
356  C  CA   . SER   A 46  ? 0.306256  0.405116 0.530743 -0.00997546 -0.0390361  -0.106403   46  SER   A CA   
357  C  C    . SER   A 46  ? 0.36022   0.428308 0.536534 0.00510945  -0.0458564  -0.119795   46  SER   A C    
358  O  O    . SER   A 46  ? 0.382505  0.444083 0.453879 0.0292959   -0.0762982  -0.152321   46  SER   A O    
359  C  CB   . SER   A 46  ? 0.349642  0.412984 0.536252 -0.00969633 -0.0463364  -0.0900148  46  SER   A CB   
360  O  OG   . SER   A 46  ? 0.401195  0.43151  0.567554 -0.0272815  -0.0428956  -0.0548671  46  SER   A OG   
361  N  N    . GLU   A 47  ? 0.374301  0.454366 0.565173 0.00644434  -0.0598549  -0.130621   47  GLU   A N    
362  C  CA   . GLU   A 47  ? 0.418708  0.519829 0.588615 0.00796013  -0.0694485  -0.129929   47  GLU   A CA   
363  C  C    . GLU   A 47  ? 0.390912  0.480445 0.567216 0.0330239   -0.0639122  -0.162007   47  GLU   A C    
364  O  O    . GLU   A 47  ? 0.511395  0.573639 0.612259 0.0547813   -0.0928439  -0.132269   47  GLU   A O    
365  C  CB   . GLU   A 47  ? 0.476261  0.576334 0.61992  -0.0175273  -0.0586412  -0.118558   47  GLU   A CB   
366  C  CG   . GLU   A 47  ? 0.528217  0.627934 0.62602  -0.0188384  -0.0484821  -0.10716    47  GLU   A CG   
367  C  CD   . GLU   A 47  ? 0.595087  0.664357 0.655562 -0.00719626 -0.0440026  -0.101933   47  GLU   A CD   
368  O  OE1  . GLU   A 47  ? 0.654881  0.71108  0.649279 -0.0148985  -0.0463605  -0.112802   47  GLU   A OE1  
369  O  OE2  . GLU   A 47  ? 0.68225   0.727531 0.673055 -0.00839932 -0.0215996  -0.0829086  47  GLU   A OE2  
370  N  N    . ASP   A 48  ? 0.21489   0.466231 0.539618 0.0294321   -0.0636732  -0.156363   48  ASP   A N    
371  C  CA   . ASP   A 48  ? 0.178816  0.473018 0.510962 0.0256943   -0.0589424  -0.156537   48  ASP   A CA   
372  C  C    . ASP   A 48  ? 0.170926  0.457737 0.473632 0.0442015   -0.0547793  -0.143124   48  ASP   A C    
373  O  O    . ASP   A 48  ? 0.174282  0.461572 0.474694 0.0600753   -0.0835624  -0.145272   48  ASP   A O    
374  C  CB   . ASP   A 48  ? 0.186742  0.476707 0.522833 0.021514    -0.0327363  -0.167855   48  ASP   A CB   
375  C  CG   . ASP   A 48  ? 0.192283  0.488399 0.566652 0.0100918   -0.0274425  -0.178302   48  ASP   A CG   
376  O  OD1  . ASP   A 48  ? 0.202326  0.524847 0.635663 -0.00483761 -0.0453551  -0.185646   48  ASP   A OD1  
377  O  OD2  . ASP   A 48  ? 0.240532  0.523829 0.581254 -0.034535   -0.00065734 -0.197311   48  ASP   A OD2  
378  N  N    . MET   A 49  ? 0.157689  0.449811 0.492753 0.0319582   -0.041173   -0.112938   49  MET   A N    
379  C  CA   . MET   A 49  ? 0.158121  0.430467 0.433414 0.0264137   -0.0271911  -0.106638   49  MET   A CA   
380  C  C    . MET   A 49  ? 0.146971  0.408207 0.428614 0.0246736   -0.045286   -0.120083   49  MET   A C    
381  O  O    . MET   A 49  ? 0.141793  0.403982 0.371343 0.020369    -0.0399478  -0.109593   49  MET   A O    
382  C  CB   . MET   A 49  ? 0.167525  0.424603 0.418579 0.0247801   -0.0308198  -0.0985341  49  MET   A CB   
383  C  CG   . MET   A 49  ? 0.198882  0.40127  0.400458 0.0192046   -0.034318   -0.0962568  49  MET   A CG   
384  S  SD   . MET   A 49  ? 0.195765  0.406819 0.345036 0.0406149   -0.0273681  -0.0849235  49  MET   A SD   
385  C  CE   . MET   A 49  ? 0.217627  0.382943 0.375699 0.0339604   -0.0580282  -0.0693294  49  MET   A CE   
386  N  N    . LEU   A 50  ? 0.132937  0.400931 0.469583 3.761e-05   -0.03705    -0.133186   50  LEU   A N    
387  C  CA   . LEU   A 50  ? 0.133797  0.40046  0.461262 0.0197675   -0.0543609  -0.150003   50  LEU   A CA   
388  C  C    . LEU   A 50  ? 0.129417  0.400344 0.390321 0.0357214   -0.0657708  -0.157434   50  LEU   A C    
389  O  O    . LEU   A 50  ? 0.155498  0.408176 0.399861 0.0505376   -0.0963237  -0.164135   50  LEU   A O    
390  C  CB   . LEU   A 50  ? 0.175786  0.425614 0.505435 -0.00657538 -0.0717702  -0.148337   50  LEU   A CB   
391  C  CG   . LEU   A 50  ? 0.230861  0.435174 0.539578 -0.0084657  -0.0548778  -0.125706   50  LEU   A CG   
392  C  CD1  . LEU   A 50  ? 0.271618  0.414    0.531969 -0.0101631  -0.0474075  -0.128095   50  LEU   A CD1  
393  C  CD2  . LEU   A 50  ? 0.225594  0.455621 0.553385 -0.00461312 -0.0522286  -0.120605   50  LEU   A CD2  
394  N  N    . ASN   A 51  ? 0.14057   0.403392 0.360397 0.0478888   -0.0654883  -0.148282   51  ASN   A N    
395  C  CA   . ASN   A 51  ? 0.16815   0.384342 0.318144 0.0408985   -0.0635272  -0.140124   51  ASN   A CA   
396  C  C    . ASN   A 51  ? 0.151128  0.400138 0.313415 0.0427288   -0.0607067  -0.141551   51  ASN   A C    
397  O  O    . ASN   A 51  ? 0.198241  0.456979 0.358601 0.0738543   -0.0890947  -0.149791   51  ASN   A O    
398  C  CB   . ASN   A 51  ? 0.211694  0.38193  0.285754 0.0364782   -0.0554944  -0.11344    51  ASN   A CB   
399  C  CG   . ASN   A 51  ? 0.22995   0.379439 0.283265 0.0337176   -0.0293011  -0.0644989  51  ASN   A CG   
400  O  OD1  . ASN   A 51  ? 0.237192  0.384003 0.265173 0.0418875   -0.0323977  -0.0215644  51  ASN   A OD1  
401  N  ND2  . ASN   A 51  ? 0.238485  0.361197 0.26982  0.0249087   -0.0290546  -0.0422933  51  ASN   A ND2  
402  N  N    . PRO   A 52  ? 0.146249  0.378483 0.27751  0.0693509   -0.0557291  -0.121447   52  PRO   A N    
403  C  CA   . PRO   A 52  ? 0.141102  0.381444 0.281805 0.0639852   -0.0301132  -0.0990862  52  PRO   A CA   
404  C  C    . PRO   A 52  ? 0.129957  0.389173 0.252011 0.0653514   -0.0319061  -0.0824213  52  PRO   A C    
405  O  O    . PRO   A 52  ? 0.133489  0.418278 0.296852 0.0746036   -0.00451081 -0.0583323  52  PRO   A O    
406  C  CB   . PRO   A 52  ? 0.17182   0.381664 0.281475 0.0724757   -0.0428648  -0.108417   52  PRO   A CB   
407  C  CG   . PRO   A 52  ? 0.153693  0.372189 0.289372 0.0756252   -0.0575346  -0.113574   52  PRO   A CG   
408  C  CD   . PRO   A 52  ? 0.14692   0.382872 0.281655 0.0696209   -0.0588225  -0.115293   52  PRO   A CD   
409  N  N    . ASN   A 53  ? 0.12295   0.378672 0.230331 0.0437344   -0.0207671  -0.0791053  53  ASN   A N    
410  C  CA   . ASN   A 53  ? 0.135159  0.382085 0.202379 0.0374177   -0.0296434  -0.0612859  53  ASN   A CA   
411  C  C    . ASN   A 53  ? 0.113479  0.354623 0.183656 0.0376849   -0.0244005  -0.0483162  53  ASN   A C    
412  O  O    . ASN   A 53  ? 0.111763  0.346576 0.188481 0.0445844   -0.0220798  -0.0486136  53  ASN   A O    
413  C  CB   . ASN   A 53  ? 0.142777  0.406571 0.207043 0.0233058   -0.0336186  -0.0570258  53  ASN   A CB   
414  C  CG   . ASN   A 53  ? 0.173295  0.4384   0.22268  0.0221056   -0.0344146  -0.030362   53  ASN   A CG   
415  O  OD1  . ASN   A 53  ? 0.133535  0.426524 0.229141 0.00708688  -0.022385   0.0122261   53  ASN   A OD1  
416  N  ND2  . ASN   A 53  ? 0.232921  0.466116 0.251044 0.00646739  -0.0621475  -0.0253371  53  ASN   A ND2  
417  N  N    . TYR   A 54  ? 0.108364  0.348868 0.190981 0.0339956   -0.00720267 -0.0321761  54  TYR   A N    
418  C  CA   . TYR   A 54  ? 0.0947859 0.334436 0.187404 0.0310351   -0.0146186  -0.0253961  54  TYR   A CA   
419  C  C    . TYR   A 54  ? 0.0799189 0.341312 0.190154 0.0331741   -0.00971276 -0.0172888  54  TYR   A C    
420  O  O    . TYR   A 54  ? 0.0837286 0.351073 0.187636 0.0250215   -0.0130752  -0.0248236  54  TYR   A O    
421  C  CB   . TYR   A 54  ? 0.0927224 0.327746 0.191824 0.0353799   -0.0112689  -0.0175051  54  TYR   A CB   
422  C  CG   . TYR   A 54  ? 0.0967298 0.312819 0.177374 0.0278404   -0.0165196  -0.0193255  54  TYR   A CG   
423  C  CD1  . TYR   A 54  ? 0.0994853 0.31339  0.175965 0.0258328   -0.0115748  -0.0185308  54  TYR   A CD1  
424  C  CD2  . TYR   A 54  ? 0.103973  0.311515 0.164134 0.0234401   -0.0188026  -0.0223751  54  TYR   A CD2  
425  C  CE1  . TYR   A 54  ? 0.10138   0.317464 0.169022 0.0313984   -0.0166696  -0.0192188  54  TYR   A CE1  
426  C  CE2  . TYR   A 54  ? 0.0895348 0.31834  0.180853 0.0243644   -0.00785609 -0.0236963  54  TYR   A CE2  
427  C  CZ   . TYR   A 54  ? 0.0910893 0.312315 0.182131 0.0306954   -0.0134404  -0.0170648  54  TYR   A CZ   
428  O  OH   . TYR   A 54  ? 0.108113  0.322768 0.208442 0.0413263   -0.0183586  -0.012183   54  TYR   A OH   
429  N  N    . GLU   A 55  ? 0.0936538 0.338421 0.186305 0.0286329   0.00207867  -0.0083156  55  GLU   A N    
430  C  CA   . GLU   A 55  ? 0.0992877 0.340153 0.207012 0.0269264   0.00201963  -0.00509494 55  GLU   A CA   
431  C  C    . GLU   A 55  ? 0.0966057 0.325444 0.188699 0.0305837   -0.00629763 -0.00360496 55  GLU   A C    
432  O  O    . GLU   A 55  ? 0.0927302 0.322945 0.189054 0.030531    -0.00552989 0.00399435  55  GLU   A O    
433  C  CB   . GLU   A 55  ? 0.121436  0.361122 0.230299 0.0214103   -0.00750571 0.00703238  55  GLU   A CB   
434  C  CG   . GLU   A 55  ? 0.160287  0.401732 0.259475 -0.0091663  -0.00872315 0.0157337   55  GLU   A CG   
435  C  CD   . GLU   A 55  ? 0.194727  0.441012 0.316758 0.00250231  -0.00068541 0.0129149   55  GLU   A CD   
436  O  OE1  . GLU   A 55  ? 0.236062  0.473272 0.274909 -0.0188367  -0.00094127 0.00401039  55  GLU   A OE1  
437  O  OE2  . GLU   A 55  ? 0.252809  0.497241 0.382562 -0.0399738  -0.0328276  0.0289218   55  GLU   A OE2  
438  N  N    . ASP   A 56  ? 0.0864786 0.31118  0.187697 0.0290544   -0.00184254 -0.00579789 56  ASP   A N    
439  C  CA   . ASP   A 56  ? 0.0926911 0.310981 0.188479 0.0254999   -0.00745541 -0.00345414 56  ASP   A CA   
440  C  C    . ASP   A 56  ? 0.0920224 0.312513 0.185951 0.0293972   -0.010323   -0.00145324 56  ASP   A C    
441  O  O    . ASP   A 56  ? 0.105099  0.330153 0.201015 0.0349124   0.00032237  0.0131706   56  ASP   A O    
442  C  CB   . ASP   A 56  ? 0.101728  0.312964 0.199092 0.0193383   -0.00594127 -0.00481033 56  ASP   A CB   
443  C  CG   . ASP   A 56  ? 0.114816  0.311276 0.208912 0.0143678   -0.00638974 -0.00766627 56  ASP   A CG   
444  O  OD1  . ASP   A 56  ? 0.117188  0.322046 0.246415 0.0180973   -0.0127469  -0.00361689 56  ASP   A OD1  
445  O  OD2  . ASP   A 56  ? 0.177932  0.325883 0.252465 -0.00363666 0.0200748   -0.00282673 56  ASP   A OD2  
446  N  N    . LEU   A 57  ? 0.0824786 0.309516 0.181269 0.0298983   -0.0137527  -0.00946692 57  LEU   A N    
447  C  CA   . LEU   A 57  ? 0.0954492 0.29954  0.193323 0.0314257   -0.0110322  -0.0146631  57  LEU   A CA   
448  C  C    . LEU   A 57  ? 0.0889098 0.291936 0.176674 0.022822    -0.0212102  -0.0145551  57  LEU   A C    
449  O  O    . LEU   A 57  ? 0.104908  0.300184 0.193373 0.0164299   -0.00230235 -0.0134803  57  LEU   A O    
450  C  CB   . LEU   A 57  ? 0.0994475 0.300693 0.203855 0.0349057   -0.0220347  -0.0129723  57  LEU   A CB   
451  C  CG   . LEU   A 57  ? 0.13693   0.313412 0.229644 0.0412596   -0.0217574  -0.0230115  57  LEU   A CG   
452  C  CD1  . LEU   A 57  ? 0.14889   0.329705 0.247771 0.0490017   -0.0199543  -0.0308172  57  LEU   A CD1  
453  C  CD2  . LEU   A 57  ? 0.161123  0.320406 0.264254 0.038796    -0.0117768  -0.0263193  57  LEU   A CD2  
454  N  N    . LEU   A 58  ? 0.0894381 0.286032 0.177222 0.025413    -0.0127966  -0.0147883  58  LEU   A N    
455  C  CA   . LEU   A 58  ? 0.0867931 0.287719 0.182349 0.019946    -0.00793056 -0.0203267  58  LEU   A CA   
456  C  C    . LEU   A 58  ? 0.0902778 0.289924 0.181359 0.0259744   -0.002163   -0.0205986  58  LEU   A C    
457  O  O    . LEU   A 58  ? 0.0982882 0.299867 0.183206 0.0267522   -0.00223551 -0.0271455  58  LEU   A O    
458  C  CB   . LEU   A 58  ? 0.0908339 0.294286 0.207843 0.0148177   -0.0027357  -0.0262609  58  LEU   A CB   
459  C  CG   . LEU   A 58  ? 0.0934181 0.290576 0.227694 0.00428921  -0.00637062 -0.0301739  58  LEU   A CG   
460  C  CD1  . LEU   A 58  ? 0.0985475 0.288745 0.221607 0.00688896  -0.0115424  -0.0343855  58  LEU   A CD1  
461  C  CD2  . LEU   A 58  ? 0.109311  0.30098  0.258209 -0.00523665 0.00262167  -0.0350575  58  LEU   A CD2  
462  N  N    A ILE   A 59  ? 0.0863815 0.291725 0.180485 0.0345801   0.00253505  -0.0194719  59  ILE   A N    
463  N  N    B ILE   A 59  ? 0.0829998 0.290009 0.183321 0.0330087   0.00098503  -0.017842   59  ILE   A N    
464  C  CA   A ILE   A 59  ? 0.0846192 0.291934 0.182616 0.0328713   0.0026169   -0.0179326  59  ILE   A CA   
465  C  CA   B ILE   A 59  ? 0.0791978 0.288973 0.185779 0.030069    -0.00080158 -0.0154978  59  ILE   A CA   
466  C  C    A ILE   A 59  ? 0.0868352 0.287859 0.178334 0.0288725   -0.00338013 -0.018099   59  ILE   A C    
467  C  C    B ILE   A 59  ? 0.0829205 0.286077 0.180018 0.027238    -0.00487027 -0.0165773  59  ILE   A C    
468  O  O    A ILE   A 59  ? 0.109466  0.286469 0.193025 0.0348766   0.00702581  -0.0198435  59  ILE   A O    
469  O  O    B ILE   A 59  ? 0.10258   0.28318  0.194074 0.0329242   0.00501619  -0.0168565  59  ILE   A O    
470  C  CB   A ILE   A 59  ? 0.0915699 0.295258 0.186778 0.0349653   0.00454309  -0.0118756  59  ILE   A CB   
471  C  CB   B ILE   A 59  ? 0.0821035 0.29045  0.193728 0.0301083   -0.00077826 -0.00835915 59  ILE   A CB   
472  C  CG1  A ILE   A 59  ? 0.103759  0.294376 0.200102 0.0369318   0.00132579  -0.0128358  59  ILE   A CG1  
473  C  CG1  B ILE   A 59  ? 0.0924476 0.287548 0.207063 0.0284928   -0.00413671 -0.010429   59  ILE   A CG1  
474  C  CG2  A ILE   A 59  ? 0.093066  0.295159 0.185272 0.0356163   0.00993657  -0.0124808  59  ILE   A CG2  
475  C  CG2  B ILE   A 59  ? 0.0783239 0.288518 0.193995 0.0307318   0.00210659  -0.00928679 59  ILE   A CG2  
476  C  CD1  A ILE   A 59  ? 0.115194  0.296028 0.202017 0.0366818   0.00373159  -0.0144106  59  ILE   A CD1  
477  C  CD1  B ILE   A 59  ? 0.10422   0.292371 0.208816 0.0270965   -0.00048296 -0.0103089  59  ILE   A CD1  
478  N  N    . ARG   A 60  ? 0.0849293 0.288022 0.177812 0.0288555   -0.00700632 -0.017479   60  ARG   A N    
479  C  CA   . ARG   A 60  ? 0.095307  0.296237 0.178986 0.0241669   -0.0123282  -0.0196999  60  ARG   A CA   
480  C  C    . ARG   A 60  ? 0.107276  0.30373  0.17846  0.015558    -0.0112021  -0.0154337  60  ARG   A C    
481  O  O    . ARG   A 60  ? 0.11238   0.312604 0.19097  0.0104312   -0.00997901 -0.00773313 60  ARG   A O    
482  C  CB   . ARG   A 60  ? 0.0843541 0.2923   0.178597 0.0153659   -0.0177241  -0.0200467  60  ARG   A CB   
483  C  CG   . ARG   A 60  ? 0.0969122 0.297999 0.178351 0.0150377   -0.00880498 -0.026819   60  ARG   A CG   
484  C  CD   . ARG   A 60  ? 0.108485  0.301699 0.182268 0.0118866   -0.00932433 -0.033847   60  ARG   A CD   
485  N  NE   . ARG   A 60  ? 0.0993918 0.311886 0.182732 0.012019    -0.00901561 -0.0345648  60  ARG   A NE   
486  C  CZ   . ARG   A 60  ? 0.105214  0.308342 0.181748 0.0101821   -0.0100734  -0.0319694  60  ARG   A CZ   
487  N  NH1  . ARG   A 60  ? 0.102306  0.308    0.187    0.0155275   -0.00884627 -0.0264044  60  ARG   A NH1  
488  N  NH2  . ARG   A 60  ? 0.113269  0.322475 0.190517 0.00995312  -0.0153665  -0.0320646  60  ARG   A NH2  
489  N  N    . LYS   A 61  ? 0.130327  0.307747 0.175793 0.00516546  -0.00939329 -0.0304495  61  LYS   A N    
490  C  CA   . LYS   A 61  ? 0.121724  0.319947 0.188328 0.0100335   -0.0165547  -0.0307614  61  LYS   A CA   
491  C  C    . LYS   A 61  ? 0.149279  0.318325 0.204091 0.0094986   -0.0115924  -0.0332965  61  LYS   A C    
492  O  O    . LYS   A 61  ? 0.176784  0.319896 0.220705 0.032485    -0.00261861 -0.0250965  61  LYS   A O    
493  C  CB   . LYS   A 61  ? 0.12089   0.336806 0.199088 0.00766007  -0.0128241  -0.0370476  61  LYS   A CB   
494  C  CG   . LYS   A 61  ? 0.150932  0.355054 0.231112 0.0123185   -0.0107372  -0.0364402  61  LYS   A CG   
495  C  CD   . LYS   A 61  ? 0.183963  0.367525 0.27429  0.00511508  -0.0110501  -0.0366313  61  LYS   A CD   
496  C  CE   . LYS   A 61  ? 0.223215  0.381822 0.288206 0.00541718  -0.00064718 -0.0440889  61  LYS   A CE   
497  N  NZ   . LYS   A 61  ? 0.286579  0.413565 0.34589  -0.00518675 -0.00265048 -0.038963   61  LYS   A NZ   
498  N  N    . SER   A 62  ? 0.157444  0.328001 0.214588 0.0014835   -0.00480555 -0.0488625  62  SER   A N    
499  C  CA   . SER   A 62  ? 0.16307   0.346682 0.21916  0.00724816  -0.00450655 -0.0592314  62  SER   A CA   
500  C  C    . SER   A 62  ? 0.143918  0.336493 0.241855 0.0153448   -0.00431762 -0.0679468  62  SER   A C    
501  O  O    . SER   A 62  ? 0.139566  0.35421  0.249128 0.0221698   4.901e-05   -0.0808452  62  SER   A O    
502  C  CB   . SER   A 62  ? 0.199713  0.369029 0.247034 -0.00305504 0.00954904  -0.0497225  62  SER   A CB   
503  O  OG   . SER   A 62  ? 0.208509  0.417695 0.285806 0.0120341   0.00299315  -0.0383022  62  SER   A OG   
504  N  N    . ASN   A 63  ? 0.130854  0.329196 0.239608 0.0202847   4.328e-05   -0.0626423  63  ASN   A N    
505  C  CA   . ASN   A 63  ? 0.110896  0.342366 0.238984 0.0118449   0.00936916  -0.0688337  63  ASN   A CA   
506  C  C    . ASN   A 63  ? 0.105644  0.352695 0.235887 0.00855865  -0.00012133 -0.06204    63  ASN   A C    
507  O  O    . ASN   A 63  ? 0.113781  0.371363 0.21353  0.0155699   -0.0208604  -0.0639241  63  ASN   A O    
508  C  CB   . ASN   A 63  ? 0.12893   0.34265  0.263607 0.016635    0.0147499   -0.0725909  63  ASN   A CB   
509  C  CG   . ASN   A 63  ? 0.148014  0.355087 0.294883 0.0211716   0.0195839   -0.0636157  63  ASN   A CG   
510  O  OD1  . ASN   A 63  ? 0.209387  0.372326 0.308037 0.0281396   0.0554829   -0.0568451  63  ASN   A OD1  
511  N  ND2  . ASN   A 63  ? 0.131214  0.361002 0.320933 0.0269369   0.0120226   -0.057501   63  ASN   A ND2  
512  N  N    . HIS   A 64  ? 0.104711  0.37639  0.221691 -0.00358198 -0.0022741  -0.0518906  64  HIS   A N    
513  C  CA   . HIS   A 64  ? 0.119343  0.392233 0.217506 -0.0107528  0.0156434   -0.039519   64  HIS   A CA   
514  C  C    . HIS   A 64  ? 0.148793  0.382135 0.226206 -0.015261   0.0182316   -0.0295839  64  HIS   A C    
515  O  O    . HIS   A 64  ? 0.199567  0.405235 0.251523 -0.0127234  0.0186868   -0.0106418  64  HIS   A O    
516  C  CB   . HIS   A 64  ? 0.135371  0.41963  0.212364 -0.00729573 0.0235698   -0.0395651  64  HIS   A CB   
517  C  CG   . HIS   A 64  ? 0.159246  0.451824 0.214934 -0.0210356  0.0185302   -0.0357751  64  HIS   A CG   
518  N  ND1  . HIS   A 64  ? 0.177374  0.476371 0.230856 -0.0203276  -0.00213808 -0.0208474  64  HIS   A ND1  
519  C  CD2  . HIS   A 64  ? 0.196077  0.466029 0.236378 -0.0419678  0.00796202  -0.0231099  64  HIS   A CD2  
520  C  CE1  . HIS   A 64  ? 0.185669  0.483605 0.251048 -0.0410222  -0.00714419 -0.0133778  64  HIS   A CE1  
521  N  NE2  . HIS   A 64  ? 0.178794  0.483071 0.266422 -0.0506239  -0.00258926 -0.00900972 64  HIS   A NE2  
522  N  N    . ASN   A 65  ? 0.125646  0.374121 0.217191 -0.00441171 0.00065101  -0.0262652  65  ASN   A N    
523  C  CA   . ASN   A 65  ? 0.135389  0.356782 0.24703  -0.0180859  -0.00409417 -0.0306153  65  ASN   A CA   
524  C  C    . ASN   A 65  ? 0.128532  0.350679 0.254079 -0.00323876 0.0125065   -0.0402803  65  ASN   A C    
525  O  O    . ASN   A 65  ? 0.156035  0.350927 0.310235 0.00619349  -0.00621379 -0.0329606  65  ASN   A O    
526  C  CB   . ASN   A 65  ? 0.157525  0.372159 0.247015 -0.0281947  -0.00243252 -0.0266117  65  ASN   A CB   
527  C  CG   . ASN   A 65  ? 0.17264   0.395232 0.256514 -0.0457108  -0.0163131  -0.00510408 65  ASN   A CG   
528  O  OD1  . ASN   A 65  ? 0.203064  0.403285 0.243452 -0.0448847  -0.009176   -0.00454188 65  ASN   A OD1  
529  N  ND2  . ASN   A 65  ? 0.209643  0.422511 0.285994 -0.0616495  -0.0272736  0.021652    65  ASN   A ND2  
530  N  N    . PHE   A 66  ? 0.113911  0.353195 0.223284 0.00796517  0.00073384  -0.0479102  66  PHE   A N    
531  C  CA   . PHE   A 66  ? 0.115593  0.355125 0.232833 0.0177947   -0.0010169  -0.0492886  66  PHE   A CA   
532  C  C    . PHE   A 66  ? 0.134972  0.365672 0.22774  0.0234496   0.00847006  -0.0464327  66  PHE   A C    
533  O  O    . PHE   A 66  ? 0.220466  0.371211 0.227911 0.0429033   0.00530667  -0.0600895  66  PHE   A O    
534  C  CB   . PHE   A 66  ? 0.114911  0.351543 0.233093 0.0170678   -0.00132878 -0.0478237  66  PHE   A CB   
535  C  CG   . PHE   A 66  ? 0.115965  0.347935 0.229324 0.0134211   0.0117068   -0.045402   66  PHE   A CG   
536  C  CD1  . PHE   A 66  ? 0.12808   0.352452 0.223942 0.0162629   0.0210995   -0.0476799  66  PHE   A CD1  
537  C  CD2  . PHE   A 66  ? 0.110946  0.353419 0.229115 0.0164196   0.0135178   -0.0469606  66  PHE   A CD2  
538  C  CE1  . PHE   A 66  ? 0.135128  0.354748 0.220247 0.00787945  0.0228588   -0.0375183  66  PHE   A CE1  
539  C  CE2  . PHE   A 66  ? 0.116076  0.359207 0.229051 0.00570662  0.00879446  -0.0407569  66  PHE   A CE2  
540  C  CZ   . PHE   A 66  ? 0.131551  0.359493 0.215334 0.00669253  0.016247    -0.0415835  66  PHE   A CZ   
541  N  N    . LEU   A 67  ? 0.129475  0.37931  0.227423 0.019375    0.00292387  -0.0420272  67  LEU   A N    
542  C  CA   . LEU   A 67  ? 0.132679  0.395921 0.238927 0.0242218   0.00981902  -0.037768   67  LEU   A CA   
543  C  C    . LEU   A 67  ? 0.120065  0.374253 0.223292 0.0298101   0.0176663   -0.0410527  67  LEU   A C    
544  O  O    . LEU   A 67  ? 0.130951  0.434492 0.23536  0.0356224   0.00702822  -0.0881925  67  LEU   A O    
545  C  CB   . LEU   A 67  ? 0.209339  0.412248 0.27095  0.0272808   0.0189185   -0.0165012  67  LEU   A CB   
546  C  CG   . LEU   A 67  ? 0.267494  0.445954 0.345076 -0.00411448 0.0274424   -0.0071129  67  LEU   A CG   
547  C  CD1  . LEU   A 67  ? 0.31056   0.452353 0.361052 0.0051884   0.0341242   0.0113695   67  LEU   A CD1  
548  C  CD2  . LEU   A 67  ? 0.314012  0.474    0.373058 0.00969147  0.0373655   -0.0107608  67  LEU   A CD2  
549  N  N    . VAL   A 68  ? 0.128127  0.36328  0.208019 0.0336371   0.0341098   -0.0196566  68  VAL   A N    
550  C  CA   . VAL   A 68  ? 0.125889  0.338613 0.208084 0.0341064   0.0402335   -0.0217866  68  VAL   A CA   
551  C  C    . VAL   A 68  ? 0.129652  0.327081 0.208525 0.0321838   0.0315792   -0.0220738  68  VAL   A C    
552  O  O    . VAL   A 68  ? 0.145254  0.355456 0.2286   0.0462753   0.0371239   -0.0291774  68  VAL   A O    
553  C  CB   . VAL   A 68  ? 0.156989  0.351617 0.231391 0.0248546   0.0451565   -0.0146792  68  VAL   A CB   
554  C  CG1  . VAL   A 68  ? 0.160645  0.354161 0.24211  0.018077    0.0438322   -0.0068917  68  VAL   A CG1  
555  C  CG2  . VAL   A 68  ? 0.172054  0.357262 0.238325 0.0256713   0.0436582   -0.0132051  68  VAL   A CG2  
556  N  N    . GLN   A 69  ? 0.127788  0.32697  0.222146 0.0350232   0.0359892   -0.0281421  69  GLN   A N    
557  C  CA   . GLN   A 69  ? 0.166742  0.356118 0.233663 0.0287708   0.0221703   -0.0221644  69  GLN   A CA   
558  C  C    . GLN   A 69  ? 0.166191  0.353366 0.225788 0.0373475   0.0221617   -0.0233338  69  GLN   A C    
559  O  O    . GLN   A 69  ? 0.146316  0.350971 0.192719 0.0232988   0.0122035   -0.0274539  69  GLN   A O    
560  C  CB   . GLN   A 69  ? 0.225051  0.383428 0.284566 0.0109189   0.0153431   -0.0157939  69  GLN   A CB   
561  C  CG   . GLN   A 69  ? 0.31421   0.430769 0.332836 0.00497715  -0.00083599 0.00669286  69  GLN   A CG   
562  C  CD   . GLN   A 69  ? 0.388872  0.456927 0.410069 -0.00894508 -0.0175607  0.0201976   69  GLN   A CD   
563  O  OE1  . GLN   A 69  ? 0.443897  0.507968 0.459986 -0.041238   -0.0318815  0.0131153   69  GLN   A OE1  
564  N  NE2  . GLN   A 69  ? 0.424687  0.495807 0.437981 0.00670786  -0.0260022  0.0296241   69  GLN   A NE2  
565  N  N    . ALA   A 70  ? 0.185836  0.38177  0.220776 0.0448099   0.024368    -0.03304    70  ALA   A N    
566  C  CA   . ALA   A 70  ? 0.218289  0.399502 0.238582 0.0304107   0.0245181   -0.0454383  70  ALA   A CA   
567  C  C    . ALA   A 70  ? 0.259153  0.427192 0.258161 0.0332278   0.00977736  -0.0308467  70  ALA   A C    
568  O  O    . ALA   A 70  ? 0.304622  0.452415 0.256694 0.0414004   0.0202549   -0.0387448  70  ALA   A O    
569  C  CB   . ALA   A 70  ? 0.229919  0.398069 0.257863 0.0405363   0.0358656   -0.0491366  70  ALA   A CB   
570  N  N    . GLY   A 71  ? 0.268472  0.431799 0.268073 0.0391513   -0.00643897 -0.0119032  71  GLY   A N    
571  C  CA   . GLY   A 71  ? 0.321167  0.469945 0.28436  0.0336287   -0.00114611 0.00613813  71  GLY   A CA   
572  C  C    . GLY   A 71  ? 0.348985  0.498111 0.344243 0.0253433   0.0079762   0.0252276   71  GLY   A C    
573  O  O    . GLY   A 71  ? 0.393612  0.506063 0.416659 0.0225133   0.0149854   0.00248018  71  GLY   A O    
574  N  N    . ASN   A 72  ? 0.382488  0.545009 0.357546 0.0172012   0.0373406   0.0440082   72  ASN   A N    
575  C  CA   . ASN   A 72  ? 0.39772   0.588892 0.367541 0.0137511   0.0498475   0.0584511   72  ASN   A CA   
576  C  C    . ASN   A 72  ? 0.387233  0.612575 0.376022 0.020741    0.0563954   0.0521872   72  ASN   A C    
577  O  O    . ASN   A 72  ? 0.423036  0.646777 0.413695 -2.551e-05  0.0874      0.0696384   72  ASN   A O    
578  C  CB   . ASN   A 72  ? 0.427774  0.609627 0.374702 0.00229758  0.0469164   0.0748588   72  ASN   A CB   
579  N  N    . VAL   A 73  ? 0.359846  0.607935 0.286598 0.0409456   0.0384919   0.035729    73  VAL   A N    
580  C  CA   . VAL   A 73  ? 0.335007  0.604994 0.283959 0.0474701   0.0416639   0.00674326  73  VAL   A CA   
581  C  C    . VAL   A 73  ? 0.25187   0.572803 0.262401 0.0518428   0.0728955   -0.00447324 73  VAL   A C    
582  O  O    . VAL   A 73  ? 0.253861  0.546242 0.250131 0.0743294   0.0804682   -0.013609   73  VAL   A O    
583  C  CB   . VAL   A 73  ? 0.35814   0.621837 0.306425 0.033354    0.00338311  -0.0052696  73  VAL   A CB   
584  C  CG1  . VAL   A 73  ? 0.391712  0.620744 0.322207 0.0429531   0.00814082  -0.0139088  73  VAL   A CG1  
585  C  CG2  . VAL   A 73  ? 0.389696  0.636189 0.304975 0.0305868   0.00223987  0.00057003  73  VAL   A CG2  
586  N  N    . GLN   A 74  ? 0.241725  0.559339 0.303868 0.0385833   0.104313    -0.0119671  74  GLN   A N    
587  C  CA   . GLN   A 74  ? 0.219228  0.519755 0.318984 0.0300537   0.0983069   -0.0272193  74  GLN   A CA   
588  C  C    . GLN   A 74  ? 0.206398  0.476784 0.311323 0.0467651   0.074494    -0.0631859  74  GLN   A C    
589  O  O    . GLN   A 74  ? 0.32437   0.498564 0.310721 0.0553832   0.107654    -0.0740648  74  GLN   A O    
590  C  CB   . GLN   A 74  ? 0.24423   0.551734 0.387575 0.00899174  0.0873491   -0.00328404 74  GLN   A CB   
591  C  CG   . GLN   A 74  ? 0.317394  0.586565 0.427431 0.00063808  0.0747343   0.0200316   74  GLN   A CG   
592  C  CD   . GLN   A 74  ? 0.397345  0.611255 0.466753 0.0125025   0.0546739   0.00925613  74  GLN   A CD   
593  O  OE1  . GLN   A 74  ? 0.459718  0.658271 0.461001 -0.00569088 0.0605501   0.00134311  74  GLN   A OE1  
594  N  NE2  . GLN   A 74  ? 0.429907  0.62435  0.510059 0.01874     0.0412114   0.0263144   74  GLN   A NE2  
595  N  N    . LEU   A 75  ? 0.165472  0.40305  0.284794 0.035656    0.0426599   -0.0858126  75  LEU   A N    
596  C  CA   . LEU   A 75  ? 0.179191  0.390796 0.2859   0.031801    0.0126635   -0.0842578  75  LEU   A CA   
597  C  C    . LEU   A 75  ? 0.19744   0.404158 0.30029  0.0376599   -0.00753546 -0.0914026  75  LEU   A C    
598  O  O    . LEU   A 75  ? 0.287637  0.409484 0.372478 0.0479685   -0.0648021  -0.114522   75  LEU   A O    
599  C  CB   . LEU   A 75  ? 0.197716  0.382764 0.306355 0.0288301   0.017205    -0.0669485  75  LEU   A CB   
600  C  CG   . LEU   A 75  ? 0.194579  0.379864 0.325015 0.0252126   0.0202145   -0.0467357  75  LEU   A CG   
601  C  CD1  . LEU   A 75  ? 0.21763   0.382535 0.351939 0.00149691  0.0387105   -0.0376989  75  LEU   A CD1  
602  C  CD2  . LEU   A 75  ? 0.227006  0.393175 0.339422 0.0201009   0.0147443   -0.0537308  75  LEU   A CD2  
603  N  N    . ARG   A 76  ? 0.161512  0.40517  0.273573 0.0182513   0.00549932  -0.0892597  76  ARG   A N    
604  C  CA   . ARG   A 76  ? 0.15996   0.430208 0.281253 0.00374657  0.00377433  -0.092227   76  ARG   A CA   
605  C  C    . ARG   A 76  ? 0.130311  0.38987  0.272611 0.00982762  0.00840789  -0.0972498  76  ARG   A C    
606  O  O    . ARG   A 76  ? 0.112559  0.385137 0.265085 0.00579967  0.019164    -0.106561   76  ARG   A O    
607  C  CB   . ARG   A 76  ? 0.203791  0.476765 0.314032 0.025498    0.0178393   -0.101998   76  ARG   A CB   
608  C  CG   . ARG   A 76  ? 0.218154  0.520507 0.353576 0.0237578   0.0144764   -0.103536   76  ARG   A CG   
609  C  CD   . ARG   A 76  ? 0.265123  0.561337 0.392602 0.0488393   0.0409826   -0.0991146  76  ARG   A CD   
610  N  NE   . ARG   A 76  ? 0.369064  0.592971 0.464662 0.0496514   0.0297404   -0.0802872  76  ARG   A NE   
611  C  CZ   . ARG   A 76  ? 0.419455  0.644035 0.482506 0.0403812   0.0115973   -0.0650498  76  ARG   A CZ   
612  N  NH1  . ARG   A 76  ? 0.462866  0.657507 0.520954 0.0330508   0.0255947   -0.0790694  76  ARG   A NH1  
613  N  NH2  . ARG   A 76  ? 0.465504  0.654622 0.513123 0.0557464   0.0114132   -0.0711985  76  ARG   A NH2  
614  N  N    . VAL   A 77  ? 0.115871  0.393106 0.262143 0.00965996  0.00801036  -0.0890628  77  VAL   A N    
615  C  CA   . VAL   A 77  ? 0.106642  0.366726 0.258863 0.0149929   -0.00024251 -0.0803355  77  VAL   A CA   
616  C  C    . VAL   A 77  ? 0.113172  0.362347 0.254466 0.0237033   0.00423683  -0.0859032  77  VAL   A C    
617  O  O    . VAL   A 77  ? 0.134144  0.389154 0.2721   0.00370451  0.00414229  -0.0938086  77  VAL   A O    
618  C  CB   . VAL   A 77  ? 0.103691  0.367439 0.26301  0.00807808  -0.00546685 -0.0789268  77  VAL   A CB   
619  C  CG1  . VAL   A 77  ? 0.0881281 0.367652 0.271136 0.0151125   -0.00306615 -0.0736245  77  VAL   A CG1  
620  C  CG2  . VAL   A 77  ? 0.121059  0.377618 0.276034 0.00943211  -0.00851955 -0.0694124  77  VAL   A CG2  
621  N  N    . ILE   A 78  ? 0.118569  0.366526 0.278176 0.0343197   0.00138936  -0.0704919  78  ILE   A N    
622  C  CA   . ILE   A 78  ? 0.125794  0.372565 0.311951 0.0422137   0.00468224  -0.0663169  78  ILE   A CA   
623  C  C    . ILE   A 78  ? 0.132497  0.367056 0.316015 0.0494318   -0.0041831  -0.0572619  78  ILE   A C    
624  O  O    . ILE   A 78  ? 0.17462   0.387377 0.338644 0.0754591   -0.00713203 -0.0527398  78  ILE   A O    
625  C  CB   . ILE   A 78  ? 0.165696  0.382012 0.337219 0.0395828   0.00492444  -0.0724536  78  ILE   A CB   
626  C  CG1  . ILE   A 78  ? 0.175403  0.391079 0.359102 0.0334586   3.622e-05   -0.0791752  78  ILE   A CG1  
627  C  CG2  . ILE   A 78  ? 0.16843   0.394827 0.342789 0.0405563   0.01301     -0.0705716  78  ILE   A CG2  
628  C  CD1  . ILE   A 78  ? 0.196544  0.396083 0.383869 0.0378401   0.00538632  -0.0763435  78  ILE   A CD1  
629  N  N    . GLY   A 79  ? 0.111184  0.354645 0.289061 0.0473037   -0.0143141  -0.0457445  79  GLY   A N    
630  C  CA   . GLY   A 79  ? 0.117882  0.35366  0.305972 0.0500717   -0.0117199  -0.0417009  79  GLY   A CA   
631  C  C    . GLY   A 79  ? 0.104935  0.351158 0.290778 0.0456642   -0.00532378 -0.030101   79  GLY   A C    
632  O  O    . GLY   A 79  ? 0.109659  0.356357 0.289995 0.03847     -0.0229579  -0.0349089  79  GLY   A O    
633  N  N    . HIS   A 80  ? 0.100387  0.352874 0.286738 0.0603541   -0.0147867  -0.0276557  80  HIS   A N    
634  C  CA   . HIS   A 80  ? 0.111172  0.36697  0.284477 0.0683328   -0.0178828  -0.0275126  80  HIS   A CA   
635  C  C    . HIS   A 80  ? 0.116525  0.3812   0.28321  0.0785664   -0.0315958  -0.0161593  80  HIS   A C    
636  O  O    . HIS   A 80  ? 0.128345  0.419949 0.284948 0.0889665   -0.0432869  -0.00459755 80  HIS   A O    
637  C  CB   . HIS   A 80  ? 0.130524  0.362185 0.2748   0.0704929   -0.0123398  -0.0309874  80  HIS   A CB   
638  C  CG   . HIS   A 80  ? 0.15342   0.376112 0.28523  0.0511512   -0.0252645  -0.0381569  80  HIS   A CG   
639  N  ND1  . HIS   A 80  ? 0.168332  0.393716 0.287129 0.0286448   -0.0175053  -0.0377997  80  HIS   A ND1  
640  C  CD2  . HIS   A 80  ? 0.17869   0.377851 0.286458 0.0491757   -0.0173707  -0.0480702  80  HIS   A CD2  
641  C  CE1  . HIS   A 80  ? 0.185623  0.400348 0.301269 0.0281239   -0.0264263  -0.0466618  80  HIS   A CE1  
642  N  NE2  . HIS   A 80  ? 0.189132  0.399325 0.306823 0.0230079   -0.0271483  -0.0535203  80  HIS   A NE2  
643  N  N    . SER   A 81  ? 0.118189  0.380178 0.276328 0.0846638   -0.0362109  -0.00807219 81  SER   A N    
644  C  CA   . SER   A 81  ? 0.153404  0.358424 0.289885 0.0882605   -0.0299897  -0.00305105 81  SER   A CA   
645  C  C    . SER   A 81  ? 0.132048  0.336402 0.266303 0.0758515   -0.0361133  0.0055989   81  SER   A C    
646  O  O    . SER   A 81  ? 0.155335  0.358929 0.265567 0.104746    -0.0529468  -0.0137438  81  SER   A O    
647  C  CB   . SER   A 81  ? 0.190416  0.35736  0.333363 0.10094     -0.0288289  -0.0019484  81  SER   A CB   
648  O  OG   . SER   A 81  ? 0.228006  0.358351 0.372031 0.0823704   -0.0248633  -0.0118169  81  SER   A OG   
649  N  N    . MET   A 82  ? 0.123729  0.320781 0.268263 0.0568614   -0.0246828  0.0162974   82  MET   A N    
650  C  CA   . MET   A 82  ? 0.151678  0.311757 0.277671 0.0506848   -0.012445   0.0114784   82  MET   A CA   
651  C  C    . MET   A 82  ? 0.163372  0.303995 0.273679 0.0605821   -0.00762963 0.0244691   82  MET   A C    
652  O  O    . MET   A 82  ? 0.180236  0.330284 0.297427 0.0732902   0.0172883   0.0490277   82  MET   A O    
653  C  CB   . MET   A 82  ? 0.17968   0.327916 0.310954 0.0331947   -0.00879801 -0.00282056 82  MET   A CB   
654  C  CG   . MET   A 82  ? 0.163728  0.335586 0.324867 0.0395915   -0.0140613  -0.00771963 82  MET   A CG   
655  S  SD   . MET   A 82  ? 0.139679  0.342001 0.332705 0.0401836   -0.043812   -0.00799151 82  MET   A SD   
656  C  CE   . MET   A 82  ? 0.136505  0.332424 0.346539 0.0455832   -0.0434064  -0.0119885  82  MET   A CE   
657  N  N    . GLN   A 83  ? 0.155768  0.276058 0.258513 0.0542875   -0.00347389 0.0428429   83  GLN   A N    
658  C  CA   . GLN   A 83  ? 0.165591  0.279606 0.258606 0.0556355   -0.0031     0.0510928   83  GLN   A CA   
659  C  C    . GLN   A 83  ? 0.148907  0.289722 0.242912 0.0494794   -0.00694494 0.0458963   83  GLN   A C    
660  O  O    . GLN   A 83  ? 0.161722  0.283929 0.234599 0.0527343   -0.021024   0.0418198   83  GLN   A O    
661  C  CB   . GLN   A 83  ? 0.172742  0.289154 0.278503 0.0530197   -0.00630882 0.0574324   83  GLN   A CB   
662  C  CG   . GLN   A 83  ? 0.18877   0.300316 0.295648 0.0428647   -0.00637623 0.0644448   83  GLN   A CG   
663  C  CD   . GLN   A 83  ? 0.195635  0.320383 0.329879 0.0414202   -0.0204478  0.0663838   83  GLN   A CD   
664  O  OE1  . GLN   A 83  ? 0.223564  0.355614 0.35376  0.0399068   -0.0534649  0.0614462   83  GLN   A OE1  
665  N  NE2  . GLN   A 83  ? 0.236196  0.35132  0.367457 0.0255524   -0.0180836  0.0689439   83  GLN   A NE2  
666  N  N    . ASN   A 84  ? 0.14086   0.295902 0.236106 0.042102    -0.0160889  0.0528511   84  ASN   A N    
667  C  CA   . ASN   A 84  ? 0.127804  0.30474  0.217585 0.0334154   -0.0124224  0.0456212   84  ASN   A CA   
668  C  C    . ASN   A 84  ? 0.107546  0.295075 0.195977 0.0340126   -0.0108571  0.0373999   84  ASN   A C    
669  O  O    . ASN   A 84  ? 0.103956  0.312127 0.22381  0.033195    -0.0165618  0.0431103   84  ASN   A O    
670  C  CB   . ASN   A 84  ? 0.132992  0.319092 0.214896 0.0331484   -0.0118733  0.0542127   84  ASN   A CB   
671  C  CG   . ASN   A 84  ? 0.151587  0.33011  0.228089 0.0408609   -0.017637   0.0643813   84  ASN   A CG   
672  O  OD1  . ASN   A 84  ? 0.179792  0.364688 0.231719 0.0332652   -0.0234989  0.0775139   84  ASN   A OD1  
673  N  ND2  . ASN   A 84  ? 0.169717  0.32864  0.240284 0.0414538   -0.0191354  0.071934    84  ASN   A ND2  
674  N  N    . CYS   A 85  ? 0.0997072 0.28211  0.178488 0.0302133   -0.00578552 0.0274753   85  CYS   A N    
675  C  CA   . CYS   A 85  ? 0.09321   0.281774 0.181457 0.0311534   -0.0125178  0.0191384   85  CYS   A CA   
676  C  C    . CYS   A 85  ? 0.0848734 0.268592 0.18279  0.0336429   -0.00997185 0.0173538   85  CYS   A C    
677  O  O    . CYS   A 85  ? 0.0984813 0.256965 0.182026 0.0341539   -0.0152502  0.0144947   85  CYS   A O    
678  C  CB   . CYS   A 85  ? 0.101661  0.298455 0.184999 0.0321527   -0.00774632 0.0152139   85  CYS   A CB   
679  S  SG   . CYS   A 85  ? 0.136227  0.344185 0.184285 0.0350945   0.00328041  0.00346606  85  CYS   A SG   
680  N  N    A VAL   A 86  ? 0.104235  0.276338 0.187958 0.0378612   -0.0125043  0.0137865   86  VAL   A N    
681  N  N    B VAL   A 86  ? 0.105178  0.272768 0.183314 0.0354322   -0.00791139 0.013402    86  VAL   A N    
682  C  CA   A VAL   A 86  ? 0.118079  0.285281 0.195723 0.047054    -0.00920619 0.00955067  86  VAL   A CA   
683  C  CA   B VAL   A 86  ? 0.118377  0.276669 0.189642 0.0428577   -0.00233421 0.0078771   86  VAL   A CA   
684  C  C    A VAL   A 86  ? 0.121738  0.287945 0.19272  0.051213    -0.00773404 0.0132642   86  VAL   A C    
685  C  C    B VAL   A 86  ? 0.121316  0.283235 0.1902   0.0494166   -0.00430762 0.0114668   86  VAL   A C    
686  O  O    A VAL   A 86  ? 0.147658  0.295568 0.206618 0.0645723   0.00180437  0.0276198   86  VAL   A O    
687  O  O    B VAL   A 86  ? 0.147165  0.290779 0.203233 0.0625735   0.00540502  0.0260158   86  VAL   A O    
688  C  CB   A VAL   A 86  ? 0.139113  0.299172 0.211714 0.0399796   -0.0152953  0.00315109  86  VAL   A CB   
689  C  CB   B VAL   A 86  ? 0.137853  0.281202 0.196059 0.0333647   -0.00019717 0.00232238  86  VAL   A CB   
690  C  CG1  A VAL   A 86  ? 0.148438  0.302831 0.225572 0.0444534   -0.0110845  0.00280154  86  VAL   A CG1  
691  C  CG1  B VAL   A 86  ? 0.138451  0.280347 0.203382 0.0245785   0.00742685  -0.00505804 86  VAL   A CG1  
692  C  CG2  A VAL   A 86  ? 0.133964  0.299904 0.216252 0.0363815   -0.0171035  0.0014198   86  VAL   A CG2  
693  C  CG2  B VAL   A 86  ? 0.145522  0.285158 0.210032 0.0377992   0.0035162   0.00219929  86  VAL   A CG2  
694  N  N    . LEU   A 87  ? 0.125744  0.280164 0.182254 0.0457362   -0.0106479  0.00615244  87  LEU   A N    
695  C  CA   . LEU   A 87  ? 0.128663  0.297245 0.204808 0.0438376   -0.0077201  0.00071444  87  LEU   A CA   
696  C  C    . LEU   A 87  ? 0.110484  0.300561 0.208593 0.0413867   -0.0116842  -0.00311309 87  LEU   A C    
697  O  O    . LEU   A 87  ? 0.119496  0.285082 0.190436 0.039938    -0.0200343  -0.00814562 87  LEU   A O    
698  C  CB   . LEU   A 87  ? 0.15291   0.308559 0.231221 0.0299659   0.00080392  0.00264601  87  LEU   A CB   
699  C  CG   . LEU   A 87  ? 0.167554  0.326913 0.27808  0.0436723   0.0137354   -0.00814768 87  LEU   A CG   
700  C  CD1  . LEU   A 87  ? 0.15764   0.333654 0.288775 0.0442807   0.0102939   -0.0139633  87  LEU   A CD1  
701  C  CD2  . LEU   A 87  ? 0.178544  0.32651  0.300795 0.0336431   0.019781    -0.00586414 87  LEU   A CD2  
702  N  N    . LYS   A 88  ? 0.105612  0.314868 0.214728 0.0462248   -0.0209683  -0.0108641  88  LYS   A N    
703  C  CA   . LYS   A 88  ? 0.0992587 0.32437  0.227152 0.0457794   -0.019411   -0.019184   88  LYS   A CA   
704  C  C    . LYS   A 88  ? 0.100913  0.321597 0.230634 0.0557532   -0.0131423  -0.0260975  88  LYS   A C    
705  O  O    . LYS   A 88  ? 0.117847  0.37592  0.231744 0.0674835   -0.0213252  -0.0174876  88  LYS   A O    
706  C  CB   . LYS   A 88  ? 0.122974  0.332137 0.241231 0.0397881   -0.020309   -0.0058615  88  LYS   A CB   
707  C  CG   . LYS   A 88  ? 0.12902   0.345935 0.277387 0.0261668   -0.0149245  0.00533245  88  LYS   A CG   
708  C  CD   . LYS   A 88  ? 0.193561  0.36334  0.327289 0.0153584   -0.00484121 0.0163184   88  LYS   A CD   
709  C  CE   . LYS   A 88  ? 0.222664  0.375221 0.35093  0.00759905  -0.00101809 0.0321834   88  LYS   A CE   
710  N  NZ   . LYS   A 88  ? 0.273686  0.38259  0.373841 0.00710564  0.0159828   0.0419924   88  LYS   A NZ   
711  N  N    . LEU   A 89  ? 0.0776113 0.30144  0.226288 0.0474388   -0.0149177  -0.0320637  89  LEU   A N    
712  C  CA   . LEU   A 89  ? 0.0887553 0.30376  0.221059 0.0408062   -0.0117772  -0.0338276  89  LEU   A CA   
713  C  C    . LEU   A 89  ? 0.091966  0.307261 0.255376 0.0416603   -0.0110558  -0.0463219  89  LEU   A C    
714  O  O    . LEU   A 89  ? 0.106882  0.313999 0.255767 0.0378476   -0.0278936  -0.0654345  89  LEU   A O    
715  C  CB   . LEU   A 89  ? 0.106528  0.305329 0.223376 0.0276429   -0.0116597  -0.0300127  89  LEU   A CB   
716  C  CG   . LEU   A 89  ? 0.126203  0.301455 0.228526 0.0257164   -0.0140047  -0.0249845  89  LEU   A CG   
717  C  CD1  . LEU   A 89  ? 0.151746  0.31444  0.239883 0.0187084   -0.011277   -0.0190512  89  LEU   A CD1  
718  C  CD2  . LEU   A 89  ? 0.131897  0.3078   0.233596 0.0277252   -0.0217896  -0.0249512  89  LEU   A CD2  
719  N  N    . LYS   A 90  ? 0.0999179 0.311556 0.274237 0.0477007   -0.0165005  -0.051553   90  LYS   A N    
720  C  CA   . LYS   A 90  ? 0.111622  0.318806 0.298077 0.0423168   -0.0107335  -0.0577763  90  LYS   A CA   
721  C  C    . LYS   A 90  ? 0.104086  0.320371 0.30184  0.0354947   -0.00140919 -0.0572804  90  LYS   A C    
722  O  O    . LYS   A 90  ? 0.11322   0.324837 0.2859   0.0261954   0.0124076   -0.06772    90  LYS   A O    
723  C  CB   . LYS   A 90  ? 0.136644  0.337805 0.341321 0.0538362   -0.0258581  -0.0462217  90  LYS   A CB   
724  C  CG   . LYS   A 90  ? 0.192533  0.369994 0.371947 0.0412251   -0.0249566  -0.0570129  90  LYS   A CG   
725  C  CD   . LYS   A 90  ? 0.242673  0.416178 0.424085 0.0533717   -0.0332097  -0.0396284  90  LYS   A CD   
726  C  CE   . LYS   A 90  ? 0.315339  0.461855 0.44656  0.0567985   -0.0202333  -0.0465387  90  LYS   A CE   
727  N  NZ   . LYS   A 90  ? 0.358724  0.509215 0.480472 0.0649808   -0.0245505  -0.0270024  90  LYS   A NZ   
728  N  N    . VAL   A 91  ? 0.0850975 0.317359 0.296542 0.0307525   0.00801875  -0.0711867  91  VAL   A N    
729  C  CA   . VAL   A 91  ? 0.0999437 0.324595 0.303821 0.0298007   0.00697706  -0.0765969  91  VAL   A CA   
730  C  C    . VAL   A 91  ? 0.110978  0.344526 0.321122 0.0295212   0.0125532   -0.0986271  91  VAL   A C    
731  O  O    . VAL   A 91  ? 0.126318  0.344551 0.32357  0.0409135   0.0236779   -0.108527   91  VAL   A O    
732  C  CB   . VAL   A 91  ? 0.110467  0.320428 0.296257 0.0287369   0.00294063  -0.0768544  91  VAL   A CB   
733  C  CG1  . VAL   A 91  ? 0.11362   0.31756  0.289814 0.0301743   -0.00846459 -0.0681505  91  VAL   A CG1  
734  C  CG2  . VAL   A 91  ? 0.117463  0.319026 0.301982 0.0289314   -0.00544908 -0.076456   91  VAL   A CG2  
735  N  N    . ASP   A 92  ? 0.141922  0.388185 0.324484 0.0221858   0.0187399   -0.115569   92  ASP   A N    
736  C  CA   . ASP   A 92  ? 0.140191  0.439526 0.345551 0.0235921   0.0350698   -0.144525   92  ASP   A CA   
737  C  C    . ASP   A 92  ? 0.155772  0.448625 0.359927 0.039643    0.0222817   -0.15863    92  ASP   A C    
738  O  O    . ASP   A 92  ? 0.202875  0.468575 0.410239 0.0611872   0.0189803   -0.185723   92  ASP   A O    
739  C  CB   . ASP   A 92  ? 0.174271  0.487558 0.371512 -0.00746751 0.0571987   -0.151936   92  ASP   A CB   
740  C  CG   . ASP   A 92  ? 0.260951  0.566444 0.404227 -0.0233644  0.0555437   -0.139577   92  ASP   A CG   
741  O  OD1  . ASP   A 92  ? 0.306047  0.637854 0.444433 -0.0355001  0.0341734   -0.139476   92  ASP   A OD1  
742  O  OD2  . ASP   A 92  ? 0.346151  0.650636 0.477665 -0.0680852  0.0944703   -0.110769   92  ASP   A OD2  
743  N  N    . THR   A 93  ? 0.147842  0.430972 0.336975 0.0391908   0.0181325   -0.153413   93  THR   A N    
744  C  CA   . THR   A 93  ? 0.16046   0.433497 0.309942 0.0395163   0.0160136   -0.13389    93  THR   A CA   
745  C  C    . THR   A 93  ? 0.141129  0.388123 0.313223 0.0503083   0.00655054  -0.131279   93  THR   A C    
746  O  O    . THR   A 93  ? 0.158567  0.407943 0.317087 0.0444284   0.0111597   -0.148791   93  THR   A O    
747  C  CB   . THR   A 93  ? 0.187615  0.46944  0.327509 0.0215567   0.0317435   -0.105184   93  THR   A CB   
748  O  OG1  . THR   A 93  ? 0.225576  0.523538 0.343045 -0.0209637  0.0326231   -0.0730263  93  THR   A OG1  
749  C  CG2  . THR   A 93  ? 0.18877   0.480313 0.339048 0.0178764   0.0306035   -0.0898713  93  THR   A CG2  
750  N  N    . ALA   A 94  ? 0.138323  0.356905 0.301245 0.0603407   0.00669178  -0.11977    94  ALA   A N    
751  C  CA   . ALA   A 94  ? 0.144376  0.336344 0.2926   0.0622564   0.0018577   -0.0928025  94  ALA   A CA   
752  C  C    . ALA   A 94  ? 0.163634  0.321217 0.277381 0.0609229   0.00717746  -0.0761981  94  ALA   A C    
753  O  O    . ALA   A 94  ? 0.190052  0.340968 0.27737  0.0858978   -0.00311292 -0.0733641  94  ALA   A O    
754  C  CB   . ALA   A 94  ? 0.178035  0.352894 0.304459 0.0548585   -0.0021299  -0.0831664  94  ALA   A CB   
755  N  N    . ASN   A 95  ? 0.143103  0.280372 0.257565 0.0568675   -0.00244702 -0.0530412  95  ASN   A N    
756  C  CA   . ASN   A 95  ? 0.135265  0.264307 0.242312 0.0498301   0.00100411  -0.0522118  95  ASN   A CA   
757  C  C    . ASN   A 95  ? 0.142832  0.256176 0.24892  0.046082    0.00565841  -0.0501052  95  ASN   A C    
758  O  O    . ASN   A 95  ? 0.147748  0.255261 0.256064 0.0285305   0.00449701  -0.0538266  95  ASN   A O    
759  C  CB   . ASN   A 95  ? 0.144321  0.244928 0.226824 0.054162    -0.00389321 -0.0472418  95  ASN   A CB   
760  C  CG   . ASN   A 95  ? 0.139646  0.257553 0.228131 0.0502185   -0.0145057  -0.0499563  95  ASN   A CG   
761  O  OD1  . ASN   A 95  ? 0.165567  0.271223 0.233946 0.0561619   -0.0102291  -0.0468775  95  ASN   A OD1  
762  N  ND2  . ASN   A 95  ? 0.150044  0.263152 0.222029 0.0648679   -0.0225319  -0.047954   95  ASN   A ND2  
763  N  N    . PRO   A 96  ? 0.147456  0.284298 0.251024 0.0436372   0.00230679  -0.0534329  96  PRO   A N    
764  C  CA   . PRO   A 96  ? 0.166378  0.298384 0.249695 0.0404457   -0.00264134 -0.0543318  96  PRO   A CA   
765  C  C    . PRO   A 96  ? 0.163835  0.289172 0.258593 0.0418438   -0.0114955  -0.0605832  96  PRO   A C    
766  O  O    . PRO   A 96  ? 0.189757  0.31056  0.308358 0.0109411   -0.0136936  -0.069508   96  PRO   A O    
767  C  CB   . PRO   A 96  ? 0.180863  0.320627 0.258551 0.0422334   0.00699371  -0.0593725  96  PRO   A CB   
768  C  CG   . PRO   A 96  ? 0.191742  0.331079 0.26161  0.034876    0.00289075  -0.0497737  96  PRO   A CG   
769  C  CD   . PRO   A 96  ? 0.157424  0.304503 0.24847  0.0413037   0.00817853  -0.0540682  96  PRO   A CD   
770  N  N    . LYS   A 97  ? 0.153533  0.289111 0.237945 0.0494796   -0.00039555 -0.0581193  97  LYS   A N    
771  C  CA   . LYS   A 97  ? 0.163755  0.296304 0.239054 0.0607204   -0.00174533 -0.0495599  97  LYS   A CA   
772  C  C    . LYS   A 97  ? 0.15205   0.267664 0.239688 0.0558643   0.00075221  -0.0497303  97  LYS   A C    
773  O  O    . LYS   A 97  ? 0.160067  0.276502 0.247331 0.0618358   0.0220484   -0.0314656  97  LYS   A O    
774  C  CB   . LYS   A 97  ? 0.19522   0.318457 0.249435 0.0755624   0.00402667  -0.0360025  97  LYS   A CB   
775  C  CG   . LYS   A 97  ? 0.233752  0.360016 0.265447 0.0735812   0.013393    -0.0246631  97  LYS   A CG   
776  C  CD   . LYS   A 97  ? 0.28233   0.386515 0.295121 0.0897942   0.025241    -0.0123529  97  LYS   A CD   
777  C  CE   . LYS   A 97  ? 0.352766  0.434824 0.322357 0.0819958   0.0245312   0.00631591  97  LYS   A CE   
778  N  NZ   . LYS   A 97  ? 0.40875   0.465133 0.375153 0.0834718   0.0174906   0.0143489   97  LYS   A NZ   
779  N  N    . THR   A 98  ? 0.147304  0.256376 0.239354 0.054918    0.00754638  -0.0547377  98  THR   A N    
780  C  CA   . THR   A 98  ? 0.141058  0.253464 0.249451 0.0384961   0.00094939  -0.048458   98  THR   A CA   
781  C  C    . THR   A 98  ? 0.138453  0.243935 0.252835 0.0426118   -0.00525524 -0.044078   98  THR   A C    
782  O  O    . THR   A 98  ? 0.148959  0.258336 0.276154 0.0407126   -0.0157249  -0.0512869  98  THR   A O    
783  C  CB   . THR   A 98  ? 0.12673   0.266002 0.262737 0.0371973   -0.00504613 -0.0509404  98  THR   A CB   
784  O  OG1  . THR   A 98  ? 0.120826  0.272133 0.255082 0.0298704   -0.00321685 -0.045399   98  THR   A OG1  
785  C  CG2  . THR   A 98  ? 0.119101  0.276724 0.269102 0.0322252   -0.00582434 -0.0483557  98  THR   A CG2  
786  N  N    . PRO   A 99  ? 0.128393  0.232906 0.249306 0.0312827   -0.00633652 -0.0340297  99  PRO   A N    
787  C  CA   . PRO   A 99  ? 0.132074  0.23055  0.256156 0.0186755   -0.00758991 -0.0310146  99  PRO   A CA   
788  C  C    . PRO   A 99  ? 0.128564  0.231794 0.262036 0.00921633  -0.00918754 -0.0265338  99  PRO   A C    
789  O  O    . PRO   A 99  ? 0.133903  0.263353 0.266639 0.00381805  -0.00980391 -0.0197663  99  PRO   A O    
790  C  CB   . PRO   A 99  ? 0.136531  0.236219 0.254996 0.0278873   -0.0123442  -0.025807   99  PRO   A CB   
791  C  CG   . PRO   A 99  ? 0.131235  0.234543 0.246582 0.0338732   -0.0110767  -0.0310076  99  PRO   A CG   
792  C  CD   . PRO   A 99  ? 0.139295  0.237453 0.241772 0.0343689   -0.00886036 -0.0335493  99  PRO   A CD   
793  N  N    . LYS   A 100 ? 0.139     0.241996 0.27725  0.00323807  -0.00173014 -0.035375   100 LYS   A N    
794  C  CA   . LYS   A 100 ? 0.164697  0.24146  0.298032 0.0116068   -0.00035601 -0.0251114  100 LYS   A CA   
795  C  C    . LYS   A 100 ? 0.156645  0.218234 0.289837 0.0233417   0.00081209  -0.0188781  100 LYS   A C    
796  O  O    . LYS   A 100 ? 0.171345  0.221239 0.277336 0.0363682   -0.00964326 -0.0162807  100 LYS   A O    
797  C  CB   . LYS   A 100 ? 0.186354  0.281865 0.339701 -0.00609107 0.00378032  -0.0279143  100 LYS   A CB   
798  C  CG   . LYS   A 100 ? 0.249079  0.335576 0.377395 -0.0058263  0.00686009  -0.0434958  100 LYS   A CG   
799  C  CD   . LYS   A 100 ? 0.291128  0.379719 0.42702  -0.0320193  -0.00065095 -0.0500639  100 LYS   A CD   
800  C  CE   . LYS   A 100 ? 0.357118  0.425644 0.459438 -0.0327076  0.00103127  -0.060892   100 LYS   A CE   
801  N  NZ   . LYS   A 100 ? 0.374485  0.479239 0.480636 -0.0436832  -0.0054022  -0.0592525  100 LYS   A NZ   
802  N  N    . TYR   A 101 ? 0.155465  0.207731 0.271181 0.0319708   0.0021408   -0.0198555  101 TYR   A N    
803  C  CA   . TYR   A 101 ? 0.154569  0.201502 0.26547  0.0295549   -0.00554213 -0.0101159  101 TYR   A CA   
804  C  C    . TYR   A 101 ? 0.154817  0.206388 0.267955 0.0339026   -0.00234689 -0.00093031 101 TYR   A C    
805  O  O    . TYR   A 101 ? 0.203061  0.207809 0.27373  0.040775    -0.00189763 0.00287662  101 TYR   A O    
806  C  CB   . TYR   A 101 ? 0.157475  0.214057 0.268205 0.0231385   -0.00257744 -0.0109431  101 TYR   A CB   
807  C  CG   . TYR   A 101 ? 0.164406  0.218309 0.276325 0.0206171   -0.0156643  -0.0123141  101 TYR   A CG   
808  C  CD1  . TYR   A 101 ? 0.16403   0.237058 0.278561 0.0298161   -0.0177496  -0.0121866  101 TYR   A CD1  
809  C  CD2  . TYR   A 101 ? 0.18191   0.233156 0.281289 0.0116347   -0.0230651  -0.0177765  101 TYR   A CD2  
810  C  CE1  . TYR   A 101 ? 0.16829   0.247585 0.314223 0.0295613   -0.0277933  -0.0091731  101 TYR   A CE1  
811  C  CE2  . TYR   A 101 ? 0.192571  0.244589 0.293639 0.023505    -0.043258   -0.0144156  101 TYR   A CE2  
812  C  CZ   . TYR   A 101 ? 0.162391  0.251245 0.320707 0.0348903   -0.0387879  -0.00606377 101 TYR   A CZ   
813  O  OH   . TYR   A 101 ? 0.16436   0.289075 0.398944 0.0476353   -0.0398214  -2.681e-05  101 TYR   A OH   
814  N  N    . LYS   A 102 ? 0.149573  0.198162 0.266636 0.03481     -0.00694423 0.0111068   102 LYS   A N    
815  C  CA   . LYS   A 102 ? 0.154509  0.209599 0.264437 0.0264303   -0.00787109 0.0227165   102 LYS   A CA   
816  C  C    . LYS   A 102 ? 0.148317  0.206456 0.25598  0.0318761   -0.0108264  0.0275359   102 LYS   A C    
817  O  O    . LYS   A 102 ? 0.13581   0.202175 0.253335 0.0337172   -0.0191661  0.021044    102 LYS   A O    
818  C  CB   . LYS   A 102 ? 0.21639   0.255529 0.284761 -0.0121286  -0.00837159 0.0297575   102 LYS   A CB   
819  C  CG   . LYS   A 102 ? 0.23348   0.291928 0.320527 -0.0194434  -0.011084   0.0362551   102 LYS   A CG   
820  C  CD   . LYS   A 102 ? 0.299751  0.337328 0.351258 -0.0382782  0.0015485   0.0536437   102 LYS   A CD   
821  C  CE   . LYS   A 102 ? 0.336058  0.34381  0.374128 -0.0551626  -0.00751814 0.0550421   102 LYS   A CE   
822  N  NZ   . LYS   A 102 ? 0.350546  0.37202  0.401385 -0.0675374  -0.00185777 0.055416    102 LYS   A NZ   
823  N  N    . PHE   A 103 ? 0.123163  0.208588 0.255348 0.0359485   -0.00962589 0.0376589   103 PHE   A N    
824  C  CA   . PHE   A 103 ? 0.137096  0.211335 0.249284 0.0342371   -0.0153462  0.0403085   103 PHE   A CA   
825  C  C    . PHE   A 103 ? 0.151969  0.218975 0.249367 0.0314491   -0.0126235  0.0475403   103 PHE   A C    
826  O  O    . PHE   A 103 ? 0.183288  0.221105 0.275749 0.0463923   -0.00381395 0.0539049   103 PHE   A O    
827  C  CB   . PHE   A 103 ? 0.136064  0.219238 0.25236  0.037594    -0.0192195  0.03278     103 PHE   A CB   
828  C  CG   . PHE   A 103 ? 0.116369  0.222118 0.250696 0.0455747   -0.0188241  0.0273007   103 PHE   A CG   
829  C  CD1  . PHE   A 103 ? 0.124796  0.227092 0.250385 0.042983    -0.00528642 0.0268019   103 PHE   A CD1  
830  C  CD2  . PHE   A 103 ? 0.117834  0.247461 0.268567 0.0473428   -0.0175613  0.0247416   103 PHE   A CD2  
831  C  CE1  . PHE   A 103 ? 0.120309  0.232739 0.257245 0.0508871   0.00087253  0.0220036   103 PHE   A CE1  
832  C  CE2  . PHE   A 103 ? 0.116418  0.26033  0.268837 0.0476615   -0.0100456  0.0222258   103 PHE   A CE2  
833  C  CZ   . PHE   A 103 ? 0.124953  0.25053  0.269025 0.0504598   -0.0059656  0.0210151   103 PHE   A CZ   
834  N  N    . VAL   A 104 ? 0.15496   0.213077 0.235255 0.0270218   -0.0106488  0.0625511   104 VAL   A N    
835  C  CA   . VAL   A 104 ? 0.160158  0.23562  0.257256 0.0338155   -0.00560992 0.0671688   104 VAL   A CA   
836  C  C    . VAL   A 104 ? 0.151596  0.232969 0.241363 0.0333      0.00483747  0.0691616   104 VAL   A C    
837  O  O    . VAL   A 104 ? 0.228204  0.221678 0.238919 0.0301294   0.0119916   0.0620045   104 VAL   A O    
838  C  CB   . VAL   A 104 ? 0.168746  0.273713 0.277507 0.0278788   -0.0130082  0.0676115   104 VAL   A CB   
839  C  CG1  . VAL   A 104 ? 0.186299  0.308578 0.290436 0.0213074   -0.00558115 0.065446    104 VAL   A CG1  
840  C  CG2  . VAL   A 104 ? 0.191097  0.289955 0.303708 0.0373103   -0.0171064  0.0613177   104 VAL   A CG2  
841  N  N    . ARG   A 105 ? 0.124415  0.241471 0.247526 0.0466384   0.00428704  0.0807749   105 ARG   A N    
842  C  CA   . ARG   A 105 ? 0.12434   0.263011 0.248545 0.0272177   0.0120573   0.073247    105 ARG   A CA   
843  C  C    . ARG   A 105 ? 0.125819  0.248795 0.249268 0.0272834   0.0204117   0.0728133   105 ARG   A C    
844  O  O    . ARG   A 105 ? 0.165702  0.2827   0.311594 0.0313369   0.047654    0.102674    105 ARG   A O    
845  C  CB   . ARG   A 105 ? 0.139149  0.296725 0.248449 0.0331865   0.0155486   0.0753044   105 ARG   A CB   
846  C  CG   . ARG   A 105 ? 0.131911  0.31501  0.252097 0.0181601   0.018434    0.0717878   105 ARG   A CG   
847  C  CD   . ARG   A 105 ? 0.149252  0.320505 0.243243 0.014411    0.0197897   0.0833188   105 ARG   A CD   
848  N  NE   . ARG   A 105 ? 0.159794  0.338018 0.231488 0.0151933   0.0204721   0.0880482   105 ARG   A NE   
849  C  CZ   . ARG   A 105 ? 0.159068  0.345343 0.231585 0.0195696   0.0025886   0.10043     105 ARG   A CZ   
850  N  NH1  . ARG   A 105 ? 0.145679  0.365184 0.238939 0.0232268   0.00650282  0.104898    105 ARG   A NH1  
851  N  NH2  . ARG   A 105 ? 0.174308  0.347864 0.244012 0.0105162   -0.00363491 0.0959811   105 ARG   A NH2  
852  N  N    . ILE   A 106 ? 0.112616  0.224834 0.223832 0.0136371   0.0218712   0.0488357   106 ILE   A N    
853  C  CA   . ILE   A 106 ? 0.106845  0.219966 0.208929 0.00835662  0.00639664  0.0409211   106 ILE   A CA   
854  C  C    . ILE   A 106 ? 0.122344  0.224463 0.203341 0.00301292  0.00395077  0.0397236   106 ILE   A C    
855  O  O    . ILE   A 106 ? 0.127124  0.253584 0.204227 -0.00169529 0.00164138  0.0383319   106 ILE   A O    
856  C  CB   . ILE   A 106 ? 0.104404  0.224245 0.204824 0.0172487   0.00449225  0.0365164   106 ILE   A CB   
857  C  CG1  . ILE   A 106 ? 0.12291   0.234529 0.216925 0.0146902   0.00507474  0.0388442   106 ILE   A CG1  
858  C  CG2  . ILE   A 106 ? 0.128725  0.229966 0.210292 0.00428321  0.00356705  0.0329642   106 ILE   A CG2  
859  C  CD1  . ILE   A 106 ? 0.134508  0.238511 0.223033 0.0185199   0.00486768  0.0365168   106 ILE   A CD1  
860  N  N    . GLN   A 107 ? 0.123417  0.223202 0.187618 0.0074552   0.00284701  0.0218722   107 GLN   A N    
861  C  CA   . GLN   A 107 ? 0.13356   0.234325 0.196751 0.0118246   0.0136865   0.0182875   107 GLN   A CA   
862  C  C    . GLN   A 107 ? 0.142062  0.232183 0.188545 0.0153687   0.0216309   0.027153    107 GLN   A C    
863  O  O    . GLN   A 107 ? 0.159272  0.253766 0.1812   0.0410353   0.0267436   0.0290139   107 GLN   A O    
864  C  CB   . GLN   A 107 ? 0.177291  0.256136 0.200941 0.0131614   0.0363322   0.0272391   107 GLN   A CB   
865  C  CG   . GLN   A 107 ? 0.239771  0.273449 0.215096 0.031081    0.0460993   0.0294972   107 GLN   A CG   
866  C  CD   . GLN   A 107 ? 0.278076  0.330052 0.251761 0.0610992   0.0212712   0.0332971   107 GLN   A CD   
867  O  OE1  . GLN   A 107 ? 0.369026  0.373803 0.255961 0.0863227   -0.025806   0.0315644   107 GLN   A OE1  
868  N  NE2  . GLN   A 107 ? 0.299692  0.383643 0.283119 0.078273    0.0158025   0.0327999   107 GLN   A NE2  
869  N  N    . PRO   A 108 ? 0.161419  0.239711 0.195779 0.0218284   0.026062    0.0250032   108 PRO   A N    
870  C  CA   . PRO   A 108 ? 0.18603   0.240524 0.21622  0.0283538   0.0336186   0.0203102   108 PRO   A CA   
871  C  C    . PRO   A 108 ? 0.168937  0.232296 0.212866 0.025901    0.0493014   0.0350748   108 PRO   A C    
872  O  O    . PRO   A 108 ? 0.187147  0.247691 0.227789 0.0149601   0.0647177   0.0440357   108 PRO   A O    
873  C  CB   . PRO   A 108 ? 0.223873  0.259269 0.223864 0.0206404   0.0305772   0.0131782   108 PRO   A CB   
874  C  CG   . PRO   A 108 ? 0.228453  0.289204 0.253247 0.0252519   0.0148587   0.00146491  108 PRO   A CG   
875  C  CD   . PRO   A 108 ? 0.175985  0.267554 0.217088 0.0228824   0.0113136   0.00931775  108 PRO   A CD   
876  N  N    . GLY   A 109 ? 0.144713  0.232407 0.207479 0.0279137   0.051333    0.0396587   109 GLY   A N    
877  C  CA   . GLY   A 109 ? 0.141211  0.244815 0.233044 0.02195     0.0449174   0.0416199   109 GLY   A CA   
878  C  C    . GLY   A 109 ? 0.115685  0.232235 0.227307 0.0278754   0.0281424   0.0448614   109 GLY   A C    
879  O  O    . GLY   A 109 ? 0.0949695 0.269958 0.246661 0.0274354   0.0141999   0.0205639   109 GLY   A O    
880  N  N    . GLN   A 110 ? 0.11072   0.216252 0.209637 0.0255679   0.0164766   0.0394229   110 GLN   A N    
881  C  CA   . GLN   A 110 ? 0.0990121 0.205234 0.206244 0.0129361   0.00790729  0.0361211   110 GLN   A CA   
882  C  C    . GLN   A 110 ? 0.0902365 0.19529  0.19938  0.0149898   0.00930191  0.0269963   110 GLN   A C    
883  O  O    . GLN   A 110 ? 0.111695  0.203675 0.18948  0.00881777  -5.263e-05  0.0312821   110 GLN   A O    
884  C  CB   . GLN   A 110 ? 0.101709  0.193556 0.202286 0.010829    0.00056513  0.0361511   110 GLN   A CB   
885  C  CG   . GLN   A 110 ? 0.114766  0.194725 0.211426 0.00935057  -0.00736005 0.0317392   110 GLN   A CG   
886  C  CD   . GLN   A 110 ? 0.130153  0.198675 0.218439 0.00140933  -0.0101311  0.031907    110 GLN   A CD   
887  O  OE1  . GLN   A 110 ? 0.145034  0.207328 0.246909 0.00804838  -0.0238961  0.0391068   110 GLN   A OE1  
888  N  NE2  . GLN   A 110 ? 0.142784  0.206846 0.22718  -0.00806017 -0.018558   0.035777    110 GLN   A NE2  
889  N  N    . THR   A 111 ? 0.095798  0.190312 0.186867 0.00880291  0.00896863  0.0295668   111 THR   A N    
890  C  CA   . THR   A 111 ? 0.103227  0.184603 0.180753 0.0199899   0.010855    0.0256403   111 THR   A CA   
891  C  C    . THR   A 111 ? 0.110049  0.176436 0.171593 0.0144006   0.0147288   0.027919    111 THR   A C    
892  O  O    . THR   A 111 ? 0.105013  0.187294 0.201746 0.0127837   0.0247882   0.0314681   111 THR   A O    
893  C  CB   . THR   A 111 ? 0.105247  0.190888 0.194494 0.0231078   0.00864504  0.0212391   111 THR   A CB   
894  O  OG1  . THR   A 111 ? 0.110823  0.20457  0.192285 0.0188893   0.00941601  0.0149846   111 THR   A OG1  
895  C  CG2  . THR   A 111 ? 0.106539  0.197665 0.201904 0.0258518   0.00331337  0.0177817   111 THR   A CG2  
896  N  N    . PHE   A 112 ? 0.101225  0.175496 0.167003 0.0151562   0.0158619   0.0235873   112 PHE   A N    
897  C  CA   . PHE   A 112 ? 0.0938765 0.170614 0.164881 0.0146084   0.00740323  0.0170357   112 PHE   A CA   
898  C  C    . PHE   A 112 ? 0.0938368 0.164119 0.160523 0.00889303  0.00221837  0.00971901  112 PHE   A C    
899  O  O    . PHE   A 112 ? 0.103027  0.166954 0.158866 0.0118172   0.00921535  0.0123073   112 PHE   A O    
900  C  CB   . PHE   A 112 ? 0.093836  0.182617 0.169741 0.0114012   0.00824152  0.0197966   112 PHE   A CB   
901  C  CG   . PHE   A 112 ? 0.114209  0.200532 0.172786 0.00541531  0.00376385  0.0180673   112 PHE   A CG   
902  C  CD1  . PHE   A 112 ? 0.137173  0.230136 0.178638 -0.0124347  0.00285939  0.0133168   112 PHE   A CD1  
903  C  CD2  . PHE   A 112 ? 0.124641  0.203492 0.1746   -0.00623006 0.00088178  0.0138378   112 PHE   A CD2  
904  C  CE1  . PHE   A 112 ? 0.182455  0.237609 0.185702 -0.0178289  0.00635449  0.00425824  112 PHE   A CE1  
905  C  CE2  . PHE   A 112 ? 0.159413  0.217427 0.186586 -0.0186069  -0.00298741 0.011893    112 PHE   A CE2  
906  C  CZ   . PHE   A 112 ? 0.17843   0.235412 0.19624  -0.0216843  0.00050869  0.00360637  112 PHE   A CZ   
907  N  N    . SER   A 113 ? 0.0965533 0.15976  0.156544 0.00872877  0.00342093  0.0116624   113 SER   A N    
908  C  CA   . SER   A 113 ? 0.0996969 0.158009 0.164026 0.00515875  -0.002538   0.0112419   113 SER   A CA   
909  C  C    . SER   A 113 ? 0.0980721 0.159044 0.170671 0.0104464   -0.00440687 0.0136284   113 SER   A C    
910  O  O    . SER   A 113 ? 0.104585  0.159948 0.210662 0.0106537   -0.0193206  0.0165681   113 SER   A O    
911  C  CB   . SER   A 113 ? 0.109802  0.171042 0.162463 -0.00054739 -0.0038368  0.00865404  113 SER   A CB   
912  O  OG   . SER   A 113 ? 0.114161  0.198793 0.164604 -0.0094455  -0.0156815  0.00159143  113 SER   A OG   
913  N  N    . VAL   A 114 ? 0.0842999 0.159837 0.168201 0.0122373   -0.00626597 0.018487    114 VAL   A N    
914  C  CA   . VAL   A 114 ? 0.0896022 0.162909 0.16793  0.0100311   -0.00391264 0.014035    114 VAL   A CA   
915  C  C    . VAL   A 114 ? 0.0875403 0.168391 0.16207  0.0161991   -0.00568011 0.0104352   114 VAL   A C    
916  O  O    . VAL   A 114 ? 0.0848106 0.183369 0.165396 0.0151335   -0.00386128 0.0196277   114 VAL   A O    
917  C  CB   . VAL   A 114 ? 0.12012   0.178559 0.178238 0.00773091  -0.00818589 0.00350736  114 VAL   A CB   
918  C  CG1  . VAL   A 114 ? 0.125963  0.18129  0.185809 0.00601475  -0.013367   0.00131783  114 VAL   A CG1  
919  C  CG2  . VAL   A 114 ? 0.148794  0.194111 0.186399 0.00610113  -0.00863471 0.00330734  114 VAL   A CG2  
920  N  N    . LEU   A 115 ? 0.0880971 0.180996 0.165234 0.0166254   -0.00539993 0.00557797  115 LEU   A N    
921  C  CA   . LEU   A 115 ? 0.0937791 0.183718 0.159509 0.0143862   -0.00648049 0.00417191  115 LEU   A CA   
922  C  C    . LEU   A 115 ? 0.0919601 0.185558 0.14781  0.0133653   -0.00514762 0.00410082  115 LEU   A C    
923  O  O    . LEU   A 115 ? 0.10059   0.197133 0.156592 0.0227308   -0.0130384  -0.00208244 115 LEU   A O    
924  C  CB   . LEU   A 115 ? 0.106155  0.186708 0.164864 0.0117251   -0.00634668 -0.00160365 115 LEU   A CB   
925  C  CG   . LEU   A 115 ? 0.117678  0.196121 0.166463 0.0174376   -0.00499829 -0.00314583 115 LEU   A CG   
926  C  CD1  . LEU   A 115 ? 0.128837  0.203374 0.161277 0.0203704   -0.00931878 -0.00827546 115 LEU   A CD1  
927  C  CD2  . LEU   A 115 ? 0.128556  0.206701 0.169385 0.022956    -0.00178008 -0.00401748 115 LEU   A CD2  
928  N  N    . ALA   A 116 ? 0.0991052 0.189985 0.151306 0.00464945  0.00137293  0.00740721  116 ALA   A N    
929  C  CA   . ALA   A 116 ? 0.111078  0.19787  0.156564 0.0007877   0.0045413   0.00608381  116 ALA   A CA   
930  C  C    . ALA   A 116 ? 0.110939  0.221774 0.152113 -0.00285983 0.00249025  0.01296     116 ALA   A C    
931  O  O    . ALA   A 116 ? 0.109721  0.281282 0.151017 -0.00804547 0.00315964  0.0185707   116 ALA   A O    
932  C  CB   . ALA   A 116 ? 0.135052  0.196493 0.196276 -0.00270195 0.00553407  0.00128513  116 ALA   A CB   
933  N  N    . CYS   A 117 ? 0.10904   0.223444 0.149148 -0.00490893 0.00189807  0.00603234  117 CYS   A N    
934  C  CA   A CYS   A 117 ? 0.102037  0.212967 0.153318 -0.00345377 0.00295562  0.00465168  117 CYS   A CA   
935  C  CA   B CYS   A 117 ? 0.114589  0.239357 0.172701 -0.00944646 0.00606731  0.00877384  117 CYS   A CA   
936  C  C    . CYS   A 117 ? 0.105522  0.227217 0.162587 -0.00253197 -0.00217484 0.00704911  117 CYS   A C    
937  O  O    . CYS   A 117 ? 0.105182  0.230594 0.159837 -0.00343494 0.00336942  0.0179263   117 CYS   A O    
938  C  CB   A CYS   A 117 ? 0.0932145 0.199254 0.143614 -0.00706929 0.00325662  -0.0048944  117 CYS   A CB   
939  C  CB   B CYS   A 117 ? 0.143106  0.255215 0.213504 -0.00679425 0.00095653  0.0121502   117 CYS   A CB   
940  S  SG   A CYS   A 117 ? 0.0785829 0.184725 0.14646  -0.00467857 0.00688321  -0.0108582  117 CYS   A SG   
941  S  SG   B CYS   A 117 ? 0.214383  0.323994 0.267815 -0.00437237 0.0214827   -0.00312835 117 CYS   A SG   
942  N  N    . TYR   A 118 ? 0.105752  0.235922 0.160313 -0.00212326 -0.0006543  0.0105599   118 TYR   A N    
943  C  CA   . TYR   A 118 ? 0.112139  0.241184 0.172434 -0.00558165 0.00550088  0.0118075   118 TYR   A CA   
944  C  C    . TYR   A 118 ? 0.117576  0.272959 0.177021 -0.00217971 0.011652    0.0117034   118 TYR   A C    
945  O  O    . TYR   A 118 ? 0.123958  0.283023 0.177071 -0.00758228 0.0172141   0.0103301   118 TYR   A O    
946  C  CB   . TYR   A 118 ? 0.124652  0.23907  0.179186 -0.00587225 0.00230419  0.0129079   118 TYR   A CB   
947  C  CG   . TYR   A 118 ? 0.127368  0.228    0.181329 -0.00653587 -0.0032459  0.010098    118 TYR   A CG   
948  C  CD1  . TYR   A 118 ? 0.129684  0.216442 0.184518 -0.0132619  -0.0103957  0.00681324  118 TYR   A CD1  
949  C  CD2  . TYR   A 118 ? 0.130037  0.232771 0.183819 -0.00697873 -0.0123038  0.00611994  118 TYR   A CD2  
950  C  CE1  . TYR   A 118 ? 0.136425  0.215492 0.179371 -0.00586691 -0.011656   0.00257323  118 TYR   A CE1  
951  C  CE2  . TYR   A 118 ? 0.131642  0.227271 0.175398 -0.0060271  -0.0101794  5.04e-05    118 TYR   A CE2  
952  C  CZ   . TYR   A 118 ? 0.134856  0.225129 0.16928  -0.0027501  -0.00500707 0.00388071  118 TYR   A CZ   
953  O  OH   . TYR   A 118 ? 0.135779  0.235657 0.169624 0.0046831   -0.00318337 -0.00141127 118 TYR   A OH   
954  N  N    . ASN   A 119 ? 0.120767  0.29764  0.184516 -0.00186964 0.00878645  0.00352599  119 ASN   A N    
955  C  CA   . ASN   A 119 ? 0.127527  0.319882 0.200281 -0.00629624 0.027894    0.0135911   119 ASN   A CA   
956  C  C    . ASN   A 119 ? 0.120672  0.322371 0.193403 -0.00141643 0.0256153   0.0134671   119 ASN   A C    
957  O  O    . ASN   A 119 ? 0.152987  0.354692 0.200999 -0.00351656 0.0403767   0.00984284  119 ASN   A O    
958  C  CB   . ASN   A 119 ? 0.155945  0.341576 0.233624 -0.0255501  0.0283642   0.0214419   119 ASN   A CB   
959  C  CG   . ASN   A 119 ? 0.19522   0.360397 0.276844 -0.0323923  0.0166114   0.019548    119 ASN   A CG   
960  O  OD1  . ASN   A 119 ? 0.264223  0.375151 0.337554 -0.0203604  0.0110359   0.0200451   119 ASN   A OD1  
961  N  ND2  . ASN   A 119 ? 0.227187  0.396295 0.319214 -0.0442275  -0.0147259  0.0217604   119 ASN   A ND2  
962  N  N    . GLY   A 120 ? 0.120266  0.308691 0.177243 0.00895802  0.0301311   0.0100936   120 GLY   A N    
963  C  CA   . GLY   A 120 ? 0.13836   0.308787 0.185279 0.0167054   0.0288385   0.0020257   120 GLY   A CA   
964  C  C    . GLY   A 120 ? 0.148835  0.301347 0.188853 0.00541231  0.0243325   -0.00474601 120 GLY   A C    
965  O  O    . GLY   A 120 ? 0.185614  0.313986 0.209762 0.0132562   0.0196208   -0.0245282  120 GLY   A O    
966  N  N    . SER   A 121 ? 0.136578  0.310054 0.183077 -0.00246589 0.014136    0.00176113  121 SER   A N    
967  C  CA   . SER   A 121 ? 0.154753  0.338957 0.187459 -0.0104726  0.0118027   -0.00559432 121 SER   A CA   
968  C  C    . SER   A 121 ? 0.153404  0.3338   0.186881 -0.0223084  0.0122146   -0.00030702 121 SER   A C    
969  O  O    . SER   A 121 ? 0.126311  0.309188 0.198007 -0.0220689  0.0184652   -0.00206975 121 SER   A O    
970  C  CB   . SER   A 121 ? 0.176234  0.365929 0.207255 -0.0130426  0.0195695   0.0127026   121 SER   A CB   
971  O  OG   . SER   A 121 ? 0.189391  0.441758 0.257829 -0.0092662  0.0275226   0.00031714  121 SER   A OG   
972  N  N    . PRO   A 122 ? 0.158007  0.372563 0.198355 -0.0388519  0.0155113   -0.0195416  122 PRO   A N    
973  C  CA   . PRO   A 122 ? 0.15188   0.386683 0.192047 -0.0422598  0.0114292   -0.00792518 122 PRO   A CA   
974  C  C    . PRO   A 122 ? 0.153074  0.389496 0.178489 -0.0464395  -0.00166025 0.0250104   122 PRO   A C    
975  O  O    . PRO   A 122 ? 0.155808  0.440524 0.186834 -0.0578054  0.00493888  0.0475606   122 PRO   A O    
976  C  CB   . PRO   A 122 ? 0.168966  0.402087 0.236176 -0.0553401  0.0150535   -0.0168012  122 PRO   A CB   
977  C  CG   . PRO   A 122 ? 0.226086  0.410422 0.275533 -0.0523094  0.0173096   -0.0198919  122 PRO   A CG   
978  C  CD   . PRO   A 122 ? 0.182006  0.400476 0.250113 -0.0434195  0.0282564   -0.0411386  122 PRO   A CD   
979  N  N    . SER   A 123 ? 0.132357  0.360726 0.169379 -0.0294047  -0.00774384 0.0450637   123 SER   A N    
980  C  CA   . SER   A 123 ? 0.15327   0.342648 0.196718 -0.0313294  -0.00570162 0.0547578   123 SER   A CA   
981  C  C    . SER   A 123 ? 0.147781  0.277364 0.178398 -0.0178254  -0.0154221  0.0506504   123 SER   A C    
982  O  O    . SER   A 123 ? 0.157515  0.294781 0.192972 -0.0280835  -0.0392031  0.0550586   123 SER   A O    
983  C  CB   . SER   A 123 ? 0.188503  0.366564 0.24601  -0.0278107  -0.00924058 0.0411177   123 SER   A CB   
984  O  OG   . SER   A 123 ? 0.256831  0.398512 0.290408 -0.0313813  -0.00168798 0.0502301   123 SER   A OG   
985  N  N    . GLY   A 124 ? 0.118168  0.242742 0.170869 -0.00468192 -0.0153543  0.0405235   124 GLY   A N    
986  C  CA   . GLY   A 124 ? 0.11686   0.22219  0.173897 -0.00516669 -0.0150506  0.0321913   124 GLY   A CA   
987  C  C    . GLY   A 124 ? 0.10425   0.209456 0.164624 0.00217101  -0.0122055  0.0250574   124 GLY   A C    
988  O  O    . GLY   A 124 ? 0.101208  0.213857 0.173309 0.00347762  -0.0155978  0.0299594   124 GLY   A O    
989  N  N    . VAL   A 125 ? 0.101496  0.197676 0.172576 0.0049165   -0.0147853  0.0172716   125 VAL   A N    
990  C  CA   . VAL   A 125 ? 0.103805  0.202245 0.174255 0.00908562  -0.00270805 0.0129813   125 VAL   A CA   
991  C  C    . VAL   A 125 ? 0.0958158 0.211044 0.168064 0.0197714   -0.00717356 0.0239886   125 VAL   A C    
992  O  O    . VAL   A 125 ? 0.105259  0.237255 0.175002 0.0258064   -0.0151121  0.0408203   125 VAL   A O    
993  C  CB   . VAL   A 125 ? 0.145707  0.220956 0.204631 -0.00432425 -0.00225907 -0.00133861 125 VAL   A CB   
994  C  CG1  . VAL   A 125 ? 0.162662  0.244473 0.232056 -0.00756889 -0.00967349 0.00890851  125 VAL   A CG1  
995  C  CG2  . VAL   A 125 ? 0.15377   0.219816 0.215566 -0.00702868 0.00731279  -0.00558033 125 VAL   A CG2  
996  N  N    . TYR   A 126 ? 0.0863151 0.204524 0.161037 0.0230998   -0.00502921 0.0195338   126 TYR   A N    
997  C  CA   . TYR   A 126 ? 0.0870616 0.193121 0.171042 0.0250753   0.00329094  0.0189526   126 TYR   A CA   
998  C  C    . TYR   A 126 ? 0.0917343 0.187295 0.183001 0.0183928   0.00854198  0.0230406   126 TYR   A C    
999  O  O    . TYR   A 126 ? 0.078698  0.192584 0.214174 0.0196211   0.0245611   0.0378004   126 TYR   A O    
1000 C  CB   . TYR   A 126 ? 0.114788  0.198798 0.176023 0.0108086   0.00752457  0.0153556   126 TYR   A CB   
1001 C  CG   . TYR   A 126 ? 0.128909  0.201653 0.179661 0.00111282  0.00204739  -0.00099905 126 TYR   A CG   
1002 C  CD1  . TYR   A 126 ? 0.142371  0.206315 0.186076 -0.00757257 -0.00114232 -0.0104483  126 TYR   A CD1  
1003 C  CD2  . TYR   A 126 ? 0.138521  0.237582 0.186984 -0.0117942  0.00220109  -0.00311539 126 TYR   A CD2  
1004 C  CE1  . TYR   A 126 ? 0.162286  0.21127  0.18584  -0.0107902  -0.00951049 -0.0176659  126 TYR   A CE1  
1005 C  CE2  . TYR   A 126 ? 0.126775  0.245076 0.210138 -0.00550674 0.00055888  -0.0180589  126 TYR   A CE2  
1006 C  CZ   . TYR   A 126 ? 0.146156  0.22446  0.213208 -0.00167949 -0.00881762 -0.0239547  126 TYR   A CZ   
1007 O  OH   . TYR   A 126 ? 0.1686    0.247108 0.24803  0.0111344   -0.0317744  -0.0608224  126 TYR   A OH   
1008 N  N    . GLN   A 127 ? 0.0938304 0.198168 0.194908 0.019289    0.0138675   0.0181434   127 GLN   A N    
1009 C  CA   . GLN   A 127 ? 0.109624  0.19547  0.202096 0.0176287   0.00900476  0.0149987   127 GLN   A CA   
1010 C  C    . GLN   A 127 ? 0.130611  0.19466  0.196929 0.0199812   0.0221216   0.0119519   127 GLN   A C    
1011 O  O    . GLN   A 127 ? 0.174699  0.199204 0.214395 0.0277895   0.011658    0.0126825   127 GLN   A O    
1012 C  CB   . GLN   A 127 ? 0.114094  0.213091 0.223396 0.0205015   0.00908841  0.00655277  127 GLN   A CB   
1013 C  CG   . GLN   A 127 ? 0.125953  0.216001 0.22137  0.017141    -0.0047157  0.00833522  127 GLN   A CG   
1014 C  CD   . GLN   A 127 ? 0.120377  0.210992 0.215424 0.00913969  -0.0165499  0.00386485  127 GLN   A CD   
1015 O  OE1  . GLN   A 127 ? 0.112873  0.225566 0.214954 0.00824635  -0.0188908  -0.00543061 127 GLN   A OE1  
1016 N  NE2  . GLN   A 127 ? 0.145103  0.230119 0.220092 0.00784347  -0.0179508  0.0203141   127 GLN   A NE2  
1017 N  N    . CYS   A 128 ? 0.144253  0.187168 0.186444 0.0200313   0.0285059   0.0133232   128 CYS   A N    
1018 C  CA   . CYS   A 128 ? 0.156504  0.201187 0.200916 0.014518    0.0122571   0.0083795   128 CYS   A CA   
1019 C  C    . CYS   A 128 ? 0.175908  0.195144 0.192877 0.0136504   0.0308628   0.00488833  128 CYS   A C    
1020 O  O    . CYS   A 128 ? 0.272943  0.213601 0.193813 -0.0137814  0.0867106   -0.00229174 128 CYS   A O    
1021 C  CB   . CYS   A 128 ? 0.17277   0.242084 0.250853 -0.00768908 -0.0164608  0.0129509   128 CYS   A CB   
1022 S  SG   . CYS   A 128 ? 0.182225  0.280954 0.39152  -0.0184404  -0.0359937  0.0336751   128 CYS   A SG   
1023 N  N    . ALA   A 129 ? 0.227137  0.196003 0.177287 0.00987026  -0.00428534 0.00599453  129 ALA   A N    
1024 C  CA   . ALA   A 129 ? 0.20932   0.217781 0.168112 0.00485329  -0.00069954 0.00684728  129 ALA   A CA   
1025 C  C    . ALA   A 129 ? 0.170501  0.219578 0.170448 0.00791436  0.0144404   -0.00118669 129 ALA   A C    
1026 O  O    . ALA   A 129 ? 0.209194  0.225051 0.184665 -0.00136853 -0.00558223 0.00522586  129 ALA   A O    
1027 C  CB   . ALA   A 129 ? 0.209159  0.236045 0.189413 0.00926638  -0.0118105  0.0110937   129 ALA   A CB   
1028 N  N    . MET   A 130 ? 0.134234  0.225333 0.148764 0.00238222  0.0228707   -0.00482675 130 MET   A N    
1029 C  CA   . MET   A 130 ? 0.119715  0.245057 0.150031 0.00744822  0.0216227   -0.00087502 130 MET   A CA   
1030 C  C    . MET   A 130 ? 0.109186  0.23878  0.148073 0.00564666  0.0212126   0.00605879  130 MET   A C    
1031 O  O    . MET   A 130 ? 0.1105    0.234593 0.167461 0.00636913  0.0333577   0.00253368  130 MET   A O    
1032 C  CB   . MET   A 130 ? 0.132895  0.268116 0.163599 0.0143907   0.02071     0.00165507  130 MET   A CB   
1033 C  CG   . MET   A 130 ? 0.139312  0.309493 0.177626 0.0199311   0.0125988   0.00246678  130 MET   A CG   
1034 S  SD   . MET   A 130 ? 0.130866  0.359547 0.194556 0.0236626   -0.00105314 -0.00386279 130 MET   A SD   
1035 C  CE   . MET   A 130 ? 0.108381  0.361257 0.175879 0.0195715   -0.00496293 0.00450733  130 MET   A CE   
1036 N  N    . ARG   A 131 ? 0.0989757 0.246581 0.147156 0.0109919   0.0277635   0.00607656  131 ARG   A N    
1037 C  CA   . ARG   A 131 ? 0.100001  0.257402 0.144694 0.0169677   0.0194583   0.00102937  131 ARG   A CA   
1038 C  C    . ARG   A 131 ? 0.104786  0.270078 0.153572 0.0234112   0.0149349   0.01144     131 ARG   A C    
1039 O  O    . ARG   A 131 ? 0.112565  0.272441 0.164688 0.0343449   0.0118142   0.00445173  131 ARG   A O    
1040 C  CB   . ARG   A 131 ? 0.100799  0.265529 0.156268 0.0205806   0.0199249   -0.00016159 131 ARG   A CB   
1041 C  CG   . ARG   A 131 ? 0.100115  0.271573 0.163463 0.0143125   0.0102858   0.00221851  131 ARG   A CG   
1042 C  CD   . ARG   A 131 ? 0.0987085 0.273869 0.151721 0.00818469  0.0108719   -0.00045977 131 ARG   A CD   
1043 N  NE   . ARG   A 131 ? 0.0991083 0.291342 0.159392 0.00779327  0.010625    -0.00224231 131 ARG   A NE   
1044 C  CZ   . ARG   A 131 ? 0.095303  0.298901 0.161203 0.00972906  0.01119     0.0014239   131 ARG   A CZ   
1045 N  NH1  . ARG   A 131 ? 0.0891054 0.288623 0.162172 0.0111479   0.00667996  0.00656198  131 ARG   A NH1  
1046 N  NH2  . ARG   A 131 ? 0.0859218 0.315002 0.166674 0.0186348   0.00287699  -0.00455742 131 ARG   A NH2  
1047 N  N    . PRO   A 132 ? 0.105585  0.287035 0.153041 0.0327249   0.0175118   0.0154016   132 PRO   A N    
1048 C  CA   . PRO   A 132 ? 0.112459  0.289223 0.157886 0.0278991   0.0210299   0.0207757   132 PRO   A CA   
1049 C  C    . PRO   A 132 ? 0.119211  0.307765 0.152949 0.030619    0.0186979   0.0172174   132 PRO   A C    
1050 O  O    . PRO   A 132 ? 0.144446  0.327832 0.181485 0.0295488   0.00817673  0.0349539   132 PRO   A O    
1051 C  CB   . PRO   A 132 ? 0.120287  0.292123 0.160951 0.030496    0.0256732   0.016999    132 PRO   A CB   
1052 C  CG   . PRO   A 132 ? 0.120282  0.290228 0.164997 0.0315061   0.024028    0.0200356   132 PRO   A CG   
1053 C  CD   . PRO   A 132 ? 0.105329  0.287673 0.167819 0.0301846   0.0178358   0.0217838   132 PRO   A CD   
1054 N  N    . ASN   A 133 ? 0.119208  0.311824 0.144946 0.0227681   0.0149408   0.00209313  133 ASN   A N    
1055 C  CA   . ASN   A 133 ? 0.119836  0.33495  0.153421 0.0138402   0.0136809   -0.00026909 133 ASN   A CA   
1056 C  C    . ASN   A 133 ? 0.107491  0.339835 0.16742  0.0197001   0.00561058  0.00180999  133 ASN   A C    
1057 O  O    . ASN   A 133 ? 0.118089  0.35641  0.178324 0.00138937  0.00905174  -0.0144292  133 ASN   A O    
1058 C  CB   . ASN   A 133 ? 0.120765  0.338653 0.158752 0.020408    0.021657    -0.0235847  133 ASN   A CB   
1059 C  CG   . ASN   A 133 ? 0.131672  0.332406 0.17745  0.0146987   0.0274571   -0.0161871  133 ASN   A CG   
1060 O  OD1  . ASN   A 133 ? 0.122534  0.33393  0.165337 0.0132389   0.017282    -0.011976   133 ASN   A OD1  
1061 N  ND2  . ASN   A 133 ? 0.15661   0.345096 0.185157 0.00869012  0.0425643   -0.031288   133 ASN   A ND2  
1062 N  N    . PHE   A 134 ? 0.0957401 0.336842 0.167575 0.0322773   0.0118064   0.0077552   134 PHE   A N    
1063 C  CA   . PHE   A 134 ? 0.102297  0.33544  0.165522 0.0392716   0.00958967  0.0169      134 PHE   A CA   
1064 C  C    . PHE   A 134 ? 0.0959216 0.333415 0.192331 0.0367646   0.0162143   0.0190735   134 PHE   A C    
1065 O  O    . PHE   A 134 ? 0.124265  0.37876  0.24761  0.074531    0.0500981   0.0461969   134 PHE   A O    
1066 C  CB   . PHE   A 134 ? 0.107174  0.342496 0.203167 0.0360289   -0.00498747 0.0293103   134 PHE   A CB   
1067 C  CG   . PHE   A 134 ? 0.138316  0.357683 0.252045 0.0288199   -0.0213919  0.0461922   134 PHE   A CG   
1068 C  CD1  . PHE   A 134 ? 0.18071   0.365139 0.287213 0.0210481   -0.0202769  0.0502669   134 PHE   A CD1  
1069 C  CD2  . PHE   A 134 ? 0.151888  0.3684   0.26134  0.0306999   -0.0161086  0.0651561   134 PHE   A CD2  
1070 C  CE1  . PHE   A 134 ? 0.223226  0.381057 0.327129 0.004852    -0.0256238  0.056244    134 PHE   A CE1  
1071 C  CE2  . PHE   A 134 ? 0.178697  0.371828 0.294114 0.0123047   -0.0259921  0.0778864   134 PHE   A CE2  
1072 C  CZ   . PHE   A 134 ? 0.219588  0.371029 0.311743 0.0139941   -0.0209271  0.0770831   134 PHE   A CZ   
1073 N  N    . THR   A 135 ? 0.110082  0.295587 0.181971 0.0292882   0.0184266   0.00434631  135 THR   A N    
1074 C  CA   . THR   A 135 ? 0.107049  0.281384 0.180405 0.0193341   0.0117244   0.00346544  135 THR   A CA   
1075 C  C    . THR   A 135 ? 0.107443  0.250717 0.182751 0.00419207  0.0184933   0.00326018  135 THR   A C    
1076 O  O    . THR   A 135 ? 0.113372  0.270172 0.176347 -0.00857057 0.0239078   0.00457049  135 THR   A O    
1077 C  CB   . THR   A 135 ? 0.124237  0.285779 0.182745 0.0181011   0.00658576  0.00030411  135 THR   A CB   
1078 O  OG1  . THR   A 135 ? 0.133558  0.298695 0.197367 0.0234219   0.00417937  -0.0110206  135 THR   A OG1  
1079 C  CG2  . THR   A 135 ? 0.135219  0.308975 0.198567 0.0138948   -0.00146465 -0.00364885 135 THR   A CG2  
1080 N  N    . ILE   A 136 ? 0.102636  0.244875 0.178814 0.0109891   0.0202624   0.00086716  136 ILE   A N    
1081 C  CA   . ILE   A 136 ? 0.108269  0.245914 0.17978  0.00257268  0.0220835   -0.00374544 136 ILE   A CA   
1082 C  C    . ILE   A 136 ? 0.111624  0.241282 0.18001  -0.00442323 0.0184376   -0.00935374 136 ILE   A C    
1083 O  O    . ILE   A 136 ? 0.130242  0.251181 0.17565  -0.0139286  0.011894    -0.0107196  136 ILE   A O    
1084 C  CB   . ILE   A 136 ? 0.15311   0.246464 0.197397 -0.0011188  0.0292803   -0.00574218 136 ILE   A CB   
1085 C  CG1  . ILE   A 136 ? 0.142954  0.23318  0.193012 -0.00010906 0.0242872   -0.00151848 136 ILE   A CG1  
1086 C  CG2  . ILE   A 136 ? 0.20069   0.254533 0.204452 -0.00096846 0.0465818   -0.00665487 136 ILE   A CG2  
1087 C  CD1  . ILE   A 136 ? 0.140202  0.237278 0.197299 -0.00109111 0.0214167   -0.0046519  136 ILE   A CD1  
1088 N  N    . LYS   A 137 ? 0.112676  0.240267 0.196591 -0.00296078 0.00528713  -0.0133873  137 LYS   A N    
1089 C  CA   . LYS   A 137 ? 0.134673  0.254502 0.220735 0.00122785  0.00150266  -0.0121107  137 LYS   A CA   
1090 C  C    . LYS   A 137 ? 0.123605  0.246302 0.221055 -0.00244112 0.0105485   -0.0267953  137 LYS   A C    
1091 O  O    . LYS   A 137 ? 0.137559  0.260093 0.207764 -0.0204573  0.00663619  -0.0215119  137 LYS   A O    
1092 C  CB   . LYS   A 137 ? 0.152445  0.275962 0.242413 0.0156894   0.0121522   -0.0107635  137 LYS   A CB   
1093 C  CG   . LYS   A 137 ? 0.206683  0.312841 0.266628 0.0274257   0.0262794   -0.00992175 137 LYS   A CG   
1094 C  CD   . LYS   A 137 ? 0.231877  0.370469 0.330519 0.0349766   0.0465365   -0.0150122  137 LYS   A CD   
1095 C  CE   . LYS   A 137 ? 0.310252  0.428589 0.367625 0.0342815   0.0298936   -0.0122675  137 LYS   A CE   
1096 N  NZ   . LYS   A 137 ? 0.342308  0.465379 0.419369 0.052247    0.0339892   -0.018434   137 LYS   A NZ   
1097 N  N    . GLY   A 138 ? 0.146936  0.263068 0.230079 -0.0159812  0.0223554   -0.0406541  138 GLY   A N    
1098 C  CA   . GLY   A 138 ? 0.157752  0.258875 0.231432 -0.0113886  0.0188819   -0.0451832  138 GLY   A CA   
1099 C  C    . GLY   A 138 ? 0.127942  0.247436 0.225425 -0.00924183 0.00436917  -0.0505833  138 GLY   A C    
1100 O  O    . GLY   A 138 ? 0.146249  0.24945  0.254253 -0.0172358  0.0250431   -0.0587211  138 GLY   A O    
1101 N  N    . SER   A 139 ? 0.0916812 0.226378 0.198359 -0.00154232 -0.0204235  -0.0431728  139 SER   A N    
1102 C  CA   . SER   A 139 ? 0.113281  0.231552 0.220276 0.0128863   -0.0276325  -0.0323503  139 SER   A CA   
1103 C  C    . SER   A 139 ? 0.112183  0.209402 0.198524 0.0162334   -0.0247092  -0.0245415  139 SER   A C    
1104 O  O    . SER   A 139 ? 0.104519  0.206139 0.198815 0.0227682   -0.0201004  -0.0188456  139 SER   A O    
1105 C  CB   . SER   A 139 ? 0.114516  0.246173 0.236994 0.0191091   -0.0431075  -0.0307654  139 SER   A CB   
1106 O  OG   . SER   A 139 ? 0.175642  0.257995 0.258321 0.0168825   -0.0709516  -0.021026   139 SER   A OG   
1107 N  N    . PHE   A 140 ? 0.111062  0.208627 0.182585 0.00883392  -0.00925509 -0.0273254  140 PHE   A N    
1108 C  CA   . PHE   A 140 ? 0.109055  0.213324 0.181738 0.00663778  -0.00722785 -0.0162001  140 PHE   A CA   
1109 C  C    . PHE   A 140 ? 0.114349  0.217191 0.193203 0.00506333  -0.00858993 -0.0133662  140 PHE   A C    
1110 O  O    . PHE   A 140 ? 0.133536  0.220775 0.199457 -0.00572529 -0.00082278 -0.0230252  140 PHE   A O    
1111 C  CB   . PHE   A 140 ? 0.113531  0.218155 0.182195 -0.00587194 -0.00614169 -0.0157338  140 PHE   A CB   
1112 C  CG   . PHE   A 140 ? 0.117357  0.223864 0.19074  -0.0194403  -0.00443298 -0.0125067  140 PHE   A CG   
1113 C  CD1  . PHE   A 140 ? 0.132642  0.227215 0.244146 -0.0186762  0.02438     -0.0160714  140 PHE   A CD1  
1114 C  CD2  . PHE   A 140 ? 0.184006  0.230145 0.187579 -0.0364141  0.00544829  -0.0228681  140 PHE   A CD2  
1115 C  CE1  . PHE   A 140 ? 0.150539  0.2342   0.268196 -0.00993996 0.0111599   -0.0226607  140 PHE   A CE1  
1116 C  CE2  . PHE   A 140 ? 0.210568  0.244527 0.20931  -0.0454976  0.0014367   -0.00394805 140 PHE   A CE2  
1117 C  CZ   . PHE   A 140 ? 0.190627  0.221409 0.235201 -0.0187576  -0.00973016 -0.00598979 140 PHE   A CZ   
1118 N  N    . LEU   A 141 ? 0.124734  0.213736 0.199751 -0.0041025  -0.00189008 -0.00979508 141 LEU   A N    
1119 C  CA   . LEU   A 141 ? 0.125239  0.205198 0.218004 -0.00120718 -0.0126428  0.00082266  141 LEU   A CA   
1120 C  C    . LEU   A 141 ? 0.117953  0.201776 0.218145 -0.00957427 0.00280949  0.00118255  141 LEU   A C    
1121 O  O    . LEU   A 141 ? 0.112897  0.196512 0.217289 -0.0122498  0.00632358  -0.00402952 141 LEU   A O    
1122 C  CB   . LEU   A 141 ? 0.152072  0.223738 0.229109 -0.00961485 -0.0185844  0.00843971  141 LEU   A CB   
1123 C  CG   . LEU   A 141 ? 0.162912  0.253023 0.257802 -0.00284901 -0.0272024  0.0144937   141 LEU   A CG   
1124 C  CD1  . LEU   A 141 ? 0.16254   0.273998 0.261552 -0.00984728 -0.0397463  0.0193528   141 LEU   A CD1  
1125 C  CD2  . LEU   A 141 ? 0.17323   0.255904 0.273466 0.0139507   -0.0292248  0.017319    141 LEU   A CD2  
1126 N  N    . ASN   A 142 ? 0.133025  0.201275 0.234994 -0.00915396 -0.005972   0.00424199  142 ASN   A N    
1127 C  CA   . ASN   A 142 ? 0.132494  0.217027 0.240699 -0.0113059  -0.00448115 -0.00139548 142 ASN   A CA   
1128 C  C    . ASN   A 142 ? 0.120644  0.218838 0.229157 -0.0102278  0.00032839  0.0030817   142 ASN   A C    
1129 O  O    . ASN   A 142 ? 0.131417  0.237365 0.224973 -0.0170015  -0.00507608 0.00068115  142 ASN   A O    
1130 C  CB   . ASN   A 142 ? 0.150173  0.222684 0.275894 -0.0168726  -0.00676307 0.00190238  142 ASN   A CB   
1131 C  CG   . ASN   A 142 ? 0.15661   0.262228 0.327945 -0.0148366  -0.00116081 0.00275264  142 ASN   A CG   
1132 O  OD1  . ASN   A 142 ? 0.160694  0.28334  0.359076 -0.0146269  -0.0282836  -0.00759803 142 ASN   A OD1  
1133 N  ND2  . ASN   A 142 ? 0.200531  0.313544 0.383143 -0.0295635  0.00851978  0.0266398   142 ASN   A ND2  
1134 N  N    . GLY   A 143 ? 0.10659   0.210527 0.209455 -0.0125534  -0.00121795 -0.0034394  143 GLY   A N    
1135 C  CA   . GLY   A 143 ? 0.11157   0.209741 0.19633  -0.00760111 -0.0040508  -0.00313966 143 GLY   A CA   
1136 C  C    . GLY   A 143 ? 0.0929727 0.210895 0.181136 -0.00381749 -0.00477208 -0.0077562  143 GLY   A C    
1137 O  O    . GLY   A 143 ? 0.10699   0.208368 0.191331 -0.00563956 0.00156319  -0.0124334  143 GLY   A O    
1138 N  N    . SER   A 144 ? 0.0924818 0.2012   0.16463  -0.00091706 -0.00432415 -0.00512729 144 SER   A N    
1139 C  CA   . SER   A 144 ? 0.0972605 0.204448 0.168947 0.00097562  -0.00123675 -0.00452897 144 SER   A CA   
1140 C  C    . SER   A 144 ? 0.0902627 0.199675 0.158206 0.00577734  -0.00153296 -0.00736598 144 SER   A C    
1141 O  O    . SER   A 144 ? 0.0865856 0.198417 0.154927 0.00388885  -0.00778663 -0.00249079 144 SER   A O    
1142 C  CB   . SER   A 144 ? 0.0942272 0.205531 0.179865 0.00474513  -0.00378941 0.00042497  144 SER   A CB   
1143 O  OG   . SER   A 144 ? 0.0906014 0.212898 0.188355 0.00029462  0.00957457  -0.0040584  144 SER   A OG   
1144 N  N    . CYS   A 145 ? 0.0973591 0.20544  0.161027 -0.00060292 -0.0106233  -0.0058601  145 CYS   A N    
1145 C  CA   . CYS   A 145 ? 0.0946795 0.214442 0.157502 -0.003221   -0.00908369 -0.00343859 145 CYS   A CA   
1146 C  C    . CYS   A 145 ? 0.0817837 0.210404 0.153582 0.00231417  -0.01106    0.00436172  145 CYS   A C    
1147 O  O    . CYS   A 145 ? 0.0824284 0.225501 0.159372 -0.00826653 -0.0002759  0.0052125   145 CYS   A O    
1148 C  CB   . CYS   A 145 ? 0.1019    0.23089  0.166541 0.00393397  -0.0212686  -0.00446051 145 CYS   A CB   
1149 S  SG   . CYS   A 145 ? 0.133371  0.252413 0.18753  0.0180627   -0.0279026  -0.0183978  145 CYS   A SG   
1150 N  N    . GLY   A 146 ? 0.0910281 0.200174 0.148821 0.00045113  -0.010409   0.00236244  146 GLY   A N    
1151 C  CA   . GLY   A 146 ? 0.0975495 0.197748 0.159866 -0.00111594 -0.0113447  0.00517327  146 GLY   A CA   
1152 C  C    . GLY   A 146 ? 0.093199  0.188835 0.162676 0.0014461   -0.011367   0.00311976  146 GLY   A C    
1153 O  O    . GLY   A 146 ? 0.0925976 0.206987 0.18767  0.0065633   -0.00954532 -0.0109203  146 GLY   A O    
1154 N  N    . SER   A 147 ? 0.0916324 0.187133 0.161307 -5.377e-05  -0.0149726  0.00082514  147 SER   A N    
1155 C  CA   . SER   A 147 ? 0.0907458 0.186845 0.154564 -0.0011275  -0.0171468  0.00409932  147 SER   A CA   
1156 C  C    . SER   A 147 ? 0.0977812 0.185952 0.145179 0.00467788  -0.0124223  0.0030273   147 SER   A C    
1157 O  O    . SER   A 147 ? 0.115482  0.203341 0.14756  -0.00057721 -0.0137276  -0.00256991 147 SER   A O    
1158 C  CB   . SER   A 147 ? 0.0966673 0.182166 0.166854 0.00040247  -0.0164581  0.0058018   147 SER   A CB   
1159 O  OG   . SER   A 147 ? 0.103506  0.185297 0.172012 -0.00673439 -0.022215   0.00885697  147 SER   A OG   
1160 N  N    . VAL   A 148 ? 0.0976514 0.184463 0.143547 0.00208987  -0.00671303 0.00217681  148 VAL   A N    
1161 C  CA   . VAL   A 148 ? 0.0954263 0.186108 0.162937 0.00013     -0.00495645 0.00146338  148 VAL   A CA   
1162 C  C    . VAL   A 148 ? 0.0944993 0.176063 0.153248 0.00927321  -0.00795534 0.00750089  148 VAL   A C    
1163 O  O    . VAL   A 148 ? 0.110192  0.178595 0.155537 0.0159852   -0.00689102 0.0118445   148 VAL   A O    
1164 C  CB   . VAL   A 148 ? 0.107333  0.192099 0.184961 0.00282891  -0.00127691 0.00044753  148 VAL   A CB   
1165 C  CG1  . VAL   A 148 ? 0.106156  0.19688  0.191725 0.00425944  0.00067396  -0.00355148 148 VAL   A CG1  
1166 C  CG2  . VAL   A 148 ? 0.117125  0.20358  0.195118 0.00209197  -0.00181588 -0.0117491  148 VAL   A CG2  
1167 N  N    . GLY   A 149 ? 0.0919053 0.181487 0.156343 0.00370508  -0.0102056  0.00954193  149 GLY   A N    
1168 C  CA   . GLY   A 149 ? 0.0837712 0.180394 0.164697 0.0136186   -0.00473783 0.00951225  149 GLY   A CA   
1169 C  C    . GLY   A 149 ? 0.0891117 0.179302 0.173792 0.0149543   0.00024348  0.0138833   149 GLY   A C    
1170 O  O    . GLY   A 149 ? 0.0952555 0.176153 0.208296 0.0217205   -0.00638774 0.0191753   149 GLY   A O    
1171 N  N    . PHE   A 150 ? 0.0950132 0.172571 0.176267 0.0170387   -0.00275246 0.00999282  150 PHE   A N    
1172 C  CA   . PHE   A 150 ? 0.0969422 0.180398 0.188833 0.00662612  0.00328733  0.00178874  150 PHE   A CA   
1173 C  C    . PHE   A 150 ? 0.0975648 0.172142 0.186153 0.0139645   -0.0067665  0.00425941  150 PHE   A C    
1174 O  O    . PHE   A 150 ? 0.0947158 0.168115 0.181946 0.0153254   -0.00058073 0.00309466  150 PHE   A O    
1175 C  CB   . PHE   A 150 ? 0.108598  0.188207 0.201421 0.006242    0.0190168   -0.0011268  150 PHE   A CB   
1176 C  CG   . PHE   A 150 ? 0.118164  0.203717 0.193945 0.0105176   0.0337334   -0.00020763 150 PHE   A CG   
1177 C  CD1  . PHE   A 150 ? 0.144741  0.212656 0.204381 0.00782437  0.033856    -0.00355992 150 PHE   A CD1  
1178 C  CD2  . PHE   A 150 ? 0.117542  0.214957 0.193864 0.0047157   0.0318425   0.00516129  150 PHE   A CD2  
1179 C  CE1  . PHE   A 150 ? 0.174417  0.209969 0.211775 0.00225212  0.0433767   0.00566114  150 PHE   A CE1  
1180 C  CE2  . PHE   A 150 ? 0.126137  0.226122 0.201094 0.0138362   0.0371381   0.00462405  150 PHE   A CE2  
1181 C  CZ   . PHE   A 150 ? 0.164275  0.218248 0.20583  0.0224078   0.0394244   0.012345    150 PHE   A CZ   
1182 N  N    . ASN   A 151 ? 0.102478  0.17409  0.200025 0.0163081   -0.0146637  0.0100051   151 ASN   A N    
1183 C  CA   . ASN   A 151 ? 0.106953  0.178657 0.205509 0.011612    -0.0167055  0.00444559  151 ASN   A CA   
1184 C  C    . ASN   A 151 ? 0.125098  0.190744 0.216075 0.0182697   -0.0166822  -0.00031117 151 ASN   A C    
1185 O  O    . ASN   A 151 ? 0.127644  0.211574 0.239714 0.0303989   -0.0234495  -0.0109949  151 ASN   A O    
1186 C  CB   . ASN   A 151 ? 0.106463  0.186608 0.21441  0.00848988  -0.0180552  0.00715387  151 ASN   A CB   
1187 C  CG   . ASN   A 151 ? 0.121626  0.189916 0.222785 0.00373554  -0.0114681  0.00978342  151 ASN   A CG   
1188 O  OD1  . ASN   A 151 ? 0.115394  0.223066 0.240309 0.0274979   -0.0214157  -0.0128548  151 ASN   A OD1  
1189 N  ND2  . ASN   A 151 ? 0.127274  0.196925 0.222419 0.0143975   -0.0135335  0.0074142   151 ASN   A ND2  
1190 N  N    . ILE   A 152 ? 0.123126  0.198695 0.220243 0.020412    -0.0139122  -0.00639123 152 ILE   A N    
1191 C  CA   . ILE   A 152 ? 0.158699  0.211791 0.244109 0.0180228   -0.0143757  -0.010948   152 ILE   A CA   
1192 C  C    . ILE   A 152 ? 0.213519  0.242486 0.283242 -0.0218282  -0.0215386  -0.00890555 152 ILE   A C    
1193 O  O    . ILE   A 152 ? 0.238938  0.29555  0.333145 -0.0397511  -0.0442913  0.0109783   152 ILE   A O    
1194 C  CB   . ILE   A 152 ? 0.169299  0.229808 0.247103 0.0302424   -0.00491752 -0.00914211 152 ILE   A CB   
1195 C  CG1  . ILE   A 152 ? 0.175671  0.233316 0.243069 0.0357264   0.00836079  -0.00230232 152 ILE   A CG1  
1196 C  CG2  . ILE   A 152 ? 0.185594  0.230142 0.25384  0.0294354   -0.00271319 -0.0103529  152 ILE   A CG2  
1197 C  CD1  . ILE   A 152 ? 0.180081  0.244281 0.249707 0.0386933   0.016505    0.00283599  152 ILE   A CD1  
1198 N  N    . ASP   A 153 ? 0.268008  0.266188 0.301574 -0.0311394  -0.0145179  -0.00773133 153 ASP   A N    
1199 C  CA   . ASP   A 153 ? 0.287079  0.293742 0.330007 -0.0371056  0.0117791   0.00272105  153 ASP   A CA   
1200 C  C    . ASP   A 153 ? 0.349946  0.314933 0.376579 -0.0361844  0.0249347   -0.0210797  153 ASP   A C    
1201 O  O    . ASP   A 153 ? 0.401883  0.33989  0.426964 -0.0363281  0.0270148   -0.00619899 153 ASP   A O    
1202 C  CB   . ASP   A 153 ? 0.295014  0.282798 0.312682 -0.0113838  0.00131199  0.00478605  153 ASP   A CB   
1203 C  CG   . ASP   A 153 ? 0.286522  0.287267 0.292853 0.0137844   0.00046882  0.0184113   153 ASP   A CG   
1204 O  OD1  . ASP   A 153 ? 0.265798  0.2961   0.311807 0.0116899   0.0216848   0.0418709   153 ASP   A OD1  
1205 O  OD2  . ASP   A 153 ? 0.289224  0.281554 0.301298 0.0234902   -0.0160396  0.0312313   153 ASP   A OD2  
1206 N  N    . TYR   A 154 ? 0.37743   0.379132 0.413213 -0.0367658  0.0180246   -0.0139778  154 TYR   A N    
1207 C  CA   . TYR   A 154 ? 0.401019  0.393133 0.442463 -0.0199515  0.0268655   -0.0434203  154 TYR   A CA   
1208 C  C    . TYR   A 154 ? 0.378305  0.394748 0.465926 -0.0303544  0.0067459   -0.0350896  154 TYR   A C    
1209 O  O    . TYR   A 154 ? 0.404087  0.372719 0.508584 -0.01701    -0.0321853  -0.0892071  154 TYR   A O    
1210 C  CB   . TYR   A 154 ? 0.432238  0.432595 0.468798 -0.0215557  0.0539076   -0.0243335  154 TYR   A CB   
1211 C  CG   . TYR   A 154 ? 0.492692  0.49396  0.501668 -0.0258311  0.0786171   -0.0202164  154 TYR   A CG   
1212 C  CD1  . TYR   A 154 ? 0.504159  0.518911 0.522481 -0.0486905  0.0784094   -0.0255834  154 TYR   A CD1  
1213 C  CD2  . TYR   A 154 ? 0.517286  0.518078 0.519611 -0.0340877  0.0776986   -0.0188041  154 TYR   A CD2  
1214 C  CE1  . TYR   A 154 ? 0.519229  0.553735 0.571418 -0.0395129  0.0913774   -0.0273046  154 TYR   A CE1  
1215 C  CE2  . TYR   A 154 ? 0.537176  0.528235 0.556248 -0.0366108  0.0845931   -0.00317392 154 TYR   A CE2  
1216 C  CZ   . TYR   A 154 ? 0.540748  0.549109 0.564433 -0.0394205  0.0983324   -0.012921   154 TYR   A CZ   
1217 O  OH   . TYR   A 154 ? 0.583932  0.568602 0.629032 -0.0466665  0.12913     -0.0160519  154 TYR   A OH   
1218 N  N    . ASP   A 155 ? 0.379507  0.387576 0.465287 -0.0266     -0.0103079  -0.0348218  155 ASP   A N    
1219 C  CA   . ASP   A 155 ? 0.354797  0.406439 0.441009 -0.0188094  -0.0163592  -0.0355105  155 ASP   A CA   
1220 C  C    . ASP   A 155 ? 0.357792  0.406909 0.424555 -0.0269062  -0.0227287  -0.0380264  155 ASP   A C    
1221 O  O    . ASP   A 155 ? 0.365906  0.46508  0.456436 -0.015685   -0.0241569  -0.0648827  155 ASP   A O    
1222 C  CB   . ASP   A 155 ? 0.399742  0.428966 0.479663 -0.0449568  -0.020389   -0.0523245  155 ASP   A CB   
1223 N  N    . CYS   A 156 ? 0.237407  0.336799 0.396582 -0.025234   -0.0409052  -0.0229072  156 CYS   A N    
1224 C  CA   . CYS   A 156 ? 0.218204  0.262455 0.370012 0.00171558  -0.024279   -0.0150349  156 CYS   A CA   
1225 C  C    . CYS   A 156 ? 0.158758  0.234492 0.333404 0.00309807  -0.0208884  -0.0007694  156 CYS   A C    
1226 O  O    . CYS   A 156 ? 0.144183  0.239418 0.351885 0.00341967  -0.0277997  0.0133695   156 CYS   A O    
1227 C  CB   . CYS   A 156 ? 0.253212  0.266167 0.397907 0.00830877  -0.0302519  0.00085913  156 CYS   A CB   
1228 S  SG   . CYS   A 156 ? 0.283932  0.280256 0.406352 0.0218225   -0.0462305  0.0403178   156 CYS   A SG   
1229 N  N    . VAL   A 157 ? 0.138224  0.203327 0.284471 0.0225057   -0.0156774  -0.00135553 157 VAL   A N    
1230 C  CA   . VAL   A 157 ? 0.118188  0.200852 0.262803 0.0311927   -0.00902281 0.0065383   157 VAL   A CA   
1231 C  C    . VAL   A 157 ? 0.119953  0.203238 0.261646 0.0354537   -0.0094847  0.00778055  157 VAL   A C    
1232 O  O    . VAL   A 157 ? 0.133974  0.245981 0.26307  0.0700387   -0.00347597 -0.0007338  157 VAL   A O    
1233 C  CB   . VAL   A 157 ? 0.112405  0.212795 0.24769  0.0281803   -0.00649845 0.0137017   157 VAL   A CB   
1234 C  CG1  . VAL   A 157 ? 0.113612  0.214919 0.253951 0.0201503   -0.00684905 0.0180252   157 VAL   A CG1  
1235 C  CG2  . VAL   A 157 ? 0.13006   0.225191 0.24431  0.0325754   0.00279868  0.020968    157 VAL   A CG2  
1236 N  N    . SER   A 158 ? 0.117896  0.199361 0.254692 0.0269636   -0.0122678  0.01096     158 SER   A N    
1237 C  CA   . SER   A 158 ? 0.119801  0.202962 0.258831 0.0228758   -0.00497884 0.016586    158 SER   A CA   
1238 C  C    . SER   A 158 ? 0.107979  0.196489 0.256314 0.026772    -0.0124983  0.0184134   158 SER   A C    
1239 O  O    . SER   A 158 ? 0.108961  0.206835 0.293763 0.0298138   -0.0106651  0.0189596   158 SER   A O    
1240 C  CB   . SER   A 158 ? 0.148151  0.222405 0.275609 0.00560767  0.00631784  0.0197632   158 SER   A CB   
1241 O  OG   . SER   A 158 ? 0.19154   0.283219 0.310165 0.0202741   0.00100717  0.032756    158 SER   A OG   
1242 N  N    . PHE   A 159 ? 0.0976743 0.185975 0.232552 0.0351727   -0.00024414 0.0187692   159 PHE   A N    
1243 C  CA   . PHE   A 159 ? 0.10136   0.19326  0.218274 0.0305827   -0.00039976 0.0216003   159 PHE   A CA   
1244 C  C    . PHE   A 159 ? 0.10668   0.19036  0.213283 0.0245115   -0.00180246 0.0278687   159 PHE   A C    
1245 O  O    . PHE   A 159 ? 0.130785  0.194391 0.213381 0.0358538   0.0028641   0.0333774   159 PHE   A O    
1246 C  CB   . PHE   A 159 ? 0.10511   0.198156 0.214918 0.032188    0.00511683  0.0184117   159 PHE   A CB   
1247 C  CG   . PHE   A 159 ? 0.10468   0.199351 0.218796 0.0224893   0.0082281   0.00849406  159 PHE   A CG   
1248 C  CD1  . PHE   A 159 ? 0.109532  0.191688 0.215649 0.0236733   0.00505291  0.00274203  159 PHE   A CD1  
1249 C  CD2  . PHE   A 159 ? 0.111662  0.194257 0.222612 0.0243835   0.00141095  0.00614738  159 PHE   A CD2  
1250 C  CE1  . PHE   A 159 ? 0.105597  0.197211 0.21247  0.0217919   -0.00484995 0.00054724  159 PHE   A CE1  
1251 C  CE2  . PHE   A 159 ? 0.104403  0.196771 0.217353 0.0271499   -0.00085802 -0.00115029 159 PHE   A CE2  
1252 C  CZ   . PHE   A 159 ? 0.107088  0.197155 0.211803 0.023457    -0.00092419 -0.0029287  159 PHE   A CZ   
1253 N  N    . CYS   A 160 ? 0.0988047 0.194998 0.19801  0.0231776   0.00764753  0.0276466   160 CYS   A N    
1254 C  CA   . CYS   A 160 ? 0.104713  0.203733 0.201216 0.0226819   0.00592941  0.022415    160 CYS   A CA   
1255 C  C    . CYS   A 160 ? 0.108234  0.196555 0.183811 0.0240236   0.0044957   0.0264451   160 CYS   A C    
1256 O  O    . CYS   A 160 ? 0.156068  0.227732 0.182766 -0.00201679 0.00651131  0.0312573   160 CYS   A O    
1257 C  CB   . CYS   A 160 ? 0.109204  0.200708 0.209456 0.0116699   0.0121123   0.0239129   160 CYS   A CB   
1258 S  SG   . CYS   A 160 ? 0.125705  0.232064 0.225089 0.0213838   0.00452841  0.0294897   160 CYS   A SG   
1259 N  N    . TYR   A 161 ? 0.0973999 0.183979 0.170673 0.024191    0.00479894  0.0193179   161 TYR   A N    
1260 C  CA   . TYR   A 161 ? 0.0898384 0.196905 0.159852 0.0212607   -0.00021723 0.0138803   161 TYR   A CA   
1261 C  C    . TYR   A 161 ? 0.0948539 0.203726 0.160756 0.0130882   -0.00479722 0.013125    161 TYR   A C    
1262 O  O    . TYR   A 161 ? 0.095778  0.206103 0.158967 0.00745212  -0.0108172  0.0108912   161 TYR   A O    
1263 C  CB   . TYR   A 161 ? 0.0754292 0.202174 0.166844 0.0180631   0.00841664  0.00984006  161 TYR   A CB   
1264 C  CG   . TYR   A 161 ? 0.0786103 0.203047 0.16252  0.0199613   0.00459115  0.00690054  161 TYR   A CG   
1265 C  CD1  . TYR   A 161 ? 0.0958704 0.205107 0.159329 0.015595    0.0043677   0.0122569   161 TYR   A CD1  
1266 C  CD2  . TYR   A 161 ? 0.0905881 0.20144  0.156179 0.0207462   0.0044809   0.00785886  161 TYR   A CD2  
1267 C  CE1  . TYR   A 161 ? 0.101259  0.206527 0.154563 0.0166821   0.00396316  0.00675913  161 TYR   A CE1  
1268 C  CE2  . TYR   A 161 ? 0.0880113 0.208797 0.157938 0.0109192   0.00441764  0.00787151  161 TYR   A CE2  
1269 C  CZ   . TYR   A 161 ? 0.0991059 0.205373 0.165245 0.0128313   0.00643327  0.00353317  161 TYR   A CZ   
1270 O  OH   . TYR   A 161 ? 0.116678  0.212346 0.177129 0.0180636   0.0022061   -0.00602269 161 TYR   A OH   
1271 N  N    . MET   A 162 ? 0.0989266 0.195454 0.1472   0.0115328   -0.0075659  0.0140042   162 MET   A N    
1272 C  CA   . MET   A 162 ? 0.0910643 0.202279 0.15631  0.0182239   -0.00743589 0.0118509   162 MET   A CA   
1273 C  C    . MET   A 162 ? 0.0778862 0.200008 0.154213 0.0207617   -0.0060745  0.00947949  162 MET   A C    
1274 O  O    . MET   A 162 ? 0.0765552 0.223277 0.154513 0.0230416   -0.00672454 0.013457    162 MET   A O    
1275 C  CB   . MET   A 162 ? 0.0931404 0.214549 0.185736 0.0196435   -0.0118355  0.0111934   162 MET   A CB   
1276 C  CG   . MET   A 162 ? 0.0826557 0.237358 0.20699  0.0173276   -0.0159771  0.0117139   162 MET   A CG   
1277 S  SD   . MET   A 162 ? 0.10982   0.285344 0.314647 0.0256458   0.017821    0.00699525  162 MET   A SD   
1278 C  CE   . MET   A 162 ? 0.10246   0.288733 0.309398 0.035757    -0.0149084  -0.0331474  162 MET   A CE   
1279 N  N    . HIS   A 163 ? 0.0904652 0.199298 0.14382  0.0198836   0.00236272  0.0052753   163 HIS   A N    
1280 C  CA   . HIS   A 163 ? 0.0942613 0.204941 0.143438 0.0154139   -0.00142796 -0.00172583 163 HIS   A CA   
1281 C  C    . HIS   A 163 ? 0.095155  0.219567 0.148994 0.0128728   -0.00241215 -0.00444057 163 HIS   A C    
1282 O  O    . HIS   A 163 ? 0.0943792 0.230294 0.147659 0.0102674   6.132e-05   -0.00399661 163 HIS   A O    
1283 C  CB   . HIS   A 163 ? 0.0902708 0.201511 0.150543 0.0156151   0.00126497  0.00379472  163 HIS   A CB   
1284 C  CG   . HIS   A 163 ? 0.0899741 0.212489 0.151262 0.0232986   -0.00400228 -0.00227449 163 HIS   A CG   
1285 N  ND1  . HIS   A 163 ? 0.0981219 0.221923 0.157634 0.0196119   -3.213e-05  0.00282505  163 HIS   A ND1  
1286 C  CD2  . HIS   A 163 ? 0.0925384 0.210473 0.153248 0.0246759   -0.00451381 0.00050379  163 HIS   A CD2  
1287 C  CE1  . HIS   A 163 ? 0.101361  0.217304 0.161394 0.0180036   0.00149456  -0.00060628 163 HIS   A CE1  
1288 N  NE2  . HIS   A 163 ? 0.0892251 0.223439 0.160236 0.0210791   -0.00040211 -0.00535807 163 HIS   A NE2  
1289 N  N    . HIS   A 164 ? 0.0857093 0.215659 0.159014 0.0106649   -0.00305026 -0.0135373  164 HIS   A N    
1290 C  CA   . HIS   A 164 ? 0.0815059 0.225572 0.162278 0.0110825   -0.0121766  -0.00470889 164 HIS   A CA   
1291 C  C    . HIS   A 164 ? 0.0905308 0.223051 0.158632 0.00676194  -0.00903809 -0.0104432  164 HIS   A C    
1292 O  O    . HIS   A 164 ? 0.0980482 0.236278 0.181457 -0.0010173  -0.00160869 -0.00300555 164 HIS   A O    
1293 C  CB   . HIS   A 164 ? 0.0936408 0.227321 0.169657 0.0117404   -0.0153783  -0.00191575 164 HIS   A CB   
1294 C  CG   . HIS   A 164 ? 0.0792697 0.233561 0.17093  0.0219168   -0.0148361  0.00204235  164 HIS   A CG   
1295 N  ND1  . HIS   A 164 ? 0.141232  0.233318 0.187028 0.0341875   -0.00620267 0.00047217  164 HIS   A ND1  
1296 C  CD2  . HIS   A 164 ? 0.067939  0.220968 0.143853 0.0121771   -0.0153375  0.0001835   164 HIS   A CD2  
1297 C  CE1  . HIS   A 164 ? 0.0877569 0.212498 0.151644 0.0269678   -0.00802303 -0.00383211 164 HIS   A CE1  
1298 N  NE2  . HIS   A 164 ? 0.121381  0.248287 0.187236 0.00262064  -0.00393328 -0.00575111 164 HIS   A NE2  
1299 N  N    . MET   A 165 ? 0.0977674 0.227671 0.169436 0.014871    -0.00822648 -0.0114089  165 MET   A N    
1300 C  CA   . MET   A 165 ? 0.109113  0.235321 0.17309  0.0168065   -0.0142079  -0.0174289  165 MET   A CA   
1301 C  C    . MET   A 165 ? 0.112798  0.227208 0.174407 0.0125796   -0.00731074 -0.0228556  165 MET   A C    
1302 O  O    . MET   A 165 ? 0.117566  0.232167 0.165043 0.00585386  -0.00300314 -0.0135881  165 MET   A O    
1303 C  CB   . MET   A 165 ? 0.131324  0.257103 0.183301 0.0207859   -0.0175008  -0.0200061  165 MET   A CB   
1304 C  CG   . MET   A 165 ? 0.157002  0.282145 0.189365 0.0238668   -0.0123327  -0.014488   165 MET   A CG   
1305 S  SD   . MET   A 165 ? 0.200793  0.308473 0.192262 0.0277497   0.00311782  -0.011564   165 MET   A SD   
1306 C  CE   . MET   A 165 ? 0.179865  0.317693 0.189121 0.0322412   -0.00151083 -0.0202978  165 MET   A CE   
1307 N  N    . GLU   A 166 ? 0.103731  0.224203 0.194114 0.0111704   -0.0102307  -0.0254746  166 GLU   A N    
1308 C  CA   . GLU   A 166 ? 0.106079  0.226505 0.196416 0.0105007   -0.0147169  -0.0308236  166 GLU   A CA   
1309 C  C    . GLU   A 166 ? 0.124517  0.247558 0.200856 0.00140533  -0.0188307  -0.0323277  166 GLU   A C    
1310 O  O    . GLU   A 166 ? 0.131681  0.259539 0.206492 -0.0060002  -0.0261359  -0.0382626  166 GLU   A O    
1311 C  CB   . GLU   A 166 ? 0.11538   0.225806 0.200738 0.0104385   -0.0196868  -0.0305955  166 GLU   A CB   
1312 C  CG   . GLU   A 166 ? 0.125815  0.224066 0.215508 0.0132983   -0.0239392  -0.0325775  166 GLU   A CG   
1313 C  CD   . GLU   A 166 ? 0.151509  0.227199 0.227796 0.0116703   -0.0257814  -0.0284433  166 GLU   A CD   
1314 O  OE1  . GLU   A 166 ? 0.12524   0.219619 0.225409 0.0149976   -0.0170718  -0.0269042  166 GLU   A OE1  
1315 O  OE2  . GLU   A 166 ? 0.201174  0.244443 0.243942 0.0228355   -0.0373561  -0.0346528  166 GLU   A OE2  
1316 N  N    . LEU   A 167 ? 0.126172  0.272709 0.194521 0.0109507   -0.0201728  -0.0371727  167 LEU   A N    
1317 C  CA   . LEU   A 167 ? 0.175037  0.290862 0.205567 0.0132921   -0.0182854  -0.0469906  167 LEU   A CA   
1318 C  C    . LEU   A 167 ? 0.188105  0.299901 0.218318 0.0291874   -0.0376697  -0.0516291  167 LEU   A C    
1319 O  O    . LEU   A 167 ? 0.191974  0.309793 0.215782 0.0443247   -0.0388929  -0.0536538  167 LEU   A O    
1320 C  CB   . LEU   A 167 ? 0.188005  0.315367 0.204203 0.00865749  -0.0175357  -0.0350134  167 LEU   A CB   
1321 C  CG   . LEU   A 167 ? 0.219027  0.334679 0.220386 0.013884    -0.0123963  -0.0127123  167 LEU   A CG   
1322 C  CD1  . LEU   A 167 ? 0.229131  0.339392 0.229969 0.0157647   -0.0115556  -0.00753268 167 LEU   A CD1  
1323 C  CD2  . LEU   A 167 ? 0.224645  0.360216 0.263523 0.0138324   -0.0155199  0.00510256  167 LEU   A CD2  
1324 N  N    . PRO   A 168 ? 0.258591  0.329015 0.236722 0.0341561   -0.0540473  -0.0813354  168 PRO   A N    
1325 C  CA   . PRO   A 168 ? 0.297549  0.328112 0.265592 0.0289854   -0.0565531  -0.0832194  168 PRO   A CA   
1326 C  C    . PRO   A 168 ? 0.301751  0.334754 0.265921 0.029046    -0.040839   -0.0898274  168 PRO   A C    
1327 O  O    . PRO   A 168 ? 0.333237  0.339832 0.325485 0.0320132   -0.0406989  -0.0704615  168 PRO   A O    
1328 C  CB   . PRO   A 168 ? 0.322098  0.348225 0.285412 0.0213334   -0.0668175  -0.0962751  168 PRO   A CB   
1329 C  CG   . PRO   A 168 ? 0.320653  0.353537 0.27891  0.0268093   -0.0620273  -0.0924225  168 PRO   A CG   
1330 C  CD   . PRO   A 168 ? 0.28662   0.338407 0.24255  0.0434966   -0.0568636  -0.0855425  168 PRO   A CD   
1331 N  N    . THR   A 169 ? 0.315276  0.335933 0.284007 0.0301622   -0.028494   -0.100793   169 THR   A N    
1332 C  CA   . THR   A 169 ? 0.308526  0.358157 0.293577 0.0344404   -0.00842028 -0.0970085  169 THR   A CA   
1333 C  C    . THR   A 169 ? 0.243988  0.338163 0.292769 0.0286788   -0.0104192  -0.0733765  169 THR   A C    
1334 O  O    . THR   A 169 ? 0.23266   0.366346 0.341809 0.0626057   0.00945248  -0.0629304  169 THR   A O    
1335 C  CB   . THR   A 169 ? 0.362015  0.40174  0.278744 0.0265849   0.00197229  -0.10276    169 THR   A CB   
1336 O  OG1  . THR   A 169 ? 0.412043  0.418935 0.28212  0.0315969   0.0104757   -0.107811   169 THR   A OG1  
1337 C  CG2  . THR   A 169 ? 0.391225  0.422725 0.279478 0.0293829   0.0184654   -0.117441   169 THR   A CG2  
1338 N  N    . GLY   A 170 ? 0.217125  0.301108 0.254023 0.015808    -0.0277954  -0.0569598  170 GLY   A N    
1339 C  CA   . GLY   A 170 ? 0.196742  0.274183 0.251651 0.00768463  -0.0195833  -0.0438213  170 GLY   A CA   
1340 C  C    . GLY   A 170 ? 0.2024    0.268364 0.228581 0.00320286  -0.0130372  -0.0344822  170 GLY   A C    
1341 O  O    . GLY   A 170 ? 0.282144  0.298857 0.256254 -0.0230896  -0.0452817  -0.024606   170 GLY   A O    
1342 N  N    . VAL   A 171 ? 0.161618  0.245675 0.225324 0.012565    0.0002503   -0.0388253  171 VAL   A N    
1343 C  CA   . VAL   A 171 ? 0.138163  0.24584  0.215026 0.0213822   0.00665218  -0.0296248  171 VAL   A CA   
1344 C  C    . VAL   A 171 ? 0.123508  0.236568 0.197276 0.0125179   0.00528693  -0.0245568  171 VAL   A C    
1345 O  O    . VAL   A 171 ? 0.134889  0.244486 0.192428 0.00472061  0.00170765  -0.0363178  171 VAL   A O    
1346 C  CB   . VAL   A 171 ? 0.15823   0.265881 0.228633 0.0218845   0.0110351   -0.0230049  171 VAL   A CB   
1347 C  CG1  . VAL   A 171 ? 0.169268  0.273229 0.263907 0.0279781   0.0224655   -0.023483   171 VAL   A CG1  
1348 C  CG2  . VAL   A 171 ? 0.183175  0.277683 0.223293 0.0220709   0.0111025   -0.0292178  171 VAL   A CG2  
1349 N  N    . HIS   A 172 ? 0.107905  0.232667 0.170765 0.0104971   0.0109785   -0.0218015  172 HIS   A N    
1350 C  CA   . HIS   A 172 ? 0.109548  0.23437  0.182374 0.00963877  0.0127202   -0.0196429  172 HIS   A CA   
1351 C  C    . HIS   A 172 ? 0.10567   0.245493 0.176587 0.00950253  0.0150455   -0.0101214  172 HIS   A C    
1352 O  O    . HIS   A 172 ? 0.111619  0.261422 0.197184 0.0101545   0.018936    0.0083675   172 HIS   A O    
1353 C  CB   . HIS   A 172 ? 0.125953  0.238441 0.183093 0.00356423  0.0164683   -0.020958   172 HIS   A CB   
1354 C  CG   . HIS   A 172 ? 0.142109  0.226072 0.182279 -0.00481959 0.0132504   -0.0264848  172 HIS   A CG   
1355 N  ND1  . HIS   A 172 ? 0.156568  0.225041 0.180607 -0.00089644 0.00414308  -0.0189039  172 HIS   A ND1  
1356 C  CD2  . HIS   A 172 ? 0.140825  0.22575  0.18465  -0.0124762  0.0135718   -0.0318054  172 HIS   A CD2  
1357 C  CE1  . HIS   A 172 ? 0.156968  0.219929 0.185604 -0.00422435 0.00066012  -0.0209154  172 HIS   A CE1  
1358 N  NE2  . HIS   A 172 ? 0.168714  0.231439 0.200999 -0.0149259  0.0118505   -0.0239509  172 HIS   A NE2  
1359 N  N    . ALA   A 173 ? 0.104064  0.244205 0.170292 0.0129344   0.0135588   -0.00626671 173 ALA   A N    
1360 C  CA   . ALA   A 173 ? 0.106449  0.248905 0.16862  0.0172192   0.0136223   -0.00579934 173 ALA   A CA   
1361 C  C    . ALA   A 173 ? 0.0964252 0.239326 0.150089 0.0161474   0.0094254   0.00047287  173 ALA   A C    
1362 O  O    . ALA   A 173 ? 0.0992991 0.251761 0.1673   0.0140273   0.0114882   0.00940351  173 ALA   A O    
1363 C  CB   . ALA   A 173 ? 0.12768   0.266949 0.168804 0.0202156   0.0114632   -0.00862702 173 ALA   A CB   
1364 N  N    . GLY   A 174 ? 0.0938835 0.240082 0.148012 0.019265    0.0101881   0.00021638  174 GLY   A N    
1365 C  CA   . GLY   A 174 ? 0.0951118 0.227905 0.151232 0.0210893   0.00693382  0.00550891  174 GLY   A CA   
1366 C  C    . GLY   A 174 ? 0.0858003 0.238129 0.148769 0.0189213   -0.00241242 0.013866    174 GLY   A C    
1367 O  O    . GLY   A 174 ? 0.102389  0.267252 0.158001 0.0202875   0.00684027  0.0172642   174 GLY   A O    
1368 N  N    . THR   A 175 ? 0.0973794 0.237241 0.148678 0.0195133   0.00092798  0.0133006   175 THR   A N    
1369 C  CA   . THR   A 175 ? 0.095502  0.239628 0.158182 0.0209169   0.00292528  0.0245782   175 THR   A CA   
1370 C  C    . THR   A 175 ? 0.0994551 0.244223 0.160319 0.0156474   0.00087671  0.0313681   175 THR   A C    
1371 O  O    . THR   A 175 ? 0.111765  0.254977 0.165279 0.0110935   -0.014524   0.0366062   175 THR   A O    
1372 C  CB   . THR   A 175 ? 0.0957183 0.246027 0.17305  0.0243581   -0.00016373 0.0212901   175 THR   A CB   
1373 O  OG1  . THR   A 175 ? 0.085374  0.254765 0.1793   0.021255    -0.00239968 0.0150445   175 THR   A OG1  
1374 C  CG2  . THR   A 175 ? 0.099534  0.242552 0.180036 0.0261893   0.00222016  0.0183918   175 THR   A CG2  
1375 N  N    . ASP   A 176 ? 0.105028  0.248855 0.164209 0.0213411   -0.0052879  0.0406353   176 ASP   A N    
1376 C  CA   . ASP   A 176 ? 0.114341  0.252052 0.190262 0.0182744   -0.00653838 0.0361059   176 ASP   A CA   
1377 C  C    . ASP   A 176 ? 0.110716  0.24103  0.20064  0.022923    -0.00993227 0.0315548   176 ASP   A C    
1378 O  O    . ASP   A 176 ? 0.0984515 0.236371 0.207246 0.0213721   -0.00943895 0.0291494   176 ASP   A O    
1379 C  CB   . ASP   A 176 ? 0.115734  0.261331 0.192948 0.0163867   -0.00177721 0.0427524   176 ASP   A CB   
1380 C  CG   . ASP   A 176 ? 0.12233   0.283666 0.20375  0.0110332   -0.00208548 0.0567698   176 ASP   A CG   
1381 O  OD1  . ASP   A 176 ? 0.11221   0.285987 0.221895 0.0194574   -0.0062765  0.0465118   176 ASP   A OD1  
1382 O  OD2  . ASP   A 176 ? 0.148368  0.31678  0.219638 0.0105385   0.00621051  0.0734505   176 ASP   A OD2  
1383 N  N    . LEU   A 177 ? 0.111636  0.237833 0.21043  0.0263268   -0.00032905 0.0266856   177 LEU   A N    
1384 C  CA   . LEU   A 177 ? 0.113145  0.241234 0.205935 0.028342    -0.0018692  0.0203239   177 LEU   A CA   
1385 C  C    . LEU   A 177 ? 0.117621  0.255025 0.225475 0.0335324   -0.00188806 0.031005    177 LEU   A C    
1386 O  O    . LEU   A 177 ? 0.108125  0.292353 0.237955 0.0424963   -0.00799469 0.0281206   177 LEU   A O    
1387 C  CB   . LEU   A 177 ? 0.115136  0.243646 0.218618 0.0257601   -0.00932447 0.00886801  177 LEU   A CB   
1388 C  CG   . LEU   A 177 ? 0.147643  0.245695 0.218752 0.0244308   -0.0119854  0.00170348  177 LEU   A CG   
1389 C  CD1  . LEU   A 177 ? 0.171141  0.253689 0.216749 0.0138354   -0.0118389  0.00569054  177 LEU   A CD1  
1390 C  CD2  . LEU   A 177 ? 0.157066  0.247723 0.221375 0.0323366   -0.0234745  0.00050427  177 LEU   A CD2  
1391 N  N    . GLU   A 178 ? 0.109892  0.26085  0.230217 0.0333533   -0.00927948 0.044411    178 GLU   A N    
1392 C  CA   . GLU   A 178 ? 0.135947  0.272458 0.23973  0.0470469   -0.0145049  0.0506877   178 GLU   A CA   
1393 C  C    . GLU   A 178 ? 0.109773  0.271539 0.228764 0.0415691   -0.011418   0.0488517   178 GLU   A C    
1394 O  O    . GLU   A 178 ? 0.127174  0.29506  0.250234 0.0410353   -0.0228754  0.0629252   178 GLU   A O    
1395 C  CB   . GLU   A 178 ? 0.177792  0.296858 0.269606 0.0406264   -0.0151835  0.064869    178 GLU   A CB   
1396 C  CG   . GLU   A 178 ? 0.232366  0.32528  0.307033 0.0318827   -0.0218134  0.0590152   178 GLU   A CG   
1397 C  CD   . GLU   A 178 ? 0.298981  0.350921 0.354658 0.0127592   0.00239855  0.0586457   178 GLU   A CD   
1398 O  OE1  . GLU   A 178 ? 0.338119  0.412992 0.381353 -0.0074276  0.0309686   0.0714648   178 GLU   A OE1  
1399 O  OE2  . GLU   A 178 ? 0.377007  0.390993 0.434307 0.0200933   0.011199    0.0421277   178 GLU   A OE2  
1400 N  N    . GLY   A 179 ? 0.110317  0.266163 0.217965 0.0398759   -0.00492622 0.0391664   179 GLY   A N    
1401 C  CA   . GLY   A 179 ? 0.0956612 0.271265 0.213405 0.041051    -0.00783207 0.0380311   179 GLY   A CA   
1402 C  C    . GLY   A 179 ? 0.0948508 0.286354 0.201938 0.0298196   -0.00701207 0.0431159   179 GLY   A C    
1403 O  O    . GLY   A 179 ? 0.112854  0.291534 0.201218 0.0243954   -0.00252267 0.032849    179 GLY   A O    
1404 N  N    . ASN   A 180 ? 0.101292  0.299056 0.192885 0.028521    -7.846e-05  0.0498851   180 ASN   A N    
1405 C  CA   . ASN   A 180 ? 0.111749  0.311471 0.208222 0.0419085   0.00422146  0.0528924   180 ASN   A CA   
1406 C  C    . ASN   A 180 ? 0.101302  0.295831 0.177061 0.0325929   0.00752251  0.0470354   180 ASN   A C    
1407 O  O    . ASN   A 180 ? 0.114782  0.289168 0.171161 0.0368003   0.00176048  0.0434882   180 ASN   A O    
1408 C  CB   . ASN   A 180 ? 0.134283  0.335505 0.221415 0.0485209   0.0218945   0.0708122   180 ASN   A CB   
1409 C  CG   . ASN   A 180 ? 0.184573  0.364391 0.274623 0.0683282   0.0363607   0.0782464   180 ASN   A CG   
1410 O  OD1  . ASN   A 180 ? 0.226509  0.452689 0.274796 0.125452    0.015793    0.0991034   180 ASN   A OD1  
1411 N  ND2  . ASN   A 180 ? 0.21617   0.352373 0.346618 0.0770907   0.0537352   0.0854076   180 ASN   A ND2  
1412 N  N    . PHE   A 181 ? 0.0889663 0.300449 0.183131 0.0215388   -0.00347743 0.0427155   181 PHE   A N    
1413 C  CA   . PHE   A 181 ? 0.108679  0.295448 0.177321 0.0191738   -0.00409284 0.0352526   181 PHE   A CA   
1414 C  C    . PHE   A 181 ? 0.106545  0.303011 0.16861  0.022801    -0.00132344 0.0376355   181 PHE   A C    
1415 O  O    . PHE   A 181 ? 0.118251  0.326826 0.182815 0.0407539   -0.00274152 0.0609131   181 PHE   A O    
1416 C  CB   . PHE   A 181 ? 0.119188  0.297553 0.169768 0.023211    -0.0144843  0.0277963   181 PHE   A CB   
1417 C  CG   . PHE   A 181 ? 0.110509  0.296699 0.177067 0.0178097   -0.0256223  0.0258415   181 PHE   A CG   
1418 C  CD1  . PHE   A 181 ? 0.107503  0.310825 0.183385 0.0110791   -0.0312078  0.0310658   181 PHE   A CD1  
1419 C  CD2  . PHE   A 181 ? 0.109715  0.297394 0.177964 0.0222851   -0.0225818  0.0256942   181 PHE   A CD2  
1420 C  CE1  . PHE   A 181 ? 0.10318   0.307943 0.186634 0.00808063  -0.0329125  0.0283708   181 PHE   A CE1  
1421 C  CE2  . PHE   A 181 ? 0.117195  0.298799 0.182259 0.0159532   -0.0280343  0.0251452   181 PHE   A CE2  
1422 C  CZ   . PHE   A 181 ? 0.117624  0.298825 0.176254 0.00831227  -0.0216653  0.0226053   181 PHE   A CZ   
1423 N  N    . TYR   A 182 ? 0.103616  0.300339 0.144675 0.0234648   0.00210656  0.0316413   182 TYR   A N    
1424 C  CA   . TYR   A 182 ? 0.10042   0.305985 0.168681 0.0193418   0.00298926  0.031094    182 TYR   A CA   
1425 C  C    . TYR   A 182 ? 0.121061  0.337932 0.172748 0.0291747   0.0120931   0.0228572   182 TYR   A C    
1426 O  O    . TYR   A 182 ? 0.139521  0.344832 0.206762 0.0139966   0.0328105   -0.006836   182 TYR   A O    
1427 C  CB   . TYR   A 182 ? 0.0979194 0.282135 0.176662 0.0155222   -0.00081479 0.037526    182 TYR   A CB   
1428 C  CG   . TYR   A 182 ? 0.0973418 0.258185 0.183536 0.013348    -0.0020827  0.0385441   182 TYR   A CG   
1429 C  CD1  . TYR   A 182 ? 0.103401  0.259148 0.188217 0.00946182  0.00446214  0.0389855   182 TYR   A CD1  
1430 C  CD2  . TYR   A 182 ? 0.0812488 0.250927 0.189006 0.0137613   -0.00434365 0.0386313   182 TYR   A CD2  
1431 C  CE1  . TYR   A 182 ? 0.112082  0.256974 0.200359 0.00489237  0.00015861  0.0394235   182 TYR   A CE1  
1432 C  CE2  . TYR   A 182 ? 0.0822899 0.240489 0.196935 0.0117455   -0.00813279 0.0449323   182 TYR   A CE2  
1433 C  CZ   . TYR   A 182 ? 0.0974401 0.237832 0.197324 0.00763818  -0.00486967 0.0401413   182 TYR   A CZ   
1434 O  OH   . TYR   A 182 ? 0.113751  0.23326  0.199637 0.00021913  -0.00588596 0.036057    182 TYR   A OH   
1435 N  N    . GLY   A 183 ? 0.118239  0.395481 0.181347 0.0401063   0.013002    0.0237665   183 GLY   A N    
1436 C  CA   . GLY   A 183 ? 0.114574  0.430301 0.172964 0.0488118   0.00417669  0.0159259   183 GLY   A CA   
1437 C  C    . GLY   A 183 ? 0.129523  0.473528 0.170255 0.0551312   -0.00871823 0.00864392  183 GLY   A C    
1438 O  O    . GLY   A 183 ? 0.146042  0.505087 0.216024 0.072968    -0.0131479  -0.0258604  183 GLY   A O    
1439 N  N    . PRO   A 184 ? 0.168901  0.502955 0.164624 0.042972    0.0019652   0.0121951   184 PRO   A N    
1440 C  CA   . PRO   A 184 ? 0.1741    0.519471 0.171654 0.0461673   -0.00777346 0.0153232   184 PRO   A CA   
1441 C  C    . PRO   A 184 ? 0.193832  0.520186 0.196823 0.0351525   -0.0107409  0.0240717   184 PRO   A C    
1442 O  O    . PRO   A 184 ? 0.199998  0.548158 0.2707   0.0632844   -0.0321142  0.00914192  184 PRO   A O    
1443 C  CB   . PRO   A 184 ? 0.198396  0.536242 0.170155 0.0362056   0.00517061  0.0131635   184 PRO   A CB   
1444 C  CG   . PRO   A 184 ? 0.224837  0.529856 0.17872  0.043341    -0.00029702 0.00288713  184 PRO   A CG   
1445 C  CD   . PRO   A 184 ? 0.20142   0.513699 0.168407 0.0546113   -0.00181953 0.00900448  184 PRO   A CD   
1446 N  N    . PHE   A 185 ? 0.134546  0.46677  0.191362 0.0553364   0.0224735   0.0205499   185 PHE   A N    
1447 C  CA   . PHE   A 185 ? 0.133013  0.435392 0.194707 0.0706741   0.0237251   0.0180607   185 PHE   A CA   
1448 C  C    . PHE   A 185 ? 0.134318  0.423291 0.209933 0.0713573   0.0264626   0.0152634   185 PHE   A C    
1449 O  O    . PHE   A 185 ? 0.155409  0.436619 0.217473 0.0724879   0.0452199   0.0168116   185 PHE   A O    
1450 C  CB   . PHE   A 185 ? 0.145884  0.418177 0.18325  0.0704169   0.0121721   0.00026472  185 PHE   A CB   
1451 C  CG   . PHE   A 185 ? 0.146463  0.403451 0.179282 0.0726333   -0.00253583 -0.0107146  185 PHE   A CG   
1452 C  CD1  . PHE   A 185 ? 0.15021   0.401895 0.187624 0.0748047   -0.00807273 -0.0100968  185 PHE   A CD1  
1453 C  CD2  . PHE   A 185 ? 0.135937  0.391709 0.180608 0.0732236   -0.0086615  -0.0146328  185 PHE   A CD2  
1454 C  CE1  . PHE   A 185 ? 0.148574  0.402752 0.192787 0.0731151   -0.0157477  -0.0203776  185 PHE   A CE1  
1455 C  CE2  . PHE   A 185 ? 0.130665  0.395546 0.192154 0.0667158   -0.0157047  -0.0112452  185 PHE   A CE2  
1456 C  CZ   . PHE   A 185 ? 0.138776  0.401353 0.201014 0.0725886   -0.0139131  -0.0165357  185 PHE   A CZ   
1457 N  N    . VAL   A 186 ? 0.140224  0.411275 0.214132 0.0711918   0.0351436   0.0161915   186 VAL   A N    
1458 C  CA   . VAL   A 186 ? 0.13199   0.405447 0.210575 0.0647868   0.024499    0.00909761  186 VAL   A CA   
1459 C  C    . VAL   A 186 ? 0.108483  0.37791  0.184925 0.0598751   0.00995483  -0.00171236 186 VAL   A C    
1460 O  O    . VAL   A 186 ? 0.11514   0.371148 0.18679  0.0696855   0.0103893   -0.0173907  186 VAL   A O    
1461 C  CB   . VAL   A 186 ? 0.171317  0.425648 0.205515 0.0575664   0.0268444   0.00022784  186 VAL   A CB   
1462 C  CG1  . VAL   A 186 ? 0.180164  0.440795 0.191832 0.0670149   0.0241879   0.00034559  186 VAL   A CG1  
1463 C  CG2  . VAL   A 186 ? 0.186188  0.44402  0.219527 0.0583721   0.0353976   -0.00450346 186 VAL   A CG2  
1464 N  N    . ASP   A 187 ? 0.0964377 0.362284 0.186403 0.0537754   0.00991299  0.00180713  187 ASP   A N    
1465 C  CA   . ASP   A 187 ? 0.106269  0.345866 0.1799   0.0500524   0.00428491  -0.00698007 187 ASP   A CA   
1466 C  C    . ASP   A 187 ? 0.096476  0.361539 0.198214 0.0471778   -0.00176611 -0.022345   187 ASP   A C    
1467 O  O    . ASP   A 187 ? 0.104311  0.358564 0.242819 0.0579157   0.0116362   -0.0371578  187 ASP   A O    
1468 C  CB   . ASP   A 187 ? 0.108996  0.343836 0.189946 0.0406303   0.00548401  -0.00913446 187 ASP   A CB   
1469 C  CG   . ASP   A 187 ? 0.0976331 0.345697 0.173705 0.0412759   0.00373857  -0.00572979 187 ASP   A CG   
1470 O  OD1  . ASP   A 187 ? 0.121932  0.353884 0.174858 0.0582915   0.00321673  -0.0036766  187 ASP   A OD1  
1471 O  OD2  . ASP   A 187 ? 0.112125  0.325869 0.174444 0.0386406   -0.00868453 -0.00710542 187 ASP   A OD2  
1472 N  N    . ARG   A 188 ? 0.116252  0.372613 0.211681 0.0577439   -0.00911324 -0.0283941  188 ARG   A N    
1473 C  CA   . ARG   A 188 ? 0.166784  0.402207 0.243134 0.0487803   -0.0320089  -0.041571   188 ARG   A CA   
1474 C  C    . ARG   A 188 ? 0.147388  0.408543 0.2216   0.0602991   -0.0388669  -0.0585159  188 ARG   A C    
1475 O  O    . ARG   A 188 ? 0.13523   0.41522  0.22685  0.0629032   -0.0250992  -0.0582681  188 ARG   A O    
1476 C  CB   . ARG   A 188 ? 0.203364  0.446744 0.28027  0.0377184   -0.0626943  -0.0239954  188 ARG   A CB   
1477 C  CG   . ARG   A 188 ? 0.253115  0.467563 0.30473  0.0221366   -0.0323509  0.00721896  188 ARG   A CG   
1478 C  CD   . ARG   A 188 ? 0.219427  0.4585   0.2808   0.0422588   -0.0644536  0.0174256   188 ARG   A CD   
1479 N  NE   . ARG   A 188 ? 0.217924  0.439217 0.24366  0.0522089   -0.0223374  0.0332961   188 ARG   A NE   
1480 C  CZ   . ARG   A 188 ? 0.2385    0.45857  0.252022 0.03679     -0.00745485 0.0240328   188 ARG   A CZ   
1481 N  NH1  . ARG   A 188 ? 0.229233  0.485888 0.225412 0.0410759   0.00297067  0.0326466   188 ARG   A NH1  
1482 N  NH2  . ARG   A 188 ? 0.273132  0.457026 0.231073 0.0472438   0.0283353   0.0109032   188 ARG   A NH2  
1483 N  N    . GLN   A 189 ? 0.169192  0.417961 0.231997 0.0638042   -0.0352642  -0.0565857  189 GLN   A N    
1484 C  CA   . GLN   A 189 ? 0.211664  0.442754 0.269827 0.0871532   -0.0372985  -0.0621142  189 GLN   A CA   
1485 C  C    . GLN   A 189 ? 0.323371  0.465249 0.30091  0.10192     -0.034008   -0.0917225  189 GLN   A C    
1486 O  O    . GLN   A 189 ? 0.471402  0.507301 0.320207 0.0642611   -0.0459937  -0.0674916  189 GLN   A O    
1487 C  CB   . GLN   A 189 ? 0.264893  0.481715 0.354288 0.0622784   -0.0212058  -0.0456751  189 GLN   A CB   
1488 C  CG   . GLN   A 189 ? 0.343471  0.512651 0.39025  0.0519463   -0.0199549  -0.0309108  189 GLN   A CG   
1489 C  CD   . GLN   A 189 ? 0.359215  0.545797 0.427316 0.0363986   -0.0150021  -0.0185421  189 GLN   A CD   
1490 O  OE1  . GLN   A 189 ? 0.366847  0.574049 0.460491 0.0691174   0.00271555  -0.0276737  189 GLN   A OE1  
1491 N  NE2  . GLN   A 189 ? 0.354595  0.544469 0.421389 0.0333041   -0.0307951  -0.0380668  189 GLN   A NE2  
1492 N  N    . THR   A 190 ? 0.359077  0.480292 0.233733 0.152497    -0.0489541  -0.100984   190 THR   A N    
1493 C  CA   . THR   A 190 ? 0.331191  0.57276  0.25741  0.180666    -0.0474957  -0.117687   190 THR   A CA   
1494 C  C    . THR   A 190 ? 0.323673  0.627143 0.228935 0.189946    -0.0771421  -0.143108   190 THR   A C    
1495 O  O    . THR   A 190 ? 0.311167  0.64797  0.249977 0.209467    -0.07398    -0.166133   190 THR   A O    
1496 C  CB   . THR   A 190 ? 0.320093  0.615077 0.268814 0.190969    -0.0299523  -0.090897   190 THR   A CB   
1497 O  OG1  . THR   A 190 ? 0.336751  0.673946 0.300033 0.203816    -0.0373059  -0.107      190 THR   A OG1  
1498 C  CG2  . THR   A 190 ? 0.316567  0.609518 0.251881 0.182342    -0.0156676  -0.0858858  190 THR   A CG2  
1499 N  N    . ALA   A 191 ? 0.304989  0.679465 0.276891 0.215735    -0.0769917  -0.176961   191 ALA   A N    
1500 C  CA   . ALA   A 191 ? 0.308416  0.733712 0.29134  0.202258    -0.069502   -0.186054   191 ALA   A CA   
1501 C  C    . ALA   A 191 ? 0.255126  0.761171 0.268212 0.173904    -0.0534774  -0.208908   191 ALA   A C    
1502 O  O    . ALA   A 191 ? 0.301114  0.835966 0.329256 0.173196    -0.0426228  -0.155044   191 ALA   A O    
1503 C  CB   . ALA   A 191 ? 0.339519  0.748705 0.323104 0.208246    -0.0489763  -0.201553   191 ALA   A CB   
1504 N  N    . GLN   A 192 ? 0.244265  0.76041  0.341758 0.157545    -0.04689    -0.215951   192 GLN   A N    
1505 C  CA   . GLN   A 192 ? 0.158167  0.744958 0.336181 0.139355    0.0174847   -0.21012    192 GLN   A CA   
1506 C  C    . GLN   A 192 ? 0.22617   0.771817 0.410265 0.135754    -0.061482   -0.192616   192 GLN   A C    
1507 O  O    . GLN   A 192 ? 0.307134  0.768349 0.389228 0.164595    -0.105076   -0.202841   192 GLN   A O    
1508 C  CB   . GLN   A 192 ? 0.220086  0.698219 0.37636  0.113634    0.0112653   -0.153428   192 GLN   A CB   
1509 C  CG   . GLN   A 192 ? 0.23276   0.625174 0.359186 0.12815     0.0376562   -0.137214   192 GLN   A CG   
1510 C  CD   . GLN   A 192 ? 0.203523  0.565889 0.349174 0.118596    0.050065    -0.0780904  192 GLN   A CD   
1511 O  OE1  . GLN   A 192 ? 0.208048  0.555624 0.375262 0.0995453   0.0807521   -0.06121    192 GLN   A OE1  
1512 N  NE2  . GLN   A 192 ? 0.207014  0.510237 0.294734 0.116952    0.043282    -0.0606481  192 GLN   A NE2  
1513 N  N    . ALA   A 193 ? 0.204825  0.746399 0.491749 0.0710864   -0.0497676  -0.221535   193 ALA   A N    
1514 C  CA   . ALA   A 193 ? 0.198878  0.723531 0.501325 0.0789746   -0.037015   -0.24904    193 ALA   A CA   
1515 C  C    . ALA   A 193 ? 0.227384  0.719686 0.48049  0.0737898   -0.0104467  -0.254389   193 ALA   A C    
1516 O  O    . ALA   A 193 ? 0.254949  0.739343 0.466071 0.0822646   -0.00806714 -0.265404   193 ALA   A O    
1517 C  CB   . ALA   A 193 ? 0.239337  0.712852 0.515688 0.0606302   -0.0341451  -0.253092   193 ALA   A CB   
1518 N  N    . ALA   A 194 ? 0.192511  0.713184 0.486962 0.080295    -0.00561047 -0.257876   194 ALA   A N    
1519 C  CA   . ALA   A 194 ? 0.172575  0.701325 0.471887 0.0761671   0.0242576   -0.259825   194 ALA   A CA   
1520 C  C    . ALA   A 194 ? 0.219619  0.703403 0.447547 0.0701694   0.0268349   -0.257879   194 ALA   A C    
1521 O  O    . ALA   A 194 ? 0.188256  0.711939 0.462979 0.0940342   -0.00350627 -0.274818   194 ALA   A O    
1522 C  CB   . ALA   A 194 ? 0.198702  0.71384  0.47856  0.0642075   0.0109112   -0.256276   194 ALA   A CB   
1523 N  N    . GLY   A 195 ? 0.200218  0.710769 0.393454 0.0669701   0.0314415   -0.234987   195 GLY   A N    
1524 C  CA   . GLY   A 195 ? 0.228811  0.695315 0.368333 0.0589177   0.0334355   -0.215071   195 GLY   A CA   
1525 C  C    . GLY   A 195 ? 0.186866  0.668334 0.350377 0.0215192   0.032252    -0.198041   195 GLY   A C    
1526 O  O    . GLY   A 195 ? 0.171207  0.659364 0.355832 0.0206173   0.0502772   -0.198772   195 GLY   A O    
1527 N  N    . THR   A 196 ? 0.223102  0.631135 0.32607  0.0315303   0.0372009   -0.176459   196 THR   A N    
1528 C  CA   . THR   A 196 ? 0.227794  0.574566 0.340183 0.0071312   0.0334808   -0.149333   196 THR   A CA   
1529 C  C    . THR   A 196 ? 0.196485  0.522588 0.324324 0.0212555   0.0427185   -0.115697   196 THR   A C    
1530 O  O    . THR   A 196 ? 0.251375  0.532111 0.372311 0.0232151   0.0202284   -0.106743   196 THR   A O    
1531 C  CB   . THR   A 196 ? 0.294148  0.607332 0.34822  0.007721    0.0565417   -0.145072   196 THR   A CB   
1532 O  OG1  . THR   A 196 ? 0.390541  0.665734 0.441233 0.0230504   0.063257    -0.088889   196 THR   A OG1  
1533 C  CG2  . THR   A 196 ? 0.299017  0.60589  0.338804 0.0102178   0.0323859   -0.163447   196 THR   A CG2  
1534 N  N    . ASP   A 197 ? 0.155869  0.459733 0.326616 0.0048987   0.0374818   -0.115317   197 ASP   A N    
1535 C  CA   . ASP   A 197 ? 0.148015  0.429386 0.318066 0.0192519   0.0493191   -0.103676   197 ASP   A CA   
1536 C  C    . ASP   A 197 ? 0.140387  0.401837 0.307679 0.020661    0.0356202   -0.0900846  197 ASP   A C    
1537 O  O    . ASP   A 197 ? 0.182844  0.409738 0.324237 0.00968555  0.0298407   -0.109007   197 ASP   A O    
1538 C  CB   . ASP   A 197 ? 0.158442  0.42269  0.309978 0.0285973   0.0371367   -0.112554   197 ASP   A CB   
1539 C  CG   . ASP   A 197 ? 0.164264  0.417827 0.303037 0.0267018   0.0396149   -0.102232   197 ASP   A CG   
1540 O  OD1  . ASP   A 197 ? 0.193822  0.392781 0.299296 0.0075375   0.0657179   -0.0728475  197 ASP   A OD1  
1541 O  OD2  . ASP   A 197 ? 0.153024  0.445461 0.302363 0.0516353   -0.0278995  -0.106975   197 ASP   A OD2  
1542 N  N    . THR   A 198 ? 0.111013  0.374891 0.232432 0.0267863   0.0278582   -0.0738827  198 THR   A N    
1543 C  CA   . THR   A 198 ? 0.109532  0.350604 0.190064 0.0242539   0.018731    -0.0439958  198 THR   A CA   
1544 C  C    . THR   A 198 ? 0.0950543 0.313154 0.175562 0.018392    0.0229771   -0.024003   198 THR   A C    
1545 O  O    . THR   A 198 ? 0.0890646 0.326195 0.177796 0.0135648   0.0232242   -0.0161426  198 THR   A O    
1546 C  CB   . THR   A 198 ? 0.15726   0.370828 0.186317 0.0420543   0.0140043   -0.0423318  198 THR   A CB   
1547 O  OG1  . THR   A 198 ? 0.188219  0.395971 0.193738 0.0584453   0.0201601   -0.0405407  198 THR   A OG1  
1548 C  CG2  . THR   A 198 ? 0.182925  0.397854 0.188589 0.0464431   -0.0048902  -0.0408515  198 THR   A CG2  
1549 N  N    . THR   A 199 ? 0.0914775 0.284713 0.166365 0.00856646  0.0286576   -0.00936768 199 THR   A N    
1550 C  CA   . THR   A 199 ? 0.10567   0.284714 0.157265 0.00829848  0.028746    -0.00720263 199 THR   A CA   
1551 C  C    . THR   A 199 ? 0.0965468 0.282551 0.151713 0.00798634  0.0204711   -0.00235224 199 THR   A C    
1552 O  O    . THR   A 199 ? 0.110057  0.281431 0.160147 0.00535905  0.0263103   -0.00291883 199 THR   A O    
1553 C  CB   . THR   A 199 ? 0.10195   0.287734 0.173841 0.0102305   0.0278764   -0.0069492  199 THR   A CB   
1554 O  OG1  . THR   A 199 ? 0.11966   0.302191 0.200676 0.0100566   0.0199001   -0.00406309 199 THR   A OG1  
1555 C  CG2  . THR   A 199 ? 0.0971174 0.292967 0.182989 0.00714681  0.0333594   -0.00960467 199 THR   A CG2  
1556 N  N    . ILE   A 200 ? 0.0993371 0.276993 0.139495 0.00369933  0.0170566   0.002905    200 ILE   A N    
1557 C  CA   . ILE   A 200 ? 0.0941701 0.273911 0.136447 0.00616745  0.0121617   0.00112851  200 ILE   A CA   
1558 C  C    . ILE   A 200 ? 0.0885001 0.270099 0.136261 0.0102991   0.0199081   0.00514822  200 ILE   A C    
1559 O  O    . ILE   A 200 ? 0.0762345 0.275111 0.142673 0.0109767   0.0131972   0.00789586  200 ILE   A O    
1560 C  CB   . ILE   A 200 ? 0.0953105 0.277182 0.142925 0.0041803   0.0153775   0.00224681  200 ILE   A CB   
1561 C  CG1  . ILE   A 200 ? 0.0994991 0.275964 0.164354 0.00199956  0.0229212   0.00421237  200 ILE   A CG1  
1562 C  CG2  . ILE   A 200 ? 0.0966515 0.280189 0.140146 7.21e-05    0.0188993   0.00657829  200 ILE   A CG2  
1563 C  CD1  . ILE   A 200 ? 0.0957031 0.272793 0.16955  0.00232044  0.0275373   0.0122339   200 ILE   A CD1  
1564 N  N    . THR   A 201 ? 0.0906613 0.265652 0.134489 0.0105851   0.0181608   0.0085547   201 THR   A N    
1565 C  CA   . THR   A 201 ? 0.0901657 0.258636 0.141763 0.0166457   0.0248477   0.0108914   201 THR   A CA   
1566 C  C    . THR   A 201 ? 0.0832171 0.256047 0.144377 0.0148291   0.0194147   0.0123273   201 THR   A C    
1567 O  O    . THR   A 201 ? 0.0791653 0.264895 0.154074 0.0109585   0.0135047   0.0205193   201 THR   A O    
1568 C  CB   . THR   A 201 ? 0.103243  0.264216 0.145778 0.0180408   0.0303376   0.00914201  201 THR   A CB   
1569 O  OG1  . THR   A 201 ? 0.123728  0.264444 0.154564 0.0156254   0.0295713   0.00560673  201 THR   A OG1  
1570 C  CG2  . THR   A 201 ? 0.102142  0.275158 0.155266 0.021032    0.0301772   0.00901512  201 THR   A CG2  
1571 N  N    . VAL   A 202 ? 0.0671391 0.259274 0.154922 0.0149499   0.0189823   0.00601539  202 VAL   A N    
1572 C  CA   . VAL   A 202 ? 0.0832256 0.252799 0.164995 0.00765951  0.02802     0.0122004   202 VAL   A CA   
1573 C  C    . VAL   A 202 ? 0.0860628 0.245635 0.163428 0.00879757  0.0218678   0.012391    202 VAL   A C    
1574 O  O    . VAL   A 202 ? 0.0946561 0.255265 0.155679 0.0043863   0.0208769   0.0100624   202 VAL   A O    
1575 C  CB   . VAL   A 202 ? 0.0916618 0.257036 0.177089 0.0126534   0.0240524   0.00976799  202 VAL   A CB   
1576 C  CG1  . VAL   A 202 ? 0.0962317 0.273818 0.18898  0.0101682   0.0301399   0.00415019  202 VAL   A CG1  
1577 C  CG2  . VAL   A 202 ? 0.107825  0.263713 0.184211 0.0177763   0.00979591  0.0106029   202 VAL   A CG2  
1578 N  N    . ASN   A 203 ? 0.0791158 0.246717 0.156748 0.00734302  0.019081    0.014239    203 ASN   A N    
1579 C  CA   . ASN   A 203 ? 0.0801971 0.243857 0.149997 0.00617301  0.0227105   0.0135147   203 ASN   A CA   
1580 C  C    . ASN   A 203 ? 0.07642   0.246227 0.153046 0.00420215  0.0217456   0.0133461   203 ASN   A C    
1581 O  O    . ASN   A 203 ? 0.0849638 0.26363  0.152849 0.00261441  0.0234519   0.00152774  203 ASN   A O    
1582 C  CB   . ASN   A 203 ? 0.0861887 0.241449 0.143098 0.00527551  0.0224636   0.0191462   203 ASN   A CB   
1583 C  CG   . ASN   A 203 ? 0.0919096 0.239076 0.143292 0.00564     0.0218173   0.0243308   203 ASN   A CG   
1584 O  OD1  . ASN   A 203 ? 0.0893717 0.24493  0.152571 0.00638917  0.027536    0.0168343   203 ASN   A OD1  
1585 N  ND2  . ASN   A 203 ? 0.0851201 0.232851 0.171821 0.00822304  0.0173034   0.027904    203 ASN   A ND2  
1586 N  N    . VAL   A 204 ? 0.0748766 0.239692 0.155681 0.0107361   0.0120728   0.00911828  204 VAL   A N    
1587 C  CA   . VAL   A 204 ? 0.0713299 0.236483 0.158683 0.0101376   0.016321    0.00951969  204 VAL   A CA   
1588 C  C    . VAL   A 204 ? 0.0760821 0.230089 0.157832 0.0136691   0.0121148   0.0146843   204 VAL   A C    
1589 O  O    . VAL   A 204 ? 0.0712736 0.241173 0.150525 0.0131532   0.0117834   0.016792    204 VAL   A O    
1590 C  CB   . VAL   A 204 ? 0.0821449 0.236581 0.161988 0.0117846   0.0204831   0.00591448  204 VAL   A CB   
1591 C  CG1  . VAL   A 204 ? 0.081434  0.240695 0.166509 0.0114069   0.0192781   0.00216575  204 VAL   A CG1  
1592 C  CG2  . VAL   A 204 ? 0.0896571 0.241864 0.164412 0.00787716  0.00896221  -0.00185639 204 VAL   A CG2  
1593 N  N    . LEU   A 205 ? 0.0784595 0.233674 0.148511 0.0139929   0.00807216  0.0143041   205 LEU   A N    
1594 C  CA   . LEU   A 205 ? 0.0780032 0.243245 0.15415  0.0128773   0.0147521   0.0126025   205 LEU   A CA   
1595 C  C    . LEU   A 205 ? 0.0832437 0.243201 0.153153 0.0166202   0.012588    0.0116514   205 LEU   A C    
1596 O  O    . LEU   A 205 ? 0.094676  0.254014 0.155033 0.0108849   0.00479995  0.00476526  205 LEU   A O    
1597 C  CB   . LEU   A 205 ? 0.087157  0.247998 0.153125 0.0150837   0.0213868   0.0113917   205 LEU   A CB   
1598 C  CG   . LEU   A 205 ? 0.0893146 0.255736 0.154448 0.0154325   0.019393    0.0105558   205 LEU   A CG   
1599 C  CD1  . LEU   A 205 ? 0.0916671 0.26763  0.161453 0.0162215   0.0154159   0.015594    205 LEU   A CD1  
1600 C  CD2  . LEU   A 205 ? 0.0895896 0.267053 0.162227 0.0147156   0.0135782   0.0127974   205 LEU   A CD2  
1601 N  N    . ALA   A 206 ? 0.0787276 0.250931 0.153532 0.0190071   0.0102175   0.00446641  206 ALA   A N    
1602 C  CA   . ALA   A 206 ? 0.0885859 0.246836 0.158943 0.0196682   0.0160799   0.00832984  206 ALA   A CA   
1603 C  C    . ALA   A 206 ? 0.0832964 0.251632 0.148137 0.0152982   0.0152517   0.00715039  206 ALA   A C    
1604 O  O    . ALA   A 206 ? 0.07819   0.258296 0.155785 0.0159851   0.0153592   0.00187898  206 ALA   A O    
1605 C  CB   . ALA   A 206 ? 0.0902271 0.252095 0.161894 0.0256652   0.0116432   0.00927789  206 ALA   A CB   
1606 N  N    . TRP   A 207 ? 0.0892546 0.25273  0.147767 0.0099326   0.0023803   0.0111968   207 TRP   A N    
1607 C  CA   . TRP   A 207 ? 0.0839524 0.252702 0.1533   0.00725672  0.00190854  0.0106917   207 TRP   A CA   
1608 C  C    . TRP   A 207 ? 0.0850937 0.251868 0.138462 0.00852535  0.00533394  0.0118478   207 TRP   A C    
1609 O  O    . TRP   A 207 ? 0.0992642 0.247345 0.139705 0.00165607  -0.00132596 0.00724761  207 TRP   A O    
1610 C  CB   . TRP   A 207 ? 0.0900167 0.258456 0.165666 0.00279905  0.00367454  0.0144651   207 TRP   A CB   
1611 C  CG   . TRP   A 207 ? 0.0999467 0.263497 0.176561 -0.00481147 -0.00368425 0.0132246   207 TRP   A CG   
1612 C  CD1  . TRP   A 207 ? 0.120569  0.276332 0.181445 -0.00902247 -0.00290857 0.0145069   207 TRP   A CD1  
1613 C  CD2  . TRP   A 207 ? 0.111846  0.270633 0.200307 -0.00144616 -0.0174611  0.0123786   207 TRP   A CD2  
1614 N  NE1  . TRP   A 207 ? 0.132252  0.282994 0.191813 -0.0127665  -0.0126     0.0289381   207 TRP   A NE1  
1615 C  CE2  . TRP   A 207 ? 0.12201   0.274783 0.211463 -0.0004382  -0.0216902  0.0123476   207 TRP   A CE2  
1616 C  CE3  . TRP   A 207 ? 0.0988792 0.281689 0.220379 -0.00297552 -0.010356   0.0019444   207 TRP   A CE3  
1617 C  CZ2  . TRP   A 207 ? 0.117199  0.281427 0.234119 0.00681364  -0.0211416  0.0177079   207 TRP   A CZ2  
1618 C  CZ3  . TRP   A 207 ? 0.120512  0.291874 0.245849 0.00885521  -0.00490216 0.00024318  207 TRP   A CZ3  
1619 C  CH2  . TRP   A 207 ? 0.112848  0.277541 0.244088 0.00946289  -0.0224524  0.00610221  207 TRP   A CH2  
1620 N  N    . LEU   A 208 ? 0.0871286 0.258299 0.132217 0.00814995  -0.00290776 0.0115118   208 LEU   A N    
1621 C  CA   . LEU   A 208 ? 0.090658  0.254063 0.143225 0.00938287  0.00455759  0.00604977  208 LEU   A CA   
1622 C  C    . LEU   A 208 ? 0.101071  0.251317 0.145011 0.00484962  0.00559842  0.00919812  208 LEU   A C    
1623 O  O    . LEU   A 208 ? 0.0992514 0.25894  0.153869 0.00504947  -0.00449996 0.00814567  208 LEU   A O    
1624 C  CB   . LEU   A 208 ? 0.0885271 0.264994 0.149409 0.00729225  0.0101604   0.00622634  208 LEU   A CB   
1625 C  CG   . LEU   A 208 ? 0.08921   0.267832 0.152698 0.0114104   0.0112349   0.00277754  208 LEU   A CG   
1626 C  CD1  . LEU   A 208 ? 0.102327  0.276689 0.157236 0.00878534  0.0162023   -0.00097894 208 LEU   A CD1  
1627 C  CD2  . LEU   A 208 ? 0.110358  0.271329 0.163092 0.0103704   0.0107453   0.00391644  208 LEU   A CD2  
1628 N  N    . TYR   A 209 ? 0.091785  0.240243 0.148083 0.00407873  0.00437468  0.00617472  209 TYR   A N    
1629 C  CA   . TYR   A 209 ? 0.097063  0.237114 0.160755 0.00061232  0.0015047   0.00705238  209 TYR   A CA   
1630 C  C    . TYR   A 209 ? 0.103353  0.244568 0.162867 -0.00333517 0.00127847  0.00070601  209 TYR   A C    
1631 O  O    . TYR   A 209 ? 0.114795  0.260982 0.169841 -0.00508645 -0.00951747 -0.00106041 209 TYR   A O    
1632 C  CB   . TYR   A 209 ? 0.100757  0.240816 0.162213 0.00603443  0.00685546  0.00760998  209 TYR   A CB   
1633 C  CG   . TYR   A 209 ? 0.102435  0.246839 0.171575 0.000516    0.0108205   0.0180185   209 TYR   A CG   
1634 C  CD1  . TYR   A 209 ? 0.104633  0.248797 0.174975 8.79e-05    0.00580978  0.0201175   209 TYR   A CD1  
1635 C  CD2  . TYR   A 209 ? 0.102443  0.250144 0.178697 -0.00279575 0.0104662   0.0231634   209 TYR   A CD2  
1636 C  CE1  . TYR   A 209 ? 0.105014  0.258474 0.180222 0.00150259  0.0177752   0.0221288   209 TYR   A CE1  
1637 C  CE2  . TYR   A 209 ? 0.1126    0.25615  0.179783 -0.00462039 0.00847626  0.0235176   209 TYR   A CE2  
1638 C  CZ   . TYR   A 209 ? 0.111962  0.254675 0.181496 -0.00059863 0.0150167   0.0193026   209 TYR   A CZ   
1639 O  OH   . TYR   A 209 ? 0.1237    0.262307 0.18729  0.00359754  0.0220462   0.0187901   209 TYR   A OH   
1640 N  N    . ALA   A 210 ? 0.0991253 0.242072 0.161678 -0.00218432 -0.00085789 0.00384854  210 ALA   A N    
1641 C  CA   . ALA   A 210 ? 0.11669   0.23528  0.159132 0.00026204  -0.00273915 -0.00286541 210 ALA   A CA   
1642 C  C    . ALA   A 210 ? 0.117698  0.237372 0.154878 0.00499649  -0.00399886 -0.00789365 210 ALA   A C    
1643 O  O    . ALA   A 210 ? 0.118025  0.247194 0.156809 -0.00097878 0.00040072  -0.0116735  210 ALA   A O    
1644 C  CB   . ALA   A 210 ? 0.114769  0.230861 0.160517 0.00419959  0.00614353  -0.00251613 210 ALA   A CB   
1645 N  N    . ALA   A 211 ? 0.0981295 0.235615 0.150761 0.00951846  -0.0112774  -0.00764682 211 ALA   A N    
1646 C  CA   . ALA   A 211 ? 0.107329  0.237045 0.158365 0.0114297   -0.00306492 0.00394171  211 ALA   A CA   
1647 C  C    . ALA   A 211 ? 0.114704  0.24059  0.151935 0.00970379  -0.0016914  -0.00139851 211 ALA   A C    
1648 O  O    . ALA   A 211 ? 0.10507   0.274491 0.150078 0.015431    0.00172691  0.00974014  211 ALA   A O    
1649 C  CB   . ALA   A 211 ? 0.100935  0.23627  0.166981 0.00618775  -0.00300844 0.00139349  211 ALA   A CB   
1650 N  N    . VAL   A 212 ? 0.107411  0.24383  0.160485 0.00513999  0.00067298  0.00326238  212 VAL   A N    
1651 C  CA   . VAL   A 212 ? 0.109848  0.239531 0.180217 0.00504755  -0.0027442  -0.00203041 212 VAL   A CA   
1652 C  C    . VAL   A 212 ? 0.114539  0.250674 0.177015 0.00377341  -0.00400468 -0.00621415 212 VAL   A C    
1653 O  O    . VAL   A 212 ? 0.112768  0.255362 0.174011 -0.00519462 -0.00265555 -0.00859907 212 VAL   A O    
1654 C  CB   . VAL   A 212 ? 0.102433  0.235514 0.189642 0.00778298  -0.00506321 0.00094581  212 VAL   A CB   
1655 C  CG1  . VAL   A 212 ? 0.117217  0.242246 0.195827 0.00110864  0.00075868  -0.00237106 212 VAL   A CG1  
1656 C  CG2  . VAL   A 212 ? 0.10341   0.24137  0.189302 0.00395013  -0.00010005 0.00504112  212 VAL   A CG2  
1657 N  N    . ILE   A 213 ? 0.103419  0.258189 0.186878 -0.00189692 -0.00842075 -0.0241654  213 ILE   A N    
1658 C  CA   . ILE   A 213 ? 0.109456  0.268513 0.196653 0.0120761   -0.00098942 -0.0247533  213 ILE   A CA   
1659 C  C    . ILE   A 213 ? 0.125074  0.280095 0.184998 0.0140307   -0.00601221 -0.0318561  213 ILE   A C    
1660 O  O    . ILE   A 213 ? 0.13183   0.297516 0.212352 0.013202    -0.0264206  -0.0468591  213 ILE   A O    
1661 C  CB   . ILE   A 213 ? 0.115518  0.265715 0.214383 0.0144959   0.0100885   -0.019253   213 ILE   A CB   
1662 C  CG1  . ILE   A 213 ? 0.134462  0.263375 0.229715 0.0185793   0.00750671  -0.0196384  213 ILE   A CG1  
1663 C  CG2  . ILE   A 213 ? 0.139706  0.269618 0.217524 0.00922779  0.0161716   -0.0130737  213 ILE   A CG2  
1664 C  CD1  . ILE   A 213 ? 0.142186  0.275784 0.245507 0.0189285   0.00620173  -0.0146338  213 ILE   A CD1  
1665 N  N    . ASN   A 214 ? 0.123549  0.28467  0.171607 0.0127839   -0.00098771 -0.0242835  214 ASN   A N    
1666 C  CA   . ASN   A 214 ? 0.143929  0.311742 0.174532 0.0177512   0.00685515  -0.0143939  214 ASN   A CA   
1667 C  C    . ASN   A 214 ? 0.140461  0.317762 0.17823  0.0188792   -0.00227426 -0.00627869 214 ASN   A C    
1668 O  O    . ASN   A 214 ? 0.171756  0.364803 0.178713 0.0249431   0.0137267   0.0165661   214 ASN   A O    
1669 C  CB   . ASN   A 214 ? 0.154627  0.317919 0.195071 0.0153206   0.0153238   -0.00851919 214 ASN   A CB   
1670 C  CG   . ASN   A 214 ? 0.186103  0.331996 0.242006 0.0271497   0.0379542   -0.00911023 214 ASN   A CG   
1671 O  OD1  . ASN   A 214 ? 0.189094  0.341488 0.281791 0.0339639   0.0532716   -0.00291276 214 ASN   A OD1  
1672 N  ND2  . ASN   A 214 ? 0.199543  0.361094 0.293893 0.0179696   0.0579143   -0.00260535 214 ASN   A ND2  
1673 N  N    . GLY   A 215 ? 0.129569  0.311495 0.173055 0.023388    -0.0110732  -0.00605571 215 GLY   A N    
1674 C  CA   . GLY   A 215 ? 0.130341  0.297963 0.180606 0.0315533   -0.0211056  -0.0108356  215 GLY   A CA   
1675 C  C    . GLY   A 215 ? 0.123277  0.305412 0.203482 0.0405158   -0.0151568  -0.0169881  215 GLY   A C    
1676 O  O    . GLY   A 215 ? 0.13508   0.345562 0.25957  0.0583154   -0.0498324  -0.0295473  215 GLY   A O    
1677 N  N    . ASP   A 216 ? 0.109731  0.284415 0.177003 0.037434    -0.00448468 -0.00555154 216 ASP   A N    
1678 C  CA   . ASP   A 216 ? 0.125637  0.308637 0.205244 0.0407376   0.00077151  -0.00903148 216 ASP   A CA   
1679 C  C    . ASP   A 216 ? 0.126553  0.29597  0.197437 0.0333433   -0.00138912 -0.0094045  216 ASP   A C    
1680 O  O    . ASP   A 216 ? 0.166226  0.312556 0.196121 0.0563816   -0.00109941 0.00799573  216 ASP   A O    
1681 C  CB   . ASP   A 216 ? 0.170647  0.340863 0.240563 0.0184107   0.0099409   -0.0186177  216 ASP   A CB   
1682 C  CG   . ASP   A 216 ? 0.206489  0.386772 0.296816 0.0439516   0.00390328  -0.022077   216 ASP   A CG   
1683 O  OD1  . ASP   A 216 ? 0.236587  0.419337 0.36623  0.049216    0.0369377   -0.038562   216 ASP   A OD1  
1684 O  OD2  . ASP   A 216 ? 0.27413   0.445611 0.358412 0.0301281   0.0124788   -0.0315413  216 ASP   A OD2  
1685 N  N    . ARG   A 217 ? 0.117917  0.292028 0.188452 0.0316309   -0.00052821 0.00886869  217 ARG   A N    
1686 C  CA   . ARG   A 217 ? 0.113112  0.300369 0.196613 0.0178937   0.00407774  0.00387431  217 ARG   A CA   
1687 C  C    . ARG   A 217 ? 0.111916  0.298126 0.186625 0.021085    -0.0136488  0.00289506  217 ARG   A C    
1688 O  O    . ARG   A 217 ? 0.104064  0.314819 0.186228 0.0233402   -0.00773536 -0.00226144 217 ARG   A O    
1689 C  CB   . ARG   A 217 ? 0.12941   0.299261 0.213307 0.0120063   0.023889    0.0112635   217 ARG   A CB   
1690 C  CG   . ARG   A 217 ? 0.149858  0.298041 0.225072 0.0125769   0.0207461   0.0124676   217 ARG   A CG   
1691 C  CD   . ARG   A 217 ? 0.150473  0.288465 0.22468  0.0157468   0.0216496   0.0148504   217 ARG   A CD   
1692 N  NE   . ARG   A 217 ? 0.125856  0.275881 0.224141 0.0261659   0.0271347   0.00406586  217 ARG   A NE   
1693 C  CZ   . ARG   A 217 ? 0.120497  0.26874  0.220524 0.0254472   0.0163568   0.00097645  217 ARG   A CZ   
1694 N  NH1  . ARG   A 217 ? 0.130265  0.271151 0.223602 0.0275435   0.0168511   -0.00309564 217 ARG   A NH1  
1695 N  NH2  . ARG   A 217 ? 0.132266  0.270122 0.233011 0.0199602   0.0239146   0.00228463  217 ARG   A NH2  
1696 N  N    . TRP   A 218 ? 0.10773   0.288162 0.179892 0.0306694   -0.00189697 -0.00649945 218 TRP   A N    
1697 C  CA   . TRP   A 218 ? 0.120484  0.285078 0.184709 0.0356392   0.00012344  -0.0106913  218 TRP   A CA   
1698 C  C    . TRP   A 218 ? 0.106126  0.276529 0.17613  0.0338341   0.00323905  -0.00618717 218 TRP   A C    
1699 O  O    . TRP   A 218 ? 0.0935724 0.284939 0.18573  0.0223603   0.010337    -0.0101691  218 TRP   A O    
1700 C  CB   . TRP   A 218 ? 0.133561  0.289549 0.194872 0.0503797   0.00157157  -0.00083908 218 TRP   A CB   
1701 C  CG   . TRP   A 218 ? 0.132254  0.299099 0.213397 0.0540655   0.0166119   0.0158958   218 TRP   A CG   
1702 C  CD1  . TRP   A 218 ? 0.149023  0.313763 0.22969  0.0600769   0.0223238   0.0273799   218 TRP   A CD1  
1703 C  CD2  . TRP   A 218 ? 0.105902  0.292901 0.240028 0.0496507   0.0118339   0.0199923   218 TRP   A CD2  
1704 N  NE1  . TRP   A 218 ? 0.140335  0.326029 0.246092 0.0681025   0.0377962   0.0272758   218 TRP   A NE1  
1705 C  CE2  . TRP   A 218 ? 0.123144  0.310256 0.248161 0.0423269   0.014336    0.0222721   218 TRP   A CE2  
1706 C  CE3  . TRP   A 218 ? 0.130484  0.297474 0.249808 0.0353586   0.00634239  0.022572    218 TRP   A CE3  
1707 C  CZ2  . TRP   A 218 ? 0.136935  0.308139 0.254876 0.0376406   0.00503623  0.0253643   218 TRP   A CZ2  
1708 C  CZ3  . TRP   A 218 ? 0.146264  0.299561 0.253161 0.037525    0.00541713  0.0182895   218 TRP   A CZ3  
1709 C  CH2  . TRP   A 218 ? 0.13711   0.303488 0.261142 0.0322485   -0.00931777 0.0210057   218 TRP   A CH2  
1710 N  N    . PHE   A 219 ? 0.0961167 0.286045 0.169653 0.0228146   0.00460702  -0.00557256 219 PHE   A N    
1711 C  CA   . PHE   A 219 ? 0.0888435 0.287566 0.174937 0.0229252   0.00253606  -0.0105459  219 PHE   A CA   
1712 C  C    . PHE   A 219 ? 0.0745805 0.293187 0.164015 0.0264873   0.00577202  -0.0134174  219 PHE   A C    
1713 O  O    . PHE   A 219 ? 0.101233  0.328766 0.162023 0.0122194   -0.003074   0.00450754  219 PHE   A O    
1714 C  CB   . PHE   A 219 ? 0.0870049 0.27957  0.187849 0.021845    0.00415308  -0.00961213 219 PHE   A CB   
1715 C  CG   . PHE   A 219 ? 0.0867829 0.27164  0.187581 0.0167947   0.00680078  -0.00616933 219 PHE   A CG   
1716 C  CD1  . PHE   A 219 ? 0.0903842 0.269518 0.192641 0.0117198   0.0144391   -0.00284194 219 PHE   A CD1  
1717 C  CD2  . PHE   A 219 ? 0.103339  0.265664 0.19342  0.0231462   0.00768539  -0.00038578 219 PHE   A CD2  
1718 C  CE1  . PHE   A 219 ? 0.0796586 0.263876 0.196122 0.019106    0.0185482   0.0045885   219 PHE   A CE1  
1719 C  CE2  . PHE   A 219 ? 0.0980927 0.267789 0.189052 0.0179231   0.0170599   -0.00371739 219 PHE   A CE2  
1720 C  CZ   . PHE   A 219 ? 0.0870981 0.274132 0.199118 0.0219772   0.0214626   0.00115311  219 PHE   A CZ   
1721 N  N    . LEU   A 220 ? 0.0746151 0.284912 0.173012 0.0323855   -0.00349868 -0.00767959 220 LEU   A N    
1722 C  CA   . LEU   A 220 ? 0.0919297 0.294283 0.173975 0.0343538   -0.00597881 -0.00332899 220 LEU   A CA   
1723 C  C    . LEU   A 220 ? 0.0830346 0.292343 0.181193 0.0364852   -0.00624609 0.0049201   220 LEU   A C    
1724 O  O    . LEU   A 220 ? 0.0998117 0.299223 0.19316  0.0434012   -0.00076965 0.0080823   220 LEU   A O    
1725 C  CB   . LEU   A 220 ? 0.0962378 0.292258 0.19063  0.0359536   -0.0102667  0.00224827  220 LEU   A CB   
1726 C  CG   . LEU   A 220 ? 0.104618  0.303739 0.203761 0.0407232   -0.0137832  -0.00867414 220 LEU   A CG   
1727 C  CD1  . LEU   A 220 ? 0.115114  0.313645 0.232451 0.0430325   -0.0172577  -0.012611   220 LEU   A CD1  
1728 C  CD2  . LEU   A 220 ? 0.106109  0.317046 0.224442 0.0481706   -0.0115684  -0.0062893  220 LEU   A CD2  
1729 N  N    . ASN   A 221 ? 0.098212  0.305413 0.185817 0.034705    0.00806684  0.0106679   221 ASN   A N    
1730 C  CA   . ASN   A 221 ? 0.0928193 0.305477 0.195762 0.0273327   0.00271328  0.00685985  221 ASN   A CA   
1731 C  C    . ASN   A 221 ? 0.098503  0.306892 0.196005 0.0216971   -0.0052568  0.0107434   221 ASN   A C    
1732 O  O    . ASN   A 221 ? 0.104229  0.318048 0.186865 0.020058    -0.00198063 0.00923627  221 ASN   A O    
1733 C  CB   . ASN   A 221 ? 0.0938567 0.306993 0.213382 0.0240533   0.00066279  0.00551697  221 ASN   A CB   
1734 C  CG   . ASN   A 221 ? 0.11464   0.317462 0.248377 0.0206125   -0.0241032  0.00170052  221 ASN   A CG   
1735 O  OD1  . ASN   A 221 ? 0.102839  0.32116  0.22244  0.0131346   -0.0159147  0.00582595  221 ASN   A OD1  
1736 N  ND2  . ASN   A 221 ? 0.146809  0.349203 0.359686 0.00957787  -0.0692123  0.00258315  221 ASN   A ND2  
1737 N  N    . ARG   A 222 ? 0.101893  0.304649 0.212452 0.0235125   0.00746693  0.00652742  222 ARG   A N    
1738 C  CA   . ARG   A 222 ? 0.113536  0.320708 0.224074 0.00352546  0.00035587  0.0135648   222 ARG   A CA   
1739 C  C    . ARG   A 222 ? 0.108727  0.329602 0.226755 7.944e-05   0.0017858   0.0231865   222 ARG   A C    
1740 O  O    . ARG   A 222 ? 0.144625  0.34178  0.259783 -0.00870778 -0.00554801 0.0380898   222 ARG   A O    
1741 C  CB   . ARG   A 222 ? 0.10953   0.327291 0.234437 0.00297089  7.791e-05   0.0149284   222 ARG   A CB   
1742 C  CG   . ARG   A 222 ? 0.144903  0.347389 0.252941 0.0136675   0.0129589   0.0121029   222 ARG   A CG   
1743 C  CD   . ARG   A 222 ? 0.159418  0.360945 0.268894 0.0266334   0.0200387   0.0137805   222 ARG   A CD   
1744 N  NE   . ARG   A 222 ? 0.210847  0.393153 0.303113 0.023696    0.0214515   0.0263003   222 ARG   A NE   
1745 C  CZ   . ARG   A 222 ? 0.238679  0.406337 0.316824 0.0221141   0.0442002   0.0343339   222 ARG   A CZ   
1746 N  NH1  . ARG   A 222 ? 0.273856  0.422777 0.298558 0.0427468   0.0344196   0.0313764   222 ARG   A NH1  
1747 N  NH2  . ARG   A 222 ? 0.299977  0.425315 0.348138 0.00908212  0.0548159   0.054212    222 ARG   A NH2  
1748 N  N    . PHE   A 223 ? 0.11227   0.352972 0.202174 -0.00085597 0.00072851  0.016345    223 PHE   A N    
1749 C  CA   . PHE   A 223 ? 0.126487  0.384125 0.203122 0.00863645  0.00501963  0.012991    223 PHE   A CA   
1750 C  C    . PHE   A 223 ? 0.116033  0.391479 0.205189 0.00545394  0.00622584  0.0230522   223 PHE   A C    
1751 O  O    . PHE   A 223 ? 0.134042  0.363797 0.201129 0.00611432  0.006483    0.023842    223 PHE   A O    
1752 C  CB   . PHE   A 223 ? 0.148809  0.392614 0.220545 0.00856663  0.0143499   -0.00768086 223 PHE   A CB   
1753 C  CG   . PHE   A 223 ? 0.161891  0.425993 0.258516 0.0169067   0.0168694   -0.0406528  223 PHE   A CG   
1754 C  CD1  . PHE   A 223 ? 0.19751   0.452508 0.289602 0.020307    0.0433236   -0.0456751  223 PHE   A CD1  
1755 C  CD2  . PHE   A 223 ? 0.16352   0.428436 0.320515 0.023929    0.0501983   -0.0531605  223 PHE   A CD2  
1756 C  CE1  . PHE   A 223 ? 0.221976  0.462257 0.322057 0.0340367   0.0538842   -0.0497047  223 PHE   A CE1  
1757 C  CE2  . PHE   A 223 ? 0.215091  0.429989 0.350611 0.0419447   0.0520523   -0.0626964  223 PHE   A CE2  
1758 C  CZ   . PHE   A 223 ? 0.232245  0.435026 0.361196 0.03396     0.0541039   -0.0585718  223 PHE   A CZ   
1759 N  N    . THR   A 224 ? 0.125076  0.415851 0.221585 0.00679529  0.0049364   0.0366266   224 THR   A N    
1760 C  CA   . THR   A 224 ? 0.147363  0.403197 0.221445 0.0121461   -0.00709352 0.0423237   224 THR   A CA   
1761 C  C    . THR   A 224 ? 0.144896  0.377948 0.221182 0.0062919   0.0135262   0.033416    224 THR   A C    
1762 O  O    . THR   A 224 ? 0.14256   0.386307 0.229582 0.0276506   -0.00915812 0.0316507   224 THR   A O    
1763 C  CB   . THR   A 224 ? 0.174176  0.424139 0.252225 -0.00235012 -0.00645421 0.0393427   224 THR   A CB   
1764 O  OG1  . THR   A 224 ? 0.186196  0.432846 0.280244 0.00488507  -0.0258171  0.0297075   224 THR   A OG1  
1765 C  CG2  . THR   A 224 ? 0.194998  0.433804 0.267705 -0.0200122  -0.0004693  0.0491609   224 THR   A CG2  
1766 N  N    . THR   A 225 ? 0.143912  0.349101 0.185968 0.0076375   0.0136578   0.0239781   225 THR   A N    
1767 C  CA   . THR   A 225 ? 0.14243   0.324828 0.175118 0.0129905   0.0179709   0.0177013   225 THR   A CA   
1768 C  C    . THR   A 225 ? 0.135953  0.314123 0.187484 0.00901436  0.0246745   0.0145755   225 THR   A C    
1769 O  O    . THR   A 225 ? 0.167685  0.315892 0.184411 0.00626459  0.0104133   0.00865136  225 THR   A O    
1770 C  CB   . THR   A 225 ? 0.151437  0.326893 0.173614 0.00816286  0.0188802   0.0168156   225 THR   A CB   
1771 O  OG1  . THR   A 225 ? 0.141723  0.311209 0.176594 0.00730828  0.0289024   0.0167758   225 THR   A OG1  
1772 C  CG2  . THR   A 225 ? 0.151594  0.341054 0.176499 0.00056763  0.0130991   0.0164634   225 THR   A CG2  
1773 N  N    . THR   A 226 ? 0.130701  0.300298 0.180346 0.0183728   0.0288879   0.018356    226 THR   A N    
1774 C  CA   . THR   A 226 ? 0.131316  0.295199 0.185181 0.0178611   0.0237651   0.0257893   226 THR   A CA   
1775 C  C    . THR   A 226 ? 0.137636  0.28067  0.182564 0.0173936   0.0289179   0.0304992   226 THR   A C    
1776 O  O    . THR   A 226 ? 0.125931  0.272779 0.176564 0.021968    0.0226508   0.0210841   226 THR   A O    
1777 C  CB   . THR   A 226 ? 0.159163  0.297779 0.193821 0.0140909   0.0309962   0.0289041   226 THR   A CB   
1778 O  OG1  . THR   A 226 ? 0.140429  0.294953 0.195604 0.0133055   0.029855    0.0330128   226 THR   A OG1  
1779 C  CG2  . THR   A 226 ? 0.164901  0.300184 0.202182 0.00949125  0.0299823   0.0325442   226 THR   A CG2  
1780 N  N    . LEU   A 227 ? 0.140291  0.28375  0.18672  0.025029    0.0277126   0.0256034   227 LEU   A N    
1781 C  CA   . LEU   A 227 ? 0.144374  0.29064  0.187601 0.0246558   0.0372562   0.0283503   227 LEU   A CA   
1782 C  C    . LEU   A 227 ? 0.136237  0.290508 0.182558 0.0337327   0.0326332   0.026183    227 LEU   A C    
1783 O  O    . LEU   A 227 ? 0.121813  0.29554  0.191844 0.0384474   0.0357946   0.0296718   227 LEU   A O    
1784 C  CB   . LEU   A 227 ? 0.165018  0.290397 0.204607 0.0235184   0.0365784   0.0230006   227 LEU   A CB   
1785 C  CG   . LEU   A 227 ? 0.161954  0.298477 0.226315 0.023939    0.0327961   0.0194545   227 LEU   A CG   
1786 C  CD1  . LEU   A 227 ? 0.165327  0.299231 0.226676 0.026822    0.0447133   0.0225463   227 LEU   A CD1  
1787 C  CD2  . LEU   A 227 ? 0.17182   0.298547 0.238449 0.0286916   0.0300288   0.0202271   227 LEU   A CD2  
1788 N  N    A ASN   A 228 ? 0.14118   0.303364 0.178426 0.0331748   0.0344442   0.0241632   228 ASN   A N    
1789 N  N    B ASN   A 228 ? 0.138927  0.297775 0.176311 0.0287225   0.0261618   0.0260726   228 ASN   A N    
1790 C  CA   A ASN   A 228 ? 0.146382  0.313431 0.183085 0.0349041   0.0282641   0.0200557   228 ASN   A CA   
1791 C  CA   B ASN   A 228 ? 0.144196  0.305831 0.180177 0.0275965   0.0147902   0.0251358   228 ASN   A CA   
1792 C  C    A ASN   A 228 ? 0.132072  0.304545 0.177344 0.0269654   0.0286166   0.0214562   228 ASN   A C    
1793 C  C    B ASN   A 228 ? 0.132876  0.300866 0.176421 0.0233653   0.0210333   0.0242463   228 ASN   A C    
1794 O  O    A ASN   A 228 ? 0.130707  0.298343 0.174018 0.0307398   0.0288927   0.020891    228 ASN   A O    
1795 O  O    B ASN   A 228 ? 0.132616  0.299278 0.178112 0.0252423   0.020953    0.0232267   228 ASN   A O    
1796 C  CB   A ASN   A 228 ? 0.177432  0.331212 0.18664  0.0399124   0.0265818   0.0239212   228 ASN   A CB   
1797 C  CB   B ASN   A 228 ? 0.162073  0.313976 0.179623 0.0252549   0.00354078  0.0348711   228 ASN   A CB   
1798 C  CG   A ASN   A 228 ? 0.200538  0.354904 0.200404 0.0471038   0.00983559  0.0179985   228 ASN   A CG   
1799 C  CG   B ASN   A 228 ? 0.194027  0.326023 0.194575 0.0208892   -0.00965441 0.0317113   228 ASN   A CG   
1800 O  OD1  A ASN   A 228 ? 0.225792  0.375401 0.220433 0.0633021   0.0170382   0.0155792   228 ASN   A OD1  
1801 O  OD1  B ASN   A 228 ? 0.208591  0.352488 0.211573 0.0243762   -0.0221409  0.0295514   228 ASN   A OD1  
1802 N  ND2  A ASN   A 228 ? 0.211497  0.374883 0.197469 0.0383413   0.0106033   0.00830469  228 ASN   A ND2  
1803 N  ND2  B ASN   A 228 ? 0.212053  0.33164  0.184977 0.0166347   -0.0135323  0.0432215   228 ASN   A ND2  
1804 N  N    . ASP   A 229 ? 0.124912  0.296383 0.174869 0.0182417   0.037435    0.0179095   229 ASP   A N    
1805 C  CA   . ASP   A 229 ? 0.115329  0.299506 0.17236  0.0205348   0.0360038   0.0214497   229 ASP   A CA   
1806 C  C    . ASP   A 229 ? 0.106017  0.274809 0.176222 0.0142472   0.0356535   0.0171374   229 ASP   A C    
1807 O  O    . ASP   A 229 ? 0.12526   0.283264 0.185572 0.0133624   0.0539097   0.0299469   229 ASP   A O    
1808 C  CB   . ASP   A 229 ? 0.115337  0.314858 0.178024 0.0229251   0.0461487   0.0273173   229 ASP   A CB   
1809 C  CG   . ASP   A 229 ? 0.140691  0.330803 0.1801   0.0287389   0.0508968   0.0278438   229 ASP   A CG   
1810 O  OD1  . ASP   A 229 ? 0.148795  0.344755 0.19589  0.0282092   0.0467582   0.0155736   229 ASP   A OD1  
1811 O  OD2  . ASP   A 229 ? 0.134133  0.33042  0.195452 0.0356872   0.0504322   0.0342433   229 ASP   A OD2  
1812 N  N    . PHE   A 230 ? 0.112025  0.269834 0.164096 0.0127082   0.0351078   0.0239802   230 PHE   A N    
1813 C  CA   . PHE   A 230 ? 0.122893  0.277859 0.164734 0.0111844   0.0294854   0.0241859   230 PHE   A CA   
1814 C  C    . PHE   A 230 ? 0.122152  0.2792   0.165426 0.02012     0.0236727   0.0187122   230 PHE   A C    
1815 O  O    . PHE   A 230 ? 0.119394  0.278489 0.176394 0.0194598   0.0286659   0.0172907   230 PHE   A O    
1816 C  CB   . PHE   A 230 ? 0.124593  0.278369 0.166166 0.0125352   0.0280634   0.0286965   230 PHE   A CB   
1817 C  CG   . PHE   A 230 ? 0.128242  0.289442 0.164125 0.0148122   0.0267299   0.0329095   230 PHE   A CG   
1818 C  CD1  . PHE   A 230 ? 0.132177  0.293988 0.175271 0.0150962   0.0163854   0.0273088   230 PHE   A CD1  
1819 C  CD2  . PHE   A 230 ? 0.145075  0.293933 0.178827 0.0376777   0.036767    0.0331041   230 PHE   A CD2  
1820 C  CE1  . PHE   A 230 ? 0.141228  0.299181 0.171077 0.0176716   0.011153    0.033747    230 PHE   A CE1  
1821 C  CE2  . PHE   A 230 ? 0.141786  0.305587 0.181148 0.0297069   0.0442585   0.0323776   230 PHE   A CE2  
1822 C  CZ   . PHE   A 230 ? 0.149401  0.305989 0.172819 0.0210788   0.0333838   0.0308252   230 PHE   A CZ   
1823 N  N    . ASN   A 231 ? 0.109155  0.287452 0.164252 0.0202909   0.0242078   0.0138234   231 ASN   A N    
1824 C  CA   . ASN   A 231 ? 0.114902  0.303768 0.180842 0.0175135   0.0232079   0.0127433   231 ASN   A CA   
1825 C  C    . ASN   A 231 ? 0.106518  0.309221 0.169005 0.0174028   0.0296355   0.0124467   231 ASN   A C    
1826 O  O    . ASN   A 231 ? 0.125436  0.331006 0.178852 0.00507479  0.033715    0.0101736   231 ASN   A O    
1827 C  CB   . ASN   A 231 ? 0.114405  0.314079 0.19617  0.0257542   0.0244169   0.00505779  231 ASN   A CB   
1828 C  CG   . ASN   A 231 ? 0.135224  0.323288 0.201751 0.0331856   0.0282132   0.00325102  231 ASN   A CG   
1829 O  OD1  . ASN   A 231 ? 0.171577  0.336105 0.198162 0.062482    0.0341016   0.00304602  231 ASN   A OD1  
1830 N  ND2  . ASN   A 231 ? 0.165259  0.330467 0.231512 0.023229    0.0270757   0.00055877  231 ASN   A ND2  
1831 N  N    . LEU   A 232 ? 0.120247  0.299877 0.159658 0.0262284   0.0288415   0.00860779  232 LEU   A N    
1832 C  CA   . LEU   A 232 ? 0.132522  0.304729 0.164247 0.0227573   0.0278626   0.00778855  232 LEU   A CA   
1833 C  C    . LEU   A 232 ? 0.154611  0.298728 0.155435 0.0129601   0.0279474   0.0103152   232 LEU   A C    
1834 O  O    . LEU   A 232 ? 0.178451  0.307533 0.186453 0.0103056   0.00993404  0.00541975  232 LEU   A O    
1835 C  CB   . LEU   A 232 ? 0.134207  0.307568 0.164341 0.0273324   0.0279797   0.0154984   232 LEU   A CB   
1836 C  CG   . LEU   A 232 ? 0.154668  0.315713 0.174342 0.0327082   0.0260583   0.0192021   232 LEU   A CG   
1837 C  CD1  . LEU   A 232 ? 0.156132  0.319203 0.16415  0.0399165   0.026569    0.0216604   232 LEU   A CD1  
1838 C  CD2  . LEU   A 232 ? 0.165702  0.342159 0.188474 0.0265662   0.0196564   0.0229024   232 LEU   A CD2  
1839 N  N    . VAL   A 233 ? 0.135137  0.292853 0.158909 0.0115013   0.0339764   0.0105775   233 VAL   A N    
1840 C  CA   . VAL   A 233 ? 0.147701  0.291149 0.174956 0.00726807  0.0292733   0.0172823   233 VAL   A CA   
1841 C  C    . VAL   A 233 ? 0.147411  0.289791 0.164174 0.00336883  0.0246545   0.0135391   233 VAL   A C    
1842 O  O    . VAL   A 233 ? 0.136619  0.298518 0.16949  -0.00624147 0.0258617   0.0108416   233 VAL   A O    
1843 C  CB   . VAL   A 233 ? 0.142185  0.298055 0.192468 0.00759578  0.0316343   0.0324669   233 VAL   A CB   
1844 C  CG1  . VAL   A 233 ? 0.141327  0.303362 0.196752 0.0140447   0.0287378   0.0357553   233 VAL   A CG1  
1845 C  CG2  . VAL   A 233 ? 0.144785  0.300916 0.203044 0.0140407   0.0395593   0.0435362   233 VAL   A CG2  
1846 N  N    . ALA   A 234 ? 0.156729  0.296935 0.180765 -0.00791806 0.0514126   0.00058582  234 ALA   A N    
1847 C  CA   . ALA   A 234 ? 0.179001  0.311317 0.198487 -0.0165845  0.0697142   -0.00815905 234 ALA   A CA   
1848 C  C    . ALA   A 234 ? 0.154204  0.313517 0.19863  -0.00471577 0.0752482   -0.0100665  234 ALA   A C    
1849 O  O    . ALA   A 234 ? 0.154137  0.299386 0.20259  -0.00801437 0.0686439   -0.0113568  234 ALA   A O    
1850 C  CB   . ALA   A 234 ? 0.20274   0.31808  0.212922 -0.02903    0.0755125   -0.0192397  234 ALA   A CB   
1851 N  N    . MET   A 235 ? 0.148121  0.319235 0.215669 -0.00519322 0.0774613   0.00490943  235 MET   A N    
1852 C  CA   . MET   A 235 ? 0.143131  0.34682  0.240638 0.00937844  0.0595329   0.001622    235 MET   A CA   
1853 C  C    . MET   A 235 ? 0.13069   0.333563 0.206996 0.00211212  0.0461701   -0.00336584 235 MET   A C    
1854 O  O    . MET   A 235 ? 0.141397  0.337431 0.208398 -0.00506363 0.0330899   0.00067061  235 MET   A O    
1855 C  CB   . MET   A 235 ? 0.175587  0.391927 0.279116 0.0137737   0.0585852   0.0271967   235 MET   A CB   
1856 C  CG   . MET   A 235 ? 0.228765  0.433464 0.356142 0.0346254   0.0642928   0.034111    235 MET   A CG   
1857 S  SD   . MET   A 235 ? 0.34566   0.547688 0.457717 0.0846667   0.0930313   0.0973968   235 MET   A SD   
1858 C  CE   . MET   A 235 ? 0.361281  0.538226 0.456614 0.0678361   0.0765152   0.0690268   235 MET   A CE   
1859 N  N    . LYS   A 236 ? 0.136716  0.325637 0.196012 0.00733498  0.0381721   -0.0162781  236 LYS   A N    
1860 C  CA   . LYS   A 236 ? 0.156609  0.323438 0.19909  0.0136216   0.0259366   -0.0185149  236 LYS   A CA   
1861 C  C    . LYS   A 236 ? 0.154698  0.311476 0.195594 0.00940052  0.0272159   -0.0279805  236 LYS   A C    
1862 O  O    . LYS   A 236 ? 0.237493  0.325418 0.219754 -0.00099173 0.0337535   -0.039822   236 LYS   A O    
1863 C  CB   . LYS   A 236 ? 0.169655  0.345925 0.200798 0.0188095   0.0322484   -0.025275   236 LYS   A CB   
1864 C  CG   . LYS   A 236 ? 0.185042  0.363875 0.208915 0.0135788   0.0464598   -0.012206   236 LYS   A CG   
1865 C  CD   . LYS   A 236 ? 0.1781    0.390489 0.223682 0.0185157   0.0311655   -0.0111603  236 LYS   A CD   
1866 C  CE   . LYS   A 236 ? 0.185636  0.400616 0.238981 0.0196314   0.0512318   -0.00516427 236 LYS   A CE   
1867 N  NZ   . LYS   A 236 ? 0.170521  0.409796 0.269256 0.020268    0.036923    -0.0104904  236 LYS   A NZ   
1868 N  N    . TYR   A 237 ? 0.150164  0.293773 0.188989 0.0121359   0.0197234   -0.0237997  237 TYR   A N    
1869 C  CA   . TYR   A 237 ? 0.150937  0.29665  0.181295 0.00975357  0.0126474   -0.0238727  237 TYR   A CA   
1870 C  C    . TYR   A 237 ? 0.163789  0.303218 0.178205 0.0133207   0.0175006   -0.0281859  237 TYR   A C    
1871 O  O    . TYR   A 237 ? 0.171136  0.305516 0.181278 0.00135929  0.0331689   -0.0289248  237 TYR   A O    
1872 C  CB   . TYR   A 237 ? 0.144808  0.29449  0.180861 0.0256965   0.0148596   -0.0130659  237 TYR   A CB   
1873 C  CG   . TYR   A 237 ? 0.142036  0.29486  0.173977 0.0288566   0.0103993   -0.00520595 237 TYR   A CG   
1874 C  CD1  . TYR   A 237 ? 0.144304  0.298156 0.17992  0.0344945   0.0180108   0.00358878  237 TYR   A CD1  
1875 C  CD2  . TYR   A 237 ? 0.139     0.306329 0.178595 0.0460385   0.0166568   0.015015    237 TYR   A CD2  
1876 C  CE1  . TYR   A 237 ? 0.146698  0.296295 0.188242 0.0466734   0.0212396   0.0110156   237 TYR   A CE1  
1877 C  CE2  . TYR   A 237 ? 0.138089  0.312501 0.166737 0.0402796   0.0237875   0.0110271   237 TYR   A CE2  
1878 C  CZ   . TYR   A 237 ? 0.146118  0.31194  0.185127 0.0455109   0.028018    0.0154321   237 TYR   A CZ   
1879 O  OH   . TYR   A 237 ? 0.149814  0.344462 0.204353 0.05377     0.0344746   0.0279756   237 TYR   A OH   
1880 N  N    . ASN   A 238 ? 0.139421  0.30534  0.202141 0.0168312   0.0178373   -0.0252909  238 ASN   A N    
1881 C  CA   . ASN   A 238 ? 0.141772  0.320101 0.203772 0.00508244  0.0203082   -0.0256057  238 ASN   A CA   
1882 C  C    . ASN   A 238 ? 0.113846  0.293897 0.177156 0.00692319  0.0200509   -0.00641582 238 ASN   A C    
1883 O  O    . ASN   A 238 ? 0.112979  0.307154 0.187017 0.00199315  0.0263071   -0.0196887  238 ASN   A O    
1884 C  CB   . ASN   A 238 ? 0.190485  0.347501 0.247665 -0.00224109 0.015245    -0.0351081  238 ASN   A CB   
1885 C  CG   . ASN   A 238 ? 0.225876  0.421249 0.308814 0.00913374  -0.0102782  -0.0298008  238 ASN   A CG   
1886 O  OD1  . ASN   A 238 ? 0.280408  0.513991 0.372936 -0.00985863 -0.0652014  -0.00675825 238 ASN   A OD1  
1887 N  ND2  . ASN   A 238 ? 0.241348  0.463321 0.351234 0.00344525  -0.00192238 -0.0172006  238 ASN   A ND2  
1888 N  N    . TYR   A 239 ? 0.102471  0.275916 0.167649 0.0111286   0.0191648   -0.003025   239 TYR   A N    
1889 C  CA   . TYR   A 239 ? 0.108159  0.282531 0.155474 0.00836086  0.0194435   0.00192106  239 TYR   A CA   
1890 C  C    . TYR   A 239 ? 0.139662  0.292969 0.161787 0.0116895   0.0155174   0.0109767   239 TYR   A C    
1891 O  O    . TYR   A 239 ? 0.15828   0.312352 0.16168  0.0191071   0.0174334   0.0126556   239 TYR   A O    
1892 C  CB   . TYR   A 239 ? 0.10128   0.283184 0.1592   0.0080139   0.0238961   0.00498995  239 TYR   A CB   
1893 C  CG   . TYR   A 239 ? 0.0936216 0.28925  0.154073 0.00751516  0.0222198   0.00297001  239 TYR   A CG   
1894 C  CD1  . TYR   A 239 ? 0.102977  0.290964 0.162735 0.0148892   0.0143856   -0.0108012  239 TYR   A CD1  
1895 C  CD2  . TYR   A 239 ? 0.116826  0.291824 0.165999 0.00278832  0.0212136   -0.00416733 239 TYR   A CD2  
1896 C  CE1  . TYR   A 239 ? 0.10267   0.289981 0.177609 0.0293541   0.00990445  -0.00684383 239 TYR   A CE1  
1897 C  CE2  . TYR   A 239 ? 0.0957045 0.301321 0.17067  0.0151796   0.0127907   -0.00685006 239 TYR   A CE2  
1898 C  CZ   . TYR   A 239 ? 0.0959341 0.299893 0.161243 0.02948     0.00881222  -0.00257319 239 TYR   A CZ   
1899 O  OH   . TYR   A 239 ? 0.115299  0.321776 0.166143 0.0304304   -0.00163002 0.00420653  239 TYR   A OH   
1900 N  N    . GLU   A 240 ? 0.149083  0.290315 0.161172 0.0219902   0.0148783   0.0181867   240 GLU   A N    
1901 C  CA   . GLU   A 240 ? 0.168166  0.309148 0.179318 0.034575    0.00915927  0.0260507   240 GLU   A CA   
1902 C  C    . GLU   A 240 ? 0.18124   0.311724 0.175416 0.0349658   0.00578657  0.0271159   240 GLU   A C    
1903 O  O    . GLU   A 240 ? 0.147953  0.327698 0.16993  0.0274398   0.0234939   0.0361157   240 GLU   A O    
1904 C  CB   . GLU   A 240 ? 0.203138  0.329036 0.218444 0.0502867   0.0269482   0.0309255   240 GLU   A CB   
1905 C  CG   . GLU   A 240 ? 0.246143  0.36731  0.266836 0.0265379   0.016929    0.0241709   240 GLU   A CG   
1906 C  CD   . GLU   A 240 ? 0.258309  0.415207 0.290946 0.0446801   0.00511821  0.0157842   240 GLU   A CD   
1907 O  OE1  . GLU   A 240 ? 0.399205  0.447811 0.36203  0.0400673   -0.0156906  0.0141777   240 GLU   A OE1  
1908 O  OE2  . GLU   A 240 ? 0.357701  0.431072 0.351653 0.0457126   0.0466779   -0.00849043 240 GLU   A OE2  
1909 N  N    . PRO   A 241 ? 0.185311  0.321833 0.17805  0.0436201   0.00097348  0.022173    241 PRO   A N    
1910 C  CA   . PRO   A 241 ? 0.200655  0.316657 0.186405 0.0371924   0.00503775  0.0259032   241 PRO   A CA   
1911 C  C    . PRO   A 241 ? 0.170594  0.310782 0.179181 0.0376908   0.0261221   0.0286888   241 PRO   A C    
1912 O  O    . PRO   A 241 ? 0.164883  0.320449 0.226376 0.0295944   0.0446503   0.00722764  241 PRO   A O    
1913 C  CB   . PRO   A 241 ? 0.230525  0.333009 0.195148 0.0329021   -0.0131959  0.0284069   241 PRO   A CB   
1914 C  CG   . PRO   A 241 ? 0.214202  0.343531 0.203849 0.0301982   -0.0112483  0.0263951   241 PRO   A CG   
1915 C  CD   . PRO   A 241 ? 0.201346  0.338003 0.203056 0.0329282   -0.00993847 0.0192185   241 PRO   A CD   
1916 N  N    . LEU   A 242 ? 0.129486  0.308026 0.17265  0.0603505   0.0304164   0.0262941   242 LEU   A N    
1917 C  CA   . LEU   A 242 ? 0.118468  0.300273 0.183069 0.0583181   0.0317528   0.0262646   242 LEU   A CA   
1918 C  C    . LEU   A 242 ? 0.142208  0.306201 0.18907  0.0602457   0.0181118   0.0253629   242 LEU   A C    
1919 O  O    . LEU   A 242 ? 0.155825  0.31067  0.207167 0.0577727   0.04523     0.0330639   242 LEU   A O    
1920 C  CB   . LEU   A 242 ? 0.115591  0.315944 0.191028 0.0573571   0.0290579   0.0257749   242 LEU   A CB   
1921 C  CG   . LEU   A 242 ? 0.122159  0.308004 0.198029 0.0627302   0.0266796   0.0287335   242 LEU   A CG   
1922 C  CD1  . LEU   A 242 ? 0.139093  0.305529 0.198474 0.0672775   0.0267768   0.0230269   242 LEU   A CD1  
1923 C  CD2  . LEU   A 242 ? 0.12398   0.325746 0.202064 0.0579688   0.0248051   0.0366878   242 LEU   A CD2  
1924 N  N    . THR   A 243 ? 0.150385  0.301699 0.200123 0.0571214   0.0324799   0.0261208   243 THR   A N    
1925 C  CA   . THR   A 243 ? 0.155612  0.301031 0.212206 0.0597774   0.0187146   0.027426    243 THR   A CA   
1926 C  C    . THR   A 243 ? 0.167176  0.296636 0.219884 0.0528363   0.0270726   0.0310543   243 THR   A C    
1927 O  O    . THR   A 243 ? 0.148877  0.295344 0.201171 0.039332    0.0306682   0.0298424   243 THR   A O    
1928 C  CB   . THR   A 243 ? 0.162666  0.3089   0.217698 0.0636475   0.0159772   0.0291314   243 THR   A CB   
1929 O  OG1  . THR   A 243 ? 0.164409  0.320158 0.221827 0.074103    0.0159855   0.0146924   243 THR   A OG1  
1930 C  CG2  . THR   A 243 ? 0.172891  0.321706 0.216644 0.0553021   0.00894416  0.027242    243 THR   A CG2  
1931 N  N    . GLN   A 244 ? 0.177143  0.295821 0.226407 0.0467863   0.0254922   0.035627    244 GLN   A N    
1932 C  CA   . GLN   A 244 ? 0.190278  0.303673 0.252083 0.0411856   0.0173982   0.0268057   244 GLN   A CA   
1933 C  C    . GLN   A 244 ? 0.168817  0.295413 0.25939  0.0404818   0.0130287   0.0185441   244 GLN   A C    
1934 O  O    . GLN   A 244 ? 0.176722  0.300714 0.269885 0.024544    0.00473375  0.0124782   244 GLN   A O    
1935 C  CB   . GLN   A 244 ? 0.21113   0.313016 0.282985 0.0356249   0.0212491   0.0333643   244 GLN   A CB   
1936 C  CG   . GLN   A 244 ? 0.238417  0.329024 0.319564 0.0345786   0.0241288   0.0238154   244 GLN   A CG   
1937 C  CD   . GLN   A 244 ? 0.220916  0.353978 0.333264 0.0219666   0.041312    0.0144619   244 GLN   A CD   
1938 O  OE1  . GLN   A 244 ? 0.229493  0.377397 0.356628 0.0275348   0.0547519   0.00490715  244 GLN   A OE1  
1939 N  NE2  . GLN   A 244 ? 0.22607   0.377219 0.352991 0.0282072   0.0410071   0.0039611   244 GLN   A NE2  
1940 N  N    . ASP   A 245 ? 0.16303   0.317904 0.254258 0.0515014   0.00052013  0.0131957   245 ASP   A N    
1941 C  CA   . ASP   A 245 ? 0.169766  0.325951 0.262006 0.0588295   -0.00311667 0.00573731  245 ASP   A CA   
1942 C  C    . ASP   A 245 ? 0.138846  0.322518 0.249141 0.0632289   0.00765218  0.00136195  245 ASP   A C    
1943 O  O    . ASP   A 245 ? 0.169564  0.351764 0.25414  0.0839436   -0.00656969 -0.00166319 245 ASP   A O    
1944 C  CB   . ASP   A 245 ? 0.170356  0.330614 0.268333 0.0611414   -0.00280401 0.010866    245 ASP   A CB   
1945 C  CG   . ASP   A 245 ? 0.200328  0.343614 0.290703 0.0666864   -0.0127079  0.0190728   245 ASP   A CG   
1946 O  OD1  . ASP   A 245 ? 0.22596   0.36234  0.284413 0.0580727   -0.00529436 0.0105609   245 ASP   A OD1  
1947 O  OD2  . ASP   A 245 ? 0.207332  0.373911 0.36778  0.0730169   -0.0100181  0.0510298   245 ASP   A OD2  
1948 N  N    . HIS   A 246 ? 0.142624  0.322967 0.217202 0.0684678   0.00916784  0.00123688  246 HIS   A N    
1949 C  CA   . HIS   A 246 ? 0.142329  0.323118 0.20586  0.0756883   0.0213442   0.0025519   246 HIS   A CA   
1950 C  C    . HIS   A 246 ? 0.15232   0.337705 0.202813 0.069138    0.0160502   -0.00626166 246 HIS   A C    
1951 O  O    . HIS   A 246 ? 0.159076  0.34485  0.202305 0.0757769   0.00930602  -0.00110938 246 HIS   A O    
1952 C  CB   . HIS   A 246 ? 0.139496  0.311755 0.201426 0.0764461   0.0187807   0.0112929   246 HIS   A CB   
1953 C  CG   . HIS   A 246 ? 0.150875  0.314804 0.203654 0.0713046   0.0192065   0.0208188   246 HIS   A CG   
1954 N  ND1  . HIS   A 246 ? 0.163234  0.310296 0.223587 0.0564127   0.0186034   0.0221497   246 HIS   A ND1  
1955 C  CD2  . HIS   A 246 ? 0.169676  0.325282 0.211891 0.0683851   0.0368615   0.0151478   246 HIS   A CD2  
1956 C  CE1  . HIS   A 246 ? 0.168388  0.32934  0.229035 0.0436664   0.0211936   0.0200234   246 HIS   A CE1  
1957 N  NE2  . HIS   A 246 ? 0.17043   0.332591 0.215762 0.0560753   0.0269902   0.0241197   246 HIS   A NE2  
1958 N  N    . VAL   A 247 ? 0.140349  0.340029 0.203664 0.0682424   0.00597864  -0.00673776 247 VAL   A N    
1959 C  CA   . VAL   A 247 ? 0.133865  0.348127 0.224248 0.0730756   0.0134256   -0.0106755  247 VAL   A CA   
1960 C  C    . VAL   A 247 ? 0.151501  0.350603 0.243405 0.0870404   0.00453227  -0.023113   247 VAL   A C    
1961 O  O    . VAL   A 247 ? 0.164352  0.372301 0.256194 0.0764334   -0.00147156 -0.029037   247 VAL   A O    
1962 C  CB   . VAL   A 247 ? 0.144854  0.358125 0.225521 0.0605678   0.0171996   -0.00537842 247 VAL   A CB   
1963 C  CG1  . VAL   A 247 ? 0.155869  0.363814 0.23601  0.0562893   0.0173044   -0.01761    247 VAL   A CG1  
1964 C  CG2  . VAL   A 247 ? 0.139824  0.346637 0.232008 0.0596423   0.0195322   0.00810606  247 VAL   A CG2  
1965 N  N    . ASP   A 248 ? 0.15414   0.351614 0.266018 0.09225     -0.0150661  -0.0340539  248 ASP   A N    
1966 C  CA   . ASP   A 248 ? 0.16836   0.350217 0.276721 0.0995807   -0.0238623  -0.04284    248 ASP   A CA   
1967 C  C    . ASP   A 248 ? 0.162996  0.359625 0.274178 0.1084      -0.0232495  -0.0386618  248 ASP   A C    
1968 O  O    . ASP   A 248 ? 0.201433  0.3707   0.284095 0.105844    -0.0294286  -0.0529999  248 ASP   A O    
1969 C  CB   . ASP   A 248 ? 0.205963  0.3472   0.309433 0.10738     -0.0379849  -0.0396842  248 ASP   A CB   
1970 C  CG   . ASP   A 248 ? 0.251096  0.361166 0.320406 0.110489    -0.0497773  -0.0290367  248 ASP   A CG   
1971 O  OD1  . ASP   A 248 ? 0.272404  0.378465 0.346666 0.101442    -0.0362359  -0.00899853 248 ASP   A OD1  
1972 O  OD2  . ASP   A 248 ? 0.284833  0.406857 0.329972 0.105105    -0.0819646  -0.0225042  248 ASP   A OD2  
1973 N  N    . ILE   A 249 ? 0.183732  0.365495 0.265414 0.107025    -0.0149627  -0.0268394  249 ILE   A N    
1974 C  CA   . ILE   A 249 ? 0.169548  0.399183 0.275563 0.0991636   -0.00050414 -0.0192546  249 ILE   A CA   
1975 C  C    . ILE   A 249 ? 0.179001  0.373492 0.247817 0.096242    0.00085392  -0.0261522  249 ILE   A C    
1976 O  O    . ILE   A 249 ? 0.175807  0.420086 0.250842 0.0982409   0.0121158   -0.0212344  249 ILE   A O    
1977 C  CB   . ILE   A 249 ? 0.161088  0.478149 0.289501 0.0773735   0.00069099  -0.00443704 249 ILE   A CB   
1978 C  CG1  . ILE   A 249 ? 0.209435  0.508459 0.314344 0.0921201   -0.0157439  0.010365    249 ILE   A CG1  
1979 C  CG2  . ILE   A 249 ? 0.224289  0.50628  0.329903 0.0600614   -0.00660734 0.00542432  249 ILE   A CG2  
1980 C  CD1  . ILE   A 249 ? 0.243362  0.529321 0.342996 0.0689391   -0.00303992 0.00235728  249 ILE   A CD1  
1981 N  N    . LEU   A 250 ? 0.157088  0.352497 0.233563 0.0825602   0.00475059  -0.0132014  250 LEU   A N    
1982 C  CA   . LEU   A 250 ? 0.141862  0.320211 0.232469 0.0619743   0.00439697  -0.0152762  250 LEU   A CA   
1983 C  C    . LEU   A 250 ? 0.159102  0.317778 0.249657 0.0603284   0.00226324  -0.0218119  250 LEU   A C    
1984 O  O    . LEU   A 250 ? 0.163495  0.306593 0.250754 0.0574787   -0.00751598 -0.0226062  250 LEU   A O    
1985 C  CB   . LEU   A 250 ? 0.114275  0.311442 0.234385 0.0431687   0.00779002  -0.00988486 250 LEU   A CB   
1986 C  CG   . LEU   A 250 ? 0.0910504 0.313319 0.239023 0.036235    0.00909515  -0.00298385 250 LEU   A CG   
1987 C  CD1  . LEU   A 250 ? 0.0918805 0.302721 0.247912 0.034944    0.0137701   -0.00143278 250 LEU   A CD1  
1988 C  CD2  . LEU   A 250 ? 0.09745   0.338872 0.235825 0.0104815   0.0190813   -0.00255424 250 LEU   A CD2  
1989 N  N    . GLY   A 251 ? 0.166345  0.321589 0.267729 0.0574414   -0.0166261  -0.019879   251 GLY   A N    
1990 C  CA   . GLY   A 251 ? 0.190933  0.314097 0.279222 0.0508932   -0.0236048  -0.0295439  251 GLY   A CA   
1991 C  C    . GLY   A 251 ? 0.198801  0.313986 0.279033 0.0485012   -0.0234441  -0.0333766  251 GLY   A C    
1992 O  O    . GLY   A 251 ? 0.194593  0.285077 0.277226 0.0505617   -0.0278377  -0.0284023  251 GLY   A O    
1993 N  N    . PRO   A 252 ? 0.20382   0.309185 0.286143 0.0698696   -0.0268533  -0.0486236  252 PRO   A N    
1994 C  CA   . PRO   A 252 ? 0.200604  0.311087 0.278211 0.052592    -0.0140922  -0.0565111  252 PRO   A CA   
1995 C  C    . PRO   A 252 ? 0.174846  0.30874  0.244845 0.0403836   0.00079397  -0.0473485  252 PRO   A C    
1996 O  O    . PRO   A 252 ? 0.177752  0.305002 0.265701 0.0271538   -0.0115991  -0.0556886  252 PRO   A O    
1997 C  CB   . PRO   A 252 ? 0.220162  0.321724 0.293273 0.075341    -0.00900499 -0.0710923  252 PRO   A CB   
1998 C  CG   . PRO   A 252 ? 0.230275  0.318873 0.307665 0.0723413   -0.0131081  -0.0673765  252 PRO   A CG   
1999 C  CD   . PRO   A 252 ? 0.213175  0.322956 0.305445 0.0767915   -0.0140882  -0.0597012  252 PRO   A CD   
2000 N  N    . LEU   A 253 ? 0.14644   0.29845  0.221059 0.0304031   0.021216    -0.0206305  253 LEU   A N    
2001 C  CA   . LEU   A 253 ? 0.127976  0.293259 0.203597 0.0206427   0.0287354   -0.00797751 253 LEU   A CA   
2002 C  C    . LEU   A 253 ? 0.125744  0.283022 0.202113 0.0157933   0.0251318   -0.00390855 253 LEU   A C    
2003 O  O    . LEU   A 253 ? 0.133889  0.282923 0.207728 0.0164842   0.0125501   -0.00120108 253 LEU   A O    
2004 C  CB   . LEU   A 253 ? 0.131243  0.296391 0.2058   0.0158199   0.0322626   -0.00374974 253 LEU   A CB   
2005 C  CG   . LEU   A 253 ? 0.128067  0.311513 0.218729 0.0204098   0.0332542   0.00414289  253 LEU   A CG   
2006 C  CD1  . LEU   A 253 ? 0.125683  0.327425 0.22133  0.00962488  0.034223    0.011826    253 LEU   A CD1  
2007 C  CD2  . LEU   A 253 ? 0.141661  0.315349 0.221811 0.022441    0.0332593   -0.00176624 253 LEU   A CD2  
2008 N  N    . SER   A 254 ? 0.127484  0.274655 0.200891 0.0193747   0.0183958   -0.0007244  254 SER   A N    
2009 C  CA   . SER   A 254 ? 0.141902  0.280071 0.209604 0.0174896   0.0278581   -0.0050495  254 SER   A CA   
2010 C  C    . SER   A 254 ? 0.154872  0.275542 0.207612 0.0144105   0.0178446   -0.00145303 254 SER   A C    
2011 O  O    . SER   A 254 ? 0.159617  0.287932 0.227194 0.0129589   0.0028823   0.0125948   254 SER   A O    
2012 C  CB   . SER   A 254 ? 0.16297   0.293502 0.216346 0.0294381   0.0235603   -0.00267005 254 SER   A CB   
2013 O  OG   . SER   A 254 ? 0.16862   0.325642 0.235823 0.0300493   0.0274573   -0.00023809 254 SER   A OG   
2014 N  N    . ALA   A 255 ? 0.162959  0.274239 0.239685 0.0108646   -0.00322578 -0.00671425 255 ALA   A N    
2015 C  CA   . ALA   A 255 ? 0.192842  0.278889 0.259944 0.00649481  -0.00512687 -0.00573327 255 ALA   A CA   
2016 C  C    . ALA   A 255 ? 0.185179  0.286413 0.252715 -0.00559569 0.00013672  -0.00750987 255 ALA   A C    
2017 O  O    . ALA   A 255 ? 0.176409  0.316657 0.275079 -0.020863   -0.00094955 -0.0021588  255 ALA   A O    
2018 C  CB   . ALA   A 255 ? 0.22152   0.286976 0.273782 0.0185898   -0.00642119 -0.00871918 255 ALA   A CB   
2019 N  N    . GLN   A 256 ? 0.167674  0.290744 0.245727 0.00867907  0.00382643  -0.00659683 256 GLN   A N    
2020 C  CA   . GLN   A 256 ? 0.171868  0.305644 0.233769 0.00217203  0.014313    -0.0113392  256 GLN   A CA   
2021 C  C    . GLN   A 256 ? 0.158951  0.302231 0.224143 -0.00315418 0.0128851   -0.0114065  256 GLN   A C    
2022 O  O    . GLN   A 256 ? 0.174367  0.357468 0.252    -0.00061649 0.00132205  -0.024278   256 GLN   A O    
2023 C  CB   . GLN   A 256 ? 0.185324  0.318174 0.262319 0.00447907  0.0302825   -0.0087273  256 GLN   A CB   
2024 C  CG   . GLN   A 256 ? 0.196314  0.33444  0.272898 0.0087637   0.0287819   -0.0121418  256 GLN   A CG   
2025 C  CD   . GLN   A 256 ? 0.225451  0.341764 0.284827 0.00954159  0.0426853   -0.00729131 256 GLN   A CD   
2026 O  OE1  . GLN   A 256 ? 0.229771  0.396356 0.345792 0.0258715   0.049464    0.0242219   256 GLN   A OE1  
2027 N  NE2  . GLN   A 256 ? 0.232591  0.34944  0.276701 0.0103436   0.0454257   -0.00868715 256 GLN   A NE2  
2028 N  N    . THR   A 257 ? 0.147137  0.274172 0.218176 -0.00494296 0.00247349  -0.00632201 257 THR   A N    
2029 C  CA   . THR   A 257 ? 0.147797  0.275238 0.211615 -0.00354909 -0.00114738 -0.00046259 257 THR   A CA   
2030 C  C    . THR   A 257 ? 0.151732  0.264695 0.211561 -0.00459702 -0.00218534 -0.00094152 257 THR   A C    
2031 O  O    . THR   A 257 ? 0.158337  0.263861 0.235647 0.00409242  -0.00726376 0.0108675   257 THR   A O    
2032 C  CB   . THR   A 257 ? 0.139678  0.273527 0.196169 -0.0109366  -0.00574713 0.0100237   257 THR   A CB   
2033 O  OG1  . THR   A 257 ? 0.123108  0.274447 0.181615 -0.00540679 0.00556797  0.0131587   257 THR   A OG1  
2034 C  CG2  . THR   A 257 ? 0.147857  0.276603 0.193956 -0.00703581 -0.0005886  0.0118785   257 THR   A CG2  
2035 N  N    . GLY   A 258 ? 0.142257  0.265935 0.211621 -0.00113186 0.00079626  0.00027676  258 GLY   A N    
2036 C  CA   . GLY   A 258 ? 0.153594  0.277061 0.219898 -0.00944648 0.0037064   0.00975307  258 GLY   A CA   
2037 C  C    . GLY   A 258 ? 0.161956  0.285933 0.227431 -0.00365305 0.0137232   0.00659396  258 GLY   A C    
2038 O  O    . GLY   A 258 ? 0.173119  0.331415 0.264544 -0.0264772  0.0399903   -0.0021117  258 GLY   A O    
2039 N  N    . ILE   A 259 ? 0.135509  0.265213 0.20065  0.00914125  0.0151577   0.0120449   259 ILE   A N    
2040 C  CA   . ILE   A 259 ? 0.120168  0.268797 0.200349 0.00902298  0.00946756  0.0132237   259 ILE   A CA   
2041 C  C    . ILE   A 259 ? 0.114247  0.270175 0.18873  0.00474157  0.0105939   0.0101107   259 ILE   A C    
2042 O  O    . ILE   A 259 ? 0.113771  0.278595 0.201323 -0.00095917 0.0268004   0.00844788  259 ILE   A O    
2043 C  CB   . ILE   A 259 ? 0.122484  0.263629 0.204467 0.0145207   0.0057821   0.00941306  259 ILE   A CB   
2044 C  CG1  . ILE   A 259 ? 0.148409  0.2771   0.202984 0.0160936   -0.0059774  -0.00345256 259 ILE   A CG1  
2045 C  CG2  . ILE   A 259 ? 0.112593  0.26778  0.212237 0.00454372  0.00253679  0.0140525   259 ILE   A CG2  
2046 C  CD1  . ILE   A 259 ? 0.146852  0.289094 0.221916 0.00606767  -0.0019666  -0.00348872 259 ILE   A CD1  
2047 N  N    . ALA   A 260 ? 0.112418  0.275901 0.194064 0.00268946  0.0144117   0.0196084   260 ALA   A N    
2048 C  CA   . ALA   A 260 ? 0.116404  0.273373 0.1861   0.0110391   0.0208357   0.0229253   260 ALA   A CA   
2049 C  C    . ALA   A 260 ? 0.122247  0.267142 0.180126 0.0129819   0.0165768   0.0293554   260 ALA   A C    
2050 O  O    . ALA   A 260 ? 0.115327  0.268047 0.174865 0.0123174   0.0191391   0.0295101   260 ALA   A O    
2051 C  CB   . ALA   A 260 ? 0.13955   0.277398 0.190711 0.00226775  0.0209568   0.0312739   260 ALA   A CB   
2052 N  N    . VAL   A 261 ? 0.127757  0.278425 0.188793 0.023306    0.0153082   0.031412    261 VAL   A N    
2053 C  CA   . VAL   A 261 ? 0.125973  0.283334 0.192549 0.0316571   0.00296177  0.025756    261 VAL   A CA   
2054 C  C    . VAL   A 261 ? 0.109077  0.279896 0.182983 0.0264118   0.0107248   0.0293648   261 VAL   A C    
2055 O  O    . VAL   A 261 ? 0.0923491 0.277749 0.18048  0.0300517   -0.00198598 0.0308408   261 VAL   A O    
2056 C  CB   . VAL   A 261 ? 0.13794   0.306268 0.193345 0.0492901   0.0068703   0.0204165   261 VAL   A CB   
2057 C  CG1  . VAL   A 261 ? 0.130451  0.319742 0.201741 0.0500765   0.0104566   0.0119935   261 VAL   A CG1  
2058 C  CG2  . VAL   A 261 ? 0.140038  0.320101 0.209479 0.0549809   0.0019595   0.0104546   261 VAL   A CG2  
2059 N  N    . LEU   A 262 ? 0.113355  0.266073 0.182982 0.0170828   0.0135872   0.0271529   262 LEU   A N    
2060 C  CA   . LEU   A 262 ? 0.127807  0.272195 0.181167 0.0188439   0.0219146   0.0261924   262 LEU   A CA   
2061 C  C    . LEU   A 262 ? 0.121965  0.272257 0.174946 0.0166241   0.0168149   0.0191947   262 LEU   A C    
2062 O  O    . LEU   A 262 ? 0.119386  0.28168  0.189754 0.018435    -0.00133734 0.00802909  262 LEU   A O    
2063 C  CB   . LEU   A 262 ? 0.159881  0.284969 0.182966 0.0239977   0.0183306   0.0306298   262 LEU   A CB   
2064 C  CG   . LEU   A 262 ? 0.173367  0.300588 0.193316 0.0244944   0.0103347   0.0375499   262 LEU   A CG   
2065 C  CD1  . LEU   A 262 ? 0.208545  0.306475 0.201987 0.031717    0.0161404   0.0458492   262 LEU   A CD1  
2066 C  CD2  . LEU   A 262 ? 0.176827  0.312114 0.20833  0.0266463   -0.00987494 0.0358401   262 LEU   A CD2  
2067 N  N    . ASP   A 263 ? 0.102301  0.269825 0.190332 0.0160711   0.0202516   0.0132176   263 ASP   A N    
2068 C  CA   . ASP   A 263 ? 0.110901  0.276885 0.194416 0.0138821   0.0165703   0.0118253   263 ASP   A CA   
2069 C  C    . ASP   A 263 ? 0.103512  0.266438 0.191173 0.0150237   0.0140358   0.00635708  263 ASP   A C    
2070 O  O    . ASP   A 263 ? 0.0987676 0.268656 0.201847 0.0160818   0.0208099   0.00663225  263 ASP   A O    
2071 C  CB   . ASP   A 263 ? 0.121967  0.307444 0.202806 0.00582626  0.00869677  0.00995761  263 ASP   A CB   
2072 C  CG   . ASP   A 263 ? 0.13452   0.341742 0.220604 -0.00214717 0.0242047   0.00918975  263 ASP   A CG   
2073 O  OD1  . ASP   A 263 ? 0.177161  0.406028 0.233524 -0.046229   0.0335134   0.00489094  263 ASP   A OD1  
2074 O  OD2  . ASP   A 263 ? 0.165576  0.375363 0.267104 -0.0407842  0.041923    -0.00257641 263 ASP   A OD2  
2075 N  N    . MET   A 264 ? 0.106238  0.256139 0.177682 0.0227524   0.00827326  0.00635542  264 MET   A N    
2076 C  CA   . MET   A 264 ? 0.104453  0.255976 0.167594 0.0244829   0.00414557  0.0113508   264 MET   A CA   
2077 C  C    . MET   A 264 ? 0.104742  0.257996 0.162748 0.0215665   0.012012    0.0145187   264 MET   A C    
2078 O  O    . MET   A 264 ? 0.116691  0.257435 0.16123  0.0213323   0.00507402  0.00760605  264 MET   A O    
2079 C  CB   . MET   A 264 ? 0.104958  0.257307 0.163176 0.0211341   0.00277463  0.0103149   264 MET   A CB   
2080 C  CG   . MET   A 264 ? 0.106258  0.260956 0.168367 0.0207695   0.0058383   0.010651    264 MET   A CG   
2081 S  SD   . MET   A 264 ? 0.105038  0.274857 0.170131 0.0167476   0.00876636  0.0165132   264 MET   A SD   
2082 C  CE   . MET   A 264 ? 0.10956   0.280514 0.178446 0.00917372  0.00659609  0.018709    264 MET   A CE   
2083 N  N    . CYS   A 265 ? 0.0998421 0.26093  0.165752 0.0174233   0.00781398  0.0209542   265 CYS   A N    
2084 C  CA   . CYS   A 265 ? 0.104479  0.278479 0.167261 0.0131475   0.00953761  0.0202035   265 CYS   A CA   
2085 C  C    . CYS   A 265 ? 0.110087  0.274092 0.168214 0.0120134   0.00999667  0.0195511   265 CYS   A C    
2086 O  O    . CYS   A 265 ? 0.0923236 0.280441 0.179955 0.0169315   0.0114351   0.0169415   265 CYS   A O    
2087 C  CB   . CYS   A 265 ? 0.0974527 0.291446 0.173359 0.0161133   0.00815889  0.0282026   265 CYS   A CB   
2088 S  SG   . CYS   A 265 ? 0.101177  0.334249 0.194605 0.0230653   0.0107967   0.0353793   265 CYS   A SG   
2089 N  N    . ALA   A 266 ? 0.108747  0.27305  0.182927 0.0126717   0.00334689  0.00903177  266 ALA   A N    
2090 C  CA   . ALA   A 266 ? 0.106853  0.278509 0.177373 0.00722802  0.01211     0.00358961  266 ALA   A CA   
2091 C  C    . ALA   A 266 ? 0.0980231 0.276194 0.187047 0.0052558   0.0098689   0.00393805  266 ALA   A C    
2092 O  O    . ALA   A 266 ? 0.10537   0.294846 0.191098 0.0129747   0.00615074  0.00204463  266 ALA   A O    
2093 C  CB   . ALA   A 266 ? 0.119617  0.28149  0.19154  0.00417183  0.0244801   0.0025345   266 ALA   A CB   
2094 N  N    . SER   A 267 ? 0.0836911 0.269721 0.188988 0.0145965   0.00831549  0.00171548  267 SER   A N    
2095 C  CA   . SER   A 267 ? 0.104667  0.266926 0.193496 0.0219671   0.00627021  0.00399006  267 SER   A CA   
2096 C  C    . SER   A 267 ? 0.106933  0.265255 0.18129  0.0236495   0.00161933  0.00797335  267 SER   A C    
2097 O  O    . SER   A 267 ? 0.115965  0.277245 0.177934 0.0245943   0.00273641  0.00229751  267 SER   A O    
2098 C  CB   . SER   A 267 ? 0.130279  0.281669 0.198076 0.0263596   0.0100195   0.00599768  267 SER   A CB   
2099 O  OG   . SER   A 267 ? 0.163723  0.301262 0.205472 0.0255485   0.00601149  0.0117582   267 SER   A OG   
2100 N  N    . LEU   A 268 ? 0.113839  0.255415 0.174199 0.0268027   -0.00192795 0.00911124  268 LEU   A N    
2101 C  CA   . LEU   A 268 ? 0.105902  0.253867 0.167092 0.0246674   0.00621927  0.00870051  268 LEU   A CA   
2102 C  C    . LEU   A 268 ? 0.0899424 0.258125 0.172103 0.0253911   0.00671876  0.00651737  268 LEU   A C    
2103 O  O    . LEU   A 268 ? 0.0889974 0.258846 0.177831 0.0206472   0.0136472   -0.00643954 268 LEU   A O    
2104 C  CB   . LEU   A 268 ? 0.0979358 0.260867 0.166926 0.0206679   0.0120423   0.00559079  268 LEU   A CB   
2105 C  CG   . LEU   A 268 ? 0.100845  0.264149 0.168896 0.0157734   0.0130372   0.0066866   268 LEU   A CG   
2106 C  CD1  . LEU   A 268 ? 0.110299  0.259747 0.169645 0.0214568   0.017138    0.00635866  268 LEU   A CD1  
2107 C  CD2  . LEU   A 268 ? 0.102253  0.272473 0.173034 0.0174592   0.0145972   0.00862185  268 LEU   A CD2  
2108 N  N    . LYS   A 269 ? 0.0873575 0.2741   0.173666 0.0149893   0.00810429  0.00428569  269 LYS   A N    
2109 C  CA   . LYS   A 269 ? 0.0867736 0.290903 0.186098 0.0118913   0.01762     -0.00304799 269 LYS   A CA   
2110 C  C    . LYS   A 269 ? 0.10519   0.282717 0.187191 0.0074611   0.0194169   9.49e-06    269 LYS   A C    
2111 O  O    . LYS   A 269 ? 0.0966527 0.288029 0.197299 0.0119088   0.0265845   -0.00884738 269 LYS   A O    
2112 C  CB   . LYS   A 269 ? 0.117138  0.319998 0.206307 0.00657118  0.0226122   0.0112817   269 LYS   A CB   
2113 C  CG   . LYS   A 269 ? 0.15188   0.343569 0.237944 0.0167842   0.0228586   0.0131985   269 LYS   A CG   
2114 C  CD   . LYS   A 269 ? 0.186059  0.369845 0.259071 0.021208    0.0260728   0.0225182   269 LYS   A CD   
2115 C  CE   . LYS   A 269 ? 0.191393  0.395987 0.261417 0.0229697   0.036456    0.0201152   269 LYS   A CE   
2116 N  NZ   . LYS   A 269 ? 0.197705  0.406247 0.24288  0.0280169   0.0437149   0.0218093   269 LYS   A NZ   
2117 N  N    . GLU   A 270 ? 0.107682  0.27998  0.178707 0.00681176  0.0169984   0.0007427   270 GLU   A N    
2118 C  CA   . GLU   A 270 ? 0.1191    0.285157 0.187157 0.0128559   0.0134458   -0.00304025 270 GLU   A CA   
2119 C  C    . GLU   A 270 ? 0.102902  0.284651 0.175016 0.0151644   0.0066614   0.00022072  270 GLU   A C    
2120 O  O    . GLU   A 270 ? 0.100364  0.297433 0.190575 0.0113899   0.0184789   -0.0006929  270 GLU   A O    
2121 C  CB   . GLU   A 270 ? 0.117914  0.307713 0.202124 0.00599015  0.0146892   -0.00210974 270 GLU   A CB   
2122 C  CG   . GLU   A 270 ? 0.130703  0.327914 0.214815 0.0133727   0.00642557  -0.00784894 270 GLU   A CG   
2123 C  CD   . GLU   A 270 ? 0.129708  0.353263 0.239229 0.00753266  0.00804225  -0.00735201 270 GLU   A CD   
2124 O  OE1  . GLU   A 270 ? 0.167752  0.386813 0.259495 -0.0114926  0.00706488  0.00643718  270 GLU   A OE1  
2125 O  OE2  . GLU   A 270 ? 0.145422  0.383841 0.250055 -0.00277984 0.0212929   -0.0237903  270 GLU   A OE2  
2126 N  N    . LEU   A 271 ? 0.106988  0.282193 0.174058 0.0220136   0.00283512  0.00507356  271 LEU   A N    
2127 C  CA   . LEU   A 271 ? 0.117858  0.284867 0.161002 0.0252898   0.00583678  0.00269564  271 LEU   A CA   
2128 C  C    . LEU   A 271 ? 0.132583  0.284837 0.165192 0.0212117   0.013506    0.00373547  271 LEU   A C    
2129 O  O    . LEU   A 271 ? 0.140834  0.290758 0.174171 0.0261504   0.0047385   0.00917906  271 LEU   A O    
2130 C  CB   . LEU   A 271 ? 0.137645  0.282648 0.16512  0.0200411   -0.00274249 -0.0109891  271 LEU   A CB   
2131 C  CG   . LEU   A 271 ? 0.132019  0.286458 0.171191 0.0214622   -0.00964933 -0.0141071  271 LEU   A CG   
2132 C  CD1  . LEU   A 271 ? 0.133537  0.300104 0.169512 0.0211783   -0.00649628 -0.0177238  271 LEU   A CD1  
2133 C  CD2  . LEU   A 271 ? 0.162821  0.290614 0.182733 0.0202479   -0.0146941  -0.0175826  271 LEU   A CD2  
2134 N  N    . LEU   A 272 ? 0.110396  0.272276 0.160538 0.0221419   0.0124235   -0.00287038 272 LEU   A N    
2135 C  CA   . LEU   A 272 ? 0.116184  0.282418 0.165424 0.0190467   0.00778126  -0.00657712 272 LEU   A CA   
2136 C  C    . LEU   A 272 ? 0.117736  0.279398 0.175724 0.0166444   0.0122282   0.0032211   272 LEU   A C    
2137 O  O    . LEU   A 272 ? 0.127591  0.280853 0.190827 0.0204625   0.0116353   0.00576089  272 LEU   A O    
2138 C  CB   . LEU   A 272 ? 0.117248  0.283869 0.174471 0.0242103   0.00774267  -0.0133325  272 LEU   A CB   
2139 C  CG   . LEU   A 272 ? 0.118914  0.296212 0.188122 0.0258249   0.00852796  -0.0173376  272 LEU   A CG   
2140 C  CD1  . LEU   A 272 ? 0.134103  0.297495 0.196872 0.0274515   0.00351251  -0.0113395  272 LEU   A CD1  
2141 C  CD2  . LEU   A 272 ? 0.12745   0.313932 0.185326 0.0231496   0.0166323   -0.00971937 272 LEU   A CD2  
2142 N  N    . GLN   A 273 ? 0.121924  0.285624 0.171198 0.0194848   0.0185261   0.0110138   273 GLN   A N    
2143 C  CA   . GLN   A 273 ? 0.137795  0.293869 0.179745 0.0343336   0.0172447   0.0167162   273 GLN   A CA   
2144 C  C    . GLN   A 273 ? 0.128743  0.297597 0.177168 0.0375176   0.0390962   0.0204404   273 GLN   A C    
2145 O  O    . GLN   A 273 ? 0.137822  0.305253 0.186724 0.0374925   0.038585    0.0232088   273 GLN   A O    
2146 C  CB   . GLN   A 273 ? 0.145565  0.305257 0.183629 0.0406195   0.0217791   0.0236671   273 GLN   A CB   
2147 C  CG   . GLN   A 273 ? 0.150599  0.326553 0.197001 0.0484544   0.0168809   0.0247802   273 GLN   A CG   
2148 C  CD   . GLN   A 273 ? 0.166446  0.331968 0.212237 0.0491035   0.0268236   0.0328961   273 GLN   A CD   
2149 O  OE1  . GLN   A 273 ? 0.183252  0.373774 0.237809 0.0490319   0.0248174   0.0617017   273 GLN   A OE1  
2150 N  NE2  . GLN   A 273 ? 0.168261  0.331777 0.219134 0.055606    0.0224206   0.033391    273 GLN   A NE2  
2151 N  N    . ASN   A 274 ? 0.133597  0.30391  0.176353 0.0360024   0.0336804   0.0239084   274 ASN   A N    
2152 C  CA   . ASN   A 274 ? 0.146927  0.310052 0.182942 0.0402916   0.0354213   0.0262784   274 ASN   A CA   
2153 C  C    . ASN   A 274 ? 0.179883  0.322722 0.186068 0.0464413   0.0412764   0.0340411   274 ASN   A C    
2154 O  O    . ASN   A 274 ? 0.220036  0.332158 0.217236 0.0517341   0.0420347   0.048295    274 ASN   A O    
2155 C  CB   . ASN   A 274 ? 0.148154  0.318028 0.18115  0.0377743   0.0290562   0.0216569   274 ASN   A CB   
2156 C  CG   . ASN   A 274 ? 0.151947  0.31765  0.185822 0.0294739   0.0314378   0.012556    274 ASN   A CG   
2157 O  OD1  . ASN   A 274 ? 0.160413  0.351508 0.192577 0.022301    0.044068    0.00102357  274 ASN   A OD1  
2158 N  ND2  . ASN   A 274 ? 0.155512  0.323097 0.185714 0.0198782   0.0279502   0.0158192   274 ASN   A ND2  
2159 N  N    . GLY   A 275 ? 0.196468  0.324358 0.18351  0.0547592   0.0560501   0.0385002   275 GLY   A N    
2160 C  CA   . GLY   A 275 ? 0.223471  0.331932 0.188363 0.0532734   0.0533809   0.0446184   275 GLY   A CA   
2161 C  C    . GLY   A 275 ? 0.242061  0.330693 0.195742 0.0603621   0.0553952   0.0369751   275 GLY   A C    
2162 O  O    . GLY   A 275 ? 0.253564  0.343675 0.209735 0.0525811   0.0513853   0.0406307   275 GLY   A O    
2163 N  N    . MET   A 276 ? 0.245832  0.332487 0.206083 0.0616778   0.059488    0.0392855   276 MET   A N    
2164 C  CA   A MET   A 276 ? 0.245219  0.343661 0.238493 0.0623356   0.053663    0.0354684   276 MET   A CA   
2165 C  CA   B MET   A 276 ? 0.225923  0.322372 0.202392 0.0566303   0.0619786   0.034281    276 MET   A CA   
2166 C  C    . MET   A 276 ? 0.243003  0.337584 0.235687 0.0673091   0.0605474   0.0373967   276 MET   A C    
2167 O  O    . MET   A 276 ? 0.254782  0.347875 0.248119 0.0695254   0.0534119   0.0499922   276 MET   A O    
2168 C  CB   A MET   A 276 ? 0.2343    0.355013 0.261279 0.0592393   0.0568429   0.0370156   276 MET   A CB   
2169 C  CB   B MET   A 276 ? 0.192515  0.296275 0.185101 0.0503429   0.0456042   0.0302951   276 MET   A CB   
2170 C  CG   A MET   A 276 ? 0.232899  0.353698 0.310486 0.0524386   0.0487426   0.0274524   276 MET   A CG   
2171 C  CG   B MET   A 276 ? 0.167612  0.280887 0.163138 0.0385525   0.0445222   0.0229012   276 MET   A CG   
2172 S  SD   A MET   A 276 ? 0.217954  0.359079 0.388431 0.0170761   0.0480088   0.0171518   276 MET   A SD   
2173 S  SD   B MET   A 276 ? 0.139056  0.25782  0.145054 0.0298072   0.0239182   0.0140765   276 MET   A SD   
2174 C  CE   A MET   A 276 ? 0.219493  0.361841 0.380885 0.0240382   0.0519622   0.0139959   276 MET   A CE   
2175 C  CE   B MET   A 276 ? 0.140281  0.2652   0.158395 0.0292998   0.018733    0.0168702   276 MET   A CE   
2176 N  N    . ASN   A 277 ? 0.261625  0.359563 0.249586 0.0863217   0.0632368   0.0365458   277 ASN   A N    
2177 C  CA   . ASN   A 277 ? 0.278692  0.381335 0.287069 0.103165    0.0631441   0.0372114   277 ASN   A CA   
2178 C  C    . ASN   A 277 ? 0.262249  0.38202  0.294396 0.108397    0.0548096   0.0513949   277 ASN   A C    
2179 O  O    . ASN   A 277 ? 0.266061  0.428742 0.31834  0.100326    0.047648    0.0436643   277 ASN   A O    
2180 C  CB   . ASN   A 277 ? 0.279815  0.403552 0.319968 0.11567     0.0769815   0.035735    277 ASN   A CB   
2181 C  CG   . ASN   A 277 ? 0.361816  0.438115 0.347255 0.116105    0.0958233   0.0141638   277 ASN   A CG   
2182 O  OD1  . ASN   A 277 ? 0.444895  0.463528 0.408267 0.121411    0.119857    -0.00359181 277 ASN   A OD1  
2183 N  ND2  . ASN   A 277 ? 0.368849  0.447617 0.341234 0.117485    0.104125    0.0104267   277 ASN   A ND2  
2184 N  N    . GLY   A 278 ? 0.268385  0.358332 0.290138 0.11849     0.058385    0.0488667   278 GLY   A N    
2185 C  CA   . GLY   A 278 ? 0.284982  0.353894 0.271714 0.108196    0.054071    0.0441013   278 GLY   A CA   
2186 C  C    . GLY   A 278 ? 0.281671  0.357585 0.255226 0.102631    0.0420205   0.0448834   278 GLY   A C    
2187 O  O    . GLY   A 278 ? 0.340575  0.386044 0.247971 0.09097     0.0434563   0.0491265   278 GLY   A O    
2188 N  N    . ARG   A 279 ? 0.24577   0.351844 0.255344 0.09867     0.0268305   0.0420288   279 ARG   A N    
2189 C  CA   . ARG   A 279 ? 0.237819  0.35735  0.255676 0.0896919   0.00886598  0.0399593   279 ARG   A CA   
2190 C  C    . ARG   A 279 ? 0.21861   0.329643 0.220923 0.0713051   0.00239827  0.0205231   279 ARG   A C    
2191 O  O    . ARG   A 279 ? 0.216072  0.350239 0.212508 0.0731884   0.0154128   0.00369485  279 ARG   A O    
2192 C  CB   . ARG   A 279 ? 0.235872  0.390365 0.305007 0.0777897   0.011617    0.0413563   279 ARG   A CB   
2193 C  CG   . ARG   A 279 ? 0.24126   0.43054  0.346961 0.0792077   0.0185375   0.0475274   279 ARG   A CG   
2194 C  CD   . ARG   A 279 ? 0.278999  0.452391 0.383019 0.0594112   0.00032867  0.0696362   279 ARG   A CD   
2195 N  NE   . ARG   A 279 ? 0.29628   0.490781 0.404069 0.0532195   -0.00350066 0.0737889   279 ARG   A NE   
2196 C  CZ   . ARG   A 279 ? 0.297856  0.509847 0.423483 0.0602399   -0.00017966 0.0697676   279 ARG   A CZ   
2197 N  NH1  . ARG   A 279 ? 0.296257  0.518446 0.461086 0.0560637   -0.0205389  0.068119    279 ARG   A NH1  
2198 N  NH2  . ARG   A 279 ? 0.295944  0.512932 0.417973 0.0835838   -0.0160659  0.070562    279 ARG   A NH2  
2199 N  N    . THR   A 280 ? 0.193793  0.309381 0.233127 0.0691246   -0.0227597  0.0170503   280 THR   A N    
2200 C  CA   . THR   A 280 ? 0.171946  0.294581 0.226857 0.0511464   -0.016504   0.0169362   280 THR   A CA   
2201 C  C    . THR   A 280 ? 0.167097  0.285908 0.230478 0.0400124   -0.013121   0.0129827   280 THR   A C    
2202 O  O    . THR   A 280 ? 0.153372  0.303969 0.26015  0.0468817   -0.0259072  0.022992    280 THR   A O    
2203 C  CB   . THR   A 280 ? 0.209685  0.312424 0.227391 0.0456376   -0.0102504  0.0110309   280 THR   A CB   
2204 O  OG1  . THR   A 280 ? 0.241492  0.346242 0.241115 0.0430286   -0.0363966  0.0222648   280 THR   A OG1  
2205 C  CG2  . THR   A 280 ? 0.227082  0.323106 0.234813 0.0351441   -0.00218707 0.00783231  280 THR   A CG2  
2206 N  N    . ILE   A 281 ? 0.156994  0.265631 0.203819 0.0299734   -0.00801515 0.0110626   281 ILE   A N    
2207 C  CA   . ILE   A 281 ? 0.147576  0.257804 0.193748 0.0220632   -0.00616854 0.0054204   281 ILE   A CA   
2208 C  C    . ILE   A 281 ? 0.161152  0.264732 0.184248 0.0268375   -0.00637901 0.0129278   281 ILE   A C    
2209 O  O    . ILE   A 281 ? 0.153506  0.273976 0.173637 0.0189121   0.00138817  0.0132727   281 ILE   A O    
2210 C  CB   . ILE   A 281 ? 0.130973  0.256857 0.195879 0.0231127   -0.00780101 0.00556365  281 ILE   A CB   
2211 C  CG1  . ILE   A 281 ? 0.127847  0.261595 0.20435  0.0143778   0.00270144  0.0138716   281 ILE   A CG1  
2212 C  CG2  . ILE   A 281 ? 0.136857  0.266258 0.193987 0.0249496   -0.0147145  -7.377e-05  281 ILE   A CG2  
2213 C  CD1  . ILE   A 281 ? 0.117949  0.267368 0.20477  0.0099827   -0.00040114 0.0114047   281 ILE   A CD1  
2214 N  N    . LEU   A 282 ? 0.173466  0.255887 0.195078 0.0257769   0.00381264  0.00713816  282 LEU   A N    
2215 C  CA   . LEU   A 282 ? 0.1887    0.262544 0.188796 0.0339941   0.00514749  0.0106122   282 LEU   A CA   
2216 C  C    . LEU   A 282 ? 0.232137  0.260519 0.191986 0.0250906   0.00281455  0.00678722  282 LEU   A C    
2217 O  O    . LEU   A 282 ? 0.252922  0.275244 0.203805 0.0187686   0.041685    0.0192537   282 LEU   A O    
2218 C  CB   . LEU   A 282 ? 0.16385   0.256141 0.193963 0.0308177   0.0165124   0.0126658   282 LEU   A CB   
2219 C  CG   . LEU   A 282 ? 0.146251  0.255932 0.197515 0.0247498   0.0238958   0.0193135   282 LEU   A CG   
2220 C  CD1  . LEU   A 282 ? 0.138696  0.254557 0.204019 0.0266868   0.0310184   0.0189923   282 LEU   A CD1  
2221 C  CD2  . LEU   A 282 ? 0.138756  0.269426 0.200374 0.0220343   0.0207696   0.0184533   282 LEU   A CD2  
2222 N  N    . GLY   A 283 ? 0.26059   0.264641 0.191659 0.0224674   -0.0143252  0.0152821   283 GLY   A N    
2223 C  CA   . GLY   A 283 ? 0.2823    0.275425 0.189075 0.0160344   -0.00225915 0.0183718   283 GLY   A CA   
2224 C  C    . GLY   A 283 ? 0.273857  0.276253 0.20193  0.00870617  -0.00299737 0.020372    283 GLY   A C    
2225 O  O    . GLY   A 283 ? 0.383012  0.284044 0.233015 -0.0149598  -0.0018995  0.0246354   283 GLY   A O    
2226 N  N    A SER   A 284 ? 0.235614  0.269311 0.183445 0.0182387   0.00672898  0.00876324  284 SER   A N    
2227 N  N    B SER   A 284 ? 0.2366    0.267618 0.186723 0.0176772   0.0064299   0.0126655   284 SER   A N    
2228 C  CA   A SER   A 284 ? 0.217899  0.267208 0.188058 0.022045    0.0107608   0.00092484  284 SER   A CA   
2229 C  CA   B SER   A 284 ? 0.217901  0.263846 0.191778 0.0212647   0.00984192  0.00730734  284 SER   A CA   
2230 C  C    A SER   A 284 ? 0.197153  0.258079 0.189731 0.0192213   0.00738326  0.0033805   284 SER   A C    
2231 C  C    B SER   A 284 ? 0.197902  0.256138 0.192157 0.0183074   0.00643672  0.00713485  284 SER   A C    
2232 O  O    A SER   A 284 ? 0.193214  0.269503 0.202776 0.0139537   0.00600882  -0.00170431 284 SER   A O    
2233 O  O    B SER   A 284 ? 0.194222  0.267551 0.204735 0.0126742   0.00542267  0.00128077  284 SER   A O    
2234 C  CB   A SER   A 284 ? 0.220168  0.272242 0.18126  0.0252838   0.00753567  -0.00225738 284 SER   A CB   
2235 C  CB   B SER   A 284 ? 0.220564  0.267738 0.187711 0.0233218   0.00673768  0.00844533  284 SER   A CB   
2236 O  OG   A SER   A 284 ? 0.220278  0.282461 0.19395  0.0244295   0.0135291   -0.0204803  284 SER   A OG   
2237 O  OG   B SER   A 284 ? 0.220898  0.276998 0.206945 0.0215889   0.013287    -0.00140115 284 SER   A OG   
2238 N  N    . ALA   A 285 ? 0.198591  0.254222 0.199864 0.0146331   0.00965856  0.00727433  285 ALA   A N    
2239 C  CA   . ALA   A 285 ? 0.219593  0.253573 0.208257 0.0113711   0.0103575   0.00178333  285 ALA   A CA   
2240 C  C    . ALA   A 285 ? 0.223049  0.263422 0.198768 0.00527483  0.0126767   -0.0068882  285 ALA   A C    
2241 O  O    . ALA   A 285 ? 0.265731  0.321304 0.20402  0.0352312   0.0147794   -0.0230498  285 ALA   A O    
2242 C  CB   . ALA   A 285 ? 0.23833   0.257533 0.236034 0.0129041   0.0138607   -0.00274113 285 ALA   A CB   
2243 N  N    . LEU   A 286 ? 0.218164  0.261078 0.184241 0.00453072  0.0155518   0.0108547   286 LEU   A N    
2244 C  CA   . LEU   A 286 ? 0.226267  0.270887 0.185925 0.00320064  0.0107771   0.00838768  286 LEU   A CA   
2245 C  C    . LEU   A 286 ? 0.182557  0.259636 0.177174 0.00802488  0.0111775   0.00973216  286 LEU   A C    
2246 O  O    . LEU   A 286 ? 0.216865  0.264453 0.172914 0.00826681  0.00493768  0.015049    286 LEU   A O    
2247 C  CB   . LEU   A 286 ? 0.255224  0.308795 0.231981 -0.01168    -0.0244466  0.0125552   286 LEU   A CB   
2248 C  CG   . LEU   A 286 ? 0.308726  0.340517 0.288767 -0.0153215  -0.0235223  0.0216721   286 LEU   A CG   
2249 C  CD1  . LEU   A 286 ? 0.307104  0.375226 0.305113 -0.0273584  -0.0318276  0.0329415   286 LEU   A CD1  
2250 C  CD2  . LEU   A 286 ? 0.364397  0.370814 0.310909 -0.0211751  -0.0260612  0.0136043   286 LEU   A CD2  
2251 N  N    . LEU   A 287 ? 0.144859  0.259609 0.171894 0.00139891  0.0249253   0.00395306  287 LEU   A N    
2252 C  CA   . LEU   A 287 ? 0.115728  0.266692 0.188092 0.00671824  0.0153295   0.00631613  287 LEU   A CA   
2253 C  C    . LEU   A 287 ? 0.107139  0.281971 0.195071 0.00940743  0.00751274  0.00117003  287 LEU   A C    
2254 O  O    . LEU   A 287 ? 0.113514  0.352824 0.246042 0.00345029  0.00499541  -0.0465985  287 LEU   A O    
2255 C  CB   . LEU   A 287 ? 0.121012  0.284781 0.196994 0.00175611  0.0198347   0.0126565   287 LEU   A CB   
2256 C  CG   . LEU   A 287 ? 0.128019  0.309973 0.205715 0.0102866   0.02176     0.00687365  287 LEU   A CG   
2257 C  CD1  . LEU   A 287 ? 0.134635  0.330911 0.215319 0.00828585  0.0213189   0.0168139   287 LEU   A CD1  
2258 C  CD2  . LEU   A 287 ? 0.151635  0.329594 0.225604 0.00645788  0.0201528   -0.00450604 287 LEU   A CD2  
2259 N  N    . GLU   A 288 ? 0.0969757 0.268553 0.192467 0.0103129   -0.00219687 0.0107178   288 GLU   A N    
2260 C  CA   . GLU   A 288 ? 0.104805  0.270836 0.191507 0.0118581   -0.00165584 0.0173388   288 GLU   A CA   
2261 C  C    . GLU   A 288 ? 0.0884711 0.250435 0.17359  -0.00041831 0.00070555  0.0107075   288 GLU   A C    
2262 O  O    . GLU   A 288 ? 0.0887996 0.246361 0.167991 0.00032842  0.00179564  0.0178802   288 GLU   A O    
2263 C  CB   . GLU   A 288 ? 0.125904  0.299384 0.195708 0.0193363   -0.00230848 0.0210442   288 GLU   A CB   
2264 C  CG   . GLU   A 288 ? 0.175607  0.334298 0.252439 0.0155948   -0.00237215 0.0417452   288 GLU   A CG   
2265 C  CD   . GLU   A 288 ? 0.184163  0.384852 0.28964  0.00922016  0.00084416  0.0803826   288 GLU   A CD   
2266 O  OE1  . GLU   A 288 ? 0.160428  0.439971 0.335385 -0.0292711  0.0034872   0.105272    288 GLU   A OE1  
2267 O  OE2  . GLU   A 288 ? 0.224325  0.446227 0.387125 0.0309398   -0.0199099  0.123286    288 GLU   A OE2  
2268 N  N    . ASP   A 289 ? 0.0813253 0.250294 0.159235 -0.00093977 0.00812825  0.0134905   289 ASP   A N    
2269 C  CA   . ASP   A 289 ? 0.083073  0.253361 0.167614 -0.00235483 0.00981276  0.0172736   289 ASP   A CA   
2270 C  C    . ASP   A 289 ? 0.0903583 0.24419  0.169994 0.00617186  0.0114712   0.0252393   289 ASP   A C    
2271 O  O    . ASP   A 289 ? 0.0925318 0.259907 0.16301  -0.00149    0.00617367  0.0283608   289 ASP   A O    
2272 C  CB   . ASP   A 289 ? 0.097332  0.276731 0.1705   -0.00329423 0.0141503   0.0149726   289 ASP   A CB   
2273 C  CG   . ASP   A 289 ? 0.0907212 0.280463 0.161105 -0.00170915 0.0141671   0.0209288   289 ASP   A CG   
2274 O  OD1  . ASP   A 289 ? 0.110697  0.288867 0.160278 -0.00866581 0.00611201  0.0304111   289 ASP   A OD1  
2275 O  OD2  . ASP   A 289 ? 0.091609  0.30373  0.16176  -0.0108595  0.00908272  0.0166401   289 ASP   A OD2  
2276 N  N    . GLU   A 290 ? 0.0894353 0.23831  0.163445 0.0121339   0.00752868  0.0172124   290 GLU   A N    
2277 C  CA   . GLU   A 290 ? 0.0905662 0.239706 0.165137 0.00780694  0.0175248   0.0202827   290 GLU   A CA   
2278 C  C    . GLU   A 290 ? 0.0928081 0.228388 0.169685 0.00868717  0.0207592   0.0269383   290 GLU   A C    
2279 O  O    . GLU   A 290 ? 0.102925  0.2284   0.189821 0.0159601   0.0263595   0.016151    290 GLU   A O    
2280 C  CB   . GLU   A 290 ? 0.0980585 0.259058 0.167723 -0.00176594 0.0208356   0.0140588   290 GLU   A CB   
2281 C  CG   . GLU   A 290 ? 0.116594  0.265136 0.179231 -0.012611   0.0111408   0.0123023   290 GLU   A CG   
2282 C  CD   . GLU   A 290 ? 0.116159  0.276294 0.171115 -0.0162128  0.00439976  0.0108445   290 GLU   A CD   
2283 O  OE1  . GLU   A 290 ? 0.139226  0.296943 0.177103 -0.0151847  0.0102571   0.00136389  290 GLU   A OE1  
2284 O  OE2  . GLU   A 290 ? 0.131133  0.28127  0.171687 -0.0210561  0.0126638   0.00297277  290 GLU   A OE2  
2285 N  N    . PHE   A 291 ? 0.0936265 0.23149  0.168887 0.00576126  0.0255571   0.0188051   291 PHE   A N    
2286 C  CA   . PHE   A 291 ? 0.0946741 0.249914 0.161988 0.00563601  0.0227217   0.0165285   291 PHE   A CA   
2287 C  C    . PHE   A 291 ? 0.0893166 0.247477 0.153261 0.00482121  0.0224789   0.0152299   291 PHE   A C    
2288 O  O    . PHE   A 291 ? 0.104287  0.252506 0.148403 0.0111451   0.0302124   0.0131624   291 PHE   A O    
2289 C  CB   . PHE   A 291 ? 0.112718  0.280934 0.162888 0.00088299  0.0133276   0.0164626   291 PHE   A CB   
2290 C  CG   . PHE   A 291 ? 0.117259  0.315001 0.176332 0.00285323  0.0143375   0.0337627   291 PHE   A CG   
2291 C  CD1  . PHE   A 291 ? 0.123213  0.336866 0.174262 0.00798771  0.0231109   0.0445902   291 PHE   A CD1  
2292 C  CD2  . PHE   A 291 ? 0.151777  0.319194 0.18237  -0.00394062 0.0169053   0.0517526   291 PHE   A CD2  
2293 C  CE1  . PHE   A 291 ? 0.167584  0.355262 0.190982 0.00334806  0.0207488   0.053065    291 PHE   A CE1  
2294 C  CE2  . PHE   A 291 ? 0.184201  0.337041 0.196356 0.0128534   0.00916633  0.0612225   291 PHE   A CE2  
2295 C  CZ   . PHE   A 291 ? 0.177601  0.346364 0.191727 0.00728567  0.0157046   0.066747    291 PHE   A CZ   
2296 N  N    . THR   A 292 ? 0.10303   0.246492 0.158904 0.00464468  0.0227643   0.00962856  292 THR   A N    
2297 C  CA   . THR   A 292 ? 0.107631  0.242934 0.173054 0.0060365   0.0132135   0.0122215   292 THR   A CA   
2298 C  C    . THR   A 292 ? 0.101328  0.252985 0.178616 0.00534604  0.0197193   0.0218889   292 THR   A C    
2299 O  O    . THR   A 292 ? 0.0872037 0.270926 0.172291 0.00741052  0.0201446   0.0194416   292 THR   A O    
2300 C  CB   . THR   A 292 ? 0.100873  0.247429 0.187991 0.00370449  0.00322615  0.00944049  292 THR   A CB   
2301 O  OG1  . THR   A 292 ? 0.103203  0.252794 0.189302 0.00567854  0.00865014  0.00576533  292 THR   A OG1  
2302 C  CG2  . THR   A 292 ? 0.108339  0.255549 0.190653 -0.00554068 -0.00133707 0.00839088  292 THR   A CG2  
2303 N  N    . PRO   A 293 ? 0.109968  0.246447 0.186199 -0.00090919 0.0118471   0.0273922   293 PRO   A N    
2304 C  CA   . PRO   A 293 ? 0.11443   0.251941 0.199814 -0.0122009  0.0160707   0.0204551   293 PRO   A CA   
2305 C  C    . PRO   A 293 ? 0.108664  0.251788 0.209847 -0.00575772 0.0169215   0.0131783   293 PRO   A C    
2306 O  O    . PRO   A 293 ? 0.107041  0.279864 0.204048 0.00299598  0.0131849   0.0082803   293 PRO   A O    
2307 C  CB   . PRO   A 293 ? 0.129641  0.25409  0.203847 -0.0171132  0.023569    0.0278224   293 PRO   A CB   
2308 C  CG   . PRO   A 293 ? 0.138407  0.259358 0.200886 -0.0153836  0.010743    0.0359549   293 PRO   A CG   
2309 C  CD   . PRO   A 293 ? 0.128294  0.265185 0.192346 -0.0111816  0.00899396  0.0306024   293 PRO   A CD   
2310 N  N    . PHE   A 294 ? 0.10533   0.258715 0.215673 -0.003586   0.00300947  0.00214209  294 PHE   A N    
2311 C  CA   . PHE   A 294 ? 0.106844  0.263553 0.227591 0.00874304  0.0113994   -0.00281518 294 PHE   A CA   
2312 C  C    . PHE   A 294 ? 0.103078  0.258973 0.213852 0.0136146   0.0202068   -0.00680385 294 PHE   A C    
2313 O  O    . PHE   A 294 ? 0.121601  0.288961 0.216775 0.020521    0.00242243  -0.00881302 294 PHE   A O    
2314 C  CB   . PHE   A 294 ? 0.118837  0.272702 0.247986 0.0132241   0.00350424  0.00479165  294 PHE   A CB   
2315 C  CG   . PHE   A 294 ? 0.172454  0.288304 0.27317  0.0001638   0.00450464  -0.00859961 294 PHE   A CG   
2316 C  CD1  . PHE   A 294 ? 0.185586  0.300033 0.279022 -0.00107918 0.0155479   -0.00986458 294 PHE   A CD1  
2317 C  CD2  . PHE   A 294 ? 0.206122  0.294808 0.281428 -0.00840155 0.00941489  -0.00453959 294 PHE   A CD2  
2318 C  CE1  . PHE   A 294 ? 0.206604  0.308786 0.29013  -0.00225444 0.0178773   -0.0238897  294 PHE   A CE1  
2319 C  CE2  . PHE   A 294 ? 0.21685   0.297017 0.297589 -0.00556951 0.00744943  -0.0161053  294 PHE   A CE2  
2320 C  CZ   . PHE   A 294 ? 0.224541  0.305067 0.300373 -0.00842146 0.0176192   -0.0161329  294 PHE   A CZ   
2321 N  N    . ASP   A 295 ? 0.101991  0.256569 0.191238 0.00850316  0.0166281   -0.00933497 295 ASP   A N    
2322 C  CA   . ASP   A 295 ? 0.0963662 0.259087 0.184869 0.0163938   0.0252876   -0.00274172 295 ASP   A CA   
2323 C  C    . ASP   A 295 ? 0.101191  0.260631 0.187466 0.0131256   0.0218587   0.00498722  295 ASP   A C    
2324 O  O    . ASP   A 295 ? 0.101036  0.286887 0.187943 -0.00057425 0.0365491   0.0177583   295 ASP   A O    
2325 C  CB   . ASP   A 295 ? 0.109495  0.258759 0.187548 0.0189964   0.0256606   0.0053543   295 ASP   A CB   
2326 C  CG   . ASP   A 295 ? 0.117557  0.261184 0.195598 0.0134181   0.02347     0.00928011  295 ASP   A CG   
2327 O  OD1  . ASP   A 295 ? 0.119771  0.280828 0.196655 0.00708684  0.0277243   -0.00513988 295 ASP   A OD1  
2328 O  OD2  . ASP   A 295 ? 0.104939  0.268869 0.188505 0.00937028  0.0347544   0.015507    295 ASP   A OD2  
2329 N  N    . VAL   A 296 ? 0.096243  0.251439 0.179585 0.0126542   0.0177852   0.00970413  296 VAL   A N    
2330 C  CA   . VAL   A 296 ? 0.10048   0.253443 0.180449 0.0165592   0.0154657   0.011421    296 VAL   A CA   
2331 C  C    . VAL   A 296 ? 0.113013  0.254253 0.181711 0.0081961   0.0196081   0.0134455   296 VAL   A C    
2332 O  O    . VAL   A 296 ? 0.108436  0.258866 0.186007 0.00419603  0.00943952  0.00925447  296 VAL   A O    
2333 C  CB   . VAL   A 296 ? 0.104841  0.261831 0.180876 0.0150367   0.0194142   0.0174268   296 VAL   A CB   
2334 C  CG1  . VAL   A 296 ? 0.105934  0.265349 0.186016 0.0167817   0.0170735   0.0119725   296 VAL   A CG1  
2335 C  CG2  . VAL   A 296 ? 0.0987677 0.271731 0.170771 0.0126888   0.0214969   0.012004    296 VAL   A CG2  
2336 N  N    . VAL   A 297 ? 0.127922  0.245001 0.195807 0.0067792   0.0166996   0.00782945  297 VAL   A N    
2337 C  CA   . VAL   A 297 ? 0.160521  0.256919 0.209786 -0.00343974 0.0205673   0.00314712  297 VAL   A CA   
2338 C  C    . VAL   A 297 ? 0.171346  0.260249 0.207092 -0.010759   0.0240343   -0.00564639 297 VAL   A C    
2339 O  O    . VAL   A 297 ? 0.209955  0.28233  0.20976  -0.0172009  0.0152953   -0.0142587  297 VAL   A O    
2340 C  CB   . VAL   A 297 ? 0.176901  0.26099  0.225915 -0.00639203 0.0300917   0.0127961   297 VAL   A CB   
2341 C  CG1  . VAL   A 297 ? 0.203309  0.25562  0.244238 -0.00618083 0.0251214   0.0160981   297 VAL   A CG1  
2342 C  CG2  . VAL   A 297 ? 0.182005  0.270871 0.237518 -0.00925234 0.0359846   0.0191405   297 VAL   A CG2  
2343 N  N    . ARG   A 298 ? 0.165369  0.267187 0.195648 -0.00551325 0.024389    -0.00953204 298 ARG   A N    
2344 C  CA   . ARG   A 298 ? 0.185565  0.278985 0.19818  -0.0116142  0.0275381   -0.01434    298 ARG   A CA   
2345 C  C    . ARG   A 298 ? 0.171066  0.272142 0.202978 -0.0196353  0.0296233   -0.0109176  298 ARG   A C    
2346 O  O    . ARG   A 298 ? 0.213365  0.293261 0.203928 -0.0211045  0.00710059  -0.0117906  298 ARG   A O    
2347 C  CB   . ARG   A 298 ? 0.179022  0.288931 0.210643 -0.00493917 0.0320333   -0.0129768  298 ARG   A CB   
2348 C  CG   . ARG   A 298 ? 0.191973  0.299842 0.228354 -0.0190846  0.0318935   -0.0107841  298 ARG   A CG   
2349 C  CD   . ARG   A 298 ? 0.198057  0.288443 0.23576  -0.0141253  0.0202048   -0.0156073  298 ARG   A CD   
2350 N  NE   . ARG   A 298 ? 0.187249  0.272963 0.241092 0.00025189  0.0227585   -0.00734129 298 ARG   A NE   
2351 C  CZ   . ARG   A 298 ? 0.180021  0.272682 0.242262 0.0150978   0.00703445  -0.00706072 298 ARG   A CZ   
2352 N  NH1  . ARG   A 298 ? 0.221261  0.270229 0.238994 0.023903    -0.00786164 0.00303903  298 ARG   A NH1  
2353 N  NH2  . ARG   A 298 ? 0.168842  0.269801 0.234219 0.0215077   0.0037484   -0.00694939 298 ARG   A NH2  
2354 N  N    . GLN   A 299 ? 0.157433  0.26496  0.190907 -0.0250306  0.0290105   -0.00633361 299 GLN   A N    
2355 C  CA   . GLN   A 299 ? 0.16583   0.276785 0.178998 -0.0249446  0.0135225   -0.0029602  299 GLN   A CA   
2356 C  C    . GLN   A 299 ? 0.176714  0.311911 0.186404 -0.0323676  0.00449499  0.00204926  299 GLN   A C    
2357 O  O    . GLN   A 299 ? 0.20119   0.323843 0.188089 -0.0558451  -0.00448697 0.0117114   299 GLN   A O    
2358 C  CB   . GLN   A 299 ? 0.160314  0.259937 0.182718 -0.0090349  0.00878267  -0.00274131 299 GLN   A CB   
2359 C  CG   . GLN   A 299 ? 0.154095  0.261888 0.187882 -0.00246641 -0.00103027 -0.00389338 299 GLN   A CG   
2360 C  CD   . GLN   A 299 ? 0.140628  0.247645 0.175727 0.00088834  -0.00736199 0.00258387  299 GLN   A CD   
2361 O  OE1  . GLN   A 299 ? 0.119494  0.264578 0.178884 0.0135905   -0.00924006 0.00114252  299 GLN   A OE1  
2362 N  NE2  . GLN   A 299 ? 0.156953  0.257311 0.169236 0.00015728  -0.0147097  0.0138972   299 GLN   A NE2  
2363 N  N    . CYS   A 300 ? 0.176201  0.343796 0.180312 -0.029787   -0.00682414 0.0229276   300 CYS   A N    
2364 C  CA   . CYS   A 300 ? 0.185004  0.359553 0.202556 -0.0121856  -0.012973   0.0158591   300 CYS   A CA   
2365 C  C    . CYS   A 300 ? 0.199409  0.351018 0.2322   -0.0234859  0.0123366   0.0225726   300 CYS   A C    
2366 O  O    . CYS   A 300 ? 0.206598  0.33693  0.238099 -0.0391245  0.0105975   0.0289147   300 CYS   A O    
2367 C  CB   . CYS   A 300 ? 0.157482  0.378197 0.201776 0.00501094  -0.0220847  0.00965909  300 CYS   A CB   
2368 S  SG   . CYS   A 300 ? 0.244417  0.404994 0.275626 0.0289526   -0.048043   -0.0139552  300 CYS   A SG   
2369 N  N    . SER   A 301 ? 0.208124  0.325386 0.244158 -0.0194869  0.00205612  0.00725501  301 SER   A N    
2370 C  CA   . SER   A 301 ? 0.214028  0.316293 0.25514  -0.0155452  0.0229369   0.00045072  301 SER   A CA   
2371 C  C    . SER   A 301 ? 0.221501  0.321068 0.265444 -0.0181875  0.0383312   -0.0043008  301 SER   A C    
2372 O  O    . SER   A 301 ? 0.225705  0.324495 0.266173 -0.0140794  0.0410427   -0.0143065  301 SER   A O    
2373 C  CB   . SER   A 301 ? 0.219326  0.31877  0.261168 -0.0249535  0.0158364   -0.00465113 301 SER   A CB   
2374 O  OG   . SER   A 301 ? 0.256149  0.320444 0.296814 -0.0501298  0.0286883   -0.00815247 301 SER   A OG   
2375 N  N    . GLY   A 302 ? 0.226342  0.319367 0.278141 -0.00604875 0.0510952   -0.00748356 302 GLY   A N    
2376 C  CA   . GLY   A 302 ? 0.244587  0.325965 0.294422 -0.0238708  0.0452784   -0.00300147 302 GLY   A CA   
2377 C  C    . GLY   A 302 ? 0.243611  0.349724 0.313702 -0.035748   0.0426915   -0.0107978  302 GLY   A C    
2378 O  O    . GLY   A 302 ? 0.295953  0.366134 0.325201 -0.0398216  0.0432303   -0.00267708 302 GLY   A O    
2379 N  N    . VAL   A 303 ? 0.202505  0.372908 0.335022 -0.0330756  0.0384107   -0.0180541  303 VAL   A N    
2380 C  CA   . VAL   A 303 ? 0.210067  0.383885 0.365498 -0.0323219  0.0374475   -0.0325826  303 VAL   A CA   
2381 C  C    . VAL   A 303 ? 0.209265  0.370537 0.353518 -0.0329028  0.0517484   -0.0201535  303 VAL   A C    
2382 O  O    . VAL   A 303 ? 0.262299  0.348735 0.38804  -0.0294535  0.0726823   -0.0273295  303 VAL   A O    
2383 C  CB   . VAL   A 303 ? 0.246633  0.411622 0.394077 -0.0266031  0.0161082   -0.0403466  303 VAL   A CB   
2384 C  CG1  . VAL   A 303 ? 0.251531  0.420749 0.41879  -0.0292045  0.0155916   -0.0416671  303 VAL   A CG1  
2385 C  CG2  . VAL   A 303 ? 0.274119  0.417785 0.409967 -0.015832   0.00501284  -0.0427146  303 VAL   A CG2  
2386 N  N    . THR   A 304 ? 0.196754  0.359568 0.34346  -0.0225672  0.0428071   -0.0197     304 THR   A N    
2387 C  CA   . THR   A 304 ? 0.210365  0.357895 0.313082 -0.0230224  0.025059    -0.00796486 304 THR   A CA   
2388 C  C    . THR   A 304 ? 0.206082  0.351908 0.313869 -0.0139551  0.0234338   -0.0101128  304 THR   A C    
2389 O  O    . THR   A 304 ? 0.205938  0.356344 0.342561 -0.0173498  0.0230288   -0.01303    304 THR   A O    
2390 C  CB   . THR   A 304 ? 0.21848   0.36308  0.311484 -0.0217702  0.0213198   0.00721718  304 THR   A CB   
2391 O  OG1  . THR   A 304 ? 0.241297  0.392275 0.31095  -0.0240882  -0.00868808 0.0205752   304 THR   A OG1  
2392 C  CG2  . THR   A 304 ? 0.253601  0.372532 0.303968 -0.0272434  0.0457733   0.00698518  304 THR   A CG2  
2393 N  N    . PHE   A 305 ? 0.190155  0.355777 0.298202 -0.00798166 0.0190836   -0.0137751  305 PHE   A N    
2394 C  CA   . PHE   A 305 ? 0.200581  0.364574 0.280615 -0.00256866 0.010316    -0.014249   305 PHE   A CA   
2395 C  C    . PHE   A 305 ? 0.195989  0.374561 0.296774 -0.00324844 0.0147592   -0.0277043  305 PHE   A C    
2396 O  O    . PHE   A 305 ? 0.239042  0.366448 0.284619 -0.0149006  0.0100588   -0.0171418  305 PHE   A O    
2397 C  CB   . PHE   A 305 ? 0.207713  0.368561 0.28809  -0.00044372 0.0045354   -0.00683748 305 PHE   A CB   
2398 C  CG   . PHE   A 305 ? 0.215038  0.389852 0.273974 0.00161736  0.00163196  -0.00178803 305 PHE   A CG   
2399 C  CD1  . PHE   A 305 ? 0.232471  0.400861 0.285724 -0.00532901 -0.00217793 -0.00144261 305 PHE   A CD1  
2400 C  CD2  . PHE   A 305 ? 0.247456  0.395665 0.285069 0.00388286  -0.00288428 -0.00513871 305 PHE   A CD2  
2401 C  CE1  . PHE   A 305 ? 0.237987  0.414619 0.299785 -0.00134469 -0.0061371  -0.00089088 305 PHE   A CE1  
2402 C  CE2  . PHE   A 305 ? 0.25089   0.417807 0.294771 0.00241098  -0.00506311 0.00029942  305 PHE   A CE2  
2403 C  CZ   . PHE   A 305 ? 0.258203  0.420469 0.282393 -0.00336322 -9.789e-05  -0.00426834 305 PHE   A CZ   
2404 N  N    . GLN   A 306 ? 0.215383  0.394037 0.306491 -0.013263   0.017926    -0.0377662  306 GLN   A N    
2405 C  CA   . GLN   A 306 ? 0.188674  0.424157 0.328097 -0.00444332 0.0245815   -0.0414489  306 GLN   A CA   
2406 C  C    . GLN   A 306 ? 0.174894  0.448295 0.303781 -0.00076886 0.0354582   -0.0525929  306 GLN   A C    
2407 O  O    . GLN   A 306 ? 0.165445  0.469916 0.276479 0.0245871   0.0279315   -0.0407143  306 GLN   A O    
2408 C  CB   . GLN   A 306 ? 0.212486  0.427272 0.368104 -0.00272352 0.0205263   -0.0384323  306 GLN   A CB   
2409 C  CG   . GLN   A 306 ? 0.238598  0.44237  0.404672 0.0159049   0.0346181   -0.038917   306 GLN   A CG   
2410 C  CD   . GLN   A 306 ? 0.314207  0.457759 0.467649 0.0118121   0.0404134   -0.0265362  306 GLN   A CD   
2411 O  OE1  . GLN   A 306 ? 0.364235  0.504637 0.510186 0.0190795   0.0658621   -0.00802146 306 GLN   A OE1  
2412 N  NE2  . GLN   A 306 ? 0.349958  0.482115 0.503671 0.0257981   0.0358489   -0.0371749  306 GLN   A NE2  
2413 O  OXT  . GLN   A 306 ? 0.159233  0.495568 0.296524 -0.0529463  0.0393454   -0.0609336  306 GLN   A OXT  
2414 N  N    . SER   B 1   ? 0.188353  0.232275 0.231451 0.0327586   -0.0282179  -0.0336047  1   SER   B N    
2415 C  CA   . SER   B 1   ? 0.185882  0.247135 0.233206 0.0368418   -0.0311548  -0.033121   1   SER   B CA   
2416 C  C    . SER   B 1   ? 0.17617   0.240412 0.232143 0.0474905   -0.0282323  -0.0283466  1   SER   B C    
2417 O  O    . SER   B 1   ? 0.160308  0.239607 0.229666 0.0400391   -0.0288962  -0.00888575 1   SER   B O    
2418 C  CB   . SER   B 1   ? 0.210299  0.268903 0.257412 0.046614    -0.0219871  -0.0369668  1   SER   B CB   
2419 O  OG   . SER   B 1   ? 0.224607  0.298861 0.252595 0.0594226   -0.0159047  -0.0371767  1   SER   B OG   
2420 N  N    . GLY   B 2   ? 0.183674  0.266033 0.228586 0.0590882   -0.046417   -0.0447106  2   GLY   B N    
2421 C  CA   . GLY   B 2   ? 0.187255  0.279243 0.214045 0.0647637   -0.0302384  -0.0481635  2   GLY   B CA   
2422 C  C    . GLY   B 2   ? 0.200239  0.301595 0.203598 0.0743081   -0.0311461  -0.0560296  2   GLY   B C    
2423 O  O    . GLY   B 2   ? 0.246463  0.333861 0.208024 0.0255641   -0.0366671  -0.031268   2   GLY   B O    
2424 N  N    . PHE   B 3   ? 0.202776  0.339192 0.199375 0.0935545   -0.0321016  -0.0585426  3   PHE   B N    
2425 C  CA   . PHE   B 3   ? 0.22239   0.342913 0.202384 0.110379    -0.0438308  -0.0671831  3   PHE   B CA   
2426 C  C    . PHE   B 3   ? 0.194458  0.355097 0.203548 0.104655    -0.0330273  -0.059227   3   PHE   B C    
2427 O  O    . PHE   B 3   ? 0.238521  0.435571 0.241363 0.104653    -0.0148715  -0.0671885  3   PHE   B O    
2428 C  CB   . PHE   B 3   ? 0.248636  0.339118 0.217639 0.12155     -0.0544501  -0.0798966  3   PHE   B CB   
2429 C  CG   . PHE   B 3   ? 0.262051  0.340518 0.225332 0.125638    -0.0687401  -0.0810533  3   PHE   B CG   
2430 C  CD1  . PHE   B 3   ? 0.263505  0.339998 0.254301 0.133166    -0.0750869  -0.079656   3   PHE   B CD1  
2431 C  CD2  . PHE   B 3   ? 0.27978   0.342739 0.248698 0.114175    -0.0719571  -0.0811165  3   PHE   B CD2  
2432 C  CE1  . PHE   B 3   ? 0.270997  0.347412 0.255171 0.122988    -0.0740786  -0.0801186  3   PHE   B CE1  
2433 C  CE2  . PHE   B 3   ? 0.275842  0.334528 0.243253 0.118915    -0.082822   -0.0780867  3   PHE   B CE2  
2434 C  CZ   . PHE   B 3   ? 0.267553  0.33565  0.250186 0.12896     -0.0911451  -0.0811084  3   PHE   B CZ   
2435 N  N    . ARG   B 4   ? 0.182436  0.340955 0.19289  0.10021     -0.0266745  -0.0442673  4   ARG   B N    
2436 C  CA   . ARG   B 4   ? 0.172717  0.329678 0.189319 0.0840457   -0.025303   -0.0216346  4   ARG   B CA   
2437 C  C    . ARG   B 4   ? 0.174687  0.303422 0.188698 0.0632472   -0.0268523  -0.0152382  4   ARG   B C    
2438 O  O    . ARG   B 4   ? 0.183111  0.289761 0.185222 0.0428433   -0.0342848  -0.014899   4   ARG   B O    
2439 C  CB   . ARG   B 4   ? 0.183574  0.330124 0.200144 0.0750855   -0.0275565  -0.00558744 4   ARG   B CB   
2440 C  CG   . ARG   B 4   ? 0.184844  0.350678 0.21799  0.0569209   -0.0424556  0.00014918  4   ARG   B CG   
2441 C  CD   . ARG   B 4   ? 0.199906  0.332837 0.239523 0.0437608   -0.0395702  0.00646603  4   ARG   B CD   
2442 N  NE   . ARG   B 4   ? 0.202351  0.322642 0.255438 0.0222467   -0.0296823  0.0254066   4   ARG   B NE   
2443 C  CZ   . ARG   B 4   ? 0.195537  0.332815 0.265251 0.0249813   -0.0415453  0.0392376   4   ARG   B CZ   
2444 N  NH1  . ARG   B 4   ? 0.180685  0.331922 0.277449 0.00249018  -0.0442036  0.0646616   4   ARG   B NH1  
2445 N  NH2  . ARG   B 4   ? 0.211169  0.324018 0.272392 0.0177165   -0.0182037  0.0317514   4   ARG   B NH2  
2446 N  N    . LYS   B 5   ? 0.160402  0.305486 0.191062 0.0503124   -0.0183048  -0.00545125 5   LYS   B N    
2447 C  CA   . LYS   B 5   ? 0.179077  0.293639 0.194476 0.0363448   -0.0253688  -0.00114001 5   LYS   B CA   
2448 C  C    . LYS   B 5   ? 0.179251  0.259423 0.191767 0.0208257   -0.0156379  0.00680351  5   LYS   B C    
2449 O  O    . LYS   B 5   ? 0.211504  0.261061 0.241236 0.0109235   0.0107912   0.0296546   5   LYS   B O    
2450 C  CB   . LYS   B 5   ? 0.210399  0.338959 0.221769 0.0167951   -0.0326876  -0.00534464 5   LYS   B CB   
2451 C  CG   . LYS   B 5   ? 0.247349  0.358823 0.226421 0.010266    -0.0461795  -0.0216382  5   LYS   B CG   
2452 C  CD   . LYS   B 5   ? 0.299697  0.382582 0.243346 0.0244207   -0.0529816  -0.0212579  5   LYS   B CD   
2453 C  CE   . LYS   B 5   ? 0.366201  0.365553 0.229992 0.0827507   -0.0342517  -0.0580829  5   LYS   B CE   
2454 N  N    . MET   B 6   ? 0.169982  0.218909 0.171128 0.0249715   -0.0238497  0.0118052   6   MET   B N    
2455 C  CA   . MET   B 6   ? 0.169864  0.22999  0.180429 0.021534    -0.0309676  -0.00309523 6   MET   B CA   
2456 C  C    . MET   B 6   ? 0.171594  0.205787 0.177493 0.0173675   -0.0369752  0.00364508  6   MET   B C    
2457 O  O    . MET   B 6   ? 0.241618  0.213388 0.179657 0.0189212   -0.0605927  0.00363402  6   MET   B O    
2458 C  CB   . MET   B 6   ? 0.193495  0.27933  0.224821 0.00266     -0.0375792  -0.0160127  6   MET   B CB   
2459 C  CG   . MET   B 6   ? 0.212961  0.324118 0.286198 0.00093489  -0.0356247  -0.0332016  6   MET   B CG   
2460 S  SD   . MET   B 6   ? 0.214935  0.439376 0.412494 -0.0364278  -0.040556   -0.0822521  6   MET   B SD   
2461 C  CE   . MET   B 6   ? 0.140724  0.328669 0.380104 -0.0373592  -0.0607328  -0.0676226  6   MET   B CE   
2462 N  N    . ALA   B 7   ? 0.142736  0.197429 0.174011 0.0205881   -0.0282979  0.00890325  7   ALA   B N    
2463 C  CA   . ALA   B 7   ? 0.134933  0.201214 0.181137 0.0211532   -0.0306349  0.00386402  7   ALA   B CA   
2464 C  C    . ALA   B 7   ? 0.123923  0.207515 0.172959 0.0181732   -0.0375636  -0.00029949 7   ALA   B C    
2465 O  O    . ALA   B 7   ? 0.118547  0.230817 0.170741 0.0182873   -0.0366423  0.00037544  7   ALA   B O    
2466 C  CB   . ALA   B 7   ? 0.140395  0.205347 0.198396 0.0194584   -0.0273343  0.00824174  7   ALA   B CB   
2467 N  N    . PHE   B 8   ? 0.137642  0.212875 0.170691 0.0248736   -0.031046   -0.0122119  8   PHE   B N    
2468 C  CA   . PHE   B 8   ? 0.14671   0.227217 0.178607 0.0297296   -0.0312986  -0.0202172  8   PHE   B CA   
2469 C  C    . PHE   B 8   ? 0.140342  0.221322 0.181748 0.0247073   -0.0364851  -0.0192352  8   PHE   B C    
2470 O  O    . PHE   B 8   ? 0.136117  0.219308 0.195435 0.024191    -0.0333863  -0.0119802  8   PHE   B O    
2471 C  CB   . PHE   B 8   ? 0.183474  0.234823 0.179234 0.0291141   -0.026651   -0.0209331  8   PHE   B CB   
2472 C  CG   . PHE   B 8   ? 0.231199  0.23919  0.179057 0.0331401   -0.0184675  -0.022438   8   PHE   B CG   
2473 C  CD1  . PHE   B 8   ? 0.269165  0.237256 0.208576 0.0280445   -0.00767255 -0.0160981  8   PHE   B CD1  
2474 C  CD2  . PHE   B 8   ? 0.269105  0.247885 0.199247 0.0456048   -0.0265012  -0.00748317 8   PHE   B CD2  
2475 C  CE1  . PHE   B 8   ? 0.303755  0.2487   0.225238 0.0196152   0.00543438  -0.00560293 8   PHE   B CE1  
2476 C  CE2  . PHE   B 8   ? 0.302566  0.251774 0.215619 0.0457455   -0.0170339  -0.0047209  8   PHE   B CE2  
2477 C  CZ   . PHE   B 8   ? 0.319486  0.24781  0.228217 0.0376663   -0.00119026 -0.00520942 8   PHE   B CZ   
2478 N  N    . PRO   B 9   ? 0.145953  0.240053 0.189423 0.0313026   -0.0356363  -0.0215035  9   PRO   B N    
2479 C  CA   . PRO   B 9   ? 0.147959  0.233959 0.185706 0.0321779   -0.0367961  -0.0242938  9   PRO   B CA   
2480 C  C    . PRO   B 9   ? 0.139416  0.237701 0.183607 0.0300981   -0.0381978  -0.0203157  9   PRO   B C    
2481 O  O    . PRO   B 9   ? 0.20042   0.253248 0.191243 0.00700131  -0.0342898  -0.0180922  9   PRO   B O    
2482 C  CB   . PRO   B 9   ? 0.1503    0.256254 0.200668 0.0322634   -0.0367632  -0.0303436  9   PRO   B CB   
2483 C  CG   . PRO   B 9   ? 0.15354   0.260319 0.226059 0.0317717   -0.0328152  -0.0270904  9   PRO   B CG   
2484 C  CD   . PRO   B 9   ? 0.15462   0.245968 0.195659 0.0282538   -0.0294368  -0.0281999  9   PRO   B CD   
2485 N  N    . SER   B 10  ? 0.145318  0.233258 0.170063 0.0324709   -0.0339569  -0.0193857  10  SER   B N    
2486 C  CA   . SER   B 10  ? 0.140804  0.227668 0.150966 0.0336858   -0.02363    -0.0218729  10  SER   B CA   
2487 C  C    . SER   B 10  ? 0.15035   0.229098 0.158754 0.0402441   -0.0275787  -0.0212564  10  SER   B C    
2488 O  O    . SER   B 10  ? 0.159741  0.222961 0.165971 0.0248897   -0.0268149  -0.0265527  10  SER   B O    
2489 C  CB   . SER   B 10  ? 0.138448  0.238923 0.159507 0.0393427   -0.0161555  -0.0233649  10  SER   B CB   
2490 O  OG   . SER   B 10  ? 0.142382  0.256328 0.154167 0.0364852   -0.0136993  -0.0185043  10  SER   B OG   
2491 N  N    . GLY   B 11  ? 0.153182  0.253767 0.167699 0.0480813   -0.0294537  -0.0277744  11  GLY   B N    
2492 C  CA   . GLY   B 11  ? 0.164228  0.252319 0.18057  0.0567392   -0.024965   -0.0204717  11  GLY   B CA   
2493 C  C    . GLY   B 11  ? 0.161657  0.259523 0.185626 0.0605861   -0.0194327  -0.0229941  11  GLY   B C    
2494 O  O    . GLY   B 11  ? 0.200519  0.253889 0.189524 0.0640507   0.00228602  -0.0285176  11  GLY   B O    
2495 N  N    . LYS   B 12  ? 0.162826  0.268988 0.171823 0.0557588   -0.0184877  -0.020744   12  LYS   B N    
2496 C  CA   . LYS   B 12  ? 0.169893  0.290138 0.177146 0.0533283   -0.0232649  -0.0197283  12  LYS   B CA   
2497 C  C    . LYS   B 12  ? 0.174913  0.280062 0.162504 0.048697    -0.0266856  -0.0237293  12  LYS   B C    
2498 O  O    . LYS   B 12  ? 0.194148  0.319693 0.169139 0.0642237   -0.0313179  -0.0410427  12  LYS   B O    
2499 C  CB   . LYS   B 12  ? 0.196749  0.319558 0.199293 0.0373888   -0.0145065  -0.00773256 12  LYS   B CB   
2500 C  CG   . LYS   B 12  ? 0.2198    0.366807 0.245988 0.0196497   -0.0244393  0.00173499  12  LYS   B CG   
2501 C  CD   . LYS   B 12  ? 0.264051  0.407858 0.314078 0.0110193   -0.0256685  0.0138452   12  LYS   B CD   
2502 C  CE   . LYS   B 12  ? 0.286356  0.462326 0.35798  0.00122568  -0.0120894  0.0108738   12  LYS   B CE   
2503 N  NZ   . LYS   B 12  ? 0.318798  0.50126  0.389858 0.00907648  -0.0239261  0.00619578  12  LYS   B NZ   
2504 N  N    . VAL   B 13  ? 0.161358  0.24069  0.156551 0.0423697   -0.0329018  -0.0215299  13  VAL   B N    
2505 C  CA   . VAL   B 13  ? 0.169404  0.231113 0.167032 0.0397639   -0.0364791  -0.0168969  13  VAL   B CA   
2506 C  C    . VAL   B 13  ? 0.162951  0.224973 0.170745 0.0451339   -0.0307748  -0.0225127  13  VAL   B C    
2507 O  O    . VAL   B 13  ? 0.167291  0.225476 0.165062 0.0494021   -0.0423156  -0.025341   13  VAL   B O    
2508 C  CB   . VAL   B 13  ? 0.166445  0.22321  0.185402 0.0383402   -0.038923   -0.0109961  13  VAL   B CB   
2509 C  CG1  . VAL   B 13  ? 0.176464  0.224328 0.190419 0.0307479   -0.0463012  -0.00384516 13  VAL   B CG1  
2510 C  CG2  . VAL   B 13  ? 0.179754  0.222273 0.1982   0.0428927   -0.0428981  -0.0130096  13  VAL   B CG2  
2511 N  N    . GLU   B 14  ? 0.178035  0.216375 0.164994 0.0394836   -0.0340457  -0.0248927  14  GLU   B N    
2512 C  CA   . GLU   B 14  ? 0.171635  0.214419 0.169535 0.0456115   -0.0276717  -0.0245459  14  GLU   B CA   
2513 C  C    . GLU   B 14  ? 0.184821  0.227933 0.167087 0.0519803   -0.0331677  -0.0259751  14  GLU   B C    
2514 O  O    . GLU   B 14  ? 0.219822  0.227663 0.190971 0.0418604   -0.0290013  -0.0333764  14  GLU   B O    
2515 C  CB   . GLU   B 14  ? 0.163636  0.214155 0.16872  0.0432273   -0.0255366  -0.0218021  14  GLU   B CB   
2516 C  CG   . GLU   B 14  ? 0.158592  0.220047 0.174529 0.0378694   -0.0277879  -0.0247998  14  GLU   B CG   
2517 C  CD   . GLU   B 14  ? 0.162407  0.226789 0.167915 0.0391764   -0.0239266  -0.0250911  14  GLU   B CD   
2518 O  OE1  . GLU   B 14  ? 0.149147  0.234209 0.179314 0.0344629   -0.0187019  -0.0271617  14  GLU   B OE1  
2519 O  OE2  . GLU   B 14  ? 0.199649  0.24188  0.182511 0.0379257   -0.0309503  -0.0135088  14  GLU   B OE2  
2520 N  N    . GLY   B 15  ? 0.191011  0.248322 0.16725  0.059558    -0.0322838  -0.0260121  15  GLY   B N    
2521 C  CA   . GLY   B 15  ? 0.194148  0.263818 0.182687 0.0686169   -0.0294315  -0.0360899  15  GLY   B CA   
2522 C  C    . GLY   B 15  ? 0.191195  0.26517  0.183913 0.075439    -0.02837    -0.0348472  15  GLY   B C    
2523 O  O    . GLY   B 15  ? 0.220268  0.289053 0.209539 0.0908271   -0.0319488  -0.0571394  15  GLY   B O    
2524 N  N    . CYS   B 16  ? 0.166977  0.247266 0.160725 0.0614906   -0.0189768  -0.0329984  16  CYS   B N    
2525 C  CA   . CYS   B 16  ? 0.179773  0.253545 0.163552 0.0410661   -0.0232119  -0.027159   16  CYS   B CA   
2526 C  C    . CYS   B 16  ? 0.176408  0.234534 0.154008 0.0480949   -0.00964037 -0.0179723  16  CYS   B C    
2527 O  O    . CYS   B 16  ? 0.19375   0.255841 0.150183 0.0376212   -0.0127159  -0.0130067  16  CYS   B O    
2528 C  CB   . CYS   B 16  ? 0.179139  0.258526 0.168309 0.0242398   -0.0332961  -0.0202875  16  CYS   B CB   
2529 S  SG   . CYS   B 16  ? 0.195779  0.297877 0.194915 -0.00395802 -0.0273546  -0.00385868 16  CYS   B SG   
2530 N  N    . MET   B 17  ? 0.177851  0.222047 0.162473 0.0460349   -0.0173894  -0.0110663  17  MET   B N    
2531 C  CA   . MET   B 17  ? 0.174561  0.215749 0.175322 0.0421598   -0.0254551  -0.0214423  17  MET   B CA   
2532 C  C    . MET   B 17  ? 0.185211  0.20808  0.177237 0.0448959   -0.0214852  -0.0115549  17  MET   B C    
2533 O  O    . MET   B 17  ? 0.206073  0.223586 0.222184 0.0531092   -0.0300448  0.001435    17  MET   B O    
2534 C  CB   . MET   B 17  ? 0.171864  0.229242 0.181255 0.038916    -0.0163359  -0.017967   17  MET   B CB   
2535 C  CG   . MET   B 17  ? 0.17762   0.230782 0.174826 0.0310247   -0.0117909  -0.0276144  17  MET   B CG   
2536 S  SD   . MET   B 17  ? 0.1874    0.224967 0.195226 0.0305226   -0.0136833  -0.03028    17  MET   B SD   
2537 C  CE   . MET   B 17  ? 0.192862  0.250456 0.178631 0.0226749   -0.0275448  -0.0426509  17  MET   B CE   
2538 N  N    . VAL   B 18  ? 0.186913  0.204453 0.17746  0.0294251   -0.00894517 -0.0227726  18  VAL   B N    
2539 C  CA   . VAL   B 18  ? 0.210911  0.202079 0.187149 0.0319016   -0.00711724 -0.0243611  18  VAL   B CA   
2540 C  C    . VAL   B 18  ? 0.23111   0.200006 0.187874 0.0173336   0.00390627  -0.0257752  18  VAL   B C    
2541 O  O    . VAL   B 18  ? 0.207819  0.194024 0.192934 0.0118485   0.0137568   -0.0157429  18  VAL   B O    
2542 C  CB   . VAL   B 18  ? 0.21096   0.199529 0.188723 0.0308854   -0.00837201 -0.0299916  18  VAL   B CB   
2543 C  CG1  . VAL   B 18  ? 0.216477  0.219704 0.202009 0.0305575   -0.00775388 -0.0246393  18  VAL   B CG1  
2544 C  CG2  . VAL   B 18  ? 0.202584  0.207599 0.18368  0.019995    -0.0140703  -0.0317383  18  VAL   B CG2  
2545 N  N    . GLN   B 19  ? 0.26932   0.207661 0.229105 0.0115301   0.0156398   -0.0263532  19  GLN   B N    
2546 C  CA   . GLN   B 19  ? 0.289777  0.216304 0.240469 -0.0106847  0.0291933   -0.0374721  19  GLN   B CA   
2547 C  C    . GLN   B 19  ? 0.287724  0.226896 0.253583 -0.0168019  0.0322465   -0.0533534  19  GLN   B C    
2548 O  O    . GLN   B 19  ? 0.293932  0.252745 0.249041 0.00302481  0.0306477   -0.0582631  19  GLN   B O    
2549 C  CB   . GLN   B 19  ? 0.346233  0.239875 0.292185 -0.0232401  0.0155845   -0.0240043  19  GLN   B CB   
2550 C  CG   . GLN   B 19  ? 0.373207  0.274378 0.333734 -0.0453412  0.0265839   -0.0222263  19  GLN   B CG   
2551 C  CD   . GLN   B 19  ? 0.463093  0.318765 0.39074  -0.0350312  0.0137999   0.00258378  19  GLN   B CD   
2552 O  OE1  . GLN   B 19  ? 0.534936  0.387691 0.412704 -0.056558   0.0186282   0.0280202   19  GLN   B OE1  
2553 N  NE2  . GLN   B 19  ? 0.511129  0.302544 0.447624 -0.018855   0.0123647   0.0146345   19  GLN   B NE2  
2554 N  N    . VAL   B 20  ? 0.271693  0.204564 0.248246 -0.0214759  0.0593138   -0.0571547  20  VAL   B N    
2555 C  CA   . VAL   B 20  ? 0.263194  0.213444 0.255645 -0.0423175  0.0607317   -0.0635494  20  VAL   B CA   
2556 C  C    . VAL   B 20  ? 0.28227   0.22862  0.286761 -0.0605081  0.0651913   -0.0734332  20  VAL   B C    
2557 O  O    . VAL   B 20  ? 0.294489  0.23145  0.259807 -0.0574245  0.053904    -0.0743214  20  VAL   B O    
2558 C  CB   . VAL   B 20  ? 0.251611  0.221597 0.256184 -0.0370067  0.0588277   -0.0606853  20  VAL   B CB   
2559 C  CG1  . VAL   B 20  ? 0.251781  0.237721 0.268365 -0.0277677  0.0502291   -0.0612365  20  VAL   B CG1  
2560 C  CG2  . VAL   B 20  ? 0.254058  0.221    0.251312 -0.0416248  0.0591445   -0.0459964  20  VAL   B CG2  
2561 N  N    . THR   B 21  ? 0.325176  0.243604 0.33086  -0.0716746  0.095855    -0.102764   21  THR   B N    
2562 C  CA   . THR   B 21  ? 0.337615  0.261702 0.362749 -0.0917984  0.101084    -0.123073   21  THR   B CA   
2563 C  C    . THR   B 21  ? 0.351876  0.29865  0.365557 -0.10484    0.104899    -0.143901   21  THR   B C    
2564 O  O    . THR   B 21  ? 0.340651  0.336105 0.384452 -0.0997747  0.11222     -0.167385   21  THR   B O    
2565 C  CB   . THR   B 21  ? 0.370781  0.264414 0.403964 -0.104858   0.107402    -0.104238   21  THR   B CB   
2566 O  OG1  . THR   B 21  ? 0.405946  0.289668 0.425555 -0.0919241  0.103063    -0.0876307  21  THR   B OG1  
2567 C  CG2  . THR   B 21  ? 0.389462  0.277283 0.437156 -0.107985   0.0980799   -0.106345   21  THR   B CG2  
2568 N  N    . CYS   B 22  ? 0.347687  0.303962 0.363569 -0.115078   0.0984764   -0.154976   22  CYS   B N    
2569 C  CA   . CYS   B 22  ? 0.356409  0.322109 0.367641 -0.138546   0.101152    -0.166234   22  CYS   B CA   
2570 C  C    . CYS   B 22  ? 0.357077  0.315037 0.396157 -0.146691   0.0968784   -0.167169   22  CYS   B C    
2571 O  O    . CYS   B 22  ? 0.35465   0.32671  0.423641 -0.135062   0.100413    -0.154235   22  CYS   B O    
2572 C  CB   . CYS   B 22  ? 0.360986  0.346462 0.373201 -0.12583    0.103637    -0.17803    22  CYS   B CB   
2573 S  SG   . CYS   B 22  ? 0.372853  0.401657 0.404991 -0.154556   0.0983235   -0.166465   22  CYS   B SG   
2574 N  N    . GLY   B 23  ? 0.3803    0.310792 0.425866 -0.144809   0.0967761   -0.155955   23  GLY   B N    
2575 C  CA   . GLY   B 23  ? 0.378628  0.321332 0.441606 -0.151802   0.0847457   -0.149017   23  GLY   B CA   
2576 C  C    . GLY   B 23  ? 0.392264  0.310573 0.446483 -0.153749   0.0894265   -0.135315   23  GLY   B C    
2577 O  O    . GLY   B 23  ? 0.438364  0.328969 0.487041 -0.139128   0.103503    -0.114239   23  GLY   B O    
2578 N  N    . THR   B 24  ? 0.387341  0.307962 0.430175 -0.159815   0.078985    -0.120511   24  THR   B N    
2579 C  CA   . THR   B 24  ? 0.397536  0.314298 0.415742 -0.141663   0.0758804   -0.11907    24  THR   B CA   
2580 C  C    . THR   B 24  ? 0.372458  0.26986  0.395548 -0.130163   0.0777576   -0.0879137  24  THR   B C    
2581 O  O    . THR   B 24  ? 0.383762  0.270473 0.402599 -0.130532   0.0657489   -0.0860318  24  THR   B O    
2582 C  CB   . THR   B 24  ? 0.404555  0.340945 0.417348 -0.139822   0.0671849   -0.132126   24  THR   B CB   
2583 O  OG1  . THR   B 24  ? 0.411871  0.37738  0.431336 -0.1374     0.0564388   -0.103142   24  THR   B OG1  
2584 C  CG2  . THR   B 24  ? 0.426331  0.350717 0.431238 -0.137955   0.0609028   -0.13623    24  THR   B CG2  
2585 N  N    . THR   B 25  ? 0.331145  0.264909 0.364062 -0.117347   0.0680248   -0.0827802  25  THR   B N    
2586 C  CA   . THR   B 25  ? 0.30897   0.265864 0.345061 -0.107712   0.0584607   -0.080956   25  THR   B CA   
2587 C  C    . THR   B 25  ? 0.304601  0.262833 0.326236 -0.0974774  0.0595195   -0.0735794  25  THR   B C    
2588 O  O    . THR   B 25  ? 0.323394  0.288534 0.317569 -0.0848674  0.0549211   -0.0906981  25  THR   B O    
2589 C  CB   . THR   B 25  ? 0.309123  0.275019 0.337529 -0.112607   0.0343522   -0.0825842  25  THR   B CB   
2590 O  OG1  . THR   B 25  ? 0.309312  0.318093 0.331458 -0.108987   0.028165    -0.0873995  25  THR   B OG1  
2591 C  CG2  . THR   B 25  ? 0.310028  0.271209 0.337629 -0.110565   0.0256764   -0.0782704  25  THR   B CG2  
2592 N  N    . THR   B 26  ? 0.288548  0.226566 0.321854 -0.0920856  0.0574222   -0.0705046  26  THR   B N    
2593 C  CA   . THR   B 26  ? 0.286528  0.213178 0.319956 -0.083472   0.0609291   -0.0508155  26  THR   B CA   
2594 C  C    . THR   B 26  ? 0.25856   0.219648 0.269499 -0.0784442  0.0524757   -0.0513824  26  THR   B C    
2595 O  O    . THR   B 26  ? 0.257256  0.22976  0.293084 -0.0824795  0.0697843   -0.0415394  26  THR   B O    
2596 C  CB   . THR   B 26  ? 0.321927  0.224588 0.363119 -0.0676621  0.0508176   -0.044625   26  THR   B CB   
2597 O  OG1  . THR   B 26  ? 0.376489  0.22892  0.430298 -0.0538424  0.0538231   -0.0577491  26  THR   B OG1  
2598 C  CG2  . THR   B 26  ? 0.339718  0.229877 0.380044 -0.0664299  0.0455119   -0.0382307  26  THR   B CG2  
2599 N  N    . LEU   B 27  ? 0.236055  0.2065   0.251181 -0.06432    0.0417285   -0.0465656  27  LEU   B N    
2600 C  CA   . LEU   B 27  ? 0.229495  0.200185 0.235074 -0.051414   0.0274662   -0.0426089  27  LEU   B CA   
2601 C  C    . LEU   B 27  ? 0.215355  0.186797 0.214965 -0.0314292  0.0163016   -0.0396322  27  LEU   B C    
2602 O  O    . LEU   B 27  ? 0.239985  0.193591 0.250828 -0.0276807  0.0186478   -0.0553364  27  LEU   B O    
2603 C  CB   . LEU   B 27  ? 0.203906  0.218968 0.226649 -0.0552227  0.0259623   -0.0445597  27  LEU   B CB   
2604 C  CG   . LEU   B 27  ? 0.210782  0.221901 0.227111 -0.0468394  0.0150113   -0.0408396  27  LEU   B CG   
2605 C  CD1  . LEU   B 27  ? 0.203014  0.220858 0.220335 -0.0399428  0.00883491  -0.0333727  27  LEU   B CD1  
2606 C  CD2  . LEU   B 27  ? 0.208082  0.23066  0.225463 -0.0419371  0.0149033   -0.052354   27  LEU   B CD2  
2607 N  N    . ASN   B 28  ? 0.195583  0.181823 0.193104 -0.017603   0.00263924  -0.0269312  28  ASN   B N    
2608 C  CA   . ASN   B 28  ? 0.189745  0.172179 0.183202 -0.0091042  -0.00112785 -0.0232568  28  ASN   B CA   
2609 C  C    . ASN   B 28  ? 0.185022  0.182058 0.180019 -0.00376719 -0.00684369 -0.0253205  28  ASN   B C    
2610 O  O    . ASN   B 28  ? 0.18384   0.197875 0.177515 0.00922588  0.00317782  -0.0178664  28  ASN   B O    
2611 C  CB   . ASN   B 28  ? 0.183934  0.165265 0.16824  -0.00309831 -0.002622   -0.0167411  28  ASN   B CB   
2612 C  CG   . ASN   B 28  ? 0.188476  0.176096 0.166983 0.00738257  -0.00351384 -0.0118587  28  ASN   B CG   
2613 O  OD1  . ASN   B 28  ? 0.209131  0.174245 0.181621 0.00878854  0.0036471   -0.00454746 28  ASN   B OD1  
2614 N  ND2  . ASN   B 28  ? 0.196508  0.200573 0.169351 0.00895534  0.00022054  -0.00971591 28  ASN   B ND2  
2615 N  N    . GLY   B 29  ? 0.179246  0.194805 0.163928 0.0028706   -0.00680756 -0.0220584  29  GLY   B N    
2616 C  CA   . GLY   B 29  ? 0.172658  0.191205 0.169753 -0.00442919 -0.00942047 -0.0216914  29  GLY   B CA   
2617 C  C    . GLY   B 29  ? 0.158071  0.190815 0.16148  0.00979082  -0.0143527  -0.0193571  29  GLY   B C    
2618 O  O    . GLY   B 29  ? 0.149953  0.1954   0.164343 0.0136631   -0.00696444 -0.012282   29  GLY   B O    
2619 N  N    . LEU   B 30  ? 0.135213  0.1978   0.155833 0.00663268  -0.00940355 -0.0191789  30  LEU   B N    
2620 C  CA   . LEU   B 30  ? 0.129356  0.200848 0.147388 0.0100455   -0.00636365 -0.0218564  30  LEU   B CA   
2621 C  C    . LEU   B 30  ? 0.138735  0.207738 0.155083 0.0278268   -0.00604981 -0.0266412  30  LEU   B C    
2622 O  O    . LEU   B 30  ? 0.143994  0.218998 0.161664 0.0314278   -0.00967935 -0.0226185  30  LEU   B O    
2623 C  CB   . LEU   B 30  ? 0.131178  0.202764 0.152404 0.00710408  -0.00597912 -0.0241677  30  LEU   B CB   
2624 C  CG   . LEU   B 30  ? 0.137744  0.204531 0.15986  0.00472714  0.00137555  -0.0213903  30  LEU   B CG   
2625 C  CD1  . LEU   B 30  ? 0.140801  0.209288 0.176814 -0.00018708 -0.0130107  -0.0181702  30  LEU   B CD1  
2626 C  CD2  . LEU   B 30  ? 0.138769  0.209715 0.155545 0.00399005  0.0006171   -0.0146142  30  LEU   B CD2  
2627 N  N    . TRP   B 31  ? 0.131353  0.216157 0.161889 0.0340626   -0.00341607 -0.0333788  31  TRP   B N    
2628 C  CA   . TRP   B 31  ? 0.129394  0.219007 0.165814 0.0383179   -0.00816155 -0.0320741  31  TRP   B CA   
2629 C  C    . TRP   B 31  ? 0.120625  0.225192 0.163423 0.0332969   -0.0119119  -0.0250181  31  TRP   B C    
2630 O  O    . TRP   B 31  ? 0.114419  0.234642 0.164992 0.0259074   -0.0125592  -0.0310179  31  TRP   B O    
2631 C  CB   . TRP   B 31  ? 0.14625   0.226862 0.190054 0.0516983   -0.00784527 -0.0341795  31  TRP   B CB   
2632 C  CG   . TRP   B 31  ? 0.157597  0.252653 0.211531 0.0638491   -0.00809599 -0.0428881  31  TRP   B CG   
2633 C  CD1  . TRP   B 31  ? 0.164852  0.263574 0.218826 0.0748982   -0.0111734  -0.0538669  31  TRP   B CD1  
2634 C  CD2  . TRP   B 31  ? 0.189899  0.263044 0.233774 0.0747327   -0.0155333  -0.0454854  31  TRP   B CD2  
2635 N  NE1  . TRP   B 31  ? 0.184178  0.277596 0.237315 0.0846469   -0.0104176  -0.0585131  31  TRP   B NE1  
2636 C  CE2  . TRP   B 31  ? 0.182636  0.272735 0.246353 0.082257    -0.00773471 -0.0499804  31  TRP   B CE2  
2637 C  CE3  . TRP   B 31  ? 0.201485  0.26616  0.250022 0.0709368   -0.00749758 -0.035337   31  TRP   B CE3  
2638 C  CZ2  . TRP   B 31  ? 0.203289  0.278663 0.266346 0.0882195   -0.00518961 -0.0494145  31  TRP   B CZ2  
2639 C  CZ3  . TRP   B 31  ? 0.210121  0.28639  0.275127 0.0788257   -0.0162489  -0.0339272  31  TRP   B CZ3  
2640 C  CH2  . TRP   B 31  ? 0.199398  0.279557 0.285513 0.0882983   -0.0114476  -0.0413635  31  TRP   B CH2  
2641 N  N    . LEU   B 32  ? 0.122828  0.244434 0.166575 0.0283974   -0.00614809 -0.02501    32  LEU   B N    
2642 C  CA   . LEU   B 32  ? 0.124427  0.255681 0.16918  0.023685    0.00169157  -0.0307381  32  LEU   B CA   
2643 C  C    . LEU   B 32  ? 0.124124  0.292112 0.178596 0.0254689   0.0124631   -0.0404683  32  LEU   B C    
2644 O  O    . LEU   B 32  ? 0.135621  0.288241 0.161118 0.0250895   0.0108309   -0.0427663  32  LEU   B O    
2645 C  CB   . LEU   B 32  ? 0.12705   0.25147  0.175247 0.0261362   0.012279    -0.0262698  32  LEU   B CB   
2646 C  CG   . LEU   B 32  ? 0.150622  0.240786 0.181562 0.0329685   0.0180265   -0.0276413  32  LEU   B CG   
2647 C  CD1  . LEU   B 32  ? 0.151899  0.238801 0.186178 0.0378149   0.0224892   -0.0274993  32  LEU   B CD1  
2648 C  CD2  . LEU   B 32  ? 0.181714  0.246901 0.182656 0.0497558   0.00805146  -0.0293731  32  LEU   B CD2  
2649 N  N    . ASP   B 33  ? 0.126152  0.339482 0.203969 0.0260314   0.0111753   -0.0676376  33  ASP   B N    
2650 C  CA   . ASP   B 33  ? 0.151388  0.352095 0.220664 0.0294487   0.0198065   -0.0841291  33  ASP   B CA   
2651 C  C    . ASP   B 33  ? 0.148534  0.34303  0.217052 0.0398498   0.0222187   -0.0850803  33  ASP   B C    
2652 O  O    . ASP   B 33  ? 0.162097  0.35757  0.240822 0.0638056   -0.00096552 -0.0844523  33  ASP   B O    
2653 C  CB   . ASP   B 33  ? 0.203033  0.388372 0.230599 0.0116615   0.0415661   -0.0863935  33  ASP   B CB   
2654 C  CG   . ASP   B 33  ? 0.245841  0.403363 0.279461 0.00847925  0.0623221   -0.0883972  33  ASP   B CG   
2655 O  OD1  . ASP   B 33  ? 0.28735   0.474421 0.337808 0.0210558   0.0405081   -0.101561   33  ASP   B OD1  
2656 O  OD2  . ASP   B 33  ? 0.414895  0.422129 0.306373 0.01107     0.0344569   -0.0934293  33  ASP   B OD2  
2657 N  N    . ASP   B 34  ? 0.148226  0.338451 0.220648 0.0359194   0.0143235   -0.0797674  34  ASP   B N    
2658 C  CA   . ASP   B 34  ? 0.15453   0.312857 0.204926 0.0381304   0.0136865   -0.0690651  34  ASP   B CA   
2659 C  C    . ASP   B 34  ? 0.152624  0.283952 0.186511 0.0247044   0.00389577  -0.0631101  34  ASP   B C    
2660 O  O    . ASP   B 34  ? 0.160629  0.27659  0.192812 0.0195697   0.00395021  -0.0606295  34  ASP   B O    
2661 C  CB   . ASP   B 34  ? 0.167383  0.344442 0.213769 0.0396952   0.0244669   -0.0768858  34  ASP   B CB   
2662 C  CG   . ASP   B 34  ? 0.205601  0.364316 0.218107 0.0336882   0.0407138   -0.0677941  34  ASP   B CG   
2663 O  OD1  . ASP   B 34  ? 0.239791  0.373681 0.215775 0.0213971   0.0317675   -0.0615911  34  ASP   B OD1  
2664 O  OD2  . ASP   B 34  ? 0.309723  0.404005 0.222982 0.0467425   0.0384111   -0.0749691  34  ASP   B OD2  
2665 N  N    . VAL   B 35  ? 0.145932  0.258487 0.174072 0.0220209   -0.00359512 -0.046396   35  VAL   B N    
2666 C  CA   . VAL   B 35  ? 0.14525   0.245909 0.179816 0.00682277  0.00257585  -0.0344887  35  VAL   B CA   
2667 C  C    . VAL   B 35  ? 0.145998  0.220487 0.178243 0.00800765  0.00535027  -0.0411589  35  VAL   B C    
2668 O  O    . VAL   B 35  ? 0.144471  0.252445 0.172218 0.00194521  0.0081789   -0.0428605  35  VAL   B O    
2669 C  CB   . VAL   B 35  ? 0.16252   0.254383 0.193518 -0.00056869 -0.00082199 -0.0194143  35  VAL   B CB   
2670 C  CG1  . VAL   B 35  ? 0.165455  0.246605 0.193767 0.00643488  -0.00458263 -0.0114154  35  VAL   B CG1  
2671 C  CG2  . VAL   B 35  ? 0.182421  0.26783  0.200073 -0.00729725 0.00966781  -0.00701181 35  VAL   B CG2  
2672 N  N    . VAL   B 36  ? 0.152213  0.215938 0.173858 0.00548748  0.00155133  -0.0403504  36  VAL   B N    
2673 C  CA   . VAL   B 36  ? 0.149981  0.21428  0.177507 0.00874637  0.00097192  -0.0425199  36  VAL   B CA   
2674 C  C    . VAL   B 36  ? 0.140049  0.20855  0.170225 0.00265474  -0.00327272 -0.0407852  36  VAL   B C    
2675 O  O    . VAL   B 36  ? 0.140038  0.227104 0.177049 0.00194492  -0.0058539  -0.0536072  36  VAL   B O    
2676 C  CB   . VAL   B 36  ? 0.158453  0.219956 0.195054 0.00765367  0.00594146  -0.036337   36  VAL   B CB   
2677 C  CG1  . VAL   B 36  ? 0.166106  0.225522 0.201059 0.0101995   0.00626851  -0.0366336  36  VAL   B CG1  
2678 C  CG2  . VAL   B 36  ? 0.170269  0.233878 0.197596 0.0159886   0.0136501   -0.0362312  36  VAL   B CG2  
2679 N  N    . TYR   B 37  ? 0.1262    0.200402 0.165445 0.0115115   -0.00789675 -0.0313971  37  TYR   B N    
2680 C  CA   . TYR   B 37  ? 0.11564   0.204988 0.154005 0.00890482  -0.0105085  -0.0232456  37  TYR   B CA   
2681 C  C    . TYR   B 37  ? 0.125877  0.202568 0.156186 -0.00279866 -0.0110943  -0.0202323  37  TYR   B C    
2682 O  O    . TYR   B 37  ? 0.139041  0.215385 0.160238 -1.614e-05  -0.0145288  -0.0147845  37  TYR   B O    
2683 C  CB   . TYR   B 37  ? 0.122927  0.200264 0.158503 0.00293608  -0.0073439  -0.0173884  37  TYR   B CB   
2684 C  CG   . TYR   B 37  ? 0.13528   0.207947 0.174281 -0.00234843 -0.00011359 -0.0114365  37  TYR   B CG   
2685 C  CD1  . TYR   B 37  ? 0.136359  0.222824 0.181698 -0.00817483 0.00193386  -0.00659145 37  TYR   B CD1  
2686 C  CD2  . TYR   B 37  ? 0.145519  0.230683 0.184705 -0.00060648 0.00622373  0.00112312  37  TYR   B CD2  
2687 C  CE1  . TYR   B 37  ? 0.133386  0.234559 0.193268 -0.00863801 0.00726249  -0.00451278 37  TYR   B CE1  
2688 C  CE2  . TYR   B 37  ? 0.140502  0.24007  0.17955  -0.00195109 0.00695769  0.00299053  37  TYR   B CE2  
2689 C  CZ   . TYR   B 37  ? 0.144874  0.24075  0.19808  -0.00687572 0.0114548   0.00259715  37  TYR   B CZ   
2690 O  OH   . TYR   B 37  ? 0.175415  0.269804 0.210482 -0.0113923  0.0288559   0.0149127   37  TYR   B OH   
2691 N  N    . CYS   B 38  ? 0.127397  0.209501 0.152532 -0.00166445 -0.0125512  -0.0169184  38  CYS   B N    
2692 C  CA   . CYS   B 38  ? 0.125905  0.20434  0.165284 -0.00833008 -0.00825685 -0.0174529  38  CYS   B CA   
2693 C  C    . CYS   B 38  ? 0.13032   0.205104 0.15492  -0.00408623 -0.00792038 -0.0105141  38  CYS   B C    
2694 O  O    . CYS   B 38  ? 0.135517  0.228137 0.159534 -0.00528342 -0.00915272 -0.00692544 38  CYS   B O    
2695 C  CB   . CYS   B 38  ? 0.136293  0.202734 0.185351 -0.00491773 -0.0032253  -0.0159926  38  CYS   B CB   
2696 S  SG   . CYS   B 38  ? 0.17489   0.228524 0.239295 -0.0185523  -0.0186798  -0.039795   38  CYS   B SG   
2697 N  N    . PRO   B 39  ? 0.134172  0.216109 0.151558 -0.0114407  -0.00925462 -0.00787583 39  PRO   B N    
2698 C  CA   . PRO   B 39  ? 0.130064  0.205378 0.158448 -0.0138499  -0.0142939  -0.00933237 39  PRO   B CA   
2699 C  C    . PRO   B 39  ? 0.135442  0.221695 0.163722 -0.0142897  -0.0120443  -0.0203156  39  PRO   B C    
2700 O  O    . PRO   B 39  ? 0.131849  0.225297 0.179484 -0.0164859  -0.0278277  -0.0233682  39  PRO   B O    
2701 C  CB   . PRO   B 39  ? 0.139678  0.219865 0.156463 -0.0169629  -0.0119447  -0.00926983 39  PRO   B CB   
2702 C  CG   . PRO   B 39  ? 0.136688  0.215489 0.151069 -0.0174898  -0.0137705  -0.00994734 39  PRO   B CG   
2703 C  CD   . PRO   B 39  ? 0.141391  0.216345 0.155191 -0.0137323  -0.0158197  -0.00897533 39  PRO   B CD   
2704 N  N    . ARG   B 40  ? 0.123857  0.225189 0.1643   -0.0117912  -0.0177919  -0.0349088  40  ARG   B N    
2705 C  CA   . ARG   B 40  ? 0.132028  0.24173  0.169546 -0.010718   -0.0213012  -0.0429505  40  ARG   B CA   
2706 C  C    . ARG   B 40  ? 0.136779  0.254547 0.1687   -0.0185134  -0.0219421  -0.0448704  40  ARG   B C    
2707 O  O    . ARG   B 40  ? 0.157801  0.25973  0.186257 -0.0213421  -0.0219893  -0.0503797  40  ARG   B O    
2708 C  CB   . ARG   B 40  ? 0.132712  0.251299 0.160769 -0.00514582 -0.0154292  -0.0412514  40  ARG   B CB   
2709 C  CG   . ARG   B 40  ? 0.127575  0.25656  0.155974 -0.00091734 -0.0244552  -0.0331898  40  ARG   B CG   
2710 C  CD   . ARG   B 40  ? 0.124869  0.261109 0.156412 -0.00230711 -0.0166002  -0.0285906  40  ARG   B CD   
2711 N  NE   . ARG   B 40  ? 0.123454  0.273544 0.158781 0.00183516  -0.0303327  -0.0263935  40  ARG   B NE   
2712 C  CZ   . ARG   B 40  ? 0.133298  0.288037 0.171233 0.0082977   -0.0317312  -0.0231448  40  ARG   B CZ   
2713 N  NH1  . ARG   B 40  ? 0.127375  0.301916 0.169126 0.00452322  -0.0257754  -0.0186697  40  ARG   B NH1  
2714 N  NH2  . ARG   B 40  ? 0.125681  0.296501 0.178704 0.00726455  -0.0295744  -0.0226703  40  ARG   B NH2  
2715 N  N    . HIS   B 41  ? 0.13418   0.255851 0.17912  -0.0363112  -0.0159746  -0.0521125  41  HIS   B N    
2716 C  CA   . HIS   B 41  ? 0.160376  0.263306 0.189155 -0.047202   -0.00309736 -0.0481836  41  HIS   B CA   
2717 C  C    . HIS   B 41  ? 0.17194   0.259428 0.207018 -0.0586527  0.00461863  -0.0585433  41  HIS   B C    
2718 O  O    . HIS   B 41  ? 0.193929  0.259775 0.210523 -0.0770976  0.0164652   -0.0637463  41  HIS   B O    
2719 C  CB   . HIS   B 41  ? 0.156581  0.258932 0.193166 -0.0500943  0.00855763  -0.0431424  41  HIS   B CB   
2720 C  CG   . HIS   B 41  ? 0.155876  0.261614 0.18743  -0.0389142  0.0107822   -0.0366198  41  HIS   B CG   
2721 N  ND1  . HIS   B 41  ? 0.170722  0.263613 0.196408 -0.0493978  0.00607595  -0.0322451  41  HIS   B ND1  
2722 C  CD2  . HIS   B 41  ? 0.164958  0.265601 0.196483 -0.0425276  0.00440707  -0.0272711  41  HIS   B CD2  
2723 C  CE1  . HIS   B 41  ? 0.170685  0.265705 0.193818 -0.0486776  -0.00023777 -0.0313929  41  HIS   B CE1  
2724 N  NE2  . HIS   B 41  ? 0.166649  0.266983 0.19527  -0.0465382  0.0062492   -0.0215143  41  HIS   B NE2  
2725 N  N    . VAL   B 42  ? 0.1737    0.249902 0.219231 -0.0627471  0.00194742  -0.0629038  42  VAL   B N    
2726 C  CA   . VAL   B 42  ? 0.190116  0.251625 0.232428 -0.0618235  -0.00250711 -0.0686596  42  VAL   B CA   
2727 C  C    . VAL   B 42  ? 0.203495  0.278625 0.256155 -0.0705864  0.00739502  -0.0949037  42  VAL   B C    
2728 O  O    . VAL   B 42  ? 0.242357  0.287128 0.286746 -0.0829094  0.0123857   -0.0971565  42  VAL   B O    
2729 C  CB   . VAL   B 42  ? 0.189761  0.237594 0.239678 -0.0631301  -0.00508947 -0.0642508  42  VAL   B CB   
2730 C  CG1  . VAL   B 42  ? 0.189315  0.231533 0.241563 -0.0597865  -0.00472178 -0.0636305  42  VAL   B CG1  
2731 C  CG2  . VAL   B 42  ? 0.203375  0.234253 0.247032 -0.0646305  -0.00930695 -0.0673223  42  VAL   B CG2  
2732 N  N    . ILE   B 43  ? 0.188901  0.309175 0.257871 -0.0753953  -0.00350317 -0.120188   43  ILE   B N    
2733 C  CA   . ILE   B 43  ? 0.1937    0.343018 0.271603 -0.0826977  -0.00164802 -0.135507   43  ILE   B CA   
2734 C  C    . ILE   B 43  ? 0.199736  0.373749 0.289451 -0.0838913  0.0122443   -0.13111    43  ILE   B C    
2735 O  O    . ILE   B 43  ? 0.213283  0.395833 0.332644 -0.0859654  0.0168701   -0.160173   43  ILE   B O    
2736 C  CB   . ILE   B 43  ? 0.21418   0.382557 0.26031  -0.0777449  -0.00649098 -0.146428   43  ILE   B CB   
2737 C  CG1  . ILE   B 43  ? 0.229519  0.397537 0.26412  -0.0758817  -0.0103978  -0.141955   43  ILE   B CG1  
2738 C  CG2  . ILE   B 43  ? 0.218061  0.394788 0.269049 -0.0590379  0.016597    -0.139211   43  ILE   B CG2  
2739 C  CD1  . ILE   B 43  ? 0.237982  0.410703 0.270094 -0.064827   -0.0158808  -0.135986   43  ILE   B CD1  
2740 N  N    . CYS   B 44  ? 0.183409  0.3543   0.299549 -0.0942769  0.00748217  -0.133737   44  CYS   B N    
2741 C  CA   . CYS   B 44  ? 0.181896  0.366334 0.306231 -0.0989498  0.00047191  -0.122482   44  CYS   B CA   
2742 C  C    . CYS   B 44  ? 0.205629  0.369746 0.327372 -0.0978039  -0.00099114 -0.121421   44  CYS   B C    
2743 O  O    . CYS   B 44  ? 0.226464  0.410124 0.338017 -0.0733863  0.0014777   -0.101982   44  CYS   B O    
2744 C  CB   . CYS   B 44  ? 0.187973  0.364132 0.307829 -0.0942457  0.00748389  -0.108761   44  CYS   B CB   
2745 S  SG   . CYS   B 44  ? 0.226909  0.380938 0.313866 -0.0595752  0.00348711  -0.0965127  44  CYS   B SG   
2746 N  N    . THR   B 45  ? 0.217096  0.379728 0.360392 -0.11133    0.00389603  -0.125642   45  THR   B N    
2747 C  CA   . THR   B 45  ? 0.223956  0.385277 0.385141 -0.109319   0.00118264  -0.115411   45  THR   B CA   
2748 C  C    . THR   B 45  ? 0.219436  0.384906 0.378911 -0.114111   0.0113336   -0.111303   45  THR   B C    
2749 O  O    . THR   B 45  ? 0.200111  0.377704 0.367008 -0.113087   0.0349479   -0.1209     45  THR   B O    
2750 C  CB   . THR   B 45  ? 0.246305  0.38141  0.415893 -0.106789   -0.00191607 -0.130709   45  THR   B CB   
2751 O  OG1  . THR   B 45  ? 0.236736  0.381281 0.446946 -0.107327   -0.0151297  -0.126441   45  THR   B OG1  
2752 C  CG2  . THR   B 45  ? 0.251095  0.390443 0.43848  -0.098435   0.00593159  -0.129968   45  THR   B CG2  
2753 N  N    . SER   B 46  ? 0.243153  0.386707 0.391151 -0.118287   0.0141431   -0.0976838  46  SER   B N    
2754 C  CA   . SER   B 46  ? 0.261876  0.408079 0.377636 -0.113953   0.0270504   -0.0912866  46  SER   B CA   
2755 C  C    . SER   B 46  ? 0.255378  0.399374 0.368539 -0.120465   0.025283    -0.0977263  46  SER   B C    
2756 O  O    . SER   B 46  ? 0.258633  0.393686 0.359215 -0.116981   0.0483717   -0.0871413  46  SER   B O    
2757 C  CB   . SER   B 46  ? 0.299355  0.44066  0.388864 -0.108736   0.0207212   -0.0747088  46  SER   B CB   
2758 O  OG   . SER   B 46  ? 0.398082  0.497616 0.418523 -0.0696003  0.00205874  -0.0540125  46  SER   B OG   
2759 N  N    . GLU   B 47  ? 0.264069  0.407767 0.382628 -0.124408   0.0345137   -0.112603   47  GLU   B N    
2760 C  CA   . GLU   B 47  ? 0.252074  0.419799 0.394592 -0.135398   0.011297    -0.115759   47  GLU   B CA   
2761 C  C    . GLU   B 47  ? 0.208996  0.426667 0.357827 -0.125137   -0.010666   -0.123687   47  GLU   B C    
2762 O  O    . GLU   B 47  ? 0.24725   0.452518 0.35198  -0.104334   -0.00253161 -0.112241   47  GLU   B O    
2763 C  CB   . GLU   B 47  ? 0.30429   0.440438 0.439807 -0.145345   -0.00547621 -0.129299   47  GLU   B CB   
2764 C  CG   . GLU   B 47  ? 0.326082  0.49305  0.48495  -0.134576   -0.0181196  -0.11437    47  GLU   B CG   
2765 C  CD   . GLU   B 47  ? 0.364799  0.539145 0.519272 -0.114037   -0.0182691  -0.113143   47  GLU   B CD   
2766 O  OE1  . GLU   B 47  ? 0.404643  0.551162 0.542627 -0.104922   -0.0216748  -0.0887507  47  GLU   B OE1  
2767 O  OE2  . GLU   B 47  ? 0.411181  0.634371 0.595488 -0.0913628  -0.0422579  -0.0761504  47  GLU   B OE2  
2768 N  N    . ASP   B 48  ? 0.206589  0.40901  0.335124 -0.113616   -0.0105318  -0.115745   48  ASP   B N    
2769 C  CA   . ASP   B 48  ? 0.207727  0.41764  0.32344  -0.103146   -0.0105013  -0.114074   48  ASP   B CA   
2770 C  C    . ASP   B 48  ? 0.186156  0.393326 0.2899   -0.100178   -0.00348698 -0.0876311  48  ASP   B C    
2771 O  O    . ASP   B 48  ? 0.204232  0.405429 0.289747 -0.0923798  -0.00908936 -0.0790417  48  ASP   B O    
2772 C  CB   . ASP   B 48  ? 0.213483  0.438459 0.346111 -0.109027   -0.0127524  -0.135519   48  ASP   B CB   
2773 C  CG   . ASP   B 48  ? 0.252251  0.454862 0.379353 -0.114826   -0.0195747  -0.151405   48  ASP   B CG   
2774 O  OD1  . ASP   B 48  ? 0.257416  0.521673 0.401995 -0.117118   -0.0242507  -0.169555   48  ASP   B OD1  
2775 O  OD2  . ASP   B 48  ? 0.274466  0.461131 0.389005 -0.115192   -0.0253756  -0.176247   48  ASP   B OD2  
2776 N  N    . MET   B 49  ? 0.179765  0.367303 0.279057 -0.0905179  0.0106216   -0.0620492  49  MET   B N    
2777 C  CA   . MET   B 49  ? 0.168899  0.344735 0.254319 -0.0804402  0.0180523   -0.0528224  49  MET   B CA   
2778 C  C    . MET   B 49  ? 0.191486  0.345226 0.26826  -0.0748118  0.0160227   -0.0511003  49  MET   B C    
2779 O  O    . MET   B 49  ? 0.193127  0.330656 0.265439 -0.0699894  0.0155471   -0.0526137  49  MET   B O    
2780 C  CB   . MET   B 49  ? 0.166936  0.331777 0.258302 -0.0728055  0.0155381   -0.0442359  49  MET   B CB   
2781 C  CG   . MET   B 49  ? 0.17316   0.314708 0.251738 -0.0674151  0.012986    -0.0413269  49  MET   B CG   
2782 S  SD   . MET   B 49  ? 0.175982  0.312046 0.254525 -0.054248   -0.00117352 -0.0354471  49  MET   B SD   
2783 C  CE   . MET   B 49  ? 0.153822  0.32318  0.242654 -0.0556135  -0.0144565  -0.0283232  49  MET   B CE   
2784 N  N    . LEU   B 50  ? 0.205943  0.364545 0.269263 -0.0873625  0.0128288   -0.0530617  50  LEU   B N    
2785 C  CA   . LEU   B 50  ? 0.209741  0.401392 0.290571 -0.0875079  0.0143815   -0.048662   50  LEU   B CA   
2786 C  C    . LEU   B 50  ? 0.195649  0.417329 0.285989 -0.101751   0.00230802  -0.0438143  50  LEU   B C    
2787 O  O    . LEU   B 50  ? 0.217208  0.442878 0.309698 -0.0788694  0.00787453  -0.0263472  50  LEU   B O    
2788 C  CB   . LEU   B 50  ? 0.224136  0.413102 0.310145 -0.0955432  0.0204995   -0.0521752  50  LEU   B CB   
2789 C  CG   . LEU   B 50  ? 0.239803  0.42779  0.330036 -0.0930194  0.0198623   -0.0430833  50  LEU   B CG   
2790 C  CD1  . LEU   B 50  ? 0.260065  0.430417 0.353688 -0.0984092  0.0120721   -0.0468069  50  LEU   B CD1  
2791 C  CD2  . LEU   B 50  ? 0.250752  0.431675 0.337599 -0.095653   0.0334573   -0.0467009  50  LEU   B CD2  
2792 N  N    . ASN   B 51  ? 0.205325  0.464295 0.279769 -0.0929591  -0.00154835 -0.0392504  51  ASN   B N    
2793 C  CA   . ASN   B 51  ? 0.211054  0.504905 0.28534  -0.0851964  -0.00500585 -0.0249145  51  ASN   B CA   
2794 C  C    . ASN   B 51  ? 0.19652   0.50842  0.267945 -0.108227   -0.0129477  -0.0459501  51  ASN   B C    
2795 O  O    . ASN   B 51  ? 0.211698  0.553576 0.281918 -0.106724   -0.0275028  -0.0690161  51  ASN   B O    
2796 C  CB   . ASN   B 51  ? 0.214677  0.54626  0.32064  -0.0877717  -0.0165412  -0.0105909  51  ASN   B CB   
2797 C  CG   . ASN   B 51  ? 0.255274  0.589228 0.353896 -0.0775705  -0.0157617  0.0171224   51  ASN   B CG   
2798 O  OD1  . ASN   B 51  ? 0.272879  0.615146 0.383075 -0.0574219  0.00357109  0.0462538   51  ASN   B OD1  
2799 N  ND2  . ASN   B 51  ? 0.288554  0.620715 0.353758 -0.0725909  -0.0371459  0.0215338   51  ASN   B ND2  
2800 N  N    . PRO   B 52  ? 0.189721  0.501207 0.238387 -0.108099   -0.00636861 -0.0524723  52  PRO   B N    
2801 C  CA   . PRO   B 52  ? 0.186905  0.50983  0.219058 -0.122547   -0.00598332 -0.0537324  52  PRO   B CA   
2802 C  C    . PRO   B 52  ? 0.204489  0.542737 0.228579 -0.11654    -0.0243724  -0.0486874  52  PRO   B C    
2803 O  O    . PRO   B 52  ? 0.247595  0.550734 0.276285 -0.0831688  -0.0108174  -0.0321502  52  PRO   B O    
2804 C  CB   . PRO   B 52  ? 0.181164  0.503873 0.219154 -0.106888   -0.00135773 -0.0524862  52  PRO   B CB   
2805 C  CG   . PRO   B 52  ? 0.18433   0.490184 0.24216  -0.115734   -0.0156436  -0.0524437  52  PRO   B CG   
2806 C  CD   . PRO   B 52  ? 0.187874  0.503683 0.249226 -0.101916   -0.0100305  -0.0516145  52  PRO   B CD   
2807 N  N    . ASN   B 53  ? 0.245624  0.595805 0.233986 -0.137118   -0.0264591  -0.0744654  53  ASN   B N    
2808 C  CA   . ASN   B 53  ? 0.270081  0.642487 0.20528  -0.141798   -0.0238634  -0.0862467  53  ASN   B CA   
2809 C  C    . ASN   B 53  ? 0.252768  0.656179 0.217484 -0.153619   -0.0248235  -0.110585   53  ASN   B C    
2810 O  O    . ASN   B 53  ? 0.251397  0.658555 0.258765 -0.157899   -0.00138574 -0.112297   53  ASN   B O    
2811 C  CB   . ASN   B 53  ? 0.285526  0.691227 0.241393 -0.148436   -0.0511775  -0.0874582  53  ASN   B CB   
2812 C  CG   . ASN   B 53  ? 0.319131  0.726809 0.263817 -0.151178   -0.0514475  -0.0693008  53  ASN   B CG   
2813 O  OD1  . ASN   B 53  ? 0.332567  0.787304 0.263865 -0.139602   -0.0412443  -0.0323638  53  ASN   B OD1  
2814 N  ND2  . ASN   B 53  ? 0.329845  0.751043 0.306494 -0.12374    -0.0749496  -0.0616773  53  ASN   B ND2  
2815 N  N    . TYR   B 54  ? 0.254415  0.643412 0.249548 -0.153786   -0.0108328  -0.105439   54  TYR   B N    
2816 C  CA   . TYR   B 54  ? 0.259616  0.647178 0.243641 -0.142868   -0.0115522  -0.109769   54  TYR   B CA   
2817 C  C    . TYR   B 54  ? 0.237866  0.739585 0.26073  -0.155315   -0.0120309  -0.135696   54  TYR   B C    
2818 O  O    . TYR   B 54  ? 0.228928  0.793066 0.221946 -0.151884   0.0195884   -0.16327    54  TYR   B O    
2819 C  CB   . TYR   B 54  ? 0.236257  0.582493 0.221662 -0.125062   -0.0100204  -0.0812574  54  TYR   B CB   
2820 C  CG   . TYR   B 54  ? 0.180197  0.48271  0.205973 -0.107346   -0.0296413  -0.0761415  54  TYR   B CG   
2821 C  CD1  . TYR   B 54  ? 0.183212  0.457153 0.223191 -0.0867353  -0.00852641 -0.0707924  54  TYR   B CD1  
2822 C  CD2  . TYR   B 54  ? 0.152915  0.45504  0.206125 -0.101631   -0.0304267  -0.0585316  54  TYR   B CD2  
2823 C  CE1  . TYR   B 54  ? 0.172434  0.41749  0.211602 -0.0709831  -0.0291188  -0.0720712  54  TYR   B CE1  
2824 C  CE2  . TYR   B 54  ? 0.156127  0.424518 0.202468 -0.079774   -0.0257533  -0.0577183  54  TYR   B CE2  
2825 C  CZ   . TYR   B 54  ? 0.152171  0.400267 0.20838  -0.0694099  -0.022157   -0.0604179  54  TYR   B CZ   
2826 O  OH   . TYR   B 54  ? 0.150215  0.338163 0.204416 -0.0427426  -0.0237376  -0.0546907  54  TYR   B OH   
2827 N  N    . GLU   B 55  ? 0.317827  0.803963 0.281149 -0.172595   0.00873233  -0.133687   55  GLU   B N    
2828 C  CA   . GLU   B 55  ? 0.340401  0.870964 0.317231 -0.162749   0.0166112   -0.170641   55  GLU   B CA   
2829 C  C    . GLU   B 55  ? 0.322038  0.901783 0.280576 -0.169543   0.0213826   -0.230042   55  GLU   B C    
2830 O  O    . GLU   B 55  ? 0.342861  0.956028 0.335636 -0.178535   -0.00836737 -0.277246   55  GLU   B O    
2831 C  CB   . GLU   B 55  ? 0.425104  0.8951   0.325376 -0.15856    0.00571533  -0.166538   55  GLU   B CB   
2832 N  N    . ASP   B 56  ? 0.305722  0.930505 0.295275 -0.14375    0.0171307   -0.265794   56  ASP   B N    
2833 C  CA   . ASP   B 56  ? 0.334988  0.918864 0.339742 -0.149033   0.0109365   -0.25496    56  ASP   B CA   
2834 C  C    . ASP   B 56  ? 0.267929  0.900619 0.358697 -0.1545     -0.0259324  -0.279561   56  ASP   B C    
2835 O  O    . ASP   B 56  ? 0.374972  0.925834 0.386595 -0.112164   -0.0222488  -0.287763   56  ASP   B O    
2836 C  CB   . ASP   B 56  ? 0.334995  0.933388 0.374742 -0.157426   -0.0184675  -0.230833   56  ASP   B CB   
2837 C  CG   . ASP   B 56  ? 0.373403  0.931408 0.420149 -0.15545    -0.0334129  -0.222771   56  ASP   B CG   
2838 O  OD1  . ASP   B 56  ? 0.378243  0.93969  0.425743 -0.127913   -0.0358821  -0.218231   56  ASP   B OD1  
2839 O  OD2  . ASP   B 56  ? 0.390448  0.929469 0.493061 -0.165067   -0.0157832  -0.2025     56  ASP   B OD2  
2840 N  N    . LEU   B 57  ? 0.290201  0.887497 0.361579 -0.133824   -0.00535757 -0.29137    57  LEU   B N    
2841 C  CA   . LEU   B 57  ? 0.302647  0.882279 0.381705 -0.133305   0.0111327   -0.288585   57  LEU   B CA   
2842 C  C    . LEU   B 57  ? 0.301045  0.947963 0.426007 -0.121066   0.0242229   -0.29053    57  LEU   B C    
2843 O  O    . LEU   B 57  ? 0.250091  0.972084 0.493289 -0.093165   0.0302352   -0.276632   57  LEU   B O    
2844 C  CB   . LEU   B 57  ? 0.333152  0.830596 0.375325 -0.134666   0.0108889   -0.279638   57  LEU   B CB   
2845 C  CG   . LEU   B 57  ? 0.354306  0.810603 0.421681 -0.132886   0.0306816   -0.258353   57  LEU   B CG   
2846 C  CD1  . LEU   B 57  ? 0.369159  0.795011 0.417795 -0.127531   0.0254769   -0.244379   57  LEU   B CD1  
2847 C  CD2  . LEU   B 57  ? 0.386329  0.799674 0.438351 -0.126438   0.041504    -0.264843   57  LEU   B CD2  
2848 N  N    . LEU   B 58  ? 0.289871  1.01163  0.390549 -0.144081   0.00015142  -0.29214    58  LEU   B N    
2849 C  CA   . LEU   B 58  ? 0.307911  1.04989  0.426089 -0.144324   0.0394376   -0.318014   58  LEU   B CA   
2850 C  C    . LEU   B 58  ? 0.308983  1.098    0.44976  -0.160535   0.0409135   -0.349878   58  LEU   B C    
2851 O  O    . LEU   B 58  ? 0.303753  1.15368  0.400192 -0.147048   0.00978363  -0.354292   58  LEU   B O    
2852 C  CB   . LEU   B 58  ? 0.287618  1.05955  0.437301 -0.146839   0.0709193   -0.302924   58  LEU   B CB   
2853 C  CG   . LEU   B 58  ? 0.28372   1.05397  0.450767 -0.160526   0.0889813   -0.293398   58  LEU   B CG   
2854 C  CD1  . LEU   B 58  ? 0.281998  1.0478   0.476153 -0.180386   0.0945231   -0.286631   58  LEU   B CD1  
2855 C  CD2  . LEU   B 58  ? 0.298549  1.05823  0.452167 -0.16095    0.10891     -0.279849   58  LEU   B CD2  
2856 N  N    . ILE   B 59  ? 0.400956  1.15974  0.442285 -0.149497   0.0388237   -0.378414   59  ILE   B N    
2857 C  CA   . ILE   B 59  ? 0.454034  1.18549  0.462723 -0.202351   0.00295707  -0.414713   59  ILE   B CA   
2858 C  C    . ILE   B 59  ? 0.488008  1.19007  0.469592 -0.244385   -0.0276848  -0.448034   59  ILE   B C    
2859 O  O    . ILE   B 59  ? 0.535693  1.22174  0.561584 -0.254346   -0.0375283  -0.482052   59  ILE   B O    
2860 C  CB   . ILE   B 59  ? 0.481302  1.17828  0.430127 -0.15456    0.0389805   -0.415423   59  ILE   B CB   
2861 N  N    . ARG   B 60  ? 0.493109  1.18683  0.530383 -0.289425   -0.0454924  -0.427288   60  ARG   B N    
2862 C  CA   . ARG   B 60  ? 0.515539  1.15713  0.56822  -0.303631   0.00389664  -0.425023   60  ARG   B CA   
2863 C  C    . ARG   B 60  ? 0.515952  1.11426  0.599753 -0.313886   0.0359152   -0.409565   60  ARG   B C    
2864 O  O    . ARG   B 60  ? 0.477989  1.12367  0.611004 -0.412847   0.0546986   -0.390983   60  ARG   B O    
2865 C  CB   . ARG   B 60  ? 0.551423  1.18338  0.609629 -0.290532   0.0338922   -0.399133   60  ARG   B CB   
2866 N  N    . LYS   B 61  ? 0.469783  1.08067  0.603064 -0.298183   0.0620156   -0.395604   61  LYS   B N    
2867 C  CA   . LYS   B 61  ? 0.451522  1.05416  0.597494 -0.262476   0.108981    -0.386503   61  LYS   B CA   
2868 C  C    . LYS   B 61  ? 0.444979  0.975359 0.607489 -0.242299   0.121624    -0.373583   61  LYS   B C    
2869 O  O    . LYS   B 61  ? 0.455039  1.03115  0.615932 -0.237606   0.12134     -0.386839   61  LYS   B O    
2870 C  CB   . LYS   B 61  ? 0.439081  1.05168  0.607171 -0.263787   0.0961127   -0.38182    61  LYS   B CB   
2871 C  CG   . LYS   B 61  ? 0.467728  1.0562   0.606738 -0.244298   0.0945966   -0.375773   61  LYS   B CG   
2872 C  CD   . LYS   B 61  ? 0.468861  1.0614   0.600934 -0.227462   0.105222    -0.360629   61  LYS   B CD   
2873 C  CE   . LYS   B 61  ? 0.466526  1.06388  0.630797 -0.213394   0.114773    -0.346198   61  LYS   B CE   
2874 N  NZ   . LYS   B 61  ? 0.482515  1.07624  0.659784 -0.20125    0.114527    -0.331004   61  LYS   B NZ   
2875 N  N    . SER   B 62  ? 0.409037  0.895269 0.602658 -0.247154   0.153906    -0.348964   62  SER   B N    
2876 C  CA   . SER   B 62  ? 0.423258  0.814085 0.583198 -0.212911   0.158907    -0.331038   62  SER   B CA   
2877 C  C    . SER   B 62  ? 0.392435  0.68633  0.549009 -0.2172     0.177239    -0.318322   62  SER   B C    
2878 O  O    . SER   B 62  ? 0.389451  0.670368 0.540238 -0.250742   0.16925     -0.328414   62  SER   B O    
2879 C  CB   . SER   B 62  ? 0.455164  0.802373 0.613437 -0.222355   0.140613    -0.345715   62  SER   B CB   
2880 N  N    . ASN   B 63  ? 0.395769  0.582819 0.50543  -0.196143   0.175821    -0.289167   63  ASN   B N    
2881 C  CA   . ASN   B 63  ? 0.396314  0.466485 0.483431 -0.181766   0.172849    -0.27805    63  ASN   B CA   
2882 C  C    . ASN   B 63  ? 0.428835  0.433233 0.537132 -0.177216   0.186807    -0.267029   63  ASN   B C    
2883 O  O    . ASN   B 63  ? 0.417625  0.401445 0.533491 -0.157429   0.203444    -0.223046   63  ASN   B O    
2884 C  CB   . ASN   B 63  ? 0.394081  0.436833 0.43368  -0.155944   0.16066     -0.267074   63  ASN   B CB   
2885 C  CG   . ASN   B 63  ? 0.403139  0.436092 0.416902 -0.129086   0.131023    -0.256545   63  ASN   B CG   
2886 O  OD1  . ASN   B 63  ? 0.398343  0.426124 0.392453 -0.121126   0.121935    -0.22074    63  ASN   B OD1  
2887 N  ND2  . ASN   B 63  ? 0.402765  0.458833 0.397362 -0.121926   0.116837    -0.237844   63  ASN   B ND2  
2888 N  N    . HIS   B 64  ? 0.517221  0.426053 0.599736 -0.177965   0.219201    -0.268393   64  HIS   B N    
2889 C  CA   . HIS   B 64  ? 0.568819  0.453634 0.623065 -0.159952   0.224989    -0.239958   64  HIS   B CA   
2890 C  C    . HIS   B 64  ? 0.563349  0.433674 0.621198 -0.186524   0.221703    -0.227383   64  HIS   B C    
2891 O  O    . HIS   B 64  ? 0.597505  0.397656 0.61515  -0.186583   0.282799    -0.24141    64  HIS   B O    
2892 C  CB   . HIS   B 64  ? 0.625892  0.466991 0.684728 -0.15998    0.197126    -0.253291   64  HIS   B CB   
2893 C  CG   . HIS   B 64  ? 0.692375  0.558527 0.724863 -0.126151   0.155046    -0.249154   64  HIS   B CG   
2894 N  ND1  . HIS   B 64  ? 0.694638  0.61782  0.778213 -0.088257   0.122759    -0.235355   64  HIS   B ND1  
2895 C  CD2  . HIS   B 64  ? 0.724678  0.620512 0.752689 -0.100986   0.137022    -0.213028   64  HIS   B CD2  
2896 C  CE1  . HIS   B 64  ? 0.724253  0.630841 0.778087 -0.0562834  0.126078    -0.223797   64  HIS   B CE1  
2897 N  NE2  . HIS   B 64  ? 0.735059  0.640044 0.773167 -0.0744136  0.129403    -0.208612   64  HIS   B NE2  
2898 N  N    . ASN   B 65  ? 0.47781   0.443073 0.552011 -0.206917   0.221906    -0.229909   65  ASN   B N    
2899 C  CA   . ASN   B 65  ? 0.470328  0.422427 0.498938 -0.191359   0.184643    -0.224674   65  ASN   B CA   
2900 C  C    . ASN   B 65  ? 0.427799  0.405706 0.461812 -0.171949   0.18658     -0.191122   65  ASN   B C    
2901 O  O    . ASN   B 65  ? 0.42381   0.440705 0.482906 -0.18485    0.20097     -0.210321   65  ASN   B O    
2902 C  CB   . ASN   B 65  ? 0.432702  0.430289 0.48282  -0.214569   0.138447    -0.249732   65  ASN   B CB   
2903 N  N    . PHE   B 66  ? 0.41101   0.316075 0.407213 -0.128192   0.164992    -0.150192   66  PHE   B N    
2904 C  CA   . PHE   B 66  ? 0.384054  0.321452 0.38152  -0.086775   0.15302     -0.136006   66  PHE   B CA   
2905 C  C    . PHE   B 66  ? 0.412839  0.321067 0.392772 -0.0611187  0.138505    -0.127826   66  PHE   B C    
2906 O  O    . PHE   B 66  ? 0.457007  0.379027 0.440145 -0.0105479  0.168994    -0.0866852  66  PHE   B O    
2907 C  CB   . PHE   B 66  ? 0.365739  0.30219  0.378845 -0.0828617  0.104297    -0.138364   66  PHE   B CB   
2908 C  CG   . PHE   B 66  ? 0.321065  0.319374 0.36394  -0.0975995  0.0767777   -0.139676   66  PHE   B CG   
2909 C  CD1  . PHE   B 66  ? 0.320386  0.32329  0.354111 -0.0833039  0.055892    -0.141194   66  PHE   B CD1  
2910 C  CD2  . PHE   B 66  ? 0.327829  0.330227 0.357867 -0.0802574  0.0699797   -0.145424   66  PHE   B CD2  
2911 C  CE1  . PHE   B 66  ? 0.302326  0.343855 0.359964 -0.081547   0.0488197   -0.143578   66  PHE   B CE1  
2912 C  CE2  . PHE   B 66  ? 0.305794  0.343525 0.358951 -0.0946129  0.0472969   -0.154339   66  PHE   B CE2  
2913 C  CZ   . PHE   B 66  ? 0.305759  0.35339  0.35379  -0.0838065  0.0432811   -0.150638   66  PHE   B CZ   
2914 N  N    . LEU   B 67  ? 0.394215  0.297599 0.387848 -0.0449064  0.115157    -0.16141    67  LEU   B N    
2915 C  CA   . LEU   B 67  ? 0.391045  0.301004 0.393312 -0.0389913  0.101484    -0.153892   67  LEU   B CA   
2916 C  C    . LEU   B 67  ? 0.368597  0.287686 0.372733 -0.0291072  0.0946309   -0.144987   67  LEU   B C    
2917 O  O    . LEU   B 67  ? 0.383936  0.328474 0.402688 -0.0449953  0.0984661   -0.184808   67  LEU   B O    
2918 C  CB   . LEU   B 67  ? 0.414683  0.310635 0.421158 -0.0365886  0.0930923   -0.142145   67  LEU   B CB   
2919 C  CG   . LEU   B 67  ? 0.443186  0.349691 0.464513 -0.0508896  0.0641267   -0.134726   67  LEU   B CG   
2920 C  CD1  . LEU   B 67  ? 0.444645  0.339297 0.488043 -0.0649639  0.0607375   -0.12417    67  LEU   B CD1  
2921 C  CD2  . LEU   B 67  ? 0.468148  0.379645 0.476775 -0.0447872  0.0610428   -0.138933   67  LEU   B CD2  
2922 N  N    . VAL   B 68  ? 0.347609  0.269689 0.337932 -0.00651991 0.0686019   -0.128273   68  VAL   B N    
2923 C  CA   . VAL   B 68  ? 0.333869  0.243149 0.314922 0.021812    0.0580649   -0.107423   68  VAL   B CA   
2924 C  C    . VAL   B 68  ? 0.348685  0.242657 0.320389 0.0224018   0.0518681   -0.0795478  68  VAL   B C    
2925 O  O    . VAL   B 68  ? 0.344528  0.26097  0.326023 0.0347544   0.0523315   -0.0777877  68  VAL   B O    
2926 C  CB   . VAL   B 68  ? 0.328559  0.245905 0.306255 0.0342735   0.0459025   -0.0929957  68  VAL   B CB   
2927 C  CG1  . VAL   B 68  ? 0.326837  0.249366 0.320397 0.0208864   0.0340248   -0.078045   68  VAL   B CG1  
2928 C  CG2  . VAL   B 68  ? 0.329714  0.244425 0.31186  0.0447615   0.0450814   -0.0943082  68  VAL   B CG2  
2929 N  N    . GLN   B 69  ? 0.360608  0.256695 0.321936 0.0327246   0.0377811   -0.0612803  69  GLN   B N    
2930 C  CA   . GLN   B 69  ? 0.398166  0.276977 0.327218 0.0509656   0.0395376   -0.0248666  69  GLN   B CA   
2931 C  C    . GLN   B 69  ? 0.368627  0.259211 0.285531 0.0761008   0.0356545   -0.00152468 69  GLN   B C    
2932 O  O    . GLN   B 69  ? 0.354288  0.256163 0.266156 0.0674538   0.0400409   -0.0148356  69  GLN   B O    
2933 C  CB   . GLN   B 69  ? 0.437955  0.334975 0.388024 0.0314392   0.0366452   0.0012046   69  GLN   B CB   
2934 C  CG   . GLN   B 69  ? 0.47051   0.410444 0.446518 0.0350106   0.0102505   0.0275      69  GLN   B CG   
2935 C  CD   . GLN   B 69  ? 0.521133  0.446155 0.485827 0.0182337   0.00101183  0.0619625   69  GLN   B CD   
2936 O  OE1  . GLN   B 69  ? 0.550195  0.421987 0.531143 0.00795375  -0.0080388  0.0733044   69  GLN   B OE1  
2937 N  NE2  . GLN   B 69  ? 0.553158  0.505283 0.492003 0.0241768   -0.00469719 0.0573642   69  GLN   B NE2  
2938 N  N    . ALA   B 70  ? 0.374151  0.278015 0.296221 0.107663    0.0486017   0.00934129  70  ALA   B N    
2939 C  CA   . ALA   B 70  ? 0.363265  0.305612 0.306025 0.122361    0.0402468   0.0156354   70  ALA   B CA   
2940 C  C    . ALA   B 70  ? 0.398687  0.340746 0.319984 0.128015    0.0254863   0.0244461   70  ALA   B C    
2941 O  O    . ALA   B 70  ? 0.432194  0.345037 0.356096 0.137315    0.0257882   0.0244269   70  ALA   B O    
2942 C  CB   . ALA   B 70  ? 0.367223  0.321752 0.323838 0.121569    0.0425267   0.0191498   70  ALA   B CB   
2943 N  N    . GLY   B 71  ? 0.417547  0.3761   0.347332 0.130837    0.0241116   0.0146728   71  GLY   B N    
2944 C  CA   . GLY   B 71  ? 0.460013  0.395009 0.386162 0.134865    0.0205271   0.0235646   71  GLY   B CA   
2945 C  C    . GLY   B 71  ? 0.497332  0.410909 0.419172 0.1072      0.0233898   0.021214    71  GLY   B C    
2946 O  O    . GLY   B 71  ? 0.515072  0.434747 0.429369 0.0875481   0.0225676   0.0327431   71  GLY   B O    
2947 N  N    . ASN   B 72  ? 0.523579  0.44925  0.457495 0.124959    0.028877    0.026755    72  ASN   B N    
2948 C  CA   . ASN   B 72  ? 0.564574  0.447484 0.524818 0.134138    0.0431448   0.0206355   72  ASN   B CA   
2949 C  C    . ASN   B 72  ? 0.545094  0.422568 0.560707 0.149397    0.0703378   -0.0105169  72  ASN   B C    
2950 O  O    . ASN   B 72  ? 0.566203  0.397688 0.608891 0.135327    0.0913981   -0.0279189  72  ASN   B O    
2951 C  CB   . ASN   B 72  ? 0.612945  0.485397 0.558437 0.135995    0.0276239   0.0475506   72  ASN   B CB   
2952 C  CG   . ASN   B 72  ? 0.667226  0.540863 0.583329 0.134921    0.0305706   0.0496182   72  ASN   B CG   
2953 O  OD1  . ASN   B 72  ? 0.693367  0.567744 0.591808 0.14265     0.049221    0.0624239   72  ASN   B OD1  
2954 N  ND2  . ASN   B 72  ? 0.706354  0.61137  0.615421 0.110846    0.00808739  0.0518166   72  ASN   B ND2  
2955 N  N    . VAL   B 73  ? 0.512996  0.45221  0.547248 0.16666     0.0883545   -0.0422319  73  VAL   B N    
2956 C  CA   . VAL   B 73  ? 0.507009  0.419912 0.523239 0.172304    0.0979003   -0.035679   73  VAL   B CA   
2957 C  C    . VAL   B 73  ? 0.511885  0.372256 0.459493 0.169512    0.107684    -0.0451557  73  VAL   B C    
2958 O  O    . VAL   B 73  ? 0.505454  0.37592  0.457017 0.186589    0.11275     -0.0554655  73  VAL   B O    
2959 C  CB   . VAL   B 73  ? 0.490892  0.48704  0.526937 0.164191    0.0949185   -0.0156855  73  VAL   B CB   
2960 C  CG1  . VAL   B 73  ? 0.490175  0.49885  0.531268 0.158538    0.101527    -0.0046602  73  VAL   B CG1  
2961 C  CG2  . VAL   B 73  ? 0.498482  0.517813 0.546412 0.156553    0.0802928   0.0004551   73  VAL   B CG2  
2962 N  N    . GLN   B 74  ? 0.509477  0.355814 0.462467 0.1547      0.129312    -0.0495418  74  GLN   B N    
2963 C  CA   . GLN   B 74  ? 0.523586  0.346074 0.44692  0.131268    0.116897    -0.0623144  74  GLN   B CA   
2964 C  C    . GLN   B 74  ? 0.468071  0.362399 0.432149 0.126088    0.117106    -0.0609314  74  GLN   B C    
2965 O  O    . GLN   B 74  ? 0.496682  0.427161 0.462419 0.159542    0.141481    -0.0555479  74  GLN   B O    
2966 C  CB   . GLN   B 74  ? 0.5821    0.352214 0.452648 0.110225    0.107564    -0.0767875  74  GLN   B CB   
2967 N  N    . LEU   B 75  ? 0.409477  0.345138 0.385557 0.0967898   0.0896611   -0.0594869  75  LEU   B N    
2968 C  CA   . LEU   B 75  ? 0.392884  0.384806 0.400154 0.062737    0.0818891   -0.0452093  75  LEU   B CA   
2969 C  C    . LEU   B 75  ? 0.433038  0.421503 0.394982 0.0511288   0.0703863   -0.0355265  75  LEU   B C    
2970 O  O    . LEU   B 75  ? 0.44885   0.50356  0.421225 0.0703876   0.0712435   -0.0296105  75  LEU   B O    
2971 C  CB   . LEU   B 75  ? 0.36592   0.376118 0.397784 0.0449999   0.066514    -0.0354419  75  LEU   B CB   
2972 C  CG   . LEU   B 75  ? 0.364839  0.378839 0.388645 0.0470272   0.0580668   -0.02928    75  LEU   B CG   
2973 C  CD1  . LEU   B 75  ? 0.340783  0.373501 0.390019 0.0413611   0.0472452   -0.041386   75  LEU   B CD1  
2974 C  CD2  . LEU   B 75  ? 0.365361  0.393713 0.415299 0.0453135   0.0580314   -0.0232481  75  LEU   B CD2  
2975 N  N    . ARG   B 76  ? 0.448449  0.350433 0.393579 0.0648729   0.0703713   -0.043805   76  ARG   B N    
2976 C  CA   . ARG   B 76  ? 0.463996  0.340652 0.408482 0.0473564   0.0523539   -0.0380549  76  ARG   B CA   
2977 C  C    . ARG   B 76  ? 0.42287   0.29511  0.345081 0.0348213   0.0560065   -0.064719   76  ARG   B C    
2978 O  O    . ARG   B 76  ? 0.39735   0.274221 0.336144 0.0421465   0.0414035   -0.0798982  76  ARG   B O    
2979 C  CB   . ARG   B 76  ? 0.521848  0.358555 0.458077 0.0642683   0.0653368   -0.0445679  76  ARG   B CB   
2980 C  CG   . ARG   B 76  ? 0.555894  0.436228 0.501408 0.0663867   0.0503411   -0.0400692  76  ARG   B CG   
2981 C  CD   . ARG   B 76  ? 0.591401  0.495319 0.548812 0.0876087   0.0751149   -0.0507661  76  ARG   B CD   
2982 N  NE   . ARG   B 76  ? 0.633195  0.562704 0.591313 0.0834613   0.0820199   -0.0311696  76  ARG   B NE   
2983 C  CZ   . ARG   B 76  ? 0.64173   0.614518 0.634137 0.0949375   0.0870072   -0.0368809  76  ARG   B CZ   
2984 N  NH1  . ARG   B 76  ? 0.653857  0.616669 0.661538 0.109818    0.0719528   -0.0411767  76  ARG   B NH1  
2985 N  NH2  . ARG   B 76  ? 0.64784   0.618403 0.635192 0.104603    0.103492    -0.0420563  76  ARG   B NH2  
2986 N  N    . VAL   B 77  ? 0.409837  0.282579 0.306623 -0.00123373 0.0495384   -0.0683516  77  VAL   B N    
2987 C  CA   . VAL   B 77  ? 0.370159  0.27956  0.284474 -0.0134864  0.0501608   -0.072116   77  VAL   B CA   
2988 C  C    . VAL   B 77  ? 0.348163  0.280945 0.28973  -0.0192939  0.0428044   -0.0974699  77  VAL   B C    
2989 O  O    . VAL   B 77  ? 0.37363   0.28928  0.317308 -0.0361922  0.0509202   -0.111932   77  VAL   B O    
2990 C  CB   . VAL   B 77  ? 0.366079  0.283789 0.280538 -0.0319229  0.0448386   -0.0707082  77  VAL   B CB   
2991 C  CG1  . VAL   B 77  ? 0.345476  0.288786 0.269358 -0.0323706  0.0454468   -0.0798282  77  VAL   B CG1  
2992 C  CG2  . VAL   B 77  ? 0.366838  0.298382 0.271789 -0.0329237  0.0448678   -0.0520388  77  VAL   B CG2  
2993 N  N    . ILE   B 78  ? 0.299066  0.284338 0.27706  -0.0153891  0.0286849   -0.0958588  78  ILE   B N    
2994 C  CA   . ILE   B 78  ? 0.287582  0.313805 0.275243 -0.00060586 0.036602    -0.0934062  78  ILE   B CA   
2995 C  C    . ILE   B 78  ? 0.252343  0.319998 0.257388 -0.0126886  0.023216    -0.0958857  78  ILE   B C    
2996 O  O    . ILE   B 78  ? 0.280482  0.361723 0.252961 -0.00516622 0.0222707   -0.0883562  78  ILE   B O    
2997 C  CB   . ILE   B 78  ? 0.277483  0.335402 0.286133 0.0201767   0.0413434   -0.0916982  78  ILE   B CB   
2998 C  CG1  . ILE   B 78  ? 0.272137  0.350597 0.30063  0.0235036   0.0443559   -0.0890839  78  ILE   B CG1  
2999 C  CG2  . ILE   B 78  ? 0.295591  0.335743 0.302718 0.0198594   0.0399112   -0.0885642  78  ILE   B CG2  
3000 C  CD1  . ILE   B 78  ? 0.263054  0.368616 0.318777 0.0295136   0.0434512   -0.095421   78  ILE   B CD1  
3001 N  N    . GLY   B 79  ? 0.231369  0.319773 0.249024 -0.010374   0.00840311  -0.0841212  79  GLY   B N    
3002 C  CA   . GLY   B 79  ? 0.232244  0.331812 0.235349 -0.00177814 0.00139074  -0.0867873  79  GLY   B CA   
3003 C  C    . GLY   B 79  ? 0.242731  0.338788 0.233671 0.0055042   -0.0186354  -0.107948   79  GLY   B C    
3004 O  O    . GLY   B 79  ? 0.212141  0.324978 0.232537 -0.0165204  -0.0297145  -0.0886492  79  GLY   B O    
3005 N  N    . HIS   B 80  ? 0.26195   0.389036 0.240608 0.0300336   -0.0350529  -0.12079    80  HIS   B N    
3006 C  CA   . HIS   B 80  ? 0.293903  0.406724 0.255999 0.0500391   -0.0397295  -0.140427   80  HIS   B CA   
3007 C  C    . HIS   B 80  ? 0.27984   0.415403 0.243814 0.0691565   -0.0546352  -0.138822   80  HIS   B C    
3008 O  O    . HIS   B 80  ? 0.323056  0.445021 0.245994 0.0969597   -0.0724161  -0.1576     80  HIS   B O    
3009 C  CB   . HIS   B 80  ? 0.293688  0.453099 0.284796 0.0429383   -0.0258791  -0.161376   80  HIS   B CB   
3010 C  CG   . HIS   B 80  ? 0.306119  0.517121 0.337681 0.0133848   -0.0257124  -0.192089   80  HIS   B CG   
3011 N  ND1  . HIS   B 80  ? 0.343336  0.536651 0.368353 -0.0268282  -0.0440452  -0.236993   80  HIS   B ND1  
3012 C  CD2  . HIS   B 80  ? 0.330915  0.570652 0.363301 0.00979513  -0.0400701  -0.196228   80  HIS   B CD2  
3013 C  CE1  . HIS   B 80  ? 0.348905  0.582491 0.387381 -0.0197443  -0.0638587  -0.214692   80  HIS   B CE1  
3014 N  NE2  . HIS   B 80  ? 0.348053  0.590237 0.410936 -0.0160036  -0.0369216  -0.208386   80  HIS   B NE2  
3015 N  N    . SER   B 81  ? 0.245588  0.385114 0.209688 0.0645348   -0.050713   -0.112722   81  SER   B N    
3016 C  CA   . SER   B 81  ? 0.230025  0.389124 0.207051 0.0586695   -0.0464919  -0.0888931  81  SER   B CA   
3017 C  C    . SER   B 81  ? 0.201657  0.378067 0.194494 0.0485683   -0.039821   -0.0762948  81  SER   B C    
3018 O  O    . SER   B 81  ? 0.205593  0.384528 0.190914 0.0693916   -0.042095   -0.0733049  81  SER   B O    
3019 C  CB   . SER   B 81  ? 0.260824  0.412896 0.229897 0.0655909   -0.0176549  -0.0640251  81  SER   B CB   
3020 O  OG   . SER   B 81  ? 0.252228  0.441348 0.277968 0.0382788   0.0107436   -0.0397035  81  SER   B OG   
3021 N  N    . MET   B 82  ? 0.21334   0.373511 0.193628 0.0482787   -0.044979   -0.0678387  82  MET   B N    
3022 C  CA   . MET   B 82  ? 0.207701  0.366945 0.183683 0.0357427   -0.0335523  -0.0506537  82  MET   B CA   
3023 C  C    . MET   B 82  ? 0.19024   0.351351 0.17858  0.0396486   -0.0196336  -0.0350362  82  MET   B C    
3024 O  O    . MET   B 82  ? 0.252989  0.36462  0.17496  0.0223517   -0.00918044 -0.0352655  82  MET   B O    
3025 C  CB   . MET   B 82  ? 0.22489   0.428621 0.241965 0.0169208   -0.0163418  -0.0575452  82  MET   B CB   
3026 C  CG   . MET   B 82  ? 0.239597  0.48887  0.264277 -0.00871481 -0.0111637  -0.0691507  82  MET   B CG   
3027 S  SD   . MET   B 82  ? 0.250336  0.628423 0.285109 -0.0532795  -0.00262363 -0.132046   82  MET   B SD   
3028 C  CE   . MET   B 82  ? 0.192614  0.553048 0.206826 -0.0698083  -0.0155394  -0.13866    82  MET   B CE   
3029 N  N    . GLN   B 83  ? 0.162185  0.30828  0.159646 0.0373745   -0.00010636 -0.0157862  83  GLN   B N    
3030 C  CA   . GLN   B 83  ? 0.168404  0.306437 0.156357 0.035877    0.0103043   -0.00909039 83  GLN   B CA   
3031 C  C    . GLN   B 83  ? 0.148422  0.293219 0.157146 0.0388581   0.00278193  -0.0039285  83  GLN   B C    
3032 O  O    . GLN   B 83  ? 0.147222  0.301677 0.160567 0.0395731   -0.00635233 0.00474794  83  GLN   B O    
3033 C  CB   . GLN   B 83  ? 0.180424  0.308304 0.180692 0.0284242   0.0167084   -0.0014762  83  GLN   B CB   
3034 C  CG   . GLN   B 83  ? 0.196878  0.313994 0.198723 0.0245221   0.026072    0.00689988  83  GLN   B CG   
3035 C  CD   . GLN   B 83  ? 0.205158  0.328506 0.237227 0.0157409   0.0241916   0.0186658   83  GLN   B CD   
3036 O  OE1  . GLN   B 83  ? 0.215917  0.370982 0.273624 0.00959919  -0.00502501 0.0352131   83  GLN   B OE1  
3037 N  NE2  . GLN   B 83  ? 0.224642  0.34395  0.255893 0.0107106   0.028411    0.0266403   83  GLN   B NE2  
3038 N  N    . ASN   B 84  ? 0.139364  0.284549 0.151931 0.0271228   -0.00601914 -0.00708669 84  ASN   B N    
3039 C  CA   . ASN   B 84  ? 0.124535  0.272157 0.151374 0.0273505   -0.0121064  -0.00402284 84  ASN   B CA   
3040 C  C    . ASN   B 84  ? 0.123875  0.257053 0.150969 0.0210174   -0.0243082  -0.0131063  84  ASN   B C    
3041 O  O    . ASN   B 84  ? 0.138895  0.261985 0.140014 0.0167411   -0.0125334  -0.0257935  84  ASN   B O    
3042 C  CB   . ASN   B 84  ? 0.128582  0.286451 0.152793 0.0242699   -0.0240883  -0.00180606 84  ASN   B CB   
3043 C  CG   . ASN   B 84  ? 0.1666    0.308967 0.160204 0.0133578   -0.0246683  0.00135722  84  ASN   B CG   
3044 O  OD1  . ASN   B 84  ? 0.179419  0.326632 0.182635 0.0135622   -0.0393117  0.0242687   84  ASN   B OD1  
3045 N  ND2  . ASN   B 84  ? 0.182486  0.323587 0.162574 0.00138096  -0.021306   8.49e-05    84  ASN   B ND2  
3046 N  N    . CYS   B 85  ? 0.117508  0.246628 0.148723 0.00623581  -0.0189838  -0.0230484  85  CYS   B N    
3047 C  CA   . CYS   B 85  ? 0.116547  0.25323  0.142149 0.00232064  -0.0187839  -0.0228707  85  CYS   B CA   
3048 C  C    . CYS   B 85  ? 0.121835  0.24025  0.138278 0.00040389  -0.0133351  -0.0262236  85  CYS   B C    
3049 O  O    . CYS   B 85  ? 0.12896   0.235873 0.144769 -0.00448935 -0.0127168  -0.0256204  85  CYS   B O    
3050 C  CB   . CYS   B 85  ? 0.113672  0.262472 0.15114  0.0132275   -0.0176933  -0.026409   85  CYS   B CB   
3051 S  SG   . CYS   B 85  ? 0.124867  0.289493 0.180493 0.0237301   -0.0179915  -0.0244848  85  CYS   B SG   
3052 N  N    . VAL   B 86  ? 0.12106   0.247847 0.162288 0.00763365  -0.0112653  -0.0179378  86  VAL   B N    
3053 C  CA   . VAL   B 86  ? 0.143164  0.255793 0.177154 0.0183008   -0.0188962  -0.0250636  86  VAL   B CA   
3054 C  C    . VAL   B 86  ? 0.149248  0.256204 0.170619 0.0223602   -0.0192598  -0.0233854  86  VAL   B C    
3055 O  O    . VAL   B 86  ? 0.207266  0.274871 0.178375 0.0390527   -0.0107617  -0.0241284  86  VAL   B O    
3056 C  CB   . VAL   B 86  ? 0.141939  0.266562 0.207615 0.023087    -0.0292572  -0.0294972  86  VAL   B CB   
3057 C  CG1  . VAL   B 86  ? 0.156982  0.283319 0.244527 0.026472    -0.00898815 -0.0272641  86  VAL   B CG1  
3058 C  CG2  . VAL   B 86  ? 0.146974  0.275487 0.208222 0.0208578   -0.03138    -0.0340838  86  VAL   B CG2  
3059 N  N    . LEU   B 87  ? 0.154457  0.248622 0.157747 0.00129766  -0.00843007 -0.030387   87  LEU   B N    
3060 C  CA   . LEU   B 87  ? 0.174948  0.249904 0.171921 0.00494017  -0.0114375  -0.0355843  87  LEU   B CA   
3061 C  C    . LEU   B 87  ? 0.172864  0.253352 0.166318 0.00881116  -0.0174144  -0.0440532  87  LEU   B C    
3062 O  O    . LEU   B 87  ? 0.177012  0.26026  0.166456 0.0252839   -0.0211295  -0.043461   87  LEU   B O    
3063 C  CB   . LEU   B 87  ? 0.206837  0.271684 0.195474 -0.0101385  0.00336624  -0.0391364  87  LEU   B CB   
3064 C  CG   . LEU   B 87  ? 0.239234  0.283486 0.211364 -0.0266629  0.0122663   -0.0503746  87  LEU   B CG   
3065 C  CD1  . LEU   B 87  ? 0.255981  0.303458 0.227128 -0.022991   0.00925452  -0.0589305  87  LEU   B CD1  
3066 C  CD2  . LEU   B 87  ? 0.259496  0.282428 0.22605  -0.0253918  0.0149682   -0.0507568  87  LEU   B CD2  
3067 N  N    . LYS   B 88  ? 0.152584  0.24751  0.169123 0.0196629   -0.0170695  -0.0400394  88  LYS   B N    
3068 C  CA   . LYS   B 88  ? 0.155373  0.248725 0.181378 0.00896516  -0.0134802  -0.0424621  88  LYS   B CA   
3069 C  C    . LYS   B 88  ? 0.17975   0.249151 0.18488  0.00288262  -0.0165658  -0.0538904  88  LYS   B C    
3070 O  O    . LYS   B 88  ? 0.210831  0.292687 0.203653 0.00879855  -0.0358218  -0.0675432  88  LYS   B O    
3071 C  CB   . LYS   B 88  ? 0.180866  0.262213 0.196359 0.00413636  -0.0136478  -0.0316068  88  LYS   B CB   
3072 C  CG   . LYS   B 88  ? 0.2131    0.263133 0.229672 0.00804445  -0.0185723  -0.0197874  88  LYS   B CG   
3073 C  CD   . LYS   B 88  ? 0.291233  0.304399 0.278506 0.00481075  -0.0175236  -0.00308002 88  LYS   B CD   
3074 C  CE   . LYS   B 88  ? 0.346179  0.366532 0.331985 -0.00259911 -0.021789   0.00427227  88  LYS   B CE   
3075 N  NZ   . LYS   B 88  ? 0.395376  0.397326 0.356607 -0.00567694 -0.0147339  0.0285065   88  LYS   B NZ   
3076 N  N    . LEU   B 89  ? 0.182889  0.229202 0.181402 0.00320502  -0.0148325  -0.0621656  89  LEU   B N    
3077 C  CA   . LEU   B 89  ? 0.185028  0.232311 0.190029 -0.00095145 -0.0119665  -0.0642619  89  LEU   B CA   
3078 C  C    . LEU   B 89  ? 0.190119  0.249688 0.19956  0.00220017  -0.00662757 -0.0761544  89  LEU   B C    
3079 O  O    . LEU   B 89  ? 0.188076  0.255835 0.212601 0.0120929   -0.0103269  -0.0720408  89  LEU   B O    
3080 C  CB   . LEU   B 89  ? 0.194965  0.245688 0.210883 -0.00313167 -0.00571485 -0.0517591  89  LEU   B CB   
3081 C  CG   . LEU   B 89  ? 0.213409  0.261687 0.223919 -0.00536553 0.00943599  -0.0459688  89  LEU   B CG   
3082 C  CD1  . LEU   B 89  ? 0.244968  0.272694 0.234003 -0.0063388  0.0107278   -0.0351003  89  LEU   B CD1  
3083 C  CD2  . LEU   B 89  ? 0.209821  0.276562 0.232023 -0.00882981 0.00798162  -0.041992   89  LEU   B CD2  
3084 N  N    . LYS   B 90  ? 0.198537  0.260992 0.19821  0.0169719   -0.0167909  -0.0654765  90  LYS   B N    
3085 C  CA   . LYS   B 90  ? 0.207547  0.265588 0.207039 0.0150956   0.00141283  -0.0723135  90  LYS   B CA   
3086 C  C    . LYS   B 90  ? 0.230292  0.260436 0.219982 0.0196418   0.00414794  -0.0702591  90  LYS   B C    
3087 O  O    . LYS   B 90  ? 0.228282  0.255148 0.247246 0.0209317   0.00101236  -0.0757316  90  LYS   B O    
3088 C  CB   . LYS   B 90  ? 0.2313    0.299154 0.214532 0.0214258   -0.0025072  -0.0677548  90  LYS   B CB   
3089 C  CG   . LYS   B 90  ? 0.269383  0.347235 0.250368 0.00663522  0.0111023   -0.0683347  90  LYS   B CG   
3090 C  CD   . LYS   B 90  ? 0.320112  0.383073 0.294861 -0.00767454 -0.00217571 -0.0675273  90  LYS   B CD   
3091 C  CE   . LYS   B 90  ? 0.364433  0.427121 0.319475 -0.00426818 0.00555003  -0.0477629  90  LYS   B CE   
3092 N  NZ   . LYS   B 90  ? 0.393293  0.446825 0.332294 -0.00639765 -0.0058531  -0.0406984  90  LYS   B NZ   
3093 N  N    . VAL   B 91  ? 0.235518  0.264562 0.233327 0.0256726   0.0083627   -0.0745185  91  VAL   B N    
3094 C  CA   . VAL   B 91  ? 0.248417  0.275974 0.252412 0.0395584   0.00568009  -0.0851258  91  VAL   B CA   
3095 C  C    . VAL   B 91  ? 0.245249  0.312165 0.273921 0.0596572   -0.0122347  -0.103296   91  VAL   B C    
3096 O  O    . VAL   B 91  ? 0.219331  0.336023 0.273822 0.0661357   -0.00470783 -0.0963399  91  VAL   B O    
3097 C  CB   . VAL   B 91  ? 0.256934  0.274804 0.255192 0.0407964   0.0094273   -0.0780304  91  VAL   B CB   
3098 C  CG1  . VAL   B 91  ? 0.273275  0.277976 0.248681 0.0399454   0.0189424   -0.0805648  91  VAL   B CG1  
3099 C  CG2  . VAL   B 91  ? 0.258672  0.280683 0.24297  0.0332476   0.00937892  -0.0714072  91  VAL   B CG2  
3100 N  N    . ASP   B 92  ? 0.293035  0.347409 0.314951 0.0855556   -0.0279432  -0.120708   92  ASP   B N    
3101 C  CA   . ASP   B 92  ? 0.300528  0.380577 0.361972 0.119737    -0.050625   -0.148851   92  ASP   B CA   
3102 C  C    . ASP   B 92  ? 0.287458  0.420304 0.361588 0.138472    -0.0614534  -0.161898   92  ASP   B C    
3103 O  O    . ASP   B 92  ? 0.290276  0.463846 0.419198 0.125938    -0.0484859  -0.192611   92  ASP   B O    
3104 C  CB   . ASP   B 92  ? 0.398512  0.382121 0.43463  0.131775    -0.0603022  -0.149271   92  ASP   B CB   
3105 C  CG   . ASP   B 92  ? 0.469926  0.402039 0.505319 0.15266     -0.0737643  -0.125247   92  ASP   B CG   
3106 O  OD1  . ASP   B 92  ? 0.559993  0.442228 0.518151 0.146207    -0.123356   -0.103722   92  ASP   B OD1  
3107 O  OD2  . ASP   B 92  ? 0.549658  0.407174 0.619081 0.141679    -0.0961896  -0.116353   92  ASP   B OD2  
3108 N  N    . THR   B 93  ? 0.291276  0.428202 0.376314 0.155918    -0.0655261  -0.175053   93  THR   B N    
3109 C  CA   . THR   B 93  ? 0.323716  0.452186 0.370936 0.155547    -0.0791661  -0.170564   93  THR   B CA   
3110 C  C    . THR   B 93  ? 0.270109  0.44207  0.329862 0.14364     -0.0514252  -0.166794   93  THR   B C    
3111 O  O    . THR   B 93  ? 0.263362  0.440274 0.362546 0.140104    -0.0478648  -0.168179   93  THR   B O    
3112 C  CB   . THR   B 93  ? 0.397829  0.469329 0.408111 0.163404    -0.101017   -0.155975   93  THR   B CB   
3113 O  OG1  . THR   B 93  ? 0.468588  0.484988 0.435235 0.171907    -0.124185   -0.170862   93  THR   B OG1  
3114 C  CG2  . THR   B 93  ? 0.4005    0.487943 0.430744 0.161578    -0.110268   -0.152069   93  THR   B CG2  
3115 N  N    . ALA   B 94  ? 0.26761   0.456319 0.294372 0.131962    -0.0534212  -0.144207   94  ALA   B N    
3116 C  CA   . ALA   B 94  ? 0.236455  0.43829  0.285089 0.125466    -0.0417412  -0.122389   94  ALA   B CA   
3117 C  C    . ALA   B 94  ? 0.221495  0.408706 0.266989 0.119426    -0.0269756  -0.122489   94  ALA   B C    
3118 O  O    . ALA   B 94  ? 0.251118  0.431755 0.282276 0.138415    -0.0467348  -0.126654   94  ALA   B O    
3119 C  CB   . ALA   B 94  ? 0.248936  0.457099 0.290933 0.130165    -0.0257963  -0.118385   94  ALA   B CB   
3120 N  N    . ASN   B 95  ? 0.185392  0.374756 0.240781 0.109703    -0.0281537  -0.0978383  95  ASN   B N    
3121 C  CA   . ASN   B 95  ? 0.169756  0.345625 0.238734 0.101966    -0.0321905  -0.0778297  95  ASN   B CA   
3122 C  C    . ASN   B 95  ? 0.166018  0.346419 0.23384  0.0985558   -0.0152834  -0.069719   95  ASN   B C    
3123 O  O    . ASN   B 95  ? 0.155086  0.343129 0.248326 0.0998169   -0.0173525  -0.0666448  95  ASN   B O    
3124 C  CB   . ASN   B 95  ? 0.151453  0.326287 0.225683 0.0860699   -0.0270788  -0.0663844  95  ASN   B CB   
3125 C  CG   . ASN   B 95  ? 0.159475  0.327293 0.225488 0.0914347   -0.0336562  -0.0582276  95  ASN   B CG   
3126 O  OD1  . ASN   B 95  ? 0.166821  0.324072 0.227373 0.103597    -0.0264985  -0.0531144  95  ASN   B OD1  
3127 N  ND2  . ASN   B 95  ? 0.158439  0.331635 0.22056  0.0936065   -0.0394794  -0.0543277  95  ASN   B ND2  
3128 N  N    . PRO   B 96  ? 0.177788  0.347922 0.260742 0.0975115   -0.0268155  -0.0707291  96  PRO   B N    
3129 C  CA   . PRO   B 96  ? 0.178574  0.365136 0.269961 0.0895166   -0.0180783  -0.0638656  96  PRO   B CA   
3130 C  C    . PRO   B 96  ? 0.184979  0.366396 0.268426 0.0846251   -0.028286   -0.0626128  96  PRO   B C    
3131 O  O    . PRO   B 96  ? 0.195928  0.420379 0.296287 0.0523428   -0.0113119  -0.0736835  96  PRO   B O    
3132 C  CB   . PRO   B 96  ? 0.184967  0.372375 0.292977 0.102399    -0.0170457  -0.0651087  96  PRO   B CB   
3133 C  CG   . PRO   B 96  ? 0.209158  0.371395 0.301063 0.0969233   -0.0293239  -0.0594794  96  PRO   B CG   
3134 C  CD   . PRO   B 96  ? 0.195938  0.361648 0.273233 0.0974106   -0.0224873  -0.0696621  96  PRO   B CD   
3135 N  N    . LYS   B 97  ? 0.178664  0.347287 0.243673 0.0917656   -0.0335502  -0.0568218  97  LYS   B N    
3136 C  CA   . LYS   B 97  ? 0.210492  0.333347 0.237191 0.0942503   -0.0253013  -0.0534538  97  LYS   B CA   
3137 C  C    . LYS   B 97  ? 0.168126  0.327044 0.219822 0.0800562   -0.0218203  -0.0487264  97  LYS   B C    
3138 O  O    . LYS   B 97  ? 0.190958  0.327437 0.226548 0.0893189   -0.00359226 -0.0420548  97  LYS   B O    
3139 C  CB   . LYS   B 97  ? 0.253612  0.362626 0.248306 0.102521    -0.0174904  -0.0464926  97  LYS   B CB   
3140 C  CG   . LYS   B 97  ? 0.306483  0.391199 0.291154 0.109302    -0.0225688  -0.0343326  97  LYS   B CG   
3141 C  CD   . LYS   B 97  ? 0.369691  0.441372 0.336665 0.0943891   -0.00819861 -0.0240398  97  LYS   B CD   
3142 C  CE   . LYS   B 97  ? 0.414169  0.472293 0.363788 0.0968175   -0.0150877  -0.00727876 97  LYS   B CE   
3143 N  NZ   . LYS   B 97  ? 0.455082  0.52523  0.397963 0.0760083   -0.00129064 -0.0106107  97  LYS   B NZ   
3144 N  N    . THR   B 98  ? 0.158933  0.30575  0.215267 0.0636165   -0.0154505  -0.0500795  98  THR   B N    
3145 C  CA   . THR   B 98  ? 0.131548  0.305475 0.221188 0.0555629   -0.0129026  -0.0456344  98  THR   B CA   
3146 C  C    . THR   B 98  ? 0.135436  0.315686 0.203398 0.0412373   -0.0151084  -0.0357435  98  THR   B C    
3147 O  O    . THR   B 98  ? 0.142359  0.341354 0.220254 0.0213463   -0.00313448 -0.034037   98  THR   B O    
3148 C  CB   . THR   B 98  ? 0.130837  0.304119 0.229439 0.0519246   -0.0261369  -0.0480538  98  THR   B CB   
3149 O  OG1  . THR   B 98  ? 0.130913  0.304802 0.241396 0.0456018   -0.0158696  -0.0577965  98  THR   B OG1  
3150 C  CG2  . THR   B 98  ? 0.14274   0.311167 0.225829 0.0569954   -0.0220072  -0.0492793  98  THR   B CG2  
3151 N  N    . PRO   B 99  ? 0.131286  0.295701 0.194372 0.0288076   -0.0105927  -0.0259799  99  PRO   B N    
3152 C  CA   . PRO   B 99  ? 0.133424  0.295838 0.211469 0.0283445   -0.00864782 -0.0239253  99  PRO   B CA   
3153 C  C    . PRO   B 99  ? 0.137017  0.296857 0.191709 0.0203133   -0.00406779 -0.0239611  99  PRO   B C    
3154 O  O    . PRO   B 99  ? 0.146111  0.307368 0.198001 0.0283755   -0.0233829  -0.00942273 99  PRO   B O    
3155 C  CB   . PRO   B 99  ? 0.15974   0.297789 0.196827 0.0257083   -0.0134217  -0.0213326  99  PRO   B CB   
3156 C  CG   . PRO   B 99  ? 0.152422  0.299975 0.206272 0.0321803   -0.00190889 -0.0195815  99  PRO   B CG   
3157 C  CD   . PRO   B 99  ? 0.139449  0.299414 0.206336 0.0364456   -0.00319579 -0.0220663  99  PRO   B CD   
3158 N  N    . LYS   B 100 ? 0.121748  0.301545 0.215788 0.0257989   -0.0088439  -0.0270269  100 LYS   B N    
3159 C  CA   . LYS   B 100 ? 0.13052   0.304976 0.211463 0.0191973   0.00425963  -0.0206478  100 LYS   B CA   
3160 C  C    . LYS   B 100 ? 0.130495  0.290701 0.191232 0.0285431   -0.00145087 -0.0142894  100 LYS   B C    
3161 O  O    . LYS   B 100 ? 0.135693  0.30434  0.187635 0.0344234   0.0106014   -0.0185633  100 LYS   B O    
3162 C  CB   . LYS   B 100 ? 0.152314  0.332727 0.254835 0.0022475   -0.0118927  -0.0275336  100 LYS   B CB   
3163 C  CG   . LYS   B 100 ? 0.205442  0.367111 0.305899 -0.012834   -0.019887   -0.0166439  100 LYS   B CG   
3164 C  CD   . LYS   B 100 ? 0.23428   0.408136 0.369494 -0.0369487  -0.0171188  -0.00711372 100 LYS   B CD   
3165 C  CE   . LYS   B 100 ? 0.293117  0.445664 0.411109 -0.0374495  -0.0120407  0.0107003   100 LYS   B CE   
3166 N  NZ   . LYS   B 100 ? 0.341825  0.47844  0.461888 -0.0529942  -0.0104538  0.00254042  100 LYS   B NZ   
3167 N  N    . TYR   B 101 ? 0.127631  0.268639 0.16903  0.0276      0.00584231  -0.0173838  101 TYR   B N    
3168 C  CA   . TYR   B 101 ? 0.131228  0.255182 0.178147 0.0261436   0.00958552  -0.00829961 101 TYR   B CA   
3169 C  C    . TYR   B 101 ? 0.143357  0.260663 0.193311 0.0172252   0.00217964  0.00293846  101 TYR   B C    
3170 O  O    . TYR   B 101 ? 0.141846  0.281291 0.194127 0.0208113   4.354e-05   0.0144768   101 TYR   B O    
3171 C  CB   . TYR   B 101 ? 0.153333  0.247757 0.169261 0.0234469   0.00568302  -0.00522574 101 TYR   B CB   
3172 C  CG   . TYR   B 101 ? 0.156273  0.244091 0.167107 0.0229871   -0.0148374  0.00147739  101 TYR   B CG   
3173 C  CD1  . TYR   B 101 ? 0.173786  0.242459 0.163047 0.0175325   -0.0112847  -0.00394421 101 TYR   B CD1  
3174 C  CD2  . TYR   B 101 ? 0.160555  0.246854 0.183986 0.0195118   -0.0178262  -0.00248303 101 TYR   B CD2  
3175 C  CE1  . TYR   B 101 ? 0.192255  0.245473 0.171438 0.0207934   -0.0160075  -0.0100607  101 TYR   B CE1  
3176 C  CE2  . TYR   B 101 ? 0.167137  0.249569 0.180483 0.0126531   -0.0277582  0.00588962  101 TYR   B CE2  
3177 C  CZ   . TYR   B 101 ? 0.197773  0.249305 0.179603 0.00883415  -0.0247569  -0.00385703 101 TYR   B CZ   
3178 O  OH   . TYR   B 101 ? 0.236687  0.27892  0.185401 0.00374367  -0.0383922  -0.00427426 101 TYR   B OH   
3179 N  N    . LYS   B 102 ? 0.136161  0.261312 0.196584 0.0181306   0.00186071  0.0195478   102 LYS   B N    
3180 C  CA   . LYS   B 102 ? 0.145683  0.268685 0.209181 0.0204776   -0.0040977  0.0229156   102 LYS   B CA   
3181 C  C    . LYS   B 102 ? 0.146899  0.251633 0.182214 0.0188348   -0.0101669  0.0182025   102 LYS   B C    
3182 O  O    . LYS   B 102 ? 0.142361  0.246056 0.175351 0.0170574   -0.0195427  0.0191369   102 LYS   B O    
3183 C  CB   . LYS   B 102 ? 0.187689  0.291818 0.277254 0.0142427   -0.00515933 0.0459915   102 LYS   B CB   
3184 C  CG   . LYS   B 102 ? 0.243507  0.344701 0.341388 -0.00512759 0.0201515   0.0405206   102 LYS   B CG   
3185 C  CD   . LYS   B 102 ? 0.33598   0.372305 0.406381 -0.0257256  0.0200886   0.0327349   102 LYS   B CD   
3186 C  CE   . LYS   B 102 ? 0.373424  0.41287  0.463655 -0.0429001  0.0236709   0.0291332   102 LYS   B CE   
3187 N  NZ   . LYS   B 102 ? 0.435029  0.441865 0.505499 -0.0367947  0.020419    0.0121847   102 LYS   B NZ   
3188 N  N    . PHE   B 103 ? 0.130337  0.247436 0.170926 0.0235203   -0.00150889 0.0158861   103 PHE   B N    
3189 C  CA   . PHE   B 103 ? 0.135558  0.236405 0.175728 0.0155806   0.00362088  0.00449448  103 PHE   B CA   
3190 C  C    . PHE   B 103 ? 0.160098  0.240223 0.189549 0.0154701   0.00278953  0.0126766   103 PHE   B C    
3191 O  O    . PHE   B 103 ? 0.183485  0.253663 0.196994 0.0236811   0.0193404   0.0247123   103 PHE   B O    
3192 C  CB   . PHE   B 103 ? 0.135876  0.24533  0.178307 0.0153736   -0.0046746  0.00166233  103 PHE   B CB   
3193 C  CG   . PHE   B 103 ? 0.139045  0.248025 0.171316 0.0183817   -0.0114714  -0.00690245 103 PHE   B CG   
3194 C  CD1  . PHE   B 103 ? 0.139531  0.24101  0.169144 0.0238519   -0.0117652  -0.0122246  103 PHE   B CD1  
3195 C  CD2  . PHE   B 103 ? 0.168265  0.255323 0.16906  0.0218438   -0.0142157  -0.014813   103 PHE   B CD2  
3196 C  CE1  . PHE   B 103 ? 0.13157   0.246527 0.176642 0.0229408   -0.00222847 -0.015339   103 PHE   B CE1  
3197 C  CE2  . PHE   B 103 ? 0.163082  0.261621 0.175509 0.0244602   -0.0126004  -0.0260671  103 PHE   B CE2  
3198 C  CZ   . PHE   B 103 ? 0.159329  0.24405  0.176129 0.029978    -0.00132154 -0.0206959  103 PHE   B CZ   
3199 N  N    . VAL   B 104 ? 0.13072   0.226345 0.184313 0.00630509  0.00487384  0.0161352   104 VAL   B N    
3200 C  CA   . VAL   B 104 ? 0.143528  0.230411 0.212818 0.00706392  0.00785274  0.011263    104 VAL   B CA   
3201 C  C    . VAL   B 104 ? 0.156472  0.228832 0.202889 0.00764675  0.025739    0.0226578   104 VAL   B C    
3202 O  O    . VAL   B 104 ? 0.194984  0.234978 0.24832  0.0279519   0.0389655   0.050988    104 VAL   B O    
3203 C  CB   . VAL   B 104 ? 0.169796  0.261707 0.260098 -0.0104257  0.00035836  -0.00166082 104 VAL   B CB   
3204 C  CG1  . VAL   B 104 ? 0.17026   0.280282 0.25662  -0.0207088  0.00051934  0.00364128  104 VAL   B CG1  
3205 C  CG2  . VAL   B 104 ? 0.200187  0.288411 0.284004 -0.0165585  -0.00172158 -0.00353521 104 VAL   B CG2  
3206 N  N    . ARG   B 105 ? 0.145469  0.223328 0.195701 0.00227257  0.0225578   0.0169302   105 ARG   B N    
3207 C  CA   . ARG   B 105 ? 0.151421  0.223894 0.201256 -0.00233014 0.0266338   0.0146245   105 ARG   B CA   
3208 C  C    . ARG   B 105 ? 0.153954  0.213608 0.2148   -0.00253659 0.0267698   0.00960935  105 ARG   B C    
3209 O  O    . ARG   B 105 ? 0.213633  0.213565 0.255778 -0.0048069  0.0428216   0.0108906   105 ARG   B O    
3210 C  CB   . ARG   B 105 ? 0.153712  0.233134 0.213586 0.0159939   0.0196861   0.0166566   105 ARG   B CB   
3211 C  CG   . ARG   B 105 ? 0.148823  0.232221 0.223934 0.0164037   0.0195285   0.0166701   105 ARG   B CG   
3212 C  CD   . ARG   B 105 ? 0.155602  0.233719 0.227138 0.0203767   0.0171435   0.0225546   105 ARG   B CD   
3213 N  NE   . ARG   B 105 ? 0.149356  0.233093 0.240461 0.0257172   0.0106921   0.0197895   105 ARG   B NE   
3214 C  CZ   . ARG   B 105 ? 0.148456  0.22885  0.219367 0.0233876   -0.00285172 0.015387    105 ARG   B CZ   
3215 N  NH1  . ARG   B 105 ? 0.115851  0.230892 0.199343 0.0186697   -0.00446319 0.00876161  105 ARG   B NH1  
3216 N  NH2  . ARG   B 105 ? 0.169734  0.2302   0.231711 0.0309267   0.0176045   0.0129369   105 ARG   B NH2  
3217 N  N    . ILE   B 106 ? 0.16604   0.215885 0.201741 -0.00502721 0.0144614   -0.00358807 106 ILE   B N    
3218 C  CA   . ILE   B 106 ? 0.185318  0.22887  0.212205 -0.00634418 0.0117655   -0.00571281 106 ILE   B CA   
3219 C  C    . ILE   B 106 ? 0.206198  0.229669 0.206129 0.00330306  0.0120001   -0.00502117 106 ILE   B C    
3220 O  O    . ILE   B 106 ? 0.199532  0.230289 0.240596 -0.0100896  0.0170871   -0.00607951 106 ILE   B O    
3221 C  CB   . ILE   B 106 ? 0.197553  0.24389  0.218285 0.00046382  0.0114069   -0.00354155 106 ILE   B CB   
3222 C  CG1  . ILE   B 106 ? 0.219647  0.237139 0.202175 0.00506797  0.0102329   0.00210658  106 ILE   B CG1  
3223 C  CG2  . ILE   B 106 ? 0.198425  0.254919 0.241306 0.00044913  0.0116714   0.00039947  106 ILE   B CG2  
3224 C  CD1  . ILE   B 106 ? 0.227856  0.262317 0.213868 0.0111361   0.0204786   0.0104737   106 ILE   B CD1  
3225 N  N    . GLN   B 107 ? 0.24299   0.243384 0.212765 0.00738476  -0.00770425 -0.0118307  107 GLN   B N    
3226 C  CA   . GLN   B 107 ? 0.265541  0.262585 0.221641 0.0244428   -0.012925   -0.00816327 107 GLN   B CA   
3227 C  C    . GLN   B 107 ? 0.227179  0.242501 0.220799 0.0235869   -0.0281321  0.00715294  107 GLN   B C    
3228 O  O    . GLN   B 107 ? 0.220905  0.211328 0.205569 0.0164242   -0.0246497  0.00987236  107 GLN   B O    
3229 C  CB   . GLN   B 107 ? 0.326142  0.284357 0.272874 0.0217026   0.0115012   0.0035329   107 GLN   B CB   
3230 C  CG   . GLN   B 107 ? 0.388531  0.361422 0.322679 0.0040497   0.0286119   0.0153908   107 GLN   B CG   
3231 C  CD   . GLN   B 107 ? 0.438873  0.418714 0.407356 0.0206043   0.0155763   0.0368113   107 GLN   B CD   
3232 O  OE1  . GLN   B 107 ? 0.475422  0.54269  0.487201 0.0344982   -0.00114616 0.0372143   107 GLN   B OE1  
3233 N  NE2  . GLN   B 107 ? 0.45731   0.489772 0.476322 -0.00512407 0.0142295   0.0320127   107 GLN   B NE2  
3234 N  N    . PRO   B 108 ? 0.213282  0.264618 0.230253 0.0362143   -0.0515446  0.0123448   108 PRO   B N    
3235 C  CA   . PRO   B 108 ? 0.194561  0.262836 0.236763 0.0385429   -0.040852   0.0184217   108 PRO   B CA   
3236 C  C    . PRO   B 108 ? 0.193383  0.222621 0.228102 0.0350531   -0.0137355  0.0110143   108 PRO   B C    
3237 O  O    . PRO   B 108 ? 0.212334  0.2262   0.247716 0.0193771   -0.01001    0.0251187   108 PRO   B O    
3238 C  CB   . PRO   B 108 ? 0.196244  0.288872 0.268498 0.0404514   -0.0489963  0.0276034   108 PRO   B CB   
3239 C  CG   . PRO   B 108 ? 0.226101  0.322779 0.279377 0.0463556   -0.0577907  0.00568135  108 PRO   B CG   
3240 C  CD   . PRO   B 108 ? 0.224161  0.308156 0.248153 0.0304946   -0.0656493  0.0183123   108 PRO   B CD   
3241 N  N    . GLY   B 109 ? 0.175893  0.215454 0.210995 0.0373166   -0.00354749 0.00555029  109 GLY   B N    
3242 C  CA   . GLY   B 109 ? 0.186647  0.227515 0.203688 0.0331323   -0.0014822  -0.0109978  109 GLY   B CA   
3243 C  C    . GLY   B 109 ? 0.180331  0.232871 0.183129 0.02946     -0.0092302  -0.00953563 109 GLY   B C    
3244 O  O    . GLY   B 109 ? 0.194104  0.307006 0.197083 0.0239821   -0.013291   -0.0533271  109 GLY   B O    
3245 N  N    . GLN   B 110 ? 0.168779  0.210641 0.172248 0.0330414   -0.0159291  -0.00095714 110 GLN   B N    
3246 C  CA   . GLN   B 110 ? 0.166764  0.221971 0.198536 0.0306702   -0.0183287  0.00372635  110 GLN   B CA   
3247 C  C    . GLN   B 110 ? 0.15989   0.213633 0.183012 0.029309    -0.0200744  -0.0043571  110 GLN   B C    
3248 O  O    . GLN   B 110 ? 0.164936  0.222323 0.178975 0.020517    -0.020056   0.0197282   110 GLN   B O    
3249 C  CB   . GLN   B 110 ? 0.192907  0.248986 0.214383 0.0395319   -0.00594725 0.00260826  110 GLN   B CB   
3250 C  CG   . GLN   B 110 ? 0.245728  0.30158  0.270482 0.0185442   -0.00826091 0.0181166   110 GLN   B CG   
3251 C  CD   . GLN   B 110 ? 0.273363  0.390532 0.297414 0.00325345  -0.0192942  -0.00254594 110 GLN   B CD   
3252 O  OE1  . GLN   B 110 ? 0.316831  0.395977 0.347224 -0.025541   -0.072069   -0.0210456  110 GLN   B OE1  
3253 N  NE2  . GLN   B 110 ? 0.297721  0.467696 0.37592  -0.0133333  -0.0349267  -0.0117254  110 GLN   B NE2  
3254 N  N    . THR   B 111 ? 0.145539  0.203182 0.198474 0.0238225   -0.0205853  -0.00509433 111 THR   B N    
3255 C  CA   . THR   B 111 ? 0.140317  0.209019 0.188004 0.020467    -0.0215502  -0.00313216 111 THR   B CA   
3256 C  C    . THR   B 111 ? 0.140727  0.195856 0.181064 0.019114    -0.0216888  0.00269123  111 THR   B C    
3257 O  O    . THR   B 111 ? 0.148953  0.206458 0.199789 0.0251035   -0.00300501 0.0148919   111 THR   B O    
3258 C  CB   . THR   B 111 ? 0.156502  0.223716 0.200055 0.0199234   -0.0279036  -0.0108717  111 THR   B CB   
3259 O  OG1  . THR   B 111 ? 0.1475    0.228377 0.210656 0.0159985   -0.0287716  -0.0147061  111 THR   B OG1  
3260 C  CG2  . THR   B 111 ? 0.15714   0.235096 0.200611 0.0244517   -0.03376    -0.0187061  111 THR   B CG2  
3261 N  N    . PHE   B 112 ? 0.123087  0.192082 0.184856 0.0237924   -0.0143446  0.00791785  112 PHE   B N    
3262 C  CA   . PHE   B 112 ? 0.12179   0.181836 0.186595 0.0166723   -0.0271018  0.0010766   112 PHE   B CA   
3263 C  C    . PHE   B 112 ? 0.112217  0.17957  0.166653 0.0150214   -0.0264574  -0.00128872 112 PHE   B C    
3264 O  O    . PHE   B 112 ? 0.116952  0.198535 0.168061 0.0286006   -0.0278691  8.697e-05   112 PHE   B O    
3265 C  CB   . PHE   B 112 ? 0.123857  0.194663 0.188985 0.0141624   -0.0308005  0.00384725  112 PHE   B CB   
3266 C  CG   . PHE   B 112 ? 0.122595  0.192026 0.198439 0.0188204   -0.0410347  0.00406647  112 PHE   B CG   
3267 C  CD1  . PHE   B 112 ? 0.12359   0.202304 0.24079  0.0201664   -0.0413123  0.00552576  112 PHE   B CD1  
3268 C  CD2  . PHE   B 112 ? 0.131466  0.195853 0.207169 0.0224221   -0.0417879  0.00758176  112 PHE   B CD2  
3269 C  CE1  . PHE   B 112 ? 0.132424  0.212893 0.257656 0.0153112   -0.0463164  0.0133315   112 PHE   B CE1  
3270 C  CE2  . PHE   B 112 ? 0.141716  0.199118 0.224848 0.0106266   -0.0387526  0.0112177   112 PHE   B CE2  
3271 C  CZ   . PHE   B 112 ? 0.122412  0.213948 0.250648 0.0118551   -0.0396248  0.0147558   112 PHE   B CZ   
3272 N  N    . SER   B 113 ? 0.109246  0.175146 0.169932 0.013074    -0.0288176  -0.004552   113 SER   B N    
3273 C  CA   . SER   B 113 ? 0.122789  0.17325  0.167971 0.0119234   -0.0306428  -0.00390718 113 SER   B CA   
3274 C  C    . SER   B 113 ? 0.124672  0.171489 0.154509 0.00589615  -0.0219715  -0.00256212 113 SER   B C    
3275 O  O    . SER   B 113 ? 0.128369  0.210784 0.152318 -0.011982   -0.0173413  -0.013667   113 SER   B O    
3276 C  CB   . SER   B 113 ? 0.129382  0.180798 0.194652 0.0135247   -0.0504127  -0.00563188 113 SER   B CB   
3277 O  OG   . SER   B 113 ? 0.154695  0.203211 0.242041 0.00036341  -0.0748672  -0.00751739 113 SER   B OG   
3278 N  N    . VAL   B 114 ? 0.139956  0.171967 0.14911  0.00754569  -0.00691934 -0.0092704  114 VAL   B N    
3279 C  CA   . VAL   B 114 ? 0.129423  0.171799 0.14933  0.0113358   -0.00857514 -0.0080346  114 VAL   B CA   
3280 C  C    . VAL   B 114 ? 0.133602  0.168308 0.146859 0.00872186  -0.0122363  -0.00748428 114 VAL   B C    
3281 O  O    . VAL   B 114 ? 0.157299  0.19071  0.148388 0.0168377   -0.0188037  -0.012406   114 VAL   B O    
3282 C  CB   . VAL   B 114 ? 0.135968  0.193127 0.172297 0.0225886   0.00560725  5.397e-05   114 VAL   B CB   
3283 C  CG1  . VAL   B 114 ? 0.132891  0.202443 0.16901  0.0223425   0.0109916   0.00056101  114 VAL   B CG1  
3284 C  CG2  . VAL   B 114 ? 0.146615  0.197658 0.193822 0.0202904   0.00564547  0.0128698   114 VAL   B CG2  
3285 N  N    . LEU   B 115 ? 0.132227  0.170098 0.15027  0.00756912  -0.0203732  -0.0129514  115 LEU   B N    
3286 C  CA   . LEU   B 115 ? 0.131805  0.178003 0.15351  0.0117343   -0.017358   -0.0165226  115 LEU   B CA   
3287 C  C    . LEU   B 115 ? 0.131054  0.182782 0.153272 0.00680763  -0.0150945  -0.0152394  115 LEU   B C    
3288 O  O    . LEU   B 115 ? 0.130482  0.20025  0.161506 0.00141918  -0.00792701 -0.0210016  115 LEU   B O    
3289 C  CB   . LEU   B 115 ? 0.130901  0.188491 0.165336 0.0178665   -0.0168709  -0.0214338  115 LEU   B CB   
3290 C  CG   . LEU   B 115 ? 0.141571  0.196867 0.178673 0.0197882   -0.0151668  -0.0188872  115 LEU   B CG   
3291 C  CD1  . LEU   B 115 ? 0.144497  0.208833 0.187916 0.0200996   -0.0193591  -0.0210863  115 LEU   B CD1  
3292 C  CD2  . LEU   B 115 ? 0.152954  0.208386 0.180654 0.0292353   -0.0142313  -0.0230409  115 LEU   B CD2  
3293 N  N    . ALA   B 116 ? 0.144464  0.191805 0.146026 0.00483353  -0.016948   -0.0167561  116 ALA   B N    
3294 C  CA   . ALA   B 116 ? 0.164245  0.189476 0.161154 -0.00253337 -0.0155171  -0.0116518  116 ALA   B CA   
3295 C  C    . ALA   B 116 ? 0.160682  0.190987 0.169004 0.0062259   -0.0133136  -0.00885888 116 ALA   B C    
3296 O  O    . ALA   B 116 ? 0.213361  0.209182 0.198008 0.0206342   -0.0494316  -0.0123629  116 ALA   B O    
3297 C  CB   . ALA   B 116 ? 0.163657  0.198211 0.172968 -0.00965748 -0.00580928 -0.00757909 116 ALA   B CB   
3298 N  N    A CYS   B 117 ? 0.149628  0.184151 0.170371 0.00323937  -0.00677038 -0.011366   117 CYS   B N    
3299 N  N    B CYS   B 117 ? 0.1829    0.200338 0.189626 0.00246224  -0.016483   -0.0128686  117 CYS   B N    
3300 C  CA   A CYS   B 117 ? 0.146762  0.181426 0.165059 0.00031509  -0.00753395 -0.00829252 117 CYS   B CA   
3301 C  CA   B CYS   B 117 ? 0.200409  0.202644 0.204937 0.00347959  -0.0167039  -0.00738819 117 CYS   B CA   
3302 C  C    A CYS   B 117 ? 0.163169  0.179609 0.172155 -0.00589847 -0.00268201 -0.00714457 117 CYS   B C    
3303 C  C    B CYS   B 117 ? 0.199846  0.190287 0.193138 0.00071081  -0.00745011 -0.0050773  117 CYS   B C    
3304 O  O    A CYS   B 117 ? 0.164581  0.1789   0.167266 -0.00608614 -0.0001385  -0.0100711  117 CYS   B O    
3305 O  O    B CYS   B 117 ? 0.196408  0.193691 0.184581 -0.00362245 -0.00380243 -0.0113905  117 CYS   B O    
3306 C  CB   A CYS   B 117 ? 0.133234  0.177293 0.162911 -0.00245884 -0.00687322 -0.0110049  117 CYS   B CB   
3307 C  CB   B CYS   B 117 ? 0.235441  0.225139 0.220055 0.00163302  -0.0120679  -0.00181401 117 CYS   B CB   
3308 S  SG   A CYS   B 117 ? 0.119251  0.173179 0.149522 -0.00404038 -0.0093722  -0.0143328  117 CYS   B SG   
3309 S  SG   B CYS   B 117 ? 0.304234  0.271383 0.287251 0.0233942   -0.00951696 -0.00774056 117 CYS   B SG   
3310 N  N    . TYR   B 118 ? 0.192746  0.191589 0.193491 -0.00530703 -0.00557627 0.00047466  118 TYR   B N    
3311 C  CA   . TYR   B 118 ? 0.201241  0.185991 0.19883  -0.00991584 -0.00012505 -0.00797091 118 TYR   B CA   
3312 C  C    . TYR   B 118 ? 0.232068  0.189104 0.211216 -0.00514329 0.00603343  -0.01368    118 TYR   B C    
3313 O  O    . TYR   B 118 ? 0.24924   0.200192 0.218431 0.0105383   0.00398044  -0.00834248 118 TYR   B O    
3314 C  CB   . TYR   B 118 ? 0.206071  0.205321 0.195087 -0.016327   -0.00433889 -0.00249469 118 TYR   B CB   
3315 C  CG   . TYR   B 118 ? 0.205695  0.202193 0.19086  -0.0212674  -0.00509883 -0.00238196 118 TYR   B CG   
3316 C  CD1  . TYR   B 118 ? 0.209174  0.204793 0.18614  -0.0239761  -0.00849069 -0.002632   118 TYR   B CD1  
3317 C  CD2  . TYR   B 118 ? 0.196048  0.21156  0.185458 -0.017862   -0.00569521 -0.00622358 118 TYR   B CD2  
3318 C  CE1  . TYR   B 118 ? 0.206702  0.210972 0.181674 -0.0231671  -0.00816048 -0.00594723 118 TYR   B CE1  
3319 C  CE2  . TYR   B 118 ? 0.207864  0.209285 0.185375 -0.0201781  -0.00750678 -0.0101977  118 TYR   B CE2  
3320 C  CZ   . TYR   B 118 ? 0.200407  0.205962 0.174073 -0.0204908  -0.00822609 -0.00798437 118 TYR   B CZ   
3321 O  OH   . TYR   B 118 ? 0.196496  0.2118   0.181054 -0.0152542  0.00260642  -0.00382164 118 TYR   B OH   
3322 N  N    . ASN   B 119 ? 0.270518  0.200395 0.226898 -0.0102668  0.00658432  -0.0196989  119 ASN   B N    
3323 C  CA   . ASN   B 119 ? 0.305672  0.212302 0.255001 0.00267377  0.0105643   -0.0250381  119 ASN   B CA   
3324 C  C    . ASN   B 119 ? 0.292924  0.206658 0.231253 0.0127796   0.00458879  -0.0317906  119 ASN   B C    
3325 O  O    . ASN   B 119 ? 0.320669  0.214007 0.269012 0.0245078   0.0224064   -0.0308557  119 ASN   B O    
3326 C  CB   . ASN   B 119 ? 0.361003  0.228062 0.296612 0.00048812  0.0206545   -0.0174597  119 ASN   B CB   
3327 C  CG   . ASN   B 119 ? 0.396695  0.306333 0.367372 -0.00712394 0.0208287   -0.00687698 119 ASN   B CG   
3328 O  OD1  . ASN   B 119 ? 0.468048  0.423534 0.469375 -0.0243973  -0.0148343  -0.00717675 119 ASN   B OD1  
3329 N  ND2  . ASN   B 119 ? 0.451034  0.367314 0.403068 0.00235766  0.0311095   0.00243178  119 ASN   B ND2  
3330 N  N    . GLY   B 120 ? 0.263196  0.202806 0.211157 0.0230362   -0.0039188  -0.0265575  120 GLY   B N    
3331 C  CA   . GLY   B 120 ? 0.254587  0.209172 0.212393 0.0228116   0.00038045  -0.0277818  120 GLY   B CA   
3332 C  C    . GLY   B 120 ? 0.248412  0.22546  0.235611 0.0183045   0.00041285  -0.0313231  120 GLY   B C    
3333 O  O    . GLY   B 120 ? 0.235747  0.271205 0.256795 0.0218706   0.00871751  -0.0254031  120 GLY   B O    
3334 N  N    A SER   B 121 ? 0.242518  0.22302  0.231777 0.0172315   -0.0123419  -0.0263381  121 SER   B N    
3335 N  N    B SER   B 121 ? 0.244621  0.214216 0.228086 0.0229507   -0.00635979 -0.026584   121 SER   B N    
3336 C  CA   A SER   B 121 ? 0.253625  0.228807 0.240385 0.0192926   -0.0186542  -0.0268204  121 SER   B CA   
3337 C  CA   B SER   B 121 ? 0.255376  0.216589 0.227854 0.0284124   -0.00740421 -0.0272105  121 SER   B CA   
3338 C  C    A SER   B 121 ? 0.234323  0.223972 0.227205 0.0275514   -0.0140387  -0.020967   121 SER   B C    
3339 C  C    B SER   B 121 ? 0.229773  0.212956 0.210946 0.0330763   -0.00672165 -0.0199073  121 SER   B C    
3340 O  O    A SER   B 121 ? 0.233078  0.218364 0.238836 0.0359192   -0.0111872  -0.0205845  121 SER   B O    
3341 O  O    B SER   B 121 ? 0.213456  0.208485 0.194383 0.0306855   -0.0112727  -0.0109902  121 SER   B O    
3342 C  CB   A SER   B 121 ? 0.277629  0.23636  0.261065 0.0200038   -0.0265713  -0.0237163  121 SER   B CB   
3343 C  CB   B SER   B 121 ? 0.280008  0.214087 0.245007 0.0357299   -0.00520207 -0.0299353  121 SER   B CB   
3344 O  OG   A SER   B 121 ? 0.284576  0.260874 0.29251  0.0166124   -0.0404569  -0.0223492  121 SER   B OG   
3345 O  OG   B SER   B 121 ? 0.310474  0.221167 0.267882 0.0474049   -0.00168504 -0.0389416  121 SER   B OG   
3346 N  N    . PRO   B 122 ? 0.228147  0.215928 0.211709 0.0329347   -0.0139057  -0.0216143  122 PRO   B N    
3347 C  CA   . PRO   B 122 ? 0.236845  0.211539 0.218836 0.0385625   -0.020994   -0.0192227  122 PRO   B CA   
3348 C  C    . PRO   B 122 ? 0.23604   0.203288 0.220242 0.0403684   -0.0254587  -0.00458986 122 PRO   B C    
3349 O  O    . PRO   B 122 ? 0.267121  0.213517 0.228496 0.0617555   -0.0277861  -0.00194905 122 PRO   B O    
3350 C  CB   . PRO   B 122 ? 0.241552  0.222115 0.220307 0.0310922   -0.0194167  -0.0136059  122 PRO   B CB   
3351 C  CG   . PRO   B 122 ? 0.244336  0.243828 0.224892 0.0279377   -0.0225219  -0.0167769  122 PRO   B CG   
3352 C  CD   . PRO   B 122 ? 0.237     0.240914 0.218651 0.0295946   -0.0184752  -0.0182758  122 PRO   B CD   
3353 N  N    . SER   B 123 ? 0.22926   0.195915 0.211292 0.0351236   -0.019417   -0.00420826 123 SER   B N    
3354 C  CA   . SER   B 123 ? 0.225096  0.209777 0.212016 0.0112469   -0.0274868  0.00091926  123 SER   B CA   
3355 C  C    . SER   B 123 ? 0.179352  0.190225 0.198498 0.0196012   -0.0157561  0.00774044  123 SER   B C    
3356 O  O    . SER   B 123 ? 0.201196  0.221706 0.197226 0.0232191   -0.0277976  0.00010268  123 SER   B O    
3357 C  CB   . SER   B 123 ? 0.254184  0.25348  0.268335 -0.0183987  -0.0277638  -0.011113   123 SER   B CB   
3358 O  OG   . SER   B 123 ? 0.291934  0.340978 0.336959 -0.0127051  -0.0328916  0.0033725   123 SER   B OG   
3359 N  N    . GLY   B 124 ? 0.157515  0.177927 0.174716 0.0118041   -0.00785116 -0.00201599 124 GLY   B N    
3360 C  CA   . GLY   B 124 ? 0.150508  0.178328 0.178688 0.0142734   -0.0146313  -0.00612178 124 GLY   B CA   
3361 C  C    . GLY   B 124 ? 0.147469  0.178285 0.170547 0.00762212  -0.0219005  -0.0122723  124 GLY   B C    
3362 O  O    . GLY   B 124 ? 0.164582  0.189434 0.16969  -0.00265872 -0.0309198  -0.00945181 124 GLY   B O    
3363 N  N    . VAL   B 125 ? 0.136011  0.174529 0.161043 0.0120494   -0.030951   -0.0168475  125 VAL   B N    
3364 C  CA   . VAL   B 125 ? 0.140136  0.180135 0.177221 0.0157038   -0.0265806  -0.0120826  125 VAL   B CA   
3365 C  C    . VAL   B 125 ? 0.157138  0.182137 0.16188  0.0206781   -0.0277718  -0.00990275 125 VAL   B C    
3366 O  O    . VAL   B 125 ? 0.20079   0.206124 0.169337 0.0348139   -0.0423386  -0.0178914  125 VAL   B O    
3367 C  CB   . VAL   B 125 ? 0.15731   0.214432 0.231131 0.00822622  -0.0146541  -0.00733773 125 VAL   B CB   
3368 C  CG1  . VAL   B 125 ? 0.192285  0.239924 0.237598 0.0103264   -0.0172693  -0.0146963  125 VAL   B CG1  
3369 C  CG2  . VAL   B 125 ? 0.159834  0.223626 0.256716 -0.00095629 -0.0127047  -0.00613715 125 VAL   B CG2  
3370 N  N    . TYR   B 126 ? 0.136203  0.18777  0.146973 0.0268985   -0.0269245  -0.0135547  126 TYR   B N    
3371 C  CA   . TYR   B 126 ? 0.139142  0.189002 0.161622 0.0253625   -0.0151375  -0.0179674  126 TYR   B CA   
3372 C  C    . TYR   B 126 ? 0.144041  0.188527 0.160434 0.0217392   -0.0138175  -0.0193915  126 TYR   B C    
3373 O  O    . TYR   B 126 ? 0.1807    0.196654 0.158003 0.0137103   0.00706829  -0.0124775  126 TYR   B O    
3374 C  CB   . TYR   B 126 ? 0.150854  0.202041 0.170002 0.025587    -0.00293926 -0.0118921  126 TYR   B CB   
3375 C  CG   . TYR   B 126 ? 0.143643  0.215519 0.188599 0.0131375   0.00969373  -0.0136025  126 TYR   B CG   
3376 C  CD1  . TYR   B 126 ? 0.137367  0.223327 0.20045  0.00783031  0.0105282   -0.0133502  126 TYR   B CD1  
3377 C  CD2  . TYR   B 126 ? 0.169173  0.231792 0.224436 0.00546427  -0.00051749 -0.0221663  126 TYR   B CD2  
3378 C  CE1  . TYR   B 126 ? 0.131049  0.24542  0.214962 0.00279575  0.0111494   -0.0162087  126 TYR   B CE1  
3379 C  CE2  . TYR   B 126 ? 0.168932  0.235165 0.236256 -0.00360023 0.00790495  -0.0319661  126 TYR   B CE2  
3380 C  CZ   . TYR   B 126 ? 0.140098  0.254329 0.205168 -0.00748201 0.00960635  -0.0364857  126 TYR   B CZ   
3381 O  OH   . TYR   B 126 ? 0.129275  0.324113 0.234526 -0.0298797  0.0128954   -0.0498245  126 TYR   B OH   
3382 N  N    . GLN   B 127 ? 0.184587  0.201032 0.179995 0.0300118   -0.0226643  -0.0257582  127 GLN   B N    
3383 C  CA   . GLN   B 127 ? 0.183684  0.216975 0.204115 0.0421887   -0.0219394  -0.0214777  127 GLN   B CA   
3384 C  C    . GLN   B 127 ? 0.178381  0.23131  0.224021 0.0508103   -0.0048703  -0.00271994 127 GLN   B C    
3385 O  O    . GLN   B 127 ? 0.18863   0.238371 0.236899 0.0601535   0.00554459  0.00780819  127 GLN   B O    
3386 C  CB   . GLN   B 127 ? 0.235741  0.267318 0.225946 0.0233567   -0.0268042  -0.0532355  127 GLN   B CB   
3387 C  CG   . GLN   B 127 ? 0.250447  0.310459 0.241702 0.0208062   -0.0253271  -0.0651917  127 GLN   B CG   
3388 C  CD   . GLN   B 127 ? 0.215335  0.324572 0.240513 0.0168111   -0.0459816  -0.0670097  127 GLN   B CD   
3389 O  OE1  . GLN   B 127 ? 0.189221  0.335853 0.249911 0.019989    -0.0513872  -0.0768951  127 GLN   B OE1  
3390 N  NE2  . GLN   B 127 ? 0.192993  0.325036 0.224428 0.0640997   -0.0595545  -0.0677591  127 GLN   B NE2  
3391 N  N    . CYS   B 128 ? 0.154944  0.227513 0.229089 0.0492175   -0.00189784 0.0198959   128 CYS   B N    
3392 C  CA   . CYS   B 128 ? 0.154909  0.239972 0.24066  0.0444229   -0.0128473  0.0226946   128 CYS   B CA   
3393 C  C    . CYS   B 128 ? 0.135613  0.23084  0.234244 0.0381071   0.00127831  0.0249041   128 CYS   B C    
3394 O  O    . CYS   B 128 ? 0.152251  0.240308 0.327083 0.0650663   0.034147    0.0619086   128 CYS   B O    
3395 C  CB   . CYS   B 128 ? 0.131092  0.266417 0.264578 0.0150526   -0.0332355  0.0308812   128 CYS   B CB   
3396 S  SG   . CYS   B 128 ? 0.29556   0.301243 0.284909 -0.0151662  -0.0178631  0.00809455  128 CYS   B SG   
3397 N  N    . ALA   B 129 ? 0.138163  0.247102 0.216354 0.0427978   -0.00398008 0.0430141   129 ALA   B N    
3398 C  CA   . ALA   B 129 ? 0.136398  0.2377   0.200519 0.0365953   -0.0204894  0.0284807   129 ALA   B CA   
3399 C  C    . ALA   B 129 ? 0.135862  0.225443 0.198572 0.0265935   -0.0197729  0.0172807   129 ALA   B C    
3400 O  O    . ALA   B 129 ? 0.145322  0.233942 0.210738 0.0224898   -0.019107   0.0197475   129 ALA   B O    
3401 C  CB   . ALA   B 129 ? 0.159151  0.241137 0.213037 0.0263578   -0.0311717  0.0260692   129 ALA   B CB   
3402 N  N    . MET   B 130 ? 0.128456  0.209737 0.177499 0.0305021   -0.0257831  0.00308927  130 MET   B N    
3403 C  CA   . MET   B 130 ? 0.132034  0.20419  0.185446 0.0252607   -0.0334504  -0.00919581 130 MET   B CA   
3404 C  C    . MET   B 130 ? 0.131365  0.190849 0.187789 0.0240529   -0.0371774  -0.00414511 130 MET   B C    
3405 O  O    . MET   B 130 ? 0.133942  0.185508 0.210113 0.0253614   -0.0346481  -0.0112955  130 MET   B O    
3406 C  CB   . MET   B 130 ? 0.143664  0.212939 0.193754 0.0339458   -0.0318768  -0.0112896  130 MET   B CB   
3407 C  CG   . MET   B 130 ? 0.144255  0.232698 0.210302 0.0422832   -0.0383442  -0.0125047  130 MET   B CG   
3408 S  SD   . MET   B 130 ? 0.17692   0.251187 0.203457 0.0348438   -0.0395816  -0.0287021  130 MET   B SD   
3409 C  CE   . MET   B 130 ? 0.180709  0.234739 0.190643 0.0371301   -0.0510638  -0.0307821  130 MET   B CE   
3410 N  N    . ARG   B 131 ? 0.132614  0.178348 0.18381  0.0136869   -0.0414454  -0.0198641  131 ARG   B N    
3411 C  CA   . ARG   B 131 ? 0.130406  0.184009 0.176602 0.014283    -0.0354309  -0.0214504  131 ARG   B CA   
3412 C  C    . ARG   B 131 ? 0.123525  0.196369 0.169876 0.0155717   -0.0358787  -0.0259313  131 ARG   B C    
3413 O  O    . ARG   B 131 ? 0.113995  0.216292 0.162913 0.0280862   -0.0283934  -0.0151762  131 ARG   B O    
3414 C  CB   . ARG   B 131 ? 0.136598  0.191207 0.178876 0.0123294   -0.0332154  -0.020848   131 ARG   B CB   
3415 C  CG   . ARG   B 131 ? 0.149787  0.19478  0.181764 0.0122351   -0.0344368  -0.0217109  131 ARG   B CG   
3416 C  CD   . ARG   B 131 ? 0.15196   0.192637 0.18445  0.0111375   -0.0373312  -0.0238241  131 ARG   B CD   
3417 N  NE   . ARG   B 131 ? 0.144375  0.198759 0.183472 0.0142761   -0.040461   -0.0317007  131 ARG   B NE   
3418 C  CZ   . ARG   B 131 ? 0.136029  0.197481 0.192061 0.0115494   -0.0356679  -0.0376028  131 ARG   B CZ   
3419 N  NH1  . ARG   B 131 ? 0.137064  0.198896 0.191129 0.0169947   -0.0363428  -0.0439508  131 ARG   B NH1  
3420 N  NH2  . ARG   B 131 ? 0.14179   0.2089   0.211327 0.0233658   -0.039385   -0.0385206  131 ARG   B NH2  
3421 N  N    . PRO   B 132 ? 0.130933  0.190292 0.169321 0.0212933   -0.0432234  -0.0197364  132 PRO   B N    
3422 C  CA   . PRO   B 132 ? 0.137756  0.19769  0.173303 0.0253394   -0.0404049  -0.0161148  132 PRO   B CA   
3423 C  C    . PRO   B 132 ? 0.132003  0.198337 0.175882 0.0253362   -0.0353952  -0.0166333  132 PRO   B C    
3424 O  O    . PRO   B 132 ? 0.148848  0.224316 0.177363 0.0234034   -0.0362914  -0.00702245 132 PRO   B O    
3425 C  CB   . PRO   B 132 ? 0.152692  0.200612 0.181973 0.0225582   -0.0395026  -0.0197436  132 PRO   B CB   
3426 C  CG   . PRO   B 132 ? 0.154726  0.20338  0.184207 0.0152642   -0.0421723  -0.0243642  132 PRO   B CG   
3427 C  CD   . PRO   B 132 ? 0.150844  0.201312 0.172014 0.0186108   -0.0441491  -0.022107   132 PRO   B CD   
3428 N  N    . ASN   B 133 ? 0.123334  0.209325 0.164611 0.0196466   -0.0360976  -0.0150621  133 ASN   B N    
3429 C  CA   . ASN   B 133 ? 0.131773  0.217238 0.161306 0.014249    -0.033978   -0.015882   133 ASN   B CA   
3430 C  C    . ASN   B 133 ? 0.141891  0.215785 0.165835 0.0145458   -0.0332519  -0.0201492  133 ASN   B C    
3431 O  O    . ASN   B 133 ? 0.136313  0.235018 0.173535 0.0143098   -0.0388193  -0.0286549  133 ASN   B O    
3432 C  CB   . ASN   B 133 ? 0.140976  0.226567 0.165218 0.0186977   -0.023008   -0.0198897  133 ASN   B CB   
3433 C  CG   . ASN   B 133 ? 0.132514  0.224357 0.168536 0.0251216   -0.0163779  -0.0196417  133 ASN   B CG   
3434 O  OD1  . ASN   B 133 ? 0.1289    0.231261 0.167247 0.0251906   -0.0224533  -0.0186273  133 ASN   B OD1  
3435 N  ND2  . ASN   B 133 ? 0.136344  0.237971 0.170708 0.0217417   -0.00939501 -0.0138682  133 ASN   B ND2  
3436 N  N    . PHE   B 134 ? 0.140242  0.215199 0.144919 0.0157443   -0.0303695  -0.0215463  134 PHE   B N    
3437 C  CA   . PHE   B 134 ? 0.162063  0.215117 0.147606 0.0187308   -0.0216989  -0.0210379  134 PHE   B CA   
3438 C  C    . PHE   B 134 ? 0.180491  0.211031 0.153722 0.0201687   -0.0142426  -0.021936   134 PHE   B C    
3439 O  O    . PHE   B 134 ? 0.284658  0.214107 0.170548 0.0393917   0.0193511   -0.0155703  134 PHE   B O    
3440 C  CB   . PHE   B 134 ? 0.161024  0.225667 0.150595 0.0182998   -0.0232994  -0.0214448  134 PHE   B CB   
3441 C  CG   . PHE   B 134 ? 0.183103  0.221389 0.162909 0.0229614   -0.0176276  -0.0125435  134 PHE   B CG   
3442 C  CD1  . PHE   B 134 ? 0.196111  0.234486 0.194768 0.0164717   -0.0111716  0.00520667  134 PHE   B CD1  
3443 C  CD2  . PHE   B 134 ? 0.189213  0.229738 0.187118 0.0173403   -0.0189122  0.00485666  134 PHE   B CD2  
3444 C  CE1  . PHE   B 134 ? 0.209523  0.253138 0.212804 0.0130339   0.00432224  0.0127158   134 PHE   B CE1  
3445 C  CE2  . PHE   B 134 ? 0.218381  0.244163 0.203345 0.0231852   -0.0147224  0.0188297   134 PHE   B CE2  
3446 C  CZ   . PHE   B 134 ? 0.227835  0.243186 0.22017  0.00854275  -0.00515896 0.0305325   134 PHE   B CZ   
3447 N  N    . THR   B 135 ? 0.170021  0.209276 0.149686 0.00887282  -0.0114766  -0.0281499  135 THR   B N    
3448 C  CA   . THR   B 135 ? 0.153743  0.208907 0.159647 0.00724091  -0.0127158  -0.024485   135 THR   B CA   
3449 C  C    . THR   B 135 ? 0.140978  0.191716 0.163276 0.00293642  -0.00525555 -0.0211565  135 THR   B C    
3450 O  O    . THR   B 135 ? 0.150014  0.196376 0.184543 -0.00032234 -0.00951411 -0.0291206  135 THR   B O    
3451 C  CB   . THR   B 135 ? 0.150327  0.217182 0.164924 0.00166545  -0.0180869  -0.0143111  135 THR   B CB   
3452 O  OG1  . THR   B 135 ? 0.148921  0.226415 0.174579 0.00927843  -0.00815976 -0.00873738 135 THR   B OG1  
3453 C  CG2  . THR   B 135 ? 0.15183   0.234455 0.181918 0.00300875  -0.0210725  -0.0108732  135 THR   B CG2  
3454 N  N    . ILE   B 136 ? 0.135156  0.192857 0.168063 -0.00147968 -0.00738294 -0.0159115  136 ILE   B N    
3455 C  CA   . ILE   B 136 ? 0.133561  0.202951 0.176333 0.00506694  -0.00628303 -0.0132017  136 ILE   B CA   
3456 C  C    . ILE   B 136 ? 0.129994  0.196803 0.177371 -0.00085379 -0.00596312 -0.0171319  136 ILE   B C    
3457 O  O    . ILE   B 136 ? 0.129032  0.210958 0.185357 -0.00723196 -0.00868974 -0.0150119  136 ILE   B O    
3458 C  CB   . ILE   B 136 ? 0.157322  0.230757 0.202235 0.0126871   0.0140769   -0.0154939  136 ILE   B CB   
3459 C  CG1  . ILE   B 136 ? 0.162363  0.234474 0.185692 0.00632478  0.0145699   -0.0184999  136 ILE   B CG1  
3460 C  CG2  . ILE   B 136 ? 0.17157   0.237795 0.24082  0.00666922  0.0281424   -0.0113616  136 ILE   B CG2  
3461 C  CD1  . ILE   B 136 ? 0.173623  0.226988 0.189236 0.0127524   0.00910072  -0.0242184  136 ILE   B CD1  
3462 N  N    . LYS   B 137 ? 0.133298  0.209689 0.185632 -0.00497193 -0.011794   -0.0189582  137 LYS   B N    
3463 C  CA   . LYS   B 137 ? 0.140729  0.220992 0.196726 -0.00799264 -0.00473815 -0.0163038  137 LYS   B CA   
3464 C  C    . LYS   B 137 ? 0.148403  0.212394 0.204652 -0.0119634  0.00146596  -0.0154708  137 LYS   B C    
3465 O  O    . LYS   B 137 ? 0.153764  0.217609 0.213782 -0.00728667 -0.0106017  -0.0148153  137 LYS   B O    
3466 C  CB   . LYS   B 137 ? 0.183126  0.242347 0.221625 -0.00137678 -0.0122348  -0.02968    137 LYS   B CB   
3467 C  CG   . LYS   B 137 ? 0.211916  0.27544  0.252991 0.0150212   -0.00801301 -0.0316872  137 LYS   B CG   
3468 C  CD   . LYS   B 137 ? 0.27693   0.324976 0.28465  0.0226271   -0.00119745 -0.0471     137 LYS   B CD   
3469 C  CE   . LYS   B 137 ? 0.344554  0.364144 0.334743 0.0325062   -0.00131072 -0.0376379  137 LYS   B CE   
3470 N  NZ   . LYS   B 137 ? 0.39453   0.408139 0.346213 0.0294864   -5.682e-05  -0.0503379  137 LYS   B NZ   
3471 N  N    . GLY   B 138 ? 0.137901  0.212571 0.218986 -0.0145852  0.00274091  -0.021229   138 GLY   B N    
3472 C  CA   . GLY   B 138 ? 0.147388  0.214723 0.223303 -0.00962801 0.00596144  -0.0264347  138 GLY   B CA   
3473 C  C    . GLY   B 138 ? 0.138127  0.22066  0.192967 -0.0148751  0.00841184  -0.0329343  138 GLY   B C    
3474 O  O    . GLY   B 138 ? 0.147384  0.249363 0.220898 -0.0170489  0.0329664   -0.0449529  138 GLY   B O    
3475 N  N    . SER   B 139 ? 0.136079  0.217909 0.169186 -0.0127773  -0.00294524 -0.0179632  139 SER   B N    
3476 C  CA   . SER   B 139 ? 0.131593  0.227591 0.154232 -0.00959473 -0.00798701 -0.0119978  139 SER   B CA   
3477 C  C    . SER   B 139 ? 0.131371  0.217851 0.161713 -0.00879359 -0.00598168 -0.00778177 139 SER   B C    
3478 O  O    . SER   B 139 ? 0.131867  0.23464  0.179004 0.00781959  -0.00910312 -0.0108567  139 SER   B O    
3479 C  CB   . SER   B 139 ? 0.142669  0.249177 0.163383 -0.0123457  -0.0133441  -0.00366248 139 SER   B CB   
3480 O  OG   . SER   B 139 ? 0.177824  0.272526 0.164688 -0.0184755  -0.0132765  0.010672    139 SER   B OG   
3481 N  N    . PHE   B 140 ? 0.126824  0.216571 0.158471 -0.012833   -0.00204634 -0.00835891 140 PHE   B N    
3482 C  CA   . PHE   B 140 ? 0.13716   0.206184 0.171551 -0.0178667  -0.0036537  -0.00656708 140 PHE   B CA   
3483 C  C    . PHE   B 140 ? 0.1471    0.216719 0.172789 -0.0274237  0.00949975  -0.00711448 140 PHE   B C    
3484 O  O    . PHE   B 140 ? 0.142165  0.216331 0.215963 -0.0230375  0.00010672  -0.00422297 140 PHE   B O    
3485 C  CB   . PHE   B 140 ? 0.144912  0.211099 0.176407 -0.0211108  -0.00632647 -0.00736168 140 PHE   B CB   
3486 C  CG   . PHE   B 140 ? 0.139566  0.209898 0.184657 -0.0216888  -0.00608914 -0.00951029 140 PHE   B CG   
3487 C  CD1  . PHE   B 140 ? 0.161965  0.210913 0.211622 -0.0205503  0.00770372  -0.0158032  140 PHE   B CD1  
3488 C  CD2  . PHE   B 140 ? 0.145542  0.226165 0.221849 -0.0166662  -0.0006839  0.0134033   140 PHE   B CD2  
3489 C  CE1  . PHE   B 140 ? 0.172046  0.235627 0.209322 -0.0279505  0.0102903   -0.0203714  140 PHE   B CE1  
3490 C  CE2  . PHE   B 140 ? 0.170219  0.231984 0.240357 -0.0222668  -0.00632865 0.0289893   140 PHE   B CE2  
3491 C  CZ   . PHE   B 140 ? 0.183404  0.240922 0.210396 -0.0332998  0.00566253  0.00839105  140 PHE   B CZ   
3492 N  N    . LEU   B 141 ? 0.17173   0.221609 0.182015 -0.041615   0.0157636   -0.00644071 141 LEU   B N    
3493 C  CA   . LEU   B 141 ? 0.18551   0.22483  0.184145 -0.0500627  0.021643    -0.00283431 141 LEU   B CA   
3494 C  C    . LEU   B 141 ? 0.19246   0.225391 0.186977 -0.0623949  0.0198529   -0.00375776 141 LEU   B C    
3495 O  O    . LEU   B 141 ? 0.187799  0.221011 0.180727 -0.0611278  0.0225396   -0.00429766 141 LEU   B O    
3496 C  CB   . LEU   B 141 ? 0.215153  0.233743 0.181914 -0.054136   0.0192809   -0.00480967 141 LEU   B CB   
3497 C  CG   . LEU   B 141 ? 0.254418  0.255805 0.18933  -0.0472009  0.0177647   -0.0067012  141 LEU   B CG   
3498 C  CD1  . LEU   B 141 ? 0.274718  0.266102 0.206799 -0.0471828  0.0152291   -0.00042148 141 LEU   B CD1  
3499 C  CD2  . LEU   B 141 ? 0.273702  0.270995 0.209932 -0.039239   0.0279743   -0.00468905 141 LEU   B CD2  
3500 N  N    . ASN   B 142 ? 0.197165  0.228156 0.198304 -0.0660137  0.0261762   -0.00600382 142 ASN   B N    
3501 C  CA   . ASN   B 142 ? 0.209568  0.232187 0.211292 -0.0713017  0.0138957   -0.0124433  142 ASN   B CA   
3502 C  C    . ASN   B 142 ? 0.209464  0.225938 0.1927   -0.0623006  0.00591456  -0.0116648  142 ASN   B C    
3503 O  O    . ASN   B 142 ? 0.227214  0.243242 0.190628 -0.0465019  0.00297166  -0.00972475 142 ASN   B O    
3504 C  CB   . ASN   B 142 ? 0.226102  0.253357 0.235036 -0.0902797  0.020672    -0.0125946  142 ASN   B CB   
3505 C  CG   . ASN   B 142 ? 0.269077  0.296229 0.262418 -0.101917   0.0135751   -0.0225992  142 ASN   B CG   
3506 O  OD1  . ASN   B 142 ? 0.289148  0.337084 0.273565 -0.124068   -0.00087287 -0.0235179  142 ASN   B OD1  
3507 N  ND2  . ASN   B 142 ? 0.349493  0.317611 0.306401 -0.0856457  0.0115835   -0.0117311  142 ASN   B ND2  
3508 N  N    . GLY   B 143 ? 0.202073  0.214408 0.192414 -0.050095   0.00958963  -0.0226151  143 GLY   B N    
3509 C  CA   . GLY   B 143 ? 0.205497  0.199351 0.189595 -0.0389955  0.0092251   -0.0243254  143 GLY   B CA   
3510 C  C    . GLY   B 143 ? 0.194134  0.187358 0.19035  -0.0283591  0.00952571  -0.0215269  143 GLY   B C    
3511 O  O    . GLY   B 143 ? 0.192326  0.198099 0.205419 -0.0193865  0.00735944  -0.0290865  143 GLY   B O    
3512 N  N    . SER   B 144 ? 0.172769  0.179421 0.178693 -0.0264355  0.00510019  -0.0163457  144 SER   B N    
3513 C  CA   . SER   B 144 ? 0.163611  0.176969 0.171728 -0.0244677  0.0022845   -0.0149067  144 SER   B CA   
3514 C  C    . SER   B 144 ? 0.158826  0.181588 0.164276 -0.0280333  0.00287994  -0.0206263  144 SER   B C    
3515 O  O    . SER   B 144 ? 0.13662   0.185107 0.156676 -0.0238681  -0.00176436 -0.0137808  144 SER   B O    
3516 C  CB   . SER   B 144 ? 0.168085  0.185391 0.171169 -0.0271983  0.00564618  -0.0176981  144 SER   B CB   
3517 O  OG   . SER   B 144 ? 0.16302   0.192541 0.174848 -0.0208575  0.014611    -0.0163527  144 SER   B OG   
3518 N  N    . CYS   B 145 ? 0.156676  0.192832 0.158633 -0.0254766  -0.00044153 -0.0160582  145 CYS   B N    
3519 C  CA   . CYS   B 145 ? 0.157915  0.192922 0.155974 -0.0246004  -0.00100435 -0.0162427  145 CYS   B CA   
3520 C  C    . CYS   B 145 ? 0.151336  0.174307 0.157335 -0.0238821  -0.00672546 -0.0188599  145 CYS   B C    
3521 O  O    . CYS   B 145 ? 0.163881  0.178565 0.176225 -0.0241805  -0.00315015 -0.014187   145 CYS   B O    
3522 C  CB   . CYS   B 145 ? 0.158548  0.215605 0.158109 -0.0299954  0.00348946  -0.0161437  145 CYS   B CB   
3523 S  SG   . CYS   B 145 ? 0.154035  0.263823 0.193839 -0.0295089  0.0059825   -0.016843   145 CYS   B SG   
3524 N  N    . GLY   B 146 ? 0.139884  0.169304 0.158679 -0.0137731  -0.00519034 -0.0153752  146 GLY   B N    
3525 C  CA   . GLY   B 146 ? 0.138102  0.181306 0.14728  -0.0141942  -0.00330303 -0.0184538  146 GLY   B CA   
3526 C  C    . GLY   B 146 ? 0.137884  0.186322 0.154567 -0.0131269  -0.00627303 -0.0173706  146 GLY   B C    
3527 O  O    . GLY   B 146 ? 0.132354  0.20867  0.16894  -0.0197443  -0.00603629 -0.0196937  146 GLY   B O    
3528 N  N    . SER   B 147 ? 0.130841  0.17442  0.154908 -0.0147655  -0.0138963  -0.00810775 147 SER   B N    
3529 C  CA   . SER   B 147 ? 0.125566  0.175508 0.154174 -0.0067169  -0.0238082  -0.0010059  147 SER   B CA   
3530 C  C    . SER   B 147 ? 0.125747  0.178743 0.155252 -0.00500917 -0.0192771  -0.00029779 147 SER   B C    
3531 O  O    . SER   B 147 ? 0.123271  0.179719 0.172591 -0.00601562 -0.0214174  0.00976601  147 SER   B O    
3532 C  CB   . SER   B 147 ? 0.128234  0.172205 0.156539 -0.00330018 -0.0250231  -0.00298271 147 SER   B CB   
3533 O  OG   . SER   B 147 ? 0.145088  0.181914 0.16432  -0.00243444 -0.0243151  0.00973619  147 SER   B OG   
3534 N  N    . VAL   B 148 ? 0.113589  0.1754   0.156857 -0.00145137 -0.0188256  0.00229879  148 VAL   B N    
3535 C  CA   . VAL   B 148 ? 0.117814  0.181355 0.161014 -0.00627751 -0.0164248  -0.00458164 148 VAL   B CA   
3536 C  C    . VAL   B 148 ? 0.118684  0.177743 0.157367 -0.00578561 -0.0229798  0.00165936  148 VAL   B C    
3537 O  O    . VAL   B 148 ? 0.139988  0.190171 0.155506 -0.00578291 -0.0265905  0.00554024  148 VAL   B O    
3538 C  CB   . VAL   B 148 ? 0.131359  0.206947 0.186711 -0.0070346  -0.00354434 -0.0191718  148 VAL   B CB   
3539 C  CG1  . VAL   B 148 ? 0.153459  0.220782 0.187603 -0.0114959  0.0044308   -0.0234361  148 VAL   B CG1  
3540 C  CG2  . VAL   B 148 ? 0.14964   0.230856 0.211302 0.0008063   -0.0132542  -0.021691   148 VAL   B CG2  
3541 N  N    . GLY   B 149 ? 0.124237  0.181705 0.155604 -0.00379597 -0.0294544  0.00218892  149 GLY   B N    
3542 C  CA   . GLY   B 149 ? 0.113907  0.180593 0.148501 -0.00460235 -0.0244342  -0.00145986 149 GLY   B CA   
3543 C  C    . GLY   B 149 ? 0.118927  0.184634 0.14647  -0.00545656 -0.0216348  -0.00156826 149 GLY   B C    
3544 O  O    . GLY   B 149 ? 0.11295   0.194705 0.151523 -0.00073151 -0.0217551  -0.00190467 149 GLY   B O    
3545 N  N    . PHE   B 150 ? 0.120845  0.190616 0.144257 -0.00922543 -0.018808   -0.0128566  150 PHE   B N    
3546 C  CA   . PHE   B 150 ? 0.121512  0.190699 0.157714 -0.00343742 -0.0158295  -0.00736558 150 PHE   B CA   
3547 C  C    . PHE   B 150 ? 0.117596  0.195153 0.160162 -0.00310238 -0.0210775  -0.00645545 150 PHE   B C    
3548 O  O    . PHE   B 150 ? 0.107861  0.202294 0.159755 -0.00880586 -0.0150768  -0.0182288  150 PHE   B O    
3549 C  CB   . PHE   B 150 ? 0.131408  0.192572 0.176306 0.00625259  -0.0121742  -0.0107284  150 PHE   B CB   
3550 C  CG   . PHE   B 150 ? 0.149795  0.210689 0.198282 0.0284145   -0.0170905  -0.0112204  150 PHE   B CG   
3551 C  CD1  . PHE   B 150 ? 0.17121   0.215556 0.210976 0.0456395   -0.0148082  4.79e-06    150 PHE   B CD1  
3552 C  CD2  . PHE   B 150 ? 0.159531  0.217279 0.206905 0.0346568   -0.0213812  -0.0140852  150 PHE   B CD2  
3553 C  CE1  . PHE   B 150 ? 0.195373  0.226686 0.22047  0.0495237   -0.0182167  0.00137182  150 PHE   B CE1  
3554 C  CE2  . PHE   B 150 ? 0.170492  0.236248 0.216819 0.0475304   -0.0271962  -0.0136741  150 PHE   B CE2  
3555 C  CZ   . PHE   B 150 ? 0.196433  0.232505 0.21464  0.0589407   -0.0299876  0.00300561  150 PHE   B CZ   
3556 N  N    . ASN   B 151 ? 0.121767  0.202636 0.161576 -0.0178565  -0.0189392  -0.00563234 151 ASN   B N    
3557 C  CA   . ASN   B 151 ? 0.131325  0.213597 0.175151 -0.0200324  -0.0166566  -0.0196722  151 ASN   B CA   
3558 C  C    . ASN   B 151 ? 0.136071  0.232654 0.183114 -0.0214434  -0.00198193 -0.0236212  151 ASN   B C    
3559 O  O    . ASN   B 151 ? 0.1314    0.255436 0.191174 -0.0131926  -0.0128122  -0.0278952  151 ASN   B O    
3560 C  CB   . ASN   B 151 ? 0.149429  0.220539 0.203956 -0.0148033  -0.0218103  -0.018353   151 ASN   B CB   
3561 C  CG   . ASN   B 151 ? 0.173176  0.243037 0.208734 -0.00164712 -0.014261   -0.020031   151 ASN   B CG   
3562 O  OD1  . ASN   B 151 ? 0.206391  0.341502 0.236963 0.0223975   -0.0148737  -0.0481529  151 ASN   B OD1  
3563 N  ND2  . ASN   B 151 ? 0.165627  0.25327  0.209203 0.00823674  -0.0149367  -0.0194583  151 ASN   B ND2  
3564 N  N    . ILE   B 152 ? 0.135262  0.263847 0.170713 -0.0274338  0.00860058  -0.0313874  152 ILE   B N    
3565 C  CA   . ILE   B 152 ? 0.169004  0.31395  0.198183 -0.0179285  0.0391974   -0.0359146  152 ILE   B CA   
3566 C  C    . ILE   B 152 ? 0.211481  0.340514 0.243629 -0.052133   0.0500572   -0.0643316  152 ILE   B C    
3567 O  O    . ILE   B 152 ? 0.230392  0.342936 0.269212 -0.0758061  0.0619541   -0.0827577  152 ILE   B O    
3568 C  CB   . ILE   B 152 ? 0.171815  0.358794 0.215898 0.00688293  0.0235812   -0.0315602  152 ILE   B CB   
3569 C  CG1  . ILE   B 152 ? 0.200013  0.361418 0.225293 0.03137     0.0186073   -0.00251312 152 ILE   B CG1  
3570 C  CG2  . ILE   B 152 ? 0.176443  0.385586 0.232714 0.0124763   0.0258665   -0.0344274  152 ILE   B CG2  
3571 C  CD1  . ILE   B 152 ? 0.240859  0.391434 0.249514 0.0436309   0.0127816   0.0128643   152 ILE   B CD1  
3572 N  N    . ASP   B 153 ? 0.293762  0.401099 0.272736 -0.0768993  0.0833711   -0.0741442  153 ASP   B N    
3573 C  CA   . ASP   B 153 ? 0.332909  0.452728 0.340919 -0.0996637  0.064364    -0.0713786  153 ASP   B CA   
3574 C  C    . ASP   B 153 ? 0.325134  0.535946 0.353    -0.121439   0.076569    -0.0970934  153 ASP   B C    
3575 O  O    . ASP   B 153 ? 0.367237  0.514152 0.404552 -0.163279   0.0850033   -0.137149   153 ASP   B O    
3576 C  CB   . ASP   B 153 ? 0.401265  0.469567 0.366591 -0.082023   0.0412332   -0.0420868  153 ASP   B CB   
3577 N  N    . TYR   B 154 ? 0.335348  0.620349 0.40349  -0.113867   0.0581878   -0.124175   154 TYR   B N    
3578 C  CA   . TYR   B 154 ? 0.353051  0.652401 0.430873 -0.0898799  0.0732298   -0.129006   154 TYR   B CA   
3579 C  C    . TYR   B 154 ? 0.336581  0.688934 0.457443 -0.088127   0.0430772   -0.132249   154 TYR   B C    
3580 O  O    . TYR   B 154 ? 0.306898  0.75897  0.448044 -0.0787041  0.091422    -0.139373   154 TYR   B O    
3581 C  CB   . TYR   B 154 ? 0.272537  0.667169 0.458386 -0.071565   0.0931083   -0.124148   154 TYR   B CB   
3582 N  N    . ASP   B 155 ? 0.317215  0.681376 0.464081 -0.0649992  0.025381    -0.145461   155 ASP   B N    
3583 C  CA   . ASP   B 155 ? 0.286838  0.673444 0.452766 -0.0290905  -0.00100601 -0.128737   155 ASP   B CA   
3584 C  C    . ASP   B 155 ? 0.259221  0.574962 0.425651 1.092e-05   -0.0181285  -0.121497   155 ASP   B C    
3585 O  O    . ASP   B 155 ? 0.28122   0.599573 0.424729 0.0894492   -0.0230241  -0.131647   155 ASP   B O    
3586 C  CB   . ASP   B 155 ? 0.294799  0.737806 0.497534 -0.0229564  0.0281567   -0.117134   155 ASP   B CB   
3587 C  CG   . ASP   B 155 ? 0.324917  0.795232 0.518088 -0.0220237  0.0658874   -0.102218   155 ASP   B CG   
3588 O  OD1  . ASP   B 155 ? 0.304197  0.808892 0.589281 -0.0483237  0.0755583   -0.091528   155 ASP   B OD1  
3589 O  OD2  . ASP   B 155 ? 0.391314  0.854203 0.55845  -0.017148   0.123928    -0.104785   155 ASP   B OD2  
3590 N  N    . CYS   B 156 ? 0.255598  0.468561 0.322984 -0.0314682  -0.0114428  -0.103162   156 CYS   B N    
3591 C  CA   . CYS   B 156 ? 0.209316  0.385658 0.265955 -0.0393387  0.028216    -0.077113   156 CYS   B CA   
3592 C  C    . CYS   B 156 ? 0.18245   0.334297 0.234349 -0.00929089 0.0103719   -0.0588304  156 CYS   B C    
3593 O  O    . CYS   B 156 ? 0.209988  0.326383 0.245403 -0.0243921  0.0179979   -0.0572816  156 CYS   B O    
3594 C  CB   . CYS   B 156 ? 0.274827  0.390959 0.306653 -0.0487416  0.0691225   -0.0619548  156 CYS   B CB   
3595 S  SG   . CYS   B 156 ? 0.343718  0.391718 0.314397 -0.0549653  0.0726165   -0.0134801  156 CYS   B SG   
3596 N  N    . VAL   B 157 ? 0.142166  0.299279 0.192594 0.00657659  0.00073415  -0.034177   157 VAL   B N    
3597 C  CA   . VAL   B 157 ? 0.133427  0.276041 0.185241 0.0142177   -0.0130025  -0.0208746  157 VAL   B CA   
3598 C  C    . VAL   B 157 ? 0.129216  0.254288 0.179305 0.0110811   -0.013118   -0.0187338  157 VAL   B C    
3599 O  O    . VAL   B 157 ? 0.157017  0.276203 0.194502 0.02623     -0.0130933  -0.0334993  157 VAL   B O    
3600 C  CB   . VAL   B 157 ? 0.161545  0.275132 0.193579 0.028265    -0.0201628  -0.0154299  157 VAL   B CB   
3601 C  CG1  . VAL   B 157 ? 0.170756  0.269271 0.192424 0.0300445   -0.017214   -0.0134185  157 VAL   B CG1  
3602 C  CG2  . VAL   B 157 ? 0.165367  0.287989 0.206538 0.0419511   -0.0113855  -0.00942309 157 VAL   B CG2  
3603 N  N    . SER   B 158 ? 0.120895  0.230893 0.172248 -0.00206108 -0.017603   -0.0131725  158 SER   B N    
3604 C  CA   . SER   B 158 ? 0.125807  0.231279 0.171963 -0.00661555 -0.017375   -0.00603587 158 SER   B CA   
3605 C  C    . SER   B 158 ? 0.115781  0.221248 0.162022 -0.00426834 -0.0190054  -0.011701   158 SER   B C    
3606 O  O    . SER   B 158 ? 0.138938  0.232642 0.166841 -0.0143111  -0.00418674 -0.0215749  158 SER   B O    
3607 C  CB   . SER   B 158 ? 0.144579  0.238569 0.199473 -0.0128637  -0.009596   -0.00714579 158 SER   B CB   
3608 O  OG   . SER   B 158 ? 0.171075  0.278115 0.250862 -0.0265635  -0.00200863 0.00605823  158 SER   B OG   
3609 N  N    . PHE   B 159 ? 0.124386  0.205252 0.158411 -0.0047562  -0.00673085 -0.0129708  159 PHE   B N    
3610 C  CA   . PHE   B 159 ? 0.123636  0.198352 0.169136 0.00209989  -0.011323   0.00097019  159 PHE   B CA   
3611 C  C    . PHE   B 159 ? 0.111876  0.202051 0.16421  -0.00124844 -0.0120128  0.00719266  159 PHE   B C    
3612 O  O    . PHE   B 159 ? 0.118008  0.218053 0.174876 0.00687005  0.00081235  0.0200167   159 PHE   B O    
3613 C  CB   . PHE   B 159 ? 0.117257  0.203448 0.163837 0.00275843  -0.0170594  -0.00678697 159 PHE   B CB   
3614 C  CG   . PHE   B 159 ? 0.124663  0.198261 0.168574 0.00362696  -0.0177408  -0.00657902 159 PHE   B CG   
3615 C  CD1  . PHE   B 159 ? 0.131621  0.205335 0.168387 0.00807906  -0.00969678 -0.00785682 159 PHE   B CD1  
3616 C  CD2  . PHE   B 159 ? 0.138487  0.206127 0.172399 0.0139792   -0.0105675  -0.00175892 159 PHE   B CD2  
3617 C  CE1  . PHE   B 159 ? 0.14709   0.209914 0.177391 0.0103268   -0.0135801  -0.00240267 159 PHE   B CE1  
3618 C  CE2  . PHE   B 159 ? 0.142563  0.205715 0.187258 0.0129717   -0.0150672  -0.0058051  159 PHE   B CE2  
3619 C  CZ   . PHE   B 159 ? 0.147216  0.211968 0.182045 0.0118694   -0.0150744  -0.0107243  159 PHE   B CZ   
3620 N  N    . CYS   B 160 ? 0.107307  0.185407 0.158104 0.00384533  -0.0128516  0.00961027  160 CYS   B N    
3621 C  CA   . CYS   B 160 ? 0.111307  0.18749  0.174191 0.00359792  -0.0100536  0.0114788   160 CYS   B CA   
3622 C  C    . CYS   B 160 ? 0.110046  0.18407  0.17406  -0.00050621 -0.0144629  0.00987492  160 CYS   B C    
3623 O  O    . CYS   B 160 ? 0.0923013 0.200628 0.205727 0.00393721  -0.00672954 0.016564    160 CYS   B O    
3624 C  CB   . CYS   B 160 ? 0.121425  0.196151 0.190566 -0.00100384 -0.0183487  0.00474218  160 CYS   B CB   
3625 S  SG   . CYS   B 160 ? 0.154064  0.210057 0.18911  0.00287768  -0.0228688  -0.0121671  160 CYS   B SG   
3626 N  N    . TYR   B 161 ? 0.101724  0.17731  0.156406 -0.00330894 -0.0141473  0.00050162  161 TYR   B N    
3627 C  CA   . TYR   B 161 ? 0.108711  0.179905 0.148457 -0.00354069 -0.0126432  0.00064401  161 TYR   B CA   
3628 C  C    . TYR   B 161 ? 0.115369  0.177049 0.141411 -0.0062444  -0.0134571  0.00045251  161 TYR   B C    
3629 O  O    . TYR   B 161 ? 0.114756  0.17894  0.154328 -0.00852838 -0.0223274  0.00586983  161 TYR   B O    
3630 C  CB   . TYR   B 161 ? 0.117571  0.177451 0.143319 -0.00761759 -0.0155012  -0.00279363 161 TYR   B CB   
3631 C  CG   . TYR   B 161 ? 0.1202    0.187427 0.146906 -0.0046171  -0.013843   -0.00238161 161 TYR   B CG   
3632 C  CD1  . TYR   B 161 ? 0.124492  0.192918 0.144294 -3.472e-05  -0.0122719  -0.00040379 161 TYR   B CD1  
3633 C  CD2  . TYR   B 161 ? 0.122598  0.183907 0.139366 -0.00909293 -0.0154865  -0.00475834 161 TYR   B CD2  
3634 C  CE1  . TYR   B 161 ? 0.131665  0.198288 0.14985  -0.00303195 -0.0036602  -0.00947011 161 TYR   B CE1  
3635 C  CE2  . TYR   B 161 ? 0.129311  0.188557 0.143059 -0.0103654  -0.00982391 -0.00473729 161 TYR   B CE2  
3636 C  CZ   . TYR   B 161 ? 0.128833  0.196509 0.14879  -0.00890806 -0.00733559 -0.00997343 161 TYR   B CZ   
3637 O  OH   . TYR   B 161 ? 0.131905  0.2105   0.167214 -0.0158959  0.0018572   -0.00739034 161 TYR   B OH   
3638 N  N    . MET   B 162 ? 0.11484   0.177675 0.145823 -0.00409598 -0.0144804  -0.00597286 162 MET   B N    
3639 C  CA   A MET   B 162 ? 0.123048  0.182886 0.154376 -0.00580134 -0.00799446 -0.00820647 162 MET   B CA   
3640 C  CA   B MET   B 162 ? 0.108378  0.174048 0.13804  0.00163565  -0.0164428  -0.0111736  162 MET   B CA   
3641 C  C    . MET   B 162 ? 0.116163  0.172948 0.144341 -0.00168809 -0.0120044  -0.00867384 162 MET   B C    
3642 O  O    . MET   B 162 ? 0.108307  0.184601 0.147613 0.00365302  -0.0195611  -0.0049488  162 MET   B O    
3643 C  CB   A MET   B 162 ? 0.152384  0.203322 0.172027 -0.00899021 0.00586163  -0.0191387  162 MET   B CB   
3644 C  CB   B MET   B 162 ? 0.102151  0.173614 0.139691 0.00708545  -0.016002   -0.0161895  162 MET   B CB   
3645 C  CG   A MET   B 162 ? 0.172123  0.215661 0.202086 -0.0188952  0.0179156   -0.0235309  162 MET   B CG   
3646 C  CG   B MET   B 162 ? 0.0913108 0.171444 0.133006 0.00984002  -0.017083   -0.0225191  162 MET   B CG   
3647 S  SD   A MET   B 162 ? 0.236795  0.257383 0.234602 -0.0346667  0.0432908   -0.0540253  162 MET   B SD   
3648 S  SD   B MET   B 162 ? 0.0755155 0.169857 0.126692 0.0160432   -0.0265502  -0.0260281  162 MET   B SD   
3649 C  CE   A MET   B 162 ? 0.22399   0.259861 0.236697 -0.0211749  0.0365237   -0.0503692  162 MET   B CE   
3650 C  CE   B MET   B 162 ? 0.0725925 0.173137 0.126813 0.0130064   -0.0238626  -0.0360113  162 MET   B CE   
3651 N  N    . HIS   B 163 ? 0.108872  0.175659 0.141304 -0.00121747 -0.00951082 -0.00294177 163 HIS   B N    
3652 C  CA   . HIS   B 163 ? 0.110795  0.173332 0.142063 -0.00501727 -0.00718528 -0.00878257 163 HIS   B CA   
3653 C  C    . HIS   B 163 ? 0.124408  0.174526 0.149412 -0.00797701 -0.00704409 -0.0143507  163 HIS   B C    
3654 O  O    . HIS   B 163 ? 0.146622  0.168808 0.160417 -0.00861047 -0.0215626  -0.0174807  163 HIS   B O    
3655 C  CB   . HIS   B 163 ? 0.118203  0.183708 0.141172 -0.00825788 -0.00877875 -0.00944935 163 HIS   B CB   
3656 C  CG   . HIS   B 163 ? 0.125752  0.19102  0.148709 -0.0124506  -0.00669807 -0.0101587  163 HIS   B CG   
3657 N  ND1  . HIS   B 163 ? 0.133492  0.192255 0.147795 -0.0158975  -0.00568464 -0.0141434  163 HIS   B ND1  
3658 C  CD2  . HIS   B 163 ? 0.131254  0.185899 0.14872  -0.00925114 -0.00416179 -0.0134122  163 HIS   B CD2  
3659 C  CE1  . HIS   B 163 ? 0.130705  0.200785 0.147085 -0.00897192 0.00075279  -0.0162186  163 HIS   B CE1  
3660 N  NE2  . HIS   B 163 ? 0.13365   0.201779 0.150579 -0.00963244 -0.00729298 -0.0169452  163 HIS   B NE2  
3661 N  N    . HIS   B 164 ? 0.116017  0.182661 0.150005 -0.0126409  -0.0135169  -0.0185599  164 HIS   B N    
3662 C  CA   . HIS   B 164 ? 0.118136  0.1986   0.151783 -0.0250698  -0.00523142 -0.0216569  164 HIS   B CA   
3663 C  C    . HIS   B 164 ? 0.12463   0.21587  0.156016 -0.0309785  -0.00266626 -0.0206043  164 HIS   B C    
3664 O  O    . HIS   B 164 ? 0.157852  0.226235 0.178184 -0.0473857  0.00587513  -0.0129788  164 HIS   B O    
3665 C  CB   . HIS   B 164 ? 0.113905  0.208736 0.146007 -0.0220668  -0.0130007  -0.0294049  164 HIS   B CB   
3666 C  CG   . HIS   B 164 ? 0.123636  0.214408 0.145535 -0.0175697  -0.0117307  -0.031867   164 HIS   B CG   
3667 N  ND1  . HIS   B 164 ? 0.128952  0.215803 0.145182 -0.0123528  -0.0109546  -0.0315776  164 HIS   B ND1  
3668 C  CD2  . HIS   B 164 ? 0.128154  0.218543 0.145274 -0.0156809  -0.0154183  -0.0294517  164 HIS   B CD2  
3669 C  CE1  . HIS   B 164 ? 0.128087  0.212827 0.143075 -0.0103723  -0.00866613 -0.030621   164 HIS   B CE1  
3670 N  NE2  . HIS   B 164 ? 0.147339  0.218836 0.138246 -0.0146159  -0.0161199  -0.0320834  164 HIS   B NE2  
3671 N  N    . MET   B 165 ? 0.127459  0.220821 0.164528 -0.0320126  -2.362e-05  -0.0214906  165 MET   B N    
3672 C  CA   . MET   B 165 ? 0.12565   0.236811 0.165729 -0.0303397  0.00337895  -0.0266352  165 MET   B CA   
3673 C  C    . MET   B 165 ? 0.125711  0.227867 0.175114 -0.0321018  0.0112922   -0.0261362  165 MET   B C    
3674 O  O    . MET   B 165 ? 0.118613  0.22132  0.181533 -0.0322485  0.00605356  -0.0253839  165 MET   B O    
3675 C  CB   . MET   B 165 ? 0.15096   0.27924  0.180837 -0.0178959  -0.00456765 -0.0211842  165 MET   B CB   
3676 C  CG   . MET   B 165 ? 0.167773  0.293053 0.197578 -0.0118963  -0.0195734  -0.0207225  165 MET   B CG   
3677 S  SD   . MET   B 165 ? 0.198349  0.309688 0.266155 -0.018024   -0.00238319 -0.0094922  165 MET   B SD   
3678 C  CE   . MET   B 165 ? 0.156451  0.336371 0.237836 -0.0159926  -0.0570584  -0.0418993  165 MET   B CE   
3679 N  N    . GLU   B 166 ? 0.141619  0.23787  0.173421 -0.0399793  0.0126114   -0.0211043  166 GLU   B N    
3680 C  CA   . GLU   B 166 ? 0.130346  0.242336 0.180237 -0.0330919  0.00340562  -0.0248777  166 GLU   B CA   
3681 C  C    . GLU   B 166 ? 0.125742  0.270784 0.189233 -0.0345829  0.00178907  -0.0151287  166 GLU   B C    
3682 O  O    . GLU   B 166 ? 0.12929   0.297259 0.217686 -0.0394009  -0.00047817 -0.0269837  166 GLU   B O    
3683 C  CB   . GLU   B 166 ? 0.12349   0.241039 0.177921 -0.0419059  0.00855268  -0.0247285  166 GLU   B CB   
3684 C  CG   . GLU   B 166 ? 0.132576  0.2491   0.18021  -0.0359598  0.00673945  -0.024734   166 GLU   B CG   
3685 C  CD   . GLU   B 166 ? 0.145167  0.2701   0.181239 -0.0321364  0.00842737  -0.0164004  166 GLU   B CD   
3686 O  OE1  . GLU   B 166 ? 0.17731   0.312703 0.217206 -0.0353604  0.0352337   0.0185923   166 GLU   B OE1  
3687 O  OE2  . GLU   B 166 ? 0.138576  0.259498 0.186516 -0.0365211  0.00376104  -0.00818114 166 GLU   B OE2  
3688 N  N    . LEU   B 167 ? 0.110968  0.272852 0.203595 -0.0263458  -0.0105764  -0.00291543 167 LEU   B N    
3689 C  CA   . LEU   B 167 ? 0.118301  0.308764 0.222603 -0.0150413  -0.011499   0.00974037  167 LEU   B CA   
3690 C  C    . LEU   B 167 ? 0.13282   0.352367 0.235591 -0.0111661  -0.00619378 0.0253757   167 LEU   B C    
3691 O  O    . LEU   B 167 ? 0.131547  0.345593 0.21169  -0.00407616 0.0051383   0.0202808   167 LEU   B O    
3692 C  CB   . LEU   B 167 ? 0.121557  0.312995 0.234334 -0.0145818  -0.021423   0.0195244   167 LEU   B CB   
3693 C  CG   . LEU   B 167 ? 0.141167  0.334666 0.250775 -0.0269344  -0.0228291  0.0243714   167 LEU   B CG   
3694 C  CD1  . LEU   B 167 ? 0.17997   0.333044 0.254544 -0.0157167  -0.0303609  0.0248932   167 LEU   B CD1  
3695 C  CD2  . LEU   B 167 ? 0.188293  0.361146 0.260401 -0.0459527  -0.0333124  0.0286465   167 LEU   B CD2  
3696 N  N    . PRO   B 168 ? 0.132571  0.40381  0.259981 -0.0114852  0.00587897  0.0466499   168 PRO   B N    
3697 C  CA   . PRO   B 168 ? 0.141143  0.425753 0.277783 -0.0103844  0.0236795   0.0586858   168 PRO   B CA   
3698 C  C    . PRO   B 168 ? 0.141364  0.434682 0.281635 -0.00109984 0.0341568   0.0560524   168 PRO   B C    
3699 O  O    . PRO   B 168 ? 0.201084  0.475359 0.297511 -0.00446091 0.0447046   0.0863507   168 PRO   B O    
3700 C  CB   . PRO   B 168 ? 0.140976  0.444897 0.302958 -0.00893673 0.0162959   0.0555269   168 PRO   B CB   
3701 C  CG   . PRO   B 168 ? 0.14919   0.44918  0.310818 -0.0122022  0.00059372  0.0548759   168 PRO   B CG   
3702 C  CD   . PRO   B 168 ? 0.149144  0.431983 0.280222 -0.0172264  -0.00200527 0.0561626   168 PRO   B CD   
3703 N  N    . THR   B 169 ? 0.144187  0.408883 0.277577 0.0112751   0.0414475   0.0462767   169 THR   B N    
3704 C  CA   . THR   B 169 ? 0.176697  0.400176 0.258657 0.0318619   0.0533662   0.0357251   169 THR   B CA   
3705 C  C    . THR   B 169 ? 0.192459  0.3587   0.213409 0.0253997   0.0357865   0.0152955   169 THR   B C    
3706 O  O    . THR   B 169 ? 0.264582  0.387349 0.214639 0.0447494   0.033283    -0.0128278  169 THR   B O    
3707 C  CB   . THR   B 169 ? 0.197819  0.421725 0.305971 0.0553167   0.0454837   0.0384234   169 THR   B CB   
3708 O  OG1  . THR   B 169 ? 0.187453  0.428533 0.308846 0.0526447   0.0384383   0.065349    169 THR   B OG1  
3709 C  CG2  . THR   B 169 ? 0.217725  0.437184 0.350657 0.0713936   0.0455256   0.0431682   169 THR   B CG2  
3710 N  N    . GLY   B 170 ? 0.166041  0.311409 0.185691 0.013561    0.0156801   0.0146807   170 GLY   B N    
3711 C  CA   . GLY   B 170 ? 0.159011  0.294042 0.175972 0.00665222  0.0209737   0.0199968   170 GLY   B CA   
3712 C  C    . GLY   B 170 ? 0.153585  0.274472 0.184845 0.00735092  0.0108875   0.0147696   170 GLY   B C    
3713 O  O    . GLY   B 170 ? 0.157295  0.325445 0.244283 0.00872264  -0.00383122 0.0490157   170 GLY   B O    
3714 N  N    . VAL   B 171 ? 0.133477  0.264327 0.165049 0.0164677   0.0159792   0.00716634  171 VAL   B N    
3715 C  CA   . VAL   B 171 ? 0.145177  0.248497 0.16072  0.00448284  0.0125309   -0.00158748 171 VAL   B CA   
3716 C  C    . VAL   B 171 ? 0.129491  0.219414 0.160882 -0.00609324 0.00492717  -0.0121214  171 VAL   B C    
3717 O  O    . VAL   B 171 ? 0.125261  0.2341   0.190664 -0.0178514  0.0139925   -0.0103767  171 VAL   B O    
3718 C  CB   . VAL   B 171 ? 0.161756  0.249253 0.165986 0.0094392   0.0148662   -0.00945555 171 VAL   B CB   
3719 C  CG1  . VAL   B 171 ? 0.189631  0.255666 0.180369 0.0159878   0.0181695   -0.0225614  171 VAL   B CG1  
3720 C  CG2  . VAL   B 171 ? 0.15769   0.250967 0.170655 0.0124843   0.0184519   0.00614907  171 VAL   B CG2  
3721 N  N    . HIS   B 172 ? 0.13646   0.211939 0.150217 -0.00923816 0.0104263   -0.0145103  172 HIS   B N    
3722 C  CA   . HIS   B 172 ? 0.140067  0.195297 0.161988 -0.0146334  0.00729503  -0.0244362  172 HIS   B CA   
3723 C  C    . HIS   B 172 ? 0.136088  0.19581  0.167921 -0.0145056  0.00654913  -0.0239576  172 HIS   B C    
3724 O  O    . HIS   B 172 ? 0.168947  0.200453 0.172472 -0.0141409  0.00827319  -0.0260272  172 HIS   B O    
3725 C  CB   . HIS   B 172 ? 0.135424  0.195529 0.17735  -0.00548248 0.0212429   -0.0186521  172 HIS   B CB   
3726 C  CG   . HIS   B 172 ? 0.13825   0.206581 0.185566 -0.00321774 0.0183749   -0.00809799 172 HIS   B CG   
3727 N  ND1  . HIS   B 172 ? 0.14096   0.203759 0.180922 -0.0100577  0.01787     -0.00020023 172 HIS   B ND1  
3728 C  CD2  . HIS   B 172 ? 0.142062  0.217705 0.193366 -0.00688431 0.0135795   -0.00279354 172 HIS   B CD2  
3729 C  CE1  . HIS   B 172 ? 0.154608  0.21154  0.179489 -0.011726   0.0139549   0.00146584  172 HIS   B CE1  
3730 N  NE2  . HIS   B 172 ? 0.149472  0.223958 0.183263 -0.0085762  0.0157114   -0.00296413 172 HIS   B NE2  
3731 N  N    . ALA   B 173 ? 0.138458  0.196143 0.16566  -0.0178707  0.00752562  -0.0247243  173 ALA   B N    
3732 C  CA   . ALA   B 173 ? 0.135724  0.200594 0.166486 -0.0110346  0.00700874  -0.023785   173 ALA   B CA   
3733 C  C    . ALA   B 173 ? 0.123222  0.20003  0.159348 -0.00933111 0.00195335  -0.0162151  173 ALA   B C    
3734 O  O    . ALA   B 173 ? 0.123973  0.198389 0.157153 -0.0113368  0.00472691  -0.0183962  173 ALA   B O    
3735 C  CB   . ALA   B 173 ? 0.13799   0.218547 0.173121 -0.00871387 0.011663    -0.0243212  173 ALA   B CB   
3736 N  N    . GLY   B 174 ? 0.109566  0.192995 0.148734 0.00079304  -0.00510678 -0.0103585  174 GLY   B N    
3737 C  CA   . GLY   B 174 ? 0.111782  0.189973 0.151059 -0.00035066 -0.00512041 -0.0155008  174 GLY   B CA   
3738 C  C    . GLY   B 174 ? 0.10965   0.181869 0.147634 -0.00233806 -0.00977249 -0.0128427  174 GLY   B C    
3739 O  O    . GLY   B 174 ? 0.117403  0.197283 0.155743 0.00932058  -0.00255414 -0.0126112  174 GLY   B O    
3740 N  N    . THR   B 175 ? 0.110756  0.179493 0.146982 0.00205297  -0.0129642  -0.0113837  175 THR   B N    
3741 C  CA   . THR   B 175 ? 0.112088  0.189947 0.148115 0.00353703  -0.013132   -0.00634426 175 THR   B CA   
3742 C  C    . THR   B 175 ? 0.10805   0.187398 0.138431 0.00753429  -0.0105891  -0.00073718 175 THR   B C    
3743 O  O    . THR   B 175 ? 0.120569  0.201171 0.142156 -0.00106292 -0.0182906  0.00722328  175 THR   B O    
3744 C  CB   . THR   B 175 ? 0.107693  0.196257 0.150516 0.00017643  -0.0109937  -0.00753682 175 THR   B CB   
3745 O  OG1  . THR   B 175 ? 0.117672  0.198176 0.151902 0.00448927  -0.0181067  -0.00756595 175 THR   B OG1  
3746 C  CG2  . THR   B 175 ? 0.111891  0.206787 0.171279 -0.00370786 -0.0141074  -0.0135171  175 THR   B CG2  
3747 N  N    . ASP   B 176 ? 0.0957097 0.190037 0.144447 0.0130978   -0.010522   0.00380119  176 ASP   B N    
3748 C  CA   . ASP   B 176 ? 0.100724  0.198263 0.157813 0.00434527  -0.00708857 0.00132996  176 ASP   B CA   
3749 C  C    . ASP   B 176 ? 0.116953  0.204286 0.147967 0.00374855  -0.0103869  -0.00346785 176 ASP   B C    
3750 O  O    . ASP   B 176 ? 0.124981  0.21036  0.153714 0.00081763  -0.00063647 -0.0101197  176 ASP   B O    
3751 C  CB   . ASP   B 176 ? 0.113331  0.20609  0.17478  0.0025386   0.00373695  0.0057103   176 ASP   B CB   
3752 C  CG   . ASP   B 176 ? 0.130206  0.213802 0.181722 0.00365057  0.00399852  0.00985958  176 ASP   B CG   
3753 O  OD1  . ASP   B 176 ? 0.149206  0.223795 0.173844 0.00582924  -0.00376088 0.00758349  176 ASP   B OD1  
3754 O  OD2  . ASP   B 176 ? 0.152974  0.224662 0.204452 0.0057124   -0.00256893 0.017925    176 ASP   B OD2  
3755 N  N    . LEU   B 177 ? 0.114266  0.211719 0.148748 0.00739978  -0.0146614  -0.00891839 177 LEU   B N    
3756 C  CA   . LEU   B 177 ? 0.119899  0.228021 0.162562 0.019368    -0.0162101  -0.01428    177 LEU   B CA   
3757 C  C    . LEU   B 177 ? 0.126238  0.246417 0.166173 0.0267099   -0.0145806  -0.0209505  177 LEU   B C    
3758 O  O    . LEU   B 177 ? 0.165559  0.261002 0.183506 0.0393276   -0.0256162  -0.037821   177 LEU   B O    
3759 C  CB   . LEU   B 177 ? 0.118145  0.232231 0.166696 0.0242599   -0.0160164  -0.0116469  177 LEU   B CB   
3760 C  CG   . LEU   B 177 ? 0.123075  0.25726  0.177299 0.0229006   -0.0272232  -0.00519779 177 LEU   B CG   
3761 C  CD1  . LEU   B 177 ? 0.140636  0.267854 0.212341 0.0258272   -0.0258742  0.00360799  177 LEU   B CD1  
3762 C  CD2  . LEU   B 177 ? 0.12733   0.273703 0.186953 0.0205474   -0.0175711  -0.0046421  177 LEU   B CD2  
3763 N  N    . GLU   B 178 ? 0.137712  0.255175 0.146977 0.0340193   -0.0142414  -0.0163214  178 GLU   B N    
3764 C  CA   . GLU   B 178 ? 0.155936  0.293264 0.15396  0.0280605   -0.0148386  -0.0155562  178 GLU   B CA   
3765 C  C    . GLU   B 178 ? 0.15042   0.286709 0.153231 0.0344416   -0.0197065  -0.0255057  178 GLU   B C    
3766 O  O    . GLU   B 178 ? 0.170437  0.329744 0.1557   0.0345034   -0.0237989  -0.040288   178 GLU   B O    
3767 C  CB   . GLU   B 178 ? 0.186534  0.324716 0.181486 0.0327425   -0.00944186 0.00420518  178 GLU   B CB   
3768 C  CG   . GLU   B 178 ? 0.212074  0.375769 0.234526 0.0293769   -0.00039247 0.00821686  178 GLU   B CG   
3769 C  CD   . GLU   B 178 ? 0.291887  0.41536  0.294436 0.0296207   0.00011172  0.0288324   178 GLU   B CD   
3770 O  OE1  . GLU   B 178 ? 0.350321  0.440765 0.351895 0.0467829   0.019641    0.0306981   178 GLU   B OE1  
3771 O  OE2  . GLU   B 178 ? 0.334449  0.511262 0.360224 0.0145396   0.025977    0.0259509   178 GLU   B OE2  
3772 N  N    . GLY   B 179 ? 0.146737  0.269098 0.150988 0.0261528   -0.0274329  -0.0282602  179 GLY   B N    
3773 C  CA   . GLY   B 179 ? 0.152632  0.255926 0.159122 0.0259124   -0.0212328  -0.0351055  179 GLY   B CA   
3774 C  C    . GLY   B 179 ? 0.13375   0.247421 0.155718 0.0168643   -0.0202065  -0.0309034  179 GLY   B C    
3775 O  O    . GLY   B 179 ? 0.136001  0.267356 0.158496 0.00931341  -0.0251193  -0.0277197  179 GLY   B O    
3776 N  N    . ASN   B 180 ? 0.116972  0.242445 0.146875 0.0269413   -0.0197554  -0.0260909  180 ASN   B N    
3777 C  CA   . ASN   B 180 ? 0.126522  0.246105 0.150999 0.0298472   -0.0232983  -0.0233158  180 ASN   B CA   
3778 C  C    . ASN   B 180 ? 0.112389  0.240791 0.15033  0.0193523   -0.0174491  -0.010391   180 ASN   B C    
3779 O  O    . ASN   B 180 ? 0.114956  0.234507 0.144267 0.0182173   -0.022963   -0.00500513 180 ASN   B O    
3780 C  CB   . ASN   B 180 ? 0.134466  0.26729  0.16162  0.0306167   -0.0220895  -0.0140574  180 ASN   B CB   
3781 C  CG   . ASN   B 180 ? 0.173108  0.30976  0.175922 0.0283921   -0.0146132  -0.0134289  180 ASN   B CG   
3782 O  OD1  . ASN   B 180 ? 0.212557  0.370487 0.177245 0.0197909   -0.0321962  -0.011325   180 ASN   B OD1  
3783 N  ND2  . ASN   B 180 ? 0.172667  0.345188 0.191421 0.0302559   -0.00703002 -0.0105915  180 ASN   B ND2  
3784 N  N    . PHE   B 181 ? 0.111928  0.241783 0.162826 0.0155151   -0.013652   -0.0191371  181 PHE   B N    
3785 C  CA   . PHE   B 181 ? 0.105634  0.237621 0.166122 0.0134643   -0.0122049  -0.0158996  181 PHE   B CA   
3786 C  C    . PHE   B 181 ? 0.106462  0.229237 0.164442 0.0172532   -0.0118337  -0.00940284 181 PHE   B C    
3787 O  O    . PHE   B 181 ? 0.130584  0.228137 0.161143 0.0232123   -0.00964755 -0.0134938  181 PHE   B O    
3788 C  CB   . PHE   B 181 ? 0.108815  0.251759 0.175467 0.0101751   -0.00826436 -0.0211119  181 PHE   B CB   
3789 C  CG   . PHE   B 181 ? 0.109615  0.250472 0.183654 -0.0013905  -0.0159868  -0.0272263  181 PHE   B CG   
3790 C  CD1  . PHE   B 181 ? 0.11388   0.261753 0.185291 -0.00584575 -0.0195234  -0.0320519  181 PHE   B CD1  
3791 C  CD2  . PHE   B 181 ? 0.120373  0.254334 0.180109 -0.00954525 -0.0229478  -0.0257385  181 PHE   B CD2  
3792 C  CE1  . PHE   B 181 ? 0.11851   0.265822 0.185316 -0.00964838 -0.0192798  -0.0269891  181 PHE   B CE1  
3793 C  CE2  . PHE   B 181 ? 0.139433  0.262027 0.185786 -0.0138583  -0.0300643  -0.0273298  181 PHE   B CE2  
3794 C  CZ   . PHE   B 181 ? 0.134303  0.266103 0.186714 -0.0107609  -0.0194701  -0.0257915  181 PHE   B CZ   
3795 N  N    . TYR   B 182 ? 0.104783  0.213948 0.162017 0.0212676   -0.0170931  -0.0022392  182 TYR   B N    
3796 C  CA   . TYR   B 182 ? 0.114363  0.217069 0.158604 0.0190035   -0.0157133  -0.0020656  182 TYR   B CA   
3797 C  C    . TYR   B 182 ? 0.115308  0.224263 0.163897 0.0121068   -0.0140308  -0.0104399  182 TYR   B C    
3798 O  O    . TYR   B 182 ? 0.140217  0.229443 0.177579 0.0206301   -0.00550256 -0.0033818  182 TYR   B O    
3799 C  CB   . TYR   B 182 ? 0.113088  0.215185 0.159884 0.0166868   -0.0127082  -0.00341066 182 TYR   B CB   
3800 C  CG   . TYR   B 182 ? 0.110869  0.204406 0.158203 0.0112621   -0.012075   -0.00079905 182 TYR   B CG   
3801 C  CD1  . TYR   B 182 ? 0.116836  0.19595  0.17006  0.0175558   -0.0081906  0.00098111  182 TYR   B CD1  
3802 C  CD2  . TYR   B 182 ? 0.106194  0.198722 0.152675 0.0116341   -0.0159252  -0.00099893 182 TYR   B CD2  
3803 C  CE1  . TYR   B 182 ? 0.113516  0.199566 0.178307 0.0151494   -0.00961735 0.00714529  182 TYR   B CE1  
3804 C  CE2  . TYR   B 182 ? 0.108639  0.205298 0.166179 0.0106254   -0.00838479 0.00681084  182 TYR   B CE2  
3805 C  CZ   . TYR   B 182 ? 0.103933  0.197016 0.170968 0.01617     -0.00653193 0.00715386  182 TYR   B CZ   
3806 O  OH   . TYR   B 182 ? 0.104232  0.207947 0.189947 0.00221687  0.00431133  0.0101344   182 TYR   B OH   
3807 N  N    . GLY   B 183 ? 0.10745   0.235735 0.163556 0.0186214   -0.0118089  -0.0173447  183 GLY   B N    
3808 C  CA   . GLY   B 183 ? 0.107403  0.25286  0.176742 0.0223149   -0.0176698  -0.0297383  183 GLY   B CA   
3809 C  C    . GLY   B 183 ? 0.119627  0.260967 0.185945 0.0259903   -0.0211927  -0.0366313  183 GLY   B C    
3810 O  O    . GLY   B 183 ? 0.116843  0.269217 0.185098 0.0203747   -0.0238576  -0.0435952  183 GLY   B O    
3811 N  N    . PRO   B 184 ? 0.105129  0.278002 0.195542 0.0277944   -0.0293521  -0.0298003  184 PRO   B N    
3812 C  CA   . PRO   B 184 ? 0.106206  0.291229 0.205853 0.0257814   -0.0313532  -0.0239412  184 PRO   B CA   
3813 C  C    . PRO   B 184 ? 0.117012  0.281306 0.222104 0.0272804   -0.0285309  -0.0242296  184 PRO   B C    
3814 O  O    . PRO   B 184 ? 0.121098  0.312728 0.3199   0.0254392   -0.0248539  -0.0203965  184 PRO   B O    
3815 C  CB   . PRO   B 184 ? 0.1062    0.299763 0.236277 0.0296426   -0.0278575  -0.0222588  184 PRO   B CB   
3816 C  CG   . PRO   B 184 ? 0.111068  0.301441 0.230978 0.0294592   -0.00715853 -0.0250471  184 PRO   B CG   
3817 C  CD   . PRO   B 184 ? 0.114973  0.292672 0.206367 0.0331566   -0.0178959  -0.0267901  184 PRO   B CD   
3818 N  N    . PHE   B 185 ? 0.109331  0.274941 0.186305 0.0284033   -0.0200046  -0.0228685  185 PHE   B N    
3819 C  CA   . PHE   B 185 ? 0.1171    0.26983  0.186361 0.0204753   -0.0165416  -0.0168682  185 PHE   B CA   
3820 C  C    . PHE   B 185 ? 0.135751  0.264165 0.176485 0.0169567   -0.0177921  -0.0133083  185 PHE   B C    
3821 O  O    . PHE   B 185 ? 0.159287  0.276398 0.203502 0.00862017  0.00431573  -0.0153998  185 PHE   B O    
3822 C  CB   . PHE   B 185 ? 0.126126  0.276217 0.186445 0.0211528   -0.0143748  -0.00679152 185 PHE   B CB   
3823 C  CG   . PHE   B 185 ? 0.138164  0.282445 0.178586 0.0112601   -0.0172146  -0.00408278 185 PHE   B CG   
3824 C  CD1  . PHE   B 185 ? 0.136718  0.295899 0.171559 0.021128    -0.0181681  -0.0099006  185 PHE   B CD1  
3825 C  CD2  . PHE   B 185 ? 0.141258  0.288983 0.185291 0.00836219  -0.0205676  -0.00915867 185 PHE   B CD2  
3826 C  CE1  . PHE   B 185 ? 0.148092  0.302674 0.166655 0.0231196   -0.016556   -0.0117988  185 PHE   B CE1  
3827 C  CE2  . PHE   B 185 ? 0.169995  0.293684 0.177095 0.0084443   -0.0126411  -0.00459518 185 PHE   B CE2  
3828 C  CZ   . PHE   B 185 ? 0.173347  0.294974 0.165866 0.0140445   -0.0155034  -0.0164371  185 PHE   B CZ   
3829 N  N    . VAL   B 186 ? 0.113853  0.270016 0.171794 0.0109974   -0.0243692  -0.0149956  186 VAL   B N    
3830 C  CA   . VAL   B 186 ? 0.132798  0.277597 0.171133 0.00949826  -0.0207778  -0.020647   186 VAL   B CA   
3831 C  C    . VAL   B 186 ? 0.1292    0.274712 0.173904 -0.00736037 -0.0177682  -0.0202434  186 VAL   B C    
3832 O  O    . VAL   B 186 ? 0.134595  0.285609 0.175891 0.00445025  -0.00268642 -0.0256646  186 VAL   B O    
3833 C  CB   . VAL   B 186 ? 0.154537  0.302908 0.16968  0.0123413   -0.0304857  -0.019082   186 VAL   B CB   
3834 C  CG1  . VAL   B 186 ? 0.185425  0.314506 0.176228 0.0147056   -0.0179448  -0.0167464  186 VAL   B CG1  
3835 C  CG2  . VAL   B 186 ? 0.158137  0.313435 0.167568 0.0066112   -0.0376806  -0.0153435  186 VAL   B CG2  
3836 N  N    . ASP   B 187 ? 0.136882  0.272486 0.176922 -0.00839993 -0.0127275  -0.0233379  187 ASP   B N    
3837 C  CA   . ASP   B 187 ? 0.133046  0.272285 0.184635 -0.00844288 -0.0128173  -0.0284307  187 ASP   B CA   
3838 C  C    . ASP   B 187 ? 0.135856  0.277199 0.188781 -0.0104417  -0.00966394 -0.0391134  187 ASP   B C    
3839 O  O    . ASP   B 187 ? 0.148607  0.273787 0.190699 -0.0160559  -0.0023758  -0.0306994  187 ASP   B O    
3840 C  CB   . ASP   B 187 ? 0.131886  0.275496 0.179109 -0.00671706 -0.0148479  -0.0270181  187 ASP   B CB   
3841 C  CG   . ASP   B 187 ? 0.140289  0.278431 0.179271 -0.00570888 -0.021228   -0.0304005  187 ASP   B CG   
3842 O  OD1  . ASP   B 187 ? 0.144998  0.29588  0.175727 -0.00447988 -0.0197888  -0.0233994  187 ASP   B OD1  
3843 O  OD2  . ASP   B 187 ? 0.136523  0.274939 0.175238 -0.00206407 -0.0130285  -0.0286218  187 ASP   B OD2  
3844 N  N    . ARG   B 188 ? 0.122472  0.295556 0.222473 -0.0206465  0.00487217  -0.0471141  188 ARG   B N    
3845 C  CA   . ARG   B 188 ? 0.141114  0.327586 0.238493 -0.0346765  -0.00165408 -0.0558772  188 ARG   B CA   
3846 C  C    . ARG   B 188 ? 0.145449  0.335685 0.249603 -0.0416421  0.00865126  -0.0614717  188 ARG   B C    
3847 O  O    . ARG   B 188 ? 0.143804  0.327023 0.275655 -0.0366152  0.00258719  -0.0671256  188 ARG   B O    
3848 C  CB   . ARG   B 188 ? 0.164028  0.348701 0.269403 -0.0313604  -0.008768   -0.0494232  188 ARG   B CB   
3849 C  CG   . ARG   B 188 ? 0.166465  0.381759 0.300406 -0.0299443  -0.0143947  -0.0448496  188 ARG   B CG   
3850 C  CD   . ARG   B 188 ? 0.201818  0.412837 0.343596 -0.0151865  -0.0228408  -0.0412042  188 ARG   B CD   
3851 N  NE   . ARG   B 188 ? 0.227089  0.456888 0.408528 -0.025149   -0.00885905 -0.0189219  188 ARG   B NE   
3852 C  CZ   . ARG   B 188 ? 0.247838  0.485365 0.497306 -0.00518661 -0.00680362 0.00336266  188 ARG   B CZ   
3853 N  NH1  . ARG   B 188 ? 0.268035  0.545451 0.534987 -0.0274373  -0.0110259  -0.00215581 188 ARG   B NH1  
3854 N  NH2  . ARG   B 188 ? 0.293036  0.498414 0.550385 0.00617802  0.0045515   0.0262114   188 ARG   B NH2  
3855 N  N    . GLN   B 189 ? 0.15659   0.357117 0.261715 -0.0552901  0.020211    -0.0593179  189 GLN   B N    
3856 C  CA   . GLN   B 189 ? 0.163711  0.37801  0.28909  -0.0610212  0.0407823   -0.0724556  189 GLN   B CA   
3857 C  C    . GLN   B 189 ? 0.15302   0.388911 0.333801 -0.0661721  0.0435528   -0.0805156  189 GLN   B C    
3858 O  O    . GLN   B 189 ? 0.184507  0.398653 0.382003 -0.0805395  0.0334523   -0.0824764  189 GLN   B O    
3859 C  CB   . GLN   B 189 ? 0.194716  0.394453 0.293857 -0.0717945  0.0423077   -0.0566862  189 GLN   B CB   
3860 C  CG   . GLN   B 189 ? 0.246053  0.426975 0.304153 -0.0741634  0.0465896   -0.0469771  189 GLN   B CG   
3861 C  CD   . GLN   B 189 ? 0.306573  0.459448 0.331936 -0.076698   0.0151076   -0.0389192  189 GLN   B CD   
3862 O  OE1  . GLN   B 189 ? 0.343571  0.517836 0.409203 -0.0587624  0.00986036  -0.00080178 189 GLN   B OE1  
3863 N  NE2  . GLN   B 189 ? 0.33781   0.476463 0.321801 -0.0662292  0.0163967   -0.0460917  189 GLN   B NE2  
3864 N  N    . THR   B 190 ? 0.159456  0.400382 0.389171 -0.0461249  0.0558183   -0.0990302  190 THR   B N    
3865 C  CA   . THR   B 190 ? 0.163339  0.412299 0.412995 -0.0482441  0.0431854   -0.11902    190 THR   B CA   
3866 C  C    . THR   B 190 ? 0.168464  0.416678 0.406745 -0.049601   0.054164    -0.122185   190 THR   B C    
3867 O  O    . THR   B 190 ? 0.177899  0.418791 0.402649 -0.0726107  0.0511169   -0.120825   190 THR   B O    
3868 C  CB   . THR   B 190 ? 0.165173  0.435248 0.429294 -0.0423802  0.039675    -0.124222   190 THR   B CB   
3869 O  OG1  . THR   B 190 ? 0.202539  0.466329 0.468302 -0.00794148 0.0213128   -0.139798   190 THR   B OG1  
3870 C  CG2  . THR   B 190 ? 0.195887  0.443518 0.463671 -0.038933   0.0349023   -0.114371   190 THR   B CG2  
3871 N  N    . ALA   B 191 ? 0.165009  0.421625 0.418385 -0.0509846  0.0505477   -0.117846   191 ALA   B N    
3872 C  CA   . ALA   B 191 ? 0.171963  0.423911 0.381268 -0.0353531  0.0585686   -0.110213   191 ALA   B CA   
3873 C  C    . ALA   B 191 ? 0.15272   0.404213 0.322039 -0.0312727  0.0300632   -0.0936329  191 ALA   B C    
3874 O  O    . ALA   B 191 ? 0.164623  0.442835 0.328171 -0.0211807  -0.0228362  -0.101013   191 ALA   B O    
3875 C  CB   . ALA   B 191 ? 0.176285  0.437771 0.41332  -0.0225466  0.0693529   -0.112953   191 ALA   B CB   
3876 N  N    . GLN   B 192 ? 0.180197  0.368849 0.260927 -0.0297753  0.0252553   -0.070632   192 GLN   B N    
3877 C  CA   . GLN   B 192 ? 0.164298  0.346805 0.227679 -0.0163657  0.0221849   -0.0596444  192 GLN   B CA   
3878 C  C    . GLN   B 192 ? 0.181537  0.378331 0.22371  -0.0152609  0.02        -0.0618523  192 GLN   B C    
3879 O  O    . GLN   B 192 ? 0.254151  0.408168 0.240469 -0.0126686  0.0122576   -0.0310424  192 GLN   B O    
3880 C  CB   . GLN   B 192 ? 0.15747   0.330344 0.221091 -0.0108403  0.00963956  -0.0465845  192 GLN   B CB   
3881 C  CG   . GLN   B 192 ? 0.144069  0.32265  0.218881 -0.0115444  0.00651084  -0.0433143  192 GLN   B CG   
3882 C  CD   . GLN   B 192 ? 0.131334  0.307602 0.206194 -0.00866407 -0.00325156 -0.0374129  192 GLN   B CD   
3883 O  OE1  . GLN   B 192 ? 0.14404   0.300234 0.206832 0.00248412  0.00925144  -0.0285396  192 GLN   B OE1  
3884 N  NE2  . GLN   B 192 ? 0.139132  0.306105 0.227525 -0.0174908  0.00357655  -0.0283665  192 GLN   B NE2  
3885 N  N    . ALA   B 193 ? 0.16763   0.389779 0.218337 -0.0283861  0.0379873   -0.0779388  193 ALA   B N    
3886 C  CA   . ALA   B 193 ? 0.185977  0.416917 0.265395 -0.0268835  0.0312123   -0.115546   193 ALA   B CA   
3887 C  C    . ALA   B 193 ? 0.209462  0.427492 0.339459 -0.0238325  0.0467623   -0.135107   193 ALA   B C    
3888 O  O    . ALA   B 193 ? 0.238892  0.429525 0.3632   -0.0668428  0.0950575   -0.141183   193 ALA   B O    
3889 C  CB   . ALA   B 193 ? 0.185673  0.434334 0.262168 -0.0209774  0.0387604   -0.115918   193 ALA   B CB   
3890 N  N    . ALA   B 194 ? 0.212877  0.448458 0.428136 0.00173276  0.0163049   -0.165529   194 ALA   B N    
3891 C  CA   . ALA   B 194 ? 0.226424  0.446082 0.476357 0.00819413  -0.0128941  -0.174424   194 ALA   B CA   
3892 C  C    . ALA   B 194 ? 0.175843  0.436969 0.413833 0.0105631   -0.0272291  -0.172981   194 ALA   B C    
3893 O  O    . ALA   B 194 ? 0.190098  0.453944 0.408651 0.0204235   -0.0173382  -0.186062   194 ALA   B O    
3894 C  CB   . ALA   B 194 ? 0.241771  0.484286 0.522602 0.0197164   -0.0346537  -0.17022    194 ALA   B CB   
3895 N  N    . GLY   B 195 ? 0.151928  0.422042 0.382189 0.0277519   -0.0254307  -0.154831   195 GLY   B N    
3896 C  CA   . GLY   B 195 ? 0.140977  0.403495 0.339783 0.0394652   -0.0400641  -0.12359    195 GLY   B CA   
3897 C  C    . GLY   B 195 ? 0.132557  0.36829  0.315095 0.0369562   -0.035707   -0.100863   195 GLY   B C    
3898 O  O    . GLY   B 195 ? 0.14875   0.34837  0.324075 0.0528207   -0.0398286  -0.104594   195 GLY   B O    
3899 N  N    A THR   B 196 ? 0.144616  0.369213 0.310529 0.0462431   -0.030094   -0.0845075  196 THR   B N    
3900 N  N    B THR   B 196 ? 0.13244   0.368095 0.292116 0.0388587   -0.0348524  -0.0955589  196 THR   B N    
3901 C  CA   A THR   B 196 ? 0.147082  0.379751 0.315586 0.0316731   -0.0296807  -0.0770098  196 THR   B CA   
3902 C  CA   B THR   B 196 ? 0.124562  0.372709 0.294544 0.0262687   -0.0332628  -0.0953585  196 THR   B CA   
3903 C  C    A THR   B 196 ? 0.141389  0.374219 0.307866 0.0348216   -0.0295121  -0.0620332  196 THR   B C    
3904 C  C    B THR   B 196 ? 0.126667  0.373075 0.295609 0.0254067   -0.0284197  -0.0733509  196 THR   B C    
3905 O  O    A THR   B 196 ? 0.155204  0.39831  0.354647 0.0292089   -0.0502955  -0.0185223  196 THR   B O    
3906 O  O    B THR   B 196 ? 0.153797  0.404664 0.349091 0.0112478   -0.0438624  -0.0311205  196 THR   B O    
3907 C  CB   A THR   B 196 ? 0.179502  0.39268  0.338716 0.043859    -0.0168484  -0.0695577  196 THR   B CB   
3908 C  CB   B THR   B 196 ? 0.135626  0.381361 0.299972 0.0295778   -0.0273669  -0.101562   196 THR   B CB   
3909 O  OG1  A THR   B 196 ? 0.22354   0.411691 0.366141 0.0347678   -0.00609025 -0.0529996  196 THR   B OG1  
3910 O  OG1  B THR   B 196 ? 0.12755   0.401581 0.317944 0.0299026   -0.0273238  -0.111187   196 THR   B OG1  
3911 C  CG2  A THR   B 196 ? 0.175744  0.40191  0.347976 0.0466746   -0.0169239  -0.073242   196 THR   B CG2  
3912 C  CG2  B THR   B 196 ? 0.137148  0.379321 0.299096 0.0298232   -0.0238834  -0.109897   196 THR   B CG2  
3913 N  N    . ASP   B 197 ? 0.134418  0.356249 0.278207 0.0213414   -0.0179862  -0.0745126  197 ASP   B N    
3914 C  CA   . ASP   B 197 ? 0.133489  0.328427 0.262534 0.0235087   -0.0184858  -0.082693   197 ASP   B CA   
3915 C  C    . ASP   B 197 ? 0.139791  0.327693 0.270688 0.0305734   -0.0184739  -0.0907839  197 ASP   B C    
3916 O  O    . ASP   B 197 ? 0.138616  0.375665 0.302834 0.0283016   -0.0142209  -0.11488    197 ASP   B O    
3917 C  CB   . ASP   B 197 ? 0.136066  0.32045  0.249776 0.02371     -0.0258533  -0.0785515  197 ASP   B CB   
3918 C  CG   . ASP   B 197 ? 0.144448  0.310139 0.2318   0.0251518   -0.0150974  -0.0614838  197 ASP   B CG   
3919 O  OD1  . ASP   B 197 ? 0.150454  0.25776  0.243489 0.0229758   -0.0198611  -0.0529368  197 ASP   B OD1  
3920 O  OD2  . ASP   B 197 ? 0.157037  0.339762 0.233876 0.0219308   -0.0377039  -0.0551948  197 ASP   B OD2  
3921 N  N    . THR   B 198 ? 0.130846  0.286447 0.243997 0.0324951   -0.0317077  -0.0880665  198 THR   B N    
3922 C  CA   . THR   B 198 ? 0.135011  0.2732   0.241383 0.0355076   -0.0401383  -0.0655961  198 THR   B CA   
3923 C  C    . THR   B 198 ? 0.133631  0.240629 0.225145 0.0383739   -0.0389523  -0.063016   198 THR   B C    
3924 O  O    . THR   B 198 ? 0.153947  0.23683  0.223152 0.0389863   -0.0484732  -0.0602692  198 THR   B O    
3925 C  CB   . THR   B 198 ? 0.168472  0.301818 0.264198 0.0532239   -0.0430161  -0.0544965  198 THR   B CB   
3926 O  OG1  . THR   B 198 ? 0.225289  0.31326  0.249213 0.0660045   -0.028496   -0.0361942  198 THR   B OG1  
3927 C  CG2  . THR   B 198 ? 0.180079  0.323996 0.286626 0.0575715   -0.0522772  -0.0456378  198 THR   B CG2  
3928 N  N    . THR   B 199 ? 0.128875  0.218768 0.222019 0.0349481   -0.0394551  -0.0534838  199 THR   B N    
3929 C  CA   . THR   B 199 ? 0.125348  0.220723 0.209797 0.027699    -0.0304743  -0.0463545  199 THR   B CA   
3930 C  C    . THR   B 199 ? 0.137416  0.204756 0.202231 0.0247162   -0.0290511  -0.0369125  199 THR   B C    
3931 O  O    . THR   B 199 ? 0.136975  0.211937 0.220596 0.0202865   -0.0267508  -0.0273971  199 THR   B O    
3932 C  CB   . THR   B 199 ? 0.13929   0.234816 0.211712 0.0236823   -0.0205744  -0.0472587  199 THR   B CB   
3933 O  OG1  . THR   B 199 ? 0.166861  0.250989 0.213732 0.0116281   -0.0110981  -0.0439206  199 THR   B OG1  
3934 C  CG2  . THR   B 199 ? 0.149072  0.239081 0.219981 0.0203653   -0.027062   -0.0576296  199 THR   B CG2  
3935 N  N    . ILE   B 200 ? 0.143636  0.199651 0.189152 0.0259346   -0.0348635  -0.0278276  200 ILE   B N    
3936 C  CA   . ILE   B 200 ? 0.149191  0.187796 0.172647 0.0192363   -0.0336731  -0.0270006  200 ILE   B CA   
3937 C  C    . ILE   B 200 ? 0.14498   0.188348 0.174524 0.0170753   -0.0377423  -0.0171321  200 ILE   B C    
3938 O  O    . ILE   B 200 ? 0.130947  0.195659 0.175855 0.0108639   -0.0372214  -0.0134265  200 ILE   B O    
3939 C  CB   . ILE   B 200 ? 0.152806  0.196312 0.16559  0.0163844   -0.0301474  -0.0315938  200 ILE   B CB   
3940 C  CG1  . ILE   B 200 ? 0.155535  0.206292 0.171267 0.00997709  -0.0283539  -0.032157   200 ILE   B CG1  
3941 C  CG2  . ILE   B 200 ? 0.155376  0.206935 0.169317 0.01283     -0.0365385  -0.0224338  200 ILE   B CG2  
3942 C  CD1  . ILE   B 200 ? 0.1551    0.202158 0.168822 0.00743848  -0.0212425  -0.0324754  200 ILE   B CD1  
3943 N  N    . THR   B 201 ? 0.153833  0.187252 0.183429 0.0158307   -0.0443589  -0.0108894  201 THR   B N    
3944 C  CA   . THR   B 201 ? 0.15733   0.191871 0.181879 0.0113712   -0.0408884  -0.00752241 201 THR   B CA   
3945 C  C    . THR   B 201 ? 0.159921  0.195263 0.179698 0.0102443   -0.0244762  -0.00268496 201 THR   B C    
3946 O  O    . THR   B 201 ? 0.149356  0.194181 0.181695 0.0145137   -0.0248814  -0.00022565 201 THR   B O    
3947 C  CB   . THR   B 201 ? 0.154439  0.202974 0.192588 0.0142515   -0.044485   -0.00270019 201 THR   B CB   
3948 O  OG1  . THR   B 201 ? 0.153369  0.217057 0.21264  0.0171665   -0.0415527  -0.00791728 201 THR   B OG1  
3949 C  CG2  . THR   B 201 ? 0.172339  0.203414 0.207956 0.0234293   -0.044102   -0.00380185 201 THR   B CG2  
3950 N  N    . VAL   B 202 ? 0.146138  0.20045  0.182694 0.0026216   -0.02024    -0.0015998  202 VAL   B N    
3951 C  CA   . VAL   B 202 ? 0.148503  0.199114 0.185795 -0.00824656 -0.0255387  0.0107154   202 VAL   B CA   
3952 C  C    . VAL   B 202 ? 0.147191  0.200486 0.179025 -0.00118238 -0.0212154  0.00493057  202 VAL   B C    
3953 O  O    . VAL   B 202 ? 0.143645  0.207499 0.180471 0.00189124  -0.0242535  0.0174418   202 VAL   B O    
3954 C  CB   . VAL   B 202 ? 0.172251  0.236544 0.195766 -0.00480983 -0.0223499  0.0209966   202 VAL   B CB   
3955 C  CG1  . VAL   B 202 ? 0.19061   0.240662 0.193706 0.00040829  -0.0165837  0.0216152   202 VAL   B CG1  
3956 C  CG2  . VAL   B 202 ? 0.1749    0.247572 0.209257 -0.0070676  -0.022638   0.0244951   202 VAL   B CG2  
3957 N  N    . ASN   B 203 ? 0.128456  0.185306 0.16244  0.00677668  -0.0297544  -0.00618737 203 ASN   B N    
3958 C  CA   . ASN   B 203 ? 0.120737  0.182004 0.167636 0.0112633   -0.0246726  -0.00748455 203 ASN   B CA   
3959 C  C    . ASN   B 203 ? 0.128331  0.176038 0.162983 0.0135277   -0.0269132  -0.00755719 203 ASN   B C    
3960 O  O    . ASN   B 203 ? 0.121062  0.180885 0.176519 0.00763176  -0.0287819  -0.00026157 203 ASN   B O    
3961 C  CB   . ASN   B 203 ? 0.134828  0.18333  0.168069 0.0159323   -0.0260914  -0.0135954  203 ASN   B CB   
3962 C  CG   . ASN   B 203 ? 0.137318  0.194421 0.164799 0.0231373   -0.0280458  -0.00741631 203 ASN   B CG   
3963 O  OD1  . ASN   B 203 ? 0.13027   0.218321 0.173926 0.0214694   -0.0244357  -0.00288438 203 ASN   B OD1  
3964 N  ND2  . ASN   B 203 ? 0.14411   0.195907 0.166534 0.0202051   -0.0168953  -0.0151009  203 ASN   B ND2  
3965 N  N    . VAL   B 204 ? 0.129034  0.174661 0.1614   0.00807077  -0.0305091  -0.0087019  204 VAL   B N    
3966 C  CA   . VAL   B 204 ? 0.141607  0.162439 0.164882 0.00893783  -0.026413   -0.00545104 204 VAL   B CA   
3967 C  C    . VAL   B 204 ? 0.141225  0.168358 0.158551 0.00018881  -0.0243151  -0.00411636 204 VAL   B C    
3968 O  O    . VAL   B 204 ? 0.149732  0.167663 0.158585 -0.00241098 -0.0236769  -0.0118118  204 VAL   B O    
3969 C  CB   . VAL   B 204 ? 0.141656  0.171051 0.167042 0.00475376  -0.0244114  -0.00780719 204 VAL   B CB   
3970 C  CG1  . VAL   B 204 ? 0.157041  0.183219 0.17573  -0.00429954 -0.022227   -0.0108005  204 VAL   B CG1  
3971 C  CG2  . VAL   B 204 ? 0.139551  0.173616 0.174105 0.00632871  -0.0231193  -0.00813396 204 VAL   B CG2  
3972 N  N    . LEU   B 205 ? 0.150054  0.16746  0.16725  -0.00434304 -0.0384199  0.0018707   205 LEU   B N    
3973 C  CA   . LEU   B 205 ? 0.160771  0.173621 0.177167 -0.0122349  -0.0382747  0.00424151  205 LEU   B CA   
3974 C  C    . LEU   B 205 ? 0.15847   0.19175  0.18331  -0.0138888  -0.0357905  0.0103758   205 LEU   B C    
3975 O  O    . LEU   B 205 ? 0.146665  0.196641 0.18371  -0.0282397  -0.0354121  0.0107259   205 LEU   B O    
3976 C  CB   . LEU   B 205 ? 0.18335   0.172492 0.184757 -0.0140396  -0.0392761  0.00481465  205 LEU   B CB   
3977 C  CG   . LEU   B 205 ? 0.197303  0.176357 0.190358 -0.00555174 -0.0448934  0.00804267  205 LEU   B CG   
3978 C  CD1  . LEU   B 205 ? 0.192831  0.183844 0.19618  0.00020628  -0.050723   0.0124442   205 LEU   B CD1  
3979 C  CD2  . LEU   B 205 ? 0.216155  0.172989 0.19817  -0.00294014 -0.0447684  0.00587764  205 LEU   B CD2  
3980 N  N    . ALA   B 206 ? 0.141455  0.19618  0.185296 -0.0102598  -0.0354601  0.0148393   206 ALA   B N    
3981 C  CA   . ALA   B 206 ? 0.144582  0.206311 0.195538 0.00061686  -0.0268432  0.0149829   206 ALA   B CA   
3982 C  C    . ALA   B 206 ? 0.135617  0.208246 0.184652 -0.00562093 -0.0294623  0.00875907  206 ALA   B C    
3983 O  O    . ALA   B 206 ? 0.131276  0.236065 0.19094  0.00164855  -0.0300694  0.015873    206 ALA   B O    
3984 C  CB   . ALA   B 206 ? 0.144136  0.219512 0.193201 -0.00176397 -0.0250505  0.0158376   206 ALA   B CB   
3985 N  N    . TRP   B 207 ? 0.128567  0.192616 0.177349 -0.00580892 -0.0395105  0.00820769  207 TRP   B N    
3986 C  CA   . TRP   B 207 ? 0.133939  0.182208 0.17308  -0.00078989 -0.0386026  0.00424245  207 TRP   B CA   
3987 C  C    . TRP   B 207 ? 0.12961   0.171448 0.168729 -0.00203914 -0.0409233  0.00663214  207 TRP   B C    
3988 O  O    . TRP   B 207 ? 0.121759  0.188116 0.182168 0.00484399  -0.0509388  -0.00080327 207 TRP   B O    
3989 C  CB   . TRP   B 207 ? 0.149648  0.189296 0.175978 -0.00766159 -0.0407258  0.00383516  207 TRP   B CB   
3990 C  CG   . TRP   B 207 ? 0.155563  0.205929 0.174981 -0.022194   -0.0364566  -0.00082362 207 TRP   B CG   
3991 C  CD1  . TRP   B 207 ? 0.178849  0.223221 0.187517 -0.0120351  -0.0343643  0.00659174  207 TRP   B CD1  
3992 C  CD2  . TRP   B 207 ? 0.17695   0.235419 0.183845 -0.0332581  -0.0288073  -0.0110047  207 TRP   B CD2  
3993 N  NE1  . TRP   B 207 ? 0.184372  0.24894  0.190881 -0.0260606  -0.0415928  0.0205886   207 TRP   B NE1  
3994 C  CE2  . TRP   B 207 ? 0.194304  0.251145 0.186542 -0.03694    -0.0261856  -0.0157457  207 TRP   B CE2  
3995 C  CE3  . TRP   B 207 ? 0.187641  0.254307 0.199252 -0.0395115  -0.0112425  -0.030509   207 TRP   B CE3  
3996 C  CZ2  . TRP   B 207 ? 0.196132  0.283911 0.193242 -0.0569447  -0.0186007  -0.0157129  207 TRP   B CZ2  
3997 C  CZ3  . TRP   B 207 ? 0.212432  0.28432  0.205985 -0.0382024  -0.00566764 -0.0367846  207 TRP   B CZ3  
3998 C  CH2  . TRP   B 207 ? 0.211953  0.293712 0.193499 -0.0512965  -0.00943374 -0.0285489  207 TRP   B CH2  
3999 N  N    . LEU   B 208 ? 0.134774  0.169144 0.169461 -0.00496513 -0.0401135  -0.00318716 208 LEU   B N    
4000 C  CA   . LEU   B 208 ? 0.15231   0.170341 0.182096 -0.00683831 -0.0424898  -0.00766156 208 LEU   B CA   
4001 C  C    . LEU   B 208 ? 0.15724   0.187915 0.189458 -0.0138735  -0.0439913  -0.00893522 208 LEU   B C    
4002 O  O    . LEU   B 208 ? 0.146219  0.200303 0.200694 -0.0192641  -0.0512086  -0.0116775  208 LEU   B O    
4003 C  CB   . LEU   B 208 ? 0.154714  0.177382 0.188497 -0.00204991 -0.0399429  -0.00683035 208 LEU   B CB   
4004 C  CG   . LEU   B 208 ? 0.155252  0.183636 0.185366 0.00438419  -0.0309275  -0.00542283 208 LEU   B CG   
4005 C  CD1  . LEU   B 208 ? 0.167742  0.200554 0.188242 0.0119162   -0.0270695  0.00563701  208 LEU   B CD1  
4006 C  CD2  . LEU   B 208 ? 0.159657  0.199905 0.196311 0.00587478  -0.0284771  -0.00096403 208 LEU   B CD2  
4007 N  N    . TYR   B 209 ? 0.149716  0.212802 0.205602 -0.0234926  -0.0546646  0.0064461   209 TYR   B N    
4008 C  CA   . TYR   B 209 ? 0.155495  0.223114 0.229382 -0.0335782  -0.0511549  0.0161012   209 TYR   B CA   
4009 C  C    . TYR   B 209 ? 0.139107  0.23013  0.225461 -0.0246851  -0.053074   0.0107768   209 TYR   B C    
4010 O  O    . TYR   B 209 ? 0.128651  0.246076 0.246921 -0.025861   -0.060537   0.0183519   209 TYR   B O    
4011 C  CB   . TYR   B 209 ? 0.159711  0.234858 0.243735 -0.0518141  -0.0495894  0.0340135   209 TYR   B CB   
4012 C  CG   . TYR   B 209 ? 0.185372  0.235944 0.261213 -0.0640439  -0.054642   0.0425587   209 TYR   B CG   
4013 C  CD1  . TYR   B 209 ? 0.215346  0.248974 0.293216 -0.0763594  -0.0633925  0.0442878   209 TYR   B CD1  
4014 C  CD2  . TYR   B 209 ? 0.176961  0.231663 0.270368 -0.0625681  -0.0507947  0.0562399   209 TYR   B CD2  
4015 C  CE1  . TYR   B 209 ? 0.230249  0.248558 0.297069 -0.0834895  -0.0661959  0.0560085   209 TYR   B CE1  
4016 C  CE2  . TYR   B 209 ? 0.222727  0.233263 0.286752 -0.0745163  -0.051201   0.0653917   209 TYR   B CE2  
4017 C  CZ   . TYR   B 209 ? 0.227966  0.23733  0.310601 -0.0807428  -0.0706972  0.065883    209 TYR   B CZ   
4018 O  OH   . TYR   B 209 ? 0.282927  0.237289 0.329161 -0.0874732  -0.099114   0.0841047   209 TYR   B OH   
4019 N  N    . ALA   B 210 ? 0.131041  0.223471 0.209438 -0.00851522 -0.0583565  0.00910299  210 ALA   B N    
4020 C  CA   . ALA   B 210 ? 0.124919  0.220461 0.212052 -0.00224084 -0.0559697  0.00438581  210 ALA   B CA   
4021 C  C    . ALA   B 210 ? 0.14242   0.212952 0.211582 0.00580144  -0.0622077  0.00397897  210 ALA   B C    
4022 O  O    . ALA   B 210 ? 0.148529  0.225725 0.217463 0.00881739  -0.0707813  0.00242731  210 ALA   B O    
4023 C  CB   . ALA   B 210 ? 0.128061  0.216324 0.207313 0.00864067  -0.0597234  0.00400408  210 ALA   B CB   
4024 N  N    . ALA   B 211 ? 0.137464  0.204498 0.209222 -1.974e-05  -0.0636918  -0.00087464 211 ALA   B N    
4025 C  CA   . ALA   B 211 ? 0.163848  0.19438  0.213233 0.00137196  -0.0666061  0.0013359   211 ALA   B CA   
4026 C  C    . ALA   B 211 ? 0.163946  0.204359 0.221847 -0.00859906 -0.0763728  0.0087438   211 ALA   B C    
4027 O  O    . ALA   B 211 ? 0.178206  0.218914 0.229317 0.00574093  -0.0828542  0.00350271  211 ALA   B O    
4028 C  CB   . ALA   B 211 ? 0.156873  0.203184 0.217143 -0.00099088 -0.0693003  -0.00035913 211 ALA   B CB   
4029 N  N    . VAL   B 212 ? 0.178613  0.198416 0.234555 -0.0198975  -0.100314   0.00296355  212 VAL   B N    
4030 C  CA   . VAL   B 212 ? 0.207945  0.2124   0.273582 -0.0367271  -0.103382   0.00221705  212 VAL   B CA   
4031 C  C    . VAL   B 212 ? 0.20981   0.251491 0.292921 -0.029827   -0.113495   0.00675728  212 VAL   B C    
4032 O  O    . VAL   B 212 ? 0.220706  0.253167 0.313646 -0.0407485  -0.131809   -0.00446919 212 VAL   B O    
4033 C  CB   . VAL   B 212 ? 0.233336  0.206854 0.283452 -0.0395828  -0.107593   0.00569757  212 VAL   B CB   
4034 C  CG1  . VAL   B 212 ? 0.248445  0.208488 0.303106 -0.0474859  -0.109005   9.788e-05   212 VAL   B CG1  
4035 C  CG2  . VAL   B 212 ? 0.22677   0.190814 0.264348 -0.0343881  -0.114507   0.00737647  212 VAL   B CG2  
4036 N  N    . ILE   B 213 ? 0.191636  0.262227 0.289259 -0.0291322  -0.107143   0.00782594  213 ILE   B N    
4037 C  CA   . ILE   B 213 ? 0.177928  0.295648 0.319605 -0.0290202  -0.0963865  0.0223796   213 ILE   B CA   
4038 C  C    . ILE   B 213 ? 0.184642  0.29008  0.306847 -0.0128779  -0.107514   0.0080723   213 ILE   B C    
4039 O  O    . ILE   B 213 ? 0.169346  0.329619 0.325606 -0.00776447 -0.0961128  0.0199444   213 ILE   B O    
4040 C  CB   . ILE   B 213 ? 0.154867  0.333494 0.327739 -0.0240104  -0.0835963  0.0330165   213 ILE   B CB   
4041 C  CG1  . ILE   B 213 ? 0.167065  0.35193  0.344737 -0.0391865  -0.0668094  0.0492445   213 ILE   B CG1  
4042 C  CG2  . ILE   B 213 ? 0.160975  0.363276 0.34442  -0.0125721  -0.0727428  0.0396365   213 ILE   B CG2  
4043 C  CD1  . ILE   B 213 ? 0.184571  0.370251 0.347651 -0.0448702  -0.0582326  0.0529803   213 ILE   B CD1  
4044 N  N    . ASN   B 214 ? 0.189074  0.266775 0.287396 -0.00767946 -0.11871    0.00492008  214 ASN   B N    
4045 C  CA   . ASN   B 214 ? 0.229132  0.278793 0.293966 0.00824493  -0.128508   0.0003614   214 ASN   B CA   
4046 C  C    . ASN   B 214 ? 0.240352  0.284565 0.286227 0.0225855   -0.11654    0.00565495  214 ASN   B C    
4047 O  O    . ASN   B 214 ? 0.301183  0.299739 0.283842 0.0387952   -0.0995477  0.00222449  214 ASN   B O    
4048 C  CB   . ASN   B 214 ? 0.245829  0.275578 0.325116 0.0110962   -0.133871   -0.00373672 214 ASN   B CB   
4049 C  CG   . ASN   B 214 ? 0.264979  0.299129 0.368804 0.0317942   -0.141328   -0.0260745  214 ASN   B CG   
4050 O  OD1  . ASN   B 214 ? 0.335515  0.319623 0.445946 0.0590277   -0.205811   -0.0417201  214 ASN   B OD1  
4051 N  ND2  . ASN   B 214 ? 0.265934  0.326784 0.370269 0.0410564   -0.133178   -0.0362208  214 ASN   B ND2  
4052 N  N    . GLY   B 215 ? 0.260971  0.289661 0.260429 0.0243155   -0.125539   -0.00673846 215 GLY   B N    
4053 C  CA   . GLY   B 215 ? 0.288862  0.321001 0.27024  0.0228744   -0.116719   -0.0140408  215 GLY   B CA   
4054 C  C    . GLY   B 215 ? 0.301628  0.338601 0.268183 0.0116194   -0.11591    -0.0160324  215 GLY   B C    
4055 O  O    . GLY   B 215 ? 0.35155   0.388878 0.277608 0.0110583   -0.118555   -0.0379425  215 GLY   B O    
4056 N  N    . ASP   B 216 ? 0.306699  0.32495  0.257264 0.0117325   -0.112587   -0.0197793  216 ASP   B N    
4057 C  CA   . ASP   B 216 ? 0.318522  0.338337 0.263259 -0.00586507 -0.108906   -0.0268256  216 ASP   B CA   
4058 C  C    . ASP   B 216 ? 0.300024  0.365588 0.263314 0.0200366   -0.112127   -0.00287469 216 ASP   B C    
4059 O  O    . ASP   B 216 ? 0.3079    0.405215 0.264557 0.0794333   -0.0924506  -0.00365379 216 ASP   B O    
4060 C  CB   . ASP   B 216 ? 0.360716  0.361567 0.30672  -0.0309916  -0.0872778  -0.0309914  216 ASP   B CB   
4061 C  CG   . ASP   B 216 ? 0.362274  0.37841  0.33107  -0.0454337  -0.0893351  -0.0392896  216 ASP   B CG   
4062 O  OD1  . ASP   B 216 ? 0.37763   0.418    0.36641  -0.0127677  -0.0678691  -0.0371903  216 ASP   B OD1  
4063 O  OD2  . ASP   B 216 ? 0.351998  0.388841 0.351954 -0.0668412  -0.114521   -0.0224378  216 ASP   B OD2  
4064 N  N    . ARG   B 217 ? 0.322873  0.329291 0.275164 0.00744458  -0.116681   0.0182007   217 ARG   B N    
4065 C  CA   . ARG   B 217 ? 0.333693  0.329227 0.322689 8.148e-05   -0.117515   0.0172811   217 ARG   B CA   
4066 C  C    . ARG   B 217 ? 0.326688  0.295649 0.292989 -0.00228417 -0.117242   0.0150066   217 ARG   B C    
4067 O  O    . ARG   B 217 ? 0.331348  0.298409 0.320691 -0.0140937  -0.128988   0.0294736   217 ARG   B O    
4068 C  CB   . ARG   B 217 ? 0.359062  0.360974 0.395366 -0.022144   -0.104763   0.0327086   217 ARG   B CB   
4069 C  CG   . ARG   B 217 ? 0.355876  0.38772  0.426915 -0.025299   -0.116372   0.0403327   217 ARG   B CG   
4070 C  CD   . ARG   B 217 ? 0.38954   0.39348  0.457978 -0.046898   -0.112491   0.0367867   217 ARG   B CD   
4071 N  NE   . ARG   B 217 ? 0.388006  0.403214 0.451754 -0.0533959  -0.127606   0.040926    217 ARG   B NE   
4072 C  CZ   . ARG   B 217 ? 0.355085  0.385283 0.461066 -0.0835427  -0.128188   0.0283012   217 ARG   B CZ   
4073 N  NH1  . ARG   B 217 ? 0.35772   0.353694 0.450532 -0.0979258  -0.157042   0.00099977  217 ARG   B NH1  
4074 N  NH2  . ARG   B 217 ? 0.359784  0.38339  0.481089 -0.0745683  -0.116679   0.0340981   217 ARG   B NH2  
4075 N  N    . TRP   B 218 ? 0.304897  0.288058 0.255027 0.0102547   -0.108214   -0.0137411  218 TRP   B N    
4076 C  CA   . TRP   B 218 ? 0.319028  0.275299 0.239368 0.015844    -0.0947277  -0.0295285  218 TRP   B CA   
4077 C  C    . TRP   B 218 ? 0.330592  0.257295 0.247528 0.0340596   -0.0902335  -0.0420299  218 TRP   B C    
4078 O  O    . TRP   B 218 ? 0.402681  0.269357 0.271126 0.0595821   -0.0857488  -0.0531299  218 TRP   B O    
4079 C  CB   . TRP   B 218 ? 0.308478  0.300115 0.230641 0.0186246   -0.0698224  -0.0349755  218 TRP   B CB   
4080 C  CG   . TRP   B 218 ? 0.298388  0.312495 0.227739 0.0125795   -0.0452148  -0.0416326  218 TRP   B CG   
4081 C  CD1  . TRP   B 218 ? 0.293943  0.317205 0.231334 0.0146274   -0.0402702  -0.0429921  218 TRP   B CD1  
4082 C  CD2  . TRP   B 218 ? 0.285716  0.338664 0.223496 0.0207744   -0.0196427  -0.0463389  218 TRP   B CD2  
4083 N  NE1  . TRP   B 218 ? 0.299502  0.320825 0.230448 0.00512009  -0.0186563  -0.054844   218 TRP   B NE1  
4084 C  CE2  . TRP   B 218 ? 0.288434  0.348693 0.221867 0.00842167  -0.0117808  -0.0434339  218 TRP   B CE2  
4085 C  CE3  . TRP   B 218 ? 0.299781  0.354566 0.239772 0.0273552   -0.00986518 -0.0386826  218 TRP   B CE3  
4086 C  CZ2  . TRP   B 218 ? 0.295973  0.358672 0.21265  -0.00234007 -0.00218842 -0.0354451  218 TRP   B CZ2  
4087 C  CZ3  . TRP   B 218 ? 0.303494  0.374175 0.222784 0.0228187   -0.00639879 -0.0330014  218 TRP   B CZ3  
4088 C  CH2  . TRP   B 218 ? 0.293661  0.379675 0.215733 0.00595268  0.00253504  -0.0238108  218 TRP   B CH2  
4089 N  N    . PHE   B 219 ? 0.300705  0.23815  0.24369  0.0452596   -0.0932414  -0.0399354  219 PHE   B N    
4090 C  CA   . PHE   B 219 ? 0.28709   0.22212  0.239697 0.0482836   -0.0907518  -0.0478142  219 PHE   B CA   
4091 C  C    . PHE   B 219 ? 0.295997  0.208039 0.249306 0.0583141   -0.105781   -0.0459244  219 PHE   B C    
4092 O  O    . PHE   B 219 ? 0.305774  0.233678 0.252885 0.0783854   -0.113935   -0.0518139  219 PHE   B O    
4093 C  CB   . PHE   B 219 ? 0.271945  0.209397 0.242123 0.0414219   -0.0830279  -0.0417594  219 PHE   B CB   
4094 C  CG   . PHE   B 219 ? 0.256526  0.196795 0.237298 0.0310565   -0.0794626  -0.0407156  219 PHE   B CG   
4095 C  CD1  . PHE   B 219 ? 0.252326  0.192998 0.24741  0.0287553   -0.0729264  -0.0402749  219 PHE   B CD1  
4096 C  CD2  . PHE   B 219 ? 0.251011  0.18482  0.237971 0.0200671   -0.0662608  -0.0355114  219 PHE   B CD2  
4097 C  CE1  . PHE   B 219 ? 0.2453    0.188116 0.240433 0.00885959  -0.0712872  -0.052273   219 PHE   B CE1  
4098 C  CE2  . PHE   B 219 ? 0.25414   0.185609 0.230347 0.0212072   -0.0707009  -0.0454004  219 PHE   B CE2  
4099 C  CZ   . PHE   B 219 ? 0.236847  0.190659 0.252103 0.0131543   -0.0716987  -0.0467278  219 PHE   B CZ   
4100 N  N    . LEU   B 220 ? 0.300514  0.206571 0.267244 0.0574163   -0.11424    -0.0485763  220 LEU   B N    
4101 C  CA   . LEU   B 220 ? 0.311672  0.213224 0.270483 0.0533109   -0.105687   -0.0458495  220 LEU   B CA   
4102 C  C    . LEU   B 220 ? 0.328649  0.215013 0.282674 0.044799    -0.0894195  -0.0510404  220 LEU   B C    
4103 O  O    . LEU   B 220 ? 0.370906  0.234105 0.300421 0.0513816   -0.0750582  -0.0624743  220 LEU   B O    
4104 C  CB   . LEU   B 220 ? 0.317171  0.222867 0.283427 0.0476195   -0.111195   -0.046447   220 LEU   B CB   
4105 C  CG   . LEU   B 220 ? 0.300989  0.23509  0.294266 0.0563408   -0.113239   -0.0451031  220 LEU   B CG   
4106 C  CD1  . LEU   B 220 ? 0.302015  0.258133 0.298259 0.0428866   -0.116951   -0.046972   220 LEU   B CD1  
4107 C  CD2  . LEU   B 220 ? 0.288373  0.226984 0.294298 0.052932    -0.112306   -0.0465248  220 LEU   B CD2  
4108 N  N    . ASN   B 221 ? 0.313938  0.221229 0.271893 0.0307286   -0.0882716  -0.0501773  221 ASN   B N    
4109 C  CA   . ASN   B 221 ? 0.277725  0.209508 0.27088  0.010856    -0.0804483  -0.0443833  221 ASN   B CA   
4110 C  C    . ASN   B 221 ? 0.242095  0.209393 0.255746 0.0128706   -0.071481   -0.0438864  221 ASN   B C    
4111 O  O    . ASN   B 221 ? 0.241852  0.250572 0.291174 0.0297018   -0.0667973  -0.0605231  221 ASN   B O    
4112 C  CB   . ASN   B 221 ? 0.281251  0.211066 0.271268 -0.00876916 -0.0819184  -0.0261889  221 ASN   B CB   
4113 C  CG   . ASN   B 221 ? 0.29216   0.216802 0.275521 -0.0264316  -0.0838219  -0.0164315  221 ASN   B CG   
4114 O  OD1  . ASN   B 221 ? 0.281377  0.233702 0.268947 -0.0233115  -0.094781   0.00225264  221 ASN   B OD1  
4115 N  ND2  . ASN   B 221 ? 0.298333  0.241579 0.287429 -0.0416397  -0.084096   -0.0149642  221 ASN   B ND2  
4116 N  N    . ARG   B 222 ? 0.22094   0.208839 0.243936 0.00702789  -0.0550751  -0.042754   222 ARG   B N    
4117 C  CA   . ARG   B 222 ? 0.20878   0.205504 0.240186 0.00963956  -0.0403168  -0.0421254  222 ARG   B CA   
4118 C  C    . ARG   B 222 ? 0.20807   0.195106 0.241769 0.0110875   -0.0369127  -0.039471   222 ARG   B C    
4119 O  O    . ARG   B 222 ? 0.197498  0.222115 0.260837 0.015515    -0.0454804  -0.0284755  222 ARG   B O    
4120 C  CB   . ARG   B 222 ? 0.216046  0.202215 0.238126 0.00467732  -0.0346529  -0.0388775  222 ARG   B CB   
4121 C  CG   . ARG   B 222 ? 0.228875  0.206929 0.247328 0.00783829  -0.0258767  -0.0412712  222 ARG   B CG   
4122 C  CD   . ARG   B 222 ? 0.235933  0.219047 0.26683  0.00846524  -0.017497   -0.0398688  222 ARG   B CD   
4123 N  NE   . ARG   B 222 ? 0.234132  0.237362 0.265733 0.00790713  -0.0143839  -0.034919   222 ARG   B NE   
4124 C  CZ   . ARG   B 222 ? 0.212317  0.233052 0.254548 0.00757416  -0.0162012  -0.0364267  222 ARG   B CZ   
4125 N  NH1  . ARG   B 222 ? 0.202314  0.238415 0.224417 0.0133177   -0.025747   -0.0370969  222 ARG   B NH1  
4126 N  NH2  . ARG   B 222 ? 0.227831  0.257811 0.261854 0.00709011  -0.0118525  -0.0328746  222 ARG   B NH2  
4127 N  N    . PHE   B 223 ? 0.210964  0.188843 0.220301 0.00634176  -0.0359445  -0.0312761  223 PHE   B N    
4128 C  CA   . PHE   B 223 ? 0.206804  0.184342 0.23716  0.00545416  -0.0428165  -0.023269   223 PHE   B CA   
4129 C  C    . PHE   B 223 ? 0.250279  0.18804  0.231288 0.0201252   -0.0540699  -0.0300555  223 PHE   B C    
4130 O  O    . PHE   B 223 ? 0.262716  0.191062 0.228791 0.0167628   -0.0454957  -0.0212752  223 PHE   B O    
4131 C  CB   . PHE   B 223 ? 0.200944  0.209282 0.263462 -0.00021531 -0.0364146  -0.00820675 223 PHE   B CB   
4132 C  CG   . PHE   B 223 ? 0.185807  0.230101 0.276731 -0.00269418 -0.0221215  0.00922565  223 PHE   B CG   
4133 C  CD1  . PHE   B 223 ? 0.174072  0.230961 0.286445 0.00622357  -0.0106195  0.0147086   223 PHE   B CD1  
4134 C  CD2  . PHE   B 223 ? 0.181967  0.241795 0.302541 -0.00106696 -0.0137321  0.0234197   223 PHE   B CD2  
4135 C  CE1  . PHE   B 223 ? 0.188853  0.247625 0.291894 0.00516038  -0.00273347 0.0222959   223 PHE   B CE1  
4136 C  CE2  . PHE   B 223 ? 0.193142  0.260487 0.300165 0.00370239  0.00087861  0.0302644   223 PHE   B CE2  
4137 C  CZ   . PHE   B 223 ? 0.183536  0.257813 0.294621 0.010749    0.00929432  0.0278822   223 PHE   B CZ   
4138 N  N    . THR   B 224 ? 0.301004  0.188586 0.23915  0.0226426   -0.0652924  -0.0340365  224 THR   B N    
4139 C  CA   . THR   B 224 ? 0.331094  0.228094 0.250173 0.0184383   -0.0787882  -0.0375416  224 THR   B CA   
4140 C  C    . THR   B 224 ? 0.341822  0.256135 0.265304 0.0142165   -0.0943119  -0.0370656  224 THR   B C    
4141 O  O    . THR   B 224 ? 0.378388  0.299941 0.279113 0.0474374   -0.119799   -0.0658964  224 THR   B O    
4142 C  CB   . THR   B 224 ? 0.347608  0.23302  0.282961 0.00367143  -0.0820901  -0.0382696  224 THR   B CB   
4143 O  OG1  . THR   B 224 ? 0.377137  0.284055 0.294034 0.00439071  -0.0455918  -0.0436581  224 THR   B OG1  
4144 C  CG2  . THR   B 224 ? 0.336957  0.230874 0.281593 -0.00053217 -0.0928424  -0.0324762  224 THR   B CG2  
4145 N  N    . THR   B 225 ? 0.339718  0.246065 0.256901 -0.0031395  -0.0936073  -0.0150104  225 THR   B N    
4146 C  CA   . THR   B 225 ? 0.341791  0.268337 0.258693 -0.00025132 -0.103675   -0.00225053 225 THR   B CA   
4147 C  C    . THR   B 225 ? 0.344262  0.266957 0.268516 -0.0210492  -0.099571   0.0194581   225 THR   B C    
4148 O  O    . THR   B 225 ? 0.362803  0.313706 0.280952 -0.0455728  -0.10607    0.0597813   225 THR   B O    
4149 C  CB   . THR   B 225 ? 0.329554  0.291821 0.257425 -0.00078651 -0.10377    -0.00054005 225 THR   B CB   
4150 O  OG1  . THR   B 225 ? 0.344058  0.365678 0.293503 0.0326449   -0.108456   -0.0201985  225 THR   B OG1  
4151 C  CG2  . THR   B 225 ? 0.337643  0.289599 0.272145 -0.00667049 -0.090979   -0.00215371 225 THR   B CG2  
4152 N  N    . THR   B 226 ? 0.369326  0.285645 0.270706 -0.0222775  -0.11058    0.0288945   226 THR   B N    
4153 C  CA   . THR   B 226 ? 0.385044  0.26306  0.278688 -0.0446904  -0.103895   0.0284676   226 THR   B CA   
4154 C  C    . THR   B 226 ? 0.413324  0.24193  0.253631 -0.0314181  -0.102703   0.0412421   226 THR   B C    
4155 O  O    . THR   B 226 ? 0.404717  0.2466   0.267167 -0.0497246  -0.093914   0.0233566   226 THR   B O    
4156 C  CB   . THR   B 226 ? 0.398783  0.250902 0.3026   -0.0469779  -0.105096   0.0297356   226 THR   B CB   
4157 O  OG1  . THR   B 226 ? 0.399332  0.254986 0.308321 -0.047137   -0.0964622  0.0227042   226 THR   B OG1  
4158 C  CG2  . THR   B 226 ? 0.40532   0.265793 0.331465 -0.0549405  -0.103582   0.0124513   226 THR   B CG2  
4159 N  N    . LEU   B 227 ? 0.414889  0.253897 0.25602  -0.0271586  -0.106961   0.0546776   227 LEU   B N    
4160 C  CA   . LEU   B 227 ? 0.449332  0.249748 0.271969 -0.0144753  -0.106448   0.0473229   227 LEU   B CA   
4161 C  C    . LEU   B 227 ? 0.449149  0.253503 0.307465 -0.00146313 -0.114576   0.0352902   227 LEU   B C    
4162 O  O    . LEU   B 227 ? 0.481551  0.250313 0.309248 -0.0069073  -0.126867   0.0392321   227 LEU   B O    
4163 C  CB   . LEU   B 227 ? 0.472174  0.287108 0.288017 -0.0218847  -0.0962596  0.0404288   227 LEU   B CB   
4164 C  CG   . LEU   B 227 ? 0.48288   0.294472 0.299959 -0.0291518  -0.0935178  0.0382861   227 LEU   B CG   
4165 C  CD1  . LEU   B 227 ? 0.491854  0.286504 0.322915 -0.0192792  -0.0936294  0.0359516   227 LEU   B CD1  
4166 C  CD2  . LEU   B 227 ? 0.493143  0.327158 0.317445 -0.0337511  -0.0846092  0.0234725   227 LEU   B CD2  
4167 N  N    A ASN   B 228 ? 0.444638  0.258091 0.298841 0.0017769   -0.12711    0.0319375   228 ASN   B N    
4168 N  N    B ASN   B 228 ? 0.443931  0.26344  0.309473 0.00369512  -0.124496   0.0312547   228 ASN   B N    
4169 C  CA   A ASN   B 228 ? 0.441797  0.265149 0.327842 0.014109    -0.129986   0.0317084   228 ASN   B CA   
4170 C  CA   B ASN   B 228 ? 0.441918  0.285592 0.344396 0.0130291   -0.1255     0.0257951   228 ASN   B CA   
4171 C  C    A ASN   B 228 ? 0.431523  0.249868 0.330433 0.0204471   -0.136123   0.027643    228 ASN   B C    
4172 C  C    B ASN   B 228 ? 0.433727  0.254045 0.340503 0.0173489   -0.132077   0.0210751   228 ASN   B C    
4173 O  O    A ASN   B 228 ? 0.419132  0.284223 0.354599 0.0135097   -0.139918   0.0235631   228 ASN   B O    
4174 O  O    B ASN   B 228 ? 0.433421  0.269336 0.372021 0.0105826   -0.125756   0.0115803   228 ASN   B O    
4175 C  CB   A ASN   B 228 ? 0.443137  0.278729 0.34103  0.0242755   -0.12853    0.040845    228 ASN   B CB   
4176 C  CB   B ASN   B 228 ? 0.440306  0.308921 0.368697 0.0262536   -0.124371   0.0408404   228 ASN   B CB   
4177 C  CG   A ASN   B 228 ? 0.461949  0.302793 0.352385 0.0201499   -0.120963   0.0406134   228 ASN   B CG   
4178 C  CG   B ASN   B 228 ? 0.446976  0.359257 0.402924 0.0273541   -0.119986   0.0392944   228 ASN   B CG   
4179 O  OD1  A ASN   B 228 ? 0.485701  0.317759 0.354813 0.024014    -0.117303   0.0388423   228 ASN   B OD1  
4180 O  OD1  B ASN   B 228 ? 0.462925  0.387939 0.425198 0.0266761   -0.12794    0.0361414   228 ASN   B OD1  
4181 N  ND2  A ASN   B 228 ? 0.469772  0.306766 0.372972 0.0181446   -0.118522   0.0460159   228 ASN   B ND2  
4182 N  ND2  B ASN   B 228 ? 0.438077  0.374857 0.417953 0.0317078   -0.114399   0.0473185   228 ASN   B ND2  
4183 N  N    . ASP   B 229 ? 0.435132  0.261773 0.342192 0.0175077   -0.131546   0.0195307   229 ASP   B N    
4184 C  CA   . ASP   B 229 ? 0.443013  0.26748  0.347188 0.0160263   -0.130316   0.0167182   229 ASP   B CA   
4185 C  C    . ASP   B 229 ? 0.426411  0.272779 0.349851 0.00863455  -0.115228   0.0252293   229 ASP   B C    
4186 O  O    . ASP   B 229 ? 0.4164    0.268392 0.367034 0.00164058  -0.102852   0.0188922   229 ASP   B O    
4187 C  CB   . ASP   B 229 ? 0.48287   0.290097 0.390179 0.0218202   -0.130899   -0.010277   229 ASP   B CB   
4188 C  CG   . ASP   B 229 ? 0.521552  0.311184 0.45094  0.0309721   -0.131363   -0.0208146  229 ASP   B CG   
4189 O  OD1  . ASP   B 229 ? 0.575703  0.348178 0.518305 0.0778339   -0.148448   -0.00111161 229 ASP   B OD1  
4190 O  OD2  . ASP   B 229 ? 0.54624   0.35248  0.522037 0.0198772   -0.118888   -0.062015   229 ASP   B OD2  
4191 N  N    . PHE   B 230 ? 0.398696  0.242942 0.322434 -0.00020588 -0.125725   0.0302151   230 PHE   B N    
4192 C  CA   . PHE   B 230 ? 0.389141  0.244132 0.308852 -0.0062923  -0.135051   0.0251849   230 PHE   B CA   
4193 C  C    . PHE   B 230 ? 0.361773  0.232834 0.327726 -0.00457643 -0.128602   0.0296454   230 PHE   B C    
4194 O  O    . PHE   B 230 ? 0.336819  0.271055 0.315684 -0.033752   -0.135631   0.0279102   230 PHE   B O    
4195 C  CB   . PHE   B 230 ? 0.397849  0.236429 0.295547 -0.00824269 -0.145909   0.0226097   230 PHE   B CB   
4196 C  CG   . PHE   B 230 ? 0.393077  0.232055 0.316276 -0.0159818  -0.156016   0.0204236   230 PHE   B CG   
4197 C  CD1  . PHE   B 230 ? 0.432912  0.238767 0.328157 -0.00349171 -0.149485   0.0211055   230 PHE   B CD1  
4198 C  CD2  . PHE   B 230 ? 0.422532  0.244788 0.331788 0.00020572  -0.144648   0.015727    230 PHE   B CD2  
4199 C  CE1  . PHE   B 230 ? 0.44102   0.246151 0.32132  -0.00766254 -0.154961   0.0323741   230 PHE   B CE1  
4200 C  CE2  . PHE   B 230 ? 0.432612  0.23908  0.342813 -0.00618891 -0.147839   0.0195665   230 PHE   B CE2  
4201 C  CZ   . PHE   B 230 ? 0.449373  0.239029 0.349371 0.00129283  -0.143867   0.0318281   230 PHE   B CZ   
4202 N  N    . ASN   B 231 ? 0.323443  0.233065 0.328879 0.0102908   -0.124149   0.0291763   231 ASN   B N    
4203 C  CA   . ASN   B 231 ? 0.326777  0.236965 0.343833 0.0175508   -0.122281   0.0260037   231 ASN   B CA   
4204 C  C    . ASN   B 231 ? 0.328329  0.257402 0.366315 0.0219886   -0.12489    0.0213883   231 ASN   B C    
4205 O  O    . ASN   B 231 ? 0.332507  0.260798 0.394629 0.0220165   -0.130187   0.0305939   231 ASN   B O    
4206 C  CB   . ASN   B 231 ? 0.342959  0.246594 0.3564   0.0254388   -0.10509    0.0308547   231 ASN   B CB   
4207 C  CG   . ASN   B 231 ? 0.341966  0.264147 0.379826 0.0231594   -0.0803166  0.0345368   231 ASN   B CG   
4208 O  OD1  . ASN   B 231 ? 0.372424  0.286364 0.481477 0.0296488   -0.0389694  0.0741827   231 ASN   B OD1  
4209 N  ND2  . ASN   B 231 ? 0.36639   0.26222  0.351013 0.025534    -0.0679986  0.0233264   231 ASN   B ND2  
4210 N  N    . LEU   B 232 ? 0.345561  0.269097 0.381478 0.0280176   -0.132747   0.0120521   232 LEU   B N    
4211 C  CA   . LEU   B 232 ? 0.361063  0.295879 0.387836 0.03738     -0.115131   -0.0146548  232 LEU   B CA   
4212 C  C    . LEU   B 232 ? 0.339253  0.28857  0.359176 0.0386291   -0.122836   -0.0284584  232 LEU   B C    
4213 O  O    . LEU   B 232 ? 0.3397    0.319325 0.355417 0.0341294   -0.128411   -0.0379867  232 LEU   B O    
4214 C  CB   . LEU   B 232 ? 0.392137  0.308061 0.425955 0.0514884   -0.110496   -0.0114579  232 LEU   B CB   
4215 C  CG   . LEU   B 232 ? 0.433345  0.334404 0.449916 0.060532    -0.10566    -0.00494378 232 LEU   B CG   
4216 C  CD1  . LEU   B 232 ? 0.450808  0.338428 0.467542 0.0629654   -0.098767   -0.0145726  232 LEU   B CD1  
4217 C  CD2  . LEU   B 232 ? 0.453706  0.367669 0.45181  0.0613758   -0.113978   0.00296076  232 LEU   B CD2  
4218 N  N    . VAL   B 233 ? 0.352285  0.284856 0.332662 0.0317467   -0.113858   -0.0262053  233 VAL   B N    
4219 C  CA   . VAL   B 233 ? 0.330112  0.288072 0.302218 0.0297647   -0.108318   -0.0330057  233 VAL   B CA   
4220 C  C    . VAL   B 233 ? 0.291215  0.279594 0.305711 0.0300134   -0.0970785  -0.0241124  233 VAL   B C    
4221 O  O    . VAL   B 233 ? 0.273625  0.282326 0.294738 0.0322599   -0.0829988  -0.0329775  233 VAL   B O    
4222 C  CB   . VAL   B 233 ? 0.334165  0.3002   0.321291 0.0275216   -0.114731   -0.0339483  233 VAL   B CB   
4223 C  CG1  . VAL   B 233 ? 0.331843  0.309957 0.323542 0.0222146   -0.112628   -0.0320369  233 VAL   B CG1  
4224 C  CG2  . VAL   B 233 ? 0.338961  0.297647 0.308299 0.0314746   -0.115994   -0.0325488  233 VAL   B CG2  
4225 N  N    . ALA   B 234 ? 0.305638  0.268063 0.320898 0.0191171   -0.085507   -0.0284695  234 ALA   B N    
4226 C  CA   . ALA   B 234 ? 0.293838  0.264171 0.342255 0.034592    -0.0797132  -0.0282977  234 ALA   B CA   
4227 C  C    . ALA   B 234 ? 0.280251  0.265814 0.362621 0.0478379   -0.0684839  -0.0379437  234 ALA   B C    
4228 O  O    . ALA   B 234 ? 0.260939  0.26807  0.355639 0.0528166   -0.0429485  -0.0385439  234 ALA   B O    
4229 C  CB   . ALA   B 234 ? 0.314518  0.259974 0.35289  0.031182    -0.0755339  -0.0179808  234 ALA   B CB   
4230 N  N    . MET   B 235 ? 0.284359  0.282556 0.372758 0.0480801   -0.0824633  -0.0447065  235 MET   B N    
4231 C  CA   . MET   B 235 ? 0.294761  0.319948 0.407866 0.050358    -0.089737   -0.0511024  235 MET   B CA   
4232 C  C    . MET   B 235 ? 0.273574  0.301088 0.395402 0.0592157   -0.0908625  -0.059835   235 MET   B C    
4233 O  O    . MET   B 235 ? 0.24527   0.303656 0.415724 0.0507862   -0.0991264  -0.0540039  235 MET   B O    
4234 C  CB   . MET   B 235 ? 0.341804  0.369425 0.446218 0.0638904   -0.104285   -0.0286307  235 MET   B CB   
4235 C  CG   . MET   B 235 ? 0.363813  0.428578 0.489594 0.0662499   -0.124085   -0.0119183  235 MET   B CG   
4236 S  SD   . MET   B 235 ? 0.452902  0.566269 0.523752 0.0620938   -0.154076   0.0322208   235 MET   B SD   
4237 C  CE   . MET   B 235 ? 0.452936  0.553764 0.5395   0.0748129   -0.153947   0.010928    235 MET   B CE   
4238 N  N    . LYS   B 236 ? 0.264643  0.311362 0.37641  0.0587504   -0.0663321  -0.0610609  236 LYS   B N    
4239 C  CA   . LYS   B 236 ? 0.239415  0.330739 0.390703 0.0684858   -0.0460737  -0.0685447  236 LYS   B CA   
4240 C  C    . LYS   B 236 ? 0.194959  0.323229 0.364629 0.0633257   -0.0111785  -0.0719456  236 LYS   B C    
4241 O  O    . LYS   B 236 ? 0.188368  0.363622 0.398787 0.0407447   0.00278378  -0.0767494  236 LYS   B O    
4242 C  CB   . LYS   B 236 ? 0.270857  0.355498 0.412599 0.0674677   -0.0454467  -0.0901121  236 LYS   B CB   
4243 C  CG   . LYS   B 236 ? 0.330485  0.392724 0.44491  0.05483     -0.0313103  -0.107176   236 LYS   B CG   
4244 C  CD   . LYS   B 236 ? 0.383393  0.431028 0.480429 0.0519576   -0.0277742  -0.136342   236 LYS   B CD   
4245 C  CE   . LYS   B 236 ? 0.419491  0.474104 0.503257 0.0495314   -0.0150837  -0.133745   236 LYS   B CE   
4246 N  NZ   . LYS   B 236 ? 0.468115  0.500192 0.533534 0.0503203   -0.00531605 -0.144384   236 LYS   B NZ   
4247 N  N    . TYR   B 237 ? 0.169153  0.293393 0.32494  0.0427036   -0.012985   -0.0735747  237 TYR   B N    
4248 C  CA   . TYR   B 237 ? 0.178818  0.293095 0.308259 0.0347137   -0.0122767  -0.064862   237 TYR   B CA   
4249 C  C    . TYR   B 237 ? 0.164986  0.287773 0.296345 0.0462995   -0.0180919  -0.0549225  237 TYR   B C    
4250 O  O    . TYR   B 237 ? 0.169572  0.290935 0.296665 0.048277    -0.0156563  -0.0390316  237 TYR   B O    
4251 C  CB   . TYR   B 237 ? 0.184627  0.295062 0.312734 0.0362822   -0.0103104  -0.0647929  237 TYR   B CB   
4252 C  CG   . TYR   B 237 ? 0.200597  0.313298 0.312428 0.029759    -0.0124161  -0.0722055  237 TYR   B CG   
4253 C  CD1  . TYR   B 237 ? 0.219688  0.334429 0.328714 0.0237558   0.00414083  -0.0735871  237 TYR   B CD1  
4254 C  CD2  . TYR   B 237 ? 0.211652  0.322577 0.319632 0.0261915   -0.00562334 -0.0787207  237 TYR   B CD2  
4255 C  CE1  . TYR   B 237 ? 0.235632  0.356534 0.327235 0.024363    0.0119224   -0.0818997  237 TYR   B CE1  
4256 C  CE2  . TYR   B 237 ? 0.233543  0.327528 0.330622 0.0344911   -0.00376477 -0.0841345  237 TYR   B CE2  
4257 C  CZ   . TYR   B 237 ? 0.238233  0.346057 0.32929  0.0338672   0.00731715  -0.0895846  237 TYR   B CZ   
4258 O  OH   . TYR   B 237 ? 0.282038  0.385914 0.334381 0.0381968   0.00767088  -0.109287   237 TYR   B OH   
4259 N  N    A ASN   B 238 ? 0.15856   0.283855 0.291714 0.0393894   -0.0257138  -0.0586316  238 ASN   B N    
4260 N  N    B ASN   B 238 ? 0.159061  0.292665 0.298518 0.0361046   -0.022334   -0.0504201  238 ASN   B N    
4261 C  CA   A ASN   B 238 ? 0.162138  0.276468 0.283333 0.0394205   -0.033535   -0.0566575  238 ASN   B CA   
4262 C  CA   B ASN   B 238 ? 0.162495  0.287458 0.296998 0.0341834   -0.0263471  -0.0466479  238 ASN   B CA   
4263 C  C    A ASN   B 238 ? 0.159882  0.259122 0.257892 0.0400437   -0.0402385  -0.0476763  238 ASN   B C    
4264 C  C    B ASN   B 238 ? 0.161936  0.264468 0.266591 0.0366014   -0.0377206  -0.0395734  238 ASN   B C    
4265 O  O    A ASN   B 238 ? 0.166851  0.258054 0.241036 0.033985    -0.034784   -0.0547596  238 ASN   B O    
4266 O  O    B ASN   B 238 ? 0.166073  0.261404 0.25472  0.0318214   -0.0352919  -0.0386655  238 ASN   B O    
4267 C  CB   A ASN   B 238 ? 0.180389  0.285768 0.29613  0.0354093   -0.0372039  -0.0552376  238 ASN   B CB   
4268 C  CB   B ASN   B 238 ? 0.181994  0.308247 0.324865 0.022778    -0.0235116  -0.0381557  238 ASN   B CB   
4269 C  CG   A ASN   B 238 ? 0.199056  0.30086  0.310487 0.0255434   -0.0451944  -0.0601715  238 ASN   B CG   
4270 C  CG   B ASN   B 238 ? 0.188594  0.340375 0.358346 0.023621    -0.0164563  -0.0321673  238 ASN   B CG   
4271 O  OD1  A ASN   B 238 ? 0.27987   0.33284  0.319345 0.00550411  -0.0636894  -0.0490959  238 ASN   B OD1  
4272 O  OD1  B ASN   B 238 ? 0.215333  0.364628 0.376092 -0.00473762 -0.0240182  -0.0240139  238 ASN   B OD1  
4273 N  ND2  A ASN   B 238 ? 0.205998  0.306806 0.31808  0.0267279   -0.0405064  -0.0506137  238 ASN   B ND2  
4274 N  ND2  B ASN   B 238 ? 0.210904  0.358208 0.376912 0.0147854   -0.00683318 -0.0312482  238 ASN   B ND2  
4275 N  N    . TYR   B 239 ? 0.154161  0.247588 0.250798 0.0440958   -0.0427855  -0.0345041  239 TYR   B N    
4276 C  CA   . TYR   B 239 ? 0.165176  0.239471 0.2366   0.0439716   -0.0367879  -0.0291155  239 TYR   B CA   
4277 C  C    . TYR   B 239 ? 0.171813  0.257736 0.235634 0.0354417   -0.0486433  -0.0186465  239 TYR   B C    
4278 O  O    . TYR   B 239 ? 0.192619  0.28025  0.239731 0.0505618   -0.0464697  -0.00637251 239 TYR   B O    
4279 C  CB   . TYR   B 239 ? 0.16624   0.226264 0.228941 0.0404114   -0.0379953  -0.0222126  239 TYR   B CB   
4280 C  CG   . TYR   B 239 ? 0.169959  0.213206 0.217046 0.0436549   -0.0291666  -0.019286   239 TYR   B CG   
4281 C  CD1  . TYR   B 239 ? 0.172537  0.209493 0.222057 0.0394385   -0.035208   -0.0178791  239 TYR   B CD1  
4282 C  CD2  . TYR   B 239 ? 0.178389  0.225412 0.221241 0.0388213   -0.0400094  -0.0178763  239 TYR   B CD2  
4283 C  CE1  . TYR   B 239 ? 0.184634  0.208742 0.216778 0.0370393   -0.0295711  -0.0186715  239 TYR   B CE1  
4284 C  CE2  . TYR   B 239 ? 0.184205  0.225842 0.221903 0.0367113   -0.0415427  -0.0159996  239 TYR   B CE2  
4285 C  CZ   . TYR   B 239 ? 0.192617  0.212037 0.217001 0.0404146   -0.0402285  -0.014888   239 TYR   B CZ   
4286 O  OH   . TYR   B 239 ? 0.229048  0.240725 0.221127 0.0401      -0.0465024  -0.016348   239 TYR   B OH   
4287 N  N    . GLU   B 240 ? 0.168628  0.268275 0.230991 0.0380009   -0.0510635  -0.010016   240 GLU   B N    
4288 C  CA   . GLU   B 240 ? 0.197667  0.288599 0.233653 0.0279451   -0.054374   -0.00100395 240 GLU   B CA   
4289 C  C    . GLU   B 240 ? 0.197711  0.290288 0.224574 0.0231787   -0.0651307  0.00593878  240 GLU   B C    
4290 O  O    . GLU   B 240 ? 0.197834  0.262791 0.217739 0.0320771   -0.0713252  0.0114515   240 GLU   B O    
4291 C  CB   . GLU   B 240 ? 0.22554   0.297362 0.22122  0.0293865   -0.0474306  -0.00582539 240 GLU   B CB   
4292 C  CG   . GLU   B 240 ? 0.282634  0.316824 0.252772 0.0155276   -0.043409   -0.00667766 240 GLU   B CG   
4293 C  CD   . GLU   B 240 ? 0.314763  0.368507 0.273316 0.00436651  -0.0567042  -0.0098635  240 GLU   B CD   
4294 O  OE1  . GLU   B 240 ? 0.383324  0.460404 0.301145 -0.0123214  -0.0477608  -0.00089531 240 GLU   B OE1  
4295 O  OE2  . GLU   B 240 ? 0.327329  0.37135  0.323249 0.0349458   -0.0358759  -0.00355567 240 GLU   B OE2  
4296 N  N    . PRO   B 241 ? 0.215122  0.311988 0.25332  0.00691942  -0.0893875  0.031131    241 PRO   B N    
4297 C  CA   . PRO   B 241 ? 0.241044  0.312898 0.25831  0.00253685  -0.0853773  0.0377122   241 PRO   B CA   
4298 C  C    . PRO   B 241 ? 0.241699  0.299407 0.259179 0.00340133  -0.0774405  0.033232    241 PRO   B C    
4299 O  O    . PRO   B 241 ? 0.24154   0.33182  0.246221 -0.00613709 -0.0512783  0.0127107   241 PRO   B O    
4300 C  CB   . PRO   B 241 ? 0.255898  0.338577 0.26782  -0.00308014 -0.0915298  0.0491697   241 PRO   B CB   
4301 C  CG   . PRO   B 241 ? 0.25427   0.343794 0.27614  -0.00440449 -0.0980175  0.0467972   241 PRO   B CG   
4302 C  CD   . PRO   B 241 ? 0.245132  0.337596 0.263557 0.00195228  -0.101707   0.0384149   241 PRO   B CD   
4303 N  N    . LEU   B 242 ? 0.25472   0.286548 0.260107 -0.00417656 -0.0726828  0.0447204   242 LEU   B N    
4304 C  CA   . LEU   B 242 ? 0.263993  0.281821 0.254562 -0.0163976  -0.0698638  0.0516454   242 LEU   B CA   
4305 C  C    . LEU   B 242 ? 0.277495  0.280035 0.254839 -0.0188405  -0.0785115  0.0563437   242 LEU   B C    
4306 O  O    . LEU   B 242 ? 0.329741  0.289883 0.259418 -0.0071157  -0.0569424  0.0516744   242 LEU   B O    
4307 C  CB   . LEU   B 242 ? 0.274696  0.265608 0.262472 -0.0200518  -0.0701586  0.0474909   242 LEU   B CB   
4308 C  CG   . LEU   B 242 ? 0.277053  0.27497  0.262879 -0.0319248  -0.0700359  0.0445926   242 LEU   B CG   
4309 C  CD1  . LEU   B 242 ? 0.256866  0.275645 0.252866 -0.0223585  -0.0705541  0.0371721   242 LEU   B CD1  
4310 C  CD2  . LEU   B 242 ? 0.28654   0.271695 0.267174 -0.0285195  -0.0688325  0.0416592   242 LEU   B CD2  
4311 N  N    . THR   B 243 ? 0.265992  0.304474 0.269703 -0.0156648  -0.0731678  0.0767621   243 THR   B N    
4312 C  CA   . THR   B 243 ? 0.277442  0.326412 0.278503 -0.0139232  -0.0627461  0.0932978   243 THR   B CA   
4313 C  C    . THR   B 243 ? 0.292078  0.331207 0.263876 -0.0305134  -0.0616284  0.101852    243 THR   B C    
4314 O  O    . THR   B 243 ? 0.280878  0.345698 0.254356 -0.0189024  -0.0511995  0.0998344   243 THR   B O    
4315 C  CB   . THR   B 243 ? 0.289897  0.337612 0.283851 -0.0196469  -0.0619804  0.0891519   243 THR   B CB   
4316 O  OG1  . THR   B 243 ? 0.281116  0.352909 0.27418  -0.0205474  -0.0402083  0.0877732   243 THR   B OG1  
4317 C  CG2  . THR   B 243 ? 0.301643  0.347616 0.297387 -0.0258391  -0.0661159  0.0783204   243 THR   B CG2  
4318 N  N    . GLN   B 244 ? 0.296599  0.356698 0.290657 -0.0419481  -0.0601941  0.124221    244 GLN   B N    
4319 C  CA   . GLN   B 244 ? 0.306885  0.395078 0.31043  -0.064457   -0.0629736  0.128172    244 GLN   B CA   
4320 C  C    . GLN   B 244 ? 0.296731  0.410876 0.310561 -0.0664959  -0.0455406  0.147024    244 GLN   B C    
4321 O  O    . GLN   B 244 ? 0.261317  0.451224 0.318075 -0.0778363  -0.0277341  0.151176    244 GLN   B O    
4322 C  CB   . GLN   B 244 ? 0.355275  0.406484 0.332254 -0.0749623  -0.0706322  0.141552    244 GLN   B CB   
4323 C  CG   . GLN   B 244 ? 0.372751  0.433764 0.359602 -0.0854706  -0.0801566  0.135886    244 GLN   B CG   
4324 C  CD   . GLN   B 244 ? 0.414691  0.443909 0.353316 -0.0943029  -0.0803612  0.139381    244 GLN   B CD   
4325 O  OE1  . GLN   B 244 ? 0.443146  0.459522 0.389362 -0.105762   -0.0894766  0.118209    244 GLN   B OE1  
4326 N  NE2  . GLN   B 244 ? 0.430588  0.466424 0.392992 -0.103181   -0.0786328  0.151872    244 GLN   B NE2  
4327 N  N    . ASP   B 245 ? 0.28889   0.423043 0.318657 -0.0596681  -0.0391654  0.148707    245 ASP   B N    
4328 C  CA   . ASP   B 245 ? 0.313497  0.441466 0.330042 -0.0465682  -0.0181482  0.149606    245 ASP   B CA   
4329 C  C    . ASP   B 245 ? 0.262028  0.428639 0.315121 -0.0266381  -0.013617   0.141703    245 ASP   B C    
4330 O  O    . ASP   B 245 ? 0.251636  0.467474 0.323601 -0.0139542  -0.00837473 0.136615    245 ASP   B O    
4331 C  CB   . ASP   B 245 ? 0.364832  0.480137 0.347044 -0.054634   -0.01562    0.134871    245 ASP   B CB   
4332 C  CG   . ASP   B 245 ? 0.429176  0.520702 0.414506 -0.0528698  -0.00234749 0.112396    245 ASP   B CG   
4333 O  OD1  . ASP   B 245 ? 0.480216  0.602812 0.465378 -0.0754844  0.0385926   0.0804488   245 ASP   B OD1  
4334 O  OD2  . ASP   B 245 ? 0.518349  0.518814 0.467462 -0.0509463  -0.0052814  0.123842    245 ASP   B OD2  
4335 N  N    . HIS   B 246 ? 0.241945  0.398723 0.280231 -0.0212606  -0.0208237  0.129901    246 HIS   B N    
4336 C  CA   . HIS   B 246 ? 0.246043  0.385466 0.272224 -0.0261464  -0.0263046  0.120418    246 HIS   B CA   
4337 C  C    . HIS   B 246 ? 0.244976  0.395226 0.262141 -0.040793   -0.0315139  0.13423     246 HIS   B C    
4338 O  O    . HIS   B 246 ? 0.239104  0.437808 0.276024 -0.0351447  -0.0256255  0.136882    246 HIS   B O    
4339 C  CB   . HIS   B 246 ? 0.227713  0.360832 0.250239 -0.0292107  -0.033876   0.102738    246 HIS   B CB   
4340 C  CG   . HIS   B 246 ? 0.238556  0.356553 0.254405 -0.019351   -0.0389563  0.0817185   246 HIS   B CG   
4341 N  ND1  . HIS   B 246 ? 0.244334  0.34825  0.271559 -0.0265759  -0.0335304  0.065839    246 HIS   B ND1  
4342 C  CD2  . HIS   B 246 ? 0.235722  0.356825 0.250898 -0.0198496  -0.0411392  0.0767224   246 HIS   B CD2  
4343 C  CE1  . HIS   B 246 ? 0.235004  0.361713 0.270145 -0.0248841  -0.0296709  0.0568937   246 HIS   B CE1  
4344 N  NE2  . HIS   B 246 ? 0.230788  0.34772  0.260889 -0.0297529  -0.021132   0.0699736   246 HIS   B NE2  
4345 N  N    . VAL   B 247 ? 0.279749  0.39445  0.286847 -0.0573493  -0.041731   0.137485    247 VAL   B N    
4346 C  CA   . VAL   B 247 ? 0.279405  0.410117 0.320378 -0.0636714  -0.0719661  0.148594    247 VAL   B CA   
4347 C  C    . VAL   B 247 ? 0.301904  0.455621 0.338108 -0.06728    -0.0560145  0.159208    247 VAL   B C    
4348 O  O    . VAL   B 247 ? 0.298275  0.456599 0.332393 -0.0726492  -0.0617109  0.1647      247 VAL   B O    
4349 C  CB   . VAL   B 247 ? 0.30484   0.396845 0.34691  -0.0670269  -0.0903242  0.155712    247 VAL   B CB   
4350 C  CG1  . VAL   B 247 ? 0.304659  0.390895 0.358967 -0.066853   -0.106301   0.158772    247 VAL   B CG1  
4351 C  CG2  . VAL   B 247 ? 0.293268  0.3909   0.355698 -0.0605817  -0.0871837  0.157718    247 VAL   B CG2  
4352 N  N    . ASP   B 248 ? 0.296916  0.516411 0.34204  -0.0643563  -0.0207087  0.185139    248 ASP   B N    
4353 C  CA   . ASP   B 248 ? 0.317166  0.566369 0.362224 -0.055045   0.00144334  0.18902     248 ASP   B CA   
4354 C  C    . ASP   B 248 ? 0.28498   0.592922 0.336847 -0.026809   0.0260725   0.193667    248 ASP   B C    
4355 O  O    . ASP   B 248 ? 0.267672  0.661115 0.377358 -0.0417194  0.0340172   0.199962    248 ASP   B O    
4356 C  CB   . ASP   B 248 ? 0.349526  0.589238 0.36075  -0.0606817  0.0035892   0.202747    248 ASP   B CB   
4357 C  CG   . ASP   B 248 ? 0.380026  0.597918 0.389134 -0.0576645  0.0043634   0.206884    248 ASP   B CG   
4358 O  OD1  . ASP   B 248 ? 0.411071  0.606737 0.390584 -0.0717518  0.00193432  0.205451    248 ASP   B OD1  
4359 O  OD2  . ASP   B 248 ? 0.398782  0.640771 0.400435 -0.0552766  0.00494729  0.227762    248 ASP   B OD2  
4360 N  N    . ILE   B 249 ? 0.288387  0.581951 0.334858 0.00441459  0.0219404   0.158544    249 ILE   B N    
4361 C  CA   . ILE   B 249 ? 0.309187  0.588295 0.308598 0.0382432   0.046358    0.156883    249 ILE   B CA   
4362 C  C    . ILE   B 249 ? 0.295534  0.562797 0.313074 0.0505495   0.038432    0.121688    249 ILE   B C    
4363 O  O    . ILE   B 249 ? 0.290094  0.6247   0.320595 0.0868151   0.0594632   0.126454    249 ILE   B O    
4364 C  CB   . ILE   B 249 ? 0.354819  0.59754  0.321967 0.0310646   0.0368591   0.15399     249 ILE   B CB   
4365 C  CG1  . ILE   B 249 ? 0.380107  0.615198 0.342878 0.0302919   0.0178987   0.148059    249 ILE   B CG1  
4366 C  CG2  . ILE   B 249 ? 0.379981  0.619216 0.338389 0.0361437   0.0335924   0.160433    249 ILE   B CG2  
4367 C  CD1  . ILE   B 249 ? 0.401584  0.613017 0.344802 0.0236806   0.0239463   0.147894    249 ILE   B CD1  
4368 N  N    . LEU   B 250 ? 0.238087  0.519566 0.306483 0.0207696   0.0469299   0.126786    250 LEU   B N    
4369 C  CA   . LEU   B 250 ? 0.261192  0.464935 0.315731 -0.00182596 0.0300356   0.108083    250 LEU   B CA   
4370 C  C    . LEU   B 250 ? 0.244827  0.536665 0.325359 -0.038946   0.032559    0.101956    250 LEU   B C    
4371 O  O    . LEU   B 250 ? 0.226168  0.578691 0.359171 -0.0664811  -0.00570359 0.145992    250 LEU   B O    
4372 C  CB   . LEU   B 250 ? 0.236235  0.370717 0.290222 -0.00702333 0.0321427   0.0990245   250 LEU   B CB   
4373 C  CG   . LEU   B 250 ? 0.245299  0.324403 0.282747 0.00692348  0.0359529   0.0733491   250 LEU   B CG   
4374 C  CD1  . LEU   B 250 ? 0.235178  0.304504 0.290288 -0.00956906 0.0405645   0.063777    250 LEU   B CD1  
4375 C  CD2  . LEU   B 250 ? 0.254     0.30599  0.288815 0.0184501   0.0344784   0.060365    250 LEU   B CD2  
4376 N  N    . GLY   B 251 ? 0.301228  0.517487 0.334945 -0.0499714  0.00635847  0.0960197   251 GLY   B N    
4377 C  CA   . GLY   B 251 ? 0.306944  0.494684 0.336649 -0.0432782  0.0213972   0.0595819   251 GLY   B CA   
4378 C  C    . GLY   B 251 ? 0.302249  0.474734 0.30876  -0.0498881  0.0260279   0.00814314  251 GLY   B C    
4379 O  O    . GLY   B 251 ? 0.330895  0.454271 0.345649 -0.0390294  0.0155143   -0.00100932 251 GLY   B O    
4380 N  N    . PRO   B 252 ? 0.245018  0.462819 0.315349 -0.0527717  0.0542771   0.00491288  252 PRO   B N    
4381 C  CA   . PRO   B 252 ? 0.300889  0.466592 0.353342 -0.052835   0.0253162   -0.0153076  252 PRO   B CA   
4382 C  C    . PRO   B 252 ? 0.280002  0.456987 0.358956 -0.0568418  0.021045    -0.0165906  252 PRO   B C    
4383 O  O    . PRO   B 252 ? 0.28855   0.522316 0.424828 -0.0959413  0.00455067  -0.0328336  252 PRO   B O    
4384 C  CB   . PRO   B 252 ? 0.30906   0.471951 0.35694  -0.0321539  0.0186678   -0.0255858  252 PRO   B CB   
4385 C  CG   . PRO   B 252 ? 0.33788   0.487704 0.376858 -0.0354717  0.0106835   -0.0259154  252 PRO   B CG   
4386 C  CD   . PRO   B 252 ? 0.259874  0.47907  0.340616 -0.0689247  0.022314    -0.0229383  252 PRO   B CD   
4387 N  N    . LEU   B 253 ? 0.261422  0.417755 0.356861 -0.0550362  -0.0105899  0.00104344  253 LEU   B N    
4388 C  CA   . LEU   B 253 ? 0.203799  0.377703 0.358963 -0.0317545  0.037824    -0.00027551 253 LEU   B CA   
4389 C  C    . LEU   B 253 ? 0.244424  0.364308 0.408038 -0.0485863  0.00761634  0.00078859  253 LEU   B C    
4390 O  O    . LEU   B 253 ? 0.252984  0.346613 0.450012 -0.0537685  -0.026563   -0.00874781 253 LEU   B O    
4391 C  CB   . LEU   B 253 ? 0.221772  0.395903 0.330791 -0.0232083  -0.00635782 0.0261369   253 LEU   B CB   
4392 C  CG   . LEU   B 253 ? 0.236401  0.41085  0.294462 0.00507045  -0.00410603 0.0319308   253 LEU   B CG   
4393 C  CD1  . LEU   B 253 ? 0.283774  0.44572  0.305434 9.479e-05   -0.0149533  0.0329244   253 LEU   B CD1  
4394 C  CD2  . LEU   B 253 ? 0.274531  0.447657 0.305362 0.00970355  -0.0205682  0.0390132   253 LEU   B CD2  
4395 N  N    . SER   B 254 ? 0.228968  0.318372 0.374868 -0.046645   5.281e-05   -0.0137536  254 SER   B N    
4396 C  CA   . SER   B 254 ? 0.272072  0.332331 0.370402 -0.028855   -0.00220727 -0.0250332  254 SER   B CA   
4397 C  C    . SER   B 254 ? 0.29977   0.338245 0.384522 -0.0464353  -0.0149715  -0.0486456  254 SER   B C    
4398 O  O    . SER   B 254 ? 0.315744  0.308636 0.417991 -0.0261624  -0.0389139  -0.0569463  254 SER   B O    
4399 C  CB   . SER   B 254 ? 0.283789  0.28614  0.362064 -0.0254248  -0.0203137  -0.0284561  254 SER   B CB   
4400 O  OG   . SER   B 254 ? 0.339943  0.323558 0.372696 0.0084382   0.00774896  -0.0395367  254 SER   B OG   
4401 N  N    . ALA   B 255 ? 0.257012  0.378322 0.422968 -0.0205228  -0.0145951  -0.0806192  255 ALA   B N    
4402 C  CA   . ALA   B 255 ? 0.275507  0.386089 0.431568 -0.0403695  -0.0259354  -0.0539201  255 ALA   B CA   
4403 C  C    . ALA   B 255 ? 0.287502  0.386914 0.446669 -0.043243   -0.0478154  -0.0448985  255 ALA   B C    
4404 O  O    . ALA   B 255 ? 0.286387  0.408158 0.445176 -0.0645559  -0.0319094  -0.0495792  255 ALA   B O    
4405 C  CB   . ALA   B 255 ? 0.299142  0.408106 0.447508 -0.0164951  -0.0112248  -0.0417689  255 ALA   B CB   
4406 N  N    . GLN   B 256 ? 0.262076  0.390583 0.474188 -0.0326146  -0.0686998  -0.0271504  256 GLN   B N    
4407 C  CA   . GLN   B 256 ? 0.281412  0.432176 0.466817 -0.0297385  -0.0777749  -0.012823   256 GLN   B CA   
4408 C  C    . GLN   B 256 ? 0.285167  0.421777 0.454599 -0.0277206  -0.0906932  0.00060804  256 GLN   B C    
4409 O  O    . GLN   B 256 ? 0.259399  0.465494 0.492663 -0.0279139  -0.105606   -0.00678145 256 GLN   B O    
4410 C  CB   . GLN   B 256 ? 0.24949   0.427634 0.485956 -0.0307879  -0.0909296  -0.00052891 256 GLN   B CB   
4411 C  CG   . GLN   B 256 ? 0.262946  0.473435 0.509602 -0.0116889  -0.073095   0.013347    256 GLN   B CG   
4412 C  CD   . GLN   B 256 ? 0.306035  0.48247  0.543219 -0.0228574  -0.0664393  0.00565325  256 GLN   B CD   
4413 O  OE1  . GLN   B 256 ? 0.368578  0.496396 0.548405 -0.0249159  -0.0267575  -0.0336496  256 GLN   B OE1  
4414 N  NE2  . GLN   B 256 ? 0.329736  0.512334 0.57145  -0.0223104  -0.0712986  0.0136809   256 GLN   B NE2  
4415 N  N    . THR   B 257 ? 0.247619  0.431095 0.394808 -0.0373354  -0.112097   0.0101775   257 THR   B N    
4416 C  CA   . THR   B 257 ? 0.30176   0.383601 0.394401 -0.0472083  -0.111691   0.0436702   257 THR   B CA   
4417 C  C    . THR   B 257 ? 0.359466  0.347602 0.396697 -0.105745   -0.117854   0.0172213   257 THR   B C    
4418 O  O    . THR   B 257 ? 0.377182  0.338221 0.402824 -0.085846   -0.124487   0.0437598   257 THR   B O    
4419 C  CB   . THR   B 257 ? 0.290581  0.418282 0.375171 -0.0686952  -0.123294   0.0563874   257 THR   B CB   
4420 O  OG1  . THR   B 257 ? 0.284086  0.409127 0.392861 -0.120887   -0.124561   0.0887213   257 THR   B OG1  
4421 C  CG2  . THR   B 257 ? 0.253364  0.430742 0.350074 -0.0558597  -0.140391   0.0538509   257 THR   B CG2  
4422 N  N    . GLY   B 258 ? 0.362504  0.305017 0.422821 -0.0865341  -0.11097    0.00926872  258 GLY   B N    
4423 C  CA   . GLY   B 258 ? 0.390452  0.302591 0.474576 -0.0793908  -0.0822155  0.00817709  258 GLY   B CA   
4424 C  C    . GLY   B 258 ? 0.414585  0.286174 0.496174 -0.059168   -0.0900028  0.00602665  258 GLY   B C    
4425 O  O    . GLY   B 258 ? 0.459013  0.28266  0.523944 -0.0311318  -0.0405537  0.0130427   258 GLY   B O    
4426 N  N    . ILE   B 259 ? 0.426085  0.300664 0.500554 -0.0649321  -0.131907   0.0462311   259 ILE   B N    
4427 C  CA   . ILE   B 259 ? 0.459066  0.321044 0.473812 -0.0704834  -0.169206   0.0427699   259 ILE   B CA   
4428 C  C    . ILE   B 259 ? 0.475268  0.310616 0.480917 -0.0761372  -0.208667   0.0633993   259 ILE   B C    
4429 O  O    . ILE   B 259 ? 0.484172  0.275624 0.506105 -0.100674   -0.241708   0.0863726   259 ILE   B O    
4430 C  CB   . ILE   B 259 ? 0.461357  0.328189 0.48052  -0.0683593  -0.163576   0.0394157   259 ILE   B CB   
4431 C  CG1  . ILE   B 259 ? 0.493425  0.367877 0.488952 -0.0489629  -0.150974   0.0531079   259 ILE   B CG1  
4432 C  CG2  . ILE   B 259 ? 0.473311  0.317237 0.496943 -0.0834095  -0.143323   0.0232255   259 ILE   B CG2  
4433 C  CD1  . ILE   B 259 ? 0.497438  0.373297 0.492747 -0.0346375  -0.155557   0.0513743   259 ILE   B CD1  
4434 N  N    . ALA   B 260 ? 0.515279  0.298561 0.42196  -0.103864   -0.230386   0.0686872   260 ALA   B N    
4435 C  CA   . ALA   B 260 ? 0.509349  0.27796  0.407096 -0.0883134  -0.221455   0.0549711   260 ALA   B CA   
4436 C  C    . ALA   B 260 ? 0.500154  0.257727 0.370105 -0.0753494  -0.212411   0.0456688   260 ALA   B C    
4437 O  O    . ALA   B 260 ? 0.505167  0.233347 0.34848  -0.0721429  -0.228269   0.038223    260 ALA   B O    
4438 C  CB   . ALA   B 260 ? 0.520104  0.267091 0.390895 -0.0905816  -0.217258   0.0646593   260 ALA   B CB   
4439 N  N    . VAL   B 261 ? 0.484126  0.242515 0.347387 -0.0750132  -0.198166   0.0594511   261 VAL   B N    
4440 C  CA   . VAL   B 261 ? 0.462611  0.237939 0.346728 -0.0589023  -0.182222   0.0419212   261 VAL   B CA   
4441 C  C    . VAL   B 261 ? 0.468404  0.208994 0.340538 -0.041621   -0.190502   0.0175837   261 VAL   B C    
4442 O  O    . VAL   B 261 ? 0.433415  0.195151 0.300925 -0.0169701  -0.181769   0.00430669  261 VAL   B O    
4443 C  CB   . VAL   B 261 ? 0.440248  0.229211 0.331128 -0.0787182  -0.174674   0.0438291   261 VAL   B CB   
4444 C  CG1  . VAL   B 261 ? 0.435662  0.243021 0.335588 -0.0748344  -0.173161   0.0341996   261 VAL   B CG1  
4445 C  CG2  . VAL   B 261 ? 0.439123  0.236459 0.323858 -0.096683   -0.171463   0.0418633   261 VAL   B CG2  
4446 N  N    . LEU   B 262 ? 0.489821  0.218352 0.335827 -0.0321387  -0.201934   0.0254168   262 LEU   B N    
4447 C  CA   . LEU   B 262 ? 0.504781  0.225027 0.348822 -0.015775   -0.20887    0.0187468   262 LEU   B CA   
4448 C  C    . LEU   B 262 ? 0.492874  0.260643 0.367481 0.00246529  -0.197817   0.00134532  262 LEU   B C    
4449 O  O    . LEU   B 262 ? 0.4962    0.262042 0.348808 0.0398759   -0.207592   -0.0279254  262 LEU   B O    
4450 C  CB   . LEU   B 262 ? 0.531345  0.233908 0.35156  -0.0216579  -0.208168   0.0293048   262 LEU   B CB   
4451 C  CG   . LEU   B 262 ? 0.540249  0.255632 0.354726 -0.0206172  -0.208957   0.03351     262 LEU   B CG   
4452 C  CD1  . LEU   B 262 ? 0.543608  0.253708 0.370286 -0.0193582  -0.199746   0.0362925   262 LEU   B CD1  
4453 C  CD2  . LEU   B 262 ? 0.543182  0.265014 0.33853  -0.027074   -0.209258   0.0347112   262 LEU   B CD2  
4454 N  N    . ASP   B 263 ? 0.489015  0.209062 0.349216 -0.010047   -0.191058   -0.00582999 263 ASP   B N    
4455 C  CA   . ASP   B 263 ? 0.471283  0.221379 0.358899 -0.00879681 -0.178006   -0.0179327  263 ASP   B CA   
4456 C  C    . ASP   B 263 ? 0.445778  0.209722 0.308114 0.00238007  -0.177507   -0.0267455  263 ASP   B C    
4457 O  O    . ASP   B 263 ? 0.438249  0.222623 0.319183 0.019803    -0.17565    -0.0387623  263 ASP   B O    
4458 C  CB   . ASP   B 263 ? 0.468293  0.272818 0.396729 -0.0251942  -0.158525   -0.0352767  263 ASP   B CB   
4459 C  CG   . ASP   B 263 ? 0.43576   0.346299 0.412788 -0.0542862  -0.150545   -0.0471341  263 ASP   B CG   
4460 O  OD1  . ASP   B 263 ? 0.452318  0.378381 0.454817 -0.009233   -0.096617   -0.0767853  263 ASP   B OD1  
4461 O  OD2  . ASP   B 263 ? 0.435674  0.382692 0.514267 -0.110753   -0.0493584  -0.0655042  263 ASP   B OD2  
4462 N  N    . MET   B 264 ? 0.438959  0.190096 0.287223 0.0078261   -0.162455   -0.00621843 264 MET   B N    
4463 C  CA   . MET   B 264 ? 0.393314  0.183822 0.269465 0.00338378  -0.149187   -0.00773902 264 MET   B CA   
4464 C  C    . MET   B 264 ? 0.411087  0.167249 0.263996 0.0144359   -0.139563   -0.00581112 264 MET   B C    
4465 O  O    . MET   B 264 ? 0.401521  0.182547 0.261424 0.0210304   -0.122207   -0.00907253 264 MET   B O    
4466 C  CB   . MET   B 264 ? 0.374153  0.192418 0.259255 -0.0063735  -0.136281   -0.00972827 264 MET   B CB   
4467 C  CG   . MET   B 264 ? 0.342198  0.200819 0.267206 -0.00468805 -0.13112    -0.00038463 264 MET   B CG   
4468 S  SD   . MET   B 264 ? 0.306465  0.203607 0.26338  -0.00825801 -0.111282   0.0004935   264 MET   B SD   
4469 C  CE   . MET   B 264 ? 0.310928  0.227118 0.280959 -0.00719891 -0.112336   0.00348968  264 MET   B CE   
4470 N  N    . CYS   B 265 ? 0.420307  0.186253 0.261311 0.0211367   -0.152838   -0.0059206  265 CYS   B N    
4471 C  CA   . CYS   B 265 ? 0.437485  0.185821 0.261266 0.0225796   -0.155521   -0.0139103  265 CYS   B CA   
4472 C  C    . CYS   B 265 ? 0.437721  0.174811 0.270728 0.0280257   -0.145048   -0.0180321  265 CYS   B C    
4473 O  O    . CYS   B 265 ? 0.430851  0.183674 0.272145 0.0283749   -0.154295   -0.034848   265 CYS   B O    
4474 C  CB   . CYS   B 265 ? 0.465046  0.192063 0.270711 0.0178509   -0.166374   -0.00723151 265 CYS   B CB   
4475 S  SG   . CYS   B 265 ? 0.482796  0.218205 0.270084 0.0106081   -0.169598   -0.00911078 265 CYS   B SG   
4476 N  N    . ALA   B 266 ? 0.434861  0.187    0.270103 0.0219487   -0.133782   -0.0279645  266 ALA   B N    
4477 C  CA   . ALA   B 266 ? 0.423906  0.199225 0.278829 0.0341741   -0.134418   -0.0345189  266 ALA   B CA   
4478 C  C    . ALA   B 266 ? 0.385599  0.205539 0.27027  0.0449467   -0.132445   -0.0348484  266 ALA   B C    
4479 O  O    . ALA   B 266 ? 0.431107  0.266052 0.260229 0.0691491   -0.107347   -0.0514922  266 ALA   B O    
4480 C  CB   . ALA   B 266 ? 0.431538  0.207234 0.301687 0.0309601   -0.138044   -0.043094   266 ALA   B CB   
4481 N  N    . SER   B 267 ? 0.344602  0.205825 0.27003  0.0283668   -0.128164   -0.0392751  267 SER   B N    
4482 C  CA   . SER   B 267 ? 0.324077  0.212788 0.252205 0.0252713   -0.113396   -0.0336672  267 SER   B CA   
4483 C  C    . SER   B 267 ? 0.301004  0.204893 0.23294  0.0399845   -0.106936   -0.0314249  267 SER   B C    
4484 O  O    . SER   B 267 ? 0.303348  0.218043 0.235881 0.0436731   -0.0915266  -0.0351354  267 SER   B O    
4485 C  CB   . SER   B 267 ? 0.325582  0.220382 0.257937 0.0234844   -0.109258   -0.0342508  267 SER   B CB   
4486 O  OG   . SER   B 267 ? 0.322194  0.23384  0.256837 0.0116717   -0.0999727  -0.0283427  267 SER   B OG   
4487 N  N    . LEU   B 268 ? 0.302027  0.188551 0.239554 0.0272674   -0.0949624  -0.034267   268 LEU   B N    
4488 C  CA   . LEU   B 268 ? 0.299669  0.188954 0.245806 0.0276387   -0.0887299  -0.034271   268 LEU   B CA   
4489 C  C    . LEU   B 268 ? 0.322096  0.207006 0.272179 0.0433032   -0.0964008  -0.0504377  268 LEU   B C    
4490 O  O    . LEU   B 268 ? 0.279242  0.223574 0.258085 0.0516523   -0.0802955  -0.0711056  268 LEU   B O    
4491 C  CB   . LEU   B 268 ? 0.29461   0.177506 0.226804 0.0172486   -0.0862196  -0.0230394  268 LEU   B CB   
4492 C  CG   . LEU   B 268 ? 0.285039  0.177525 0.226337 0.015847    -0.0758379  -0.0219226  268 LEU   B CG   
4493 C  CD1  . LEU   B 268 ? 0.275505  0.172627 0.225596 0.0115258   -0.0574668  -0.0290565  268 LEU   B CD1  
4494 C  CD2  . LEU   B 268 ? 0.283681  0.188288 0.227001 0.00726447  -0.0815561  -0.0277779  268 LEU   B CD2  
4495 N  N    . LYS   B 269 ? 0.344309  0.2208   0.299318 0.0627472   -0.120782   -0.0585162  269 LYS   B N    
4496 C  CA   . LYS   B 269 ? 0.352464  0.251348 0.338556 0.0621079   -0.122984   -0.0744954  269 LYS   B CA   
4497 C  C    . LYS   B 269 ? 0.320774  0.259059 0.342862 0.0810349   -0.130363   -0.0788302  269 LYS   B C    
4498 O  O    . LYS   B 269 ? 0.316594  0.287701 0.352576 0.0969743   -0.13371    -0.100088   269 LYS   B O    
4499 C  CB   . LYS   B 269 ? 0.382337  0.263777 0.372661 0.0703188   -0.134521   -0.0571087  269 LYS   B CB   
4500 C  CG   . LYS   B 269 ? 0.428363  0.290818 0.411374 0.0752161   -0.119949   -0.0556511  269 LYS   B CG   
4501 C  CD   . LYS   B 269 ? 0.472403  0.31327  0.463313 0.0697699   -0.106719   -0.0366001  269 LYS   B CD   
4502 C  CE   . LYS   B 269 ? 0.499415  0.35095  0.506189 0.0686996   -0.0647316  -0.0466823  269 LYS   B CE   
4503 N  NZ   . LYS   B 269 ? 0.504764  0.356532 0.539574 0.0524345   -0.0512878  -0.0395071  269 LYS   B NZ   
4504 N  N    . GLU   B 270 ? 0.295842  0.261205 0.318757 0.102665    -0.116363   -0.0806849  270 GLU   B N    
4505 C  CA   . GLU   B 270 ? 0.285874  0.268907 0.316225 0.099171    -0.101089   -0.0976433  270 GLU   B CA   
4506 C  C    . GLU   B 270 ? 0.276181  0.282619 0.288725 0.0990604   -0.082248   -0.0874489  270 GLU   B C    
4507 O  O    . GLU   B 270 ? 0.295836  0.319718 0.30622  0.0956366   -0.0724185  -0.0966679  270 GLU   B O    
4508 C  CB   . GLU   B 270 ? 0.281511  0.299954 0.332514 0.0951535   -0.10327    -0.103696   270 GLU   B CB   
4509 C  CG   . GLU   B 270 ? 0.312199  0.325155 0.353864 0.0908126   -0.0980231  -0.102902   270 GLU   B CG   
4510 C  CD   . GLU   B 270 ? 0.33098   0.339885 0.375364 0.097649    -0.100928   -0.0988015  270 GLU   B CD   
4511 O  OE1  . GLU   B 270 ? 0.366796  0.380766 0.40954  0.108662    -0.0691291  -0.104128   270 GLU   B OE1  
4512 O  OE2  . GLU   B 270 ? 0.353189  0.350734 0.390322 0.0846352   -0.10864    -0.0896813  270 GLU   B OE2  
4513 N  N    . LEU   B 271 ? 0.269309  0.267384 0.267189 0.0901302   -0.0700831  -0.0765294  271 LEU   B N    
4514 C  CA   . LEU   B 271 ? 0.250116  0.272639 0.254246 0.0871809   -0.0598156  -0.0634297  271 LEU   B CA   
4515 C  C    . LEU   B 271 ? 0.258176  0.289733 0.298344 0.0808968   -0.0541808  -0.0730806  271 LEU   B C    
4516 O  O    . LEU   B 271 ? 0.256458  0.330344 0.325627 0.077259    -0.048416   -0.0529559  271 LEU   B O    
4517 C  CB   . LEU   B 271 ? 0.23037   0.279847 0.232578 0.0782544   -0.0528994  -0.0523146  271 LEU   B CB   
4518 C  CG   . LEU   B 271 ? 0.230502  0.294699 0.234796 0.0637655   -0.0534142  -0.0349854  271 LEU   B CG   
4519 C  CD1  . LEU   B 271 ? 0.235589  0.281566 0.231579 0.0745915   -0.0550207  -0.0306157  271 LEU   B CD1  
4520 C  CD2  . LEU   B 271 ? 0.236756  0.321532 0.240805 0.05352     -0.0417751  -0.0221971  271 LEU   B CD2  
4521 N  N    . LEU   B 272 ? 0.264192  0.290671 0.299481 0.0876443   -0.065705   -0.0951035  272 LEU   B N    
4522 C  CA   . LEU   B 272 ? 0.250832  0.305794 0.317616 0.0799084   -0.0555594  -0.110478   272 LEU   B CA   
4523 C  C    . LEU   B 272 ? 0.261238  0.321803 0.356727 0.0931277   -0.0574432  -0.126566   272 LEU   B C    
4524 O  O    . LEU   B 272 ? 0.264084  0.379218 0.382059 0.0904875   -0.0520036  -0.115318   272 LEU   B O    
4525 C  CB   . LEU   B 272 ? 0.245648  0.301349 0.3228   0.0778362   -0.0678917  -0.103516   272 LEU   B CB   
4526 C  CG   . LEU   B 272 ? 0.251602  0.299674 0.306795 0.0740231   -0.0674125  -0.101177   272 LEU   B CG   
4527 C  CD1  . LEU   B 272 ? 0.251691  0.308324 0.311044 0.0694305   -0.0752602  -0.0986052  272 LEU   B CD1  
4528 C  CD2  . LEU   B 272 ? 0.257503  0.301352 0.308463 0.0717778   -0.0614342  -0.0986751  272 LEU   B CD2  
4529 N  N    . GLN   B 273 ? 0.290721  0.339182 0.380738 0.0958395   -0.0751846  -0.150682   273 GLN   B N    
4530 C  CA   . GLN   B 273 ? 0.308336  0.349998 0.415559 0.103999    -0.0588892  -0.146725   273 GLN   B CA   
4531 C  C    . GLN   B 273 ? 0.3112    0.401306 0.423544 0.101506    -0.0259794  -0.143861   273 GLN   B C    
4532 O  O    . GLN   B 273 ? 0.312728  0.456076 0.468454 0.107465    -0.00897785 -0.136037   273 GLN   B O    
4533 C  CB   . GLN   B 273 ? 0.320274  0.338438 0.435192 0.0914439   -0.0810106  -0.149002   273 GLN   B CB   
4534 C  CG   . GLN   B 273 ? 0.332604  0.31844  0.453129 0.0926035   -0.100111   -0.143467   273 GLN   B CG   
4535 C  CD   . GLN   B 273 ? 0.374019  0.306258 0.46666  0.0827694   -0.111552   -0.151013   273 GLN   B CD   
4536 O  OE1  . GLN   B 273 ? 0.381486  0.312146 0.492937 0.0682874   -0.118162   -0.158503   273 GLN   B OE1  
4537 N  NE2  . GLN   B 273 ? 0.394779  0.284902 0.501228 0.0657481   -0.129392   -0.145639   273 GLN   B NE2  
4538 N  N    . ASN   B 274 ? 0.306     0.391216 0.418625 0.104372    -0.0124195  -0.154157   274 ASN   B N    
4539 C  CA   . ASN   B 274 ? 0.317671  0.408963 0.417626 0.0886301   0.00466867  -0.142575   274 ASN   B CA   
4540 C  C    . ASN   B 274 ? 0.336455  0.415397 0.399554 0.0724817   0.0378013   -0.121064   274 ASN   B C    
4541 O  O    . ASN   B 274 ? 0.365873  0.467979 0.410474 0.0553824   0.0662534   -0.112869   274 ASN   B O    
4542 C  CB   . ASN   B 274 ? 0.35545   0.428866 0.425975 0.0758702   0.00211475  -0.156052   274 ASN   B CB   
4543 C  CG   . ASN   B 274 ? 0.356943  0.43698  0.436342 0.0951506   0.00536064  -0.173086   274 ASN   B CG   
4544 O  OD1  . ASN   B 274 ? 0.412187  0.501446 0.485485 0.124417    0.0308016   -0.173206   274 ASN   B OD1  
4545 N  ND2  . ASN   B 274 ? 0.394853  0.444367 0.455126 0.0948003   -0.0201152  -0.169874   274 ASN   B ND2  
4546 N  N    . GLY   B 275 ? 0.312425  0.409559 0.368433 0.0623035   0.0500907   -0.102271   275 GLY   B N    
4547 C  CA   . GLY   B 275 ? 0.322348  0.395369 0.358123 0.0466659   0.0677848   -0.0824204  275 GLY   B CA   
4548 C  C    . GLY   B 275 ? 0.308959  0.39625  0.356398 0.0271938   0.0756944   -0.0689519  275 GLY   B C    
4549 O  O    . GLY   B 275 ? 0.321544  0.378524 0.358749 0.0387917   0.0621576   -0.0402551  275 GLY   B O    
4550 N  N    . MET   B 276 ? 0.312634  0.415543 0.352133 0.0108432   0.0902058   -0.051008   276 MET   B N    
4551 C  CA   . MET   B 276 ? 0.309128  0.428656 0.373621 0.00545651  0.0888632   -0.0373756  276 MET   B CA   
4552 C  C    . MET   B 276 ? 0.311133  0.472084 0.374487 -0.0065945  0.0958397   -0.0298811  276 MET   B C    
4553 O  O    . MET   B 276 ? 0.302099  0.464815 0.373914 -0.00284398 0.116904    -0.011691   276 MET   B O    
4554 C  CB   . MET   B 276 ? 0.33446   0.421971 0.383156 -0.00485647 0.0631867   -0.0296622  276 MET   B CB   
4555 C  CG   . MET   B 276 ? 0.346101  0.399116 0.368908 -0.00779056 0.0283518   -0.0335604  276 MET   B CG   
4556 S  SD   . MET   B 276 ? 0.309945  0.385924 0.335996 -0.0319672  -0.00474983 -0.0247135  276 MET   B SD   
4557 C  CE   . MET   B 276 ? 0.352601  0.352812 0.327424 -0.0314654  -0.00548682 -0.0338253  276 MET   B CE   
4558 N  N    . ASN   B 277 ? 0.313181  0.525408 0.372887 0.00394351  0.105151    -0.0497151  277 ASN   B N    
4559 C  CA   . ASN   B 277 ? 0.346054  0.575108 0.377446 0.00810096  0.100171    -0.0343692  277 ASN   B CA   
4560 C  C    . ASN   B 277 ? 0.325025  0.573378 0.338647 0.00495979  0.111022    -0.03013    277 ASN   B C    
4561 O  O    . ASN   B 277 ? 0.335047  0.620115 0.374419 0.0131748   0.0919707   -0.0396538  277 ASN   B O    
4562 C  CB   . ASN   B 277 ? 0.40849   0.605606 0.439853 0.00915886  0.0898229   -0.0434754  277 ASN   B CB   
4563 C  CG   . ASN   B 277 ? 0.453855  0.665844 0.496551 0.0187682   0.082556    -0.0306292  277 ASN   B CG   
4564 O  OD1  . ASN   B 277 ? 0.488072  0.740054 0.574209 0.0476365   0.108425    -0.0427875  277 ASN   B OD1  
4565 N  ND2  . ASN   B 277 ? 0.477017  0.702803 0.501782 0.00848485  0.0680779   -0.0178786  277 ASN   B ND2  
4566 N  N    . GLY   B 278 ? 0.317998  0.565195 0.321681 0.00329671  0.115966    -0.0109846  278 GLY   B N    
4567 C  CA   . GLY   B 278 ? 0.35431   0.559568 0.314021 -0.0111365  0.112956    0.00437754  278 GLY   B CA   
4568 C  C    . GLY   B 278 ? 0.355441  0.533705 0.309606 -0.0240274  0.0914688   0.0153132   278 GLY   B C    
4569 O  O    . GLY   B 278 ? 0.38827   0.549948 0.325512 -0.0362319  0.0834119   0.0411264   278 GLY   B O    
4570 N  N    . ARG   B 279 ? 0.358375  0.48687  0.282754 -0.0180562  0.0745186   0.00868329  279 ARG   B N    
4571 C  CA   . ARG   B 279 ? 0.33852   0.452105 0.255741 -0.0218976  0.0337563   -0.00348264 279 ARG   B CA   
4572 C  C    . ARG   B 279 ? 0.290755  0.407538 0.247657 -0.0214442  0.0223482   0.0106668   279 ARG   B C    
4573 O  O    . ARG   B 279 ? 0.280264  0.436321 0.282086 -0.01145    0.00864113  -0.00291879 279 ARG   B O    
4574 C  CB   . ARG   B 279 ? 0.380202  0.457509 0.262528 -0.0187585  0.0437411   -0.00347365 279 ARG   B CB   
4575 C  CG   . ARG   B 279 ? 0.426529  0.474936 0.295043 -0.0171432  0.040185    -0.0288266  279 ARG   B CG   
4576 C  CD   . ARG   B 279 ? 0.46436   0.485555 0.304611 -0.0125714  0.0427461   -0.028327   279 ARG   B CD   
4577 N  NE   . ARG   B 279 ? 0.509562  0.513347 0.338928 -0.00410469 0.0244474   -0.0289607  279 ARG   B NE   
4578 C  CZ   . ARG   B 279 ? 0.554159  0.52751  0.399688 0.00764786  0.00627537  -0.0538433  279 ARG   B CZ   
4579 N  NH1  . ARG   B 279 ? 0.575249  0.533741 0.396132 0.00135729  0.00808821  -0.0736606  279 ARG   B NH1  
4580 N  NH2  . ARG   B 279 ? 0.564773  0.548596 0.414408 0.0196122   -0.00314577 -0.0576095  279 ARG   B NH2  
4581 N  N    . THR   B 280 ? 0.25991   0.347381 0.216352 -0.031657   0.00412669  0.0162434   280 THR   B N    
4582 C  CA   . THR   B 280 ? 0.250214  0.326764 0.201664 -0.0377089  0.00318475  0.0239211   280 THR   B CA   
4583 C  C    . THR   B 280 ? 0.237441  0.279905 0.196085 -0.0341945  -0.00342818 0.0102016   280 THR   B C    
4584 O  O    . THR   B 280 ? 0.255198  0.28887  0.204958 -0.0336719  -0.00641054 0.00685289  280 THR   B O    
4585 C  CB   . THR   B 280 ? 0.279067  0.342563 0.210415 -0.0410499  -0.000506   0.036005    280 THR   B CB   
4586 O  OG1  . THR   B 280 ? 0.296352  0.352354 0.226891 -0.0409425  -0.0136738  0.0393719   280 THR   B OG1  
4587 C  CG2  . THR   B 280 ? 0.300669  0.354347 0.225271 -0.0521579  0.00328009  0.0508765   280 THR   B CG2  
4588 N  N    . ILE   B 281 ? 0.206383  0.254268 0.185719 -0.0223459  -0.0164863  0.00901071  281 ILE   B N    
4589 C  CA   . ILE   B 281 ? 0.188082  0.247515 0.187473 -0.0153949  -0.0243359  0.00752389  281 ILE   B CA   
4590 C  C    . ILE   B 281 ? 0.192197  0.239232 0.194273 -0.0114213  -0.0281818  0.0160298   281 ILE   B C    
4591 O  O    . ILE   B 281 ? 0.191745  0.23577  0.192558 -0.01455    -0.041049   0.0194538   281 ILE   B O    
4592 C  CB   . ILE   B 281 ? 0.182824  0.246286 0.18535  -0.0115496  -0.016508   0.0021433   281 ILE   B CB   
4593 C  CG1  . ILE   B 281 ? 0.199006  0.252789 0.194042 -0.00646305 -0.0120397  -0.00299562 281 ILE   B CG1  
4594 C  CG2  . ILE   B 281 ? 0.180422  0.254768 0.182684 -0.0149706  -0.01608    -0.00103574 281 ILE   B CG2  
4595 C  CD1  . ILE   B 281 ? 0.192717  0.256538 0.199441 0.00259998  -0.00868741 -0.0015809  281 ILE   B CD1  
4596 N  N    . LEU   B 282 ? 0.188085  0.24808  0.211824 -0.0102937  -0.0314066  0.0175699   282 LEU   B N    
4597 C  CA   . LEU   B 282 ? 0.181443  0.244225 0.234229 -0.00173772 -0.0352727  0.0288614   282 LEU   B CA   
4598 C  C    . LEU   B 282 ? 0.195498  0.25943  0.267225 -0.00091305 -0.0365093  0.0410069   282 LEU   B C    
4599 O  O    . LEU   B 282 ? 0.233212  0.257182 0.319195 -0.00677158 -0.0172673  0.0390011   282 LEU   B O    
4600 C  CB   . LEU   B 282 ? 0.196921  0.232416 0.231381 0.00470158  -0.0371006  0.0184193   282 LEU   B CB   
4601 C  CG   . LEU   B 282 ? 0.212627  0.22965  0.222766 0.00323644  -0.032675   0.00703587  282 LEU   B CG   
4602 C  CD1  . LEU   B 282 ? 0.227405  0.228787 0.223734 0.00628916  -0.0256116  -0.00149022 282 LEU   B CD1  
4603 C  CD2  . LEU   B 282 ? 0.201201  0.243699 0.225047 0.00175826  -0.024524   0.000463    282 LEU   B CD2  
4604 N  N    . GLY   B 283 ? 0.191254  0.283697 0.273202 -0.00028273 -0.0337062  0.0680951   283 GLY   B N    
4605 C  CA   . GLY   B 283 ? 0.211418  0.280881 0.296989 0.00151027  -0.0323662  0.0780841   283 GLY   B CA   
4606 C  C    . GLY   B 283 ? 0.216593  0.293917 0.291464 -0.0011613  -0.0270156  0.0753144   283 GLY   B C    
4607 O  O    . GLY   B 283 ? 0.233583  0.309064 0.374065 -0.0180505  -0.033065   0.107325    283 GLY   B O    
4608 N  N    A SER   B 284 ? 0.194279  0.280064 0.263713 0.00072063  -0.0203674  0.060563    284 SER   B N    
4609 N  N    B SER   B 284 ? 0.207857  0.288732 0.276687 0.00477904  -0.0203814  0.0653113   284 SER   B N    
4610 C  CA   A SER   B 284 ? 0.189207  0.277086 0.250825 -0.0009246  -0.0109232  0.0420193   284 SER   B CA   
4611 C  CA   B SER   B 284 ? 0.205498  0.293651 0.271887 0.00272697  -0.0114662  0.0440249   284 SER   B CA   
4612 C  C    A SER   B 284 ? 0.198232  0.278258 0.229966 -0.00685783 -0.0047827  0.0314555   284 SER   B C    
4613 C  C    B SER   B 284 ? 0.203265  0.288163 0.240779 -0.00815336 -0.00410732 0.0335      284 SER   B C    
4614 O  O    A SER   B 284 ? 0.205995  0.288528 0.221454 -0.0153931  -0.00406477 0.0186537   284 SER   B O    
4615 O  O    B SER   B 284 ? 0.204045  0.296353 0.23089  -0.0156946  -0.00202589 0.0221265   284 SER   B O    
4616 C  CB   A SER   B 284 ? 0.177877  0.26373  0.247245 0.0124345   -0.0118859  0.030221    284 SER   B CB   
4617 C  CB   B SER   B 284 ? 0.212293  0.291763 0.274841 0.020325    -0.0106879  0.0331593   284 SER   B CB   
4618 O  OG   A SER   B 284 ? 0.163646  0.257829 0.242381 0.0242149   -0.00455552 0.024124    284 SER   B OG   
4619 O  OG   B SER   B 284 ? 0.222283  0.312107 0.298256 0.0363594   -0.00784969 0.0235257   284 SER   B OG   
4620 N  N    . ALA   B 285 ? 0.205726  0.28313  0.233064 -0.00804506 0.0050344   0.0391129   285 ALA   B N    
4621 C  CA   . ALA   B 285 ? 0.200284  0.302231 0.224585 -0.0153882  0.0182607   0.0210487   285 ALA   B CA   
4622 C  C    . ALA   B 285 ? 0.196266  0.296724 0.23644  0.0085448   0.0182596   0.0125985   285 ALA   B C    
4623 O  O    . ALA   B 285 ? 0.206965  0.375611 0.268069 0.0391696   0.019604    -0.0236894  285 ALA   B O    
4624 C  CB   . ALA   B 285 ? 0.226507  0.324309 0.22201  -0.025439   0.0207122   0.0262247   285 ALA   B CB   
4625 N  N    . LEU   B 286 ? 0.191209  0.264971 0.215282 0.00593961  0.00487466  0.0163057   286 LEU   B N    
4626 C  CA   . LEU   B 286 ? 0.204785  0.26518  0.230005 0.00487616  -0.00835057 0.0203132   286 LEU   B CA   
4627 C  C    . LEU   B 286 ? 0.180217  0.24926  0.213755 0.0134499   -0.00390472 0.00235444  286 LEU   B C    
4628 O  O    . LEU   B 286 ? 0.176934  0.244937 0.223786 0.013084    -0.00194761 0.0139682   286 LEU   B O    
4629 C  CB   . LEU   B 286 ? 0.220267  0.302141 0.250987 -0.00917654 -0.0328653  0.028867    286 LEU   B CB   
4630 C  CG   . LEU   B 286 ? 0.259502  0.326448 0.284242 -0.0131247  -0.0243761  0.0439112   286 LEU   B CG   
4631 C  CD1  . LEU   B 286 ? 0.283021  0.325365 0.290604 -0.0335     -0.0328272  0.0510248   286 LEU   B CD1  
4632 C  CD2  . LEU   B 286 ? 0.260211  0.355863 0.309796 -0.00658996 -0.0191788  0.0446793   286 LEU   B CD2  
4633 N  N    . LEU   B 287 ? 0.169211  0.214229 0.194589 0.00809949  0.00112062  -0.0108853  287 LEU   B N    
4634 C  CA   . LEU   B 287 ? 0.191621  0.220332 0.193747 0.00600394  0.00167887  -0.0198097  287 LEU   B CA   
4635 C  C    . LEU   B 287 ? 0.186999  0.225462 0.197373 0.00388661  -0.0150895  -0.0369408  287 LEU   B C    
4636 O  O    . LEU   B 287 ? 0.203457  0.291994 0.241221 0.0165712   -0.0331608  -0.0882966  287 LEU   B O    
4637 C  CB   . LEU   B 287 ? 0.214618  0.21384  0.197017 -0.00143647 -0.00131735 -0.0136977  287 LEU   B CB   
4638 C  CG   . LEU   B 287 ? 0.237478  0.216584 0.213189 0.00166056  -0.00096268 -0.0185779  287 LEU   B CG   
4639 C  CD1  . LEU   B 287 ? 0.275956  0.223949 0.232284 0.00457418  -0.0141259  -0.0177966  287 LEU   B CD1  
4640 C  CD2  . LEU   B 287 ? 0.258056  0.231396 0.227082 -0.00128784 -0.00216814 -0.0243961  287 LEU   B CD2  
4641 N  N    . GLU   B 288 ? 0.17927   0.209469 0.169147 -0.00728152 -0.0253815  -0.0251276  288 GLU   B N    
4642 C  CA   . GLU   B 288 ? 0.195391  0.199807 0.173906 -0.00901096 -0.0281588  -0.0235554  288 GLU   B CA   
4643 C  C    . GLU   B 288 ? 0.166767  0.172008 0.170345 -0.00284016 -0.0288402  -0.0239009  288 GLU   B C    
4644 O  O    . GLU   B 288 ? 0.14851   0.180564 0.170753 -0.00521795 -0.0266648  -0.0228441  288 GLU   B O    
4645 C  CB   . GLU   B 288 ? 0.233968  0.22175  0.184069 -0.00031932 -0.0406363  -0.00937037 288 GLU   B CB   
4646 C  CG   . GLU   B 288 ? 0.292225  0.252193 0.216393 0.0106443   -0.0387262  -0.0111064  288 GLU   B CG   
4647 C  CD   . GLU   B 288 ? 0.373358  0.263727 0.24576  -0.00817    -0.0368272  -0.00283126 288 GLU   B CD   
4648 O  OE1  . GLU   B 288 ? 0.417163  0.262556 0.221803 -0.0069031  -0.0396821  -0.00488991 288 GLU   B OE1  
4649 O  OE2  . GLU   B 288 ? 0.457936  0.27909  0.303689 -0.0227607  -0.0322706  0.0424286   288 GLU   B OE2  
4650 N  N    . ASP   B 289 ? 0.146477  0.173198 0.164697 -0.00416608 -0.0263201  -0.0236635  289 ASP   B N    
4651 C  CA   . ASP   B 289 ? 0.140773  0.17563  0.165678 0.00767796  -0.035127   -0.0225837  289 ASP   B CA   
4652 C  C    . ASP   B 289 ? 0.141038  0.174187 0.159363 0.00138182  -0.0329545  -0.0202729  289 ASP   B C    
4653 O  O    . ASP   B 289 ? 0.16217   0.190631 0.159199 0.00290898  -0.0370133  -0.0163672  289 ASP   B O    
4654 C  CB   . ASP   B 289 ? 0.136474  0.181761 0.176918 0.011899    -0.03339    -0.020292   289 ASP   B CB   
4655 C  CG   . ASP   B 289 ? 0.14745   0.191077 0.181378 0.00955751  -0.0308308  -0.022247   289 ASP   B CG   
4656 O  OD1  . ASP   B 289 ? 0.140249  0.192241 0.20256  0.00804577  -0.0376854  -0.0253213  289 ASP   B OD1  
4657 O  OD2  . ASP   B 289 ? 0.154013  0.204087 0.206965 0.0197886   -0.0421018  -0.0273023  289 ASP   B OD2  
4658 N  N    . GLU   B 290 ? 0.155108  0.176624 0.164372 0.00801605  -0.0338321  -0.0134015  290 GLU   B N    
4659 C  CA   . GLU   B 290 ? 0.164005  0.185917 0.176648 0.0148796   -0.0342187  -0.0179953  290 GLU   B CA   
4660 C  C    . GLU   B 290 ? 0.164381  0.195033 0.186033 0.0229352   -0.0325565  -0.0202966  290 GLU   B C    
4661 O  O    . GLU   B 290 ? 0.167921  0.233974 0.210494 0.0286966   -0.0140125  -0.0386678  290 GLU   B O    
4662 C  CB   . GLU   B 290 ? 0.180559  0.197159 0.206915 0.0112279   -0.035796   -0.016106   290 GLU   B CB   
4663 C  CG   . GLU   B 290 ? 0.1816    0.209715 0.220169 0.0100441   -0.0351997  -0.0173425  290 GLU   B CG   
4664 C  CD   . GLU   B 290 ? 0.176994  0.21326  0.211081 0.0162615   -0.0483955  -0.0225971  290 GLU   B CD   
4665 O  OE1  . GLU   B 290 ? 0.17833   0.204958 0.230209 0.00851987  -0.0363876  -0.0204303  290 GLU   B OE1  
4666 O  OE2  . GLU   B 290 ? 0.175506  0.212435 0.229141 0.0235728   -0.0633178  -0.0313937  290 GLU   B OE2  
4667 N  N    . PHE   B 291 ? 0.143839  0.197992 0.184846 0.0234454   -0.0318962  -0.0177943  291 PHE   B N    
4668 C  CA   . PHE   B 291 ? 0.145559  0.20436  0.19585  0.0294506   -0.0358971  -0.0174155  291 PHE   B CA   
4669 C  C    . PHE   B 291 ? 0.131915  0.204075 0.198771 0.0163325   -0.0289022  -0.0200984  291 PHE   B C    
4670 O  O    . PHE   B 291 ? 0.133455  0.207351 0.215565 0.0234554   -0.0248616  -0.0164448  291 PHE   B O    
4671 C  CB   . PHE   B 291 ? 0.165983  0.214222 0.205533 0.0342257   -0.041656   -0.0229609  291 PHE   B CB   
4672 C  CG   . PHE   B 291 ? 0.181468  0.229279 0.204155 0.0480936   -0.0596861  -0.0186083  291 PHE   B CG   
4673 C  CD1  . PHE   B 291 ? 0.200412  0.233376 0.213613 0.0584364   -0.0514515  -0.019798   291 PHE   B CD1  
4674 C  CD2  . PHE   B 291 ? 0.186871  0.241749 0.212596 0.0639454   -0.0619343  -0.0100987  291 PHE   B CD2  
4675 C  CE1  . PHE   B 291 ? 0.222996  0.246318 0.227064 0.0608913   -0.0581501  -0.00893145 291 PHE   B CE1  
4676 C  CE2  . PHE   B 291 ? 0.220079  0.259953 0.216893 0.0696507   -0.0503205  0.00340464  291 PHE   B CE2  
4677 C  CZ   . PHE   B 291 ? 0.223315  0.256887 0.220141 0.0724645   -0.0547962  0.00131932  291 PHE   B CZ   
4678 N  N    . THR   B 292 ? 0.124323  0.223624 0.201265 0.0186783   -0.0361112  -0.0136409  292 THR   B N    
4679 C  CA   . THR   B 292 ? 0.126547  0.24768  0.198319 0.0113865   -0.0237443  -0.00988865 292 THR   B CA   
4680 C  C    . THR   B 292 ? 0.123555  0.267133 0.193218 0.00713033  -0.0232996  -0.00670996 292 THR   B C    
4681 O  O    . THR   B 292 ? 0.124756  0.277929 0.194067 0.0041231   -0.0231738  -0.00976971 292 THR   B O    
4682 C  CB   . THR   B 292 ? 0.142803  0.266028 0.209436 0.0206075   -0.0292555  -0.0191419  292 THR   B CB   
4683 O  OG1  . THR   B 292 ? 0.138062  0.300184 0.228571 0.0247625   -0.0196432  -0.0274469  292 THR   B OG1  
4684 C  CG2  . THR   B 292 ? 0.139947  0.26839  0.203144 0.0243207   -0.0397868  -0.0184278  292 THR   B CG2  
4685 N  N    . PRO   B 293 ? 0.122553  0.292845 0.201161 -0.00264206 -0.0264119  0.00150492  293 PRO   B N    
4686 C  CA   . PRO   B 293 ? 0.12393   0.312165 0.204803 -0.0115976  -0.0214309  0.00401693  293 PRO   B CA   
4687 C  C    . PRO   B 293 ? 0.137299  0.343866 0.218149 0.00371472  -0.0227536  -0.00573357 293 PRO   B C    
4688 O  O    . PRO   B 293 ? 0.132555  0.384817 0.222551 -0.00189808 -0.0220414  -0.00272445 293 PRO   B O    
4689 C  CB   . PRO   B 293 ? 0.150327  0.309228 0.211095 -0.0187202  -0.0208545  0.00796966  293 PRO   B CB   
4690 C  CG   . PRO   B 293 ? 0.152372  0.299871 0.207074 -0.0145978  -0.0201346  0.0092782   293 PRO   B CG   
4691 C  CD   . PRO   B 293 ? 0.1477    0.291931 0.198051 -0.00253489 -0.0302696  0.00653141  293 PRO   B CD   
4692 N  N    . PHE   B 294 ? 0.143752  0.367642 0.236062 0.0184492   -0.0216125  -0.0226536  294 PHE   B N    
4693 C  CA   . PHE   B 294 ? 0.162009  0.395144 0.267256 0.0238506   -0.00868108 -0.0401896  294 PHE   B CA   
4694 C  C    . PHE   B 294 ? 0.153941  0.382241 0.258266 0.0447612   -0.022751   -0.0437536  294 PHE   B C    
4695 O  O    . PHE   B 294 ? 0.152035  0.429649 0.287296 0.036039    -0.0220109  -0.0413773  294 PHE   B O    
4696 C  CB   . PHE   B 294 ? 0.208244  0.439943 0.304534 0.012533    0.00665721  -0.069357   294 PHE   B CB   
4697 C  CG   . PHE   B 294 ? 0.261359  0.479077 0.406449 0.0385552   0.0119797   -0.0957522  294 PHE   B CG   
4698 C  CD1  . PHE   B 294 ? 0.286615  0.505959 0.440305 0.0307593   0.0481899   -0.10439    294 PHE   B CD1  
4699 C  CD2  . PHE   B 294 ? 0.284707  0.491506 0.467969 0.0333454   0.0121626   -0.118534   294 PHE   B CD2  
4700 C  CE1  . PHE   B 294 ? 0.315127  0.523191 0.508035 0.0467924   0.0499615   -0.112115   294 PHE   B CE1  
4701 C  CE2  . PHE   B 294 ? 0.299805  0.511281 0.49094  0.0398106   0.0223627   -0.120454   294 PHE   B CE2  
4702 C  CZ   . PHE   B 294 ? 0.318447  0.526345 0.505175 0.0309777   0.0509597   -0.118991   294 PHE   B CZ   
4703 N  N    . ASP   B 295 ? 0.146422  0.363838 0.227808 0.0435769   -0.0478419  -0.0332377  295 ASP   B N    
4704 C  CA   . ASP   B 295 ? 0.161336  0.353658 0.238918 0.0529375   -0.0426412  -0.0367298  295 ASP   B CA   
4705 C  C    . ASP   B 295 ? 0.154442  0.367949 0.231763 0.0563408   -0.0478634  -0.0285721  295 ASP   B C    
4706 O  O    . ASP   B 295 ? 0.162963  0.383703 0.251415 0.0758727   -0.0604395  -0.0469252  295 ASP   B O    
4707 C  CB   . ASP   B 295 ? 0.157287  0.334928 0.236511 0.0572912   -0.0466092  -0.0404369  295 ASP   B CB   
4708 C  CG   . ASP   B 295 ? 0.16808   0.313958 0.235837 0.0579059   -0.0373139  -0.0485768  295 ASP   B CG   
4709 O  OD1  . ASP   B 295 ? 0.186069  0.354344 0.265766 0.0598584   -0.0219032  -0.0628831  295 ASP   B OD1  
4710 O  OD2  . ASP   B 295 ? 0.16405   0.291723 0.241579 0.0542863   -0.0534354  -0.0547651  295 ASP   B OD2  
4711 N  N    . VAL   B 296 ? 0.134135  0.371653 0.213969 0.042988    -0.0513029  -0.0256009  296 VAL   B N    
4712 C  CA   . VAL   B 296 ? 0.133437  0.3963   0.225591 0.0246019   -0.054456   -0.0222195  296 VAL   B CA   
4713 C  C    . VAL   B 296 ? 0.138215  0.445955 0.257206 0.011188    -0.0521337  -0.00902032 296 VAL   B C    
4714 O  O    . VAL   B 296 ? 0.166862  0.487621 0.2664   0.0174834   -0.0621637  0.00443319  296 VAL   B O    
4715 C  CB   . VAL   B 296 ? 0.14733   0.368267 0.222973 0.00816085  -0.0520418  -0.0218349  296 VAL   B CB   
4716 C  CG1  . VAL   B 296 ? 0.162467  0.369727 0.230987 -0.00377251 -0.0500977  -0.0328812  296 VAL   B CG1  
4717 C  CG2  . VAL   B 296 ? 0.137378  0.341169 0.215345 0.0301972   -0.0518879  -0.0119526  296 VAL   B CG2  
4718 N  N    . VAL   B 297 ? 0.123415  0.485235 0.286174 -0.0001275  -0.0530342  0.00202514  297 VAL   B N    
4719 C  CA   . VAL   B 297 ? 0.14297   0.523783 0.325097 -0.00490217 -0.0279431  0.00933245  297 VAL   B CA   
4720 C  C    . VAL   B 297 ? 0.128378  0.530485 0.319636 0.0171442   -0.0365133  0.00946785  297 VAL   B C    
4721 O  O    . VAL   B 297 ? 0.139788  0.54913  0.316949 0.0339821   -0.0572973  0.00212529  297 VAL   B O    
4722 C  CB   . VAL   B 297 ? 0.16572   0.544246 0.333625 -0.0200892  -0.0124422  0.0191722   297 VAL   B CB   
4723 C  CG1  . VAL   B 297 ? 0.181082  0.570598 0.363063 -0.0221166  0.0065019   0.0237315   297 VAL   B CG1  
4724 C  CG2  . VAL   B 297 ? 0.181329  0.548561 0.335286 -0.0335493  -0.0157077  0.0302424   297 VAL   B CG2  
4725 N  N    A ARG   B 298 ? 0.144741  0.519344 0.333122 0.0351006   -0.0455074  0.00799563  298 ARG   B N    
4726 N  N    B ARG   B 298 ? 0.171888  0.532089 0.330884 0.0274985   -0.0330412  -0.00898795 298 ARG   B N    
4727 C  CA   A ARG   B 298 ? 0.135891  0.510964 0.344695 0.0419791   -0.0460353  0.0134939   298 ARG   B CA   
4728 C  CA   B ARG   B 298 ? 0.185009  0.526885 0.341229 0.0319322   -0.0235242  -0.0165785  298 ARG   B CA   
4729 C  C    A ARG   B 298 ? 0.128222  0.495078 0.339066 0.0472586   -0.0467361  -0.00409759 298 ARG   B C    
4730 C  C    B ARG   B 298 ? 0.175829  0.520303 0.343771 0.0407858   -0.0236225  -0.0185647  298 ARG   B C    
4731 O  O    A ARG   B 298 ? 0.128019  0.480352 0.336533 0.0495237   -0.051331   -0.0162391  298 ARG   B O    
4732 O  O    B ARG   B 298 ? 0.203284  0.551908 0.356208 0.0678773   -0.0200695  -0.0179658  298 ARG   B O    
4733 C  CB   A ARG   B 298 ? 0.186641  0.501942 0.356736 0.0331609   -0.0454065  0.0270901   298 ARG   B CB   
4734 C  CB   B ARG   B 298 ? 0.257485  0.520897 0.342961 0.0198444   -0.0103056  -0.0277104  298 ARG   B CB   
4735 C  CG   A ARG   B 298 ? 0.193646  0.494978 0.350503 0.0283768   -0.0507695  0.0459488   298 ARG   B CG   
4736 C  CG   B ARG   B 298 ? 0.300579  0.506782 0.346209 0.0068916   -0.00163681 -0.0409031  298 ARG   B CG   
4737 C  CD   A ARG   B 298 ? 0.197958  0.484684 0.331293 0.0222254   -0.0505898  0.0654071   298 ARG   B CD   
4738 C  CD   B ARG   B 298 ? 0.372984  0.499948 0.348121 0.00155857  0.00696197  -0.0457772  298 ARG   B CD   
4739 N  NE   A ARG   B 298 ? 0.196462  0.470585 0.309776 -0.0021725  -0.0302894  0.0740745   298 ARG   B NE   
4740 N  NE   B ARG   B 298 ? 0.404541  0.480726 0.329337 -0.0132781  0.0211339   -0.0591292  298 ARG   B NE   
4741 C  CZ   A ARG   B 298 ? 0.192558  0.454798 0.278677 0.00528473  -0.0416676  0.0797934   298 ARG   B CZ   
4742 C  CZ   B ARG   B 298 ? 0.430032  0.459184 0.30926  -0.0137597  0.0237478   -0.0617942  298 ARG   B CZ   
4743 N  NH1  A ARG   B 298 ? 0.178943  0.44673  0.263344 0.0155593   -0.0665947  0.100721    298 ARG   B NH1  
4744 N  NH1  B ARG   B 298 ? 0.424613  0.429985 0.336817 -0.00481513 0.03754     -0.057226   298 ARG   B NH1  
4745 N  NH2  A ARG   B 298 ? 0.177605  0.437434 0.244956 -0.00706776 -0.039739   0.0823966   298 ARG   B NH2  
4746 N  NH2  B ARG   B 298 ? 0.46935   0.469698 0.264852 -0.0101302  0.0356997   -0.05503    298 ARG   B NH2  
4747 N  N    . GLN   B 299 ? 0.148922  0.46816  0.332613 0.0430797   -0.0370021  -0.0191234  299 GLN   B N    
4748 C  CA   . GLN   B 299 ? 0.146842  0.43821  0.326963 0.0359197   -0.0454023  -0.0257445  299 GLN   B CA   
4749 C  C    . GLN   B 299 ? 0.168417  0.459697 0.33748  0.0270661   -0.0812898  -0.00589227 299 GLN   B C    
4750 O  O    . GLN   B 299 ? 0.193463  0.455676 0.399721 0.0202034   -0.110098   0.0178103   299 GLN   B O    
4751 C  CB   . GLN   B 299 ? 0.140449  0.3893   0.295875 0.0480723   -0.0460402  -0.0399322  299 GLN   B CB   
4752 C  CG   . GLN   B 299 ? 0.138659  0.353838 0.27539  0.0440001   -0.0490062  -0.0468976  299 GLN   B CG   
4753 C  CD   . GLN   B 299 ? 0.137001  0.331097 0.243258 0.0480928   -0.0522525  -0.0447314  299 GLN   B CD   
4754 O  OE1  . GLN   B 299 ? 0.141841  0.329906 0.234114 0.054749    -0.0548947  -0.0527611  299 GLN   B OE1  
4755 N  NE2  . GLN   B 299 ? 0.143742  0.325212 0.236106 0.0355053   -0.0569017  -0.0327147  299 GLN   B NE2  
4756 N  N    . CYS   B 300 ? 0.185752  0.465743 0.336595 0.0240493   -0.0986009  -0.00574208 300 CYS   B N    
4757 C  CA   . CYS   B 300 ? 0.230184  0.493003 0.33149  0.0122237   -0.105525   -0.00921482 300 CYS   B CA   
4758 C  C    . CYS   B 300 ? 0.248773  0.489548 0.328902 -0.0113089  -0.0716667  -0.00307397 300 CYS   B C    
4759 O  O    . CYS   B 300 ? 0.24205   0.488427 0.313533 -0.00879351 -0.0713855  0.00910246  300 CYS   B O    
4760 C  CB   . CYS   B 300 ? 0.238414  0.526595 0.335847 0.0273295   -0.111445   -0.0445803  300 CYS   B CB   
4761 S  SG   . CYS   B 300 ? 0.29224   0.632206 0.360398 0.0355166   -0.105752   -0.0946879  300 CYS   B SG   
4762 N  N    . SER   B 301 ? 0.240164  0.484117 0.331767 -0.0415894  -0.0552811  0.00487009  301 SER   B N    
4763 C  CA   . SER   B 301 ? 0.249586  0.472495 0.350262 -0.0469071  -0.0324163  0.0189131   301 SER   B CA   
4764 C  C    . SER   B 301 ? 0.261382  0.452004 0.347961 -0.0495052  -0.0198315  0.0295965   301 SER   B C    
4765 O  O    . SER   B 301 ? 0.275147  0.421548 0.3723   -0.0356126  -0.00551299 0.0383343   301 SER   B O    
4766 C  CB   . SER   B 301 ? 0.265311  0.510196 0.363456 -0.0628327  -0.0204731  0.0223988   301 SER   B CB   
4767 O  OG   . SER   B 301 ? 0.297358  0.5491   0.358561 -0.0724271  -0.00071103 0.0179193   301 SER   B OG   
4768 N  N    . GLY   B 302 ? 0.271713  0.439282 0.331527 -0.0389398  -0.0240049  0.0387314   302 GLY   B N    
4769 C  CA   . GLY   B 302 ? 0.274794  0.437668 0.310759 -0.0402778  -0.0175178  0.0473273   302 GLY   B CA   
4770 C  C    . GLY   B 302 ? 0.270869  0.434236 0.303757 -0.026988   -0.0249933  0.0489938   302 GLY   B C    
4771 O  O    . GLY   B 302 ? 0.237174  0.445122 0.277014 -0.0372932  -0.0387873  0.0538926   302 GLY   B O    
4772 N  N    . VAL   B 303 ? 0.263086  0.427979 0.291298 -0.0315433  -0.020565   0.0443777   303 VAL   B N    
4773 C  CA   . VAL   B 303 ? 0.262512  0.410366 0.295083 -0.0312698  -0.00941215 0.0435308   303 VAL   B CA   
4774 C  C    . VAL   B 303 ? 0.237826  0.400302 0.283571 -0.0398052  -0.0058872  0.0487317   303 VAL   B C    
4775 O  O    . VAL   B 303 ? 0.236996  0.40874  0.282293 -0.055533   -0.00027508 0.0526157   303 VAL   B O    
4776 C  CB   . VAL   B 303 ? 0.28125   0.419481 0.303044 -0.0230561  -0.00353296 0.0478022   303 VAL   B CB   
4777 C  CG1  . VAL   B 303 ? 0.298803  0.441545 0.320066 -0.0245659  -0.00749161 0.0370129   303 VAL   B CG1  
4778 C  CG2  . VAL   B 303 ? 0.284625  0.418589 0.297364 -0.0117172  0.0117898   0.0470452   303 VAL   B CG2  
4779 N  N    . THR   B 304 ? 0.233393  0.392144 0.253224 -0.0414959  -0.00615096 0.0543961   304 THR   B N    
4780 C  CA   . THR   B 304 ? 0.252897  0.401849 0.266005 -0.0269591  -0.0198204  0.0538787   304 THR   B CA   
4781 C  C    . THR   B 304 ? 0.255323  0.419417 0.270963 -0.0211442  -0.041531   0.0537067   304 THR   B C    
4782 O  O    . THR   B 304 ? 0.287227  0.437499 0.275814 -0.0508583  -0.0376562  0.0573164   304 THR   B O    
4783 C  CB   . THR   B 304 ? 0.243391  0.397584 0.267413 -0.0170288  -0.00303329 0.0590976   304 THR   B CB   
4784 O  OG1  . THR   B 304 ? 0.255759  0.408312 0.27714  -0.0258759  0.0164367   0.0620604   304 THR   B OG1  
4785 C  CG2  . THR   B 304 ? 0.244254  0.37472  0.257433 -0.0124103  -0.0152617  0.0606085   304 THR   B CG2  
4786 N  N    . PHE   B 305 ? 0.277434  0.430565 0.290425 -0.0199546  -0.0556089  0.0470843   305 PHE   B N    
4787 C  CA   . PHE   B 305 ? 0.289924  0.453466 0.302083 -0.00715458 -0.0705331  0.0411837   305 PHE   B CA   
4788 C  C    . PHE   B 305 ? 0.336252  0.477064 0.354075 0.0132075   -0.076151   0.0236284   305 PHE   B C    
4789 O  O    . PHE   B 305 ? 0.393255  0.50318  0.434143 0.0201987   -0.108204   0.0491062   305 PHE   B O    
4790 C  CB   . PHE   B 305 ? 0.278189  0.466769 0.319407 0.00204722  -0.0752082  0.0400932   305 PHE   B CB   
4791 C  CG   . PHE   B 305 ? 0.234812  0.48268  0.331817 -0.00167178 -0.0786451  0.0423808   305 PHE   B CG   
4792 C  CD1  . PHE   B 305 ? 0.230557  0.488977 0.326595 -0.00812642 -0.0813963  0.0413457   305 PHE   B CD1  
4793 C  CD2  . PHE   B 305 ? 0.248965  0.495875 0.340898 0.0160519   -0.0741069  0.0513171   305 PHE   B CD2  
4794 C  CE1  . PHE   B 305 ? 0.258103  0.494617 0.335707 0.0103367   -0.0898253  0.0523263   305 PHE   B CE1  
4795 C  CE2  . PHE   B 305 ? 0.297952  0.507792 0.368327 0.0277562   -0.0699246  0.0565584   305 PHE   B CE2  
4796 C  CZ   . PHE   B 305 ? 0.304726  0.51199  0.3518   0.0185172   -0.0726247  0.0541899   305 PHE   B CZ   
4797 C  C4   . A1ITI C .   ? 0.136945  0.367299 0.222138 -0.00549944 -0.0250393  -0.0445312  401 A1ITI A C4   
4798 C  C5   . A1ITI C .   ? 0.150484  0.349984 0.222379 0.00076745  -0.0221902  -0.0397978  401 A1ITI A C5   
4799 C  C7   . A1ITI C .   ? 0.120727  0.301252 0.206205 -0.00577514 -0.0249993  -0.0326768  401 A1ITI A C7   
4800 C  C8   . A1ITI C .   ? 0.129652  0.282596 0.208079 -0.00626807 -0.015533   -0.0340427  401 A1ITI A C8   
4801 C  C10  . A1ITI C .   ? 0.128565  0.291319 0.210094 -0.0135439  -0.00830529 -0.0328484  401 A1ITI A C10  
4802 C  C13  . A1ITI C .   ? 0.122969  0.226627 0.196501 -0.0027953  -0.0101426  -0.0191774  401 A1ITI A C13  
4803 C  C15  . A1ITI C .   ? 0.145027  0.219677 0.25021  -0.0157577  -0.00862481 -0.0147702  401 A1ITI A C15  
4804 C  C21  . A1ITI C .   ? 0.126336  0.215675 0.198427 0.00214966  -0.0122588  -0.0142604  401 A1ITI A C21  
4805 C  C24  . A1ITI C .   ? 0.129837  0.362482 0.251092 -0.00819353 -0.0270879  -0.0446255  401 A1ITI A C24  
4806 C  C26  . A1ITI C .   ? 0.131117  0.412016 0.29855  -0.0174173  -0.0390117  -0.0330185  401 A1ITI A C26  
4807 C  C1   . A1ITI C .   ? 0.193824  0.416944 0.245767 0.0454851   -0.0212154  -0.0268338  401 A1ITI A C1   
4808 C  C2   . A1ITI C .   ? 0.19398   0.41477  0.240132 0.0298307   -0.0201281  -0.0213479  401 A1ITI A C2   
4809 C  C3   . A1ITI C .   ? 0.168789  0.389364 0.235193 0.0094441   -0.0243391  -0.0371804  401 A1ITI A C3   
4810 N  N6   . A1ITI C .   ? 0.131077  0.323265 0.219496 -0.00862023 -0.0256368  -0.0461034  401 A1ITI A N6   
4811 N  N9   . A1ITI C .   ? 0.117896  0.270548 0.200927 -0.00853393 -0.0192199  -0.0312173  401 A1ITI A N9   
4812 C  C11  . A1ITI C .   ? 0.128723  0.308173 0.218742 -0.0116158  -0.0120539  -0.0348998  401 A1ITI A C11  
4813 C  C12  . A1ITI C .   ? 0.125978  0.252109 0.19659  0.00141218  -0.0160962  -0.0258693  401 A1ITI A C12  
4814 C  C14  . A1ITI C .   ? 0.13613   0.214015 0.218434 -0.0123308  -0.00992004 -0.0194133  401 A1ITI A C14  
4815 C  C16  . A1ITI C .   ? 0.147151  0.218122 0.274155 -0.0168296  -0.0022045  -0.0204166  401 A1ITI A C16  
4816 S  S17  . A1ITI C .   ? 0.139305  0.228916 0.272791 -0.0057491  -0.00584981 -0.0247206  401 A1ITI A S17  
4817 C  C18  . A1ITI C .   ? 0.133202  0.21311  0.206952 -0.00785021 -0.0119851  -0.0131594  401 A1ITI A C18  
4818 C  C19  . A1ITI C .   ? 0.129368  0.217392 0.20113  -0.00461654 -0.0104347  -0.0138593  401 A1ITI A C19  
4819 N  N20  . A1ITI C .   ? 0.124863  0.215563 0.205438 -0.00527955 -0.00391159 -0.0147232  401 A1ITI A N20  
4820 O  O22  . A1ITI C .   ? 0.138279  0.260826 0.189116 0.00431961  -0.0210967  -0.0232234  401 A1ITI A O22  
4821 C  C23  . A1ITI C .   ? 0.130761  0.330382 0.222949 -0.00949237 -0.0200437  -0.0427736  401 A1ITI A C23  
4822 N  N25  . A1ITI C .   ? 0.118687  0.38604  0.284759 -0.00267874 -0.0285023  -0.0336399  401 A1ITI A N25  
4823 C  C27  . A1ITI C .   ? 0.132351  0.421235 0.316987 -0.0289071  -0.0361073  -0.0323768  401 A1ITI A C27  
4824 O  O28  . A1ITI C .   ? 0.156302  0.379967 0.300256 -0.0276046  -0.0240153  -0.0690524  401 A1ITI A O28  
4825 C  C29  . A1ITI C .   ? 0.162573  0.364736 0.2245   -0.00789777 -0.0263323  -0.0541777  401 A1ITI A C29  
4826 C  C30  . A1ITI C .   ? 0.181938  0.374795 0.240466 0.00753665  -0.0153733  -0.056348   401 A1ITI A C30  
4827 C  C31  . A1ITI C .   ? 0.193015  0.387394 0.227912 0.0115138   -0.0270986  -0.0586394  401 A1ITI A C31  
4828 BR BR32 . A1ITI C .   ? 0.202502  0.436478 0.251628 0.0297842   -0.0156557  -0.0780055  401 A1ITI A BR32 
4829 C  C33  . A1ITI C .   ? 0.169817  0.396941 0.222796 0.0109197   -0.0299802  -0.0458138  401 A1ITI A C33  
4830 CL CL   . CL    D .   ? 0.157783  0.205172 0.214691 -0.00533626 -0.0112828  0.0246844   402 CL    A CL   
4831 C  C4   . A1ITI E .   ? 0.202228  0.287682 0.234075 -0.0597765  -0.0239108  -0.0329031  401 A1ITI B C4   
4832 C  C5   . A1ITI E .   ? 0.203149  0.288598 0.224785 -0.0577741  -0.0228357  -0.0335411  401 A1ITI B C5   
4833 C  C7   . A1ITI E .   ? 0.185989  0.260637 0.20696  -0.0568742  -0.0132458  -0.038594   401 A1ITI B C7   
4834 C  C8   . A1ITI E .   ? 0.187653  0.252893 0.209218 -0.0532749  -0.0103145  -0.0357054  401 A1ITI B C8   
4835 C  C10  . A1ITI E .   ? 0.188452  0.251656 0.209613 -0.0518499  -0.0129274  -0.0323374  401 A1ITI B C10  
4836 C  C13  . A1ITI E .   ? 0.171381  0.231001 0.180737 -0.042324   0.00426736  -0.0172542  401 A1ITI B C13  
4837 C  C15  . A1ITI E .   ? 0.194597  0.252723 0.208498 -0.0659029  0.030944    -0.0255994  401 A1ITI B C15  
4838 C  C21  . A1ITI E .   ? 0.177117  0.228378 0.176816 -0.0408678  0.00812553  -0.0106793  401 A1ITI B C21  
4839 C  C24  . A1ITI E .   ? 0.219104  0.299888 0.242566 -0.0706125  -0.0355243  -0.0454706  401 A1ITI B C24  
4840 C  C26  . A1ITI E .   ? 0.266178  0.32021  0.262093 -0.0764735  -0.0325947  -0.0573577  401 A1ITI B C26  
4841 C  C1   . A1ITI E .   ? 0.259823  0.318148 0.216174 -0.0392879  -0.0292696  -0.0197245  401 A1ITI B C1   
4842 C  C2   . A1ITI E .   ? 0.258597  0.313239 0.225067 -0.0441539  -0.0379197  -0.0295125  401 A1ITI B C2   
4843 C  C3   . A1ITI E .   ? 0.233337  0.298094 0.232159 -0.0551532  -0.029131   -0.0300271  401 A1ITI B C3   
4844 N  N6   . A1ITI E .   ? 0.190063  0.277831 0.217073 -0.0624215  -0.0172133  -0.0361973  401 A1ITI B N6   
4845 N  N9   . A1ITI E .   ? 0.189534  0.243867 0.196551 -0.0580833  -0.0116058  -0.0294618  401 A1ITI B N9   
4846 C  C11  . A1ITI E .   ? 0.193973  0.265936 0.219939 -0.0618265  -0.0160553  -0.0352361  401 A1ITI B C11  
4847 C  C12  . A1ITI E .   ? 0.172739  0.238012 0.1877   -0.0439613  0.00042861  -0.0220878  401 A1ITI B C12  
4848 C  C14  . A1ITI E .   ? 0.178593  0.243187 0.196703 -0.0549981  0.018645    -0.0187849  401 A1ITI B C14  
4849 C  C16  . A1ITI E .   ? 0.192912  0.270867 0.212894 -0.058724   0.0378452   -0.0245319  401 A1ITI B C16  
4850 S  S17  . A1ITI E .   ? 0.192459  0.273232 0.202649 -0.0612678  0.0402197   -0.0187062  401 A1ITI B S17  
4851 C  C18  . A1ITI E .   ? 0.171025  0.23846  0.178694 -0.0540791  0.0194545   -0.0132527  401 A1ITI B C18  
4852 C  C19  . A1ITI E .   ? 0.159001  0.227683 0.177306 -0.0476504  0.00311332  -0.0118117  401 A1ITI B C19  
4853 N  N20  . A1ITI E .   ? 0.168364  0.221092 0.175729 -0.0399741  0.00613381  -0.0118283  401 A1ITI B N20  
4854 O  O22  . A1ITI E .   ? 0.201403  0.249059 0.1994   -0.0298086  -0.0152507  -0.016464   401 A1ITI B O22  
4855 C  C23  . A1ITI E .   ? 0.202237  0.280117 0.222428 -0.0620423  -0.0262437  -0.0397796  401 A1ITI B C23  
4856 N  N25  . A1ITI E .   ? 0.245586  0.310561 0.257295 -0.0717922  -0.0265344  -0.05609    401 A1ITI B N25  
4857 C  C27  . A1ITI E .   ? 0.275353  0.31564  0.270511 -0.0806639  -0.029639   -0.061892   401 A1ITI B C27  
4858 O  O28  . A1ITI E .   ? 0.222149  0.333158 0.288875 -0.0824592  -0.0158833  -0.0501332  401 A1ITI B O28  
4859 C  C29  . A1ITI E .   ? 0.21143   0.312276 0.249111 -0.0406219  -0.0136649  -0.0251389  401 A1ITI B C29  
4860 C  C30  . A1ITI E .   ? 0.210494  0.326299 0.271782 -0.0439113  0.0135841   -0.0198149  401 A1ITI B C30  
4861 C  C31  . A1ITI E .   ? 0.215471  0.3335   0.270333 -0.0284996  -0.00150713 -0.0151942  401 A1ITI B C31  
4862 BR BR32 . A1ITI E .   ? 0.272227  0.379357 0.284457 0.005182    0.0291516   0.00130181  401 A1ITI B BR32 
4863 C  C33  . A1ITI E .   ? 0.236054  0.306539 0.247595 -0.0424974  -0.0163559  -0.0203292  401 A1ITI B C33  
4864 NA NA   . NA    F .   ? 0.365509  0.276904 0.330688 0.0725792   -0.0613751  -0.00593825 402 NA    B NA   
4865 O  O    . HOH   G .   ? 0.204122  0.493461 0.379598 -0.0634275  0.00385909  0.0439091   501 HOH   A O    
4866 O  O    . HOH   G .   ? 0.453092  0.569161 0.498502 0.219749    -0.0190275  -0.0229952  502 HOH   A O    
4867 O  O    . HOH   G .   ? 0.694952  0.355472 0.760987 0.0772926   0.123309    -0.0410863  503 HOH   A O    
4868 O  O    . HOH   G .   ? 0.303483  0.475352 0.444446 -0.00385069 0.0420434   0.0575443   504 HOH   A O    
4869 O  O    . HOH   G .   ? 0.149251  0.475913 0.567863 -0.0128625  0.0742483   -0.113421   505 HOH   A O    
4870 O  O    . HOH   G .   ? 0.208009  0.386659 0.522016 -0.00808329 -0.0142136  0.0387164   506 HOH   A O    
4871 O  O    . HOH   G .   ? 0.891513  0.466573 0.496458 -0.0206201  -0.272786   0.0310525   507 HOH   A O    
4872 O  O    . HOH   G .   ? 0.207287  0.391158 0.309495 0.0222799   0.0577032   0.156903    508 HOH   A O    
4873 O  O    . HOH   G .   ? 0.357729  0.664886 0.265297 0.0893335   -0.011868   0.121125    509 HOH   A O    
4874 O  O    . HOH   G .   ? 0.339741  0.553985 0.324214 0.193913    0.0197556   -0.0318088  510 HOH   A O    
4875 O  O    . HOH   G .   ? 0.12922   0.418096 0.258602 0.0255831   0.0479189   0.0186002   511 HOH   A O    
4876 O  O    . HOH   G .   ? 0.46302   0.381467 0.622967 -0.011038   0.0948914   -0.0429912  512 HOH   A O    
4877 O  O    . HOH   G .   ? 0.449376  0.431659 0.412227 -0.0126453  0.0606778   -0.0154514  513 HOH   A O    
4878 O  O    . HOH   G .   ? 0.287008  0.296031 0.352883 0.0304358   -0.0283687  0.0236649   514 HOH   A O    
4879 O  O    . HOH   G .   ? 0.730521  0.543555 0.47703  0.0851834   0.00783075  -0.145429   515 HOH   A O    
4880 O  O    . HOH   G .   ? 0.248645  0.73717  0.304944 0.165013    -0.00043352 0.0424227   516 HOH   A O    
4881 O  O    . HOH   G .   ? 0.378686  0.500279 0.484664 -0.088107   -0.0705939  0.090853    517 HOH   A O    
4882 O  O    . HOH   G .   ? 0.329831  0.502774 0.289787 0.0679639   -0.0420011  0.0321267   518 HOH   A O    
4883 O  O    . HOH   G .   ? 0.339669  0.643815 0.417706 0.050591    -0.00783723 -0.131984   519 HOH   A O    
4884 O  O    . HOH   G .   ? 0.44626   0.687635 0.501981 -0.115344   0.0235245   0.0595229   520 HOH   A O    
4885 O  O    . HOH   G .   ? 0.22156   0.669504 0.512536 -0.00620537 0.0969469   -0.0898644  521 HOH   A O    
4886 O  O    . HOH   G .   ? 0.340562  0.389552 0.671879 -0.0135683  0.0574327   -0.10797    522 HOH   A O    
4887 O  O    . HOH   G .   ? 0.219077  0.297896 0.199978 -0.00832531 0.0245496   0.0160813   523 HOH   A O    
4888 O  O    . HOH   G .   ? 0.565567  0.97326  0.584318 0.0406862   0.0517499   0.0220694   524 HOH   A O    
4889 O  O    . HOH   G .   ? 0.187846  0.375348 0.393334 -0.0284027  0.022961    -0.0328714  525 HOH   A O    
4890 O  O    . HOH   G .   ? 0.591858  0.649257 0.431556 -0.190381   -0.163549   0.0600842   526 HOH   A O    
4891 O  O    . HOH   G .   ? 0.365329  0.436443 0.613807 -0.100828   0.140157    -0.088334   527 HOH   A O    
4892 O  O    . HOH   G .   ? 0.225997  0.453033 0.423687 0.0617683   0.00437319  0.00948282  528 HOH   A O    
4893 O  O    . HOH   G .   ? 0.301972  0.725344 0.32753  -0.0442514  0.124348    -0.0575678  529 HOH   A O    
4894 O  O    . HOH   G .   ? 0.158401  0.313281 0.234459 -0.00833959 0.00522294  -0.0211661  530 HOH   A O    
4895 O  O    . HOH   G .   ? 0.405527  0.413555 0.301746 -0.0212627  0.129222    -0.0253936  531 HOH   A O    
4896 O  O    . HOH   G .   ? 0.393733  0.597523 0.578783 -0.120853   -0.0108736  0.0775148   532 HOH   A O    
4897 O  O    . HOH   G .   ? 0.479269  0.497721 0.604142 0.19838     0.229688    0.307742    533 HOH   A O    
4898 O  O    . HOH   G .   ? 0.275434  0.570692 0.341782 -0.107336   0.0205262   0.0151342   534 HOH   A O    
4899 O  O    . HOH   G .   ? 0.1637    0.401982 0.375705 0.0136399   -0.0596046  0.00388047  535 HOH   A O    
4900 O  O    . HOH   G .   ? 0.197192  0.386393 0.321937 0.0167578   -0.0187234  -0.00121242 536 HOH   A O    
4901 O  O    . HOH   G .   ? 0.197209  0.347941 0.234816 -0.0133282  -0.0140397  0.00477513  537 HOH   A O    
4902 O  O    . HOH   G .   ? 0.65276   0.836551 0.424416 -0.121334   -0.111307   -0.0655492  538 HOH   A O    
4903 O  O    . HOH   G .   ? 0.286988  0.412006 0.296388 0.00770449  0.0297978   0.0453331   539 HOH   A O    
4904 O  O    . HOH   G .   ? 0.283717  0.546935 0.508179 0.136322    0.12859     0.0446595   540 HOH   A O    
4905 O  O    . HOH   G .   ? 0.403056  0.654593 0.325552 -0.0744496  -0.0281885  0.0865886   541 HOH   A O    
4906 O  O    . HOH   G .   ? 0.266361  0.40347  0.329922 0.00574945  -0.0286144  0.0437115   542 HOH   A O    
4907 O  O    . HOH   G .   ? 0.321137  0.584664 0.353147 0.0205964   0.0571436   -0.0691808  543 HOH   A O    
4908 O  O    . HOH   G .   ? 0.373435  0.48156  0.899884 0.111916    0.0832653   -0.144739   544 HOH   A O    
4909 O  O    . HOH   G .   ? 0.131854  0.243473 0.180918 0.0408251   -0.00944564 -0.00809057 545 HOH   A O    
4910 O  O    . HOH   G .   ? 0.351228  0.855386 0.423373 -0.0133293  -0.0636305  0.169948    546 HOH   A O    
4911 O  O    . HOH   G .   ? 0.394019  0.394684 0.438673 0.0412411   -0.0213965  -0.010128   547 HOH   A O    
4912 O  O    . HOH   G .   ? 0.217098  0.541943 0.534091 -0.0384233  -0.0724681  0.143074    548 HOH   A O    
4913 O  O    . HOH   G .   ? 0.179219  0.267682 0.207316 0.0277946   0.0309959   0.0113914   549 HOH   A O    
4914 O  O    . HOH   G .   ? 0.210264  0.757986 0.365953 0.119296    0.0408815   0.165692    550 HOH   A O    
4915 O  O    . HOH   G .   ? 0.144842  0.280419 0.311738 -0.0166335  0.0174831   -0.0140941  551 HOH   A O    
4916 O  O    . HOH   G .   ? 0.361303  0.454927 0.659541 0.122665    0.226957    0.144308    552 HOH   A O    
4917 O  O    . HOH   G .   ? 0.125176  0.350438 0.198605 -0.00122225 -0.00592883 -0.0025356  553 HOH   A O    
4918 O  O    . HOH   G .   ? 0.251233  0.446692 0.32674  0.00299849  -0.00186922 -0.0878708  554 HOH   A O    
4919 O  O    . HOH   G .   ? 0.220133  0.367101 0.26233  0.0314358   0.0142672   -0.0215919  555 HOH   A O    
4920 O  O    . HOH   G .   ? 0.61804   0.403938 0.861847 0.100692    -0.190442   0.0663273   556 HOH   A O    
4921 O  O    . HOH   G .   ? 0.123746  0.236828 0.19071  0.0222005   -0.00016546 0.00877203  557 HOH   A O    
4922 O  O    . HOH   G .   ? 0.246522  0.362754 0.277301 -0.0278031  -0.0162471  0.0656331   558 HOH   A O    
4923 O  O    . HOH   G .   ? 0.194869  0.303895 0.175016 0.0173966   0.0437105   0.0222216   559 HOH   A O    
4924 O  O    . HOH   G .   ? 0.141451  0.243539 0.190943 -0.0209194  -0.00942814 -0.00392031 560 HOH   A O    
4925 O  O    . HOH   G .   ? 0.178075  0.494341 0.628702 -0.0441359  0.0554567   -0.0859036  561 HOH   A O    
4926 O  O    . HOH   G .   ? 0.500165  0.528513 0.491666 0.167517    -0.0715427  -0.0442816  562 HOH   A O    
4927 O  O    . HOH   G .   ? 0.347093  0.660656 0.278279 0.154691    -0.0242446  0.150612    563 HOH   A O    
4928 O  O    . HOH   G .   ? 0.391349  0.407941 0.687512 0.121186    -0.0585335  0.0321542   564 HOH   A O    
4929 O  O    . HOH   G .   ? 0.340354  0.670599 0.791354 0.0864595   0.0343149   0.225678    565 HOH   A O    
4930 O  O    . HOH   G .   ? 0.269786  0.749713 0.340065 -0.0622387  -0.024546   -0.0682331  566 HOH   A O    
4931 O  O    . HOH   G .   ? 0.206075  0.372007 0.257497 0.118781    0.00166305  -0.0168735  567 HOH   A O    
4932 O  O    . HOH   G .   ? 0.238529  0.426839 0.294538 0.0661685   -0.0698688  -0.0515688  568 HOH   A O    
4933 O  O    . HOH   G .   ? 0.306701  0.470243 0.338045 -0.129486   0.0252666   -0.0337977  569 HOH   A O    
4934 O  O    . HOH   G .   ? 0.245554  0.428122 0.283961 0.145591    -0.0255984  -0.0170769  570 HOH   A O    
4935 O  O    . HOH   G .   ? 0.291811  0.369209 0.429926 -0.0101516  -0.0437367  -0.141741   571 HOH   A O    
4936 O  O    . HOH   G .   ? 0.345329  0.396633 0.338651 0.080411    0.0746695   -0.0882261  572 HOH   A O    
4937 O  O    . HOH   G .   ? 0.366047  0.645418 0.373826 0.0618222   0.0411338   0.134103    573 HOH   A O    
4938 O  O    . HOH   G .   ? 0.29212   0.37954  0.324797 0.00998438  0.08048     -0.0572797  574 HOH   A O    
4939 O  O    . HOH   G .   ? 0.154895  0.254849 0.323944 0.00156779  -0.0488057  0.0309395   575 HOH   A O    
4940 O  O    . HOH   G .   ? 0.259848  0.545782 0.325057 0.105511    -0.0517911  -0.0685294  576 HOH   A O    
4941 O  O    . HOH   G .   ? 0.262766  0.425998 0.228469 0.0400374   0.0435711   0.0431701   577 HOH   A O    
4942 O  O    . HOH   G .   ? 0.277502  0.512519 0.720832 -0.140277   0.058296    -0.0247289  578 HOH   A O    
4943 O  O    . HOH   G .   ? 0.134896  0.378877 0.273888 0.053576    0.0431919   0.0412152   579 HOH   A O    
4944 O  O    . HOH   G .   ? 0.267852  0.31285  0.279856 -0.0650404  -0.0343578  0.00936325  580 HOH   A O    
4945 O  O    . HOH   G .   ? 0.237321  0.478169 0.304419 -0.0268437  -0.00024436 -0.0681823  581 HOH   A O    
4946 O  O    . HOH   G .   ? 0.486476  0.356368 0.420135 -0.145814   -0.244252   0.09197     582 HOH   A O    
4947 O  O    . HOH   G .   ? 0.3484    0.748447 0.317327 -0.037116   -0.0118526  -0.0382592  583 HOH   A O    
4948 O  O    . HOH   G .   ? 0.207912  0.276612 0.237779 0.00194399  0.0299057   4.714e-05   584 HOH   A O    
4949 O  O    . HOH   G .   ? 0.194618  0.348543 0.295613 0.0861027   -0.0119674  0.00750389  585 HOH   A O    
4950 O  O    . HOH   G .   ? 0.12492   0.21913  0.210672 0.00593838  0.00275136  0.0141307   586 HOH   A O    
4951 O  O    . HOH   G .   ? 0.183807  0.427675 0.240339 0.0563724   0.046791    0.0346375   587 HOH   A O    
4952 O  O    . HOH   G .   ? 0.592481  0.44257  0.564344 0.0563738   0.0724595   0.0595507   588 HOH   A O    
4953 O  O    . HOH   G .   ? 0.144309  0.387201 0.302042 0.0179092   0.024046    0.0762303   589 HOH   A O    
4954 O  O    . HOH   G .   ? 0.189788  0.342467 0.373812 0.0150081   -0.0340103  -0.0677649  590 HOH   A O    
4955 O  O    . HOH   G .   ? 0.329765  0.380378 0.340358 0.0970331   -0.132985   -0.0175719  591 HOH   A O    
4956 O  O    . HOH   G .   ? 0.212596  0.386849 0.364717 -0.0167103  0.100067    0.0587762   592 HOH   A O    
4957 O  O    . HOH   G .   ? 0.290238  0.298646 0.677357 -0.040606   -0.106576   0.0702116   593 HOH   A O    
4958 O  O    . HOH   G .   ? 0.152376  0.357968 0.216613 0.0305645   -0.0237668  0.0349221   594 HOH   A O    
4959 O  O    . HOH   G .   ? 0.413283  0.608671 0.43104  -0.109024   -0.0631561  -0.00022753 595 HOH   A O    
4960 O  O    . HOH   G .   ? 0.358888  0.295652 0.537844 0.026849    -0.092283   -0.00535062 596 HOH   A O    
4961 O  O    . HOH   G .   ? 0.415637  0.67966  0.35781  0.0296915   0.0223957   0.00333748  597 HOH   A O    
4962 O  O    . HOH   G .   ? 0.262837  0.502119 0.803992 -0.0771649  -0.00767235 -0.136658   598 HOH   A O    
4963 O  O    . HOH   G .   ? 0.285659  0.622678 0.272791 -0.121533   0.00480009  -0.106004   599 HOH   A O    
4964 O  O    . HOH   G .   ? 0.258551  0.536016 0.482398 0.0471737   -0.0410221  -0.0299092  600 HOH   A O    
4965 O  O    . HOH   G .   ? 0.358939  0.441284 0.740692 -0.0277621  0.126126    0.152841    601 HOH   A O    
4966 O  O    . HOH   G .   ? 0.346314  0.53595  0.851178 0.0720998   0.121545    0.246072    602 HOH   A O    
4967 O  O    . HOH   G .   ? 0.125844  0.349732 0.216575 0.0172887   0.0335337   0.0127705   603 HOH   A O    
4968 O  O    . HOH   G .   ? 0.265323  0.463477 0.316583 0.0139853   0.018586    0.0248839   604 HOH   A O    
4969 O  O    . HOH   G .   ? 0.237893  0.309039 0.266023 0.0188541   -0.00315096 -0.0334204  605 HOH   A O    
4970 O  O    . HOH   G .   ? 0.178428  0.411044 0.364343 0.0545531   0.00322246  0.058461    606 HOH   A O    
4971 O  O    . HOH   G .   ? 0.178185  0.312253 0.26466  0.0117813   -0.0059711  0.0229698   607 HOH   A O    
4972 O  O    . HOH   G .   ? 0.270309  0.366115 0.379034 -0.0640716  0.0845081   -0.00137502 608 HOH   A O    
4973 O  O    . HOH   G .   ? 0.460654  0.43042  0.410891 0.0693664   -0.0682343  -0.164106   609 HOH   A O    
4974 O  O    . HOH   G .   ? 0.399118  0.36296  0.340005 0.00708956  0.0892699   0.139734    610 HOH   A O    
4975 O  O    . HOH   G .   ? 0.259713  0.609357 0.487772 0.0657469   0.00659746  0.101417    611 HOH   A O    
4976 O  O    . HOH   G .   ? 0.387851  0.764956 0.508689 -0.0994022  -0.0342508  0.154988    612 HOH   A O    
4977 O  O    . HOH   G .   ? 0.346221  0.262811 0.281249 0.00274431  -0.0147315  0.0491081   613 HOH   A O    
4978 O  O    . HOH   G .   ? 0.165881  0.450905 0.378411 0.0774374   0.076508    0.0248445   614 HOH   A O    
4979 O  O    . HOH   G .   ? 0.220557  0.531062 0.259198 0.00397068  0.0115795   -0.0105971  615 HOH   A O    
4980 O  O    . HOH   G .   ? 0.351837  0.32287  0.290268 0.0770912   -0.0632602  -0.00766379 616 HOH   A O    
4981 O  O    . HOH   G .   ? 0.145841  0.65255  0.265975 -0.0157448  -0.0236973  -0.142835   617 HOH   A O    
4982 O  O    . HOH   G .   ? 0.257371  0.418569 0.244372 0.00339274  0.0303173   0.0154114   618 HOH   A O    
4983 O  O    . HOH   G .   ? 0.557156  0.51083  0.392169 -0.0757937  0.037184    0.00191595  619 HOH   A O    
4984 O  O    . HOH   G .   ? 0.306857  0.4319   0.46084  -0.0372191  -0.00111622 -0.0941131  620 HOH   A O    
4985 O  O    . HOH   G .   ? 0.195917  0.351145 0.200487 0.0341245   0.0222088   0.00289475  621 HOH   A O    
4986 O  O    . HOH   G .   ? 0.149632  0.398275 0.253091 0.0107716   0.0206262   0.0449574   622 HOH   A O    
4987 O  O    . HOH   G .   ? 0.381407  0.408607 0.332852 -0.0714664  -0.0770897  0.0392134   623 HOH   A O    
4988 O  O    . HOH   G .   ? 0.329128  0.402146 0.430453 -0.0754264  -0.078693   0.0501795   624 HOH   A O    
4989 O  O    . HOH   G .   ? 0.898168  0.551217 0.500394 -0.195243   -0.316817   -0.0728615  625 HOH   A O    
4990 O  O    . HOH   G .   ? 0.21149   0.72197  0.40564  -0.0459884  0.00992707  -0.0406638  626 HOH   A O    
4991 O  O    . HOH   G .   ? 0.287973  0.412479 0.309692 0.0569896   0.0786106   0.0745681   627 HOH   A O    
4992 O  O    . HOH   G .   ? 0.160546  0.355316 0.24297  0.0446069   0.0126186   -0.00332725 628 HOH   A O    
4993 O  O    . HOH   G .   ? 0.74315   0.29112  0.585848 0.116888    -0.22324    -0.0684096  629 HOH   A O    
4994 O  O    . HOH   G .   ? 0.283683  0.278944 0.343068 0.0347789   -0.0903677  0.00764133  630 HOH   A O    
4995 O  O    . HOH   G .   ? 0.177743  0.427301 0.338929 0.0436095   -0.0802588  0.0844735   631 HOH   A O    
4996 O  O    . HOH   G .   ? 0.230646  0.338031 0.221387 -0.00259278 0.0551506   0.00509699  632 HOH   A O    
4997 O  O    . HOH   G .   ? 0.107318  0.339422 0.348966 0.0127423   -0.0180901  0.0393116   633 HOH   A O    
4998 O  O    . HOH   G .   ? 0.206998  0.272675 0.25222  0.0169962   -0.00551966 0.0207576   634 HOH   A O    
4999 O  O    . HOH   G .   ? 0.204624  0.402104 0.368967 -0.0194411  0.0739837   -0.100095   635 HOH   A O    
5000 O  O    . HOH   G .   ? 0.171704  0.529206 0.467963 0.0845097   0.0452589   0.0122109   636 HOH   A O    
5001 O  O    . HOH   G .   ? 0.148694  0.290674 0.222475 0.0213281   0.0638891   0.0120865   637 HOH   A O    
5002 O  O    . HOH   G .   ? 0.246445  0.290286 0.338947 -0.014234   -0.0249107  0.0260044   638 HOH   A O    
5003 O  O    . HOH   G .   ? 0.37136   0.695349 0.378094 0.092261    -0.02915    -0.211034   639 HOH   A O    
5004 O  O    . HOH   G .   ? 0.0866698 0.255785 0.150712 -0.00401207 0.00036523  0.00766838  640 HOH   A O    
5005 O  O    . HOH   G .   ? 0.217171  0.555819 0.580438 0.0245661   -0.00426041 -0.000517   641 HOH   A O    
5006 O  O    . HOH   G .   ? 0.397286  0.533625 0.532831 0.0325824   -0.104244   0.0134353   642 HOH   A O    
5007 O  O    . HOH   G .   ? 0.162942  0.248756 0.219839 0.0415973   -0.0236501  0.00379464  643 HOH   A O    
5008 O  O    . HOH   G .   ? 0.135359  0.30923  0.293036 -0.0399678  0.0136299   -0.0179806  644 HOH   A O    
5009 O  O    . HOH   G .   ? 0.429467  0.441154 0.393967 0.205077    0.218511    0.115       645 HOH   A O    
5010 O  O    . HOH   G .   ? 0.153273  0.436975 0.279812 -0.00471312 -0.00126101 0.00605361  646 HOH   A O    
5011 O  O    . HOH   G .   ? 0.304696  0.369496 0.378486 -0.0169382  -0.00531705 0.00417574  647 HOH   A O    
5012 O  O    . HOH   G .   ? 0.507365  0.555851 0.288851 -0.0622636  -0.0850056  0.0347809   648 HOH   A O    
5013 O  O    . HOH   G .   ? 0.346322  0.423147 0.604441 0.0791516   -0.0883097  -0.165364   649 HOH   A O    
5014 O  O    . HOH   G .   ? 0.330405  0.598983 0.53902  -0.075605   -0.010729   -0.114291   650 HOH   A O    
5015 O  O    . HOH   G .   ? 0.367921  0.49479  0.446235 -0.017458   0.037563    0.116712    651 HOH   A O    
5016 O  O    . HOH   G .   ? 0.273752  0.646905 0.480963 -0.0478027  -0.0974404  0.126702    652 HOH   A O    
5017 O  O    . HOH   G .   ? 0.108339  0.287825 0.252104 -0.0113992  -0.00310319 -0.0569403  653 HOH   A O    
5018 O  O    . HOH   G .   ? 0.114555  0.277375 0.179603 0.0129208   -0.00777295 -0.00433787 654 HOH   A O    
5019 O  O    . HOH   G .   ? 0.192723  0.326217 0.289649 -0.00098631 0.0178832   0.00895286  655 HOH   A O    
5020 O  O    . HOH   G .   ? 0.398544  0.509368 0.314766 0.125497    0.143247    0.117321    656 HOH   A O    
5021 O  O    . HOH   G .   ? 0.78022   0.794944 0.565809 -0.236304   0.0209162   0.138836    657 HOH   A O    
5022 O  O    . HOH   G .   ? 0.439879  0.801267 0.253736 0.170835    -0.0425723  -0.0941779  658 HOH   A O    
5023 O  O    . HOH   G .   ? 0.372495  0.53708  0.469415 0.0388233   0.075949    -0.060643   659 HOH   A O    
5024 O  O    . HOH   G .   ? 0.403218  0.586389 0.312512 0.0336736   0.163817    0.0144209   660 HOH   A O    
5025 O  O    . HOH   G .   ? 0.383135  0.642066 0.296355 0.262482    0.12707     0.144723    661 HOH   A O    
5026 O  O    . HOH   G .   ? 0.699112  0.580368 0.729968 -0.120612   0.201635    -0.133059   662 HOH   A O    
5027 O  O    . HOH   G .   ? 0.308067  0.364052 0.508228 -0.0461666  -0.198633   0.0928189   663 HOH   A O    
5028 O  O    . HOH   G .   ? 0.245515  0.518043 0.303771 0.0478375   0.0469154   -0.0486573  664 HOH   A O    
5029 O  O    . HOH   G .   ? 0.300835  0.377826 0.394579 -0.0771812  0.0135253   0.0385531   665 HOH   A O    
5030 O  O    . HOH   G .   ? 0.524219  0.806379 0.529911 0.0225973   0.0233723   0.015041    666 HOH   A O    
5031 O  O    . HOH   G .   ? 0.302983  0.315099 0.398229 0.0105757   -0.0423241  0.112198    667 HOH   A O    
5032 O  O    . HOH   G .   ? 0.358244  0.426576 0.494645 0.126471    -0.0572488  -0.0162509  668 HOH   A O    
5033 O  O    . HOH   G .   ? 0.268617  0.315909 0.48254  0.058592    -0.0862872  0.123992    669 HOH   A O    
5034 O  O    . HOH   G .   ? 0.419066  0.489569 0.563247 0.0414448   -0.052796   0.0403939   670 HOH   A O    
5035 O  O    . HOH   G .   ? 0.495504  0.667094 0.479234 0.0543537   0.132569    0.00173898  671 HOH   A O    
5036 O  O    . HOH   G .   ? 0.164175  0.403869 0.310374 0.0355231   -0.0664174  0.0736896   672 HOH   A O    
5037 O  O    . HOH   G .   ? 0.227612  0.695652 0.547438 -0.0518077  -0.0318367  0.231589    673 HOH   A O    
5038 O  O    . HOH   G .   ? 0.173082  0.449719 0.219604 0.0759263   0.00977738  -0.00177527 674 HOH   A O    
5039 O  O    . HOH   G .   ? 0.631345  0.298875 0.332152 -0.115258   0.0849619   0.00771237  675 HOH   A O    
5040 O  O    . HOH   G .   ? 0.375091  0.548422 0.311369 -0.0564645  -0.00749598 -0.00222374 676 HOH   A O    
5041 O  O    . HOH   G .   ? 0.190993  0.440579 0.216043 0.0823881   0.0225706   0.00452013  677 HOH   A O    
5042 O  O    . HOH   G .   ? 0.190426  0.48691  0.390893 -0.0588514  0.00083087  0.00555059  678 HOH   A O    
5043 O  O    . HOH   G .   ? 0.277267  0.380156 0.31675  0.107173    0.0407759   0.164505    679 HOH   A O    
5044 O  O    . HOH   G .   ? 0.242784  0.44917  0.217774 0.0446479   0.0150562   -0.0091181  680 HOH   A O    
5045 O  O    . HOH   G .   ? 0.332063  0.794259 0.401551 -0.0689791  0.0801316   -0.021457   681 HOH   A O    
5046 O  O    . HOH   G .   ? 0.561344  0.624097 0.322669 0.014881    0.10339     -0.0646313  682 HOH   A O    
5047 O  O    . HOH   G .   ? 0.439613  0.470437 0.725529 0.0357943   -0.0380423  -0.115039   683 HOH   A O    
5048 O  O    . HOH   G .   ? 0.351576  0.343367 0.27706  -0.0559204  0.0599065   -0.0651838  684 HOH   A O    
5049 O  O    . HOH   G .   ? 0.549076  0.554439 0.270298 -0.188062   -0.100584   0.11313     685 HOH   A O    
5050 O  O    . HOH   G .   ? 0.253024  0.309646 0.252351 0.0212089   0.0320982   0.0393952   686 HOH   A O    
5051 O  O    . HOH   G .   ? 0.225687  0.299468 0.371266 0.0276573   -0.0449755  -0.0232313  687 HOH   A O    
5052 O  O    . HOH   G .   ? 0.342777  0.402568 0.246448 -0.103615   -0.050602   0.0961998   688 HOH   A O    
5053 O  O    . HOH   G .   ? 0.374796  0.576615 0.275692 0.12597     0.0645388   0.0188681   689 HOH   A O    
5054 O  O    . HOH   G .   ? 0.299706  0.527534 0.548308 -0.11953    -0.111929   0.1867      690 HOH   A O    
5055 O  O    . HOH   G .   ? 0.220574  0.391135 0.443537 0.0907279   -0.0252     0.0190466   691 HOH   A O    
5056 O  O    . HOH   G .   ? 0.136436  0.319419 0.232232 0.0203845   -0.00617004 -0.0253483  692 HOH   A O    
5057 O  O    . HOH   G .   ? 0.230684  0.403961 0.389251 -0.028835   -0.110012   -0.0202993  693 HOH   A O    
5058 O  O    . HOH   G .   ? 0.289562  0.397334 0.23658  0.00750602  0.0333458   -0.0199572  694 HOH   A O    
5059 O  O    . HOH   G .   ? 0.357402  0.514826 0.45249  -0.0136097  0.0983647   0.0649099   695 HOH   A O    
5060 O  O    . HOH   G .   ? 0.186139  0.462587 0.412711 0.117816    -0.0422325  -0.012644   696 HOH   A O    
5061 O  O    . HOH   G .   ? 0.301259  0.357544 0.204919 -0.0353329  0.0119686   -0.00285214 697 HOH   A O    
5062 O  O    . HOH   G .   ? 0.291091  0.374592 0.439971 0.0298296   -0.056385   -0.070472   698 HOH   A O    
5063 O  O    . HOH   G .   ? 0.673646  0.353736 0.713358 -0.0531466  -0.0993482  -0.0197151  699 HOH   A O    
5064 O  O    . HOH   G .   ? 0.237575  0.376421 0.267456 0.0595468   0.0097352   0.0400302   700 HOH   A O    
5065 O  O    . HOH   G .   ? 0.251419  0.506637 0.317443 0.128186    -0.106786   0.0144493   701 HOH   A O    
5066 O  O    . HOH   G .   ? 0.534354  0.564196 0.719027 0.107957    0.311659    0.220056    702 HOH   A O    
5067 O  O    . HOH   G .   ? 0.330489  0.77088  0.353703 0.089008    0.0123016   0.12687     703 HOH   A O    
5068 O  O    . HOH   G .   ? 0.157934  0.301267 0.183553 -0.0127525  0.00232136  0.0314337   704 HOH   A O    
5069 O  O    . HOH   G .   ? 0.14936   0.330342 0.275705 -0.0448173  -0.019842   0.0848824   705 HOH   A O    
5070 O  O    . HOH   G .   ? 0.661943  0.412447 0.797804 0.148352    0.298827    0.19905     706 HOH   A O    
5071 O  O    . HOH   G .   ? 0.217887  0.233707 0.325297 0.00704448  -0.0207259  -0.0417832  707 HOH   A O    
5072 O  O    . HOH   G .   ? 0.248073  0.369182 0.38888  0.0771773   0.0265827   -0.148727   708 HOH   A O    
5073 O  O    . HOH   G .   ? 0.152883  0.312771 0.206485 0.048823    0.00152097  -0.00874112 709 HOH   A O    
5074 O  O    . HOH   G .   ? 0.199598  0.434137 0.443459 0.0537829   0.00523535  -0.0872895  710 HOH   A O    
5075 O  O    . HOH   G .   ? 0.246929  0.322437 0.25965  0.0330337   0.0451472   0.0742045   711 HOH   A O    
5076 O  O    . HOH   G .   ? 0.285973  0.499217 0.191065 0.0748187   -0.00480034 0.0210598   712 HOH   A O    
5077 O  O    . HOH   G .   ? 0.28887   0.31662  0.310597 0.0695361   0.00538071  0.0537727   713 HOH   A O    
5078 O  O    . HOH   G .   ? 0.300005  0.297913 0.547989 -0.00595488 0.0139402   -0.0440422  714 HOH   A O    
5079 O  O    . HOH   G .   ? 0.262505  0.580607 0.625703 -0.0375629  0.172864    -0.012758   715 HOH   A O    
5080 O  O    . HOH   G .   ? 0.209793  0.417094 0.300836 0.0166469   -0.0157033  -0.0857921  716 HOH   A O    
5081 O  O    . HOH   G .   ? 0.410473  0.776579 0.598714 0.0358266   -0.0179669  -0.150594   717 HOH   A O    
5082 O  O    . HOH   G .   ? 0.331054  0.472397 0.35291  0.011365    0.0772247   0.107982    718 HOH   A O    
5083 O  O    . HOH   G .   ? 0.229873  0.851829 0.258523 -0.121976   -0.0477957  0.102639    719 HOH   A O    
5084 O  O    . HOH   G .   ? 0.274256  0.307226 0.238424 0.0212389   0.0297336   0.0398148   720 HOH   A O    
5085 O  O    . HOH   G .   ? 0.200168  0.628589 0.191534 -0.0102394  0.00076918  0.0164237   721 HOH   A O    
5086 O  O    . HOH   G .   ? 0.247533  0.398579 0.267431 0.0739039   -0.00135483 0.0134913   722 HOH   A O    
5087 O  O    . HOH   G .   ? 0.215203  0.462248 0.33379  0.0355437   0.0402053   0.079404    723 HOH   A O    
5088 O  O    . HOH   G .   ? 0.270886  0.610379 0.467931 0.135675    -0.150789   -0.18459    724 HOH   A O    
5089 O  O    . HOH   G .   ? 0.197646  0.407045 0.25593  0.00288951  0.00756339  0.0254114   725 HOH   A O    
5090 O  O    . HOH   G .   ? 0.380812  0.304717 0.456473 0.156356    0.00786373  -0.0241346  726 HOH   A O    
5091 O  O    . HOH   G .   ? 0.272826  0.581162 0.47377  -0.0644052  0.0190891   -0.204181   727 HOH   A O    
5092 O  O    . HOH   G .   ? 0.394544  0.495802 0.438614 0.023322    -0.0467425  0.0657464   728 HOH   A O    
5093 O  O    . HOH   G .   ? 0.338188  0.368648 0.208175 0.0133168   0.0303794   0.0132205   729 HOH   A O    
5094 O  O    . HOH   G .   ? 0.369169  0.347584 0.410658 0.0238071   -0.0809215  -0.0450986  730 HOH   A O    
5095 O  O    . HOH   G .   ? 0.193919  0.520315 0.560042 0.0190291   0.0095808   -0.0138707  731 HOH   A O    
5096 O  O    . HOH   G .   ? 0.211664  0.549677 0.401043 -0.00830975 0.0462067   -0.10725    732 HOH   A O    
5097 O  O    . HOH   G .   ? 0.258516  0.408457 0.898932 -0.0288789  0.0173882   0.00354657  733 HOH   A O    
5098 O  O    . HOH   G .   ? 0.663666  0.570805 0.474412 0.00725117  -0.00525666 0.0436016   734 HOH   A O    
5099 O  O    . HOH   G .   ? 0.238749  0.456189 0.315982 -0.00492081 -0.0302415  -0.0759548  735 HOH   A O    
5100 O  O    . HOH   G .   ? 0.27148   0.528378 0.462631 0.0395894   -0.0336157  0.0235854   736 HOH   A O    
5101 O  O    . HOH   G .   ? 0.268028  0.386127 0.35019  0.0631919   -0.0533599  0.0586051   737 HOH   A O    
5102 O  O    . HOH   G .   ? 0.558637  0.625287 0.593759 -0.137447   0.173423    -0.205475   738 HOH   A O    
5103 O  O    . HOH   G .   ? 0.226904  0.362993 0.327696 0.0447071   -0.0685637  0.0268567   739 HOH   A O    
5104 O  O    . HOH   G .   ? 0.337742  0.42354  0.410342 0.0645812   -0.0517329  -0.028118   740 HOH   A O    
5105 O  O    . HOH   G .   ? 0.362068  0.550519 0.288918 0.0281937   -0.030743   -0.0667148  741 HOH   A O    
5106 O  O    . HOH   G .   ? 0.214564  0.472153 0.346008 -0.0456709  0.0776668   -0.108805   742 HOH   A O    
5107 O  O    . HOH   G .   ? 0.28872   0.598291 0.32401  -0.0668565  -0.0221936  0.0683693   743 HOH   A O    
5108 O  O    . HOH   G .   ? 0.362424  0.754057 0.443568 0.132458    -0.0692654  -0.0702435  744 HOH   A O    
5109 O  O    . HOH   G .   ? 0.354427  0.431307 0.318048 -0.0552122  -0.0111667  0.00557815  745 HOH   A O    
5110 O  O    . HOH   G .   ? 0.585575  0.532886 0.450203 0.165426    -0.121858   -0.228665   746 HOH   A O    
5111 O  O    . HOH   G .   ? 0.338644  0.5553   0.346205 0.0621669   0.0683097   0.0263577   747 HOH   A O    
5112 O  O    . HOH   G .   ? 0.823133  0.424492 0.680385 0.0903301   -0.184228   -0.0187468  748 HOH   A O    
5113 O  O    . HOH   G .   ? 0.285769  0.381869 0.334611 0.0244454   -0.0665138  0.0292193   749 HOH   A O    
5114 O  O    . HOH   G .   ? 0.322852  0.711847 0.287171 0.223805    -0.0629637  -0.0514394  750 HOH   A O    
5115 O  O    . HOH   G .   ? 0.683552  0.445741 0.533491 -0.186582   -0.171171   0.10298     751 HOH   A O    
5116 O  O    . HOH   G .   ? 0.564279  1.06048  0.617118 0.101598    0.144144    0.0915663   752 HOH   A O    
5117 O  O    . HOH   G .   ? 0.675412  0.953434 0.679905 0.0598487   -0.0351981  0.0434232   753 HOH   A O    
5118 O  O    . HOH   G .   ? 0.363802  0.530397 0.356729 0.154891    0.0950688   -0.0325633  754 HOH   A O    
5119 O  O    . HOH   G .   ? 0.429079  0.548357 0.734837 -0.0495326  -0.0199968  -0.237968   755 HOH   A O    
5120 O  O    . HOH   G .   ? 0.367492  0.471982 0.369053 0.0545044   0.0477      0.0299076   756 HOH   A O    
5121 O  O    . HOH   G .   ? 0.335878  0.550357 0.816716 -0.0780057  0.178297    -0.275065   757 HOH   A O    
5122 O  O    . HOH   G .   ? 0.549293  0.852927 0.331257 0.352569    0.0110395   0.0594638   758 HOH   A O    
5123 O  O    . HOH   G .   ? 0.234314  0.499507 0.359901 0.0280359   0.0345845   0.0805403   759 HOH   A O    
5124 O  O    . HOH   G .   ? 0.174841  0.615123 0.340592 0.0833431   0.0107093   0.135469    760 HOH   A O    
5125 O  O    . HOH   G .   ? 0.389038  0.663866 0.410685 0.00270881  -0.00257118 0.0598476   761 HOH   A O    
5126 O  O    . HOH   G .   ? 0.343936  0.854195 0.30254  0.2179      0.0978143   0.182259    762 HOH   A O    
5127 O  O    . HOH   G .   ? 0.211403  0.612148 0.323753 0.100491    -0.049069   -0.150207   763 HOH   A O    
5128 O  O    . HOH   G .   ? 0.155038  0.447672 0.603139 0.0122427   0.069469    -0.0836504  764 HOH   A O    
5129 O  O    . HOH   G .   ? 0.438729  0.709806 0.669998 0.141918    -0.118654   -0.279939   765 HOH   A O    
5130 O  O    . HOH   G .   ? 0.22327   0.368184 0.262605 0.0857499   0.00856587  0.024774    766 HOH   A O    
5131 O  O    . HOH   G .   ? 0.260564  0.486837 0.410349 -0.0358864  -0.0091629  0.0880735   767 HOH   A O    
5132 O  O    . HOH   G .   ? 0.330228  0.436971 0.299319 -0.0498939  -0.00976088 0.0705863   768 HOH   A O    
5133 O  O    . HOH   G .   ? 0.299102  0.398031 0.427444 -0.0178874  -0.04835    0.154466    769 HOH   A O    
5134 O  O    . HOH   G .   ? 0.510456  0.511859 0.731189 -0.0807695  0.0593524   -0.161361   770 HOH   A O    
5135 O  O    . HOH   G .   ? 0.236584  0.465341 0.397809 -0.0132743  -0.0300545  -0.0687892  771 HOH   A O    
5136 O  O    . HOH   G .   ? 0.269599  0.574099 0.531998 0.0861041   -0.0177917  -0.0789445  772 HOH   A O    
5137 O  O    . HOH   G .   ? 1.10159   0.939996 1.11138  0.346624    0.00318789  0.0201342   773 HOH   A O    
5138 O  O    . HOH   G .   ? 0.303421  0.528008 0.410284 0.00099804  0.00359888  -0.0571222  774 HOH   A O    
5139 O  O    . HOH   G .   ? 0.640219  0.414416 0.409156 0.209473    -0.176718   -0.141209   775 HOH   A O    
5140 O  O    . HOH   G .   ? 0.28414   0.504632 0.543625 0.0733366   -0.0979389  0.130137    776 HOH   A O    
5141 O  O    . HOH   G .   ? 0.241562  0.382455 0.330986 0.0328093   0.0266695   -0.0150352  777 HOH   A O    
5142 O  O    . HOH   G .   ? 0.435476  0.51684  0.436528 0.16907     0.122872    0.117176    778 HOH   A O    
5143 O  O    . HOH   G .   ? 0.373801  0.892649 0.585035 0.0470623   0.00889215  0.0343325   779 HOH   A O    
5144 O  O    . HOH   G .   ? 0.314661  0.479863 0.385684 -0.0220917  0.0406226   -0.0422315  780 HOH   A O    
5145 O  O    . HOH   G .   ? 0.557113  0.438902 0.585311 0.218535    -0.064682   0.00968401  781 HOH   A O    
5146 O  O    . HOH   G .   ? 0.612928  0.642666 0.325031 0.146692    -0.0972123  -0.0029392  782 HOH   A O    
5147 O  O    . HOH   G .   ? 0.477736  0.834495 0.37417  0.305187    -0.053673   -0.0100883  783 HOH   A O    
5148 O  O    . HOH   G .   ? 0.358656  0.533458 0.500286 -0.0338662  0.0309003   -0.0102043  784 HOH   A O    
5149 O  O    . HOH   G .   ? 0.218737  0.441874 0.355853 0.0386711   -0.00894445 0.0597095   785 HOH   A O    
5150 O  O    . HOH   G .   ? 0.285468  0.50266  0.62607  -0.0956415  -0.0775518  0.00140661  786 HOH   A O    
5151 O  O    . HOH   G .   ? 0.43769   0.402959 0.549152 0.11447     -0.186486   0.0283966   787 HOH   A O    
5152 O  O    . HOH   G .   ? 0.825304  0.576484 0.703756 -0.0139476  -0.0110234  -0.230103   788 HOH   A O    
5153 O  O    . HOH   G .   ? 0.254902  0.439839 0.353961 0.087742    0.00062138  -0.00670807 789 HOH   A O    
5154 O  O    . HOH   G .   ? 0.353791  0.525847 0.713353 -0.0864597  -0.120478   -0.115216   790 HOH   A O    
5155 O  O    . HOH   G .   ? 0.299972  0.603904 0.631288 0.0414582   -0.111181   -0.0819942  791 HOH   A O    
5156 O  O    . HOH   G .   ? 0.263849  0.591896 0.341443 -0.0008106  0.0500175   -0.0308813  792 HOH   A O    
5157 O  O    . HOH   G .   ? 0.35926   0.399388 0.353612 0.0551741   0.0964765   0.00581162  793 HOH   A O    
5158 O  O    . HOH   G .   ? 0.241991  0.812968 0.466239 -0.00636325 -0.00293836 0.0243777   794 HOH   A O    
5159 O  O    . HOH   G .   ? 0.413263  0.435783 0.578731 -0.0150127  -0.0907755  -0.14334    795 HOH   A O    
5160 O  O    . HOH   G .   ? 0.180295  0.477262 0.41136  -0.0871738  0.0790444   -0.0628504  796 HOH   A O    
5161 O  O    . HOH   G .   ? 0.465756  0.875639 0.433604 -0.081578   -0.106006   0.0980866   797 HOH   A O    
5162 O  O    . HOH   G .   ? 0.406983  0.371861 0.254565 0.0285332   -0.0340679  -0.0010939  798 HOH   A O    
5163 O  O    . HOH   G .   ? 0.533957  0.509652 0.959835 0.0298077   -0.0274376  -0.170727   799 HOH   A O    
5164 O  O    . HOH   G .   ? 0.456853  0.430251 0.501118 -0.0101853  0.0836524   -0.0945813  800 HOH   A O    
5165 O  O    . HOH   G .   ? 0.289243  0.492508 0.389148 -0.0603005  -0.0638483  0.0850805   801 HOH   A O    
5166 O  O    . HOH   G .   ? 0.266984  0.87892  0.33713  0.0531682   -0.0357577  0.187374    802 HOH   A O    
5167 O  O    . HOH   G .   ? 0.218731  0.348174 0.413979 -0.0581088  0.0320399   -0.0935709  803 HOH   A O    
5168 O  O    . HOH   G .   ? 0.297916  0.758314 0.42123  0.118165    -0.0268768  -0.159926   804 HOH   A O    
5169 O  O    . HOH   G .   ? 0.423542  0.895939 0.279303 0.038786    0.0290931   0.0664266   805 HOH   A O    
5170 O  O    . HOH   G .   ? 0.410015  0.574547 0.570445 -0.168444   -0.103166   0.189411    806 HOH   A O    
5171 O  O    . HOH   G .   ? 0.204513  0.383642 0.392907 0.00457077  -0.022458   0.00999464  807 HOH   A O    
5172 O  O    . HOH   G .   ? 0.77524   0.605797 0.380414 0.282354    -0.122258   -0.0549442  808 HOH   A O    
5173 O  O    . HOH   G .   ? 0.798389  0.709563 0.593319 0.142301    -0.0894966  0.180266    809 HOH   A O    
5174 O  O    . HOH   G .   ? 0.332746  0.405075 0.433777 0.00629319  0.0667854   0.0677299   810 HOH   A O    
5175 O  O    . HOH   G .   ? 0.238261  0.405121 0.60804  -0.0533919  0.0529975   -0.0247733  811 HOH   A O    
5176 O  O    . HOH   G .   ? 0.45783   0.700409 0.608143 0.0465164   -0.0754959  -0.151423   812 HOH   A O    
5177 O  O    . HOH   G .   ? 0.563842  0.883501 0.352285 0.329678    0.0800962   0.143481    813 HOH   A O    
5178 O  O    . HOH   G .   ? 0.459514  0.83356  0.367206 -0.0483402  -0.0862853  0.0616816   814 HOH   A O    
5179 O  O    . HOH   G .   ? 0.417443  0.348429 0.625091 -0.026175   -0.0599268  0.0516103   815 HOH   A O    
5180 O  O    . HOH   G .   ? 0.486599  0.324343 0.648227 0.0405145   0.0154693   0.0811898   816 HOH   A O    
5181 O  O    . HOH   G .   ? 0.456854  0.511652 0.366404 -0.168779   0.108955    0.0569782   817 HOH   A O    
5182 O  O    . HOH   G .   ? 0.366488  0.373287 0.408576 -0.100025   -0.0372745  -0.0198004  818 HOH   A O    
5183 O  O    . HOH   G .   ? 0.638955  0.497033 0.785543 0.16239     -0.157752   -0.205329   819 HOH   A O    
5184 O  O    . HOH   G .   ? 0.422882  0.643747 0.482343 0.0846553   0.0208801   0.252154    820 HOH   A O    
5185 O  O    . HOH   G .   ? 0.309623  0.450277 0.742663 -0.032318   -0.110872   0.00691963  821 HOH   A O    
5186 O  O    . HOH   G .   ? 0.280854  0.497329 0.463971 0.0163877   0.0944774   0.103895    822 HOH   A O    
5187 O  O    . HOH   G .   ? 0.230091  0.532582 0.365852 0.00500974  0.00737661  0.00937135  823 HOH   A O    
5188 O  O    . HOH   G .   ? 0.210539  0.393862 0.312032 0.0581174   0.0415633   0.0212078   824 HOH   A O    
5189 O  O    . HOH   G .   ? 0.49494   0.512195 0.771203 0.073404    0.239241    0.200814    825 HOH   A O    
5190 O  O    . HOH   G .   ? 0.364176  0.537303 0.39723  0.0394209   0.0594975   0.0515083   826 HOH   A O    
5191 O  O    . HOH   G .   ? 0.346367  0.405337 0.47317  -0.00495662 0.0191005   0.122234    827 HOH   A O    
5192 O  O    . HOH   G .   ? 0.676897  0.455203 0.405336 -0.00449268 0.0359294   0.130552    828 HOH   A O    
5193 O  O    . HOH   G .   ? 0.563586  0.566505 0.733552 -0.14389    -0.169913   -0.158891   829 HOH   A O    
5194 O  O    . HOH   G .   ? 0.302196  0.548777 0.412101 0.0796958   0.10351     0.0320618   830 HOH   A O    
5195 O  O    . HOH   G .   ? 0.421281  0.479354 0.472309 0.0223901   0.17386     0.0636106   831 HOH   A O    
5196 O  O    . HOH   H .   ? 0.418532  0.614167 0.373529 -0.210044   0.0703212   0.0153857   501 HOH   B O    
5197 O  O    . HOH   H .   ? 0.45235   0.365379 0.492458 -0.0420161  0.133752    -0.191407   502 HOH   B O    
5198 O  O    . HOH   H .   ? 0.651955  0.886763 0.79853  0.164505    -0.0611919  -0.254189   503 HOH   B O    
5199 O  O    . HOH   H .   ? 0.197148  0.460673 0.289455 0.0469713   0.00172629  0.00193664  504 HOH   B O    
5200 O  O    . HOH   H .   ? 0.640983  0.646537 0.46996  -0.298236   -0.0616961  0.0494063   505 HOH   B O    
5201 O  O    . HOH   H .   ? 0.431153  0.620448 0.421147 0.00053281  -0.10795    0.0113088   506 HOH   B O    
5202 O  O    . HOH   H .   ? 0.412061  0.615704 0.479125 -0.107906   -0.0191698  -0.211115   507 HOH   B O    
5203 O  O    . HOH   H .   ? 0.47487   0.413746 0.506751 0.0827716   -0.00059032 0.0199015   508 HOH   B O    
5204 O  O    . HOH   H .   ? 0.260999  0.292415 0.271929 -0.0847699  0.0184982   -0.066493   509 HOH   B O    
5205 O  O    . HOH   H .   ? 0.782759  1.15394  0.601952 0.324438    -0.19638    -0.0219216  510 HOH   B O    
5206 O  O    . HOH   H .   ? 0.601631  0.450592 0.493562 -0.202867   -0.18991    0.181274    511 HOH   B O    
5207 O  O    . HOH   H .   ? 0.284822  0.419685 0.483905 -0.037942   -0.0324742  -0.0954619  512 HOH   B O    
5208 O  O    . HOH   H .   ? 0.321297  0.745206 0.436151 -0.0608463  -0.0405231  -0.165089   513 HOH   B O    
5209 O  O    . HOH   H .   ? 0.215941  0.380925 0.247782 0.0451223   -0.00104981 -0.0574352  514 HOH   B O    
5210 O  O    . HOH   H .   ? 0.254438  0.477947 0.312304 -0.080439   0.0213361   -0.0435258  515 HOH   B O    
5211 O  O    . HOH   H .   ? 0.99426   0.458059 0.308368 0.0761268   -0.140741   0.0461149   516 HOH   B O    
5212 O  O    . HOH   H .   ? 0.216648  0.268744 0.242082 -0.0079132  -0.0246389  -0.0399459  517 HOH   B O    
5213 O  O    . HOH   H .   ? 0.49053   0.758403 0.672346 0.140566    -0.172521   0.0736165   518 HOH   B O    
5214 O  O    . HOH   H .   ? 0.763278  0.365179 0.325944 0.00566232  0.0635118   0.0500809   519 HOH   B O    
5215 O  O    . HOH   H .   ? 0.278927  0.586852 0.357669 0.0438195   0.0397674   0.023591    520 HOH   B O    
5216 O  O    . HOH   H .   ? 0.366321  0.598966 0.235625 0.271194    -0.0724319  -0.102632   521 HOH   B O    
5217 O  O    . HOH   H .   ? 0.206856  0.455395 0.396118 -0.0265088  0.0691175   0.0871772   522 HOH   B O    
5218 O  O    . HOH   H .   ? 0.562955  0.412364 0.556185 -0.184847   -0.0275171  -0.0688175  523 HOH   B O    
5219 O  O    . HOH   H .   ? 0.204648  0.628222 0.477702 0.0647918   0.0264293   0.11886     524 HOH   B O    
5220 O  O    . HOH   H .   ? 0.665391  0.33454  0.554485 -0.0354795  -0.252628   -0.0655259  525 HOH   B O    
5221 O  O    . HOH   H .   ? 0.414366  0.641255 0.433027 -0.257518   0.0438662   -0.182837   526 HOH   B O    
5222 O  O    . HOH   H .   ? 0.546407  0.585526 0.381373 -0.0429502  -0.0218944  0.11381     527 HOH   B O    
5223 O  O    . HOH   H .   ? 0.266009  0.508986 0.303965 0.0247223   0.0534726   -0.0478888  528 HOH   B O    
5224 O  O    . HOH   H .   ? 0.414174  0.489247 0.301928 -0.093681   -0.0449962  -0.0489558  529 HOH   B O    
5225 O  O    . HOH   H .   ? 0.34638   0.662864 0.409031 0.0730705   -0.0679412  0.119816    530 HOH   B O    
5226 O  O    . HOH   H .   ? 0.29222   0.532389 0.500424 -0.0602563  -0.0292171  -0.0892467  531 HOH   B O    
5227 O  O    . HOH   H .   ? 0.406775  0.326587 0.354184 -0.0867258  -0.00149937 0.0215853   532 HOH   B O    
5228 O  O    . HOH   H .   ? 0.222217  0.26333  0.247511 0.0562671   -0.027243   -0.00877914 533 HOH   B O    
5229 O  O    . HOH   H .   ? 0.660949  0.659081 0.71769  -0.00660681 0.0222728   0.205411    534 HOH   B O    
5230 O  O    . HOH   H .   ? 0.419634  0.480016 0.318578 -0.00220555 -0.0469513  0.0534493   535 HOH   B O    
5231 O  O    . HOH   H .   ? 0.195173  0.233697 0.2266   -0.0400632  -0.0193829  -0.0234702  536 HOH   B O    
5232 O  O    . HOH   H .   ? 0.226337  0.363289 0.323834 -0.0728907  -0.0408222  0.012801    537 HOH   B O    
5233 O  O    . HOH   H .   ? 0.168755  0.474929 0.242365 -0.00158967 0.0100558   0.055244    538 HOH   B O    
5234 O  O    . HOH   H .   ? 0.194622  0.452857 0.457718 -0.0231779  0.0407097   -0.142775   539 HOH   B O    
5235 O  O    . HOH   H .   ? 0.560391  0.855166 0.384934 0.00999434  0.138999    0.0257309   540 HOH   B O    
5236 O  O    . HOH   H .   ? 0.515875  0.384966 0.513129 -0.0719419  0.0602669   -0.00322326 541 HOH   B O    
5237 O  O    . HOH   H .   ? 0.15015   0.476783 0.447786 0.0385687   -0.0898448  -0.240683   542 HOH   B O    
5238 O  O    . HOH   H .   ? 0.350069  0.624813 0.405499 -0.0332229  0.124052    -0.236254   543 HOH   B O    
5239 O  O    . HOH   H .   ? 0.321353  0.429146 0.294368 -0.0543733  0.0448251   -0.0392491  544 HOH   B O    
5240 O  O    . HOH   H .   ? 0.325661  0.431275 0.631817 0.0279248   -0.163656   0.0102041   545 HOH   B O    
5241 O  O    . HOH   H .   ? 0.381683  0.636945 0.668833 0.0114091   -0.140418   0.129821    546 HOH   B O    
5242 O  O    . HOH   H .   ? 0.434345  0.402739 0.274217 0.00983804  0.0345507   -0.0312651  547 HOH   B O    
5243 O  O    . HOH   H .   ? 0.300874  0.349173 0.333863 -0.109944   0.0829109   -0.0147845  548 HOH   B O    
5244 O  O    . HOH   H .   ? 0.256208  0.251256 0.263735 -0.0816829  0.0224801   -0.0535713  549 HOH   B O    
5245 O  O    . HOH   H .   ? 0.492701  0.375553 0.478691 0.0132823   0.116403    -0.0780355  550 HOH   B O    
5246 O  O    . HOH   H .   ? 0.26115   0.716011 0.2957   0.0188579   -0.00560355 0.0270988   551 HOH   B O    
5247 O  O    . HOH   H .   ? 0.565462  0.402745 0.621575 0.0807357   -0.079575   0.0917352   552 HOH   B O    
5248 O  O    . HOH   H .   ? 0.251898  0.236979 0.307619 -0.0221835  -0.0109407  -0.0669315  553 HOH   B O    
5249 O  O    . HOH   H .   ? 0.602428  0.356933 0.332678 0.0804548   -0.00287148 0.0931193   554 HOH   B O    
5250 O  O    . HOH   H .   ? 0.331509  0.484394 0.410355 0.143375    -0.00099578 0.0838272   555 HOH   B O    
5251 O  O    . HOH   H .   ? 0.228401  0.408638 0.244072 0.122933    -0.0527146  -0.0709934  556 HOH   B O    
5252 O  O    . HOH   H .   ? 0.496518  0.486083 0.552096 0.0501498   0.0799896   0.0427598   557 HOH   B O    
5253 O  O    . HOH   H .   ? 0.330069  0.653108 0.545034 0.0317899   0.19203     0.0752096   558 HOH   B O    
5254 O  O    . HOH   H .   ? 0.651601  0.581105 0.386876 0.132007    -0.10806    -0.0851923  559 HOH   B O    
5255 O  O    . HOH   H .   ? 0.373093  0.379391 0.326044 0.0252341   -0.0504313  -0.00025642 560 HOH   B O    
5256 O  O    . HOH   H .   ? 0.264944  0.380952 0.269247 0.0115254   -0.0417968  0.033468    561 HOH   B O    
5257 O  O    . HOH   H .   ? 0.456591  0.630603 0.370312 -0.197489   0.0660625   -0.135726   562 HOH   B O    
5258 O  O    . HOH   H .   ? 0.558979  0.469223 0.5651   -0.0238971  0.159699    -0.166082   563 HOH   B O    
5259 O  O    . HOH   H .   ? 0.721462  0.288284 0.352821 -0.0528537  0.0596072   -0.053014   564 HOH   B O    
5260 O  O    . HOH   H .   ? 0.495102  0.453167 0.492602 -0.167864   0.0901704   -0.0504413  565 HOH   B O    
5261 O  O    . HOH   H .   ? 0.300896  0.292857 0.340863 -0.00208222 -0.0556766  -0.0174321  566 HOH   B O    
5262 O  O    . HOH   H .   ? 0.133054  0.484008 0.181231 0.0109957   -0.0354554  -0.0470216  567 HOH   B O    
5263 O  O    . HOH   H .   ? 0.505421  0.329326 0.211177 -0.117029   -0.0656324  0.0347398   568 HOH   B O    
5264 O  O    . HOH   H .   ? 0.382233  0.421042 0.362197 -0.0880172  0.0200252   -0.0646046  569 HOH   B O    
5265 O  O    . HOH   H .   ? 0.448502  0.564089 0.546401 -0.127245   0.18007     -0.190295   570 HOH   B O    
5266 O  O    . HOH   H .   ? 0.359344  0.384967 0.511516 0.0640891   0.0500521   -0.0330014  571 HOH   B O    
5267 O  O    . HOH   H .   ? 0.296889  0.448738 0.393834 0.112085    0.0117571   -0.00782379 572 HOH   B O    
5268 O  O    . HOH   H .   ? 0.138272  0.253599 0.199347 0.0435387   -0.00019267 -0.00085586 573 HOH   B O    
5269 O  O    . HOH   H .   ? 0.297502  0.47292  0.27355  0.0231967   -0.00691329 0.0722111   574 HOH   B O    
5270 O  O    . HOH   H .   ? 0.17913   0.206727 0.180432 -0.00180622 -0.0280479  -0.00286562 575 HOH   B O    
5271 O  O    . HOH   H .   ? 0.576996  0.431199 0.465704 0.0194748   -0.109215   0.0380095   576 HOH   B O    
5272 O  O    . HOH   H .   ? 0.339811  0.235501 0.280637 0.0423825   -0.131183   -0.0390614  577 HOH   B O    
5273 O  O    . HOH   H .   ? 0.440928  0.475032 0.561273 -0.078609   0.0144447   -0.0550452  578 HOH   B O    
5274 O  O    . HOH   H .   ? 0.356601  0.417659 0.448399 -0.0122275  -0.0787609  0.0427998   579 HOH   B O    
5275 O  O    . HOH   H .   ? 0.464734  0.342744 0.386723 -0.0127968  -0.194357   0.0401244   580 HOH   B O    
5276 O  O    . HOH   H .   ? 0.291197  0.670096 0.511105 0.0737263   -0.156727   -0.0804631  581 HOH   B O    
5277 O  O    . HOH   H .   ? 0.330714  0.509181 0.661259 0.0193014   -0.00445354 -0.0183924  582 HOH   B O    
5278 O  O    . HOH   H .   ? 0.604926  0.594106 0.541656 -0.16604    -0.134472   0.262324    583 HOH   B O    
5279 O  O    . HOH   H .   ? 0.366941  0.318751 0.201378 0.0359392   -0.0080351  0.017845    584 HOH   B O    
5280 O  O    . HOH   H .   ? 0.168599  0.348074 0.197823 0.0321168   -0.0365866  -0.0579738  585 HOH   B O    
5281 O  O    . HOH   H .   ? 0.292487  0.271778 0.26978  -0.00423302 -0.0221593  0.0323738   586 HOH   B O    
5282 O  O    . HOH   H .   ? 0.374877  0.703677 0.31388  -0.159578   0.0756869   0.0228396   587 HOH   B O    
5283 O  O    . HOH   H .   ? 0.420284  0.586457 0.555138 -0.167331   -0.105291   0.113812    588 HOH   B O    
5284 O  O    . HOH   H .   ? 0.240543  0.556447 0.473134 -0.083859   0.0859088   -0.105751   589 HOH   B O    
5285 O  O    . HOH   H .   ? 0.51547   0.91376  0.50795  -0.0150446  -0.103227   0.0544397   590 HOH   B O    
5286 O  O    . HOH   H .   ? 0.24664   0.378575 0.280396 -0.00111306 0.0412791   0.0652836   591 HOH   B O    
5287 O  O    . HOH   H .   ? 0.607518  0.385083 0.481849 -0.0667114  0.00137234  0.0239396   592 HOH   B O    
5288 O  O    . HOH   H .   ? 0.629058  0.39742  0.600871 -0.125396   -0.257225   0.0469253   593 HOH   B O    
5289 O  O    . HOH   H .   ? 0.30234   0.945998 0.667497 0.0154831   0.0428193   -0.0907153  594 HOH   B O    
5290 O  O    . HOH   H .   ? 0.748745  0.553348 0.36271  -0.151457   0.157528    0.0546768   595 HOH   B O    
5291 O  O    . HOH   H .   ? 0.521719  0.395039 0.679112 -0.152073   -0.113876   0.0992832   596 HOH   B O    
5292 O  O    . HOH   H .   ? 0.729865  0.42959  0.645985 0.00394404  -0.355651   -0.0819874  597 HOH   B O    
5293 O  O    . HOH   H .   ? 0.297349  0.336904 0.33818  0.0341574   -0.0881546  0.0261856   598 HOH   B O    
5294 O  O    . HOH   H .   ? 0.341582  0.59568  0.243937 0.0646939   -0.0248547  -0.119214   599 HOH   B O    
5295 O  O    . HOH   H .   ? 0.193444  0.278857 0.196149 0.0239438   -0.0720935  -0.00074675 600 HOH   B O    
5296 O  O    . HOH   H .   ? 0.242385  0.312486 0.230118 -0.0849581  0.0128176   -0.0600752  601 HOH   B O    
5297 O  O    . HOH   H .   ? 0.333478  0.54244  0.512426 -0.038941   -0.158193   0.182845    602 HOH   B O    
5298 O  O    . HOH   H .   ? 0.219266  0.368231 0.385289 0.0075574   -0.0431012  -0.0189778  603 HOH   B O    
5299 O  O    . HOH   H .   ? 0.160586  0.229875 0.184548 0.0139347   0.017348    -0.00717306 604 HOH   B O    
5300 O  O    . HOH   H .   ? 0.376032  0.483151 0.791886 0.020865    -0.128485   0.0233806   605 HOH   B O    
5301 O  O    . HOH   H .   ? 0.49782   0.480049 0.36705  -0.0200684  0.0238883   -0.156029   606 HOH   B O    
5302 O  O    . HOH   H .   ? 0.808019  0.322065 1.0489   0.366113    -0.230924   0.0283849   607 HOH   B O    
5303 O  O    . HOH   H .   ? 0.481372  0.369744 0.35322  0.0610328   0.0208607   0.0917537   608 HOH   B O    
5304 O  O    . HOH   H .   ? 0.515553  0.397585 0.551882 0.130983    -0.10619    -0.00877158 609 HOH   B O    
5305 O  O    . HOH   H .   ? 0.214256  0.534622 0.216544 0.103193    -0.0803768  -0.0848887  610 HOH   B O    
5306 O  O    . HOH   H .   ? 0.58402   0.918853 0.303971 -0.342651   0.122647    -0.00820304 611 HOH   B O    
5307 O  O    . HOH   H .   ? 0.204187  0.569754 0.382094 0.0169089   0.0159009   0.113571    612 HOH   B O    
5308 O  O    . HOH   H .   ? 0.324965  0.657477 0.475526 -0.0853957  0.169342    -0.134795   613 HOH   B O    
5309 O  O    . HOH   H .   ? 0.257579  0.87712  0.503812 -0.0145873  -0.0469443  -0.260576   614 HOH   B O    
5310 O  O    . HOH   H .   ? 0.298348  0.344286 0.270389 -0.0648044  0.00608937  0.0565123   615 HOH   B O    
5311 O  O    . HOH   H .   ? 0.148831  0.18149  0.177225 -0.0109372  -0.047497   -0.0199113  616 HOH   B O    
5312 O  O    . HOH   H .   ? 0.10495   0.24831  0.332793 -0.0152254  0.0168936   -0.0421004  617 HOH   B O    
5313 O  O    . HOH   H .   ? 0.356497  0.462483 0.410583 -0.169783   0.11328     -0.0579619  618 HOH   B O    
5314 O  O    . HOH   H .   ? 0.562803  0.50624  0.344739 0.0017657   -0.0226431  -0.0828849  619 HOH   B O    
5315 O  O    . HOH   H .   ? 0.139979  0.234523 0.187371 -0.00642169 -0.0193776  -0.0333691  620 HOH   B O    
5316 O  O    . HOH   H .   ? 0.393079  0.478692 0.55898  0.0456516   -0.194221   -0.109488   621 HOH   B O    
5317 O  O    . HOH   H .   ? 0.259492  0.522944 0.573652 0.0241173   -0.0618031  0.0477674   622 HOH   B O    
5318 O  O    . HOH   H .   ? 0.376611  0.309284 0.228793 -0.0337258  0.0253337   -0.00698385 623 HOH   B O    
5319 O  O    . HOH   H .   ? 0.200318  0.348782 0.220017 -0.00719874 -0.0157616  0.0277985   624 HOH   B O    
5320 O  O    . HOH   H .   ? 0.184691  0.280799 0.447969 0.0117049   0.0330684   -0.0318458  625 HOH   B O    
5321 O  O    . HOH   H .   ? 0.592466  0.427298 0.870085 -0.12692    -0.352282   0.147056    626 HOH   B O    
5322 O  O    . HOH   H .   ? 0.208783  0.428421 0.318706 0.0690076   -0.0196432  0.00524036  627 HOH   B O    
5323 O  O    . HOH   H .   ? 0.456042  0.511702 0.315172 -0.0758266  -0.0668283  0.00051235  628 HOH   B O    
5324 O  O    . HOH   H .   ? 0.544626  0.497966 0.502323 0.220435    0.117527    0.100801    629 HOH   B O    
5325 O  O    . HOH   H .   ? 0.176973  0.205994 0.239689 0.00266685  -0.030613   -0.00630769 630 HOH   B O    
5326 O  O    . HOH   H .   ? 0.460749  0.717978 0.443005 0.0293977   0.217514    0.0680142   631 HOH   B O    
5327 O  O    . HOH   H .   ? 0.290611  0.508622 0.542926 -0.0876526  -0.0441262  -0.102963   632 HOH   B O    
5328 O  O    . HOH   H .   ? 0.598046  0.615739 0.913954 0.0261251   0.195546    -0.163193   633 HOH   B O    
5329 O  O    . HOH   H .   ? 0.697239  0.432744 0.665623 -0.0758588  -0.0325818  -0.115826   634 HOH   B O    
5330 O  O    . HOH   H .   ? 0.650438  0.821607 0.346185 0.162511    -0.199176   -0.0935618  635 HOH   B O    
5331 O  O    . HOH   H .   ? 0.306373  0.554394 0.411846 -0.0702271  0.00212943  -0.0235684  636 HOH   B O    
5332 O  O    . HOH   H .   ? 0.265788  0.467786 0.278579 0.00243328  -0.0250961  0.00383807  637 HOH   B O    
5333 O  O    . HOH   H .   ? 0.152859  0.292331 0.241961 0.0217843   -0.00096364 0.0254027   638 HOH   B O    
5334 O  O    . HOH   H .   ? 0.198045  0.278394 0.256493 -0.0771225  0.00557751  -0.0571219  639 HOH   B O    
5335 O  O    . HOH   H .   ? 0.33138   0.624019 0.409703 -0.150503   0.0972056   -0.161928   640 HOH   B O    
5336 O  O    . HOH   H .   ? 0.267278  0.416863 0.197842 0.050296    0.0571489   0.021706    641 HOH   B O    
5337 O  O    . HOH   H .   ? 0.443037  0.655192 0.757081 0.0960827   0.166803    0.0340409   642 HOH   B O    
5338 O  O    . HOH   H .   ? 0.61047   0.481982 0.373889 0.164041    0.0735669   0.0100628   643 HOH   B O    
5339 O  O    . HOH   H .   ? 0.337777  0.628422 0.509394 -0.129919   -0.0601861  -0.0662446  644 HOH   B O    
5340 O  O    . HOH   H .   ? 0.333629  0.41053  0.474029 -0.0416055  -0.00867934 0.0257448   645 HOH   B O    
5341 O  O    . HOH   H .   ? 0.373912  0.400877 0.407921 -0.0498261  -0.106328   0.11131     646 HOH   B O    
5342 O  O    . HOH   H .   ? 0.40305   0.284687 0.371342 0.00937916  -0.182777   0.0041003   647 HOH   B O    
5343 O  O    . HOH   H .   ? 0.253385  0.608651 0.326031 0.162451    -0.0380862  -0.0329206  648 HOH   B O    
5344 O  O    . HOH   H .   ? 0.438836  0.28411  0.597775 -0.0861509  -0.185397   0.0777314   649 HOH   B O    
5345 O  O    . HOH   H .   ? 0.18692   0.314349 0.330205 0.0279105   -0.0175705  0.0807267   650 HOH   B O    
5346 O  O    . HOH   H .   ? 0.257936  0.378462 0.391688 0.0352453   0.125503    0.143438    651 HOH   B O    
5347 O  O    . HOH   H .   ? 0.349514  0.3635   0.46149  -0.107444   -0.163866   0.191767    652 HOH   B O    
5348 O  O    . HOH   H .   ? 0.139356  0.295477 0.256903 0.0150724   -0.0372935  -0.0107812  653 HOH   B O    
5349 O  O    . HOH   H .   ? 0.220487  0.263534 0.35351  0.014322    0.00591779  -0.00056974 654 HOH   B O    
5350 O  O    . HOH   H .   ? 0.315316  0.338542 0.248184 0.0737828   0.0262082   0.017942    655 HOH   B O    
5351 O  O    . HOH   H .   ? 0.314437  0.322312 0.345215 0.0733369   -0.0763647  -0.0631666  656 HOH   B O    
5352 O  O    . HOH   H .   ? 0.455624  0.570089 0.328138 -0.161727   -0.0231842  0.0365135   657 HOH   B O    
5353 O  O    . HOH   H .   ? 0.329023  0.508029 0.386486 -0.137552   0.0845851   -0.0214274  658 HOH   B O    
5354 O  O    . HOH   H .   ? 0.242553  0.693853 0.679841 -0.107173   0.072713    -0.20339    659 HOH   B O    
5355 O  O    . HOH   H .   ? 0.456633  0.289967 0.469005 -0.0902992  0.0538597   -0.0110116  660 HOH   B O    
5356 O  O    . HOH   H .   ? 0.866938  0.472386 0.271017 0.0676021   -0.081053   0.0230296   661 HOH   B O    
5357 O  O    . HOH   H .   ? 0.300436  0.463618 0.284431 -0.0689073  -0.00096273 0.00784444  662 HOH   B O    
5358 O  O    . HOH   H .   ? 0.281358  0.313635 0.267154 -0.0852805  -0.104817   0.0231762   663 HOH   B O    
5359 O  O    . HOH   H .   ? 0.159931  0.36436  0.198831 0.0410931   0.00433001  -0.0251767  664 HOH   B O    
5360 O  O    . HOH   H .   ? 0.25565   0.424225 0.63256  -0.0103705  0.0993233   0.0611525   665 HOH   B O    
5361 O  O    . HOH   H .   ? 0.368877  0.482483 0.506133 -0.081958   0.0770523   -0.111521   666 HOH   B O    
5362 O  O    . HOH   H .   ? 0.378582  0.419297 0.359417 0.1409      0.0427763   0.0746602   667 HOH   B O    
5363 O  O    . HOH   H .   ? 0.401886  0.378423 0.402179 0.070337    0.0521907   0.0510273   668 HOH   B O    
5364 O  O    . HOH   H .   ? 0.305894  0.49676  0.968685 -0.0212328  0.00779643  0.193862    669 HOH   B O    
5365 O  O    . HOH   H .   ? 0.265421  0.40978  0.383255 0.0368485   -0.145817   -0.0392856  670 HOH   B O    
5366 O  O    . HOH   H .   ? 0.372423  0.490835 0.416887 -0.0354444  -0.107479   0.152937    671 HOH   B O    
5367 O  O    . HOH   H .   ? 0.213383  0.56053  0.488169 0.0557353   -0.00841297 -0.063372   672 HOH   B O    
5368 O  O    . HOH   H .   ? 0.211194  0.448625 0.173225 0.0623083   -0.0181725  -0.0212828  673 HOH   B O    
5369 O  O    . HOH   H .   ? 0.180691  0.552585 0.289037 0.0266538   -0.046748   -0.00431069 674 HOH   B O    
5370 O  O    . HOH   H .   ? 0.220413  0.442925 0.258599 -0.0810444  0.0639667   0.037102    675 HOH   B O    
5371 O  O    . HOH   H .   ? 0.626054  0.438188 0.519436 0.139898    0.121027    -0.0889026  676 HOH   B O    
5372 O  O    . HOH   H .   ? 0.361817  0.521028 0.583644 -0.0133131  -0.113047   -0.0119316  677 HOH   B O    
5373 O  O    . HOH   H .   ? 0.248518  0.517588 0.333134 0.0638172   0.0144242   0.0495358   678 HOH   B O    
5374 O  O    . HOH   H .   ? 0.452158  0.232838 0.238781 -0.0458041  0.0473864   -0.0297667  679 HOH   B O    
5375 O  O    . HOH   H .   ? 0.488074  0.526382 0.312161 0.159732    0.00498651  0.0623231   680 HOH   B O    
5376 O  O    . HOH   H .   ? 0.281938  0.564088 0.321298 0.0704471   -0.0396744  0.0858092   681 HOH   B O    
5377 O  O    . HOH   H .   ? 0.20929   0.363658 0.182802 -0.0097769  -0.0327709  0.0110481   682 HOH   B O    
5378 O  O    . HOH   H .   ? 0.321382  0.574094 0.449153 -0.0749356  0.0457048   0.0796199   683 HOH   B O    
5379 O  O    . HOH   H .   ? 0.7414    0.74405  0.897694 -0.167828   0.0207462   -0.201329   684 HOH   B O    
5380 O  O    . HOH   H .   ? 0.321383  0.412598 0.273304 0.0622122   0.0609083   0.0205239   685 HOH   B O    
5381 O  O    . HOH   H .   ? 0.555709  0.546677 0.419354 -0.0897307  -0.132398   0.132688    686 HOH   B O    
5382 O  O    . HOH   H .   ? 0.769076  0.403408 0.33537  -0.0483569  0.12536     -0.030766   687 HOH   B O    
5383 O  O    . HOH   H .   ? 0.771184  1.75606  0.726862 1.07992     0.116806    0.562515    688 HOH   B O    
5384 O  O    . HOH   H .   ? 0.461828  0.325056 0.335031 -0.0529763  -0.134108   0.0875619   689 HOH   B O    
5385 O  O    . HOH   H .   ? 0.377743  0.588465 0.270565 -0.0795506  -0.0612303  0.131439    690 HOH   B O    
5386 O  O    . HOH   H .   ? 0.318053  0.622055 0.648836 -0.0910337  -0.0822164  -0.0845572  691 HOH   B O    
5387 O  O    . HOH   H .   ? 0.258576  0.441003 0.228555 0.0435584   0.0451812   0.025887    692 HOH   B O    
5388 O  O    . HOH   H .   ? 0.492796  0.313373 0.589786 -0.0480699  -0.166433   -0.0212032  693 HOH   B O    
5389 O  O    . HOH   H .   ? 0.333605  0.640245 0.422337 -0.154991   -0.0466443  0.0739455   694 HOH   B O    
5390 O  O    . HOH   H .   ? 0.609016  0.341262 0.607447 0.153839    0.205185    0.0428789   695 HOH   B O    
5391 O  O    . HOH   H .   ? 0.456383  0.545664 0.526842 -0.117237   0.195853    0.0423488   696 HOH   B O    
5392 O  O    . HOH   H .   ? 0.500809  0.389225 0.446111 -0.0102773  0.0390025   -0.005907   697 HOH   B O    
5393 O  O    . HOH   H .   ? 0.856476  0.463644 0.513752 -0.104493   -0.144401   0.108087    698 HOH   B O    
5394 O  O    . HOH   H .   ? 0.73653   0.787107 0.66602  -0.106384   0.183709    -0.188064   699 HOH   B O    
5395 O  O    . HOH   H .   ? 0.32231   0.472352 0.385931 0.0290349   0.0282534   -0.00703868 700 HOH   B O    
5396 O  O    . HOH   H .   ? 0.536714  0.667256 0.361772 -0.176191   -0.0620328  0.0612313   701 HOH   B O    
5397 O  O    . HOH   H .   ? 0.412471  0.502858 0.328177 -0.156787   -0.0856398  0.0570704   702 HOH   B O    
5398 O  O    . HOH   H .   ? 0.621685  0.632021 0.354929 -0.176716   0.0234361   -0.0320688  703 HOH   B O    
5399 O  O    . HOH   H .   ? 0.361918  0.575271 0.793813 0.0893022   0.00342806  0.27196     704 HOH   B O    
5400 O  O    . HOH   H .   ? 0.21384   0.33436  0.223325 0.0153882   -0.0131811  -0.02055    705 HOH   B O    
5401 O  O    . HOH   H .   ? 0.470157  0.380778 0.456247 0.0947801   -0.0307532  -0.0189612  706 HOH   B O    
5402 O  O    . HOH   H .   ? 0.371799  0.524097 0.457445 -0.180106   0.0468897   -0.0217489  707 HOH   B O    
5403 O  O    . HOH   H .   ? 0.348321  0.533674 0.551368 -0.158139   0.177326    -0.132169   708 HOH   B O    
5404 O  O    . HOH   H .   ? 0.658867  0.379152 0.921975 -0.0390741  -0.347819   0.117858    709 HOH   B O    
5405 O  O    . HOH   H .   ? 0.389735  0.497999 0.516537 0.041963    0.0407827   -0.00094202 710 HOH   B O    
5406 O  O    . HOH   H .   ? 0.255996  0.408217 0.261068 0.0334276   -0.00235782 -0.0175772  711 HOH   B O    
5407 O  O    . HOH   H .   ? 0.533363  0.459407 0.330998 0.0788385   -0.144527   0.0175349   712 HOH   B O    
5408 O  O    . HOH   H .   ? 0.592421  0.622144 0.408057 -0.0628591  0.0178732   0.138561    713 HOH   B O    
5409 O  O    . HOH   H .   ? 0.309089  0.581929 0.288881 0.190178    -0.0616989  0.0301058   714 HOH   B O    
5410 O  O    . HOH   H .   ? 0.521581  0.631173 0.369843 0.229377    -0.135838   -0.0934097  715 HOH   B O    
5411 O  O    . HOH   H .   ? 0.603041  0.700829 0.3564   0.0338836   0.0415767   -0.143367   716 HOH   B O    
5412 O  O    . HOH   H .   ? 1.0619    0.390938 0.639852 -0.139962   -0.295993   0.0903952   717 HOH   B O    
5413 O  O    . HOH   H .   ? 0.550808  0.520075 0.638411 -0.0929981  0.228491    -0.0967955  718 HOH   B O    
5414 O  O    . HOH   H .   ? 0.58394   0.428885 0.418535 0.0812351   -0.197931   0.00524241  719 HOH   B O    
5415 O  O    . HOH   H .   ? 0.320467  0.491536 0.418861 0.0840104   0.0243845   -0.06092    720 HOH   B O    
5416 O  O    . HOH   H .   ? 0.529105  0.802057 0.560241 0.0306774   0.0329934   -0.257336   721 HOH   B O    
5417 O  O    . HOH   H .   ? 0.543839  0.387006 0.576918 -0.0218937  -0.25145    0.00687901  722 HOH   B O    
5418 O  O    . HOH   H .   ? 0.488695  0.365347 0.513393 -0.0466286  0.0858899   0.0600361   723 HOH   B O    
5419 O  O    . HOH   H .   ? 0.507513  0.514094 0.494229 -0.155922   -0.174097   0.0716103   724 HOH   B O    
5420 O  O    . HOH   H .   ? 0.897434  1.50119  0.41225  0.215632    -0.249584   0.220537    725 HOH   B O    
5421 O  O    . HOH   H .   ? 0.257445  0.334511 0.249037 -0.0582743  0.0233953   -0.0630696  726 HOH   B O    
5422 O  O    . HOH   H .   ? 0.528411  0.601174 0.352489 -0.0920398  -0.0462626  0.10961     727 HOH   B O    
5423 O  O    . HOH   H .   ? 0.216573  0.478314 0.320022 0.109168    0.0212854   0.0855179   728 HOH   B O    
5424 O  O    . HOH   H .   ? 0.645633  0.4478   0.428767 -0.0854754  -0.070152   0.149196    729 HOH   B O    
5425 O  O    . HOH   H .   ? 0.581621  0.442533 0.569873 0.130531    0.138339    0.145325    730 HOH   B O    
5426 O  O    . HOH   H .   ? 0.688381  0.327156 0.402554 -0.125012   -0.170621   0.0243802   731 HOH   B O    
5427 O  O    . HOH   H .   ? 0.40607   0.527368 0.513193 0.0387441   -0.0235696  0.123765    732 HOH   B O    
5428 O  O    . HOH   H .   ? 0.433151  0.382649 0.255116 -0.0424368  -0.100933   0.00951227  733 HOH   B O    
5429 O  O    . HOH   H .   ? 0.597578  0.518704 0.549345 0.109988    -0.0430696  -0.234442   734 HOH   B O    
5430 O  O    . HOH   H .   ? 0.36701   0.559658 0.464319 0.186496    0.0769751   -0.012776   735 HOH   B O    
5431 O  O    . HOH   H .   ? 0.61086   0.646713 0.840824 -0.0600887  0.303909    -0.0379407  736 HOH   B O    
5432 O  O    . HOH   H .   ? 0.359244  0.710699 0.519312 -0.00476805 -0.128001   -0.0152782  737 HOH   B O    
5433 O  O    . HOH   H .   ? 0.619151  0.558374 0.519788 0.224646    0.0382067   -0.0456376  738 HOH   B O    
5434 O  O    . HOH   H .   ? 0.281759  0.691244 0.532543 0.149728    0.0291067   0.0919577   739 HOH   B O    
5435 O  O    . HOH   H .   ? 0.36653   0.381103 0.295328 -0.106193   -0.00809278 -4.991e-05  740 HOH   B O    
5436 O  O    . HOH   H .   ? 0.231795  0.46546  0.264721 0.0544829   -0.0433892  -0.0128479  741 HOH   B O    
5437 O  O    . HOH   H .   ? 0.34677   0.381548 0.20338  -0.062926   -0.11263    0.0274235   742 HOH   B O    
5438 O  O    . HOH   H .   ? 0.357704  0.546326 0.38302  0.0369999   -0.0407346  0.0586674   743 HOH   B O    
5439 O  O    . HOH   H .   ? 0.455308  0.449528 0.460131 -0.0103419  -0.108798   0.0520858   744 HOH   B O    
5440 O  O    . HOH   H .   ? 0.597391  0.471645 0.520094 0.14093     -0.0622554  0.0262852   745 HOH   B O    
5441 O  O    . HOH   H .   ? 0.356454  0.725443 0.385086 -0.0960199  0.0471232   0.00965062  746 HOH   B O    
5442 O  O    . HOH   H .   ? 0.42266   0.500033 0.684816 -0.054575   0.0981756   -0.0602246  747 HOH   B O    
5443 O  O    . HOH   H .   ? 0.450445  0.420022 0.464927 0.0671749   -0.211207   0.0458927   748 HOH   B O    
5444 O  O    . HOH   H .   ? 0.427156  0.452258 0.548709 -0.0375728  0.13738     0.10644     749 HOH   B O    
5445 O  O    . HOH   H .   ? 0.595856  0.444354 0.459936 0.179331    0.0266851   0.0504354   750 HOH   B O    
5446 O  O    . HOH   H .   ? 0.256924  0.400734 0.286231 0.0494129   -0.0507068  -0.0620417  751 HOH   B O    
5447 O  O    . HOH   H .   ? 0.296997  0.49507  0.65404  0.0225898   0.0510863   -0.0345646  752 HOH   B O    
5448 O  O    . HOH   H .   ? 0.853146  0.480194 0.448597 -0.0787293  0.287857    -0.0202287  753 HOH   B O    
5449 O  O    . HOH   H .   ? 0.2831    0.446427 0.574673 -0.02981    0.133711    0.079282    754 HOH   B O    
5450 O  O    . HOH   H .   ? 0.48861   0.518098 0.605182 -0.103595   0.030761    -0.0340505  755 HOH   B O    
5451 O  O    . HOH   H .   ? 0.518441  0.631285 0.352808 -0.0131518  -0.180952   0.0284647   756 HOH   B O    
5452 O  O    . HOH   H .   ? 0.456174  0.371527 0.451036 -0.0415861  0.115492    -0.0328756  757 HOH   B O    
5453 O  O    . HOH   H .   ? 0.447863  0.629471 0.587613 0.105471    0.147966    -0.012628   758 HOH   B O    
5454 O  O    . HOH   H .   ? 0.514223  0.889504 0.478209 -0.0989121  0.00681439  0.021457    759 HOH   B O    
5455 O  O    . HOH   H .   ? 0.736485  0.564443 0.43646  0.199477    0.227283    0.152487    760 HOH   B O    
5456 O  O    . HOH   H .   ? 0.396517  0.67692  0.387235 -0.259941   0.0441594   0.0427069   761 HOH   B O    
5457 O  O    . HOH   H .   ? 0.235683  0.571166 0.303112 -0.00916218 0.0303653   -0.0827847  762 HOH   B O    
5458 O  O    . HOH   H .   ? 0.302896  0.547208 0.423084 0.0808717   -0.0058251  -0.0639385  763 HOH   B O    
5459 O  O    . HOH   H .   ? 0.808603  0.717966 0.505764 0.294904    -0.132334   -0.0224124  764 HOH   B O    
5460 O  O    . HOH   H .   ? 0.316484  0.450866 0.344262 -0.0516632  -0.124464   0.0303217   765 HOH   B O    
5461 O  O    . HOH   H .   ? 0.275233  0.819374 0.452713 0.0450918   0.0691528   -0.0551478  766 HOH   B O    
5462 O  O    . HOH   H .   ? 1.12159   0.874862 0.489472 -0.0450458  0.0412001   0.0323339   767 HOH   B O    
5463 O  O    . HOH   H .   ? 0.55173   0.662233 0.395956 0.12536     -0.158313   0.0639015   768 HOH   B O    
5464 O  O    . HOH   H .   ? 0.610125  0.405393 0.257403 0.118373    -0.0629495  -0.0298064  769 HOH   B O    
5465 O  O    . HOH   H .   ? 0.534441  0.609105 0.405845 0.00394095  -0.0786935  -0.0286261  770 HOH   B O    
5466 O  O    . HOH   H .   ? 0.682787  0.487005 0.741837 -0.0289878  -0.383112   0.0254158   771 HOH   B O    
5467 O  O    . HOH   H .   ? 0.569734  0.962031 0.737812 0.0502807   0.0835465   -0.119096   772 HOH   B O    
5468 O  O    . HOH   H .   ? 0.498493  0.908719 0.561454 0.0411228   0.0257882   0.106455    773 HOH   B O    
# 
