data_9HAJ
# 
_entry.id   9HAJ 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9HAJ         pdb_00009haj 10.2210/pdb9haj/pdb 
WWPDB D_1292142903 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-03-05 ? 
2 'Structure model' 1 1 2025-04-16 ? 
3 'Structure model' 1 2 2025-05-07 ? 
# 
_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             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Database references' 
2 3 'Structure model' 'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
3 3 'Structure model' citation        
4 3 'Structure model' citation_author 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1  2 'Structure model' '_citation.country'                 
2  2 'Structure model' '_citation.journal_abbrev'          
3  2 'Structure model' '_citation.journal_id_ASTM'         
4  2 'Structure model' '_citation.journal_id_CSD'          
5  2 'Structure model' '_citation.journal_id_ISSN'         
6  2 'Structure model' '_citation.pdbx_database_id_DOI'    
7  2 'Structure model' '_citation.pdbx_database_id_PubMed' 
8  2 'Structure model' '_citation.title'                   
9  2 'Structure model' '_citation.year'                    
10 3 'Structure model' '_citation.journal_volume'          
11 3 'Structure model' '_citation.page_first'              
12 3 'Structure model' '_citation.page_last'               
13 3 'Structure model' '_citation_author.identifier_ORCID' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9HAJ 
_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                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            J.Med.Chem. 
_citation.journal_id_ASTM           JMCMAR 
_citation.journal_id_CSD            0151 
_citation.journal_id_ISSN           0022-2623 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            68 
_citation.language                  ? 
_citation.page_first                8269 
_citation.page_last                 8294 
_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                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/acs.jmedchem.4c02941 
_citation.pdbx_database_id_PubMed   40186586 
_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 'Kimmerlin, T.'         2 ? 
primary 'Mac Sweeney, A.'       3 ? 
primary 'Bourquin, G.'          4 ? 
primary 'Lange, R.'             5 ? 
primary 'Ritz, D.'              6 ? 
primary 'Richard-Bildstein, S.' 7 ? 
primary 'Regeon, S.'            8 ? 
primary 'Czodrowski, P.'        9 ? 
# 
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]-1-(5-chloranylpyridin-3-yl)carbonyl-~{N}-ethyl-1,4-diazepane-5-carboxamide' 507.851 
2   ?         ? ? ? 
3 non-polymer syn 'DIMETHYL SULFOXIDE' 78.133    1   ?         ? ? ? 
4 non-polymer syn 'CHLORIDE ION' 35.453    1   ?         ? ? ? 
5 water       nat water 18.015    644 ?         ? ? ? 
# 
_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]-1-(5-chloranylpyridin-3-yl)carbonyl-~{N}-ethyl-1,4-diazepane-5-carboxamide' A1ITJ 
3 'DIMETHYL SULFOXIDE'                                                                                                       DMS   
4 'CHLORIDE ION'                                                                                                             CL    
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 
A1ITJ non-polymer         . 
'(5~{R})-4-[(4-bromanyl-2-ethyl-phenyl)methyl]-1-(5-chloranylpyridin-3-yl)carbonyl-~{N}-ethyl-1,4-diazepane-5-carboxamide' ? 
'C23 H28 Br Cl N4 O2' 507.851 
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 
DMS   non-polymer         . 'DIMETHYL SULFOXIDE' ? 'C2 H6 O S'           78.133  
GLN   'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3'        146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'          147.129 
GLY   'peptide linking'   y GLYCINE ? 'C2 H5 N O2'          75.067  
HIS   'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1'      156.162 
HOH   non-polymer         . WATER ? 'H2 O'                18.015  
ILE   'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2'         131.173 
LEU   'L-peptide linking' y LEUCINE ? 'C6 H13 N O2'         131.173 
LYS   'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1'      147.195 
MET   'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S'       149.211 
PHE   'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2'         165.189 
PRO   'L-peptide linking' y PROLINE ? 'C5 H9 N O2'          115.130 
SER   'L-peptide linking' y SERINE ? 'C3 H7 N O3'          105.093 
THR   'L-peptide linking' y THREONINE ? 'C4 H9 N O3'          119.119 
TRP   'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2'       204.225 
TYR   'L-peptide linking' y TYROSINE ? 'C9 H11 N O3'         181.189 
VAL   'L-peptide linking' y VALINE ? 'C5 H11 N O2'         117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   1   1   SER SER A . n 
A 1 2   GLY 2   2   2   GLY GLY A . n 
A 1 3   PHE 3   3   3   PHE PHE A . n 
A 1 4   ARG 4   4   4   ARG ARG A . n 
A 1 5   LYS 5   5   5   LYS LYS A . n 
A 1 6   MET 6   6   6   MET MET A . n 
A 1 7   ALA 7   7   7   ALA ALA A . n 
A 1 8   PHE 8   8   8   PHE PHE A . n 
A 1 9   PRO 9   9   9   PRO PRO A . n 
A 1 10  SER 10  10  10  SER SER A . n 
A 1 11  GLY 11  11  11  GLY GLY A . n 
A 1 12  LYS 12  12  12  LYS LYS A . n 
A 1 13  VAL 13  13  13  VAL VAL A . n 
A 1 14  GLU 14  14  14  GLU GLU A . n 
A 1 15  GLY 15  15  15  GLY GLY A . n 
A 1 16  CYS 16  16  16  CYS CYS A . n 
A 1 17  MET 17  17  17  MET MET A . n 
A 1 18  VAL 18  18  18  VAL VAL A . n 
A 1 19  GLN 19  19  19  GLN GLN A . n 
A 1 20  VAL 20  20  20  VAL VAL A . n 
A 1 21  THR 21  21  21  THR THR A . n 
A 1 22  CYS 22  22  22  CYS CYS A . n 
A 1 23  GLY 23  23  23  GLY GLY A . n 
A 1 24  THR 24  24  24  THR THR A . n 
A 1 25  THR 25  25  25  THR THR A . n 
A 1 26  THR 26  26  26  THR THR A . n 
A 1 27  LEU 27  27  27  LEU LEU A . n 
A 1 28  ASN 28  28  28  ASN ASN A . n 
A 1 29  GLY 29  29  29  GLY GLY A . n 
A 1 30  LEU 30  30  30  LEU LEU A . n 
A 1 31  TRP 31  31  31  TRP TRP A . n 
A 1 32  LEU 32  32  32  LEU LEU A . n 
A 1 33  ASP 33  33  33  ASP ASP A . n 
A 1 34  ASP 34  34  34  ASP ASP A . n 
A 1 35  VAL 35  35  35  VAL VAL A . n 
A 1 36  VAL 36  36  36  VAL VAL A . n 
A 1 37  TYR 37  37  37  TYR TYR A . n 
A 1 38  CYS 38  38  38  CYS CYS A . n 
A 1 39  PRO 39  39  39  PRO PRO A . n 
A 1 40  ARG 40  40  40  ARG ARG A . n 
A 1 41  HIS 41  41  41  HIS HIS A . n 
A 1 42  VAL 42  42  42  VAL VAL A . n 
A 1 43  ILE 43  43  43  ILE ILE A . n 
A 1 44  CYS 44  44  44  CYS CYS A . n 
A 1 45  THR 45  45  45  THR THR A . n 
A 1 46  SER 46  46  46  SER SER A . n 
A 1 47  GLU 47  47  47  GLU GLU A . n 
A 1 48  ASP 48  48  48  ASP ASP A . n 
A 1 49  MET 49  49  49  MET MET A . n 
A 1 50  LEU 50  50  50  LEU LEU A . n 
A 1 51  ASN 51  51  51  ASN ASN A . n 
A 1 52  PRO 52  52  52  PRO PRO A . n 
A 1 53  ASN 53  53  53  ASN ASN A . n 
A 1 54  TYR 54  54  54  TYR TYR A . n 
A 1 55  GLU 55  55  55  GLU GLU A . n 
A 1 56  ASP 56  56  56  ASP ASP A . n 
A 1 57  LEU 57  57  57  LEU LEU A . n 
A 1 58  LEU 58  58  58  LEU LEU A . n 
A 1 59  ILE 59  59  59  ILE ILE A . n 
A 1 60  ARG 60  60  60  ARG ARG A . n 
A 1 61  LYS 61  61  61  LYS LYS A . n 
A 1 62  SER 62  62  62  SER SER A . n 
A 1 63  ASN 63  63  63  ASN ASN A . n 
A 1 64  HIS 64  64  64  HIS HIS A . n 
A 1 65  ASN 65  65  65  ASN ASN A . n 
A 1 66  PHE 66  66  66  PHE PHE A . n 
A 1 67  LEU 67  67  67  LEU LEU A . n 
A 1 68  VAL 68  68  68  VAL VAL A . n 
A 1 69  GLN 69  69  69  GLN GLN A . n 
A 1 70  ALA 70  70  70  ALA ALA A . n 
A 1 71  GLY 71  71  71  GLY GLY A . n 
A 1 72  ASN 72  72  72  ASN ASN A . n 
A 1 73  VAL 73  73  73  VAL VAL A . n 
A 1 74  GLN 74  74  74  GLN GLN A . n 
A 1 75  LEU 75  75  75  LEU LEU A . n 
A 1 76  ARG 76  76  76  ARG ARG A . n 
A 1 77  VAL 77  77  77  VAL VAL A . n 
A 1 78  ILE 78  78  78  ILE ILE A . n 
A 1 79  GLY 79  79  79  GLY GLY A . n 
A 1 80  HIS 80  80  80  HIS HIS A . n 
A 1 81  SER 81  81  81  SER SER A . n 
A 1 82  MET 82  82  82  MET MET A . n 
A 1 83  GLN 83  83  83  GLN GLN A . n 
A 1 84  ASN 84  84  84  ASN ASN A . n 
A 1 85  CYS 85  85  85  CYS CYS A . n 
A 1 86  VAL 86  86  86  VAL VAL A . n 
A 1 87  LEU 87  87  87  LEU LEU A . n 
A 1 88  LYS 88  88  88  LYS LYS A . n 
A 1 89  LEU 89  89  89  LEU LEU A . n 
A 1 90  LYS 90  90  90  LYS LYS A . n 
A 1 91  VAL 91  91  91  VAL VAL A . n 
A 1 92  ASP 92  92  92  ASP ASP A . n 
A 1 93  THR 93  93  93  THR THR A . n 
A 1 94  ALA 94  94  94  ALA ALA A . n 
A 1 95  ASN 95  95  95  ASN ASN A . n 
A 1 96  PRO 96  96  96  PRO PRO A . n 
A 1 97  LYS 97  97  97  LYS LYS A . n 
A 1 98  THR 98  98  98  THR THR A . n 
A 1 99  PRO 99  99  99  PRO PRO A . n 
A 1 100 LYS 100 100 100 LYS LYS A . n 
A 1 101 TYR 101 101 101 TYR TYR A . n 
A 1 102 LYS 102 102 102 LYS LYS A . n 
A 1 103 PHE 103 103 103 PHE PHE A . n 
A 1 104 VAL 104 104 104 VAL VAL A . n 
A 1 105 ARG 105 105 105 ARG ARG A . n 
A 1 106 ILE 106 106 106 ILE ILE A . n 
A 1 107 GLN 107 107 107 GLN GLN A . n 
A 1 108 PRO 108 108 108 PRO PRO A . n 
A 1 109 GLY 109 109 109 GLY GLY A . n 
A 1 110 GLN 110 110 110 GLN GLN A . n 
A 1 111 THR 111 111 111 THR THR A . n 
A 1 112 PHE 112 112 112 PHE PHE A . n 
A 1 113 SER 113 113 113 SER SER A . n 
A 1 114 VAL 114 114 114 VAL VAL A . n 
A 1 115 LEU 115 115 115 LEU LEU A . n 
A 1 116 ALA 116 116 116 ALA ALA A . n 
A 1 117 CYS 117 117 117 CYS CYS A . n 
A 1 118 TYR 118 118 118 TYR TYR A . n 
A 1 119 ASN 119 119 119 ASN ASN A . n 
A 1 120 GLY 120 120 120 GLY GLY A . n 
A 1 121 SER 121 121 121 SER SER A . n 
A 1 122 PRO 122 122 122 PRO PRO A . n 
A 1 123 SER 123 123 123 SER SER A . n 
A 1 124 GLY 124 124 124 GLY GLY A . n 
A 1 125 VAL 125 125 125 VAL VAL A . n 
A 1 126 TYR 126 126 126 TYR TYR A . n 
A 1 127 GLN 127 127 127 GLN GLN A . n 
A 1 128 CYS 128 128 128 CYS CYS A . n 
A 1 129 ALA 129 129 129 ALA ALA A . n 
A 1 130 MET 130 130 130 MET MET A . n 
A 1 131 ARG 131 131 131 ARG ARG A . n 
A 1 132 PRO 132 132 132 PRO PRO A . n 
A 1 133 ASN 133 133 133 ASN ASN A . n 
A 1 134 PHE 134 134 134 PHE PHE A . n 
A 1 135 THR 135 135 135 THR THR A . n 
A 1 136 ILE 136 136 136 ILE ILE A . n 
A 1 137 LYS 137 137 137 LYS LYS A . n 
A 1 138 GLY 138 138 138 GLY GLY A . n 
A 1 139 SER 139 139 139 SER SER A . n 
A 1 140 PHE 140 140 140 PHE PHE A . n 
A 1 141 LEU 141 141 141 LEU LEU A . n 
A 1 142 ASN 142 142 142 ASN ASN A . n 
A 1 143 GLY 143 143 143 GLY GLY A . n 
A 1 144 SER 144 144 144 SER SER A . n 
A 1 145 CYS 145 145 145 CYS CYS A . n 
A 1 146 GLY 146 146 146 GLY GLY A . n 
A 1 147 SER 147 147 147 SER SER A . n 
A 1 148 VAL 148 148 148 VAL VAL A . n 
A 1 149 GLY 149 149 149 GLY GLY A . n 
A 1 150 PHE 150 150 150 PHE PHE A . n 
A 1 151 ASN 151 151 151 ASN ASN A . n 
A 1 152 ILE 152 152 152 ILE ILE A . n 
A 1 153 ASP 153 153 153 ASP ASP A . n 
A 1 154 TYR 154 154 154 TYR TYR A . n 
A 1 155 ASP 155 155 155 ASP ASP A . n 
A 1 156 CYS 156 156 156 CYS CYS A . n 
A 1 157 VAL 157 157 157 VAL VAL A . n 
A 1 158 SER 158 158 158 SER SER A . n 
A 1 159 PHE 159 159 159 PHE PHE A . n 
A 1 160 CYS 160 160 160 CYS CYS A . n 
A 1 161 TYR 161 161 161 TYR TYR A . n 
A 1 162 MET 162 162 162 MET MET A . n 
A 1 163 HIS 163 163 163 HIS HIS A . n 
A 1 164 HIS 164 164 164 HIS HIS A . n 
A 1 165 MET 165 165 165 MET MET A . n 
A 1 166 GLU 166 166 166 GLU GLU A . n 
A 1 167 LEU 167 167 167 LEU LEU A . n 
A 1 168 PRO 168 168 168 PRO PRO A . n 
A 1 169 THR 169 169 169 THR THR A . n 
A 1 170 GLY 170 170 170 GLY GLY A . n 
A 1 171 VAL 171 171 171 VAL VAL A . n 
A 1 172 HIS 172 172 172 HIS HIS A . n 
A 1 173 ALA 173 173 173 ALA ALA A . n 
A 1 174 GLY 174 174 174 GLY GLY A . n 
A 1 175 THR 175 175 175 THR THR A . n 
A 1 176 ASP 176 176 176 ASP ASP A . n 
A 1 177 LEU 177 177 177 LEU LEU A . n 
A 1 178 GLU 178 178 178 GLU GLU A . n 
A 1 179 GLY 179 179 179 GLY GLY A . n 
A 1 180 ASN 180 180 180 ASN ASN A . n 
A 1 181 PHE 181 181 181 PHE PHE A . n 
A 1 182 TYR 182 182 182 TYR TYR A . n 
A 1 183 GLY 183 183 183 GLY GLY A . n 
A 1 184 PRO 184 184 184 PRO PRO A . n 
A 1 185 PHE 185 185 185 PHE PHE A . n 
A 1 186 VAL 186 186 186 VAL VAL A . n 
A 1 187 ASP 187 187 187 ASP ASP A . n 
A 1 188 ARG 188 188 188 ARG ARG A . n 
A 1 189 GLN 189 189 189 GLN GLN A . n 
A 1 190 THR 190 190 190 THR THR A . n 
A 1 191 ALA 191 191 191 ALA ALA A . n 
A 1 192 GLN 192 192 192 GLN GLN A . n 
A 1 193 ALA 193 193 193 ALA ALA A . n 
A 1 194 ALA 194 194 194 ALA ALA A . n 
A 1 195 GLY 195 195 195 GLY GLY A . n 
A 1 196 THR 196 196 196 THR THR A . n 
A 1 197 ASP 197 197 197 ASP ASP A . n 
A 1 198 THR 198 198 198 THR THR A . n 
A 1 199 THR 199 199 199 THR THR A . n 
A 1 200 ILE 200 200 200 ILE ILE A . n 
A 1 201 THR 201 201 201 THR THR A . n 
A 1 202 VAL 202 202 202 VAL VAL A . n 
A 1 203 ASN 203 203 203 ASN ASN A . n 
A 1 204 VAL 204 204 204 VAL VAL A . n 
A 1 205 LEU 205 205 205 LEU LEU A . n 
A 1 206 ALA 206 206 206 ALA ALA A . n 
A 1 207 TRP 207 207 207 TRP TRP A . n 
A 1 208 LEU 208 208 208 LEU LEU A . n 
A 1 209 TYR 209 209 209 TYR TYR A . n 
A 1 210 ALA 210 210 210 ALA ALA A . n 
A 1 211 ALA 211 211 211 ALA ALA A . n 
A 1 212 VAL 212 212 212 VAL VAL A . n 
A 1 213 ILE 213 213 213 ILE ILE A . n 
A 1 214 ASN 214 214 214 ASN ASN A . n 
A 1 215 GLY 215 215 215 GLY GLY A . n 
A 1 216 ASP 216 216 216 ASP ASP A . n 
A 1 217 ARG 217 217 217 ARG ARG A . n 
A 1 218 TRP 218 218 218 TRP TRP A . n 
A 1 219 PHE 219 219 219 PHE PHE A . n 
A 1 220 LEU 220 220 220 LEU LEU A . n 
A 1 221 ASN 221 221 221 ASN ASN A . n 
A 1 222 ARG 222 222 222 ARG ARG A . n 
A 1 223 PHE 223 223 223 PHE PHE A . n 
A 1 224 THR 224 224 224 THR THR A . n 
A 1 225 THR 225 225 225 THR THR A . n 
A 1 226 THR 226 226 226 THR THR A . n 
A 1 227 LEU 227 227 227 LEU LEU A . n 
A 1 228 ASN 228 228 228 ASN ASN A . n 
A 1 229 ASP 229 229 229 ASP ASP A . n 
A 1 230 PHE 230 230 230 PHE PHE A . n 
A 1 231 ASN 231 231 231 ASN ASN A . n 
A 1 232 LEU 232 232 232 LEU LEU A . n 
A 1 233 VAL 233 233 233 VAL VAL A . n 
A 1 234 ALA 234 234 234 ALA ALA A . n 
A 1 235 MET 235 235 235 MET MET A . n 
A 1 236 LYS 236 236 236 LYS LYS A . n 
A 1 237 TYR 237 237 237 TYR TYR A . n 
A 1 238 ASN 238 238 238 ASN ASN A . n 
A 1 239 TYR 239 239 239 TYR TYR A . n 
A 1 240 GLU 240 240 240 GLU GLU A . n 
A 1 241 PRO 241 241 241 PRO PRO A . n 
A 1 242 LEU 242 242 242 LEU LEU A . n 
A 1 243 THR 243 243 243 THR THR A . n 
A 1 244 GLN 244 244 244 GLN GLN A . n 
A 1 245 ASP 245 245 245 ASP ASP A . n 
A 1 246 HIS 246 246 246 HIS HIS A . n 
A 1 247 VAL 247 247 247 VAL VAL A . n 
A 1 248 ASP 248 248 248 ASP ASP A . n 
A 1 249 ILE 249 249 249 ILE ILE A . n 
A 1 250 LEU 250 250 250 LEU LEU A . n 
A 1 251 GLY 251 251 251 GLY GLY A . n 
A 1 252 PRO 252 252 252 PRO PRO A . n 
A 1 253 LEU 253 253 253 LEU LEU A . n 
A 1 254 SER 254 254 254 SER SER A . n 
A 1 255 ALA 255 255 255 ALA ALA A . n 
A 1 256 GLN 256 256 256 GLN GLN A . n 
A 1 257 THR 257 257 257 THR THR A . n 
A 1 258 GLY 258 258 258 GLY GLY A . n 
A 1 259 ILE 259 259 259 ILE ILE A . n 
A 1 260 ALA 260 260 260 ALA ALA A . n 
A 1 261 VAL 261 261 261 VAL VAL A . n 
A 1 262 LEU 262 262 262 LEU LEU A . n 
A 1 263 ASP 263 263 263 ASP ASP A . n 
A 1 264 MET 264 264 264 MET MET A . n 
A 1 265 CYS 265 265 265 CYS CYS A . n 
A 1 266 ALA 266 266 266 ALA ALA A . n 
A 1 267 SER 267 267 267 SER SER A . n 
A 1 268 LEU 268 268 268 LEU LEU A . n 
A 1 269 LYS 269 269 269 LYS LYS A . n 
A 1 270 GLU 270 270 270 GLU GLU A . n 
A 1 271 LEU 271 271 271 LEU LEU A . n 
A 1 272 LEU 272 272 272 LEU LEU A . n 
A 1 273 GLN 273 273 273 GLN GLN A . n 
A 1 274 ASN 274 274 274 ASN ASN A . n 
A 1 275 GLY 275 275 275 GLY GLY A . n 
A 1 276 MET 276 276 276 MET MET A . n 
A 1 277 ASN 277 277 277 ASN ASN A . n 
A 1 278 GLY 278 278 278 GLY GLY A . n 
A 1 279 ARG 279 279 279 ARG ARG A . n 
A 1 280 THR 280 280 280 THR THR A . n 
A 1 281 ILE 281 281 281 ILE ILE A . n 
A 1 282 LEU 282 282 282 LEU LEU A . n 
A 1 283 GLY 283 283 283 GLY GLY A . n 
A 1 284 SER 284 284 284 SER SER A . n 
A 1 285 ALA 285 285 285 ALA ALA A . n 
A 1 286 LEU 286 286 286 LEU LEU A . n 
A 1 287 LEU 287 287 287 LEU LEU A . n 
A 1 288 GLU 288 288 288 GLU GLU A . n 
A 1 289 ASP 289 289 289 ASP ASP A . n 
A 1 290 GLU 290 290 290 GLU GLU A . n 
A 1 291 PHE 291 291 291 PHE PHE A . n 
A 1 292 THR 292 292 292 THR THR A . n 
A 1 293 PRO 293 293 293 PRO PRO A . n 
A 1 294 PHE 294 294 294 PHE PHE A . n 
A 1 295 ASP 295 295 295 ASP ASP A . n 
A 1 296 VAL 296 296 296 VAL VAL A . n 
A 1 297 VAL 297 297 297 VAL VAL A . n 
A 1 298 ARG 298 298 298 ARG ARG A . n 
A 1 299 GLN 299 299 299 GLN GLN A . n 
A 1 300 CYS 300 300 300 CYS CYS A . n 
A 1 301 SER 301 301 301 SER SER A . n 
A 1 302 GLY 302 302 302 GLY GLY A . n 
A 1 303 VAL 303 303 303 VAL VAL A . n 
A 1 304 THR 304 304 304 THR THR A . n 
A 1 305 PHE 305 305 305 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        A1ITJ 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1ITJ 
_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 A1ITJ 1   401 401 A1ITJ LIG A . 
D 2 A1ITJ 1   401 401 A1ITJ LIG B . 
E 3 DMS   1   402 501 DMS   DMS B . 
F 4 CL    1   403 1   CL    CL  B . 
G 5 HOH   1   501 366 HOH   HOH A . 
G 5 HOH   2   502 204 HOH   HOH A . 
G 5 HOH   3   503 367 HOH   HOH A . 
G 5 HOH   4   504 564 HOH   HOH A . 
G 5 HOH   5   505 538 HOH   HOH A . 
G 5 HOH   6   506 352 HOH   HOH A . 
G 5 HOH   7   507 448 HOH   HOH A . 
G 5 HOH   8   508 360 HOH   HOH A . 
G 5 HOH   9   509 525 HOH   HOH A . 
G 5 HOH   10  510 168 HOH   HOH A . 
G 5 HOH   11  511 604 HOH   HOH A . 
G 5 HOH   12  512 575 HOH   HOH A . 
G 5 HOH   13  513 590 HOH   HOH A . 
G 5 HOH   14  514 236 HOH   HOH A . 
G 5 HOH   15  515 411 HOH   HOH A . 
G 5 HOH   16  516 639 HOH   HOH A . 
G 5 HOH   17  517 635 HOH   HOH A . 
G 5 HOH   18  518 544 HOH   HOH A . 
G 5 HOH   19  519 269 HOH   HOH A . 
G 5 HOH   20  520 331 HOH   HOH A . 
G 5 HOH   21  521 91  HOH   HOH A . 
G 5 HOH   22  522 13  HOH   HOH A . 
G 5 HOH   23  523 292 HOH   HOH A . 
G 5 HOH   24  524 268 HOH   HOH A . 
G 5 HOH   25  525 210 HOH   HOH A . 
G 5 HOH   26  526 350 HOH   HOH A . 
G 5 HOH   27  527 397 HOH   HOH A . 
G 5 HOH   28  528 355 HOH   HOH A . 
G 5 HOH   29  529 337 HOH   HOH A . 
G 5 HOH   30  530 190 HOH   HOH A . 
G 5 HOH   31  531 71  HOH   HOH A . 
G 5 HOH   32  532 318 HOH   HOH A . 
G 5 HOH   33  533 285 HOH   HOH A . 
G 5 HOH   34  534 187 HOH   HOH A . 
G 5 HOH   35  535 273 HOH   HOH A . 
G 5 HOH   36  536 258 HOH   HOH A . 
G 5 HOH   37  537 612 HOH   HOH A . 
G 5 HOH   38  538 377 HOH   HOH A . 
G 5 HOH   39  539 321 HOH   HOH A . 
G 5 HOH   40  540 57  HOH   HOH A . 
G 5 HOH   41  541 92  HOH   HOH A . 
G 5 HOH   42  542 8   HOH   HOH A . 
G 5 HOH   43  543 666 HOH   HOH A . 
G 5 HOH   44  544 146 HOH   HOH A . 
G 5 HOH   45  545 24  HOH   HOH A . 
G 5 HOH   46  546 129 HOH   HOH A . 
G 5 HOH   47  547 550 HOH   HOH A . 
G 5 HOH   48  548 643 HOH   HOH A . 
G 5 HOH   49  549 101 HOH   HOH A . 
G 5 HOH   50  550 117 HOH   HOH A . 
G 5 HOH   51  551 335 HOH   HOH A . 
G 5 HOH   52  552 195 HOH   HOH A . 
G 5 HOH   53  553 64  HOH   HOH A . 
G 5 HOH   54  554 462 HOH   HOH A . 
G 5 HOH   55  555 26  HOH   HOH A . 
G 5 HOH   56  556 338 HOH   HOH A . 
G 5 HOH   57  557 108 HOH   HOH A . 
G 5 HOH   58  558 69  HOH   HOH A . 
G 5 HOH   59  559 261 HOH   HOH A . 
G 5 HOH   60  560 388 HOH   HOH A . 
G 5 HOH   61  561 191 HOH   HOH A . 
G 5 HOH   62  562 241 HOH   HOH A . 
G 5 HOH   63  563 342 HOH   HOH A . 
G 5 HOH   64  564 245 HOH   HOH A . 
G 5 HOH   65  565 246 HOH   HOH A . 
G 5 HOH   66  566 302 HOH   HOH A . 
G 5 HOH   67  567 46  HOH   HOH A . 
G 5 HOH   68  568 138 HOH   HOH A . 
G 5 HOH   69  569 223 HOH   HOH A . 
G 5 HOH   70  570 242 HOH   HOH A . 
G 5 HOH   71  571 237 HOH   HOH A . 
G 5 HOH   72  572 116 HOH   HOH A . 
G 5 HOH   73  573 523 HOH   HOH A . 
G 5 HOH   74  574 591 HOH   HOH A . 
G 5 HOH   75  575 45  HOH   HOH A . 
G 5 HOH   76  576 540 HOH   HOH A . 
G 5 HOH   77  577 79  HOH   HOH A . 
G 5 HOH   78  578 133 HOH   HOH A . 
G 5 HOH   79  579 68  HOH   HOH A . 
G 5 HOH   80  580 5   HOH   HOH A . 
G 5 HOH   81  581 474 HOH   HOH A . 
G 5 HOH   82  582 155 HOH   HOH A . 
G 5 HOH   83  583 170 HOH   HOH A . 
G 5 HOH   84  584 275 HOH   HOH A . 
G 5 HOH   85  585 135 HOH   HOH A . 
G 5 HOH   86  586 472 HOH   HOH A . 
G 5 HOH   87  587 137 HOH   HOH A . 
G 5 HOH   88  588 552 HOH   HOH A . 
G 5 HOH   89  589 22  HOH   HOH A . 
G 5 HOH   90  590 80  HOH   HOH A . 
G 5 HOH   91  591 134 HOH   HOH A . 
G 5 HOH   92  592 78  HOH   HOH A . 
G 5 HOH   93  593 123 HOH   HOH A . 
G 5 HOH   94  594 400 HOH   HOH A . 
G 5 HOH   95  595 34  HOH   HOH A . 
G 5 HOH   96  596 476 HOH   HOH A . 
G 5 HOH   97  597 83  HOH   HOH A . 
G 5 HOH   98  598 132 HOH   HOH A . 
G 5 HOH   99  599 280 HOH   HOH A . 
G 5 HOH   100 600 678 HOH   HOH A . 
G 5 HOH   101 601 158 HOH   HOH A . 
G 5 HOH   102 602 131 HOH   HOH A . 
G 5 HOH   103 603 283 HOH   HOH A . 
G 5 HOH   104 604 128 HOH   HOH A . 
G 5 HOH   105 605 139 HOH   HOH A . 
G 5 HOH   106 606 205 HOH   HOH A . 
G 5 HOH   107 607 50  HOH   HOH A . 
G 5 HOH   108 608 239 HOH   HOH A . 
G 5 HOH   109 609 284 HOH   HOH A . 
G 5 HOH   110 610 97  HOH   HOH A . 
G 5 HOH   111 611 649 HOH   HOH A . 
G 5 HOH   112 612 378 HOH   HOH A . 
G 5 HOH   113 613 253 HOH   HOH A . 
G 5 HOH   114 614 43  HOH   HOH A . 
G 5 HOH   115 615 86  HOH   HOH A . 
G 5 HOH   116 616 185 HOH   HOH A . 
G 5 HOH   117 617 458 HOH   HOH A . 
G 5 HOH   118 618 316 HOH   HOH A . 
G 5 HOH   119 619 233 HOH   HOH A . 
G 5 HOH   120 620 63  HOH   HOH A . 
G 5 HOH   121 621 62  HOH   HOH A . 
G 5 HOH   122 622 27  HOH   HOH A . 
G 5 HOH   123 623 178 HOH   HOH A . 
G 5 HOH   124 624 428 HOH   HOH A . 
G 5 HOH   125 625 23  HOH   HOH A . 
G 5 HOH   126 626 16  HOH   HOH A . 
G 5 HOH   127 627 156 HOH   HOH A . 
G 5 HOH   128 628 165 HOH   HOH A . 
G 5 HOH   129 629 305 HOH   HOH A . 
G 5 HOH   130 630 2   HOH   HOH A . 
G 5 HOH   131 631 74  HOH   HOH A . 
G 5 HOH   132 632 89  HOH   HOH A . 
G 5 HOH   133 633 548 HOH   HOH A . 
G 5 HOH   134 634 259 HOH   HOH A . 
G 5 HOH   135 635 67  HOH   HOH A . 
G 5 HOH   136 636 206 HOH   HOH A . 
G 5 HOH   137 637 569 HOH   HOH A . 
G 5 HOH   138 638 270 HOH   HOH A . 
G 5 HOH   139 639 144 HOH   HOH A . 
G 5 HOH   140 640 658 HOH   HOH A . 
G 5 HOH   141 641 571 HOH   HOH A . 
G 5 HOH   142 642 361 HOH   HOH A . 
G 5 HOH   143 643 568 HOH   HOH A . 
G 5 HOH   144 644 75  HOH   HOH A . 
G 5 HOH   145 645 42  HOH   HOH A . 
G 5 HOH   146 646 140 HOH   HOH A . 
G 5 HOH   147 647 84  HOH   HOH A . 
G 5 HOH   148 648 142 HOH   HOH A . 
G 5 HOH   149 649 288 HOH   HOH A . 
G 5 HOH   150 650 650 HOH   HOH A . 
G 5 HOH   151 651 634 HOH   HOH A . 
G 5 HOH   152 652 319 HOH   HOH A . 
G 5 HOH   153 653 9   HOH   HOH A . 
G 5 HOH   154 654 323 HOH   HOH A . 
G 5 HOH   155 655 211 HOH   HOH A . 
G 5 HOH   156 656 583 HOH   HOH A . 
G 5 HOH   157 657 473 HOH   HOH A . 
G 5 HOH   158 658 60  HOH   HOH A . 
G 5 HOH   159 659 286 HOH   HOH A . 
G 5 HOH   160 660 41  HOH   HOH A . 
G 5 HOH   161 661 10  HOH   HOH A . 
G 5 HOH   162 662 655 HOH   HOH A . 
G 5 HOH   163 663 252 HOH   HOH A . 
G 5 HOH   164 664 317 HOH   HOH A . 
G 5 HOH   165 665 163 HOH   HOH A . 
G 5 HOH   166 666 103 HOH   HOH A . 
G 5 HOH   167 667 542 HOH   HOH A . 
G 5 HOH   168 668 446 HOH   HOH A . 
G 5 HOH   169 669 98  HOH   HOH A . 
G 5 HOH   170 670 87  HOH   HOH A . 
G 5 HOH   171 671 256 HOH   HOH A . 
G 5 HOH   172 672 35  HOH   HOH A . 
G 5 HOH   173 673 99  HOH   HOH A . 
G 5 HOH   174 674 306 HOH   HOH A . 
G 5 HOH   175 675 28  HOH   HOH A . 
G 5 HOH   176 676 312 HOH   HOH A . 
G 5 HOH   177 677 143 HOH   HOH A . 
G 5 HOH   178 678 121 HOH   HOH A . 
G 5 HOH   179 679 630 HOH   HOH A . 
G 5 HOH   180 680 96  HOH   HOH A . 
G 5 HOH   181 681 399 HOH   HOH A . 
G 5 HOH   182 682 588 HOH   HOH A . 
G 5 HOH   183 683 346 HOH   HOH A . 
G 5 HOH   184 684 271 HOH   HOH A . 
G 5 HOH   185 685 20  HOH   HOH A . 
G 5 HOH   186 686 547 HOH   HOH A . 
G 5 HOH   187 687 181 HOH   HOH A . 
G 5 HOH   188 688 55  HOH   HOH A . 
G 5 HOH   189 689 110 HOH   HOH A . 
G 5 HOH   190 690 405 HOH   HOH A . 
G 5 HOH   191 691 276 HOH   HOH A . 
G 5 HOH   192 692 445 HOH   HOH A . 
G 5 HOH   193 693 53  HOH   HOH A . 
G 5 HOH   194 694 667 HOH   HOH A . 
G 5 HOH   195 695 102 HOH   HOH A . 
G 5 HOH   196 696 177 HOH   HOH A . 
G 5 HOH   197 697 314 HOH   HOH A . 
G 5 HOH   198 698 174 HOH   HOH A . 
G 5 HOH   199 699 212 HOH   HOH A . 
G 5 HOH   200 700 457 HOH   HOH A . 
G 5 HOH   201 701 106 HOH   HOH A . 
G 5 HOH   202 702 380 HOH   HOH A . 
G 5 HOH   203 703 186 HOH   HOH A . 
G 5 HOH   204 704 114 HOH   HOH A . 
G 5 HOH   205 705 33  HOH   HOH A . 
G 5 HOH   206 706 85  HOH   HOH A . 
G 5 HOH   207 707 266 HOH   HOH A . 
G 5 HOH   208 708 44  HOH   HOH A . 
G 5 HOH   209 709 73  HOH   HOH A . 
G 5 HOH   210 710 166 HOH   HOH A . 
G 5 HOH   211 711 160 HOH   HOH A . 
G 5 HOH   212 712 94  HOH   HOH A . 
G 5 HOH   213 713 289 HOH   HOH A . 
G 5 HOH   214 714 262 HOH   HOH A . 
G 5 HOH   215 715 30  HOH   HOH A . 
G 5 HOH   216 716 153 HOH   HOH A . 
G 5 HOH   217 717 14  HOH   HOH A . 
G 5 HOH   218 718 119 HOH   HOH A . 
G 5 HOH   219 719 77  HOH   HOH A . 
G 5 HOH   220 720 539 HOH   HOH A . 
G 5 HOH   221 721 32  HOH   HOH A . 
G 5 HOH   222 722 36  HOH   HOH A . 
G 5 HOH   223 723 327 HOH   HOH A . 
G 5 HOH   224 724 278 HOH   HOH A . 
G 5 HOH   225 725 104 HOH   HOH A . 
G 5 HOH   226 726 230 HOH   HOH A . 
G 5 HOH   227 727 11  HOH   HOH A . 
G 5 HOH   228 728 240 HOH   HOH A . 
G 5 HOH   229 729 557 HOH   HOH A . 
G 5 HOH   230 730 300 HOH   HOH A . 
G 5 HOH   231 731 194 HOH   HOH A . 
G 5 HOH   232 732 59  HOH   HOH A . 
G 5 HOH   233 733 257 HOH   HOH A . 
G 5 HOH   234 734 254 HOH   HOH A . 
G 5 HOH   235 735 38  HOH   HOH A . 
G 5 HOH   236 736 308 HOH   HOH A . 
G 5 HOH   237 737 226 HOH   HOH A . 
G 5 HOH   238 738 336 HOH   HOH A . 
G 5 HOH   239 739 497 HOH   HOH A . 
G 5 HOH   240 740 120 HOH   HOH A . 
G 5 HOH   241 741 442 HOH   HOH A . 
G 5 HOH   242 742 375 HOH   HOH A . 
G 5 HOH   243 743 356 HOH   HOH A . 
G 5 HOH   244 744 461 HOH   HOH A . 
G 5 HOH   245 745 531 HOH   HOH A . 
G 5 HOH   246 746 543 HOH   HOH A . 
G 5 HOH   247 747 541 HOH   HOH A . 
G 5 HOH   248 748 469 HOH   HOH A . 
G 5 HOH   249 749 389 HOH   HOH A . 
G 5 HOH   250 750 596 HOH   HOH A . 
G 5 HOH   251 751 392 HOH   HOH A . 
G 5 HOH   252 752 422 HOH   HOH A . 
G 5 HOH   253 753 386 HOH   HOH A . 
G 5 HOH   254 754 291 HOH   HOH A . 
G 5 HOH   255 755 345 HOH   HOH A . 
G 5 HOH   256 756 680 HOH   HOH A . 
G 5 HOH   257 757 657 HOH   HOH A . 
G 5 HOH   258 758 629 HOH   HOH A . 
G 5 HOH   259 759 1   HOH   HOH A . 
G 5 HOH   260 760 602 HOH   HOH A . 
G 5 HOH   261 761 549 HOH   HOH A . 
G 5 HOH   262 762 231 HOH   HOH A . 
G 5 HOH   263 763 3   HOH   HOH A . 
G 5 HOH   264 764 172 HOH   HOH A . 
G 5 HOH   265 765 263 HOH   HOH A . 
G 5 HOH   266 766 496 HOH   HOH A . 
G 5 HOH   267 767 626 HOH   HOH A . 
G 5 HOH   268 768 229 HOH   HOH A . 
G 5 HOH   269 769 622 HOH   HOH A . 
G 5 HOH   270 770 488 HOH   HOH A . 
G 5 HOH   271 771 503 HOH   HOH A . 
G 5 HOH   272 772 343 HOH   HOH A . 
G 5 HOH   273 773 315 HOH   HOH A . 
G 5 HOH   274 774 175 HOH   HOH A . 
G 5 HOH   275 775 281 HOH   HOH A . 
G 5 HOH   276 776 487 HOH   HOH A . 
G 5 HOH   277 777 295 HOH   HOH A . 
G 5 HOH   278 778 500 HOH   HOH A . 
G 5 HOH   279 779 159 HOH   HOH A . 
G 5 HOH   280 780 623 HOH   HOH A . 
G 5 HOH   281 781 580 HOH   HOH A . 
G 5 HOH   282 782 605 HOH   HOH A . 
G 5 HOH   283 783 374 HOH   HOH A . 
G 5 HOH   284 784 546 HOH   HOH A . 
G 5 HOH   285 785 636 HOH   HOH A . 
G 5 HOH   286 786 297 HOH   HOH A . 
G 5 HOH   287 787 668 HOH   HOH A . 
G 5 HOH   288 788 415 HOH   HOH A . 
G 5 HOH   289 789 396 HOH   HOH A . 
G 5 HOH   290 790 489 HOH   HOH A . 
G 5 HOH   291 791 329 HOH   HOH A . 
G 5 HOH   292 792 665 HOH   HOH A . 
G 5 HOH   293 793 582 HOH   HOH A . 
G 5 HOH   294 794 169 HOH   HOH A . 
G 5 HOH   295 795 410 HOH   HOH A . 
G 5 HOH   296 796 654 HOH   HOH A . 
G 5 HOH   297 797 486 HOH   HOH A . 
G 5 HOH   298 798 480 HOH   HOH A . 
G 5 HOH   299 799 464 HOH   HOH A . 
G 5 HOH   300 800 527 HOH   HOH A . 
G 5 HOH   301 801 491 HOH   HOH A . 
G 5 HOH   302 802 482 HOH   HOH A . 
G 5 HOH   303 803 648 HOH   HOH A . 
G 5 HOH   304 804 176 HOH   HOH A . 
G 5 HOH   305 805 624 HOH   HOH A . 
G 5 HOH   306 806 611 HOH   HOH A . 
G 5 HOH   307 807 115 HOH   HOH A . 
G 5 HOH   308 808 570 HOH   HOH A . 
G 5 HOH   309 809 180 HOH   HOH A . 
G 5 HOH   310 810 675 HOH   HOH A . 
G 5 HOH   311 811 272 HOH   HOH A . 
G 5 HOH   312 812 617 HOH   HOH A . 
G 5 HOH   313 813 294 HOH   HOH A . 
G 5 HOH   314 814 376 HOH   HOH A . 
G 5 HOH   315 815 603 HOH   HOH A . 
G 5 HOH   316 816 625 HOH   HOH A . 
G 5 HOH   317 817 183 HOH   HOH A . 
G 5 HOH   318 818 659 HOH   HOH A . 
G 5 HOH   319 819 670 HOH   HOH A . 
G 5 HOH   320 820 597 HOH   HOH A . 
G 5 HOH   321 821 615 HOH   HOH A . 
G 5 HOH   322 822 279 HOH   HOH A . 
G 5 HOH   323 823 395 HOH   HOH A . 
G 5 HOH   324 824 213 HOH   HOH A . 
G 5 HOH   325 825 672 HOH   HOH A . 
G 5 HOH   326 826 362 HOH   HOH A . 
G 5 HOH   327 827 301 HOH   HOH A . 
G 5 HOH   328 828 431 HOH   HOH A . 
G 5 HOH   329 829 532 HOH   HOH A . 
G 5 HOH   330 830 522 HOH   HOH A . 
G 5 HOH   331 831 322 HOH   HOH A . 
G 5 HOH   332 832 424 HOH   HOH A . 
G 5 HOH   333 833 450 HOH   HOH A . 
G 5 HOH   334 834 309 HOH   HOH A . 
G 5 HOH   335 835 506 HOH   HOH A . 
G 5 HOH   336 836 347 HOH   HOH A . 
G 5 HOH   337 837 407 HOH   HOH A . 
G 5 HOH   338 838 149 HOH   HOH A . 
G 5 HOH   339 839 130 HOH   HOH A . 
G 5 HOH   340 840 513 HOH   HOH A . 
G 5 HOH   341 841 595 HOH   HOH A . 
G 5 HOH   342 842 499 HOH   HOH A . 
G 5 HOH   343 843 455 HOH   HOH A . 
G 5 HOH   344 844 509 HOH   HOH A . 
G 5 HOH   345 845 614 HOH   HOH A . 
G 5 HOH   346 846 679 HOH   HOH A . 
H 5 HOH   1   501 524 HOH   HOH B . 
H 5 HOH   2   502 528 HOH   HOH B . 
H 5 HOH   3   503 167 HOH   HOH B . 
H 5 HOH   4   504 601 HOH   HOH B . 
H 5 HOH   5   505 207 HOH   HOH B . 
H 5 HOH   6   506 606 HOH   HOH B . 
H 5 HOH   7   507 559 HOH   HOH B . 
H 5 HOH   8   508 58  HOH   HOH B . 
H 5 HOH   9   509 560 HOH   HOH B . 
H 5 HOH   10  510 385 HOH   HOH B . 
H 5 HOH   11  511 390 HOH   HOH B . 
H 5 HOH   12  512 566 HOH   HOH B . 
H 5 HOH   13  513 219 HOH   HOH B . 
H 5 HOH   14  514 325 HOH   HOH B . 
H 5 HOH   15  515 19  HOH   HOH B . 
H 5 HOH   16  516 412 HOH   HOH B . 
H 5 HOH   17  517 579 HOH   HOH B . 
H 5 HOH   18  518 136 HOH   HOH B . 
H 5 HOH   19  519 311 HOH   HOH B . 
H 5 HOH   20  520 238 HOH   HOH B . 
H 5 HOH   21  521 363 HOH   HOH B . 
H 5 HOH   22  522 255 HOH   HOH B . 
H 5 HOH   23  523 383 HOH   HOH B . 
H 5 HOH   24  524 200 HOH   HOH B . 
H 5 HOH   25  525 651 HOH   HOH B . 
H 5 HOH   26  526 671 HOH   HOH B . 
H 5 HOH   27  527 290 HOH   HOH B . 
H 5 HOH   28  528 631 HOH   HOH B . 
H 5 HOH   29  529 328 HOH   HOH B . 
H 5 HOH   30  530 562 HOH   HOH B . 
H 5 HOH   31  531 184 HOH   HOH B . 
H 5 HOH   32  532 586 HOH   HOH B . 
H 5 HOH   33  533 164 HOH   HOH B . 
H 5 HOH   34  534 373 HOH   HOH B . 
H 5 HOH   35  535 296 HOH   HOH B . 
H 5 HOH   36  536 402 HOH   HOH B . 
H 5 HOH   37  537 417 HOH   HOH B . 
H 5 HOH   38  538 369 HOH   HOH B . 
H 5 HOH   39  539 438 HOH   HOH B . 
H 5 HOH   40  540 637 HOH   HOH B . 
H 5 HOH   41  541 628 HOH   HOH B . 
H 5 HOH   42  542 72  HOH   HOH B . 
H 5 HOH   43  543 162 HOH   HOH B . 
H 5 HOH   44  544 662 HOH   HOH B . 
H 5 HOH   45  545 189 HOH   HOH B . 
H 5 HOH   46  546 193 HOH   HOH B . 
H 5 HOH   47  547 154 HOH   HOH B . 
H 5 HOH   48  548 49  HOH   HOH B . 
H 5 HOH   49  549 217 HOH   HOH B . 
H 5 HOH   50  550 341 HOH   HOH B . 
H 5 HOH   51  551 627 HOH   HOH B . 
H 5 HOH   52  552 209 HOH   HOH B . 
H 5 HOH   53  553 161 HOH   HOH B . 
H 5 HOH   54  554 220 HOH   HOH B . 
H 5 HOH   55  555 202 HOH   HOH B . 
H 5 HOH   56  556 561 HOH   HOH B . 
H 5 HOH   57  557 354 HOH   HOH B . 
H 5 HOH   58  558 587 HOH   HOH B . 
H 5 HOH   59  559 572 HOH   HOH B . 
H 5 HOH   60  560 479 HOH   HOH B . 
H 5 HOH   61  561 553 HOH   HOH B . 
H 5 HOH   62  562 554 HOH   HOH B . 
H 5 HOH   63  563 208 HOH   HOH B . 
H 5 HOH   64  564 348 HOH   HOH B . 
H 5 HOH   65  565 66  HOH   HOH B . 
H 5 HOH   66  566 29  HOH   HOH B . 
H 5 HOH   67  567 203 HOH   HOH B . 
H 5 HOH   68  568 199 HOH   HOH B . 
H 5 HOH   69  569 150 HOH   HOH B . 
H 5 HOH   70  570 248 HOH   HOH B . 
H 5 HOH   71  571 439 HOH   HOH B . 
H 5 HOH   72  572 61  HOH   HOH B . 
H 5 HOH   73  573 232 HOH   HOH B . 
H 5 HOH   74  574 95  HOH   HOH B . 
H 5 HOH   75  575 298 HOH   HOH B . 
H 5 HOH   76  576 277 HOH   HOH B . 
H 5 HOH   77  577 93  HOH   HOH B . 
H 5 HOH   78  578 216 HOH   HOH B . 
H 5 HOH   79  579 125 HOH   HOH B . 
H 5 HOH   80  580 12  HOH   HOH B . 
H 5 HOH   81  581 545 HOH   HOH B . 
H 5 HOH   82  582 353 HOH   HOH B . 
H 5 HOH   83  583 214 HOH   HOH B . 
H 5 HOH   84  584 565 HOH   HOH B . 
H 5 HOH   85  585 449 HOH   HOH B . 
H 5 HOH   86  586 468 HOH   HOH B . 
H 5 HOH   87  587 48  HOH   HOH B . 
H 5 HOH   88  588 107 HOH   HOH B . 
H 5 HOH   89  589 90  HOH   HOH B . 
H 5 HOH   90  590 265 HOH   HOH B . 
H 5 HOH   91  591 222 HOH   HOH B . 
H 5 HOH   92  592 526 HOH   HOH B . 
H 5 HOH   93  593 310 HOH   HOH B . 
H 5 HOH   94  594 436 HOH   HOH B . 
H 5 HOH   95  595 467 HOH   HOH B . 
H 5 HOH   96  596 451 HOH   HOH B . 
H 5 HOH   97  597 485 HOH   HOH B . 
H 5 HOH   98  598 577 HOH   HOH B . 
H 5 HOH   99  599 551 HOH   HOH B . 
H 5 HOH   100 600 475 HOH   HOH B . 
H 5 HOH   101 601 332 HOH   HOH B . 
H 5 HOH   102 602 364 HOH   HOH B . 
H 5 HOH   103 603 576 HOH   HOH B . 
H 5 HOH   104 604 31  HOH   HOH B . 
H 5 HOH   105 605 398 HOH   HOH B . 
H 5 HOH   106 606 197 HOH   HOH B . 
H 5 HOH   107 607 598 HOH   HOH B . 
H 5 HOH   108 608 387 HOH   HOH B . 
H 5 HOH   109 609 330 HOH   HOH B . 
H 5 HOH   110 610 563 HOH   HOH B . 
H 5 HOH   111 611 459 HOH   HOH B . 
H 5 HOH   112 612 299 HOH   HOH B . 
H 5 HOH   113 613 56  HOH   HOH B . 
H 5 HOH   114 614 148 HOH   HOH B . 
H 5 HOH   115 615 640 HOH   HOH B . 
H 5 HOH   116 616 221 HOH   HOH B . 
H 5 HOH   117 617 427 HOH   HOH B . 
H 5 HOH   118 618 17  HOH   HOH B . 
H 5 HOH   119 619 173 HOH   HOH B . 
H 5 HOH   120 620 370 HOH   HOH B . 
H 5 HOH   121 621 15  HOH   HOH B . 
H 5 HOH   122 622 198 HOH   HOH B . 
H 5 HOH   123 623 247 HOH   HOH B . 
H 5 HOH   124 624 483 HOH   HOH B . 
H 5 HOH   125 625 127 HOH   HOH B . 
H 5 HOH   126 626 589 HOH   HOH B . 
H 5 HOH   127 627 234 HOH   HOH B . 
H 5 HOH   128 628 303 HOH   HOH B . 
H 5 HOH   129 629 381 HOH   HOH B . 
H 5 HOH   130 630 307 HOH   HOH B . 
H 5 HOH   131 631 88  HOH   HOH B . 
H 5 HOH   132 632 452 HOH   HOH B . 
H 5 HOH   133 633 401 HOH   HOH B . 
H 5 HOH   134 634 6   HOH   HOH B . 
H 5 HOH   135 635 113 HOH   HOH B . 
H 5 HOH   136 636 54  HOH   HOH B . 
H 5 HOH   137 637 646 HOH   HOH B . 
H 5 HOH   138 638 47  HOH   HOH B . 
H 5 HOH   139 639 409 HOH   HOH B . 
H 5 HOH   140 640 600 HOH   HOH B . 
H 5 HOH   141 641 51  HOH   HOH B . 
H 5 HOH   142 642 656 HOH   HOH B . 
H 5 HOH   143 643 147 HOH   HOH B . 
H 5 HOH   144 644 21  HOH   HOH B . 
H 5 HOH   145 645 536 HOH   HOH B . 
H 5 HOH   146 646 516 HOH   HOH B . 
H 5 HOH   147 647 7   HOH   HOH B . 
H 5 HOH   148 648 339 HOH   HOH B . 
H 5 HOH   149 649 109 HOH   HOH B . 
H 5 HOH   150 650 218 HOH   HOH B . 
H 5 HOH   151 651 621 HOH   HOH B . 
H 5 HOH   152 652 609 HOH   HOH B . 
H 5 HOH   153 653 70  HOH   HOH B . 
H 5 HOH   154 654 324 HOH   HOH B . 
H 5 HOH   155 655 40  HOH   HOH B . 
H 5 HOH   156 656 111 HOH   HOH B . 
H 5 HOH   157 657 394 HOH   HOH B . 
H 5 HOH   158 658 151 HOH   HOH B . 
H 5 HOH   159 659 39  HOH   HOH B . 
H 5 HOH   160 660 660 HOH   HOH B . 
H 5 HOH   161 661 357 HOH   HOH B . 
H 5 HOH   162 662 118 HOH   HOH B . 
H 5 HOH   163 663 274 HOH   HOH B . 
H 5 HOH   164 664 453 HOH   HOH B . 
H 5 HOH   165 665 633 HOH   HOH B . 
H 5 HOH   166 666 664 HOH   HOH B . 
H 5 HOH   167 667 368 HOH   HOH B . 
H 5 HOH   168 668 535 HOH   HOH B . 
H 5 HOH   169 669 421 HOH   HOH B . 
H 5 HOH   170 670 171 HOH   HOH B . 
H 5 HOH   171 671 196 HOH   HOH B . 
H 5 HOH   172 672 76  HOH   HOH B . 
H 5 HOH   173 673 112 HOH   HOH B . 
H 5 HOH   174 674 414 HOH   HOH B . 
H 5 HOH   175 675 25  HOH   HOH B . 
H 5 HOH   176 676 65  HOH   HOH B . 
H 5 HOH   177 677 558 HOH   HOH B . 
H 5 HOH   178 678 145 HOH   HOH B . 
H 5 HOH   179 679 443 HOH   HOH B . 
H 5 HOH   180 680 182 HOH   HOH B . 
H 5 HOH   181 681 537 HOH   HOH B . 
H 5 HOH   182 682 4   HOH   HOH B . 
H 5 HOH   183 683 105 HOH   HOH B . 
H 5 HOH   184 684 267 HOH   HOH B . 
H 5 HOH   185 685 141 HOH   HOH B . 
H 5 HOH   186 686 512 HOH   HOH B . 
H 5 HOH   187 687 157 HOH   HOH B . 
H 5 HOH   188 688 225 HOH   HOH B . 
H 5 HOH   189 689 260 HOH   HOH B . 
H 5 HOH   190 690 556 HOH   HOH B . 
H 5 HOH   191 691 179 HOH   HOH B . 
H 5 HOH   192 692 372 HOH   HOH B . 
H 5 HOH   193 693 585 HOH   HOH B . 
H 5 HOH   194 694 81  HOH   HOH B . 
H 5 HOH   195 695 126 HOH   HOH B . 
H 5 HOH   196 696 320 HOH   HOH B . 
H 5 HOH   197 697 647 HOH   HOH B . 
H 5 HOH   198 698 215 HOH   HOH B . 
H 5 HOH   199 699 663 HOH   HOH B . 
H 5 HOH   200 700 669 HOH   HOH B . 
H 5 HOH   201 701 249 HOH   HOH B . 
H 5 HOH   202 702 674 HOH   HOH B . 
H 5 HOH   203 703 371 HOH   HOH B . 
H 5 HOH   204 704 359 HOH   HOH B . 
H 5 HOH   205 705 287 HOH   HOH B . 
H 5 HOH   206 706 52  HOH   HOH B . 
H 5 HOH   207 707 18  HOH   HOH B . 
H 5 HOH   208 708 37  HOH   HOH B . 
H 5 HOH   209 709 420 HOH   HOH B . 
H 5 HOH   210 710 645 HOH   HOH B . 
H 5 HOH   211 711 201 HOH   HOH B . 
H 5 HOH   212 712 529 HOH   HOH B . 
H 5 HOH   213 713 100 HOH   HOH B . 
H 5 HOH   214 714 264 HOH   HOH B . 
H 5 HOH   215 715 581 HOH   HOH B . 
H 5 HOH   216 716 578 HOH   HOH B . 
H 5 HOH   217 717 642 HOH   HOH B . 
H 5 HOH   218 718 124 HOH   HOH B . 
H 5 HOH   219 719 340 HOH   HOH B . 
H 5 HOH   220 720 555 HOH   HOH B . 
H 5 HOH   221 721 444 HOH   HOH B . 
H 5 HOH   222 722 632 HOH   HOH B . 
H 5 HOH   223 723 584 HOH   HOH B . 
H 5 HOH   224 724 82  HOH   HOH B . 
H 5 HOH   225 725 188 HOH   HOH B . 
H 5 HOH   226 726 152 HOH   HOH B . 
H 5 HOH   227 727 344 HOH   HOH B . 
H 5 HOH   228 728 608 HOH   HOH B . 
H 5 HOH   229 729 653 HOH   HOH B . 
H 5 HOH   230 730 251 HOH   HOH B . 
H 5 HOH   231 731 304 HOH   HOH B . 
H 5 HOH   232 732 510 HOH   HOH B . 
H 5 HOH   233 733 393 HOH   HOH B . 
H 5 HOH   234 734 235 HOH   HOH B . 
H 5 HOH   235 735 620 HOH   HOH B . 
H 5 HOH   236 736 244 HOH   HOH B . 
H 5 HOH   237 737 607 HOH   HOH B . 
H 5 HOH   238 738 493 HOH   HOH B . 
H 5 HOH   239 739 498 HOH   HOH B . 
H 5 HOH   240 740 228 HOH   HOH B . 
H 5 HOH   241 741 423 HOH   HOH B . 
H 5 HOH   242 742 192 HOH   HOH B . 
H 5 HOH   243 743 613 HOH   HOH B . 
H 5 HOH   244 744 514 HOH   HOH B . 
H 5 HOH   245 745 490 HOH   HOH B . 
H 5 HOH   246 746 515 HOH   HOH B . 
H 5 HOH   247 747 365 HOH   HOH B . 
H 5 HOH   248 748 673 HOH   HOH B . 
H 5 HOH   249 749 122 HOH   HOH B . 
H 5 HOH   250 750 517 HOH   HOH B . 
H 5 HOH   251 751 661 HOH   HOH B . 
H 5 HOH   252 752 243 HOH   HOH B . 
H 5 HOH   253 753 334 HOH   HOH B . 
H 5 HOH   254 754 495 HOH   HOH B . 
H 5 HOH   255 755 599 HOH   HOH B . 
H 5 HOH   256 756 384 HOH   HOH B . 
H 5 HOH   257 757 227 HOH   HOH B . 
H 5 HOH   258 758 574 HOH   HOH B . 
H 5 HOH   259 759 492 HOH   HOH B . 
H 5 HOH   260 760 224 HOH   HOH B . 
H 5 HOH   261 761 519 HOH   HOH B . 
H 5 HOH   262 762 511 HOH   HOH B . 
H 5 HOH   263 763 504 HOH   HOH B . 
H 5 HOH   264 764 652 HOH   HOH B . 
H 5 HOH   265 765 618 HOH   HOH B . 
H 5 HOH   266 766 293 HOH   HOH B . 
H 5 HOH   267 767 403 HOH   HOH B . 
H 5 HOH   268 768 644 HOH   HOH B . 
H 5 HOH   269 769 508 HOH   HOH B . 
H 5 HOH   270 770 313 HOH   HOH B . 
H 5 HOH   271 771 518 HOH   HOH B . 
H 5 HOH   272 772 379 HOH   HOH B . 
H 5 HOH   273 773 406 HOH   HOH B . 
H 5 HOH   274 774 501 HOH   HOH B . 
H 5 HOH   275 775 282 HOH   HOH B . 
H 5 HOH   276 776 494 HOH   HOH B . 
H 5 HOH   277 777 471 HOH   HOH B . 
H 5 HOH   278 778 413 HOH   HOH B . 
H 5 HOH   279 779 433 HOH   HOH B . 
H 5 HOH   280 780 502 HOH   HOH B . 
H 5 HOH   281 781 440 HOH   HOH B . 
H 5 HOH   282 782 619 HOH   HOH B . 
H 5 HOH   283 783 594 HOH   HOH B . 
H 5 HOH   284 784 333 HOH   HOH B . 
H 5 HOH   285 785 351 HOH   HOH B . 
H 5 HOH   286 786 419 HOH   HOH B . 
H 5 HOH   287 787 592 HOH   HOH B . 
H 5 HOH   288 788 616 HOH   HOH B . 
H 5 HOH   289 789 349 HOH   HOH B . 
H 5 HOH   290 790 418 HOH   HOH B . 
H 5 HOH   291 791 638 HOH   HOH B . 
H 5 HOH   292 792 676 HOH   HOH B . 
H 5 HOH   293 793 505 HOH   HOH B . 
H 5 HOH   294 794 641 HOH   HOH B . 
H 5 HOH   295 795 520 HOH   HOH B . 
H 5 HOH   296 796 677 HOH   HOH B . 
H 5 HOH   297 797 382 HOH   HOH B . 
H 5 HOH   298 798 426 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 GLU 47  ? CG  ? A GLU 47  CG  
2  1 Y 1 A GLU 47  ? CD  ? A GLU 47  CD  
3  1 Y 1 A GLU 47  ? OE1 ? A GLU 47  OE1 
4  1 Y 1 A GLU 47  ? OE2 ? A GLU 47  OE2 
5  1 Y 1 A ASN 72  ? CG  ? A ASN 72  CG  
6  1 Y 1 A ASN 72  ? OD1 ? A ASN 72  OD1 
7  1 Y 1 A ASN 72  ? ND2 ? A ASN 72  ND2 
8  1 Y 1 A ASP 155 ? CG  ? A ASP 155 CG  
9  1 Y 1 A ASP 155 ? OD1 ? A ASP 155 OD1 
10 1 Y 1 A ASP 155 ? OD2 ? A ASP 155 OD2 
11 1 Y 1 B ARG 60  ? CG  ? B ARG 60  CG  
12 1 Y 1 B ARG 60  ? CD  ? B ARG 60  CD  
13 1 Y 1 B ARG 60  ? NE  ? B ARG 60  NE  
14 1 Y 1 B ARG 60  ? CZ  ? B ARG 60  CZ  
15 1 Y 1 B ARG 60  ? NH1 ? B ARG 60  NH1 
16 1 Y 1 B ARG 60  ? NH2 ? B ARG 60  NH2 
17 1 Y 1 B GLN 74  ? CG  ? B GLN 74  CG  
18 1 Y 1 B GLN 74  ? CD  ? B GLN 74  CD  
19 1 Y 1 B GLN 74  ? OE1 ? B GLN 74  OE1 
20 1 Y 1 B GLN 74  ? NE2 ? B GLN 74  NE2 
21 1 Y 1 B GLN 110 ? CD  ? B GLN 110 CD  
22 1 Y 1 B GLN 110 ? OE1 ? B GLN 110 OE1 
23 1 Y 1 B GLN 110 ? NE2 ? B GLN 110 NE2 
24 1 Y 1 B TYR 154 ? CG  ? B TYR 154 CG  
25 1 Y 1 B TYR 154 ? CD1 ? B TYR 154 CD1 
26 1 Y 1 B TYR 154 ? CD2 ? B TYR 154 CD2 
27 1 Y 1 B TYR 154 ? CE1 ? B TYR 154 CE1 
28 1 Y 1 B TYR 154 ? CE2 ? B TYR 154 CE2 
29 1 Y 1 B TYR 154 ? CZ  ? B TYR 154 CZ  
30 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                     9HAJ 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     68.046 
_cell.length_a_esd                 ? 
_cell.length_b                     99.654 
_cell.length_b_esd                 ? 
_cell.length_c                     104.145 
_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                         9HAJ 
_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                   9HAJ 
_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             2.61 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          52.87 
_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 B3' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            298 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER2 X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2022-12-11 
_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                        'SLS BEAMLINE X06DA' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.00 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   X06DA 
_diffrn_source.pdbx_synchrotron_site       SLS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9HAJ 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.276 
_reflns.d_resolution_low                               57.03 
_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                                     183140 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.8 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.0 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          8.2 
_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                                0.048 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.997 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.136 
_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                                    1.276 
_reflns_shell.d_res_low                                     1.299 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           0.7 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             8918 
_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                               1.01 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.371 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          98.1 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  2.77 
_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]                            -0.358 
_refine.aniso_B[1][2]                            0.000 
_refine.aniso_B[1][3]                            -0.000 
_refine.aniso_B[2][2]                            -0.187 
_refine.aniso_B[2][3]                            0.000 
_refine.aniso_B[3][3]                            0.546 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               16.904 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.973 
_refine.correlation_coeff_Fo_to_Fc_free          0.961 
_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                                 9HAJ 
_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                            1.276 
_refine.ls_d_res_low                             57.030 
_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                     182872 
_refine.ls_number_reflns_R_free                  9101 
_refine.ls_number_reflns_R_work                  173771 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.593 
_refine.ls_percent_reflns_R_free                 4.977 
_refine.ls_R_factor_all                          0.165 
_refine.ls_R_factor_obs                          ? 
_refine.ls_R_factor_R_free                       0.1918 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1640 
_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                       0.045 
_refine.pdbx_overall_ESU_R_Free                  0.044 
_refine.pdbx_solvent_vdw_probe_radii             1.200 
_refine.pdbx_solvent_ion_probe_radii             0.800 
_refine.pdbx_solvent_shrinkage_radii             0.800 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             2.088 
_refine.overall_SU_ML                            0.037 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.276 
_refine_hist.d_res_low                        57.030 
_refine_hist.number_atoms_solvent             644 
_refine_hist.number_atoms_total               5407 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        4696 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         67 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.005  0.012  4941  ? r_bond_refined_d               ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.016  4590  ? r_bond_other_d                 ? ? 
'X-RAY DIFFRACTION' ? 1.489  1.801  6731  ? r_angle_refined_deg            ? ? 
'X-RAY DIFFRACTION' ? 0.532  1.748  10545 ? r_angle_other_deg              ? ? 
'X-RAY DIFFRACTION' ? 6.866  5.000  627   ? r_dihedral_angle_1_deg         ? ? 
'X-RAY DIFFRACTION' ? 6.968  5.000  21    ? r_dihedral_angle_2_deg         ? ? 
'X-RAY DIFFRACTION' ? 10.779 10.000 780   ? r_dihedral_angle_3_deg         ? ? 
'X-RAY DIFFRACTION' ? 14.846 10.000 213   ? r_dihedral_angle_6_deg         ? ? 
'X-RAY DIFFRACTION' ? 0.076  0.200  757   ? r_chiral_restr                 ? ? 
'X-RAY DIFFRACTION' ? 0.007  0.020  5896  ? r_gen_planes_refined           ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  1170  ? r_gen_planes_other             ? ? 
'X-RAY DIFFRACTION' ? 0.209  0.200  848   ? r_nbd_refined                  ? ? 
'X-RAY DIFFRACTION' ? 0.195  0.200  4225  ? r_symmetry_nbd_other           ? ? 
'X-RAY DIFFRACTION' ? 0.181  0.200  2465  ? r_nbtor_refined                ? ? 
'X-RAY DIFFRACTION' ? 0.081  0.200  2517  ? r_symmetry_nbtor_other         ? ? 
'X-RAY DIFFRACTION' ? 0.113  0.200  390   ? r_xyhbond_nbd_refined          ? ? 
'X-RAY DIFFRACTION' ? 0.180  0.200  12    ? r_symmetry_nbd_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.200  0.200  69    ? r_nbd_other                    ? ? 
'X-RAY DIFFRACTION' ? 0.169  0.200  41    ? r_symmetry_xyhbond_nbd_refined ? ? 
'X-RAY DIFFRACTION' ? 0.099  0.200  1     ? r_xyhbond_nbd_other            ? ? 
'X-RAY DIFFRACTION' ? 2.867  1.500  2481  ? r_mcbond_it                    ? ? 
'X-RAY DIFFRACTION' ? 2.856  1.500  2481  ? r_mcbond_other                 ? ? 
'X-RAY DIFFRACTION' ? 4.429  2.702  3111  ? r_mcangle_it                   ? ? 
'X-RAY DIFFRACTION' ? 4.430  2.703  3112  ? r_mcangle_other                ? ? 
'X-RAY DIFFRACTION' ? 3.765  1.680  2460  ? r_scbond_it                    ? ? 
'X-RAY DIFFRACTION' ? 3.764  1.680  2461  ? r_scbond_other                 ? ? 
'X-RAY DIFFRACTION' ? 5.683  3.011  3618  ? r_scangle_it                   ? ? 
'X-RAY DIFFRACTION' ? 5.682  3.011  3619  ? r_scangle_other                ? ? 
'X-RAY DIFFRACTION' ? 10.460 19.154 5558  ? r_lrange_it                    ? ? 
'X-RAY DIFFRACTION' ? 8.980  15.587 5379  ? r_lrange_other                 ? ? 
'X-RAY DIFFRACTION' ? 2.251  3.000  9531  ? r_rigid_bond_restr             ? ? 
'X-RAY DIFFRACTION' ? 0.122  0.050  9324  ? 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 ? ? 0.12161 ? 0.05008 1 'Local ncs' ? A ? ? ? 1 
'X-RAY DIFFRACTION' 2 ? ? 0.12161 ? 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' 1.276 1.310  13484 . 673 12289 96.1287  . 0.369 . . 0.369 . . . . . 0.369 . 20 . 0.911 0.911 0.365 
'X-RAY DIFFRACTION' 1.310 1.345  13041 . 659 12318 99.5092  . 0.327 . . 0.327 . . . . . 0.329 . 20 . 0.930 0.932 0.314 
'X-RAY DIFFRACTION' 1.345 1.384  12812 . 670 12104 99.7034  . 0.298 . . 0.298 . . . . . 0.297 . 20 . 0.943 0.939 0.303 
'X-RAY DIFFRACTION' 1.384 1.427  12374 . 677 11660 99.7010  . 0.259 . . 0.259 . . . . . 0.254 . 20 . 0.957 0.954 0.276 
'X-RAY DIFFRACTION' 1.427 1.474  12005 . 561 11433 99.9084  . 0.224 . . 0.224 . . . . . 0.214 . 20 . 0.968 0.963 0.240 
'X-RAY DIFFRACTION' 1.474 1.526  11657 . 553 11092 99.8971  . 0.190 . . 0.189 . . . . . 0.174 . 20 . 0.977 0.970 0.215 
'X-RAY DIFFRACTION' 1.526 1.583  11255 . 585 10667 99.9733  . 0.166 . . 0.166 . . . . . 0.148 . 20 . 0.982 0.979 0.178 
'X-RAY DIFFRACTION' 1.583 1.648  10796 . 514 10282 100.0000 . 0.150 . . 0.148 . . . . . 0.131 . 20 . 0.986 0.975 0.190 
'X-RAY DIFFRACTION' 1.648 1.721  10419 . 520 9899  100.0000 . 0.130 . . 0.129 . . . . . 0.112 . 20 . 0.990 0.982 0.163 
'X-RAY DIFFRACTION' 1.721 1.805  9952  . 477 9475  100.0000 . 0.124 . . 0.122 . . . . . 0.107 . 20 . 0.991 0.982 0.165 
'X-RAY DIFFRACTION' 1.805 1.902  9442  . 448 8994  100.0000 . 0.119 . . 0.118 . . . . . 0.106 . 20 . 0.992 0.986 0.150 
'X-RAY DIFFRACTION' 1.902 2.018  8993  . 447 8546  100.0000 . 0.129 . . 0.127 . . . . . 0.118 . 20 . 0.991 0.985 0.165 
'X-RAY DIFFRACTION' 2.018 2.157  8476  . 451 8023  99.9764  . 0.130 . . 0.130 . . . . . 0.123 . 20 . 0.991 0.988 0.140 
'X-RAY DIFFRACTION' 2.157 2.329  7878  . 377 7501  100.0000 . 0.135 . . 0.133 . . . . . 0.130 . 20 . 0.989 0.982 0.170 
'X-RAY DIFFRACTION' 2.329 2.551  7278  . 358 6920  100.0000 . 0.137 . . 0.135 . . . . . 0.136 . 20 . 0.989 0.981 0.174 
'X-RAY DIFFRACTION' 2.551 2.851  6626  . 303 6323  100.0000 . 0.146 . . 0.145 . . . . . 0.151 . 20 . 0.986 0.983 0.170 
'X-RAY DIFFRACTION' 2.851 3.291  5852  . 288 5564  100.0000 . 0.152 . . 0.150 . . . . . 0.164 . 20 . 0.985 0.979 0.185 
'X-RAY DIFFRACTION' 3.291 4.027  5007  . 236 4770  99.9800  . 0.157 . . 0.156 . . . . . 0.178 . 20 . 0.984 0.974 0.183 
'X-RAY DIFFRACTION' 4.027 5.682  3940  . 170 3769  99.9746  . 0.171 . . 0.170 . . . . . 0.204 . 20 . 0.984 0.976 0.197 
'X-RAY DIFFRACTION' 5.682 57.030 2288  . 134 2142  99.4755  . 0.216 . . 0.215 . . . . . 0.262 . 20 . 0.974 0.974 0.231 
# 
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                     9HAJ 
_struct.title                        'Structure of compound 1 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        9HAJ 
_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 2 ? 
E N N 3 ? 
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 9HAJ A 1 ? 306 ? P0DTC1 3264 ? 3569 ? 1 306 
2 1 9HAJ 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)' 3130  ? 
1 MORE         -17   ? 
1 'SSA (A^2)'  25380 ? 
# 
_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 THR A 45  ? MET A 49  ? THR A 45  MET A 49  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 SER A 62  ? HIS A 64  ? SER A 62  HIS A 64  5 ? 3  
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 ? MET A 235 ? THR A 226 MET A 235 1 ? 10 
HELX_P HELX_P9  AA9 LYS A 236 ? ASN A 238 ? LYS A 236 ASN A 238 5 ? 3  
HELX_P HELX_P10 AB1 THR A 243 ? LEU A 250 ? THR A 243 LEU A 250 1 ? 8  
HELX_P HELX_P11 AB2 LEU A 250 ? GLY A 258 ? LEU A 250 GLY A 258 1 ? 9  
HELX_P HELX_P12 AB3 ALA A 260 ? GLY A 275 ? ALA A 260 GLY A 275 1 ? 16 
HELX_P HELX_P13 AB4 THR A 292 ? CYS A 300 ? THR A 292 CYS A 300 1 ? 9  
HELX_P HELX_P14 AB5 SER B 10  ? GLY B 15  ? SER B 10  GLY B 15  1 ? 6  
HELX_P HELX_P15 AB6 HIS B 41  ? CYS B 44  ? HIS B 41  CYS B 44  5 ? 4  
HELX_P HELX_P16 AB7 THR B 45  ? LEU B 50  ? THR B 45  LEU B 50  1 ? 6  
HELX_P HELX_P17 AB8 ASN B 53  ? ARG B 60  ? ASN B 53  ARG B 60  1 ? 8  
HELX_P HELX_P18 AB9 LYS B 61  ? HIS B 64  ? LYS B 61  HIS B 64  5 ? 4  
HELX_P HELX_P19 AC1 ILE B 200 ? ASN B 214 ? ILE B 200 ASN B 214 1 ? 15 
HELX_P HELX_P20 AC2 THR B 226 ? TYR B 237 ? THR B 226 TYR B 237 1 ? 12 
HELX_P HELX_P21 AC3 THR B 243 ? LEU B 250 ? THR B 243 LEU B 250 1 ? 8  
HELX_P HELX_P22 AC4 LEU B 250 ? GLY B 258 ? LEU B 250 GLY B 258 1 ? 9  
HELX_P HELX_P23 AC5 ALA B 260 ? GLY B 275 ? ALA B 260 GLY B 275 1 ? 16 
HELX_P HELX_P24 AC6 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_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 LEU B 75  ? O LEU B 75  N VAL B 68  ? N VAL B 68  
AA4 2 3 O GLN B 69  ? O GLN B 69  N GLN B 19  ? N GLN B 19  
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                   9HAJ 
_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_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 CG A MET 162 ? ? SD A MET 162 ? ? CE  A MET 162 ? ? 88.58  100.20 -11.62 1.60 N 
2 1 CG B MET 162 ? ? SD B MET 162 ? ? CE  B MET 162 ? ? 84.71  100.20 -15.49 1.60 N 
3 1 CG B MET 165 ? ? SD B MET 165 ? ? CE  B MET 165 ? ? 88.85  100.20 -11.35 1.60 N 
4 1 CD B ARG 188 ? ? NE B ARG 188 ? ? CZ  B ARG 188 ? ? 132.80 123.60 9.20   1.40 N 
5 1 NE B ARG 188 ? ? CZ B ARG 188 ? ? NH1 B ARG 188 ? ? 114.71 120.30 -5.59  0.50 N 
6 1 NE B ARG 188 ? ? CZ B ARG 188 ? ? NH2 B ARG 188 ? ? 124.54 120.30 4.24   0.50 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 PHE A 3   ? ? -160.86 114.69  
2 1 ASP A 33  ? ? 54.01   -131.30 
3 1 ASN A 84  ? ? 53.48   -124.71 
4 1 ASP A 155 ? ? 84.24   -9.17   
5 1 GLN A 189 ? ? -86.63  48.18   
6 1 ASP B 33  ? ? 52.96   -134.29 
7 1 ASN B 51  ? ? -167.46 70.90   
8 1 ASN B 84  ? ? 53.67   -125.40 
9 1 TYR B 154 ? ? 54.25   -103.08 
# 
_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            0.110 
_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 844 ? 5.83 . 
2 1 O ? A HOH 845 ? 6.45 . 
3 1 O ? A HOH 846 ? 6.47 . 
# 
_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 
A1ITJ C4   C  Y N 1   
A1ITJ C5   C  N N 2   
A1ITJ C7   C  N N 3   
A1ITJ C8   C  N N 4   
A1ITJ C10  C  N N 5   
A1ITJ C13  C  Y N 6   
A1ITJ C17  C  Y N 7   
A1ITJ C21  C  N R 8   
A1ITJ C22  C  N N 9   
A1ITJ C24  C  N N 10  
A1ITJ C28  C  Y N 11  
A1ITJ C1   C  N N 12  
A1ITJ C2   C  N N 13  
A1ITJ C3   C  Y N 14  
A1ITJ N6   N  N N 15  
A1ITJ N9   N  N N 16  
A1ITJ C11  C  N N 17  
A1ITJ C12  C  N N 18  
A1ITJ C14  C  Y N 19  
A1ITJ N15  N  Y N 20  
A1ITJ C16  C  Y N 21  
A1ITJ CL18 CL N N 22  
A1ITJ C19  C  Y N 23  
A1ITJ O20  O  N N 24  
A1ITJ N23  N  N N 25  
A1ITJ C25  C  N N 26  
A1ITJ O26  O  N N 27  
A1ITJ C27  C  Y N 28  
A1ITJ C29  C  Y N 29  
A1ITJ BR30 BR N N 30  
A1ITJ C31  C  Y N 31  
A1ITJ H1   H  N N 32  
A1ITJ H2   H  N N 33  
A1ITJ H3   H  N N 34  
A1ITJ H4   H  N N 35  
A1ITJ H5   H  N N 36  
A1ITJ H6   H  N N 37  
A1ITJ H7   H  N N 38  
A1ITJ H8   H  N N 39  
A1ITJ H9   H  N N 40  
A1ITJ H10  H  N N 41  
A1ITJ H11  H  N N 42  
A1ITJ H12  H  N N 43  
A1ITJ H13  H  N N 44  
A1ITJ H14  H  N N 45  
A1ITJ H15  H  N N 46  
A1ITJ H16  H  N N 47  
A1ITJ H17  H  N N 48  
A1ITJ H19  H  N N 49  
A1ITJ H20  H  N N 50  
A1ITJ H21  H  N N 51  
A1ITJ H22  H  N N 52  
A1ITJ H23  H  N N 53  
A1ITJ H24  H  N N 54  
A1ITJ H25  H  N N 55  
A1ITJ H26  H  N N 56  
A1ITJ H27  H  N N 57  
A1ITJ H28  H  N N 58  
A1ITJ H29  H  N N 59  
ALA   N    N  N N 60  
ALA   CA   C  N S 61  
ALA   C    C  N N 62  
ALA   O    O  N N 63  
ALA   CB   C  N N 64  
ALA   OXT  O  N N 65  
ALA   H    H  N N 66  
ALA   H2   H  N N 67  
ALA   HA   H  N N 68  
ALA   HB1  H  N N 69  
ALA   HB2  H  N N 70  
ALA   HB3  H  N N 71  
ALA   HXT  H  N N 72  
ARG   N    N  N N 73  
ARG   CA   C  N S 74  
ARG   C    C  N N 75  
ARG   O    O  N N 76  
ARG   CB   C  N N 77  
ARG   CG   C  N N 78  
ARG   CD   C  N N 79  
ARG   NE   N  N N 80  
ARG   CZ   C  N N 81  
ARG   NH1  N  N N 82  
ARG   NH2  N  N N 83  
ARG   OXT  O  N N 84  
ARG   H    H  N N 85  
ARG   H2   H  N N 86  
ARG   HA   H  N N 87  
ARG   HB2  H  N N 88  
ARG   HB3  H  N N 89  
ARG   HG2  H  N N 90  
ARG   HG3  H  N N 91  
ARG   HD2  H  N N 92  
ARG   HD3  H  N N 93  
ARG   HE   H  N N 94  
ARG   HH11 H  N N 95  
ARG   HH12 H  N N 96  
ARG   HH21 H  N N 97  
ARG   HH22 H  N N 98  
ARG   HXT  H  N N 99  
ASN   N    N  N N 100 
ASN   CA   C  N S 101 
ASN   C    C  N N 102 
ASN   O    O  N N 103 
ASN   CB   C  N N 104 
ASN   CG   C  N N 105 
ASN   OD1  O  N N 106 
ASN   ND2  N  N N 107 
ASN   OXT  O  N N 108 
ASN   H    H  N N 109 
ASN   H2   H  N N 110 
ASN   HA   H  N N 111 
ASN   HB2  H  N N 112 
ASN   HB3  H  N N 113 
ASN   HD21 H  N N 114 
ASN   HD22 H  N N 115 
ASN   HXT  H  N N 116 
ASP   N    N  N N 117 
ASP   CA   C  N S 118 
ASP   C    C  N N 119 
ASP   O    O  N N 120 
ASP   CB   C  N N 121 
ASP   CG   C  N N 122 
ASP   OD1  O  N N 123 
ASP   OD2  O  N N 124 
ASP   OXT  O  N N 125 
ASP   H    H  N N 126 
ASP   H2   H  N N 127 
ASP   HA   H  N N 128 
ASP   HB2  H  N N 129 
ASP   HB3  H  N N 130 
ASP   HD2  H  N N 131 
ASP   HXT  H  N N 132 
CL    CL   CL N N 133 
CYS   N    N  N N 134 
CYS   CA   C  N R 135 
CYS   C    C  N N 136 
CYS   O    O  N N 137 
CYS   CB   C  N N 138 
CYS   SG   S  N N 139 
CYS   OXT  O  N N 140 
CYS   H    H  N N 141 
CYS   H2   H  N N 142 
CYS   HA   H  N N 143 
CYS   HB2  H  N N 144 
CYS   HB3  H  N N 145 
CYS   HG   H  N N 146 
CYS   HXT  H  N N 147 
DMS   S    S  N N 148 
DMS   O    O  N N 149 
DMS   C1   C  N N 150 
DMS   C2   C  N N 151 
DMS   H11  H  N N 152 
DMS   H12  H  N N 153 
DMS   H13  H  N N 154 
DMS   H21  H  N N 155 
DMS   H22  H  N N 156 
DMS   H23  H  N N 157 
GLN   N    N  N N 158 
GLN   CA   C  N S 159 
GLN   C    C  N N 160 
GLN   O    O  N N 161 
GLN   CB   C  N N 162 
GLN   CG   C  N N 163 
GLN   CD   C  N N 164 
GLN   OE1  O  N N 165 
GLN   NE2  N  N N 166 
GLN   OXT  O  N N 167 
GLN   H    H  N N 168 
GLN   H2   H  N N 169 
GLN   HA   H  N N 170 
GLN   HB2  H  N N 171 
GLN   HB3  H  N N 172 
GLN   HG2  H  N N 173 
GLN   HG3  H  N N 174 
GLN   HE21 H  N N 175 
GLN   HE22 H  N N 176 
GLN   HXT  H  N N 177 
GLU   N    N  N N 178 
GLU   CA   C  N S 179 
GLU   C    C  N N 180 
GLU   O    O  N N 181 
GLU   CB   C  N N 182 
GLU   CG   C  N N 183 
GLU   CD   C  N N 184 
GLU   OE1  O  N N 185 
GLU   OE2  O  N N 186 
GLU   OXT  O  N N 187 
GLU   H    H  N N 188 
GLU   H2   H  N N 189 
GLU   HA   H  N N 190 
GLU   HB2  H  N N 191 
GLU   HB3  H  N N 192 
GLU   HG2  H  N N 193 
GLU   HG3  H  N N 194 
GLU   HE2  H  N N 195 
GLU   HXT  H  N N 196 
GLY   N    N  N N 197 
GLY   CA   C  N N 198 
GLY   C    C  N N 199 
GLY   O    O  N N 200 
GLY   OXT  O  N N 201 
GLY   H    H  N N 202 
GLY   H2   H  N N 203 
GLY   HA2  H  N N 204 
GLY   HA3  H  N N 205 
GLY   HXT  H  N N 206 
HIS   N    N  N N 207 
HIS   CA   C  N S 208 
HIS   C    C  N N 209 
HIS   O    O  N N 210 
HIS   CB   C  N N 211 
HIS   CG   C  Y N 212 
HIS   ND1  N  Y N 213 
HIS   CD2  C  Y N 214 
HIS   CE1  C  Y N 215 
HIS   NE2  N  Y N 216 
HIS   OXT  O  N N 217 
HIS   H    H  N N 218 
HIS   H2   H  N N 219 
HIS   HA   H  N N 220 
HIS   HB2  H  N N 221 
HIS   HB3  H  N N 222 
HIS   HD1  H  N N 223 
HIS   HD2  H  N N 224 
HIS   HE1  H  N N 225 
HIS   HE2  H  N N 226 
HIS   HXT  H  N N 227 
HOH   O    O  N N 228 
HOH   H1   H  N N 229 
HOH   H2   H  N N 230 
ILE   N    N  N N 231 
ILE   CA   C  N S 232 
ILE   C    C  N N 233 
ILE   O    O  N N 234 
ILE   CB   C  N S 235 
ILE   CG1  C  N N 236 
ILE   CG2  C  N N 237 
ILE   CD1  C  N N 238 
ILE   OXT  O  N N 239 
ILE   H    H  N N 240 
ILE   H2   H  N N 241 
ILE   HA   H  N N 242 
ILE   HB   H  N N 243 
ILE   HG12 H  N N 244 
ILE   HG13 H  N N 245 
ILE   HG21 H  N N 246 
ILE   HG22 H  N N 247 
ILE   HG23 H  N N 248 
ILE   HD11 H  N N 249 
ILE   HD12 H  N N 250 
ILE   HD13 H  N N 251 
ILE   HXT  H  N N 252 
LEU   N    N  N N 253 
LEU   CA   C  N S 254 
LEU   C    C  N N 255 
LEU   O    O  N N 256 
LEU   CB   C  N N 257 
LEU   CG   C  N N 258 
LEU   CD1  C  N N 259 
LEU   CD2  C  N N 260 
LEU   OXT  O  N N 261 
LEU   H    H  N N 262 
LEU   H2   H  N N 263 
LEU   HA   H  N N 264 
LEU   HB2  H  N N 265 
LEU   HB3  H  N N 266 
LEU   HG   H  N N 267 
LEU   HD11 H  N N 268 
LEU   HD12 H  N N 269 
LEU   HD13 H  N N 270 
LEU   HD21 H  N N 271 
LEU   HD22 H  N N 272 
LEU   HD23 H  N N 273 
LEU   HXT  H  N N 274 
LYS   N    N  N N 275 
LYS   CA   C  N S 276 
LYS   C    C  N N 277 
LYS   O    O  N N 278 
LYS   CB   C  N N 279 
LYS   CG   C  N N 280 
LYS   CD   C  N N 281 
LYS   CE   C  N N 282 
LYS   NZ   N  N N 283 
LYS   OXT  O  N N 284 
LYS   H    H  N N 285 
LYS   H2   H  N N 286 
LYS   HA   H  N N 287 
LYS   HB2  H  N N 288 
LYS   HB3  H  N N 289 
LYS   HG2  H  N N 290 
LYS   HG3  H  N N 291 
LYS   HD2  H  N N 292 
LYS   HD3  H  N N 293 
LYS   HE2  H  N N 294 
LYS   HE3  H  N N 295 
LYS   HZ1  H  N N 296 
LYS   HZ2  H  N N 297 
LYS   HZ3  H  N N 298 
LYS   HXT  H  N N 299 
MET   N    N  N N 300 
MET   CA   C  N S 301 
MET   C    C  N N 302 
MET   O    O  N N 303 
MET   CB   C  N N 304 
MET   CG   C  N N 305 
MET   SD   S  N N 306 
MET   CE   C  N N 307 
MET   OXT  O  N N 308 
MET   H    H  N N 309 
MET   H2   H  N N 310 
MET   HA   H  N N 311 
MET   HB2  H  N N 312 
MET   HB3  H  N N 313 
MET   HG2  H  N N 314 
MET   HG3  H  N N 315 
MET   HE1  H  N N 316 
MET   HE2  H  N N 317 
MET   HE3  H  N N 318 
MET   HXT  H  N N 319 
PHE   N    N  N N 320 
PHE   CA   C  N S 321 
PHE   C    C  N N 322 
PHE   O    O  N N 323 
PHE   CB   C  N N 324 
PHE   CG   C  Y N 325 
PHE   CD1  C  Y N 326 
PHE   CD2  C  Y N 327 
PHE   CE1  C  Y N 328 
PHE   CE2  C  Y N 329 
PHE   CZ   C  Y N 330 
PHE   OXT  O  N N 331 
PHE   H    H  N N 332 
PHE   H2   H  N N 333 
PHE   HA   H  N N 334 
PHE   HB2  H  N N 335 
PHE   HB3  H  N N 336 
PHE   HD1  H  N N 337 
PHE   HD2  H  N N 338 
PHE   HE1  H  N N 339 
PHE   HE2  H  N N 340 
PHE   HZ   H  N N 341 
PHE   HXT  H  N N 342 
PRO   N    N  N N 343 
PRO   CA   C  N S 344 
PRO   C    C  N N 345 
PRO   O    O  N N 346 
PRO   CB   C  N N 347 
PRO   CG   C  N N 348 
PRO   CD   C  N N 349 
PRO   OXT  O  N N 350 
PRO   H    H  N N 351 
PRO   HA   H  N N 352 
PRO   HB2  H  N N 353 
PRO   HB3  H  N N 354 
PRO   HG2  H  N N 355 
PRO   HG3  H  N N 356 
PRO   HD2  H  N N 357 
PRO   HD3  H  N N 358 
PRO   HXT  H  N N 359 
SER   N    N  N N 360 
SER   CA   C  N S 361 
SER   C    C  N N 362 
SER   O    O  N N 363 
SER   CB   C  N N 364 
SER   OG   O  N N 365 
SER   OXT  O  N N 366 
SER   H    H  N N 367 
SER   H2   H  N N 368 
SER   HA   H  N N 369 
SER   HB2  H  N N 370 
SER   HB3  H  N N 371 
SER   HG   H  N N 372 
SER   HXT  H  N N 373 
THR   N    N  N N 374 
THR   CA   C  N S 375 
THR   C    C  N N 376 
THR   O    O  N N 377 
THR   CB   C  N R 378 
THR   OG1  O  N N 379 
THR   CG2  C  N N 380 
THR   OXT  O  N N 381 
THR   H    H  N N 382 
THR   H2   H  N N 383 
THR   HA   H  N N 384 
THR   HB   H  N N 385 
THR   HG1  H  N N 386 
THR   HG21 H  N N 387 
THR   HG22 H  N N 388 
THR   HG23 H  N N 389 
THR   HXT  H  N N 390 
TRP   N    N  N N 391 
TRP   CA   C  N S 392 
TRP   C    C  N N 393 
TRP   O    O  N N 394 
TRP   CB   C  N N 395 
TRP   CG   C  Y N 396 
TRP   CD1  C  Y N 397 
TRP   CD2  C  Y N 398 
TRP   NE1  N  Y N 399 
TRP   CE2  C  Y N 400 
TRP   CE3  C  Y N 401 
TRP   CZ2  C  Y N 402 
TRP   CZ3  C  Y N 403 
TRP   CH2  C  Y N 404 
TRP   OXT  O  N N 405 
TRP   H    H  N N 406 
TRP   H2   H  N N 407 
TRP   HA   H  N N 408 
TRP   HB2  H  N N 409 
TRP   HB3  H  N N 410 
TRP   HD1  H  N N 411 
TRP   HE1  H  N N 412 
TRP   HE3  H  N N 413 
TRP   HZ2  H  N N 414 
TRP   HZ3  H  N N 415 
TRP   HH2  H  N N 416 
TRP   HXT  H  N N 417 
TYR   N    N  N N 418 
TYR   CA   C  N S 419 
TYR   C    C  N N 420 
TYR   O    O  N N 421 
TYR   CB   C  N N 422 
TYR   CG   C  Y N 423 
TYR   CD1  C  Y N 424 
TYR   CD2  C  Y N 425 
TYR   CE1  C  Y N 426 
TYR   CE2  C  Y N 427 
TYR   CZ   C  Y N 428 
TYR   OH   O  N N 429 
TYR   OXT  O  N N 430 
TYR   H    H  N N 431 
TYR   H2   H  N N 432 
TYR   HA   H  N N 433 
TYR   HB2  H  N N 434 
TYR   HB3  H  N N 435 
TYR   HD1  H  N N 436 
TYR   HD2  H  N N 437 
TYR   HE1  H  N N 438 
TYR   HE2  H  N N 439 
TYR   HH   H  N N 440 
TYR   HXT  H  N N 441 
VAL   N    N  N N 442 
VAL   CA   C  N S 443 
VAL   C    C  N N 444 
VAL   O    O  N N 445 
VAL   CB   C  N N 446 
VAL   CG1  C  N N 447 
VAL   CG2  C  N N 448 
VAL   OXT  O  N N 449 
VAL   H    H  N N 450 
VAL   H2   H  N N 451 
VAL   HA   H  N N 452 
VAL   HB   H  N N 453 
VAL   HG11 H  N N 454 
VAL   HG12 H  N N 455 
VAL   HG13 H  N N 456 
VAL   HG21 H  N N 457 
VAL   HG22 H  N N 458 
VAL   HG23 H  N N 459 
VAL   HXT  H  N N 460 
# 
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 
A1ITJ BR30 C29  sing N N 1   
A1ITJ C29  C31  doub Y N 2   
A1ITJ C29  C28  sing Y N 3   
A1ITJ C31  C3   sing Y N 4   
A1ITJ C28  C27  doub Y N 5   
A1ITJ C3   C2   sing N N 6   
A1ITJ C3   C4   doub Y N 7   
A1ITJ C2   C1   sing N N 8   
A1ITJ C27  C4   sing Y N 9   
A1ITJ C4   C5   sing N N 10  
A1ITJ C5   N6   sing N N 11  
A1ITJ O26  C22  doub N N 12  
A1ITJ N6   C7   sing N N 13  
A1ITJ N6   C21  sing N N 14  
A1ITJ C22  N23  sing N N 15  
A1ITJ C22  C21  sing N N 16  
A1ITJ C24  N23  sing N N 17  
A1ITJ C24  C25  sing N N 18  
A1ITJ C7   C8   sing N N 19  
A1ITJ C21  C11  sing N N 20  
A1ITJ C8   N9   sing N N 21  
A1ITJ C11  C10  sing N N 22  
A1ITJ N9   C10  sing N N 23  
A1ITJ N9   C12  sing N N 24  
A1ITJ CL18 C17  sing N N 25  
A1ITJ C16  C17  doub Y N 26  
A1ITJ C16  N15  sing Y N 27  
A1ITJ C17  C19  sing Y N 28  
A1ITJ N15  C14  doub Y N 29  
A1ITJ C19  C13  doub Y N 30  
A1ITJ C14  C13  sing Y N 31  
A1ITJ C13  C12  sing N N 32  
A1ITJ C12  O20  doub N N 33  
A1ITJ C5   H1   sing N N 34  
A1ITJ C5   H2   sing N N 35  
A1ITJ C7   H3   sing N N 36  
A1ITJ C7   H4   sing N N 37  
A1ITJ C8   H5   sing N N 38  
A1ITJ C8   H6   sing N N 39  
A1ITJ C10  H7   sing N N 40  
A1ITJ C10  H8   sing N N 41  
A1ITJ C21  H9   sing N N 42  
A1ITJ C24  H10  sing N N 43  
A1ITJ C24  H11  sing N N 44  
A1ITJ C28  H12  sing N N 45  
A1ITJ C1   H13  sing N N 46  
A1ITJ C1   H14  sing N N 47  
A1ITJ C1   H15  sing N N 48  
A1ITJ C2   H16  sing N N 49  
A1ITJ C2   H17  sing N N 50  
A1ITJ C11  H19  sing N N 51  
A1ITJ C11  H20  sing N N 52  
A1ITJ C14  H21  sing N N 53  
A1ITJ C16  H22  sing N N 54  
A1ITJ C19  H23  sing N N 55  
A1ITJ N23  H24  sing N N 56  
A1ITJ C25  H25  sing N N 57  
A1ITJ C25  H26  sing N N 58  
A1ITJ C25  H27  sing N N 59  
A1ITJ C27  H28  sing N N 60  
A1ITJ C31  H29  sing N N 61  
ALA   N    CA   sing N N 62  
ALA   N    H    sing N N 63  
ALA   N    H2   sing N N 64  
ALA   CA   C    sing N N 65  
ALA   CA   CB   sing N N 66  
ALA   CA   HA   sing N N 67  
ALA   C    O    doub N N 68  
ALA   C    OXT  sing N N 69  
ALA   CB   HB1  sing N N 70  
ALA   CB   HB2  sing N N 71  
ALA   CB   HB3  sing N N 72  
ALA   OXT  HXT  sing N N 73  
ARG   N    CA   sing N N 74  
ARG   N    H    sing N N 75  
ARG   N    H2   sing N N 76  
ARG   CA   C    sing N N 77  
ARG   CA   CB   sing N N 78  
ARG   CA   HA   sing N N 79  
ARG   C    O    doub N N 80  
ARG   C    OXT  sing N N 81  
ARG   CB   CG   sing N N 82  
ARG   CB   HB2  sing N N 83  
ARG   CB   HB3  sing N N 84  
ARG   CG   CD   sing N N 85  
ARG   CG   HG2  sing N N 86  
ARG   CG   HG3  sing N N 87  
ARG   CD   NE   sing N N 88  
ARG   CD   HD2  sing N N 89  
ARG   CD   HD3  sing N N 90  
ARG   NE   CZ   sing N N 91  
ARG   NE   HE   sing N N 92  
ARG   CZ   NH1  sing N N 93  
ARG   CZ   NH2  doub N N 94  
ARG   NH1  HH11 sing N N 95  
ARG   NH1  HH12 sing N N 96  
ARG   NH2  HH21 sing N N 97  
ARG   NH2  HH22 sing N N 98  
ARG   OXT  HXT  sing N N 99  
ASN   N    CA   sing N N 100 
ASN   N    H    sing N N 101 
ASN   N    H2   sing N N 102 
ASN   CA   C    sing N N 103 
ASN   CA   CB   sing N N 104 
ASN   CA   HA   sing N N 105 
ASN   C    O    doub N N 106 
ASN   C    OXT  sing N N 107 
ASN   CB   CG   sing N N 108 
ASN   CB   HB2  sing N N 109 
ASN   CB   HB3  sing N N 110 
ASN   CG   OD1  doub N N 111 
ASN   CG   ND2  sing N N 112 
ASN   ND2  HD21 sing N N 113 
ASN   ND2  HD22 sing N N 114 
ASN   OXT  HXT  sing N N 115 
ASP   N    CA   sing N N 116 
ASP   N    H    sing N N 117 
ASP   N    H2   sing N N 118 
ASP   CA   C    sing N N 119 
ASP   CA   CB   sing N N 120 
ASP   CA   HA   sing N N 121 
ASP   C    O    doub N N 122 
ASP   C    OXT  sing N N 123 
ASP   CB   CG   sing N N 124 
ASP   CB   HB2  sing N N 125 
ASP   CB   HB3  sing N N 126 
ASP   CG   OD1  doub N N 127 
ASP   CG   OD2  sing N N 128 
ASP   OD2  HD2  sing N N 129 
ASP   OXT  HXT  sing N N 130 
CYS   N    CA   sing N N 131 
CYS   N    H    sing N N 132 
CYS   N    H2   sing N N 133 
CYS   CA   C    sing N N 134 
CYS   CA   CB   sing N N 135 
CYS   CA   HA   sing N N 136 
CYS   C    O    doub N N 137 
CYS   C    OXT  sing N N 138 
CYS   CB   SG   sing N N 139 
CYS   CB   HB2  sing N N 140 
CYS   CB   HB3  sing N N 141 
CYS   SG   HG   sing N N 142 
CYS   OXT  HXT  sing N N 143 
DMS   S    O    doub N N 144 
DMS   S    C1   sing N N 145 
DMS   S    C2   sing N N 146 
DMS   C1   H11  sing N N 147 
DMS   C1   H12  sing N N 148 
DMS   C1   H13  sing N N 149 
DMS   C2   H21  sing N N 150 
DMS   C2   H22  sing N N 151 
DMS   C2   H23  sing N N 152 
GLN   N    CA   sing N N 153 
GLN   N    H    sing N N 154 
GLN   N    H2   sing N N 155 
GLN   CA   C    sing N N 156 
GLN   CA   CB   sing N N 157 
GLN   CA   HA   sing N N 158 
GLN   C    O    doub N N 159 
GLN   C    OXT  sing N N 160 
GLN   CB   CG   sing N N 161 
GLN   CB   HB2  sing N N 162 
GLN   CB   HB3  sing N N 163 
GLN   CG   CD   sing N N 164 
GLN   CG   HG2  sing N N 165 
GLN   CG   HG3  sing N N 166 
GLN   CD   OE1  doub N N 167 
GLN   CD   NE2  sing N N 168 
GLN   NE2  HE21 sing N N 169 
GLN   NE2  HE22 sing N N 170 
GLN   OXT  HXT  sing N N 171 
GLU   N    CA   sing N N 172 
GLU   N    H    sing N N 173 
GLU   N    H2   sing N N 174 
GLU   CA   C    sing N N 175 
GLU   CA   CB   sing N N 176 
GLU   CA   HA   sing N N 177 
GLU   C    O    doub N N 178 
GLU   C    OXT  sing N N 179 
GLU   CB   CG   sing N N 180 
GLU   CB   HB2  sing N N 181 
GLU   CB   HB3  sing N N 182 
GLU   CG   CD   sing N N 183 
GLU   CG   HG2  sing N N 184 
GLU   CG   HG3  sing N N 185 
GLU   CD   OE1  doub N N 186 
GLU   CD   OE2  sing N N 187 
GLU   OE2  HE2  sing N N 188 
GLU   OXT  HXT  sing N N 189 
GLY   N    CA   sing N N 190 
GLY   N    H    sing N N 191 
GLY   N    H2   sing N N 192 
GLY   CA   C    sing N N 193 
GLY   CA   HA2  sing N N 194 
GLY   CA   HA3  sing N N 195 
GLY   C    O    doub N N 196 
GLY   C    OXT  sing N N 197 
GLY   OXT  HXT  sing N N 198 
HIS   N    CA   sing N N 199 
HIS   N    H    sing N N 200 
HIS   N    H2   sing N N 201 
HIS   CA   C    sing N N 202 
HIS   CA   CB   sing N N 203 
HIS   CA   HA   sing N N 204 
HIS   C    O    doub N N 205 
HIS   C    OXT  sing N N 206 
HIS   CB   CG   sing N N 207 
HIS   CB   HB2  sing N N 208 
HIS   CB   HB3  sing N N 209 
HIS   CG   ND1  sing Y N 210 
HIS   CG   CD2  doub Y N 211 
HIS   ND1  CE1  doub Y N 212 
HIS   ND1  HD1  sing N N 213 
HIS   CD2  NE2  sing Y N 214 
HIS   CD2  HD2  sing N N 215 
HIS   CE1  NE2  sing Y N 216 
HIS   CE1  HE1  sing N N 217 
HIS   NE2  HE2  sing N N 218 
HIS   OXT  HXT  sing N N 219 
HOH   O    H1   sing N N 220 
HOH   O    H2   sing N N 221 
ILE   N    CA   sing N N 222 
ILE   N    H    sing N N 223 
ILE   N    H2   sing N N 224 
ILE   CA   C    sing N N 225 
ILE   CA   CB   sing N N 226 
ILE   CA   HA   sing N N 227 
ILE   C    O    doub N N 228 
ILE   C    OXT  sing N N 229 
ILE   CB   CG1  sing N N 230 
ILE   CB   CG2  sing N N 231 
ILE   CB   HB   sing N N 232 
ILE   CG1  CD1  sing N N 233 
ILE   CG1  HG12 sing N N 234 
ILE   CG1  HG13 sing N N 235 
ILE   CG2  HG21 sing N N 236 
ILE   CG2  HG22 sing N N 237 
ILE   CG2  HG23 sing N N 238 
ILE   CD1  HD11 sing N N 239 
ILE   CD1  HD12 sing N N 240 
ILE   CD1  HD13 sing N N 241 
ILE   OXT  HXT  sing N N 242 
LEU   N    CA   sing N N 243 
LEU   N    H    sing N N 244 
LEU   N    H2   sing N N 245 
LEU   CA   C    sing N N 246 
LEU   CA   CB   sing N N 247 
LEU   CA   HA   sing N N 248 
LEU   C    O    doub N N 249 
LEU   C    OXT  sing N N 250 
LEU   CB   CG   sing N N 251 
LEU   CB   HB2  sing N N 252 
LEU   CB   HB3  sing N N 253 
LEU   CG   CD1  sing N N 254 
LEU   CG   CD2  sing N N 255 
LEU   CG   HG   sing N N 256 
LEU   CD1  HD11 sing N N 257 
LEU   CD1  HD12 sing N N 258 
LEU   CD1  HD13 sing N N 259 
LEU   CD2  HD21 sing N N 260 
LEU   CD2  HD22 sing N N 261 
LEU   CD2  HD23 sing N N 262 
LEU   OXT  HXT  sing N N 263 
LYS   N    CA   sing N N 264 
LYS   N    H    sing N N 265 
LYS   N    H2   sing N N 266 
LYS   CA   C    sing N N 267 
LYS   CA   CB   sing N N 268 
LYS   CA   HA   sing N N 269 
LYS   C    O    doub N N 270 
LYS   C    OXT  sing N N 271 
LYS   CB   CG   sing N N 272 
LYS   CB   HB2  sing N N 273 
LYS   CB   HB3  sing N N 274 
LYS   CG   CD   sing N N 275 
LYS   CG   HG2  sing N N 276 
LYS   CG   HG3  sing N N 277 
LYS   CD   CE   sing N N 278 
LYS   CD   HD2  sing N N 279 
LYS   CD   HD3  sing N N 280 
LYS   CE   NZ   sing N N 281 
LYS   CE   HE2  sing N N 282 
LYS   CE   HE3  sing N N 283 
LYS   NZ   HZ1  sing N N 284 
LYS   NZ   HZ2  sing N N 285 
LYS   NZ   HZ3  sing N N 286 
LYS   OXT  HXT  sing N N 287 
MET   N    CA   sing N N 288 
MET   N    H    sing N N 289 
MET   N    H2   sing N N 290 
MET   CA   C    sing N N 291 
MET   CA   CB   sing N N 292 
MET   CA   HA   sing N N 293 
MET   C    O    doub N N 294 
MET   C    OXT  sing N N 295 
MET   CB   CG   sing N N 296 
MET   CB   HB2  sing N N 297 
MET   CB   HB3  sing N N 298 
MET   CG   SD   sing N N 299 
MET   CG   HG2  sing N N 300 
MET   CG   HG3  sing N N 301 
MET   SD   CE   sing N N 302 
MET   CE   HE1  sing N N 303 
MET   CE   HE2  sing N N 304 
MET   CE   HE3  sing N N 305 
MET   OXT  HXT  sing N N 306 
PHE   N    CA   sing N N 307 
PHE   N    H    sing N N 308 
PHE   N    H2   sing N N 309 
PHE   CA   C    sing N N 310 
PHE   CA   CB   sing N N 311 
PHE   CA   HA   sing N N 312 
PHE   C    O    doub N N 313 
PHE   C    OXT  sing N N 314 
PHE   CB   CG   sing N N 315 
PHE   CB   HB2  sing N N 316 
PHE   CB   HB3  sing N N 317 
PHE   CG   CD1  doub Y N 318 
PHE   CG   CD2  sing Y N 319 
PHE   CD1  CE1  sing Y N 320 
PHE   CD1  HD1  sing N N 321 
PHE   CD2  CE2  doub Y N 322 
PHE   CD2  HD2  sing N N 323 
PHE   CE1  CZ   doub Y N 324 
PHE   CE1  HE1  sing N N 325 
PHE   CE2  CZ   sing Y N 326 
PHE   CE2  HE2  sing N N 327 
PHE   CZ   HZ   sing N N 328 
PHE   OXT  HXT  sing N N 329 
PRO   N    CA   sing N N 330 
PRO   N    CD   sing N N 331 
PRO   N    H    sing N N 332 
PRO   CA   C    sing N N 333 
PRO   CA   CB   sing N N 334 
PRO   CA   HA   sing N N 335 
PRO   C    O    doub N N 336 
PRO   C    OXT  sing N N 337 
PRO   CB   CG   sing N N 338 
PRO   CB   HB2  sing N N 339 
PRO   CB   HB3  sing N N 340 
PRO   CG   CD   sing N N 341 
PRO   CG   HG2  sing N N 342 
PRO   CG   HG3  sing N N 343 
PRO   CD   HD2  sing N N 344 
PRO   CD   HD3  sing N N 345 
PRO   OXT  HXT  sing N N 346 
SER   N    CA   sing N N 347 
SER   N    H    sing N N 348 
SER   N    H2   sing N N 349 
SER   CA   C    sing N N 350 
SER   CA   CB   sing N N 351 
SER   CA   HA   sing N N 352 
SER   C    O    doub N N 353 
SER   C    OXT  sing N N 354 
SER   CB   OG   sing N N 355 
SER   CB   HB2  sing N N 356 
SER   CB   HB3  sing N N 357 
SER   OG   HG   sing N N 358 
SER   OXT  HXT  sing N N 359 
THR   N    CA   sing N N 360 
THR   N    H    sing N N 361 
THR   N    H2   sing N N 362 
THR   CA   C    sing N N 363 
THR   CA   CB   sing N N 364 
THR   CA   HA   sing N N 365 
THR   C    O    doub N N 366 
THR   C    OXT  sing N N 367 
THR   CB   OG1  sing N N 368 
THR   CB   CG2  sing N N 369 
THR   CB   HB   sing N N 370 
THR   OG1  HG1  sing N N 371 
THR   CG2  HG21 sing N N 372 
THR   CG2  HG22 sing N N 373 
THR   CG2  HG23 sing N N 374 
THR   OXT  HXT  sing N N 375 
TRP   N    CA   sing N N 376 
TRP   N    H    sing N N 377 
TRP   N    H2   sing N N 378 
TRP   CA   C    sing N N 379 
TRP   CA   CB   sing N N 380 
TRP   CA   HA   sing N N 381 
TRP   C    O    doub N N 382 
TRP   C    OXT  sing N N 383 
TRP   CB   CG   sing N N 384 
TRP   CB   HB2  sing N N 385 
TRP   CB   HB3  sing N N 386 
TRP   CG   CD1  doub Y N 387 
TRP   CG   CD2  sing Y N 388 
TRP   CD1  NE1  sing Y N 389 
TRP   CD1  HD1  sing N N 390 
TRP   CD2  CE2  doub Y N 391 
TRP   CD2  CE3  sing Y N 392 
TRP   NE1  CE2  sing Y N 393 
TRP   NE1  HE1  sing N N 394 
TRP   CE2  CZ2  sing Y N 395 
TRP   CE3  CZ3  doub Y N 396 
TRP   CE3  HE3  sing N N 397 
TRP   CZ2  CH2  doub Y N 398 
TRP   CZ2  HZ2  sing N N 399 
TRP   CZ3  CH2  sing Y N 400 
TRP   CZ3  HZ3  sing N N 401 
TRP   CH2  HH2  sing N N 402 
TRP   OXT  HXT  sing N N 403 
TYR   N    CA   sing N N 404 
TYR   N    H    sing N N 405 
TYR   N    H2   sing N N 406 
TYR   CA   C    sing N N 407 
TYR   CA   CB   sing N N 408 
TYR   CA   HA   sing N N 409 
TYR   C    O    doub N N 410 
TYR   C    OXT  sing N N 411 
TYR   CB   CG   sing N N 412 
TYR   CB   HB2  sing N N 413 
TYR   CB   HB3  sing N N 414 
TYR   CG   CD1  doub Y N 415 
TYR   CG   CD2  sing Y N 416 
TYR   CD1  CE1  sing Y N 417 
TYR   CD1  HD1  sing N N 418 
TYR   CD2  CE2  doub Y N 419 
TYR   CD2  HD2  sing N N 420 
TYR   CE1  CZ   doub Y N 421 
TYR   CE1  HE1  sing N N 422 
TYR   CE2  CZ   sing Y N 423 
TYR   CE2  HE2  sing N N 424 
TYR   CZ   OH   sing N N 425 
TYR   OH   HH   sing N N 426 
TYR   OXT  HXT  sing N N 427 
VAL   N    CA   sing N N 428 
VAL   N    H    sing N N 429 
VAL   N    H2   sing N N 430 
VAL   CA   C    sing N N 431 
VAL   CA   CB   sing N N 432 
VAL   CA   HA   sing N N 433 
VAL   C    O    doub N N 434 
VAL   C    OXT  sing N N 435 
VAL   CB   CG1  sing N N 436 
VAL   CB   CG2  sing N N 437 
VAL   CB   HB   sing N N 438 
VAL   CG1  HG11 sing N N 439 
VAL   CG1  HG12 sing N N 440 
VAL   CG1  HG13 sing N N 441 
VAL   CG2  HG21 sing N N 442 
VAL   CG2  HG22 sing N N 443 
VAL   CG2  HG23 sing N N 444 
VAL   OXT  HXT  sing N N 445 
# 
_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                    9HAJ 
_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]   0.014696 
_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]   0.010035 
_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]   0.009602 
_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  0.7273   
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  -9.3378  
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 0.7359   
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  1.0555   
# 
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   ? 13.667  9.293   -12.837 1   14.395 ? 1   SER   A N    1 
ATOM   2    C  CA   . SER   A 1 1   ? 13.877  8.316   -13.935 1   14.611 ? 1   SER   A CA   1 
ATOM   3    C  C    . SER   A 1 1   ? 12.722  7.321   -13.964 1   13.633 ? 1   SER   A C    1 
ATOM   4    O  O    . SER   A 1 1   ? 11.823  7.379   -13.134 1   12.465 ? 1   SER   A O    1 
ATOM   5    C  CB   . SER   A 1 1   ? 15.229  7.614   -13.819 1   15.428 ? 1   SER   A CB   1 
ATOM   6    O  OG   . SER   A 1 1   ? 15.531  6.9     -15.012 1   20.308 ? 1   SER   A OG   1 
ATOM   7    N  N    . GLY   A 1 2   ? 12.773  6.403   -14.935 1   13.712 ? 2   GLY   A N    1 
ATOM   8    C  CA   . GLY   A 1 2   ? 11.699  5.472   -15.211 1   13.352 ? 2   GLY   A CA   1 
ATOM   9    C  C    . GLY   A 1 2   ? 10.86   5.93    -16.399 1   12.837 ? 2   GLY   A C    1 
ATOM   10   O  O    . GLY   A 1 2   ? 10.909  7.085   -16.81  1   13.903 ? 2   GLY   A O    1 
ATOM   11   N  N    . PHE   A 1 3   ? 10.053  5.007   -16.907 1   12.507 ? 3   PHE   A N    1 
ATOM   12   C  CA   . PHE   A 1 3   ? 9.166   5.334   -18.013 1   12.767 ? 3   PHE   A CA   1 
ATOM   13   C  C    . PHE   A 1 3   ? 8.072   4.284   -18.055 1   13.083 ? 3   PHE   A C    1 
ATOM   14   O  O    . PHE   A 1 3   ? 8.345   3.113   -18.306 1   14.127 ? 3   PHE   A O    1 
ATOM   15   C  CB   . PHE   A 1 3   ? 9.935   5.434   -19.339 1   13.534 ? 3   PHE   A CB   1 
ATOM   16   C  CG   . PHE   A 1 3   ? 9.191   6.284   -20.356 1   14.219 ? 3   PHE   A CG   1 
ATOM   17   C  CD1  . PHE   A 1 3   ? 9.173   7.671   -20.256 1   14.858 ? 3   PHE   A CD1  1 
ATOM   18   C  CD2  . PHE   A 1 3   ? 8.465   5.685   -21.381 1   15.336 ? 3   PHE   A CD2  1 
ATOM   19   C  CE1  . PHE   A 1 3   ? 8.455   8.441   -21.156 1   15.794 ? 3   PHE   A CE1  1 
ATOM   20   C  CE2  . PHE   A 1 3   ? 7.771   6.463   -22.295 1   15.487 ? 3   PHE   A CE2  1 
ATOM   21   C  CZ   . PHE   A 1 3   ? 7.757   7.835   -22.172 1   16.146 ? 3   PHE   A CZ   1 
ATOM   22   N  N    . ARG   A 1 4   ? 6.836   4.729   -17.796 1   12.2   ? 4   ARG   A N    1 
ATOM   23   C  CA   . ARG   A 1 4   ? 5.706   3.832   -17.657 1   12.821 ? 4   ARG   A CA   1 
ATOM   24   C  C    . ARG   A 1 4   ? 4.576   4.316   -18.55  1   12.152 ? 4   ARG   A C    1 
ATOM   25   O  O    . ARG   A 1 4   ? 4.483   5.504   -18.847 1   11.678 ? 4   ARG   A O    1 
ATOM   26   C  CB   . ARG   A 1 4   ? 5.195   3.867   -16.212 1   13.693 ? 4   ARG   A CB   1 
ATOM   27   C  CG   . ARG   A 1 4   ? 6.052   3.161   -15.172 1   15.367 ? 4   ARG   A CG   1 
ATOM   28   C  CD   . ARG   A 1 4   ? 5.726   1.69    -15.291 1   17.839 ? 4   ARG   A CD   1 
ATOM   29   N  NE   . ARG   A 1 4   ? 6.374   0.841   -14.292 1   18.139 ? 4   ARG   A NE   1 
ATOM   30   C  CZ   . ARG   A 1 4   ? 6.262   -0.478  -14.273 1   17.542 ? 4   ARG   A CZ   1 
ATOM   31   N  NH1  . ARG   A 1 4   ? 5.478   -1.082  -15.144 1   17.824 ? 4   ARG   A NH1  1 
ATOM   32   N  NH2  . ARG   A 1 4   ? 6.918   -1.193  -13.378 1   17.236 ? 4   ARG   A NH2  1 
ATOM   33   N  N    . LYS   A 1 5   ? 3.686   3.395   -18.918 1   13.773 ? 5   LYS   A N    1 
ATOM   34   C  CA   . LYS   A 1 5   ? 2.406   3.8     -19.474 1   14.432 ? 5   LYS   A CA   1 
ATOM   35   C  C    . LYS   A 1 5   ? 1.644   4.485   -18.342 1   13.769 ? 5   LYS   A C    1 
ATOM   36   O  O    . LYS   A 1 5   ? 1.19    3.827   -17.401 1   17.71  ? 5   LYS   A O    1 
ATOM   37   C  CB   . LYS   A 1 5   ? 1.62    2.606   -20.013 1   17.864 ? 5   LYS   A CB   1 
ATOM   38   C  CG   . LYS   A 1 5   ? 2.089   2.108   -21.354 1   21.859 ? 5   LYS   A CG   1 
ATOM   39   C  CD   . LYS   A 1 5   ? 1.02    1.249   -22.015 1   26.088 ? 5   LYS   A CD   1 
ATOM   40   C  CE   . LYS   A 1 5   ? 1.462   0.606   -23.278 1   29.827 ? 5   LYS   A CE   1 
ATOM   41   N  NZ   . LYS   A 1 5   ? 1.86    1.634   -24.232 1   30.599 ? 5   LYS   A NZ   1 
ATOM   42   N  N    . MET   A 1 6   ? 1.543   5.805   -18.419 1   12.965 ? 6   MET   A N    1 
ATOM   43   C  CA   A MET   A 1 6   ? 1.039   6.624   -17.332 0.6 13.14  ? 6   MET   A CA   1 
ATOM   44   C  CA   B MET   A 1 6   ? 1.009   6.574   -17.317 0.4 13.369 ? 6   MET   A CA   1 
ATOM   45   C  C    . MET   A 1 6   ? -0.298  7.237   -17.729 1   12.66  ? 6   MET   A C    1 
ATOM   46   O  O    . MET   A 1 6   ? -0.351  8.043   -18.657 1   12.947 ? 6   MET   A O    1 
ATOM   47   C  CB   A MET   A 1 6   ? 2.043   7.743   -17.057 0.6 14.455 ? 6   MET   A CB   1 
ATOM   48   C  CB   B MET   A 1 6   ? 1.996   7.631   -16.83  0.4 14.476 ? 6   MET   A CB   1 
ATOM   49   C  CG   A MET   A 1 6   ? 1.62    8.722   -15.996 0.6 15.656 ? 6   MET   A CG   1 
ATOM   50   C  CG   B MET   A 1 6   ? 1.506   8.175   -15.526 0.4 15.705 ? 6   MET   A CG   1 
ATOM   51   S  SD   A MET   A 1 6   ? 3.06    9.617   -15.389 0.6 20.646 ? 6   MET   A SD   1 
ATOM   52   S  SD   B MET   A 1 6   ? 2.715   9.171   -14.66  0.4 17.955 ? 6   MET   A SD   1 
ATOM   53   C  CE   A MET   A 1 6   ? 3.226   10.977  -16.545 0.6 20.106 ? 6   MET   A CE   1 
ATOM   54   C  CE   B MET   A 1 6   ? 4.334   8.568   -15.146 0.4 16.45  ? 6   MET   A CE   1 
ATOM   55   N  N    . ALA   A 1 7   ? -1.349  6.883   -16.998 1   11.315 ? 7   ALA   A N    1 
ATOM   56   C  CA   . ALA   A 1 7   ? -2.667  7.452   -17.209 1   11.092 ? 7   ALA   A CA   1 
ATOM   57   C  C    . ALA   A 1 7   ? -2.825  8.731   -16.401 1   10.78  ? 7   ALA   A C    1 
ATOM   58   O  O    . ALA   A 1 7   ? -2.044  9.035   -15.512 1   10.934 ? 7   ALA   A O    1 
ATOM   59   C  CB   . ALA   A 1 7   ? -3.741  6.452   -16.837 1   11.359 ? 7   ALA   A CB   1 
ATOM   60   N  N    . PHE   A 1 8   ? -3.841  9.509   -16.732 1   10.515 ? 8   PHE   A N    1 
ATOM   61   C  CA   . PHE   A 1 8   ? -4.248  10.606  -15.876 1   10.922 ? 8   PHE   A CA   1 
ATOM   62   C  C    . PHE   A 1 8   ? -4.986  10.058  -14.666 1   11.192 ? 8   PHE   A C    1 
ATOM   63   O  O    . PHE   A 1 8   ? -5.702  9.069   -14.763 1   11.633 ? 8   PHE   A O    1 
ATOM   64   C  CB   . PHE   A 1 8   ? -5.13   11.6    -16.631 1   11.22  ? 8   PHE   A CB   1 
ATOM   65   C  CG   . PHE   A 1 8   ? -4.284  12.454  -17.56  1   11.807 ? 8   PHE   A CG   1 
ATOM   66   C  CD1  . PHE   A 1 8   ? -3.571  13.539  -17.064 1   12.726 ? 8   PHE   A CD1  1 
ATOM   67   C  CD2  . PHE   A 1 8   ? -4.16   12.127  -18.907 1   12.42  ? 8   PHE   A CD2  1 
ATOM   68   C  CE1  . PHE   A 1 8   ? -2.756  14.281  -17.89  1   13.051 ? 8   PHE   A CE1  1 
ATOM   69   C  CE2  . PHE   A 1 8   ? -3.361  12.893  -19.739 1   12.381 ? 8   PHE   A CE2  1 
ATOM   70   C  CZ   . PHE   A 1 8   ? -2.669  13.967  -19.229 1   13.056 ? 8   PHE   A CZ   1 
ATOM   71   N  N    . PRO   A 1 9   ? -4.869  10.732  -13.5   1   11.846 ? 9   PRO   A N    1 
ATOM   72   C  CA   . PRO   A 1 9   ? -5.682  10.379  -12.339 1   11.682 ? 9   PRO   A CA   1 
ATOM   73   C  C    . PRO   A 1 9   ? -7.15   10.424  -12.751 1   11.325 ? 9   PRO   A C    1 
ATOM   74   O  O    . PRO   A 1 9   ? -7.565  11.376  -13.409 1   12.149 ? 9   PRO   A O    1 
ATOM   75   C  CB   . PRO   A 1 9   ? -5.321  11.469  -11.316 1   12.609 ? 9   PRO   A CB   1 
ATOM   76   C  CG   . PRO   A 1 9   ? -3.967  11.99   -11.779 1   12.927 ? 9   PRO   A CG   1 
ATOM   77   C  CD   . PRO   A 1 9   ? -4.072  11.94   -13.291 1   12.44  ? 9   PRO   A CD   1 
ATOM   78   N  N    . SER   A 1 10  ? -7.928  9.416   -12.34  1   10.821 ? 10  SER   A N    1 
ATOM   79   C  CA   . SER   A 1 10  ? -9.259  9.195   -12.896 1   10.792 ? 10  SER   A CA   1 
ATOM   80   C  C    . SER   A 1 10  ? -10.393 9.812   -12.079 1   10.63  ? 10  SER   A C    1 
ATOM   81   O  O    . SER   A 1 10  ? -11.541 9.753   -12.518 1   10.789 ? 10  SER   A O    1 
ATOM   82   C  CB   . SER   A 1 10  ? -9.499  7.736   -13.1   1   11.457 ? 10  SER   A CB   1 
ATOM   83   O  OG   . SER   A 1 10  ? -9.35   7.008   -11.89  1   12.485 ? 10  SER   A OG   1 
ATOM   84   N  N    . GLY   A 1 11  ? -10.104 10.405  -10.916 1   10.895 ? 11  GLY   A N    1 
ATOM   85   C  CA   . GLY   A 1 11  ? -11.16  10.826  -10.007 1   10.991 ? 11  GLY   A CA   1 
ATOM   86   C  C    . GLY   A 1 11  ? -12.175 11.779  -10.63  1   11.326 ? 11  GLY   A C    1 
ATOM   87   O  O    . GLY   A 1 11  ? -13.372 11.656  -10.374 1   11.983 ? 11  GLY   A O    1 
ATOM   88   N  N    . LYS   A 1 12  ? -11.708 12.749  -11.422 1   10.894 ? 12  LYS   A N    1 
ATOM   89   C  CA   . LYS   A 1 12  ? -12.624 13.712  -12.014 1   11.71  ? 12  LYS   A CA   1 
ATOM   90   C  C    . LYS   A 1 12  ? -13.635 13.027  -12.927 1   11.199 ? 12  LYS   A C    1 
ATOM   91   O  O    . LYS   A 1 12  ? -14.747 13.516  -13.068 1   12.272 ? 12  LYS   A O    1 
ATOM   92   C  CB   . LYS   A 1 12  ? -11.862 14.81   -12.752 1   12.568 ? 12  LYS   A CB   1 
ATOM   93   C  CG   . LYS   A 1 12  ? -11.102 15.777  -11.863 1   14.535 ? 12  LYS   A CG   1 
ATOM   94   C  CD   . LYS   A 1 12  ? -10.295 16.794  -12.664 1   17.365 ? 12  LYS   A CD   1 
ATOM   95   C  CE   . LYS   A 1 12  ? -9.701  17.868  -11.826 1   20.447 ? 12  LYS   A CE   1 
ATOM   96   N  NZ   . LYS   A 1 12  ? -8.782  17.316  -10.829 1   23.131 ? 12  LYS   A NZ   1 
ATOM   97   N  N    . VAL   A 1 13  ? -13.251 11.91   -13.551 1   10.267 ? 13  VAL   A N    1 
ATOM   98   C  CA   . VAL   A 1 13  ? -14.158 11.172  -14.42  1   10.344 ? 13  VAL   A CA   1 
ATOM   99   C  C    . VAL   A 1 13  ? -15.021 10.202  -13.61  1   10.293 ? 13  VAL   A C    1 
ATOM   100  O  O    . VAL   A 1 13  ? -16.2   10.009  -13.918 1   10.249 ? 13  VAL   A O    1 
ATOM   101  C  CB   . VAL   A 1 13  ? -13.379 10.474  -15.545 1   10.973 ? 13  VAL   A CB   1 
ATOM   102  C  CG1  . VAL   A 1 13  ? -14.293 9.657   -16.443 1   11.079 ? 13  VAL   A CG1  1 
ATOM   103  C  CG2  . VAL   A 1 13  ? -12.603 11.496  -16.36  1   11.815 ? 13  VAL   A CG2  1 
ATOM   104  N  N    . GLU   A 1 14  ? -14.442 9.577   -12.578 1   10.539 ? 14  GLU   A N    1 
ATOM   105  C  CA   . GLU   A 1 14  ? -15.199 8.661   -11.731 1   10.935 ? 14  GLU   A CA   1 
ATOM   106  C  C    . GLU   A 1 14  ? -16.486 9.314   -11.219 1   11.476 ? 14  GLU   A C    1 
ATOM   107  O  O    . GLU   A 1 14  ? -17.546 8.672   -11.185 1   12.825 ? 14  GLU   A O    1 
ATOM   108  C  CB   . GLU   A 1 14  ? -14.372 8.21    -10.526 1   11.357 ? 14  GLU   A CB   1 
ATOM   109  C  CG   . GLU   A 1 14  ? -13.218 7.281   -10.874 1   11.999 ? 14  GLU   A CG   1 
ATOM   110  C  CD   . GLU   A 1 14  ? -12.287 7.079   -9.695  1   13.076 ? 14  GLU   A CD   1 
ATOM   111  O  OE1  . GLU   A 1 14  ? -11.081 7.277   -9.897  1   12.582 ? 14  GLU   A OE1  1 
ATOM   112  O  OE2  . GLU   A 1 14  ? -12.752 6.751   -8.579  1   15.955 ? 14  GLU   A OE2  1 
ATOM   113  N  N    . GLY   A 1 15  ? -16.397 10.6    -10.87  1   11.521 ? 15  GLY   A N    1 
ATOM   114  C  CA   . GLY   A 1 15  ? -17.524 11.319  -10.3   1   12.507 ? 15  GLY   A CA   1 
ATOM   115  C  C    . GLY   A 1 15  ? -18.616 11.632  -11.316 1   12.5   ? 15  GLY   A C    1 
ATOM   116  O  O    . GLY   A 1 15  ? -19.656 12.165  -10.928 1   13.699 ? 15  GLY   A O    1 
ATOM   117  N  N    . CYS   A 1 16  ? -18.382 11.274  -12.59  1   11.818 ? 16  CYS   A N    1 
ATOM   118  C  CA   . CYS   A 1 16  ? -19.34  11.522  -13.654 1   11.617 ? 16  CYS   A CA   1 
ATOM   119  C  C    . CYS   A 1 16  ? -19.983 10.234  -14.162 1   10.551 ? 16  CYS   A C    1 
ATOM   120  O  O    . CYS   A 1 16  ? -20.872 10.295  -15.004 1   11.788 ? 16  CYS   A O    1 
ATOM   121  C  CB   . CYS   A 1 16  ? -18.664 12.216  -14.828 1   12.626 ? 16  CYS   A CB   1 
ATOM   122  S  SG   . CYS   A 1 16  ? -17.96  13.822  -14.406 1   15.508 ? 16  CYS   A SG   1 
ATOM   123  N  N    . MET   A 1 17  ? -19.562 9.059   -13.692 1   10.05  ? 17  MET   A N    1 
ATOM   124  C  CA   . MET   A 1 17  ? -20.079 7.825   -14.252 1   10.65  ? 17  MET   A CA   1 
ATOM   125  C  C    . MET   A 1 17  ? -21.395 7.435   -13.586 1   11.01  ? 17  MET   A C    1 
ATOM   126  O  O    . MET   A 1 17  ? -21.517 7.44    -12.357 1   12.149 ? 17  MET   A O    1 
ATOM   127  C  CB   . MET   A 1 17  ? -19.075 6.679   -14.125 1   11.489 ? 17  MET   A CB   1 
ATOM   128  C  CG   . MET   A 1 17  ? -17.748 6.962   -14.809 1   12.262 ? 17  MET   A CG   1 
ATOM   129  S  SD   . MET   A 1 17  ? -17.86  7.474   -16.544 1   13.219 ? 17  MET   A SD   1 
ATOM   130  C  CE   . MET   A 1 17  ? -18.795 6.124   -17.273 1   12.951 ? 17  MET   A CE   1 
ATOM   131  N  N    . VAL   A 1 18  ? -22.358 7.042   -14.428 1   10.49  ? 18  VAL   A N    1 
ATOM   132  C  CA   . VAL   A 1 18  ? -23.677 6.604   -14.004 1   11.09  ? 18  VAL   A CA   1 
ATOM   133  C  C    . VAL   A 1 18  ? -24.065 5.358   -14.788 1   11.142 ? 18  VAL   A C    1 
ATOM   134  O  O    . VAL   A 1 18  ? -23.418 4.998   -15.778 1   11.138 ? 18  VAL   A O    1 
ATOM   135  C  CB   . VAL   A 1 18  ? -24.733 7.711   -14.182 1   11.265 ? 18  VAL   A CB   1 
ATOM   136  C  CG1  . VAL   A 1 18  ? -24.424 8.942   -13.344 1   11.623 ? 18  VAL   A CG1  1 
ATOM   137  C  CG2  . VAL   A 1 18  ? -24.941 8.103   -15.642 1   11.811 ? 18  VAL   A CG2  1 
ATOM   138  N  N    . GLN   A 1 19  ? -25.136 4.715   -14.322 1   12.181 ? 19  GLN   A N    1 
ATOM   139  C  CA   . GLN   A 1 19  ? -25.72  3.593   -15.018 1   13.331 ? 19  GLN   A CA   1 
ATOM   140  C  C    . GLN   A 1 19  ? -26.983 4.065   -15.736 1   12.874 ? 19  GLN   A C    1 
ATOM   141  O  O    . GLN   A 1 19  ? -27.809 4.752   -15.148 1   12.757 ? 19  GLN   A O    1 
ATOM   142  C  CB   . GLN   A 1 19  ? -26.063 2.532   -13.971 1   16.074 ? 19  GLN   A CB   1 
ATOM   143  C  CG   . GLN   A 1 19  ? -26.646 1.267   -14.572 1   18.99  ? 19  GLN   A CG   1 
ATOM   144  C  CD   . GLN   A 1 19  ? -27.014 0.255   -13.519 1   21.795 ? 19  GLN   A CD   1 
ATOM   145  O  OE1  . GLN   A 1 19  ? -26.275 -0.696  -13.252 1   25.13  ? 19  GLN   A OE1  1 
ATOM   146  N  NE2  . GLN   A 1 19  ? -28.173 0.468   -12.909 1   23.406 ? 19  GLN   A NE2  1 
ATOM   147  N  N    . VAL   A 1 20  ? -27.135 3.657   -17.002 1   11.626 ? 20  VAL   A N    1 
ATOM   148  C  CA   . VAL   A 1 20  ? -28.315 3.961   -17.798 1   12.129 ? 20  VAL   A CA   1 
ATOM   149  C  C    . VAL   A 1 20  ? -28.982 2.647   -18.195 1   12.232 ? 20  VAL   A C    1 
ATOM   150  O  O    . VAL   A 1 20  ? -28.326 1.759   -18.74  1   12.951 ? 20  VAL   A O    1 
ATOM   151  C  CB   . VAL   A 1 20  ? -27.975 4.781   -19.059 1   12.759 ? 20  VAL   A CB   1 
ATOM   152  C  CG1  . VAL   A 1 20  ? -29.227 5.101   -19.865 1   13.249 ? 20  VAL   A CG1  1 
ATOM   153  C  CG2  . VAL   A 1 20  ? -27.207 6.057   -18.74  1   13.038 ? 20  VAL   A CG2  1 
ATOM   154  N  N    . THR   A 1 21  ? -30.299 2.555   -17.945 1   13.288 ? 21  THR   A N    1 
ATOM   155  C  CA   . THR   A 1 21  ? -31.075 1.386   -18.314 1   14.6   ? 21  THR   A CA   1 
ATOM   156  C  C    . THR   A 1 21  ? -32.238 1.802   -19.214 1   14.834 ? 21  THR   A C    1 
ATOM   157  O  O    . THR   A 1 21  ? -32.94  2.762   -18.939 1   15.551 ? 21  THR   A O    1 
ATOM   158  C  CB   . THR   A 1 21  ? -31.61  0.677   -17.068 1   16.152 ? 21  THR   A CB   1 
ATOM   159  O  OG1  . THR   A 1 21  ? -30.509 0.287   -16.25  1   18.214 ? 21  THR   A OG1  1 
ATOM   160  C  CG2  . THR   A 1 21  ? -32.391 -0.574  -17.413 1   17.1   ? 21  THR   A CG2  1 
ATOM   161  N  N    . CYS   A 1 22  ? -32.434 1.045   -20.292 1   14.772 ? 22  CYS   A N    1 
ATOM   162  C  CA   . CYS   A 1 22  ? -33.598 1.162   -21.151 1   15.902 ? 22  CYS   A CA   1 
ATOM   163  C  C    . CYS   A 1 22  ? -34.078 -0.257  -21.429 1   17.084 ? 22  CYS   A C    1 
ATOM   164  O  O    . CYS   A 1 22  ? -33.343 -1.06   -21.989 1   17.272 ? 22  CYS   A O    1 
ATOM   165  C  CB   . CYS   A 1 22  ? -33.24  1.913   -22.43  1   16.595 ? 22  CYS   A CB   1 
ATOM   166  S  SG   . CYS   A 1 22  ? -34.664 2.247   -23.485 1   19.714 ? 22  CYS   A SG   1 
ATOM   167  N  N    . GLY   A 1 23  ? -35.276 -0.596  -20.951 1   19.076 ? 23  GLY   A N    1 
ATOM   168  C  CA   . GLY   A 1 23  ? -35.756 -1.963  -21.07  1   20.826 ? 23  GLY   A CA   1 
ATOM   169  C  C    . GLY   A 1 23  ? -34.824 -2.923  -20.331 1   20.749 ? 23  GLY   A C    1 
ATOM   170  O  O    . GLY   A 1 23  ? -34.503 -2.704  -19.17  1   21.512 ? 23  GLY   A O    1 
ATOM   171  N  N    . THR   A 1 24  ? -34.351 -3.956  -21.033 1   20.91  ? 24  THR   A N    1 
ATOM   172  C  CA   . THR   A 1 24  ? -33.487 -4.976  -20.454 1   22.841 ? 24  THR   A CA   1 
ATOM   173  C  C    . THR   A 1 24  ? -32.011 -4.602  -20.605 1   21.418 ? 24  THR   A C    1 
ATOM   174  O  O    . THR   A 1 24  ? -31.161 -5.349  -20.124 1   23.373 ? 24  THR   A O    1 
ATOM   175  C  CB   . THR   A 1 24  ? -33.761 -6.346  -21.083 1   24.418 ? 24  THR   A CB   1 
ATOM   176  O  OG1  . THR   A 1 24  ? -33.564 -6.21   -22.487 1   27.764 ? 24  THR   A OG1  1 
ATOM   177  C  CG2  . THR   A 1 24  ? -35.163 -6.855  -20.799 1   25.983 ? 24  THR   A CG2  1 
ATOM   178  N  N    . THR   A 1 25  ? -31.699 -3.465  -21.245 1   19.601 ? 25  THR   A N    1 
ATOM   179  C  CA   . THR   A 1 25  ? -30.312 -3.095  -21.52  1   19.794 ? 25  THR   A CA   1 
ATOM   180  C  C    . THR   A 1 25  ? -29.816 -2.078  -20.498 1   18.052 ? 25  THR   A C    1 
ATOM   181  O  O    . THR   A 1 25  ? -30.414 -1.02   -20.332 1   18.165 ? 25  THR   A O    1 
ATOM   182  C  CB   . THR   A 1 25  ? -30.164 -2.495  -22.914 1   21.609 ? 25  THR   A CB   1 
ATOM   183  O  OG1  . THR   A 1 25  ? -30.614 -3.452  -23.865 1   23.993 ? 25  THR   A OG1  1 
ATOM   184  C  CG2  . THR   A 1 25  ? -28.728 -2.09   -23.193 1   22.941 ? 25  THR   A CG2  1 
ATOM   185  N  N    . THR   A 1 26  ? -28.661 -2.381  -19.893 1   18.767 ? 26  THR   A N    1 
ATOM   186  C  CA   . THR   A 1 26  ? -27.989 -1.477  -18.974 1   17.917 ? 26  THR   A CA   1 
ATOM   187  C  C    . THR   A 1 26  ? -26.567 -1.248  -19.475 1   15.496 ? 26  THR   A C    1 
ATOM   188  O  O    . THR   A 1 26  ? -25.886 -2.204  -19.845 1   17.417 ? 26  THR   A O    1 
ATOM   189  C  CB   . THR   A 1 26  ? -27.968 -2.087  -17.575 1   20.241 ? 26  THR   A CB   1 
ATOM   190  O  OG1  . THR   A 1 26  ? -29.315 -2.171  -17.119 1   23.101 ? 26  THR   A OG1  1 
ATOM   191  C  CG2  . THR   A 1 26  ? -27.157 -1.25   -16.608 1   20.072 ? 26  THR   A CG2  1 
ATOM   192  N  N    . LEU   A 1 27  ? -26.123 0.014   -19.479 1   13.042 ? 27  LEU   A N    1 
ATOM   193  C  CA   . LEU   A 1 27  ? -24.743 0.333   -19.822 1   12.193 ? 27  LEU   A CA   1 
ATOM   194  C  C    . LEU   A 1 27  ? -24.35  1.595   -19.048 1   11.391 ? 27  LEU   A C    1 
ATOM   195  O  O    . LEU   A 1 27  ? -25.095 2.045   -18.176 1   12.045 ? 27  LEU   A O    1 
ATOM   196  C  CB   . LEU   A 1 27  ? -24.485 0.408   -21.334 1   12.175 ? 27  LEU   A CB   1 
ATOM   197  C  CG   . LEU   A 1 27  ? -25.508 1.175   -22.177 1   11.849 ? 27  LEU   A CG   1 
ATOM   198  C  CD1  . LEU   A 1 27  ? -25.62  2.639   -21.801 1   12.353 ? 27  LEU   A CD1  1 
ATOM   199  C  CD2  . LEU   A 1 27  ? -25.131 1.037   -23.641 1   12.246 ? 27  LEU   A CD2  1 
ATOM   200  N  N    . ASN   A 1 28  ? -23.168 2.139   -19.322 1   10.588 ? 28  ASN   A N    1 
ATOM   201  C  CA   . ASN   A 1 28  ? -22.665 3.308   -18.623 1   10.155 ? 28  ASN   A CA   1 
ATOM   202  C  C    . ASN   A 1 28  ? -23.015 4.604   -19.349 1   10.299 ? 28  ASN   A C    1 
ATOM   203  O  O    . ASN   A 1 28  ? -23.075 4.643   -20.578 1   10.775 ? 28  ASN   A O    1 
ATOM   204  C  CB   . ASN   A 1 28  ? -21.144 3.258   -18.485 1   10.286 ? 28  ASN   A CB   1 
ATOM   205  C  CG   . ASN   A 1 28  ? -20.677 1.956   -17.886 1   10.904 ? 28  ASN   A CG   1 
ATOM   206  O  OD1  . ASN   A 1 28  ? -20.76  1.771   -16.663 1   12.411 ? 28  ASN   A OD1  1 
ATOM   207  N  ND2  . ASN   A 1 28  ? -20.192 1.044   -18.708 1   11.737 ? 28  ASN   A ND2  1 
ATOM   208  N  N    . GLY   A 1 29  ? -23.238 5.666   -18.57  1   10.286 ? 29  GLY   A N    1 
ATOM   209  C  CA   . GLY   A 1 29  ? -23.377 7.015   -19.083 1   10.501 ? 29  GLY   A CA   1 
ATOM   210  C  C    . GLY   A 1 29  ? -22.425 7.974   -18.377 1   10.178 ? 29  GLY   A C    1 
ATOM   211  O  O    . GLY   A 1 29  ? -21.887 7.674   -17.302 1   10.233 ? 29  GLY   A O    1 
ATOM   212  N  N    . LEU   A 1 30  ? -22.261 9.144   -18.992 1   10.291 ? 30  LEU   A N    1 
ATOM   213  C  CA   . LEU   A 1 30  ? -21.394 10.207  -18.502 1   10.132 ? 30  LEU   A CA   1 
ATOM   214  C  C    . LEU   A 1 30  ? -22.274 11.399  -18.148 1   10.313 ? 30  LEU   A C    1 
ATOM   215  O  O    . LEU   A 1 30  ? -22.97  11.945  -19.012 1   10.657 ? 30  LEU   A O    1 
ATOM   216  C  CB   . LEU   A 1 30  ? -20.393 10.56   -19.604 1   10.286 ? 30  LEU   A CB   1 
ATOM   217  C  CG   . LEU   A 1 30  ? -19.343 11.608  -19.235 1   10.916 ? 30  LEU   A CG   1 
ATOM   218  C  CD1  . LEU   A 1 30  ? -18.356 11.094  -18.202 1   11.086 ? 30  LEU   A CD1  1 
ATOM   219  C  CD2  . LEU   A 1 30  ? -18.641 12.1    -20.488 1   11.242 ? 30  LEU   A CD2  1 
ATOM   220  N  N    . TRP   A 1 31  ? -22.284 11.751  -16.849 1   9.949  ? 31  TRP   A N    1 
ATOM   221  C  CA   . TRP   A 1 31  ? -23.143 12.778  -16.29  1   10.517 ? 31  TRP   A CA   1 
ATOM   222  C  C    . TRP   A 1 31  ? -22.347 14.06   -16.076 1   10.631 ? 31  TRP   A C    1 
ATOM   223  O  O    . TRP   A 1 31  ? -21.496 14.121  -15.19  1   10.924 ? 31  TRP   A O    1 
ATOM   224  C  CB   . TRP   A 1 31  ? -23.732 12.25   -14.979 1   10.676 ? 31  TRP   A CB   1 
ATOM   225  C  CG   . TRP   A 1 31  ? -24.701 13.164  -14.276 1   11.238 ? 31  TRP   A CG   1 
ATOM   226  C  CD1  . TRP   A 1 31  ? -25.466 14.166  -14.799 1   11.655 ? 31  TRP   A CD1  1 
ATOM   227  C  CD2  . TRP   A 1 31  ? -24.986 13.133  -12.861 1   12.226 ? 31  TRP   A CD2  1 
ATOM   228  N  NE1  . TRP   A 1 31  ? -26.233 14.736  -13.807 1   12.413 ? 31  TRP   A NE1  1 
ATOM   229  C  CE2  . TRP   A 1 31  ? -25.942 14.134  -12.61  1   13.022 ? 31  TRP   A CE2  1 
ATOM   230  C  CE3  . TRP   A 1 31  ? -24.508 12.367  -11.79  1   12.771 ? 31  TRP   A CE3  1 
ATOM   231  C  CZ2  . TRP   A 1 31  ? -26.432 14.386  -11.329 1   13.662 ? 31  TRP   A CZ2  1 
ATOM   232  C  CZ3  . TRP   A 1 31  ? -24.983 12.632  -10.52  1   13.688 ? 31  TRP   A CZ3  1 
ATOM   233  C  CH2  . TRP   A 1 31  ? -25.936 13.621  -10.303 1   13.927 ? 31  TRP   A CH2  1 
ATOM   234  N  N    . LEU   A 1 32  ? -22.623 15.065  -16.91  1   10.684 ? 32  LEU   A N    1 
ATOM   235  C  CA   . LEU   A 1 32  ? -21.961 16.361  -16.882 1   11.137 ? 32  LEU   A CA   1 
ATOM   236  C  C    . LEU   A 1 32  ? -23.031 17.44   -16.82  1   12.344 ? 32  LEU   A C    1 
ATOM   237  O  O    . LEU   A 1 32  ? -23.921 17.467  -17.663 1   12.913 ? 32  LEU   A O    1 
ATOM   238  C  CB   . LEU   A 1 32  ? -21.084 16.55   -18.121 1   11.404 ? 32  LEU   A CB   1 
ATOM   239  C  CG   . LEU   A 1 32  ? -19.986 15.508  -18.331 1   12.503 ? 32  LEU   A CG   1 
ATOM   240  C  CD1  . LEU   A 1 32  ? -19.391 15.6    -19.733 1   13.057 ? 32  LEU   A CD1  1 
ATOM   241  C  CD2  . LEU   A 1 32  ? -18.894 15.692  -17.298 1   13.29  ? 32  LEU   A CD2  1 
ATOM   242  N  N    . ASP   A 1 33  ? -22.965 18.322  -15.827 1   13.156 ? 33  ASP   A N    1 
ATOM   243  C  CA   . ASP   A 1 33  ? -24.036 19.286  -15.629 1   14.513 ? 33  ASP   A CA   1 
ATOM   244  C  C    . ASP   A 1 33  ? -25.339 18.486  -15.529 1   13.628 ? 33  ASP   A C    1 
ATOM   245  O  O    . ASP   A 1 33  ? -25.379 17.484  -14.819 1   13.309 ? 33  ASP   A O    1 
ATOM   246  C  CB   . ASP   A 1 33  ? -23.937 20.407  -16.655 1   16.548 ? 33  ASP   A CB   1 
ATOM   247  C  CG   . ASP   A 1 33  ? -22.611 21.165  -16.654 1   19.568 ? 33  ASP   A CG   1 
ATOM   248  O  OD1  . ASP   A 1 33  ? -22.153 21.543  -15.553 1   23.97  ? 33  ASP   A OD1  1 
ATOM   249  O  OD2  . ASP   A 1 33  ? -22.024 21.33   -17.747 1   23.936 ? 33  ASP   A OD2  1 
ATOM   250  N  N    . ASP   A 1 34  ? -26.381 18.878  -16.268 1   14.379 ? 34  ASP   A N    1 
ATOM   251  C  CA   . ASP   A 1 34  ? -27.668 18.201  -16.19  1   14.498 ? 34  ASP   A CA   1 
ATOM   252  C  C    . ASP   A 1 34  ? -27.933 17.31   -17.407 1   13.748 ? 34  ASP   A C    1 
ATOM   253  O  O    . ASP   A 1 34  ? -29.096 17.078  -17.738 1   14.419 ? 34  ASP   A O    1 
ATOM   254  C  CB   . ASP   A 1 34  ? -28.803 19.202  -16.022 1   16.962 ? 34  ASP   A CB   1 
ATOM   255  C  CG   . ASP   A 1 34  ? -28.924 20.256  -17.111 1   19.598 ? 34  ASP   A CG   1 
ATOM   256  O  OD1  . ASP   A 1 34  ? -28.02  20.346  -17.967 1   19.52  ? 34  ASP   A OD1  1 
ATOM   257  O  OD2  . ASP   A 1 34  ? -29.927 20.99   -17.091 1   24.313 ? 34  ASP   A OD2  1 
ATOM   258  N  N    . VAL   A 1 35  ? -26.874 16.79   -18.037 1   12.809 ? 35  VAL   A N    1 
ATOM   259  C  CA   . VAL   A 1 35  ? -27.001 15.91   -19.19  1   12.413 ? 35  VAL   A CA   1 
ATOM   260  C  C    . VAL   A 1 35  ? -26.229 14.616  -18.945 1   11.237 ? 35  VAL   A C    1 
ATOM   261  O  O    . VAL   A 1 35  ? -25.107 14.644  -18.444 1   11.888 ? 35  VAL   A O    1 
ATOM   262  C  CB   . VAL   A 1 35  ? -26.535 16.581  -20.495 1   13.693 ? 35  VAL   A CB   1 
ATOM   263  C  CG1  . VAL   A 1 35  ? -26.661 15.626  -21.675 1   14.3   ? 35  VAL   A CG1  1 
ATOM   264  C  CG2  . VAL   A 1 35  ? -27.296 17.883  -20.74  1   15.231 ? 35  VAL   A CG2  1 
ATOM   265  N  N    . VAL   A 1 36  ? -26.84  13.49   -19.316 1   10.798 ? 36  VAL   A N    1 
ATOM   266  C  CA   . VAL   A 1 36  ? -26.193 12.191  -19.342 1   10.96  ? 36  VAL   A CA   1 
ATOM   267  C  C    . VAL   A 1 36  ? -26.01  11.756  -20.794 1   10.895 ? 36  VAL   A C    1 
ATOM   268  O  O    . VAL   A 1 36  ? -26.972 11.71   -21.557 1   11.39  ? 36  VAL   A O    1 
ATOM   269  C  CB   . VAL   A 1 36  ? -26.97  11.141  -18.536 1   11.625 ? 36  VAL   A CB   1 
ATOM   270  C  CG1  . VAL   A 1 36  ? -26.373 9.748   -18.669 1   11.845 ? 36  VAL   A CG1  1 
ATOM   271  C  CG2  . VAL   A 1 36  ? -27.074 11.558  -17.066 1   11.84  ? 36  VAL   A CG2  1 
ATOM   272  N  N    . TYR   A 1 37  ? -24.765 11.425  -21.146 1   10.554 ? 37  TYR   A N    1 
ATOM   273  C  CA   . TYR   A 1 37  ? -24.389 11.002  -22.492 1   10.525 ? 37  TYR   A CA   1 
ATOM   274  C  C    . TYR   A 1 37  ? -24.15  9.498   -22.479 1   10.386 ? 37  TYR   A C    1 
ATOM   275  O  O    . TYR   A 1 37  ? -23.44  8.989   -21.614 1   10.656 ? 37  TYR   A O    1 
ATOM   276  C  CB   . TYR   A 1 37  ? -23.093 11.701  -22.933 1   10.817 ? 37  TYR   A CB   1 
ATOM   277  C  CG   . TYR   A 1 37  ? -23.137 13.22   -22.896 1   11.397 ? 37  TYR   A CG   1 
ATOM   278  C  CD1  . TYR   A 1 37  ? -22.996 13.928  -21.707 1   11.93  ? 37  TYR   A CD1  1 
ATOM   279  C  CD2  . TYR   A 1 37  ? -23.364 13.956  -24.054 1   12.19  ? 37  TYR   A CD2  1 
ATOM   280  C  CE1  . TYR   A 1 37  ? -23.068 15.309  -21.673 1   12.525 ? 37  TYR   A CE1  1 
ATOM   281  C  CE2  . TYR   A 1 37  ? -23.438 15.336  -24.026 1   12.458 ? 37  TYR   A CE2  1 
ATOM   282  C  CZ   . TYR   A 1 37  ? -23.319 16.018  -22.831 1   13.038 ? 37  TYR   A CZ   1 
ATOM   283  O  OH   . TYR   A 1 37  ? -23.412 17.38   -22.811 1   15.661 ? 37  TYR   A OH   1 
ATOM   284  N  N    . CYS   A 1 38  ? -24.674 8.78    -23.473 1   10.594 ? 38  CYS   A N    1 
ATOM   285  C  CA   . CYS   A 1 38  ? -24.42  7.353   -23.544 1   10.753 ? 38  CYS   A CA   1 
ATOM   286  C  C    . CYS   A 1 38  ? -24.583 6.895   -24.986 1   10.639 ? 38  CYS   A C    1 
ATOM   287  O  O    . CYS   A 1 38  ? -25.096 7.645   -25.809 1   11.176 ? 38  CYS   A O    1 
ATOM   288  C  CB   . CYS   A 1 38  ? -25.314 6.561   -22.59  1   11.516 ? 38  CYS   A CB   1 
ATOM   289  S  SG   . CYS   A 1 38  ? -27.053 6.454   -23.085 1   13.218 ? 38  CYS   A SG   1 
ATOM   290  N  N    . PRO   A 1 39  ? -24.151 5.666   -25.327 1   10.356 ? 39  PRO   A N    1 
ATOM   291  C  CA   . PRO   A 1 39  ? -24.334 5.169   -26.688 1   10.374 ? 39  PRO   A CA   1 
ATOM   292  C  C    . PRO   A 1 39  ? -25.819 5.02    -26.992 1   10.536 ? 39  PRO   A C    1 
ATOM   293  O  O    . PRO   A 1 39  ? -26.586 4.518   -26.164 1   10.777 ? 39  PRO   A O    1 
ATOM   294  C  CB   . PRO   A 1 39  ? -23.626 3.826   -26.707 1   10.398 ? 39  PRO   A CB   1 
ATOM   295  C  CG   . PRO   A 1 39  ? -22.637 3.939   -25.579 1   10.681 ? 39  PRO   A CG   1 
ATOM   296  C  CD   . PRO   A 1 39  ? -23.344 4.749   -24.501 1   10.954 ? 39  PRO   A CD   1 
ATOM   297  N  N    . ARG   A 1 40  ? -26.217 5.414   -28.203 1   10.63  ? 40  ARG   A N    1 
ATOM   298  C  CA   . ARG   A 1 40  ? -27.625 5.332   -28.549 1   10.813 ? 40  ARG   A CA   1 
ATOM   299  C  C    . ARG   A 1 40  ? -28.093 3.883   -28.641 1   11.068 ? 40  ARG   A C    1 
ATOM   300  O  O    . ARG   A 1 40  ? -29.297 3.641   -28.551 1   11.457 ? 40  ARG   A O    1 
ATOM   301  C  CB   . ARG   A 1 40  ? -27.987 6.115   -29.812 1   11.226 ? 40  ARG   A CB   1 
ATOM   302  C  CG   . ARG   A 1 40  ? -27.364 5.575   -31.085 1   11.717 ? 40  ARG   A CG   1 
ATOM   303  C  CD   . ARG   A 1 40  ? -27.887 6.364   -32.271 1   12.136 ? 40  ARG   A CD   1 
ATOM   304  N  NE   . ARG   A 1 40  ? -27.21  5.922   -33.491 1   12.495 ? 40  ARG   A NE   1 
ATOM   305  C  CZ   . ARG   A 1 40  ? -27.614 6.204   -34.722 1   13.149 ? 40  ARG   A CZ   1 
ATOM   306  N  NH1  . ARG   A 1 40  ? -28.602 7.063   -34.914 1   13.368 ? 40  ARG   A NH1  1 
ATOM   307  N  NH2  . ARG   A 1 40  ? -26.987 5.647   -35.739 1   13.609 ? 40  ARG   A NH2  1 
ATOM   308  N  N    . HIS   A 1 41  ? -27.185 2.917   -28.82  1   10.944 ? 41  HIS   A N    1 
ATOM   309  C  CA   . HIS   A 1 41  ? -27.577 1.516   -28.891 1   11.755 ? 41  HIS   A CA   1 
ATOM   310  C  C    . HIS   A 1 41  ? -28.199 1.003   -27.591 1   12.182 ? 41  HIS   A C    1 
ATOM   311  O  O    . HIS   A 1 41  ? -28.742 -0.092  -27.574 1   12.942 ? 41  HIS   A O    1 
ATOM   312  C  CB   . HIS   A 1 41  ? -26.47  0.625   -29.462 1   12.239 ? 41  HIS   A CB   1 
ATOM   313  C  CG   . HIS   A 1 41  ? -25.294 0.336   -28.591 1   12.752 ? 41  HIS   A CG   1 
ATOM   314  N  ND1  . HIS   A 1 41  ? -25.363 -0.416  -27.441 1   13.907 ? 41  HIS   A ND1  1 
ATOM   315  C  CD2  . HIS   A 1 41  ? -23.998 0.642   -28.766 1   13.06  ? 41  HIS   A CD2  1 
ATOM   316  C  CE1  . HIS   A 1 41  ? -24.134 -0.551  -26.946 1   13.504 ? 41  HIS   A CE1  1 
ATOM   317  N  NE2  . HIS   A 1 41  ? -23.287 0.076   -27.745 1   13.281 ? 41  HIS   A NE2  1 
ATOM   318  N  N    . VAL   A 1 42  ? -28.183 1.803   -26.515 1   11.944 ? 42  VAL   A N    1 
ATOM   319  C  CA   . VAL   A 1 42  ? -28.927 1.435   -25.318 1   12.709 ? 42  VAL   A CA   1 
ATOM   320  C  C    . VAL   A 1 42  ? -30.411 1.177   -25.617 1   12.978 ? 42  VAL   A C    1 
ATOM   321  O  O    . VAL   A 1 42  ? -31.054 0.416   -24.902 1   13.912 ? 42  VAL   A O    1 
ATOM   322  C  CB   . VAL   A 1 42  ? -28.76  2.495   -24.217 1   12.742 ? 42  VAL   A CB   1 
ATOM   323  C  CG1  . VAL   A 1 42  ? -29.476 3.799   -24.534 1   13.157 ? 42  VAL   A CG1  1 
ATOM   324  C  CG2  . VAL   A 1 42  ? -29.194 1.957   -22.854 1   13.17  ? 42  VAL   A CG2  1 
ATOM   325  N  N    . ILE   A 1 43  ? -30.974 1.779   -26.68  1   12.536 ? 43  ILE   A N    1 
ATOM   326  C  CA   . ILE   A 1 43  ? -32.399 1.617   -26.978 1   13.379 ? 43  ILE   A CA   1 
ATOM   327  C  C    . ILE   A 1 43  ? -32.67  0.374   -27.838 1   14.748 ? 43  ILE   A C    1 
ATOM   328  O  O    . ILE   A 1 43  ? -33.813 0.119   -28.216 1   17.445 ? 43  ILE   A O    1 
ATOM   329  C  CB   . ILE   A 1 43  ? -33.006 2.889   -27.607 1   13.791 ? 43  ILE   A CB   1 
ATOM   330  C  CG1  . ILE   A 1 43  ? -32.551 3.125   -29.047 1   13.906 ? 43  ILE   A CG1  1 
ATOM   331  C  CG2  . ILE   A 1 43  ? -32.768 4.115   -26.716 1   14.636 ? 43  ILE   A CG2  1 
ATOM   332  C  CD1  . ILE   A 1 43  ? -33.201 4.326   -29.707 1   14.34  ? 43  ILE   A CD1  1 
ATOM   333  N  N    . CYS   A 1 44  ? -31.63  -0.375  -28.196 1   15.653 ? 44  CYS   A N    1 
ATOM   334  C  CA   . CYS   A 1 44  ? -31.776 -1.604  -28.959 1   17.464 ? 44  CYS   A CA   1 
ATOM   335  C  C    . CYS   A 1 44  ? -31.817 -2.853  -28.084 1   21.286 ? 44  CYS   A C    1 
ATOM   336  O  O    . CYS   A 1 44  ? -31.02  -3.011  -27.154 1   23.637 ? 44  CYS   A O    1 
ATOM   337  C  CB   . CYS   A 1 44  ? -30.583 -1.807  -29.874 1   17.45  ? 44  CYS   A CB   1 
ATOM   338  S  SG   . CYS   A 1 44  ? -30.427 -0.462  -31.062 1   18.979 ? 44  CYS   A SG   1 
ATOM   339  N  N    . THR   A 1 45  ? -32.708 -3.772  -28.473 1   24.513 ? 45  THR   A N    1 
ATOM   340  C  CA   . THR   A 1 45  ? -32.684 -5.157  -28.018 1   26.817 ? 45  THR   A CA   1 
ATOM   341  C  C    . THR   A 1 45  ? -31.795 -5.955  -28.972 1   24.411 ? 45  THR   A C    1 
ATOM   342  O  O    . THR   A 1 45  ? -31.413 -5.456  -30.023 1   22.955 ? 45  THR   A O    1 
ATOM   343  C  CB   . THR   A 1 45  ? -34.103 -5.737  -27.995 1   29.277 ? 45  THR   A CB   1 
ATOM   344  O  OG1  . THR   A 1 45  ? -34.527 -5.828  -29.353 1   32.433 ? 45  THR   A OG1  1 
ATOM   345  C  CG2  . THR   A 1 45  ? -35.097 -4.86   -27.255 1   31.595 ? 45  THR   A CG2  1 
ATOM   346  N  N    . SER   A 1 46  ? -31.529 -7.221  -28.635 1   24.086 ? 46  SER   A N    1 
ATOM   347  C  CA   . SER   A 1 46  ? -30.778 -8.105  -29.514 1   25.389 ? 46  SER   A CA   1 
ATOM   348  C  C    . SER   A 1 46  ? -31.457 -8.216  -30.882 1   26.033 ? 46  SER   A C    1 
ATOM   349  O  O    . SER   A 1 46  ? -30.781 -8.262  -31.903 1   26.618 ? 46  SER   A O    1 
ATOM   350  C  CB   . SER   A 1 46  ? -30.582 -9.462  -28.88  1   26.438 ? 46  SER   A CB   1 
ATOM   351  O  OG   . SER   A 1 46  ? -31.819 -10.084 -28.558 1   28.202 ? 46  SER   A OG   1 
ATOM   352  N  N    . GLU   A 1 47  ? -32.795 -8.237  -30.895 1   24.695 ? 47  GLU   A N    1 
ATOM   353  C  CA   . GLU   A 1 47  ? -33.557 -8.332  -32.13  1   26.039 ? 47  GLU   A CA   1 
ATOM   354  C  C    . GLU   A 1 47  ? -33.419 -7.065  -32.982 1   26.56  ? 47  GLU   A C    1 
ATOM   355  O  O    . GLU   A 1 47  ? -33.661 -7.129  -34.178 1   31.168 ? 47  GLU   A O    1 
ATOM   356  C  CB   . GLU   A 1 47  ? -35.028 -8.638  -31.832 1   26.83  ? 47  GLU   A CB   1 
ATOM   357  N  N    . ASP   A 1 48  ? -33.05  -5.919  -32.392 1   23.962 ? 48  ASP   A N    1 
ATOM   358  C  CA   . ASP   A 1 48  ? -32.953 -4.647  -33.098 1   22.922 ? 48  ASP   A CA   1 
ATOM   359  C  C    . ASP   A 1 48  ? -31.549 -4.407  -33.672 1   22.597 ? 48  ASP   A C    1 
ATOM   360  O  O    . ASP   A 1 48  ? -31.373 -3.511  -34.487 1   20.944 ? 48  ASP   A O    1 
ATOM   361  C  CB   . ASP   A 1 48  ? -33.302 -3.469  -32.186 1   23.103 ? 48  ASP   A CB   1 
ATOM   362  C  CG   . ASP   A 1 48  ? -34.692 -3.49   -31.55  1   24.98  ? 48  ASP   A CG   1 
ATOM   363  O  OD1  . ASP   A 1 48  ? -35.657 -3.906  -32.223 1   26.341 ? 48  ASP   A OD1  1 
ATOM   364  O  OD2  . ASP   A 1 48  ? -34.821 -3.051  -30.392 1   28.697 ? 48  ASP   A OD2  1 
ATOM   365  N  N    . MET   A 1 49  ? -30.537 -5.168  -33.235 1   22.915 ? 49  MET   A N    1 
ATOM   366  C  CA   . MET   A 1 49  ? -29.155 -4.703  -33.335 1   21.958 ? 49  MET   A CA   1 
ATOM   367  C  C    . MET   A 1 49  ? -28.573 -4.817  -34.749 1   21.671 ? 49  MET   A C    1 
ATOM   368  O  O    . MET   A 1 49  ? -27.598 -4.146  -35.075 1   19.588 ? 49  MET   A O    1 
ATOM   369  C  CB   . MET   A 1 49  ? -28.268 -5.434  -32.319 1   22.404 ? 49  MET   A CB   1 
ATOM   370  C  CG   . MET   A 1 49  ? -27.019 -4.674  -31.889 1   22.251 ? 49  MET   A CG   1 
ATOM   371  S  SD   . MET   A 1 49  ? -27.275 -3.08   -31.081 1   20.653 ? 49  MET   A SD   1 
ATOM   372  C  CE   . MET   A 1 49  ? -27.161 -1.889  -32.423 1   20.478 ? 49  MET   A CE   1 
ATOM   373  N  N    . LEU   A 1 50  ? -29.154 -5.645  -35.615 1   23.884 ? 50  LEU   A N    1 
ATOM   374  C  CA   . LEU   A 1 50  ? -28.583 -5.846  -36.941 1   24.148 ? 50  LEU   A CA   1 
ATOM   375  C  C    . LEU   A 1 50  ? -28.915 -4.689  -37.901 1   23.529 ? 50  LEU   A C    1 
ATOM   376  O  O    . LEU   A 1 50  ? -28.061 -4.219  -38.65  1   23.649 ? 50  LEU   A O    1 
ATOM   377  C  CB   . LEU   A 1 50  ? -29.057 -7.223  -37.402 1   25.061 ? 50  LEU   A CB   1 
ATOM   378  C  CG   . LEU   A 1 50  ? -28.583 -7.696  -38.772 1   25.264 ? 50  LEU   A CG   1 
ATOM   379  C  CD1  . LEU   A 1 50  ? -27.079 -7.679  -38.923 1   25.442 ? 50  LEU   A CD1  1 
ATOM   380  C  CD2  . LEU   A 1 50  ? -29.121 -9.102  -38.994 1   25.692 ? 50  LEU   A CD2  1 
ATOM   381  N  N    . ASN   A 1 51  ? -30.166 -4.21   -37.902 1   23.795 ? 51  ASN   A N    1 
ATOM   382  C  CA   . ASN   A 1 51  ? -30.57  -3.066  -38.716 1   23.236 ? 51  ASN   A CA   1 
ATOM   383  C  C    . ASN   A 1 51  ? -31.533 -2.242  -37.864 1   22.181 ? 51  ASN   A C    1 
ATOM   384  O  O    . ASN   A 1 51  ? -32.755 -2.269  -38.043 1   27.181 ? 51  ASN   A O    1 
ATOM   385  C  CB   . ASN   A 1 51  ? -31.21  -3.433  -40.063 1   25.566 ? 51  ASN   A CB   1 
ATOM   386  C  CG   . ASN   A 1 51  ? -30.221 -3.805  -41.157 1   27.611 ? 51  ASN   A CG   1 
ATOM   387  O  OD1  . ASN   A 1 51  ? -29.551 -2.944  -41.757 1   28.194 ? 51  ASN   A OD1  1 
ATOM   388  N  ND2  . ASN   A 1 51  ? -30.143 -5.087  -41.478 1   26.55  ? 51  ASN   A ND2  1 
ATOM   389  N  N    . PRO   A 1 52  ? -31.007 -1.507  -36.871 1   18.282 ? 52  PRO   A N    1 
ATOM   390  C  CA   . PRO   A 1 52  ? -31.829 -0.614  -36.065 1   17.436 ? 52  PRO   A CA   1 
ATOM   391  C  C    . PRO   A 1 52  ? -32.231 0.62    -36.866 1   16.462 ? 52  PRO   A C    1 
ATOM   392  O  O    . PRO   A 1 52  ? -31.408 1.235   -37.53  1   17.751 ? 52  PRO   A O    1 
ATOM   393  C  CB   . PRO   A 1 52  ? -30.895 -0.256  -34.9   1   18.029 ? 52  PRO   A CB   1 
ATOM   394  C  CG   . PRO   A 1 52  ? -29.509 -0.332  -35.504 1   17.869 ? 52  PRO   A CG   1 
ATOM   395  C  CD   . PRO   A 1 52  ? -29.594 -1.492  -36.474 1   18.044 ? 52  PRO   A CD   1 
ATOM   396  N  N    . ASN   A 1 53  ? -33.492 1.028   -36.716 1   15.176 ? 53  ASN   A N    1 
ATOM   397  C  CA   . ASN   A 1 53  ? -33.938 2.325   -37.172 1   14.703 ? 53  ASN   A CA   1 
ATOM   398  C  C    . ASN   A 1 53  ? -34.055 3.204   -35.934 1   13.284 ? 53  ASN   A C    1 
ATOM   399  O  O    . ASN   A 1 53  ? -35.058 3.145   -35.231 1   12.786 ? 53  ASN   A O    1 
ATOM   400  C  CB   . ASN   A 1 53  ? -35.257 2.197   -37.92  1   15.427 ? 53  ASN   A CB   1 
ATOM   401  C  CG   . ASN   A 1 53  ? -35.68  3.491   -38.558 1   17.129 ? 53  ASN   A CG   1 
ATOM   402  O  OD1  . ASN   A 1 53  ? -35.555 4.576   -37.967 1   17.109 ? 53  ASN   A OD1  1 
ATOM   403  N  ND2  . ASN   A 1 53  ? -36.166 3.378   -39.788 1   20.035 ? 53  ASN   A ND2  1 
ATOM   404  N  N    . TYR   A 1 54  ? -32.999 3.958   -35.621 1   13.101 ? 54  TYR   A N    1 
ATOM   405  C  CA   . TYR   A 1 54  ? -32.913 4.612   -34.325 1   12.641 ? 54  TYR   A CA   1 
ATOM   406  C  C    . TYR   A 1 54  ? -34.01  5.659   -34.132 1   12.828 ? 54  TYR   A C    1 
ATOM   407  O  O    . TYR   A 1 54  ? -34.551 5.781   -33.037 1   13.244 ? 54  TYR   A O    1 
ATOM   408  C  CB   . TYR   A 1 54  ? -31.525 5.21    -34.12  1   12.98  ? 54  TYR   A CB   1 
ATOM   409  C  CG   . TYR   A 1 54  ? -30.485 4.162   -33.776 1   12.324 ? 54  TYR   A CG   1 
ATOM   410  C  CD1  . TYR   A 1 54  ? -30.387 3.664   -32.484 1   12.664 ? 54  TYR   A CD1  1 
ATOM   411  C  CD2  . TYR   A 1 54  ? -29.569 3.712   -34.717 1   12.314 ? 54  TYR   A CD2  1 
ATOM   412  C  CE1  . TYR   A 1 54  ? -29.407 2.747   -32.136 1   13.049 ? 54  TYR   A CE1  1 
ATOM   413  C  CE2  . TYR   A 1 54  ? -28.606 2.781   -34.394 1   12.901 ? 54  TYR   A CE2  1 
ATOM   414  C  CZ   . TYR   A 1 54  ? -28.514 2.307   -33.097 1   13.299 ? 54  TYR   A CZ   1 
ATOM   415  O  OH   . TYR   A 1 54  ? -27.546 1.418   -32.735 1   14.68  ? 54  TYR   A OH   1 
ATOM   416  N  N    . GLU   A 1 55  ? -34.387 6.385   -35.189 1   12.848 ? 55  GLU   A N    1 
ATOM   417  C  CA   . GLU   A 1 55  ? -35.448 7.366   -35.062 1   13.404 ? 55  GLU   A CA   1 
ATOM   418  C  C    . GLU   A 1 55  ? -36.755 6.678   -34.675 1   12.974 ? 55  GLU   A C    1 
ATOM   419  O  O    . GLU   A 1 55  ? -37.496 7.162   -33.822 1   12.881 ? 55  GLU   A O    1 
ATOM   420  C  CB   . GLU   A 1 55  ? -35.598 8.118   -36.379 1   14.812 ? 55  GLU   A CB   1 
ATOM   421  C  CG   . GLU   A 1 55  ? -34.38  8.987   -36.668 1   17.833 ? 55  GLU   A CG   1 
ATOM   422  C  CD   . GLU   A 1 55  ? -33.148 8.325   -37.277 1   21.49  ? 55  GLU   A CD   1 
ATOM   423  O  OE1  . GLU   A 1 55  ? -33.076 7.098   -37.622 1   22.303 ? 55  GLU   A OE1  1 
ATOM   424  O  OE2  . GLU   A 1 55  ? -32.2   9.137   -37.399 1   26.777 ? 55  GLU   A OE2  1 
ATOM   425  N  N    . ASP   A 1 56  ? -37.036 5.545   -35.317 1   12.121 ? 56  ASP   A N    1 
ATOM   426  C  CA   . ASP   A 1 56  ? -38.268 4.815   -35.065 1   12.432 ? 56  ASP   A CA   1 
ATOM   427  C  C    . ASP   A 1 56  ? -38.256 4.186   -33.673 1   12.718 ? 56  ASP   A C    1 
ATOM   428  O  O    . ASP   A 1 56  ? -39.284 4.097   -33.021 1   13.735 ? 56  ASP   A O    1 
ATOM   429  C  CB   . ASP   A 1 56  ? -38.51  3.772   -36.142 1   13.129 ? 56  ASP   A CB   1 
ATOM   430  C  CG   . ASP   A 1 56  ? -39.9   3.168   -36.117 1   14.06  ? 56  ASP   A CG   1 
ATOM   431  O  OD1  . ASP   A 1 56  ? -40.819 3.852   -36.574 1   16.085 ? 56  ASP   A OD1  1 
ATOM   432  O  OD2  . ASP   A 1 56  ? -40.054 2.043   -35.627 1   16.841 ? 56  ASP   A OD2  1 
ATOM   433  N  N    . LEU   A 1 57  ? -37.106 3.681   -33.238 1   12.138 ? 57  LEU   A N    1 
ATOM   434  C  CA   . LEU   A 1 57  ? -36.989 3.099   -31.909 1   13.006 ? 57  LEU   A CA   1 
ATOM   435  C  C    . LEU   A 1 57  ? -37.18  4.172   -30.839 1   12.936 ? 57  LEU   A C    1 
ATOM   436  O  O    . LEU   A 1 57  ? -37.837 3.928   -29.822 1   12.971 ? 57  LEU   A O    1 
ATOM   437  C  CB   . LEU   A 1 57  ? -35.63  2.422   -31.769 1   13.762 ? 57  LEU   A CB   1 
ATOM   438  C  CG   . LEU   A 1 57  ? -35.416 1.15    -32.591 1   15.33  ? 57  LEU   A CG   1 
ATOM   439  C  CD1  . LEU   A 1 57  ? -33.956 0.709   -32.514 1   16.882 ? 57  LEU   A CD1  1 
ATOM   440  C  CD2  . LEU   A 1 57  ? -36.35  0.032   -32.136 1   17.072 ? 57  LEU   A CD2  1 
ATOM   441  N  N    . LEU   A 1 58  ? -36.613 5.353   -31.073 1   12.267 ? 58  LEU   A N    1 
ATOM   442  C  CA   . LEU   A 1 58  ? -36.564 6.388   -30.049 1   12.55  ? 58  LEU   A CA   1 
ATOM   443  C  C    . LEU   A 1 58  ? -37.933 7.055   -29.873 1   11.877 ? 58  LEU   A C    1 
ATOM   444  O  O    . LEU   A 1 58  ? -38.296 7.427   -28.745 1   11.972 ? 58  LEU   A O    1 
ATOM   445  C  CB   . LEU   A 1 58  ? -35.459 7.41    -30.327 1   13.375 ? 58  LEU   A CB   1 
ATOM   446  C  CG   . LEU   A 1 58  ? -35.21  8.474   -29.251 1   13.909 ? 58  LEU   A CG   1 
ATOM   447  C  CD1  . LEU   A 1 58  ? -34.809 7.885   -27.905 1   13.574 ? 58  LEU   A CD1  1 
ATOM   448  C  CD2  . LEU   A 1 58  ? -34.127 9.435   -29.74  1   15.352 ? 58  LEU   A CD2  1 
ATOM   449  N  N    A ILE   A 1 59  ? -38.702 7.192   -30.966 0.5 11.99  ? 59  ILE   A N    1 
ATOM   450  N  N    B ILE   A 1 59  ? -38.708 7.196   -30.959 0.5 11.811 ? 59  ILE   A N    1 
ATOM   451  C  CA   A ILE   A 1 59  ? -39.966 7.917   -30.903 0.5 12.065 ? 59  ILE   A CA   1 
ATOM   452  C  CA   B ILE   A 1 59  ? -39.957 7.94    -30.86  0.5 11.708 ? 59  ILE   A CA   1 
ATOM   453  C  C    A ILE   A 1 59  ? -40.945 7.173   -29.989 0.5 11.841 ? 59  ILE   A C    1 
ATOM   454  C  C    B ILE   A 1 59  ? -40.947 7.175   -29.977 0.5 11.622 ? 59  ILE   A C    1 
ATOM   455  O  O    A ILE   A 1 59  ? -41.868 7.774   -29.433 0.5 12.516 ? 59  ILE   A O    1 
ATOM   456  O  O    B ILE   A 1 59  ? -41.88  7.767   -29.427 0.5 12.142 ? 59  ILE   A O    1 
ATOM   457  C  CB   A ILE   A 1 59  ? -40.537 8.138   -32.317 0.5 12.374 ? 59  ILE   A CB   1 
ATOM   458  C  CB   B ILE   A 1 59  ? -40.54  8.254   -32.247 0.5 11.834 ? 59  ILE   A CB   1 
ATOM   459  C  CG1  A ILE   A 1 59  ? -41.677 9.161   -32.311 0.5 12.832 ? 59  ILE   A CG1  1 
ATOM   460  C  CG1  B ILE   A 1 59  ? -41.522 9.425   -32.168 0.5 12.044 ? 59  ILE   A CG1  1 
ATOM   461  C  CG2  A ILE   A 1 59  ? -40.948 6.818   -32.961 0.5 12.216 ? 59  ILE   A CG2  1 
ATOM   462  C  CG2  B ILE   A 1 59  ? -41.164 7.015   -32.881 0.5 11.634 ? 59  ILE   A CG2  1 
ATOM   463  C  CD1  A ILE   A 1 59  ? -41.211 10.582  -32.055 0.5 13.118 ? 59  ILE   A CD1  1 
ATOM   464  C  CD1  B ILE   A 1 59  ? -41.816 10.075  -33.507 0.5 12.019 ? 59  ILE   A CD1  1 
ATOM   465  N  N    . ARG   A 1 60  ? -40.722 5.863   -29.822 1   11.687 ? 60  ARG   A N    1 
ATOM   466  C  CA   . ARG   A 1 60  ? -41.575 4.991   -29.017 1   12.074 ? 60  ARG   A CA   1 
ATOM   467  C  C    . ARG   A 1 60  ? -41.246 5.064   -27.528 1   12.381 ? 60  ARG   A C    1 
ATOM   468  O  O    . ARG   A 1 60  ? -41.926 4.418   -26.735 1   12.73  ? 60  ARG   A O    1 
ATOM   469  C  CB   . ARG   A 1 60  ? -41.394 3.546   -29.499 1   12.046 ? 60  ARG   A CB   1 
ATOM   470  C  CG   . ARG   A 1 60  ? -41.792 3.362   -30.958 1   12.498 ? 60  ARG   A CG   1 
ATOM   471  C  CD   . ARG   A 1 60  ? -41.399 2.004   -31.446 1   12.695 ? 60  ARG   A CD   1 
ATOM   472  N  NE   . ARG   A 1 60  ? -41.599 1.882   -32.892 1   12.789 ? 60  ARG   A NE   1 
ATOM   473  C  CZ   . ARG   A 1 60  ? -42.695 1.413   -33.495 1   12.609 ? 60  ARG   A CZ   1 
ATOM   474  N  NH1  . ARG   A 1 60  ? -43.749 1.038   -32.782 1   12.45  ? 60  ARG   A NH1  1 
ATOM   475  N  NH2  . ARG   A 1 60  ? -42.714 1.329   -34.818 1   13.196 ? 60  ARG   A NH2  1 
ATOM   476  N  N    . LYS   A 1 61  ? -40.191 5.807   -27.158 1   12.657 ? 61  LYS   A N    1 
ATOM   477  C  CA   . LYS   A 1 61  ? -39.764 5.93    -25.774 1   13.335 ? 61  LYS   A CA   1 
ATOM   478  C  C    . LYS   A 1 61  ? -40.264 7.241   -25.188 1   13.445 ? 61  LYS   A C    1 
ATOM   479  O  O    . LYS   A 1 61  ? -40.241 8.287   -25.835 1   14.123 ? 61  LYS   A O    1 
ATOM   480  C  CB   . LYS   A 1 61  ? -38.236 5.931   -25.672 1   14.714 ? 61  LYS   A CB   1 
ATOM   481  C  CG   . LYS   A 1 61  ? -37.54  4.708   -26.218 1   16.448 ? 61  LYS   A CG   1 
ATOM   482  C  CD   . LYS   A 1 61  ? -37.954 3.404   -25.563 1   18.66  ? 61  LYS   A CD   1 
ATOM   483  C  CE   . LYS   A 1 61  ? -37.189 2.256   -26.136 1   21.475 ? 61  LYS   A CE   1 
ATOM   484  N  NZ   . LYS   A 1 61  ? -37.665 0.977   -25.607 1   25.045 ? 61  LYS   A NZ   1 
ATOM   485  N  N    . SER   A 1 62  ? -40.674 7.158   -23.914 1   13.554 ? 62  SER   A N    1 
ATOM   486  C  CA   . SER   A 1 62  ? -40.894 8.324   -23.075 1   13.803 ? 62  SER   A CA   1 
ATOM   487  C  C    . SER   A 1 62  ? -39.647 8.593   -22.233 1   13.574 ? 62  SER   A C    1 
ATOM   488  O  O    . SER   A 1 62  ? -38.774 7.733   -22.118 1   14.95  ? 62  SER   A O    1 
ATOM   489  C  CB   . SER   A 1 62  ? -42.09  8.108   -22.202 1   15.261 ? 62  SER   A CB   1 
ATOM   490  O  OG   . SER   A 1 62  ? -41.835 7.06    -21.28  1   16.754 ? 62  SER   A OG   1 
ATOM   491  N  N    . ASN   A 1 63  ? -39.619 9.755   -21.576 1   13.732 ? 63  ASN   A N    1 
ATOM   492  C  CA   . ASN   A 1 63  ? -38.558 10.059  -20.63  1   13.504 ? 63  ASN   A CA   1 
ATOM   493  C  C    . ASN   A 1 63  ? -38.449 8.977   -19.558 1   13.763 ? 63  ASN   A C    1 
ATOM   494  O  O    . ASN   A 1 63  ? -37.352 8.612   -19.143 1   13.924 ? 63  ASN   A O    1 
ATOM   495  C  CB   . ASN   A 1 63  ? -38.76  11.428  -20.001 1   13.969 ? 63  ASN   A CB   1 
ATOM   496  C  CG   . ASN   A 1 63  ? -38.526 12.575  -20.951 1   15.355 ? 63  ASN   A CG   1 
ATOM   497  O  OD1  . ASN   A 1 63  ? -37.656 12.505  -21.839 1   17.086 ? 63  ASN   A OD1  1 
ATOM   498  N  ND2  . ASN   A 1 63  ? -39.234 13.668  -20.711 1   16.189 ? 63  ASN   A ND2  1 
ATOM   499  N  N    . HIS   A 1 64  ? -39.598 8.497   -19.071 1   13.658 ? 64  HIS   A N    1 
ATOM   500  C  CA   . HIS   A 1 64  ? -39.644 7.548   -17.966 1   14.516 ? 64  HIS   A CA   1 
ATOM   501  C  C    . HIS   A 1 64  ? -39.287 6.12    -18.385 1   15.184 ? 64  HIS   A C    1 
ATOM   502  O  O    . HIS   A 1 64  ? -39.19  5.24    -17.529 1   17.452 ? 64  HIS   A O    1 
ATOM   503  C  CB   . HIS   A 1 64  ? -40.96  7.673   -17.196 1   14.783 ? 64  HIS   A CB   1 
ATOM   504  C  CG   . HIS   A 1 64  ? -42.205 7.406   -17.959 1   15.547 ? 64  HIS   A CG   1 
ATOM   505  N  ND1  . HIS   A 1 64  ? -42.869 8.411   -18.625 1   16.435 ? 64  HIS   A ND1  1 
ATOM   506  C  CD2  . HIS   A 1 64  ? -42.932 6.305   -18.115 1   16.477 ? 64  HIS   A CD2  1 
ATOM   507  C  CE1  . HIS   A 1 64  ? -43.962 7.909   -19.199 1   16.754 ? 64  HIS   A CE1  1 
ATOM   508  N  NE2  . HIS   A 1 64  ? -44.02  6.623   -18.899 1   17.541 ? 64  HIS   A NE2  1 
ATOM   509  N  N    . ASN   A 1 65  ? -39.029 5.892   -19.68  1   14.336 ? 65  ASN   A N    1 
ATOM   510  C  CA   . ASN   A 1 65  ? -38.482 4.621   -20.122 1   15.466 ? 65  ASN   A CA   1 
ATOM   511  C  C    . ASN   A 1 65  ? -36.965 4.539   -19.903 1   15.604 ? 65  ASN   A C    1 
ATOM   512  O  O    . ASN   A 1 65  ? -36.358 3.483   -20.118 1   17.766 ? 65  ASN   A O    1 
ATOM   513  C  CB   . ASN   A 1 65  ? -38.779 4.348   -21.592 1   16.548 ? 65  ASN   A CB   1 
ATOM   514  C  CG   . ASN   A 1 65  ? -40.24  4.093   -21.87  1   18.445 ? 65  ASN   A CG   1 
ATOM   515  O  OD1  . ASN   A 1 65  ? -40.755 4.546   -22.895 1   18.208 ? 65  ASN   A OD1  1 
ATOM   516  N  ND2  . ASN   A 1 65  ? -40.928 3.352   -21.01  1   20.853 ? 65  ASN   A ND2  1 
ATOM   517  N  N    . PHE   A 1 66  ? -36.349 5.653   -19.506 1   14.39  ? 66  PHE   A N    1 
ATOM   518  C  CA   . PHE   A 1 66  ? -34.928 5.681   -19.2   1   14.355 ? 66  PHE   A CA   1 
ATOM   519  C  C    . PHE   A 1 66  ? -34.724 5.793   -17.696 1   14.992 ? 66  PHE   A C    1 
ATOM   520  O  O    . PHE   A 1 66  ? -35.237 6.731   -17.091 1   16.812 ? 66  PHE   A O    1 
ATOM   521  C  CB   . PHE   A 1 66  ? -34.261 6.882   -19.864 1   14.288 ? 66  PHE   A CB   1 
ATOM   522  C  CG   . PHE   A 1 66  ? -34.337 6.803   -21.375 1   14.738 ? 66  PHE   A CG   1 
ATOM   523  C  CD1  . PHE   A 1 66  ? -33.432 6.016   -22.075 1   15.523 ? 66  PHE   A CD1  1 
ATOM   524  C  CD2  . PHE   A 1 66  ? -35.323 7.478   -22.086 1   14.762 ? 66  PHE   A CD2  1 
ATOM   525  C  CE1  . PHE   A 1 66  ? -33.513 5.92    -23.455 1   15.977 ? 66  PHE   A CE1  1 
ATOM   526  C  CE2  . PHE   A 1 66  ? -35.382 7.395   -23.465 1   15.734 ? 66  PHE   A CE2  1 
ATOM   527  C  CZ   . PHE   A 1 66  ? -34.49  6.598   -24.141 1   15.41  ? 66  PHE   A CZ   1 
ATOM   528  N  N    . LEU   A 1 67  ? -33.967 4.846   -17.137 1   15.148 ? 67  LEU   A N    1 
ATOM   529  C  CA   . LEU   A 1 67  ? -33.595 4.883   -15.733 1   15.958 ? 67  LEU   A CA   1 
ATOM   530  C  C    . LEU   A 1 67  ? -32.116 5.23    -15.638 1   15.224 ? 67  LEU   A C    1 
ATOM   531  O  O    . LEU   A 1 67  ? -31.298 4.576   -16.272 1   16.656 ? 67  LEU   A O    1 
ATOM   532  C  CB   . LEU   A 1 67  ? -33.876 3.52    -15.105 1   19.291 ? 67  LEU   A CB   1 
ATOM   533  C  CG   . LEU   A 1 67  ? -35.336 3.061   -15.124 1   23.064 ? 67  LEU   A CG   1 
ATOM   534  C  CD1  . LEU   A 1 67  ? -35.436 1.73    -14.391 1   25.374 ? 67  LEU   A CD1  1 
ATOM   535  C  CD2  . LEU   A 1 67  ? -36.285 4.082   -14.516 1   25.19  ? 67  LEU   A CD2  1 
ATOM   536  N  N    . VAL   A 1 68  ? -31.797 6.268   -14.867 1   14.386 ? 68  VAL   A N    1 
ATOM   537  C  CA   . VAL   A 1 68  ? -30.417 6.658   -14.638 1   13.526 ? 68  VAL   A CA   1 
ATOM   538  C  C    . VAL   A 1 68  ? -30.146 6.593   -13.142 1   13.629 ? 68  VAL   A C    1 
ATOM   539  O  O    . VAL   A 1 68  ? -30.875 7.192   -12.357 1   14.663 ? 68  VAL   A O    1 
ATOM   540  C  CB   . VAL   A 1 68  ? -30.155 8.073   -15.16  1   14.662 ? 68  VAL   A CB   1 
ATOM   541  C  CG1  . VAL   A 1 68  ? -28.713 8.483   -14.9   1   15.879 ? 68  VAL   A CG1  1 
ATOM   542  C  CG2  . VAL   A 1 68  ? -30.536 8.185   -16.628 1   15.163 ? 68  VAL   A CG2  1 
ATOM   543  N  N    . GLN   A 1 69  ? -29.094 5.865   -12.776 1   13.529 ? 69  GLN   A N    1 
ATOM   544  C  CA   . GLN   A 1 69  ? -28.714 5.693   -11.386 1   15.297 ? 69  GLN   A CA   1 
ATOM   545  C  C    . GLN   A 1 69  ? -27.287 6.189   -11.19  1   14.9   ? 69  GLN   A C    1 
ATOM   546  O  O    . GLN   A 1 69  ? -26.38  5.761   -11.9   1   14.27  ? 69  GLN   A O    1 
ATOM   547  C  CB   . GLN   A 1 69  ? -28.871 4.214   -11.054 1   18.687 ? 69  GLN   A CB   1 
ATOM   548  C  CG   . GLN   A 1 69  ? -28.607 3.847   -9.602  1   22.561 ? 69  GLN   A CG   1 
ATOM   549  C  CD   . GLN   A 1 69  ? -29.013 2.43    -9.26   1   27.632 ? 69  GLN   A CD   1 
ATOM   550  O  OE1  . GLN   A 1 69  ? -29.874 1.819   -9.906  1   32.573 ? 69  GLN   A OE1  1 
ATOM   551  N  NE2  . GLN   A 1 69  ? -28.414 1.901   -8.205  1   30.891 ? 69  GLN   A NE2  1 
ATOM   552  N  N    . ALA   A 1 70  ? -27.128 7.105   -10.231 1   16.521 ? 70  ALA   A N    1 
ATOM   553  C  CA   . ALA   A 1 70  ? -25.829 7.642   -9.875  1   17.76  ? 70  ALA   A CA   1 
ATOM   554  C  C    . ALA   A 1 70  ? -25.526 7.137   -8.472  1   20.454 ? 70  ALA   A C    1 
ATOM   555  O  O    . ALA   A 1 70  ? -26.126 7.6     -7.509  1   21.376 ? 70  ALA   A O    1 
ATOM   556  C  CB   . ALA   A 1 70  ? -25.84  9.152   -9.944  1   18.459 ? 70  ALA   A CB   1 
ATOM   557  N  N    . GLY   A 1 71  ? -24.634 6.15    -8.374  1   22.345 ? 71  GLY   A N    1 
ATOM   558  C  CA   . GLY   A 1 71  ? -24.481 5.421   -7.128  1   24.889 ? 71  GLY   A CA   1 
ATOM   559  C  C    . GLY   A 1 71  ? -25.817 4.818   -6.699  1   27.618 ? 71  GLY   A C    1 
ATOM   560  O  O    . GLY   A 1 71  ? -26.389 4.022   -7.437  1   29.841 ? 71  GLY   A O    1 
ATOM   561  N  N    . ASN   A 1 72  ? -26.327 5.248   -5.536  1   29.14  ? 72  ASN   A N    1 
ATOM   562  C  CA   . ASN   A 1 72  ? -27.55  4.699   -4.962  1   30.615 ? 72  ASN   A CA   1 
ATOM   563  C  C    . ASN   A 1 72  ? -28.768 5.569   -5.288  1   31.069 ? 72  ASN   A C    1 
ATOM   564  O  O    . ASN   A 1 72  ? -29.857 5.279   -4.808  1   34.167 ? 72  ASN   A O    1 
ATOM   565  C  CB   . ASN   A 1 72  ? -27.427 4.523   -3.449  1   32.589 ? 72  ASN   A CB   1 
ATOM   566  N  N    . VAL   A 1 73  ? -28.597 6.615   -6.113  1   28.378 ? 73  VAL   A N    1 
ATOM   567  C  CA   . VAL   A 1 73  ? -29.604 7.654   -6.3    1   27.552 ? 73  VAL   A CA   1 
ATOM   568  C  C    . VAL   A 1 73  ? -30.178 7.555   -7.713  1   23.935 ? 73  VAL   A C    1 
ATOM   569  O  O    . VAL   A 1 73  ? -29.427 7.571   -8.681  1   22.064 ? 73  VAL   A O    1 
ATOM   570  C  CB   . VAL   A 1 73  ? -28.988 9.053   -6.077  1   29.665 ? 73  VAL   A CB   1 
ATOM   571  C  CG1  . VAL   A 1 73  ? -29.952 10.185  -6.412  1   31.443 ? 73  VAL   A CG1  1 
ATOM   572  C  CG2  . VAL   A 1 73  ? -28.465 9.232   -4.659  1   31.392 ? 73  VAL   A CG2  1 
ATOM   573  N  N    . GLN   A 1 74  ? -31.505 7.501   -7.843  1   24.185 ? 74  GLN   A N    1 
ATOM   574  C  CA   . GLN   A 1 74  ? -32.144 7.586   -9.149  1   23.042 ? 74  GLN   A CA   1 
ATOM   575  C  C    . GLN   A 1 74  ? -32.25  9.049   -9.571  1   20.991 ? 74  GLN   A C    1 
ATOM   576  O  O    . GLN   A 1 74  ? -32.752 9.878   -8.812  1   23.951 ? 74  GLN   A O    1 
ATOM   577  C  CB   . GLN   A 1 74  ? -33.555 6.987   -9.169  1   26.406 ? 74  GLN   A CB   1 
ATOM   578  C  CG   . GLN   A 1 74  ? -33.624 5.484   -8.921  1   29.579 ? 74  GLN   A CG   1 
ATOM   579  C  CD   . GLN   A 1 74  ? -32.817 4.668   -9.909  1   32.986 ? 74  GLN   A CD   1 
ATOM   580  O  OE1  . GLN   A 1 74  ? -32.935 4.819   -11.132 1   35.151 ? 74  GLN   A OE1  1 
ATOM   581  N  NE2  . GLN   A 1 74  ? -31.979 3.789   -9.38   1   35.544 ? 74  GLN   A NE2  1 
ATOM   582  N  N    . LEU   A 1 75  ? -31.796 9.355   -10.795 1   16.874 ? 75  LEU   A N    1 
ATOM   583  C  CA   . LEU   A 1 75  ? -32.009 10.66   -11.404 1   17.272 ? 75  LEU   A CA   1 
ATOM   584  C  C    . LEU   A 1 75  ? -33.266 10.603  -12.266 1   18.032 ? 75  LEU   A C    1 
ATOM   585  O  O    . LEU   A 1 75  ? -33.552 9.58    -12.871 1   23.793 ? 75  LEU   A O    1 
ATOM   586  C  CB   . LEU   A 1 75  ? -30.822 11.057  -12.273 1   17.387 ? 75  LEU   A CB   1 
ATOM   587  C  CG   . LEU   A 1 75  ? -29.456 11.064  -11.581 1   18.132 ? 75  LEU   A CG   1 
ATOM   588  C  CD1  . LEU   A 1 75  ? -28.371 11.534  -12.527 1   18.436 ? 75  LEU   A CD1  1 
ATOM   589  C  CD2  . LEU   A 1 75  ? -29.468 11.926  -10.343 1   19.542 ? 75  LEU   A CD2  1 
ATOM   590  N  N    . ARG   A 1 76  ? -33.984 11.717  -12.367 1   17.216 ? 76  ARG   A N    1 
ATOM   591  C  CA   . ARG   A 1 76  ? -35.187 11.751  -13.184 1   17.712 ? 76  ARG   A CA   1 
ATOM   592  C  C    . ARG   A 1 76  ? -34.869 12.337  -14.554 1   16.033 ? 76  ARG   A C    1 
ATOM   593  O  O    . ARG   A 1 76  ? -34.393 13.465  -14.648 1   15.982 ? 76  ARG   A O    1 
ATOM   594  C  CB   . ARG   A 1 76  ? -36.261 12.598  -12.497 1   20.136 ? 76  ARG   A CB   1 
ATOM   595  C  CG   . ARG   A 1 76  ? -37.587 12.721  -13.232 1   22.829 ? 76  ARG   A CG   1 
ATOM   596  C  CD   . ARG   A 1 76  ? -38.618 13.488  -12.395 1   26.55  ? 76  ARG   A CD   1 
ATOM   597  N  NE   . ARG   A 1 76  ? -39.682 14.109  -13.196 1   31.828 ? 76  ARG   A NE   1 
ATOM   598  C  CZ   . ARG   A 1 76  ? -39.935 15.419  -13.296 1   37.056 ? 76  ARG   A CZ   1 
ATOM   599  N  NH1  . ARG   A 1 76  ? -39.123 16.324  -12.77  1   39.853 ? 76  ARG   A NH1  1 
ATOM   600  N  NH2  . ARG   A 1 76  ? -40.995 15.832  -13.967 1   39.78  ? 76  ARG   A NH2  1 
ATOM   601  N  N    . VAL   A 1 77  ? -35.199 11.578  -15.61  1   15.579 ? 77  VAL   A N    1 
ATOM   602  C  CA   . VAL   A 1 77  ? -35.023 12.045  -16.978 1   15.155 ? 77  VAL   A CA   1 
ATOM   603  C  C    . VAL   A 1 77  ? -36.189 12.957  -17.352 1   15.257 ? 77  VAL   A C    1 
ATOM   604  O  O    . VAL   A 1 77  ? -37.352 12.591  -17.185 1   15.903 ? 77  VAL   A O    1 
ATOM   605  C  CB   . VAL   A 1 77  ? -34.872 10.862  -17.951 1   15.21  ? 77  VAL   A CB   1 
ATOM   606  C  CG1  . VAL   A 1 77  ? -34.826 11.324  -19.405 1   15.063 ? 77  VAL   A CG1  1 
ATOM   607  C  CG2  . VAL   A 1 77  ? -33.631 10.036  -17.618 1   15.862 ? 77  VAL   A CG2  1 
ATOM   608  N  N    . ILE   A 1 78  ? -35.853 14.158  -17.833 1   15.515 ? 78  ILE   A N    1 
ATOM   609  C  CA   . ILE   A 1 78  ? -36.851 15.158  -18.177 1   16.243 ? 78  ILE   A CA   1 
ATOM   610  C  C    . ILE   A 1 78  ? -36.76  15.579  -19.644 1   16.247 ? 78  ILE   A C    1 
ATOM   611  O  O    . ILE   A 1 78  ? -37.503 16.469  -20.064 1   18.017 ? 78  ILE   A O    1 
ATOM   612  C  CB   . ILE   A 1 78  ? -36.741 16.372  -17.236 1   18.083 ? 78  ILE   A CB   1 
ATOM   613  C  CG1  . ILE   A 1 78  ? -35.367 17.065  -17.308 1   18.811 ? 78  ILE   A CG1  1 
ATOM   614  C  CG2  . ILE   A 1 78  ? -37.099 15.955  -15.808 1   18.558 ? 78  ILE   A CG2  1 
ATOM   615  C  CD1  . ILE   A 1 78  ? -35.335 18.43   -16.638 1   20.073 ? 78  ILE   A CD1  1 
ATOM   616  N  N    . GLY   A 1 79  ? -35.889 14.934  -20.425 1   15.3   ? 79  GLY   A N    1 
ATOM   617  C  CA   . GLY   A 1 79  ? -35.805 15.194  -21.852 1   15.045 ? 79  GLY   A CA   1 
ATOM   618  C  C    . GLY   A 1 79  ? -34.809 14.229  -22.473 1   15.269 ? 79  GLY   A C    1 
ATOM   619  O  O    . GLY   A 1 79  ? -33.962 13.671  -21.777 1   15.688 ? 79  GLY   A O    1 
ATOM   620  N  N    . HIS   A 1 80  ? -34.924 14.021  -23.777 1   15.719 ? 80  HIS   A N    1 
ATOM   621  C  CA   . HIS   A 1 80  ? -33.964 13.184  -24.467 1   15.777 ? 80  HIS   A CA   1 
ATOM   622  C  C    . HIS   A 1 80  ? -33.835 13.639  -25.911 1   16.548 ? 80  HIS   A C    1 
ATOM   623  O  O    . HIS   A 1 80  ? -34.794 14.116  -26.51  1   17.312 ? 80  HIS   A O    1 
ATOM   624  C  CB   . HIS   A 1 80  ? -34.353 11.706  -24.372 1   16.035 ? 80  HIS   A CB   1 
ATOM   625  C  CG   . HIS   A 1 80  ? -35.697 11.403  -24.928 1   16.998 ? 80  HIS   A CG   1 
ATOM   626  N  ND1  . HIS   A 1 80  ? -36.842 11.483  -24.17  1   18.244 ? 80  HIS   A ND1  1 
ATOM   627  C  CD2  . HIS   A 1 80  ? -36.085 11.019  -26.162 1   18.157 ? 80  HIS   A CD2  1 
ATOM   628  C  CE1  . HIS   A 1 80  ? -37.882 11.122  -24.921 1   18.964 ? 80  HIS   A CE1  1 
ATOM   629  N  NE2  . HIS   A 1 80  ? -37.444 10.864  -26.132 1   18.623 ? 80  HIS   A NE2  1 
ATOM   630  N  N    . SER   A 1 81  ? -32.641 13.425  -26.46  1   16.43  ? 81  SER   A N    1 
ATOM   631  C  CA   . SER   A 1 81  ? -32.39  13.686  -27.86  1   16.61  ? 81  SER   A CA   1 
ATOM   632  C  C    . SER   A 1 81  ? -31.205 12.837  -28.291 1   16.262 ? 81  SER   A C    1 
ATOM   633  O  O    . SER   A 1 81  ? -30.413 12.392  -27.473 1   17.109 ? 81  SER   A O    1 
ATOM   634  C  CB   . SER   A 1 81  ? -32.131 15.141  -28.109 1   18.703 ? 81  SER   A CB   1 
ATOM   635  O  OG   . SER   A 1 81  ? -30.91  15.565  -27.522 1   20.712 ? 81  SER   A OG   1 
ATOM   636  N  N    . MET   A 1 82  ? -31.127 12.631  -29.597 1   15.381 ? 82  MET   A N    1 
ATOM   637  C  CA   . MET   A 1 82  ? -30.074 11.854  -30.211 1   16.19  ? 82  MET   A CA   1 
ATOM   638  C  C    . MET   A 1 82  ? -29.204 12.824  -31.004 1   15.719 ? 82  MET   A C    1 
ATOM   639  O  O    . MET   A 1 82  ? -29.725 13.694  -31.701 1   17.079 ? 82  MET   A O    1 
ATOM   640  C  CB   . MET   A 1 82  ? -30.76  10.791  -31.083 1   18.267 ? 82  MET   A CB   1 
ATOM   641  C  CG   . MET   A 1 82  ? -29.849 9.904   -31.851 1   18.632 ? 82  MET   A CG   1 
ATOM   642  S  SD   . MET   A 1 82  ? -30.747 8.458   -32.447 1   19.6   ? 82  MET   A SD   1 
ATOM   643  C  CE   . MET   A 1 82  ? -31.93  9.085   -33.648 1   20.485 ? 82  MET   A CE   1 
ATOM   644  N  N    . GLN   A 1 83  ? -27.886 12.715  -30.835 1   14.75  ? 83  GLN   A N    1 
ATOM   645  C  CA   . GLN   A 1 83  ? -26.932 13.472  -31.621 1   15.344 ? 83  GLN   A CA   1 
ATOM   646  C  C    . GLN   A 1 83  ? -25.974 12.461  -32.233 1   14.486 ? 83  GLN   A C    1 
ATOM   647  O  O    . GLN   A 1 83  ? -25.197 11.833  -31.525 1   13.939 ? 83  GLN   A O    1 
ATOM   648  C  CB   . GLN   A 1 83  ? -26.183 14.49   -30.766 1   16.417 ? 83  GLN   A CB   1 
ATOM   649  C  CG   . GLN   A 1 83  ? -25.114 15.26   -31.532 1   17.258 ? 83  GLN   A CG   1 
ATOM   650  C  CD   . GLN   A 1 83  ? -24.333 16.23   -30.671 1   20.026 ? 83  GLN   A CD   1 
ATOM   651  O  OE1  . GLN   A 1 83  ? -24.399 16.195  -29.443 1   22.517 ? 83  GLN   A OE1  1 
ATOM   652  N  NE2  . GLN   A 1 83  ? -23.577 17.111  -31.305 1   22.396 ? 83  GLN   A NE2  1 
ATOM   653  N  N    . ASN   A 1 84  ? -26.069 12.267  -33.552 1   14.355 ? 84  ASN   A N    1 
ATOM   654  C  CA   . ASN   A 1 84  ? -25.264 11.245  -34.204 1   13.941 ? 84  ASN   A CA   1 
ATOM   655  C  C    . ASN   A 1 84  ? -25.505 9.922   -33.473 1   12.838 ? 84  ASN   A C    1 
ATOM   656  O  O    . ASN   A 1 84  ? -26.661 9.528   -33.319 1   13.495 ? 84  ASN   A O    1 
ATOM   657  C  CB   . ASN   A 1 84  ? -23.82  11.723  -34.345 1   14.314 ? 84  ASN   A CB   1 
ATOM   658  C  CG   . ASN   A 1 84  ? -23.748 13.035  -35.09  1   14.894 ? 84  ASN   A CG   1 
ATOM   659  O  OD1  . ASN   A 1 84  ? -24.297 13.137  -36.198 1   16.841 ? 84  ASN   A OD1  1 
ATOM   660  N  ND2  . ASN   A 1 84  ? -23.13  14.052  -34.497 1   14.888 ? 84  ASN   A ND2  1 
ATOM   661  N  N    . CYS   A 1 85  ? -24.446 9.25    -32.983 1   11.826 ? 85  CYS   A N    1 
ATOM   662  C  CA   . CYS   A 1 85  ? -24.611 7.956   -32.33  1   12.126 ? 85  CYS   A CA   1 
ATOM   663  C  C    . CYS   A 1 85  ? -24.642 8.027   -30.795 1   11.515 ? 85  CYS   A C    1 
ATOM   664  O  O    . CYS   A 1 85  ? -24.511 6.989   -30.146 1   10.821 ? 85  CYS   A O    1 
ATOM   665  C  CB   . CYS   A 1 85  ? -23.525 6.993   -32.788 1   13.099 ? 85  CYS   A CB   1 
ATOM   666  S  SG   . CYS   A 1 85  ? -23.513 6.735   -34.578 1   14.263 ? 85  CYS   A SG   1 
ATOM   667  N  N    A VAL   A 1 86  ? -24.836 9.228   -30.239 0.5 12.096 ? 86  VAL   A N    1 
ATOM   668  N  N    B VAL   A 1 86  ? -24.835 9.228   -30.236 0.5 11.677 ? 86  VAL   A N    1 
ATOM   669  C  CA   A VAL   A 1 86  ? -24.976 9.376   -28.798 0.5 12.886 ? 86  VAL   A CA   1 
ATOM   670  C  CA   B VAL   A 1 86  ? -24.959 9.402   -28.794 0.5 12.284 ? 86  VAL   A CA   1 
ATOM   671  C  C    A VAL   A 1 86  ? -26.399 9.803   -28.44  0.5 13.1   ? 86  VAL   A C    1 
ATOM   672  C  C    B VAL   A 1 86  ? -26.381 9.822   -28.426 0.5 12.745 ? 86  VAL   A C    1 
ATOM   673  O  O    A VAL   A 1 86  ? -27.053 10.572  -29.15  0.5 13.848 ? 86  VAL   A O    1 
ATOM   674  O  O    B VAL   A 1 86  ? -27.029 10.604  -29.128 0.5 13.587 ? 86  VAL   A O    1 
ATOM   675  C  CB   A VAL   A 1 86  ? -23.927 10.326  -28.194 0.5 14.109 ? 86  VAL   A CB   1 
ATOM   676  C  CB   B VAL   A 1 86  ? -23.89  10.394  -28.294 0.5 12.747 ? 86  VAL   A CB   1 
ATOM   677  C  CG1  A VAL   A 1 86  ? -22.528 9.796   -28.432 0.5 14.911 ? 86  VAL   A CG1  1 
ATOM   678  C  CG1  B VAL   A 1 86  ? -24.225 11.047  -26.956 0.5 12.925 ? 86  VAL   A CG1  1 
ATOM   679  C  CG2  A VAL   A 1 86  ? -24.077 11.764  -28.657 0.5 14.379 ? 86  VAL   A CG2  1 
ATOM   680  C  CG2  B VAL   A 1 86  ? -22.561 9.685   -28.169 0.5 13.183 ? 86  VAL   A CG2  1 
ATOM   681  N  N    . LEU   A 1 87  ? -26.877 9.234   -27.332 1   12.694 ? 87  LEU   A N    1 
ATOM   682  C  CA   . LEU   A 1 87  ? -28.112 9.657   -26.712 1   13.168 ? 87  LEU   A CA   1 
ATOM   683  C  C    . LEU   A 1 87  ? -27.762 10.637  -25.6   1   12.812 ? 87  LEU   A C    1 
ATOM   684  O  O    . LEU   A 1 87  ? -26.841 10.38   -24.825 1   12.348 ? 87  LEU   A O    1 
ATOM   685  C  CB   . LEU   A 1 87  ? -28.801 8.407   -26.176 1   15.132 ? 87  LEU   A CB   1 
ATOM   686  C  CG   . LEU   A 1 87  ? -30.156 8.607   -25.508 1   16.763 ? 87  LEU   A CG   1 
ATOM   687  C  CD1  . LEU   A 1 87  ? -31.206 9.099   -26.488 1   17.697 ? 87  LEU   A CD1  1 
ATOM   688  C  CD2  . LEU   A 1 87  ? -30.538 7.282   -24.861 1   17.195 ? 87  LEU   A CD2  1 
ATOM   689  N  N    . LYS   A 1 88  ? -28.502 11.745  -25.541 1   13.074 ? 88  LYS   A N    1 
ATOM   690  C  CA   . LYS   A 1 88  ? -28.362 12.735  -24.493 1   13.56  ? 88  LYS   A CA   1 
ATOM   691  C  C    . LYS   A 1 88  ? -29.642 12.767  -23.674 1   13.498 ? 88  LYS   A C    1 
ATOM   692  O  O    . LYS   A 1 88  ? -30.701 13.09   -24.195 1   14.711 ? 88  LYS   A O    1 
ATOM   693  C  CB   . LYS   A 1 88  ? -28.076 14.114  -25.085 1   14.86  ? 88  LYS   A CB   1 
ATOM   694  C  CG   . LYS   A 1 88  ? -26.789 14.174  -25.875 1   15.944 ? 88  LYS   A CG   1 
ATOM   695  C  CD   . LYS   A 1 88  ? -26.431 15.578  -26.344 1   19.207 ? 88  LYS   A CD   1 
ATOM   696  C  CE   . LYS   A 1 88  ? -27.342 16.086  -27.404 1   21.132 ? 88  LYS   A CE   1 
ATOM   697  N  NZ   . LYS   A 1 88  ? -26.752 17.275  -28.023 1   23.456 ? 88  LYS   A NZ   1 
ATOM   698  N  N    . LEU   A 1 89  ? -29.526 12.423  -22.388 1   12.634 ? 89  LEU   A N    1 
ATOM   699  C  CA   . LEU   A 1 89  ? -30.659 12.44   -21.479 1   12.771 ? 89  LEU   A CA   1 
ATOM   700  C  C    . LEU   A 1 89  ? -30.533 13.661  -20.585 1   13.44  ? 89  LEU   A C    1 
ATOM   701  O  O    . LEU   A 1 89  ? -29.574 13.769  -19.825 1   14.863 ? 89  LEU   A O    1 
ATOM   702  C  CB   . LEU   A 1 89  ? -30.665 11.154  -20.657 1   13.061 ? 89  LEU   A CB   1 
ATOM   703  C  CG   . LEU   A 1 89  ? -30.724 9.84    -21.436 1   13.781 ? 89  LEU   A CG   1 
ATOM   704  C  CD1  . LEU   A 1 89  ? -30.618 8.67    -20.483 1   14.404 ? 89  LEU   A CD1  1 
ATOM   705  C  CD2  . LEU   A 1 89  ? -31.984 9.72    -22.266 1   14.002 ? 89  LEU   A CD2  1 
ATOM   706  N  N    . LYS   A 1 90  ? -31.515 14.556  -20.661 1   14.049 ? 90  LYS   A N    1 
ATOM   707  C  CA   . LYS   A 1 90  ? -31.579 15.67   -19.731 1   14.642 ? 90  LYS   A CA   1 
ATOM   708  C  C    . LYS   A 1 90  ? -32.168 15.166  -18.418 1   14.625 ? 90  LYS   A C    1 
ATOM   709  O  O    . LYS   A 1 90  ? -33.179 14.48   -18.436 1   15.174 ? 90  LYS   A O    1 
ATOM   710  C  CB   . LYS   A 1 90  ? -32.412 16.812  -20.315 1   16.438 ? 90  LYS   A CB   1 
ATOM   711  C  CG   . LYS   A 1 90  ? -32.388 18.083  -19.517 1   20.09  ? 90  LYS   A CG   1 
ATOM   712  C  CD   . LYS   A 1 90  ? -33.227 19.214  -20.082 1   25.174 ? 90  LYS   A CD   1 
ATOM   713  C  CE   . LYS   A 1 90  ? -33.08  20.422  -19.224 1   29.644 ? 90  LYS   A CE   1 
ATOM   714  N  NZ   . LYS   A 1 90  ? -33.944 21.518  -19.666 1   33.748 ? 90  LYS   A NZ   1 
ATOM   715  N  N    . VAL   A 1 91  ? -31.485 15.471  -17.306 1   14.151 ? 91  VAL   A N    1 
ATOM   716  C  CA   . VAL   A 1 91  ? -31.92  15.031  -15.991 1   14.718 ? 91  VAL   A CA   1 
ATOM   717  C  C    . VAL   A 1 91  ? -32.201 16.261  -15.133 1   15.489 ? 91  VAL   A C    1 
ATOM   718  O  O    . VAL   A 1 91  ? -31.811 17.383  -15.47  1   15.111 ? 91  VAL   A O    1 
ATOM   719  C  CB   . VAL   A 1 91  ? -30.911 14.067  -15.334 1   14.796 ? 91  VAL   A CB   1 
ATOM   720  C  CG1  . VAL   A 1 91  ? -30.885 12.727  -16.065 1   15.367 ? 91  VAL   A CG1  1 
ATOM   721  C  CG2  . VAL   A 1 91  ? -29.5   14.661  -15.206 1   14.88  ? 91  VAL   A CG2  1 
ATOM   722  N  N    . ASP   A 1 92  ? -32.906 16.035  -14.017 1   16.529 ? 92  ASP   A N    1 
ATOM   723  C  CA   . ASP   A 1 92  ? -33.398 17.132  -13.202 1   18.355 ? 92  ASP   A CA   1 
ATOM   724  C  C    . ASP   A 1 92  ? -32.415 17.512  -12.094 1   18.78  ? 92  ASP   A C    1 
ATOM   725  O  O    . ASP   A 1 92  ? -32.782 18.275  -11.199 1   22.055 ? 92  ASP   A O    1 
ATOM   726  C  CB   . ASP   A 1 92  ? -34.766 16.808  -12.625 1   20.707 ? 92  ASP   A CB   1 
ATOM   727  C  CG   . ASP   A 1 92  ? -35.686 18.007  -12.466 1   24.697 ? 92  ASP   A CG   1 
ATOM   728  O  OD1  . ASP   A 1 92  ? -35.368 19.077  -13.027 1   28.795 ? 92  ASP   A OD1  1 
ATOM   729  O  OD2  . ASP   A 1 92  ? -36.703 17.866  -11.767 1   30.455 ? 92  ASP   A OD2  1 
ATOM   730  N  N    . THR   A 1 93  ? -31.179 17.006  -12.158 1   17.835 ? 93  THR   A N    1 
ATOM   731  C  CA   . THR   A 1 93  ? -30.135 17.344  -11.195 1   17.416 ? 93  THR   A CA   1 
ATOM   732  C  C    . THR   A 1 93  ? -28.848 17.618  -11.97  1   16.295 ? 93  THR   A C    1 
ATOM   733  O  O    . THR   A 1 93  ? -28.465 16.807  -12.806 1   16.326 ? 93  THR   A O    1 
ATOM   734  C  CB   . THR   A 1 93  ? -29.914 16.187  -10.217 1   18.349 ? 93  THR   A CB   1 
ATOM   735  O  OG1  . THR   A 1 93  ? -31.155 15.827  -9.611  1   21.09  ? 93  THR   A OG1  1 
ATOM   736  C  CG2  . THR   A 1 93  ? -28.897 16.528  -9.138  1   19.266 ? 93  THR   A CG2  1 
ATOM   737  N  N    . ALA   A 1 94  ? -28.178 18.742  -11.707 1   15.085 ? 94  ALA   A N    1 
ATOM   738  C  CA   . ALA   A 1 94  ? -26.835 18.957  -12.229 1   14.571 ? 94  ALA   A CA   1 
ATOM   739  C  C    . ALA   A 1 94  ? -25.852 18.159  -11.376 1   14.571 ? 94  ALA   A C    1 
ATOM   740  O  O    . ALA   A 1 94  ? -25.956 18.136  -10.161 1   14.652 ? 94  ALA   A O    1 
ATOM   741  C  CB   . ALA   A 1 94  ? -26.498 20.432  -12.22  1   15.473 ? 94  ALA   A CB   1 
ATOM   742  N  N    . ASN   A 1 95  ? -24.893 17.492  -12.013 1   13.047 ? 95  ASN   A N    1 
ATOM   743  C  CA   . ASN   A 1 95  ? -23.914 16.712  -11.276 1   12.636 ? 95  ASN   A CA   1 
ATOM   744  C  C    . ASN   A 1 95  ? -23.052 17.655  -10.438 1   13.021 ? 95  ASN   A C    1 
ATOM   745  O  O    . ASN   A 1 95  ? -22.307 18.46   -10.993 1   13.443 ? 95  ASN   A O    1 
ATOM   746  C  CB   . ASN   A 1 95  ? -23.055 15.897  -12.231 1   11.935 ? 95  ASN   A CB   1 
ATOM   747  C  CG   . ASN   A 1 95  ? -22.062 15.01   -11.526 1   12.258 ? 95  ASN   A CG   1 
ATOM   748  O  OD1  . ASN   A 1 95  ? -21.956 15.041  -10.299 1   12.92  ? 95  ASN   A OD1  1 
ATOM   749  N  ND2  . ASN   A 1 95  ? -21.312 14.234  -12.284 1   12.825 ? 95  ASN   A ND2  1 
ATOM   750  N  N    . PRO   A 1 96  ? -23.077 17.564  -9.089  1   14.024 ? 96  PRO   A N    1 
ATOM   751  C  CA   . PRO   A 1 96  ? -22.267 18.462  -8.267  1   14.664 ? 96  PRO   A CA   1 
ATOM   752  C  C    . PRO   A 1 96  ? -20.767 18.214  -8.39   1   14.929 ? 96  PRO   A C    1 
ATOM   753  O  O    . PRO   A 1 96  ? -19.983 19.08   -8.009  1   17.139 ? 96  PRO   A O    1 
ATOM   754  C  CB   . PRO   A 1 96  ? -22.788 18.197  -6.846  1   15.405 ? 96  PRO   A CB   1 
ATOM   755  C  CG   . PRO   A 1 96  ? -23.307 16.789  -6.896  1   15.77  ? 96  PRO   A CG   1 
ATOM   756  C  CD   . PRO   A 1 96  ? -23.86  16.601  -8.296  1   14.882 ? 96  PRO   A CD   1 
ATOM   757  N  N    . LYS   A 1 97  ? -20.394 17.058  -8.96   1   13.755 ? 97  LYS   A N    1 
ATOM   758  C  CA   . LYS   A 1 97  ? -18.998 16.705  -9.148  1   14.004 ? 97  LYS   A CA   1 
ATOM   759  C  C    . LYS   A 1 97  ? -18.536 16.97   -10.583 1   13.714 ? 97  LYS   A C    1 
ATOM   760  O  O    . LYS   A 1 97  ? -17.456 16.523  -10.957 1   14.333 ? 97  LYS   A O    1 
ATOM   761  C  CB   . LYS   A 1 97  ? -18.798 15.229  -8.79   1   15.159 ? 97  LYS   A CB   1 
ATOM   762  C  CG   . LYS   A 1 97  ? -19.125 14.882  -7.345  1   17.357 ? 97  LYS   A CG   1 
ATOM   763  C  CD   . LYS   A 1 97  ? -18.766 13.45   -6.988  1   19.948 ? 97  LYS   A CD   1 
ATOM   764  C  CE   . LYS   A 1 97  ? -19.042 13.15   -5.563  1   23.588 ? 97  LYS   A CE   1 
ATOM   765  N  NZ   . LYS   A 1 97  ? -18.949 11.71   -5.333  1   27.217 ? 97  LYS   A NZ   1 
ATOM   766  N  N    . THR   A 1 98  ? -19.311 17.722  -11.372 1   13.14  ? 98  THR   A N    1 
ATOM   767  C  CA   . THR   A 1 98  ? -18.884 18.032  -12.733 1   13.431 ? 98  THR   A CA   1 
ATOM   768  C  C    . THR   A 1 98  ? -17.554 18.776  -12.686 1   13.241 ? 98  THR   A C    1 
ATOM   769  O  O    . THR   A 1 98  ? -17.469 19.846  -12.091 1   14.699 ? 98  THR   A O    1 
ATOM   770  C  CB   . THR   A 1 98  ? -19.912 18.881  -13.481 1   13.206 ? 98  THR   A CB   1 
ATOM   771  O  OG1  . THR   A 1 98  ? -21.17  18.212  -13.465 1   13.401 ? 98  THR   A OG1  1 
ATOM   772  C  CG2  . THR   A 1 98  ? -19.5   19.148  -14.918 1   13.744 ? 98  THR   A CG2  1 
ATOM   773  N  N    . PRO   A 1 99  ? -16.489 18.263  -13.343 1   12.942 ? 99  PRO   A N    1 
ATOM   774  C  CA   . PRO   A 1 99  ? -15.214 18.97   -13.429 1   13.503 ? 99  PRO   A CA   1 
ATOM   775  C  C    . PRO   A 1 99  ? -15.264 20.027  -14.521 1   13.947 ? 99  PRO   A C    1 
ATOM   776  O  O    . PRO   A 1 99  ? -16.204 20.052  -15.305 1   14.318 ? 99  PRO   A O    1 
ATOM   777  C  CB   . PRO   A 1 99  ? -14.259 17.83   -13.792 1   13.901 ? 99  PRO   A CB   1 
ATOM   778  C  CG   . PRO   A 1 99  ? -15.087 16.963  -14.726 1   13.302 ? 99  PRO   A CG   1 
ATOM   779  C  CD   . PRO   A 1 99  ? -16.457 16.977  -14.058 1   12.692 ? 99  PRO   A CD   1 
ATOM   780  N  N    . LYS   A 1 100 ? -14.247 20.886  -14.584 1   14.303 ? 100 LYS   A N    1 
ATOM   781  C  CA   . LYS   A 1 100 ? -14.028 21.649  -15.804 1   15.047 ? 100 LYS   A CA   1 
ATOM   782  C  C    . LYS   A 1 100 ? -13.809 20.641  -16.924 1   14.218 ? 100 LYS   A C    1 
ATOM   783  O  O    . LYS   A 1 100 ? -13.042 19.706  -16.743 1   14.517 ? 100 LYS   A O    1 
ATOM   784  C  CB   . LYS   A 1 100 ? -12.796 22.554  -15.701 1   17.415 ? 100 LYS   A CB   1 
ATOM   785  C  CG   . LYS   A 1 100 ? -12.909 23.703  -14.712 1   20.803 ? 100 LYS   A CG   1 
ATOM   786  C  CD   . LYS   A 1 100 ? -11.827 24.77   -14.855 1   25.3   ? 100 LYS   A CD   1 
ATOM   787  C  CE   . LYS   A 1 100 ? -10.432 24.253  -15.03  1   30.252 ? 100 LYS   A CE   1 
ATOM   788  N  NZ   . LYS   A 1 100 ? -9.854  23.8    -13.762 1   34.164 ? 100 LYS   A NZ   1 
ATOM   789  N  N    . TYR   A 1 101 ? -14.483 20.818  -18.071 1   13.97  ? 101 TYR   A N    1 
ATOM   790  C  CA   . TYR   A 1 101 ? -14.384 19.823  -19.13  1   14.144 ? 101 TYR   A CA   1 
ATOM   791  C  C    . TYR   A 1 101 ? -14.629 20.446  -20.501 1   14.084 ? 101 TYR   A C    1 
ATOM   792  O  O    . TYR   A 1 101 ? -15.189 21.531  -20.634 1   14.399 ? 101 TYR   A O    1 
ATOM   793  C  CB   . TYR   A 1 101 ? -15.349 18.651  -18.926 1   13.857 ? 101 TYR   A CB   1 
ATOM   794  C  CG   . TYR   A 1 101 ? -16.794 19.006  -19.235 1   14.426 ? 101 TYR   A CG   1 
ATOM   795  C  CD1  . TYR   A 1 101 ? -17.594 19.611  -18.275 1   14.794 ? 101 TYR   A CD1  1 
ATOM   796  C  CD2  . TYR   A 1 101 ? -17.354 18.758  -20.485 1   15.251 ? 101 TYR   A CD2  1 
ATOM   797  C  CE1  . TYR   A 1 101 ? -18.908 19.952  -18.539 1   15.956 ? 101 TYR   A CE1  1 
ATOM   798  C  CE2  . TYR   A 1 101 ? -18.668 19.101  -20.765 1   15.983 ? 101 TYR   A CE2  1 
ATOM   799  C  CZ   . TYR   A 1 101 ? -19.445 19.705  -19.79  1   16.21  ? 101 TYR   A CZ   1 
ATOM   800  O  OH   . TYR   A 1 101 ? -20.752 20.051  -20.024 1   18.266 ? 101 TYR   A OH   1 
ATOM   801  N  N    . LYS   A 1 102 ? -14.177 19.708  -21.518 1   13.794 ? 102 LYS   A N    1 
ATOM   802  C  CA   . LYS   A 1 102 ? -14.466 20.012  -22.904 1   14.06  ? 102 LYS   A CA   1 
ATOM   803  C  C    . LYS   A 1 102 ? -14.519 18.702  -23.673 1   12.733 ? 102 LYS   A C    1 
ATOM   804  O  O    . LYS   A 1 102 ? -14.08  17.664  -23.179 1   12.8   ? 102 LYS   A O    1 
ATOM   805  C  CB   . LYS   A 1 102 ? -13.39  20.916  -23.507 1   16.829 ? 102 LYS   A CB   1 
ATOM   806  C  CG   . LYS   A 1 102 ? -11.99  20.346  -23.425 1   19.464 ? 102 LYS   A CG   1 
ATOM   807  C  CD   . LYS   A 1 102 ? -10.969 21.135  -24.227 1   22.791 ? 102 LYS   A CD   1 
ATOM   808  C  CE   . LYS   A 1 102 ? -10.878 22.542  -23.768 1   24.773 ? 102 LYS   A CE   1 
ATOM   809  N  NZ   . LYS   A 1 102 ? -9.898  23.25   -24.595 1   27.504 ? 102 LYS   A NZ   1 
ATOM   810  N  N    . PHE   A 1 103 ? -15.096 18.772  -24.874 1   11.679 ? 103 PHE   A N    1 
ATOM   811  C  CA   . PHE   A 1 103 ? -15.14  17.642  -25.778 1   12.171 ? 103 PHE   A CA   1 
ATOM   812  C  C    . PHE   A 1 103 ? -14.152 17.911  -26.911 1   12.744 ? 103 PHE   A C    1 
ATOM   813  O  O    . PHE   A 1 103 ? -14.173 18.994  -27.497 1   14.324 ? 103 PHE   A O    1 
ATOM   814  C  CB   . PHE   A 1 103 ? -16.544 17.433  -26.359 1   12.791 ? 103 PHE   A CB   1 
ATOM   815  C  CG   . PHE   A 1 103 ? -17.646 17.041  -25.393 1   12.901 ? 103 PHE   A CG   1 
ATOM   816  C  CD1  . PHE   A 1 103 ? -17.355 16.519  -24.136 1   12.621 ? 103 PHE   A CD1  1 
ATOM   817  C  CD2  . PHE   A 1 103 ? -18.984 17.135  -25.765 1   13.756 ? 103 PHE   A CD2  1 
ATOM   818  C  CE1  . PHE   A 1 103 ? -18.36  16.125  -23.27  1   12.8   ? 103 PHE   A CE1  1 
ATOM   819  C  CE2  . PHE   A 1 103 ? -19.986 16.748  -24.876 1   14.068 ? 103 PHE   A CE2  1 
ATOM   820  C  CZ   . PHE   A 1 103 ? -19.666 16.232  -23.642 1   13.561 ? 103 PHE   A CZ   1 
ATOM   821  N  N    . VAL   A 1 104 ? -13.286 16.934  -27.189 1   12.624 ? 104 VAL   A N    1 
ATOM   822  C  CA   . VAL   A 1 104 ? -12.304 17.069  -28.254 1   13.358 ? 104 VAL   A CA   1 
ATOM   823  C  C    . VAL   A 1 104 ? -12.308 15.799  -29.094 1   13.676 ? 104 VAL   A C    1 
ATOM   824  O  O    . VAL   A 1 104 ? -12.246 14.705  -28.557 1   14.864 ? 104 VAL   A O    1 
ATOM   825  C  CB   . VAL   A 1 104 ? -10.897 17.337  -27.684 1   14.827 ? 104 VAL   A CB   1 
ATOM   826  C  CG1  . VAL   A 1 104 ? -9.889  17.532  -28.799 1   15.728 ? 104 VAL   A CG1  1 
ATOM   827  C  CG2  . VAL   A 1 104 ? -10.867 18.548  -26.772 1   15.662 ? 104 VAL   A CG2  1 
ATOM   828  N  N    . ARG   A 1 105 ? -12.319 15.959  -30.424 1   12.99  ? 105 ARG   A N    1 
ATOM   829  C  CA   . ARG   A 1 105 ? -12.133 14.835  -31.328 1   12.77  ? 105 ARG   A CA   1 
ATOM   830  C  C    . ARG   A 1 105 ? -10.648 14.735  -31.661 1   12.814 ? 105 ARG   A C    1 
ATOM   831  O  O    . ARG   A 1 105 ? -10.054 15.723  -32.085 1   15.65  ? 105 ARG   A O    1 
ATOM   832  C  CB   . ARG   A 1 105 ? -12.942 15.038  -32.611 1   13.586 ? 105 ARG   A CB   1 
ATOM   833  C  CG   . ARG   A 1 105 ? -12.865 13.844  -33.554 1   13.92  ? 105 ARG   A CG   1 
ATOM   834  C  CD   . ARG   A 1 105 ? -13.671 14.053  -34.824 1   14.81  ? 105 ARG   A CD   1 
ATOM   835  N  NE   . ARG   A 1 105 ? -13.562 12.892  -35.714 1   15.4   ? 105 ARG   A NE   1 
ATOM   836  C  CZ   . ARG   A 1 105 ? -14.218 11.754  -35.608 1   15.49  ? 105 ARG   A CZ   1 
ATOM   837  N  NH1  . ARG   A 1 105 ? -15.131 11.602  -34.667 1   15.381 ? 105 ARG   A NH1  1 
ATOM   838  N  NH2  . ARG   A 1 105 ? -13.998 10.77   -36.466 1   16.897 ? 105 ARG   A NH2  1 
ATOM   839  N  N    . ILE   A 1 106 ? -10.083 13.547  -31.469 1   11.209 ? 106 ILE   A N    1 
ATOM   840  C  CA   . ILE   A 1 106 ? -8.653  13.362  -31.645 1   10.803 ? 106 ILE   A CA   1 
ATOM   841  C  C    . ILE   A 1 106 ? -8.343  12.749  -33.003 1   11.453 ? 106 ILE   A C    1 
ATOM   842  O  O    . ILE   A 1 106 ? -9.221  12.269  -33.716 1   12.44  ? 106 ILE   A O    1 
ATOM   843  C  CB   . ILE   A 1 106 ? -8.071  12.525  -30.488 1   10.816 ? 106 ILE   A CB   1 
ATOM   844  C  CG1  . ILE   A 1 106 ? -8.677  11.116  -30.414 1   12.018 ? 106 ILE   A CG1  1 
ATOM   845  C  CG2  . ILE   A 1 106 ? -8.203  13.306  -29.178 1   11.185 ? 106 ILE   A CG2  1 
ATOM   846  C  CD1  . ILE   A 1 106 ? -8.02   10.171  -29.424 1   12.664 ? 106 ILE   A CD1  1 
ATOM   847  N  N    . GLN   A 1 107 ? -7.055  12.796  -33.348 1   11.167 ? 107 GLN   A N    1 
ATOM   848  C  CA   . GLN   A 1 107 ? -6.541  12.208  -34.567 1   12.066 ? 107 GLN   A CA   1 
ATOM   849  C  C    . GLN   A 1 107 ? -5.813  10.901  -34.281 1   12.139 ? 107 GLN   A C    1 
ATOM   850  O  O    . GLN   A 1 107 ? -5.304  10.685  -33.181 1   12.418 ? 107 GLN   A O    1 
ATOM   851  C  CB   . GLN   A 1 107 ? -5.602  13.2    -35.253 1   13.414 ? 107 GLN   A CB   1 
ATOM   852  C  CG   . GLN   A 1 107 ? -6.306  14.444  -35.791 1   15.177 ? 107 GLN   A CG   1 
ATOM   853  C  CD   . GLN   A 1 107 ? -7.445  14.113  -36.73  1   18.005 ? 107 GLN   A CD   1 
ATOM   854  O  OE1  . GLN   A 1 107 ? -7.291  13.34   -37.677 1   20.72  ? 107 GLN   A OE1  1 
ATOM   855  N  NE2  . GLN   A 1 107 ? -8.618  14.658  -36.467 1   20.11  ? 107 GLN   A NE2  1 
ATOM   856  N  N    . PRO   A 1 108 ? -5.684  9.996   -35.269 1   12.78  ? 108 PRO   A N    1 
ATOM   857  C  CA   . PRO   A 1 108 ? -4.865  8.804   -35.103 1   13.429 ? 108 PRO   A CA   1 
ATOM   858  C  C    . PRO   A 1 108 ? -3.47   9.181   -34.624 1   12.833 ? 108 PRO   A C    1 
ATOM   859  O  O    . PRO   A 1 108 ? -2.891  10.163  -35.088 1   13.874 ? 108 PRO   A O    1 
ATOM   860  C  CB   . PRO   A 1 108 ? -4.841  8.159   -36.485 1   14.814 ? 108 PRO   A CB   1 
ATOM   861  C  CG   . PRO   A 1 108 ? -6.077  8.661   -37.137 1   16.077 ? 108 PRO   A CG   1 
ATOM   862  C  CD   . PRO   A 1 108 ? -6.31   10.063  -36.599 1   14.387 ? 108 PRO   A CD   1 
ATOM   863  N  N    . GLY   A 1 109 ? -2.975  8.384   -33.671 1   12.118 ? 109 GLY   A N    1 
ATOM   864  C  CA   . GLY   A 1 109 ? -1.676  8.574   -33.056 1   12.497 ? 109 GLY   A CA   1 
ATOM   865  C  C    . GLY   A 1 109 ? -1.784  9.183   -31.664 1   11.486 ? 109 GLY   A C    1 
ATOM   866  O  O    . GLY   A 1 109 ? -0.877  9.021   -30.842 1   12.454 ? 109 GLY   A O    1 
ATOM   867  N  N    . GLN   A 1 110 ? -2.889  9.883   -31.404 1   10.416 ? 110 GLN   A N    1 
ATOM   868  C  CA   . GLN   A 1 110 ? -3.09   10.508  -30.107 1   10.106 ? 110 GLN   A CA   1 
ATOM   869  C  C    . GLN   A 1 110 ? -3.4    9.457   -29.041 1   9.874  ? 110 GLN   A C    1 
ATOM   870  O  O    . GLN   A 1 110 ? -3.982  8.416   -29.33  1   10.162 ? 110 GLN   A O    1 
ATOM   871  C  CB   . GLN   A 1 110 ? -4.259  11.485  -30.218 1   10.362 ? 110 GLN   A CB   1 
ATOM   872  C  CG   . GLN   A 1 110 ? -4.537  12.254  -28.933 1   10.414 ? 110 GLN   A CG   1 
ATOM   873  C  CD   . GLN   A 1 110 ? -3.367  13.123  -28.538 1   10.818 ? 110 GLN   A CD   1 
ATOM   874  O  OE1  . GLN   A 1 110 ? -2.498  12.715  -27.757 1   11.417 ? 110 GLN   A OE1  1 
ATOM   875  N  NE2  . GLN   A 1 110 ? -3.302  14.317  -29.095 1   11.048 ? 110 GLN   A NE2  1 
ATOM   876  N  N    . THR   A 1 111 ? -2.974  9.748   -27.803 1   10.101 ? 111 THR   A N    1 
ATOM   877  C  CA   . THR   A 1 111 ? -3.212  8.864   -26.673 1   10.161 ? 111 THR   A CA   1 
ATOM   878  C  C    . THR   A 1 111 ? -4.235  9.487   -25.734 1   9.697  ? 111 THR   A C    1 
ATOM   879  O  O    . THR   A 1 111 ? -4.499  10.684  -25.769 1   9.766  ? 111 THR   A O    1 
ATOM   880  C  CB   . THR   A 1 111 ? -1.908  8.555   -25.935 1   10.569 ? 111 THR   A CB   1 
ATOM   881  O  OG1  . THR   A 1 111 ? -1.399  9.807   -25.49  1   10.62  ? 111 THR   A OG1  1 
ATOM   882  C  CG2  . THR   A 1 111 ? -0.956  7.791   -26.836 1   10.61  ? 111 THR   A CG2  1 
ATOM   883  N  N    . PHE   A 1 112 ? -4.767  8.639   -24.854 1   9.847  ? 112 PHE   A N    1 
ATOM   884  C  CA   . PHE   A 1 112 ? -5.727  9.056   -23.848 1   9.648  ? 112 PHE   A CA   1 
ATOM   885  C  C    . PHE   A 1 112 ? -5.829  7.949   -22.807 1   9.022  ? 112 PHE   A C    1 
ATOM   886  O  O    . PHE   A 1 112 ? -5.472  6.803   -23.046 1   9.219  ? 112 PHE   A O    1 
ATOM   887  C  CB   . PHE   A 1 112 ? -7.074  9.382   -24.494 1   10.017 ? 112 PHE   A CB   1 
ATOM   888  C  CG   . PHE   A 1 112 ? -7.672  8.275   -25.345 1   10.916 ? 112 PHE   A CG   1 
ATOM   889  C  CD1  . PHE   A 1 112 ? -7.357  8.164   -26.7   1   12.448 ? 112 PHE   A CD1  1 
ATOM   890  C  CD2  . PHE   A 1 112 ? -8.566  7.365   -24.805 1   11.866 ? 112 PHE   A CD2  1 
ATOM   891  C  CE1  . PHE   A 1 112 ? -7.917  7.161   -27.465 1   13.908 ? 112 PHE   A CE1  1 
ATOM   892  C  CE2  . PHE   A 1 112 ? -9.167  6.403   -25.593 1   13.258 ? 112 PHE   A CE2  1 
ATOM   893  C  CZ   . PHE   A 1 112 ? -8.84   6.303   -26.916 1   13.938 ? 112 PHE   A CZ   1 
ATOM   894  N  N    . SER   A 1 113 ? -6.385  8.325   -21.647 1   9.594  ? 113 SER   A N    1 
ATOM   895  C  CA   . SER   A 1 113 ? -6.7    7.407   -20.567 1   9.841  ? 113 SER   A CA   1 
ATOM   896  C  C    . SER   A 1 113 ? -8.119  6.887   -20.744 1   9.789  ? 113 SER   A C    1 
ATOM   897  O  O    . SER   A 1 113 ? -8.997  7.657   -21.116 1   10.854 ? 113 SER   A O    1 
ATOM   898  C  CB   . SER   A 1 113 ? -6.576  8.112   -19.243 1   10.308 ? 113 SER   A CB   1 
ATOM   899  O  OG   . SER   A 1 113 ? -5.284  8.686   -19.076 1   10.821 ? 113 SER   A OG   1 
ATOM   900  N  N    . VAL   A 1 114 ? -8.311  5.604   -20.449 1   9.721  ? 114 VAL   A N    1 
ATOM   901  C  CA   . VAL   A 1 114 ? -9.628  4.983   -20.468 1   9.993  ? 114 VAL   A CA   1 
ATOM   902  C  C    . VAL   A 1 114 ? -9.971  4.599   -19.037 1   9.903  ? 114 VAL   A C    1 
ATOM   903  O  O    . VAL   A 1 114 ? -9.163  3.961   -18.377 1   10.003 ? 114 VAL   A O    1 
ATOM   904  C  CB   . VAL   A 1 114 ? -9.638  3.736   -21.368 1   11.158 ? 114 VAL   A CB   1 
ATOM   905  C  CG1  . VAL   A 1 114 ? -10.909 2.927   -21.174 1   11.753 ? 114 VAL   A CG1  1 
ATOM   906  C  CG2  . VAL   A 1 114 ? -9.43   4.118   -22.825 1   11.97  ? 114 VAL   A CG2  1 
ATOM   907  N  N    . LEU   A 1 115 ? -11.175 4.968   -18.602 1   9.637  ? 115 LEU   A N    1 
ATOM   908  C  CA   . LEU   A 1 115 ? -11.713 4.484   -17.345 1   9.823  ? 115 LEU   A CA   1 
ATOM   909  C  C    . LEU   A 1 115 ? -12.757 3.415   -17.665 1   9.658  ? 115 LEU   A C    1 
ATOM   910  O  O    . LEU   A 1 115 ? -13.881 3.739   -18.057 1   10.053 ? 115 LEU   A O    1 
ATOM   911  C  CB   . LEU   A 1 115 ? -12.276 5.632   -16.512 1   10.267 ? 115 LEU   A CB   1 
ATOM   912  C  CG   . LEU   A 1 115 ? -12.88  5.216   -15.17  1   10.791 ? 115 LEU   A CG   1 
ATOM   913  C  CD1  . LEU   A 1 115 ? -11.771 4.759   -14.238 1   10.987 ? 115 LEU   A CD1  1 
ATOM   914  C  CD2  . LEU   A 1 115 ? -13.668 6.361   -14.586 1   11.347 ? 115 LEU   A CD2  1 
ATOM   915  N  N    . ALA   A 1 116 ? -12.361 2.144   -17.556 1   9.734  ? 116 ALA   A N    1 
ATOM   916  C  CA   . ALA   A 1 116 ? -13.265 1.039   -17.842 1   10.528 ? 116 ALA   A CA   1 
ATOM   917  C  C    . ALA   A 1 116 ? -14.273 0.932   -16.711 1   10.709 ? 116 ALA   A C    1 
ATOM   918  O  O    . ALA   A 1 116 ? -13.866 0.888   -15.553 1   12.167 ? 116 ALA   A O    1 
ATOM   919  C  CB   . ALA   A 1 116 ? -12.506 -0.25   -18.034 1   11.516 ? 116 ALA   A CB   1 
ATOM   920  N  N    . CYS   A 1 117 ? -15.558 0.878   -17.067 1   10.486 ? 117 CYS   A N    1 
ATOM   921  C  CA   . CYS   A 1 117 ? -16.634 0.873   -16.101 1   11     ? 117 CYS   A CA   1 
ATOM   922  C  C    . CYS   A 1 117 ? -17.68  -0.176  -16.456 1   10.747 ? 117 CYS   A C    1 
ATOM   923  O  O    . CYS   A 1 117 ? -17.882 -0.501  -17.618 1   10.985 ? 117 CYS   A O    1 
ATOM   924  C  CB   . CYS   A 1 117 ? -17.37  2.201   -16.11  1   12.299 ? 117 CYS   A CB   1 
ATOM   925  S  SG   . CYS   A 1 117 ? -16.373 3.576   -15.499 1   14.112 ? 117 CYS   A SG   1 
ATOM   926  N  N    . TYR   A 1 118 ? -18.353 -0.665  -15.412 1   11.191 ? 118 TYR   A N    1 
ATOM   927  C  CA   . TYR   A 1 118 ? -19.426 -1.64   -15.515 1   12.028 ? 118 TYR   A CA   1 
ATOM   928  C  C    . TYR   A 1 118 ? -20.519 -1.206  -14.548 1   13.063 ? 118 TYR   A C    1 
ATOM   929  O  O    . TYR   A 1 118 ? -20.215 -0.902  -13.397 1   13.402 ? 118 TYR   A O    1 
ATOM   930  C  CB   . TYR   A 1 118 ? -18.924 -3.054  -15.188 1   12.252 ? 118 TYR   A CB   1 
ATOM   931  C  CG   . TYR   A 1 118 ? -17.823 -3.451  -16.149 1   12.029 ? 118 TYR   A CG   1 
ATOM   932  C  CD1  . TYR   A 1 118 ? -18.14  -4.053  -17.355 1   12.485 ? 118 TYR   A CD1  1 
ATOM   933  C  CD2  . TYR   A 1 118 ? -16.496 -3.157  -15.886 1   12.265 ? 118 TYR   A CD2  1 
ATOM   934  C  CE1  . TYR   A 1 118 ? -17.173 -4.325  -18.294 1   12.458 ? 118 TYR   A CE1  1 
ATOM   935  C  CE2  . TYR   A 1 118 ? -15.512 -3.435  -16.82  1   11.732 ? 118 TYR   A CE2  1 
ATOM   936  C  CZ   . TYR   A 1 118 ? -15.849 -4.034  -18.02  1   12.126 ? 118 TYR   A CZ   1 
ATOM   937  O  OH   . TYR   A 1 118 ? -14.889 -4.276  -18.948 1   12.541 ? 118 TYR   A OH   1 
ATOM   938  N  N    . ASN   A 1 119 ? -21.761 -1.118  -15.032 1   14.137 ? 119 ASN   A N    1 
ATOM   939  C  CA   . ASN   A 1 119 ? -22.892 -0.776  -14.177 1   14.956 ? 119 ASN   A CA   1 
ATOM   940  C  C    . ASN   A 1 119 ? -22.68  0.564   -13.477 1   14.379 ? 119 ASN   A C    1 
ATOM   941  O  O    . ASN   A 1 119 ? -23.114 0.765   -12.333 1   16.009 ? 119 ASN   A O    1 
ATOM   942  C  CB   . ASN   A 1 119 ? -23.176 -1.885  -13.176 1   17.019 ? 119 ASN   A CB   1 
ATOM   943  C  CG   . ASN   A 1 119 ? -23.617 -3.135  -13.891 1   19.432 ? 119 ASN   A CG   1 
ATOM   944  O  OD1  . ASN   A 1 119 ? -22.876 -4.119  -13.931 1   22.998 ? 119 ASN   A OD1  1 
ATOM   945  N  ND2  . ASN   A 1 119 ? -24.798 -3.092  -14.494 1   21.273 ? 119 ASN   A ND2  1 
ATOM   946  N  N    . GLY   A 1 120 ? -22.021 1.485   -14.175 1   13.582 ? 120 GLY   A N    1 
ATOM   947  C  CA   . GLY   A 1 120 ? -21.776 2.83    -13.685 1   13.973 ? 120 GLY   A CA   1 
ATOM   948  C  C    . GLY   A 1 120 ? -20.637 2.921   -12.664 1   14.318 ? 120 GLY   A C    1 
ATOM   949  O  O    . GLY   A 1 120 ? -20.403 3.997   -12.132 1   15.894 ? 120 GLY   A O    1 
ATOM   950  N  N    . SER   A 1 121 ? -19.928 1.81    -12.411 1   14.258 ? 121 SER   A N    1 
ATOM   951  C  CA   . SER   A 1 121 ? -18.875 1.759   -11.408 1   15.147 ? 121 SER   A CA   1 
ATOM   952  C  C    . SER   A 1 121 ? -17.517 1.531   -12.065 1   14.877 ? 121 SER   A C    1 
ATOM   953  O  O    . SER   A 1 121 ? -17.355 0.634   -12.882 1   13.831 ? 121 SER   A O    1 
ATOM   954  C  CB   . SER   A 1 121 ? -19.171 0.675   -10.412 1   16.95  ? 121 SER   A CB   1 
ATOM   955  O  OG   . SER   A 1 121 ? -20.294 1.021   -9.613  1   20.171 ? 121 SER   A OG   1 
ATOM   956  N  N    . PRO   A 1 122 ? -16.467 2.281   -11.681 1   15.552 ? 122 PRO   A N    1 
ATOM   957  C  CA   . PRO   A 1 122 ? -15.166 2.118   -12.322 1   15.744 ? 122 PRO   A CA   1 
ATOM   958  C  C    . PRO   A 1 122 ? -14.464 0.823   -11.924 1   15.166 ? 122 PRO   A C    1 
ATOM   959  O  O    . PRO   A 1 122 ? -14.444 0.441   -10.755 1   16.622 ? 122 PRO   A O    1 
ATOM   960  C  CB   . PRO   A 1 122 ? -14.438 3.374   -11.841 1   17.247 ? 122 PRO   A CB   1 
ATOM   961  C  CG   . PRO   A 1 122 ? -14.929 3.488   -10.435 1   18.225 ? 122 PRO   A CG   1 
ATOM   962  C  CD   . PRO   A 1 122 ? -16.437 3.291   -10.614 1   18.375 ? 122 PRO   A CD   1 
ATOM   963  N  N    . SER   A 1 123 ? -13.801 0.205   -12.908 1   14.235 ? 123 SER   A N    1 
ATOM   964  C  CA   . SER   A 1 123 ? -13.033 -1.016  -12.73  1   15.215 ? 123 SER   A CA   1 
ATOM   965  C  C    . SER   A 1 123 ? -11.529 -0.724  -12.729 1   13.547 ? 123 SER   A C    1 
ATOM   966  O  O    . SER   A 1 123 ? -10.775 -1.269  -11.923 1   14.351 ? 123 SER   A O    1 
ATOM   967  C  CB   . SER   A 1 123 ? -13.409 -2.019  -13.802 1   17.827 ? 123 SER   A CB   1 
ATOM   968  O  OG   . SER   A 1 123 ? -12.616 -3.201  -13.747 1   23.187 ? 123 SER   A OG   1 
ATOM   969  N  N    . GLY   A 1 124 ? -11.084 0.156   -13.623 1   12.267 ? 124 GLY   A N    1 
ATOM   970  C  CA   . GLY   A 1 124 ? -9.659  0.376   -13.784 1   12.037 ? 124 GLY   A CA   1 
ATOM   971  C  C    . GLY   A 1 124 ? -9.389  1.457   -14.819 1   11.183 ? 124 GLY   A C    1 
ATOM   972  O  O    . GLY   A 1 124 ? -10.286 1.836   -15.577 1   11.572 ? 124 GLY   A O    1 
ATOM   973  N  N    . VAL   A 1 125 ? -8.141  1.912   -14.833 1   10.98  ? 125 VAL   A N    1 
ATOM   974  C  CA   . VAL   A 1 125 ? -7.713  2.969   -15.72  1   11.493 ? 125 VAL   A CA   1 
ATOM   975  C  C    . VAL   A 1 125 ? -6.439  2.519   -16.433 1   11.372 ? 125 VAL   A C    1 
ATOM   976  O  O    . VAL   A 1 125 ? -5.558  1.908   -15.825 1   12.117 ? 125 VAL   A O    1 
ATOM   977  C  CB   . VAL   A 1 125 ? -7.565  4.323   -14.995 1   13.453 ? 125 VAL   A CB   1 
ATOM   978  C  CG1  . VAL   A 1 125 ? -6.515  4.328   -13.892 1   15.134 ? 125 VAL   A CG1  1 
ATOM   979  C  CG2  . VAL   A 1 125 ? -7.323  5.467   -15.969 1   13.795 ? 125 VAL   A CG2  1 
ATOM   980  N  N    . TYR   A 1 126 ? -6.372  2.796   -17.739 1   10.474 ? 126 TYR   A N    1 
ATOM   981  C  CA   . TYR   A 1 126 ? -5.202  2.467   -18.534 1   10.923 ? 126 TYR   A CA   1 
ATOM   982  C  C    . TYR   A 1 126 ? -5.076  3.424   -19.711 1   11.021 ? 126 TYR   A C    1 
ATOM   983  O  O    . TYR   A 1 126 ? -6.023  4.104   -20.079 1   11.723 ? 126 TYR   A O    1 
ATOM   984  C  CB   . TYR   A 1 126 ? -5.245  1.021   -19.034 1   11.242 ? 126 TYR   A CB   1 
ATOM   985  C  CG   . TYR   A 1 126 ? -6.511  0.64    -19.78  1   11.798 ? 126 TYR   A CG   1 
ATOM   986  C  CD1  . TYR   A 1 126 ? -6.645  0.842   -21.154 1   12.173 ? 126 TYR   A CD1  1 
ATOM   987  C  CD2  . TYR   A 1 126 ? -7.578  0.063   -19.119 1   12.864 ? 126 TYR   A CD2  1 
ATOM   988  C  CE1  . TYR   A 1 126 ? -7.809  0.5     -21.824 1   13.279 ? 126 TYR   A CE1  1 
ATOM   989  C  CE2  . TYR   A 1 126 ? -8.734  -0.305  -19.781 1   13.403 ? 126 TYR   A CE2  1 
ATOM   990  C  CZ   . TYR   A 1 126 ? -8.852  -0.088  -21.137 1   13.874 ? 126 TYR   A CZ   1 
ATOM   991  O  OH   . TYR   A 1 126 ? -9.999  -0.453  -21.787 1   16.098 ? 126 TYR   A OH   1 
ATOM   992  N  N    . GLN   A 1 127 ? -3.884  3.419   -20.325 1   11.474 ? 127 GLN   A N    1 
ATOM   993  C  CA   . GLN   A 1 127 ? -3.607  4.248   -21.487 1   12.214 ? 127 GLN   A CA   1 
ATOM   994  C  C    . GLN   A 1 127 ? -3.907  3.485   -22.778 1   12.837 ? 127 GLN   A C    1 
ATOM   995  O  O    . GLN   A 1 127 ? -3.611  2.3     -22.882 1   14.023 ? 127 GLN   A O    1 
ATOM   996  C  CB   . GLN   A 1 127 ? -2.122  4.59    -21.612 1   12.943 ? 127 GLN   A CB   1 
ATOM   997  C  CG   . GLN   A 1 127 ? -1.656  5.743   -20.743 1   13.409 ? 127 GLN   A CG   1 
ATOM   998  C  CD   . GLN   A 1 127 ? -2.404  7.017   -21.037 1   13.344 ? 127 GLN   A CD   1 
ATOM   999  O  OE1  . GLN   A 1 127 ? -3.416  7.279   -20.392 1   12.448 ? 127 GLN   A OE1  1 
ATOM   1000 N  NE2  . GLN   A 1 127 ? -1.893  7.825   -21.953 1   13.917 ? 127 GLN   A NE2  1 
ATOM   1001 N  N    . CYS   A 1 128 ? -4.422  4.225   -23.765 1   13.267 ? 128 CYS   A N    1 
ATOM   1002 C  CA   . CYS   A 1 128 ? -4.709  3.733   -25.109 1   14.388 ? 128 CYS   A CA   1 
ATOM   1003 C  C    . CYS   A 1 128 ? -4.217  4.75    -26.131 1   13.719 ? 128 CYS   A C    1 
ATOM   1004 O  O    . CYS   A 1 128 ? -4.04   5.913   -25.813 1   15.591 ? 128 CYS   A O    1 
ATOM   1005 C  CB   . CYS   A 1 128 ? -6.212  3.592   -25.349 1   17.924 ? 128 CYS   A CB   1 
ATOM   1006 S  SG   . CYS   A 1 128 ? -6.812  1.956   -24.89  1   24.228 ? 128 CYS   A SG   1 
ATOM   1007 N  N    . ALA   A 1 129 ? -4.002  4.296   -27.37  1   14.304 ? 129 ALA   A N    1 
ATOM   1008 C  CA   . ALA   A 1 129 ? -3.795  5.204   -28.491 1   13.203 ? 129 ALA   A CA   1 
ATOM   1009 C  C    . ALA   A 1 129 ? -4.882  4.968   -29.527 1   12.432 ? 129 ALA   A C    1 
ATOM   1010 O  O    . ALA   A 1 129 ? -5.319  3.842   -29.728 1   13.535 ? 129 ALA   A O    1 
ATOM   1011 C  CB   . ALA   A 1 129 ? -2.437  5.019   -29.131 1   13.784 ? 129 ALA   A CB   1 
ATOM   1012 N  N    . MET   A 1 130 ? -5.263  6.035   -30.218 1   11.326 ? 130 MET   A N    1 
ATOM   1013 C  CA   . MET   A 1 130 ? -6.076  5.888   -31.411 1   11.625 ? 130 MET   A CA   1 
ATOM   1014 C  C    . MET   A 1 130 ? -5.177  5.348   -32.524 1   11.3   ? 130 MET   A C    1 
ATOM   1015 O  O    . MET   A 1 130 ? -4.222  5.999   -32.921 1   11.589 ? 130 MET   A O    1 
ATOM   1016 C  CB   . MET   A 1 130 ? -6.696  7.235   -31.789 1   12.666 ? 130 MET   A CB   1 
ATOM   1017 C  CG   . MET   A 1 130 ? -7.599  7.156   -33.002 1   13.607 ? 130 MET   A CG   1 
ATOM   1018 S  SD   . MET   A 1 130 ? -9.041  6.089   -32.864 1   16.093 ? 130 MET   A SD   1 
ATOM   1019 C  CE   . MET   A 1 130 ? -9.887  6.885   -31.491 1   14.202 ? 130 MET   A CE   1 
ATOM   1020 N  N    . ARG   A 1 131 ? -5.434  4.119   -32.968 1   10.987 ? 131 ARG   A N    1 
ATOM   1021 C  CA   . ARG   A 1 131 ? -4.612  3.499   -33.993 1   11.361 ? 131 ARG   A CA   1 
ATOM   1022 C  C    . ARG   A 1 131 ? -4.851  4.172   -35.346 1   11.652 ? 131 ARG   A C    1 
ATOM   1023 O  O    . ARG   A 1 131 ? -5.886  4.789   -35.595 1   11.861 ? 131 ARG   A O    1 
ATOM   1024 C  CB   . ARG   A 1 131 ? -4.938  2.011   -34.112 1   11.713 ? 131 ARG   A CB   1 
ATOM   1025 C  CG   . ARG   A 1 131 ? -4.771  1.165   -32.859 1   11.808 ? 131 ARG   A CG   1 
ATOM   1026 C  CD   . ARG   A 1 131 ? -3.401  1.316   -32.212 1   11.943 ? 131 ARG   A CD   1 
ATOM   1027 N  NE   . ARG   A 1 131 ? -2.345  0.973   -33.167 1   12.342 ? 131 ARG   A NE   1 
ATOM   1028 C  CZ   . ARG   A 1 131 ? -1.045  1.12    -32.923 1   12.187 ? 131 ARG   A CZ   1 
ATOM   1029 N  NH1  . ARG   A 1 131 ? -0.622  1.462   -31.72  1   11.939 ? 131 ARG   A NH1  1 
ATOM   1030 N  NH2  . ARG   A 1 131 ? -0.161  0.892   -33.871 1   12.895 ? 131 ARG   A NH2  1 
ATOM   1031 N  N    . PRO   A 1 132 ? -3.887  4.051   -36.285 1   12.109 ? 132 PRO   A N    1 
ATOM   1032 C  CA   . PRO   A 1 132 ? -4.09   4.549   -37.647 1   12.097 ? 132 PRO   A CA   1 
ATOM   1033 C  C    . PRO   A 1 132 ? -5.357  4.05    -38.329 1   12.218 ? 132 PRO   A C    1 
ATOM   1034 O  O    . PRO   A 1 132 ? -5.894  4.742   -39.19  1   14.507 ? 132 PRO   A O    1 
ATOM   1035 C  CB   . PRO   A 1 132 ? -2.805  4.09    -38.347 1   12.319 ? 132 PRO   A CB   1 
ATOM   1036 C  CG   . PRO   A 1 132 ? -1.768  4.145   -37.248 1   12.475 ? 132 PRO   A CG   1 
ATOM   1037 C  CD   . PRO   A 1 132 ? -2.506  3.585   -36.054 1   12.322 ? 132 PRO   A CD   1 
ATOM   1038 N  N    . ASN   A 1 133 ? -5.839  2.863   -37.964 1   12.223 ? 133 ASN   A N    1 
ATOM   1039 C  CA   . ASN   A 1 133 ? -7.065  2.323   -38.544 1   12.999 ? 133 ASN   A CA   1 
ATOM   1040 C  C    . ASN   A 1 133 ? -8.307  2.68    -37.714 1   13.67  ? 133 ASN   A C    1 
ATOM   1041 O  O    . ASN   A 1 133 ? -9.379  2.109   -37.931 1   14.296 ? 133 ASN   A O    1 
ATOM   1042 C  CB   . ASN   A 1 133 ? -6.969  0.812   -38.717 1   14.063 ? 133 ASN   A CB   1 
ATOM   1043 C  CG   . ASN   A 1 133 ? -6.93   0.043   -37.417 1   14.587 ? 133 ASN   A CG   1 
ATOM   1044 O  OD1  . ASN   A 1 133 ? -7.003  0.629   -36.33  1   15.083 ? 133 ASN   A OD1  1 
ATOM   1045 N  ND2  . ASN   A 1 133 ? -6.831  -1.272  -37.509 1   16.282 ? 133 ASN   A ND2  1 
ATOM   1046 N  N    . PHE   A 1 134 ? -8.165  3.645   -36.794 1   13.276 ? 134 PHE   A N    1 
ATOM   1047 C  CA   . PHE   A 1 134 ? -9.286  4.247   -36.068 1   13.677 ? 134 PHE   A CA   1 
ATOM   1048 C  C    . PHE   A 1 134 ? -9.945  3.268   -35.092 1   14.058 ? 134 PHE   A C    1 
ATOM   1049 O  O    . PHE   A 1 134 ? -11.104 3.471   -34.707 1   16.961 ? 134 PHE   A O    1 
ATOM   1050 C  CB   . PHE   A 1 134 ? -10.349 4.819   -37.006 1   15.072 ? 134 PHE   A CB   1 
ATOM   1051 C  CG   . PHE   A 1 134 ? -9.832  5.95    -37.877 1   17.55  ? 134 PHE   A CG   1 
ATOM   1052 C  CD1  . PHE   A 1 134 ? -9.697  7.238   -37.376 1   20.006 ? 134 PHE   A CD1  1 
ATOM   1053 C  CD2  . PHE   A 1 134 ? -9.51   5.716   -39.205 1   19.547 ? 134 PHE   A CD2  1 
ATOM   1054 C  CE1  . PHE   A 1 134 ? -9.23   8.261   -38.191 1   22.164 ? 134 PHE   A CE1  1 
ATOM   1055 C  CE2  . PHE   A 1 134 ? -9.045  6.739   -40.016 1   21.17  ? 134 PHE   A CE2  1 
ATOM   1056 C  CZ   . PHE   A 1 134 ? -8.904  8.006   -39.504 1   22.418 ? 134 PHE   A CZ   1 
ATOM   1057 N  N    . THR   A 1 135 ? -9.186  2.267   -34.642 1   13.136 ? 135 THR   A N    1 
ATOM   1058 C  CA   . THR   A 1 135 ? -9.584  1.42    -33.529 1   12.689 ? 135 THR   A CA   1 
ATOM   1059 C  C    . THR   A 1 135 ? -8.686  1.726   -32.339 1   12.161 ? 135 THR   A C    1 
ATOM   1060 O  O    . THR   A 1 135 ? -7.662  2.387   -32.48  1   12.381 ? 135 THR   A O    1 
ATOM   1061 C  CB   . THR   A 1 135 ? -9.503  -0.064  -33.894 1   13.869 ? 135 THR   A CB   1 
ATOM   1062 O  OG1  . THR   A 1 135 ? -8.142  -0.422  -34.125 1   14.711 ? 135 THR   A OG1  1 
ATOM   1063 C  CG2  . THR   A 1 135 ? -10.355 -0.398  -35.108 1   15.264 ? 135 THR   A CG2  1 
ATOM   1064 N  N    . ILE   A 1 136 ? -9.071  1.187   -31.176 1   11.803 ? 136 ILE   A N    1 
ATOM   1065 C  CA   . ILE   A 1 136 ? -8.184  1.204   -30.024 1   12.153 ? 136 ILE   A CA   1 
ATOM   1066 C  C    . ILE   A 1 136 ? -8.017  -0.222  -29.522 1   11.826 ? 136 ILE   A C    1 
ATOM   1067 O  O    . ILE   A 1 136 ? -8.884  -1.064  -29.693 1   12.336 ? 136 ILE   A O    1 
ATOM   1068 C  CB   . ILE   A 1 136 ? -8.648  2.18    -28.925 1   13.457 ? 136 ILE   A CB   1 
ATOM   1069 C  CG1  . ILE   A 1 136 ? -9.857  1.686   -28.141 1   13.157 ? 136 ILE   A CG1  1 
ATOM   1070 C  CG2  . ILE   A 1 136 ? -8.878  3.577   -29.502 1   14.676 ? 136 ILE   A CG2  1 
ATOM   1071 C  CD1  . ILE   A 1 136 ? -10.233 2.583   -26.975 1   13.237 ? 136 ILE   A CD1  1 
ATOM   1072 N  N    . LYS   A 1 137 ? -6.861  -0.493  -28.917 1   12.556 ? 137 LYS   A N    1 
ATOM   1073 C  CA   . LYS   A 1 137 ? -6.554  -1.8    -28.368 1   14.017 ? 137 LYS   A CA   1 
ATOM   1074 C  C    . LYS   A 1 137 ? -6.742  -1.706  -26.862 1   13.714 ? 137 LYS   A C    1 
ATOM   1075 O  O    . LYS   A 1 137 ? -5.806  -1.414  -26.119 1   14.658 ? 137 LYS   A O    1 
ATOM   1076 C  CB   . LYS   A 1 137 ? -5.132  -2.217  -28.761 1   15.866 ? 137 LYS   A CB   1 
ATOM   1077 C  CG   . LYS   A 1 137 ? -5.007  -2.414  -30.264 1   18.654 ? 137 LYS   A CG   1 
ATOM   1078 C  CD   . LYS   A 1 137 ? -3.61   -2.673  -30.81  1   23.792 ? 137 LYS   A CD   1 
ATOM   1079 C  CE   . LYS   A 1 137 ? -2.904  -3.82   -30.184 1   27.456 ? 137 LYS   A CE   1 
ATOM   1080 N  NZ   . LYS   A 1 137 ? -1.639  -4.031  -30.892 1   31.469 ? 137 LYS   A NZ   1 
ATOM   1081 N  N    . GLY   A 1 138 ? -7.985  -1.88   -26.437 1   14.048 ? 138 GLY   A N    1 
ATOM   1082 C  CA   . GLY   A 1 138 ? -8.332  -1.69   -25.044 1   13.94  ? 138 GLY   A CA   1 
ATOM   1083 C  C    . GLY   A 1 138 ? -8.518  -3.009  -24.313 1   13.104 ? 138 GLY   A C    1 
ATOM   1084 O  O    . GLY   A 1 138 ? -8.08   -4.064  -24.751 1   14.181 ? 138 GLY   A O    1 
ATOM   1085 N  N    . SER   A 1 139 ? -9.188  -2.9    -23.165 1   11.781 ? 139 SER   A N    1 
ATOM   1086 C  CA   . SER   A 1 139 ? -9.568  -4.025  -22.339 1   12.479 ? 139 SER   A CA   1 
ATOM   1087 C  C    . SER   A 1 139 ? -10.993 -3.763  -21.867 1   11.924 ? 139 SER   A C    1 
ATOM   1088 O  O    . SER   A 1 139 ? -11.228 -2.91   -21.015 1   11.969 ? 139 SER   A O    1 
ATOM   1089 C  CB   . SER   A 1 139 ? -8.625  -4.16   -21.19  1   13.372 ? 139 SER   A CB   1 
ATOM   1090 O  OG   . SER   A 1 139 ? -9.045  -5.193  -20.327 1   14.881 ? 139 SER   A OG   1 
ATOM   1091 N  N    . PHE   A 1 140 ? -11.937 -4.393  -22.559 1   11.466 ? 140 PHE   A N    1 
ATOM   1092 C  CA   . PHE   A 1 140 ? -13.349 -4.12   -22.369 1   11.559 ? 140 PHE   A CA   1 
ATOM   1093 C  C    . PHE   A 1 140 ? -14.116 -5.429  -22.454 1   12.345 ? 140 PHE   A C    1 
ATOM   1094 O  O    . PHE   A 1 140 ? -13.922 -6.184  -23.397 1   13.22  ? 140 PHE   A O    1 
ATOM   1095 C  CB   . PHE   A 1 140 ? -13.861 -3.207  -23.474 1   11.869 ? 140 PHE   A CB   1 
ATOM   1096 C  CG   . PHE   A 1 140 ? -13.366 -1.777  -23.512 1   12.657 ? 140 PHE   A CG   1 
ATOM   1097 C  CD1  . PHE   A 1 140 ? -13.725 -0.865  -22.534 1   14.371 ? 140 PHE   A CD1  1 
ATOM   1098 C  CD2  . PHE   A 1 140 ? -12.56  -1.324  -24.546 1   14.222 ? 140 PHE   A CD2  1 
ATOM   1099 C  CE1  . PHE   A 1 140 ? -13.345 0.467   -22.626 1   15.675 ? 140 PHE   A CE1  1 
ATOM   1100 C  CE2  . PHE   A 1 140 ? -12.144 -0.009  -24.606 1   15.071 ? 140 PHE   A CE2  1 
ATOM   1101 C  CZ   . PHE   A 1 140 ? -12.558 0.887   -23.667 1   15.165 ? 140 PHE   A CZ   1 
ATOM   1102 N  N    . LEU   A 1 141 ? -15.044 -5.62   -21.511 1   12.145 ? 141 LEU   A N    1 
ATOM   1103 C  CA   . LEU   A 1 141 ? -15.899 -6.79   -21.461 1   13.268 ? 141 LEU   A CA   1 
ATOM   1104 C  C    . LEU   A 1 141 ? -17.35  -6.364  -21.672 1   13.259 ? 141 LEU   A C    1 
ATOM   1105 O  O    . LEU   A 1 141 ? -17.665 -5.181  -21.727 1   12.257 ? 141 LEU   A O    1 
ATOM   1106 C  CB   . LEU   A 1 141 ? -15.755 -7.487  -20.113 1   14.535 ? 141 LEU   A CB   1 
ATOM   1107 C  CG   . LEU   A 1 141 ? -14.345 -7.912  -19.717 1   15.881 ? 141 LEU   A CG   1 
ATOM   1108 C  CD1  . LEU   A 1 141 ? -14.351 -8.302  -18.257 1   16.195 ? 141 LEU   A CD1  1 
ATOM   1109 C  CD2  . LEU   A 1 141 ? -13.901 -9.042  -20.579 1   16.753 ? 141 LEU   A CD2  1 
ATOM   1110 N  N    . ASN   A 1 142 ? -18.227 -7.358  -21.773 1   14.422 ? 142 ASN   A N    1 
ATOM   1111 C  CA   . ASN   A 1 142 ? -19.657 -7.117  -21.782 1   15.173 ? 142 ASN   A CA   1 
ATOM   1112 C  C    . ASN   A 1 142 ? -20.037 -6.178  -20.634 1   14.162 ? 142 ASN   A C    1 
ATOM   1113 O  O    . ASN   A 1 142 ? -19.633 -6.404  -19.489 1   14.974 ? 142 ASN   A O    1 
ATOM   1114 C  CB   . ASN   A 1 142 ? -20.387 -8.445  -21.673 1   17.728 ? 142 ASN   A CB   1 
ATOM   1115 C  CG   . ASN   A 1 142 ? -21.878 -8.273  -21.739 1   20.753 ? 142 ASN   A CG   1 
ATOM   1116 O  OD1  . ASN   A 1 142 ? -22.368 -7.555  -22.611 1   22.186 ? 142 ASN   A OD1  1 
ATOM   1117 N  ND2  . ASN   A 1 142 ? -22.595 -8.907  -20.823 1   24.862 ? 142 ASN   A ND2  1 
ATOM   1118 N  N    . GLY   A 1 143 ? -20.776 -5.109  -20.963 1   12.907 ? 143 GLY   A N    1 
ATOM   1119 C  CA   . GLY   A 1 143 ? -21.214 -4.134  -19.97  1   12.833 ? 143 GLY   A CA   1 
ATOM   1120 C  C    . GLY   A 1 143 ? -20.377 -2.857  -19.939 1   11.696 ? 143 GLY   A C    1 
ATOM   1121 O  O    . GLY   A 1 143 ? -20.692 -1.945  -19.178 1   12.179 ? 143 GLY   A O    1 
ATOM   1122 N  N    . SER   A 1 144 ? -19.308 -2.783  -20.754 1   10.741 ? 144 SER   A N    1 
ATOM   1123 C  CA   . SER   A 1 144 ? -18.385 -1.655  -20.708 1   10.779 ? 144 SER   A CA   1 
ATOM   1124 C  C    . SER   A 1 144 ? -18.789 -0.496  -21.614 1   10.198 ? 144 SER   A C    1 
ATOM   1125 O  O    . SER   A 1 144 ? -18.141 0.546   -21.612 1   9.807  ? 144 SER   A O    1 
ATOM   1126 C  CB   . SER   A 1 144 ? -16.986 -2.091  -21.057 1   11.086 ? 144 SER   A CB   1 
ATOM   1127 O  OG   . SER   A 1 144 ? -16.943 -2.604  -22.379 1   11.436 ? 144 SER   A OG   1 
ATOM   1128 N  N    . CYS   A 1 145 ? -19.856 -0.664  -22.408 1   10.644 ? 145 CYS   A N    1 
ATOM   1129 C  CA   . CYS   A 1 145 ? -20.236 0.407   -23.311 1   10.781 ? 145 CYS   A CA   1 
ATOM   1130 C  C    . CYS   A 1 145 ? -20.552 1.672   -22.525 1   9.905  ? 145 CYS   A C    1 
ATOM   1131 O  O    . CYS   A 1 145 ? -21.129 1.616   -21.431 1   10.187 ? 145 CYS   A O    1 
ATOM   1132 C  CB   . CYS   A 1 145 ? -21.405 0.011   -24.192 1   11.603 ? 145 CYS   A CB   1 
ATOM   1133 S  SG   . CYS   A 1 145 ? -21.095 -1.427  -25.243 1   14.199 ? 145 CYS   A SG   1 
ATOM   1134 N  N    . GLY   A 1 146 ? -20.145 2.809   -23.078 1   9.45   ? 146 GLY   A N    1 
ATOM   1135 C  CA   . GLY   A 1 146 ? -20.299 4.111   -22.462 1   9.6    ? 146 GLY   A CA   1 
ATOM   1136 C  C    . GLY   A 1 146 ? -19.127 4.493   -21.559 1   9.391  ? 146 GLY   A C    1 
ATOM   1137 O  O    . GLY   A 1 146 ? -19.067 5.629   -21.107 1   10.351 ? 146 GLY   A O    1 
ATOM   1138 N  N    . SER   A 1 147 ? -18.186 3.571   -21.336 1   9.644  ? 147 SER   A N    1 
ATOM   1139 C  CA   . SER   A 1 147 ? -16.902 3.939   -20.752 1   9.664  ? 147 SER   A CA   1 
ATOM   1140 C  C    . SER   A 1 147 ? -16.247 4.993   -21.64  1   9.617  ? 147 SER   A C    1 
ATOM   1141 O  O    . SER   A 1 147 ? -16.418 4.966   -22.877 1   10.157 ? 147 SER   A O    1 
ATOM   1142 C  CB   . SER   A 1 147 ? -15.974 2.751   -20.613 1   10.09  ? 147 SER   A CB   1 
ATOM   1143 O  OG   . SER   A 1 147 ? -16.471 1.737   -19.752 1   10.147 ? 147 SER   A OG   1 
ATOM   1144 N  N    . VAL   A 1 148 ? -15.479 5.907   -21.036 1   9.026  ? 148 VAL   A N    1 
ATOM   1145 C  CA   . VAL   A 1 148 ? -14.912 7.017   -21.778 1   9.35   ? 148 VAL   A CA   1 
ATOM   1146 C  C    . VAL   A 1 148 ? -13.389 7.072   -21.693 1   9.254  ? 148 VAL   A C    1 
ATOM   1147 O  O    . VAL   A 1 148 ? -12.743 6.552   -20.769 1   9.684  ? 148 VAL   A O    1 
ATOM   1148 C  CB   . VAL   A 1 148 ? -15.511 8.38    -21.401 1   10.035 ? 148 VAL   A CB   1 
ATOM   1149 C  CG1  . VAL   A 1 148 ? -17.007 8.389   -21.698 1   10.434 ? 148 VAL   A CG1  1 
ATOM   1150 C  CG2  . VAL   A 1 148 ? -15.244 8.766   -19.957 1   10.83  ? 148 VAL   A CG2  1 
ATOM   1151 N  N    . GLY   A 1 149 ? -12.858 7.761   -22.708 1   9.332  ? 149 GLY   A N    1 
ATOM   1152 C  CA   . GLY   A 1 149 ? -11.459 8.115   -22.815 1   9.123  ? 149 GLY   A CA   1 
ATOM   1153 C  C    . GLY   A 1 149 ? -11.277 9.624   -22.709 1   9.298  ? 149 GLY   A C    1 
ATOM   1154 O  O    . GLY   A 1 149 ? -12.12  10.401  -23.148 1   10.314 ? 149 GLY   A O    1 
ATOM   1155 N  N    . PHE   A 1 150 ? -10.146 10.034  -22.12  1   9.276  ? 150 PHE   A N    1 
ATOM   1156 C  CA   . PHE   A 1 150 ? -9.956  11.429  -21.76  1   9.896  ? 150 PHE   A CA   1 
ATOM   1157 C  C    . PHE   A 1 150 ? -8.483  11.743  -21.526 1   9.608  ? 150 PHE   A C    1 
ATOM   1158 O  O    . PHE   A 1 150 ? -7.693  10.836  -21.299 1   9.653  ? 150 PHE   A O    1 
ATOM   1159 C  CB   . PHE   A 1 150 ? -10.742 11.753  -20.478 1   11.155 ? 150 PHE   A CB   1 
ATOM   1160 C  CG   . PHE   A 1 150 ? -10.326 10.913  -19.274 1   11.877 ? 150 PHE   A CG   1 
ATOM   1161 C  CD1  . PHE   A 1 150 ? -10.827 9.626   -19.109 1   12.781 ? 150 PHE   A CD1  1 
ATOM   1162 C  CD2  . PHE   A 1 150 ? -9.391  11.371  -18.348 1   11.954 ? 150 PHE   A CD2  1 
ATOM   1163 C  CE1  . PHE   A 1 150 ? -10.424 8.835   -18.034 1   13.648 ? 150 PHE   A CE1  1 
ATOM   1164 C  CE2  . PHE   A 1 150 ? -8.976  10.56   -17.294 1   12.454 ? 150 PHE   A CE2  1 
ATOM   1165 C  CZ   . PHE   A 1 150 ? -9.496  9.304   -17.139 1   13.78  ? 150 PHE   A CZ   1 
ATOM   1166 N  N    . ASN   A 1 151 ? -8.175  13.045  -21.568 1   9.964  ? 151 ASN   A N    1 
ATOM   1167 C  CA   . ASN   A 1 151 ? -6.905  13.574  -21.086 1   10.861 ? 151 ASN   A CA   1 
ATOM   1168 C  C    . ASN   A 1 151 ? -7.228  14.661  -20.067 1   11.502 ? 151 ASN   A C    1 
ATOM   1169 O  O    . ASN   A 1 151 ? -8.345  15.166  -20.046 1   12.257 ? 151 ASN   A O    1 
ATOM   1170 C  CB   . ASN   A 1 151 ? -6.045  14.104  -22.23  1   11.541 ? 151 ASN   A CB   1 
ATOM   1171 C  CG   . ASN   A 1 151 ? -5.472  12.996  -23.074 1   12.086 ? 151 ASN   A CG   1 
ATOM   1172 O  OD1  . ASN   A 1 151 ? -4.598  12.254  -22.619 1   13.257 ? 151 ASN   A OD1  1 
ATOM   1173 N  ND2  . ASN   A 1 151 ? -5.967  12.831  -24.29  1   12.331 ? 151 ASN   A ND2  1 
ATOM   1174 N  N    . ILE   A 1 152 ? -6.281  14.975  -19.178 1   11.87  ? 152 ILE   A N    1 
ATOM   1175 C  CA   . ILE   A 1 152 ? -6.465  16.047  -18.211 1   13.264 ? 152 ILE   A CA   1 
ATOM   1176 C  C    . ILE   A 1 152 ? -5.184  16.865  -18.145 1   16.766 ? 152 ILE   A C    1 
ATOM   1177 O  O    . ILE   A 1 152 ? -4.552  16.987  -17.092 1   20.411 ? 152 ILE   A O    1 
ATOM   1178 C  CB   . ILE   A 1 152 ? -6.844  15.542  -16.806 1   13.632 ? 152 ILE   A CB   1 
ATOM   1179 C  CG1  . ILE   A 1 152 ? -7.865  14.416  -16.829 1   13.286 ? 152 ILE   A CG1  1 
ATOM   1180 C  CG2  . ILE   A 1 152 ? -7.306  16.728  -15.961 1   14.658 ? 152 ILE   A CG2  1 
ATOM   1181 C  CD1  . ILE   A 1 152 ? -8.217  13.858  -15.456 1   13.935 ? 152 ILE   A CD1  1 
ATOM   1182 N  N    . ASP   A 1 153 ? -4.808  17.422  -19.279 1   19.441 ? 153 ASP   A N    1 
ATOM   1183 C  CA   . ASP   A 1 153 ? -3.78   18.436  -19.318 1   21.632 ? 153 ASP   A CA   1 
ATOM   1184 C  C    . ASP   A 1 153 ? -4.389  19.667  -18.641 1   24.526 ? 153 ASP   A C    1 
ATOM   1185 O  O    . ASP   A 1 153 ? -5.499  20.085  -18.968 1   29.53  ? 153 ASP   A O    1 
ATOM   1186 C  CB   . ASP   A 1 153 ? -3.292  18.643  -20.743 1   21.085 ? 153 ASP   A CB   1 
ATOM   1187 C  CG   . ASP   A 1 153 ? -3.012  17.381  -21.551 1   20.638 ? 153 ASP   A CG   1 
ATOM   1188 O  OD1  . ASP   A 1 153 ? -2.189  16.54   -21.113 1   20.519 ? 153 ASP   A OD1  1 
ATOM   1189 O  OD2  . ASP   A 1 153 ? -3.611  17.246  -22.635 1   19.309 ? 153 ASP   A OD2  1 
ATOM   1190 N  N    . TYR   A 1 154 ? -3.693  20.192  -17.638 1   27.134 ? 154 TYR   A N    1 
ATOM   1191 C  CA   . TYR   A 1 154 ? -3.945  21.525  -17.11  1   27.51  ? 154 TYR   A CA   1 
ATOM   1192 C  C    . TYR   A 1 154 ? -5.312  21.634  -16.421 1   28.146 ? 154 TYR   A C    1 
ATOM   1193 O  O    . TYR   A 1 154 ? -5.931  22.693  -16.475 1   31.453 ? 154 TYR   A O    1 
ATOM   1194 C  CB   . TYR   A 1 154 ? -3.792  22.559  -18.241 1   29.422 ? 154 TYR   A CB   1 
ATOM   1195 C  CG   . TYR   A 1 154 ? -2.662  22.321  -19.244 1   32.135 ? 154 TYR   A CG   1 
ATOM   1196 C  CD1  . TYR   A 1 154 ? -1.33   22.454  -18.866 1   33.832 ? 154 TYR   A CD1  1 
ATOM   1197 C  CD2  . TYR   A 1 154 ? -2.922  22.005  -20.577 1   34.189 ? 154 TYR   A CD2  1 
ATOM   1198 C  CE1  . TYR   A 1 154 ? -0.293  22.251  -19.764 1   35.849 ? 154 TYR   A CE1  1 
ATOM   1199 C  CE2  . TYR   A 1 154 ? -1.893  21.805  -21.487 1   36.13  ? 154 TYR   A CE2  1 
ATOM   1200 C  CZ   . TYR   A 1 154 ? -0.575  21.931  -21.081 1   36.056 ? 154 TYR   A CZ   1 
ATOM   1201 O  OH   . TYR   A 1 154 ? 0.446   21.728  -21.962 1   39.432 ? 154 TYR   A OH   1 
ATOM   1202 N  N    . ASP   A 1 155 ? -5.773  20.581  -15.724 1   28.481 ? 155 ASP   A N    1 
ATOM   1203 C  CA   . ASP   A 1 155 ? -6.888  20.668  -14.776 1   28.451 ? 155 ASP   A CA   1 
ATOM   1204 C  C    . ASP   A 1 155 ? -8.27   20.554  -15.432 1   27.22  ? 155 ASP   A C    1 
ATOM   1205 O  O    . ASP   A 1 155 ? -9.279  20.473  -14.736 1   30.095 ? 155 ASP   A O    1 
ATOM   1206 C  CB   . ASP   A 1 155 ? -6.849  21.937  -13.941 1   31.014 ? 155 ASP   A CB   1 
ATOM   1207 N  N    . CYS   A 1 156 ? -8.325  20.581  -16.766 1   22.321 ? 156 CYS   A N    1 
ATOM   1208 C  CA   . CYS   A 1 156 ? -9.571  20.487  -17.507 1   19.096 ? 156 CYS   A CA   1 
ATOM   1209 C  C    . CYS   A 1 156 ? -9.628  19.103  -18.133 1   15.416 ? 156 CYS   A C    1 
ATOM   1210 O  O    . CYS   A 1 156 ? -8.65   18.68   -18.745 1   15.388 ? 156 CYS   A O    1 
ATOM   1211 C  CB   . CYS   A 1 156 ? -9.563  21.557  -18.586 1   20.702 ? 156 CYS   A CB   1 
ATOM   1212 S  SG   . CYS   A 1 156 ? -10.966 21.492  -19.723 1   23.068 ? 156 CYS   A SG   1 
ATOM   1213 N  N    . VAL   A 1 157 ? -10.749 18.399  -17.976 1   13.683 ? 157 VAL   A N    1 
ATOM   1214 C  CA   . VAL   A 1 157 ? -10.893 17.094  -18.597 1   12.363 ? 157 VAL   A CA   1 
ATOM   1215 C  C    . VAL   A 1 157 ? -11.336 17.265  -20.048 1   12.954 ? 157 VAL   A C    1 
ATOM   1216 O  O    . VAL   A 1 157 ? -12.408 17.791  -20.299 1   13.354 ? 157 VAL   A O    1 
ATOM   1217 C  CB   . VAL   A 1 157 ? -11.891 16.2    -17.844 1   12.353 ? 157 VAL   A CB   1 
ATOM   1218 C  CG1  . VAL   A 1 157 ? -11.963 14.815  -18.459 1   12.678 ? 157 VAL   A CG1  1 
ATOM   1219 C  CG2  . VAL   A 1 157 ? -11.527 16.093  -16.368 1   12.419 ? 157 VAL   A CG2  1 
ATOM   1220 N  N    . SER   A 1 158 ? -10.535 16.733  -20.974 1   12.423 ? 158 SER   A N    1 
ATOM   1221 C  CA   . SER   A 1 158 ? -10.881 16.694  -22.386 1   12.715 ? 158 SER   A CA   1 
ATOM   1222 C  C    . SER   A 1 158 ? -11.362 15.29   -22.722 1   11.543 ? 158 SER   A C    1 
ATOM   1223 O  O    . SER   A 1 158 ? -10.574 14.355  -22.795 1   12.949 ? 158 SER   A O    1 
ATOM   1224 C  CB   . SER   A 1 158 ? -9.718  17.104  -23.257 1   14.499 ? 158 SER   A CB   1 
ATOM   1225 O  OG   . SER   A 1 158 ? -8.564  16.318  -22.99  1   17.915 ? 158 SER   A OG   1 
ATOM   1226 N  N    . PHE   A 1 159 ? -12.679 15.135  -22.892 1   10.868 ? 159 PHE   A N    1 
ATOM   1227 C  CA   . PHE   A 1 159 ? -13.254 13.847  -23.229 1   10.781 ? 159 PHE   A CA   1 
ATOM   1228 C  C    . PHE   A 1 159 ? -13.136 13.646  -24.739 1   10.89  ? 159 PHE   A C    1 
ATOM   1229 O  O    . PHE   A 1 159 ? -13.563 14.513  -25.505 1   11.695 ? 159 PHE   A O    1 
ATOM   1230 C  CB   . PHE   A 1 159 ? -14.733 13.782  -22.834 1   10.995 ? 159 PHE   A CB   1 
ATOM   1231 C  CG   . PHE   A 1 159 ? -14.974 13.781  -21.337 1   10.723 ? 159 PHE   A CG   1 
ATOM   1232 C  CD1  . PHE   A 1 159 ? -14.777 12.62   -20.602 1   10.785 ? 159 PHE   A CD1  1 
ATOM   1233 C  CD2  . PHE   A 1 159 ? -15.373 14.931  -20.685 1   10.644 ? 159 PHE   A CD2  1 
ATOM   1234 C  CE1  . PHE   A 1 159 ? -14.985 12.604  -19.232 1   10.971 ? 159 PHE   A CE1  1 
ATOM   1235 C  CE2  . PHE   A 1 159 ? -15.606 14.907  -19.319 1   10.88  ? 159 PHE   A CE2  1 
ATOM   1236 C  CZ   . PHE   A 1 159 ? -15.409 13.745  -18.599 1   10.963 ? 159 PHE   A CZ   1 
ATOM   1237 N  N    . CYS   A 1 160 ? -12.595 12.491  -25.15  1   10.23  ? 160 CYS   A N    1 
ATOM   1238 C  CA   . CYS   A 1 160 ? -12.329 12.253  -26.562 1   11.037 ? 160 CYS   A CA   1 
ATOM   1239 C  C    . CYS   A 1 160 ? -12.894 10.939  -27.09  1   10.819 ? 160 CYS   A C    1 
ATOM   1240 O  O    . CYS   A 1 160 ? -12.907 10.748  -28.308 1   13.03  ? 160 CYS   A O    1 
ATOM   1241 C  CB   . CYS   A 1 160 ? -10.845 12.29   -26.899 1   11.848 ? 160 CYS   A CB   1 
ATOM   1242 S  SG   . CYS   A 1 160 ? -9.814  11.175  -25.919 1   13.441 ? 160 CYS   A SG   1 
ATOM   1243 N  N    . TYR   A 1 161 ? -13.339 10.026  -26.227 1   9.895  ? 161 TYR   A N    1 
ATOM   1244 C  CA   . TYR   A 1 161 ? -13.767 8.713   -26.681 1   9.605  ? 161 TYR   A CA   1 
ATOM   1245 C  C    . TYR   A 1 161 ? -14.906 8.214   -25.802 1   9.785  ? 161 TYR   A C    1 
ATOM   1246 O  O    . TYR   A 1 161 ? -14.872 8.4     -24.591 1   10.021 ? 161 TYR   A O    1 
ATOM   1247 C  CB   . TYR   A 1 161 ? -12.609 7.717   -26.637 1   9.534  ? 161 TYR   A CB   1 
ATOM   1248 C  CG   . TYR   A 1 161 ? -12.948 6.293   -27.046 1   9.788  ? 161 TYR   A CG   1 
ATOM   1249 C  CD1  . TYR   A 1 161 ? -12.958 5.916   -28.388 1   9.964  ? 161 TYR   A CD1  1 
ATOM   1250 C  CD2  . TYR   A 1 161 ? -13.263 5.314   -26.11  1   9.936  ? 161 TYR   A CD2  1 
ATOM   1251 C  CE1  . TYR   A 1 161 ? -13.257 4.621   -28.761 1   10.347 ? 161 TYR   A CE1  1 
ATOM   1252 C  CE2  . TYR   A 1 161 ? -13.539 4.005   -26.478 1   10.29  ? 161 TYR   A CE2  1 
ATOM   1253 C  CZ   . TYR   A 1 161 ? -13.565 3.66    -27.818 1   10.865 ? 161 TYR   A CZ   1 
ATOM   1254 O  OH   . TYR   A 1 161 ? -13.859 2.382   -28.209 1   11.548 ? 161 TYR   A OH   1 
ATOM   1255 N  N    . MET   A 1 162 ? -15.902 7.595   -26.44  1   9.674  ? 162 MET   A N    1 
ATOM   1256 C  CA   . MET   A 1 162 ? -16.916 6.828   -25.748 1   9.881  ? 162 MET   A CA   1 
ATOM   1257 C  C    . MET   A 1 162 ? -16.984 5.456   -26.405 1   9.535  ? 162 MET   A C    1 
ATOM   1258 O  O    . MET   A 1 162 ? -17.08  5.367   -27.634 1   9.688  ? 162 MET   A O    1 
ATOM   1259 C  CB   . MET   A 1 162 ? -18.29  7.506   -25.783 1   10.853 ? 162 MET   A CB   1 
ATOM   1260 C  CG   . MET   A 1 162 ? -19.337 6.702   -25.026 1   12.364 ? 162 MET   A CG   1 
ATOM   1261 S  SD   . MET   A 1 162 ? -20.886 7.541   -24.638 1   17.159 ? 162 MET   A SD   1 
ATOM   1262 C  CE   . MET   A 1 162 ? -21.323 7.428   -26.341 1   15.999 ? 162 MET   A CE   1 
ATOM   1263 N  N    . HIS   A 1 163 ? -16.944 4.396   -25.6   1   9.356  ? 163 HIS   A N    1 
ATOM   1264 C  CA   . HIS   A 1 163 ? -16.872 3.029   -26.092 1   9.518  ? 163 HIS   A CA   1 
ATOM   1265 C  C    . HIS   A 1 163 ? -18.233 2.537   -26.585 1   10.286 ? 163 HIS   A C    1 
ATOM   1266 O  O    . HIS   A 1 163 ? -19.209 2.569   -25.834 1   10.675 ? 163 HIS   A O    1 
ATOM   1267 C  CB   . HIS   A 1 163 ? -16.371 2.099   -24.98  1   9.955  ? 163 HIS   A CB   1 
ATOM   1268 C  CG   . HIS   A 1 163 ? -16.137 0.719   -25.462 1   10.251 ? 163 HIS   A CG   1 
ATOM   1269 N  ND1  . HIS   A 1 163 ? -15.375 0.461   -26.592 1   10.747 ? 163 HIS   A ND1  1 
ATOM   1270 C  CD2  . HIS   A 1 163 ? -16.582 -0.464  -25.022 1   10.891 ? 163 HIS   A CD2  1 
ATOM   1271 C  CE1  . HIS   A 1 163 ? -15.338 -0.847  -26.78  1   11.052 ? 163 HIS   A CE1  1 
ATOM   1272 N  NE2  . HIS   A 1 163 ? -16.072 -1.431  -25.844 1   11.227 ? 163 HIS   A NE2  1 
ATOM   1273 N  N    . HIS   A 1 164 ? -18.279 2.008   -27.819 1   10.704 ? 164 HIS   A N    1 
ATOM   1274 C  CA   . HIS   A 1 164 ? -19.507 1.451   -28.379 1   10.622 ? 164 HIS   A CA   1 
ATOM   1275 C  C    . HIS   A 1 164 ? -19.463 -0.057  -28.615 1   10.915 ? 164 HIS   A C    1 
ATOM   1276 O  O    . HIS   A 1 164 ? -20.475 -0.714  -28.376 1   12.298 ? 164 HIS   A O    1 
ATOM   1277 C  CB   . HIS   A 1 164 ? -19.937 2.138   -29.677 1   10.773 ? 164 HIS   A CB   1 
ATOM   1278 C  CG   . HIS   A 1 164 ? -20.512 3.486   -29.497 1   10.705 ? 164 HIS   A CG   1 
ATOM   1279 N  ND1  . HIS   A 1 164 ? -19.904 4.609   -28.982 1   12.587 ? 164 HIS   A ND1  1 
ATOM   1280 C  CD2  . HIS   A 1 164 ? -21.759 3.868   -29.86  1   9.472  ? 164 HIS   A CD2  1 
ATOM   1281 C  CE1  . HIS   A 1 164 ? -20.779 5.618   -29.013 1   10.444 ? 164 HIS   A CE1  1 
ATOM   1282 N  NE2  . HIS   A 1 164 ? -21.899 5.185   -29.567 1   11.852 ? 164 HIS   A NE2  1 
ATOM   1283 N  N    . MET   A 1 165 ? -18.38  -0.619  -29.171 1   11.362 ? 165 MET   A N    1 
ATOM   1284 C  CA   . MET   A 1 165 ? -18.377 -2.054  -29.387 1   12.312 ? 165 MET   A CA   1 
ATOM   1285 C  C    . MET   A 1 165 ? -16.969 -2.611  -29.577 1   12.255 ? 165 MET   A C    1 
ATOM   1286 O  O    . MET   A 1 165 ? -16.011 -1.887  -29.814 1   12.174 ? 165 MET   A O    1 
ATOM   1287 C  CB   . MET   A 1 165 ? -19.223 -2.469  -30.6   1   13.633 ? 165 MET   A CB   1 
ATOM   1288 C  CG   . MET   A 1 165 ? -18.636 -2.103  -31.933 1   14.871 ? 165 MET   A CG   1 
ATOM   1289 S  SD   . MET   A 1 165 ? -18.966 -0.388  -32.377 1   16.912 ? 165 MET   A SD   1 
ATOM   1290 C  CE   . MET   A 1 165 ? -18.706 -0.567  -34.144 1   16.406 ? 165 MET   A CE   1 
ATOM   1291 N  N    . GLU   A 1 166 ? -16.886 -3.936  -29.441 1   12.819 ? 166 GLU   A N    1 
ATOM   1292 C  CA   . GLU   A 1 166 ? -15.727 -4.709  -29.842 1   13.426 ? 166 GLU   A CA   1 
ATOM   1293 C  C    . GLU   A 1 166 ? -15.992 -5.308  -31.219 1   14.398 ? 166 GLU   A C    1 
ATOM   1294 O  O    . GLU   A 1 166 ? -17.059 -5.884  -31.463 1   14.707 ? 166 GLU   A O    1 
ATOM   1295 C  CB   . GLU   A 1 166 ? -15.428 -5.794  -28.813 1   13.715 ? 166 GLU   A CB   1 
ATOM   1296 C  CG   . GLU   A 1 166 ? -14.186 -6.615  -29.15  1   14.232 ? 166 GLU   A CG   1 
ATOM   1297 C  CD   . GLU   A 1 166 ? -13.707 -7.493  -28.009 1   15.605 ? 166 GLU   A CD   1 
ATOM   1298 O  OE1  . GLU   A 1 166 ? -13.521 -6.982  -26.882 1   15.297 ? 166 GLU   A OE1  1 
ATOM   1299 O  OE2  . GLU   A 1 166 ? -13.478 -8.692  -28.276 1   17.516 ? 166 GLU   A OE2  1 
ATOM   1300 N  N    . LEU   A 1 167 ? -14.982 -5.172  -32.089 1   14.669 ? 167 LEU   A N    1 
ATOM   1301 C  CA   . LEU   A 1 167 ? -15.022 -5.702  -33.441 1   16.558 ? 167 LEU   A CA   1 
ATOM   1302 C  C    . LEU   A 1 167 ? -14.551 -7.149  -33.412 1   18.113 ? 167 LEU   A C    1 
ATOM   1303 O  O    . LEU   A 1 167 ? -13.95  -7.597  -32.435 1   18.299 ? 167 LEU   A O    1 
ATOM   1304 C  CB   . LEU   A 1 167 ? -14.165 -4.843  -34.365 1   17.52  ? 167 LEU   A CB   1 
ATOM   1305 C  CG   . LEU   A 1 167 ? -14.679 -3.42   -34.597 1   19.041 ? 167 LEU   A CG   1 
ATOM   1306 C  CD1  . LEU   A 1 167 ? -13.629 -2.595  -35.307 1   19.832 ? 167 LEU   A CD1  1 
ATOM   1307 C  CD2  . LEU   A 1 167 ? -15.962 -3.438  -35.4   1   21.031 ? 167 LEU   A CD2  1 
ATOM   1308 N  N    . PRO   A 1 168 ? -14.84  -7.938  -34.471 1   21.026 ? 168 PRO   A N    1 
ATOM   1309 C  CA   . PRO   A 1 168 ? -14.483 -9.358  -34.473 1   23.162 ? 168 PRO   A CA   1 
ATOM   1310 C  C    . PRO   A 1 168 ? -13.019 -9.729  -34.229 1   23.453 ? 168 PRO   A C    1 
ATOM   1311 O  O    . PRO   A 1 168 ? -12.75  -10.828 -33.759 1   26.435 ? 168 PRO   A O    1 
ATOM   1312 C  CB   . PRO   A 1 168 ? -14.974 -9.787  -35.864 1   24.225 ? 168 PRO   A CB   1 
ATOM   1313 C  CG   . PRO   A 1 168 ? -16.142 -8.876  -36.126 1   24.25  ? 168 PRO   A CG   1 
ATOM   1314 C  CD   . PRO   A 1 168 ? -15.636 -7.537  -35.645 1   22.552 ? 168 PRO   A CD   1 
ATOM   1315 N  N    . THR   A 1 169 ? -12.082 -8.829  -34.555 1   24.067 ? 169 THR   A N    1 
ATOM   1316 C  CA   . THR   A 1 169 ? -10.659 -9.059  -34.332 1   25.314 ? 169 THR   A CA   1 
ATOM   1317 C  C    . THR   A 1 169 ? -10.249 -8.753  -32.892 1   23.099 ? 169 THR   A C    1 
ATOM   1318 O  O    . THR   A 1 169 ? -9.076  -8.896  -32.56  1   25.554 ? 169 THR   A O    1 
ATOM   1319 C  CB   . THR   A 1 169 ? -9.807  -8.236  -35.306 1   27.342 ? 169 THR   A CB   1 
ATOM   1320 O  OG1  . THR   A 1 169 ? -10.246 -6.883  -35.233 1   28.364 ? 169 THR   A OG1  1 
ATOM   1321 C  CG2  . THR   A 1 169 ? -9.875  -8.751  -36.734 1   29.051 ? 169 THR   A CG2  1 
ATOM   1322 N  N    . GLY   A 1 170 ? -11.181 -8.303  -32.043 1   19.749 ? 170 GLY   A N    1 
ATOM   1323 C  CA   . GLY   A 1 170 ? -10.887 -8.101  -30.631 1   18.839 ? 170 GLY   A CA   1 
ATOM   1324 C  C    . GLY   A 1 170 ? -10.395 -6.69   -30.305 1   18.768 ? 170 GLY   A C    1 
ATOM   1325 O  O    . GLY   A 1 170 ? -9.947  -6.438  -29.185 1   22.404 ? 170 GLY   A O    1 
ATOM   1326 N  N    . VAL   A 1 171 ? -10.473 -5.774  -31.273 1   16.856 ? 171 VAL   A N    1 
ATOM   1327 C  CA   . VAL   A 1 171 ? -10.156 -4.377  -31.03  1   16.423 ? 171 VAL   A CA   1 
ATOM   1328 C  C    . VAL   A 1 171 ? -11.466 -3.611  -30.868 1   14.249 ? 171 VAL   A C    1 
ATOM   1329 O  O    . VAL   A 1 171 ? -12.558 -4.164  -31.06  1   14.241 ? 171 VAL   A O    1 
ATOM   1330 C  CB   . VAL   A 1 171 ? -9.266  -3.782  -32.137 1   17.826 ? 171 VAL   A CB   1 
ATOM   1331 C  CG1  . VAL   A 1 171 ? -7.955  -4.544  -32.275 1   19.045 ? 171 VAL   A CG1  1 
ATOM   1332 C  CG2  . VAL   A 1 171 ? -10.001 -3.741  -33.466 1   18.326 ? 171 VAL   A CG2  1 
ATOM   1333 N  N    . HIS   A 1 172 ? -11.341 -2.342  -30.481 1   12.305 ? 172 HIS   A N    1 
ATOM   1334 C  CA   . HIS   A 1 172 ? -12.466 -1.605  -29.923 1   11.725 ? 172 HIS   A CA   1 
ATOM   1335 C  C    . HIS   A 1 172 ? -12.761 -0.372  -30.76  1   11.977 ? 172 HIS   A C    1 
ATOM   1336 O  O    . HIS   A 1 172 ? -11.849 0.258   -31.293 1   13.138 ? 172 HIS   A O    1 
ATOM   1337 C  CB   . HIS   A 1 172 ? -12.147 -1.271  -28.468 1   12.09  ? 172 HIS   A CB   1 
ATOM   1338 C  CG   . HIS   A 1 172 ? -11.913 -2.535  -27.717 1   12.696 ? 172 HIS   A CG   1 
ATOM   1339 N  ND1  . HIS   A 1 172 ? -10.703 -2.921  -27.173 1   12.299 ? 172 HIS   A ND1  1 
ATOM   1340 C  CD2  . HIS   A 1 172 ? -12.783 -3.516  -27.461 1   13.234 ? 172 HIS   A CD2  1 
ATOM   1341 C  CE1  . HIS   A 1 172 ? -10.854 -4.111  -26.614 1   13.13  ? 172 HIS   A CE1  1 
ATOM   1342 N  NE2  . HIS   A 1 172 ? -12.119 -4.487  -26.775 1   13.854 ? 172 HIS   A NE2  1 
ATOM   1343 N  N    . ALA   A 1 173 ? -14.058 -0.056  -30.882 1   11.728 ? 173 ALA   A N    1 
ATOM   1344 C  CA   . ALA   A 1 173 ? -14.508 1.071   -31.677 1   11.528 ? 173 ALA   A CA   1 
ATOM   1345 C  C    . ALA   A 1 173 ? -15.499 1.917   -30.884 1   11.18  ? 173 ALA   A C    1 
ATOM   1346 O  O    . ALA   A 1 173 ? -16.251 1.417   -30.035 1   11.262 ? 173 ALA   A O    1 
ATOM   1347 C  CB   . ALA   A 1 173 ? -15.158 0.566   -32.953 1   12.358 ? 173 ALA   A CB   1 
ATOM   1348 N  N    . GLY   A 1 174 ? -15.488 3.212   -31.184 1   10.927 ? 174 GLY   A N    1 
ATOM   1349 C  CA   . GLY   A 1 174 ? -16.357 4.14    -30.492 1   10.78  ? 174 GLY   A CA   1 
ATOM   1350 C  C    . GLY   A 1 174 ? -16.369 5.499   -31.166 1   10.717 ? 174 GLY   A C    1 
ATOM   1351 O  O    . GLY   A 1 174 ? -15.881 5.648   -32.287 1   11.216 ? 174 GLY   A O    1 
ATOM   1352 N  N    . THR   A 1 175 ? -16.913 6.475   -30.447 1   10.419 ? 175 THR   A N    1 
ATOM   1353 C  CA   . THR   A 1 175 ? -17.237 7.784   -30.977 1   10.828 ? 175 THR   A CA   1 
ATOM   1354 C  C    . THR   A 1 175 ? -16.521 8.847   -30.166 1   10.362 ? 175 THR   A C    1 
ATOM   1355 O  O    . THR   A 1 175 ? -16.06  8.608   -29.048 1   11.671 ? 175 THR   A O    1 
ATOM   1356 C  CB   . THR   A 1 175 ? -18.745 8.053   -30.937 1   11.055 ? 175 THR   A CB   1 
ATOM   1357 O  OG1  . THR   A 1 175 ? -19.208 8.111   -29.587 1   11.497 ? 175 THR   A OG1  1 
ATOM   1358 C  CG2  . THR   A 1 175 ? -19.54  7.005   -31.687 1   11.442 ? 175 THR   A CG2  1 
ATOM   1359 N  N    . ASP   A 1 176 ? -16.517 10.055  -30.717 1   10.523 ? 176 ASP   A N    1 
ATOM   1360 C  CA   . ASP   A 1 176 ? -16.287 11.249  -29.929 1   11.702 ? 176 ASP   A CA   1 
ATOM   1361 C  C    . ASP   A 1 176 ? -17.549 11.528  -29.101 1   11.908 ? 176 ASP   A C    1 
ATOM   1362 O  O    . ASP   A 1 176 ? -18.541 10.799  -29.193 1   11.325 ? 176 ASP   A O    1 
ATOM   1363 C  CB   . ASP   A 1 176 ? -15.802 12.387  -30.809 1   12.694 ? 176 ASP   A CB   1 
ATOM   1364 C  CG   . ASP   A 1 176 ? -16.802 12.917  -31.828 1   13.03  ? 176 ASP   A CG   1 
ATOM   1365 O  OD1  . ASP   A 1 176 ? -18.014 12.736  -31.585 1   13.833 ? 176 ASP   A OD1  1 
ATOM   1366 O  OD2  . ASP   A 1 176 ? -16.361 13.492  -32.854 1   15.025 ? 176 ASP   A OD2  1 
ATOM   1367 N  N    . LEU   A 1 177 ? -17.514 12.589  -28.286 1   12.054 ? 177 LEU   A N    1 
ATOM   1368 C  CA   . LEU   A 1 177 ? -18.617 12.865  -27.378 1   12.242 ? 177 LEU   A CA   1 
ATOM   1369 C  C    . LEU   A 1 177 ? -19.728 13.631  -28.093 1   12.946 ? 177 LEU   A C    1 
ATOM   1370 O  O    . LEU   A 1 177 ? -20.774 13.878  -27.494 1   14.053 ? 177 LEU   A O    1 
ATOM   1371 C  CB   . LEU   A 1 177 ? -18.154 13.546  -26.088 1   12.772 ? 177 LEU   A CB   1 
ATOM   1372 C  CG   . LEU   A 1 177 ? -17.809 12.586  -24.942 1   13.594 ? 177 LEU   A CG   1 
ATOM   1373 C  CD1  . LEU   A 1 177 ? -19.053 11.892  -24.418 1   14.249 ? 177 LEU   A CD1  1 
ATOM   1374 C  CD2  . LEU   A 1 177 ? -16.744 11.57   -25.351 1   13.955 ? 177 LEU   A CD2  1 
ATOM   1375 N  N    . GLU   A 1 178 ? -19.538 13.932  -29.384 1   13.115 ? 178 GLU   A N    1 
ATOM   1376 C  CA   . GLU   A 1 178 ? -20.617 14.398  -30.243 1   14.226 ? 178 GLU   A CA   1 
ATOM   1377 C  C    . GLU   A 1 178 ? -21.264 13.233  -31.002 1   13.367 ? 178 GLU   A C    1 
ATOM   1378 O  O    . GLU   A 1 178 ? -22.144 13.462  -31.835 1   14.204 ? 178 GLU   A O    1 
ATOM   1379 C  CB   . GLU   A 1 178 ? -20.093 15.486  -31.18  1   16.54  ? 178 GLU   A CB   1 
ATOM   1380 C  CG   . GLU   A 1 178 ? -19.694 16.767  -30.451 1   19.176 ? 178 GLU   A CG   1 
ATOM   1381 C  CD   . GLU   A 1 178 ? -19.389 17.941  -31.368 1   22.763 ? 178 GLU   A CD   1 
ATOM   1382 O  OE1  . GLU   A 1 178 ? -18.807 17.726  -32.448 1   26.816 ? 178 GLU   A OE1  1 
ATOM   1383 O  OE2  . GLU   A 1 178 ? -19.728 19.082  -30.999 1   28.115 ? 178 GLU   A OE2  1 
ATOM   1384 N  N    . GLY   A 1 179 ? -20.837 11.993  -30.732 1   12.563 ? 179 GLY   A N    1 
ATOM   1385 C  CA   . GLY   A 1 179 ? -21.458 10.803  -31.296 1   12.207 ? 179 GLY   A CA   1 
ATOM   1386 C  C    . GLY   A 1 179 ? -20.996 10.454  -32.708 1   12.489 ? 179 GLY   A C    1 
ATOM   1387 O  O    . GLY   A 1 179 ? -21.619 9.603   -33.343 1   13.005 ? 179 GLY   A O    1 
ATOM   1388 N  N    . ASN   A 1 180 ? -19.877 11.033  -33.161 1   12.409 ? 180 ASN   A N    1 
ATOM   1389 C  CA   . ASN   A 1 180 ? -19.325 10.696  -34.468 1   13.228 ? 180 ASN   A CA   1 
ATOM   1390 C  C    . ASN   A 1 180 ? -18.3   9.581   -34.3   1   12.16  ? 180 ASN   A C    1 
ATOM   1391 O  O    . ASN   A 1 180 ? -17.33  9.754   -33.561 1   12.284 ? 180 ASN   A O    1 
ATOM   1392 C  CB   . ASN   A 1 180 ? -18.633 11.901  -35.087 1   14.501 ? 180 ASN   A CB   1 
ATOM   1393 C  CG   . ASN   A 1 180 ? -19.59  13.028  -35.357 1   17.319 ? 180 ASN   A CG   1 
ATOM   1394 O  OD1  . ASN   A 1 180 ? -20.531 12.861  -36.139 1   20.253 ? 180 ASN   A OD1  1 
ATOM   1395 N  ND2  . ASN   A 1 180 ? -19.378 14.156  -34.704 1   19.771 ? 180 ASN   A ND2  1 
ATOM   1396 N  N    . PHE   A 1 181 ? -18.511 8.441   -34.967 1   12.192 ? 181 PHE   A N    1 
ATOM   1397 C  CA   . PHE   A 1 181 ? -17.553 7.352   -34.902 1   12.391 ? 181 PHE   A CA   1 
ATOM   1398 C  C    . PHE   A 1 181 ? -16.165 7.813   -35.348 1   12.177 ? 181 PHE   A C    1 
ATOM   1399 O  O    . PHE   A 1 181 ? -16.011 8.631   -36.26  1   12.783 ? 181 PHE   A O    1 
ATOM   1400 C  CB   . PHE   A 1 181 ? -17.951 6.13    -35.733 1   12.491 ? 181 PHE   A CB   1 
ATOM   1401 C  CG   . PHE   A 1 181 ? -18.691 5.109   -34.892 1   12.201 ? 181 PHE   A CG   1 
ATOM   1402 C  CD1  . PHE   A 1 181 ? -20.068 5.177   -34.755 1   12.603 ? 181 PHE   A CD1  1 
ATOM   1403 C  CD2  . PHE   A 1 181 ? -18.005 4.102   -34.228 1   12.47  ? 181 PHE   A CD2  1 
ATOM   1404 C  CE1  . PHE   A 1 181 ? -20.742 4.255   -33.972 1   13.142 ? 181 PHE   A CE1  1 
ATOM   1405 C  CE2  . PHE   A 1 181 ? -18.681 3.184   -33.435 1   12.754 ? 181 PHE   A CE2  1 
ATOM   1406 C  CZ   . PHE   A 1 181 ? -20.047 3.269   -33.31  1   12.887 ? 181 PHE   A CZ   1 
ATOM   1407 N  N    . TYR   A 1 182 ? -15.152 7.255   -34.68  1   11.299 ? 182 TYR   A N    1 
ATOM   1408 C  CA   . TYR   A 1 182 ? -13.815 7.18    -35.238 1   11.894 ? 182 TYR   A CA   1 
ATOM   1409 C  C    . TYR   A 1 182 ? -13.811 6.059   -36.267 1   13.252 ? 182 TYR   A C    1 
ATOM   1410 O  O    . TYR   A 1 182 ? -14.209 4.939   -35.967 1   14.462 ? 182 TYR   A O    1 
ATOM   1411 C  CB   . TYR   A 1 182 ? -12.79  6.942   -34.118 1   11.891 ? 182 TYR   A CB   1 
ATOM   1412 C  CG   . TYR   A 1 182 ? -12.642 8.144   -33.197 1   11.644 ? 182 TYR   A CG   1 
ATOM   1413 C  CD1  . TYR   A 1 182 ? -11.927 9.269   -33.594 1   12.273 ? 182 TYR   A CD1  1 
ATOM   1414 C  CD2  . TYR   A 1 182 ? -13.228 8.172   -31.932 1   11.606 ? 182 TYR   A CD2  1 
ATOM   1415 C  CE1  . TYR   A 1 182 ? -11.775 10.368  -32.766 1   12.273 ? 182 TYR   A CE1  1 
ATOM   1416 C  CE2  . TYR   A 1 182 ? -13.089 9.275   -31.102 1   11.442 ? 182 TYR   A CE2  1 
ATOM   1417 C  CZ   . TYR   A 1 182 ? -12.343 10.367  -31.502 1   11.55  ? 182 TYR   A CZ   1 
ATOM   1418 O  OH   . TYR   A 1 182 ? -12.181 11.473  -30.711 1   11.226 ? 182 TYR   A OH   1 
ATOM   1419 N  N    . GLY   A 1 183 ? -13.316 6.363   -37.471 1   14.729 ? 183 GLY   A N    1 
ATOM   1420 C  CA   . GLY   A 1 183 ? -13.208 5.354   -38.504 1   16.125 ? 183 GLY   A CA   1 
ATOM   1421 C  C    . GLY   A 1 183 ? -14.533 5.12    -39.217 1   17.475 ? 183 GLY   A C    1 
ATOM   1422 O  O    . GLY   A 1 183 ? -15.517 5.817   -38.978 1   19.127 ? 183 GLY   A O    1 
ATOM   1423 N  N    . PRO   A 1 184 ? -14.568 4.112   -40.103 1   18.457 ? 184 PRO   A N    1 
ATOM   1424 C  CA   . PRO   A 1 184 ? -15.727 3.892   -40.967 1   18.552 ? 184 PRO   A CA   1 
ATOM   1425 C  C    . PRO   A 1 184 ? -16.89  3.126   -40.34  1   20.347 ? 184 PRO   A C    1 
ATOM   1426 O  O    . PRO   A 1 184 ? -17.884 2.825   -40.991 1   22.863 ? 184 PRO   A O    1 
ATOM   1427 C  CB   . PRO   A 1 184 ? -15.061 3.159   -42.157 1   19.5   ? 184 PRO   A CB   1 
ATOM   1428 C  CG   . PRO   A 1 184 ? -13.957 2.356   -41.529 1   20.213 ? 184 PRO   A CG   1 
ATOM   1429 C  CD   . PRO   A 1 184 ? -13.422 3.25    -40.434 1   19.183 ? 184 PRO   A CD   1 
ATOM   1430 N  N    . PHE   A 1 185 ? -16.835 2.938   -39.028 1   18.059 ? 185 PHE   A N    1 
ATOM   1431 C  CA   . PHE   A 1 185 ? -17.701 1.989   -38.351 1   16.948 ? 185 PHE   A CA   1 
ATOM   1432 C  C    . PHE   A 1 185 ? -19.082 2.582   -38.095 1   16.995 ? 185 PHE   A C    1 
ATOM   1433 O  O    . PHE   A 1 185 ? -19.267 3.794   -38.109 1   17.734 ? 185 PHE   A O    1 
ATOM   1434 C  CB   . PHE   A 1 185 ? -17.048 1.559   -37.039 1   15.942 ? 185 PHE   A CB   1 
ATOM   1435 C  CG   . PHE   A 1 185 ? -15.625 1.074   -37.253 1   15.566 ? 185 PHE   A CG   1 
ATOM   1436 C  CD1  . PHE   A 1 185 ? -15.373 -0.059  -38.022 1   16.404 ? 185 PHE   A CD1  1 
ATOM   1437 C  CD2  . PHE   A 1 185 ? -14.546 1.771   -36.729 1   16.101 ? 185 PHE   A CD2  1 
ATOM   1438 C  CE1  . PHE   A 1 185 ? -14.078 -0.468  -38.28  1   16.678 ? 185 PHE   A CE1  1 
ATOM   1439 C  CE2  . PHE   A 1 185 ? -13.25  1.348   -36.983 1   16.512 ? 185 PHE   A CE2  1 
ATOM   1440 C  CZ   . PHE   A 1 185 ? -13.019 0.225   -37.741 1   16.791 ? 185 PHE   A CZ   1 
ATOM   1441 N  N    . VAL   A 1 186 ? -20.036 1.672   -37.879 1   17.288 ? 186 VAL   A N    1 
ATOM   1442 C  CA   . VAL   A 1 186 ? -21.427 2.019   -37.647 1   16.909 ? 186 VAL   A CA   1 
ATOM   1443 C  C    . VAL   A 1 186 ? -21.929 1.251   -36.428 1   15.591 ? 186 VAL   A C    1 
ATOM   1444 O  O    . VAL   A 1 186 ? -21.436 0.165   -36.131 1   15.223 ? 186 VAL   A O    1 
ATOM   1445 C  CB   . VAL   A 1 186 ? -22.297 1.731   -38.887 1   17.714 ? 186 VAL   A CB   1 
ATOM   1446 C  CG1  . VAL   A 1 186 ? -21.924 2.664   -40.021 1   18.647 ? 186 VAL   A CG1  1 
ATOM   1447 C  CG2  . VAL   A 1 186 ? -22.218 0.273   -39.323 1   17.932 ? 186 VAL   A CG2  1 
ATOM   1448 N  N    . ASP   A 1 187 ? -22.962 1.798   -35.772 1   14.392 ? 187 ASP   A N    1 
ATOM   1449 C  CA   . ASP   A 1 187 ? -23.539 1.149   -34.598 1   14.452 ? 187 ASP   A CA   1 
ATOM   1450 C  C    . ASP   A 1 187 ? -24.657 0.192   -35.024 1   15.619 ? 187 ASP   A C    1 
ATOM   1451 O  O    . ASP   A 1 187 ? -25.813 0.345   -34.641 1   16.104 ? 187 ASP   A O    1 
ATOM   1452 C  CB   . ASP   A 1 187 ? -23.944 2.149   -33.527 1   14.708 ? 187 ASP   A CB   1 
ATOM   1453 C  CG   . ASP   A 1 187 ? -24.838 3.306   -33.937 1   14.393 ? 187 ASP   A CG   1 
ATOM   1454 O  OD1  . ASP   A 1 187 ? -25.142 3.448   -35.147 1   14.949 ? 187 ASP   A OD1  1 
ATOM   1455 O  OD2  . ASP   A 1 187 ? -25.208 4.081   -33.034 1   14.054 ? 187 ASP   A OD2  1 
ATOM   1456 N  N    . ARG   A 1 188 ? -24.251 -0.838  -35.773 1   15.727 ? 188 ARG   A N    1 
ATOM   1457 C  CA   . ARG   A 1 188 ? -25.088 -1.918  -36.275 1   19.376 ? 188 ARG   A CA   1 
ATOM   1458 C  C    . ARG   A 1 188 ? -24.233 -3.182  -36.239 1   17.815 ? 188 ARG   A C    1 
ATOM   1459 O  O    . ARG   A 1 188 ? -23.033 -3.107  -36.491 1   17.791 ? 188 ARG   A O    1 
ATOM   1460 C  CB   . ARG   A 1 188 ? -25.54  -1.795  -37.746 1   22.659 ? 188 ARG   A CB   1 
ATOM   1461 C  CG   . ARG   A 1 188 ? -25.984 -0.448  -38.295 1   26.367 ? 188 ARG   A CG   1 
ATOM   1462 C  CD   . ARG   A 1 188 ? -26.029 -0.257  -39.832 1   26.595 ? 188 ARG   A CD   1 
ATOM   1463 N  NE   . ARG   A 1 188 ? -26.29  -1.412  -40.701 1   25.368 ? 188 ARG   A NE   1 
ATOM   1464 C  CZ   . ARG   A 1 188 ? -26.008 -1.481  -42.005 1   26.794 ? 188 ARG   A CZ   1 
ATOM   1465 N  NH1  . ARG   A 1 188 ? -25.404 -0.47   -42.612 1   25.864 ? 188 ARG   A NH1  1 
ATOM   1466 N  NH2  . ARG   A 1 188 ? -26.294 -2.578  -42.693 1   26.359 ? 188 ARG   A NH2  1 
ATOM   1467 N  N    . GLN   A 1 189 ? -24.839 -4.332  -35.932 1   18.951 ? 189 GLN   A N    1 
ATOM   1468 C  CA   . GLN   A 1 189 ? -24.116 -5.594  -35.852 1   21.204 ? 189 GLN   A CA   1 
ATOM   1469 C  C    . GLN   A 1 189 ? -24.023 -6.271  -37.218 1   23.171 ? 189 GLN   A C    1 
ATOM   1470 O  O    . GLN   A 1 189 ? -24.268 -7.474  -37.356 1   26.594 ? 189 GLN   A O    1 
ATOM   1471 C  CB   . GLN   A 1 189 ? -24.796 -6.477  -34.811 1   24.542 ? 189 GLN   A CB   1 
ATOM   1472 C  CG   . GLN   A 1 189 ? -23.984 -7.686  -34.378 1   27.706 ? 189 GLN   A CG   1 
ATOM   1473 C  CD   . GLN   A 1 189 ? -24.528 -8.247  -33.085 1   30.857 ? 189 GLN   A CD   1 
ATOM   1474 O  OE1  . GLN   A 1 189 ? -25.744 -8.242  -32.855 1   32.434 ? 189 GLN   A OE1  1 
ATOM   1475 N  NE2  . GLN   A 1 189 ? -23.631 -8.66   -32.205 1   32.492 ? 189 GLN   A NE2  1 
ATOM   1476 N  N    . THR   A 1 190 ? -23.627 -5.493  -38.228 1   22.266 ? 190 THR   A N    1 
ATOM   1477 C  CA   . THR   A 1 190 ? -23.373 -5.981  -39.572 1   22.134 ? 190 THR   A CA   1 
ATOM   1478 C  C    . THR   A 1 190 ? -21.879 -6.265  -39.679 1   21.928 ? 190 THR   A C    1 
ATOM   1479 O  O    . THR   A 1 190 ? -21.092 -5.799  -38.85  1   22.755 ? 190 THR   A O    1 
ATOM   1480 C  CB   . THR   A 1 190 ? -23.853 -4.93   -40.574 1   22.976 ? 190 THR   A CB   1 
ATOM   1481 O  OG1  . THR   A 1 190 ? -23.846 -5.555  -41.853 1   25.08  ? 190 THR   A OG1  1 
ATOM   1482 C  CG2  . THR   A 1 190 ? -22.997 -3.674  -40.554 1   22.006 ? 190 THR   A CG2  1 
ATOM   1483 N  N    . ALA   A 1 191 ? -21.484 -7.049  -40.685 1   23.071 ? 191 ALA   A N    1 
ATOM   1484 C  CA   . ALA   A 1 191 ? -20.075 -7.337  -40.895 1   24.483 ? 191 ALA   A CA   1 
ATOM   1485 C  C    . ALA   A 1 191 ? -19.343 -6.026  -41.165 1   24.421 ? 191 ALA   A C    1 
ATOM   1486 O  O    . ALA   A 1 191 ? -19.695 -5.257  -42.055 1   26.929 ? 191 ALA   A O    1 
ATOM   1487 C  CB   . ALA   A 1 191 ? -19.884 -8.314  -42.03  1   25.322 ? 191 ALA   A CB   1 
ATOM   1488 N  N    . GLN   A 1 192 ? -18.368 -5.738  -40.31  1   26.733 ? 192 GLN   A N    1 
ATOM   1489 C  CA   . GLN   A 1 192 ? -17.457 -4.636  -40.531 1   25.572 ? 192 GLN   A CA   1 
ATOM   1490 C  C    . GLN   A 1 192 ? -16.129 -5.136  -39.987 1   27.431 ? 192 GLN   A C    1 
ATOM   1491 O  O    . GLN   A 1 192 ? -16.088 -6.008  -39.115 1   28.991 ? 192 GLN   A O    1 
ATOM   1492 C  CB   . GLN   A 1 192 ? -17.872 -3.292  -39.92  1   28.41  ? 192 GLN   A CB   1 
ATOM   1493 C  CG   . GLN   A 1 192 ? -18.595 -3.396  -38.583 1   26.563 ? 192 GLN   A CG   1 
ATOM   1494 C  CD   . GLN   A 1 192 ? -19.269 -2.114  -38.126 1   23.767 ? 192 GLN   A CD   1 
ATOM   1495 O  OE1  . GLN   A 1 192 ? -18.877 -0.992  -38.456 1   22.514 ? 192 GLN   A OE1  1 
ATOM   1496 N  NE2  . GLN   A 1 192 ? -20.279 -2.272  -37.294 1   22.466 ? 192 GLN   A NE2  1 
ATOM   1497 N  N    . ALA   A 1 193 ? -15.065 -4.614  -40.585 1   27.859 ? 193 ALA   A N    1 
ATOM   1498 C  CA   . ALA   A 1 193 ? -13.714 -4.985  -40.23  1   28.686 ? 193 ALA   A CA   1 
ATOM   1499 C  C    . ALA   A 1 193 ? -12.835 -3.745  -40.314 1   28.972 ? 193 ALA   A C    1 
ATOM   1500 O  O    . ALA   A 1 193 ? -12.98  -2.914  -41.21  1   31.178 ? 193 ALA   A O    1 
ATOM   1501 C  CB   . ALA   A 1 193 ? -13.213 -6.075  -41.139 1   29.072 ? 193 ALA   A CB   1 
ATOM   1502 N  N    . ALA   A 1 194 ? -11.945 -3.635  -39.33  1   29.108 ? 194 ALA   A N    1 
ATOM   1503 C  CA   . ALA   A 1 194 ? -10.914 -2.62   -39.326 1   27.391 ? 194 ALA   A CA   1 
ATOM   1504 C  C    . ALA   A 1 194 ? -9.953  -2.881  -40.477 1   26.831 ? 194 ALA   A C    1 
ATOM   1505 O  O    . ALA   A 1 194 ? -9.717  -4.033  -40.846 1   26.369 ? 194 ALA   A O    1 
ATOM   1506 C  CB   . ALA   A 1 194 ? -10.198 -2.657  -38.002 1   29.256 ? 194 ALA   A CB   1 
ATOM   1507 N  N    . GLY   A 1 195 ? -9.417  -1.791  -41.035 1   27.182 ? 195 GLY   A N    1 
ATOM   1508 C  CA   . GLY   A 1 195 ? -8.325  -1.875  -41.986 1   27.684 ? 195 GLY   A CA   1 
ATOM   1509 C  C    . GLY   A 1 195 ? -7.068  -2.42   -41.314 1   26.75  ? 195 GLY   A C    1 
ATOM   1510 O  O    . GLY   A 1 195 ? -6.965  -2.474  -40.089 1   26.749 ? 195 GLY   A O    1 
ATOM   1511 N  N    . THR   A 1 196 ? -6.108  -2.845  -42.134 1   26.403 ? 196 THR   A N    1 
ATOM   1512 C  CA   . THR   A 1 196 ? -4.835  -3.299  -41.612 1   26.474 ? 196 THR   A CA   1 
ATOM   1513 C  C    . THR   A 1 196 ? -4.187  -2.142  -40.863 1   24.937 ? 196 THR   A C    1 
ATOM   1514 O  O    . THR   A 1 196 ? -4.121  -1.014  -41.348 1   27.11  ? 196 THR   A O    1 
ATOM   1515 C  CB   . THR   A 1 196 ? -3.969  -3.813  -42.752 1   29.277 ? 196 THR   A CB   1 
ATOM   1516 O  OG1  . THR   A 1 196 ? -4.022  -2.752  -43.7   1   37.213 ? 196 THR   A OG1  1 
ATOM   1517 C  CG2  . THR   A 1 196 ? -4.527  -5.093  -43.344 1   28.017 ? 196 THR   A CG2  1 
ATOM   1518 N  N    . ASP   A 1 197 ? -3.742  -2.437  -39.65  1   22.54  ? 197 ASP   A N    1 
ATOM   1519 C  CA   . ASP   A 1 197 ? -3.144  -1.404  -38.841 1   21.697 ? 197 ASP   A CA   1 
ATOM   1520 C  C    . ASP   A 1 197 ? -1.665  -1.256  -39.184 1   19.786 ? 197 ASP   A C    1 
ATOM   1521 O  O    . ASP   A 1 197 ? -1.058  -2.133  -39.805 1   21.269 ? 197 ASP   A O    1 
ATOM   1522 C  CB   . ASP   A 1 197 ? -3.366  -1.66   -37.371 1   21.773 ? 197 ASP   A CB   1 
ATOM   1523 C  CG   . ASP   A 1 197 ? -3.268  -0.399  -36.531 1   21.473 ? 197 ASP   A CG   1 
ATOM   1524 O  OD1  . ASP   A 1 197 ? -3.553  0.727   -37.072 1   22.362 ? 197 ASP   A OD1  1 
ATOM   1525 O  OD2  . ASP   A 1 197 ? -2.864  -0.559  -35.389 1   21.502 ? 197 ASP   A OD2  1 
ATOM   1526 N  N    . THR   A 1 198 ? -1.138  -0.09   -38.807 1   16.733 ? 198 THR   A N    1 
ATOM   1527 C  CA   . THR   A 1 198 ? 0.238   0.286   -39.063 1   14.868 ? 198 THR   A CA   1 
ATOM   1528 C  C    . THR   A 1 198 ? 0.832   0.865   -37.786 1   13.052 ? 198 THR   A C    1 
ATOM   1529 O  O    . THR   A 1 198 ? 0.115   1.196   -36.848 1   13.045 ? 198 THR   A O    1 
ATOM   1530 C  CB   . THR   A 1 198 ? 0.288   1.297   -40.213 1   16.036 ? 198 THR   A CB   1 
ATOM   1531 O  OG1  . THR   A 1 198 ? -0.685  2.289   -39.915 1   18.188 ? 198 THR   A OG1  1 
ATOM   1532 C  CG2  . THR   A 1 198 ? -0.055  0.691   -41.562 1   17.343 ? 198 THR   A CG2  1 
ATOM   1533 N  N    . THR   A 1 199 ? 2.16    0.999   -37.765 1   11.803 ? 199 THR   A N    1 
ATOM   1534 C  CA   . THR   A 1 199 ? 2.874   1.5     -36.6   1   11.481 ? 199 THR   A CA   1 
ATOM   1535 C  C    . THR   A 1 199 ? 2.96    3.024   -36.653 1   11.618 ? 199 THR   A C    1 
ATOM   1536 O  O    . THR   A 1 199 ? 3.204   3.601   -37.711 1   12.262 ? 199 THR   A O    1 
ATOM   1537 C  CB   . THR   A 1 199 ? 4.258   0.846   -36.522 1   12.166 ? 199 THR   A CB   1 
ATOM   1538 O  OG1  . THR   A 1 199 ? 4.07    -0.564  -36.407 1   13.496 ? 199 THR   A OG1  1 
ATOM   1539 C  CG2  . THR   A 1 199 ? 5.076   1.358   -35.351 1   12.72  ? 199 THR   A CG2  1 
ATOM   1540 N  N    . ILE   A 1 200 ? 2.775   3.675   -35.491 1   10.994 ? 200 ILE   A N    1 
ATOM   1541 C  CA   . ILE   A 1 200 ? 2.741   5.125   -35.417 1   10.391 ? 200 ILE   A CA   1 
ATOM   1542 C  C    . ILE   A 1 200 ? 4.17    5.658   -35.304 1   10.521 ? 200 ILE   A C    1 
ATOM   1543 O  O    . ILE   A 1 200 ? 4.725   5.784   -34.213 1   10.658 ? 200 ILE   A O    1 
ATOM   1544 C  CB   . ILE   A 1 200 ? 1.868   5.61    -34.247 1   10.646 ? 200 ILE   A CB   1 
ATOM   1545 C  CG1  . ILE   A 1 200 ? 0.474   4.978   -34.273 1   11.408 ? 200 ILE   A CG1  1 
ATOM   1546 C  CG2  . ILE   A 1 200 ? 1.777   7.129   -34.264 1   10.806 ? 200 ILE   A CG2  1 
ATOM   1547 C  CD1  . ILE   A 1 200 ? -0.206  4.949   -32.921 1   11.282 ? 200 ILE   A CD1  1 
ATOM   1548 N  N    . THR   A 1 201 ? 4.76    5.991   -36.462 1   10.371 ? 201 THR   A N    1 
ATOM   1549 C  CA   . THR   A 1 201 ? 6.177   6.287   -36.572 1   10.543 ? 201 THR   A CA   1 
ATOM   1550 C  C    . THR   A 1 201 ? 6.604   7.429   -35.646 1   9.669  ? 201 THR   A C    1 
ATOM   1551 O  O    . THR   A 1 201 ? 7.626   7.339   -34.964 1   10.184 ? 201 THR   A O    1 
ATOM   1552 C  CB   . THR   A 1 201 ? 6.499   6.619   -38.026 1   11.087 ? 201 THR   A CB   1 
ATOM   1553 O  OG1  . THR   A 1 201 ? 5.99    5.518   -38.771 1   11.502 ? 201 THR   A OG1  1 
ATOM   1554 C  CG2  . THR   A 1 201 ? 7.988   6.808   -38.242 1   11.419 ? 201 THR   A CG2  1 
ATOM   1555 N  N    . VAL   A 1 202 ? 5.872   8.539   -35.654 1   9.839  ? 202 VAL   A N    1 
ATOM   1556 C  CA   . VAL   A 1 202 ? 6.249   9.702   -34.863 1   10.141 ? 202 VAL   A CA   1 
ATOM   1557 C  C    . VAL   A 1 202 ? 6.345   9.332   -33.379 1   9.955  ? 202 VAL   A C    1 
ATOM   1558 O  O    . VAL   A 1 202 ? 7.193   9.854   -32.656 1   10.265 ? 202 VAL   A O    1 
ATOM   1559 C  CB   . VAL   A 1 202 ? 5.306   10.892  -35.097 1   10.882 ? 202 VAL   A CB   1 
ATOM   1560 C  CG1  . VAL   A 1 202 ? 3.865   10.601  -34.702 1   11.004 ? 202 VAL   A CG1  1 
ATOM   1561 C  CG2  . VAL   A 1 202 ? 5.834   12.154  -34.429 1   11.669 ? 202 VAL   A CG2  1 
ATOM   1562 N  N    . ASN   A 1 203 ? 5.459   8.445   -32.926 1   9.626  ? 203 ASN   A N    1 
ATOM   1563 C  CA   . ASN   A 1 203 ? 5.457   8.008   -31.536 1   9.396  ? 203 ASN   A CA   1 
ATOM   1564 C  C    . ASN   A 1 203 ? 6.675   7.134   -31.226 1   9.495  ? 203 ASN   A C    1 
ATOM   1565 O  O    . ASN   A 1 203 ? 7.276   7.258   -30.155 1   9.897  ? 203 ASN   A O    1 
ATOM   1566 C  CB   . ASN   A 1 203 ? 4.163   7.276   -31.173 1   9.532  ? 203 ASN   A CB   1 
ATOM   1567 C  CG   . ASN   A 1 203 ? 2.96    8.189   -31.098 1   9.234  ? 203 ASN   A CG   1 
ATOM   1568 O  OD1  . ASN   A 1 203 ? 3.065   9.402   -31.31  1   8.901  ? 203 ASN   A OD1  1 
ATOM   1569 N  ND2  . ASN   A 1 203 ? 1.816   7.618   -30.749 1   9.753  ? 203 ASN   A ND2  1 
ATOM   1570 N  N    . VAL   A 1 204 ? 7.06    6.243   -32.143 1   9.285  ? 204 VAL   A N    1 
ATOM   1571 C  CA   . VAL   A 1 204 ? 8.255   5.436   -31.938 1   9.174  ? 204 VAL   A CA   1 
ATOM   1572 C  C    . VAL   A 1 204 ? 9.459   6.368   -31.774 1   9.339  ? 204 VAL   A C    1 
ATOM   1573 O  O    . VAL   A 1 204 ? 10.294  6.178   -30.88  1   9.255  ? 204 VAL   A O    1 
ATOM   1574 C  CB   . VAL   A 1 204 ? 8.491   4.417   -33.071 1   9.555  ? 204 VAL   A CB   1 
ATOM   1575 C  CG1  . VAL   A 1 204 ? 9.803   3.684   -32.844 1   9.805  ? 204 VAL   A CG1  1 
ATOM   1576 C  CG2  . VAL   A 1 204 ? 7.349   3.412   -33.169 1   9.84   ? 204 VAL   A CG2  1 
ATOM   1577 N  N    . LEU   A 1 205 ? 9.559   7.394   -32.63  1   9.127  ? 205 LEU   A N    1 
ATOM   1578 C  CA   . LEU   A 1 205 ? 10.673  8.331   -32.54  1   9.615  ? 205 LEU   A CA   1 
ATOM   1579 C  C    . LEU   A 1 205 ? 10.653  9.063   -31.195 1   9.473  ? 205 LEU   A C    1 
ATOM   1580 O  O    . LEU   A 1 205 ? 11.695  9.207   -30.552 1   9.642  ? 205 LEU   A O    1 
ATOM   1581 C  CB   . LEU   A 1 205 ? 10.643  9.3     -33.711 1   9.903  ? 205 LEU   A CB   1 
ATOM   1582 C  CG   . LEU   A 1 205 ? 10.952  8.667   -35.068 1   10.509 ? 205 LEU   A CG   1 
ATOM   1583 C  CD1  . LEU   A 1 205 ? 10.579  9.634   -36.164 1   10.973 ? 205 LEU   A CD1  1 
ATOM   1584 C  CD2  . LEU   A 1 205 ? 12.414  8.266   -35.177 1   10.938 ? 205 LEU   A CD2  1 
ATOM   1585 N  N    . ALA   A 1 206 ? 9.465   9.476   -30.737 1   9.656  ? 206 ALA   A N    1 
ATOM   1586 C  CA   . ALA   A 1 206 ? 9.344   10.144  -29.446 1   9.813  ? 206 ALA   A CA   1 
ATOM   1587 C  C    . ALA   A 1 206 ? 9.89    9.257   -28.322 1   9.588  ? 206 ALA   A C    1 
ATOM   1588 O  O    . ALA   A 1 206 ? 10.596  9.725   -27.424 1   9.776  ? 206 ALA   A O    1 
ATOM   1589 C  CB   . ALA   A 1 206 ? 7.904   10.51   -29.172 1   10.152 ? 206 ALA   A CB   1 
ATOM   1590 N  N    . TRP   A 1 207 ? 9.56    7.967   -28.38  1   9.665  ? 207 TRP   A N    1 
ATOM   1591 C  CA   . TRP   A 1 207 ? 9.959   7.015   -27.361 1   9.812  ? 207 TRP   A CA   1 
ATOM   1592 C  C    . TRP   A 1 207 ? 11.464  6.749   -27.411 1   9.657  ? 207 TRP   A C    1 
ATOM   1593 O  O    . TRP   A 1 207 ? 12.106  6.609   -26.368 1   10.036 ? 207 TRP   A O    1 
ATOM   1594 C  CB   . TRP   A 1 207 ? 9.1     5.762   -27.539 1   10.78  ? 207 TRP   A CB   1 
ATOM   1595 C  CG   . TRP   A 1 207 ? 9.468   4.562   -26.735 1   11.833 ? 207 TRP   A CG   1 
ATOM   1596 C  CD1  . TRP   A 1 207 ? 9.098   4.226   -25.461 1   12.558 ? 207 TRP   A CD1  1 
ATOM   1597 C  CD2  . TRP   A 1 207 ? 10.188  3.452   -27.272 1   12.817 ? 207 TRP   A CD2  1 
ATOM   1598 N  NE1  . TRP   A 1 207 ? 9.594   2.985   -25.166 1   13.316 ? 207 TRP   A NE1  1 
ATOM   1599 C  CE2  . TRP   A 1 207 ? 10.26   2.481   -26.26  1   13.604 ? 207 TRP   A CE2  1 
ATOM   1600 C  CE3  . TRP   A 1 207 ? 10.773  3.206   -28.517 1   13.738 ? 207 TRP   A CE3  1 
ATOM   1601 C  CZ2  . TRP   A 1 207 ? 10.899  1.26    -26.481 1   14.641 ? 207 TRP   A CZ2  1 
ATOM   1602 C  CZ3  . TRP   A 1 207 ? 11.406  2.006   -28.721 1   14.813 ? 207 TRP   A CZ3  1 
ATOM   1603 C  CH2  . TRP   A 1 207 ? 11.453  1.044   -27.721 1   14.981 ? 207 TRP   A CH2  1 
ATOM   1604 N  N    . LEU   A 1 208 ? 12.068  6.752   -28.609 1   9.516  ? 208 LEU   A N    1 
ATOM   1605 C  CA   . LEU   A 1 208 ? 13.521  6.668   -28.696 1   9.896  ? 208 LEU   A CA   1 
ATOM   1606 C  C    . LEU   A 1 208 ? 14.167  7.892   -28.051 1   9.414  ? 208 LEU   A C    1 
ATOM   1607 O  O    . LEU   A 1 208 ? 15.205  7.777   -27.378 1   10.08  ? 208 LEU   A O    1 
ATOM   1608 C  CB   . LEU   A 1 208 ? 13.993  6.492   -30.142 1   10.203 ? 208 LEU   A CB   1 
ATOM   1609 C  CG   . LEU   A 1 208 ? 13.618  5.158   -30.797 1   10.76  ? 208 LEU   A CG   1 
ATOM   1610 C  CD1  . LEU   A 1 208 ? 14.019  5.214   -32.258 1   11.305 ? 208 LEU   A CD1  1 
ATOM   1611 C  CD2  . LEU   A 1 208 ? 14.254  3.964   -30.125 1   11.493 ? 208 LEU   A CD2  1 
ATOM   1612 N  N    . TYR   A 1 209 ? 13.58   9.074   -28.253 1   9.505  ? 209 TYR   A N    1 
ATOM   1613 C  CA   . TYR   A 1 209 ? 14.056  10.268  -27.571 1   9.957  ? 209 TYR   A CA   1 
ATOM   1614 C  C    . TYR   A 1 209 ? 13.936  10.109  -26.053 1   10.017 ? 209 TYR   A C    1 
ATOM   1615 O  O    . TYR   A 1 209 ? 14.841  10.529  -25.329 1   10.672 ? 209 TYR   A O    1 
ATOM   1616 C  CB   . TYR   A 1 209 ? 13.358  11.546  -28.025 1   10.712 ? 209 TYR   A CB   1 
ATOM   1617 C  CG   . TYR   A 1 209 ? 13.893  12.1    -29.339 1   10.595 ? 209 TYR   A CG   1 
ATOM   1618 C  CD1  . TYR   A 1 209 ? 15.158  12.659  -29.402 1   11.222 ? 209 TYR   A CD1  1 
ATOM   1619 C  CD2  . TYR   A 1 209 ? 13.142  12.085  -30.51  1   11.125 ? 209 TYR   A CD2  1 
ATOM   1620 C  CE1  . TYR   A 1 209 ? 15.667  13.198  -30.566 1   11.17  ? 209 TYR   A CE1  1 
ATOM   1621 C  CE2  . TYR   A 1 209 ? 13.652  12.596  -31.693 1   11.127 ? 209 TYR   A CE2  1 
ATOM   1622 C  CZ   . TYR   A 1 209 ? 14.912  13.168  -31.725 1   11.492 ? 209 TYR   A CZ   1 
ATOM   1623 O  OH   . TYR   A 1 209 ? 15.427  13.69   -32.883 1   12.176 ? 209 TYR   A OH   1 
ATOM   1624 N  N    . ALA   A 1 210 ? 12.829  9.536   -25.571 1   9.735  ? 210 ALA   A N    1 
ATOM   1625 C  CA   . ALA   A 1 210 ? 12.669  9.282   -24.138 1   9.773  ? 210 ALA   A CA   1 
ATOM   1626 C  C    . ALA   A 1 210 ? 13.804  8.409   -23.626 1   9.807  ? 210 ALA   A C    1 
ATOM   1627 O  O    . ALA   A 1 210 ? 14.351  8.64    -22.549 1   9.889  ? 210 ALA   A O    1 
ATOM   1628 C  CB   . ALA   A 1 210 ? 11.346  8.619   -23.838 1   10.026 ? 210 ALA   A CB   1 
ATOM   1629 N  N    . ALA   A 1 211 ? 14.189  7.406   -24.416 1   9.719  ? 211 ALA   A N    1 
ATOM   1630 C  CA   . ALA   A 1 211 ? 15.255  6.507   -24.004 1   10.024 ? 211 ALA   A CA   1 
ATOM   1631 C  C    . ALA   A 1 211 ? 16.584  7.263   -23.877 1   9.995  ? 211 ALA   A C    1 
ATOM   1632 O  O    . ALA   A 1 211 ? 17.34   7.036   -22.929 1   10.415 ? 211 ALA   A O    1 
ATOM   1633 C  CB   . ALA   A 1 211 ? 15.333  5.349   -24.961 1   10.24  ? 211 ALA   A CB   1 
ATOM   1634 N  N    . VAL   A 1 212 ? 16.86   8.186   -24.802 1   10.147 ? 212 VAL   A N    1 
ATOM   1635 C  CA   . VAL   A 1 212 ? 18.075  8.984   -24.727 1   10.421 ? 212 VAL   A CA   1 
ATOM   1636 C  C    . VAL   A 1 212 ? 18.023  9.888   -23.492 1   10.439 ? 212 VAL   A C    1 
ATOM   1637 O  O    . VAL   A 1 212 ? 18.999  10.011  -22.745 1   10.935 ? 212 VAL   A O    1 
ATOM   1638 C  CB   . VAL   A 1 212 ? 18.337  9.789   -26.014 1   11.075 ? 212 VAL   A CB   1 
ATOM   1639 C  CG1  . VAL   A 1 212 ? 19.541  10.714  -25.864 1   11.483 ? 212 VAL   A CG1  1 
ATOM   1640 C  CG2  . VAL   A 1 212 ? 18.527  8.862   -27.203 1   11.217 ? 212 VAL   A CG2  1 
ATOM   1641 N  N    . ILE   A 1 213 ? 16.891  10.552  -23.272 1   10.62  ? 213 ILE   A N    1 
ATOM   1642 C  CA   . ILE   A 1 213 ? 16.728  11.435  -22.12  1   11.138 ? 213 ILE   A CA   1 
ATOM   1643 C  C    . ILE   A 1 213 ? 17.042  10.68   -20.834 1   11.471 ? 213 ILE   A C    1 
ATOM   1644 O  O    . ILE   A 1 213 ? 17.708  11.219  -19.941 1   12.205 ? 213 ILE   A O    1 
ATOM   1645 C  CB   . ILE   A 1 213 ? 15.321  12.062  -22.081 1   11.885 ? 213 ILE   A CB   1 
ATOM   1646 C  CG1  . ILE   A 1 213 ? 15.17   13.07   -23.212 1   12.675 ? 213 ILE   A CG1  1 
ATOM   1647 C  CG2  . ILE   A 1 213 ? 15.049  12.709  -20.726 1   12.428 ? 213 ILE   A CG2  1 
ATOM   1648 C  CD1  . ILE   A 1 213 ? 13.761  13.561  -23.444 1   13.467 ? 213 ILE   A CD1  1 
ATOM   1649 N  N    . ASN   A 1 214 ? 16.609  9.416   -20.78  1   11.24  ? 214 ASN   A N    1 
ATOM   1650 C  CA   . ASN   A 1 214 ? 16.768  8.6     -19.592 1   12.575 ? 214 ASN   A CA   1 
ATOM   1651 C  C    . ASN   A 1 214 ? 18.124  7.897   -19.541 1   12.574 ? 214 ASN   A C    1 
ATOM   1652 O  O    . ASN   A 1 214 ? 18.406  7.19    -18.571 1   14.779 ? 214 ASN   A O    1 
ATOM   1653 C  CB   . ASN   A 1 214 ? 15.605  7.637   -19.454 1   12.92  ? 214 ASN   A CB   1 
ATOM   1654 C  CG   . ASN   A 1 214 ? 14.35   8.317   -18.951 1   14.024 ? 214 ASN   A CG   1 
ATOM   1655 O  OD1  . ASN   A 1 214 ? 14.191  9.547   -19.012 1   15.59  ? 214 ASN   A OD1  1 
ATOM   1656 N  ND2  . ASN   A 1 214 ? 13.445  7.51    -18.434 1   16.498 ? 214 ASN   A ND2  1 
ATOM   1657 N  N    . GLY   A 1 215 ? 18.992  8.116   -20.536 1   12.013 ? 215 GLY   A N    1 
ATOM   1658 C  CA   . GLY   A 1 215 ? 20.393  7.774   -20.379 1   12.143 ? 215 GLY   A CA   1 
ATOM   1659 C  C    . GLY   A 1 215 ? 20.926  6.714   -21.335 1   12.599 ? 215 GLY   A C    1 
ATOM   1660 O  O    . GLY   A 1 215 ? 22.084  6.318   -21.159 1   15.428 ? 215 GLY   A O    1 
ATOM   1661 N  N    . ASP   A 1 216 ? 20.153  6.29    -22.352 1   12.063 ? 216 ASP   A N    1 
ATOM   1662 C  CA   . ASP   A 1 216 ? 20.609  5.212   -23.226 1   13.246 ? 216 ASP   A CA   1 
ATOM   1663 C  C    . ASP   A 1 216 ? 20.768  5.689   -24.663 1   12.507 ? 216 ASP   A C    1 
ATOM   1664 O  O    . ASP   A 1 216 ? 19.887  6.354   -25.2   1   13.693 ? 216 ASP   A O    1 
ATOM   1665 C  CB   . ASP   A 1 216 ? 19.749  3.965   -23.104 1   16.14  ? 216 ASP   A CB   1 
ATOM   1666 C  CG   . ASP   A 1 216 ? 20.068  3.193   -21.83  1   19.608 ? 216 ASP   A CG   1 
ATOM   1667 O  OD1  . ASP   A 1 216 ? 21.139  2.528   -21.77  1   22.966 ? 216 ASP   A OD1  1 
ATOM   1668 O  OD2  . ASP   A 1 216 ? 19.287  3.321   -20.872 1   23.637 ? 216 ASP   A OD2  1 
ATOM   1669 N  N    . ARG   A 1 217 ? 21.913  5.312   -25.269 1   11.916 ? 217 ARG   A N    1 
ATOM   1670 C  CA   . ARG   A 1 217 ? 22.292  5.731   -26.612 1   12.262 ? 217 ARG   A CA   1 
ATOM   1671 C  C    . ARG   A 1 217 ? 22.736  4.571   -27.491 1   11.255 ? 217 ARG   A C    1 
ATOM   1672 O  O    . ARG   A 1 217 ? 23.186  4.838   -28.612 1   12.06  ? 217 ARG   A O    1 
ATOM   1673 C  CB   . ARG   A 1 217 ? 23.499  6.676   -26.526 1   13.14  ? 217 ARG   A CB   1 
ATOM   1674 C  CG   . ARG   A 1 217 ? 23.213  8.018   -25.883 1   13.805 ? 217 ARG   A CG   1 
ATOM   1675 C  CD   . ARG   A 1 217 ? 24.389  8.948   -25.852 1   13.493 ? 217 ARG   A CD   1 
ATOM   1676 N  NE   . ARG   A 1 217 ? 24.879  9.266   -27.194 1   13.204 ? 217 ARG   A NE   1 
ATOM   1677 C  CZ   . ARG   A 1 217 ? 24.64   10.39   -27.86  1   12.973 ? 217 ARG   A CZ   1 
ATOM   1678 N  NH1  . ARG   A 1 217 ? 23.851  11.339  -27.386 1   12.949 ? 217 ARG   A NH1  1 
ATOM   1679 N  NH2  . ARG   A 1 217 ? 25.15   10.536  -29.067 1   13.089 ? 217 ARG   A NH2  1 
ATOM   1680 N  N    . TRP   A 1 218 ? 22.591  3.315   -27.05  1   11.25  ? 218 TRP   A N    1 
ATOM   1681 C  CA   . TRP   A 1 218 ? 23.233  2.189   -27.729 1   11.69  ? 218 TRP   A CA   1 
ATOM   1682 C  C    . TRP   A 1 218 ? 22.781  2.022   -29.179 1   11.562 ? 218 TRP   A C    1 
ATOM   1683 O  O    . TRP   A 1 218 ? 23.529  1.493   -29.999 1   11.837 ? 218 TRP   A O    1 
ATOM   1684 C  CB   . TRP   A 1 218 ? 23.036  0.88    -26.938 1   12.356 ? 218 TRP   A CB   1 
ATOM   1685 C  CG   . TRP   A 1 218 ? 21.635  0.332   -26.864 1   13.384 ? 218 TRP   A CG   1 
ATOM   1686 C  CD1  . TRP   A 1 218 ? 20.768  0.399   -25.804 1   14.451 ? 218 TRP   A CD1  1 
ATOM   1687 C  CD2  . TRP   A 1 218 ? 20.943  -0.424  -27.885 1   14.011 ? 218 TRP   A CD2  1 
ATOM   1688 N  NE1  . TRP   A 1 218 ? 19.603  -0.257  -26.105 1   15.152 ? 218 TRP   A NE1  1 
ATOM   1689 C  CE2  . TRP   A 1 218 ? 19.666  -0.755  -27.376 1   15.05  ? 218 TRP   A CE2  1 
ATOM   1690 C  CE3  . TRP   A 1 218 ? 21.257  -0.832  -29.186 1   14.78  ? 218 TRP   A CE3  1 
ATOM   1691 C  CZ2  . TRP   A 1 218 ? 18.731  -1.487  -28.106 1   15.748 ? 218 TRP   A CZ2  1 
ATOM   1692 C  CZ3  . TRP   A 1 218 ? 20.31   -1.525  -29.923 1   15.78  ? 218 TRP   A CZ3  1 
ATOM   1693 C  CH2  . TRP   A 1 218 ? 19.083  -1.881  -29.374 1   16.161 ? 218 TRP   A CH2  1 
ATOM   1694 N  N    . PHE   A 1 219 ? 21.553  2.457   -29.464 1   10.874 ? 219 PHE   A N    1 
ATOM   1695 C  CA   . PHE   A 1 219 ? 20.896  2.215   -30.742 1   11.14  ? 219 PHE   A CA   1 
ATOM   1696 C  C    . PHE   A 1 219 ? 21.166  3.33    -31.744 1   11.303 ? 219 PHE   A C    1 
ATOM   1697 O  O    . PHE   A 1 219 ? 20.73   3.209   -32.891 1   11.859 ? 219 PHE   A O    1 
ATOM   1698 C  CB   . PHE   A 1 219 ? 19.383  2.08    -30.511 1   11.306 ? 219 PHE   A CB   1 
ATOM   1699 C  CG   . PHE   A 1 219 ? 18.824  3.156   -29.594 1   11.301 ? 219 PHE   A CG   1 
ATOM   1700 C  CD1  . PHE   A 1 219 ? 18.482  4.415   -30.061 1   11.547 ? 219 PHE   A CD1  1 
ATOM   1701 C  CD2  . PHE   A 1 219 ? 18.68   2.897   -28.237 1   11.448 ? 219 PHE   A CD2  1 
ATOM   1702 C  CE1  . PHE   A 1 219 ? 18.006  5.395   -29.197 1   11.479 ? 219 PHE   A CE1  1 
ATOM   1703 C  CE2  . PHE   A 1 219 ? 18.222  3.876   -27.367 1   11.395 ? 219 PHE   A CE2  1 
ATOM   1704 C  CZ   . PHE   A 1 219 ? 17.896  5.125   -27.837 1   11.5   ? 219 PHE   A CZ   1 
ATOM   1705 N  N    . LEU   A 1 220 ? 21.833  4.412   -31.347 1   11.384 ? 220 LEU   A N    1 
ATOM   1706 C  CA   . LEU   A 1 220 ? 22.204  5.471   -32.276 1   11.952 ? 220 LEU   A CA   1 
ATOM   1707 C  C    . LEU   A 1 220 ? 23.273  4.989   -33.262 1   12.004 ? 220 LEU   A C    1 
ATOM   1708 O  O    . LEU   A 1 220 ? 23.923  3.972   -33.047 1   12.03  ? 220 LEU   A O    1 
ATOM   1709 C  CB   . LEU   A 1 220 ? 22.663  6.715   -31.527 1   12.762 ? 220 LEU   A CB   1 
ATOM   1710 C  CG   . LEU   A 1 220 ? 21.653  7.317   -30.548 1   13.259 ? 220 LEU   A CG   1 
ATOM   1711 C  CD1  . LEU   A 1 220 ? 22.285  8.495   -29.848 1   13.841 ? 220 LEU   A CD1  1 
ATOM   1712 C  CD2  . LEU   A 1 220 ? 20.364  7.732   -31.245 1   13.601 ? 220 LEU   A CD2  1 
ATOM   1713 N  N    . ASN   A 1 221 ? 23.435  5.733   -34.364 1   12.161 ? 221 ASN   A N    1 
ATOM   1714 C  CA   . ASN   A 1 221 ? 24.483  5.428   -35.332 1   12.252 ? 221 ASN   A CA   1 
ATOM   1715 C  C    . ASN   A 1 221 ? 25.021  6.726   -35.918 1   12.393 ? 221 ASN   A C    1 
ATOM   1716 O  O    . ASN   A 1 221 ? 24.538  7.805   -35.616 1   13.122 ? 221 ASN   A O    1 
ATOM   1717 C  CB   . ASN   A 1 221 ? 24.019  4.415   -36.377 1   12.886 ? 221 ASN   A CB   1 
ATOM   1718 C  CG   . ASN   A 1 221 ? 22.925  4.913   -37.286 1   14.548 ? 221 ASN   A CG   1 
ATOM   1719 O  OD1  . ASN   A 1 221 ? 22.857  6.095   -37.614 1   13.586 ? 221 ASN   A OD1  1 
ATOM   1720 N  ND2  . ASN   A 1 221 ? 22.036  4.021   -37.686 1   18.738 ? 221 ASN   A ND2  1 
ATOM   1721 N  N    . ARG   A 1 222 ? 26.018  6.596   -36.8   1   12.314 ? 222 ARG   A N    1 
ATOM   1722 C  CA   . ARG   A 1 222 ? 26.716  7.743   -37.356 1   13.421 ? 222 ARG   A CA   1 
ATOM   1723 C  C    . ARG   A 1 222 ? 26.025  8.299   -38.6   1   13.556 ? 222 ARG   A C    1 
ATOM   1724 O  O    . ARG   A 1 222 ? 26.521  9.256   -39.19  1   15.11  ? 222 ARG   A O    1 
ATOM   1725 C  CB   . ARG   A 1 222 ? 28.154  7.36    -37.719 1   14.499 ? 222 ARG   A CB   1 
ATOM   1726 C  CG   . ARG   A 1 222 ? 28.294  6.409   -38.905 1   15.471 ? 222 ARG   A CG   1 
ATOM   1727 C  CD   . ARG   A 1 222 ? 29.76   6.166   -39.195 1   17.455 ? 222 ARG   A CD   1 
ATOM   1728 N  NE   . ARG   A 1 222 ? 30.324  7.358   -39.831 1   20.455 ? 222 ARG   A NE   1 
ATOM   1729 C  CZ   . ARG   A 1 222 ? 31.59   7.547   -40.175 1   21.687 ? 222 ARG   A CZ   1 
ATOM   1730 N  NH1  . ARG   A 1 222 ? 32.54   6.703   -39.809 1   21.92  ? 222 ARG   A NH1  1 
ATOM   1731 N  NH2  . ARG   A 1 222 ? 31.917  8.619   -40.871 1   24.78  ? 222 ARG   A NH2  1 
ATOM   1732 N  N    . PHE   A 1 223 ? 24.896  7.71    -39.004 1   13.539 ? 223 PHE   A N    1 
ATOM   1733 C  CA   . PHE   A 1 223 ? 24.305  8.004   -40.303 1   14.569 ? 223 PHE   A CA   1 
ATOM   1734 C  C    . PHE   A 1 223 ? 23.133  8.975   -40.186 1   14.949 ? 223 PHE   A C    1 
ATOM   1735 O  O    . PHE   A 1 223 ? 22.61   9.261   -39.104 1   14.782 ? 223 PHE   A O    1 
ATOM   1736 C  CB   . PHE   A 1 223 ? 23.871  6.678   -40.93  1   16.268 ? 223 PHE   A CB   1 
ATOM   1737 C  CG   . PHE   A 1 223 ? 25.029  5.714   -41.127 1   18.19  ? 223 PHE   A CG   1 
ATOM   1738 C  CD1  . PHE   A 1 223 ? 26.027  6.002   -42.06  1   20.33  ? 223 PHE   A CD1  1 
ATOM   1739 C  CD2  . PHE   A 1 223 ? 25.137  4.554   -40.37  1   20.882 ? 223 PHE   A CD2  1 
ATOM   1740 C  CE1  . PHE   A 1 223 ? 27.09   5.134   -42.254 1   21.213 ? 223 PHE   A CE1  1 
ATOM   1741 C  CE2  . PHE   A 1 223 ? 26.211  3.691   -40.571 1   22.234 ? 223 PHE   A CE2  1 
ATOM   1742 C  CZ   . PHE   A 1 223 ? 27.188  3.992   -41.496 1   22.935 ? 223 PHE   A CZ   1 
ATOM   1743 N  N    . THR   A 1 224 ? 22.686  9.448   -41.352 1   16.255 ? 224 THR   A N    1 
ATOM   1744 C  CA   . THR   A 1 224 ? 21.463  10.225  -41.446 1   16.219 ? 224 THR   A CA   1 
ATOM   1745 C  C    . THR   A 1 224 ? 20.654  9.7     -42.629 1   15.341 ? 224 THR   A C    1 
ATOM   1746 O  O    . THR   A 1 224 ? 20.993  8.692   -43.243 1   16.258 ? 224 THR   A O    1 
ATOM   1747 C  CB   . THR   A 1 224 ? 21.794  11.717  -41.547 1   18.01  ? 224 THR   A CB   1 
ATOM   1748 O  OG1  . THR   A 1 224 ? 20.584  12.428  -41.267 1   20.133 ? 224 THR   A OG1  1 
ATOM   1749 C  CG2  . THR   A 1 224 ? 22.399  12.093  -42.89  1   18.927 ? 224 THR   A CG2  1 
ATOM   1750 N  N    . THR   A 1 225 ? 19.527  10.35   -42.874 1   13.819 ? 225 THR   A N    1 
ATOM   1751 C  CA   . THR   A 1 225 ? 18.654  9.963   -43.968 1   13.108 ? 225 THR   A CA   1 
ATOM   1752 C  C    . THR   A 1 225 ? 17.913  11.212  -44.422 1   13.063 ? 225 THR   A C    1 
ATOM   1753 O  O    . THR   A 1 225 ? 17.755  12.158  -43.644 1   13.878 ? 225 THR   A O    1 
ATOM   1754 C  CB   . THR   A 1 225 ? 17.706  8.856   -43.508 1   13.67  ? 225 THR   A CB   1 
ATOM   1755 O  OG1  . THR   A 1 225 ? 16.867  8.447   -44.584 1   13.838 ? 225 THR   A OG1  1 
ATOM   1756 C  CG2  . THR   A 1 225 ? 16.809  9.312   -42.374 1   13.793 ? 225 THR   A CG2  1 
ATOM   1757 N  N    . THR   A 1 226 ? 17.485  11.218  -45.689 1   12.238 ? 226 THR   A N    1 
ATOM   1758 C  CA   . THR   A 1 226 ? 16.462  12.172  -46.091 1   12.207 ? 226 THR   A CA   1 
ATOM   1759 C  C    . THR   A 1 226 ? 15.11   11.69   -45.558 1   11.756 ? 226 THR   A C    1 
ATOM   1760 O  O    . THR   A 1 226 ? 14.911  10.506  -45.285 1   11.644 ? 226 THR   A O    1 
ATOM   1761 C  CB   . THR   A 1 226 ? 16.397  12.395  -47.603 1   12.998 ? 226 THR   A CB   1 
ATOM   1762 O  OG1  . THR   A 1 226 ? 15.942  11.165  -48.15  1   12.701 ? 226 THR   A OG1  1 
ATOM   1763 C  CG2  . THR   A 1 226 ? 17.727  12.82   -48.201 1   13.871 ? 226 THR   A CG2  1 
ATOM   1764 N  N    . LEU   A 1 227 ? 14.169  12.623  -45.441 1   12.359 ? 227 LEU   A N    1 
ATOM   1765 C  CA   . LEU   A 1 227 ? 12.819  12.264  -45.039 1   12.8   ? 227 LEU   A CA   1 
ATOM   1766 C  C    . LEU   A 1 227 ? 12.215  11.281  -46.039 1   12.512 ? 227 LEU   A C    1 
ATOM   1767 O  O    . LEU   A 1 227 ? 11.601  10.286  -45.662 1   12.596 ? 227 LEU   A O    1 
ATOM   1768 C  CB   . LEU   A 1 227 ? 11.96   13.515  -44.9   1   13.975 ? 227 LEU   A CB   1 
ATOM   1769 C  CG   . LEU   A 1 227 ? 10.529  13.294  -44.402 1   14.509 ? 227 LEU   A CG   1 
ATOM   1770 C  CD1  . LEU   A 1 227 ? 10.498  12.59   -43.05  1   14.497 ? 227 LEU   A CD1  1 
ATOM   1771 C  CD2  . LEU   A 1 227 ? 9.835   14.628  -44.334 1   15.797 ? 227 LEU   A CD2  1 
ATOM   1772 N  N    . ASN   A 1 228 ? 12.419  11.535  -47.339 1   13.135 ? 228 ASN   A N    1 
ATOM   1773 C  CA   . ASN   A 1 228 ? 11.813  10.662  -48.332 1   14.184 ? 228 ASN   A CA   1 
ATOM   1774 C  C    . ASN   A 1 228 ? 12.407  9.258   -48.268 1   12.382 ? 228 ASN   A C    1 
ATOM   1775 O  O    . ASN   A 1 228 ? 11.675  8.282   -48.35  1   12.541 ? 228 ASN   A O    1 
ATOM   1776 C  CB   . ASN   A 1 228 ? 11.884  11.196  -49.751 1   16.545 ? 228 ASN   A CB   1 
ATOM   1777 C  CG   . ASN   A 1 228 ? 10.804  10.532  -50.582 1   20.546 ? 228 ASN   A CG   1 
ATOM   1778 O  OD1  . ASN   A 1 228 ? 11.11   9.773   -51.495 1   22.677 ? 228 ASN   A OD1  1 
ATOM   1779 N  ND2  . ASN   A 1 228 ? 9.536   10.719  -50.229 1   23.422 ? 228 ASN   A ND2  1 
ATOM   1780 N  N    . ASP   A 1 229 ? 13.733  9.13    -48.138 1   12.026 ? 229 ASP   A N    1 
ATOM   1781 C  CA   . ASP   A 1 229 ? 14.333  7.805   -48.063 1   11.982 ? 229 ASP   A CA   1 
ATOM   1782 C  C    . ASP   A 1 229 ? 13.896  7.078   -46.798 1   11.342 ? 229 ASP   A C    1 
ATOM   1783 O  O    . ASP   A 1 229 ? 13.685  5.867   -46.816 1   12.241 ? 229 ASP   A O    1 
ATOM   1784 C  CB   . ASP   A 1 229 ? 15.854  7.86    -48.148 1   12.88  ? 229 ASP   A CB   1 
ATOM   1785 C  CG   . ASP   A 1 229 ? 16.415  8.088   -49.544 1   14.01  ? 229 ASP   A CG   1 
ATOM   1786 O  OD1  . ASP   A 1 229 ? 15.64   7.91    -50.518 1   15.093 ? 229 ASP   A OD1  1 
ATOM   1787 O  OD2  . ASP   A 1 229 ? 17.619  8.416   -49.637 1   15.196 ? 229 ASP   A OD2  1 
ATOM   1788 N  N    . PHE   A 1 230 ? 13.757  7.814   -45.693 1   11.204 ? 230 PHE   A N    1 
ATOM   1789 C  CA   . PHE   A 1 230 ? 13.257  7.207   -44.473 1   11.615 ? 230 PHE   A CA   1 
ATOM   1790 C  C    . PHE   A 1 230 ? 11.867  6.608   -44.704 1   11.369 ? 230 PHE   A C    1 
ATOM   1791 O  O    . PHE   A 1 230 ? 11.62   5.462   -44.351 1   11.805 ? 230 PHE   A O    1 
ATOM   1792 C  CB   . PHE   A 1 230 ? 13.242  8.231   -43.339 1   11.725 ? 230 PHE   A CB   1 
ATOM   1793 C  CG   . PHE   A 1 230 ? 12.518  7.657   -42.133 1   12.428 ? 230 PHE   A CG   1 
ATOM   1794 C  CD1  . PHE   A 1 230 ? 13.114  6.696   -41.333 1   12.313 ? 230 PHE   A CD1  1 
ATOM   1795 C  CD2  . PHE   A 1 230 ? 11.203  8.011   -41.88  1   12.751 ? 230 PHE   A CD2  1 
ATOM   1796 C  CE1  . PHE   A 1 230 ? 12.43   6.147   -40.265 1   12.773 ? 230 PHE   A CE1  1 
ATOM   1797 C  CE2  . PHE   A 1 230 ? 10.518  7.454   -40.827 1   13.235 ? 230 PHE   A CE2  1 
ATOM   1798 C  CZ   . PHE   A 1 230 ? 11.139  6.53    -40.01  1   13.523 ? 230 PHE   A CZ   1 
ATOM   1799 N  N    . ASN   A 1 231 ? 10.979  7.383   -45.332 1   11.466 ? 231 ASN   A N    1 
ATOM   1800 C  CA   . ASN   A 1 231 ? 9.619   6.924   -45.556 1   12.312 ? 231 ASN   A CA   1 
ATOM   1801 C  C    . ASN   A 1 231 ? 9.588   5.721   -46.491 1   12.133 ? 231 ASN   A C    1 
ATOM   1802 O  O    . ASN   A 1 231 ? 8.81    4.8     -46.294 1   12.898 ? 231 ASN   A O    1 
ATOM   1803 C  CB   . ASN   A 1 231 ? 8.745   8.066   -46.041 1   12.521 ? 231 ASN   A CB   1 
ATOM   1804 C  CG   . ASN   A 1 231 ? 8.31    8.951   -44.901 1   13.419 ? 231 ASN   A CG   1 
ATOM   1805 O  OD1  . ASN   A 1 231 ? 8.041   8.457   -43.797 1   15.483 ? 231 ASN   A OD1  1 
ATOM   1806 N  ND2  . ASN   A 1 231 ? 8.257   10.25   -45.13  1   15.224 ? 231 ASN   A ND2  1 
ATOM   1807 N  N    . LEU   A 1 232 ? 10.441  5.72    -47.526 1   11.768 ? 232 LEU   A N    1 
ATOM   1808 C  CA   . LEU   A 1 232 ? 10.486  4.582   -48.429 1   12.313 ? 232 LEU   A CA   1 
ATOM   1809 C  C    . LEU   A 1 232 ? 10.863  3.301   -47.685 1   12.233 ? 232 LEU   A C    1 
ATOM   1810 O  O    . LEU   A 1 232 ? 10.309  2.238   -47.945 1   13.923 ? 232 LEU   A O    1 
ATOM   1811 C  CB   . LEU   A 1 232 ? 11.441  4.856   -49.595 1   12.549 ? 232 LEU   A CB   1 
ATOM   1812 C  CG   . LEU   A 1 232 ? 10.956  5.892   -50.611 1   13.252 ? 232 LEU   A CG   1 
ATOM   1813 C  CD1  . LEU   A 1 232 ? 12.096  6.31    -51.526 1   12.867 ? 232 LEU   A CD1  1 
ATOM   1814 C  CD2  . LEU   A 1 232 ? 9.809   5.322   -51.424 1   15.031 ? 232 LEU   A CD2  1 
ATOM   1815 N  N    . VAL   A 1 233 ? 11.811  3.389   -46.742 1   12.162 ? 233 VAL   A N    1 
ATOM   1816 C  CA   . VAL   A 1 233 ? 12.201  2.208   -45.983 1   12.658 ? 233 VAL   A CA   1 
ATOM   1817 C  C    . VAL   A 1 233 ? 11.124  1.84    -44.962 1   12.595 ? 233 VAL   A C    1 
ATOM   1818 O  O    . VAL   A 1 233 ? 10.739  0.678   -44.851 1   12.471 ? 233 VAL   A O    1 
ATOM   1819 C  CB   . VAL   A 1 233 ? 13.566  2.431   -45.307 1   13.399 ? 233 VAL   A CB   1 
ATOM   1820 C  CG1  . VAL   A 1 233 ? 13.906  1.338   -44.29  1   14.031 ? 233 VAL   A CG1  1 
ATOM   1821 C  CG2  . VAL   A 1 233 ? 14.668  2.553   -46.342 1   13.972 ? 233 VAL   A CG2  1 
ATOM   1822 N  N    . ALA   A 1 234 ? 10.672  2.826   -44.186 1   13.33  ? 234 ALA   A N    1 
ATOM   1823 C  CA   . ALA   A 1 234 ? 9.828   2.529   -43.045 1   14.356 ? 234 ALA   A CA   1 
ATOM   1824 C  C    . ALA   A 1 234 ? 8.506   1.922   -43.52  1   13.945 ? 234 ALA   A C    1 
ATOM   1825 O  O    . ALA   A 1 234 ? 7.946   1.049   -42.862 1   13.463 ? 234 ALA   A O    1 
ATOM   1826 C  CB   . ALA   A 1 234 ? 9.637   3.771   -42.21  1   15.668 ? 234 ALA   A CB   1 
ATOM   1827 N  N    . MET   A 1 235 ? 8.002   2.345   -44.676 1   14.633 ? 235 MET   A N    1 
ATOM   1828 C  CA   . MET   A 1 235 ? 6.749   1.809   -45.179 1   15.62  ? 235 MET   A CA   1 
ATOM   1829 C  C    . MET   A 1 235 ? 6.878   0.312   -45.467 1   14.288 ? 235 MET   A C    1 
ATOM   1830 O  O    . MET   A 1 235 ? 5.882   -0.407  -45.415 1   14.624 ? 235 MET   A O    1 
ATOM   1831 C  CB   . MET   A 1 235 ? 6.253   2.685   -46.333 1   18.988 ? 235 MET   A CB   1 
ATOM   1832 C  CG   . MET   A 1 235 ? 5.901   4.067   -45.783 1   23.43  ? 235 MET   A CG   1 
ATOM   1833 S  SD   . MET   A 1 235 ? 5.231   5.298   -46.915 1   33.255 ? 235 MET   A SD   1 
ATOM   1834 C  CE   . MET   A 1 235 ? 3.572   4.635   -47.123 1   32.931 ? 235 MET   A CE   1 
ATOM   1835 N  N    . LYS   A 1 236 ? 8.101   -0.18   -45.709 1   14.039 ? 236 LYS   A N    1 
ATOM   1836 C  CA   . LYS   A 1 236 ? 8.296   -1.591  -45.981 1   14.517 ? 236 LYS   A CA   1 
ATOM   1837 C  C    . LYS   A 1 236 ? 8.109   -2.419  -44.711 1   13.819 ? 236 LYS   A C    1 
ATOM   1838 O  O    . LYS   A 1 236 ? 7.952   -3.632  -44.786 1   16.051 ? 236 LYS   A O    1 
ATOM   1839 C  CB   . LYS   A 1 236 ? 9.659   -1.843  -46.635 1   15.268 ? 236 LYS   A CB   1 
ATOM   1840 C  CG   . LYS   A 1 236 ? 9.837   -1.146  -47.988 1   16.952 ? 236 LYS   A CG   1 
ATOM   1841 C  CD   . LYS   A 1 236 ? 11.216  -1.147  -48.642 1   18.847 ? 236 LYS   A CD   1 
ATOM   1842 C  CE   . LYS   A 1 236 ? 11.211  -0.329  -49.91  1   19.579 ? 236 LYS   A CE   1 
ATOM   1843 N  NZ   . LYS   A 1 236 ? 12.522  -0.28   -50.561 1   20.599 ? 236 LYS   A NZ   1 
ATOM   1844 N  N    . TYR   A 1 237 ? 8.133   -1.774  -43.541 1   13.004 ? 237 TYR   A N    1 
ATOM   1845 C  CA   . TYR   A 1 237 ? 7.867   -2.452  -42.282 1   12.942 ? 237 TYR   A CA   1 
ATOM   1846 C  C    . TYR   A 1 237 ? 6.492   -2.075  -41.725 1   13.589 ? 237 TYR   A C    1 
ATOM   1847 O  O    . TYR   A 1 237 ? 6.233   -2.278  -40.54  1   14.449 ? 237 TYR   A O    1 
ATOM   1848 C  CB   . TYR   A 1 237 ? 8.94    -2.097  -41.263 1   12.778 ? 237 TYR   A CB   1 
ATOM   1849 C  CG   . TYR   A 1 237 ? 10.369  -2.433  -41.628 1   12.728 ? 237 TYR   A CG   1 
ATOM   1850 C  CD1  . TYR   A 1 237 ? 11.162  -1.518  -42.296 1   12.799 ? 237 TYR   A CD1  1 
ATOM   1851 C  CD2  . TYR   A 1 237 ? 10.922  -3.653  -41.271 1   13.327 ? 237 TYR   A CD2  1 
ATOM   1852 C  CE1  . TYR   A 1 237 ? 12.487  -1.802  -42.598 1   12.117 ? 237 TYR   A CE1  1 
ATOM   1853 C  CE2  . TYR   A 1 237 ? 12.245  -3.95   -41.556 1   13.026 ? 237 TYR   A CE2  1 
ATOM   1854 C  CZ   . TYR   A 1 237 ? 13.027  -3.021  -42.223 1   12.921 ? 237 TYR   A CZ   1 
ATOM   1855 O  OH   . TYR   A 1 237 ? 14.349  -3.267  -42.45  1   13.892 ? 237 TYR   A OH   1 
ATOM   1856 N  N    . ASN   A 1 238 ? 5.588   -1.563  -42.566 1   13.865 ? 238 ASN   A N    1 
ATOM   1857 C  CA   . ASN   A 1 238 ? 4.221   -1.259  -42.167 1   14.263 ? 238 ASN   A CA   1 
ATOM   1858 C  C    . ASN   A 1 238 ? 4.194   -0.107  -41.156 1   12.366 ? 238 ASN   A C    1 
ATOM   1859 O  O    . ASN   A 1 238 ? 3.308   -0.061  -40.313 1   13.422 ? 238 ASN   A O    1 
ATOM   1860 C  CB   . ASN   A 1 238 ? 3.541   -2.527  -41.653 1   16.729 ? 238 ASN   A CB   1 
ATOM   1861 C  CG   . ASN   A 1 238 ? 2.041   -2.447  -41.703 1   21.437 ? 238 ASN   A CG   1 
ATOM   1862 O  OD1  . ASN   A 1 238 ? 1.502   -2.022  -42.726 1   26.693 ? 238 ASN   A OD1  1 
ATOM   1863 N  ND2  . ASN   A 1 238 ? 1.36    -2.849  -40.638 1   24.792 ? 238 ASN   A ND2  1 
ATOM   1864 N  N    . TYR   A 1 239 ? 5.114   0.849   -41.278 1   11.543 ? 239 TYR   A N    1 
ATOM   1865 C  CA   . TYR   A 1 239 ? 5.099   2.097   -40.523 1   11.212 ? 239 TYR   A CA   1 
ATOM   1866 C  C    . TYR   A 1 239 ? 4.359   3.193   -41.283 1   12.604 ? 239 TYR   A C    1 
ATOM   1867 O  O    . TYR   A 1 239 ? 4.445   3.269   -42.513 1   13.469 ? 239 TYR   A O    1 
ATOM   1868 C  CB   . TYR   A 1 239 ? 6.523   2.58    -40.231 1   11.213 ? 239 TYR   A CB   1 
ATOM   1869 C  CG   . TYR   A 1 239 ? 7.157   1.942   -39.002 1   11.05  ? 239 TYR   A CG   1 
ATOM   1870 C  CD1  . TYR   A 1 239 ? 7.183   0.562   -38.81  1   11.723 ? 239 TYR   A CD1  1 
ATOM   1871 C  CD2  . TYR   A 1 239 ? 7.701   2.739   -38.008 1   11.69  ? 239 TYR   A CD2  1 
ATOM   1872 C  CE1  . TYR   A 1 239 ? 7.714   -0.006  -37.656 1   12.065 ? 239 TYR   A CE1  1 
ATOM   1873 C  CE2  . TYR   A 1 239 ? 8.228   2.185   -36.854 1   11.948 ? 239 TYR   A CE2  1 
ATOM   1874 C  CZ   . TYR   A 1 239 ? 8.231   0.816   -36.67  1   11.743 ? 239 TYR   A CZ   1 
ATOM   1875 O  OH   . TYR   A 1 239 ? 8.771   0.349   -35.487 1   12.801 ? 239 TYR   A OH   1 
ATOM   1876 N  N    . GLU   A 1 240 ? 3.641   4.04    -40.542 1   12.821 ? 240 GLU   A N    1 
ATOM   1877 C  CA   . GLU   A 1 240 ? 2.994   5.213   -41.1   1   14.12  ? 240 GLU   A CA   1 
ATOM   1878 C  C    . GLU   A 1 240 ? 4.028   6.168   -41.671 1   13.962 ? 240 GLU   A C    1 
ATOM   1879 O  O    . GLU   A 1 240 ? 5.138   6.266   -41.159 1   12.981 ? 240 GLU   A O    1 
ATOM   1880 C  CB   . GLU   A 1 240 ? 2.179   5.927   -40.017 1   16.099 ? 240 GLU   A CB   1 
ATOM   1881 C  CG   . GLU   A 1 240 ? 0.855   5.225   -39.761 1   18.547 ? 240 GLU   A CG   1 
ATOM   1882 C  CD   . GLU   A 1 240 ? -0.092  5.355   -40.941 1   20.883 ? 240 GLU   A CD   1 
ATOM   1883 O  OE1  . GLU   A 1 240 ? -0.421  6.502   -41.297 1   26.412 ? 240 GLU   A OE1  1 
ATOM   1884 O  OE2  . GLU   A 1 240 ? -0.499  4.318   -41.508 1   24.828 ? 240 GLU   A OE2  1 
ATOM   1885 N  N    . PRO   A 1 241 ? 3.685   6.938   -42.727 1   14.515 ? 241 PRO   A N    1 
ATOM   1886 C  CA   . PRO   A 1 241 ? 4.561   8.011   -43.18  1   14.981 ? 241 PRO   A CA   1 
ATOM   1887 C  C    . PRO   A 1 241 ? 4.845   9.019   -42.074 1   14.189 ? 241 PRO   A C    1 
ATOM   1888 O  O    . PRO   A 1 241 ? 3.976   9.337   -41.254 1   15.386 ? 241 PRO   A O    1 
ATOM   1889 C  CB   . PRO   A 1 241 ? 3.793   8.65    -44.347 1   15.935 ? 241 PRO   A CB   1 
ATOM   1890 C  CG   . PRO   A 1 241 ? 2.819   7.585   -44.774 1   16.246 ? 241 PRO   A CG   1 
ATOM   1891 C  CD   . PRO   A 1 241 ? 2.454   6.82    -43.521 1   15.829 ? 241 PRO   A CD   1 
ATOM   1892 N  N    . LEU   A 1 242 ? 6.088   9.499   -42.058 1   13.288 ? 242 LEU   A N    1 
ATOM   1893 C  CA   . LEU   A 1 242 ? 6.489   10.624  -41.239 1   13.196 ? 242 LEU   A CA   1 
ATOM   1894 C  C    . LEU   A 1 242 ? 6.41    11.882  -42.094 1   13.373 ? 242 LEU   A C    1 
ATOM   1895 O  O    . LEU   A 1 242 ? 7.008   11.941  -43.166 1   14.548 ? 242 LEU   A O    1 
ATOM   1896 C  CB   . LEU   A 1 242 ? 7.911   10.387  -40.733 1   13.378 ? 242 LEU   A CB   1 
ATOM   1897 C  CG   . LEU   A 1 242 ? 8.376   11.304  -39.606 1   13.422 ? 242 LEU   A CG   1 
ATOM   1898 C  CD1  . LEU   A 1 242 ? 7.677   10.921  -38.314 1   13.314 ? 242 LEU   A CD1  1 
ATOM   1899 C  CD2  . LEU   A 1 242 ? 9.864   11.272  -39.456 1   13.629 ? 242 LEU   A CD2  1 
ATOM   1900 N  N    . THR   A 1 243 ? 5.667   12.874  -41.605 1   13.38  ? 243 THR   A N    1 
ATOM   1901 C  CA   . THR   A 1 243 ? 5.447   14.122  -42.306 1   14.296 ? 243 THR   A CA   1 
ATOM   1902 C  C    . THR   A 1 243 ? 6.358   15.201  -41.742 1   14.033 ? 243 THR   A C    1 
ATOM   1903 O  O    . THR   A 1 243 ? 6.928   15.054  -40.658 1   13.597 ? 243 THR   A O    1 
ATOM   1904 C  CB   . THR   A 1 243 ? 3.987   14.547  -42.172 1   14.187 ? 243 THR   A CB   1 
ATOM   1905 O  OG1  . THR   A 1 243 ? 3.766   14.891  -40.8   1   15.498 ? 243 THR   A OG1  1 
ATOM   1906 C  CG2  . THR   A 1 243 ? 3.034   13.456  -42.612 1   14.263 ? 243 THR   A CG2  1 
ATOM   1907 N  N    . GLN   A 1 244 ? 6.443   16.316  -42.462 1   14.978 ? 244 GLN   A N    1 
ATOM   1908 C  CA   . GLN   A 1 244 ? 7.176   17.464  -41.968 1   15.337 ? 244 GLN   A CA   1 
ATOM   1909 C  C    . GLN   A 1 244 ? 6.552   17.967  -40.669 1   15.015 ? 244 GLN   A C    1 
ATOM   1910 O  O    . GLN   A 1 244 ? 7.279   18.431  -39.798 1   16.749 ? 244 GLN   A O    1 
ATOM   1911 C  CB   . GLN   A 1 244 ? 7.303   18.553  -43.036 1   16.045 ? 244 GLN   A CB   1 
ATOM   1912 C  CG   . GLN   A 1 244 ? 8.193   19.715  -42.611 1   17.679 ? 244 GLN   A CG   1 
ATOM   1913 C  CD   . GLN   A 1 244 ? 9.617   19.296  -42.31  1   18.664 ? 244 GLN   A CD   1 
ATOM   1914 O  OE1  . GLN   A 1 244 ? 10.215  18.468  -43.007 1   20.336 ? 244 GLN   A OE1  1 
ATOM   1915 N  NE2  . GLN   A 1 244 ? 10.163  19.823  -41.226 1   19.627 ? 244 GLN   A NE2  1 
ATOM   1916 N  N    . ASP   A 1 245 ? 5.223   17.852  -40.511 1   14.974 ? 245 ASP   A N    1 
ATOM   1917 C  CA   . ASP   A 1 245 ? 4.59    18.222  -39.248 1   15.437 ? 245 ASP   A CA   1 
ATOM   1918 C  C    . ASP   A 1 245 ? 5.165   17.4    -38.097 1   14.307 ? 245 ASP   A C    1 
ATOM   1919 O  O    . ASP   A 1 245 ? 5.449   17.93   -37.025 1   15.009 ? 245 ASP   A O    1 
ATOM   1920 C  CB   . ASP   A 1 245 ? 3.079   18.069  -39.279 1   16.258 ? 245 ASP   A CB   1 
ATOM   1921 C  CG   . ASP   A 1 245 ? 2.328   19.162  -40.014 1   17.997 ? 245 ASP   A CG   1 
ATOM   1922 O  OD1  . ASP   A 1 245 ? 2.985   20.078  -40.558 1   19.527 ? 245 ASP   A OD1  1 
ATOM   1923 O  OD2  . ASP   A 1 245 ? 1.085   19.095  -40.001 1   20.549 ? 245 ASP   A OD2  1 
ATOM   1924 N  N    . HIS   A 1 246 ? 5.326   16.096  -38.316 1   13.823 ? 246 HIS   A N    1 
ATOM   1925 C  CA   . HIS   A 1 246 ? 5.897   15.22   -37.309 1   13.348 ? 246 HIS   A CA   1 
ATOM   1926 C  C    . HIS   A 1 246 ? 7.331   15.629  -36.984 1   13.68  ? 246 HIS   A C    1 
ATOM   1927 O  O    . HIS   A 1 246 ? 7.724   15.641  -35.818 1   14.286 ? 246 HIS   A O    1 
ATOM   1928 C  CB   . HIS   A 1 246 ? 5.858   13.773  -37.782 1   13.974 ? 246 HIS   A CB   1 
ATOM   1929 C  CG   . HIS   A 1 246 ? 4.505   13.209  -37.97  1   14.438 ? 246 HIS   A CG   1 
ATOM   1930 N  ND1  . HIS   A 1 246 ? 4.236   12.257  -38.929 1   14.965 ? 246 HIS   A ND1  1 
ATOM   1931 C  CD2  . HIS   A 1 246 ? 3.354   13.418  -37.307 1   15.204 ? 246 HIS   A CD2  1 
ATOM   1932 C  CE1  . HIS   A 1 246 ? 2.953   11.922  -38.854 1   15.961 ? 246 HIS   A CE1  1 
ATOM   1933 N  NE2  . HIS   A 1 246 ? 2.4     12.612  -37.877 1   15.305 ? 246 HIS   A NE2  1 
ATOM   1934 N  N    . VAL   A 1 247 ? 8.121   15.951  -38.012 1   13.476 ? 247 VAL   A N    1 
ATOM   1935 C  CA   . VAL   A 1 247 ? 9.487   16.398  -37.794 1   13.727 ? 247 VAL   A CA   1 
ATOM   1936 C  C    . VAL   A 1 247 ? 9.486   17.667  -36.94  1   14.549 ? 247 VAL   A C    1 
ATOM   1937 O  O    . VAL   A 1 247 ? 10.275  17.791  -36     1   15.036 ? 247 VAL   A O    1 
ATOM   1938 C  CB   . VAL   A 1 247 ? 10.232  16.61   -39.128 1   14.049 ? 247 VAL   A CB   1 
ATOM   1939 C  CG1  . VAL   A 1 247 ? 11.604  17.246  -38.916 1   14.384 ? 247 VAL   A CG1  1 
ATOM   1940 C  CG2  . VAL   A 1 247 ? 10.369  15.3    -39.9   1   14.736 ? 247 VAL   A CG2  1 
ATOM   1941 N  N    . ASP   A 1 248 ? 8.59    18.603  -37.265 1   15.137 ? 248 ASP   A N    1 
ATOM   1942 C  CA   . ASP   A 1 248 ? 8.494   19.854  -36.533 1   15.96  ? 248 ASP   A CA   1 
ATOM   1943 C  C    . ASP   A 1 248 ? 8.154   19.594  -35.064 1   15.932 ? 248 ASP   A C    1 
ATOM   1944 O  O    . ASP   A 1 248 ? 8.758   20.188  -34.167 1   15.714 ? 248 ASP   A O    1 
ATOM   1945 C  CB   . ASP   A 1 248 ? 7.498   20.791  -37.197 1   16.852 ? 248 ASP   A CB   1 
ATOM   1946 C  CG   . ASP   A 1 248 ? 7.928   21.376  -38.536 1   18.188 ? 248 ASP   A CG   1 
ATOM   1947 O  OD1  . ASP   A 1 248 ? 9.115   21.227  -38.9   1   19.748 ? 248 ASP   A OD1  1 
ATOM   1948 O  OD2  . ASP   A 1 248 ? 7.062   21.968  -39.212 1   20.047 ? 248 ASP   A OD2  1 
ATOM   1949 N  N    . ILE   A 1 249 ? 7.185   18.713  -34.805 1   15.636 ? 249 ILE   A N    1 
ATOM   1950 C  CA   . ILE   A 1 249 ? 6.742   18.524  -33.429 1   16.88  ? 249 ILE   A CA   1 
ATOM   1951 C  C    . ILE   A 1 249 ? 7.769   17.754  -32.602 1   15.472 ? 249 ILE   A C    1 
ATOM   1952 O  O    . ILE   A 1 249 ? 7.728   17.85   -31.373 1   16.281 ? 249 ILE   A O    1 
ATOM   1953 C  CB   . ILE   A 1 249 ? 5.341   17.911  -33.354 1   19.847 ? 249 ILE   A CB   1 
ATOM   1954 C  CG1  . ILE   A 1 249 ? 5.284   16.508  -33.875 1   21.917 ? 249 ILE   A CG1  1 
ATOM   1955 C  CG2  . ILE   A 1 249 ? 4.331   18.815  -34.051 1   21.252 ? 249 ILE   A CG2  1 
ATOM   1956 C  CD1  . ILE   A 1 249 ? 5.904   15.488  -32.966 1   24.539 ? 249 ILE   A CD1  1 
ATOM   1957 N  N    . LEU   A 1 250 ? 8.7     17.032  -33.25  1   14.073 ? 250 LEU   A N    1 
ATOM   1958 C  CA   . LEU   A 1 250 ? 9.811   16.386  -32.554 1   13.825 ? 250 LEU   A CA   1 
ATOM   1959 C  C    . LEU   A 1 250 ? 10.938  17.364  -32.224 1   14.255 ? 250 LEU   A C    1 
ATOM   1960 O  O    . LEU   A 1 250 ? 11.89   16.976  -31.555 1   14.859 ? 250 LEU   A O    1 
ATOM   1961 C  CB   . LEU   A 1 250 ? 10.334  15.196  -33.357 1   12.866 ? 250 LEU   A CB   1 
ATOM   1962 C  CG   . LEU   A 1 250 ? 9.408   13.974  -33.397 1   13.092 ? 250 LEU   A CG   1 
ATOM   1963 C  CD1  . LEU   A 1 250 ? 9.842   13.019  -34.502 1   13.548 ? 250 LEU   A CD1  1 
ATOM   1964 C  CD2  . LEU   A 1 250 ? 9.375   13.235  -32.077 1   13.159 ? 250 LEU   A CD2  1 
ATOM   1965 N  N    . GLY   A 1 251 ? 10.83   18.625  -32.653 1   14.25  ? 251 GLY   A N    1 
ATOM   1966 C  CA   . GLY   A 1 251 ? 11.894  19.599  -32.457 1   15.383 ? 251 GLY   A CA   1 
ATOM   1967 C  C    . GLY   A 1 251 ? 12.315  19.751  -30.995 1   15.411 ? 251 GLY   A C    1 
ATOM   1968 O  O    . GLY   A 1 251 ? 13.502  19.74   -30.694 1   15.532 ? 251 GLY   A O    1 
ATOM   1969 N  N    . PRO   A 1 252 ? 11.391  19.962  -30.04  1   16.123 ? 252 PRO   A N    1 
ATOM   1970 C  CA   . PRO   A 1 252 ? 11.797  20.085  -28.632 1   15.69  ? 252 PRO   A CA   1 
ATOM   1971 C  C    . PRO   A 1 252 ? 12.614  18.908  -28.1   1   14.205 ? 252 PRO   A C    1 
ATOM   1972 O  O    . PRO   A 1 252 ? 13.622  19.123  -27.419 1   14.767 ? 252 PRO   A O    1 
ATOM   1973 C  CB   . PRO   A 1 252 ? 10.438  20.273  -27.934 1   16.701 ? 252 PRO   A CB   1 
ATOM   1974 C  CG   . PRO   A 1 252 ? 9.641   21.018  -28.98  1   17.197 ? 252 PRO   A CG   1 
ATOM   1975 C  CD   . PRO   A 1 252 ? 9.964   20.257  -30.258 1   17.159 ? 252 PRO   A CD   1 
ATOM   1976 N  N    . LEU   A 1 253 ? 12.21   17.677  -28.425 1   13.1   ? 253 LEU   A N    1 
ATOM   1977 C  CA   . LEU   A 1 253 ? 12.939  16.492  -27.986 1   12.431 ? 253 LEU   A CA   1 
ATOM   1978 C  C    . LEU   A 1 253 ? 14.315  16.424  -28.644 1   12.576 ? 253 LEU   A C    1 
ATOM   1979 O  O    . LEU   A 1 253 ? 15.312  16.058  -28.016 1   12.722 ? 253 LEU   A O    1 
ATOM   1980 C  CB   . LEU   A 1 253 ? 12.126  15.227  -28.24  1   12.675 ? 253 LEU   A CB   1 
ATOM   1981 C  CG   . LEU   A 1 253 ? 10.894  15.063  -27.339 1   13.41  ? 253 LEU   A CG   1 
ATOM   1982 C  CD1  . LEU   A 1 253 ? 10.063  13.884  -27.791 1   14.083 ? 253 LEU   A CD1  1 
ATOM   1983 C  CD2  . LEU   A 1 253 ? 11.292  14.875  -25.898 1   14.28  ? 253 LEU   A CD2  1 
ATOM   1984 N  N    . SER   A 1 254 ? 14.369  16.791  -29.922 1   12.288 ? 254 SER   A N    1 
ATOM   1985 C  CA   . SER   A 1 254 ? 15.63   16.877  -30.639 1   13.147 ? 254 SER   A CA   1 
ATOM   1986 C  C    . SER   A 1 254 ? 16.583  17.868  -29.961 1   13.535 ? 254 SER   A C    1 
ATOM   1987 O  O    . SER   A 1 254 ? 17.772  17.586  -29.788 1   14.322 ? 254 SER   A O    1 
ATOM   1988 C  CB   . SER   A 1 254 ? 15.363  17.241  -32.081 1   13.947 ? 254 SER   A CB   1 
ATOM   1989 O  OG   . SER   A 1 254 ? 16.584  17.398  -32.78  1   16.239 ? 254 SER   A OG   1 
ATOM   1990 N  N    . ALA   A 1 255 ? 16.065  19.043  -29.58  1   14.14  ? 255 ALA   A N    1 
ATOM   1991 C  CA   . ALA   A 1 255 ? 16.889  20.069  -28.947 1   15.086 ? 255 ALA   A CA   1 
ATOM   1992 C  C    . ALA   A 1 255 ? 17.394  19.611  -27.582 1   14.856 ? 255 ALA   A C    1 
ATOM   1993 O  O    . ALA   A 1 255 ? 18.541  19.864  -27.232 1   15.923 ? 255 ALA   A O    1 
ATOM   1994 C  CB   . ALA   A 1 255 ? 16.119  21.359  -28.824 1   16.227 ? 255 ALA   A CB   1 
ATOM   1995 N  N    . GLN   A 1 256 ? 16.539  18.937  -26.812 1   13.84  ? 256 GLN   A N    1 
ATOM   1996 C  CA   . GLN   A 1 256 ? 16.931  18.501  -25.484 1   14.001 ? 256 GLN   A CA   1 
ATOM   1997 C  C    . GLN   A 1 256 ? 18.054  17.46   -25.515 1   13.653 ? 256 GLN   A C    1 
ATOM   1998 O  O    . GLN   A 1 256 ? 18.863  17.393  -24.584 1   15.224 ? 256 GLN   A O    1 
ATOM   1999 C  CB   . GLN   A 1 256 ? 15.737  17.942  -24.716 1   14.676 ? 256 GLN   A CB   1 
ATOM   2000 C  CG   . GLN   A 1 256 ? 16.061  17.746  -23.237 1   15.227 ? 256 GLN   A CG   1 
ATOM   2001 C  CD   . GLN   A 1 256 ? 14.905  17.231  -22.417 1   16.725 ? 256 GLN   A CD   1 
ATOM   2002 O  OE1  . GLN   A 1 256 ? 13.774  17.689  -22.583 1   19.117 ? 256 GLN   A OE1  1 
ATOM   2003 N  NE2  . GLN   A 1 256 ? 15.187  16.299  -21.52  1   16.345 ? 256 GLN   A NE2  1 
ATOM   2004 N  N    . THR   A 1 257 ? 18.083  16.617  -26.552 1   13.362 ? 257 THR   A N    1 
ATOM   2005 C  CA   . THR   A 1 257 ? 19.007  15.496  -26.632 1   13.125 ? 257 THR   A CA   1 
ATOM   2006 C  C    . THR   A 1 257 ? 20.2    15.788  -27.538 1   12.975 ? 257 THR   A C    1 
ATOM   2007 O  O    . THR   A 1 257 ? 21.165  15.039  -27.494 1   13.531 ? 257 THR   A O    1 
ATOM   2008 C  CB   . THR   A 1 257 ? 18.281  14.238  -27.12  1   12.745 ? 257 THR   A CB   1 
ATOM   2009 O  OG1  . THR   A 1 257 ? 17.75   14.501  -28.419 1   12.407 ? 257 THR   A OG1  1 
ATOM   2010 C  CG2  . THR   A 1 257 ? 17.179  13.803  -26.174 1   12.9   ? 257 THR   A CG2  1 
ATOM   2011 N  N    . GLY   A 1 258 ? 20.116  16.803  -28.403 1   13.15  ? 258 GLY   A N    1 
ATOM   2012 C  CA   . GLY   A 1 258 ? 21.182  17.065  -29.363 1   13.294 ? 258 GLY   A CA   1 
ATOM   2013 C  C    . GLY   A 1 258 ? 21.197  16.1    -30.553 1   13.905 ? 258 GLY   A C    1 
ATOM   2014 O  O    . GLY   A 1 258 ? 22.2    16.021  -31.266 1   15.864 ? 258 GLY   A O    1 
ATOM   2015 N  N    . ILE   A 1 259 ? 20.102  15.368  -30.775 1   13.016 ? 259 ILE   A N    1 
ATOM   2016 C  CA   . ILE   A 1 259 ? 20.012  14.404  -31.867 1   12.666 ? 259 ILE   A CA   1 
ATOM   2017 C  C    . ILE   A 1 259 ? 18.994  14.919  -32.881 1   12.657 ? 259 ILE   A C    1 
ATOM   2018 O  O    . ILE   A 1 259 ? 17.806  15.004  -32.566 1   12.997 ? 259 ILE   A O    1 
ATOM   2019 C  CB   . ILE   A 1 259 ? 19.645  13.002  -31.355 1   13.189 ? 259 ILE   A CB   1 
ATOM   2020 C  CG1  . ILE   A 1 259 ? 20.652  12.518  -30.33  1   14.169 ? 259 ILE   A CG1  1 
ATOM   2021 C  CG2  . ILE   A 1 259 ? 19.505  11.994  -32.498 1   13.056 ? 259 ILE   A CG2  1 
ATOM   2022 C  CD1  . ILE   A 1 259 ? 20.168  11.355  -29.498 1   15.165 ? 259 ILE   A CD1  1 
ATOM   2023 N  N    . ALA   A 1 260 ? 19.475  15.276  -34.077 1   12.773 ? 260 ALA   A N    1 
ATOM   2024 C  CA   . ALA   A 1 260 ? 18.609  15.763  -35.135 1   12.383 ? 260 ALA   A CA   1 
ATOM   2025 C  C    . ALA   A 1 260 ? 17.556  14.705  -35.458 1   11.717 ? 260 ALA   A C    1 
ATOM   2026 O  O    . ALA   A 1 260 ? 17.811  13.509  -35.386 1   11.633 ? 260 ALA   A O    1 
ATOM   2027 C  CB   . ALA   A 1 260 ? 19.435  16.102  -36.361 1   12.787 ? 260 ALA   A CB   1 
ATOM   2028 N  N    . VAL   A 1 261 ? 16.369  15.172  -35.862 1   12.155 ? 261 VAL   A N    1 
ATOM   2029 C  CA   . VAL   A 1 261 ? 15.262  14.267  -36.102 1   12.339 ? 261 VAL   A CA   1 
ATOM   2030 C  C    . VAL   A 1 261 ? 15.636  13.237  -37.168 1   11.457 ? 261 VAL   A C    1 
ATOM   2031 O  O    . VAL   A 1 261 ? 15.389  12.05   -36.985 1   11.556 ? 261 VAL   A O    1 
ATOM   2032 C  CB   . VAL   A 1 261 ? 13.972  15.028  -36.448 1   13.639 ? 261 VAL   A CB   1 
ATOM   2033 C  CG1  . VAL   A 1 261 ? 12.862  14.072  -36.862 1   13.914 ? 261 VAL   A CG1  1 
ATOM   2034 C  CG2  . VAL   A 1 261 ? 13.528  15.91   -35.287 1   14.426 ? 261 VAL   A CG2  1 
ATOM   2035 N  N    . LEU   A 1 262 ? 16.247  13.675  -38.279 1   11.595 ? 262 LEU   A N    1 
ATOM   2036 C  CA   . LEU   A 1 262 ? 16.585  12.728  -39.336 1   12.094 ? 262 LEU   A CA   1 
ATOM   2037 C  C    . LEU   A 1 262 ? 17.712  11.77   -38.921 1   11.969 ? 262 LEU   A C    1 
ATOM   2038 O  O    . LEU   A 1 262 ? 17.814  10.661  -39.447 1   12.397 ? 262 LEU   A O    1 
ATOM   2039 C  CB   . LEU   A 1 262 ? 16.908  13.479  -40.628 1   12.725 ? 262 LEU   A CB   1 
ATOM   2040 C  CG   . LEU   A 1 262 ? 15.715  14.208  -41.251 1   13.919 ? 262 LEU   A CG   1 
ATOM   2041 C  CD1  . LEU   A 1 262 ? 16.186  15.003  -42.449 1   14.633 ? 262 LEU   A CD1  1 
ATOM   2042 C  CD2  . LEU   A 1 262 ? 14.591  13.265  -41.648 1   14.74  ? 262 LEU   A CD2  1 
ATOM   2043 N  N    . ASP   A 1 263 ? 18.527  12.15   -37.931 1   12.23  ? 263 ASP   A N    1 
ATOM   2044 C  CA   . ASP   A 1 263 ? 19.495  11.232  -37.35  1   12.772 ? 263 ASP   A CA   1 
ATOM   2045 C  C    . ASP   A 1 263 ? 18.806  10.181  -36.487 1   11.604 ? 263 ASP   A C    1 
ATOM   2046 O  O    . ASP   A 1 263 ? 19.186  9.015   -36.527 1   11.792 ? 263 ASP   A O    1 
ATOM   2047 C  CB   . ASP   A 1 263 ? 20.607  11.96   -36.616 1   13.898 ? 263 ASP   A CB   1 
ATOM   2048 C  CG   . ASP   A 1 263 ? 21.499  12.848  -37.474 1   15.549 ? 263 ASP   A CG   1 
ATOM   2049 O  OD1  . ASP   A 1 263 ? 21.397  12.776  -38.708 1   18.837 ? 263 ASP   A OD1  1 
ATOM   2050 O  OD2  . ASP   A 1 263 ? 22.291  13.624  -36.908 1   18.673 ? 263 ASP   A OD2  1 
ATOM   2051 N  N    . MET   A 1 264 ? 17.77   10.571  -35.735 1   10.876 ? 264 MET   A N    1 
ATOM   2052 C  CA   . MET   A 1 264 ? 16.982  9.575   -35.031 1   11.206 ? 264 MET   A CA   1 
ATOM   2053 C  C    . MET   A 1 264 ? 16.239  8.663   -36.015 1   10.787 ? 264 MET   A C    1 
ATOM   2054 O  O    . MET   A 1 264 ? 16.125  7.461   -35.777 1   10.917 ? 264 MET   A O    1 
ATOM   2055 C  CB   . MET   A 1 264 ? 16.009  10.201  -34.028 1   11.539 ? 264 MET   A CB   1 
ATOM   2056 C  CG   . MET   A 1 264 ? 15.433  9.179   -33.057 1   11.597 ? 264 MET   A CG   1 
ATOM   2057 S  SD   . MET   A 1 264 ? 16.67   8.433   -31.972 1   11.902 ? 264 MET   A SD   1 
ATOM   2058 C  CE   . MET   A 1 264 ? 16.627  9.65    -30.652 1   12.774 ? 264 MET   A CE   1 
ATOM   2059 N  N    . CYS   A 1 265 ? 15.78   9.213   -37.149 1   11.105 ? 265 CYS   A N    1 
ATOM   2060 C  CA   . CYS   A 1 265 ? 15.217  8.379   -38.207 1   11.662 ? 265 CYS   A CA   1 
ATOM   2061 C  C    . CYS   A 1 265 ? 16.207  7.318   -38.706 1   11.043 ? 265 CYS   A C    1 
ATOM   2062 O  O    . CYS   A 1 265 ? 15.823  6.168   -38.943 1   11.357 ? 265 CYS   A O    1 
ATOM   2063 C  CB   . CYS   A 1 265 ? 14.708  9.222   -39.368 1   12.215 ? 265 CYS   A CB   1 
ATOM   2064 S  SG   . CYS   A 1 265 ? 13.24   10.199  -38.969 1   13.761 ? 265 CYS   A SG   1 
ATOM   2065 N  N    . ALA   A 1 266 ? 17.492  7.687   -38.848 1   11.303 ? 266 ALA   A N    1 
ATOM   2066 C  CA   . ALA   A 1 266 ? 18.511  6.731   -39.254 1   11.753 ? 266 ALA   A CA   1 
ATOM   2067 C  C    . ALA   A 1 266 ? 18.705  5.638   -38.205 1   11.426 ? 266 ALA   A C    1 
ATOM   2068 O  O    . ALA   A 1 266 ? 18.917  4.478   -38.545 1   11.982 ? 266 ALA   A O    1 
ATOM   2069 C  CB   . ALA   A 1 266 ? 19.814  7.443   -39.538 1   12.234 ? 266 ALA   A CB   1 
ATOM   2070 N  N    . SER   A 1 267 ? 18.587  5.992   -36.919 1   11.408 ? 267 SER   A N    1 
ATOM   2071 C  CA   . SER   A 1 267 ? 18.634  5.005   -35.851 1   11.939 ? 267 SER   A CA   1 
ATOM   2072 C  C    . SER   A 1 267 ? 17.47   4.025   -35.967 1   10.828 ? 267 SER   A C    1 
ATOM   2073 O  O    . SER   A 1 267 ? 17.655  2.818   -35.864 1   10.896 ? 267 SER   A O    1 
ATOM   2074 C  CB   . SER   A 1 267 ? 18.65   5.679   -34.494 1   12.993 ? 267 SER   A CB   1 
ATOM   2075 O  OG   . SER   A 1 267 ? 18.525  4.731   -33.443 1   14.155 ? 267 SER   A OG   1 
ATOM   2076 N  N    . LEU   A 1 268 ? 16.256  4.548   -36.161 1   10.856 ? 268 LEU   A N    1 
ATOM   2077 C  CA   . LEU   A 1 268 ? 15.084  3.705   -36.325 1   10.717 ? 268 LEU   A CA   1 
ATOM   2078 C  C    . LEU   A 1 268 ? 15.205  2.765   -37.536 1   10.4   ? 268 LEU   A C    1 
ATOM   2079 O  O    . LEU   A 1 268 ? 14.889  1.581   -37.422 1   10.285 ? 268 LEU   A O    1 
ATOM   2080 C  CB   . LEU   A 1 268 ? 13.827  4.567   -36.381 1   10.746 ? 268 LEU   A CB   1 
ATOM   2081 C  CG   . LEU   A 1 268 ? 12.505  3.824   -36.605 1   10.931 ? 268 LEU   A CG   1 
ATOM   2082 C  CD1  . LEU   A 1 268 ? 12.304  2.699   -35.601 1   10.877 ? 268 LEU   A CD1  1 
ATOM   2083 C  CD2  . LEU   A 1 268 ? 11.351  4.818   -36.559 1   11.28  ? 268 LEU   A CD2  1 
ATOM   2084 N  N    . LYS   A 1 269 ? 15.697  3.27    -38.675 1   11.388 ? 269 LYS   A N    1 
ATOM   2085 C  CA   . LYS   A 1 269 ? 15.931  2.418   -39.836 1   12.379 ? 269 LYS   A CA   1 
ATOM   2086 C  C    . LYS   A 1 269 ? 16.804  1.215   -39.466 1   11.76  ? 269 LYS   A C    1 
ATOM   2087 O  O    . LYS   A 1 269 ? 16.533  0.068   -39.849 1   11.788 ? 269 LYS   A O    1 
ATOM   2088 C  CB   . LYS   A 1 269 ? 16.565  3.221   -40.979 1   14.263 ? 269 LYS   A CB   1 
ATOM   2089 C  CG   . LYS   A 1 269 ? 15.664  4.264   -41.608 1   16.754 ? 269 LYS   A CG   1 
ATOM   2090 C  CD   . LYS   A 1 269 ? 16.387  5.259   -42.517 1   18.546 ? 269 LYS   A CD   1 
ATOM   2091 C  CE   . LYS   A 1 269 ? 16.8    4.702   -43.819 1   20.1   ? 269 LYS   A CE   1 
ATOM   2092 N  NZ   . LYS   A 1 269 ? 17.584  5.671   -44.597 1   20.183 ? 269 LYS   A NZ   1 
ATOM   2093 N  N    . GLU   A 1 270 ? 17.867  1.482   -38.691 1   11.832 ? 270 GLU   A N    1 
ATOM   2094 C  CA   . GLU   A 1 270 ? 18.809  0.437   -38.349 1   12.386 ? 270 GLU   A CA   1 
ATOM   2095 C  C    . GLU   A 1 270 ? 18.191  -0.554  -37.359 1   11.479 ? 270 GLU   A C    1 
ATOM   2096 O  O    . GLU   A 1 270 ? 18.445  -1.748  -37.45  1   12.268 ? 270 GLU   A O    1 
ATOM   2097 C  CB   . GLU   A 1 270 ? 20.109  1.075   -37.87  1   13.889 ? 270 GLU   A CB   1 
ATOM   2098 C  CG   . GLU   A 1 270 ? 21.195  0.059   -37.547 1   15.501 ? 270 GLU   A CG   1 
ATOM   2099 C  CD   . GLU   A 1 270 ? 22.525  0.742   -37.338 1   17.197 ? 270 GLU   A CD   1 
ATOM   2100 O  OE1  . GLU   A 1 270 ? 23.204  1.085   -38.33  1   19.33  ? 270 GLU   A OE1  1 
ATOM   2101 O  OE2  . GLU   A 1 270 ? 22.833  1.021   -36.176 1   18.776 ? 270 GLU   A OE2  1 
ATOM   2102 N  N    . LEU   A 1 271 ? 17.379  -0.077  -36.409 1   11.593 ? 271 LEU   A N    1 
ATOM   2103 C  CA   . LEU   A 1 271 ? 16.667  -0.963  -35.5   1   11.665 ? 271 LEU   A CA   1 
ATOM   2104 C  C    . LEU   A 1 271 ? 15.703  -1.882  -36.244 1   11.39  ? 271 LEU   A C    1 
ATOM   2105 O  O    . LEU   A 1 271 ? 15.589  -3.058  -35.9   1   11.875 ? 271 LEU   A O    1 
ATOM   2106 C  CB   . LEU   A 1 271 ? 15.938  -0.151  -34.426 1   12.066 ? 271 LEU   A CB   1 
ATOM   2107 C  CG   . LEU   A 1 271 ? 16.835  0.46    -33.344 1   13.023 ? 271 LEU   A CG   1 
ATOM   2108 C  CD1  . LEU   A 1 271 ? 16.065  1.491   -32.534 1   13.392 ? 271 LEU   A CD1  1 
ATOM   2109 C  CD2  . LEU   A 1 271 ? 17.389  -0.637  -32.435 1   14.34  ? 271 LEU   A CD2  1 
ATOM   2110 N  N    . LEU   A 1 272 ? 15.023  -1.359  -37.276 1   11.388 ? 272 LEU   A N    1 
ATOM   2111 C  CA   . LEU   A 1 272 ? 14.108  -2.179  -38.055 1   11.962 ? 272 LEU   A CA   1 
ATOM   2112 C  C    . LEU   A 1 272 ? 14.877  -3.268  -38.809 1   11.586 ? 272 LEU   A C    1 
ATOM   2113 O  O    . LEU   A 1 272 ? 14.384  -4.378  -38.965 1   12.031 ? 272 LEU   A O    1 
ATOM   2114 C  CB   . LEU   A 1 272 ? 13.284  -1.294  -38.994 1   11.814 ? 272 LEU   A CB   1 
ATOM   2115 C  CG   . LEU   A 1 272 ? 12.266  -0.403  -38.276 1   12.292 ? 272 LEU   A CG   1 
ATOM   2116 C  CD1  . LEU   A 1 272 ? 11.675  0.652   -39.179 1   12.564 ? 272 LEU   A CD1  1 
ATOM   2117 C  CD2  . LEU   A 1 272 ? 11.188  -1.247  -37.646 1   12.715 ? 272 LEU   A CD2  1 
ATOM   2118 N  N    . GLN   A 1 273 ? 16.096  -2.947  -39.26  1   11.766 ? 273 GLN   A N    1 
ATOM   2119 C  CA   . GLN   A 1 273 ? 16.912  -3.873  -40.029 1   12.653 ? 273 GLN   A CA   1 
ATOM   2120 C  C    . GLN   A 1 273 ? 17.57   -4.939  -39.153 1   12.862 ? 273 GLN   A C    1 
ATOM   2121 O  O    . GLN   A 1 273 ? 17.738  -6.087  -39.566 1   12.428 ? 273 GLN   A O    1 
ATOM   2122 C  CB   . GLN   A 1 273 ? 17.98   -3.002  -40.685 1   13.408 ? 273 GLN   A CB   1 
ATOM   2123 C  CG   . GLN   A 1 273 ? 19.142  -3.745  -41.323 1   14.181 ? 273 GLN   A CG   1 
ATOM   2124 C  CD   . GLN   A 1 273 ? 20.187  -2.751  -41.745 1   15.338 ? 273 GLN   A CD   1 
ATOM   2125 O  OE1  . GLN   A 1 273 ? 20.069  -2.136  -42.806 1   18.035 ? 273 GLN   A OE1  1 
ATOM   2126 N  NE2  . GLN   A 1 273 ? 21.168  -2.538  -40.881 1   15.641 ? 273 GLN   A NE2  1 
ATOM   2127 N  N    . ASN   A 1 274 ? 17.969  -4.545  -37.932 1   12.459 ? 274 ASN   A N    1 
ATOM   2128 C  CA   . ASN   A 1 274 ? 18.837  -5.37   -37.098 1   13.016 ? 274 ASN   A CA   1 
ATOM   2129 C  C    . ASN   A 1 274 ? 18.106  -6.052  -35.939 1   13.645 ? 274 ASN   A C    1 
ATOM   2130 O  O    . ASN   A 1 274 ? 18.608  -7.043  -35.415 1   14.218 ? 274 ASN   A O    1 
ATOM   2131 C  CB   . ASN   A 1 274 ? 19.963  -4.552  -36.476 1   13.148 ? 274 ASN   A CB   1 
ATOM   2132 C  CG   . ASN   A 1 274 ? 20.992  -4.094  -37.477 1   14.104 ? 274 ASN   A CG   1 
ATOM   2133 O  OD1  . ASN   A 1 274 ? 21.008  -4.55   -38.622 1   14.93  ? 274 ASN   A OD1  1 
ATOM   2134 N  ND2  . ASN   A 1 274 ? 21.868  -3.196  -37.064 1   14.268 ? 274 ASN   A ND2  1 
ATOM   2135 N  N    . GLY   A 1 275 ? 16.974  -5.49   -35.496 1   13.894 ? 275 GLY   A N    1 
ATOM   2136 C  CA   . GLY   A 1 275 ? 16.405  -5.865  -34.213 1   14.847 ? 275 GLY   A CA   1 
ATOM   2137 C  C    . GLY   A 1 275 ? 17.269  -5.336  -33.066 1   16.057 ? 275 GLY   A C    1 
ATOM   2138 O  O    . GLY   A 1 275 ? 18.091  -4.45   -33.273 1   15.909 ? 275 GLY   A O    1 
ATOM   2139 N  N    . MET   A 1 276 ? 17.066  -5.87   -31.849 1   15.766 ? 276 MET   A N    1 
ATOM   2140 C  CA   A MET   A 1 276 ? 17.657  -5.366  -30.623 0.6 16.803 ? 276 MET   A CA   1 
ATOM   2141 C  CA   B MET   A 1 276 ? 17.742  -5.286  -30.694 0.4 14.858 ? 276 MET   A CA   1 
ATOM   2142 C  C    . MET   A 1 276 ? 18.945  -6.105  -30.245 1   16.497 ? 276 MET   A C    1 
ATOM   2143 O  O    . MET   A 1 276 ? 19.638  -5.681  -29.324 1   16.584 ? 276 MET   A O    1 
ATOM   2144 C  CB   A MET   A 1 276 ? 16.671  -5.608  -29.478 0.6 17.712 ? 276 MET   A CB   1 
ATOM   2145 C  CB   B MET   A 1 276 ? 16.818  -5.129  -29.485 0.4 13.351 ? 276 MET   A CB   1 
ATOM   2146 C  CG   A MET   A 1 276 ? 15.293  -5.015  -29.683 0.6 19.209 ? 276 MET   A CG   1 
ATOM   2147 C  CG   B MET   A 1 276 ? 15.734  -4.125  -29.718 0.4 11.885 ? 276 MET   A CG   1 
ATOM   2148 S  SD   A MET   A 1 276 ? 15.382  -3.222  -29.562 0.6 22.406 ? 276 MET   A SD   1 
ATOM   2149 S  SD   B MET   A 1 276 ? 14.885  -3.675  -28.199 0.4 10.877 ? 276 MET   A SD   1 
ATOM   2150 C  CE   A MET   A 1 276 ? 13.719  -2.811  -29.004 0.6 23.004 ? 276 MET   A CE   1 
ATOM   2151 C  CE   B MET   A 1 276 ? 13.606  -2.678  -28.97  0.4 11.366 ? 276 MET   A CE   1 
ATOM   2152 N  N    . ASN   A 1 277 ? 19.194  -7.26   -30.872 1   17.827 ? 277 ASN   A N    1 
ATOM   2153 C  CA   . ASN   A 1 277 ? 20.333  -8.097  -30.518 1   20.026 ? 277 ASN   A CA   1 
ATOM   2154 C  C    . ASN   A 1 277 ? 20.361  -8.367  -29.012 1   19.607 ? 277 ASN   A C    1 
ATOM   2155 O  O    . ASN   A 1 277 ? 21.408  -8.283  -28.369 1   20.112 ? 277 ASN   A O    1 
ATOM   2156 C  CB   . ASN   A 1 277 ? 21.627  -7.491  -31.044 1   21.836 ? 277 ASN   A CB   1 
ATOM   2157 C  CG   . ASN   A 1 277 ? 21.797  -7.772  -32.516 1   24.481 ? 277 ASN   A CG   1 
ATOM   2158 O  OD1  . ASN   A 1 277 ? 22.121  -8.908  -32.879 1   28.408 ? 277 ASN   A OD1  1 
ATOM   2159 N  ND2  . ASN   A 1 277 ? 21.593  -6.775  -33.367 1   24.158 ? 277 ASN   A ND2  1 
ATOM   2160 N  N    . GLY   A 1 278 ? 19.193  -8.705  -28.463 1   18.886 ? 278 GLY   A N    1 
ATOM   2161 C  CA   . GLY   A 1 278 ? 19.083  -9.173  -27.092 1   19.284 ? 278 GLY   A CA   1 
ATOM   2162 C  C    . GLY   A 1 278 ? 19.027  -8.042  -26.063 1   18.953 ? 278 GLY   A C    1 
ATOM   2163 O  O    . GLY   A 1 278 ? 18.949  -8.301  -24.863 1   21.188 ? 278 GLY   A O    1 
ATOM   2164 N  N    . ARG   A 1 279 ? 19.05   -6.79   -26.521 1   18.018 ? 279 ARG   A N    1 
ATOM   2165 C  CA   . ARG   A 1 279 ? 18.93   -5.638  -25.644 1   17.692 ? 279 ARG   A CA   1 
ATOM   2166 C  C    . ARG   A 1 279 ? 17.466  -5.234  -25.52  1   16.712 ? 279 ARG   A C    1 
ATOM   2167 O  O    . ARG   A 1 279 ? 16.592  -5.794  -26.182 1   17.067 ? 279 ARG   A O    1 
ATOM   2168 C  CB   . ARG   A 1 279 ? 19.788  -4.488  -26.18  1   19     ? 279 ARG   A CB   1 
ATOM   2169 C  CG   . ARG   A 1 279 ? 21.257  -4.862  -26.061 1   21.361 ? 279 ARG   A CG   1 
ATOM   2170 C  CD   . ARG   A 1 279 ? 22.15   -3.888  -26.743 1   23.831 ? 279 ARG   A CD   1 
ATOM   2171 N  NE   . ARG   A 1 279 ? 22.112  -4.103  -28.192 1   25.587 ? 279 ARG   A NE   1 
ATOM   2172 C  CZ   . ARG   A 1 279 ? 22.985  -3.589  -29.043 1   26.968 ? 279 ARG   A CZ   1 
ATOM   2173 N  NH1  . ARG   A 1 279 ? 24.019  -2.898  -28.589 1   28.331 ? 279 ARG   A NH1  1 
ATOM   2174 N  NH2  . ARG   A 1 279 ? 22.813  -3.76   -30.343 1   26.751 ? 279 ARG   A NH2  1 
ATOM   2175 N  N    . THR   A 1 280 ? 17.217  -4.268  -24.634 1   15.667 ? 280 THR   A N    1 
ATOM   2176 C  CA   . THR   A 1 280 ? 15.914  -3.651  -24.5   1   14.774 ? 280 THR   A CA   1 
ATOM   2177 C  C    . THR   A 1 280 ? 16.076  -2.134  -24.544 1   14.323 ? 280 THR   A C    1 
ATOM   2178 O  O    . THR   A 1 280 ? 17.183  -1.598  -24.412 1   15.452 ? 280 THR   A O    1 
ATOM   2179 C  CB   . THR   A 1 280 ? 15.213  -4.094  -23.213 1   15.953 ? 280 THR   A CB   1 
ATOM   2180 O  OG1  . THR   A 1 280 ? 16.047  -3.752  -22.108 1   17.971 ? 280 THR   A OG1  1 
ATOM   2181 C  CG2  . THR   A 1 280 ? 14.884  -5.576  -23.199 1   16.221 ? 280 THR   A CG2  1 
ATOM   2182 N  N    . ILE   A 1 281 ? 14.941  -1.469  -24.77  1   12.902 ? 281 ILE   A N    1 
ATOM   2183 C  CA   . ILE   A 1 281 ? 14.856  -0.023  -24.718 1   12.548 ? 281 ILE   A CA   1 
ATOM   2184 C  C    . ILE   A 1 281 ? 13.705  0.3     -23.775 1   12.51  ? 281 ILE   A C    1 
ATOM   2185 O  O    . ILE   A 1 281 ? 12.584  -0.145  -23.998 1   12.499 ? 281 ILE   A O    1 
ATOM   2186 C  CB   . ILE   A 1 281 ? 14.626  0.587   -26.114 1   12.358 ? 281 ILE   A CB   1 
ATOM   2187 C  CG1  . ILE   A 1 281 ? 15.767  0.237   -27.072 1   12.898 ? 281 ILE   A CG1  1 
ATOM   2188 C  CG2  . ILE   A 1 281 ? 14.412  2.098   -26.013 1   12.682 ? 281 ILE   A CG2  1 
ATOM   2189 C  CD1  . ILE   A 1 281 ? 15.558  0.714   -28.497 1   12.855 ? 281 ILE   A CD1  1 
ATOM   2190 N  N    . LEU   A 1 282 ? 14.004  1.029   -22.696 1   13.261 ? 282 LEU   A N    1 
ATOM   2191 C  CA   . LEU   A 1 282 ? 12.995  1.388   -21.707 1   13.717 ? 282 LEU   A CA   1 
ATOM   2192 C  C    . LEU   A 1 282 ? 12.152  0.17    -21.32  1   15.138 ? 282 LEU   A C    1 
ATOM   2193 O  O    . LEU   A 1 282 ? 10.934  0.254   -21.178 1   15.161 ? 282 LEU   A O    1 
ATOM   2194 C  CB   . LEU   A 1 282 ? 12.15   2.554   -22.214 1   13.44  ? 282 LEU   A CB   1 
ATOM   2195 C  CG   . LEU   A 1 282 ? 12.877  3.898   -22.324 1   13.293 ? 282 LEU   A CG   1 
ATOM   2196 C  CD1  . LEU   A 1 282 ? 12.003  4.912   -23.011 1   13.506 ? 282 LEU   A CD1  1 
ATOM   2197 C  CD2  . LEU   A 1 282 ? 13.327  4.401   -20.955 1   13.262 ? 282 LEU   A CD2  1 
ATOM   2198 N  N    . GLY   A 1 283 ? 12.823  -0.97   -21.128 1   16.167 ? 283 GLY   A N    1 
ATOM   2199 C  CA   . GLY   A 1 283 ? 12.169  -2.162  -20.613 1   17.463 ? 283 GLY   A CA   1 
ATOM   2200 C  C    . GLY   A 1 283 ? 11.374  -2.95   -21.653 1   18.391 ? 283 GLY   A C    1 
ATOM   2201 O  O    . GLY   A 1 283 ? 10.663  -3.883  -21.28  1   23.229 ? 283 GLY   A O    1 
ATOM   2202 N  N    . SER   A 1 284 ? 11.498  -2.59   -22.937 1   15.548 ? 284 SER   A N    1 
ATOM   2203 C  CA   . SER   A 1 284 ? 10.757  -3.237  -24.012 1   15.265 ? 284 SER   A CA   1 
ATOM   2204 C  C    . SER   A 1 284 ? 11.709  -3.894  -25.013 1   13.801 ? 284 SER   A C    1 
ATOM   2205 O  O    . SER   A 1 284 ? 12.752  -3.324  -25.335 1   14.227 ? 284 SER   A O    1 
ATOM   2206 C  CB   . SER   A 1 284 ? 9.887   -2.233  -24.731 1   16.497 ? 284 SER   A CB   1 
ATOM   2207 O  OG   . SER   A 1 284 ? 9.121   -2.851  -25.76  1   19.223 ? 284 SER   A OG   1 
ATOM   2208 N  N    . ALA   A 1 285 ? 11.308  -5.062  -25.531 1   13.693 ? 285 ALA   A N    1 
ATOM   2209 C  CA   . ALA   A 1 285 ? 12.047  -5.721  -26.597 1   14.234 ? 285 ALA   A CA   1 
ATOM   2210 C  C    . ALA   A 1 285 ? 11.421  -5.437  -27.965 1   14.519 ? 285 ALA   A C    1 
ATOM   2211 O  O    . ALA   A 1 285 ? 11.886  -5.962  -28.978 1   16.312 ? 285 ALA   A O    1 
ATOM   2212 C  CB   . ALA   A 1 285 ? 12.139  -7.205  -26.324 1   15.48  ? 285 ALA   A CB   1 
ATOM   2213 N  N    . LEU   A 1 286 ? 10.352  -4.637  -27.99  1   14.135 ? 286 LEU   A N    1 
ATOM   2214 C  CA   . LEU   A 1 286 ? 9.736   -4.188  -29.235 1   14.199 ? 286 LEU   A CA   1 
ATOM   2215 C  C    . LEU   A 1 286 ? 9.782   -2.667  -29.297 1   13.241 ? 286 LEU   A C    1 
ATOM   2216 O  O    . LEU   A 1 286 ? 9.936   -1.999  -28.277 1   13.623 ? 286 LEU   A O    1 
ATOM   2217 C  CB   . LEU   A 1 286 ? 8.285   -4.646  -29.334 1   16.727 ? 286 LEU   A CB   1 
ATOM   2218 C  CG   . LEU   A 1 286 ? 8.031   -6.153  -29.347 1   19.702 ? 286 LEU   A CG   1 
ATOM   2219 C  CD1  . LEU   A 1 286 ? 6.553   -6.418  -29.114 1   21.07  ? 286 LEU   A CD1  1 
ATOM   2220 C  CD2  . LEU   A 1 286 ? 8.51    -6.77   -30.636 1   21.788 ? 286 LEU   A CD2  1 
ATOM   2221 N  N    . LEU   A 1 287 ? 9.56    -2.105  -30.491 1   12.667 ? 287 LEU   A N    1 
ATOM   2222 C  CA   . LEU   A 1 287 ? 9.498   -0.662  -30.625 1   12.955 ? 287 LEU   A CA   1 
ATOM   2223 C  C    . LEU   A 1 287 ? 8.1     -0.17   -30.245 1   13.731 ? 287 LEU   A C    1 
ATOM   2224 O  O    . LEU   A 1 287 ? 7.105   -0.491  -30.891 1   16.822 ? 287 LEU   A O    1 
ATOM   2225 C  CB   . LEU   A 1 287 ? 9.894   -0.292  -32.048 1   13.926 ? 287 LEU   A CB   1 
ATOM   2226 C  CG   . LEU   A 1 287 ? 11.282  -0.789  -32.469 1   15.093 ? 287 LEU   A CG   1 
ATOM   2227 C  CD1  . LEU   A 1 287 ? 11.558  -0.495  -33.933 1   16.583 ? 287 LEU   A CD1  1 
ATOM   2228 C  CD2  . LEU   A 1 287 ? 12.383  -0.213  -31.596 1   16.626 ? 287 LEU   A CD2  1 
ATOM   2229 N  N    . GLU   A 1 288 ? 8.045   0.656   -29.209 1   12.144 ? 288 GLU   A N    1 
ATOM   2230 C  CA   . GLU   A 1 288 ? 6.78    1.101   -28.649 1   12.161 ? 288 GLU   A CA   1 
ATOM   2231 C  C    . GLU   A 1 288 ? 6.25    2.317   -29.396 1   10.839 ? 288 GLU   A C    1 
ATOM   2232 O  O    . GLU   A 1 288 ? 6.989   3.275   -29.594 1   10.815 ? 288 GLU   A O    1 
ATOM   2233 C  CB   . GLU   A 1 288 ? 7.07    1.523   -27.21  1   13.221 ? 288 GLU   A CB   1 
ATOM   2234 C  CG   . GLU   A 1 288 ? 5.881   2.11    -26.481 1   16.328 ? 288 GLU   A CG   1 
ATOM   2235 C  CD   . GLU   A 1 288 ? 4.727   1.137   -26.332 1   18.15  ? 288 GLU   A CD   1 
ATOM   2236 O  OE1  . GLU   A 1 288 ? 4.983   -0.016  -25.87  1   21.095 ? 288 GLU   A OE1  1 
ATOM   2237 O  OE2  . GLU   A 1 288 ? 3.599   1.565   -26.73  1   19.391 ? 288 GLU   A OE2  1 
ATOM   2238 N  N    . ASP   A 1 289 ? 4.95    2.292   -29.745 1   10.722 ? 289 ASP   A N    1 
ATOM   2239 C  CA   . ASP   A 1 289 ? 4.37    3.368   -30.525 1   10.637 ? 289 ASP   A CA   1 
ATOM   2240 C  C    . ASP   A 1 289 ? 3.143   4.004   -29.868 1   10.841 ? 289 ASP   A C    1 
ATOM   2241 O  O    . ASP   A 1 289 ? 2.43    4.72    -30.563 1   11.213 ? 289 ASP   A O    1 
ATOM   2242 C  CB   . ASP   A 1 289 ? 4.035   2.912   -31.941 1   11.541 ? 289 ASP   A CB   1 
ATOM   2243 C  CG   . ASP   A 1 289 ? 2.789   2.061   -32.116 1   11.967 ? 289 ASP   A CG   1 
ATOM   2244 O  OD1  . ASP   A 1 289 ? 2.264   1.541   -31.097 1   12.426 ? 289 ASP   A OD1  1 
ATOM   2245 O  OD2  . ASP   A 1 289 ? 2.327   1.955   -33.268 1   12.693 ? 289 ASP   A OD2  1 
ATOM   2246 N  N    . GLU   A 1 290 ? 2.915   3.805   -28.56  1   10.725 ? 290 GLU   A N    1 
ATOM   2247 C  CA   . GLU   A 1 290 ? 1.757   4.43    -27.916 1   11.069 ? 290 GLU   A CA   1 
ATOM   2248 C  C    . GLU   A 1 290 ? 2.165   5.497   -26.897 1   10.455 ? 290 GLU   A C    1 
ATOM   2249 O  O    . GLU   A 1 290 ? 1.419   5.771   -25.953 1   11.368 ? 290 GLU   A O    1 
ATOM   2250 C  CB   . GLU   A 1 290 ? 0.737   3.411   -27.398 1   12.616 ? 290 GLU   A CB   1 
ATOM   2251 C  CG   . GLU   A 1 290 ? 0.095   2.591   -28.517 1   13.746 ? 290 GLU   A CG   1 
ATOM   2252 C  CD   . GLU   A 1 290 ? -1.215  1.876   -28.191 1   14.836 ? 290 GLU   A CD   1 
ATOM   2253 O  OE1  . GLU   A 1 290 ? -1.649  1.916   -27.008 1   17.114 ? 290 GLU   A OE1  1 
ATOM   2254 O  OE2  . GLU   A 1 290 ? -1.833  1.278   -29.118 1   14.369 ? 290 GLU   A OE2  1 
ATOM   2255 N  N    . PHE   A 1 291 ? 3.316   6.138   -27.123 1   10.165 ? 291 PHE   A N    1 
ATOM   2256 C  CA   . PHE   A 1 291 ? 3.687   7.362   -26.44  1   10.611 ? 291 PHE   A CA   1 
ATOM   2257 C  C    . PHE   A 1 291 ? 3.897   8.479   -27.451 1   10.268 ? 291 PHE   A C    1 
ATOM   2258 O  O    . PHE   A 1 291 ? 4.741   8.361   -28.341 1   10.215 ? 291 PHE   A O    1 
ATOM   2259 C  CB   . PHE   A 1 291 ? 4.978   7.25    -25.636 1   11.504 ? 291 PHE   A CB   1 
ATOM   2260 C  CG   . PHE   A 1 291 ? 4.924   6.234   -24.515 1   12.811 ? 291 PHE   A CG   1 
ATOM   2261 C  CD1  . PHE   A 1 291 ? 4.41    6.596   -23.274 1   13.588 ? 291 PHE   A CD1  1 
ATOM   2262 C  CD2  . PHE   A 1 291 ? 5.407   4.947   -24.679 1   13.917 ? 291 PHE   A CD2  1 
ATOM   2263 C  CE1  . PHE   A 1 291 ? 4.407   5.695   -22.228 1   15.237 ? 291 PHE   A CE1  1 
ATOM   2264 C  CE2  . PHE   A 1 291 ? 5.394   4.049   -23.615 1   15.575 ? 291 PHE   A CE2  1 
ATOM   2265 C  CZ   . PHE   A 1 291 ? 4.872   4.421   -22.403 1   15.286 ? 291 PHE   A CZ   1 
ATOM   2266 N  N    . THR   A 1 292 ? 3.161   9.575   -27.3   1   10.071 ? 292 THR   A N    1 
ATOM   2267 C  CA   . THR   A 1 292 ? 3.299   10.721  -28.19  1   10.415 ? 292 THR   A CA   1 
ATOM   2268 C  C    . THR   A 1 292 ? 4.461   11.603  -27.767 1   10.218 ? 292 THR   A C    1 
ATOM   2269 O  O    . THR   A 1 292 ? 4.947   11.51   -26.644 1   10.335 ? 292 THR   A O    1 
ATOM   2270 C  CB   . THR   A 1 292 ? 2.028   11.564  -28.242 1   10.739 ? 292 THR   A CB   1 
ATOM   2271 O  OG1  . THR   A 1 292 ? 1.934   12.226  -26.986 1   10.47  ? 292 THR   A OG1  1 
ATOM   2272 C  CG2  . THR   A 1 292 ? 0.785   10.743  -28.541 1   10.899 ? 292 THR   A CG2  1 
ATOM   2273 N  N    . PRO   A 1 293 ? 4.937   12.513  -28.642 1   10.496 ? 293 PRO   A N    1 
ATOM   2274 C  CA   . PRO   A 1 293 ? 5.914   13.515  -28.213 1   10.851 ? 293 PRO   A CA   1 
ATOM   2275 C  C    . PRO   A 1 293 ? 5.476   14.285  -26.965 1   11.264 ? 293 PRO   A C    1 
ATOM   2276 O  O    . PRO   A 1 293 ? 6.284   14.535  -26.066 1   11.476 ? 293 PRO   A O    1 
ATOM   2277 C  CB   . PRO   A 1 293 ? 6.089   14.389  -29.457 1   11.483 ? 293 PRO   A CB   1 
ATOM   2278 C  CG   . PRO   A 1 293 ? 5.741   13.458  -30.602 1   11.699 ? 293 PRO   A CG   1 
ATOM   2279 C  CD   . PRO   A 1 293 ? 4.648   12.563  -30.088 1   11.196 ? 293 PRO   A CD   1 
ATOM   2280 N  N    . PHE   A 1 294 ? 4.186   14.624  -26.896 1   11.877 ? 294 PHE   A N    1 
ATOM   2281 C  CA   . PHE   A 1 294 ? 3.657   15.354  -25.755 1   12.6   ? 294 PHE   A CA   1 
ATOM   2282 C  C    . PHE   A 1 294 ? 3.735   14.479  -24.496 1   11.805 ? 294 PHE   A C    1 
ATOM   2283 O  O    . PHE   A 1 294 ? 4.054   14.974  -23.415 1   12.933 ? 294 PHE   A O    1 
ATOM   2284 C  CB   . PHE   A 1 294 ? 2.237   15.801  -26.109 1   14.316 ? 294 PHE   A CB   1 
ATOM   2285 C  CG   . PHE   A 1 294 ? 1.592   16.728  -25.102 1   16.32  ? 294 PHE   A CG   1 
ATOM   2286 C  CD1  . PHE   A 1 294 ? 0.995   16.223  -23.953 1   17.512 ? 294 PHE   A CD1  1 
ATOM   2287 C  CD2  . PHE   A 1 294 ? 1.543   18.099  -25.327 1   17.66  ? 294 PHE   A CD2  1 
ATOM   2288 C  CE1  . PHE   A 1 294 ? 0.401   17.075  -23.035 1   18.419 ? 294 PHE   A CE1  1 
ATOM   2289 C  CE2  . PHE   A 1 294 ? 0.935   18.946  -24.41  1   19.009 ? 294 PHE   A CE2  1 
ATOM   2290 C  CZ   . PHE   A 1 294 ? 0.358   18.43   -23.277 1   19.121 ? 294 PHE   A CZ   1 
ATOM   2291 N  N    . ASP   A 1 295 ? 3.429   13.188  -24.636 1   11.446 ? 295 ASP   A N    1 
ATOM   2292 C  CA   . ASP   A 1 295 ? 3.485   12.245  -23.524 1   10.921 ? 295 ASP   A CA   1 
ATOM   2293 C  C    . ASP   A 1 295 ? 4.901   12.15   -22.969 1   11.15  ? 295 ASP   A C    1 
ATOM   2294 O  O    . ASP   A 1 295 ? 5.096   12.014  -21.762 1   12.098 ? 295 ASP   A O    1 
ATOM   2295 C  CB   . ASP   A 1 295 ? 3.042   10.847  -23.929 1   11.642 ? 295 ASP   A CB   1 
ATOM   2296 C  CG   . ASP   A 1 295 ? 1.578   10.691  -24.293 1   12.205 ? 295 ASP   A CG   1 
ATOM   2297 O  OD1  . ASP   A 1 295 ? 0.794   11.574  -23.888 1   12.973 ? 295 ASP   A OD1  1 
ATOM   2298 O  OD2  . ASP   A 1 295 ? 1.258   9.661   -24.953 1   12.019 ? 295 ASP   A OD2  1 
ATOM   2299 N  N    . VAL   A 1 296 ? 5.891   12.169  -23.863 1   10.774 ? 296 VAL   A N    1 
ATOM   2300 C  CA   . VAL   A 1 296 ? 7.275   12.054  -23.439 1   10.901 ? 296 VAL   A CA   1 
ATOM   2301 C  C    . VAL   A 1 296 ? 7.662   13.3    -22.653 1   11.436 ? 296 VAL   A C    1 
ATOM   2302 O  O    . VAL   A 1 296 ? 8.277   13.191  -21.598 1   11.888 ? 296 VAL   A O    1 
ATOM   2303 C  CB   . VAL   A 1 296 ? 8.2     11.794  -24.64  1   10.725 ? 296 VAL   A CB   1 
ATOM   2304 C  CG1  . VAL   A 1 296 ? 9.673   11.947  -24.261 1   11.385 ? 296 VAL   A CG1  1 
ATOM   2305 C  CG2  . VAL   A 1 296 ? 7.935   10.418  -25.224 1   10.682 ? 296 VAL   A CG2  1 
ATOM   2306 N  N    . VAL   A 1 297 ? 7.325   14.483  -23.156 1   11.944 ? 297 VAL   A N    1 
ATOM   2307 C  CA   . VAL   A 1 297 ? 7.631   15.717  -22.451 1   13.202 ? 297 VAL   A CA   1 
ATOM   2308 C  C    . VAL   A 1 297 ? 6.889   15.772  -21.106 1   13.413 ? 297 VAL   A C    1 
ATOM   2309 O  O    . VAL   A 1 297 ? 7.426   16.277  -20.109 1   14.838 ? 297 VAL   A O    1 
ATOM   2310 C  CB   . VAL   A 1 297 ? 7.328   16.926  -23.357 1   14.362 ? 297 VAL   A CB   1 
ATOM   2311 C  CG1  . VAL   A 1 297 ? 7.431   18.247  -22.608 1   15.492 ? 297 VAL   A CG1  1 
ATOM   2312 C  CG2  . VAL   A 1 297 ? 8.258   16.936  -24.566 1   15.173 ? 297 VAL   A CG2  1 
ATOM   2313 N  N    . ARG   A 1 298 ? 5.658   15.242  -21.054 1   13.369 ? 298 ARG   A N    1 
ATOM   2314 C  CA   . ARG   A 1 298 ? 4.869   15.174  -19.824 1   13.803 ? 298 ARG   A CA   1 
ATOM   2315 C  C    . ARG   A 1 298 ? 5.605   14.393  -18.733 1   13.555 ? 298 ARG   A C    1 
ATOM   2316 O  O    . ARG   A 1 298 ? 5.602   14.789  -17.567 1   15.272 ? 298 ARG   A O    1 
ATOM   2317 C  CB   . ARG   A 1 298 ? 3.504   14.524  -20.099 1   14.181 ? 298 ARG   A CB   1 
ATOM   2318 C  CG   . ARG   A 1 298 ? 2.659   14.216  -18.869 1   15.142 ? 298 ARG   A CG   1 
ATOM   2319 C  CD   . ARG   A 1 298 ? 1.355   13.497  -19.203 1   15.488 ? 298 ARG   A CD   1 
ATOM   2320 N  NE   . ARG   A 1 298 ? 0.682   13.009  -17.998 1   16.104 ? 298 ARG   A NE   1 
ATOM   2321 C  CZ   . ARG   A 1 298 ? 0.083   11.844  -17.825 1   15.972 ? 298 ARG   A CZ   1 
ATOM   2322 N  NH1  . ARG   A 1 298 ? -0.063  10.989  -18.827 1   16.564 ? 298 ARG   A NH1  1 
ATOM   2323 N  NH2  . ARG   A 1 298 ? -0.399  11.562  -16.628 1   16.24  ? 298 ARG   A NH2  1 
ATOM   2324 N  N    . GLN   A 1 299 ? 6.183   13.246  -19.098 1   12.535 ? 299 GLN   A N    1 
ATOM   2325 C  CA   . GLN   A 1 299 ? 6.666   12.275  -18.131 1   12.47  ? 299 GLN   A CA   1 
ATOM   2326 C  C    . GLN   A 1 299 ? 8.174   12.372  -17.851 1   12.859 ? 299 GLN   A C    1 
ATOM   2327 O  O    . GLN   A 1 299 ? 8.622   12.111  -16.731 1   13.506 ? 299 GLN   A O    1 
ATOM   2328 C  CB   . GLN   A 1 299 ? 6.312   10.883  -18.638 1   12.813 ? 299 GLN   A CB   1 
ATOM   2329 C  CG   . GLN   A 1 299 ? 6.732   9.804   -17.66  1   12.523 ? 299 GLN   A CG   1 
ATOM   2330 C  CD   . GLN   A 1 299 ? 6.273   8.407   -17.976 1   12.442 ? 299 GLN   A CD   1 
ATOM   2331 O  OE1  . GLN   A 1 299 ? 6.719   7.474   -17.312 1   13.029 ? 299 GLN   A OE1  1 
ATOM   2332 N  NE2  . GLN   A 1 299 ? 5.385   8.216   -18.945 1   12.995 ? 299 GLN   A NE2  1 
ATOM   2333 N  N    . CYS   A 1 300 ? 8.98    12.699  -18.863 1   12.669 ? 300 CYS   A N    1 
ATOM   2334 C  CA   . CYS   A 1 300 ? 10.429  12.666  -18.71  1   13.067 ? 300 CYS   A CA   1 
ATOM   2335 C  C    . CYS   A 1 300 ? 10.968  13.948  -18.08  1   13.431 ? 300 CYS   A C    1 
ATOM   2336 O  O    . CYS   A 1 300 ? 10.38   15.018  -18.183 1   13.79  ? 300 CYS   A O    1 
ATOM   2337 C  CB   . CYS   A 1 300 ? 11.129  12.552  -20.058 1   13.688 ? 300 CYS   A CB   1 
ATOM   2338 S  SG   . CYS   A 1 300 ? 11.116  10.889  -20.776 1   17.326 ? 300 CYS   A SG   1 
ATOM   2339 N  N    . SER   A 1 301 ? 12.171  13.842  -17.503 1   13.866 ? 301 SER   A N    1 
ATOM   2340 C  CA   . SER   A 1 301 ? 12.92   15.002  -17.068 1   14.596 ? 301 SER   A CA   1 
ATOM   2341 C  C    . SER   A 1 301 ? 13.18   15.944  -18.243 1   14.539 ? 301 SER   A C    1 
ATOM   2342 O  O    . SER   A 1 301 ? 13.371  15.504  -19.382 1   14.74  ? 301 SER   A O    1 
ATOM   2343 C  CB   . SER   A 1 301 ? 14.211  14.582  -16.454 1   14.803 ? 301 SER   A CB   1 
ATOM   2344 O  OG   . SER   A 1 301 ? 14.933  15.723  -16.018 1   16.27  ? 301 SER   A OG   1 
ATOM   2345 N  N    . GLY   A 1 302 ? 13.222  17.242  -17.937 1   15.038 ? 302 GLY   A N    1 
ATOM   2346 C  CA   . GLY   A 1 302 ? 13.667  18.258  -18.879 1   15.817 ? 302 GLY   A CA   1 
ATOM   2347 C  C    . GLY   A 1 302 ? 15.187  18.318  -19.02  1   16.257 ? 302 GLY   A C    1 
ATOM   2348 O  O    . GLY   A 1 302 ? 15.679  19.124  -19.806 1   17.746 ? 302 GLY   A O    1 
ATOM   2349 N  N    . VAL   A 1 303 ? 15.924  17.527  -18.216 1   16.943 ? 303 VAL   A N    1 
ATOM   2350 C  CA   . VAL   A 1 303 ? 17.377  17.431  -18.276 1   18.278 ? 303 VAL   A CA   1 
ATOM   2351 C  C    . VAL   A 1 303 ? 17.754  16.027  -18.754 1   17.467 ? 303 VAL   A C    1 
ATOM   2352 O  O    . VAL   A 1 303 ? 17.314  15.048  -18.167 1   18.969 ? 303 VAL   A O    1 
ATOM   2353 C  CB   . VAL   A 1 303 ? 17.961  17.719  -16.875 1   20.155 ? 303 VAL   A CB   1 
ATOM   2354 C  CG1  . VAL   A 1 303 ? 19.475  17.548  -16.813 1   20.856 ? 303 VAL   A CG1  1 
ATOM   2355 C  CG2  . VAL   A 1 303 ? 17.57   19.103  -16.369 1   21.837 ? 303 VAL   A CG2  1 
ATOM   2356 N  N    . THR   A 1 304 ? 18.543  15.922  -19.834 1   16.999 ? 304 THR   A N    1 
ATOM   2357 C  CA   . THR   A 1 304 ? 19.011  14.639  -20.346 1   15.525 ? 304 THR   A CA   1 
ATOM   2358 C  C    . THR   A 1 304 ? 20.094  14.078  -19.424 1   14.977 ? 304 THR   A C    1 
ATOM   2359 O  O    . THR   A 1 304 ? 20.968  14.816  -18.965 1   16.497 ? 304 THR   A O    1 
ATOM   2360 C  CB   . THR   A 1 304 ? 19.556  14.837  -21.764 1   15.907 ? 304 THR   A CB   1 
ATOM   2361 O  OG1  . THR   A 1 304 ? 18.439  15.223  -22.558 1   17.024 ? 304 THR   A OG1  1 
ATOM   2362 C  CG2  . THR   A 1 304 ? 20.2    13.589  -22.339 1   15.716 ? 304 THR   A CG2  1 
ATOM   2363 N  N    . PHE   A 1 305 ? 20.074  12.76   -19.206 1   14.104 ? 305 PHE   A N    1 
ATOM   2364 C  CA   . PHE   A 1 305 ? 21.159  12.089  -18.5   1   14.692 ? 305 PHE   A CA   1 
ATOM   2365 C  C    . PHE   A 1 305 ? 22.275  11.789  -19.5   1   15.078 ? 305 PHE   A C    1 
ATOM   2366 O  O    . PHE   A 1 305 ? 22.213  10.793  -20.225 1   15.638 ? 305 PHE   A O    1 
ATOM   2367 C  CB   . PHE   A 1 305 ? 20.595  10.844  -17.808 1   15.062 ? 305 PHE   A CB   1 
ATOM   2368 C  CG   . PHE   A 1 305 ? 21.58   9.982   -17.026 1   15.749 ? 305 PHE   A CG   1 
ATOM   2369 C  CD1  . PHE   A 1 305 ? 22.763  10.51   -16.517 1   17.275 ? 305 PHE   A CD1  1 
ATOM   2370 C  CD2  . PHE   A 1 305 ? 21.3    8.644   -16.767 1   16.935 ? 305 PHE   A CD2  1 
ATOM   2371 C  CE1  . PHE   A 1 305 ? 23.656  9.712   -15.81  1   18.24  ? 305 PHE   A CE1  1 
ATOM   2372 C  CE2  . PHE   A 1 305 ? 22.192  7.855   -16.049 1   17.901 ? 305 PHE   A CE2  1 
ATOM   2373 C  CZ   . PHE   A 1 305 ? 23.369  8.388   -15.578 1   18.016 ? 305 PHE   A CZ   1 
ATOM   2374 N  N    . GLN   A 1 306 ? 23.298  12.656  -19.529 1   15.595 ? 306 GLN   A N    1 
ATOM   2375 C  CA   . GLN   A 1 306 ? 24.286  12.65   -20.601 1   17.359 ? 306 GLN   A CA   1 
ATOM   2376 C  C    . GLN   A 1 306 ? 25.386  11.585  -20.398 1   18.08  ? 306 GLN   A C    1 
ATOM   2377 O  O    . GLN   A 1 306 ? 26.075  11.311  -21.409 1   18.172 ? 306 GLN   A O    1 
ATOM   2378 C  CB   . GLN   A 1 306 ? 24.907  14.037  -20.753 1   18.58  ? 306 GLN   A CB   1 
ATOM   2379 C  CG   . GLN   A 1 306 ? 23.948  15.079  -21.311 1   20.865 ? 306 GLN   A CG   1 
ATOM   2380 C  CD   . GLN   A 1 306 ? 24.627  16.388  -21.642 1   24.122 ? 306 GLN   A CD   1 
ATOM   2381 O  OE1  . GLN   A 1 306 ? 25.47   16.463  -22.542 1   27.535 ? 306 GLN   A OE1  1 
ATOM   2382 N  NE2  . GLN   A 1 306 ? 24.256  17.438  -20.925 1   25.699 ? 306 GLN   A NE2  1 
ATOM   2383 O  OXT  . GLN   A 1 306 ? 25.555  11.071  -19.259 1   19.764 ? 306 GLN   A OXT  1 
ATOM   2384 N  N    . SER   B 1 1   ? -12.931 -8.337  -24.654 1   15.465 ? 1   SER   B N    1 
ATOM   2385 C  CA   . SER   B 1 1   ? -11.584 -8.938  -24.514 1   16.033 ? 1   SER   B CA   1 
ATOM   2386 C  C    . SER   B 1 1   ? -10.523 -7.836  -24.528 1   14.957 ? 1   SER   B C    1 
ATOM   2387 O  O    . SER   B 1 1   ? -10.838 -6.653  -24.558 1   13.279 ? 1   SER   B O    1 
ATOM   2388 C  CB   . SER   B 1 1   ? -11.349 -9.983  -25.57  1   18.193 ? 1   SER   B CB   1 
ATOM   2389 O  OG   . SER   B 1 1   ? -11.195 -9.391  -26.847 1   19.21  ? 1   SER   B OG   1 
ATOM   2390 N  N    . GLY   B 1 2   ? -9.258  -8.258  -24.474 1   15.93  ? 2   GLY   B N    1 
ATOM   2391 C  CA   . GLY   B 1 2   ? -8.122  -7.361  -24.414 1   15.706 ? 2   GLY   B CA   1 
ATOM   2392 C  C    . GLY   B 1 2   ? -7.487  -7.497  -23.039 1   15.855 ? 2   GLY   B C    1 
ATOM   2393 O  O    . GLY   B 1 2   ? -8.155  -7.902  -22.096 1   18.147 ? 2   GLY   B O    1 
ATOM   2394 N  N    . PHE   B 1 3   ? -6.21   -7.139  -22.935 1   15.493 ? 3   PHE   B N    1 
ATOM   2395 C  CA   . PHE   B 1 3   ? -5.506  -7.249  -21.672 1   15.913 ? 3   PHE   B CA   1 
ATOM   2396 C  C    . PHE   B 1 3   ? -4.467  -6.143  -21.612 1   16.487 ? 3   PHE   B C    1 
ATOM   2397 O  O    . PHE   B 1 3   ? -3.556  -6.115  -22.434 1   19.958 ? 3   PHE   B O    1 
ATOM   2398 C  CB   . PHE   B 1 3   ? -4.926  -8.659  -21.518 1   16.314 ? 3   PHE   B CB   1 
ATOM   2399 C  CG   . PHE   B 1 3   ? -4.624  -8.992  -20.059 1   16.331 ? 3   PHE   B CG   1 
ATOM   2400 C  CD1  . PHE   B 1 3   ? -5.658  -9.361  -19.198 1   16.972 ? 3   PHE   B CD1  1 
ATOM   2401 C  CD2  . PHE   B 1 3   ? -3.339  -8.878  -19.529 1   16.825 ? 3   PHE   B CD2  1 
ATOM   2402 C  CE1  . PHE   B 1 3   ? -5.41   -9.646  -17.862 1   17.305 ? 3   PHE   B CE1  1 
ATOM   2403 C  CE2  . PHE   B 1 3   ? -3.098  -9.146  -18.188 1   16.729 ? 3   PHE   B CE2  1 
ATOM   2404 C  CZ   . PHE   B 1 3   ? -4.138  -9.509  -17.352 1   17.202 ? 3   PHE   B CZ   1 
ATOM   2405 N  N    . ARG   B 1 4   ? -4.624  -5.25   -20.629 1   15.593 ? 4   ARG   B N    1 
ATOM   2406 C  CA   . ARG   B 1 4   ? -3.812  -4.059  -20.506 1   15.51  ? 4   ARG   B CA   1 
ATOM   2407 C  C    . ARG   B 1 4   ? -3.242  -3.98   -19.093 1   14.882 ? 4   ARG   B C    1 
ATOM   2408 O  O    . ARG   B 1 4   ? -3.817  -4.509  -18.151 1   14.74  ? 4   ARG   B O    1 
ATOM   2409 C  CB   . ARG   B 1 4   ? -4.67   -2.818  -20.75  1   16.613 ? 4   ARG   B CB   1 
ATOM   2410 C  CG   . ARG   B 1 4   ? -4.969  -2.515  -22.21  1   18.203 ? 4   ARG   B CG   1 
ATOM   2411 C  CD   . ARG   B 1 4   ? -3.71   -1.969  -22.928 1   20.387 ? 4   ARG   B CD   1 
ATOM   2412 N  NE   . ARG   B 1 4   ? -4.038  -1.079  -24.05  1   21.652 ? 4   ARG   B NE   1 
ATOM   2413 C  CZ   . ARG   B 1 4   ? -3.108  -0.501  -24.803 1   22.723 ? 4   ARG   B CZ   1 
ATOM   2414 N  NH1  . ARG   B 1 4   ? -1.894  -0.332  -24.317 1   24.602 ? 4   ARG   B NH1  1 
ATOM   2415 N  NH2  . ARG   B 1 4   ? -3.389  -0.064  -26.023 1   21.878 ? 4   ARG   B NH2  1 
ATOM   2416 N  N    . LYS   B 1 5   ? -2.117  -3.285  -18.957 1   15.184 ? 5   LYS   B N    1 
ATOM   2417 C  CA   . LYS   B 1 5   ? -1.633  -2.934  -17.637 1   15.065 ? 5   LYS   B CA   1 
ATOM   2418 C  C    . LYS   B 1 5   ? -2.586  -1.896  -17.058 1   15.051 ? 5   LYS   B C    1 
ATOM   2419 O  O    . LYS   B 1 5   ? -2.623  -0.756  -17.496 1   18.151 ? 5   LYS   B O    1 
ATOM   2420 C  CB   . LYS   B 1 5   ? -0.176  -2.459  -17.692 1   17.461 ? 5   LYS   B CB   1 
ATOM   2421 C  CG   . LYS   B 1 5   ? 0.511   -2.423  -16.353 1   19.507 ? 5   LYS   B CG   1 
ATOM   2422 C  CD   . LYS   B 1 5   ? 0.633   -3.749  -15.608 1   20.301 ? 5   LYS   B CD   1 
ATOM   2423 C  CE   . LYS   B 1 5   ? 1.576   -4.755  -16.208 1   21.961 ? 5   LYS   B CE   1 
ATOM   2424 N  NZ   . LYS   B 1 5   ? 2.948   -4.257  -16.336 1   22.908 ? 5   LYS   B NZ   1 
ATOM   2425 N  N    . MET   B 1 6   ? -3.376  -2.318  -16.074 1   13.739 ? 6   MET   B N    1 
ATOM   2426 C  CA   . MET   B 1 6   ? -4.503  -1.54   -15.582 1   14.243 ? 6   MET   B CA   1 
ATOM   2427 C  C    . MET   B 1 6   ? -4.276  -1.142  -14.127 1   12.857 ? 6   MET   B C    1 
ATOM   2428 O  O    . MET   B 1 6   ? -3.96   -1.991  -13.3   1   14.598 ? 6   MET   B O    1 
ATOM   2429 C  CB   . MET   B 1 6   ? -5.761  -2.404  -15.702 1   16.953 ? 6   MET   B CB   1 
ATOM   2430 C  CG   . MET   B 1 6   ? -7.015  -1.75   -15.271 1   19.517 ? 6   MET   B CG   1 
ATOM   2431 S  SD   . MET   B 1 6   ? -8.396  -2.855  -15.613 1   25.298 ? 6   MET   B SD   1 
ATOM   2432 C  CE   . MET   B 1 6   ? -8.309  -3.084  -17.388 1   23.307 ? 6   MET   B CE   1 
ATOM   2433 N  N    . ALA   B 1 7   ? -4.415  0.151   -13.834 1   12.021 ? 7   ALA   B N    1 
ATOM   2434 C  CA   . ALA   B 1 7   ? -4.357  0.642   -12.464 1   12.037 ? 7   ALA   B CA   1 
ATOM   2435 C  C    . ALA   B 1 7   ? -5.755  0.668   -11.87  1   11.993 ? 7   ALA   B C    1 
ATOM   2436 O  O    . ALA   B 1 7   ? -6.755  0.702   -12.583 1   12.079 ? 7   ALA   B O    1 
ATOM   2437 C  CB   . ALA   B 1 7   ? -3.766  2.02    -12.397 1   12.375 ? 7   ALA   B CB   1 
ATOM   2438 N  N    . PHE   B 1 8   ? -5.825  0.714   -10.54  1   12.028 ? 8   PHE   B N    1 
ATOM   2439 C  CA   . PHE   B 1 8   ? -7.086  0.982   -9.866  1   12.28  ? 8   PHE   B CA   1 
ATOM   2440 C  C    . PHE   B 1 8   ? -7.518  2.423   -10.119 1   12.181 ? 8   PHE   B C    1 
ATOM   2441 O  O    . PHE   B 1 8   ? -6.702  3.325   -10.261 1   12.374 ? 8   PHE   B O    1 
ATOM   2442 C  CB   . PHE   B 1 8   ? -6.974  0.771   -8.353  1   12.876 ? 8   PHE   B CB   1 
ATOM   2443 C  CG   . PHE   B 1 8   ? -6.902  -0.689  -7.956  1   13.793 ? 8   PHE   B CG   1 
ATOM   2444 C  CD1  . PHE   B 1 8   ? -8.051  -1.462  -7.881  1   15.319 ? 8   PHE   B CD1  1 
ATOM   2445 C  CD2  . PHE   B 1 8   ? -5.681  -1.286  -7.678  1   15.466 ? 8   PHE   B CD2  1 
ATOM   2446 C  CE1  . PHE   B 1 8   ? -7.977  -2.806  -7.555  1   16.799 ? 8   PHE   B CE1  1 
ATOM   2447 C  CE2  . PHE   B 1 8   ? -5.619  -2.638  -7.375  1   17.193 ? 8   PHE   B CE2  1 
ATOM   2448 C  CZ   . PHE   B 1 8   ? -6.767  -3.386  -7.3    1   17.67  ? 8   PHE   B CZ   1 
ATOM   2449 N  N    . PRO   B 1 9   ? -8.839  2.708   -10.142 1   12.835 ? 9   PRO   B N    1 
ATOM   2450 C  CA   . PRO   B 1 9   ? -9.307  4.091   -10.189 1   12.383 ? 9   PRO   B CA   1 
ATOM   2451 C  C    . PRO   B 1 9   ? -8.724  4.838   -8.992  1   12.311 ? 9   PRO   B C    1 
ATOM   2452 O  O    . PRO   B 1 9   ? -8.772  4.322   -7.877  1   14.704 ? 9   PRO   B O    1 
ATOM   2453 C  CB   . PRO   B 1 9   ? -10.836 3.958   -10.109 1   13.239 ? 9   PRO   B CB   1 
ATOM   2454 C  CG   . PRO   B 1 9   ? -11.111 2.525   -10.508 1   14.485 ? 9   PRO   B CG   1 
ATOM   2455 C  CD   . PRO   B 1 9   ? -9.925  1.735   -9.984  1   13.89  ? 9   PRO   B CD   1 
ATOM   2456 N  N    . SER   B 1 10  ? -8.214  6.051   -9.212  1   11.765 ? 10  SER   B N    1 
ATOM   2457 C  CA   . SER   B 1 10  ? -7.398  6.737   -8.217  1   11.518 ? 10  SER   B CA   1 
ATOM   2458 C  C    . SER   B 1 10  ? -8.158  7.795   -7.42   1   11.876 ? 10  SER   B C    1 
ATOM   2459 O  O    . SER   B 1 10  ? -7.578  8.388   -6.514  1   12.042 ? 10  SER   B O    1 
ATOM   2460 C  CB   . SER   B 1 10  ? -6.179  7.36    -8.875  1   11.973 ? 10  SER   B CB   1 
ATOM   2461 O  OG   . SER   B 1 10  ? -6.555  8.252   -9.915  1   12.16  ? 10  SER   B OG   1 
ATOM   2462 N  N    . GLY   B 1 11  ? -9.443  8.01    -7.704  1   12.388 ? 11  GLY   B N    1 
ATOM   2463 C  CA   . GLY   B 1 11  ? -10.18  9.112   -7.097  1   12.349 ? 11  GLY   B CA   1 
ATOM   2464 C  C    . GLY   B 1 11  ? -10.144 9.135   -5.567  1   12.953 ? 11  GLY   B C    1 
ATOM   2465 O  O    . GLY   B 1 11  ? -9.989  10.201  -4.97   1   13.439 ? 11  GLY   B O    1 
ATOM   2466 N  N    . LYS   B 1 12  ? -10.311 7.965   -4.947  1   12.883 ? 12  LYS   B N    1 
ATOM   2467 C  CA   . LYS   B 1 12  ? -10.347 7.896   -3.493  1   13.434 ? 12  LYS   B CA   1 
ATOM   2468 C  C    . LYS   B 1 12  ? -9.029  8.379   -2.897  1   13.044 ? 12  LYS   B C    1 
ATOM   2469 O  O    . LYS   B 1 12  ? -9.009  8.908   -1.787  1   14.26  ? 12  LYS   B O    1 
ATOM   2470 C  CB   . LYS   B 1 12  ? -10.663 6.471   -3.041  1   14.876 ? 12  LYS   B CB   1 
ATOM   2471 C  CG   . LYS   B 1 12  ? -12.106 6.053   -3.263  1   17.877 ? 12  LYS   B CG   1 
ATOM   2472 C  CD   . LYS   B 1 12  ? -12.367 4.615   -2.835  1   21.955 ? 12  LYS   B CD   1 
ATOM   2473 C  CE   . LYS   B 1 12  ? -13.822 4.355   -2.585  1   26.155 ? 12  LYS   B CE   1 
ATOM   2474 N  NZ   . LYS   B 1 12  ? -14.608 4.542   -3.801  1   29.1   ? 12  LYS   B NZ   1 
ATOM   2475 N  N    . VAL   B 1 13  ? -7.92   8.151   -3.603  1   11.813 ? 13  VAL   B N    1 
ATOM   2476 C  CA   . VAL   B 1 13  ? -6.61   8.556   -3.112  1   11.832 ? 13  VAL   B CA   1 
ATOM   2477 C  C    . VAL   B 1 13  ? -6.335  10.02   -3.453  1   11.715 ? 13  VAL   B C    1 
ATOM   2478 O  O    . VAL   B 1 13  ? -5.696  10.736  -2.678  1   11.865 ? 13  VAL   B O    1 
ATOM   2479 C  CB   . VAL   B 1 13  ? -5.525  7.617   -3.673  1   12.039 ? 13  VAL   B CB   1 
ATOM   2480 C  CG1  . VAL   B 1 13  ? -4.118  8.046   -3.261  1   12.051 ? 13  VAL   B CG1  1 
ATOM   2481 C  CG2  . VAL   B 1 13  ? -5.809  6.171   -3.294  1   12.684 ? 13  VAL   B CG2  1 
ATOM   2482 N  N    . GLU   B 1 14  ? -6.798  10.475  -4.63   1   11.625 ? 14  GLU   B N    1 
ATOM   2483 C  CA   . GLU   B 1 14  ? -6.592  11.861  -5.019  1   11.971 ? 14  GLU   B CA   1 
ATOM   2484 C  C    . GLU   B 1 14  ? -7.074  12.827  -3.938  1   12.273 ? 14  GLU   B C    1 
ATOM   2485 O  O    . GLU   B 1 14  ? -6.424  13.838  -3.682  1   13.175 ? 14  GLU   B O    1 
ATOM   2486 C  CB   . GLU   B 1 14  ? -7.292  12.162  -6.336  1   11.863 ? 14  GLU   B CB   1 
ATOM   2487 C  CG   . GLU   B 1 14  ? -6.647  11.499  -7.554  1   12.106 ? 14  GLU   B CG   1 
ATOM   2488 C  CD   . GLU   B 1 14  ? -7.528  11.607  -8.791  1   12.602 ? 14  GLU   B CD   1 
ATOM   2489 O  OE1  . GLU   B 1 14  ? -7.82   10.543  -9.334  1   12.927 ? 14  GLU   B OE1  1 
ATOM   2490 O  OE2  . GLU   B 1 14  ? -7.952  12.724  -9.16   1   13.683 ? 14  GLU   B OE2  1 
ATOM   2491 N  N    . GLY   B 1 15  ? -8.208  12.503  -3.316  1   12.544 ? 15  GLY   B N    1 
ATOM   2492 C  CA   . GLY   B 1 15  ? -8.805  13.353  -2.294  1   13.246 ? 15  GLY   B CA   1 
ATOM   2493 C  C    . GLY   B 1 15  ? -8.025  13.393  -0.98   1   13.294 ? 15  GLY   B C    1 
ATOM   2494 O  O    . GLY   B 1 15  ? -8.404  14.132  -0.067  1   14.452 ? 15  GLY   B O    1 
ATOM   2495 N  N    . CYS   B 1 16  ? -6.941  12.613  -0.9    1   11.973 ? 16  CYS   B N    1 
ATOM   2496 C  CA   . CYS   B 1 16  ? -6.116  12.545  0.296   1   12.058 ? 16  CYS   B CA   1 
ATOM   2497 C  C    . CYS   B 1 16  ? -4.748  13.192  0.083   1   11.616 ? 16  CYS   B C    1 
ATOM   2498 O  O    . CYS   B 1 16  ? -3.966  13.299  1.018   1   12.203 ? 16  CYS   B O    1 
ATOM   2499 C  CB   . CYS   B 1 16  ? -5.888  11.098  0.713   1   12.885 ? 16  CYS   B CB   1 
ATOM   2500 S  SG   . CYS   B 1 16  ? -7.422  10.207  1.056   1   15.511 ? 16  CYS   B SG   1 
ATOM   2501 N  N    . MET   B 1 17  ? -4.413  13.615  -1.141  1   11.158 ? 17  MET   B N    1 
ATOM   2502 C  CA   . MET   B 1 17  ? -3.074  14.143  -1.36   1   11.226 ? 17  MET   B CA   1 
ATOM   2503 C  C    . MET   B 1 17  ? -3.018  15.634  -1.032  1   11.46  ? 17  MET   B C    1 
ATOM   2504 O  O    . MET   B 1 17  ? -3.901  16.415  -1.414  1   13.354 ? 17  MET   B O    1 
ATOM   2505 C  CB   . MET   B 1 17  ? -2.624  13.911  -2.805  1   11.997 ? 17  MET   B CB   1 
ATOM   2506 C  CG   . MET   B 1 17  ? -2.632  12.456  -3.205  1   12.236 ? 17  MET   B CG   1 
ATOM   2507 S  SD   . MET   B 1 17  ? -1.708  11.349  -2.123  1   13.779 ? 17  MET   B SD   1 
ATOM   2508 C  CE   . MET   B 1 17  ? -0.073  12.109  -2.072  1   13.293 ? 17  MET   B CE   1 
ATOM   2509 N  N    . VAL   B 1 18  ? -1.942  16.007  -0.323  1   11.489 ? 18  VAL   B N    1 
ATOM   2510 C  CA   . VAL   B 1 18  ? -1.701  17.374  0.101   1   11.591 ? 18  VAL   B CA   1 
ATOM   2511 C  C    . VAL   B 1 18  ? -0.244  17.731  -0.164  1   11.767 ? 18  VAL   B C    1 
ATOM   2512 O  O    . VAL   B 1 18  ? 0.601   16.872  -0.403  1   11.879 ? 18  VAL   B O    1 
ATOM   2513 C  CB   . VAL   B 1 18  ? -2.056  17.593  1.586   1   12.055 ? 18  VAL   B CB   1 
ATOM   2514 C  CG1  . VAL   B 1 18  ? -3.521  17.299  1.869   1   12.544 ? 18  VAL   B CG1  1 
ATOM   2515 C  CG2  . VAL   B 1 18  ? -1.173  16.777  2.513   1   11.839 ? 18  VAL   B CG2  1 
ATOM   2516 N  N    . GLN   B 1 19  ? 0.005   19.036  -0.143  1   13.194 ? 19  GLN   B N    1 
ATOM   2517 C  CA   . GLN   B 1 19  ? 1.338   19.592  -0.264  1   13.979 ? 19  GLN   B CA   1 
ATOM   2518 C  C    . GLN   B 1 19  ? 1.905   19.865  1.122   1   14.102 ? 19  GLN   B C    1 
ATOM   2519 O  O    . GLN   B 1 19  ? 1.214   20.479  1.937   1   14.771 ? 19  GLN   B O    1 
ATOM   2520 C  CB   . GLN   B 1 19  ? 1.225   20.916  -1.016  1   15.886 ? 19  GLN   B CB   1 
ATOM   2521 C  CG   . GLN   B 1 19  ? 2.582   21.525  -1.333  1   18.395 ? 19  GLN   B CG   1 
ATOM   2522 C  CD   . GLN   B 1 19  ? 2.48    22.889  -1.968  1   22.521 ? 19  GLN   B CD   1 
ATOM   2523 O  OE1  . GLN   B 1 19  ? 2.799   23.048  -3.148  1   28.39  ? 19  GLN   B OE1  1 
ATOM   2524 N  NE2  . GLN   B 1 19  ? 2.051   23.88   -1.195  1   23.984 ? 19  GLN   B NE2  1 
ATOM   2525 N  N    . VAL   B 1 20  ? 3.136   19.394  1.376   1   13.915 ? 20  VAL   B N    1 
ATOM   2526 C  CA   . VAL   B 1 20  ? 3.821   19.633  2.637   1   14.24  ? 20  VAL   B CA   1 
ATOM   2527 C  C    . VAL   B 1 20  ? 5.094   20.418  2.33    1   14.975 ? 20  VAL   B C    1 
ATOM   2528 O  O    . VAL   B 1 20  ? 5.922   19.968  1.531   1   14.187 ? 20  VAL   B O    1 
ATOM   2529 C  CB   . VAL   B 1 20  ? 4.153   18.33   3.388   1   14.388 ? 20  VAL   B CB   1 
ATOM   2530 C  CG1  . VAL   B 1 20  ? 4.922   18.597  4.681   1   15.067 ? 20  VAL   B CG1  1 
ATOM   2531 C  CG2  . VAL   B 1 20  ? 2.903   17.499  3.667   1   14.465 ? 20  VAL   B CG2  1 
ATOM   2532 N  N    . THR   B 1 21  ? 5.257   21.567  2.994   1   16.336 ? 21  THR   B N    1 
ATOM   2533 C  CA   . THR   B 1 21  ? 6.446   22.389  2.83    1   17.426 ? 21  THR   B CA   1 
ATOM   2534 C  C    . THR   B 1 21  ? 7.116   22.538  4.191   1   17.685 ? 21  THR   B C    1 
ATOM   2535 O  O    . THR   B 1 21  ? 6.468   22.897  5.171   1   18.11  ? 21  THR   B O    1 
ATOM   2536 C  CB   . THR   B 1 21  ? 6.1     23.754  2.237   1   19.008 ? 21  THR   B CB   1 
ATOM   2537 O  OG1  . THR   B 1 21  ? 5.491   23.549  0.967   1   20.323 ? 21  THR   B OG1  1 
ATOM   2538 C  CG2  . THR   B 1 21  ? 7.321   24.633  2.047   1   20.529 ? 21  THR   B CG2  1 
ATOM   2539 N  N    . CYS   B 1 22  ? 8.425   22.269  4.219   1   17.439 ? 22  CYS   B N    1 
ATOM   2540 C  CA   . CYS   B 1 22  ? 9.248   22.53   5.386   1   17.97  ? 22  CYS   B CA   1 
ATOM   2541 C  C    . CYS   B 1 22  ? 10.467  23.302  4.9     1   18.375 ? 22  CYS   B C    1 
ATOM   2542 O  O    . CYS   B 1 22  ? 11.255  22.77   4.123   1   18.643 ? 22  CYS   B O    1 
ATOM   2543 C  CB   . CYS   B 1 22  ? 9.624   21.231  6.085   1   18.267 ? 22  CYS   B CB   1 
ATOM   2544 S  SG   . CYS   B 1 22  ? 10.551  21.502  7.615   1   20.407 ? 22  CYS   B SG   1 
ATOM   2545 N  N    . GLY   B 1 23  ? 10.563  24.578  5.292   1   19.872 ? 23  GLY   B N    1 
ATOM   2546 C  CA   . GLY   B 1 23  ? 11.629  25.434  4.798   1   20.495 ? 23  GLY   B CA   1 
ATOM   2547 C  C    . GLY   B 1 23  ? 11.596  25.509  3.275   1   20.862 ? 23  GLY   B C    1 
ATOM   2548 O  O    . GLY   B 1 23  ? 10.558  25.855  2.707   1   21.781 ? 23  GLY   B O    1 
ATOM   2549 N  N    . THR   B 1 24  ? 12.721  25.137  2.639   1   20.313 ? 24  THR   B N    1 
ATOM   2550 C  CA   . THR   B 1 24  ? 12.88   25.243  1.199   1   20.159 ? 24  THR   B CA   1 
ATOM   2551 C  C    . THR   B 1 24  ? 12.365  23.996  0.474   1   17.806 ? 24  THR   B C    1 
ATOM   2552 O  O    . THR   B 1 24  ? 12.353  23.997  -0.755  1   18.897 ? 24  THR   B O    1 
ATOM   2553 C  CB   . THR   B 1 24  ? 14.353  25.501  0.855   1   21.678 ? 24  THR   B CB   1 
ATOM   2554 O  OG1  . THR   B 1 24  ? 15.132  24.392  1.299   1   22.35  ? 24  THR   B OG1  1 
ATOM   2555 C  CG2  . THR   B 1 24  ? 14.896  26.776  1.473   1   23.354 ? 24  THR   B CG2  1 
ATOM   2556 N  N    . THR   B 1 25  ? 11.933  22.953  1.201   1   16.915 ? 25  THR   B N    1 
ATOM   2557 C  CA   . THR   B 1 25  ? 11.494  21.709  0.591   1   16.114 ? 25  THR   B CA   1 
ATOM   2558 C  C    . THR   B 1 25  ? 9.971   21.65   0.514   1   16.077 ? 25  THR   B C    1 
ATOM   2559 O  O    . THR   B 1 25  ? 9.294   21.798  1.526   1   16.577 ? 25  THR   B O    1 
ATOM   2560 C  CB   . THR   B 1 25  ? 12.012  20.515  1.387   1   16.075 ? 25  THR   B CB   1 
ATOM   2561 O  OG1  . THR   B 1 25  ? 13.421  20.51   1.23    1   16.431 ? 25  THR   B OG1  1 
ATOM   2562 C  CG2  . THR   B 1 25  ? 11.473  19.193  0.868   1   16.366 ? 25  THR   B CG2  1 
ATOM   2563 N  N    . THR   B 1 26  ? 9.455   21.317  -0.671  1   15.422 ? 26  THR   B N    1 
ATOM   2564 C  CA   . THR   B 1 26  ? 8.052   20.952  -0.84   1   14.914 ? 26  THR   B CA   1 
ATOM   2565 C  C    . THR   B 1 26  ? 7.972   19.529  -1.379  1   13.806 ? 26  THR   B C    1 
ATOM   2566 O  O    . THR   B 1 26  ? 8.689   19.176  -2.316  1   14.674 ? 26  THR   B O    1 
ATOM   2567 C  CB   . THR   B 1 26  ? 7.368   21.935  -1.788  1   16.705 ? 26  THR   B CB   1 
ATOM   2568 O  OG1  . THR   B 1 26  ? 7.361   23.21   -1.156  1   19.005 ? 26  THR   B OG1  1 
ATOM   2569 C  CG2  . THR   B 1 26  ? 5.942   21.534  -2.12   1   17.749 ? 26  THR   B CG2  1 
ATOM   2570 N  N    . LEU   B 1 27  ? 7.114   18.708  -0.774  1   13.026 ? 27  LEU   B N    1 
ATOM   2571 C  CA   . LEU   B 1 27  ? 6.834   17.372  -1.278  1   12.38  ? 27  LEU   B CA   1 
ATOM   2572 C  C    . LEU   B 1 27  ? 5.383   17.034  -0.926  1   11.523 ? 27  LEU   B C    1 
ATOM   2573 O  O    . LEU   B 1 27  ? 4.606   17.943  -0.616  1   12.888 ? 27  LEU   B O    1 
ATOM   2574 C  CB   . LEU   B 1 27  ? 7.862   16.347  -0.792  1   12.544 ? 27  LEU   B CB   1 
ATOM   2575 C  CG   . LEU   B 1 27  ? 8.222   16.35   0.696   1   12.648 ? 27  LEU   B CG   1 
ATOM   2576 C  CD1  . LEU   B 1 27  ? 7.062   16.003  1.614   1   12.858 ? 27  LEU   B CD1  1 
ATOM   2577 C  CD2  . LEU   B 1 27  ? 9.381   15.376  0.904   1   13.531 ? 27  LEU   B CD2  1 
ATOM   2578 N  N    . ASN   B 1 28  ? 5.006   15.761  -1.076  1   10.849 ? 28  ASN   B N    1 
ATOM   2579 C  CA   . ASN   B 1 28  ? 3.615   15.349  -0.988  1   10.573 ? 28  ASN   B CA   1 
ATOM   2580 C  C    . ASN   B 1 28  ? 3.378   14.678  0.354   1   10.735 ? 28  ASN   B C    1 
ATOM   2581 O  O    . ASN   B 1 28  ? 4.253   13.995  0.887   1   11.286 ? 28  ASN   B O    1 
ATOM   2582 C  CB   . ASN   B 1 28  ? 3.24    14.399  -2.125  1   10.725 ? 28  ASN   B CB   1 
ATOM   2583 C  CG   . ASN   B 1 28  ? 3.652   14.966  -3.457  1   11.159 ? 28  ASN   B CG   1 
ATOM   2584 O  OD1  . ASN   B 1 28  ? 2.965   15.849  -3.976  1   11.69  ? 28  ASN   B OD1  1 
ATOM   2585 N  ND2  . ASN   B 1 28  ? 4.755   14.484  -4.021  1   11.696 ? 28  ASN   B ND2  1 
ATOM   2586 N  N    . GLY   B 1 29  ? 2.144   14.813  0.834   1   10.785 ? 29  GLY   B N    1 
ATOM   2587 C  CA   . GLY   B 1 29  ? 1.695   14.103  2.017   1   10.588 ? 29  GLY   B CA   1 
ATOM   2588 C  C    . GLY   B 1 29  ? 0.356   13.423  1.769   1   10.456 ? 29  GLY   B C    1 
ATOM   2589 O  O    . GLY   B 1 29  ? -0.373  13.796  0.86    1   10.242 ? 29  GLY   B O    1 
ATOM   2590 N  N    . LEU   B 1 30  ? 0.034   12.458  2.626   1   10.108 ? 30  LEU   B N    1 
ATOM   2591 C  CA   . LEU   B 1 30  ? -1.221  11.724  2.595   1   9.849  ? 30  LEU   B CA   1 
ATOM   2592 C  C    . LEU   B 1 30  ? -2.038  12.1    3.832   1   10.059 ? 30  LEU   B C    1 
ATOM   2593 O  O    . LEU   B 1 30  ? -1.59   11.867  4.96    1   10.707 ? 30  LEU   B O    1 
ATOM   2594 C  CB   . LEU   B 1 30  ? -0.887  10.239  2.578   1   10.273 ? 30  LEU   B CB   1 
ATOM   2595 C  CG   . LEU   B 1 30  ? -2.064  9.264   2.47    1   10.346 ? 30  LEU   B CG   1 
ATOM   2596 C  CD1  . LEU   B 1 30  ? -2.765  9.372   1.134   1   11.133 ? 30  LEU   B CD1  1 
ATOM   2597 C  CD2  . LEU   B 1 30  ? -1.639  7.842   2.725   1   10.209 ? 30  LEU   B CD2  1 
ATOM   2598 N  N    . TRP   B 1 31  ? -3.232  12.653  3.589   1   10.198 ? 31  TRP   B N    1 
ATOM   2599 C  CA   . TRP   B 1 31  ? -4.098  13.186  4.628   1   10.373 ? 31  TRP   B CA   1 
ATOM   2600 C  C    . TRP   B 1 31  ? -5.253  12.222  4.865   1   10.645 ? 31  TRP   B C    1 
ATOM   2601 O  O    . TRP   B 1 31  ? -6.132  12.101  4.009   1   11.018 ? 31  TRP   B O    1 
ATOM   2602 C  CB   . TRP   B 1 31  ? -4.585  14.573  4.213   1   11.252 ? 31  TRP   B CB   1 
ATOM   2603 C  CG   . TRP   B 1 31  ? -5.47   15.281  5.202   1   12.269 ? 31  TRP   B CG   1 
ATOM   2604 C  CD1  . TRP   B 1 31  ? -5.545  15.108  6.555   1   12.857 ? 31  TRP   B CD1  1 
ATOM   2605 C  CD2  . TRP   B 1 31  ? -6.427  16.302  4.869   1   13.398 ? 31  TRP   B CD2  1 
ATOM   2606 N  NE1  . TRP   B 1 31  ? -6.462  15.964  7.09    1   13.777 ? 31  TRP   B NE1  1 
ATOM   2607 C  CE2  . TRP   B 1 31  ? -7.033  16.697  6.085   1   14.033 ? 31  TRP   B CE2  1 
ATOM   2608 C  CE3  . TRP   B 1 31  ? -6.844  16.903  3.673   1   14.011 ? 31  TRP   B CE3  1 
ATOM   2609 C  CZ2  . TRP   B 1 31  ? -8.019  17.678  6.137   1   14.557 ? 31  TRP   B CZ2  1 
ATOM   2610 C  CZ3  . TRP   B 1 31  ? -7.841  17.853  3.726   1   14.937 ? 31  TRP   B CZ3  1 
ATOM   2611 C  CH2  . TRP   B 1 31  ? -8.411  18.233  4.94    1   14.85  ? 31  TRP   B CH2  1 
ATOM   2612 N  N    . LEU   B 1 32  ? -5.23   11.543  6.021   1   11.028 ? 32  LEU   B N    1 
ATOM   2613 C  CA   . LEU   B 1 32  ? -6.238  10.568  6.404   1   11.021 ? 32  LEU   B CA   1 
ATOM   2614 C  C    . LEU   B 1 32  ? -6.679  10.881  7.827   1   11.676 ? 32  LEU   B C    1 
ATOM   2615 O  O    . LEU   B 1 32  ? -5.832  11.036  8.719   1   12     ? 32  LEU   B O    1 
ATOM   2616 C  CB   . LEU   B 1 32  ? -5.723  9.135   6.329   1   11.678 ? 32  LEU   B CB   1 
ATOM   2617 C  CG   . LEU   B 1 32  ? -5.237  8.676   4.952   1   12.215 ? 32  LEU   B CG   1 
ATOM   2618 C  CD1  . LEU   B 1 32  ? -4.433  7.411   5.103   1   12.498 ? 32  LEU   B CD1  1 
ATOM   2619 C  CD2  . LEU   B 1 32  ? -6.408  8.468   4.011   1   12.753 ? 32  LEU   B CD2  1 
ATOM   2620 N  N    . ASP   B 1 33  ? -7.998  10.956  8.05    1   12.539 ? 33  ASP   B N    1 
ATOM   2621 C  CA   . ASP   B 1 33  ? -8.466  11.412  9.354   1   13.39  ? 33  ASP   B CA   1 
ATOM   2622 C  C    . ASP   B 1 33  ? -7.764  12.753  9.615   1   13.812 ? 33  ASP   B C    1 
ATOM   2623 O  O    . ASP   B 1 33  ? -7.679  13.595  8.706   1   15.066 ? 33  ASP   B O    1 
ATOM   2624 C  CB   . ASP   B 1 33  ? -8.298  10.284  10.37   1   15.016 ? 33  ASP   B CB   1 
ATOM   2625 C  CG   . ASP   B 1 33  ? -9.134  9.044   10.085  1   17.168 ? 33  ASP   B CG   1 
ATOM   2626 O  OD1  . ASP   B 1 33  ? -10.357 9.194   9.987   1   21.766 ? 33  ASP   B OD1  1 
ATOM   2627 O  OD2  . ASP   B 1 33  ? -8.58   7.933   9.993   1   19.73  ? 33  ASP   B OD2  1 
ATOM   2628 N  N    . ASP   B 1 34  ? -7.218  12.956  10.827  1   13.474 ? 34  ASP   B N    1 
ATOM   2629 C  CA   . ASP   B 1 34  ? -6.591  14.227  11.165  1   12.876 ? 34  ASP   B CA   1 
ATOM   2630 C  C    . ASP   B 1 34  ? -5.063  14.134  11.175  1   12.403 ? 34  ASP   B C    1 
ATOM   2631 O  O    . ASP   B 1 34  ? -4.416  14.878  11.91   1   13.283 ? 34  ASP   B O    1 
ATOM   2632 C  CB   . ASP   B 1 34  ? -7.091  14.762  12.5    1   14.501 ? 34  ASP   B CB   1 
ATOM   2633 C  CG   . ASP   B 1 34  ? -6.861  13.867  13.706  1   15.737 ? 34  ASP   B CG   1 
ATOM   2634 O  OD1  . ASP   B 1 34  ? -6.446  12.696  13.522  1   16.429 ? 34  ASP   B OD1  1 
ATOM   2635 O  OD2  . ASP   B 1 34  ? -7.104  14.356  14.836  1   19.071 ? 34  ASP   B OD2  1 
ATOM   2636 N  N    . VAL   B 1 35  ? -4.485  13.25   10.358  1   11.427 ? 35  VAL   B N    1 
ATOM   2637 C  CA   . VAL   B 1 35  ? -3.035  13.124  10.266  1   11.53  ? 35  VAL   B CA   1 
ATOM   2638 C  C    . VAL   B 1 35  ? -2.594  13.207  8.808   1   11.028 ? 35  VAL   B C    1 
ATOM   2639 O  O    . VAL   B 1 35  ? -3.231  12.633  7.925   1   11.262 ? 35  VAL   B O    1 
ATOM   2640 C  CB   . VAL   B 1 35  ? -2.537  11.821  10.908  1   12.235 ? 35  VAL   B CB   1 
ATOM   2641 C  CG1  . VAL   B 1 35  ? -1.035  11.633  10.744  1   12.546 ? 35  VAL   B CG1  1 
ATOM   2642 C  CG2  . VAL   B 1 35  ? -2.911  11.779  12.382  1   12.826 ? 35  VAL   B CG2  1 
ATOM   2643 N  N    . VAL   B 1 36  ? -1.482  13.924  8.586   1   10.667 ? 36  VAL   B N    1 
ATOM   2644 C  CA   . VAL   B 1 36  ? -0.779  13.929  7.311   1   10.678 ? 36  VAL   B CA   1 
ATOM   2645 C  C    . VAL   B 1 36  ? 0.527   13.154  7.455   1   10.791 ? 36  VAL   B C    1 
ATOM   2646 O  O    . VAL   B 1 36  ? 1.323   13.416  8.36    1   11.716 ? 36  VAL   B O    1 
ATOM   2647 C  CB   . VAL   B 1 36  ? -0.53   15.364  6.831   1   11.081 ? 36  VAL   B CB   1 
ATOM   2648 C  CG1  . VAL   B 1 36  ? 0.355   15.407  5.589   1   11.445 ? 36  VAL   B CG1  1 
ATOM   2649 C  CG2  . VAL   B 1 36  ? -1.839  16.105  6.614   1   11.226 ? 36  VAL   B CG2  1 
ATOM   2650 N  N    . TYR   B 1 37  ? 0.727   12.18   6.565   1   10.408 ? 37  TYR   B N    1 
ATOM   2651 C  CA   . TYR   B 1 37  ? 1.9     11.32   6.553   1   10.182 ? 37  TYR   B CA   1 
ATOM   2652 C  C    . TYR   B 1 37  ? 2.819   11.751  5.417   1   10.118 ? 37  TYR   B C    1 
ATOM   2653 O  O    . TYR   B 1 37  ? 2.352   11.928  4.301   1   11.067 ? 37  TYR   B O    1 
ATOM   2654 C  CB   . TYR   B 1 37  ? 1.502   9.85    6.371   1   10.406 ? 37  TYR   B CB   1 
ATOM   2655 C  CG   . TYR   B 1 37  ? 0.501   9.316   7.382   1   11.316 ? 37  TYR   B CG   1 
ATOM   2656 C  CD1  . TYR   B 1 37  ? -0.86   9.565   7.254   1   11.882 ? 37  TYR   B CD1  1 
ATOM   2657 C  CD2  . TYR   B 1 37  ? 0.925   8.601   8.499   1   12.356 ? 37  TYR   B CD2  1 
ATOM   2658 C  CE1  . TYR   B 1 37  ? -1.762  9.118   8.205   1   12.694 ? 37  TYR   B CE1  1 
ATOM   2659 C  CE2  . TYR   B 1 37  ? 0.028   8.119   9.438   1   12.77  ? 37  TYR   B CE2  1 
ATOM   2660 C  CZ   . TYR   B 1 37  ? -1.321  8.393   9.298   1   12.906 ? 37  TYR   B CZ   1 
ATOM   2661 O  OH   . TYR   B 1 37  ? -2.203  7.967   10.261  1   14.589 ? 37  TYR   B OH   1 
ATOM   2662 N  N    . CYS   B 1 38  ? 4.119   11.869  5.678   1   9.914  ? 38  CYS   B N    1 
ATOM   2663 C  CA   . CYS   B 1 38  ? 5.053   12.163  4.607   1   9.957  ? 38  CYS   B CA   1 
ATOM   2664 C  C    . CYS   B 1 38  ? 6.427   11.616  4.987   1   9.975  ? 38  CYS   B C    1 
ATOM   2665 O  O    . CYS   B 1 38  ? 6.633   11.175  6.118   1   10.524 ? 38  CYS   B O    1 
ATOM   2666 C  CB   . CYS   B 1 38  ? 5.101   13.659  4.311   1   11.092 ? 38  CYS   B CB   1 
ATOM   2667 S  SG   . CYS   B 1 38  ? 5.958   14.66   5.559   1   13.976 ? 38  CYS   B SG   1 
ATOM   2668 N  N    . PRO   B 1 39  ? 7.413   11.602  4.062   1   9.634  ? 39  PRO   B N    1 
ATOM   2669 C  CA   . PRO   B 1 39  ? 8.745   11.106  4.404   1   9.833  ? 39  PRO   B CA   1 
ATOM   2670 C  C    . PRO   B 1 39  ? 9.405   12.006  5.441   1   9.874  ? 39  PRO   B C    1 
ATOM   2671 O  O    . PRO   B 1 39  ? 9.346   13.218  5.336   1   10.726 ? 39  PRO   B O    1 
ATOM   2672 C  CB   . PRO   B 1 39  ? 9.5     11.148  3.087   1   10.049 ? 39  PRO   B CB   1 
ATOM   2673 C  CG   . PRO   B 1 39  ? 8.413   11.037  2.06    1   10.228 ? 39  PRO   B CG   1 
ATOM   2674 C  CD   . PRO   B 1 39  ? 7.279   11.887  2.622   1   9.868  ? 39  PRO   B CD   1 
ATOM   2675 N  N    . ARG   B 1 40  ? 10.094  11.4    6.413   1   10.107 ? 40  ARG   B N    1 
ATOM   2676 C  CA   . ARG   B 1 40  ? 10.76   12.194  7.429   1   10.378 ? 40  ARG   B CA   1 
ATOM   2677 C  C    . ARG   B 1 40  ? 11.911  13.025  6.85    1   10.698 ? 40  ARG   B C    1 
ATOM   2678 O  O    . ARG   B 1 40  ? 12.278  14.038  7.444   1   11.526 ? 40  ARG   B O    1 
ATOM   2679 C  CB   . ARG   B 1 40  ? 11.211  11.351  8.624   1   10.397 ? 40  ARG   B CB   1 
ATOM   2680 C  CG   . ARG   B 1 40  ? 12.329  10.362  8.355   1   10.776 ? 40  ARG   B CG   1 
ATOM   2681 C  CD   . ARG   B 1 40  ? 12.794  9.711   9.651   1   10.73  ? 40  ARG   B CD   1 
ATOM   2682 N  NE   . ARG   B 1 40  ? 13.772  8.669   9.354   1   11.223 ? 40  ARG   B NE   1 
ATOM   2683 C  CZ   . ARG   B 1 40  ? 14.512  8.019   10.239  1   12.03  ? 40  ARG   B CZ   1 
ATOM   2684 N  NH1  . ARG   B 1 40  ? 14.288  8.144   11.531  1   12.399 ? 40  ARG   B NH1  1 
ATOM   2685 N  NH2  . ARG   B 1 40  ? 15.483  7.22    9.829   1   12.263 ? 40  ARG   B NH2  1 
ATOM   2686 N  N    . HIS   B 1 41  ? 12.446  12.644  5.68    1   10.736 ? 41  HIS   B N    1 
ATOM   2687 C  CA   . HIS   B 1 41  ? 13.519  13.409  5.065   1   11.058 ? 41  HIS   B CA   1 
ATOM   2688 C  C    . HIS   B 1 41  ? 13.093  14.825  4.664   1   11.405 ? 41  HIS   B C    1 
ATOM   2689 O  O    . HIS   B 1 41  ? 13.946  15.645  4.331   1   12.659 ? 41  HIS   B O    1 
ATOM   2690 C  CB   . HIS   B 1 41  ? 14.208  12.613  3.944   1   11.63  ? 41  HIS   B CB   1 
ATOM   2691 C  CG   . HIS   B 1 41  ? 13.486  12.458  2.645   1   12.016 ? 41  HIS   B CG   1 
ATOM   2692 N  ND1  . HIS   B 1 41  ? 13.116  13.497  1.817   1   12.871 ? 41  HIS   B ND1  1 
ATOM   2693 C  CD2  . HIS   B 1 41  ? 13.151  11.339  2.01    1   12.521 ? 41  HIS   B CD2  1 
ATOM   2694 C  CE1  . HIS   B 1 41  ? 12.566  12.998  0.715   1   12.679 ? 41  HIS   B CE1  1 
ATOM   2695 N  NE2  . HIS   B 1 41  ? 12.561  11.688  0.819   1   12.82  ? 41  HIS   B NE2  1 
ATOM   2696 N  N    . VAL   B 1 42  ? 11.793  15.137  4.731   1   11.202 ? 42  VAL   B N    1 
ATOM   2697 C  CA   . VAL   B 1 42  ? 11.331  16.487  4.466   1   12.068 ? 42  VAL   B CA   1 
ATOM   2698 C  C    . VAL   B 1 42  ? 12.049  17.52   5.343   1   13.181 ? 42  VAL   B C    1 
ATOM   2699 O  O    . VAL   B 1 42  ? 12.169  18.681  4.931   1   14.524 ? 42  VAL   B O    1 
ATOM   2700 C  CB   . VAL   B 1 42  ? 9.799   16.597  4.619   1   12.613 ? 42  VAL   B CB   1 
ATOM   2701 C  CG1  . VAL   B 1 42  ? 9.347   16.5    6.07    1   13.094 ? 42  VAL   B CG1  1 
ATOM   2702 C  CG2  . VAL   B 1 42  ? 9.28    17.877  3.99    1   12.738 ? 42  VAL   B CG2  1 
ATOM   2703 N  N    . ILE   B 1 43  ? 12.527  17.128  6.535   1   13.775 ? 43  ILE   B N    1 
ATOM   2704 C  CA   . ILE   B 1 43  ? 13.14   18.088  7.453   1   14.538 ? 43  ILE   B CA   1 
ATOM   2705 C  C    . ILE   B 1 43  ? 14.625  18.333  7.15    1   15.627 ? 43  ILE   B C    1 
ATOM   2706 O  O    . ILE   B 1 43  ? 15.226  19.214  7.77    1   16.767 ? 43  ILE   B O    1 
ATOM   2707 C  CB   . ILE   B 1 43  ? 12.93   17.689  8.926   1   15.879 ? 43  ILE   B CB   1 
ATOM   2708 C  CG1  . ILE   B 1 43  ? 13.697  16.422  9.318   1   16.674 ? 43  ILE   B CG1  1 
ATOM   2709 C  CG2  . ILE   B 1 43  ? 11.439  17.578  9.252   1   16.193 ? 43  ILE   B CG2  1 
ATOM   2710 C  CD1  . ILE   B 1 43  ? 13.59   16.055  10.787  1   17.887 ? 43  ILE   B CD1  1 
ATOM   2711 N  N    . CYS   B 1 44  ? 15.212  17.626  6.178   1   15.51  ? 44  CYS   B N    1 
ATOM   2712 C  CA   . CYS   B 1 44  ? 16.655  17.692  5.969   1   16.251 ? 44  CYS   B CA   1 
ATOM   2713 C  C    . CYS   B 1 44  ? 17.082  18.749  4.95    1   16.948 ? 44  CYS   B C    1 
ATOM   2714 O  O    . CYS   B 1 44  ? 16.509  18.82   3.867   1   18.167 ? 44  CYS   B O    1 
ATOM   2715 C  CB   . CYS   B 1 44  ? 17.161  16.364  5.429   1   16.811 ? 44  CYS   B CB   1 
ATOM   2716 S  SG   . CYS   B 1 44  ? 17.028  15.031  6.646   1   18.502 ? 44  CYS   B SG   1 
ATOM   2717 N  N    . THR   B 1 45  ? 18.136  19.516  5.266   1   17.568 ? 45  THR   B N    1 
ATOM   2718 C  CA   . THR   B 1 45  ? 18.881  20.249  4.249   1   18.273 ? 45  THR   B CA   1 
ATOM   2719 C  C    . THR   B 1 45  ? 19.696  19.249  3.434   1   17.701 ? 45  THR   B C    1 
ATOM   2720 O  O    . THR   B 1 45  ? 19.84   18.102  3.837   1   16.893 ? 45  THR   B O    1 
ATOM   2721 C  CB   . THR   B 1 45  ? 19.79   21.31   4.868   1   19.145 ? 45  THR   B CB   1 
ATOM   2722 O  OG1  . THR   B 1 45  ? 20.846  20.613  5.52    1   20.049 ? 45  THR   B OG1  1 
ATOM   2723 C  CG2  . THR   B 1 45  ? 19.061  22.212  5.847   1   19.743 ? 45  THR   B CG2  1 
ATOM   2724 N  N    . SER   B 1 46  ? 20.27   19.698  2.31    1   18.836 ? 46  SER   B N    1 
ATOM   2725 C  CA   . SER   B 1 46  ? 21.142  18.85   1.51    1   19.811 ? 46  SER   B CA   1 
ATOM   2726 C  C    . SER   B 1 46  ? 22.295  18.312  2.356   1   19.258 ? 46  SER   B C    1 
ATOM   2727 O  O    . SER   B 1 46  ? 22.672  17.151  2.227   1   19.476 ? 46  SER   B O    1 
ATOM   2728 C  CB   . SER   B 1 46  ? 21.666  19.579  0.309   1   21.681 ? 46  SER   B CB   1 
ATOM   2729 O  OG   . SER   B 1 46  ? 20.608  19.871  -0.586  1   25.433 ? 46  SER   B OG   1 
ATOM   2730 N  N    . GLU   B 1 47  ? 22.838  19.154  3.24    1   19.905 ? 47  GLU   B N    1 
ATOM   2731 C  CA   . GLU   B 1 47  ? 23.956  18.74   4.075   1   20.431 ? 47  GLU   B CA   1 
ATOM   2732 C  C    . GLU   B 1 47  ? 23.498  17.719  5.119   1   19.395 ? 47  GLU   B C    1 
ATOM   2733 O  O    . GLU   B 1 47  ? 24.182  16.718  5.347   1   20.203 ? 47  GLU   B O    1 
ATOM   2734 C  CB   . GLU   B 1 47  ? 24.643  19.937  4.731   1   22.863 ? 47  GLU   B CB   1 
ATOM   2735 C  CG   . GLU   B 1 47  ? 25.961  19.566  5.406   1   25.431 ? 47  GLU   B CG   1 
ATOM   2736 C  CD   . GLU   B 1 47  ? 27.165  19.247  4.523   1   29.373 ? 47  GLU   B CD   1 
ATOM   2737 O  OE1  . GLU   B 1 47  ? 28.194  18.857  5.128   1   35.042 ? 47  GLU   B OE1  1 
ATOM   2738 O  OE2  . GLU   B 1 47  ? 27.128  19.389  3.273   1   31.001 ? 47  GLU   B OE2  1 
ATOM   2739 N  N    . ASP   B 1 48  ? 22.338  17.975  5.743   1   18.389 ? 48  ASP   B N    1 
ATOM   2740 C  CA   . ASP   B 1 48  ? 21.787  17.056  6.726   1   18.042 ? 48  ASP   B CA   1 
ATOM   2741 C  C    . ASP   B 1 48  ? 21.583  15.67   6.118   1   17.283 ? 48  ASP   B C    1 
ATOM   2742 O  O    . ASP   B 1 48  ? 21.775  14.655  6.78    1   16.894 ? 48  ASP   B O    1 
ATOM   2743 C  CB   . ASP   B 1 48  ? 20.428  17.504  7.229   1   19.108 ? 48  ASP   B CB   1 
ATOM   2744 C  CG   . ASP   B 1 48  ? 20.34   18.768  8.067   1   20.389 ? 48  ASP   B CG   1 
ATOM   2745 O  OD1  . ASP   B 1 48  ? 21.347  19.122  8.741   1   21.676 ? 48  ASP   B OD1  1 
ATOM   2746 O  OD2  . ASP   B 1 48  ? 19.245  19.388  8.013   1   21.602 ? 48  ASP   B OD2  1 
ATOM   2747 N  N    . MET   B 1 49  ? 21.154  15.642  4.851   1   16.583 ? 49  MET   B N    1 
ATOM   2748 C  CA   . MET   B 1 49  ? 20.761  14.412  4.18    1   16.11  ? 49  MET   B CA   1 
ATOM   2749 C  C    . MET   B 1 49  ? 21.918  13.413  4.096   1   16.642 ? 49  MET   B C    1 
ATOM   2750 O  O    . MET   B 1 49  ? 21.683  12.208  3.987   1   16.46  ? 49  MET   B O    1 
ATOM   2751 C  CB   . MET   B 1 49  ? 20.252  14.753  2.774   1   15.76  ? 49  MET   B CB   1 
ATOM   2752 C  CG   . MET   B 1 49  ? 19.372  13.709  2.116   1   15.692 ? 49  MET   B CG   1 
ATOM   2753 S  SD   . MET   B 1 49  ? 17.766  13.496  2.905   1   16.329 ? 49  MET   B SD   1 
ATOM   2754 C  CE   . MET   B 1 49  ? 18.145  12.013  3.845   1   16.298 ? 49  MET   B CE   1 
ATOM   2755 N  N    . LEU   B 1 50  ? 23.163  13.92   4.123   1   17.88  ? 50  LEU   B N    1 
ATOM   2756 C  CA   . LEU   B 1 50  ? 24.343  13.076  4.054   1   18.738 ? 50  LEU   B CA   1 
ATOM   2757 C  C    . LEU   B 1 50  ? 24.514  12.221  5.311   1   18.07  ? 50  LEU   B C    1 
ATOM   2758 O  O    . LEU   B 1 50  ? 25.145  11.172  5.24    1   18.561 ? 50  LEU   B O    1 
ATOM   2759 C  CB   . LEU   B 1 50  ? 25.577  13.95   3.841   1   19.967 ? 50  LEU   B CB   1 
ATOM   2760 C  CG   . LEU   B 1 50  ? 25.615  14.81   2.573   1   21.434 ? 50  LEU   B CG   1 
ATOM   2761 C  CD1  . LEU   B 1 50  ? 26.812  15.754  2.625   1   22.204 ? 50  LEU   B CD1  1 
ATOM   2762 C  CD2  . LEU   B 1 50  ? 25.658  13.961  1.316   1   22.731 ? 50  LEU   B CD2  1 
ATOM   2763 N  N    . ASN   B 1 51  ? 23.97   12.66   6.455   1   17.709 ? 51  ASN   B N    1 
ATOM   2764 C  CA   . ASN   B 1 51  ? 24.126  11.918  7.699   1   18.484 ? 51  ASN   B CA   1 
ATOM   2765 C  C    . ASN   B 1 51  ? 23.158  12.478  8.738   1   17.496 ? 51  ASN   B C    1 
ATOM   2766 O  O    . ASN   B 1 51  ? 23.556  13.172  9.665   1   19.443 ? 51  ASN   B O    1 
ATOM   2767 C  CB   . ASN   B 1 51  ? 25.567  11.969  8.195   1   20.105 ? 51  ASN   B CB   1 
ATOM   2768 C  CG   . ASN   B 1 51  ? 25.806  11.067  9.381   1   23.056 ? 51  ASN   B CG   1 
ATOM   2769 O  OD1  . ASN   B 1 51  ? 25.06   10.107  9.612   1   25.88  ? 51  ASN   B OD1  1 
ATOM   2770 N  ND2  . ASN   B 1 51  ? 26.863  11.343  10.124  1   25.668 ? 51  ASN   B ND2  1 
ATOM   2771 N  N    . PRO   B 1 52  ? 21.845  12.238  8.57    1   16.204 ? 52  PRO   B N    1 
ATOM   2772 C  CA   . PRO   B 1 52  ? 20.842  12.904  9.397   1   16.22  ? 52  PRO   B CA   1 
ATOM   2773 C  C    . PRO   B 1 52  ? 20.691  12.289  10.783  1   16.662 ? 52  PRO   B C    1 
ATOM   2774 O  O    . PRO   B 1 52  ? 20.711  11.077  10.931  1   17.627 ? 52  PRO   B O    1 
ATOM   2775 C  CB   . PRO   B 1 52  ? 19.597  12.73   8.518   1   16.282 ? 52  PRO   B CB   1 
ATOM   2776 C  CG   . PRO   B 1 52  ? 19.811  11.377  7.897   1   16.208 ? 52  PRO   B CG   1 
ATOM   2777 C  CD   . PRO   B 1 52  ? 21.272  11.411  7.5     1   16.89  ? 52  PRO   B CD   1 
ATOM   2778 N  N    . ASN   B 1 53  ? 20.534  13.158  11.776  1   16.773 ? 53  ASN   B N    1 
ATOM   2779 C  CA   . ASN   B 1 53  ? 20.045  12.777  13.092  1   17.36  ? 53  ASN   B CA   1 
ATOM   2780 C  C    . ASN   B 1 53  ? 18.623  13.323  13.196  1   15.963 ? 53  ASN   B C    1 
ATOM   2781 O  O    . ASN   B 1 53  ? 18.426  14.493  13.527  1   16.786 ? 53  ASN   B O    1 
ATOM   2782 C  CB   . ASN   B 1 53  ? 20.934  13.311  14.209  1   19.2   ? 53  ASN   B CB   1 
ATOM   2783 C  CG   . ASN   B 1 53  ? 20.536  12.794  15.573  1   20.805 ? 53  ASN   B CG   1 
ATOM   2784 O  OD1  . ASN   B 1 53  ? 19.345  12.695  15.895  1   21.892 ? 53  ASN   B OD1  1 
ATOM   2785 N  ND2  . ASN   B 1 53  ? 21.523  12.477  16.399  1   23.143 ? 53  ASN   B ND2  1 
ATOM   2786 N  N    . TYR   B 1 54  ? 17.638  12.493  12.836  1   15.598 ? 54  TYR   B N    1 
ATOM   2787 C  CA   . TYR   B 1 54  ? 16.286  12.997  12.631  1   15.651 ? 54  TYR   B CA   1 
ATOM   2788 C  C    . TYR   B 1 54  ? 15.679  13.567  13.915  1   16.413 ? 54  TYR   B C    1 
ATOM   2789 O  O    . TYR   B 1 54  ? 15.012  14.602  13.888  1   16.493 ? 54  TYR   B O    1 
ATOM   2790 C  CB   . TYR   B 1 54  ? 15.404  11.905  12.026  1   15.041 ? 54  TYR   B CB   1 
ATOM   2791 C  CG   . TYR   B 1 54  ? 15.696  11.654  10.556  1   14.854 ? 54  TYR   B CG   1 
ATOM   2792 C  CD1  . TYR   B 1 54  ? 15.205  12.542  9.616   1   14.588 ? 54  TYR   B CD1  1 
ATOM   2793 C  CD2  . TYR   B 1 54  ? 16.432  10.558  10.111  1   14.531 ? 54  TYR   B CD2  1 
ATOM   2794 C  CE1  . TYR   B 1 54  ? 15.432  12.345  8.271   1   14.623 ? 54  TYR   B CE1  1 
ATOM   2795 C  CE2  . TYR   B 1 54  ? 16.659  10.349  8.754   1   15.029 ? 54  TYR   B CE2  1 
ATOM   2796 C  CZ   . TYR   B 1 54  ? 16.153  11.25   7.839   1   14.718 ? 54  TYR   B CZ   1 
ATOM   2797 O  OH   . TYR   B 1 54  ? 16.329  11.12   6.498   1   14.452 ? 54  TYR   B OH   1 
ATOM   2798 N  N    . GLU   B 1 55  ? 15.927  12.909  15.049  1   18.005 ? 55  GLU   B N    1 
ATOM   2799 C  CA   . GLU   B 1 55  ? 15.4    13.395  16.314  1   19.24  ? 55  GLU   B CA   1 
ATOM   2800 C  C    . GLU   B 1 55  ? 15.902  14.812  16.581  1   19.859 ? 55  GLU   B C    1 
ATOM   2801 O  O    . GLU   B 1 55  ? 15.124  15.693  16.963  1   20.374 ? 55  GLU   B O    1 
ATOM   2802 C  CB   . GLU   B 1 55  ? 15.814  12.458  17.446  1   21.924 ? 55  GLU   B CB   1 
ATOM   2803 C  CG   . GLU   B 1 55  ? 15.287  12.895  18.814  1   23.864 ? 55  GLU   B CG   1 
ATOM   2804 C  CD   . GLU   B 1 55  ? 15.494  11.921  19.966  1   28.294 ? 55  GLU   B CD   1 
ATOM   2805 O  OE1  . GLU   B 1 55  ? 16.611  11.377  20.076  1   32.22  ? 55  GLU   B OE1  1 
ATOM   2806 O  OE2  . GLU   B 1 55  ? 14.559  11.738  20.788  1   33.668 ? 55  GLU   B OE2  1 
ATOM   2807 N  N    . ASP   B 1 56  ? 17.211  15.018  16.373  1   20.728 ? 56  ASP   B N    1 
ATOM   2808 C  CA   . ASP   B 1 56  ? 17.84   16.294  16.658  1   21.04  ? 56  ASP   B CA   1 
ATOM   2809 C  C    . ASP   B 1 56  ? 17.372  17.369  15.682  1   20.93  ? 56  ASP   B C    1 
ATOM   2810 O  O    . ASP   B 1 56  ? 17.177  18.518  16.074  1   22.735 ? 56  ASP   B O    1 
ATOM   2811 C  CB   . ASP   B 1 56  ? 19.354  16.172  16.628  1   24.429 ? 56  ASP   B CB   1 
ATOM   2812 C  CG   . ASP   B 1 56  ? 20.11   17.396  17.126  1   29.08  ? 56  ASP   B CG   1 
ATOM   2813 O  OD1  . ASP   B 1 56  ? 20.074  17.661  18.346  1   33.968 ? 56  ASP   B OD1  1 
ATOM   2814 O  OD2  . ASP   B 1 56  ? 20.701  18.091  16.277  1   33.176 ? 56  ASP   B OD2  1 
ATOM   2815 N  N    . LEU   B 1 57  ? 17.185  16.996  14.412  1   19.494 ? 57  LEU   B N    1 
ATOM   2816 C  CA   . LEU   B 1 57  ? 16.727  17.954  13.42   1   20.023 ? 57  LEU   B CA   1 
ATOM   2817 C  C    . LEU   B 1 57  ? 15.301  18.395  13.733  1   19.696 ? 57  LEU   B C    1 
ATOM   2818 O  O    . LEU   B 1 57  ? 14.95   19.571  13.558  1   22.217 ? 57  LEU   B O    1 
ATOM   2819 C  CB   . LEU   B 1 57  ? 16.825  17.336  12.028  1   19.912 ? 57  LEU   B CB   1 
ATOM   2820 C  CG   . LEU   B 1 57  ? 18.251  17.122  11.506  1   20.781 ? 57  LEU   B CG   1 
ATOM   2821 C  CD1  . LEU   B 1 57  ? 18.249  16.335  10.216  1   20.817 ? 57  LEU   B CD1  1 
ATOM   2822 C  CD2  . LEU   B 1 57  ? 18.991  18.443  11.334  1   21.361 ? 57  LEU   B CD2  1 
ATOM   2823 N  N    . LEU   B 1 58  ? 14.489  17.445  14.206  1   19.085 ? 58  LEU   B N    1 
ATOM   2824 C  CA   . LEU   B 1 58  ? 13.073  17.697  14.42   1   20.08  ? 58  LEU   B CA   1 
ATOM   2825 C  C    . LEU   B 1 58  ? 12.84   18.576  15.65   1   21.386 ? 58  LEU   B C    1 
ATOM   2826 O  O    . LEU   B 1 58  ? 11.893  19.348  15.655  1   20.688 ? 58  LEU   B O    1 
ATOM   2827 C  CB   . LEU   B 1 58  ? 12.302  16.382  14.516  1   20.051 ? 58  LEU   B CB   1 
ATOM   2828 C  CG   . LEU   B 1 58  ? 10.775  16.513  14.51   1   20.002 ? 58  LEU   B CG   1 
ATOM   2829 C  CD1  . LEU   B 1 58  ? 10.255  17.12   13.216  1   20.017 ? 58  LEU   B CD1  1 
ATOM   2830 C  CD2  . LEU   B 1 58  ? 10.125  15.156  14.737  1   20.208 ? 58  LEU   B CD2  1 
ATOM   2831 N  N    . ILE   B 1 59  ? 13.705  18.491  16.672  1   22.837 ? 59  ILE   B N    1 
ATOM   2832 C  CA   . ILE   B 1 59  ? 13.548  19.257  17.906  1   24.881 ? 59  ILE   B CA   1 
ATOM   2833 C  C    . ILE   B 1 59  ? 13.554  20.763  17.609  1   24.494 ? 59  ILE   B C    1 
ATOM   2834 O  O    . ILE   B 1 59  ? 12.927  21.54   18.341  1   26.52  ? 59  ILE   B O    1 
ATOM   2835 C  CB   . ILE   B 1 59  ? 14.633  18.872  18.94   1   28.617 ? 59  ILE   B CB   1 
ATOM   2836 C  CG1  . ILE   B 1 59  ? 14.522  17.411  19.386  1   33.101 ? 59  ILE   B CG1  1 
ATOM   2837 C  CG2  . ILE   B 1 59  ? 14.633  19.813  20.149  1   30.357 ? 59  ILE   B CG2  1 
ATOM   2838 C  CD1  . ILE   B 1 59  ? 13.426  17.131  20.402  1   35.301 ? 59  ILE   B CD1  1 
ATOM   2839 N  N    . ARG   B 1 60  ? 14.236  21.164  16.525  1   23.789 ? 60  ARG   B N    1 
ATOM   2840 C  CA   . ARG   B 1 60  ? 14.37   22.57   16.156  1   24.461 ? 60  ARG   B CA   1 
ATOM   2841 C  C    . ARG   B 1 60  ? 13.153  23.104  15.399  1   24.717 ? 60  ARG   B C    1 
ATOM   2842 O  O    . ARG   B 1 60  ? 13.052  24.314  15.179  1   28.211 ? 60  ARG   B O    1 
ATOM   2843 C  CB   . ARG   B 1 60  ? 15.616  22.815  15.295  1   25.803 ? 60  ARG   B CB   1 
ATOM   2844 N  N    . LYS   B 1 61  ? 12.228  22.207  15.023  1   22.649 ? 61  LYS   B N    1 
ATOM   2845 C  CA   . LYS   B 1 61  ? 11.045  22.575  14.258  1   23.075 ? 61  LYS   B CA   1 
ATOM   2846 C  C    . LYS   B 1 61  ? 9.835   22.756  15.174  1   23.479 ? 61  LYS   B C    1 
ATOM   2847 O  O    . LYS   B 1 61  ? 9.659   22.013  16.134  1   25.304 ? 61  LYS   B O    1 
ATOM   2848 C  CB   . LYS   B 1 61  ? 10.701  21.469  13.257  1   23.384 ? 61  LYS   B CB   1 
ATOM   2849 C  CG   . LYS   B 1 61  ? 11.8    21.111  12.262  1   25.395 ? 61  LYS   B CG   1 
ATOM   2850 C  CD   . LYS   B 1 61  ? 12.149  22.278  11.352  1   26.486 ? 61  LYS   B CD   1 
ATOM   2851 C  CE   . LYS   B 1 61  ? 13.196  21.946  10.334  1   28.033 ? 61  LYS   B CE   1 
ATOM   2852 N  NZ   . LYS   B 1 61  ? 13.798  23.172  9.799   1   29.054 ? 61  LYS   B NZ   1 
ATOM   2853 N  N    . SER   B 1 62  ? 9.029   23.78   14.871  1   22.878 ? 62  SER   B N    1 
ATOM   2854 C  CA   . SER   B 1 62  ? 7.734   23.977  15.498  1   23.351 ? 62  SER   B CA   1 
ATOM   2855 C  C    . SER   B 1 62  ? 6.656   23.477  14.544  1   20.883 ? 62  SER   B C    1 
ATOM   2856 O  O    . SER   B 1 62  ? 6.923   23.212  13.377  1   20.601 ? 62  SER   B O    1 
ATOM   2857 C  CB   . SER   B 1 62  ? 7.516   25.427  15.844  1   24.468 ? 62  SER   B CB   1 
ATOM   2858 O  OG   . SER   B 1 62  ? 7.443   26.222  14.669  1   28.072 ? 62  SER   B OG   1 
ATOM   2859 N  N    . ASN   B 1 63  ? 5.418   23.394  15.031  1   20.29  ? 63  ASN   B N    1 
ATOM   2860 C  CA   . ASN   B 1 63  ? 4.294   23.026  14.186  1   18.671 ? 63  ASN   B CA   1 
ATOM   2861 C  C    . ASN   B 1 63  ? 4.195   23.965  12.985  1   18.455 ? 63  ASN   B C    1 
ATOM   2862 O  O    . ASN   B 1 63  ? 3.872   23.505  11.893  1   18.658 ? 63  ASN   B O    1 
ATOM   2863 C  CB   . ASN   B 1 63  ? 2.984   23.018  14.961  1   18.713 ? 63  ASN   B CB   1 
ATOM   2864 C  CG   . ASN   B 1 63  ? 2.878   21.882  15.955  1   19.424 ? 63  ASN   B CG   1 
ATOM   2865 O  OD1  . ASN   B 1 63  ? 3.373   20.777  15.724  1   19.759 ? 63  ASN   B OD1  1 
ATOM   2866 N  ND2  . ASN   B 1 63  ? 2.205   22.128  17.064  1   20.899 ? 63  ASN   B ND2  1 
ATOM   2867 N  N    . HIS   B 1 64  ? 4.464   25.261  13.198  1   19.087 ? 64  HIS   B N    1 
ATOM   2868 C  CA   . HIS   B 1 64  ? 4.34    26.286  12.169  1   20.945 ? 64  HIS   B CA   1 
ATOM   2869 C  C    . HIS   B 1 64  ? 5.456   26.242  11.125  1   19.856 ? 64  HIS   B C    1 
ATOM   2870 O  O    . HIS   B 1 64  ? 5.393   26.958  10.126  1   20.221 ? 64  HIS   B O    1 
ATOM   2871 C  CB   . HIS   B 1 64  ? 4.286   27.683  12.805  1   23.176 ? 64  HIS   B CB   1 
ATOM   2872 C  CG   . HIS   B 1 64  ? 2.942   28.067  13.328  1   26.565 ? 64  HIS   B CG   1 
ATOM   2873 N  ND1  . HIS   B 1 64  ? 1.919   28.531  12.526  1   30.464 ? 64  HIS   B ND1  1 
ATOM   2874 C  CD2  . HIS   B 1 64  ? 2.463   28.068  14.569  1   29.259 ? 64  HIS   B CD2  1 
ATOM   2875 C  CE1  . HIS   B 1 64  ? 0.861   28.785  13.278  1   30.495 ? 64  HIS   B CE1  1 
ATOM   2876 N  NE2  . HIS   B 1 64  ? 1.167   28.514  14.524  1   31.744 ? 64  HIS   B NE2  1 
ATOM   2877 N  N    . ASN   B 1 65  ? 6.449   25.371  11.314  1   18.743 ? 65  ASN   B N    1 
ATOM   2878 C  CA   . ASN   B 1 65  ? 7.451   25.141  10.289  1   19.33  ? 65  ASN   B CA   1 
ATOM   2879 C  C    . ASN   B 1 65  ? 6.944   24.196  9.205   1   18.831 ? 65  ASN   B C    1 
ATOM   2880 O  O    . ASN   B 1 65  ? 7.628   24.018  8.199   1   20.771 ? 65  ASN   B O    1 
ATOM   2881 C  CB   . ASN   B 1 65  ? 8.746   24.593  10.877  1   19.877 ? 65  ASN   B CB   1 
ATOM   2882 C  CG   . ASN   B 1 65  ? 9.49    25.633  11.68   1   21.846 ? 65  ASN   B CG   1 
ATOM   2883 O  OD1  . ASN   B 1 65  ? 9.975   25.342  12.772  1   25.256 ? 65  ASN   B OD1  1 
ATOM   2884 N  ND2  . ASN   B 1 65  ? 9.601   26.848  11.165  1   23.52  ? 65  ASN   B ND2  1 
ATOM   2885 N  N    . PHE   B 1 66  ? 5.783   23.568  9.43    1   17.12  ? 66  PHE   B N    1 
ATOM   2886 C  CA   . PHE   B 1 66  ? 5.191   22.658  8.467   1   17.583 ? 66  PHE   B CA   1 
ATOM   2887 C  C    . PHE   B 1 66  ? 3.969   23.334  7.873   1   18.561 ? 66  PHE   B C    1 
ATOM   2888 O  O    . PHE   B 1 66  ? 2.981   23.542  8.564   1   21.296 ? 66  PHE   B O    1 
ATOM   2889 C  CB   . PHE   B 1 66  ? 4.814   21.334  9.133   1   17.254 ? 66  PHE   B CB   1 
ATOM   2890 C  CG   . PHE   B 1 66  ? 6.027   20.626  9.706   1   17.504 ? 66  PHE   B CG   1 
ATOM   2891 C  CD1  . PHE   B 1 66  ? 6.876   19.896  8.88    1   17.029 ? 66  PHE   B CD1  1 
ATOM   2892 C  CD2  . PHE   B 1 66  ? 6.333   20.728  11.058  1   17.338 ? 66  PHE   B CD2  1 
ATOM   2893 C  CE1  . PHE   B 1 66  ? 7.988   19.267  9.401   1   17.691 ? 66  PHE   B CE1  1 
ATOM   2894 C  CE2  . PHE   B 1 66  ? 7.451   20.094  11.572  1   17.79  ? 66  PHE   B CE2  1 
ATOM   2895 C  CZ   . PHE   B 1 66  ? 8.274   19.376  10.743  1   17.9   ? 66  PHE   B CZ   1 
ATOM   2896 N  N    . LEU   B 1 67  ? 4.049   23.675  6.59    1   17.868 ? 67  LEU   B N    1 
ATOM   2897 C  CA   . LEU   B 1 67  ? 2.956   24.319  5.89    1   18.936 ? 67  LEU   B CA   1 
ATOM   2898 C  C    . LEU   B 1 67  ? 2.292   23.26   5.025   1   17.787 ? 67  LEU   B C    1 
ATOM   2899 O  O    . LEU   B 1 67  ? 2.943   22.637  4.196   1   19.692 ? 67  LEU   B O    1 
ATOM   2900 C  CB   . LEU   B 1 67  ? 3.488   25.488  5.07    1   21.421 ? 67  LEU   B CB   1 
ATOM   2901 C  CG   . LEU   B 1 67  ? 4.289   26.534  5.853   1   24.985 ? 67  LEU   B CG   1 
ATOM   2902 C  CD1  . LEU   B 1 67  ? 4.823   27.603  4.922   1   25.962 ? 67  LEU   B CD1  1 
ATOM   2903 C  CD2  . LEU   B 1 67  ? 3.438   27.13   6.971   1   26.8   ? 67  LEU   B CD2  1 
ATOM   2904 N  N    . VAL   B 1 68  ? 1.008   23.03   5.281   1   16.844 ? 68  VAL   B N    1 
ATOM   2905 C  CA   . VAL   B 1 68  ? 0.267   21.972  4.624   1   16.077 ? 68  VAL   B CA   1 
ATOM   2906 C  C    . VAL   B 1 68  ? -0.911  22.603  3.902   1   16.701 ? 68  VAL   B C    1 
ATOM   2907 O  O    . VAL   B 1 68  ? -1.671  23.356  4.502   1   17.122 ? 68  VAL   B O    1 
ATOM   2908 C  CB   . VAL   B 1 68  ? -0.213  20.913  5.628   1   16.475 ? 68  VAL   B CB   1 
ATOM   2909 C  CG1  . VAL   B 1 68  ? -0.998  19.815  4.92    1   16.731 ? 68  VAL   B CG1  1 
ATOM   2910 C  CG2  . VAL   B 1 68  ? 0.96    20.329  6.401   1   16.716 ? 68  VAL   B CG2  1 
ATOM   2911 N  N    . GLN   B 1 69  ? -1.038  22.284  2.612   1   17.473 ? 69  GLN   B N    1 
ATOM   2912 C  CA   . GLN   B 1 69  ? -2.11   22.811  1.793   1   19.028 ? 69  GLN   B CA   1 
ATOM   2913 C  C    . GLN   B 1 69  ? -2.827  21.648  1.125   1   17.156 ? 69  GLN   B C    1 
ATOM   2914 O  O    . GLN   B 1 69  ? -2.186  20.81   0.508   1   16.677 ? 69  GLN   B O    1 
ATOM   2915 C  CB   . GLN   B 1 69  ? -1.552  23.759  0.732   1   22.579 ? 69  GLN   B CB   1 
ATOM   2916 C  CG   . GLN   B 1 69  ? -0.899  25.022  1.276   1   27.643 ? 69  GLN   B CG   1 
ATOM   2917 C  CD   . GLN   B 1 69  ? -0.441  25.941  0.163   1   32.079 ? 69  GLN   B CD   1 
ATOM   2918 O  OE1  . GLN   B 1 69  ? -1.098  26.048  -0.877  1   37.992 ? 69  GLN   B OE1  1 
ATOM   2919 N  NE2  . GLN   B 1 69  ? 0.709   26.576  0.342   1   36.123 ? 69  GLN   B NE2  1 
ATOM   2920 N  N    . ALA   B 1 70  ? -4.155  21.612  1.25    1   17.608 ? 70  ALA   B N    1 
ATOM   2921 C  CA   . ALA   B 1 70  ? -4.998  20.676  0.528   1   18.78  ? 70  ALA   B CA   1 
ATOM   2922 C  C    . ALA   B 1 70  ? -5.709  21.454  -0.571  1   20.122 ? 70  ALA   B C    1 
ATOM   2923 O  O    . ALA   B 1 70  ? -6.617  22.23   -0.3    1   21.216 ? 70  ALA   B O    1 
ATOM   2924 C  CB   . ALA   B 1 70  ? -5.979  20.025  1.467   1   20.113 ? 70  ALA   B CB   1 
ATOM   2925 N  N    . GLY   B 1 71  ? -5.235  21.29   -1.808  1   20.883 ? 71  GLY   B N    1 
ATOM   2926 C  CA   . GLY   B 1 71  ? -5.598  22.215  -2.865  1   23.347 ? 71  GLY   B CA   1 
ATOM   2927 C  C    . GLY   B 1 71  ? -5.24   23.642  -2.449  1   24.742 ? 71  GLY   B C    1 
ATOM   2928 O  O    . GLY   B 1 71  ? -4.082  23.935  -2.158  1   27.093 ? 71  GLY   B O    1 
ATOM   2929 N  N    . ASN   B 1 72  ? -6.253  24.51   -2.381  1   26.344 ? 72  ASN   B N    1 
ATOM   2930 C  CA   . ASN   B 1 72  ? -6.055  25.919  -2.073  1   29.31  ? 72  ASN   B CA   1 
ATOM   2931 C  C    . ASN   B 1 72  ? -6.352  26.223  -0.602  1   29.413 ? 72  ASN   B C    1 
ATOM   2932 O  O    . ASN   B 1 72  ? -6.365  27.394  -0.225  1   31.945 ? 72  ASN   B O    1 
ATOM   2933 C  CB   . ASN   B 1 72  ? -6.908  26.818  -2.966  1   31.306 ? 72  ASN   B CB   1 
ATOM   2934 C  CG   . ASN   B 1 72  ? -6.508  26.758  -4.422  1   34.146 ? 72  ASN   B CG   1 
ATOM   2935 O  OD1  . ASN   B 1 72  ? -7.377  26.664  -5.296  1   38     ? 72  ASN   B OD1  1 
ATOM   2936 N  ND2  . ASN   B 1 72  ? -5.217  26.849  -4.708  1   35.697 ? 72  ASN   B ND2  1 
ATOM   2937 N  N    . VAL   B 1 73  ? -6.549  25.187  0.23    1   30.414 ? 73  VAL   B N    1 
ATOM   2938 C  CA   . VAL   B 1 73  ? -6.949  25.354  1.621   1   27.895 ? 73  VAL   B CA   1 
ATOM   2939 C  C    . VAL   B 1 73  ? -5.771  25.014  2.535   1   24.463 ? 73  VAL   B C    1 
ATOM   2940 O  O    . VAL   B 1 73  ? -5.241  23.912  2.468   1   22.548 ? 73  VAL   B O    1 
ATOM   2941 C  CB   . VAL   B 1 73  ? -8.16   24.467  1.976   1   28.843 ? 73  VAL   B CB   1 
ATOM   2942 C  CG1  . VAL   B 1 73  ? -8.518  24.561  3.459   1   29.708 ? 73  VAL   B CG1  1 
ATOM   2943 C  CG2  . VAL   B 1 73  ? -9.38   24.788  1.118   1   30.388 ? 73  VAL   B CG2  1 
ATOM   2944 N  N    . GLN   B 1 74  ? -5.392  25.952  3.411   1   24.533 ? 74  GLN   B N    1 
ATOM   2945 C  CA   . GLN   B 1 74  ? -4.315  25.727  4.364   1   23.383 ? 74  GLN   B CA   1 
ATOM   2946 C  C    . GLN   B 1 74  ? -4.828  24.896  5.54    1   23.04  ? 74  GLN   B C    1 
ATOM   2947 O  O    . GLN   B 1 74  ? -5.901  25.18   6.077   1   25.629 ? 74  GLN   B O    1 
ATOM   2948 C  CB   . GLN   B 1 74  ? -3.776  27.061  4.883   1   27.122 ? 74  GLN   B CB   1 
ATOM   2949 N  N    . LEU   B 1 75  ? -4.072  23.854  5.906   1   20.156 ? 75  LEU   B N    1 
ATOM   2950 C  CA   . LEU   B 1 75  ? -4.382  23.043  7.075   1   20.857 ? 75  LEU   B CA   1 
ATOM   2951 C  C    . LEU   B 1 75  ? -3.471  23.475  8.208   1   22.711 ? 75  LEU   B C    1 
ATOM   2952 O  O    . LEU   B 1 75  ? -2.286  23.693  7.991   1   28.101 ? 75  LEU   B O    1 
ATOM   2953 C  CB   . LEU   B 1 75  ? -4.176  21.549  6.836   1   21.851 ? 75  LEU   B CB   1 
ATOM   2954 C  CG   . LEU   B 1 75  ? -4.988  20.924  5.706   1   22.83  ? 75  LEU   B CG   1 
ATOM   2955 C  CD1  . LEU   B 1 75  ? -4.764  19.415  5.787   1   23.217 ? 75  LEU   B CD1  1 
ATOM   2956 C  CD2  . LEU   B 1 75  ? -6.453  21.298  5.776   1   23.93  ? 75  LEU   B CD2  1 
ATOM   2957 N  N    . ARG   B 1 76  ? -3.996  23.486  9.43    1   20.922 ? 76  ARG   B N    1 
ATOM   2958 C  CA   . ARG   B 1 76  ? -3.194  23.906  10.569  1   22.315 ? 76  ARG   B CA   1 
ATOM   2959 C  C    . ARG   B 1 76  ? -2.604  22.688  11.274  1   19.879 ? 76  ARG   B C    1 
ATOM   2960 O  O    . ARG   B 1 76  ? -3.34   21.82   11.732  1   19.16  ? 76  ARG   B O    1 
ATOM   2961 C  CB   . ARG   B 1 76  ? -4.061  24.725  11.526  1   25.425 ? 76  ARG   B CB   1 
ATOM   2962 C  CG   . ARG   B 1 76  ? -3.363  25.19   12.799  1   28.381 ? 76  ARG   B CG   1 
ATOM   2963 C  CD   . ARG   B 1 76  ? -4.295  26.034  13.665  1   32.404 ? 76  ARG   B CD   1 
ATOM   2964 N  NE   . ARG   B 1 76  ? -4.656  27.285  12.986  1   35.27  ? 76  ARG   B NE   1 
ATOM   2965 C  CZ   . ARG   B 1 76  ? -3.896  28.374  12.857  1   37.375 ? 76  ARG   B CZ   1 
ATOM   2966 N  NH1  . ARG   B 1 76  ? -2.776  28.515  13.551  1   38.27  ? 76  ARG   B NH1  1 
ATOM   2967 N  NH2  . ARG   B 1 76  ? -4.296  29.351  12.06   1   38.19  ? 76  ARG   B NH2  1 
ATOM   2968 N  N    . VAL   B 1 77  ? -1.271  22.668  11.381  1   18.553 ? 77  VAL   B N    1 
ATOM   2969 C  CA   . VAL   B 1 77  ? -0.557  21.594  12.055  1   17.905 ? 77  VAL   B CA   1 
ATOM   2970 C  C    . VAL   B 1 77  ? -0.576  21.869  13.557  1   17.662 ? 77  VAL   B C    1 
ATOM   2971 O  O    . VAL   B 1 77  ? -0.24   22.968  13.988  1   19.167 ? 77  VAL   B O    1 
ATOM   2972 C  CB   . VAL   B 1 77  ? 0.877   21.456  11.511  1   18.072 ? 77  VAL   B CB   1 
ATOM   2973 C  CG1  . VAL   B 1 77  ? 1.695   20.445  12.298  1   17.438 ? 77  VAL   B CG1  1 
ATOM   2974 C  CG2  . VAL   B 1 77  ? 0.87    21.048  10.043  1   18.685 ? 77  VAL   B CG2  1 
ATOM   2975 N  N    . ILE   B 1 78  ? -0.981  20.852  14.332  1   16.517 ? 78  ILE   B N    1 
ATOM   2976 C  CA   . ILE   B 1 78  ? -1.117  20.982  15.773  1   17.546 ? 78  ILE   B CA   1 
ATOM   2977 C  C    . ILE   B 1 78  ? -0.249  19.972  16.524  1   17.358 ? 78  ILE   B C    1 
ATOM   2978 O  O    . ILE   B 1 78  ? -0.261  19.961  17.753  1   18.704 ? 78  ILE   B O    1 
ATOM   2979 C  CB   . ILE   B 1 78  ? -2.592  20.892  16.205  1   18.384 ? 78  ILE   B CB   1 
ATOM   2980 C  CG1  . ILE   B 1 78  ? -3.226  19.538  15.885  1   19.379 ? 78  ILE   B CG1  1 
ATOM   2981 C  CG2  . ILE   B 1 78  ? -3.375  22.047  15.59   1   19.534 ? 78  ILE   B CG2  1 
ATOM   2982 C  CD1  . ILE   B 1 78  ? -4.56   19.295  16.568  1   20.327 ? 78  ILE   B CD1  1 
ATOM   2983 N  N    . GLY   B 1 79  ? 0.527   19.156  15.808  1   16.465 ? 79  GLY   B N    1 
ATOM   2984 C  CA   . GLY   B 1 79  ? 1.471   18.246  16.43   1   16.518 ? 79  GLY   B CA   1 
ATOM   2985 C  C    . GLY   B 1 79  ? 2.333   17.593  15.362  1   15.868 ? 79  GLY   B C    1 
ATOM   2986 O  O    . GLY   B 1 79  ? 1.925   17.534  14.209  1   15.741 ? 79  GLY   B O    1 
ATOM   2987 N  N    . HIS   B 1 80  ? 3.515   17.118  15.751  1   17.001 ? 80  HIS   B N    1 
ATOM   2988 C  CA   . HIS   B 1 80  ? 4.41    16.457  14.818  1   18.082 ? 80  HIS   B CA   1 
ATOM   2989 C  C    . HIS   B 1 80  ? 5.217   15.401  15.563  1   17.924 ? 80  HIS   B C    1 
ATOM   2990 O  O    . HIS   B 1 80  ? 5.625   15.602  16.706  1   20.288 ? 80  HIS   B O    1 
ATOM   2991 C  CB   . HIS   B 1 80  ? 5.319   17.481  14.13   1   18.775 ? 80  HIS   B CB   1 
ATOM   2992 C  CG   . HIS   B 1 80  ? 6.133   18.3    15.072  1   20.764 ? 80  HIS   B CG   1 
ATOM   2993 N  ND1  . HIS   B 1 80  ? 5.665   19.442  15.686  1   22.076 ? 80  HIS   B ND1  1 
ATOM   2994 C  CD2  . HIS   B 1 80  ? 7.384   18.141  15.516  1   22.119 ? 80  HIS   B CD2  1 
ATOM   2995 C  CE1  . HIS   B 1 80  ? 6.602   19.934  16.476  1   22.34  ? 80  HIS   B CE1  1 
ATOM   2996 N  NE2  . HIS   B 1 80  ? 7.66    19.173  16.372  1   22.377 ? 80  HIS   B NE2  1 
ATOM   2997 N  N    . SER   B 1 81  ? 5.406   14.252  14.913  1   16.408 ? 81  SER   B N    1 
ATOM   2998 C  CA   . SER   B 1 81  ? 6.14    13.143  15.493  1   16.639 ? 81  SER   B CA   1 
ATOM   2999 C  C    . SER   B 1 81  ? 6.555   12.197  14.384  1   15.371 ? 81  SER   B C    1 
ATOM   3000 O  O    . SER   B 1 81  ? 5.972   12.238  13.306  1   15.923 ? 81  SER   B O    1 
ATOM   3001 C  CB   . SER   B 1 81  ? 5.326   12.403  16.537  1   18.738 ? 81  SER   B CB   1 
ATOM   3002 O  OG   . SER   B 1 81  ? 4.204   11.749  15.956  1   20.303 ? 81  SER   B OG   1 
ATOM   3003 N  N    . MET   B 1 82  ? 7.516   11.327  14.667  1   15.236 ? 82  MET   B N    1 
ATOM   3004 C  CA   . MET   B 1 82  ? 7.938   10.343  13.694  1   15.354 ? 82  MET   B CA   1 
ATOM   3005 C  C    . MET   B 1 82  ? 7.508   8.95    14.117  1   14.599 ? 82  MET   B C    1 
ATOM   3006 O  O    . MET   B 1 82  ? 7.464   8.622   15.297  1   16.132 ? 82  MET   B O    1 
ATOM   3007 C  CB   . MET   B 1 82  ? 9.454   10.323  13.507  1   17.415 ? 82  MET   B CB   1 
ATOM   3008 C  CG   . MET   B 1 82  ? 9.989   11.524  12.775  1   19.46  ? 82  MET   B CG   1 
ATOM   3009 S  SD   . MET   B 1 82  ? 11.789  11.481  12.667  1   23.711 ? 82  MET   B SD   1 
ATOM   3010 C  CE   . MET   B 1 82  ? 12.254  11.766  14.376  1   22.307 ? 82  MET   B CE   1 
ATOM   3011 N  N    . GLN   B 1 83  ? 7.206   8.146   13.101  1   12.883 ? 83  GLN   B N    1 
ATOM   3012 C  CA   . GLN   B 1 83  ? 7.117   6.71    13.234  1   12.635 ? 83  GLN   B CA   1 
ATOM   3013 C  C    . GLN   B 1 83  ? 8.055   6.098   12.205  1   11.899 ? 83  GLN   B C    1 
ATOM   3014 O  O    . GLN   B 1 83  ? 7.813   6.219   11.012  1   12.117 ? 83  GLN   B O    1 
ATOM   3015 C  CB   . GLN   B 1 83  ? 5.68    6.231   13.042  1   13.028 ? 83  GLN   B CB   1 
ATOM   3016 C  CG   . GLN   B 1 83  ? 5.553   4.714   13.113  1   14.131 ? 83  GLN   B CG   1 
ATOM   3017 C  CD   . GLN   B 1 83  ? 4.123   4.252   12.972  1   15.716 ? 83  GLN   B CD   1 
ATOM   3018 O  OE1  . GLN   B 1 83  ? 3.288   4.959   12.405  1   18.92  ? 83  GLN   B OE1  1 
ATOM   3019 N  NE2  . GLN   B 1 83  ? 3.835   3.061   13.469  1   17.119 ? 83  GLN   B NE2  1 
ATOM   3020 N  N    . ASN   B 1 84  ? 9.149   5.492   12.663  1   11.614 ? 84  ASN   B N    1 
ATOM   3021 C  CA   . ASN   B 1 84  ? 10.139  4.957   11.737  1   11.054 ? 84  ASN   B CA   1 
ATOM   3022 C  C    . ASN   B 1 84  ? 10.55   6.079   10.779  1   10.812 ? 84  ASN   B C    1 
ATOM   3023 O  O    . ASN   B 1 84  ? 10.897  7.175   11.221  1   10.855 ? 84  ASN   B O    1 
ATOM   3024 C  CB   . ASN   B 1 84  ? 9.64    3.651   11.127  1   11.787 ? 84  ASN   B CB   1 
ATOM   3025 C  CG   . ASN   B 1 84  ? 9.287   2.637   12.19   1   13.178 ? 84  ASN   B CG   1 
ATOM   3026 O  OD1  . ASN   B 1 84  ? 10.081  2.391   13.109  1   14.027 ? 84  ASN   B OD1  1 
ATOM   3027 N  ND2  . ASN   B 1 84  ? 8.097   2.066   12.107  1   13.443 ? 84  ASN   B ND2  1 
ATOM   3028 N  N    . CYS   B 1 85  ? 10.441  5.847   9.461   1   10.47  ? 85  CYS   B N    1 
ATOM   3029 C  CA   . CYS   B 1 85  ? 10.891  6.832   8.488   1   11.01  ? 85  CYS   B CA   1 
ATOM   3030 C  C    . CYS   B 1 85  ? 9.767   7.73    7.963   1   10.961 ? 85  CYS   B C    1 
ATOM   3031 O  O    . CYS   B 1 85  ? 9.978   8.428   6.971   1   10.878 ? 85  CYS   B O    1 
ATOM   3032 C  CB   . CYS   B 1 85  ? 11.613  6.172   7.317   1   11.363 ? 85  CYS   B CB   1 
ATOM   3033 S  SG   . CYS   B 1 85  ? 13.009  5.146   7.832   1   12.641 ? 85  CYS   B SG   1 
ATOM   3034 N  N    . VAL   B 1 86  ? 8.596   7.74    8.625   1   11.746 ? 86  VAL   B N    1 
ATOM   3035 C  CA   . VAL   B 1 86  ? 7.514   8.644   8.274   1   12.254 ? 86  VAL   B CA   1 
ATOM   3036 C  C    . VAL   B 1 86  ? 7.325   9.704   9.358   1   11.731 ? 86  VAL   B C    1 
ATOM   3037 O  O    . VAL   B 1 86  ? 7.424   9.434   10.555  1   13.115 ? 86  VAL   B O    1 
ATOM   3038 C  CB   . VAL   B 1 86  ? 6.245   7.818   7.996   1   13.424 ? 86  VAL   B CB   1 
ATOM   3039 C  CG1  . VAL   B 1 86  ? 4.95    8.602   8.146   1   15.543 ? 86  VAL   B CG1  1 
ATOM   3040 C  CG2  . VAL   B 1 86  ? 6.335   7.196   6.608   1   13.543 ? 86  VAL   B CG2  1 
ATOM   3041 N  N    . LEU   B 1 87  ? 7.086   10.931  8.904   1   11.328 ? 87  LEU   B N    1 
ATOM   3042 C  CA   . LEU   B 1 87  ? 6.65    12.034  9.736   1   12.264 ? 87  LEU   B CA   1 
ATOM   3043 C  C    . LEU   B 1 87  ? 5.128   12.069  9.723   1   12.27  ? 87  LEU   B C    1 
ATOM   3044 O  O    . LEU   B 1 87  ? 4.511   11.974  8.667   1   12.172 ? 87  LEU   B O    1 
ATOM   3045 C  CB   . LEU   B 1 87  ? 7.253   13.316  9.174   1   13.688 ? 87  LEU   B CB   1 
ATOM   3046 C  CG   . LEU   B 1 87  ? 6.926   14.626  9.894   1   14.719 ? 87  LEU   B CG   1 
ATOM   3047 C  CD1  . LEU   B 1 87  ? 7.564   14.678  11.259  1   15.914 ? 87  LEU   B CD1  1 
ATOM   3048 C  CD2  . LEU   B 1 87  ? 7.394   15.798  9.054   1   15.707 ? 87  LEU   B CD2  1 
ATOM   3049 N  N    . LYS   B 1 88  ? 4.552   12.209  10.92   1   12.848 ? 88  LYS   B N    1 
ATOM   3050 C  CA   . LYS   B 1 88  ? 3.123   12.325  11.117  1   12.866 ? 88  LYS   B CA   1 
ATOM   3051 C  C    . LYS   B 1 88  ? 2.832   13.731  11.618  1   12.905 ? 88  LYS   B C    1 
ATOM   3052 O  O    . LYS   B 1 88  ? 3.321   14.135  12.677  1   14.673 ? 88  LYS   B O    1 
ATOM   3053 C  CB   . LYS   B 1 88  ? 2.658   11.278  12.131  1   14.197 ? 88  LYS   B CB   1 
ATOM   3054 C  CG   . LYS   B 1 88  ? 2.848   9.858   11.657  1   16.171 ? 88  LYS   B CG   1 
ATOM   3055 C  CD   . LYS   B 1 88  ? 2.74    8.787   12.734  1   20.65  ? 88  LYS   B CD   1 
ATOM   3056 C  CE   . LYS   B 1 88  ? 1.404   8.294   13.061  1   25.378 ? 88  LYS   B CE   1 
ATOM   3057 N  NZ   . LYS   B 1 88  ? 1.569   6.987   13.718  1   27.965 ? 88  LYS   B NZ   1 
ATOM   3058 N  N    . LEU   B 1 89  ? 2.059   14.476  10.831  1   12.478 ? 89  LEU   B N    1 
ATOM   3059 C  CA   . LEU   B 1 89  ? 1.678   15.827  11.175  1   12.664 ? 89  LEU   B CA   1 
ATOM   3060 C  C    . LEU   B 1 89  ? 0.21    15.785  11.567  1   13.237 ? 89  LEU   B C    1 
ATOM   3061 O  O    . LEU   B 1 89  ? -0.646  15.505  10.728  1   13.163 ? 89  LEU   B O    1 
ATOM   3062 C  CB   . LEU   B 1 89  ? 1.904   16.799  10.023  1   13.779 ? 89  LEU   B CB   1 
ATOM   3063 C  CG   . LEU   B 1 89  ? 3.328   16.867  9.472   1   14.461 ? 89  LEU   B CG   1 
ATOM   3064 C  CD1  . LEU   B 1 89  ? 3.374   17.72   8.205   1   15.888 ? 89  LEU   B CD1  1 
ATOM   3065 C  CD2  . LEU   B 1 89  ? 4.253   17.401  10.553  1   14.688 ? 89  LEU   B CD2  1 
ATOM   3066 N  N    . LYS   B 1 90  ? -0.066  16.02   12.854  1   13.95  ? 90  LYS   B N    1 
ATOM   3067 C  CA   . LYS   B 1 90  ? -1.439  16.091  13.307  1   14.484 ? 90  LYS   B CA   1 
ATOM   3068 C  C    . LYS   B 1 90  ? -1.989  17.447  12.882  1   14.099 ? 90  LYS   B C    1 
ATOM   3069 O  O    . LYS   B 1 90  ? -1.325  18.456  13.079  1   14.421 ? 90  LYS   B O    1 
ATOM   3070 C  CB   . LYS   B 1 90  ? -1.482  15.941  14.831  1   16.024 ? 90  LYS   B CB   1 
ATOM   3071 C  CG   . LYS   B 1 90  ? -2.882  15.726  15.365  1   18.854 ? 90  LYS   B CG   1 
ATOM   3072 C  CD   . LYS   B 1 90  ? -3.324  14.273  15.232  1   22.673 ? 90  LYS   B CD   1 
ATOM   3073 C  CE   . LYS   B 1 90  ? -4.303  13.853  16.288  1   25.785 ? 90  LYS   B CE   1 
ATOM   3074 N  NZ   . LYS   B 1 90  ? -4.835  12.523  15.972  1   27.861 ? 90  LYS   B NZ   1 
ATOM   3075 N  N    . VAL   B 1 91  ? -3.175  17.456  12.256  1   15.305 ? 91  VAL   B N    1 
ATOM   3076 C  CA   . VAL   B 1 91  ? -3.8    18.686  11.797  1   15.701 ? 91  VAL   B CA   1 
ATOM   3077 C  C    . VAL   B 1 91  ? -5.122  18.864  12.54   1   16.734 ? 91  VAL   B C    1 
ATOM   3078 O  O    . VAL   B 1 91  ? -5.631  17.929  13.158  1   16.83  ? 91  VAL   B O    1 
ATOM   3079 C  CB   . VAL   B 1 91  ? -3.963  18.751  10.262  1   16.134 ? 91  VAL   B CB   1 
ATOM   3080 C  CG1  . VAL   B 1 91  ? -2.609  18.871  9.581   1   16.644 ? 91  VAL   B CG1  1 
ATOM   3081 C  CG2  . VAL   B 1 91  ? -4.713  17.557  9.702   1   15.778 ? 91  VAL   B CG2  1 
ATOM   3082 N  N    . ASP   B 1 92  ? -5.681  20.073  12.463  1   18.799 ? 92  ASP   B N    1 
ATOM   3083 C  CA   . ASP   B 1 92  ? -6.838  20.408  13.282  1   19.965 ? 92  ASP   B CA   1 
ATOM   3084 C  C    . ASP   B 1 92  ? -8.161  20.022  12.622  1   20.953 ? 92  ASP   B C    1 
ATOM   3085 O  O    . ASP   B 1 92  ? -9.206  20.301  13.19   1   22.678 ? 92  ASP   B O    1 
ATOM   3086 C  CB   . ASP   B 1 92  ? -6.829  21.869  13.68   1   22.925 ? 92  ASP   B CB   1 
ATOM   3087 C  CG   . ASP   B 1 92  ? -7.131  22.866  12.58   1   25.753 ? 92  ASP   B CG   1 
ATOM   3088 O  OD1  . ASP   B 1 92  ? -7.271  22.432  11.412  1   28.939 ? 92  ASP   B OD1  1 
ATOM   3089 O  OD2  . ASP   B 1 92  ? -7.22   24.068  12.917  1   29.973 ? 92  ASP   B OD2  1 
ATOM   3090 N  N    . THR   B 1 93  ? -8.106  19.403  11.436  1   20.967 ? 93  THR   B N    1 
ATOM   3091 C  CA   . THR   B 1 93  ? -9.282  19.063  10.649  1   21.726 ? 93  THR   B CA   1 
ATOM   3092 C  C    . THR   B 1 93  ? -9.113  17.636  10.14   1   19.674 ? 93  THR   B C    1 
ATOM   3093 O  O    . THR   B 1 93  ? -8.068  17.299  9.592   1   20.237 ? 93  THR   B O    1 
ATOM   3094 C  CB   . THR   B 1 93  ? -9.4    20.053  9.489   1   24.42  ? 93  THR   B CB   1 
ATOM   3095 O  OG1  . THR   B 1 93  ? -9.651  21.33   10.067  1   27.242 ? 93  THR   B OG1  1 
ATOM   3096 C  CG2  . THR   B 1 93  ? -10.526 19.747  8.513   1   25.856 ? 93  THR   B CG2  1 
ATOM   3097 N  N    . ALA   B 1 94  ? -10.147 16.807  10.334  1   17.862 ? 94  ALA   B N    1 
ATOM   3098 C  CA   . ALA   B 1 94  ? -10.184 15.486  9.738   1   17.341 ? 94  ALA   B CA   1 
ATOM   3099 C  C    . ALA   B 1 94  ? -10.506 15.647  8.254   1   16.479 ? 94  ALA   B C    1 
ATOM   3100 O  O    . ALA   B 1 94  ? -11.362 16.444  7.889   1   17.945 ? 94  ALA   B O    1 
ATOM   3101 C  CB   . ALA   B 1 94  ? -11.205 14.604  10.43   1   17.946 ? 94  ALA   B CB   1 
ATOM   3102 N  N    . ASN   B 1 95  ? -9.816  14.893  7.391   1   14.666 ? 95  ASN   B N    1 
ATOM   3103 C  CA   . ASN   B 1 95  ? -10.099 14.967  5.966   1   14.554 ? 95  ASN   B CA   1 
ATOM   3104 C  C    . ASN   B 1 95  ? -11.522 14.476  5.712   1   14.27  ? 95  ASN   B C    1 
ATOM   3105 O  O    . ASN   B 1 95  ? -11.82  13.306  5.946   1   14.525 ? 95  ASN   B O    1 
ATOM   3106 C  CB   . ASN   B 1 95  ? -9.085  14.141  5.184   1   13.935 ? 95  ASN   B CB   1 
ATOM   3107 C  CG   . ASN   B 1 95  ? -9.26   14.235  3.69    1   14.253 ? 95  ASN   B CG   1 
ATOM   3108 O  OD1  . ASN   B 1 95  ? -10.2   14.878  3.213   1   14.743 ? 95  ASN   B OD1  1 
ATOM   3109 N  ND2  . ASN   B 1 95  ? -8.375  13.59   2.948   1   14.044 ? 95  ASN   B ND2  1 
ATOM   3110 N  N    . PRO   B 1 96  ? -12.439 15.321  5.187   1   15.778 ? 96  PRO   B N    1 
ATOM   3111 C  CA   . PRO   B 1 96  ? -13.804 14.864  4.925   1   16.455 ? 96  PRO   B CA   1 
ATOM   3112 C  C    . PRO   B 1 96  ? -13.893 13.819  3.815   1   16.757 ? 96  PRO   B C    1 
ATOM   3113 O  O    . PRO   B 1 96  ? -14.907 13.126  3.701   1   18.865 ? 96  PRO   B O    1 
ATOM   3114 C  CB   . PRO   B 1 96  ? -14.562 16.152  4.571   1   17.57  ? 96  PRO   B CB   1 
ATOM   3115 C  CG   . PRO   B 1 96  ? -13.504 17.09   4.062   1   18.194 ? 96  PRO   B CG   1 
ATOM   3116 C  CD   . PRO   B 1 96  ? -12.228 16.727  4.812   1   16.667 ? 96  PRO   B CD   1 
ATOM   3117 N  N    . LYS   B 1 97  ? -12.822 13.713  3.019   1   16.265 ? 97  LYS   B N    1 
ATOM   3118 C  CA   . LYS   B 1 97  ? -12.76  12.763  1.92    1   16.841 ? 97  LYS   B CA   1 
ATOM   3119 C  C    . LYS   B 1 97  ? -11.978 11.504  2.295   1   15.71  ? 97  LYS   B C    1 
ATOM   3120 O  O    . LYS   B 1 97  ? -11.645 10.719  1.417   1   16.456 ? 97  LYS   B O    1 
ATOM   3121 C  CB   . LYS   B 1 97  ? -12.139 13.419  0.676   1   18.406 ? 97  LYS   B CB   1 
ATOM   3122 C  CG   . LYS   B 1 97  ? -12.911 14.617  0.159   1   20.841 ? 97  LYS   B CG   1 
ATOM   3123 C  CD   . LYS   B 1 97  ? -12.352 15.153  -1.149  1   24.328 ? 97  LYS   B CD   1 
ATOM   3124 C  CE   . LYS   B 1 97  ? -12.951 16.476  -1.484  1   27.881 ? 97  LYS   B CE   1 
ATOM   3125 N  NZ   . LYS   B 1 97  ? -12.754 16.787  -2.897  1   30.973 ? 97  LYS   B NZ   1 
ATOM   3126 N  N    . THR   B 1 98  ? -11.721 11.273  3.589   1   14.518 ? 98  THR   B N    1 
ATOM   3127 C  CA   . THR   B 1 98  ? -11.024 10.065  4.009   1   13.608 ? 98  THR   B CA   1 
ATOM   3128 C  C    . THR   B 1 98  ? -11.842 8.865   3.547   1   13.543 ? 98  THR   B C    1 
ATOM   3129 O  O    . THR   B 1 98  ? -12.986 8.705   3.984   1   14.196 ? 98  THR   B O    1 
ATOM   3130 C  CB   . THR   B 1 98  ? -10.826 10.004  5.526   1   14.003 ? 98  THR   B CB   1 
ATOM   3131 O  OG1  . THR   B 1 98  ? -10.122 11.167  5.941   1   14.196 ? 98  THR   B OG1  1 
ATOM   3132 C  CG2  . THR   B 1 98  ? -10.103 8.741   5.959   1   14.038 ? 98  THR   B CG2  1 
ATOM   3133 N  N    . PRO   B 1 99  ? -11.282 7.953   2.715   1   13.16  ? 99  PRO   B N    1 
ATOM   3134 C  CA   . PRO   B 1 99  ? -11.997 6.733   2.341   1   13.741 ? 99  PRO   B CA   1 
ATOM   3135 C  C    . PRO   B 1 99  ? -11.862 5.721   3.469   1   13.519 ? 99  PRO   B C    1 
ATOM   3136 O  O    . PRO   B 1 99  ? -11.043 5.901   4.365   1   14.13  ? 99  PRO   B O    1 
ATOM   3137 C  CB   . PRO   B 1 99  ? -11.259 6.288   1.079   1   13.973 ? 99  PRO   B CB   1 
ATOM   3138 C  CG   . PRO   B 1 99  ? -9.825  6.693   1.355   1   13.793 ? 99  PRO   B CG   1 
ATOM   3139 C  CD   . PRO   B 1 99  ? -9.943  8.022   2.106   1   13.616 ? 99  PRO   B CD   1 
ATOM   3140 N  N    A LYS   B 1 100 ? -12.643 4.641   3.411   0.5 13.891 ? 100 LYS   B N    1 
ATOM   3141 N  N    B LYS   B 1 100 ? -12.634 4.635   3.415   0.5 13.971 ? 100 LYS   B N    1 
ATOM   3142 C  CA   A LYS   B 1 100 ? -12.32  3.473   4.219   0.5 14.278 ? 100 LYS   B CA   1 
ATOM   3143 C  CA   B LYS   B 1 100 ? -12.322 3.487   4.255   0.5 14.428 ? 100 LYS   B CA   1 
ATOM   3144 C  C    A LYS   B 1 100 ? -10.917 3.037   3.806   0.5 13.429 ? 100 LYS   B C    1 
ATOM   3145 C  C    B LYS   B 1 100 ? -10.952 2.972   3.825   0.5 13.491 ? 100 LYS   B C    1 
ATOM   3146 O  O    A LYS   B 1 100 ? -10.629 2.983   2.609   0.5 13.88  ? 100 LYS   B O    1 
ATOM   3147 O  O    B LYS   B 1 100 ? -10.733 2.758   2.637   0.5 13.855 ? 100 LYS   B O    1 
ATOM   3148 C  CB   A LYS   B 1 100 ? -13.312 2.331   3.977   0.5 15.838 ? 100 LYS   B CB   1 
ATOM   3149 C  CB   B LYS   B 1 100 ? -13.346 2.363   4.079   0.5 16.153 ? 100 LYS   B CB   1 
ATOM   3150 C  CG   A LYS   B 1 100 ? -13.13  1.095   4.853   0.5 17.268 ? 100 LYS   B CG   1 
ATOM   3151 C  CG   B LYS   B 1 100 ? -14.759 2.717   4.489   0.5 17.724 ? 100 LYS   B CG   1 
ATOM   3152 C  CD   A LYS   B 1 100 ? -14.152 -0.004  4.575   0.5 19.143 ? 100 LYS   B CD   1 
ATOM   3153 C  CD   B LYS   B 1 100 ? -15.716 1.547   4.343   0.5 20.093 ? 100 LYS   B CD   1 
ATOM   3154 C  CE   A LYS   B 1 100 ? -13.902 -1.266  5.34    0.5 20.882 ? 100 LYS   B CE   1 
ATOM   3155 C  CE   B LYS   B 1 100 ? -17.111 1.947   4.691   0.5 21.896 ? 100 LYS   B CE   1 
ATOM   3156 N  NZ   A LYS   B 1 100 ? -14.976 -2.24   5.125   0.5 22.69  ? 100 LYS   B NZ   1 
ATOM   3157 N  NZ   B LYS   B 1 100 ? -18.05  0.98    4.133   0.5 23.783 ? 100 LYS   B NZ   1 
ATOM   3158 N  N    . TYR   B 1 101 ? -10.037 2.781   4.779   1   12.626 ? 101 TYR   B N    1 
ATOM   3159 C  CA   . TYR   B 1 101 ? -8.664  2.463   4.437   1   12.521 ? 101 TYR   B CA   1 
ATOM   3160 C  C    . TYR   B 1 101 ? -8.017  1.577   5.487   1   12.902 ? 101 TYR   B C    1 
ATOM   3161 O  O    . TYR   B 1 101 ? -8.449  1.503   6.64    1   13.918 ? 101 TYR   B O    1 
ATOM   3162 C  CB   . TYR   B 1 101 ? -7.816  3.724   4.224   1   12.397 ? 101 TYR   B CB   1 
ATOM   3163 C  CG   . TYR   B 1 101 ? -7.416  4.416   5.516   1   12.47  ? 101 TYR   B CG   1 
ATOM   3164 C  CD1  . TYR   B 1 101 ? -8.275  5.324   6.108   1   12.785 ? 101 TYR   B CD1  1 
ATOM   3165 C  CD2  . TYR   B 1 101 ? -6.217  4.144   6.158   1   12.677 ? 101 TYR   B CD2  1 
ATOM   3166 C  CE1  . TYR   B 1 101 ? -7.959  5.955   7.298   1   13.234 ? 101 TYR   B CE1  1 
ATOM   3167 C  CE2  . TYR   B 1 101 ? -5.878  4.781   7.34    1   13.257 ? 101 TYR   B CE2  1 
ATOM   3168 C  CZ   . TYR   B 1 101 ? -6.753  5.68    7.921   1   13.107 ? 101 TYR   B CZ   1 
ATOM   3169 O  OH   . TYR   B 1 101 ? -6.406  6.279   9.101   1   13.877 ? 101 TYR   B OH   1 
ATOM   3170 N  N    . LYS   B 1 102 ? -6.943  0.927   5.033   1   13.508 ? 102 LYS   B N    1 
ATOM   3171 C  CA   . LYS   B 1 102 ? -6.034  0.188   5.878   1   14.26  ? 102 LYS   B CA   1 
ATOM   3172 C  C    . LYS   B 1 102 ? -4.623  0.498   5.396   1   12.89  ? 102 LYS   B C    1 
ATOM   3173 O  O    . LYS   B 1 102 ? -4.419  0.886   4.243   1   12.573 ? 102 LYS   B O    1 
ATOM   3174 C  CB   . LYS   B 1 102 ? -6.24   -1.324  5.719   1   17.535 ? 102 LYS   B CB   1 
ATOM   3175 C  CG   . LYS   B 1 102 ? -7.618  -1.867  5.959   1   20.928 ? 102 LYS   B CG   1 
ATOM   3176 C  CD   . LYS   B 1 102 ? -7.774  -3.333  5.575   1   24.746 ? 102 LYS   B CD   1 
ATOM   3177 C  CE   . LYS   B 1 102 ? -9.179  -3.762  5.903   1   28.918 ? 102 LYS   B CE   1 
ATOM   3178 N  NZ   . LYS   B 1 102 ? -9.652  -4.962  5.208   1   32.486 ? 102 LYS   B NZ   1 
ATOM   3179 N  N    . PHE   B 1 103 ? -3.658  0.299   6.299   1   11.959 ? 103 PHE   B N    1 
ATOM   3180 C  CA   . PHE   B 1 103 ? -2.254  0.264   5.946   1   11.695 ? 103 PHE   B CA   1 
ATOM   3181 C  C    . PHE   B 1 103 ? -1.826  -1.193  5.9     1   12.536 ? 103 PHE   B C    1 
ATOM   3182 O  O    . PHE   B 1 103 ? -2.05   -1.944  6.854   1   14.016 ? 103 PHE   B O    1 
ATOM   3183 C  CB   . PHE   B 1 103 ? -1.432  1.025   6.988   1   11.684 ? 103 PHE   B CB   1 
ATOM   3184 C  CG   . PHE   B 1 103 ? -1.614  2.531   7.057   1   11.894 ? 103 PHE   B CG   1 
ATOM   3185 C  CD1  . PHE   B 1 103 ? -2.214  3.236   6.025   1   12.434 ? 103 PHE   B CD1  1 
ATOM   3186 C  CD2  . PHE   B 1 103 ? -1.092  3.256   8.131   1   13.34  ? 103 PHE   B CD2  1 
ATOM   3187 C  CE1  . PHE   B 1 103 ? -2.314  4.609   6.075   1   12.477 ? 103 PHE   B CE1  1 
ATOM   3188 C  CE2  . PHE   B 1 103 ? -1.197  4.635   8.18    1   13.547 ? 103 PHE   B CE2  1 
ATOM   3189 C  CZ   . PHE   B 1 103 ? -1.811  5.309   7.154   1   13.229 ? 103 PHE   B CZ   1 
ATOM   3190 N  N    A VAL   B 1 104 ? -1.185  -1.59   4.791   0.5 12.352 ? 104 VAL   B N    1 
ATOM   3191 N  N    B VAL   B 1 104 ? -1.246  -1.589  4.769   0.5 12.197 ? 104 VAL   B N    1 
ATOM   3192 C  CA   A VAL   B 1 104 ? -0.813  -2.976  4.56    0.5 12.866 ? 104 VAL   B CA   1 
ATOM   3193 C  CA   B VAL   B 1 104 ? -0.734  -2.936  4.652   0.5 12.52  ? 104 VAL   B CA   1 
ATOM   3194 C  C    A VAL   B 1 104 ? 0.615   -3.018  4.027   0.5 12.532 ? 104 VAL   B C    1 
ATOM   3195 C  C    B VAL   B 1 104 ? 0.731   -2.848  4.255   0.5 12.296 ? 104 VAL   B C    1 
ATOM   3196 O  O    A VAL   B 1 104 ? 0.957   -2.263  3.115   0.5 12.683 ? 104 VAL   B O    1 
ATOM   3197 O  O    B VAL   B 1 104 ? 1.205   -1.854  3.697   0.5 12.374 ? 104 VAL   B O    1 
ATOM   3198 C  CB   A VAL   B 1 104 ? -1.785  -3.645  3.57    0.5 14.348 ? 104 VAL   B CB   1 
ATOM   3199 C  CB   B VAL   B 1 104 ? -1.515  -3.827  3.671   0.5 13.62  ? 104 VAL   B CB   1 
ATOM   3200 C  CG1  A VAL   B 1 104 ? -1.348  -5.062  3.206   0.5 15.251 ? 104 VAL   B CG1  1 
ATOM   3201 C  CG1  B VAL   B 1 104 ? -2.982  -3.954  4.053   0.5 14.106 ? 104 VAL   B CG1  1 
ATOM   3202 C  CG2  A VAL   B 1 104 ? -3.213  -3.631  4.102   0.5 14.872 ? 104 VAL   B CG2  1 
ATOM   3203 C  CG2  B VAL   B 1 104 ? -1.367  -3.332  2.247   0.5 13.57  ? 104 VAL   B CG2  1 
ATOM   3204 N  N    . ARG   B 1 105 ? 1.43    -3.93   4.571   1   12.041 ? 105 ARG   B N    1 
ATOM   3205 C  CA   . ARG   B 1 105 ? 2.772   -4.141  4.074   1   12.487 ? 105 ARG   B CA   1 
ATOM   3206 C  C    . ARG   B 1 105 ? 2.728   -5.302  3.094   1   13.062 ? 105 ARG   B C    1 
ATOM   3207 O  O    . ARG   B 1 105 ? 2.316   -6.402  3.445   1   15.031 ? 105 ARG   B O    1 
ATOM   3208 C  CB   . ARG   B 1 105 ? 3.734   -4.421  5.227   1   13.132 ? 105 ARG   B CB   1 
ATOM   3209 C  CG   . ARG   B 1 105 ? 5.175   -4.527  4.758   1   13.252 ? 105 ARG   B CG   1 
ATOM   3210 C  CD   . ARG   B 1 105 ? 6.098   -4.707  5.955   1   13.801 ? 105 ARG   B CD   1 
ATOM   3211 N  NE   . ARG   B 1 105 ? 7.491   -4.843  5.52    1   14.214 ? 105 ARG   B NE   1 
ATOM   3212 C  CZ   . ARG   B 1 105 ? 8.272   -3.867  5.091   1   13.359 ? 105 ARG   B CZ   1 
ATOM   3213 N  NH1  . ARG   B 1 105 ? 7.875   -2.612  5.176   1   12.695 ? 105 ARG   B NH1  1 
ATOM   3214 N  NH2  . ARG   B 1 105 ? 9.474   -4.152  4.6     1   13.936 ? 105 ARG   B NH2  1 
ATOM   3215 N  N    . ILE   B 1 106 ? 3.183   -5.055  1.864   1   13.281 ? 106 ILE   B N    1 
ATOM   3216 C  CA   . ILE   B 1 106 ? 3.079   -6.079  0.837   1   14.432 ? 106 ILE   B CA   1 
ATOM   3217 C  C    . ILE   B 1 106 ? 4.366   -6.885  0.725   1   15.599 ? 106 ILE   B C    1 
ATOM   3218 O  O    . ILE   B 1 106 ? 5.392   -6.535  1.294   1   15.338 ? 106 ILE   B O    1 
ATOM   3219 C  CB   . ILE   B 1 106 ? 2.682   -5.471  -0.514  1   15.52  ? 106 ILE   B CB   1 
ATOM   3220 C  CG1  . ILE   B 1 106 ? 3.681   -4.409  -0.991  1   15.932 ? 106 ILE   B CG1  1 
ATOM   3221 C  CG2  . ILE   B 1 106 ? 1.25    -4.961  -0.414  1   16.111 ? 106 ILE   B CG2  1 
ATOM   3222 C  CD1  . ILE   B 1 106 ? 3.501   -4.026  -2.446  1   16.866 ? 106 ILE   B CD1  1 
ATOM   3223 N  N    . GLN   B 1 107 ? 4.246   -7.994  -0.009  1   15.872 ? 107 GLN   B N    1 
ATOM   3224 C  CA   . GLN   B 1 107 ? 5.347   -8.907  -0.226  1   17.322 ? 107 GLN   B CA   1 
ATOM   3225 C  C    . GLN   B 1 107 ? 5.866   -8.764  -1.646  1   15.562 ? 107 GLN   B C    1 
ATOM   3226 O  O    . GLN   B 1 107 ? 5.127   -8.358  -2.549  1   14.317 ? 107 GLN   B O    1 
ATOM   3227 C  CB   . GLN   B 1 107 ? 4.884   -10.341 -0.016  1   20.587 ? 107 GLN   B CB   1 
ATOM   3228 C  CG   . GLN   B 1 107 ? 4.633   -10.68  1.447   1   24.235 ? 107 GLN   B CG   1 
ATOM   3229 C  CD   . GLN   B 1 107 ? 4.275   -12.137 1.616   1   29.42  ? 107 GLN   B CD   1 
ATOM   3230 O  OE1  . GLN   B 1 107 ? 5.033   -13.027 1.212   1   34.643 ? 107 GLN   B OE1  1 
ATOM   3231 N  NE2  . GLN   B 1 107 ? 3.094   -12.398 2.158   1   34.214 ? 107 GLN   B NE2  1 
ATOM   3232 N  N    . PRO   B 1 108 ? 7.135   -9.128  -1.904  1   16.367 ? 108 PRO   B N    1 
ATOM   3233 C  CA   . PRO   B 1 108 ? 7.649   -9.123  -3.267  1   16.621 ? 108 PRO   B CA   1 
ATOM   3234 C  C    . PRO   B 1 108 ? 6.742   -9.947  -4.163  1   14.841 ? 108 PRO   B C    1 
ATOM   3235 O  O    . PRO   B 1 108 ? 6.263   -11.017 -3.782  1   16.194 ? 108 PRO   B O    1 
ATOM   3236 C  CB   . PRO   B 1 108 ? 9.035   -9.734  -3.139  1   18.086 ? 108 PRO   B CB   1 
ATOM   3237 C  CG   . PRO   B 1 108 ? 9.423   -9.368  -1.751  1   19.439 ? 108 PRO   B CG   1 
ATOM   3238 C  CD   . PRO   B 1 108 ? 8.15    -9.565  -0.923  1   17.811 ? 108 PRO   B CD   1 
ATOM   3239 N  N    . GLY   B 1 109 ? 6.506   -9.4    -5.352  1   13.972 ? 109 GLY   B N    1 
ATOM   3240 C  CA   . GLY   B 1 109 ? 5.654   -10.041 -6.338  1   14.423 ? 109 GLY   B CA   1 
ATOM   3241 C  C    . GLY   B 1 109 ? 4.271   -9.409  -6.404  1   14.055 ? 109 GLY   B C    1 
ATOM   3242 O  O    . GLY   B 1 109 ? 3.574   -9.513  -7.411  1   16.221 ? 109 GLY   B O    1 
ATOM   3243 N  N    . GLN   B 1 110 ? 3.859   -8.761  -5.313  1   12.695 ? 110 GLN   B N    1 
ATOM   3244 C  CA   . GLN   B 1 110 ? 2.551   -8.138  -5.289  1   13.178 ? 110 GLN   B CA   1 
ATOM   3245 C  C    . GLN   B 1 110 ? 2.597   -6.84   -6.082  1   12.789 ? 110 GLN   B C    1 
ATOM   3246 O  O    . GLN   B 1 110 ? 3.611   -6.144  -6.122  1   13.069 ? 110 GLN   B O    1 
ATOM   3247 C  CB   . GLN   B 1 110 ? 2.119   -7.943  -3.836  1   14.237 ? 110 GLN   B CB   1 
ATOM   3248 C  CG   . GLN   B 1 110 ? 1.839   -9.261  -3.12   1   17.531 ? 110 GLN   B CG   1 
ATOM   3249 N  N    . THR   B 1 111 ? 1.467   -6.534  -6.725  1   12.9   ? 111 THR   B N    1 
ATOM   3250 C  CA   . THR   B 1 111 ? 1.319   -5.339  -7.529  1   12.675 ? 111 THR   B CA   1 
ATOM   3251 C  C    . THR   B 1 111 ? 0.505   -4.291  -6.783  1   12.576 ? 111 THR   B C    1 
ATOM   3252 O  O    . THR   B 1 111 ? -0.212  -4.597  -5.833  1   13.63  ? 111 THR   B O    1 
ATOM   3253 C  CB   . THR   B 1 111 ? 0.682   -5.696  -8.864  1   13.304 ? 111 THR   B CB   1 
ATOM   3254 O  OG1  . THR   B 1 111 ? -0.577  -6.296  -8.572  1   13.74  ? 111 THR   B OG1  1 
ATOM   3255 C  CG2  . THR   B 1 111 ? 1.574   -6.598  -9.695  1   13.846 ? 111 THR   B CG2  1 
ATOM   3256 N  N    . PHE   B 1 112 ? 0.618   -3.054  -7.249  1   11.562 ? 112 PHE   B N    1 
ATOM   3257 C  CA   . PHE   B 1 112 ? -0.154  -1.956  -6.71   1   11.111 ? 112 PHE   B CA   1 
ATOM   3258 C  C    . PHE   B 1 112 ? -0.141  -0.799  -7.701  1   10.303 ? 112 PHE   B C    1 
ATOM   3259 O  O    . PHE   B 1 112 ? 0.71    -0.735  -8.594  1   10.514 ? 112 PHE   B O    1 
ATOM   3260 C  CB   . PHE   B 1 112 ? 0.41    -1.542  -5.356  1   11.132 ? 112 PHE   B CB   1 
ATOM   3261 C  CG   . PHE   B 1 112 ? 1.874   -1.141  -5.342  1   11.12  ? 112 PHE   B CG   1 
ATOM   3262 C  CD1  . PHE   B 1 112 ? 2.869   -2.086  -5.164  1   12.292 ? 112 PHE   B CD1  1 
ATOM   3263 C  CD2  . PHE   B 1 112 ? 2.229   0.193   -5.445  1   11.064 ? 112 PHE   B CD2  1 
ATOM   3264 C  CE1  . PHE   B 1 112 ? 4.201   -1.679  -5.101  1   12.652 ? 112 PHE   B CE1  1 
ATOM   3265 C  CE2  . PHE   B 1 112 ? 3.541   0.591   -5.351  1   12.269 ? 112 PHE   B CE2  1 
ATOM   3266 C  CZ   . PHE   B 1 112 ? 4.524   -0.345  -5.187  1   12.655 ? 112 PHE   B CZ   1 
ATOM   3267 N  N    . SER   B 1 113 ? -1.084  0.124   -7.517  1   10.244 ? 113 SER   B N    1 
ATOM   3268 C  CA   . SER   B 1 113 ? -1.165  1.338   -8.305  1   10.449 ? 113 SER   B CA   1 
ATOM   3269 C  C    . SER   B 1 113 ? -0.409  2.453   -7.601  1   9.977  ? 113 SER   B C    1 
ATOM   3270 O  O    . SER   B 1 113 ? -0.518  2.594   -6.38   1   10.788 ? 113 SER   B O    1 
ATOM   3271 C  CB   . SER   B 1 113 ? -2.59   1.737   -8.507  1   11.186 ? 113 SER   B CB   1 
ATOM   3272 O  OG   . SER   B 1 113 ? -3.295  0.714   -9.184  1   12.687 ? 113 SER   B OG   1 
ATOM   3273 N  N    . VAL   B 1 114 ? 0.332   3.246   -8.362  1   10.525 ? 114 VAL   B N    1 
ATOM   3274 C  CA   . VAL   B 1 114 ? 1.031   4.415   -7.876  1   10.185 ? 114 VAL   B CA   1 
ATOM   3275 C  C    . VAL   B 1 114 ? 0.338   5.657   -8.402  1   10.242 ? 114 VAL   B C    1 
ATOM   3276 O  O    . VAL   B 1 114 ? 0.087   5.765   -9.603  1   10.866 ? 114 VAL   B O    1 
ATOM   3277 C  CB   . VAL   B 1 114 ? 2.494   4.401   -8.338  1   11.194 ? 114 VAL   B CB   1 
ATOM   3278 C  CG1  . VAL   B 1 114 ? 3.177   5.741   -8.099  1   11.768 ? 114 VAL   B CG1  1 
ATOM   3279 C  CG2  . VAL   B 1 114 ? 3.244   3.241   -7.707  1   11.885 ? 114 VAL   B CG2  1 
ATOM   3280 N  N    . LEU   B 1 115 ? 0.045   6.582   -7.496  1   10.252 ? 115 LEU   B N    1 
ATOM   3281 C  CA   . LEU   B 1 115 ? -0.431  7.902   -7.847  1   10.101 ? 115 LEU   B CA   1 
ATOM   3282 C  C    . LEU   B 1 115 ? 0.732   8.872   -7.706  1   10.571 ? 115 LEU   B C    1 
ATOM   3283 O  O    . LEU   B 1 115 ? 1.108   9.262   -6.602  1   11.491 ? 115 LEU   B O    1 
ATOM   3284 C  CB   . LEU   B 1 115 ? -1.608  8.287   -6.961  1   10.486 ? 115 LEU   B CB   1 
ATOM   3285 C  CG   . LEU   B 1 115 ? -2.242  9.636   -7.298  1   11.189 ? 115 LEU   B CG   1 
ATOM   3286 C  CD1  . LEU   B 1 115 ? -2.892  9.562   -8.676  1   11.49  ? 115 LEU   B CD1  1 
ATOM   3287 C  CD2  . LEU   B 1 115 ? -3.256  10.088  -6.254  1   12.028 ? 115 LEU   B CD2  1 
ATOM   3288 N  N    . ALA   B 1 116 ? 1.37    9.181   -8.835  1   10.744 ? 116 ALA   B N    1 
ATOM   3289 C  CA   . ALA   B 1 116 ? 2.498   10.088  -8.856  1   10.958 ? 116 ALA   B CA   1 
ATOM   3290 C  C    . ALA   B 1 116 ? 1.974   11.5    -8.679  1   11.321 ? 116 ALA   B C    1 
ATOM   3291 O  O    . ALA   B 1 116 ? 1.039   11.912  -9.369  1   12.525 ? 116 ALA   B O    1 
ATOM   3292 C  CB   . ALA   B 1 116 ? 3.285   9.956   -10.141 1   11.425 ? 116 ALA   B CB   1 
ATOM   3293 N  N    A CYS   B 1 117 ? 2.563   12.219  -7.72   0.5 10.464 ? 117 CYS   B N    1 
ATOM   3294 N  N    B CYS   B 1 117 ? 2.636   12.239  -7.785  0.5 12.208 ? 117 CYS   B N    1 
ATOM   3295 C  CA   A CYS   B 1 117 ? 2.132   13.559  -7.388  0.5 10.15  ? 117 CYS   B CA   1 
ATOM   3296 C  CA   B CYS   B 1 117 ? 2.155   13.509  -7.288  0.5 13.332 ? 117 CYS   B CA   1 
ATOM   3297 C  C    A CYS   B 1 117 ? 3.329   14.496  -7.309  0.5 10.509 ? 117 CYS   B C    1 
ATOM   3298 C  C    B CYS   B 1 117 ? 3.318   14.498  -7.266  0.5 12.23  ? 117 CYS   B C    1 
ATOM   3299 O  O    A CYS   B 1 117 ? 4.437   14.083  -6.952  0.5 10.501 ? 117 CYS   B O    1 
ATOM   3300 O  O    B CYS   B 1 117 ? 4.436   14.105  -6.958  0.5 12.268 ? 117 CYS   B O    1 
ATOM   3301 C  CB   A CYS   B 1 117 ? 1.458   13.595  -6.025  0.5 9.547  ? 117 CYS   B CB   1 
ATOM   3302 C  CB   B CYS   B 1 117 ? 1.583   13.263  -5.898  0.5 15.307 ? 117 CYS   B CB   1 
ATOM   3303 S  SG   A CYS   B 1 117 ? 0.023   12.511  -5.84   0.5 8.812  ? 117 CYS   B SG   1 
ATOM   3304 S  SG   B CYS   B 1 117 ? 0.384   14.501  -5.357  0.5 21.435 ? 117 CYS   B SG   1 
ATOM   3305 N  N    . TYR   B 1 118 ? 3.043   15.772  -7.569  1   11.784 ? 118 TYR   B N    1 
ATOM   3306 C  CA   . TYR   B 1 118 ? 4.019   16.846  -7.465  1   12.171 ? 118 TYR   B CA   1 
ATOM   3307 C  C    . TYR   B 1 118 ? 3.317   18.055  -6.861  1   13.002 ? 118 TYR   B C    1 
ATOM   3308 O  O    . TYR   B 1 118 ? 2.207   18.371  -7.271  1   13.257 ? 118 TYR   B O    1 
ATOM   3309 C  CB   . TYR   B 1 118 ? 4.599   17.199  -8.85   1   12.649 ? 118 TYR   B CB   1 
ATOM   3310 C  CG   . TYR   B 1 118 ? 5.32    16.007  -9.452  1   12.671 ? 118 TYR   B CG   1 
ATOM   3311 C  CD1  . TYR   B 1 118 ? 6.668   15.803  -9.19   1   12.424 ? 118 TYR   B CD1  1 
ATOM   3312 C  CD2  . TYR   B 1 118 ? 4.648   15.045  -10.195 1   12.693 ? 118 TYR   B CD2  1 
ATOM   3313 C  CE1  . TYR   B 1 118 ? 7.337   14.689  -9.664  1   12.538 ? 118 TYR   B CE1  1 
ATOM   3314 C  CE2  . TYR   B 1 118 ? 5.291   13.911  -10.66  1   12.726 ? 118 TYR   B CE2  1 
ATOM   3315 C  CZ   . TYR   B 1 118 ? 6.647   13.749  -10.408 1   12.511 ? 118 TYR   B CZ   1 
ATOM   3316 O  OH   . TYR   B 1 118 ? 7.302   12.642  -10.83  1   12.854 ? 118 TYR   B OH   1 
ATOM   3317 N  N    . ASN   B 1 119 ? 3.94    18.693  -5.855  1   14.427 ? 119 ASN   B N    1 
ATOM   3318 C  CA   . ASN   B 1 119 ? 3.381   19.892  -5.243  1   16.004 ? 119 ASN   B CA   1 
ATOM   3319 C  C    . ASN   B 1 119 ? 1.989   19.616  -4.675  1   15.239 ? 119 ASN   B C    1 
ATOM   3320 O  O    . ASN   B 1 119 ? 1.133   20.496  -4.676  1   16.507 ? 119 ASN   B O    1 
ATOM   3321 C  CB   . ASN   B 1 119 ? 3.325   21.052  -6.238  1   18.97  ? 119 ASN   B CB   1 
ATOM   3322 C  CG   . ASN   B 1 119 ? 4.709   21.484  -6.646  1   24.168 ? 119 ASN   B CG   1 
ATOM   3323 O  OD1  . ASN   B 1 119 ? 5.529   21.804  -5.781  1   30.878 ? 119 ASN   B OD1  1 
ATOM   3324 N  ND2  . ASN   B 1 119 ? 4.991   21.477  -7.937  1   28.455 ? 119 ASN   B ND2  1 
ATOM   3325 N  N    . GLY   B 1 120 ? 1.766   18.383  -4.209  1   13.707 ? 120 GLY   B N    1 
ATOM   3326 C  CA   . GLY   B 1 120 ? 0.493   17.975  -3.636  1   13.826 ? 120 GLY   B CA   1 
ATOM   3327 C  C    . GLY   B 1 120 ? -0.613  17.704  -4.656  1   15.213 ? 120 GLY   B C    1 
ATOM   3328 O  O    . GLY   B 1 120 ? -1.734  17.395  -4.262  1   17.204 ? 120 GLY   B O    1 
ATOM   3329 N  N    . SER   B 1 121 ? -0.278  17.771  -5.946  1   15.039 ? 121 SER   B N    1 
ATOM   3330 C  CA   . SER   B 1 121 ? -1.248  17.628  -7.021  1   16.242 ? 121 SER   B CA   1 
ATOM   3331 C  C    . SER   B 1 121 ? -1.005  16.322  -7.768  1   15.036 ? 121 SER   B C    1 
ATOM   3332 O  O    . SER   B 1 121 ? 0.086   16.091  -8.313  1   15.055 ? 121 SER   B O    1 
ATOM   3333 C  CB   . SER   B 1 121 ? -1.205  18.822  -7.93   1   18.471 ? 121 SER   B CB   1 
ATOM   3334 O  OG   . SER   B 1 121 ? -2.158  18.684  -8.967  1   24.357 ? 121 SER   B OG   1 
ATOM   3335 N  N    . PRO   B 1 122 ? -1.992  15.399  -7.793  1   14.543 ? 122 PRO   B N    1 
ATOM   3336 C  CA   . PRO   B 1 122 ? -1.856  14.165  -8.571  1   14.526 ? 122 PRO   B CA   1 
ATOM   3337 C  C    . PRO   B 1 122 ? -1.615  14.414  -10.057 1   14.498 ? 122 PRO   B C    1 
ATOM   3338 O  O    . PRO   B 1 122 ? -2.297  15.233  -10.672 1   15.842 ? 122 PRO   B O    1 
ATOM   3339 C  CB   . PRO   B 1 122 ? -3.171  13.457  -8.316  1   14.875 ? 122 PRO   B CB   1 
ATOM   3340 C  CG   . PRO   B 1 122 ? -3.587  13.95   -6.95   1   15.528 ? 122 PRO   B CG   1 
ATOM   3341 C  CD   . PRO   B 1 122 ? -3.222  15.423  -6.979  1   15.268 ? 122 PRO   B CD   1 
ATOM   3342 N  N    . SER   B 1 123 ? -0.641  13.694  -10.615 1   13.817 ? 123 SER   B N    1 
ATOM   3343 C  CA   . SER   B 1 123 ? -0.133  13.96   -11.955 1   14.292 ? 123 SER   B CA   1 
ATOM   3344 C  C    . SER   B 1 123 ? -0.377  12.775  -12.881 1   12.644 ? 123 SER   B C    1 
ATOM   3345 O  O    . SER   B 1 123 ? -0.616  12.958  -14.082 1   12.981 ? 123 SER   B O    1 
ATOM   3346 C  CB   . SER   B 1 123 ? 1.343   14.314  -11.85  1   17.592 ? 123 SER   B CB   1 
ATOM   3347 O  OG   . SER   B 1 123 ? 1.972   14.469  -13.111 1   24.098 ? 123 SER   B OG   1 
ATOM   3348 N  N    . GLY   B 1 124 ? -0.266  11.559  -12.354 1   11.193 ? 124 GLY   B N    1 
ATOM   3349 C  CA   . GLY   B 1 124 ? -0.379  10.368  -13.166 1   11.558 ? 124 GLY   B CA   1 
ATOM   3350 C  C    . GLY   B 1 124 ? -0.603  9.13    -12.319 1   10.511 ? 124 GLY   B C    1 
ATOM   3351 O  O    . GLY   B 1 124 ? -0.346  9.141   -11.123 1   11.021 ? 124 GLY   B O    1 
ATOM   3352 N  N    . VAL   B 1 125 ? -1.087  8.065   -12.946 1   10.878 ? 125 VAL   B N    1 
ATOM   3353 C  CA   . VAL   B 1 125 ? -1.317  6.806   -12.271 1   11.495 ? 125 VAL   B CA   1 
ATOM   3354 C  C    . VAL   B 1 125 ? -0.769  5.691   -13.143 1   11.059 ? 125 VAL   B C    1 
ATOM   3355 O  O    . VAL   B 1 125 ? -0.917  5.717   -14.371 1   12.168 ? 125 VAL   B O    1 
ATOM   3356 C  CB   . VAL   B 1 125 ? -2.794  6.603   -11.865 1   14.168 ? 125 VAL   B CB   1 
ATOM   3357 C  CG1  . VAL   B 1 125 ? -3.752  6.539   -13.038 1   15.77  ? 125 VAL   B CG1  1 
ATOM   3358 C  CG2  . VAL   B 1 125 ? -2.959  5.4     -10.946 1   14.514 ? 125 VAL   B CG2  1 
ATOM   3359 N  N    . TYR   B 1 126 ? -0.106  4.719   -12.514 1   10.774 ? 126 TYR   B N    1 
ATOM   3360 C  CA   . TYR   B 1 126 ? 0.39    3.552   -13.218 1   11.396 ? 126 TYR   B CA   1 
ATOM   3361 C  C    . TYR   B 1 126 ? 0.501   2.38    -12.256 1   11.231 ? 126 TYR   B C    1 
ATOM   3362 O  O    . TYR   B 1 126 ? 0.488   2.544   -11.052 1   11.947 ? 126 TYR   B O    1 
ATOM   3363 C  CB   . TYR   B 1 126 ? 1.737   3.791   -13.906 1   12.302 ? 126 TYR   B CB   1 
ATOM   3364 C  CG   . TYR   B 1 126 ? 2.81    4.369   -13.007 1   12.771 ? 126 TYR   B CG   1 
ATOM   3365 C  CD1  . TYR   B 1 126 ? 3.64    3.556   -12.241 1   13.292 ? 126 TYR   B CD1  1 
ATOM   3366 C  CD2  . TYR   B 1 126 ? 3.003   5.74    -12.948 1   14.864 ? 126 TYR   B CD2  1 
ATOM   3367 C  CE1  . TYR   B 1 126 ? 4.606   4.11    -11.417 1   13.801 ? 126 TYR   B CE1  1 
ATOM   3368 C  CE2  . TYR   B 1 126 ? 3.974   6.3     -12.142 1   15.193 ? 126 TYR   B CE2  1 
ATOM   3369 C  CZ   . TYR   B 1 126 ? 4.769   5.481   -11.371 1   14.524 ? 126 TYR   B CZ   1 
ATOM   3370 O  OH   . TYR   B 1 126 ? 5.744   6.036   -10.603 1   17.297 ? 126 TYR   B OH   1 
ATOM   3371 N  N    . GLN   B 1 127 ? 0.641   1.194   -12.814 1   12.711 ? 127 GLN   B N    1 
ATOM   3372 C  CA   . GLN   B 1 127 ? 0.762   -0.029  -12.064 1   13.657 ? 127 GLN   B CA   1 
ATOM   3373 C  C    . GLN   B 1 127 ? 2.236   -0.412  -11.934 1   14.472 ? 127 GLN   B C    1 
ATOM   3374 O  O    . GLN   B 1 127 ? 2.997   -0.309  -12.897 1   15.599 ? 127 GLN   B O    1 
ATOM   3375 C  CB   . GLN   B 1 127 ? -0.088  -0.994  -12.874 1   15.544 ? 127 GLN   B CB   1 
ATOM   3376 C  CG   . GLN   B 1 127 ? -0.422  -2.278  -12.154 1   17.188 ? 127 GLN   B CG   1 
ATOM   3377 C  CD   . GLN   B 1 127 ? -1.448  -2.105  -11.055 1   16.759 ? 127 GLN   B CD   1 
ATOM   3378 O  OE1  . GLN   B 1 127 ? -1.876  -1.003  -10.659 1   16.384 ? 127 GLN   B OE1  1 
ATOM   3379 N  NE2  . GLN   B 1 127 ? -1.804  -3.25   -10.505 1   17.535 ? 127 GLN   B NE2  1 
ATOM   3380 N  N    . CYS   B 1 128 ? 2.59    -0.913  -10.743 1   15.143 ? 128 CYS   B N    1 
ATOM   3381 C  CA   . CYS   B 1 128 ? 3.94    -1.331  -10.365 1   16.239 ? 128 CYS   B CA   1 
ATOM   3382 C  C    . CYS   B 1 128 ? 3.861   -2.692  -9.673  1   14.503 ? 128 CYS   B C    1 
ATOM   3383 O  O    . CYS   B 1 128 ? 2.811   -3.086  -9.205  1   17.234 ? 128 CYS   B O    1 
ATOM   3384 C  CB   . CYS   B 1 128 ? 4.594   -0.365  -9.353  1   18.427 ? 128 CYS   B CB   1 
ATOM   3385 S  SG   . CYS   B 1 128 ? 5.435   0.999   -10.188 1   27.986 ? 128 CYS   B SG   1 
ATOM   3386 N  N    . ALA   B 1 129 ? 4.975   -3.414  -9.593  1   14.438 ? 129 ALA   B N    1 
ATOM   3387 C  CA   . ALA   B 1 129 ? 5.117   -4.547  -8.69   1   14.025 ? 129 ALA   B CA   1 
ATOM   3388 C  C    . ALA   B 1 129 ? 6.245   -4.252  -7.711  1   13.41  ? 129 ALA   B C    1 
ATOM   3389 O  O    . ALA   B 1 129 ? 7.234   -3.606  -8.053  1   14.082 ? 129 ALA   B O    1 
ATOM   3390 C  CB   . ALA   B 1 129 ? 5.401   -5.826  -9.434  1   14.565 ? 129 ALA   B CB   1 
ATOM   3391 N  N    . MET   B 1 130 ? 6.115   -4.795  -6.504  1   12.375 ? 130 MET   B N    1 
ATOM   3392 C  CA   . MET   B 1 130 ? 7.255   -4.865  -5.612  1   12.487 ? 130 MET   B CA   1 
ATOM   3393 C  C    . MET   B 1 130 ? 8.193   -5.944  -6.147  1   11.435 ? 130 MET   B C    1 
ATOM   3394 O  O    . MET   B 1 130 ? 7.828   -7.115  -6.245  1   12.4   ? 130 MET   B O    1 
ATOM   3395 C  CB   . MET   B 1 130 ? 6.793   -5.201  -4.193  1   13.324 ? 130 MET   B CB   1 
ATOM   3396 C  CG   . MET   B 1 130 ? 7.903   -5.288  -3.17   1   14.281 ? 130 MET   B CG   1 
ATOM   3397 S  SD   . MET   B 1 130 ? 8.839   -3.763  -2.946  1   15.583 ? 130 MET   B SD   1 
ATOM   3398 C  CE   . MET   B 1 130 ? 7.559   -2.601  -2.441  1   14.973 ? 130 MET   B CE   1 
ATOM   3399 N  N    . ARG   B 1 131 ? 9.392   -5.542  -6.572  1   11.613 ? 131 ARG   B N    1 
ATOM   3400 C  CA   . ARG   B 1 131 ? 10.326  -6.498  -7.148  1   11.541 ? 131 ARG   B CA   1 
ATOM   3401 C  C    . ARG   B 1 131 ? 10.866  -7.434  -6.067  1   11.046 ? 131 ARG   B C    1 
ATOM   3402 O  O    . ARG   B 1 131 ? 10.893  -7.078  -4.877  1   10.748 ? 131 ARG   B O    1 
ATOM   3403 C  CB   . ARG   B 1 131 ? 11.492  -5.765  -7.814  1   11.903 ? 131 ARG   B CB   1 
ATOM   3404 C  CG   . ARG   B 1 131 ? 11.112  -4.792  -8.925  1   12.027 ? 131 ARG   B CG   1 
ATOM   3405 C  CD   . ARG   B 1 131 ? 10.293  -5.411  -10.029 1   12.452 ? 131 ARG   B CD   1 
ATOM   3406 N  NE   . ARG   B 1 131 ? 10.906  -6.638  -10.551 1   12.355 ? 131 ARG   B NE   1 
ATOM   3407 C  CZ   . ARG   B 1 131 ? 10.321  -7.474  -11.393 1   12.738 ? 131 ARG   B CZ   1 
ATOM   3408 N  NH1  . ARG   B 1 131 ? 9.133   -7.174  -11.896 1   12.773 ? 131 ARG   B NH1  1 
ATOM   3409 N  NH2  . ARG   B 1 131 ? 10.921  -8.609  -11.716 1   13.308 ? 131 ARG   B NH2  1 
ATOM   3410 N  N    . PRO   B 1 132 ? 11.369  -8.633  -6.43   1   11.356 ? 132 PRO   B N    1 
ATOM   3411 C  CA   . PRO   B 1 132 ? 12.072  -9.486  -5.468  1   11.731 ? 132 PRO   B CA   1 
ATOM   3412 C  C    . PRO   B 1 132 ? 13.207  -8.802  -4.709  1   11.096 ? 132 PRO   B C    1 
ATOM   3413 O  O    . PRO   B 1 132 ? 13.458  -9.152  -3.561  1   12.274 ? 132 PRO   B O    1 
ATOM   3414 C  CB   . PRO   B 1 132 ? 12.544  -10.638 -6.349  1   12.234 ? 132 PRO   B CB   1 
ATOM   3415 C  CG   . PRO   B 1 132 ? 11.465  -10.729 -7.418  1   12.701 ? 132 PRO   B CG   1 
ATOM   3416 C  CD   . PRO   B 1 132 ? 11.183  -9.281  -7.744  1   11.9   ? 132 PRO   B CD   1 
ATOM   3417 N  N    . ASN   B 1 133 ? 13.842  -7.788  -5.309  1   11.382 ? 133 ASN   B N    1 
ATOM   3418 C  CA   . ASN   B 1 133 ? 14.917  -7.052  -4.654  1   11.288 ? 133 ASN   B CA   1 
ATOM   3419 C  C    . ASN   B 1 133 ? 14.401  -5.842  -3.871  1   11.238 ? 133 ASN   B C    1 
ATOM   3420 O  O    . ASN   B 1 133 ? 15.182  -4.987  -3.461  1   12.105 ? 133 ASN   B O    1 
ATOM   3421 C  CB   . ASN   B 1 133 ? 16.015  -6.666  -5.641  1   11.673 ? 133 ASN   B CB   1 
ATOM   3422 C  CG   . ASN   B 1 133 ? 15.607  -5.596  -6.625  1   11.832 ? 133 ASN   B CG   1 
ATOM   3423 O  OD1  . ASN   B 1 133 ? 14.471  -5.108  -6.608  1   11.599 ? 133 ASN   B OD1  1 
ATOM   3424 N  ND2  . ASN   B 1 133 ? 16.52   -5.212  -7.509  1   12.724 ? 133 ASN   B ND2  1 
ATOM   3425 N  N    . PHE   B 1 134 ? 13.077  -5.751  -3.716  1   10.979 ? 134 PHE   B N    1 
ATOM   3426 C  CA   . PHE   B 1 134 ? 12.414  -4.751  -2.891  1   11.336 ? 134 PHE   B CA   1 
ATOM   3427 C  C    . PHE   B 1 134 ? 12.532  -3.332  -3.434  1   11.939 ? 134 PHE   B C    1 
ATOM   3428 O  O    . PHE   B 1 134 ? 12.351  -2.375  -2.7    1   14.763 ? 134 PHE   B O    1 
ATOM   3429 C  CB   . PHE   B 1 134 ? 12.919  -4.791  -1.45   1   11.809 ? 134 PHE   B CB   1 
ATOM   3430 C  CG   . PHE   B 1 134 ? 12.434  -6.007  -0.689  1   13.111 ? 134 PHE   B CG   1 
ATOM   3431 C  CD1  . PHE   B 1 134 ? 11.102  -6.084  -0.287  1   14.057 ? 134 PHE   B CD1  1 
ATOM   3432 C  CD2  . PHE   B 1 134 ? 13.297  -7.029  -0.31   1   14.573 ? 134 PHE   B CD2  1 
ATOM   3433 C  CE1  . PHE   B 1 134 ? 10.647  -7.16   0.458   1   15.502 ? 134 PHE   B CE1  1 
ATOM   3434 C  CE2  . PHE   B 1 134 ? 12.831  -8.105  0.435   1   15.391 ? 134 PHE   B CE2  1 
ATOM   3435 C  CZ   . PHE   B 1 134 ? 11.509  -8.162  0.816   1   15.728 ? 134 PHE   B CZ   1 
ATOM   3436 N  N    . THR   B 1 135 ? 12.81   -3.186  -4.73   1   11.161 ? 135 THR   B N    1 
ATOM   3437 C  CA   . THR   B 1 135 ? 12.661  -1.905  -5.398  1   11.531 ? 135 THR   B CA   1 
ATOM   3438 C  C    . THR   B 1 135 ? 11.359  -1.938  -6.192  1   11.09  ? 135 THR   B C    1 
ATOM   3439 O  O    . THR   B 1 135 ? 10.754  -2.998  -6.357  1   11.713 ? 135 THR   B O    1 
ATOM   3440 C  CB   . THR   B 1 135 ? 13.865  -1.622  -6.298  1   12.245 ? 135 THR   B CB   1 
ATOM   3441 O  OG1  . THR   B 1 135 ? 13.879  -2.561  -7.372  1   12.349 ? 135 THR   B OG1  1 
ATOM   3442 C  CG2  . THR   B 1 135 ? 15.164  -1.67   -5.507  1   13.039 ? 135 THR   B CG2  1 
ATOM   3443 N  N    . ILE   B 1 136 ? 10.978  -0.772  -6.708  1   11.445 ? 136 ILE   B N    1 
ATOM   3444 C  CA   . ILE   B 1 136 ? 9.942   -0.739  -7.724  1   11.929 ? 136 ILE   B CA   1 
ATOM   3445 C  C    . ILE   B 1 136 ? 10.508  -0.016  -8.939  1   11.786 ? 136 ILE   B C    1 
ATOM   3446 O  O    . ILE   B 1 136 ? 11.311  0.896   -8.824  1   11.739 ? 136 ILE   B O    1 
ATOM   3447 C  CB   . ILE   B 1 136 ? 8.621   -0.121  -7.227  1   14.368 ? 136 ILE   B CB   1 
ATOM   3448 C  CG1  . ILE   B 1 136 ? 8.703   1.386   -7.002  1   14.408 ? 136 ILE   B CG1  1 
ATOM   3449 C  CG2  . ILE   B 1 136 ? 8.126   -0.861  -5.983  1   15.919 ? 136 ILE   B CG2  1 
ATOM   3450 C  CD1  . ILE   B 1 136 ? 7.362   2.035   -6.685  1   14.661 ? 136 ILE   B CD1  1 
ATOM   3451 N  N    . LYS   B 1 137 ? 10.051  -0.442  -10.109 1   12.435 ? 137 LYS   B N    1 
ATOM   3452 C  CA   . LYS   B 1 137 ? 10.426  0.215   -11.345 1   13.257 ? 137 LYS   B CA   1 
ATOM   3453 C  C    . LYS   B 1 137 ? 9.363   1.261   -11.622 1   12.882 ? 137 LYS   B C    1 
ATOM   3454 O  O    . LYS   B 1 137 ? 8.424   1.032   -12.376 1   13.886 ? 137 LYS   B O    1 
ATOM   3455 C  CB   . LYS   B 1 137 ? 10.556  -0.823  -12.458 1   15.054 ? 137 LYS   B CB   1 
ATOM   3456 C  CG   . LYS   B 1 137 ? 11.619  -1.867  -12.215 1   17.544 ? 137 LYS   B CG   1 
ATOM   3457 C  CD   . LYS   B 1 137 ? 11.782  -2.788  -13.418 1   20.869 ? 137 LYS   B CD   1 
ATOM   3458 C  CE   . LYS   B 1 137 ? 12.54   -4.014  -13.097 1   24.831 ? 137 LYS   B CE   1 
ATOM   3459 N  NZ   . LYS   B 1 137 ? 12.837  -4.757  -14.32  1   27.721 ? 137 LYS   B NZ   1 
ATOM   3460 N  N    . GLY   B 1 138 ? 9.491   2.398   -10.946 1   11.977 ? 138 GLY   B N    1 
ATOM   3461 C  CA   . GLY   B 1 138 ? 8.492   3.44    -11.059 1   12.534 ? 138 GLY   B CA   1 
ATOM   3462 C  C    . GLY   B 1 138 ? 8.882   4.438   -12.141 1   11.498 ? 138 GLY   B C    1 
ATOM   3463 O  O    . GLY   B 1 138 ? 9.816   4.216   -12.924 1   12.839 ? 138 GLY   B O    1 
ATOM   3464 N  N    . SER   B 1 139 ? 8.155   5.545   -12.147 1   10.636 ? 139 SER   B N    1 
ATOM   3465 C  CA   . SER   B 1 139 ? 8.445   6.693   -12.98  1   10.923 ? 139 SER   B CA   1 
ATOM   3466 C  C    . SER   B 1 139 ? 8.23    7.931   -12.125 1   10.703 ? 139 SER   B C    1 
ATOM   3467 O  O    . SER   B 1 139 ? 7.097   8.267   -11.82  1   11.308 ? 139 SER   B O    1 
ATOM   3468 C  CB   . SER   B 1 139 ? 7.588   6.712   -14.195 1   11.472 ? 139 SER   B CB   1 
ATOM   3469 O  OG   . SER   B 1 139 ? 7.927   7.858   -14.957 1   12.524 ? 139 SER   B OG   1 
ATOM   3470 N  N    . PHE   B 1 140 ? 9.332   8.496   -11.639 1   10.809 ? 140 PHE   B N    1 
ATOM   3471 C  CA   . PHE   B 1 140 ? 9.314   9.562   -10.661 1   11.204 ? 140 PHE   B CA   1 
ATOM   3472 C  C    . PHE   B 1 140 ? 10.418  10.563  -10.94  1   11.245 ? 140 PHE   B C    1 
ATOM   3473 O  O    . PHE   B 1 140 ? 11.54   10.164  -11.283 1   12.691 ? 140 PHE   B O    1 
ATOM   3474 C  CB   . PHE   B 1 140 ? 9.569   9.011   -9.266  1   11.294 ? 140 PHE   B CB   1 
ATOM   3475 C  CG   . PHE   B 1 140 ? 8.485   8.144   -8.652  1   11.465 ? 140 PHE   B CG   1 
ATOM   3476 C  CD1  . PHE   B 1 140 ? 7.23    8.67    -8.347  1   12.61  ? 140 PHE   B CD1  1 
ATOM   3477 C  CD2  . PHE   B 1 140 ? 8.745   6.821   -8.333  1   12.399 ? 140 PHE   B CD2  1 
ATOM   3478 C  CE1  . PHE   B 1 140 ? 6.278   7.897   -7.708  1   12.94  ? 140 PHE   B CE1  1 
ATOM   3479 C  CE2  . PHE   B 1 140 ? 7.791   6.061   -7.662  1   13.367 ? 140 PHE   B CE2  1 
ATOM   3480 C  CZ   . PHE   B 1 140 ? 6.567   6.598   -7.368  1   13.343 ? 140 PHE   B CZ   1 
ATOM   3481 N  N    . LEU   B 1 141 ? 10.079  11.846  -10.78  1   11.94  ? 141 LEU   B N    1 
ATOM   3482 C  CA   . LEU   B 1 141 ? 11.022  12.939  -10.932 1   12.308 ? 141 LEU   B CA   1 
ATOM   3483 C  C    . LEU   B 1 141 ? 11.182  13.657  -9.597  1   12.079 ? 141 LEU   B C    1 
ATOM   3484 O  O    . LEU   B 1 141 ? 10.484  13.38   -8.62   1   11.407 ? 141 LEU   B O    1 
ATOM   3485 C  CB   . LEU   B 1 141 ? 10.527  13.908  -12.007 1   13.402 ? 141 LEU   B CB   1 
ATOM   3486 C  CG   . LEU   B 1 141 ? 10.335  13.309  -13.405 1   14.68  ? 141 LEU   B CG   1 
ATOM   3487 C  CD1  . LEU   B 1 141 ? 9.761   14.385  -14.307 1   16     ? 141 LEU   B CD1  1 
ATOM   3488 C  CD2  . LEU   B 1 141 ? 11.608  12.704  -13.984 1   15.884 ? 141 LEU   B CD2  1 
ATOM   3489 N  N    . ASN   B 1 142 ? 12.1    14.621  -9.574  1   12.927 ? 142 ASN   B N    1 
ATOM   3490 C  CA   . ASN   B 1 142 ? 12.235  15.522  -8.449  1   14.139 ? 142 ASN   B CA   1 
ATOM   3491 C  C    . ASN   B 1 142 ? 10.869  16.084  -8.051  1   13.443 ? 142 ASN   B C    1 
ATOM   3492 O  O    . ASN   B 1 142 ? 10.112  16.556  -8.899  1   14.128 ? 142 ASN   B O    1 
ATOM   3493 C  CB   . ASN   B 1 142 ? 13.212  16.633  -8.803  1   17.138 ? 142 ASN   B CB   1 
ATOM   3494 C  CG   . ASN   B 1 142 ? 13.424  17.603  -7.671  1   21.401 ? 142 ASN   B CG   1 
ATOM   3495 O  OD1  . ASN   B 1 142 ? 13.667  17.178  -6.54   1   25.483 ? 142 ASN   B OD1  1 
ATOM   3496 N  ND2  . ASN   B 1 142 ? 13.35   18.894  -7.957  1   25.515 ? 142 ASN   B ND2  1 
ATOM   3497 N  N    . GLY   B 1 143 ? 10.551  16.012  -6.749  1   12.744 ? 143 GLY   B N    1 
ATOM   3498 C  CA   . GLY   B 1 143 ? 9.296   16.529  -6.214  1   12.335 ? 143 GLY   B CA   1 
ATOM   3499 C  C    . GLY   B 1 143 ? 8.241   15.448  -5.962  1   11.657 ? 143 GLY   B C    1 
ATOM   3500 O  O    . GLY   B 1 143 ? 7.168   15.742  -5.413  1   12.702 ? 143 GLY   B O    1 
ATOM   3501 N  N    . SER   B 1 144 ? 8.549   14.194  -6.301  1   10.766 ? 144 SER   B N    1 
ATOM   3502 C  CA   . SER   B 1 144 ? 7.585   13.108  -6.22   1   10.468 ? 144 SER   B CA   1 
ATOM   3503 C  C    . SER   B 1 144 ? 7.548   12.42   -4.858  1   10.083 ? 144 SER   B C    1 
ATOM   3504 O  O    . SER   B 1 144 ? 6.729   11.531  -4.654  1   10.003 ? 144 SER   B O    1 
ATOM   3505 C  CB   . SER   B 1 144 ? 7.847   12.081  -7.282  1   10.837 ? 144 SER   B CB   1 
ATOM   3506 O  OG   . SER   B 1 144 ? 9.139   11.511  -7.131  1   11.438 ? 144 SER   B OG   1 
ATOM   3507 N  N    . CYS   B 1 145 ? 8.463   12.769  -3.945  1   10.081 ? 145 CYS   B N    1 
ATOM   3508 C  CA   . CYS   B 1 145 ? 8.482   12.084  -2.661  1   10.482 ? 145 CYS   B CA   1 
ATOM   3509 C  C    . CYS   B 1 145 ? 7.151   12.271  -1.938  1   10.05  ? 145 CYS   B C    1 
ATOM   3510 O  O    . CYS   B 1 145 ? 6.523   13.329  -2.011  1   10.463 ? 145 CYS   B O    1 
ATOM   3511 C  CB   . CYS   B 1 145 ? 9.635   12.549  -1.789  1   11.181 ? 145 CYS   B CB   1 
ATOM   3512 S  SG   . CYS   B 1 145 ? 11.257  12.229  -2.535  1   13.612 ? 145 CYS   B SG   1 
ATOM   3513 N  N    . GLY   B 1 146 ? 6.711   11.197  -1.288  1   9.156  ? 146 GLY   B N    1 
ATOM   3514 C  CA   . GLY   B 1 146 ? 5.428   11.196  -0.609  1   9.582  ? 146 GLY   B CA   1 
ATOM   3515 C  C    . GLY   B 1 146 ? 4.285   10.713  -1.499  1   9.631  ? 146 GLY   B C    1 
ATOM   3516 O  O    . GLY   B 1 146 ? 3.176   10.526  -1.015  1   10.72  ? 146 GLY   B O    1 
ATOM   3517 N  N    . SER   B 1 147 ? 4.553   10.506  -2.796  1   9.56   ? 147 SER   B N    1 
ATOM   3518 C  CA   . SER   B 1 147 ? 3.602   9.807   -3.647  1   9.575  ? 147 SER   B CA   1 
ATOM   3519 C  C    . SER   B 1 147 ? 3.331   8.43    -3.053  1   9.676  ? 147 SER   B C    1 
ATOM   3520 O  O    . SER   B 1 147 ? 4.223   7.841   -2.448  1   10.427 ? 147 SER   B O    1 
ATOM   3521 C  CB   . SER   B 1 147 ? 4.108   9.66    -5.075  1   9.721  ? 147 SER   B CB   1 
ATOM   3522 O  OG   . SER   B 1 147 ? 4.28    10.917  -5.704  1   10.401 ? 147 SER   B OG   1 
ATOM   3523 N  N    . VAL   B 1 148 ? 2.123   7.896   -3.245  1   10.141 ? 148 VAL   B N    1 
ATOM   3524 C  CA   . VAL   B 1 148 ? 1.76    6.646   -2.609  1   10.512 ? 148 VAL   B CA   1 
ATOM   3525 C  C    . VAL   B 1 148 ? 1.316   5.582   -3.604  1   10.248 ? 148 VAL   B C    1 
ATOM   3526 O  O    . VAL   B 1 148 ? 0.866   5.849   -4.717  1   11.048 ? 148 VAL   B O    1 
ATOM   3527 C  CB   . VAL   B 1 148 ? 0.684   6.825   -1.527  1   11.677 ? 148 VAL   B CB   1 
ATOM   3528 C  CG1  . VAL   B 1 148 ? 1.185   7.723   -0.405  1   12.004 ? 148 VAL   B CG1  1 
ATOM   3529 C  CG2  . VAL   B 1 148 ? -0.634  7.33    -2.084  1   13.04  ? 148 VAL   B CG2  1 
ATOM   3530 N  N    . GLY   B 1 149 ? 1.451   4.349   -3.135  1   10.052 ? 149 GLY   B N    1 
ATOM   3531 C  CA   . GLY   B 1 149 ? 0.964   3.161   -3.799  1   10.209 ? 149 GLY   B CA   1 
ATOM   3532 C  C    . GLY   B 1 149 ? -0.153  2.505   -3.002  1   10     ? 149 GLY   B C    1 
ATOM   3533 O  O    . GLY   B 1 149 ? -0.139  2.545   -1.762  1   9.997  ? 149 GLY   B O    1 
ATOM   3534 N  N    . PHE   B 1 150 ? -1.09   1.875   -3.714  1   10.149 ? 150 PHE   B N    1 
ATOM   3535 C  CA   . PHE   B 1 150 ? -2.279  1.342   -3.079  1   10.562 ? 150 PHE   B CA   1 
ATOM   3536 C  C    . PHE   B 1 150 ? -2.929  0.264   -3.939  1   10.987 ? 150 PHE   B C    1 
ATOM   3537 O  O    . PHE   B 1 150 ? -2.691  0.182   -5.149  1   10.58  ? 150 PHE   B O    1 
ATOM   3538 C  CB   . PHE   B 1 150 ? -3.267  2.489   -2.833  1   11.419 ? 150 PHE   B CB   1 
ATOM   3539 C  CG   . PHE   B 1 150 ? -3.789  3.125   -4.111  1   12.565 ? 150 PHE   B CG   1 
ATOM   3540 C  CD1  . PHE   B 1 150 ? -3.043  4.074   -4.799  1   13.196 ? 150 PHE   B CD1  1 
ATOM   3541 C  CD2  . PHE   B 1 150 ? -5.006  2.727   -4.648  1   13.425 ? 150 PHE   B CD2  1 
ATOM   3542 C  CE1  . PHE   B 1 150 ? -3.512  4.61    -5.989  1   14.034 ? 150 PHE   B CE1  1 
ATOM   3543 C  CE2  . PHE   B 1 150 ? -5.474  3.27    -5.834  1   14.205 ? 150 PHE   B CE2  1 
ATOM   3544 C  CZ   . PHE   B 1 150 ? -4.724  4.203   -6.498  1   14.517 ? 150 PHE   B CZ   1 
ATOM   3545 N  N    . ASN   B 1 151 ? -3.797  -0.501  -3.274  1   10.935 ? 151 ASN   B N    1 
ATOM   3546 C  CA   . ASN   B 1 151 ? -4.751  -1.387  -3.906  1   12.08  ? 151 ASN   B CA   1 
ATOM   3547 C  C    . ASN   B 1 151 ? -6.137  -1.019  -3.378  1   12.363 ? 151 ASN   B C    1 
ATOM   3548 O  O    . ASN   B 1 151 ? -6.255  -0.373  -2.34   1   12.905 ? 151 ASN   B O    1 
ATOM   3549 C  CB   . ASN   B 1 151 ? -4.404  -2.84   -3.6    1   13.372 ? 151 ASN   B CB   1 
ATOM   3550 C  CG   . ASN   B 1 151 ? -3.193  -3.312  -4.364  1   15.407 ? 151 ASN   B CG   1 
ATOM   3551 O  OD1  . ASN   B 1 151 ? -3.303  -3.573  -5.556  1   19.031 ? 151 ASN   B OD1  1 
ATOM   3552 N  ND2  . ASN   B 1 151 ? -2.048  -3.463  -3.727  1   15.885 ? 151 ASN   B ND2  1 
ATOM   3553 N  N    . ILE   B 1 152 ? -7.191  -1.444  -4.08   1   12.759 ? 152 ILE   B N    1 
ATOM   3554 C  CA   . ILE   B 1 152 ? -8.552  -1.308  -3.581  1   15.149 ? 152 ILE   B CA   1 
ATOM   3555 C  C    . ILE   B 1 152 ? -9.228  -2.676  -3.548  1   18.313 ? 152 ILE   B C    1 
ATOM   3556 O  O    . ILE   B 1 152 ? -9.052  -3.492  -4.441  1   20.054 ? 152 ILE   B O    1 
ATOM   3557 C  CB   . ILE   B 1 152 ? -9.364  -0.311  -4.428  1   17.191 ? 152 ILE   B CB   1 
ATOM   3558 C  CG1  . ILE   B 1 152 ? -8.621  1.016   -4.628  1   18.345 ? 152 ILE   B CG1  1 
ATOM   3559 C  CG2  . ILE   B 1 152 ? -10.75  -0.106  -3.801  1   18.76  ? 152 ILE   B CG2  1 
ATOM   3560 C  CD1  . ILE   B 1 152 ? -9.332  2.034   -5.507  1   20.849 ? 152 ILE   B CD1  1 
ATOM   3561 N  N    . ASP   B 1 153 ? -10.053 -2.878  -2.516  1   22.182 ? 153 ASP   B N    1 
ATOM   3562 C  CA   . ASP   B 1 153 ? -10.973 -3.997  -2.418  1   26.093 ? 153 ASP   B CA   1 
ATOM   3563 C  C    . ASP   B 1 153 ? -12.34  -3.443  -2.038  1   27.172 ? 153 ASP   B C    1 
ATOM   3564 O  O    . ASP   B 1 153 ? -12.465 -2.833  -0.978  1   28.107 ? 153 ASP   B O    1 
ATOM   3565 C  CB   . ASP   B 1 153 ? -10.531 -4.953  -1.324  1   29.678 ? 153 ASP   B CB   1 
ATOM   3566 C  CG   . ASP   B 1 153 ? -9.139  -5.528  -1.524  1   34.115 ? 153 ASP   B CG   1 
ATOM   3567 O  OD1  . ASP   B 1 153 ? -8.996  -6.363  -2.433  1   38.11  ? 153 ASP   B OD1  1 
ATOM   3568 O  OD2  . ASP   B 1 153 ? -8.212  -5.128  -0.779  1   40.543 ? 153 ASP   B OD2  1 
ATOM   3569 N  N    . TYR   B 1 154 ? -13.337 -3.652  -2.908  1   30.217 ? 154 TYR   B N    1 
ATOM   3570 C  CA   . TYR   B 1 154 ? -14.663 -3.079  -2.755  1   32.434 ? 154 TYR   B CA   1 
ATOM   3571 C  C    . TYR   B 1 154 ? -14.531 -1.562  -2.6    1   33.961 ? 154 TYR   B C    1 
ATOM   3572 O  O    . TYR   B 1 154 ? -14.258 -0.858  -3.572  1   36.171 ? 154 TYR   B O    1 
ATOM   3573 C  CB   . TYR   B 1 154 ? -15.374 -3.821  -1.616  1   34.355 ? 154 TYR   B CB   1 
ATOM   3574 N  N    . ASP   B 1 155 ? -14.67  -1.08   -1.362  1   33.132 ? 155 ASP   B N    1 
ATOM   3575 C  CA   . ASP   B 1 155 ? -14.623 0.345   -1.068  1   31.812 ? 155 ASP   B CA   1 
ATOM   3576 C  C    . ASP   B 1 155 ? -13.416 0.688   -0.189  1   28.004 ? 155 ASP   B C    1 
ATOM   3577 O  O    . ASP   B 1 155 ? -13.291 1.84    0.236   1   29.095 ? 155 ASP   B O    1 
ATOM   3578 C  CB   . ASP   B 1 155 ? -15.91  0.781   -0.389  1   34.502 ? 155 ASP   B CB   1 
ATOM   3579 C  CG   . ASP   B 1 155 ? -16.275 0.001   0.866   1   37.679 ? 155 ASP   B CG   1 
ATOM   3580 O  OD1  . ASP   B 1 155 ? -15.604 -1.018  1.147   1   38.546 ? 155 ASP   B OD1  1 
ATOM   3581 O  OD2  . ASP   B 1 155 ? -17.237 0.412   1.547   1   41.48  ? 155 ASP   B OD2  1 
ATOM   3582 N  N    . CYS   B 1 156 ? -12.527 -0.286  0.07    1   22.484 ? 156 CYS   B N    1 
ATOM   3583 C  CA   . CYS   B 1 156 ? -11.46  -0.093  1.049   1   18.621 ? 156 CYS   B CA   1 
ATOM   3584 C  C    . CYS   B 1 156 ? -10.107 0.058   0.361   1   16.281 ? 156 CYS   B C    1 
ATOM   3585 O  O    . CYS   B 1 156 ? -9.674  -0.821  -0.383  1   16.943 ? 156 CYS   B O    1 
ATOM   3586 C  CB   . CYS   B 1 156 ? -11.358 -1.233  2.055   1   21.367 ? 156 CYS   B CB   1 
ATOM   3587 S  SG   . CYS   B 1 156 ? -10.074 -0.972  3.317   1   24.026 ? 156 CYS   B SG   1 
ATOM   3588 N  N    . VAL   B 1 157 ? -9.459  1.196   0.618   1   13.598 ? 157 VAL   B N    1 
ATOM   3589 C  CA   . VAL   B 1 157 ? -8.152  1.468   0.053   1   12.658 ? 157 VAL   B CA   1 
ATOM   3590 C  C    . VAL   B 1 157 ? -7.102  0.904   0.998   1   12.073 ? 157 VAL   B C    1 
ATOM   3591 O  O    . VAL   B 1 157 ? -7.016  1.317   2.153   1   14.171 ? 157 VAL   B O    1 
ATOM   3592 C  CB   . VAL   B 1 157 ? -7.921  2.968   -0.17   1   13.294 ? 157 VAL   B CB   1 
ATOM   3593 C  CG1  . VAL   B 1 157 ? -6.543  3.227   -0.77   1   13.336 ? 157 VAL   B CG1  1 
ATOM   3594 C  CG2  . VAL   B 1 157 ? -9.025  3.562   -1.036  1   14.077 ? 157 VAL   B CG2  1 
ATOM   3595 N  N    . SER   B 1 158 ? -6.27   0.008   0.474   1   11.439 ? 158 SER   B N    1 
ATOM   3596 C  CA   . SER   B 1 158 ? -5.13   -0.514  1.211   1   11.445 ? 158 SER   B CA   1 
ATOM   3597 C  C    . SER   B 1 158 ? -3.872  0.203   0.731   1   10.608 ? 158 SER   B C    1 
ATOM   3598 O  O    . SER   B 1 158 ? -3.396  -0.061  -0.371  1   11.998 ? 158 SER   B O    1 
ATOM   3599 C  CB   . SER   B 1 158 ? -4.997  -1.998  1.028   1   13.032 ? 158 SER   B CB   1 
ATOM   3600 O  OG   . SER   B 1 158 ? -6.029  -2.673  1.728   1   16.007 ? 158 SER   B OG   1 
ATOM   3601 N  N    . PHE   B 1 159 ? -3.337  1.111   1.55    1   10.291 ? 159 PHE   B N    1 
ATOM   3602 C  CA   . PHE   B 1 159 ? -2.126  1.835   1.216   1   10.408 ? 159 PHE   B CA   1 
ATOM   3603 C  C    . PHE   B 1 159 ? -0.925  0.963   1.556   1   10.492 ? 159 PHE   B C    1 
ATOM   3604 O  O    . PHE   B 1 159 ? -0.843  0.462   2.68    1   11.64  ? 159 PHE   B O    1 
ATOM   3605 C  CB   . PHE   B 1 159 ? -2.019  3.151   1.989   1   10.768 ? 159 PHE   B CB   1 
ATOM   3606 C  CG   . PHE   B 1 159 ? -3.072  4.172   1.603   1   10.925 ? 159 PHE   B CG   1 
ATOM   3607 C  CD1  . PHE   B 1 159 ? -2.921  4.945   0.462   1   11.116 ? 159 PHE   B CD1  1 
ATOM   3608 C  CD2  . PHE   B 1 159 ? -4.217  4.34    2.369   1   11.466 ? 159 PHE   B CD2  1 
ATOM   3609 C  CE1  . PHE   B 1 159 ? -3.871  5.877   0.114   1   11.217 ? 159 PHE   B CE1  1 
ATOM   3610 C  CE2  . PHE   B 1 159 ? -5.182  5.271   2.009   1   11.558 ? 159 PHE   B CE2  1 
ATOM   3611 C  CZ   . PHE   B 1 159 ? -4.994  6.049   0.892   1   11.475 ? 159 PHE   B CZ   1 
ATOM   3612 N  N    . CYS   B 1 160 ? 0.006   0.813   0.603   1   10.244 ? 160 CYS   B N    1 
ATOM   3613 C  CA   . CYS   B 1 160 ? 1.137   -0.081  0.799   1   10.925 ? 160 CYS   B CA   1 
ATOM   3614 C  C    . CYS   B 1 160 ? 2.499   0.564   0.564   1   10.641 ? 160 CYS   B C    1 
ATOM   3615 O  O    . CYS   B 1 160 ? 3.487   -0.059  0.927   1   11.903 ? 160 CYS   B O    1 
ATOM   3616 C  CB   . CYS   B 1 160 ? 1.014   -1.332  -0.067  1   11.479 ? 160 CYS   B CB   1 
ATOM   3617 S  SG   . CYS   B 1 160 ? 0.863   -1.005  -1.845  1   13.156 ? 160 CYS   B SG   1 
ATOM   3618 N  N    . TYR   B 1 161 ? 2.574   1.745   -0.055  1   9.653  ? 161 TYR   B N    1 
ATOM   3619 C  CA   . TYR   B 1 161 ? 3.866   2.309   -0.43   1   9.453  ? 161 TYR   B CA   1 
ATOM   3620 C  C    . TYR   B 1 161 ? 3.84    3.822   -0.32   1   9.162  ? 161 TYR   B C    1 
ATOM   3621 O  O    . TYR   B 1 161 ? 2.853   4.455   -0.675  1   9.517  ? 161 TYR   B O    1 
ATOM   3622 C  CB   . TYR   B 1 161 ? 4.229   1.904   -1.861  1   9.486  ? 161 TYR   B CB   1 
ATOM   3623 C  CG   . TYR   B 1 161 ? 5.549   2.451   -2.389  1   9.5    ? 161 TYR   B CG   1 
ATOM   3624 C  CD1  . TYR   B 1 161 ? 6.758   1.814   -2.121  1   9.756  ? 161 TYR   B CD1  1 
ATOM   3625 C  CD2  . TYR   B 1 161 ? 5.591   3.603   -3.166  1   9.296  ? 161 TYR   B CD2  1 
ATOM   3626 C  CE1  . TYR   B 1 161 ? 7.949   2.307   -2.625  1   9.887  ? 161 TYR   B CE1  1 
ATOM   3627 C  CE2  . TYR   B 1 161 ? 6.778   4.092   -3.692  1   9.311  ? 161 TYR   B CE2  1 
ATOM   3628 C  CZ   . TYR   B 1 161 ? 7.971   3.458   -3.395  1   9.533  ? 161 TYR   B CZ   1 
ATOM   3629 O  OH   . TYR   B 1 161 ? 9.177   3.934   -3.862  1   10.14  ? 161 TYR   B OH   1 
ATOM   3630 N  N    . MET   B 1 162 ? 4.946   4.388   0.189   1   8.924  ? 162 MET   B N    1 
ATOM   3631 C  CA   . MET   B 1 162 ? 5.195   5.81    0.119   1   9.236  ? 162 MET   B CA   1 
ATOM   3632 C  C    . MET   B 1 162 ? 6.59    5.986   -0.473  1   9.03   ? 162 MET   B C    1 
ATOM   3633 O  O    . MET   B 1 162 ? 7.543   5.348   -0.021  1   9.208  ? 162 MET   B O    1 
ATOM   3634 C  CB   . MET   B 1 162 ? 5.122   6.498   1.489   1   10.526 ? 162 MET   B CB   1 
ATOM   3635 C  CG   . MET   B 1 162 ? 5.338   8.003   1.366   1   11.781 ? 162 MET   B CG   1 
ATOM   3636 S  SD   . MET   B 1 162 ? 4.864   9.034   2.763   1   16.614 ? 162 MET   B SD   1 
ATOM   3637 C  CE   . MET   B 1 162 ? 6.281   8.347   3.542   1   13.061 ? 162 MET   B CE   1 
ATOM   3638 N  N    . HIS   B 1 163 ? 6.697   6.866   -1.465  1   8.784  ? 163 HIS   B N    1 
ATOM   3639 C  CA   . HIS   B 1 163 ? 7.937   7.037   -2.205  1   8.925  ? 163 HIS   B CA   1 
ATOM   3640 C  C    . HIS   B 1 163 ? 8.948   7.896   -1.44   1   8.856  ? 163 HIS   B C    1 
ATOM   3641 O  O    . HIS   B 1 163 ? 8.628   9.023   -1.057  1   9.236  ? 163 HIS   B O    1 
ATOM   3642 C  CB   . HIS   B 1 163 ? 7.624   7.705   -3.55   1   9.111  ? 163 HIS   B CB   1 
ATOM   3643 C  CG   . HIS   B 1 163 ? 8.82    7.802   -4.416  1   9.225  ? 163 HIS   B CG   1 
ATOM   3644 N  ND1  . HIS   B 1 163 ? 9.638   6.72    -4.616  1   9.891  ? 163 HIS   B ND1  1 
ATOM   3645 C  CD2  . HIS   B 1 163 ? 9.35    8.825   -5.082  1   10.138 ? 163 HIS   B CD2  1 
ATOM   3646 C  CE1  . HIS   B 1 163 ? 10.645  7.105   -5.389  1   9.848  ? 163 HIS   B CE1  1 
ATOM   3647 N  NE2  . HIS   B 1 163 ? 10.506  8.377   -5.683  1   10.292 ? 163 HIS   B NE2  1 
ATOM   3648 N  N    . HIS   B 1 164 ? 10.192  7.393   -1.31   1   9.145  ? 164 HIS   B N    1 
ATOM   3649 C  CA   . HIS   B 1 164 ? 11.256  8.128   -0.637  1   9.693  ? 164 HIS   B CA   1 
ATOM   3650 C  C    . HIS   B 1 164 ? 12.421  8.539   -1.542  1   10.363 ? 164 HIS   B C    1 
ATOM   3651 O  O    . HIS   B 1 164 ? 12.923  9.644   -1.37   1   11.506 ? 164 HIS   B O    1 
ATOM   3652 C  CB   . HIS   B 1 164 ? 11.821  7.382   0.579   1   9.681  ? 164 HIS   B CB   1 
ATOM   3653 C  CG   . HIS   B 1 164 ? 10.904  7.355   1.742   1   9.719  ? 164 HIS   B CG   1 
ATOM   3654 N  ND1  . HIS   B 1 164 ? 11.228  7.892   2.973   1   10.161 ? 164 HIS   B ND1  1 
ATOM   3655 C  CD2  . HIS   B 1 164 ? 9.684   6.786   1.855   1   10.071 ? 164 HIS   B CD2  1 
ATOM   3656 C  CE1  . HIS   B 1 164 ? 10.213  7.675   3.793   1   10.044 ? 164 HIS   B CE1  1 
ATOM   3657 N  NE2  . HIS   B 1 164 ? 9.252   7.018   3.148   1   10.477 ? 164 HIS   B NE2  1 
ATOM   3658 N  N    . MET   B 1 165 ? 12.921  7.664   -2.427  1   10.71  ? 165 MET   B N    1 
ATOM   3659 C  CA   . MET   B 1 165 ? 14.083  8.068   -3.215  1   11.817 ? 165 MET   B CA   1 
ATOM   3660 C  C    . MET   B 1 165 ? 14.244  7.216   -4.47   1   11.592 ? 165 MET   B C    1 
ATOM   3661 O  O    . MET   B 1 165 ? 13.636  6.16    -4.612  1   11.17  ? 165 MET   B O    1 
ATOM   3662 C  CB   . MET   B 1 165 ? 15.379  8       -2.4    1   13.442 ? 165 MET   B CB   1 
ATOM   3663 C  CG   . MET   B 1 165 ? 15.891  6.636   -2.193  1   15.489 ? 165 MET   B CG   1 
ATOM   3664 S  SD   . MET   B 1 165 ? 15.15   6.03    -0.683  1   20.244 ? 165 MET   B SD   1 
ATOM   3665 C  CE   . MET   B 1 165 ? 16.592  4.993   -0.434  1   17.686 ? 165 MET   B CE   1 
ATOM   3666 N  N    . GLU   B 1 166 ? 15.108  7.718   -5.36   1   12.445 ? 166 GLU   B N    1 
ATOM   3667 C  CA   . GLU   B 1 166 ? 15.582  6.957   -6.502  1   12.193 ? 166 GLU   B CA   1 
ATOM   3668 C  C    . GLU   B 1 166 ? 17.02   6.512   -6.254  1   12.797 ? 166 GLU   B C    1 
ATOM   3669 O  O    . GLU   B 1 166 ? 17.837  7.286   -5.748  1   14.194 ? 166 GLU   B O    1 
ATOM   3670 C  CB   . GLU   B 1 166 ? 15.526  7.836   -7.75   1   12.634 ? 166 GLU   B CB   1 
ATOM   3671 C  CG   . GLU   B 1 166 ? 15.92   7.1     -9.021  1   13.076 ? 166 GLU   B CG   1 
ATOM   3672 C  CD   . GLU   B 1 166 ? 15.625  7.918   -10.256 1   13.72  ? 166 GLU   B CD   1 
ATOM   3673 O  OE1  . GLU   B 1 166 ? 16.608  8.316   -10.933 1   15.378 ? 166 GLU   B OE1  1 
ATOM   3674 O  OE2  . GLU   B 1 166 ? 14.432  8.186   -10.511 1   13.268 ? 166 GLU   B OE2  1 
ATOM   3675 N  N    . LEU   B 1 167 ? 17.293  5.249   -6.581  1   13.376 ? 167 LEU   B N    1 
ATOM   3676 C  CA   . LEU   B 1 167 ? 18.615  4.649   -6.475  1   14.669 ? 167 LEU   B CA   1 
ATOM   3677 C  C    . LEU   B 1 167 ? 19.403  4.902   -7.755  1   16.31  ? 167 LEU   B C    1 
ATOM   3678 O  O    . LEU   B 1 167 ? 18.832  5.285   -8.78   1   16.144 ? 167 LEU   B O    1 
ATOM   3679 C  CB   . LEU   B 1 167 ? 18.462  3.151   -6.215  1   15.272 ? 167 LEU   B CB   1 
ATOM   3680 C  CG   . LEU   B 1 167 ? 17.844  2.778   -4.867  1   16.145 ? 167 LEU   B CG   1 
ATOM   3681 C  CD1  . LEU   B 1 167 ? 17.422  1.327   -4.835  1   16.148 ? 167 LEU   B CD1  1 
ATOM   3682 C  CD2  . LEU   B 1 167 ? 18.831  3.087   -3.754  1   18.031 ? 167 LEU   B CD2  1 
ATOM   3683 N  N    . PRO   B 1 168 ? 20.742  4.709   -7.734  1   18.226 ? 168 PRO   B N    1 
ATOM   3684 C  CA   . PRO   B 1 168 ? 21.571  4.994   -8.907  1   19.764 ? 168 PRO   B CA   1 
ATOM   3685 C  C    . PRO   B 1 168 ? 21.185  4.334   -10.23  1   19.698 ? 168 PRO   B C    1 
ATOM   3686 O  O    . PRO   B 1 168 ? 21.499  4.888   -11.288 1   22.527 ? 168 PRO   B O    1 
ATOM   3687 C  CB   . PRO   B 1 168 ? 22.97   4.536   -8.429  1   21.251 ? 168 PRO   B CB   1 
ATOM   3688 C  CG   . PRO   B 1 168 ? 22.939  4.793   -6.947  1   21.601 ? 168 PRO   B CG   1 
ATOM   3689 C  CD   . PRO   B 1 168 ? 21.541  4.365   -6.546  1   20.313 ? 168 PRO   B CD   1 
ATOM   3690 N  N    . THR   B 1 169 ? 20.566  3.142   -10.186 1   18.796 ? 169 THR   B N    1 
ATOM   3691 C  CA   . THR   B 1 169 ? 20.173  2.44    -11.405 1   18.653 ? 169 THR   B CA   1 
ATOM   3692 C  C    . THR   B 1 169 ? 18.834  2.956   -11.939 1   17.096 ? 169 THR   B C    1 
ATOM   3693 O  O    . THR   B 1 169 ? 18.343  2.452   -12.959 1   18.951 ? 169 THR   B O    1 
ATOM   3694 C  CB   . THR   B 1 169 ? 20.101  0.926   -11.193 1   20.824 ? 169 THR   B CB   1 
ATOM   3695 O  OG1  . THR   B 1 169 ? 19.271  0.678   -10.064 1   19.962 ? 169 THR   B OG1  1 
ATOM   3696 C  CG2  . THR   B 1 169 ? 21.457  0.273   -10.98  1   22.614 ? 169 THR   B CG2  1 
ATOM   3697 N  N    . GLY   B 1 170 ? 18.211  3.926   -11.253 1   15.351 ? 170 GLY   B N    1 
ATOM   3698 C  CA   . GLY   B 1 170 ? 17.008  4.561   -11.775 1   14.448 ? 170 GLY   B CA   1 
ATOM   3699 C  C    . GLY   B 1 170 ? 15.722  3.887   -11.304 1   13.97  ? 170 GLY   B C    1 
ATOM   3700 O  O    . GLY   B 1 170 ? 14.651  4.235   -11.779 1   16.318 ? 170 GLY   B O    1 
ATOM   3701 N  N    . VAL   B 1 171 ? 15.834  2.931   -10.381 1   12.47  ? 171 VAL   B N    1 
ATOM   3702 C  CA   . VAL   B 1 171 ? 14.681  2.323   -9.739  1   11.846 ? 171 VAL   B CA   1 
ATOM   3703 C  C    . VAL   B 1 171 ? 14.462  2.994   -8.381  1   11.342 ? 171 VAL   B C    1 
ATOM   3704 O  O    . VAL   B 1 171 ? 15.241  3.849   -7.962  1   11.699 ? 171 VAL   B O    1 
ATOM   3705 C  CB   . VAL   B 1 171 ? 14.848  0.8     -9.61   1   12.031 ? 171 VAL   B CB   1 
ATOM   3706 C  CG1  . VAL   B 1 171 ? 15.011  0.15    -10.988 1   12.996 ? 171 VAL   B CG1  1 
ATOM   3707 C  CG2  . VAL   B 1 171 ? 15.972  0.435   -8.649  1   12.258 ? 171 VAL   B CG2  1 
ATOM   3708 N  N    . HIS   B 1 172 ? 13.338  2.64    -7.751  1   10.983 ? 172 HIS   B N    1 
ATOM   3709 C  CA   . HIS   B 1 172 ? 12.769  3.442   -6.683  1   10.77  ? 172 HIS   B CA   1 
ATOM   3710 C  C    . HIS   B 1 172 ? 12.652  2.647   -5.394  1   10.709 ? 172 HIS   B C    1 
ATOM   3711 O  O    . HIS   B 1 172 ? 12.414  1.442   -5.421  1   10.954 ? 172 HIS   B O    1 
ATOM   3712 C  CB   . HIS   B 1 172 ? 11.426  3.999   -7.152  1   10.698 ? 172 HIS   B CB   1 
ATOM   3713 C  CG   . HIS   B 1 172 ? 11.647  4.844   -8.349  1   10.933 ? 172 HIS   B CG   1 
ATOM   3714 N  ND1  . HIS   B 1 172 ? 11.242  4.508   -9.62   1   11.482 ? 172 HIS   B ND1  1 
ATOM   3715 C  CD2  . HIS   B 1 172 ? 12.325  5.992   -8.446  1   11.238 ? 172 HIS   B CD2  1 
ATOM   3716 C  CE1  . HIS   B 1 172 ? 11.685  5.437   -10.461 1   11.546 ? 172 HIS   B CE1  1 
ATOM   3717 N  NE2  . HIS   B 1 172 ? 12.34   6.354   -9.773  1   11.454 ? 172 HIS   B NE2  1 
ATOM   3718 N  N    . ALA   B 1 173 ? 12.8    3.37    -4.277  1   10.91  ? 173 ALA   B N    1 
ATOM   3719 C  CA   . ALA   B 1 173 ? 12.695  2.775   -2.96   1   11.153 ? 173 ALA   B CA   1 
ATOM   3720 C  C    . ALA   B 1 173 ? 11.803  3.628   -2.073  1   10.162 ? 173 ALA   B C    1 
ATOM   3721 O  O    . ALA   B 1 173 ? 11.751  4.848   -2.188  1   10.198 ? 173 ALA   B O    1 
ATOM   3722 C  CB   . ALA   B 1 173 ? 14.066  2.617   -2.338  1   11.908 ? 173 ALA   B CB   1 
ATOM   3723 N  N    . GLY   B 1 174 ? 11.122  2.943   -1.162  1   10.257 ? 174 GLY   B N    1 
ATOM   3724 C  CA   . GLY   B 1 174 ? 10.238  3.622   -0.236  1   10.034 ? 174 GLY   B CA   1 
ATOM   3725 C  C    . GLY   B 1 174 ? 9.812   2.698   0.894   1   9.616  ? 174 GLY   B C    1 
ATOM   3726 O  O    . GLY   B 1 174 ? 10.387  1.631   1.08    1   10.05  ? 174 GLY   B O    1 
ATOM   3727 N  N    . THR   B 1 175 ? 8.784   3.159   1.625   1   9.666  ? 175 THR   B N    1 
ATOM   3728 C  CA   . THR   B 1 175 ? 8.37    2.538   2.863   1   9.624  ? 175 THR   B CA   1 
ATOM   3729 C  C    . THR   B 1 175 ? 6.92    2.108   2.759   1   9.558  ? 175 THR   B C    1 
ATOM   3730 O  O    . THR   B 1 175 ? 6.182   2.545   1.879   1   9.592  ? 175 THR   B O    1 
ATOM   3731 C  CB   . THR   B 1 175 ? 8.525   3.509   4.036   1   10.181 ? 175 THR   B CB   1 
ATOM   3732 O  OG1  . THR   B 1 175 ? 7.644   4.623   3.905   1   10.24  ? 175 THR   B OG1  1 
ATOM   3733 C  CG2  . THR   B 1 175 ? 9.943   4.024   4.193   1   10.324 ? 175 THR   B CG2  1 
ATOM   3734 N  N    . ASP   B 1 176 ? 6.51    1.297   3.727   1   9.503  ? 176 ASP   B N    1 
ATOM   3735 C  CA   . ASP   B 1 176 ? 5.1     1.159   4.045   1   10.27  ? 176 ASP   B CA   1 
ATOM   3736 C  C    . ASP   B 1 176 ? 4.631   2.432   4.751   1   9.976  ? 176 ASP   B C    1 
ATOM   3737 O  O    . ASP   B 1 176 ? 5.407   3.356   4.977   1   10.53  ? 176 ASP   B O    1 
ATOM   3738 C  CB   . ASP   B 1 176 ? 4.856   -0.148  4.773   1   10.844 ? 176 ASP   B CB   1 
ATOM   3739 C  CG   . ASP   B 1 176 ? 5.43    -0.261  6.171   1   11.378 ? 176 ASP   B CG   1 
ATOM   3740 O  OD1  . ASP   B 1 176 ? 5.659   0.805   6.776   1   12.21  ? 176 ASP   B OD1  1 
ATOM   3741 O  OD2  . ASP   B 1 176 ? 5.652   -1.421  6.585   1   12.747 ? 176 ASP   B OD2  1 
ATOM   3742 N  N    . LEU   B 1 177 ? 3.339   2.496   5.1     1   10.307 ? 177 LEU   B N    1 
ATOM   3743 C  CA   . LEU   B 1 177 ? 2.803   3.73    5.655   1   11.316 ? 177 LEU   B CA   1 
ATOM   3744 C  C    . LEU   B 1 177 ? 3.091   3.835   7.149   1   12.25  ? 177 LEU   B C    1 
ATOM   3745 O  O    . LEU   B 1 177 ? 2.775   4.867   7.739   1   14.118 ? 177 LEU   B O    1 
ATOM   3746 C  CB   . LEU   B 1 177 ? 1.31    3.884   5.334   1   11.938 ? 177 LEU   B CB   1 
ATOM   3747 C  CG   . LEU   B 1 177 ? 1       4.654   4.049   1   12.366 ? 177 LEU   B CG   1 
ATOM   3748 C  CD1  . LEU   B 1 177 ? 1.373   6.117   4.208   1   13.671 ? 177 LEU   B CD1  1 
ATOM   3749 C  CD2  . LEU   B 1 177 ? 1.683   4.038   2.835   1   12.893 ? 177 LEU   B CD2  1 
ATOM   3750 N  N    . GLU   B 1 178 ? 3.717   2.797   7.717   1   12.293 ? 178 GLU   B N    1 
ATOM   3751 C  CA   . GLU   B 1 178 ? 4.268   2.893   9.061   1   13.407 ? 178 GLU   B CA   1 
ATOM   3752 C  C    . GLU   B 1 178 ? 5.754   3.249   9.031   1   12.948 ? 178 GLU   B C    1 
ATOM   3753 O  O    . GLU   B 1 178 ? 6.405   3.208   10.066  1   13.933 ? 178 GLU   B O    1 
ATOM   3754 C  CB   . GLU   B 1 178 ? 4.013   1.581   9.79    1   15.371 ? 178 GLU   B CB   1 
ATOM   3755 C  CG   . GLU   B 1 178 ? 2.543   1.336   10.113  1   17.765 ? 178 GLU   B CG   1 
ATOM   3756 C  CD   . GLU   B 1 178 ? 2.347   0.059   10.914  1   21.86  ? 178 GLU   B CD   1 
ATOM   3757 O  OE1  . GLU   B 1 178 ? 3.159   -0.889  10.816  1   26.265 ? 178 GLU   B OE1  1 
ATOM   3758 O  OE2  . GLU   B 1 178 ? 1.388   0.042   11.689  1   26.326 ? 178 GLU   B OE2  1 
ATOM   3759 N  N    . GLY   B 1 179 ? 6.295   3.574   7.853   1   12.383 ? 179 GLY   B N    1 
ATOM   3760 C  CA   . GLY   B 1 179 ? 7.638   4.116   7.74    1   12.11  ? 179 GLY   B CA   1 
ATOM   3761 C  C    . GLY   B 1 179 ? 8.74    3.058   7.734   1   11.551 ? 179 GLY   B C    1 
ATOM   3762 O  O    . GLY   B 1 179 ? 9.898   3.423   7.907   1   11.159 ? 179 GLY   B O    1 
ATOM   3763 N  N    . ASN   B 1 180 ? 8.396   1.78    7.497   1   10.998 ? 180 ASN   B N    1 
ATOM   3764 C  CA   . ASN   B 1 180 ? 9.385   0.72    7.394   1   11.514 ? 180 ASN   B CA   1 
ATOM   3765 C  C    . ASN   B 1 180 ? 9.778   0.553   5.93    1   11.027 ? 180 ASN   B C    1 
ATOM   3766 O  O    . ASN   B 1 180 ? 8.907   0.289   5.1     1   10.615 ? 180 ASN   B O    1 
ATOM   3767 C  CB   . ASN   B 1 180 ? 8.842   -0.608  7.897   1   12.825 ? 180 ASN   B CB   1 
ATOM   3768 C  CG   . ASN   B 1 180 ? 8.391   -0.531  9.333   1   14.941 ? 180 ASN   B CG   1 
ATOM   3769 O  OD1  . ASN   B 1 180 ? 9.218   -0.395  10.236  1   18.166 ? 180 ASN   B OD1  1 
ATOM   3770 N  ND2  . ASN   B 1 180 ? 7.092   -0.596  9.57    1   15.889 ? 180 ASN   B ND2  1 
ATOM   3771 N  N    . PHE   B 1 181 ? 11.063  0.738   5.605   1   10.714 ? 181 PHE   B N    1 
ATOM   3772 C  CA   . PHE   B 1 181 ? 11.527  0.544   4.239   1   10.584 ? 181 PHE   B CA   1 
ATOM   3773 C  C    . PHE   B 1 181 ? 11.223  -0.866  3.755   1   10.603 ? 181 PHE   B C    1 
ATOM   3774 O  O    . PHE   B 1 181 ? 11.331  -1.85   4.481   1   10.945 ? 181 PHE   B O    1 
ATOM   3775 C  CB   . PHE   B 1 181 ? 13.033  0.779   4.065   1   10.992 ? 181 PHE   B CB   1 
ATOM   3776 C  CG   . PHE   B 1 181 ? 13.311  2.202   3.63    1   11.071 ? 181 PHE   B CG   1 
ATOM   3777 C  CD1  . PHE   B 1 181 ? 13.284  2.53    2.277   1   11.54  ? 181 PHE   B CD1  1 
ATOM   3778 C  CD2  . PHE   B 1 181 ? 13.535  3.216   4.552   1   11.196 ? 181 PHE   B CD2  1 
ATOM   3779 C  CE1  . PHE   B 1 181 ? 13.479  3.828   1.863   1   11.171 ? 181 PHE   B CE1  1 
ATOM   3780 C  CE2  . PHE   B 1 181 ? 13.739  4.517   4.139   1   11.577 ? 181 PHE   B CE2  1 
ATOM   3781 C  CZ   . PHE   B 1 181 ? 13.729  4.823   2.789   1   12.083 ? 181 PHE   B CZ   1 
ATOM   3782 N  N    . TYR   B 1 182 ? 10.856  -0.946  2.468   1   10.169 ? 182 TYR   B N    1 
ATOM   3783 C  CA   . TYR   B 1 182 ? 10.984  -2.179  1.713   1   10.367 ? 182 TYR   B CA   1 
ATOM   3784 C  C    . TYR   B 1 182 ? 12.435  -2.27   1.263   1   10.833 ? 182 TYR   B C    1 
ATOM   3785 O  O    . TYR   B 1 182 ? 12.943  -1.325  0.664   1   12.261 ? 182 TYR   B O    1 
ATOM   3786 C  CB   . TYR   B 1 182 ? 10.059  -2.158  0.499   1   10.267 ? 182 TYR   B CB   1 
ATOM   3787 C  CG   . TYR   B 1 182 ? 8.581   -2.193  0.855   1   9.679  ? 182 TYR   B CG   1 
ATOM   3788 C  CD1  . TYR   B 1 182 ? 7.962   -3.386  1.193   1   9.803  ? 182 TYR   B CD1  1 
ATOM   3789 C  CD2  . TYR   B 1 182 ? 7.82    -1.038  0.836   1   9.664  ? 182 TYR   B CD2  1 
ATOM   3790 C  CE1  . TYR   B 1 182 ? 6.609   -3.434  1.498   1   10.182 ? 182 TYR   B CE1  1 
ATOM   3791 C  CE2  . TYR   B 1 182 ? 6.463   -1.072  1.137   1   9.925  ? 182 TYR   B CE2  1 
ATOM   3792 C  CZ   . TYR   B 1 182 ? 5.856   -2.273  1.453   1   9.992  ? 182 TYR   B CZ   1 
ATOM   3793 O  OH   . TYR   B 1 182 ? 4.52    -2.329  1.754   1   10.394 ? 182 TYR   B OH   1 
ATOM   3794 N  N    . GLY   B 1 183 ? 13.092  -3.374  1.598   1   10.923 ? 183 GLY   B N    1 
ATOM   3795 C  CA   . GLY   B 1 183 ? 14.439  -3.609  1.143   1   11.231 ? 183 GLY   B CA   1 
ATOM   3796 C  C    . GLY   B 1 183 ? 15.478  -3.008  2.075   1   11.675 ? 183 GLY   B C    1 
ATOM   3797 O  O    . GLY   B 1 183 ? 15.172  -2.252  2.995   1   11.678 ? 183 GLY   B O    1 
ATOM   3798 N  N    . PRO   B 1 184 ? 16.752  -3.335  1.794   1   11.757 ? 184 PRO   B N    1 
ATOM   3799 C  CA   . PRO   B 1 184 ? 17.872  -2.965  2.667   1   12.748 ? 184 PRO   B CA   1 
ATOM   3800 C  C    . PRO   B 1 184 ? 18.393  -1.551  2.436   1   13.436 ? 184 PRO   B C    1 
ATOM   3801 O  O    . PRO   B 1 184 ? 19.577  -1.339  2.164   1   16.907 ? 184 PRO   B O    1 
ATOM   3802 C  CB   . PRO   B 1 184 ? 18.893  -4.05   2.288   1   13.98  ? 184 PRO   B CB   1 
ATOM   3803 C  CG   . PRO   B 1 184 ? 18.661  -4.263  0.823   1   13.646 ? 184 PRO   B CG   1 
ATOM   3804 C  CD   . PRO   B 1 184 ? 17.158  -4.23   0.695   1   12.815 ? 184 PRO   B CD   1 
ATOM   3805 N  N    . PHE   B 1 185 ? 17.475  -0.591  2.52    1   11.718 ? 185 PHE   B N    1 
ATOM   3806 C  CA   . PHE   B 1 185 ? 17.75   0.796   2.205   1   11.76  ? 185 PHE   B CA   1 
ATOM   3807 C  C    . PHE   B 1 185 ? 17.532  1.657   3.443   1   12.286 ? 185 PHE   B C    1 
ATOM   3808 O  O    . PHE   B 1 185 ? 16.735  1.308   4.326   1   13.52  ? 185 PHE   B O    1 
ATOM   3809 C  CB   . PHE   B 1 185 ? 16.875  1.283   1.045   1   12.139 ? 185 PHE   B CB   1 
ATOM   3810 C  CG   . PHE   B 1 185 ? 16.976  0.335   -0.137  1   12.3   ? 185 PHE   B CG   1 
ATOM   3811 C  CD1  . PHE   B 1 185 ? 18.19   0.156   -0.79   1   12.879 ? 185 PHE   B CD1  1 
ATOM   3812 C  CD2  . PHE   B 1 185 ? 15.892  -0.412  -0.574  1   12.94  ? 185 PHE   B CD2  1 
ATOM   3813 C  CE1  . PHE   B 1 185 ? 18.301  -0.723  -1.852  1   13.383 ? 185 PHE   B CE1  1 
ATOM   3814 C  CE2  . PHE   B 1 185 ? 16.014  -1.276  -1.655  1   13.023 ? 185 PHE   B CE2  1 
ATOM   3815 C  CZ   . PHE   B 1 185 ? 17.224  -1.447  -2.267  1   13.167 ? 185 PHE   B CZ   1 
ATOM   3816 N  N    . VAL   B 1 186 ? 18.212  2.806   3.441   1   11.79  ? 186 VAL   B N    1 
ATOM   3817 C  CA   . VAL   B 1 186 ? 18.074  3.784   4.507   1   12.227 ? 186 VAL   B CA   1 
ATOM   3818 C  C    . VAL   B 1 186 ? 17.817  5.164   3.911   1   11.707 ? 186 VAL   B C    1 
ATOM   3819 O  O    . VAL   B 1 186 ? 18.207  5.445   2.774   1   11.969 ? 186 VAL   B O    1 
ATOM   3820 C  CB   . VAL   B 1 186 ? 19.312  3.794   5.422   1   13.355 ? 186 VAL   B CB   1 
ATOM   3821 C  CG1  . VAL   B 1 186 ? 19.459  2.464   6.149   1   14.255 ? 186 VAL   B CG1  1 
ATOM   3822 C  CG2  . VAL   B 1 186 ? 20.582  4.146   4.652   1   13.68  ? 186 VAL   B CG2  1 
ATOM   3823 N  N    . ASP   B 1 187 ? 17.169  6.037   4.695   1   11.97  ? 187 ASP   B N    1 
ATOM   3824 C  CA   . ASP   B 1 187 ? 16.898  7.405   4.264   1   11.91  ? 187 ASP   B CA   1 
ATOM   3825 C  C    . ASP   B 1 187 ? 18.091  8.302   4.596   1   12.868 ? 187 ASP   B C    1 
ATOM   3826 O  O    . ASP   B 1 187 ? 18.038  9.166   5.477   1   12.694 ? 187 ASP   B O    1 
ATOM   3827 C  CB   . ASP   B 1 187 ? 15.557  7.923   4.754   1   12.348 ? 187 ASP   B CB   1 
ATOM   3828 C  CG   . ASP   B 1 187 ? 15.251  7.798   6.236   1   12.462 ? 187 ASP   B CG   1 
ATOM   3829 O  OD1  . ASP   B 1 187 ? 16.066  7.182   6.971   1   13.283 ? 187 ASP   B OD1  1 
ATOM   3830 O  OD2  . ASP   B 1 187 ? 14.171  8.29    6.633   1   12.36  ? 187 ASP   B OD2  1 
ATOM   3831 N  N    . ARG   B 1 188 ? 19.163  8.082   3.828   1   14.213 ? 188 ARG   B N    1 
ATOM   3832 C  CA   . ARG   B 1 188 ? 20.394  8.849   3.892   1   15.319 ? 188 ARG   B CA   1 
ATOM   3833 C  C    . ARG   B 1 188 ? 20.977  8.896   2.487   1   15.716 ? 188 ARG   B C    1 
ATOM   3834 O  O    . ARG   B 1 188 ? 20.948  7.879   1.797   1   16.373 ? 188 ARG   B O    1 
ATOM   3835 C  CB   . ARG   B 1 188 ? 21.395  8.139   4.806   1   17.167 ? 188 ARG   B CB   1 
ATOM   3836 C  CG   . ARG   B 1 188 ? 22.632  8.969   5.098   1   19.038 ? 188 ARG   B CG   1 
ATOM   3837 C  CD   . ARG   B 1 188 ? 23.191  8.488   6.427   1   23.701 ? 188 ARG   B CD   1 
ATOM   3838 N  NE   . ARG   B 1 188 ? 24.135  7.433   6.099   1   26.411 ? 188 ARG   B NE   1 
ATOM   3839 C  CZ   . ARG   B 1 188 ? 24.341  6.217   6.598   1   29.245 ? 188 ARG   B CZ   1 
ATOM   3840 N  NH1  . ARG   B 1 188 ? 25.42   5.607   6.139   1   31.915 ? 188 ARG   B NH1  1 
ATOM   3841 N  NH2  . ARG   B 1 188 ? 23.581  5.644   7.542   1   27.749 ? 188 ARG   B NH2  1 
ATOM   3842 N  N    . GLN   B 1 189 ? 21.51   10.062  2.098   1   16.816 ? 189 GLN   B N    1 
ATOM   3843 C  CA   . GLN   B 1 189 ? 22.263  10.191  0.856   1   18.445 ? 189 GLN   B CA   1 
ATOM   3844 C  C    . GLN   B 1 189 ? 23.658  9.608   1.087   1   19.418 ? 189 GLN   B C    1 
ATOM   3845 O  O    . GLN   B 1 189 ? 24.552  10.284  1.585   1   21.306 ? 189 GLN   B O    1 
ATOM   3846 C  CB   . GLN   B 1 189 ? 22.252  11.653  0.409   1   19.99  ? 189 GLN   B CB   1 
ATOM   3847 C  CG   . GLN   B 1 189 ? 23.064  11.956  -0.845  1   22.363 ? 189 GLN   B CG   1 
ATOM   3848 C  CD   . GLN   B 1 189 ? 22.484  11.369  -2.115  1   25.568 ? 189 GLN   B CD   1 
ATOM   3849 O  OE1  . GLN   B 1 189 ? 21.756  12.034  -2.86   1   28.97  ? 189 GLN   B OE1  1 
ATOM   3850 N  NE2  . GLN   B 1 189 ? 22.798  10.111  -2.382  1   27.11  ? 189 GLN   B NE2  1 
ATOM   3851 N  N    . THR   B 1 190 ? 23.76   8.31    0.799   1   21.39  ? 190 THR   B N    1 
ATOM   3852 C  CA   . THR   B 1 190 ? 24.985  7.534   0.856   1   23.113 ? 190 THR   B CA   1 
ATOM   3853 C  C    . THR   B 1 190 ? 24.9    6.503   -0.268  1   22.684 ? 190 THR   B C    1 
ATOM   3854 O  O    . THR   B 1 190 ? 23.818  6.291   -0.82   1   22.755 ? 190 THR   B O    1 
ATOM   3855 C  CB   . THR   B 1 190 ? 25.097  6.885   2.238   1   24.359 ? 190 THR   B CB   1 
ATOM   3856 O  OG1  . THR   B 1 190 ? 26.436  6.406   2.339   1   26.329 ? 190 THR   B OG1  1 
ATOM   3857 C  CG2  . THR   B 1 190 ? 24.079  5.779   2.462   1   25.872 ? 190 THR   B CG2  1 
ATOM   3858 N  N    . ALA   B 1 191 ? 26.024  5.865   -0.6    1   23.879 ? 191 ALA   B N    1 
ATOM   3859 C  CA   . ALA   B 1 191 ? 26.037  4.852   -1.641  1   22.897 ? 191 ALA   B CA   1 
ATOM   3860 C  C    . ALA   B 1 191 ? 25.111  3.706   -1.247  1   19.936 ? 191 ALA   B C    1 
ATOM   3861 O  O    . ALA   B 1 191 ? 25.261  3.111   -0.183  1   21.026 ? 191 ALA   B O    1 
ATOM   3862 C  CB   . ALA   B 1 191 ? 27.449  4.359   -1.885  1   24.47  ? 191 ALA   B CB   1 
ATOM   3863 N  N    . GLN   B 1 192 ? 24.123  3.436   -2.099  1   18.081 ? 192 GLN   B N    1 
ATOM   3864 C  CA   . GLN   B 1 192 ? 23.219  2.316   -1.903  1   16.586 ? 192 GLN   B CA   1 
ATOM   3865 C  C    . GLN   B 1 192 ? 22.941  1.723   -3.271  1   17.524 ? 192 GLN   B C    1 
ATOM   3866 O  O    . GLN   B 1 192 ? 23.064  2.436   -4.265  1   19.767 ? 192 GLN   B O    1 
ATOM   3867 C  CB   . GLN   B 1 192 ? 21.903  2.748   -1.256  1   15.41  ? 192 GLN   B CB   1 
ATOM   3868 C  CG   . GLN   B 1 192 ? 22.082  3.574   0.007   1   14.949 ? 192 GLN   B CG   1 
ATOM   3869 C  CD   . GLN   B 1 192 ? 20.776  3.772   0.742   1   13.908 ? 192 GLN   B CD   1 
ATOM   3870 O  OE1  . GLN   B 1 192 ? 20.143  2.802   1.179   1   13.686 ? 192 GLN   B OE1  1 
ATOM   3871 N  NE2  . GLN   B 1 192 ? 20.38   5.025   0.917   1   14.848 ? 192 GLN   B NE2  1 
ATOM   3872 N  N    . ALA   B 1 193 ? 22.651  0.425   -3.3    1   17.158 ? 193 ALA   B N    1 
ATOM   3873 C  CA   . ALA   B 1 193 ? 22.443  -0.26   -4.565  1   19.058 ? 193 ALA   B CA   1 
ATOM   3874 C  C    . ALA   B 1 193 ? 21.383  -1.334  -4.412  1   21.396 ? 193 ALA   B C    1 
ATOM   3875 O  O    . ALA   B 1 193 ? 21.377  -2.055  -3.422  1   22.541 ? 193 ALA   B O    1 
ATOM   3876 C  CB   . ALA   B 1 193 ? 23.729  -0.868  -5.071  1   19.595 ? 193 ALA   B CB   1 
ATOM   3877 N  N    . ALA   B 1 194 ? 20.526  -1.435  -5.432  1   23.186 ? 194 ALA   B N    1 
ATOM   3878 C  CA   . ALA   B 1 194 ? 19.621  -2.561  -5.579  1   25.304 ? 194 ALA   B CA   1 
ATOM   3879 C  C    . ALA   B 1 194 ? 20.426  -3.845  -5.757  1   23.339 ? 194 ALA   B C    1 
ATOM   3880 O  O    . ALA   B 1 194 ? 21.425  -3.841  -6.457  1   24.27  ? 194 ALA   B O    1 
ATOM   3881 C  CB   . ALA   B 1 194 ? 18.713  -2.329  -6.766  1   27.118 ? 194 ALA   B CB   1 
ATOM   3882 N  N    . GLY   B 1 195 ? 19.997  -4.926  -5.097  1   22.82  ? 195 GLY   B N    1 
ATOM   3883 C  CA   . GLY   B 1 195 ? 20.534  -6.248  -5.364  1   20.136 ? 195 GLY   B CA   1 
ATOM   3884 C  C    . GLY   B 1 195 ? 20.102  -6.713  -6.75   1   18.906 ? 195 GLY   B C    1 
ATOM   3885 O  O    . GLY   B 1 195 ? 19.189  -6.143  -7.345  1   18.967 ? 195 GLY   B O    1 
ATOM   3886 N  N    A THR   B 1 196 ? 20.765  -7.741  -7.275  0.5 19.007 ? 196 THR   B N    1 
ATOM   3887 N  N    B THR   B 1 196 ? 20.785  -7.741  -7.267  0.5 18.056 ? 196 THR   B N    1 
ATOM   3888 C  CA   A THR   B 1 196 ? 20.386  -8.259  -8.578  0.5 19.598 ? 196 THR   B CA   1 
ATOM   3889 C  CA   B THR   B 1 196 ? 20.387  -8.317  -8.541  0.5 17.874 ? 196 THR   B CA   1 
ATOM   3890 C  C    A THR   B 1 196 ? 18.97   -8.819  -8.484  0.5 18.523 ? 196 THR   B C    1 
ATOM   3891 C  C    B THR   B 1 196 ? 18.932  -8.75   -8.412  0.5 17.623 ? 196 THR   B C    1 
ATOM   3892 O  O    A THR   B 1 196 ? 18.639  -9.573  -7.579  0.5 20.93  ? 196 THR   B O    1 
ATOM   3893 O  O    B THR   B 1 196 ? 18.552  -9.36   -7.414  0.5 19.769 ? 196 THR   B O    1 
ATOM   3894 C  CB   A THR   B 1 196 ? 21.413  -9.294  -9.019  0.5 20.997 ? 196 THR   B CB   1 
ATOM   3895 C  CB   B THR   B 1 196 ? 21.269  -9.5    -8.934  0.5 17.854 ? 196 THR   B CB   1 
ATOM   3896 O  OG1  A THR   B 1 196 ? 21.467  -10.175 -7.902  0.5 23.061 ? 196 THR   B OG1  1 
ATOM   3897 O  OG1  B THR   B 1 196 ? 22.624  -9.104  -8.743  0.5 17.15  ? 196 THR   B OG1  1 
ATOM   3898 C  CG2  A THR   B 1 196 ? 22.765  -8.66   -9.295  0.5 20.6   ? 196 THR   B CG2  1 
ATOM   3899 C  CG2  B THR   B 1 196 ? 21.024  -9.907  -10.375 0.5 17.555 ? 196 THR   B CG2  1 
ATOM   3900 N  N    . ASP   B 1 197 ? 18.109  -8.387  -9.398  1   17.08  ? 197 ASP   B N    1 
ATOM   3901 C  CA   . ASP   B 1 197 ? 16.704  -8.736  -9.352  1   16.586 ? 197 ASP   B CA   1 
ATOM   3902 C  C    . ASP   B 1 197 ? 16.477  -10.091 -10.02  1   16.657 ? 197 ASP   B C    1 
ATOM   3903 O  O    . ASP   B 1 197 ? 17.333  -10.599 -10.756 1   18.093 ? 197 ASP   B O    1 
ATOM   3904 C  CB   . ASP   B 1 197 ? 15.883  -7.637  -9.99   1   16.622 ? 197 ASP   B CB   1 
ATOM   3905 C  CG   . ASP   B 1 197 ? 14.428  -7.598  -9.558  1   16.042 ? 197 ASP   B CG   1 
ATOM   3906 O  OD1  . ASP   B 1 197 ? 14.119  -8.119  -8.457  1   15.037 ? 197 ASP   B OD1  1 
ATOM   3907 O  OD2  . ASP   B 1 197 ? 13.63   -7.045  -10.32  1   17.039 ? 197 ASP   B OD2  1 
ATOM   3908 N  N    . THR   B 1 198 ? 15.289  -10.649 -9.764  1   15.318 ? 198 THR   B N    1 
ATOM   3909 C  CA   . THR   B 1 198 ? 14.855  -11.899 -10.367 1   15.149 ? 198 THR   B CA   1 
ATOM   3910 C  C    . THR   B 1 198 ? 13.453  -11.713 -10.941 1   13.919 ? 198 THR   B C    1 
ATOM   3911 O  O    . THR   B 1 198 ? 12.8    -10.709 -10.677 1   14.482 ? 198 THR   B O    1 
ATOM   3912 C  CB   . THR   B 1 198 ? 14.9    -13.028 -9.341  1   17.143 ? 198 THR   B CB   1 
ATOM   3913 O  OG1  . THR   B 1 198 ? 14.194  -12.545 -8.209  1   18.019 ? 198 THR   B OG1  1 
ATOM   3914 C  CG2  . THR   B 1 198 ? 16.314  -13.39  -8.928  1   17.837 ? 198 THR   B CG2  1 
ATOM   3915 N  N    . THR   B 1 199 ? 13.013  -12.689 -11.74  1   13.382 ? 199 THR   B N    1 
ATOM   3916 C  CA   . THR   B 1 199 ? 11.706  -12.602 -12.373 1   13.066 ? 199 THR   B CA   1 
ATOM   3917 C  C    . THR   B 1 199 ? 10.67   -13.313 -11.495 1   12.829 ? 199 THR   B C    1 
ATOM   3918 O  O    . THR   B 1 199 ? 10.933  -14.381 -10.934 1   13.147 ? 199 THR   B O    1 
ATOM   3919 C  CB   . THR   B 1 199 ? 11.794  -13.19  -13.779 1   13.724 ? 199 THR   B CB   1 
ATOM   3920 O  OG1  . THR   B 1 199 ? 12.721  -12.413 -14.54  1   14.828 ? 199 THR   B OG1  1 
ATOM   3921 C  CG2  . THR   B 1 199 ? 10.443  -13.198 -14.474 1   14.327 ? 199 THR   B CG2  1 
ATOM   3922 N  N    . ILE   B 1 200 ? 9.46    -12.735 -11.426 1   12.202 ? 200 ILE   B N    1 
ATOM   3923 C  CA   . ILE   B 1 200 ? 8.41    -13.247 -10.557 1   11.996 ? 200 ILE   B CA   1 
ATOM   3924 C  C    . ILE   B 1 200 ? 7.638   -14.354 -11.282 1   11.656 ? 200 ILE   B C    1 
ATOM   3925 O  O    . ILE   B 1 200 ? 6.695   -14.09  -12.024 1   11.746 ? 200 ILE   B O    1 
ATOM   3926 C  CB   . ILE   B 1 200 ? 7.483   -12.105 -10.095 1   12.313 ? 200 ILE   B CB   1 
ATOM   3927 C  CG1  . ILE   B 1 200 ? 8.249   -10.922 -9.494  1   12.858 ? 200 ILE   B CG1  1 
ATOM   3928 C  CG2  . ILE   B 1 200 ? 6.454   -12.646 -9.108  1   12.085 ? 200 ILE   B CG2  1 
ATOM   3929 C  CD1  . ILE   B 1 200 ? 7.504   -9.606  -9.59   1   12.828 ? 200 ILE   B CD1  1 
ATOM   3930 N  N    . THR   B 1 201 ? 8.014   -15.609 -11.025 1   11.758 ? 201 THR   B N    1 
ATOM   3931 C  CA   . THR   B 1 201 ? 7.55    -16.757 -11.799 1   11.481 ? 201 THR   B CA   1 
ATOM   3932 C  C    . THR   B 1 201 ? 6.03    -16.894 -11.779 1   11.762 ? 201 THR   B C    1 
ATOM   3933 O  O    . THR   B 1 201 ? 5.404   -17.111 -12.816 1   11.599 ? 201 THR   B O    1 
ATOM   3934 C  CB   . THR   B 1 201 ? 8.203   -18.028 -11.269 1   12.169 ? 201 THR   B CB   1 
ATOM   3935 O  OG1  . THR   B 1 201 ? 9.6     -17.729 -11.245 1   12.923 ? 201 THR   B OG1  1 
ATOM   3936 C  CG2  . THR   B 1 201 ? 7.884   -19.247 -12.107 1   13.048 ? 201 THR   B CG2  1 
ATOM   3937 N  N    . VAL   B 1 202 ? 5.428   -16.825 -10.587 1   11.757 ? 202 VAL   B N    1 
ATOM   3938 C  CA   . VAL   B 1 202 ? 3.989   -17.033 -10.474 1   11.696 ? 202 VAL   B CA   1 
ATOM   3939 C  C    . VAL   B 1 202 ? 3.241   -16.007 -11.333 1   11.2   ? 202 VAL   B C    1 
ATOM   3940 O  O    . VAL   B 1 202 ? 2.181   -16.307 -11.905 1   11.378 ? 202 VAL   B O    1 
ATOM   3941 C  CB   . VAL   B 1 202 ? 3.52    -17.017 -9.005  1   12.72  ? 202 VAL   B CB   1 
ATOM   3942 C  CG1  . VAL   B 1 202 ? 3.801   -15.685 -8.316  1   13.172 ? 202 VAL   B CG1  1 
ATOM   3943 C  CG2  . VAL   B 1 202 ? 2.048   -17.4   -8.891  1   13.271 ? 202 VAL   B CG2  1 
ATOM   3944 N  N    . ASN   B 1 203 ? 3.78    -14.794 -11.418 1   10.58  ? 203 ASN   B N    1 
ATOM   3945 C  CA   . ASN   B 1 203 ? 3.159   -13.735 -12.189 1   11.091 ? 203 ASN   B CA   1 
ATOM   3946 C  C    . ASN   B 1 203 ? 3.297   -14.002 -13.692 1   10.605 ? 203 ASN   B C    1 
ATOM   3947 O  O    . ASN   B 1 203 ? 2.355   -13.765 -14.46  1   10.596 ? 203 ASN   B O    1 
ATOM   3948 C  CB   . ASN   B 1 203 ? 3.72    -12.365 -11.84  1   10.539 ? 203 ASN   B CB   1 
ATOM   3949 C  CG   . ASN   B 1 203 ? 3.302   -11.865 -10.477 1   10.875 ? 203 ASN   B CG   1 
ATOM   3950 O  OD1  . ASN   B 1 203 ? 2.577   -12.549 -9.75   1   11.641 ? 203 ASN   B OD1  1 
ATOM   3951 N  ND2  . ASN   B 1 203 ? 3.709   -10.645 -10.166 1   10.802 ? 203 ASN   B ND2  1 
ATOM   3952 N  N    . VAL   B 1 204 ? 4.453   -14.498 -14.137 1   10.386 ? 204 VAL   B N    1 
ATOM   3953 C  CA   . VAL   B 1 204 ? 4.604   -14.868 -15.54  1   10.499 ? 204 VAL   B CA   1 
ATOM   3954 C  C    . VAL   B 1 204 ? 3.569   -15.932 -15.908 1   10.42  ? 204 VAL   B C    1 
ATOM   3955 O  O    . VAL   B 1 204 ? 2.916   -15.837 -16.949 1   10.518 ? 204 VAL   B O    1 
ATOM   3956 C  CB   . VAL   B 1 204 ? 6.03    -15.336 -15.88  1   10.977 ? 204 VAL   B CB   1 
ATOM   3957 C  CG1  . VAL   B 1 204 ? 6.118   -15.857 -17.308 1   11.14  ? 204 VAL   B CG1  1 
ATOM   3958 C  CG2  . VAL   B 1 204 ? 7.051   -14.222 -15.681 1   11.119 ? 204 VAL   B CG2  1 
ATOM   3959 N  N    . LEU   B 1 205 ? 3.384   -16.938 -15.052 1   10.64  ? 205 LEU   B N    1 
ATOM   3960 C  CA   . LEU   B 1 205 ? 2.392   -17.978 -15.3   1   10.788 ? 205 LEU   B CA   1 
ATOM   3961 C  C    . LEU   B 1 205 ? 0.987   -17.372 -15.378 1   11.392 ? 205 LEU   B C    1 
ATOM   3962 O  O    . LEU   B 1 205 ? 0.204   -17.689 -16.273 1   11.418 ? 205 LEU   B O    1 
ATOM   3963 C  CB   . LEU   B 1 205 ? 2.475   -19.062 -14.226 1   11.481 ? 205 LEU   B CB   1 
ATOM   3964 C  CG   . LEU   B 1 205 ? 3.738   -19.924 -14.272 1   12.115 ? 205 LEU   B CG   1 
ATOM   3965 C  CD1  . LEU   B 1 205 ? 3.829   -20.771 -13.024 1   12.495 ? 205 LEU   B CD1  1 
ATOM   3966 C  CD2  . LEU   B 1 205 ? 3.799   -20.806 -15.519 1   12.868 ? 205 LEU   B CD2  1 
ATOM   3967 N  N    . ALA   B 1 206 ? 0.663   -16.45  -14.467 1   11.141 ? 206 ALA   B N    1 
ATOM   3968 C  CA   . ALA   B 1 206 ? -0.639  -15.791 -14.498 1   11.256 ? 206 ALA   B CA   1 
ATOM   3969 C  C    . ALA   B 1 206 ? -0.874  -15.099 -15.842 1   10.978 ? 206 ALA   B C    1 
ATOM   3970 O  O    . ALA   B 1 206 ? -1.964  -15.182 -16.414 1   11.474 ? 206 ALA   B O    1 
ATOM   3971 C  CB   . ALA   B 1 206 ? -0.755  -14.814 -13.349 1   11.479 ? 206 ALA   B CB   1 
ATOM   3972 N  N    . TRP   B 1 207 ? 0.158   -14.412 -16.338 1   10.595 ? 207 TRP   B N    1 
ATOM   3973 C  CA   . TRP   B 1 207 ? 0.059   -13.676 -17.588 1   10.781 ? 207 TRP   B CA   1 
ATOM   3974 C  C    . TRP   B 1 207 ? -0.057  -14.625 -18.781 1   10.413 ? 207 TRP   B C    1 
ATOM   3975 O  O    . TRP   B 1 207 ? -0.794  -14.313 -19.718 1   10.841 ? 207 TRP   B O    1 
ATOM   3976 C  CB   . TRP   B 1 207 ? 1.246   -12.724 -17.69  1   11.381 ? 207 TRP   B CB   1 
ATOM   3977 C  CG   . TRP   B 1 207 ? 1.465   -12.043 -19.009 1   12.101 ? 207 TRP   B CG   1 
ATOM   3978 C  CD1  . TRP   B 1 207 ? 0.921   -10.896 -19.511 1   12.799 ? 207 TRP   B CD1  1 
ATOM   3979 C  CD2  . TRP   B 1 207 ? 2.466   -12.464 -19.946 1   12.983 ? 207 TRP   B CD2  1 
ATOM   3980 N  NE1  . TRP   B 1 207 ? 1.492   -10.607 -20.723 1   13.906 ? 207 TRP   B NE1  1 
ATOM   3981 C  CE2  . TRP   B 1 207 ? 2.454   -11.538 -21.003 1   13.737 ? 207 TRP   B CE2  1 
ATOM   3982 C  CE3  . TRP   B 1 207 ? 3.353   -13.541 -19.971 1   13.846 ? 207 TRP   B CE3  1 
ATOM   3983 C  CZ2  . TRP   B 1 207 ? 3.318   -11.671 -22.086 1   14.816 ? 207 TRP   B CZ2  1 
ATOM   3984 C  CZ3  . TRP   B 1 207 ? 4.218   -13.654 -21.029 1   15.286 ? 207 TRP   B CZ3  1 
ATOM   3985 C  CH2  . TRP   B 1 207 ? 4.201   -12.727 -22.062 1   15.109 ? 207 TRP   B CH2  1 
ATOM   3986 N  N    . LEU   B 1 208 ? 0.587   -15.798 -18.73  1   10.361 ? 208 LEU   B N    1 
ATOM   3987 C  CA   . LEU   B 1 208 ? 0.387   -16.796 -19.773 1   11.12  ? 208 LEU   B CA   1 
ATOM   3988 C  C    . LEU   B 1 208 ? -1.069  -17.255 -19.78  1   11.567 ? 208 LEU   B C    1 
ATOM   3989 O  O    . LEU   B 1 208 ? -1.653  -17.459 -20.842 1   12.116 ? 208 LEU   B O    1 
ATOM   3990 C  CB   . LEU   B 1 208 ? 1.354   -17.965 -19.624 1   11.278 ? 208 LEU   B CB   1 
ATOM   3991 C  CG   . LEU   B 1 208 ? 2.834   -17.646 -19.884 1   11.595 ? 208 LEU   B CG   1 
ATOM   3992 C  CD1  . LEU   B 1 208 ? 3.688   -18.858 -19.584 1   12.24  ? 208 LEU   B CD1  1 
ATOM   3993 C  CD2  . LEU   B 1 208 ? 3.105   -17.172 -21.287 1   12.072 ? 208 LEU   B CD2  1 
ATOM   3994 N  N    . TYR   B 1 209 ? -1.681  -17.419 -18.604 1   11.879 ? 209 TYR   B N    1 
ATOM   3995 C  CA   . TYR   B 1 209 ? -3.098  -17.748 -18.549 1   12.218 ? 209 TYR   B CA   1 
ATOM   3996 C  C    . TYR   B 1 209 ? -3.934  -16.621 -19.152 1   11.999 ? 209 TYR   B C    1 
ATOM   3997 O  O    . TYR   B 1 209 ? -4.892  -16.894 -19.879 1   13.085 ? 209 TYR   B O    1 
ATOM   3998 C  CB   . TYR   B 1 209 ? -3.568  -18.062 -17.132 1   12.522 ? 209 TYR   B CB   1 
ATOM   3999 C  CG   . TYR   B 1 209 ? -3.186  -19.46  -16.667 1   13.581 ? 209 TYR   B CG   1 
ATOM   4000 C  CD1  . TYR   B 1 209 ? -3.825  -20.591 -17.163 1   14.123 ? 209 TYR   B CD1  1 
ATOM   4001 C  CD2  . TYR   B 1 209 ? -2.22   -19.646 -15.684 1   13.571 ? 209 TYR   B CD2  1 
ATOM   4002 C  CE1  . TYR   B 1 209 ? -3.49   -21.862 -16.724 1   14.515 ? 209 TYR   B CE1  1 
ATOM   4003 C  CE2  . TYR   B 1 209 ? -1.874  -20.912 -15.237 1   14.396 ? 209 TYR   B CE2  1 
ATOM   4004 C  CZ   . TYR   B 1 209 ? -2.514  -22.024 -15.753 1   15.102 ? 209 TYR   B CZ   1 
ATOM   4005 O  OH   . TYR   B 1 209 ? -2.202  -23.282 -15.317 1   17.148 ? 209 TYR   B OH   1 
ATOM   4006 N  N    . ALA   B 1 210 ? -3.6    -15.361 -18.85  1   12.035 ? 210 ALA   B N    1 
ATOM   4007 C  CA   . ALA   B 1 210 ? -4.299  -14.224 -19.437 1   12.258 ? 210 ALA   B CA   1 
ATOM   4008 C  C    . ALA   B 1 210 ? -4.236  -14.293 -20.963 1   11.943 ? 210 ALA   B C    1 
ATOM   4009 O  O    . ALA   B 1 210 ? -5.218  -14.012 -21.657 1   12.246 ? 210 ALA   B O    1 
ATOM   4010 C  CB   . ALA   B 1 210 ? -3.716  -12.933 -18.933 1   11.885 ? 210 ALA   B CB   1 
ATOM   4011 N  N    . ALA   B 1 211 ? -3.063  -14.661 -21.478 1   11.477 ? 211 ALA   B N    1 
ATOM   4012 C  CA   . ALA   B 1 211 ? -2.851  -14.761 -22.911 1   12.344 ? 211 ALA   B CA   1 
ATOM   4013 C  C    . ALA   B 1 211 ? -3.768  -15.82  -23.491 1   12.95  ? 211 ALA   B C    1 
ATOM   4014 O  O    . ALA   B 1 211 ? -4.384  -15.583 -24.527 1   13.958 ? 211 ALA   B O    1 
ATOM   4015 C  CB   . ALA   B 1 211 ? -1.396  -15.063 -23.215 1   12.527 ? 211 ALA   B CB   1 
ATOM   4016 N  N    . VAL   B 1 212 ? -3.849  -16.99  -22.846 1   13.746 ? 212 VAL   B N    1 
ATOM   4017 C  CA   . VAL   B 1 212 ? -4.708  -18.062 -23.329 1   14.718 ? 212 VAL   B CA   1 
ATOM   4018 C  C    . VAL   B 1 212 ? -6.163  -17.589 -23.342 1   16.048 ? 212 VAL   B C    1 
ATOM   4019 O  O    . VAL   B 1 212 ? -6.892  -17.812 -24.316 1   17.345 ? 212 VAL   B O    1 
ATOM   4020 C  CB   . VAL   B 1 212 ? -4.528  -19.353 -22.502 1   15.547 ? 212 VAL   B CB   1 
ATOM   4021 C  CG1  . VAL   B 1 212 ? -5.572  -20.408 -22.836 1   16.353 ? 212 VAL   B CG1  1 
ATOM   4022 C  CG2  . VAL   B 1 212 ? -3.137  -19.94  -22.661 1   15.238 ? 212 VAL   B CG2  1 
ATOM   4023 N  N    . ILE   B 1 213 ? -6.593  -16.923 -22.267 1   15.94  ? 213 ILE   B N    1 
ATOM   4024 C  CA   . ILE   B 1 213 ? -7.965  -16.452 -22.176 1   17.162 ? 213 ILE   B CA   1 
ATOM   4025 C  C    . ILE   B 1 213 ? -8.264  -15.504 -23.334 1   17.346 ? 213 ILE   B C    1 
ATOM   4026 O  O    . ILE   B 1 213 ? -9.385  -15.495 -23.852 1   18.917 ? 213 ILE   B O    1 
ATOM   4027 C  CB   . ILE   B 1 213 ? -8.226  -15.807 -20.805 1   18.2   ? 213 ILE   B CB   1 
ATOM   4028 C  CG1  . ILE   B 1 213 ? -8.215  -16.872 -19.7   1   19.449 ? 213 ILE   B CG1  1 
ATOM   4029 C  CG2  . ILE   B 1 213 ? -9.535  -15.011 -20.812 1   19.261 ? 213 ILE   B CG2  1 
ATOM   4030 C  CD1  . ILE   B 1 213 ? -8.132  -16.307 -18.292 1   20.144 ? 213 ILE   B CD1  1 
ATOM   4031 N  N    . ASN   B 1 214 ? -7.259  -14.723 -23.735 1   16.411 ? 214 ASN   B N    1 
ATOM   4032 C  CA   . ASN   B 1 214 ? -7.401  -13.753 -24.812 1   17.721 ? 214 ASN   B CA   1 
ATOM   4033 C  C    . ASN   B 1 214 ? -7.053  -14.334 -26.185 1   18.394 ? 214 ASN   B C    1 
ATOM   4034 O  O    . ASN   B 1 214 ? -6.952  -13.579 -27.147 1   20.324 ? 214 ASN   B O    1 
ATOM   4035 C  CB   . ASN   B 1 214 ? -6.593  -12.499 -24.508 1   18.623 ? 214 ASN   B CB   1 
ATOM   4036 C  CG   . ASN   B 1 214 ? -7.341  -11.589 -23.573 1   20.887 ? 214 ASN   B CG   1 
ATOM   4037 O  OD1  . ASN   B 1 214 ? -8.12   -10.749 -24.042 1   24.983 ? 214 ASN   B OD1  1 
ATOM   4038 N  ND2  . ASN   B 1 214 ? -7.184  -11.792 -22.27  1   21.269 ? 214 ASN   B ND2  1 
ATOM   4039 N  N    . GLY   B 1 215 ? -6.875  -15.655 -26.291 1   18.552 ? 215 GLY   B N    1 
ATOM   4040 C  CA   . GLY   B 1 215 ? -6.79   -16.321 -27.586 1   20.07  ? 215 GLY   B CA   1 
ATOM   4041 C  C    . GLY   B 1 215 ? -5.371  -16.585 -28.116 1   20.744 ? 215 GLY   B C    1 
ATOM   4042 O  O    . GLY   B 1 215 ? -5.223  -17.071 -29.236 1   23.41  ? 215 GLY   B O    1 
ATOM   4043 N  N    . ASP   B 1 216 ? -4.337  -16.294 -27.314 1   20.68  ? 216 ASP   B N    1 
ATOM   4044 C  CA   . ASP   B 1 216 ? -2.946  -16.464 -27.699 1   22.13  ? 216 ASP   B CA   1 
ATOM   4045 C  C    . ASP   B 1 216 ? -2.465  -17.803 -27.138 1   22.751 ? 216 ASP   B C    1 
ATOM   4046 O  O    . ASP   B 1 216 ? -2.322  -17.901 -25.927 1   23.857 ? 216 ASP   B O    1 
ATOM   4047 C  CB   . ASP   B 1 216 ? -2.156  -15.285 -27.146 1   25.194 ? 216 ASP   B CB   1 
ATOM   4048 C  CG   . ASP   B 1 216 ? -1.256  -14.53  -28.11  1   28.468 ? 216 ASP   B CG   1 
ATOM   4049 O  OD1  . ASP   B 1 216 ? -0.999  -15.074 -29.195 1   32.48  ? 216 ASP   B OD1  1 
ATOM   4050 O  OD2  . ASP   B 1 216 ? -0.832  -13.399 -27.758 1   30.871 ? 216 ASP   B OD2  1 
ATOM   4051 N  N    . ARG   B 1 217 ? -2.248  -18.821 -27.99  1   22.651 ? 217 ARG   B N    1 
ATOM   4052 C  CA   . ARG   B 1 217 ? -2.084  -20.198 -27.53  1   23.692 ? 217 ARG   B CA   1 
ATOM   4053 C  C    . ARG   B 1 217 ? -0.869  -20.906 -28.134 1   20.828 ? 217 ARG   B C    1 
ATOM   4054 O  O    . ARG   B 1 217 ? -0.657  -22.084 -27.872 1   21.871 ? 217 ARG   B O    1 
ATOM   4055 C  CB   . ARG   B 1 217 ? -3.277  -21.07  -27.955 1   26.665 ? 217 ARG   B CB   1 
ATOM   4056 C  CG   . ARG   B 1 217 ? -4.639  -20.569 -27.506 1   28.011 ? 217 ARG   B CG   1 
ATOM   4057 C  CD   . ARG   B 1 217 ? -5.747  -21.539 -27.865 1   29.429 ? 217 ARG   B CD   1 
ATOM   4058 N  NE   . ARG   B 1 217 ? -5.586  -22.831 -27.192 1   29.922 ? 217 ARG   B NE   1 
ATOM   4059 C  CZ   . ARG   B 1 217 ? -6.225  -23.226 -26.093 1   28.788 ? 217 ARG   B CZ   1 
ATOM   4060 N  NH1  . ARG   B 1 217 ? -6.989  -22.392 -25.407 1   27.588 ? 217 ARG   B NH1  1 
ATOM   4061 N  NH2  . ARG   B 1 217 ? -6.069  -24.464 -25.665 1   29.79  ? 217 ARG   B NH2  1 
ATOM   4062 N  N    . TRP   B 1 218 ? -0.062  -20.208 -28.934 1   19.265 ? 218 TRP   B N    1 
ATOM   4063 C  CA   . TRP   B 1 218 ? 0.972   -20.857 -29.73  1   18.825 ? 218 TRP   B CA   1 
ATOM   4064 C  C    . TRP   B 1 218 ? 2.041   -21.528 -28.866 1   18.308 ? 218 TRP   B C    1 
ATOM   4065 O  O    . TRP   B 1 218 ? 2.739   -22.433 -29.333 1   20.246 ? 218 TRP   B O    1 
ATOM   4066 C  CB   . TRP   B 1 218 ? 1.614   -19.851 -30.696 1   18.455 ? 218 TRP   B CB   1 
ATOM   4067 C  CG   . TRP   B 1 218 ? 2.331   -18.695 -30.047 1   17.76  ? 218 TRP   B CG   1 
ATOM   4068 C  CD1  . TRP   B 1 218 ? 1.873   -17.415 -29.903 1   18.063 ? 218 TRP   B CD1  1 
ATOM   4069 C  CD2  . TRP   B 1 218 ? 3.656   -18.711 -29.468 1   17.624 ? 218 TRP   B CD2  1 
ATOM   4070 N  NE1  . TRP   B 1 218 ? 2.806   -16.644 -29.264 1   17.574 ? 218 TRP   B NE1  1 
ATOM   4071 C  CE2  . TRP   B 1 218 ? 3.91    -17.404 -28.996 1   17.767 ? 218 TRP   B CE2  1 
ATOM   4072 C  CE3  . TRP   B 1 218 ? 4.646   -19.685 -29.314 1   18.498 ? 218 TRP   B CE3  1 
ATOM   4073 C  CZ2  . TRP   B 1 218 ? 5.112   -17.049 -28.388 1   17.66  ? 218 TRP   B CZ2  1 
ATOM   4074 C  CZ3  . TRP   B 1 218 ? 5.831   -19.335 -28.703 1   18.648 ? 218 TRP   B CZ3  1 
ATOM   4075 C  CH2  . TRP   B 1 218 ? 6.049   -18.041 -28.238 1   18.051 ? 218 TRP   B CH2  1 
ATOM   4076 N  N    . PHE   B 1 219 ? 2.187   -21.069 -27.619 1   16.505 ? 219 PHE   B N    1 
ATOM   4077 C  CA   . PHE   B 1 219 ? 3.24    -21.561 -26.74  1   15.883 ? 219 PHE   B CA   1 
ATOM   4078 C  C    . PHE   B 1 219 ? 2.793   -22.787 -25.934 1   16.092 ? 219 PHE   B C    1 
ATOM   4079 O  O    . PHE   B 1 219 ? 3.612   -23.367 -25.226 1   16.474 ? 219 PHE   B O    1 
ATOM   4080 C  CB   . PHE   B 1 219 ? 3.678   -20.435 -25.802 1   15.281 ? 219 PHE   B CB   1 
ATOM   4081 C  CG   . PHE   B 1 219 ? 2.502   -19.769 -25.104 1   15.237 ? 219 PHE   B CG   1 
ATOM   4082 C  CD1  . PHE   B 1 219 ? 1.926   -20.326 -23.962 1   15.434 ? 219 PHE   B CD1  1 
ATOM   4083 C  CD2  . PHE   B 1 219 ? 1.952   -18.603 -25.608 1   15.011 ? 219 PHE   B CD2  1 
ATOM   4084 C  CE1  . PHE   B 1 219 ? 0.833   -19.726 -23.349 1   15.417 ? 219 PHE   B CE1  1 
ATOM   4085 C  CE2  . PHE   B 1 219 ? 0.879   -17.994 -24.974 1   15.309 ? 219 PHE   B CE2  1 
ATOM   4086 C  CZ   . PHE   B 1 219 ? 0.312   -18.569 -23.859 1   15.668 ? 219 PHE   B CZ   1 
ATOM   4087 N  N    . LEU   B 1 220 ? 1.512   -23.177 -26.013 1   16.313 ? 220 LEU   B N    1 
ATOM   4088 C  CA   . LEU   B 1 220 ? 1.041   -24.394 -25.368 1   16.632 ? 220 LEU   B CA   1 
ATOM   4089 C  C    . LEU   B 1 220 ? 1.628   -25.625 -26.063 1   16.704 ? 220 LEU   B C    1 
ATOM   4090 O  O    . LEU   B 1 220 ? 1.914   -25.616 -27.266 1   18.123 ? 220 LEU   B O    1 
ATOM   4091 C  CB   . LEU   B 1 220 ? -0.485  -24.459 -25.34  1   17.429 ? 220 LEU   B CB   1 
ATOM   4092 C  CG   . LEU   B 1 220 ? -1.196  -23.303 -24.634 1   18.048 ? 220 LEU   B CG   1 
ATOM   4093 C  CD1  . LEU   B 1 220 ? -2.704  -23.475 -24.788 1   19.537 ? 220 LEU   B CD1  1 
ATOM   4094 C  CD2  . LEU   B 1 220 ? -0.796  -23.218 -23.161 1   18.03  ? 220 LEU   B CD2  1 
ATOM   4095 N  N    . ASN   B 1 221 ? 1.818   -26.69  -25.27  1   16.402 ? 221 ASN   B N    1 
ATOM   4096 C  CA   . ASN   B 1 221 ? 2.413   -27.917 -25.763 1   15.568 ? 221 ASN   B CA   1 
ATOM   4097 C  C    . ASN   B 1 221 ? 1.799   -29.105 -25.027 1   14.493 ? 221 ASN   B C    1 
ATOM   4098 O  O    . ASN   B 1 221 ? 1.006   -28.929 -24.101 1   15.653 ? 221 ASN   B O    1 
ATOM   4099 C  CB   . ASN   B 1 221 ? 3.937   -27.865 -25.711 1   16.141 ? 221 ASN   B CB   1 
ATOM   4100 C  CG   . ASN   B 1 221 ? 4.506   -27.792 -24.31  1   16.782 ? 221 ASN   B CG   1 
ATOM   4101 O  OD1  . ASN   B 1 221 ? 3.935   -28.335 -23.356 1   16.078 ? 221 ASN   B OD1  1 
ATOM   4102 N  ND2  . ASN   B 1 221 ? 5.62    -27.092 -24.161 1   18.047 ? 221 ASN   B ND2  1 
ATOM   4103 N  N    . ARG   B 1 222 ? 2.202   -30.318 -25.408 1   13.23  ? 222 ARG   B N    1 
ATOM   4104 C  CA   . ARG   B 1 222 ? 1.618   -31.534 -24.86  1   13.127 ? 222 ARG   B CA   1 
ATOM   4105 C  C    . ARG   B 1 222 ? 2.254   -31.942 -23.53  1   12.819 ? 222 ARG   B C    1 
ATOM   4106 O  O    . ARG   B 1 222 ? 1.824   -32.927 -22.93  1   12.933 ? 222 ARG   B O    1 
ATOM   4107 C  CB   . ARG   B 1 222 ? 1.777   -32.727 -25.804 1   13.481 ? 222 ARG   B CB   1 
ATOM   4108 C  CG   . ARG   B 1 222 ? 3.22    -33.159 -26.02  1   13.772 ? 222 ARG   B CG   1 
ATOM   4109 C  CD   . ARG   B 1 222 ? 3.349   -34.604 -26.458 1   14.832 ? 222 ARG   B CD   1 
ATOM   4110 N  NE   . ARG   B 1 222 ? 2.753   -34.787 -27.777 1   15.222 ? 222 ARG   B NE   1 
ATOM   4111 C  CZ   . ARG   B 1 222 ? 1.952   -35.769 -28.164 1   14.688 ? 222 ARG   B CZ   1 
ATOM   4112 N  NH1  . ARG   B 1 222 ? 1.646   -36.785 -27.372 1   13.104 ? 222 ARG   B NH1  1 
ATOM   4113 N  NH2  . ARG   B 1 222 ? 1.458   -35.726 -29.383 1   16.499 ? 222 ARG   B NH2  1 
ATOM   4114 N  N    . PHE   B 1 223 ? 3.288   -31.214 -23.095 1   12.709 ? 223 PHE   B N    1 
ATOM   4115 C  CA   . PHE   B 1 223 ? 4.152   -31.693 -22.033 1   13.417 ? 223 PHE   B CA   1 
ATOM   4116 C  C    . PHE   B 1 223 ? 3.74    -31.136 -20.675 1   14.173 ? 223 PHE   B C    1 
ATOM   4117 O  O    . PHE   B 1 223 ? 3.046   -30.126 -20.551 1   14.144 ? 223 PHE   B O    1 
ATOM   4118 C  CB   . PHE   B 1 223 ? 5.606   -31.319 -22.332 1   13.666 ? 223 PHE   B CB   1 
ATOM   4119 C  CG   . PHE   B 1 223 ? 6.073   -31.873 -23.664 1   13.907 ? 223 PHE   B CG   1 
ATOM   4120 C  CD1  . PHE   B 1 223 ? 6.296   -33.235 -23.817 1   13.536 ? 223 PHE   B CD1  1 
ATOM   4121 C  CD2  . PHE   B 1 223 ? 6.302   -31.038 -24.756 1   14.423 ? 223 PHE   B CD2  1 
ATOM   4122 C  CE1  . PHE   B 1 223 ? 6.683   -33.75  -25.048 1   14.269 ? 223 PHE   B CE1  1 
ATOM   4123 C  CE2  . PHE   B 1 223 ? 6.704   -31.562 -25.968 1   15.023 ? 223 PHE   B CE2  1 
ATOM   4124 C  CZ   . PHE   B 1 223 ? 6.895   -32.906 -26.107 1   14.484 ? 223 PHE   B CZ   1 
ATOM   4125 N  N    . THR   B 1 224 ? 4.199   -31.846 -19.646 1   15.63  ? 224 THR   B N    1 
ATOM   4126 C  CA   . THR   B 1 224 ? 4.096   -31.344 -18.295 1   17.019 ? 224 THR   B CA   1 
ATOM   4127 C  C    . THR   B 1 224 ? 5.44    -31.554 -17.608 1   17.731 ? 224 THR   B C    1 
ATOM   4128 O  O    . THR   B 1 224 ? 6.41    -32.021 -18.202 1   19.017 ? 224 THR   B O    1 
ATOM   4129 C  CB   . THR   B 1 224 ? 2.926   -32.025 -17.583 1   18.522 ? 224 THR   B CB   1 
ATOM   4130 O  OG1  . THR   B 1 224 ? 2.668   -31.324 -16.374 1   19.874 ? 224 THR   B OG1  1 
ATOM   4131 C  CG2  . THR   B 1 224 ? 3.188   -33.475 -17.234 1   18.941 ? 224 THR   B CG2  1 
ATOM   4132 N  N    . THR   B 1 225 ? 5.496   -31.145 -16.351 1   18.343 ? 225 THR   B N    1 
ATOM   4133 C  CA   . THR   B 1 225 ? 6.716   -31.309 -15.583 1   19.09  ? 225 THR   B CA   1 
ATOM   4134 C  C    . THR   B 1 225 ? 6.342   -31.493 -14.123 1   19.956 ? 225 THR   B C    1 
ATOM   4135 O  O    . THR   B 1 225 ? 5.172   -31.611 -13.804 1   20.912 ? 225 THR   B O    1 
ATOM   4136 C  CB   . THR   B 1 225 ? 7.621   -30.105 -15.817 1   19.64  ? 225 THR   B CB   1 
ATOM   4137 O  OG1  . THR   B 1 225 ? 8.885   -30.394 -15.221 1   21.612 ? 225 THR   B OG1  1 
ATOM   4138 C  CG2  . THR   B 1 225 ? 7.024   -28.82  -15.272 1   19.316 ? 225 THR   B CG2  1 
ATOM   4139 N  N    . THR   B 1 226 ? 7.355   -31.548 -13.259 1   20.623 ? 226 THR   B N    1 
ATOM   4140 C  CA   . THR   B 1 226 ? 7.137   -31.593 -11.819 1   21.526 ? 226 THR   B CA   1 
ATOM   4141 C  C    . THR   B 1 226 ? 7.598   -30.269 -11.231 1   21.054 ? 226 THR   B C    1 
ATOM   4142 O  O    . THR   B 1 226 ? 8.387   -29.551 -11.84  1   20.627 ? 226 THR   B O    1 
ATOM   4143 C  CB   . THR   B 1 226 ? 7.884   -32.754 -11.159 1   22.96  ? 226 THR   B CB   1 
ATOM   4144 O  OG1  . THR   B 1 226 ? 9.274   -32.478 -11.311 1   23.054 ? 226 THR   B OG1  1 
ATOM   4145 C  CG2  . THR   B 1 226 ? 7.49    -34.105 -11.734 1   24.443 ? 226 THR   B CG2  1 
ATOM   4146 N  N    . LEU   B 1 227 ? 7.13    -29.976 -10.015 1   21.283 ? 227 LEU   B N    1 
ATOM   4147 C  CA   . LEU   B 1 227 ? 7.556   -28.771 -9.333  1   22.54  ? 227 LEU   B CA   1 
ATOM   4148 C  C    . LEU   B 1 227 ? 9.072   -28.792 -9.141  1   23.252 ? 227 LEU   B C    1 
ATOM   4149 O  O    . LEU   B 1 227 ? 9.735   -27.793 -9.395  1   22.934 ? 227 LEU   B O    1 
ATOM   4150 C  CB   . LEU   B 1 227 ? 6.793   -28.648 -8.017  1   24.204 ? 227 LEU   B CB   1 
ATOM   4151 C  CG   . LEU   B 1 227 ? 6.739   -27.259 -7.387  1   26.309 ? 227 LEU   B CG   1 
ATOM   4152 C  CD1  . LEU   B 1 227 ? 6.301   -26.195 -8.379  1   26.715 ? 227 LEU   B CD1  1 
ATOM   4153 C  CD2  . LEU   B 1 227 ? 5.817   -27.256 -6.179  1   27.99  ? 227 LEU   B CD2  1 
ATOM   4154 N  N    A ASN   B 1 228 ? 9.632   -29.931 -8.728  0.5 22.936 ? 228 ASN   B N    1 
ATOM   4155 N  N    B ASN   B 1 228 ? 9.6     -29.95  -8.715  0.5 23.231 ? 228 ASN   B N    1 
ATOM   4156 C  CA   A ASN   B 1 228 ? 11.067  -29.992 -8.486  0.5 24.236 ? 228 ASN   B CA   1 
ATOM   4157 C  CA   B ASN   B 1 228 ? 11.025  -30.16  -8.488  0.5 24.889 ? 228 ASN   B CA   1 
ATOM   4158 C  C    A ASN   B 1 228 ? 11.854  -29.729 -9.774  0.5 23.831 ? 228 ASN   B C    1 
ATOM   4159 C  C    B ASN   B 1 228 ? 11.848  -29.817 -9.73   0.5 24.186 ? 228 ASN   B C    1 
ATOM   4160 O  O    A ASN   B 1 228 ? 12.785  -28.916 -9.772  0.5 23.608 ? 228 ASN   B O    1 
ATOM   4161 O  O    B ASN   B 1 228 ? 12.811  -29.062 -9.649  0.5 24.73  ? 228 ASN   B O    1 
ATOM   4162 C  CB   A ASN   B 1 228 ? 11.488  -31.308 -7.847  0.5 24.919 ? 228 ASN   B CB   1 
ATOM   4163 C  CB   B ASN   B 1 228 ? 11.311  -31.603 -8.084  0.5 26.095 ? 228 ASN   B CB   1 
ATOM   4164 C  CG   A ASN   B 1 228 ? 11.152  -31.374 -6.376  0.5 26.066 ? 228 ASN   B CG   1 
ATOM   4165 C  CG   B ASN   B 1 228 ? 12.788  -31.887 -7.933  0.5 28.054 ? 228 ASN   B CG   1 
ATOM   4166 O  OD1  A ASN   B 1 228 ? 10.782  -30.364 -5.766  0.5 27.066 ? 228 ASN   B OD1  1 
ATOM   4167 O  OD1  B ASN   B 1 228 ? 13.386  -31.55  -6.906  0.5 29.162 ? 228 ASN   B OD1  1 
ATOM   4168 N  ND2  A ASN   B 1 228 ? 11.287  -32.55  -5.786  0.5 27.211 ? 228 ASN   B ND2  1 
ATOM   4169 N  ND2  B ASN   B 1 228 ? 13.388  -32.528 -8.926  0.5 28.953 ? 228 ASN   B ND2  1 
ATOM   4170 N  N    . ASP   B 1 229 ? 11.468  -30.393 -10.876 1   24.099 ? 229 ASP   B N    1 
ATOM   4171 C  CA   . ASP   B 1 229 ? 12.208  -30.246 -12.124 1   24.087 ? 229 ASP   B CA   1 
ATOM   4172 C  C    . ASP   B 1 229 ? 12.105  -28.805 -12.628 1   22.858 ? 229 ASP   B C    1 
ATOM   4173 O  O    . ASP   B 1 229 ? 13.075  -28.234 -13.129 1   22.625 ? 229 ASP   B O    1 
ATOM   4174 C  CB   . ASP   B 1 229 ? 11.725  -31.215 -13.193 1   26.42  ? 229 ASP   B CB   1 
ATOM   4175 C  CG   . ASP   B 1 229 ? 12.159  -32.669 -13.082 1   29.879 ? 229 ASP   B CG   1 
ATOM   4176 O  OD1  . ASP   B 1 229 ? 12.903  -33.009 -12.137 1   32.858 ? 229 ASP   B OD1  1 
ATOM   4177 O  OD2  . ASP   B 1 229 ? 11.749  -33.457 -13.968 1   32.765 ? 229 ASP   B OD2  1 
ATOM   4178 N  N    . PHE   B 1 230 ? 10.91   -28.217 -12.511 1   20.605 ? 230 PHE   B N    1 
ATOM   4179 C  CA   . PHE   B 1 230 ? 10.714  -26.866 -13     1   19.795 ? 230 PHE   B CA   1 
ATOM   4180 C  C    . PHE   B 1 230 ? 11.55   -25.88  -12.184 1   19.333 ? 230 PHE   B C    1 
ATOM   4181 O  O    . PHE   B 1 230 ? 12.115  -24.94  -12.739 1   19.998 ? 230 PHE   B O    1 
ATOM   4182 C  CB   . PHE   B 1 230 ? 9.237   -26.473 -12.987 1   19.832 ? 230 PHE   B CB   1 
ATOM   4183 C  CG   . PHE   B 1 230 ? 9.109   -25.021 -13.402 1   20.548 ? 230 PHE   B CG   1 
ATOM   4184 C  CD1  . PHE   B 1 230 ? 9.202   -24.651 -14.743 1   21.241 ? 230 PHE   B CD1  1 
ATOM   4185 C  CD2  . PHE   B 1 230 ? 8.938   -24.03  -12.446 1   22.297 ? 230 PHE   B CD2  1 
ATOM   4186 C  CE1  . PHE   B 1 230 ? 9.119   -23.317 -15.104 1   21.137 ? 230 PHE   B CE1  1 
ATOM   4187 C  CE2  . PHE   B 1 230 ? 8.867   -22.702 -12.82  1   23.268 ? 230 PHE   B CE2  1 
ATOM   4188 C  CZ   . PHE   B 1 230 ? 8.942   -22.351 -14.143 1   23.061 ? 230 PHE   B CZ   1 
ATOM   4189 N  N    . ASN   B 1 231 ? 11.626  -26.081 -10.865 1   18.933 ? 231 ASN   B N    1 
ATOM   4190 C  CA   . ASN   B 1 231 ? 12.398  -25.182 -10.022 1   20.218 ? 231 ASN   B CA   1 
ATOM   4191 C  C    . ASN   B 1 231 ? 13.886  -25.236 -10.37  1   20.833 ? 231 ASN   B C    1 
ATOM   4192 O  O    . ASN   B 1 231 ? 14.554  -24.216 -10.251 1   21.972 ? 231 ASN   B O    1 
ATOM   4193 C  CB   . ASN   B 1 231 ? 12.065  -25.368 -8.543  1   21.304 ? 231 ASN   B CB   1 
ATOM   4194 C  CG   . ASN   B 1 231 ? 10.806  -24.616 -8.178  1   22.931 ? 231 ASN   B CG   1 
ATOM   4195 O  OD1  . ASN   B 1 231 ? 10.564  -23.522 -8.695  1   26.411 ? 231 ASN   B OD1  1 
ATOM   4196 N  ND2  . ASN   B 1 231 ? 9.936   -25.21  -7.38   1   22.848 ? 231 ASN   B ND2  1 
ATOM   4197 N  N    . LEU   B 1 232 ? 14.405  -26.366 -10.856 1   22.224 ? 232 LEU   B N    1 
ATOM   4198 C  CA   . LEU   B 1 232 ? 15.784  -26.391 -11.338 1   24.185 ? 232 LEU   B CA   1 
ATOM   4199 C  C    . LEU   B 1 232 ? 15.94   -25.433 -12.523 1   23.782 ? 232 LEU   B C    1 
ATOM   4200 O  O    . LEU   B 1 232 ? 16.939  -24.724 -12.634 1   24.809 ? 232 LEU   B O    1 
ATOM   4201 C  CB   . LEU   B 1 232 ? 16.226  -27.807 -11.71  1   26.041 ? 232 LEU   B CB   1 
ATOM   4202 C  CG   . LEU   B 1 232 ? 16.286  -28.815 -10.558 1   29.119 ? 232 LEU   B CG   1 
ATOM   4203 C  CD1  . LEU   B 1 232 ? 16.395  -30.238 -11.073 1   29.874 ? 232 LEU   B CD1  1 
ATOM   4204 C  CD2  . LEU   B 1 232 ? 17.445  -28.506 -9.634  1   30.836 ? 232 LEU   B CD2  1 
ATOM   4205 N  N    . VAL   B 1 233 ? 14.947  -25.402 -13.415 1   22.977 ? 233 VAL   B N    1 
ATOM   4206 C  CA   . VAL   B 1 233 ? 14.956  -24.511 -14.568 1   22.055 ? 233 VAL   B CA   1 
ATOM   4207 C  C    . VAL   B 1 233 ? 14.832  -23.053 -14.131 1   20.983 ? 233 VAL   B C    1 
ATOM   4208 O  O    . VAL   B 1 233 ? 15.579  -22.199 -14.601 1   20.87  ? 233 VAL   B O    1 
ATOM   4209 C  CB   . VAL   B 1 233 ? 13.834  -24.879 -15.562 1   23.265 ? 233 VAL   B CB   1 
ATOM   4210 C  CG1  . VAL   B 1 233 ? 13.761  -23.904 -16.73  1   23.375 ? 233 VAL   B CG1  1 
ATOM   4211 C  CG2  . VAL   B 1 233 ? 13.964  -26.309 -16.074 1   22.909 ? 233 VAL   B CG2  1 
ATOM   4212 N  N    . ALA   B 1 234 ? 13.894  -22.757 -13.23  1   20.991 ? 234 ALA   B N    1 
ATOM   4213 C  CA   . ALA   B 1 234 ? 13.697  -21.39  -12.765 1   21.481 ? 234 ALA   B CA   1 
ATOM   4214 C  C    . ALA   B 1 234 ? 15.006  -20.818 -12.219 1   22.183 ? 234 ALA   B C    1 
ATOM   4215 O  O    . ALA   B 1 234 ? 15.394  -19.69  -12.525 1   21.652 ? 234 ALA   B O    1 
ATOM   4216 C  CB   . ALA   B 1 234 ? 12.607  -21.356 -11.711 1   22.385 ? 234 ALA   B CB   1 
ATOM   4217 N  N    . MET   B 1 235 ? 15.701  -21.632 -11.42  1   23.264 ? 235 MET   B N    1 
ATOM   4218 C  CA   . MET   B 1 235 ? 16.922  -21.175 -10.779 1   24.662 ? 235 MET   B CA   1 
ATOM   4219 C  C    . MET   B 1 235 ? 17.948  -20.812 -11.852 1   23.035 ? 235 MET   B C    1 
ATOM   4220 O  O    . MET   B 1 235 ? 18.628  -19.795 -11.746 1   22.946 ? 235 MET   B O    1 
ATOM   4221 C  CB   . MET   B 1 235 ? 17.459  -22.245 -9.826  1   27.506 ? 235 MET   B CB   1 
ATOM   4222 C  CG   . MET   B 1 235 ? 18.681  -21.831 -9.015  1   31.248 ? 235 MET   B CG   1 
ATOM   4223 S  SD   . MET   B 1 235 ? 19.107  -23.051 -7.755  1   38.402 ? 235 MET   B SD   1 
ATOM   4224 C  CE   . MET   B 1 235 ? 17.662  -23.022 -6.683  1   38.112 ? 235 MET   B CE   1 
ATOM   4225 N  N    . LYS   B 1 236 ? 17.995  -21.621 -12.92  1   22.173 ? 236 LYS   B N    1 
ATOM   4226 C  CA   . LYS   B 1 236 ? 18.978  -21.439 -13.974 1   22.515 ? 236 LYS   B CA   1 
ATOM   4227 C  C    . LYS   B 1 236 ? 18.759  -20.105 -14.693 1   20.956 ? 236 LYS   B C    1 
ATOM   4228 O  O    . LYS   B 1 236 ? 19.719  -19.479 -15.147 1   22.32  ? 236 LYS   B O    1 
ATOM   4229 C  CB   . LYS   B 1 236 ? 18.923  -22.64  -14.928 1   24.748 ? 236 LYS   B CB   1 
ATOM   4230 C  CG   . LYS   B 1 236 ? 19.755  -22.503 -16.201 1   27.632 ? 236 LYS   B CG   1 
ATOM   4231 C  CD   . LYS   B 1 236 ? 19.839  -23.756 -17.066 1   30.624 ? 236 LYS   B CD   1 
ATOM   4232 C  CE   . LYS   B 1 236 ? 20.422  -23.442 -18.412 1   33.781 ? 236 LYS   B CE   1 
ATOM   4233 N  NZ   . LYS   B 1 236 ? 20.484  -24.616 -19.285 1   36.542 ? 236 LYS   B NZ   1 
ATOM   4234 N  N    . TYR   B 1 237 ? 17.494  -19.673 -14.789 1   18.408 ? 237 TYR   B N    1 
ATOM   4235 C  CA   . TYR   B 1 237 ? 17.154  -18.479 -15.546 1   18.403 ? 237 TYR   B CA   1 
ATOM   4236 C  C    . TYR   B 1 237 ? 16.87   -17.272 -14.648 1   17.959 ? 237 TYR   B C    1 
ATOM   4237 O  O    . TYR   B 1 237 ? 16.319  -16.273 -15.121 1   17.591 ? 237 TYR   B O    1 
ATOM   4238 C  CB   . TYR   B 1 237 ? 15.972  -18.823 -16.463 1   18.638 ? 237 TYR   B CB   1 
ATOM   4239 C  CG   . TYR   B 1 237 ? 16.397  -19.701 -17.631 1   19.256 ? 237 TYR   B CG   1 
ATOM   4240 C  CD1  . TYR   B 1 237 ? 16.91   -19.137 -18.793 1   20.419 ? 237 TYR   B CD1  1 
ATOM   4241 C  CD2  . TYR   B 1 237 ? 16.289  -21.087 -17.576 1   20.129 ? 237 TYR   B CD2  1 
ATOM   4242 C  CE1  . TYR   B 1 237 ? 17.342  -19.923 -19.846 1   21.036 ? 237 TYR   B CE1  1 
ATOM   4243 C  CE2  . TYR   B 1 237 ? 16.705  -21.884 -18.629 1   21.489 ? 237 TYR   B CE2  1 
ATOM   4244 C  CZ   . TYR   B 1 237 ? 17.23   -21.299 -19.769 1   20.997 ? 237 TYR   B CZ   1 
ATOM   4245 O  OH   . TYR   B 1 237 ? 17.654  -22.048 -20.832 1   22.854 ? 237 TYR   B OH   1 
ATOM   4246 N  N    . ASN   B 1 238 ? 17.231  -17.364 -13.356 1   17.153 ? 238 ASN   B N    1 
ATOM   4247 C  CA   . ASN   B 1 238 ? 17.084  -16.23  -12.449 1   18.005 ? 238 ASN   B CA   1 
ATOM   4248 C  C    . ASN   B 1 238 ? 15.606  -15.876 -12.252 1   15.76  ? 238 ASN   B C    1 
ATOM   4249 O  O    . ASN   B 1 238 ? 15.226  -14.709 -12.166 1   15.635 ? 238 ASN   B O    1 
ATOM   4250 C  CB   . ASN   B 1 238 ? 17.922  -15.043 -12.912 1   21.249 ? 238 ASN   B CB   1 
ATOM   4251 C  CG   . ASN   B 1 238 ? 19.276  -15.005 -12.24  1   27.154 ? 238 ASN   B CG   1 
ATOM   4252 O  OD1  . ASN   B 1 238 ? 19.888  -16.049 -11.976 1   30.737 ? 238 ASN   B OD1  1 
ATOM   4253 N  ND2  . ASN   B 1 238 ? 19.743  -13.809 -11.921 1   31.751 ? 238 ASN   B ND2  1 
ATOM   4254 N  N    . TYR   B 1 239 ? 14.79   -16.933 -12.21  1   14.914 ? 239 TYR   B N    1 
ATOM   4255 C  CA   . TYR   B 1 239 ? 13.389  -16.856 -11.84  1   14.274 ? 239 TYR   B CA   1 
ATOM   4256 C  C    . TYR   B 1 239 ? 13.244  -17.257 -10.374 1   15.409 ? 239 TYR   B C    1 
ATOM   4257 O  O    . TYR   B 1 239 ? 13.972  -18.11  -9.884  1   15.97  ? 239 TYR   B O    1 
ATOM   4258 C  CB   . TYR   B 1 239 ? 12.547  -17.786 -12.72  1   13.955 ? 239 TYR   B CB   1 
ATOM   4259 C  CG   . TYR   B 1 239 ? 12.049  -17.152 -14.016 1   13.899 ? 239 TYR   B CG   1 
ATOM   4260 C  CD1  . TYR   B 1 239 ? 12.912  -16.513 -14.9   1   14.032 ? 239 TYR   B CD1  1 
ATOM   4261 C  CD2  . TYR   B 1 239 ? 10.701  -17.183 -14.346 1   14.436 ? 239 TYR   B CD2  1 
ATOM   4262 C  CE1  . TYR   B 1 239 ? 12.451  -15.933 -16.072 1   14.422 ? 239 TYR   B CE1  1 
ATOM   4263 C  CE2  . TYR   B 1 239 ? 10.228  -16.61  -15.517 1   14.95  ? 239 TYR   B CE2  1 
ATOM   4264 C  CZ   . TYR   B 1 239 ? 11.099  -15.973 -16.377 1   14.754 ? 239 TYR   B CZ   1 
ATOM   4265 O  OH   . TYR   B 1 239 ? 10.571  -15.401 -17.503 1   16.182 ? 239 TYR   B OH   1 
ATOM   4266 N  N    . GLU   B 1 240 ? 12.266  -16.648 -9.699  1   15.037 ? 240 GLU   B N    1 
ATOM   4267 C  CA   . GLU   B 1 240 ? 11.932  -17.012 -8.335  1   16.102 ? 240 GLU   B CA   1 
ATOM   4268 C  C    . GLU   B 1 240 ? 11.419  -18.447 -8.284  1   15.959 ? 240 GLU   B C    1 
ATOM   4269 O  O    . GLU   B 1 240 ? 10.796  -18.944 -9.224  1   15.377 ? 240 GLU   B O    1 
ATOM   4270 C  CB   . GLU   B 1 240 ? 10.882  -16.046 -7.788  1   17.776 ? 240 GLU   B CB   1 
ATOM   4271 C  CG   . GLU   B 1 240 ? 11.459  -14.671 -7.467  1   19.426 ? 240 GLU   B CG   1 
ATOM   4272 C  CD   . GLU   B 1 240 ? 12.465  -14.707 -6.321  1   22.234 ? 240 GLU   B CD   1 
ATOM   4273 O  OE1  . GLU   B 1 240 ? 12.055  -15.141 -5.226  1   26.842 ? 240 GLU   B OE1  1 
ATOM   4274 O  OE2  . GLU   B 1 240 ? 13.653  -14.38  -6.511  1   24.819 ? 240 GLU   B OE2  1 
ATOM   4275 N  N    . PRO   B 1 241 ? 11.637  -19.167 -7.165  1   17.286 ? 241 PRO   B N    1 
ATOM   4276 C  CA   . PRO   B 1 241 ? 11.025  -20.48  -6.989  1   18.297 ? 241 PRO   B CA   1 
ATOM   4277 C  C    . PRO   B 1 241 ? 9.506   -20.411 -7.068  1   18.449 ? 241 PRO   B C    1 
ATOM   4278 O  O    . PRO   B 1 241 ? 8.886   -19.422 -6.662  1   17.991 ? 241 PRO   B O    1 
ATOM   4279 C  CB   . PRO   B 1 241 ? 11.485  -20.904 -5.587  1   19.037 ? 241 PRO   B CB   1 
ATOM   4280 C  CG   . PRO   B 1 241 ? 12.756  -20.129 -5.386  1   19.079 ? 241 PRO   B CG   1 
ATOM   4281 C  CD   . PRO   B 1 241 ? 12.493  -18.776 -6.032  1   18.272 ? 241 PRO   B CD   1 
ATOM   4282 N  N    . LEU   B 1 242 ? 8.933   -21.475 -7.637  1   18.355 ? 242 LEU   B N    1 
ATOM   4283 C  CA   . LEU   B 1 242 ? 7.498   -21.671 -7.62   1   17.588 ? 242 LEU   B CA   1 
ATOM   4284 C  C    . LEU   B 1 242 ? 7.172   -22.604 -6.459  1   17.914 ? 242 LEU   B C    1 
ATOM   4285 O  O    . LEU   B 1 242 ? 7.754   -23.677 -6.351  1   19.087 ? 242 LEU   B O    1 
ATOM   4286 C  CB   . LEU   B 1 242 ? 7.046   -22.256 -8.953  1   17.808 ? 242 LEU   B CB   1 
ATOM   4287 C  CG   . LEU   B 1 242 ? 5.536   -22.171 -9.205  1   17.849 ? 242 LEU   B CG   1 
ATOM   4288 C  CD1  . LEU   B 1 242 ? 5.066   -20.726 -9.431  1   18.035 ? 242 LEU   B CD1  1 
ATOM   4289 C  CD2  . LEU   B 1 242 ? 5.167   -23.077 -10.363 1   18.79  ? 242 LEU   B CD2  1 
ATOM   4290 N  N    . THR   B 1 243 ? 6.249   -22.179 -5.598  1   18.396 ? 243 THR   B N    1 
ATOM   4291 C  CA   . THR   B 1 243 ? 5.862   -22.951 -4.428  1   19.316 ? 243 THR   B CA   1 
ATOM   4292 C  C    . THR   B 1 243 ? 4.533   -23.645 -4.692  1   19.24  ? 243 THR   B C    1 
ATOM   4293 O  O    . THR   B 1 243 ? 3.79    -23.284 -5.601  1   19.295 ? 243 THR   B O    1 
ATOM   4294 C  CB   . THR   B 1 243 ? 5.761   -22.065 -3.187  1   19.98  ? 243 THR   B CB   1 
ATOM   4295 O  OG1  . THR   B 1 243 ? 4.645   -21.202 -3.379  1   20.179 ? 243 THR   B OG1  1 
ATOM   4296 C  CG2  . THR   B 1 243 ? 7.025   -21.265 -2.939  1   20.696 ? 243 THR   B CG2  1 
ATOM   4297 N  N    . GLN   B 1 244 ? 4.207   -24.602 -3.822  1   19.889 ? 244 GLN   B N    1 
ATOM   4298 C  CA   . GLN   B 1 244 ? 2.907   -25.244 -3.873  1   21.401 ? 244 GLN   B CA   1 
ATOM   4299 C  C    . GLN   B 1 244 ? 1.802   -24.21  -3.664  1   21.072 ? 244 GLN   B C    1 
ATOM   4300 O  O    . GLN   B 1 244 ? 0.741   -24.327 -4.281  1   21.258 ? 244 GLN   B O    1 
ATOM   4301 C  CB   . GLN   B 1 244 ? 2.786   -26.401 -2.883  1   22.587 ? 244 GLN   B CB   1 
ATOM   4302 C  CG   . GLN   B 1 244 ? 1.48    -27.18  -3.008  1   23.451 ? 244 GLN   B CG   1 
ATOM   4303 C  CD   . GLN   B 1 244 ? 1.306   -27.82  -4.368  1   24.403 ? 244 GLN   B CD   1 
ATOM   4304 O  OE1  . GLN   B 1 244 ? 2.241   -28.414 -4.91   1   25.211 ? 244 GLN   B OE1  1 
ATOM   4305 N  NE2  . GLN   B 1 244 ? 0.127   -27.682 -4.958  1   26.673 ? 244 GLN   B NE2  1 
ATOM   4306 N  N    . ASP   B 1 245 ? 2.046   -23.191 -2.83   1   20.758 ? 245 ASP   B N    1 
ATOM   4307 C  CA   . ASP   B 1 245 ? 1.03    -22.171 -2.631  1   22.305 ? 245 ASP   B CA   1 
ATOM   4308 C  C    . ASP   B 1 245 ? 0.751   -21.441 -3.944  1   20.166 ? 245 ASP   B C    1 
ATOM   4309 O  O    . ASP   B 1 245 ? -0.404  -21.156 -4.242  1   20.473 ? 245 ASP   B O    1 
ATOM   4310 C  CB   . ASP   B 1 245 ? 1.36    -21.162 -1.545  1   24.77  ? 245 ASP   B CB   1 
ATOM   4311 C  CG   . ASP   B 1 245 ? 0.163   -20.316 -1.123  1   29.853 ? 245 ASP   B CG   1 
ATOM   4312 O  OD1  . ASP   B 1 245 ? -0.923  -20.904 -0.923  1   35.388 ? 245 ASP   B OD1  1 
ATOM   4313 O  OD2  . ASP   B 1 245 ? 0.311   -19.078 -0.994  1   35.24  ? 245 ASP   B OD2  1 
ATOM   4314 N  N    . HIS   B 1 246 ? 1.802   -21.144 -4.724  1   18.848 ? 246 HIS   B N    1 
ATOM   4315 C  CA   . HIS   B 1 246 ? 1.635   -20.519 -6.024  1   18.446 ? 246 HIS   B CA   1 
ATOM   4316 C  C    . HIS   B 1 246 ? 0.783   -21.393 -6.948  1   18.224 ? 246 HIS   B C    1 
ATOM   4317 O  O    . HIS   B 1 246 ? -0.092  -20.896 -7.659  1   19.221 ? 246 HIS   B O    1 
ATOM   4318 C  CB   . HIS   B 1 246 ? 2.994   -20.251 -6.679  1   17.653 ? 246 HIS   B CB   1 
ATOM   4319 C  CG   . HIS   B 1 246 ? 3.826   -19.237 -5.98   1   18.243 ? 246 HIS   B CG   1 
ATOM   4320 N  ND1  . HIS   B 1 246 ? 5.203   -19.304 -5.977  1   18.676 ? 246 HIS   B ND1  1 
ATOM   4321 C  CD2  . HIS   B 1 246 ? 3.502   -18.125 -5.307  1   18.39  ? 246 HIS   B CD2  1 
ATOM   4322 C  CE1  . HIS   B 1 246 ? 5.687   -18.263 -5.314  1   18.408 ? 246 HIS   B CE1  1 
ATOM   4323 N  NE2  . HIS   B 1 246 ? 4.671   -17.531 -4.897  1   18.925 ? 246 HIS   B NE2  1 
ATOM   4324 N  N    . VAL   B 1 247 ? 1.056   -22.7   -6.95   1   19.409 ? 247 VAL   B N    1 
ATOM   4325 C  CA   . VAL   B 1 247 ? 0.304   -23.627 -7.781  1   19.921 ? 247 VAL   B CA   1 
ATOM   4326 C  C    . VAL   B 1 247 ? -1.163  -23.595 -7.366  1   21.559 ? 247 VAL   B C    1 
ATOM   4327 O  O    . VAL   B 1 247 ? -2.053  -23.578 -8.212  1   20.722 ? 247 VAL   B O    1 
ATOM   4328 C  CB   . VAL   B 1 247 ? 0.882   -25.054 -7.698  1   21.008 ? 247 VAL   B CB   1 
ATOM   4329 C  CG1  . VAL   B 1 247 ? -0.006  -26.078 -8.398  1   21.458 ? 247 VAL   B CG1  1 
ATOM   4330 C  CG2  . VAL   B 1 247 ? 2.297   -25.11  -8.254  1   21.403 ? 247 VAL   B CG2  1 
ATOM   4331 N  N    . ASP   B 1 248 ? -1.406  -23.61  -6.051  1   21.859 ? 248 ASP   B N    1 
ATOM   4332 C  CA   . ASP   B 1 248 ? -2.759  -23.608 -5.516  1   22.569 ? 248 ASP   B CA   1 
ATOM   4333 C  C    . ASP   B 1 248 ? -3.505  -22.355 -5.965  1   20.954 ? 248 ASP   B C    1 
ATOM   4334 O  O    . ASP   B 1 248 ? -4.656  -22.449 -6.397  1   21.138 ? 248 ASP   B O    1 
ATOM   4335 C  CB   . ASP   B 1 248 ? -2.744  -23.77  -4.006  1   23.876 ? 248 ASP   B CB   1 
ATOM   4336 C  CG   . ASP   B 1 248 ? -2.315  -25.14  -3.506  1   25.433 ? 248 ASP   B CG   1 
ATOM   4337 O  OD1  . ASP   B 1 248 ? -2.243  -26.08  -4.33   1   27.886 ? 248 ASP   B OD1  1 
ATOM   4338 O  OD2  . ASP   B 1 248 ? -2.034  -25.255 -2.294  1   27.912 ? 248 ASP   B OD2  1 
ATOM   4339 N  N    . ILE   B 1 249 ? -2.848  -21.189 -5.872  1   21.251 ? 249 ILE   B N    1 
ATOM   4340 C  CA   . ILE   B 1 249 ? -3.476  -19.914 -6.198  1   21.738 ? 249 ILE   B CA   1 
ATOM   4341 C  C    . ILE   B 1 249 ? -3.882  -19.847 -7.676  1   20.794 ? 249 ILE   B C    1 
ATOM   4342 O  O    . ILE   B 1 249 ? -4.859  -19.172 -8.012  1   21.647 ? 249 ILE   B O    1 
ATOM   4343 C  CB   . ILE   B 1 249 ? -2.531  -18.759 -5.818  1   23.218 ? 249 ILE   B CB   1 
ATOM   4344 C  CG1  . ILE   B 1 249 ? -2.378  -18.61  -4.297  1   25.76  ? 249 ILE   B CG1  1 
ATOM   4345 C  CG2  . ILE   B 1 249 ? -2.98   -17.449 -6.461  1   24.849 ? 249 ILE   B CG2  1 
ATOM   4346 C  CD1  . ILE   B 1 249 ? -1.156  -17.806 -3.872  1   26.943 ? 249 ILE   B CD1  1 
ATOM   4347 N  N    . LEU   B 1 250 ? -3.125  -20.533 -8.549  1   19.428 ? 250 LEU   B N    1 
ATOM   4348 C  CA   . LEU   B 1 250 ? -3.406  -20.557 -9.976  1   19.853 ? 250 LEU   B CA   1 
ATOM   4349 C  C    . LEU   B 1 250 ? -4.486  -21.584 -10.345 1   20.388 ? 250 LEU   B C    1 
ATOM   4350 O  O    . LEU   B 1 250 ? -4.817  -21.736 -11.52  1   20.532 ? 250 LEU   B O    1 
ATOM   4351 C  CB   . LEU   B 1 250 ? -2.092  -20.855 -10.697 1   18.958 ? 250 LEU   B CB   1 
ATOM   4352 C  CG   . LEU   B 1 250 ? -1.055  -19.729 -10.751 1   18.368 ? 250 LEU   B CG   1 
ATOM   4353 C  CD1  . LEU   B 1 250 ? 0.296   -20.289 -11.189 1   18.543 ? 250 LEU   B CD1  1 
ATOM   4354 C  CD2  . LEU   B 1 250 ? -1.466  -18.626 -11.711 1   18.269 ? 250 LEU   B CD2  1 
ATOM   4355 N  N    . GLY   B 1 251 ? -5.03   -22.32  -9.367  1   20.838 ? 251 GLY   B N    1 
ATOM   4356 C  CA   . GLY   B 1 251 ? -6      -23.38  -9.624  1   21.074 ? 251 GLY   B CA   1 
ATOM   4357 C  C    . GLY   B 1 251 ? -7.206  -22.934 -10.457 1   20.241 ? 251 GLY   B C    1 
ATOM   4358 O  O    . GLY   B 1 251 ? -7.607  -23.614 -11.41  1   20.079 ? 251 GLY   B O    1 
ATOM   4359 N  N    . PRO   B 1 252 ? -7.869  -21.806 -10.119 1   20.149 ? 252 PRO   B N    1 
ATOM   4360 C  CA   . PRO   B 1 252 ? -8.976  -21.314 -10.938 1   21.409 ? 252 PRO   B CA   1 
ATOM   4361 C  C    . PRO   B 1 252 ? -8.651  -21.139 -12.42  1   20.894 ? 252 PRO   B C    1 
ATOM   4362 O  O    . PRO   B 1 252 ? -9.435  -21.558 -13.262 1   22.098 ? 252 PRO   B O    1 
ATOM   4363 C  CB   . PRO   B 1 252 ? -9.316  -19.991 -10.22  1   22.14  ? 252 PRO   B CB   1 
ATOM   4364 C  CG   . PRO   B 1 252 ? -8.996  -20.295 -8.782  1   22.467 ? 252 PRO   B CG   1 
ATOM   4365 C  CD   . PRO   B 1 252 ? -7.657  -20.993 -8.906  1   21.006 ? 252 PRO   B CD   1 
ATOM   4366 N  N    . LEU   B 1 253 ? -7.473  -20.582 -12.733 1   19.701 ? 253 LEU   B N    1 
ATOM   4367 C  CA   . LEU   B 1 253 ? -7.074  -20.348 -14.109 1   18.515 ? 253 LEU   B CA   1 
ATOM   4368 C  C    . LEU   B 1 253 ? -6.788  -21.686 -14.786 1   19.03  ? 253 LEU   B C    1 
ATOM   4369 O  O    . LEU   B 1 253 ? -7.118  -21.853 -15.949 1   19.817 ? 253 LEU   B O    1 
ATOM   4370 C  CB   . LEU   B 1 253 ? -5.876  -19.398 -14.148 1   18.647 ? 253 LEU   B CB   1 
ATOM   4371 C  CG   . LEU   B 1 253 ? -6.171  -17.953 -13.732 1   18.809 ? 253 LEU   B CG   1 
ATOM   4372 C  CD1  . LEU   B 1 253 ? -4.934  -17.107 -13.552 1   19.533 ? 253 LEU   B CD1  1 
ATOM   4373 C  CD2  . LEU   B 1 253 ? -7.084  -17.299 -14.763 1   20.296 ? 253 LEU   B CD2  1 
ATOM   4374 N  N    . SER   B 1 254 ? -6.193  -22.642 -14.064 1   18.265 ? 254 SER   B N    1 
ATOM   4375 C  CA   . SER   B 1 254 ? -5.988  -23.986 -14.582 1   18.625 ? 254 SER   B CA   1 
ATOM   4376 C  C    . SER   B 1 254 ? -7.318  -24.618 -14.998 1   19.586 ? 254 SER   B C    1 
ATOM   4377 O  O    . SER   B 1 254 ? -7.43   -25.233 -16.063 1   19.862 ? 254 SER   B O    1 
ATOM   4378 C  CB   . SER   B 1 254 ? -5.263  -24.839 -13.545 1   18.784 ? 254 SER   B CB   1 
ATOM   4379 O  OG   . SER   B 1 254 ? -5.166  -26.213 -13.912 1   20.495 ? 254 SER   B OG   1 
ATOM   4380 N  N    . ALA   B 1 255 ? -8.327  -24.502 -14.124 1   20.79  ? 255 ALA   B N    1 
ATOM   4381 C  CA   . ALA   B 1 255 ? -9.623  -25.121 -14.375 1   21.043 ? 255 ALA   B CA   1 
ATOM   4382 C  C    . ALA   B 1 255 ? -10.312 -24.456 -15.569 1   21.94  ? 255 ALA   B C    1 
ATOM   4383 O  O    . ALA   B 1 255 ? -10.906 -25.132 -16.406 1   22.939 ? 255 ALA   B O    1 
ATOM   4384 C  CB   . ALA   B 1 255 ? -10.474 -25.064 -13.128 1   22.254 ? 255 ALA   B CB   1 
ATOM   4385 N  N    . GLN   B 1 256 ? -10.228 -23.125 -15.645 1   22.023 ? 256 GLN   B N    1 
ATOM   4386 C  CA   . GLN   B 1 256 ? -10.927 -22.363 -16.67  1   22.711 ? 256 GLN   B CA   1 
ATOM   4387 C  C    . GLN   B 1 256 ? -10.379 -22.67  -18.062 1   22.625 ? 256 GLN   B C    1 
ATOM   4388 O  O    . GLN   B 1 256 ? -11.135 -22.646 -19.028 1   23.766 ? 256 GLN   B O    1 
ATOM   4389 C  CB   . GLN   B 1 256 ? -10.803 -20.867 -16.378 1   23.326 ? 256 GLN   B CB   1 
ATOM   4390 C  CG   . GLN   B 1 256 ? -11.456 -19.956 -17.412 1   25.766 ? 256 GLN   B CG   1 
ATOM   4391 C  CD   . GLN   B 1 256 ? -11.248 -18.489 -17.102 1   28.977 ? 256 GLN   B CD   1 
ATOM   4392 O  OE1  . GLN   B 1 256 ? -10.886 -18.096 -15.987 1   33.154 ? 256 GLN   B OE1  1 
ATOM   4393 N  NE2  . GLN   B 1 256 ? -11.467 -17.654 -18.106 1   30.804 ? 256 GLN   B NE2  1 
ATOM   4394 N  N    . THR   B 1 257 ? -9.065  -22.898 -18.165 1   20.437 ? 257 THR   B N    1 
ATOM   4395 C  CA   . THR   B 1 257 ? -8.396  -22.976 -19.456 1   19.604 ? 257 THR   B CA   1 
ATOM   4396 C  C    . THR   B 1 257 ? -8.118  -24.423 -19.835 1   18.836 ? 257 THR   B C    1 
ATOM   4397 O  O    . THR   B 1 257 ? -7.797  -24.685 -20.99  1   19.936 ? 257 THR   B O    1 
ATOM   4398 C  CB   . THR   B 1 257 ? -7.086  -22.179 -19.427 1   19.067 ? 257 THR   B CB   1 
ATOM   4399 O  OG1  . THR   B 1 257 ? -6.241  -22.72  -18.41  1   18.933 ? 257 THR   B OG1  1 
ATOM   4400 C  CG2  . THR   B 1 257 ? -7.315  -20.697 -19.186 1   19.915 ? 257 THR   B CG2  1 
ATOM   4401 N  N    . GLY   B 1 258 ? -8.165  -25.344 -18.866 1   18.372 ? 258 GLY   B N    1 
ATOM   4402 C  CA   . GLY   B 1 258 ? -7.834  -26.73  -19.139 1   19.087 ? 258 GLY   B CA   1 
ATOM   4403 C  C    . GLY   B 1 258 ? -6.326  -26.985 -19.217 1   19.492 ? 258 GLY   B C    1 
ATOM   4404 O  O    . GLY   B 1 258 ? -5.918  -28.041 -19.695 1   20.092 ? 258 GLY   B O    1 
ATOM   4405 N  N    . ILE   B 1 259 ? -5.51   -26.036 -18.735 1   19.804 ? 259 ILE   B N    1 
ATOM   4406 C  CA   . ILE   B 1 259 ? -4.058  -26.157 -18.758 1   19.184 ? 259 ILE   B CA   1 
ATOM   4407 C  C    . ILE   B 1 259 ? -3.581  -26.194 -17.311 1   19.096 ? 259 ILE   B C    1 
ATOM   4408 O  O    . ILE   B 1 259 ? -3.643  -25.184 -16.62  1   18.891 ? 259 ILE   B O    1 
ATOM   4409 C  CB   . ILE   B 1 259 ? -3.413  -24.975 -19.507 1   20.127 ? 259 ILE   B CB   1 
ATOM   4410 C  CG1  . ILE   B 1 259 ? -3.984  -24.828 -20.924 1   22.233 ? 259 ILE   B CG1  1 
ATOM   4411 C  CG2  . ILE   B 1 259 ? -1.889  -25.092 -19.532 1   20.123 ? 259 ILE   B CG2  1 
ATOM   4412 C  CD1  . ILE   B 1 259 ? -3.926  -23.411 -21.439 1   24.066 ? 259 ILE   B CD1  1 
ATOM   4413 N  N    . ALA   B 1 260 ? -3.091  -27.349 -16.865 1   18.086 ? 260 ALA   B N    1 
ATOM   4414 C  CA   . ALA   B 1 260 ? -2.613  -27.462 -15.497 1   18.544 ? 260 ALA   B CA   1 
ATOM   4415 C  C    . ALA   B 1 260 ? -1.414  -26.544 -15.295 1   17.59  ? 260 ALA   B C    1 
ATOM   4416 O  O    . ALA   B 1 260 ? -0.678  -26.261 -16.234 1   16.931 ? 260 ALA   B O    1 
ATOM   4417 C  CB   . ALA   B 1 260 ? -2.283  -28.895 -15.179 1   19.19  ? 260 ALA   B CB   1 
ATOM   4418 N  N    . VAL   B 1 261 ? -1.16   -26.141 -14.049 1   17.904 ? 261 VAL   B N    1 
ATOM   4419 C  CA   . VAL   B 1 261 ? -0.044  -25.255 -13.763 1   17.54  ? 261 VAL   B CA   1 
ATOM   4420 C  C    . VAL   B 1 261 ? 1.266   -25.886 -14.24  1   16.918 ? 261 VAL   B C    1 
ATOM   4421 O  O    . VAL   B 1 261 ? 2.05    -25.205 -14.881 1   15.852 ? 261 VAL   B O    1 
ATOM   4422 C  CB   . VAL   B 1 261 ? 0.038   -24.838 -12.286 1   17.978 ? 261 VAL   B CB   1 
ATOM   4423 C  CG1  . VAL   B 1 261 ? 1.296   -24.03  -12.012 1   18.15  ? 261 VAL   B CG1  1 
ATOM   4424 C  CG2  . VAL   B 1 261 ? -1.192  -24.054 -11.858 1   18.064 ? 261 VAL   B CG2  1 
ATOM   4425 N  N    . LEU   B 1 262 ? 1.521   -27.168 -13.938 1   17.506 ? 262 LEU   B N    1 
ATOM   4426 C  CA   . LEU   B 1 262 ? 2.776   -27.786 -14.357 1   18.126 ? 262 LEU   B CA   1 
ATOM   4427 C  C    . LEU   B 1 262 ? 2.854   -27.97  -15.881 1   17.675 ? 262 LEU   B C    1 
ATOM   4428 O  O    . LEU   B 1 262 ? 3.951   -28.006 -16.439 1   18.635 ? 262 LEU   B O    1 
ATOM   4429 C  CB   . LEU   B 1 262 ? 2.998   -29.082 -13.582 1   18.935 ? 262 LEU   B CB   1 
ATOM   4430 C  CG   . LEU   B 1 262 ? 3.254   -28.912 -12.08  1   20.225 ? 262 LEU   B CG   1 
ATOM   4431 C  CD1  . LEU   B 1 262 ? 3.211   -30.242 -11.358 1   21.172 ? 262 LEU   B CD1  1 
ATOM   4432 C  CD2  . LEU   B 1 262 ? 4.58    -28.218 -11.846 1   19.857 ? 262 LEU   B CD2  1 
ATOM   4433 N  N    . ASP   B 1 263 ? 1.716   -27.999 -16.577 1   18.913 ? 263 ASP   B N    1 
ATOM   4434 C  CA   . ASP   B 1 263 ? 1.7     -27.978 -18.037 1   19.17  ? 263 ASP   B CA   1 
ATOM   4435 C  C    . ASP   B 1 263 ? 2.102   -26.603 -18.568 1   16.429 ? 263 ASP   B C    1 
ATOM   4436 O  O    . ASP   B 1 263 ? 2.87    -26.479 -19.529 1   18.184 ? 263 ASP   B O    1 
ATOM   4437 C  CB   . ASP   B 1 263 ? 0.321   -28.27  -18.59  1   21.949 ? 263 ASP   B CB   1 
ATOM   4438 C  CG   . ASP   B 1 263 ? -0.285  -29.617 -18.259 1   24.679 ? 263 ASP   B CG   1 
ATOM   4439 O  OD1  . ASP   B 1 263 ? 0.387   -30.393 -17.545 1   27.201 ? 263 ASP   B OD1  1 
ATOM   4440 O  OD2  . ASP   B 1 263 ? -1.418  -29.859 -18.735 1   28.729 ? 263 ASP   B OD2  1 
ATOM   4441 N  N    . MET   B 1 264 ? 1.593   -25.555 -17.916 1   17.02  ? 264 MET   B N    1 
ATOM   4442 C  CA   . MET   B 1 264 ? 2.006   -24.204 -18.24  1   15.909 ? 264 MET   B CA   1 
ATOM   4443 C  C    . MET   B 1 264 ? 3.476   -24.005 -17.874 1   15.991 ? 264 MET   B C    1 
ATOM   4444 O  O    . MET   B 1 264 ? 4.176   -23.314 -18.591 1   16.244 ? 264 MET   B O    1 
ATOM   4445 C  CB   . MET   B 1 264 ? 1.123   -23.158 -17.556 1   16.239 ? 264 MET   B CB   1 
ATOM   4446 C  CG   . MET   B 1 264 ? 1.297   -21.773 -18.137 1   15.818 ? 264 MET   B CG   1 
ATOM   4447 S  SD   . MET   B 1 264 ? 0.624   -21.671 -19.806 1   16.487 ? 264 MET   B SD   1 
ATOM   4448 C  CE   . MET   B 1 264 ? -1.073  -21.222 -19.409 1   16.871 ? 264 MET   B CE   1 
ATOM   4449 N  N    . CYS   B 1 265 ? 3.968   -24.632 -16.794 1   16.437 ? 265 CYS   B N    1 
ATOM   4450 C  CA   . CYS   B 1 265 ? 5.396   -24.61  -16.499 1   16.467 ? 265 CYS   B CA   1 
ATOM   4451 C  C    . CYS   B 1 265 ? 6.225   -25.247 -17.606 1   15.961 ? 265 CYS   B C    1 
ATOM   4452 O  O    . CYS   B 1 265 ? 7.302   -24.749 -17.887 1   16.785 ? 265 CYS   B O    1 
ATOM   4453 C  CB   . CYS   B 1 265 ? 5.719   -25.313 -15.191 1   16.457 ? 265 CYS   B CB   1 
ATOM   4454 S  SG   . CYS   B 1 265 ? 5.184   -24.402 -13.719 1   18.082 ? 265 CYS   B SG   1 
ATOM   4455 N  N    . ALA   B 1 266 ? 5.737   -26.327 -18.242 1   16.916 ? 266 ALA   B N    1 
ATOM   4456 C  CA   . ALA   B 1 266 ? 6.423   -26.919 -19.385 1   17.367 ? 266 ALA   B CA   1 
ATOM   4457 C  C    . ALA   B 1 266 ? 6.473   -25.939 -20.561 1   16.625 ? 266 ALA   B C    1 
ATOM   4458 O  O    . ALA   B 1 266 ? 7.493   -25.846 -21.236 1   18.637 ? 266 ALA   B O    1 
ATOM   4459 C  CB   . ALA   B 1 266 ? 5.771   -28.235 -19.761 1   17.212 ? 266 ALA   B CB   1 
ATOM   4460 N  N    . SER   B 1 267 ? 5.413   -25.143 -20.742 1   16.924 ? 267 SER   B N    1 
ATOM   4461 C  CA   . SER   B 1 267 ? 5.419   -24.093 -21.754 1   16.845 ? 267 SER   B CA   1 
ATOM   4462 C  C    . SER   B 1 267 ? 6.483   -23.04  -21.424 1   15.866 ? 267 SER   B C    1 
ATOM   4463 O  O    . SER   B 1 267 ? 7.254   -22.607 -22.281 1   16.362 ? 267 SER   B O    1 
ATOM   4464 C  CB   . SER   B 1 267 ? 4.055   -23.438 -21.898 1   17.596 ? 267 SER   B CB   1 
ATOM   4465 O  OG   . SER   B 1 267 ? 3.115   -24.211 -22.633 1   19.007 ? 267 SER   B OG   1 
ATOM   4466 N  N    . LEU   B 1 268 ? 6.506   -22.603 -20.16  1   16.413 ? 268 LEU   B N    1 
ATOM   4467 C  CA   . LEU   B 1 268 ? 7.446   -21.591 -19.717 1   16.035 ? 268 LEU   B CA   1 
ATOM   4468 C  C    . LEU   B 1 268 ? 8.886   -22.091 -19.841 1   16.494 ? 268 LEU   B C    1 
ATOM   4469 O  O    . LEU   B 1 268 ? 9.74    -21.348 -20.288 1   16.545 ? 268 LEU   B O    1 
ATOM   4470 C  CB   . LEU   B 1 268 ? 7.085   -21.154 -18.298 1   15.379 ? 268 LEU   B CB   1 
ATOM   4471 C  CG   . LEU   B 1 268 ? 8       -20.107 -17.662 1   15.1   ? 268 LEU   B CG   1 
ATOM   4472 C  CD1  . LEU   B 1 268 ? 8.176   -18.892 -18.557 1   14.94  ? 268 LEU   B CD1  1 
ATOM   4473 C  CD2  . LEU   B 1 268 ? 7.4     -19.672 -16.332 1   15.901 ? 268 LEU   B CD2  1 
ATOM   4474 N  N    . LYS   B 1 269 ? 9.156   -23.351 -19.48  1   18.118 ? 269 LYS   B N    1 
ATOM   4475 C  CA   . LYS   B 1 269 ? 10.478  -23.941 -19.648 1   20.168 ? 269 LYS   B CA   1 
ATOM   4476 C  C    . LYS   B 1 269 ? 10.919  -23.81  -21.099 1   19.311 ? 269 LYS   B C    1 
ATOM   4477 O  O    . LYS   B 1 269 ? 12.059  -23.442 -21.362 1   19.937 ? 269 LYS   B O    1 
ATOM   4478 C  CB   . LYS   B 1 269 ? 10.5    -25.413 -19.218 1   21.971 ? 269 LYS   B CB   1 
ATOM   4479 C  CG   . LYS   B 1 269 ? 11.757  -26.193 -19.586 1   24.804 ? 269 LYS   B CG   1 
ATOM   4480 C  CD   . LYS   B 1 269 ? 11.773  -27.636 -19.089 1   26.878 ? 269 LYS   B CD   1 
ATOM   4481 C  CE   . LYS   B 1 269 ? 10.72   -28.494 -19.736 1   27.884 ? 269 LYS   B CE   1 
ATOM   4482 N  NZ   . LYS   B 1 269 ? 10.665  -29.837 -19.165 1   29.542 ? 269 LYS   B NZ   1 
ATOM   4483 N  N    . GLU   B 1 270 ? 10.015  -24.109 -22.043 1   19.382 ? 270 GLU   B N    1 
ATOM   4484 C  CA   . GLU   B 1 270 ? 10.377  -24.093 -23.45  1   19.526 ? 270 GLU   B CA   1 
ATOM   4485 C  C    . GLU   B 1 270 ? 10.66   -22.661 -23.908 1   17.733 ? 270 GLU   B C    1 
ATOM   4486 O  O    . GLU   B 1 270 ? 11.605  -22.441 -24.667 1   19.084 ? 270 GLU   B O    1 
ATOM   4487 C  CB   . GLU   B 1 270 ? 9.321   -24.819 -24.283 1   20.437 ? 270 GLU   B CB   1 
ATOM   4488 C  CG   . GLU   B 1 270 ? 9.176   -26.308 -23.957 1   22.208 ? 270 GLU   B CG   1 
ATOM   4489 C  CD   . GLU   B 1 270 ? 10.424  -27.177 -24.005 1   24.006 ? 270 GLU   B CD   1 
ATOM   4490 O  OE1  . GLU   B 1 270 ? 11.204  -27.009 -24.957 1   27.185 ? 270 GLU   B OE1  1 
ATOM   4491 O  OE2  . GLU   B 1 270 ? 10.621  -28.033 -23.112 1   25.702 ? 270 GLU   B OE2  1 
ATOM   4492 N  N    . LEU   B 1 271 ? 9.873   -21.684 -23.428 1   17.676 ? 271 LEU   B N    1 
ATOM   4493 C  CA   . LEU   B 1 271 ? 10.11   -20.282 -23.751 1   17.436 ? 271 LEU   B CA   1 
ATOM   4494 C  C    . LEU   B 1 271 ? 11.476  -19.832 -23.227 1   17.786 ? 271 LEU   B C    1 
ATOM   4495 O  O    . LEU   B 1 271 ? 12.19   -19.093 -23.9   1   19.892 ? 271 LEU   B O    1 
ATOM   4496 C  CB   . LEU   B 1 271 ? 8.982   -19.405 -23.208 1   17.475 ? 271 LEU   B CB   1 
ATOM   4497 C  CG   . LEU   B 1 271 ? 7.618   -19.578 -23.882 1   17.927 ? 271 LEU   B CG   1 
ATOM   4498 C  CD1  . LEU   B 1 271 ? 6.464   -19.028 -23.059 1   18.028 ? 271 LEU   B CD1  1 
ATOM   4499 C  CD2  . LEU   B 1 271 ? 7.617   -18.937 -25.24  1   18.971 ? 271 LEU   B CD2  1 
ATOM   4500 N  N    . LEU   B 1 272 ? 11.839  -20.245 -22.006 1   18.789 ? 272 LEU   B N    1 
ATOM   4501 C  CA   . LEU   B 1 272 ? 13.113  -19.851 -21.417 1   19.601 ? 272 LEU   B CA   1 
ATOM   4502 C  C    . LEU   B 1 272 ? 14.283  -20.431 -22.209 1   20.461 ? 272 LEU   B C    1 
ATOM   4503 O  O    . LEU   B 1 272 ? 15.281  -19.746 -22.431 1   21.794 ? 272 LEU   B O    1 
ATOM   4504 C  CB   . LEU   B 1 272 ? 13.168  -20.267 -19.947 1   19.456 ? 272 LEU   B CB   1 
ATOM   4505 C  CG   . LEU   B 1 272 ? 12.21   -19.505 -19.026 1   19.065 ? 272 LEU   B CG   1 
ATOM   4506 C  CD1  . LEU   B 1 272 ? 12.17   -20.11  -17.634 1   19.589 ? 272 LEU   B CD1  1 
ATOM   4507 C  CD2  . LEU   B 1 272 ? 12.594  -18.036 -18.996 1   19.037 ? 272 LEU   B CD2  1 
ATOM   4508 N  N    . GLN   B 1 273 ? 14.121  -21.679 -22.658 1   22.372 ? 273 GLN   B N    1 
ATOM   4509 C  CA   . GLN   B 1 273 ? 15.18   -22.424 -23.318 1   23.885 ? 273 GLN   B CA   1 
ATOM   4510 C  C    . GLN   B 1 273 ? 15.322  -21.997 -24.777 1   24.844 ? 273 GLN   B C    1 
ATOM   4511 O  O    . GLN   B 1 273 ? 16.424  -22.072 -25.311 1   27.913 ? 273 GLN   B O    1 
ATOM   4512 C  CB   . GLN   B 1 273 ? 14.927  -23.926 -23.169 1   25.345 ? 273 GLN   B CB   1 
ATOM   4513 C  CG   . GLN   B 1 273 ? 15.165  -24.441 -21.753 1   25.491 ? 273 GLN   B CG   1 
ATOM   4514 C  CD   . GLN   B 1 273 ? 14.825  -25.903 -21.531 1   26.011 ? 273 GLN   B CD   1 
ATOM   4515 O  OE1  . GLN   B 1 273 ? 14.339  -26.63  -22.409 1   28.924 ? 273 GLN   B OE1  1 
ATOM   4516 N  NE2  . GLN   B 1 273 ? 15.068  -26.355 -20.31  1   26.196 ? 273 GLN   B NE2  1 
ATOM   4517 N  N    . ASN   B 1 274 ? 14.227  -21.573 -25.423 1   24.392 ? 274 ASN   B N    1 
ATOM   4518 C  CA   . ASN   B 1 274 ? 14.219  -21.436 -26.876 1   25.074 ? 274 ASN   B CA   1 
ATOM   4519 C  C    . ASN   B 1 274 ? 13.852  -20.027 -27.335 1   25.009 ? 274 ASN   B C    1 
ATOM   4520 O  O    . ASN   B 1 274 ? 14.01   -19.707 -28.511 1   28.489 ? 274 ASN   B O    1 
ATOM   4521 C  CB   . ASN   B 1 274 ? 13.262  -22.44  -27.506 1   26.594 ? 274 ASN   B CB   1 
ATOM   4522 C  CG   . ASN   B 1 274 ? 13.732  -23.854 -27.272 1   27.984 ? 274 ASN   B CG   1 
ATOM   4523 O  OD1  . ASN   B 1 274 ? 14.729  -24.269 -27.871 1   31.848 ? 274 ASN   B OD1  1 
ATOM   4524 N  ND2  . ASN   B 1 274 ? 13.06   -24.599 -26.412 1   28.579 ? 274 ASN   B ND2  1 
ATOM   4525 N  N    . GLY   B 1 275 ? 13.337  -19.195 -26.43  1   23.847 ? 275 GLY   B N    1 
ATOM   4526 C  CA   . GLY   B 1 275 ? 12.799  -17.897 -26.806 1   23.517 ? 275 GLY   B CA   1 
ATOM   4527 C  C    . GLY   B 1 275 ? 11.447  -18.034 -27.506 1   22.706 ? 275 GLY   B C    1 
ATOM   4528 O  O    . GLY   B 1 275 ? 10.84   -19.103 -27.486 1   22.445 ? 275 GLY   B O    1 
ATOM   4529 N  N    . MET   B 1 276 ? 10.997  -16.946 -28.142 1   22.788 ? 276 MET   B N    1 
ATOM   4530 C  CA   . MET   B 1 276 ? 9.683   -16.887 -28.762 1   23.923 ? 276 MET   B CA   1 
ATOM   4531 C  C    . MET   B 1 276 ? 9.727   -17.131 -30.267 1   24.113 ? 276 MET   B C    1 
ATOM   4532 O  O    . MET   B 1 276 ? 8.675   -17.155 -30.901 1   24.086 ? 276 MET   B O    1 
ATOM   4533 C  CB   . MET   B 1 276 ? 9.032   -15.514 -28.561 1   23.53  ? 276 MET   B CB   1 
ATOM   4534 C  CG   . MET   B 1 276 ? 8.719   -15.217 -27.128 1   23.255 ? 276 MET   B CG   1 
ATOM   4535 S  SD   . MET   B 1 276 ? 7.559   -13.844 -26.982 1   21.699 ? 276 MET   B SD   1 
ATOM   4536 C  CE   . MET   B 1 276 ? 7.526   -13.677 -25.194 1   21.846 ? 276 MET   B CE   1 
ATOM   4537 N  N    . ASN   B 1 277 ? 10.929  -17.27  -30.84  1   25.46  ? 277 ASN   B N    1 
ATOM   4538 C  CA   . ASN   B 1 277 ? 11.088  -17.528 -32.263 1   26.712 ? 277 ASN   B CA   1 
ATOM   4539 C  C    . ASN   B 1 277 ? 10.335  -16.475 -33.075 1   25.777 ? 277 ASN   B C    1 
ATOM   4540 O  O    . ASN   B 1 277 ? 9.653   -16.789 -34.047 1   28.282 ? 277 ASN   B O    1 
ATOM   4541 C  CB   . ASN   B 1 277 ? 10.685  -18.953 -32.623 1   29.388 ? 277 ASN   B CB   1 
ATOM   4542 C  CG   . ASN   B 1 277 ? 11.523  -19.986 -31.906 1   33.724 ? 277 ASN   B CG   1 
ATOM   4543 O  OD1  . ASN   B 1 277 ? 10.975  -20.832 -31.189 1   37.693 ? 277 ASN   B OD1  1 
ATOM   4544 N  ND2  . ASN   B 1 277 ? 12.839  -19.929 -32.063 1   35.602 ? 277 ASN   B ND2  1 
ATOM   4545 N  N    . GLY   B 1 278 ? 10.475  -15.21  -32.672 1   25.662 ? 278 GLY   B N    1 
ATOM   4546 C  CA   . GLY   B 1 278 ? 9.975   -14.085 -33.44  1   25.507 ? 278 GLY   B CA   1 
ATOM   4547 C  C    . GLY   B 1 278 ? 8.504   -13.774 -33.175 1   24.535 ? 278 GLY   B C    1 
ATOM   4548 O  O    . GLY   B 1 278 ? 7.984   -12.816 -33.74  1   26.224 ? 278 GLY   B O    1 
ATOM   4549 N  N    . ARG   B 1 279 ? 7.85    -14.551 -32.3   1   23.831 ? 279 ARG   B N    1 
ATOM   4550 C  CA   . ARG   B 1 279 ? 6.443   -14.346 -32     1   22.278 ? 279 ARG   B CA   1 
ATOM   4551 C  C    . ARG   B 1 279 ? 6.296   -13.45  -30.774 1   20.096 ? 279 ARG   B C    1 
ATOM   4552 O  O    . ARG   B 1 279 ? 7.285   -13.093 -30.136 1   21.05  ? 279 ARG   B O    1 
ATOM   4553 C  CB   . ARG   B 1 279 ? 5.76    -15.697 -31.779 1   24.423 ? 279 ARG   B CB   1 
ATOM   4554 C  CG   . ARG   B 1 279 ? 5.709   -16.503 -33.065 1   26.072 ? 279 ARG   B CG   1 
ATOM   4555 C  CD   . ARG   B 1 279 ? 5.251   -17.91  -32.835 1   28.141 ? 279 ARG   B CD   1 
ATOM   4556 N  NE   . ARG   B 1 279 ? 6.324   -18.715 -32.242 1   29.155 ? 279 ARG   B NE   1 
ATOM   4557 C  CZ   . ARG   B 1 279 ? 6.279   -20.036 -32.117 1   31.565 ? 279 ARG   B CZ   1 
ATOM   4558 N  NH1  . ARG   B 1 279 ? 5.259   -20.719 -32.606 1   32.269 ? 279 ARG   B NH1  1 
ATOM   4559 N  NH2  . ARG   B 1 279 ? 7.26    -20.675 -31.502 1   32.898 ? 279 ARG   B NH2  1 
ATOM   4560 N  N    . THR   B 1 280 ? 5.047   -13.062 -30.483 1   17.457 ? 280 THR   B N    1 
ATOM   4561 C  CA   . THR   B 1 280 ? 4.738   -12.278 -29.297 1   16.539 ? 280 THR   B CA   1 
ATOM   4562 C  C    . THR   B 1 280 ? 3.606   -12.936 -28.513 1   15.686 ? 280 THR   B C    1 
ATOM   4563 O  O    . THR   B 1 280 ? 2.9     -13.8   -29.016 1   15.722 ? 280 THR   B O    1 
ATOM   4564 C  CB   . THR   B 1 280 ? 4.367   -10.842 -29.667 1   17.552 ? 280 THR   B CB   1 
ATOM   4565 O  OG1  . THR   B 1 280 ? 3.249   -10.869 -30.552 1   18.766 ? 280 THR   B OG1  1 
ATOM   4566 C  CG2  . THR   B 1 280 ? 5.515   -10.09  -30.308 1   18.78  ? 280 THR   B CG2  1 
ATOM   4567 N  N    . ILE   B 1 281 ? 3.479   -12.515 -27.253 1   14.03  ? 281 ILE   B N    1 
ATOM   4568 C  CA   . ILE   B 1 281 ? 2.403   -12.942 -26.37  1   14.083 ? 281 ILE   B CA   1 
ATOM   4569 C  C    . ILE   B 1 281 ? 1.753   -11.683 -25.816 1   13.928 ? 281 ILE   B C    1 
ATOM   4570 O  O    . ILE   B 1 281 ? 2.437   -10.873 -25.21  1   14.293 ? 281 ILE   B O    1 
ATOM   4571 C  CB   . ILE   B 1 281 ? 2.938   -13.844 -25.241 1   13.998 ? 281 ILE   B CB   1 
ATOM   4572 C  CG1  . ILE   B 1 281 ? 3.612   -15.095 -25.792 1   14.361 ? 281 ILE   B CG1  1 
ATOM   4573 C  CG2  . ILE   B 1 281 ? 1.823   -14.196 -24.251 1   14.04  ? 281 ILE   B CG2  1 
ATOM   4574 C  CD1  . ILE   B 1 281 ? 4.311   -15.949 -24.752 1   14.81  ? 281 ILE   B CD1  1 
ATOM   4575 N  N    . LEU   B 1 282 ? 0.443   -11.502 -26.057 1   14.592 ? 282 LEU   B N    1 
ATOM   4576 C  CA   . LEU   B 1 282 ? -0.249  -10.3   -25.614 1   15.233 ? 282 LEU   B CA   1 
ATOM   4577 C  C    . LEU   B 1 282 ? 0.555   -9.047  -25.956 1   17.085 ? 282 LEU   B C    1 
ATOM   4578 O  O    . LEU   B 1 282 ? 0.67    -8.122  -25.148 1   17.698 ? 282 LEU   B O    1 
ATOM   4579 C  CB   . LEU   B 1 282 ? -0.561  -10.372 -24.12  1   14.998 ? 282 LEU   B CB   1 
ATOM   4580 C  CG   . LEU   B 1 282 ? -1.69   -11.315 -23.719 1   15.195 ? 282 LEU   B CG   1 
ATOM   4581 C  CD1  . LEU   B 1 282 ? -1.8    -11.386 -22.211 1   15.569 ? 282 LEU   B CD1  1 
ATOM   4582 C  CD2  . LEU   B 1 282 ? -3.005  -10.853 -24.314 1   15.068 ? 282 LEU   B CD2  1 
ATOM   4583 N  N    . GLY   B 1 283 ? 1.104   -9.027  -27.176 1   17.483 ? 283 GLY   B N    1 
ATOM   4584 C  CA   . GLY   B 1 283 ? 1.779   -7.849  -27.69  1   18.728 ? 283 GLY   B CA   1 
ATOM   4585 C  C    . GLY   B 1 283 ? 3.177   -7.609  -27.118 1   19.227 ? 283 GLY   B C    1 
ATOM   4586 O  O    . GLY   B 1 283 ? 3.739   -6.54   -27.332 1   23.151 ? 283 GLY   B O    1 
ATOM   4587 N  N    . SER   B 1 284 ? 3.732   -8.595  -26.401 1   16.596 ? 284 SER   B N    1 
ATOM   4588 C  CA   . SER   B 1 284 ? 5.033   -8.473  -25.77  1   16.117 ? 284 SER   B CA   1 
ATOM   4589 C  C    . SER   B 1 284 ? 6.005   -9.502  -26.347 1   14.981 ? 284 SER   B C    1 
ATOM   4590 O  O    . SER   B 1 284 ? 5.637   -10.652 -26.571 1   15.345 ? 284 SER   B O    1 
ATOM   4591 C  CB   . SER   B 1 284 ? 4.892   -8.655  -24.277 1   16.768 ? 284 SER   B CB   1 
ATOM   4592 O  OG   . SER   B 1 284 ? 6.14    -8.482  -23.626 1   18.578 ? 284 SER   B OG   1 
ATOM   4593 N  N    . ALA   B 1 285 ? 7.269   -9.091  -26.501 1   15.607 ? 285 ALA   B N    1 
ATOM   4594 C  CA   . ALA   B 1 285 ? 8.345   -10.003 -26.861 1   15.909 ? 285 ALA   B CA   1 
ATOM   4595 C  C    . ALA   B 1 285 ? 9.133   -10.437 -25.619 1   16.205 ? 285 ALA   B C    1 
ATOM   4596 O  O    . ALA   B 1 285 ? 10.105  -11.177 -25.719 1   18.306 ? 285 ALA   B O    1 
ATOM   4597 C  CB   . ALA   B 1 285 ? 9.25    -9.336  -27.882 1   16.943 ? 285 ALA   B CB   1 
ATOM   4598 N  N    . LEU   B 1 286 ? 8.717   -9.966  -24.438 1   14.921 ? 286 LEU   B N    1 
ATOM   4599 C  CA   . LEU   B 1 286 ? 9.301   -10.38  -23.171 1   15.917 ? 286 LEU   B CA   1 
ATOM   4600 C  C    . LEU   B 1 286 ? 8.243   -11.085 -22.337 1   14.525 ? 286 LEU   B C    1 
ATOM   4601 O  O    . LEU   B 1 286 ? 7.049   -10.898 -22.542 1   15.156 ? 286 LEU   B O    1 
ATOM   4602 C  CB   . LEU   B 1 286 ? 9.797   -9.163  -22.395 1   17.477 ? 286 LEU   B CB   1 
ATOM   4603 C  CG   . LEU   B 1 286 ? 10.903  -8.326  -23.032 1   19.81  ? 286 LEU   B CG   1 
ATOM   4604 C  CD1  . LEU   B 1 286 ? 11.063  -7.057  -22.204 1   20.893 ? 286 LEU   B CD1  1 
ATOM   4605 C  CD2  . LEU   B 1 286 ? 12.196  -9.131  -23.103 1   21.43  ? 286 LEU   B CD2  1 
ATOM   4606 N  N    . LEU   B 1 287 ? 8.7     -11.874 -21.368 1   13.257 ? 287 LEU   B N    1 
ATOM   4607 C  CA   . LEU   B 1 287 ? 7.774   -12.526 -20.459 1   13.43  ? 287 LEU   B CA   1 
ATOM   4608 C  C    . LEU   B 1 287 ? 7.418   -11.56  -19.34  1   13.186 ? 287 LEU   B C    1 
ATOM   4609 O  O    . LEU   B 1 287 ? 8.265   -11.215 -18.53  1   16.231 ? 287 LEU   B O    1 
ATOM   4610 C  CB   . LEU   B 1 287 ? 8.402   -13.826 -19.967 1   14.22  ? 287 LEU   B CB   1 
ATOM   4611 C  CG   . LEU   B 1 287 ? 8.763   -14.821 -21.074 1   15.343 ? 287 LEU   B CG   1 
ATOM   4612 C  CD1  . LEU   B 1 287 ? 9.476   -16.049 -20.543 1   16.469 ? 287 LEU   B CD1  1 
ATOM   4613 C  CD2  . LEU   B 1 287 ? 7.523   -15.234 -21.834 1   16.941 ? 287 LEU   B CD2  1 
ATOM   4614 N  N    . GLU   B 1 288 ? 6.158   -11.129 -19.3   1   12.327 ? 288 GLU   B N    1 
ATOM   4615 C  CA   . GLU   B 1 288 ? 5.713   -10.094 -18.382 1   12.472 ? 288 GLU   B CA   1 
ATOM   4616 C  C    . GLU   B 1 288 ? 5.452   -10.675 -16.993 1   11.351 ? 288 GLU   B C    1 
ATOM   4617 O  O    . GLU   B 1 288 ? 4.789   -11.691 -16.868 1   10.927 ? 288 GLU   B O    1 
ATOM   4618 C  CB   . GLU   B 1 288 ? 4.406   -9.55   -18.941 1   13.986 ? 288 GLU   B CB   1 
ATOM   4619 C  CG   . GLU   B 1 288 ? 3.655   -8.591  -18.028 1   16.243 ? 288 GLU   B CG   1 
ATOM   4620 C  CD   . GLU   B 1 288 ? 4.361   -7.278  -17.84  1   19.246 ? 288 GLU   B CD   1 
ATOM   4621 O  OE1  . GLU   B 1 288 ? 4.518   -6.856  -16.664 1   18.744 ? 288 GLU   B OE1  1 
ATOM   4622 O  OE2  . GLU   B 1 288 ? 4.754   -6.697  -18.898 1   22.297 ? 288 GLU   B OE2  1 
ATOM   4623 N  N    . ASP   B 1 289 ? 5.965   -10.01  -15.949 1   11.196 ? 289 ASP   B N    1 
ATOM   4624 C  CA   . ASP   B 1 289 ? 5.863   -10.536 -14.598 1   10.973 ? 289 ASP   B CA   1 
ATOM   4625 C  C    . ASP   B 1 289 ? 5.239   -9.532  -13.631 1   10.963 ? 289 ASP   B C    1 
ATOM   4626 O  O    . ASP   B 1 289 ? 5.377   -9.743  -12.431 1   11.355 ? 289 ASP   B O    1 
ATOM   4627 C  CB   . ASP   B 1 289 ? 7.207   -11.041 -14.084 1   11.626 ? 289 ASP   B CB   1 
ATOM   4628 C  CG   . ASP   B 1 289 ? 8.211   -9.975  -13.674 1   12.072 ? 289 ASP   B CG   1 
ATOM   4629 O  OD1  . ASP   B 1 289 ? 8.012   -8.783  -14.008 1   12.832 ? 289 ASP   B OD1  1 
ATOM   4630 O  OD2  . ASP   B 1 289 ? 9.17    -10.35  -12.961 1   13.387 ? 289 ASP   B OD2  1 
ATOM   4631 N  N    . GLU   B 1 290 ? 4.502   -8.511  -14.107 1   10.892 ? 290 GLU   B N    1 
ATOM   4632 C  CA   . GLU   B 1 290 ? 3.864   -7.562  -13.196 1   11.526 ? 290 GLU   B CA   1 
ATOM   4633 C  C    . GLU   B 1 290 ? 2.337   -7.627  -13.29  1   11.67  ? 290 GLU   B C    1 
ATOM   4634 O  O    . GLU   B 1 290 ? 1.671   -6.638  -13     1   13.394 ? 290 GLU   B O    1 
ATOM   4635 C  CB   . GLU   B 1 290 ? 4.449   -6.148  -13.328 1   12.528 ? 290 GLU   B CB   1 
ATOM   4636 C  CG   . GLU   B 1 290 ? 5.922   -6.09   -12.921 1   13.308 ? 290 GLU   B CG   1 
ATOM   4637 C  CD   . GLU   B 1 290 ? 6.537   -4.738  -12.616 1   13.679 ? 290 GLU   B CD   1 
ATOM   4638 O  OE1  . GLU   B 1 290 ? 5.841   -3.721  -12.768 1   14.155 ? 290 GLU   B OE1  1 
ATOM   4639 O  OE2  . GLU   B 1 290 ? 7.733   -4.695  -12.227 1   14.716 ? 290 GLU   B OE2  1 
ATOM   4640 N  N    . PHE   B 1 291 ? 1.799   -8.824  -13.531 1   11.266 ? 291 PHE   B N    1 
ATOM   4641 C  CA   . PHE   B 1 291 ? 0.406   -9.144  -13.229 1   11.89  ? 291 PHE   B CA   1 
ATOM   4642 C  C    . PHE   B 1 291 ? 0.349   -10.336 -12.284 1   11.881 ? 291 PHE   B C    1 
ATOM   4643 O  O    . PHE   B 1 291 ? 0.883   -11.396 -12.592 1   11.977 ? 291 PHE   B O    1 
ATOM   4644 C  CB   . PHE   B 1 291 ? -0.388  -9.568  -14.466 1   12.354 ? 291 PHE   B CB   1 
ATOM   4645 C  CG   . PHE   B 1 291 ? -0.517  -8.501  -15.533 1   12.979 ? 291 PHE   B CG   1 
ATOM   4646 C  CD1  . PHE   B 1 291 ? -1.523  -7.549  -15.473 1   13.538 ? 291 PHE   B CD1  1 
ATOM   4647 C  CD2  . PHE   B 1 291 ? 0.353   -8.483  -16.611 1   13.839 ? 291 PHE   B CD2  1 
ATOM   4648 C  CE1  . PHE   B 1 291 ? -1.664  -6.596  -16.469 1   13.935 ? 291 PHE   B CE1  1 
ATOM   4649 C  CE2  . PHE   B 1 291 ? 0.209   -7.532  -17.612 1   14.742 ? 291 PHE   B CE2  1 
ATOM   4650 C  CZ   . PHE   B 1 291 ? -0.8    -6.592  -17.538 1   14.517 ? 291 PHE   B CZ   1 
ATOM   4651 N  N    . THR   B 1 292 ? -0.338  -10.17  -11.15  1   12.429 ? 292 THR   B N    1 
ATOM   4652 C  CA   . THR   B 1 292 ? -0.582  -11.278 -10.239 1   12.992 ? 292 THR   B CA   1 
ATOM   4653 C  C    . THR   B 1 292 ? -1.744  -12.131 -10.746 1   12.714 ? 292 THR   B C    1 
ATOM   4654 O  O    . THR   B 1 292 ? -2.542  -11.723 -11.599 1   12.782 ? 292 THR   B O    1 
ATOM   4655 C  CB   . THR   B 1 292 ? -0.9    -10.788 -8.826  1   14.096 ? 292 THR   B CB   1 
ATOM   4656 O  OG1  . THR   B 1 292 ? -2.194  -10.184 -8.878  1   14.928 ? 292 THR   B OG1  1 
ATOM   4657 C  CG2  . THR   B 1 292 ? 0.181   -9.877  -8.269  1   14.419 ? 292 THR   B CG2  1 
ATOM   4658 N  N    . PRO   B 1 293 ? -1.884  -13.371 -10.234 1   13.051 ? 293 PRO   B N    1 
ATOM   4659 C  CA   . PRO   B 1 293 ? -3.083  -14.166 -10.504 1   13.696 ? 293 PRO   B CA   1 
ATOM   4660 C  C    . PRO   B 1 293 ? -4.377  -13.397 -10.233 1   14.763 ? 293 PRO   B C    1 
ATOM   4661 O  O    . PRO   B 1 293 ? -5.315  -13.472 -11.023 1   15.346 ? 293 PRO   B O    1 
ATOM   4662 C  CB   . PRO   B 1 293 ? -2.9    -15.382 -9.586  1   14.486 ? 293 PRO   B CB   1 
ATOM   4663 C  CG   . PRO   B 1 293 ? -1.397  -15.501 -9.472  1   14.25  ? 293 PRO   B CG   1 
ATOM   4664 C  CD   . PRO   B 1 293 ? -0.879  -14.088 -9.431  1   13.637 ? 293 PRO   B CD   1 
ATOM   4665 N  N    . PHE   B 1 294 ? -4.411  -12.629 -9.137  1   15.179 ? 294 PHE   B N    1 
ATOM   4666 C  CA   . PHE   B 1 294 ? -5.596  -11.87  -8.787  1   17.259 ? 294 PHE   B CA   1 
ATOM   4667 C  C    . PHE   B 1 294 ? -5.862  -10.793 -9.835  1   16.335 ? 294 PHE   B C    1 
ATOM   4668 O  O    . PHE   B 1 294 ? -7.014  -10.57  -10.203 1   17.725 ? 294 PHE   B O    1 
ATOM   4669 C  CB   . PHE   B 1 294 ? -5.489  -11.208 -7.408  1   19.225 ? 294 PHE   B CB   1 
ATOM   4670 C  CG   . PHE   B 1 294 ? -6.613  -10.212 -7.137  1   25.13  ? 294 PHE   B CG   1 
ATOM   4671 C  CD1  . PHE   B 1 294 ? -7.85   -10.64  -6.671  1   28.746 ? 294 PHE   B CD1  1 
ATOM   4672 C  CD2  . PHE   B 1 294 ? -6.444  -8.847  -7.385  1   28.706 ? 294 PHE   B CD2  1 
ATOM   4673 C  CE1  . PHE   B 1 294 ? -8.871  -9.73   -6.422  1   30.831 ? 294 PHE   B CE1  1 
ATOM   4674 C  CE2  . PHE   B 1 294 ? -7.469  -7.943  -7.137  1   29.614 ? 294 PHE   B CE2  1 
ATOM   4675 C  CZ   . PHE   B 1 294 ? -8.682  -8.387  -6.668  1   30.544 ? 294 PHE   B CZ   1 
ATOM   4676 N  N    . ASP   B 1 295 ? -4.793  -10.143 -10.329 1   15.608 ? 295 ASP   B N    1 
ATOM   4677 C  CA   . ASP   B 1 295 ? -4.912  -9.115  -11.353 1   15.979 ? 295 ASP   B CA   1 
ATOM   4678 C  C    . ASP   B 1 295 ? -5.559  -9.686  -12.613 1   15.905 ? 295 ASP   B C    1 
ATOM   4679 O  O    . ASP   B 1 295 ? -6.399  -9.033  -13.238 1   17.433 ? 295 ASP   B O    1 
ATOM   4680 C  CB   . ASP   B 1 295 ? -3.558  -8.513  -11.698 1   15.597 ? 295 ASP   B CB   1 
ATOM   4681 C  CG   . ASP   B 1 295 ? -2.901  -7.691  -10.6   1   16.03  ? 295 ASP   B CG   1 
ATOM   4682 O  OD1  . ASP   B 1 295 ? -3.638  -7.259  -9.668  1   17.826 ? 295 ASP   B OD1  1 
ATOM   4683 O  OD2  . ASP   B 1 295 ? -1.665  -7.495  -10.687 1   15.583 ? 295 ASP   B OD2  1 
ATOM   4684 N  N    . VAL   B 1 296 ? -5.163  -10.909 -12.976 1   14.585 ? 296 VAL   B N    1 
ATOM   4685 C  CA   . VAL   B 1 296 ? -5.674  -11.521 -14.19  1   15.593 ? 296 VAL   B CA   1 
ATOM   4686 C  C    . VAL   B 1 296 ? -7.166  -11.808 -14.027 1   17.085 ? 296 VAL   B C    1 
ATOM   4687 O  O    . VAL   B 1 296 ? -7.976  -11.457 -14.89  1   18.625 ? 296 VAL   B O    1 
ATOM   4688 C  CB   . VAL   B 1 296 ? -4.881  -12.785 -14.553 1   15.796 ? 296 VAL   B CB   1 
ATOM   4689 C  CG1  . VAL   B 1 296 ? -5.529  -13.551 -15.699 1   16.581 ? 296 VAL   B CG1  1 
ATOM   4690 C  CG2  . VAL   B 1 296 ? -3.435  -12.439 -14.876 1   15.406 ? 296 VAL   B CG2  1 
ATOM   4691 N  N    . VAL   B 1 297 ? -7.532  -12.421 -12.895 1   18.151 ? 297 VAL   B N    1 
ATOM   4692 C  CA   . VAL   B 1 297 ? -8.925  -12.772 -12.673 1   20.581 ? 297 VAL   B CA   1 
ATOM   4693 C  C    . VAL   B 1 297 ? -9.783  -11.502 -12.604 1   20.726 ? 297 VAL   B C    1 
ATOM   4694 O  O    . VAL   B 1 297 ? -10.9   -11.484 -13.15  1   21.379 ? 297 VAL   B O    1 
ATOM   4695 C  CB   . VAL   B 1 297 ? -9.056  -13.663 -11.423 1   21.419 ? 297 VAL   B CB   1 
ATOM   4696 C  CG1  . VAL   B 1 297 ? -10.515 -13.897 -11.048 1   22.384 ? 297 VAL   B CG1  1 
ATOM   4697 C  CG2  . VAL   B 1 297 ? -8.351  -15.001 -11.626 1   22.923 ? 297 VAL   B CG2  1 
ATOM   4698 N  N    . ARG   B 1 298 ? -9.255  -10.442 -11.972 1   21.996 ? 298 ARG   B N    1 
ATOM   4699 C  CA   . ARG   B 1 298 ? -9.975  -9.184  -11.786 1   24.211 ? 298 ARG   B CA   1 
ATOM   4700 C  C    . ARG   B 1 298 ? -10.311 -8.55   -13.133 1   22.793 ? 298 ARG   B C    1 
ATOM   4701 O  O    . ARG   B 1 298 ? -11.434 -8.082  -13.354 1   24.399 ? 298 ARG   B O    1 
ATOM   4702 C  CB   . ARG   B 1 298 ? -9.17   -8.184  -10.936 1   28.742 ? 298 ARG   B CB   1 
ATOM   4703 C  CG   . ARG   B 1 298 ? -9.535  -6.708  -11.08  1   34.538 ? 298 ARG   B CG   1 
ATOM   4704 C  CD   . ARG   B 1 298 ? -8.839  -5.688  -10.154 1   38.46  ? 298 ARG   B CD   1 
ATOM   4705 N  NE   . ARG   B 1 298 ? -7.502  -5.183  -10.518 1   41.264 ? 298 ARG   B NE   1 
ATOM   4706 C  CZ   . ARG   B 1 298 ? -7.168  -3.974  -11.014 1   40.64  ? 298 ARG   B CZ   1 
ATOM   4707 N  NH1  . ARG   B 1 298 ? -5.895  -3.665  -11.202 1   39.765 ? 298 ARG   B NH1  1 
ATOM   4708 N  NH2  . ARG   B 1 298 ? -8.091  -3.077  -11.336 1   40.103 ? 298 ARG   B NH2  1 
ATOM   4709 N  N    . GLN   B 1 299 ? -9.311  -8.491  -14.015 1   20.682 ? 299 GLN   B N    1 
ATOM   4710 C  CA   . GLN   B 1 299 ? -9.445  -7.766  -15.263 1   20.435 ? 299 GLN   B CA   1 
ATOM   4711 C  C    . GLN   B 1 299 ? -10.27  -8.585  -16.243 1   21.378 ? 299 GLN   B C    1 
ATOM   4712 O  O    . GLN   B 1 299 ? -11.049 -8.023  -17.01  1   25.292 ? 299 GLN   B O    1 
ATOM   4713 C  CB   . GLN   B 1 299 ? -8.083  -7.416  -15.85  1   18.139 ? 299 GLN   B CB   1 
ATOM   4714 C  CG   . GLN   B 1 299 ? -8.193  -6.719  -17.199 1   17.036 ? 299 GLN   B CG   1 
ATOM   4715 C  CD   . GLN   B 1 299 ? -6.897  -6.176  -17.773 1   16.027 ? 299 GLN   B CD   1 
ATOM   4716 O  OE1  . GLN   B 1 299 ? -6.846  -5.776  -18.945 1   15.011 ? 299 GLN   B OE1  1 
ATOM   4717 N  NE2  . GLN   B 1 299 ? -5.83   -6.141  -16.985 1   16.206 ? 299 GLN   B NE2  1 
ATOM   4718 N  N    . CYS   B 1 300 ? -10.112 -9.914  -16.202 1   22.82  ? 300 CYS   B N    1 
ATOM   4719 C  CA   . CYS   B 1 300 ? -10.858 -10.786 -17.093 1   24.602 ? 300 CYS   B CA   1 
ATOM   4720 C  C    . CYS   B 1 300 ? -12.325 -10.916 -16.658 1   24.457 ? 300 CYS   B C    1 
ATOM   4721 O  O    . CYS   B 1 300 ? -13.148 -11.364 -17.455 1   25.04  ? 300 CYS   B O    1 
ATOM   4722 C  CB   . CYS   B 1 300 ? -10.12  -12.11  -17.273 1   27.282 ? 300 CYS   B CB   1 
ATOM   4723 S  SG   . CYS   B 1 300 ? -8.514  -11.92  -18.1   1   30.163 ? 300 CYS   B SG   1 
ATOM   4724 N  N    . SER   B 1 301 ? -12.693 -10.439 -15.448 1   25.12  ? 301 SER   B N    1 
ATOM   4725 C  CA   . SER   B 1 301 ? -14.058 -10.593 -14.947 1   25.136 ? 301 SER   B CA   1 
ATOM   4726 C  C    . SER   B 1 301 ? -14.767 -9.266  -14.632 1   25.076 ? 301 SER   B C    1 
ATOM   4727 O  O    . SER   B 1 301 ? -15.909 -9.28   -14.174 1   25.457 ? 301 SER   B O    1 
ATOM   4728 C  CB   . SER   B 1 301 ? -14.085 -11.506 -13.741 1   27.157 ? 301 SER   B CB   1 
ATOM   4729 O  OG   . SER   B 1 301 ? -13.617 -10.844 -12.578 1   28.289 ? 301 SER   B OG   1 
ATOM   4730 N  N    . GLY   B 1 302 ? -14.121 -8.118  -14.883 1   24.151 ? 302 GLY   B N    1 
ATOM   4731 C  CA   . GLY   B 1 302 ? -14.785 -6.82   -14.83  1   24.244 ? 302 GLY   B CA   1 
ATOM   4732 C  C    . GLY   B 1 302 ? -15.186 -6.388  -13.415 1   24.573 ? 302 GLY   B C    1 
ATOM   4733 O  O    . GLY   B 1 302 ? -16.237 -5.774  -13.224 1   24.375 ? 302 GLY   B O    1 
ATOM   4734 N  N    . VAL   B 1 303 ? -14.329 -6.679  -12.431 1   24.299 ? 303 VAL   B N    1 
ATOM   4735 C  CA   . VAL   B 1 303 ? -14.582 -6.289  -11.046 1   24.664 ? 303 VAL   B CA   1 
ATOM   4736 C  C    . VAL   B 1 303 ? -14.559 -4.759  -10.924 1   24.07  ? 303 VAL   B C    1 
ATOM   4737 O  O    . VAL   B 1 303 ? -13.666 -4.133  -11.471 1   25.11  ? 303 VAL   B O    1 
ATOM   4738 C  CB   . VAL   B 1 303 ? -13.528 -6.945  -10.128 1   24.957 ? 303 VAL   B CB   1 
ATOM   4739 C  CG1  . VAL   B 1 303 ? -13.648 -6.478  -8.684  1   26.042 ? 303 VAL   B CG1  1 
ATOM   4740 C  CG2  . VAL   B 1 303 ? -13.586 -8.469  -10.186 1   25.387 ? 303 VAL   B CG2  1 
ATOM   4741 N  N    . THR   B 1 304 ? -15.498 -4.164  -10.16  1   22.901 ? 304 THR   B N    1 
ATOM   4742 C  CA   . THR   B 1 304 ? -15.568 -2.713  -9.98   1   23.195 ? 304 THR   B CA   1 
ATOM   4743 C  C    . THR   B 1 304 ? -15.385 -2.317  -8.515  1   24.54  ? 304 THR   B C    1 
ATOM   4744 O  O    . THR   B 1 304 ? -15.44  -3.164  -7.624  1   25.027 ? 304 THR   B O    1 
ATOM   4745 C  CB   . THR   B 1 304 ? -16.904 -2.162  -10.482 1   22.973 ? 304 THR   B CB   1 
ATOM   4746 O  OG1  . THR   B 1 304 ? -17.923 -2.792  -9.711  1   24.056 ? 304 THR   B OG1  1 
ATOM   4747 C  CG2  . THR   B 1 304 ? -17.13  -2.414  -11.958 1   22.192 ? 304 THR   B CG2  1 
ATOM   4748 N  N    . PHE   B 1 305 ? -15.209 -1.001  -8.296  1   25.236 ? 305 PHE   B N    1 
ATOM   4749 C  CA   . PHE   B 1 305 ? -14.911 -0.433  -6.986  1   27.187 ? 305 PHE   B CA   1 
ATOM   4750 C  C    . PHE   B 1 305 ? -15.831 0.757   -6.698  1   29.971 ? 305 PHE   B C    1 
ATOM   4751 O  O    . PHE   B 1 305 ? -16.628 1.139   -7.573  1   34.983 ? 305 PHE   B O    1 
ATOM   4752 C  CB   . PHE   B 1 305 ? -13.431 -0.031  -6.954  1   28.62  ? 305 PHE   B CB   1 
ATOM   4753 C  CG   . PHE   B 1 305 ? -12.561 -1.218  -7.327  1   28.581 ? 305 PHE   B CG   1 
ATOM   4754 C  CD1  . PHE   B 1 305 ? -12.272 -2.201  -6.387  1   29.59  ? 305 PHE   B CD1  1 
ATOM   4755 C  CD2  . PHE   B 1 305 ? -12.115 -1.393  -8.635  1   27.949 ? 305 PHE   B CD2  1 
ATOM   4756 C  CE1  . PHE   B 1 305 ? -11.522 -3.313  -6.737  1   29.781 ? 305 PHE   B CE1  1 
ATOM   4757 C  CE2  . PHE   B 1 305 ? -11.376 -2.514  -8.982  1   30.042 ? 305 PHE   B CE2  1 
ATOM   4758 C  CZ   . PHE   B 1 305 ? -11.083 -3.469  -8.033  1   30.432 ? 305 PHE   B CZ   1 
HETATM 4759 C  C4   . A1ITJ C 2 .   ? -22.767 -4.14   -31.085 1   17.474 ? 401 A1ITJ A C4   1 
HETATM 4760 C  C5   . A1ITJ C 2 .   ? -23.63  -3.889  -29.876 1   16.798 ? 401 A1ITJ A C5   1 
HETATM 4761 C  C7   . A1ITJ C 2 .   ? -21.868 -4.178  -28.138 1   15.017 ? 401 A1ITJ A C7   1 
HETATM 4762 C  C8   . A1ITJ C 2 .   ? -21.159 -5.179  -27.252 1   14.922 ? 401 A1ITJ A C8   1 
HETATM 4763 C  C10  . A1ITJ C 2 .   ? -22.909 -4.814  -25.449 1   15.037 ? 401 A1ITJ A C10  1 
HETATM 4764 C  C13  . A1ITJ C 2 .   ? -19.142 -5.069  -25.1   1   13.572 ? 401 A1ITJ A C13  1 
HETATM 4765 C  C17  . A1ITJ C 2 .   ? -17.263 -6.494  -25.412 1   14.313 ? 401 A1ITJ A C17  1 
HETATM 4766 C  C21  . A1ITJ C 2 .   ? -24.278 -4.679  -27.628 1   15.866 ? 401 A1ITJ A C21  1 
HETATM 4767 C  C22  . A1ITJ C 2 .   ? -25.556 -5.288  -28.187 1   17.669 ? 401 A1ITJ A C22  1 
HETATM 4768 C  C24  . A1ITJ C 2 .   ? -28.016 -5.136  -28.156 1   19.701 ? 401 A1ITJ A C24  1 
HETATM 4769 C  C28  . A1ITJ C 2 .   ? -21.219 -5.609  -32.237 1   20.071 ? 401 A1ITJ A C28  1 
HETATM 4770 C  C1   . A1ITJ C 2 .   ? -22.643 -0.799  -31.547 1   20.364 ? 401 A1ITJ A C1   1 
HETATM 4771 C  C2   . A1ITJ C 2 .   ? -23.453 -1.924  -32.117 1   20.413 ? 401 A1ITJ A C2   1 
HETATM 4772 C  C3   . A1ITJ C 2 .   ? -22.681 -3.221  -32.141 1   19.697 ? 401 A1ITJ A C3   1 
HETATM 4773 N  N6   . A1ITJ C 2 .   ? -23.208 -4.635  -28.635 1   15.869 ? 401 A1ITJ A N6   1 
HETATM 4774 N  N9   . A1ITJ C 2 .   ? -21.502 -4.958  -25.843 1   14.341 ? 401 A1ITJ A N9   1 
HETATM 4775 C  C11  . A1ITJ C 2 .   ? -23.876 -5.488  -26.406 1   15.858 ? 401 A1ITJ A C11  1 
HETATM 4776 C  C12  . A1ITJ C 2 .   ? -20.597 -4.822  -24.864 1   14.098 ? 401 A1ITJ A C12  1 
HETATM 4777 C  C14  . A1ITJ C 2 .   ? -18.251 -4.005  -25.177 1   13.494 ? 401 A1ITJ A C14  1 
HETATM 4778 N  N15  . A1ITJ C 2 .   ? -16.932 -4.148  -25.373 1   13.535 ? 401 A1ITJ A N15  1 
HETATM 4779 C  C16  . A1ITJ C 2 .   ? -16.465 -5.391  -25.484 1   13.54  ? 401 A1ITJ A C16  1 
HETATM 4780 CL CL18 . A1ITJ C 2 .   ? -16.589 -8.086  -25.567 1   19.951 ? 401 A1ITJ A CL18 1 
HETATM 4781 C  C19  . A1ITJ C 2 .   ? -18.623 -6.353  -25.217 1   14.647 ? 401 A1ITJ A C19  1 
HETATM 4782 O  O20  . A1ITJ C 2 .   ? -20.916 -4.538  -23.728 1   13.938 ? 401 A1ITJ A O20  1 
HETATM 4783 N  N23  . A1ITJ C 2 .   ? -26.675 -4.603  -27.93  1   19.026 ? 401 A1ITJ A N23  1 
HETATM 4784 C  C25  . A1ITJ C 2 .   ? -28.481 -5.901  -26.956 1   20.501 ? 401 A1ITJ A C25  1 
HETATM 4785 O  O26  . A1ITJ C 2 .   ? -25.517 -6.368  -28.774 1   19.01  ? 401 A1ITJ A O26  1 
HETATM 4786 C  C27  . A1ITJ C 2 .   ? -22.031 -5.325  -31.153 1   18.783 ? 401 A1ITJ A C27  1 
HETATM 4787 C  C29  . A1ITJ C 2 .   ? -21.144 -4.699  -33.268 1   20.031 ? 401 A1ITJ A C29  1 
HETATM 4788 BR BR30 . A1ITJ C 2 .   ? -20.024 -5.086  -34.761 0.7 22.715 ? 401 A1ITJ A BR30 1 
HETATM 4789 C  C31  . A1ITJ C 2 .   ? -21.86  -3.512  -33.236 1   18.947 ? 401 A1ITJ A C31  1 
HETATM 4790 C  C4   . A1ITJ D 2 .   ? 17.578  11.029  -0.808  1   17.75  ? 401 A1ITJ B C4   1 
HETATM 4791 C  C5   . A1ITJ D 2 .   ? 16.742  12.26   -0.585  1   16.263 ? 401 A1ITJ B C5   1 
HETATM 4792 C  C7   . A1ITJ D 2 .   ? 15.318  12.136  -2.641  1   14.356 ? 401 A1ITJ B C7   1 
HETATM 4793 C  C8   . A1ITJ D 2 .   ? 15.235  12.578  -4.092  1   13.869 ? 401 A1ITJ B C8   1 
HETATM 4794 C  C10  . A1ITJ D 2 .   ? 14.12   14.766  -3.449  1   14.007 ? 401 A1ITJ B C10  1 
HETATM 4795 C  C13  . A1ITJ D 2 .   ? 13.152  12.423  -6.248  1   13.005 ? 401 A1ITJ B C13  1 
HETATM 4796 C  C17  . A1ITJ D 2 .   ? 13.841  11.491  -8.33   1   13.675 ? 401 A1ITJ B C17  1 
HETATM 4797 C  C21  . A1ITJ D 2 .   ? 15.818  14.332  -1.534  1   15.015 ? 401 A1ITJ B C21  1 
HETATM 4798 C  C22  . A1ITJ D 2 .   ? 16.885  15.106  -0.77   1   16.372 ? 401 A1ITJ B C22  1 
HETATM 4799 C  C24  . A1ITJ D 2 .   ? 17.292  16.764  0.98    1   17.588 ? 401 A1ITJ B C24  1 
HETATM 4800 C  C28  . A1ITJ D 2 .   ? 19.143  9.928   -2.291  1   20.254 ? 401 A1ITJ B C28  1 
HETATM 4801 C  C1   . A1ITJ D 2 .   ? 15.647  9.015   1.246   1   18.483 ? 401 A1ITJ B C1   1 
HETATM 4802 C  C2   . A1ITJ D 2 .   ? 16.837  9.896   1.346   1   19.096 ? 401 A1ITJ B C2   1 
HETATM 4803 C  C3   . A1ITJ D 2 .   ? 17.636  9.933   0.065   1   18.626 ? 401 A1ITJ B C3   1 
HETATM 4804 N  N6   . A1ITJ D 2 .   ? 16.247  12.963  -1.831  1   15.135 ? 401 A1ITJ B N6   1 
HETATM 4805 N  N9   . A1ITJ D 2 .   ? 14.181  13.575  -4.306  1   13.721 ? 401 A1ITJ B N9   1 
HETATM 4806 C  C11  . A1ITJ D 2 .   ? 15.422  15.146  -2.756  1   14.404 ? 401 A1ITJ B C11  1 
HETATM 4807 C  C12  . A1ITJ D 2 .   ? 13.183  13.484  -5.205  1   13.126 ? 401 A1ITJ B C12  1 
HETATM 4808 C  C14  . A1ITJ D 2 .   ? 12.311  11.328  -6.12   1   12.838 ? 401 A1ITJ B C14  1 
HETATM 4809 N  N15  . A1ITJ D 2 .   ? 12.22   10.347  -7.028  1   12.968 ? 401 A1ITJ B N15  1 
HETATM 4810 C  C16  . A1ITJ D 2 .   ? 12.985  10.436  -8.124  1   13.199 ? 401 A1ITJ B C16  1 
HETATM 4811 CL CL18 . A1ITJ D 2 .   ? 14.811  11.563  -9.77   1   18.453 ? 401 A1ITJ B CL18 1 
HETATM 4812 C  C19  . A1ITJ D 2 .   ? 13.935  12.503  -7.394  1   13.665 ? 401 A1ITJ B C19  1 
HETATM 4813 O  O20  . A1ITJ D 2 .   ? 12.28   14.288  -5.253  1   13.36  ? 401 A1ITJ B O20  1 
HETATM 4814 N  N23  . A1ITJ D 2 .   ? 16.445  15.828  0.258   1   16.834 ? 401 A1ITJ B N23  1 
HETATM 4815 C  C25  . A1ITJ D 2 .   ? 17.066  18.16   0.486   1   17.75  ? 401 A1ITJ B C25  1 
HETATM 4816 O  O26  . A1ITJ D 2 .   ? 18.055  15.073  -1.142  1   18.335 ? 401 A1ITJ B O26  1 
HETATM 4817 C  C27  . A1ITJ D 2 .   ? 18.339  11.003  -1.976  1   18.421 ? 401 A1ITJ B C27  1 
HETATM 4818 C  C29  . A1ITJ D 2 .   ? 19.195  8.861   -1.431  1   20.051 ? 401 A1ITJ B C29  1 
HETATM 4819 BR BR30 . A1ITJ D 2 .   ? 20.305  7.376   -1.878  0.7 22.483 ? 401 A1ITJ B BR30 1 
HETATM 4820 C  C31  . A1ITJ D 2 .   ? 18.455  8.846   -0.261  1   18.941 ? 401 A1ITJ B C31  1 
HETATM 4821 S  S    . DMS   E 3 .   ? 19.352  8.783   12.928  1   18.197 ? 402 DMS   B S    1 
HETATM 4822 O  O    . DMS   E 3 .   ? 18.133  9.663   12.902  1   18.775 ? 402 DMS   B O    1 
HETATM 4823 C  C1   . DMS   E 3 .   ? 19.021  7.525   14.129  1   18.661 ? 402 DMS   B C1   1 
HETATM 4824 C  C2   . DMS   E 3 .   ? 19.277  7.753   11.485  1   18.284 ? 402 DMS   B C2   1 
HETATM 4825 CL CL   . CL    F 4 .   ? 5.305   -34.894 -20.455 1   12.079 ? 403 CL    B CL   1 
HETATM 4826 O  O    . HOH   G 5 .   ? -37.043 -2.672  -29.426 1   34.53  ? 501 HOH   A O    1 
HETATM 4827 O  O    . HOH   G 5 .   ? 21.078  -0.536  -44.439 1   22.466 ? 502 HOH   A O    1 
HETATM 4828 O  O    . HOH   G 5 .   ? -20.133 23.022  -15.554 1   41.356 ? 503 HOH   A O    1 
HETATM 4829 O  O    . HOH   G 5 .   ? -19.097 3.849   -42.947 1   46.045 ? 504 HOH   A O    1 
HETATM 4830 O  O    . HOH   G 5 .   ? -34.045 7.143   -13.316 1   27.78  ? 505 HOH   A O    1 
HETATM 4831 O  O    . HOH   G 5 .   ? 26.23   14.739  -24.234 1   27.763 ? 506 HOH   A O    1 
HETATM 4832 O  O    . HOH   G 5 .   ? -8.885  16.434  -34.216 1   23.546 ? 507 HOH   A O    1 
HETATM 4833 O  O    . HOH   G 5 .   ? -1.449  19.059  -17.314 1   41.768 ? 508 HOH   A O    1 
HETATM 4834 O  O    . HOH   G 5 .   ? 13.627  9.703   -51.873 1   26.462 ? 509 HOH   A O    1 
HETATM 4835 O  O    . HOH   G 5 .   ? -36.321 -0.327  -28.355 1   25.081 ? 510 HOH   A O    1 
HETATM 4836 O  O    . HOH   G 5 .   ? -0.285  8.568   -39.805 1   39.316 ? 511 HOH   A O    1 
HETATM 4837 O  O    . HOH   G 5 .   ? -16.539 16.54   -32.442 1   29.489 ? 512 HOH   A O    1 
HETATM 4838 O  O    . HOH   G 5 .   ? -35.891 -3.263  -34.694 1   33.325 ? 513 HOH   A O    1 
HETATM 4839 O  O    . HOH   G 5 .   ? 5.187   21.198  -41.255 1   29.522 ? 514 HOH   A O    1 
HETATM 4840 O  O    . HOH   G 5 .   ? -20.903 -4.704  -12.375 1   30.753 ? 515 HOH   A O    1 
HETATM 4841 O  O    . HOH   G 5 .   ? -22.324 -0.514  -10.047 1   32.342 ? 516 HOH   A O    1 
HETATM 4842 O  O    . HOH   G 5 .   ? 20.998  -10.396 -34.676 1   30.693 ? 517 HOH   A O    1 
HETATM 4843 O  O    . HOH   G 5 .   ? -0.022  21.41   -40.356 1   24.476 ? 518 HOH   A O    1 
HETATM 4844 O  O    . HOH   G 5 .   ? -38.475 0.051   -35.095 1   26.804 ? 519 HOH   A O    1 
HETATM 4845 O  O    . HOH   G 5 .   ? 13.646  -7.851  -29.261 1   36.034 ? 520 HOH   A O    1 
HETATM 4846 O  O    . HOH   G 5 .   ? 22.263  14.652  -34.521 1   18.82  ? 521 HOH   A O    1 
HETATM 4847 O  O    . HOH   G 5 .   ? -12.404 -3.697  -18.442 1   15.662 ? 522 HOH   A O    1 
HETATM 4848 O  O    . HOH   G 5 .   ? -1.066  2.554   -24.553 1   21.185 ? 523 HOH   A O    1 
HETATM 4849 O  O    . HOH   G 5 .   ? -18.058 6.219   -39.388 1   29.135 ? 524 HOH   A O    1 
HETATM 4850 O  O    . HOH   G 5 .   ? -29.649 8.606   -37.229 1   29.654 ? 525 HOH   A O    1 
HETATM 4851 O  O    . HOH   G 5 .   ? -15.131 5.715   -8.207  1   33.859 ? 526 HOH   A O    1 
HETATM 4852 O  O    . HOH   G 5 .   ? -30.819 -8.248  -34.525 1   30.675 ? 527 HOH   A O    1 
HETATM 4853 O  O    . HOH   G 5 .   ? 11.157  17.402  -22.545 1   31.761 ? 528 HOH   A O    1 
HETATM 4854 O  O    . HOH   G 5 .   ? 15.874  -8.121  -27.185 1   32.665 ? 529 HOH   A O    1 
HETATM 4855 O  O    . HOH   G 5 .   ? 9.953   17.017  -19.991 1   20.454 ? 530 HOH   A O    1 
HETATM 4856 O  O    . HOH   G 5 .   ? 21.498  0.607   -33.94  1   17.002 ? 531 HOH   A O    1 
HETATM 4857 O  O    . HOH   G 5 .   ? 4.833   -2.422  -38.116 1   25.493 ? 532 HOH   A O    1 
HETATM 4858 O  O    . HOH   G 5 .   ? -43.585 5.149   -21.787 1   23.326 ? 533 HOH   A O    1 
HETATM 4859 O  O    . HOH   G 5 .   ? 15.639  -1.435  -20.896 1   32.156 ? 534 HOH   A O    1 
HETATM 4860 O  O    . HOH   G 5 .   ? 18.486  0.316   -23.126 1   34.509 ? 535 HOH   A O    1 
HETATM 4861 O  O    . HOH   G 5 .   ? -17.416 22.681  -21.525 1   35.09  ? 536 HOH   A O    1 
HETATM 4862 O  O    . HOH   G 5 .   ? 19.74   4.597   -18.582 1   43.399 ? 537 HOH   A O    1 
HETATM 4863 O  O    . HOH   G 5 .   ? 7.337   5.956   -42.64  1   32.172 ? 538 HOH   A O    1 
HETATM 4864 O  O    . HOH   G 5 .   ? 21.884  17.312  -19.228 1   30.238 ? 539 HOH   A O    1 
HETATM 4865 O  O    . HOH   G 5 .   ? -22.132 -2.505  -22.49  1   14.219 ? 540 HOH   A O    1 
HETATM 4866 O  O    . HOH   G 5 .   ? -15.526 5.842   -18.186 1   12.852 ? 541 HOH   A O    1 
HETATM 4867 O  O    . HOH   G 5 .   ? 13.157  11.104  -17.101 1   14.224 ? 542 HOH   A O    1 
HETATM 4868 O  O    . HOH   G 5 .   ? 20.477  20.823  -28.81  1   34.255 ? 543 HOH   A O    1 
HETATM 4869 O  O    . HOH   G 5 .   ? -24.679 -3.322  -21.956 1   21.14  ? 544 HOH   A O    1 
HETATM 4870 O  O    . HOH   G 5 .   ? 18.201  10.29   -51.461 1   15.612 ? 545 HOH   A O    1 
HETATM 4871 O  O    . HOH   G 5 .   ? 7.953   23.466  -41.247 1   22.864 ? 546 HOH   A O    1 
HETATM 4872 O  O    . HOH   G 5 .   ? -6.217  -5.016  -26.425 1   26.763 ? 547 HOH   A O    1 
HETATM 4873 O  O    . HOH   G 5 .   ? 2.539   2.705   -44.316 1   33.942 ? 548 HOH   A O    1 
HETATM 4874 O  O    . HOH   G 5 .   ? -0.473  11.594  -21.521 1   15.972 ? 549 HOH   A O    1 
HETATM 4875 O  O    . HOH   G 5 .   ? -12.025 -6.168  -37.117 1   27.022 ? 550 HOH   A O    1 
HETATM 4876 O  O    . HOH   G 5 .   ? 25.207  -0.77   -29.728 1   33.769 ? 551 HOH   A O    1 
HETATM 4877 O  O    . HOH   G 5 .   ? 13.704  21.251  -25.773 1   25.462 ? 552 HOH   A O    1 
HETATM 4878 O  O    . HOH   G 5 .   ? -2.596  10.478  -22.918 1   13.175 ? 553 HOH   A O    1 
HETATM 4879 O  O    . HOH   G 5 .   ? -31.115 -6.093  -23.703 1   30.529 ? 554 HOH   A O    1 
HETATM 4880 O  O    . HOH   G 5 .   ? -22.551 16.079  -27.484 1   20.912 ? 555 HOH   A O    1 
HETATM 4881 O  O    . HOH   G 5 .   ? 3.288   0.271   -45.694 1   37.841 ? 556 HOH   A O    1 
HETATM 4882 O  O    . HOH   G 5 .   ? 16.462  7.335   -53.022 1   22.971 ? 557 HOH   A O    1 
HETATM 4883 O  O    . HOH   G 5 .   ? -15.93  14.314  -10.68  1   18.141 ? 558 HOH   A O    1 
HETATM 4884 O  O    . HOH   G 5 .   ? 25.809  12.426  -16.936 1   23.047 ? 559 HOH   A O    1 
HETATM 4885 O  O    . HOH   G 5 .   ? -37.513 1.119   -20.73  1   28.693 ? 560 HOH   A O    1 
HETATM 4886 O  O    . HOH   G 5 .   ? -26.841 19.747  -8.178  1   21.787 ? 561 HOH   A O    1 
HETATM 4887 O  O    . HOH   G 5 .   ? -2.04   12.706  -34.736 1   22.863 ? 562 HOH   A O    1 
HETATM 4888 O  O    . HOH   G 5 .   ? -17.81  -8.058  -32.889 1   30.889 ? 563 HOH   A O    1 
HETATM 4889 O  O    . HOH   G 5 .   ? 25.584  12.113  -23.951 1   17.562 ? 564 HOH   A O    1 
HETATM 4890 O  O    . HOH   G 5 .   ? -11.25  -6.52   -19.476 1   21.916 ? 565 HOH   A O    1 
HETATM 4891 O  O    . HOH   G 5 .   ? -3.486  1.524   -40.639 1   30.104 ? 566 HOH   A O    1 
HETATM 4892 O  O    . HOH   G 5 .   ? -22.829 -1.745  -17.521 1   16.234 ? 567 HOH   A O    1 
HETATM 4893 O  O    . HOH   G 5 .   ? -39.005 10.068  -28.211 1   19.377 ? 568 HOH   A O    1 
HETATM 4894 O  O    . HOH   G 5 .   ? -17.595 9.712   -38.188 1   32.962 ? 569 HOH   A O    1 
HETATM 4895 O  O    . HOH   G 5 .   ? 20.041  -8.866  -36.839 1   18.502 ? 570 HOH   A O    1 
HETATM 4896 O  O    . HOH   G 5 .   ? 1.349   9.955   -41.608 1   27.046 ? 571 HOH   A O    1 
HETATM 4897 O  O    . HOH   G 5 .   ? -27.105 -2.204  -26.353 1   21.24  ? 572 HOH   A O    1 
HETATM 4898 O  O    . HOH   G 5 .   ? -0.067  13.966  -27.61  1   16.337 ? 573 HOH   A O    1 
HETATM 4899 O  O    . HOH   G 5 .   ? -4.041  16.405  -14.48  1   38.377 ? 574 HOH   A O    1 
HETATM 4900 O  O    . HOH   G 5 .   ? -10.228 0.967   -40.255 1   22.558 ? 575 HOH   A O    1 
HETATM 4901 O  O    . HOH   G 5 .   ? 11.779  21.288  -38.323 1   25.042 ? 576 HOH   A O    1 
HETATM 4902 O  O    . HOH   G 5 .   ? 20.708  -4.113  -32.581 1   18.292 ? 577 HOH   A O    1 
HETATM 4903 O  O    . HOH   G 5 .   ? 15.695  -0.894  -42.417 1   15.436 ? 578 HOH   A O    1 
HETATM 4904 O  O    . HOH   G 5 .   ? 1.22    11.187  -32.238 1   17.79  ? 579 HOH   A O    1 
HETATM 4905 O  O    . HOH   G 5 .   ? -4.611  1.405   -28.72  1   13.054 ? 580 HOH   A O    1 
HETATM 4906 O  O    . HOH   G 5 .   ? 17.948  20.43   -20.583 1   32.628 ? 581 HOH   A O    1 
HETATM 4907 O  O    . HOH   G 5 .   ? 9.458   8.791   -53.439 1   24.539 ? 582 HOH   A O    1 
HETATM 4908 O  O    . HOH   G 5 .   ? 19.188  14.361  -44.4   1   23.983 ? 583 HOH   A O    1 
HETATM 4909 O  O    . HOH   G 5 .   ? -12.833 8.628   -38.927 1   27.113 ? 584 HOH   A O    1 
HETATM 4910 O  O    . HOH   G 5 .   ? 10.603  1.586   -18.554 1   20.341 ? 585 HOH   A O    1 
HETATM 4911 O  O    . HOH   G 5 .   ? -27.304 -8.394  -29.218 1   41.955 ? 586 HOH   A O    1 
HETATM 4912 O  O    . HOH   G 5 .   ? -28.844 1.426   -38.474 1   30.682 ? 587 HOH   A O    1 
HETATM 4913 O  O    . HOH   G 5 .   ? 25.494  11.466  -40.442 1   31.665 ? 588 HOH   A O    1 
HETATM 4914 O  O    . HOH   G 5 .   ? -3.499  19.586  -24.059 1   18.25  ? 589 HOH   A O    1 
HETATM 4915 O  O    . HOH   G 5 .   ? 20.448  4.054   -40.78  1   18.857 ? 590 HOH   A O    1 
HETATM 4916 O  O    . HOH   G 5 .   ? -6.258  17.475  -21.954 1   23.128 ? 591 HOH   A O    1 
HETATM 4917 O  O    . HOH   G 5 .   ? 1.077   15.033  -40.276 1   22.076 ? 592 HOH   A O    1 
HETATM 4918 O  O    . HOH   G 5 .   ? 23.912  10.254  -36.9   1   17.932 ? 593 HOH   A O    1 
HETATM 4919 O  O    . HOH   G 5 .   ? 8.264   2.016   -49.765 1   25.86  ? 594 HOH   A O    1 
HETATM 4920 O  O    . HOH   G 5 .   ? 8.468   -2.366  -35.175 1   20.809 ? 595 HOH   A O    1 
HETATM 4921 O  O    . HOH   G 5 .   ? -45.754 4.554   -18.373 1   33.658 ? 596 HOH   A O    1 
HETATM 4922 O  O    . HOH   G 5 .   ? 11.94   -5.319  -38.125 1   20.72  ? 597 HOH   A O    1 
HETATM 4923 O  O    . HOH   G 5 .   ? 21.512  7.878   -35.591 1   17.62  ? 598 HOH   A O    1 
HETATM 4924 O  O    . HOH   G 5 .   ? 17.386  8.657   -16.039 1   35.231 ? 599 HOH   A O    1 
HETATM 4925 O  O    . HOH   G 5 .   ? -10.147 25.9    -23.884 1   38.714 ? 600 HOH   A O    1 
HETATM 4926 O  O    . HOH   G 5 .   ? 18.006  -1.667  -44.572 1   34.38  ? 601 HOH   A O    1 
HETATM 4927 O  O    . HOH   G 5 .   ? -22.16  13.232  -8.23   1   24.205 ? 602 HOH   A O    1 
HETATM 4928 O  O    . HOH   G 5 .   ? 28.811  9.623   -40.68  1   34.792 ? 603 HOH   A O    1 
HETATM 4929 O  O    . HOH   G 5 .   ? 11.405  9.562   -15.703 1   18.526 ? 604 HOH   A O    1 
HETATM 4930 O  O    . HOH   G 5 .   ? 17.108  12.371  -17.507 1   19.149 ? 605 HOH   A O    1 
HETATM 4931 O  O    . HOH   G 5 .   ? -4.787  7.02    -40.284 1   22.702 ? 606 HOH   A O    1 
HETATM 4932 O  O    . HOH   G 5 .   ? 22.123  14.261  -25.021 1   20.129 ? 607 HOH   A O    1 
HETATM 4933 O  O    . HOH   G 5 .   ? -6.554  -2.562  -34.861 1   35.573 ? 608 HOH   A O    1 
HETATM 4934 O  O    . HOH   G 5 .   ? -10.084 11.566  -36.247 1   27.419 ? 609 HOH   A O    1 
HETATM 4935 O  O    . HOH   G 5 .   ? 18.928  9.272   -47.355 1   14.738 ? 610 HOH   A O    1 
HETATM 4936 O  O    . HOH   G 5 .   ? 13.093  20.281  -23.27  1   36.589 ? 611 HOH   A O    1 
HETATM 4937 O  O    . HOH   G 5 .   ? 3.034   20.826  -43.222 1   35.349 ? 612 HOH   A O    1 
HETATM 4938 O  O    . HOH   G 5 .   ? 25.925  1.467   -37.951 1   23.367 ? 613 HOH   A O    1 
HETATM 4939 O  O    . HOH   G 5 .   ? 9.329   17.228  -29.195 1   17.836 ? 614 HOH   A O    1 
HETATM 4940 O  O    . HOH   G 5 .   ? -38.447 1.311   -29.133 1   22.64  ? 615 HOH   A O    1 
HETATM 4941 O  O    . HOH   G 5 .   ? 11.727  1.094   -52.836 1   26.77  ? 616 HOH   A O    1 
HETATM 4942 O  O    . HOH   G 5 .   ? -25.328 18.681  -24.343 1   36.551 ? 617 HOH   A O    1 
HETATM 4943 O  O    . HOH   G 5 .   ? -21.651 14.725  -37.867 1   48.697 ? 618 HOH   A O    1 
HETATM 4944 O  O    . HOH   G 5 .   ? 12.551  16.994  -42.69  1   22.752 ? 619 HOH   A O    1 
HETATM 4945 O  O    . HOH   G 5 .   ? 15.998  -5.423  -43.054 1   15.098 ? 620 HOH   A O    1 
HETATM 4946 O  O    . HOH   G 5 .   ? 15.785  11.426  -50.914 1   16.289 ? 621 HOH   A O    1 
HETATM 4947 O  O    . HOH   G 5 .   ? 23.601  14.052  -28.404 1   16.345 ? 622 HOH   A O    1 
HETATM 4948 O  O    . HOH   G 5 .   ? -28.641 10.498  -35.017 1   21.187 ? 623 HOH   A O    1 
HETATM 4949 O  O    . HOH   G 5 .   ? 6.548   18.339  -18.458 1   37.925 ? 624 HOH   A O    1 
HETATM 4950 O  O    . HOH   G 5 .   ? 21.778  10.06   -22.922 1   14.787 ? 625 HOH   A O    1 
HETATM 4951 O  O    . HOH   G 5 .   ? -32.955 14.197  -10.977 1   23.09  ? 626 HOH   A O    1 
HETATM 4952 O  O    . HOH   G 5 .   ? -13.627 3.586   -33.529 1   16.038 ? 627 HOH   A O    1 
HETATM 4953 O  O    . HOH   G 5 .   ? -38.647 10.304  -16.249 1   21.103 ? 628 HOH   A O    1 
HETATM 4954 O  O    . HOH   G 5 .   ? 3.292   -0.134  -28.922 1   29.668 ? 629 HOH   A O    1 
HETATM 4955 O  O    . HOH   G 5 .   ? 5.79    5.512   -28.429 1   10.093 ? 630 HOH   A O    1 
HETATM 4956 O  O    . HOH   G 5 .   ? -23.299 18.579  -20.289 1   17.976 ? 631 HOH   A O    1 
HETATM 4957 O  O    . HOH   G 5 .   ? 12.145  19.865  -35.876 1   24.06  ? 632 HOH   A O    1 
HETATM 4958 O  O    . HOH   G 5 .   ? 18.023  4.7     -47.183 1   23.786 ? 633 HOH   A O    1 
HETATM 4959 O  O    . HOH   G 5 .   ? -24.481 -5.949  -21.727 1   25.338 ? 634 HOH   A O    1 
HETATM 4960 O  O    . HOH   G 5 .   ? 0.763   7.455   -23.304 1   14.662 ? 635 HOH   A O    1 
HETATM 4961 O  O    . HOH   G 5 .   ? 20.377  15.115  -42.03  1   30.134 ? 636 HOH   A O    1 
HETATM 4962 O  O    . HOH   G 5 .   ? -18.348 6.087   -10.464 1   47.475 ? 637 HOH   A O    1 
HETATM 4963 O  O    . HOH   G 5 .   ? -20.731 21.453  -6.72   1   30.224 ? 638 HOH   A O    1 
HETATM 4964 O  O    . HOH   G 5 .   ? -36.296 8.798   -15.514 1   20.104 ? 639 HOH   A O    1 
HETATM 4965 O  O    . HOH   G 5 .   ? -22.949 2.622   -10.234 1   34.656 ? 640 HOH   A O    1 
HETATM 4966 O  O    . HOH   G 5 .   ? 22.945  2.594   -23.921 1   27.119 ? 641 HOH   A O    1 
HETATM 4967 O  O    . HOH   G 5 .   ? -21.67  10.653  -37.451 1   36.527 ? 642 HOH   A O    1 
HETATM 4968 O  O    . HOH   G 5 .   ? -30.13  23.64   -16.179 1   35.74  ? 643 HOH   A O    1 
HETATM 4969 O  O    . HOH   G 5 .   ? 19.056  6.073   -49.028 1   19.033 ? 644 HOH   A O    1 
HETATM 4970 O  O    . HOH   G 5 .   ? 16.925  4.812   -21.242 1   14.712 ? 645 HOH   A O    1 
HETATM 4971 O  O    . HOH   G 5 .   ? -29.961 2.39    -14.453 1   19.394 ? 646 HOH   A O    1 
HETATM 4972 O  O    . HOH   G 5 .   ? -15.295 14.317  -28.041 1   16.834 ? 647 HOH   A O    1 
HETATM 4973 O  O    . HOH   G 5 .   ? -26.358 2.31    -37.428 1   23.045 ? 648 HOH   A O    1 
HETATM 4974 O  O    . HOH   G 5 .   ? 17.083  14.785  -14.44  1   28.805 ? 649 HOH   A O    1 
HETATM 4975 O  O    . HOH   G 5 .   ? 14.237  21.136  -21.173 1   37.099 ? 650 HOH   A O    1 
HETATM 4976 O  O    . HOH   G 5 .   ? -31.716 2.577   -12.352 1   31.475 ? 651 HOH   A O    1 
HETATM 4977 O  O    . HOH   G 5 .   ? -6.999  4.203   -41.738 1   31.109 ? 652 HOH   A O    1 
HETATM 4978 O  O    . HOH   G 5 .   ? -24.634 3.379   -30.352 1   12.544 ? 653 HOH   A O    1 
HETATM 4979 O  O    . HOH   G 5 .   ? 9.525   18.4    -45.753 1   29.293 ? 654 HOH   A O    1 
HETATM 4980 O  O    . HOH   G 5 .   ? 18.207  -8.724  -33.171 1   22.421 ? 655 HOH   A O    1 
HETATM 4981 O  O    . HOH   G 5 .   ? 8.168   16.148  -16.813 1   31.689 ? 656 HOH   A O    1 
HETATM 4982 O  O    . HOH   G 5 .   ? 5.428   18.026  -29.722 1   28.796 ? 657 HOH   A O    1 
HETATM 4983 O  O    . HOH   G 5 .   ? -37.128 9.842   -32.966 1   18.792 ? 658 HOH   A O    1 
HETATM 4984 O  O    . HOH   G 5 .   ? -34.471 -9.097  -28.773 1   38.673 ? 659 HOH   A O    1 
HETATM 4985 O  O    . HOH   G 5 .   ? 16.518  2.278   -22.265 1   21.622 ? 660 HOH   A O    1 
HETATM 4986 O  O    . HOH   G 5 .   ? -18.98  -5.953  -29.37  1   15.6   ? 661 HOH   A O    1 
HETATM 4987 O  O    . HOH   G 5 .   ? 7.152   -4.421  -38.915 1   36.772 ? 662 HOH   A O    1 
HETATM 4988 O  O    . HOH   G 5 .   ? -7.053  15.413  -12.041 1   24.811 ? 663 HOH   A O    1 
HETATM 4989 O  O    . HOH   G 5 .   ? 7.038   2.123   -20.629 1   28.457 ? 664 HOH   A O    1 
HETATM 4990 O  O    . HOH   G 5 .   ? 3.866   17.672  -22.518 1   21.118 ? 665 HOH   A O    1 
HETATM 4991 O  O    . HOH   G 5 .   ? -8.499  14.234  -24.933 1   17.218 ? 666 HOH   A O    1 
HETATM 4992 O  O    . HOH   G 5 .   ? -35.862 -1.232  -25.553 1   31.706 ? 667 HOH   A O    1 
HETATM 4993 O  O    . HOH   G 5 .   ? -4.61   13.373  -38.655 1   31.184 ? 668 HOH   A O    1 
HETATM 4994 O  O    . HOH   G 5 .   ? -23.599 4.514   -37.302 1   18.876 ? 669 HOH   A O    1 
HETATM 4995 O  O    . HOH   G 5 .   ? -33.333 -1.307  -24.927 1   23.977 ? 670 HOH   A O    1 
HETATM 4996 O  O    . HOH   G 5 .   ? 0.647   14.899  -15.853 1   28.864 ? 671 HOH   A O    1 
HETATM 4997 O  O    . HOH   G 5 .   ? -20.713 8.208   -36.778 1   20.429 ? 672 HOH   A O    1 
HETATM 4998 O  O    . HOH   G 5 .   ? 14.064  4.901   -17.436 1   20.216 ? 673 HOH   A O    1 
HETATM 4999 O  O    . HOH   G 5 .   ? -8.055  -5.346  -36.247 1   45.89  ? 674 HOH   A O    1 
HETATM 5000 O  O    . HOH   G 5 .   ? 8.909   1.35    -22.878 1   21.472 ? 675 HOH   A O    1 
HETATM 5001 O  O    . HOH   G 5 .   ? -7.526  -5.081  -28.478 1   33.125 ? 676 HOH   A O    1 
HETATM 5002 O  O    . HOH   G 5 .   ? 2.917   22.923  -40.218 1   23.523 ? 677 HOH   A O    1 
HETATM 5003 O  O    . HOH   G 5 .   ? -23.317 -8.202  -28.945 1   28.031 ? 678 HOH   A O    1 
HETATM 5004 O  O    . HOH   G 5 .   ? -1.136  5.15    -24.786 1   27.318 ? 679 HOH   A O    1 
HETATM 5005 O  O    . HOH   G 5 .   ? 8.502   11.633  -47.702 1   28.413 ? 680 HOH   A O    1 
HETATM 5006 O  O    . HOH   G 5 .   ? 7.058   -0.272  -23.887 1   29.976 ? 681 HOH   A O    1 
HETATM 5007 O  O    . HOH   G 5 .   ? -34.165 -3.596  -23.887 1   54.195 ? 682 HOH   A O    1 
HETATM 5008 O  O    . HOH   G 5 .   ? -18.813 -6.777  -37.38  1   41.075 ? 683 HOH   A O    1 
HETATM 5009 O  O    . HOH   G 5 .   ? -24.588 -3.987  -17.983 1   27.153 ? 684 HOH   A O    1 
HETATM 5010 O  O    . HOH   G 5 .   ? -21.31  5.839   -38.069 1   18.573 ? 685 HOH   A O    1 
HETATM 5011 O  O    . HOH   G 5 .   ? 1.331   1.31    -15.974 1   27.772 ? 686 HOH   A O    1 
HETATM 5012 O  O    . HOH   G 5 .   ? -11.048 5.576   -6.552  1   21.817 ? 687 HOH   A O    1 
HETATM 5013 O  O    . HOH   G 5 .   ? 1.732   7.88    -20.666 1   15.4   ? 688 HOH   A O    1 
HETATM 5014 O  O    . HOH   G 5 .   ? -1.853  1.799   -19.037 1   33.143 ? 689 HOH   A O    1 
HETATM 5015 O  O    . HOH   G 5 .   ? -0.478  12.287  -38.018 1   32.498 ? 690 HOH   A O    1 
HETATM 5016 O  O    . HOH   G 5 .   ? -27.86  13.894  -35.15  1   33.62  ? 691 HOH   A O    1 
HETATM 5017 O  O    . HOH   G 5 .   ? 5.402   12.128  -45.574 1   40.563 ? 692 HOH   A O    1 
HETATM 5018 O  O    . HOH   G 5 .   ? 14.92   15.319  -46.217 1   18.401 ? 693 HOH   A O    1 
HETATM 5019 O  O    . HOH   G 5 .   ? -21.824 21.328  -10.908 1   40.449 ? 694 HOH   A O    1 
HETATM 5020 O  O    . HOH   G 5 .   ? -43.514 4.261   -24.3   1   23.129 ? 695 HOH   A O    1 
HETATM 5021 O  O    . HOH   G 5 .   ? -32.283 -6.15   -36.552 1   29.963 ? 696 HOH   A O    1 
HETATM 5022 O  O    . HOH   G 5 .   ? 12.359  18.36   -15.385 1   32.322 ? 697 HOH   A O    1 
HETATM 5023 O  O    . HOH   G 5 .   ? 9.152   -3.743  -32.873 1   20.17  ? 698 HOH   A O    1 
HETATM 5024 O  O    . HOH   G 5 .   ? -22.964 5.357   -10.634 1   27.967 ? 699 HOH   A O    1 
HETATM 5025 O  O    . HOH   G 5 .   ? -33.337 7.658   -5.573  1   39.216 ? 700 HOH   A O    1 
HETATM 5026 O  O    . HOH   G 5 .   ? 23.05   -6.938  -35.894 1   20.255 ? 701 HOH   A O    1 
HETATM 5027 O  O    . HOH   G 5 .   ? 15.069  -7.973  -31.493 1   23.426 ? 702 HOH   A O    1 
HETATM 5028 O  O    . HOH   G 5 .   ? 5.425   16.244  -45.201 1   28.716 ? 703 HOH   A O    1 
HETATM 5029 O  O    . HOH   G 5 .   ? -16.023 21.381  -25.814 1   20.672 ? 704 HOH   A O    1 
HETATM 5030 O  O    . HOH   G 5 .   ? -37.313 15.159  -25.032 1   22.364 ? 705 HOH   A O    1 
HETATM 5031 O  O    . HOH   G 5 .   ? 3.478   10.071  -20.278 1   19.239 ? 706 HOH   A O    1 
HETATM 5032 O  O    . HOH   G 5 .   ? -16.228 19.523  -29.522 1   32.108 ? 707 HOH   A O    1 
HETATM 5033 O  O    . HOH   G 5 .   ? 16.343  18.057  -36.393 1   21.04  ? 708 HOH   A O    1 
HETATM 5034 O  O    . HOH   G 5 .   ? -12.109 20.569  -12.599 1   23.39  ? 709 HOH   A O    1 
HETATM 5035 O  O    . HOH   G 5 .   ? 24.602  12.867  -30.774 1   18.087 ? 710 HOH   A O    1 
HETATM 5036 O  O    . HOH   G 5 .   ? -17.611 22.622  -15.565 1   24.881 ? 711 HOH   A O    1 
HETATM 5037 O  O    . HOH   G 5 .   ? -25.038 2.431   -42.265 1   37.078 ? 712 HOH   A O    1 
HETATM 5038 O  O    . HOH   G 5 .   ? -31.325 16.082  -24.647 1   34.863 ? 713 HOH   A O    1 
HETATM 5039 O  O    . HOH   G 5 .   ? -22.222 9.36    -10.227 1   52.293 ? 714 HOH   A O    1 
HETATM 5040 O  O    . HOH   G 5 .   ? 3.97    8.948   -37.876 1   15.438 ? 715 HOH   A O    1 
HETATM 5041 O  O    . HOH   G 5 .   ? 20.049  7.3     -45.673 1   21.223 ? 716 HOH   A O    1 
HETATM 5042 O  O    . HOH   G 5 .   ? 22.917  11.762  -24.614 1   14.119 ? 717 HOH   A O    1 
HETATM 5043 O  O    . HOH   G 5 .   ? -40.761 11.196  -25.903 1   19.755 ? 718 HOH   A O    1 
HETATM 5044 O  O    . HOH   G 5 .   ? -17.132 -10.036 -22.404 1   19.716 ? 719 HOH   A O    1 
HETATM 5045 O  O    . HOH   G 5 .   ? -20.768 16.762  -34.918 1   42.188 ? 720 HOH   A O    1 
HETATM 5046 O  O    . HOH   G 5 .   ? 13.347  14.137  -48.413 1   16.503 ? 721 HOH   A O    1 
HETATM 5047 O  O    . HOH   G 5 .   ? -35.804 -0.628  -35.876 1   19.74  ? 722 HOH   A O    1 
HETATM 5048 O  O    . HOH   G 5 .   ? 24.186  13.326  -39.552 1   39.93  ? 723 HOH   A O    1 
HETATM 5049 O  O    . HOH   G 5 .   ? -33.666 13.081  -31.085 1   26.213 ? 724 HOH   A O    1 
HETATM 5050 O  O    . HOH   G 5 .   ? 20.038  5.907   -42.799 1   19.347 ? 725 HOH   A O    1 
HETATM 5051 O  O    . HOH   G 5 .   ? 23.764  14.355  -17.128 1   25.37  ? 726 HOH   A O    1 
HETATM 5052 O  O    . HOH   G 5 .   ? 16.398  16.596  -38.869 1   17.014 ? 727 HOH   A O    1 
HETATM 5053 O  O    . HOH   G 5 .   ? 13.055  20.148  -40.554 1   25.845 ? 728 HOH   A O    1 
HETATM 5054 O  O    . HOH   G 5 .   ? -13.756 24.152  -20.517 1   42.949 ? 729 HOH   A O    1 
HETATM 5055 O  O    . HOH   G 5 .   ? 19.536  18.41   -21.162 1   35.803 ? 730 HOH   A O    1 
HETATM 5056 O  O    . HOH   G 5 .   ? -28.676 5.867   -38.207 1   31.086 ? 731 HOH   A O    1 
HETATM 5057 O  O    . HOH   G 5 .   ? -31.174 4.766   -37.861 1   22.811 ? 732 HOH   A O    1 
HETATM 5058 O  O    . HOH   G 5 .   ? 24.306  8.815   -43.81  1   32.364 ? 733 HOH   A O    1 
HETATM 5059 O  O    . HOH   G 5 .   ? -40.114 13.779  -17.833 1   23.92  ? 734 HOH   A O    1 
HETATM 5060 O  O    . HOH   G 5 .   ? 15.174  11.894  -13.114 1   24.608 ? 735 HOH   A O    1 
HETATM 5061 O  O    . HOH   G 5 .   ? -27.786 -5.252  -20.23  1   29.325 ? 736 HOH   A O    1 
HETATM 5062 O  O    . HOH   G 5 .   ? 21.754  -2.17   -34.206 1   20.088 ? 737 HOH   A O    1 
HETATM 5063 O  O    . HOH   G 5 .   ? -16.428 23.151  -17.9   1   24.419 ? 738 HOH   A O    1 
HETATM 5064 O  O    . HOH   G 5 .   ? 19.673  -3.488  -23.006 1   29.831 ? 739 HOH   A O    1 
HETATM 5065 O  O    . HOH   G 5 .   ? 3.44    17.885  -42.989 1   21.223 ? 740 HOH   A O    1 
HETATM 5066 O  O    . HOH   G 5 .   ? -18.931 18.211  -5.265  1   46.314 ? 741 HOH   A O    1 
HETATM 5067 O  O    . HOH   G 5 .   ? 13.58   16.641  -13.416 1   45.938 ? 742 HOH   A O    1 
HETATM 5068 O  O    . HOH   G 5 .   ? -39.377 15.47   -23.203 1   27.905 ? 743 HOH   A O    1 
HETATM 5069 O  O    . HOH   G 5 .   ? -37.667 13.953  -27.605 1   25.093 ? 744 HOH   A O    1 
HETATM 5070 O  O    . HOH   G 5 .   ? -37.242 4.625   -42.428 1   23.651 ? 745 HOH   A O    1 
HETATM 5071 O  O    . HOH   G 5 .   ? 2.47    14.977  -29.468 1   23.852 ? 746 HOH   A O    1 
HETATM 5072 O  O    . HOH   G 5 .   ? 22.772  9.786   -33.971 1   24.788 ? 747 HOH   A O    1 
HETATM 5073 O  O    . HOH   G 5 .   ? -30.519 12.724  -34.57  1   45.391 ? 748 HOH   A O    1 
HETATM 5074 O  O    . HOH   G 5 .   ? -23.235 17.24   -34.419 1   42.586 ? 749 HOH   A O    1 
HETATM 5075 O  O    . HOH   G 5 .   ? 15.335  21.153  -32.823 1   39.995 ? 750 HOH   A O    1 
HETATM 5076 O  O    . HOH   G 5 .   ? 15.4    3.741   -14.996 1   35.884 ? 751 HOH   A O    1 
HETATM 5077 O  O    . HOH   G 5 .   ? 6.152   -4.017  -16.116 1   28.121 ? 752 HOH   A O    1 
HETATM 5078 O  O    . HOH   G 5 .   ? -14.579 17.34   -9.913  1   44.725 ? 753 HOH   A O    1 
HETATM 5079 O  O    . HOH   G 5 .   ? 6.968   17.325  -27.406 1   25.569 ? 754 HOH   A O    1 
HETATM 5080 O  O    . HOH   G 5 .   ? -25.301 3.167   -10.414 1   42.236 ? 755 HOH   A O    1 
HETATM 5081 O  O    . HOH   G 5 .   ? -39.713 1.384   -18.823 1   40.084 ? 756 HOH   A O    1 
HETATM 5082 O  O    . HOH   G 5 .   ? -37.556 15.356  -9.997  1   39.475 ? 757 HOH   A O    1 
HETATM 5083 O  O    . HOH   G 5 .   ? -2.622  3.151   -15.659 1   30.363 ? 758 HOH   A O    1 
HETATM 5084 O  O    . HOH   G 5 .   ? 8.346   -6.296  -25.329 1   11.202 ? 759 HOH   A O    1 
HETATM 5085 O  O    . HOH   G 5 .   ? -31.202 -7.99   -25.526 1   34.816 ? 760 HOH   A O    1 
HETATM 5086 O  O    . HOH   G 5 .   ? 24.479  -2.102  -25.491 1   41.329 ? 761 HOH   A O    1 
HETATM 5087 O  O    . HOH   G 5 .   ? -21.132 -8.585  -25.423 1   36.707 ? 762 HOH   A O    1 
HETATM 5088 O  O    . HOH   G 5 .   ? 3.696   0.342   -17.751 1   13.729 ? 763 HOH   A O    1 
HETATM 5089 O  O    . HOH   G 5 .   ? -14.699 13.912  -8.353  1   28.14  ? 764 HOH   A O    1 
HETATM 5090 O  O    . HOH   G 5 .   ? -31.769 3.331   -40.148 1   27.802 ? 765 HOH   A O    1 
HETATM 5091 O  O    . HOH   G 5 .   ? -35.95  12.366  -29.201 1   22.736 ? 766 HOH   A O    1 
HETATM 5092 O  O    . HOH   G 5 .   ? -25.548 -9.817  -22.339 1   42.901 ? 767 HOH   A O    1 
HETATM 5093 O  O    . HOH   G 5 .   ? 16.513  4.279   -18.501 1   32.657 ? 768 HOH   A O    1 
HETATM 5094 O  O    . HOH   G 5 .   ? -40.441 16.488  -18.182 1   49.415 ? 769 HOH   A O    1 
HETATM 5095 O  O    . HOH   G 5 .   ? 24.5    -2.447  -34.879 1   29.275 ? 770 HOH   A O    1 
HETATM 5096 O  O    . HOH   G 5 .   ? -28.852 -6.608  -22.46  1   36.112 ? 771 HOH   A O    1 
HETATM 5097 O  O    . HOH   G 5 .   ? 19.911  1.246   -41.55  1   30.835 ? 772 HOH   A O    1 
HETATM 5098 O  O    . HOH   G 5 .   ? 0.449   11.398  -34.836 1   31.371 ? 773 HOH   A O    1 
HETATM 5099 O  O    . HOH   G 5 .   ? -40.756 11.077  -14.751 1   27.297 ? 774 HOH   A O    1 
HETATM 5100 O  O    . HOH   G 5 .   ? -0.631  12.805  -30.946 1   26.249 ? 775 HOH   A O    1 
HETATM 5101 O  O    . HOH   G 5 .   ? -15.865 16.453  -29.893 1   23.092 ? 776 HOH   A O    1 
HETATM 5102 O  O    . HOH   G 5 .   ? 30.434  10.415  -37.888 1   40.274 ? 777 HOH   A O    1 
HETATM 5103 O  O    . HOH   G 5 .   ? -15.087 9.601   -39.743 1   41.344 ? 778 HOH   A O    1 
HETATM 5104 O  O    . HOH   G 5 .   ? -25.93  -3.648  -24.4   1   23.321 ? 779 HOH   A O    1 
HETATM 5105 O  O    . HOH   G 5 .   ? 27.627  12.97   -30.447 1   37.222 ? 780 HOH   A O    1 
HETATM 5106 O  O    . HOH   G 5 .   ? -39.539 -1.243  -32.741 1   28.622 ? 781 HOH   A O    1 
HETATM 5107 O  O    . HOH   G 5 .   ? 10.383  23.231  -42.777 1   35.327 ? 782 HOH   A O    1 
HETATM 5108 O  O    . HOH   G 5 .   ? -28.259 1.89    -42.013 1   48.775 ? 783 HOH   A O    1 
HETATM 5109 O  O    . HOH   G 5 .   ? -0.773  20.363  -43.031 1   34.704 ? 784 HOH   A O    1 
HETATM 5110 O  O    . HOH   G 5 .   ? -34.601 4.463   -43.056 1   31.217 ? 785 HOH   A O    1 
HETATM 5111 O  O    . HOH   G 5 .   ? -0.092  12.47   -40.719 1   27.562 ? 786 HOH   A O    1 
HETATM 5112 O  O    . HOH   G 5 .   ? 1.068   16.556  -42.934 1   32.899 ? 787 HOH   A O    1 
HETATM 5113 O  O    . HOH   G 5 .   ? 21.603  14.362  -15.217 1   37.076 ? 788 HOH   A O    1 
HETATM 5114 O  O    . HOH   G 5 .   ? 15.409  11.207  -15.78  1   27.171 ? 789 HOH   A O    1 
HETATM 5115 O  O    . HOH   G 5 .   ? 27.768  12.999  -27.703 1   22.414 ? 790 HOH   A O    1 
HETATM 5116 O  O    . HOH   G 5 .   ? -24.559 21.099  -20.631 1   34.842 ? 791 HOH   A O    1 
HETATM 5117 O  O    . HOH   G 5 .   ? 23.302  9.012   -46.31  1   30.48  ? 792 HOH   A O    1 
HETATM 5118 O  O    . HOH   G 5 .   ? -12.464 6.983   -41.588 1   40.432 ? 793 HOH   A O    1 
HETATM 5119 O  O    . HOH   G 5 .   ? 12.902  2.444   -17.496 1   24.163 ? 794 HOH   A O    1 
HETATM 5120 O  O    . HOH   G 5 .   ? -14.983 18.488  -32.935 1   30.667 ? 795 HOH   A O    1 
HETATM 5121 O  O    . HOH   G 5 .   ? 10.746  14.904  -48.476 1   37.679 ? 796 HOH   A O    1 
HETATM 5122 O  O    . HOH   G 5 .   ? -37.927 11.031  -30.586 1   21.276 ? 797 HOH   A O    1 
HETATM 5123 O  O    . HOH   G 5 .   ? 2.84    21.917  -25.105 1   36.182 ? 798 HOH   A O    1 
HETATM 5124 O  O    . HOH   G 5 .   ? 15.078  14.124  -50.734 1   34.463 ? 799 HOH   A O    1 
HETATM 5125 O  O    . HOH   G 5 .   ? 23.444  12.436  -33.219 1   22.96  ? 800 HOH   A O    1 
HETATM 5126 O  O    . HOH   G 5 .   ? 13.575  8.305   -54.353 1   21.453 ? 801 HOH   A O    1 
HETATM 5127 O  O    . HOH   G 5 .   ? -40.712 0.088   -28.139 1   42.303 ? 802 HOH   A O    1 
HETATM 5128 O  O    . HOH   G 5 .   ? 10.57   19.879  -23.778 1   33.82  ? 803 HOH   A O    1 
HETATM 5129 O  O    . HOH   G 5 .   ? -22.124 18.709  -27.189 1   30.963 ? 804 HOH   A O    1 
HETATM 5130 O  O    . HOH   G 5 .   ? -25.931 -8.404  -25.241 1   40.932 ? 805 HOH   A O    1 
HETATM 5131 O  O    . HOH   G 5 .   ? 6.637   3.838   -49.652 1   40.169 ? 806 HOH   A O    1 
HETATM 5132 O  O    . HOH   G 5 .   ? 21.131  10.843  -47.597 1   23.971 ? 807 HOH   A O    1 
HETATM 5133 O  O    . HOH   G 5 .   ? -3.431  -4.783  -26.5   1   34.637 ? 808 HOH   A O    1 
HETATM 5134 O  O    . HOH   G 5 .   ? 25.776  14.991  -27.016 1   25.939 ? 809 HOH   A O    1 
HETATM 5135 O  O    . HOH   G 5 .   ? 10.26   19.552  -19.698 1   40.274 ? 810 HOH   A O    1 
HETATM 5136 O  O    . HOH   G 5 .   ? 13.51   17.173  -45.218 1   24.334 ? 811 HOH   A O    1 
HETATM 5137 O  O    . HOH   G 5 .   ? 1.313   8.585   -37.595 1   32.411 ? 812 HOH   A O    1 
HETATM 5138 O  O    . HOH   G 5 .   ? 21.088  13.286  -46.279 1   24.933 ? 813 HOH   A O    1 
HETATM 5139 O  O    . HOH   G 5 .   ? 22.33   -12.76  -34.553 1   31.996 ? 814 HOH   A O    1 
HETATM 5140 O  O    . HOH   G 5 .   ? 10.511  0.184   -16.138 1   29.821 ? 815 HOH   A O    1 
HETATM 5141 O  O    . HOH   G 5 .   ? -23.432 -9.236  -26.358 1   39.193 ? 816 HOH   A O    1 
HETATM 5142 O  O    . HOH   G 5 .   ? 11.061  7.372   -55.007 1   21.22  ? 817 HOH   A O    1 
HETATM 5143 O  O    . HOH   G 5 .   ? 2.199   18.218  -20.252 1   34.172 ? 818 HOH   A O    1 
HETATM 5144 O  O    . HOH   G 5 .   ? -9.772  3       -42.138 1   36.603 ? 819 HOH   A O    1 
HETATM 5145 O  O    . HOH   G 5 .   ? -2.361  13.925  -37.232 1   29.696 ? 820 HOH   A O    1 
HETATM 5146 O  O    . HOH   G 5 .   ? -19.186 -10.757 -24.358 1   36.096 ? 821 HOH   A O    1 
HETATM 5147 O  O    . HOH   G 5 .   ? -20.638 -8.275  -29.026 1   35.051 ? 822 HOH   A O    1 
HETATM 5148 O  O    . HOH   G 5 .   ? -6.083  20.847  -23.249 1   36.063 ? 823 HOH   A O    1 
HETATM 5149 O  O    . HOH   G 5 .   ? -25.314 4.082   -39.487 1   29.621 ? 824 HOH   A O    1 
HETATM 5150 O  O    . HOH   G 5 .   ? -26.926 18.415  -5.875  1   35.699 ? 825 HOH   A O    1 
HETATM 5151 O  O    . HOH   G 5 .   ? -16.772 24.299  -13.404 1   36.502 ? 826 HOH   A O    1 
HETATM 5152 O  O    . HOH   G 5 .   ? -26.518 -6.206  -23.81  1   28.423 ? 827 HOH   A O    1 
HETATM 5153 O  O    . HOH   G 5 .   ? -38.346 11.363  -35.084 1   48.977 ? 828 HOH   A O    1 
HETATM 5154 O  O    . HOH   G 5 .   ? 17.57   16.036  -45.87  1   25.486 ? 829 HOH   A O    1 
HETATM 5155 O  O    . HOH   G 5 .   ? 4.703   22.43   -43.968 1   17.932 ? 830 HOH   A O    1 
HETATM 5156 O  O    . HOH   G 5 .   ? 18.693  19.568  -36.092 1   33.696 ? 831 HOH   A O    1 
HETATM 5157 O  O    . HOH   G 5 .   ? 20.388  11.841  -50.965 1   36.86  ? 832 HOH   A O    1 
HETATM 5158 O  O    . HOH   G 5 .   ? 0.654   10.794  -44.175 1   33.82  ? 833 HOH   A O    1 
HETATM 5159 O  O    . HOH   G 5 .   ? 18.815  17.081  -40.241 1   28.789 ? 834 HOH   A O    1 
HETATM 5160 O  O    . HOH   G 5 .   ? -19.719 -8.448  -34.874 1   38.258 ? 835 HOH   A O    1 
HETATM 5161 O  O    . HOH   G 5 .   ? 4.454   20.056  -24.054 1   35.813 ? 836 HOH   A O    1 
HETATM 5162 O  O    . HOH   G 5 .   ? 9.414   -4.294  -37.449 1   28.519 ? 837 HOH   A O    1 
HETATM 5163 O  O    . HOH   G 5 .   ? 14.62   17.873  -40.833 1   21.015 ? 838 HOH   A O    1 
HETATM 5164 O  O    . HOH   G 5 .   ? -34.667 11.161  -33.124 1   26.002 ? 839 HOH   A O    1 
HETATM 5165 O  O    . HOH   G 5 .   ? 17.381  15.465  -50.631 1   37.639 ? 840 HOH   A O    1 
HETATM 5166 O  O    . HOH   G 5 .   ? 2.419   11.536  -45.985 1   41.794 ? 841 HOH   A O    1 
HETATM 5167 O  O    . HOH   G 5 .   ? 6.73    19.967  -26.115 1   28.752 ? 842 HOH   A O    1 
HETATM 5168 O  O    . HOH   G 5 .   ? 20.962  14.497  -48.692 1   45.538 ? 843 HOH   A O    1 
HETATM 5169 O  O    . HOH   G 5 .   ? 19.876  14.397  -50.997 1   33.439 ? 844 HOH   A O    1 
HETATM 5170 O  O    . HOH   G 5 .   ? 16.87   18.742  -42.229 1   34.724 ? 845 HOH   A O    1 
HETATM 5171 O  O    . HOH   G 5 .   ? 6.431   5.048   -52.564 1   38.049 ? 846 HOH   A O    1 
HETATM 5172 O  O    . HOH   H 5 .   ? 2.169   -28.316 -21.674 1   21.035 ? 501 HOH   B O    1 
HETATM 5173 O  O    . HOH   H 5 .   ? -0.191  24.737  7.355   1   24.089 ? 502 HOH   B O    1 
HETATM 5174 O  O    . HOH   H 5 .   ? 11.442  -0.022  11.189  1   23.036 ? 503 HOH   B O    1 
HETATM 5175 O  O    . HOH   H 5 .   ? -8.295  -2.945  0.425   1   27.62  ? 504 HOH   B O    1 
HETATM 5176 O  O    . HOH   H 5 .   ? 1.988   5.534   10.326  1   46.123 ? 505 HOH   B O    1 
HETATM 5177 O  O    . HOH   H 5 .   ? -11.825 11.228  10.242  1   40.392 ? 506 HOH   B O    1 
HETATM 5178 O  O    . HOH   H 5 .   ? 2.275   -17.702 -1.78   1   37.834 ? 507 HOH   B O    1 
HETATM 5179 O  O    . HOH   H 5 .   ? 1.453   0.402   4.834   1   15.912 ? 508 HOH   B O    1 
HETATM 5180 O  O    . HOH   H 5 .   ? 10.025  -9.436  -18.096 1   30.43  ? 509 HOH   B O    1 
HETATM 5181 O  O    . HOH   H 5 .   ? -1.386  20.867  -4.432  1   34.113 ? 510 HOH   B O    1 
HETATM 5182 O  O    . HOH   H 5 .   ? 12.614  18.505  -4.61   1   28.837 ? 511 HOH   B O    1 
HETATM 5183 O  O    . HOH   H 5 .   ? 5.611   -4.269  -18.986 1   34.86  ? 512 HOH   B O    1 
HETATM 5184 O  O    . HOH   H 5 .   ? 11.557  -35.989 -14.476 1   26.632 ? 513 HOH   B O    1 
HETATM 5185 O  O    . HOH   H 5 .   ? 1.402   1.691   13.699  1   25.446 ? 514 HOH   B O    1 
HETATM 5186 O  O    . HOH   H 5 .   ? 14.14   18.464  2.843   1   16.369 ? 515 HOH   B O    1 
HETATM 5187 O  O    . HOH   H 5 .   ? -18.714 -6.411  -13.74  1   54.276 ? 516 HOH   B O    1 
HETATM 5188 O  O    . HOH   H 5 .   ? 22.985  17.66   10.158  1   27.892 ? 517 HOH   B O    1 
HETATM 5189 O  O    . HOH   H 5 .   ? 13.808  -27.036 -25.183 1   23.564 ? 518 HOH   B O    1 
HETATM 5190 O  O    . HOH   H 5 .   ? 15.014  22.07   -0.142  1   29.292 ? 519 HOH   B O    1 
HETATM 5191 O  O    . HOH   H 5 .   ? -13.693 17.451  8.528   1   33.201 ? 520 HOH   B O    1 
HETATM 5192 O  O    . HOH   H 5 .   ? 9.339   -20.613 -29.011 1   40.247 ? 521 HOH   B O    1 
HETATM 5193 O  O    . HOH   H 5 .   ? -10.671 -8.351  -21.509 1   26.166 ? 522 HOH   B O    1 
HETATM 5194 O  O    . HOH   H 5 .   ? 12.338  -14.28  -31.077 1   40.227 ? 523 HOH   B O    1 
HETATM 5195 O  O    . HOH   H 5 .   ? -11.109 10.499  -1.142  1   26.431 ? 524 HOH   B O    1 
HETATM 5196 O  O    . HOH   H 5 .   ? -4.889  -29.224 -21.799 1   34.381 ? 525 HOH   B O    1 
HETATM 5197 O  O    . HOH   H 5 .   ? -2.876  -27.414 -6.502  1   38.522 ? 526 HOH   B O    1 
HETATM 5198 O  O    . HOH   H 5 .   ? 9.796   -12.333 -30.302 1   26.394 ? 527 HOH   B O    1 
HETATM 5199 O  O    . HOH   H 5 .   ? 8.299   -28.934 -22.257 1   37.008 ? 528 HOH   B O    1 
HETATM 5200 O  O    . HOH   H 5 .   ? 18.865  -18.247 -9.614  1   32.83  ? 529 HOH   B O    1 
HETATM 5201 O  O    . HOH   H 5 .   ? 6.73    -12.896 -1.973  1   35.79  ? 530 HOH   B O    1 
HETATM 5202 O  O    . HOH   H 5 .   ? -4.721  8.594   9.72    1   18.007 ? 531 HOH   B O    1 
HETATM 5203 O  O    . HOH   H 5 .   ? 26.027  15.979  7.101   1   29.259 ? 532 HOH   B O    1 
HETATM 5204 O  O    . HOH   H 5 .   ? -2.912  -8.587  -6.885  1   25.355 ? 533 HOH   B O    1 
HETATM 5205 O  O    . HOH   H 5 .   ? -7.704  -19.688 -26.014 1   34.485 ? 534 HOH   B O    1 
HETATM 5206 O  O    . HOH   H 5 .   ? 10.356  17.556  -11.351 1   34.926 ? 535 HOH   B O    1 
HETATM 5207 O  O    . HOH   H 5 .   ? 0.899   24.482  9.926   1   27.973 ? 536 HOH   B O    1 
HETATM 5208 O  O    . HOH   H 5 .   ? 0.836   -14.229 -30.927 1   34.291 ? 537 HOH   B O    1 
HETATM 5209 O  O    . HOH   H 5 .   ? -6.81   -18.236 -6.463  1   35.573 ? 538 HOH   B O    1 
HETATM 5210 O  O    . HOH   H 5 .   ? 25.729  18.829  1.079   1   41.759 ? 539 HOH   B O    1 
HETATM 5211 O  O    . HOH   H 5 .   ? -0.43   -1.989  8.966   1   29.735 ? 540 HOH   B O    1 
HETATM 5212 O  O    . HOH   H 5 .   ? 0.238   9.747   -4.133  1   24.813 ? 541 HOH   B O    1 
HETATM 5213 O  O    . HOH   H 5 .   ? 6.052   10.892  -12.411 1   16.299 ? 542 HOH   B O    1 
HETATM 5214 O  O    . HOH   H 5 .   ? 17.1    9.649   22.051  1   26.033 ? 543 HOH   B O    1 
HETATM 5215 O  O    . HOH   H 5 .   ? 9.475   -15.299 -4.547  1   34.072 ? 544 HOH   B O    1 
HETATM 5216 O  O    . HOH   H 5 .   ? 17.824  -5.065  -3.062  1   25.463 ? 545 HOH   B O    1 
HETATM 5217 O  O    . HOH   H 5 .   ? 12.888  -29.35  -22.581 1   21.378 ? 546 HOH   B O    1 
HETATM 5218 O  O    . HOH   H 5 .   ? 4.027   -2.259  8.687   1   21.371 ? 547 HOH   B O    1 
HETATM 5219 O  O    . HOH   H 5 .   ? 3.506   -2.958  -13.834 1   17.677 ? 548 HOH   B O    1 
HETATM 5220 O  O    . HOH   H 5 .   ? 19.13   7.451   -10.654 1   24.826 ? 549 HOH   B O    1 
HETATM 5221 O  O    . HOH   H 5 .   ? 20.064  16.844  -1.302  1   40.223 ? 550 HOH   B O    1 
HETATM 5222 O  O    . HOH   H 5 .   ? 7.955   25.84   6.255   1   34.132 ? 551 HOH   B O    1 
HETATM 5223 O  O    . HOH   H 5 .   ? 15.337  -13.007 -14.392 1   30.579 ? 552 HOH   B O    1 
HETATM 5224 O  O    . HOH   H 5 .   ? 16.548  10.062  15.035  1   19.851 ? 553 HOH   B O    1 
HETATM 5225 O  O    . HOH   H 5 .   ? 17.343  10.688  -11.963 1   23.113 ? 554 HOH   B O    1 
HETATM 5226 O  O    . HOH   H 5 .   ? 9.973   19.552  17.692  1   26.712 ? 555 HOH   B O    1 
HETATM 5227 O  O    . HOH   H 5 .   ? -12.47  -12.521 -19.79  1   34.05  ? 556 HOH   B O    1 
HETATM 5228 O  O    . HOH   H 5 .   ? 14.109  -2.518  5.457   1   27.714 ? 557 HOH   B O    1 
HETATM 5229 O  O    . HOH   H 5 .   ? 19.3    -25.242 -11.442 1   36.466 ? 558 HOH   B O    1 
HETATM 5230 O  O    . HOH   H 5 .   ? 14.064  -28.147 -7.444  1   26.943 ? 559 HOH   B O    1 
HETATM 5231 O  O    . HOH   H 5 .   ? -9.828  14.462  -8.295  1   44.719 ? 560 HOH   B O    1 
HETATM 5232 O  O    . HOH   H 5 .   ? 15.534  -17.145 -21.753 1   30.748 ? 561 HOH   B O    1 
HETATM 5233 O  O    . HOH   H 5 .   ? 23.963  -4.503  -5.815  1   29.508 ? 562 HOH   B O    1 
HETATM 5234 O  O    . HOH   H 5 .   ? 9.17    -18.071 -4.341  1   26.352 ? 563 HOH   B O    1 
HETATM 5235 O  O    . HOH   H 5 .   ? 16.564  -26.242 -27.689 1   28.55  ? 564 HOH   B O    1 
HETATM 5236 O  O    . HOH   H 5 .   ? -1.008  -5.54   -12.431 1   15.737 ? 565 HOH   B O    1 
HETATM 5237 O  O    . HOH   H 5 .   ? 6.426   18.232  -4.674  1   15.773 ? 566 HOH   B O    1 
HETATM 5238 O  O    . HOH   H 5 .   ? 22.527  9.176   10.286  1   25.48  ? 567 HOH   B O    1 
HETATM 5239 O  O    . HOH   H 5 .   ? 7.189   -7.291  -16.581 1   21.776 ? 568 HOH   B O    1 
HETATM 5240 O  O    . HOH   H 5 .   ? 4.747   29.499  9.449   1   17.622 ? 569 HOH   B O    1 
HETATM 5241 O  O    . HOH   H 5 .   ? 13.552  -17.564 -30.233 1   30.001 ? 570 HOH   B O    1 
HETATM 5242 O  O    . HOH   H 5 .   ? 22.554  15.814  -0.127  1   32.529 ? 571 HOH   B O    1 
HETATM 5243 O  O    . HOH   H 5 .   ? 10.237  15.02   -3.625  1   14.08  ? 572 HOH   B O    1 
HETATM 5244 O  O    . HOH   H 5 .   ? -7.435  17.043  15.044  1   25.488 ? 573 HOH   B O    1 
HETATM 5245 O  O    . HOH   H 5 .   ? -2.688  -4.476  -8.043  1   20.102 ? 574 HOH   B O    1 
HETATM 5246 O  O    . HOH   H 5 .   ? 11.276  -12.364 -27.864 1   26.073 ? 575 HOH   B O    1 
HETATM 5247 O  O    . HOH   H 5 .   ? 20.475  7.883   -6.02   1   33.854 ? 576 HOH   B O    1 
HETATM 5248 O  O    . HOH   H 5 .   ? 12.093  7.338   13.658  1   15.898 ? 577 HOH   B O    1 
HETATM 5249 O  O    . HOH   H 5 .   ? 4.593   -19.082 -1.675  1   26.875 ? 578 HOH   B O    1 
HETATM 5250 O  O    . HOH   H 5 .   ? 14.888  -20.031 -8.188  1   23.541 ? 579 HOH   B O    1 
HETATM 5251 O  O    . HOH   H 5 .   ? -8.784  13.261  -11.695 1   13.689 ? 580 HOH   B O    1 
HETATM 5252 O  O    . HOH   H 5 .   ? 22.514  22.236  6.933   1   31.005 ? 581 HOH   B O    1 
HETATM 5253 O  O    . HOH   H 5 .   ? -11.975 -14.994 -17.79  1   41.483 ? 582 HOH   B O    1 
HETATM 5254 O  O    . HOH   H 5 .   ? -6.469  14.946  -8.611  1   24.808 ? 583 HOH   B O    1 
HETATM 5255 O  O    . HOH   H 5 .   ? -20.504 -2.876  -10.593 1   45.247 ? 584 HOH   B O    1 
HETATM 5256 O  O    . HOH   H 5 .   ? -4.68   16.484  -10.197 1   36.461 ? 585 HOH   B O    1 
HETATM 5257 O  O    . HOH   H 5 .   ? 8.014   15.482  18.029  1   38.719 ? 586 HOH   B O    1 
HETATM 5258 O  O    . HOH   H 5 .   ? 10.877  17.592  -2.752  1   15.663 ? 587 HOH   B O    1 
HETATM 5259 O  O    . HOH   H 5 .   ? 12.346  -13.951 -19.006 1   22.601 ? 588 HOH   B O    1 
HETATM 5260 O  O    . HOH   H 5 .   ? 8.887   10.39   -14.532 1   26.016 ? 589 HOH   B O    1 
HETATM 5261 O  O    . HOH   H 5 .   ? -1.224  -0.691  11.288  1   35.017 ? 590 HOH   B O    1 
HETATM 5262 O  O    . HOH   H 5 .   ? 15.908  -0.646  6.064   1   25.007 ? 591 HOH   B O    1 
HETATM 5263 O  O    . HOH   H 5 .   ? 1.355   -26.298 -22.353 1   17.456 ? 592 HOH   B O    1 
HETATM 5264 O  O    . HOH   H 5 .   ? 21.545  7.188   8.55    1   24.044 ? 593 HOH   B O    1 
HETATM 5265 O  O    . HOH   H 5 .   ? 9.641   24.638  -1.711  1   39.206 ? 594 HOH   B O    1 
HETATM 5266 O  O    . HOH   H 5 .   ? 16.281  21.298  11.887  1   27.059 ? 595 HOH   B O    1 
HETATM 5267 O  O    . HOH   H 5 .   ? -8.764  -8.54   -27.805 1   30.823 ? 596 HOH   B O    1 
HETATM 5268 O  O    . HOH   H 5 .   ? 4.882   -15.271 -3.346  1   36.624 ? 597 HOH   B O    1 
HETATM 5269 O  O    . HOH   H 5 .   ? 4.127   -29.789 -3.457  1   43.094 ? 598 HOH   B O    1 
HETATM 5270 O  O    . HOH   H 5 .   ? 0.16    -8.015  2.854   1   38.328 ? 599 HOH   B O    1 
HETATM 5271 O  O    . HOH   H 5 .   ? 3.439   -6.737  -21.322 1   30.887 ? 600 HOH   B O    1 
HETATM 5272 O  O    . HOH   H 5 .   ? 22.583  8.298   -4.45   1   32.323 ? 601 HOH   B O    1 
HETATM 5273 O  O    . HOH   H 5 .   ? 24.669  15.69   9.449   1   33.166 ? 602 HOH   B O    1 
HETATM 5274 O  O    . HOH   H 5 .   ? 10.878  -28.771 -16.231 1   30.6   ? 603 HOH   B O    1 
HETATM 5275 O  O    . HOH   H 5 .   ? 8.073   -2.516  -10.45  1   12.589 ? 604 HOH   B O    1 
HETATM 5276 O  O    . HOH   H 5 .   ? 13.847  -7.58   -13.023 1   37.026 ? 605 HOH   B O    1 
HETATM 5277 O  O    . HOH   H 5 .   ? -2.963  10.497  16.148  1   30.993 ? 606 HOH   B O    1 
HETATM 5278 O  O    . HOH   H 5 .   ? 8.56    27.267  3.994   1   29.461 ? 607 HOH   B O    1 
HETATM 5279 O  O    . HOH   H 5 .   ? -12.145 -21.586 -12.707 1   35.121 ? 608 HOH   B O    1 
HETATM 5280 O  O    . HOH   H 5 .   ? 12.618  15.204  18.046  1   24.516 ? 609 HOH   B O    1 
HETATM 5281 O  O    . HOH   H 5 .   ? -3.775  -3.923  7.752   1   36.528 ? 610 HOH   B O    1 
HETATM 5282 O  O    . HOH   H 5 .   ? -0.906  -6.267  -21.622 1   41.305 ? 611 HOH   B O    1 
HETATM 5283 O  O    . HOH   H 5 .   ? -10.45  16.946  1.375   1   29.108 ? 612 HOH   B O    1 
HETATM 5284 O  O    . HOH   H 5 .   ? 12.474  -11.479 -2.405  1   21.346 ? 613 HOH   B O    1 
HETATM 5285 O  O    . HOH   H 5 .   ? 2.602   -12.615 -6.972  1   20.208 ? 614 HOH   B O    1 
HETATM 5286 O  O    . HOH   H 5 .   ? -6.139  -18.568 -10.408 1   34.521 ? 615 HOH   B O    1 
HETATM 5287 O  O    . HOH   H 5 .   ? 16.539  -15.232 -17.693 1   29.558 ? 616 HOH   B O    1 
HETATM 5288 O  O    . HOH   H 5 .   ? -0.885  22.079  19.449  1   35.14  ? 617 HOH   B O    1 
HETATM 5289 O  O    . HOH   H 5 .   ? 13.741  16.157  1.278   1   16.569 ? 618 HOH   B O    1 
HETATM 5290 O  O    . HOH   H 5 .   ? -3.489  -25.641 -9.422  1   24.014 ? 619 HOH   B O    1 
HETATM 5291 O  O    . HOH   H 5 .   ? -1.219  7.32    12.793  1   30.168 ? 620 HOH   B O    1 
HETATM 5292 O  O    . HOH   H 5 .   ? 11.839  0.117   -1.458  1   12.663 ? 621 HOH   B O    1 
HETATM 5293 O  O    . HOH   H 5 .   ? 26.931  10.441  3.04    1   31.049 ? 622 HOH   B O    1 
HETATM 5294 O  O    . HOH   H 5 .   ? 3.639   -8.491  4.745   1   31.917 ? 623 HOH   B O    1 
HETATM 5295 O  O    . HOH   H 5 .   ? -5.452  -5.404  1.87    1   38.979 ? 624 HOH   B O    1 
HETATM 5296 O  O    . HOH   H 5 .   ? 0.746   -11.072 -29.318 1   27.271 ? 625 HOH   B O    1 
HETATM 5297 O  O    . HOH   H 5 .   ? 15.818  -16.142 -6.295  1   35.608 ? 626 HOH   B O    1 
HETATM 5298 O  O    . HOH   H 5 .   ? -8.339  -22.788 -22.986 1   32.941 ? 627 HOH   B O    1 
HETATM 5299 O  O    . HOH   H 5 .   ? 2.746   23.546  1.552   1   26.75  ? 628 HOH   B O    1 
HETATM 5300 O  O    . HOH   H 5 .   ? 25.57   2.532   -5.518  1   36.711 ? 629 HOH   B O    1 
HETATM 5301 O  O    . HOH   H 5 .   ? 9.44    8.846   17.278  1   28.908 ? 630 HOH   B O    1 
HETATM 5302 O  O    . HOH   H 5 .   ? 7.595   -7.696  2.593   1   23.894 ? 631 HOH   B O    1 
HETATM 5303 O  O    . HOH   H 5 .   ? 15.816  15.373  -6.674  1   39.246 ? 632 HOH   B O    1 
HETATM 5304 O  O    . HOH   H 5 .   ? 26.96   3.221   2.053   1   38.496 ? 633 HOH   B O    1 
HETATM 5305 O  O    . HOH   H 5 .   ? 12.616  9.77    4.817   1   12.253 ? 634 HOH   B O    1 
HETATM 5306 O  O    . HOH   H 5 .   ? 15.781  -9.289  -1.98   1   15.585 ? 635 HOH   B O    1 
HETATM 5307 O  O    . HOH   H 5 .   ? 12.697  -31.149 -20.605 1   22.207 ? 636 HOH   B O    1 
HETATM 5308 O  O    . HOH   H 5 .   ? 14.792  -4.744  -11.453 1   35.379 ? 637 HOH   B O    1 
HETATM 5309 O  O    . HOH   H 5 .   ? 15.669  -3.116  -9.475  1   21.288 ? 638 HOH   B O    1 
HETATM 5310 O  O    . HOH   H 5 .   ? 10.393  -8.319  -15.447 1   27.883 ? 639 HOH   B O    1 
HETATM 5311 O  O    . HOH   H 5 .   ? 16.984  -25.434 -18.455 1   35.517 ? 640 HOH   B O    1 
HETATM 5312 O  O    . HOH   H 5 .   ? -3.107  -4.575  -14.062 1   13.589 ? 641 HOH   B O    1 
HETATM 5313 O  O    . HOH   H 5 .   ? 6.621   -7.399  -20.9   1   37.518 ? 642 HOH   B O    1 
HETATM 5314 O  O    . HOH   H 5 .   ? 9.701   2.602   -15.247 1   19.713 ? 643 HOH   B O    1 
HETATM 5315 O  O    . HOH   H 5 .   ? 12.38   2.765   -12.618 1   17.188 ? 644 HOH   B O    1 
HETATM 5316 O  O    . HOH   H 5 .   ? 8.416   1.344   15.148  1   26.094 ? 645 HOH   B O    1 
HETATM 5317 O  O    . HOH   H 5 .   ? 0.818   -33.647 -20.381 1   41.432 ? 646 HOH   B O    1 
HETATM 5318 O  O    . HOH   H 5 .   ? 2.663   -11.025 -15.114 1   11.516 ? 647 HOH   B O    1 
HETATM 5319 O  O    . HOH   H 5 .   ? 21.623  15.775  11.828  1   26.56  ? 648 HOH   B O    1 
HETATM 5320 O  O    . HOH   H 5 .   ? 9.836   -6.915  4.068   1   18.501 ? 649 HOH   B O    1 
HETATM 5321 O  O    . HOH   H 5 .   ? 2.087   13.501  15.153  1   24.181 ? 650 HOH   B O    1 
HETATM 5322 O  O    . HOH   H 5 .   ? 12.601  -14.615 -27.896 1   34.897 ? 651 HOH   B O    1 
HETATM 5323 O  O    . HOH   H 5 .   ? 18.469  10.135  16.765  1   36.271 ? 652 HOH   B O    1 
HETATM 5324 O  O    . HOH   H 5 .   ? -10.881 -27.799 -17.393 1   21.875 ? 653 HOH   B O    1 
HETATM 5325 O  O    . HOH   H 5 .   ? 18.809  14.278  -3.768  1   25.447 ? 654 HOH   B O    1 
HETATM 5326 O  O    . HOH   H 5 .   ? -1.075  -7.248  -5.252  1   21.527 ? 655 HOH   B O    1 
HETATM 5327 O  O    . HOH   H 5 .   ? 12.246  -5.529  3.26    1   16.153 ? 656 HOH   B O    1 
HETATM 5328 O  O    . HOH   H 5 .   ? 4.39    -25.082 -28.579 1   43.179 ? 657 HOH   B O    1 
HETATM 5329 O  O    . HOH   H 5 .   ? -7.26   -25.964 -23.486 1   29.332 ? 658 HOH   B O    1 
HETATM 5330 O  O    . HOH   H 5 .   ? 20.917  0.823   -7.734  1   21.928 ? 659 HOH   B O    1 
HETATM 5331 O  O    . HOH   H 5 .   ? -7.04   28.288  3.452   1   38.381 ? 660 HOH   B O    1 
HETATM 5332 O  O    . HOH   H 5 .   ? 13.202  -12.119 -17.345 1   31.175 ? 661 HOH   B O    1 
HETATM 5333 O  O    . HOH   H 5 .   ? 16.826  9.998   -5.155  1   19.064 ? 662 HOH   B O    1 
HETATM 5334 O  O    . HOH   H 5 .   ? 6.431   -22.876 -25.116 1   22.892 ? 663 HOH   B O    1 
HETATM 5335 O  O    . HOH   H 5 .   ? 3.388   -2.655  -18.669 1   29.507 ? 664 HOH   B O    1 
HETATM 5336 O  O    . HOH   H 5 .   ? 16.435  -16.986 -8.939  1   32.987 ? 665 HOH   B O    1 
HETATM 5337 O  O    . HOH   H 5 .   ? 2.909   -29.066 -7.634  1   35.972 ? 666 HOH   B O    1 
HETATM 5338 O  O    . HOH   H 5 .   ? -4.912  -7.391  -25.497 1   28.739 ? 667 HOH   B O    1 
HETATM 5339 O  O    . HOH   H 5 .   ? 5.288   -31.741 -8.669  1   30.558 ? 668 HOH   B O    1 
HETATM 5340 O  O    . HOH   H 5 .   ? -3.315  19.166  -2.623  1   30.693 ? 669 HOH   B O    1 
HETATM 5341 O  O    . HOH   H 5 .   ? 1.246   -8.139  -22.201 1   21.729 ? 670 HOH   B O    1 
HETATM 5342 O  O    . HOH   H 5 .   ? 28.657  6.909   -0.028  1   39.133 ? 671 HOH   B O    1 
HETATM 5343 O  O    . HOH   H 5 .   ? -14.785 -10.457 -24.006 1   22.02  ? 672 HOH   B O    1 
HETATM 5344 O  O    . HOH   H 5 .   ? 22.923  -8.581  -5.507  1   27.837 ? 673 HOH   B O    1 
HETATM 5345 O  O    . HOH   H 5 .   ? -12.471 17.57   11.882  1   35.458 ? 674 HOH   B O    1 
HETATM 5346 O  O    . HOH   H 5 .   ? -4.421  0.111   9.089   1   22.446 ? 675 HOH   B O    1 
HETATM 5347 O  O    . HOH   H 5 .   ? -14.386 4.447   1.101   1   23.829 ? 676 HOH   B O    1 
HETATM 5348 O  O    . HOH   H 5 .   ? 8.421   -31.316 -20.26  1   36.607 ? 677 HOH   B O    1 
HETATM 5349 O  O    . HOH   H 5 .   ? 8.956   11.728  17.156  1   26.661 ? 678 HOH   B O    1 
HETATM 5350 O  O    . HOH   H 5 .   ? 9.674   26.617  0.033   1   36.969 ? 679 HOH   B O    1 
HETATM 5351 O  O    . HOH   H 5 .   ? 4.067   17.818  18.534  1   28.533 ? 680 HOH   B O    1 
HETATM 5352 O  O    . HOH   H 5 .   ? 6.419   -25.732 -2.281  1   32.056 ? 681 HOH   B O    1 
HETATM 5353 O  O    . HOH   H 5 .   ? 16.259  4.278   7.246   1   14.829 ? 682 HOH   B O    1 
HETATM 5354 O  O    . HOH   H 5 .   ? 11.248  21.616  -2.966  1   21.925 ? 683 HOH   B O    1 
HETATM 5355 O  O    . HOH   H 5 .   ? -13.979 -4.957  -5.449  1   43.604 ? 684 HOH   B O    1 
HETATM 5356 O  O    . HOH   H 5 .   ? 11.578  -12.227 -20.962 1   17.166 ? 685 HOH   B O    1 
HETATM 5357 O  O    . HOH   H 5 .   ? 10.94   -32.576 -16.644 1   36.63  ? 686 HOH   B O    1 
HETATM 5358 O  O    . HOH   H 5 .   ? -2.031  -2.701  -0.896  1   17.566 ? 687 HOH   B O    1 
HETATM 5359 O  O    . HOH   H 5 .   ? 17.985  -1.9    -10.62  1   27.349 ? 688 HOH   B O    1 
HETATM 5360 O  O    . HOH   H 5 .   ? -16.573 2.362   -3.917  1   44.457 ? 689 HOH   B O    1 
HETATM 5361 O  O    . HOH   H 5 .   ? -13.439 7.272   6.51    1   40.061 ? 690 HOH   B O    1 
HETATM 5362 O  O    . HOH   H 5 .   ? 22.882  5.892   -3.58   1   31.151 ? 691 HOH   B O    1 
HETATM 5363 O  O    . HOH   H 5 .   ? 13.676  -22.408 -8.101  1   27.208 ? 692 HOH   B O    1 
HETATM 5364 O  O    . HOH   H 5 .   ? -8.97   28.699  -0.684  1   34.476 ? 693 HOH   B O    1 
HETATM 5365 O  O    . HOH   H 5 .   ? -5.337  -6.371  -14.086 1   20.103 ? 694 HOH   B O    1 
HETATM 5366 O  O    . HOH   H 5 .   ? 0.329   -5.77   6.601   1   22.611 ? 695 HOH   B O    1 
HETATM 5367 O  O    . HOH   H 5 .   ? -1.59   -18.133 -30.788 1   31.582 ? 696 HOH   B O    1 
HETATM 5368 O  O    . HOH   H 5 .   ? 6.657   -25.615 -26.502 1   35.316 ? 697 HOH   B O    1 
HETATM 5369 O  O    . HOH   H 5 .   ? 12.622  -9.46   -14.633 1   29.108 ? 698 HOH   B O    1 
HETATM 5370 O  O    . HOH   H 5 .   ? -5.033  16.348  -4.398  1   33.515 ? 699 HOH   B O    1 
HETATM 5371 O  O    . HOH   H 5 .   ? 18.938  -6.32   -11.353 1   41.231 ? 700 HOH   B O    1 
HETATM 5372 O  O    . HOH   H 5 .   ? 6.096   -0.447  12.36   1   24.581 ? 701 HOH   B O    1 
HETATM 5373 O  O    . HOH   H 5 .   ? 15.146  -29.588 -14.779 1   36.398 ? 702 HOH   B O    1 
HETATM 5374 O  O    . HOH   H 5 .   ? 1.26    17.823  -10.439 1   30.815 ? 703 HOH   B O    1 
HETATM 5375 O  O    . HOH   H 5 .   ? -0.984  -29.373 -7.157  1   29.505 ? 704 HOH   B O    1 
HETATM 5376 O  O    . HOH   H 5 .   ? 19.204  22.34   1.39    1   28.173 ? 705 HOH   B O    1 
HETATM 5377 O  O    . HOH   H 5 .   ? 19.002  7.709   7.911   1   18.435 ? 706 HOH   B O    1 
HETATM 5378 O  O    . HOH   H 5 .   ? 14.162  14.719  -11.753 1   22.76  ? 707 HOH   B O    1 
HETATM 5379 O  O    . HOH   H 5 .   ? 9.131   5.021   15.63   1   17.909 ? 708 HOH   B O    1 
HETATM 5380 O  O    . HOH   H 5 .   ? 26.47   0.569   -1.234  1   35.533 ? 709 HOH   B O    1 
HETATM 5381 O  O    . HOH   H 5 .   ? 28.151  11.068  5.359   1   37.711 ? 710 HOH   B O    1 
HETATM 5382 O  O    . HOH   H 5 .   ? 3.922   -23.441 -0.482  1   28.224 ? 711 HOH   B O    1 
HETATM 5383 O  O    . HOH   H 5 .   ? 7.943   -32.198 -7.573  1   25.454 ? 712 HOH   B O    1 
HETATM 5384 O  O    . HOH   H 5 .   ? 7.159   -17.098 -8.129  1   15.624 ? 713 HOH   B O    1 
HETATM 5385 O  O    . HOH   H 5 .   ? 5.341   23.282  18.05   1   34.369 ? 714 HOH   B O    1 
HETATM 5386 O  O    . HOH   H 5 .   ? 5.851   2.128   15.528  1   23.943 ? 715 HOH   B O    1 
HETATM 5387 O  O    . HOH   H 5 .   ? 11.871  -27.543 -5.583  1   40.772 ? 716 HOH   B O    1 
HETATM 5388 O  O    . HOH   H 5 .   ? 3.081   20.248  19.275  1   33.719 ? 717 HOH   B O    1 
HETATM 5389 O  O    . HOH   H 5 .   ? -11.035 3.355   7.595   1   22.231 ? 718 HOH   B O    1 
HETATM 5390 O  O    . HOH   H 5 .   ? 16.104  -10.713 -6.208  1   33.009 ? 719 HOH   B O    1 
HETATM 5391 O  O    . HOH   H 5 .   ? 7.165   -7.835  6.088   1   44.151 ? 720 HOH   B O    1 
HETATM 5392 O  O    . HOH   H 5 .   ? 22.962  22.166  2.609   1   33.52  ? 721 HOH   B O    1 
HETATM 5393 O  O    . HOH   H 5 .   ? 9.866   -23.893 -4.116  1   32.04  ? 722 HOH   B O    1 
HETATM 5394 O  O    . HOH   H 5 .   ? -17.485 -6.238  -9.009  1   37.412 ? 723 HOH   B O    1 
HETATM 5395 O  O    . HOH   H 5 .   ? -2.762  -13.073 -6.552  1   24.04  ? 724 HOH   B O    1 
HETATM 5396 O  O    . HOH   H 5 .   ? 2.951   -13.791 -32.651 1   35.285 ? 725 HOH   B O    1 
HETATM 5397 O  O    . HOH   H 5 .   ? -0.946  1.016   -15.478 1   28.577 ? 726 HOH   B O    1 
HETATM 5398 O  O    . HOH   H 5 .   ? 8.388   20.1    -5.297  1   33.133 ? 727 HOH   B O    1 
HETATM 5399 O  O    . HOH   H 5 .   ? 14.277  -13.274 -3.639  1   36.075 ? 728 HOH   B O    1 
HETATM 5400 O  O    . HOH   H 5 .   ? -11.304 -19.023 -20.929 1   41.36  ? 729 HOH   B O    1 
HETATM 5401 O  O    . HOH   H 5 .   ? -11.748 -5.061  -16.179 1   32.017 ? 730 HOH   B O    1 
HETATM 5402 O  O    . HOH   H 5 .   ? 0.467   4.528   15.429  1   29.861 ? 731 HOH   B O    1 
HETATM 5403 O  O    . HOH   H 5 .   ? -2.292  -6.97   -25.51  1   47.118 ? 732 HOH   B O    1 
HETATM 5404 O  O    . HOH   H 5 .   ? 19.622  -4.251  -9.914  1   43.358 ? 733 HOH   B O    1 
HETATM 5405 O  O    . HOH   H 5 .   ? -18.21  -8.003  -16.092 1   55.055 ? 734 HOH   B O    1 
HETATM 5406 O  O    . HOH   H 5 .   ? 7.573   19.439  -8.133  1   45.245 ? 735 HOH   B O    1 
HETATM 5407 O  O    . HOH   H 5 .   ? 4.967   -13.509 -5.554  1   31.09  ? 736 HOH   B O    1 
HETATM 5408 O  O    . HOH   H 5 .   ? -6.543  -9.538  -26.729 1   32.572 ? 737 HOH   B O    1 
HETATM 5409 O  O    . HOH   H 5 .   ? 23.405  -4.733  -3.053  1   21.28  ? 738 HOH   B O    1 
HETATM 5410 O  O    . HOH   H 5 .   ? 17.748  21.705  -0.792  1   26.16  ? 739 HOH   B O    1 
HETATM 5411 O  O    . HOH   H 5 .   ? 13.952  21.607  -2.598  1   27.951 ? 740 HOH   B O    1 
HETATM 5412 O  O    . HOH   H 5 .   ? -0.605  17.72   -12.338 1   45.558 ? 741 HOH   B O    1 
HETATM 5413 O  O    . HOH   H 5 .   ? 12.527  -4.975  5.992   1   28.133 ? 742 HOH   B O    1 
HETATM 5414 O  O    . HOH   H 5 .   ? 10.706  -5.423  7.58    1   35.859 ? 743 HOH   B O    1 
HETATM 5415 O  O    . HOH   H 5 .   ? -9.439  15.179  -5.15   1   33.704 ? 744 HOH   B O    1 
HETATM 5416 O  O    . HOH   H 5 .   ? -10.434 -11.076 -21.272 1   31.536 ? 745 HOH   B O    1 
HETATM 5417 O  O    . HOH   H 5 .   ? -9.104  -26.353 -25.579 1   29.902 ? 746 HOH   B O    1 
HETATM 5418 O  O    . HOH   H 5 .   ? 20.078  7.674   -13.05  1   46.54  ? 747 HOH   B O    1 
HETATM 5419 O  O    . HOH   H 5 .   ? 15.631  -25.909 -7.272  1   34.853 ? 748 HOH   B O    1 
HETATM 5420 O  O    . HOH   H 5 .   ? 1.771   -1.085  7.22    1   24.203 ? 749 HOH   B O    1 
HETATM 5421 O  O    . HOH   H 5 .   ? 12.36   -25.024 -4.655  1   33.354 ? 750 HOH   B O    1 
HETATM 5422 O  O    . HOH   H 5 .   ? 3.961   -31.127 -6.798  1   33.475 ? 751 HOH   B O    1 
HETATM 5423 O  O    . HOH   H 5 .   ? 4.606   -20.762 0.325   1   32.403 ? 752 HOH   B O    1 
HETATM 5424 O  O    . HOH   H 5 .   ? 8.483   -7.153  -19.095 1   36.162 ? 753 HOH   B O    1 
HETATM 5425 O  O    . HOH   H 5 .   ? -3.179  -5.065  -0.492  1   34.771 ? 754 HOH   B O    1 
HETATM 5426 O  O    . HOH   H 5 .   ? 6.877   -17.603 -1.823  1   33.986 ? 755 HOH   B O    1 
HETATM 5427 O  O    . HOH   H 5 .   ? 10.432  16.99   18.251  1   28.833 ? 756 HOH   B O    1 
HETATM 5428 O  O    . HOH   H 5 .   ? 13.118  16.983  -1.263  1   19.944 ? 757 HOH   B O    1 
HETATM 5429 O  O    . HOH   H 5 .   ? -0.996  9.708   14.863  1   36.502 ? 758 HOH   B O    1 
HETATM 5430 O  O    . HOH   H 5 .   ? 7.362   -15.026 -6.369  1   26.738 ? 759 HOH   B O    1 
HETATM 5431 O  O    . HOH   H 5 .   ? 16.99   -10.969 -3.678  1   33.788 ? 760 HOH   B O    1 
HETATM 5432 O  O    . HOH   H 5 .   ? 1.538   -15.457 -3.566  1   35.883 ? 761 HOH   B O    1 
HETATM 5433 O  O    . HOH   H 5 .   ? -1.283  -31.409 -5.469  1   45.409 ? 762 HOH   B O    1 
HETATM 5434 O  O    . HOH   H 5 .   ? -5.783  -28.115 -24.007 1   27.3   ? 763 HOH   B O    1 
HETATM 5435 O  O    . HOH   H 5 .   ? -9.383  -20.194 -22.227 1   34.47  ? 764 HOH   B O    1 
HETATM 5436 O  O    . HOH   H 5 .   ? -9.451  28.863  2.004   1   38.594 ? 765 HOH   B O    1 
HETATM 5437 O  O    . HOH   H 5 .   ? 24.914  -1.531  -0.446  1   27.97  ? 766 HOH   B O    1 
HETATM 5438 O  O    . HOH   H 5 .   ? 26.911  0.941   -3.917  1   38.869 ? 767 HOH   B O    1 
HETATM 5439 O  O    . HOH   H 5 .   ? 28.059  13.841  6.495   1   35.155 ? 768 HOH   B O    1 
HETATM 5440 O  O    . HOH   H 5 .   ? 24.921  2.608   -10.6   1   48.783 ? 769 HOH   B O    1 
HETATM 5441 O  O    . HOH   H 5 .   ? -4.978  -14.319 -5.327  1   50.267 ? 770 HOH   B O    1 
HETATM 5442 O  O    . HOH   H 5 .   ? 4.41    -4.681  -22.872 1   46.754 ? 771 HOH   B O    1 
HETATM 5443 O  O    . HOH   H 5 .   ? 12.305  -10.148 -19.297 1   30.294 ? 772 HOH   B O    1 
HETATM 5444 O  O    . HOH   H 5 .   ? 19.105  10.017  -13.935 1   34.845 ? 773 HOH   B O    1 
HETATM 5445 O  O    . HOH   H 5 .   ? 2.443   -35.749 -19.613 1   23.405 ? 774 HOH   B O    1 
HETATM 5446 O  O    . HOH   H 5 .   ? 7.702   -22.306 -27.519 1   36.693 ? 775 HOH   B O    1 
HETATM 5447 O  O    . HOH   H 5 .   ? 14.583  18.839  -2.605  1   27.72  ? 776 HOH   B O    1 
HETATM 5448 O  O    . HOH   H 5 .   ? 23.933  1.061   -8.367  1   34.482 ? 777 HOH   B O    1 
HETATM 5449 O  O    . HOH   H 5 .   ? 17.833  16.328  -5.47   1   35.262 ? 778 HOH   B O    1 
HETATM 5450 O  O    . HOH   H 5 .   ? 23.017  7.215   12.209  1   41.085 ? 779 HOH   B O    1 
HETATM 5451 O  O    . HOH   H 5 .   ? 14.426  -23.778 -5.879  1   28.617 ? 780 HOH   B O    1 
HETATM 5452 O  O    . HOH   H 5 .   ? 16.903  18.511  -3.771  1   35.809 ? 781 HOH   B O    1 
HETATM 5453 O  O    . HOH   H 5 .   ? 13.027  1.26    -14.735 1   30.872 ? 782 HOH   B O    1 
HETATM 5454 O  O    . HOH   H 5 .   ? 3.356   -33.503 -10.138 1   31.097 ? 783 HOH   B O    1 
HETATM 5455 O  O    . HOH   H 5 .   ? 13.112  -10.624 -29.1   1   32.063 ? 784 HOH   B O    1 
HETATM 5456 O  O    . HOH   H 5 .   ? 10.451  -19.52  -2.323  1   35.631 ? 785 HOH   B O    1 
HETATM 5457 O  O    . HOH   H 5 .   ? -6.702  -18.465 -3.786  1   59.121 ? 786 HOH   B O    1 
HETATM 5458 O  O    . HOH   H 5 .   ? 16.272  -19.343 -6.001  1   38.797 ? 787 HOH   B O    1 
HETATM 5459 O  O    . HOH   H 5 .   ? 26.094  -3.018  -6.768  1   41.755 ? 788 HOH   B O    1 
HETATM 5460 O  O    . HOH   H 5 .   ? 25.73   -3.479  -2.092  1   25.278 ? 789 HOH   B O    1 
HETATM 5461 O  O    . HOH   H 5 .   ? 8.867   -10.412 2.444   1   41.987 ? 790 HOH   B O    1 
HETATM 5462 O  O    . HOH   H 5 .   ? 14.855  -15.258 -19.685 1   31.74  ? 791 HOH   B O    1 
HETATM 5463 O  O    . HOH   H 5 .   ? 19.018  21.928  12.225  1   33.921 ? 792 HOH   B O    1 
HETATM 5464 O  O    . HOH   H 5 .   ? -8.532  -28.575 -27.069 1   25.869 ? 793 HOH   B O    1 
HETATM 5465 O  O    . HOH   H 5 .   ? 11.495  -11.982 0.082   1   30.694 ? 794 HOH   B O    1 
HETATM 5466 O  O    . HOH   H 5 .   ? -1.485  -7.378  0.25    1   36.209 ? 795 HOH   B O    1 
HETATM 5467 O  O    . HOH   H 5 .   ? -5.722  -29.081 -6.669  1   35.31  ? 796 HOH   B O    1 
HETATM 5468 O  O    . HOH   H 5 .   ? 27.077  -2.071  -4.321  1   38.574 ? 797 HOH   B O    1 
HETATM 5469 O  O    . HOH   H 5 .   ? 10.463  -22.302 -2.145  1   40.819 ? 798 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   ? 0.131482  0.308599 0.10685   -0.0202966  0.0239052   0.00081151  1   SER   A N    
2    C  CA   . SER   A 1   ? 0.141621  0.315123 0.0984238 -0.0190801  0.022663    -0.00482975 1   SER   A CA   
3    C  C    . SER   A 1   ? 0.133784  0.289279 0.0949108 -0.00618416 0.0119569   -0.0130343  1   SER   A C    
4    O  O    . SER   A 1   ? 0.13465   0.264041 0.0749176 -0.00271715 0.00596599  -0.0014799  1   SER   A O    
5    C  CB   . SER   A 1   ? 0.143637  0.344335 0.0982117 -0.0119262  0.0322346   -0.0128389  1   SER   A CB   
6    O  OG   . SER   A 1   ? 0.20847   0.399369 0.163756  -0.0140846  0.0368343   -0.0547896  1   SER   A OG   
7    N  N    . GLY   A 2   ? 0.139966  0.28185  0.099159  -0.00439006 0.0300714   -0.0188646  2   GLY   A N    
8    C  CA   . GLY   A 2   ? 0.138063  0.27408  0.0951558 0.00308021  0.0207793   -0.0140447  2   GLY   A CA   
9    C  C    . GLY   A 2   ? 0.137841  0.259137 0.0907788 0.00720343  0.0230543   -0.0150731  2   GLY   A C    
10   O  O    . GLY   A 2   ? 0.159232  0.25578  0.113253  -0.00450591 0.00527395  -0.0154476  2   GLY   A O    
11   N  N    . PHE   A 3   ? 0.140654  0.251275 0.0832698 0.0136832   0.0182457   -0.0115869  3   PHE   A N    
12   C  CA   . PHE   A 3   ? 0.136266  0.254287 0.0945224 0.0153233   0.0158298   -0.00658585 3   PHE   A CA   
13   C  C    . PHE   A 3   ? 0.155076  0.23686  0.105155  0.0185502   0.00571662  -0.00462802 3   PHE   A C    
14   O  O    . PHE   A 3   ? 0.151109  0.238961 0.146674  0.0230188   0.00240546  -0.0161092  3   PHE   A O    
15   C  CB   . PHE   A 3   ? 0.139674  0.269887 0.104657  0.0113349   0.0259743   -0.0050352  3   PHE   A CB   
16   C  CG   . PHE   A 3   ? 0.147628  0.286412 0.106202  0.0136063   0.0249379   -0.00238415 3   PHE   A CG   
17   C  CD1  . PHE   A 3   ? 0.154895  0.296971 0.112656  0.00990743  0.0262461   0.00816989  3   PHE   A CD1  
18   C  CD2  . PHE   A 3   ? 0.153158  0.303833 0.125726  0.0130417   0.0158308   -0.00074699 3   PHE   A CD2  
19   C  CE1  . PHE   A 3   ? 0.161516  0.30839  0.130201  0.00781216  0.0250053   0.0176585   3   PHE   A CE1  
20   C  CE2  . PHE   A 3   ? 0.160923  0.31189  0.115608  0.00635766  0.0179073   0.00789627  3   PHE   A CE2  
21   C  CZ   . PHE   A 3   ? 0.167915  0.315876 0.129665  0.00178405  0.0270308   0.018154    3   PHE   A CZ   
22   N  N    . ARG   A 4   ? 0.153129  0.226325 0.0841076 0.0144751   0.0004868   -0.00461984 4   ARG   A N    
23   C  CA   . ARG   A 4   ? 0.15775   0.231519 0.0978559 0.0104499   -0.00948453 -0.00086577 4   ARG   A CA   
24   C  C    . ARG   A 4   ? 0.152835  0.224011 0.0848904 0.0146289   0.00517612  -0.00205174 4   ARG   A C    
25   O  O    . ARG   A 4   ? 0.146499  0.232137 0.0650557 0.0105991   0.0132741   0.001777    4   ARG   A O    
26   C  CB   . ARG   A 4   ? 0.171759  0.242023 0.106488  0.00977679  -0.0133936  0.0117969   4   ARG   A CB   
27   C  CG   . ARG   A 4   ? 0.200576  0.246606 0.136697  0.00763097  -0.0415096  0.0154099   4   ARG   A CG   
28   C  CD   . ARG   A 4   ? 0.241735  0.256564 0.179515  0.00345851  -0.0587692  0.0300873   4   ARG   A CD   
29   N  NE   . ARG   A 4   ? 0.263491  0.25665  0.169069  -0.0104548  -0.0740025  0.0258506   4   ARG   A NE   
30   C  CZ   . ARG   A 4   ? 0.243394  0.248635 0.174473  -0.0188066  -0.0688861  0.0138848   4   ARG   A CZ   
31   N  NH1  . ARG   A 4   ? 0.24625   0.247624 0.183367  -0.0322556  -0.0739543  0.0240583   4   ARG   A NH1  
32   N  NH2  . ARG   A 4   ? 0.237194  0.255176 0.16251   -0.0173548  -0.0788368  0.00100254  4   ARG   A NH2  
33   N  N    . LYS   A 5   ? 0.168471  0.240821 0.114031  0.019353    -0.00170766 -0.0121466  5   LYS   A N    
34   C  CA   . LYS   A 5   ? 0.168391  0.263517 0.11643   0.0142464   0.00631342  -0.0100425  5   LYS   A CA   
35   C  C    . LYS   A 5   ? 0.164673  0.25507  0.103427  0.0110395   0.0115575   -0.00059508 5   LYS   A C    
36   O  O    . LYS   A 5   ? 0.244943  0.284886 0.143059  -0.00020297 0.0413458   0.0127556   5   LYS   A O    
37   C  CB   . LYS   A 5   ? 0.208196  0.301388 0.16916   -0.00424612 0.0128781   -0.0189426  5   LYS   A CB   
38   C  CG   . LYS   A 5   ? 0.270555  0.352009 0.20799   -0.00111564 0.0359861   -0.0346384  5   LYS   A CG   
39   C  CD   . LYS   A 5   ? 0.308401  0.406245 0.276591  -0.016147   0.0278418   -0.028195   5   LYS   A CD   
40   C  CE   . LYS   A 5   ? 0.363705  0.45098  0.318603  -0.00647336 0.0630387   -0.0289335  5   LYS   A CE   
41   N  NZ   . LYS   A 5   ? 0.371836  0.470281 0.320521  -0.00463606 0.0778634   -0.00721918 5   LYS   A NZ   
42   N  N    . MET   A 6   ? 0.149463  0.252224 0.0909077 0.0133408   0.00667647  -0.00036905 6   MET   A N    
43   C  CA   A MET   A 6   ? 0.153439  0.244987 0.100824  0.0129123   -0.0021103  -0.00503621 6   MET   A CA   
44   C  CA   B MET   A 6   ? 0.155457  0.25706  0.0954494 0.0222701   0.0004431   0.00064381  6   MET   A CA   
45   C  C    . MET   A 6   ? 0.151029  0.238739 0.0912419 0.0118      -0.00854605 0.00210828  6   MET   A C    
46   O  O    . MET   A 6   ? 0.149969  0.241335 0.100613  0.00754479  -0.0167347  0.0161371   6   MET   A O    
47   C  CB   A MET   A 6   ? 0.175593  0.250398 0.123243  0.00719913  0.00206514  -0.014042   6   MET   A CB   
48   C  CB   B MET   A 6   ? 0.167907  0.272866 0.109235  0.0276556   0.00053448  -0.00133906 6   MET   A CB   
49   C  CG   A MET   A 6   ? 0.196576  0.260061 0.138205  0.00763583  0.00944338  -0.0221122  6   MET   A CG   
50   C  CG   B MET   A 6   ? 0.182588  0.295148 0.118986  0.0444243   0.0107401   0.00069825  6   MET   A CG   
51   S  SD   A MET   A 6   ? 0.255915  0.320398 0.208129  -0.0279821  0.0125598   -0.0449093  6   MET   A SD   
52   S  SD   B MET   A 6   ? 0.205989  0.347335 0.128868  0.0528455   -0.00515761 0.00436847  6   MET   A SD   
53   C  CE   A MET   A 6   ? 0.251069  0.319607 0.193272  -0.0148196  0.00193777  -0.0448347  6   MET   A CE   
54   C  CE   B MET   A 6   ? 0.191591  0.316267 0.117151  0.049602    -0.0120948  0.0118201   6   MET   A CE   
55   N  N    . ALA   A 7   ? 0.145834  0.217276 0.0668245 0.0157682   -0.0132219  0.00302162  7   ALA   A N    
56   C  CA   . ALA   A 7   ? 0.137924  0.214957 0.0685677 0.0116129   -0.0197374  -0.00047339 7   ALA   A CA   
57   C  C    . ALA   A 7   ? 0.1261    0.210453 0.0730187 0.00978999  -0.0242967  -0.00272531 7   ALA   A C    
58   O  O    . ALA   A 7   ? 0.133272  0.221984 0.0601949 0.0164049   -0.0286498  -0.00454081 7   ALA   A O    
59   C  CB   . ALA   A 7   ? 0.136408  0.21754  0.0776478 0.0108531   -0.0206424  -0.00507171 7   ALA   A CB   
60   N  N    . PHE   A 8   ? 0.117438  0.208156 0.0739432 0.0132913   -0.0237898  -0.00581317 8   PHE   A N    
61   C  CA   . PHE   A 8   ? 0.121311  0.209461 0.0842142 0.00948082  -0.0193238  -0.00557365 8   PHE   A CA   
62   C  C    . PHE   A 8   ? 0.125517  0.219367 0.0803539 0.00922109  -0.0140457  -0.0129822  8   PHE   A C    
63   O  O    . PHE   A 8   ? 0.133524  0.229382 0.0790778 0.00600885  -0.00010163 -0.0121061  8   PHE   A O    
64   C  CB   . PHE   A 8   ? 0.12758   0.208957 0.0897788 0.0115798   -0.0211259  -0.00433573 8   PHE   A CB   
65   C  CG   . PHE   A 8   ? 0.136764  0.209456 0.102375  0.00773458  -0.0223056  0.0025546   8   PHE   A CG   
66   C  CD1  . PHE   A 8   ? 0.157625  0.212453 0.11345   0.00358856  -0.0172163  0.00381476  8   PHE   A CD1  
67   C  CD2  . PHE   A 8   ? 0.146652  0.216705 0.108528  0.0150163   -0.0166055  0.0080918   8   PHE   A CD2  
68   C  CE1  . PHE   A 8   ? 0.158927  0.210798 0.126155  0.00038852  -0.0182789  0.00590794  8   PHE   A CE1  
69   C  CE2  . PHE   A 8   ? 0.143673  0.20813  0.118626  0.016683    -0.00860316 0.00981327  8   PHE   A CE2  
70   C  CZ   . PHE   A 8   ? 0.154407  0.220854 0.120809  0.00635913  -0.00991521 0.0100601   8   PHE   A CZ   
71   N  N    . PRO   A 9   ? 0.131526  0.24466  0.0738973 0.00246895  -0.0124688  -0.0134993  9   PRO   A N    
72   C  CA   . PRO   A 9   ? 0.125988  0.244001 0.0738697 0.00761224  -0.0122489  -0.011544   9   PRO   A CA   
73   C  C    . PRO   A 9   ? 0.128548  0.230589 0.0711438 0.0119187   -0.014664   -6.951e-05  9   PRO   A C    
74   O  O    . PRO   A 9   ? 0.145814  0.236821 0.0789687 0.011546    -0.00971149 0.0170082   9   PRO   A O    
75   C  CB   . PRO   A 9   ? 0.135348  0.255659 0.0880824 0.00627617  -0.0126752  -0.0210759  9   PRO   A CB   
76   C  CG   . PRO   A 9   ? 0.146326  0.260026 0.0848261 -0.00287995 -0.016527   -0.0236505  9   PRO   A CG   
77   C  CD   . PRO   A 9   ? 0.135764  0.25515  0.0817413 -0.00362852 -0.016298   -0.0187921  9   PRO   A CD   
78   N  N    . SER   A 10  ? 0.124549  0.221645 0.0649588 0.0147168   -0.0204448  0.00195887  10  SER   A N    
79   C  CA   . SER   A 10  ? 0.122141  0.217948 0.0699435 0.018281    -0.0185477  0.00184939  10  SER   A CA   
80   C  C    . SER   A 10  ? 0.117484  0.214172 0.0722271 0.0158456   -0.0132197  0.00105889  10  SER   A C    
81   O  O    . SER   A 10  ? 0.113384  0.223    0.0735301 0.021749    -0.0100671  -0.00433741 10  SER   A O    
82   C  CB   . SER   A 10  ? 0.131943  0.218303 0.0850791 0.0230418   -0.0190194  0.00190108  10  SER   A CB   
83   O  OG   . SER   A 10  ? 0.161755  0.214412 0.0982236 0.0238171   -0.0369462  0.00642837  10  SER   A OG   
84   N  N    . GLY   A 11  ? 0.114719  0.219539 0.0797183 0.0171183   -0.00510981 -0.00520514 11  GLY   A N    
85   C  CA   . GLY   A 11  ? 0.121939  0.21552  0.0801471 0.0160339   -0.0002012  -0.00323091 11  GLY   A CA   
86   C  C    . GLY   A 11  ? 0.13761   0.211648 0.0810743 0.0174573   -0.00401109 -0.00585766 11  GLY   A C    
87   O  O    . GLY   A 11  ? 0.148002  0.220738 0.0865489 0.0183144   -0.00216346 -0.00614545 11  GLY   A O    
88   N  N    . LYS   A 12  ? 0.128234  0.199915 0.0857899 0.0183712   -0.0127507  -0.00134748 12  LYS   A N    
89   C  CA   . LYS   A 12  ? 0.130514  0.213044 0.101388  0.0227161   -0.0160145  -0.00633956 12  LYS   A CA   
90   C  C    . LYS   A 12  ? 0.120988  0.211168 0.0933407 0.0264134   -0.0152109  -0.00437592 12  LYS   A C    
91   O  O    . LYS   A 12  ? 0.121525  0.249674 0.0950847 0.0345539   -0.0217476  -0.0271601  12  LYS   A O    
92   C  CB   . LYS   A 12  ? 0.14518   0.222544 0.109805  0.0164202   -0.0253296  0.00255558  12  LYS   A CB   
93   C  CG   . LYS   A 12  ? 0.169783  0.23731  0.145176  0.00647521  -0.0416357  -0.0021952  12  LYS   A CG   
94   C  CD   . LYS   A 12  ? 0.203859  0.267173 0.18875   -0.00074072 -0.0393531  0.00432191  12  LYS   A CD   
95   C  CE   . LYS   A 12  ? 0.244176  0.291546 0.241183  -0.0081205  -0.0444303  -0.00749704 12  LYS   A CE   
96   N  NZ   . LYS   A 12  ? 0.2788    0.333974 0.26608   -0.00437228 -0.0551804  -0.0129471  12  LYS   A NZ   
97   N  N    . VAL   A 13  ? 0.11074   0.200331 0.0790137 0.0139683   -0.0144947  -0.00296806 13  VAL   A N    
98   C  CA   . VAL   A 13  ? 0.117472  0.201549 0.074004  0.0126968   -0.0154195  -0.00460877 13  VAL   A CA   
99   C  C    . VAL   A 13  ? 0.115663  0.201552 0.0738767 0.0148969   -0.0147716  -0.00432132 13  VAL   A C    
100  O  O    . VAL   A 13  ? 0.114023  0.199041 0.0763403 0.0146106   -0.00987354 -0.00316654 13  VAL   A O    
101  C  CB   . VAL   A 13  ? 0.123901  0.210822 0.0821995 0.0102269   -0.00711437 -0.00910445 13  VAL   A CB   
102  C  CG1  . VAL   A 13  ? 0.135226  0.215086 0.0706332 0.00703188  0.00322116  -0.0163037  13  VAL   A CG1  
103  C  CG2  . VAL   A 13  ? 0.135984  0.218808 0.0941338 0.00603241  -0.00861884 -0.00871573 13  VAL   A CG2  
104  N  N    . GLU   A 14  ? 0.121973  0.20403  0.0744128 0.0173077   -0.0114962  0.00119273  14  GLU   A N    
105  C  CA   . GLU   A 14  ? 0.125629  0.208311 0.0815558 0.0138851   -0.0142494  0.0017809   14  GLU   A CA   
106  C  C    . GLU   A 14  ? 0.133027  0.214149 0.0888638 0.0165078   -0.0120735  -0.00026967 14  GLU   A C    
107  O  O    . GLU   A 14  ? 0.145498  0.229112 0.112668  0.00706423  0.00465791  0.00424134  14  GLU   A O    
108  C  CB   . GLU   A 14  ? 0.135277  0.21413  0.082117  0.0180093   -0.0129684  0.00682863  14  GLU   A CB   
109  C  CG   . GLU   A 14  ? 0.13918   0.221796 0.094925  0.0188172   -0.0162742  0.00886234  14  GLU   A CG   
110  C  CD   . GLU   A 14  ? 0.159802  0.23716  0.0998837 0.0217964   -0.0228883  0.0110324   14  GLU   A CD   
111  O  OE1  . GLU   A 14  ? 0.153536  0.23605  0.0884703 0.0266981   -0.0281812  0.00991196  14  GLU   A OE1  
112  O  OE2  . GLU   A 14  ? 0.202442  0.288836 0.114952  0.026771    -0.00581491 0.0133963   14  GLU   A OE2  
113  N  N    . GLY   A 15  ? 0.126347  0.220384 0.0910311 0.0267257   -0.0208889  -0.00822096 15  GLY   A N    
114  C  CA   . GLY   A 15  ? 0.132845  0.234613 0.107764  0.0294586   -0.0218001  -0.0148047  15  GLY   A CA   
115  C  C    . GLY   A 15  ? 0.137217  0.240115 0.0976    0.0346318   -0.0169978  -0.0186744  15  GLY   A C    
116  O  O    . GLY   A 15  ? 0.14719   0.265839 0.10746   0.0520955   -0.0110391  -0.0200492  15  GLY   A O    
117  N  N    . CYS   A 16  ? 0.12888   0.224143 0.0960004 0.0246556   -0.017228   -0.0199704  16  CYS   A N    
118  C  CA   . CYS   A 16  ? 0.122998  0.221001 0.0973922 0.0196748   -0.0164193  -0.0117359  16  CYS   A CA   
119  C  C    . CYS   A 16  ? 0.110599  0.215599 0.0746814 0.0161097   -0.0069004  -0.00876035 16  CYS   A C    
120  O  O    . CYS   A 16  ? 0.133637  0.23233  0.081932  0.00958883  -0.0279326  -0.0103224  16  CYS   A O    
121  C  CB   . CYS   A 16  ? 0.138832  0.219258 0.121657  0.0149257   -0.0263261  0.00066001  16  CYS   A CB   
122  S  SG   . CYS   A 16  ? 0.176325  0.23157  0.181321  0.00432908  -0.0628711  0.0029179   16  CYS   A SG   
123  N  N    . MET   A 17  ? 0.107468  0.209737 0.0646497 0.0109735   -0.00207164 -0.00522559 17  MET   A N    
124  C  CA   . MET   A 17  ? 0.120256  0.209506 0.0748748 0.00410911  -0.00063679 -0.00201657 17  MET   A CA   
125  C  C    . MET   A 17  ? 0.128126  0.214482 0.0757082 -0.00273748 0.0027925   -4.263e-05  17  MET   A C    
126  O  O    . MET   A 17  ? 0.145354  0.241963 0.0743015 -0.012359   0.00116569  0.00661794  17  MET   A O    
127  C  CB   . MET   A 17  ? 0.131997  0.217437 0.0870826 0.00869407  -0.00366314 -0.0107687  17  MET   A CB   
128  C  CG   . MET   A 17  ? 0.136128  0.225709 0.104057  0.00774673  0.00379457  -0.0145121  17  MET   A CG   
129  S  SD   . MET   A 17  ? 0.141987  0.243096 0.117162  0.0156022   0.0157339   -0.0156524  17  MET   A SD   
130  C  CE   . MET   A 17  ? 0.155339  0.227225 0.109523  0.0169345   0.0184352   -0.0171052  17  MET   A CE   
131  N  N    . VAL   A 18  ? 0.126158  0.200118 0.0722901 -0.00305598 0.00328713  -0.00162201 18  VAL   A N    
132  C  CA   . VAL   A 18  ? 0.134025  0.203909 0.0834392 -0.0023841  0.00595571  0.00072789  18  VAL   A CA   
133  C  C    . VAL   A 18  ? 0.124119  0.207111 0.0921054 -0.00199524 0.00461088  -0.00126747 18  VAL   A C    
134  O  O    . VAL   A 18  ? 0.118697  0.219818 0.08466   -0.00441743 0.00351444  0.00230015  18  VAL   A O    
135  C  CB   . VAL   A 18  ? 0.135016  0.202917 0.0900972 0.00185704  0.008967    -0.00090848 18  VAL   A CB   
136  C  CG1  . VAL   A 18  ? 0.144253  0.199912 0.0974621 0.0061534   0.00467391  0.00102551  18  VAL   A CG1  
137  C  CG2  . VAL   A 18  ? 0.145412  0.20922  0.0941254 0.00507865  0.00218817  0.00296433  18  VAL   A CG2  
138  N  N    . GLN   A 19  ? 0.129221  0.218825 0.114771  -0.00451674 0.00891849  0.00040385  19  GLN   A N    
139  C  CA   . GLN   A 19  ? 0.140492  0.231543 0.134474  -0.00655722 0.00342036  -0.00066111 19  GLN   A CA   
140  C  C    . GLN   A 19  ? 0.13835   0.230711 0.120103  0.00071968  0.0045004   -0.0113298  19  GLN   A C    
141  O  O    . GLN   A 19  ? 0.132052  0.24359  0.109051  0.00932675  -0.00844753 -0.0157532  19  GLN   A O    
142  C  CB   . GLN   A 19  ? 0.174857  0.251018 0.184856  -0.00925288 0.0007826   0.0187596   19  GLN   A CB   
143  C  CG   . GLN   A 19  ? 0.208498  0.274271 0.238761  -0.0143154  0.0012107   0.018789    19  GLN   A CG   
144  C  CD   . GLN   A 19  ? 0.229688  0.316713 0.281715  -0.017981   0.0153059   0.0438071   19  GLN   A CD   
145  O  OE1  . GLN   A 19  ? 0.244498  0.361954 0.348364  0.00438987  -0.00276443 0.0489938   19  GLN   A OE1  
146  N  NE2  . GLN   A 19  ? 0.226367  0.351726 0.311234  -0.0173188  0.0240791   0.0486834   19  GLN   A NE2  
147  N  N    . VAL   A 20  ? 0.119533  0.215986 0.106208  -0.00511768 0.0183132   -0.0097769  20  VAL   A N    
148  C  CA   . VAL   A 20  ? 0.130247  0.214328 0.116273  -0.00089457 0.0204105   -0.0110947  20  VAL   A CA   
149  C  C    . VAL   A 20  ? 0.123221  0.215822 0.125705  -0.00223619 0.0185299   -0.0105187  20  VAL   A C    
150  O  O    . VAL   A 20  ? 0.128018  0.208157 0.1559    0.00191085  0.0149343   -0.00992942 20  VAL   A O    
151  C  CB   . VAL   A 20  ? 0.149665  0.21463  0.1205    0.00087934  0.0232914   -0.00933936 20  VAL   A CB   
152  C  CG1  . VAL   A 20  ? 0.160973  0.221364 0.121079  0.00110292  0.017749    -0.0116508  20  VAL   A CG1  
153  C  CG2  . VAL   A 20  ? 0.158188  0.216249 0.120929  0.0024223   0.0172239   -0.0118997  20  VAL   A CG2  
154  N  N    . THR   A 21  ? 0.124971  0.240695 0.13922   -0.00403623 0.0217599   -0.0127565  21  THR   A N    
155  C  CA   . THR   A 21  ? 0.140255  0.259191 0.155293  -0.0160997  0.0121773   -0.0135357  21  THR   A CA   
156  C  C    . THR   A 21  ? 0.139122  0.274458 0.150063  -0.00587852 0.0155256   -0.0213544  21  THR   A C    
157  O  O    . THR   A 21  ? 0.143658  0.296642 0.150576  0.0100336   -0.00150097 -0.0379856  21  THR   A O    
158  C  CB   . THR   A 21  ? 0.158308  0.28007  0.175322  -0.0349132  0.00988802  -0.00147184 21  THR   A CB   
159  O  OG1  . THR   A 21  ? 0.184462  0.308134 0.199469  -0.0351161  -0.0042211  0.0174481   21  THR   A OG1  
160  C  CG2  . THR   A 21  ? 0.165101  0.290159 0.194449  -0.036514   0.00841605  -0.00584084 21  THR   A CG2  
161  N  N    . CYS   A 22  ? 0.128959  0.286303 0.146025  -0.0116998  0.0183912   -0.0262629  22  CYS   A N    
162  C  CA   . CYS   A 22  ? 0.148342  0.305685 0.150173  -0.0172381  0.01515     -0.0184765  22  CYS   A CA   
163  C  C    . CYS   A 22  ? 0.159234  0.30852  0.181358  -0.0200504  0.00347397  -0.0199808  22  CYS   A C    
164  O  O    . CYS   A 22  ? 0.173816  0.306382 0.176048  -0.0107269  0.00080247  -0.0189862  22  CYS   A O    
165  C  CB   . CYS   A 22  ? 0.163374  0.326731 0.140419  -0.0137206  0.0159904   -0.0139082  22  CYS   A CB   
166  S  SG   . CYS   A 22  ? 0.220855  0.369533 0.158637  -0.0161465  -0.0185284  -0.00831686 22  CYS   A SG   
167  N  N    . GLY   A 23  ? 0.169229  0.318848 0.236733  -0.0321786  0.015215    -0.0246962  23  GLY   A N    
168  C  CA   . GLY   A 23  ? 0.194246  0.328411 0.268631  -0.0457819  0.0159486   -0.028213   23  GLY   A CA   
169  C  C    . GLY   A 23  ? 0.198488  0.325858 0.264023  -0.0570039  0.00953938  -0.0284544  23  GLY   A C    
170  O  O    . GLY   A 23  ? 0.233197  0.34469  0.239475  -0.0509149  0.0230797   -0.0170166  23  GLY   A O    
171  N  N    . THR   A 24  ? 0.207164  0.30729  0.280016  -0.0747413  0.00302009  -0.0464327  24  THR   A N    
172  C  CA   . THR   A 24  ? 0.230246  0.323384 0.314212  -0.071979   0.0146388   -0.0347315  24  THR   A CA   
173  C  C    . THR   A 24  ? 0.218803  0.291493 0.303498  -0.0593899  0.0326982   -0.0342703  24  THR   A C    
174  O  O    . THR   A 24  ? 0.249568  0.293034 0.345469  -0.0662815  0.0223692   -0.0023784  24  THR   A O    
175  C  CB   . THR   A 24  ? 0.262627  0.338196 0.326947  -0.0692405  0.00937602  -0.0415272  24  THR   A CB   
176  O  OG1  . THR   A 24  ? 0.32832   0.380853 0.345728  -0.0624637  0.0282343   -0.0563877  24  THR   A OG1  
177  C  CG2  . THR   A 24  ? 0.287644  0.355185 0.344391  -0.0774888  0.0172915   -0.0376052  24  THR   A CG2  
178  N  N    . THR   A 25  ? 0.192876  0.282524 0.269348  -0.0609659  0.0477422   -0.0470559  25  THR   A N    
179  C  CA   . THR   A 25  ? 0.200847  0.260517 0.290713  -0.0590167  0.0555661   -0.0459933  25  THR   A CA   
180  C  C    . THR   A 25  ? 0.169071  0.258292 0.258545  -0.0388349  0.0483471   -0.0389791  25  THR   A C    
181  O  O    . THR   A 25  ? 0.152144  0.272878 0.265166  -0.0199014  0.03091     -0.0315594  25  THR   A O    
182  C  CB   . THR   A 25  ? 0.243993  0.269071 0.307982  -0.064974   0.0758386   -0.0404832  25  THR   A CB   
183  O  OG1  . THR   A 25  ? 0.316385  0.261485 0.333755  -0.0747071  0.100353    -0.0439724  25  THR   A OG1  
184  C  CG2  . THR   A 25  ? 0.253787  0.285608 0.332246  -0.0549828  0.0952912   -0.0469266  25  THR   A CG2  
185  N  N    . THR   A 26  ? 0.179575  0.255927 0.277544  -0.0212202  0.0386053   -0.0301247  26  THR   A N    
186  C  CA   . THR   A 26  ? 0.169834  0.25156  0.259375  -0.0179682  0.0432754   -0.0260912  26  THR   A CA   
187  C  C    . THR   A 26  ? 0.159718  0.221222 0.207826  -0.0103233  0.0256665   -0.0232848  26  THR   A C    
188  O  O    . THR   A 26  ? 0.160226  0.237238 0.26429   -0.00897373 0.0165576   -0.0467792  26  THR   A O    
189  C  CB   . THR   A 26  ? 0.197387  0.297467 0.27423   -0.0219681  0.0718226   -0.0123311  26  THR   A CB   
190  O  OG1  . THR   A 26  ? 0.207707  0.334001 0.336041  -0.0345156  0.0908369   0.00286147  26  THR   A OG1  
191  C  CG2  . THR   A 26  ? 0.191575  0.307387 0.263677  -0.022992   0.079941    -0.0126258  26  THR   A CG2  
192  N  N    . LEU   A 27  ? 0.1243    0.214674 0.156569  -0.00477663 0.0127832   -0.023032   27  LEU   A N    
193  C  CA   . LEU   A 27  ? 0.122885  0.213759 0.126631  -0.00379622 0.0135024   -0.0187426  27  LEU   A CA   
194  C  C    . LEU   A 27  ? 0.115822  0.204585 0.112392  -0.00095349 0.0122473   -0.0131568  27  LEU   A C    
195  O  O    . LEU   A 27  ? 0.117955  0.224041 0.115655  -0.00113306 0.0216095   -0.0124035  27  LEU   A O    
196  C  CB   . LEU   A 27  ? 0.120658  0.218351 0.123575  -0.00379111 0.00832819  -0.0233895  27  LEU   A CB   
197  C  CG   . LEU   A 27  ? 0.115959  0.218435 0.11582   -0.00481555 0.00763912  -0.023963   27  LEU   A CG   
198  C  CD1  . LEU   A 27  ? 0.124158  0.222723 0.122474  -0.00212077 0.00190152  -0.0270408  27  LEU   A CD1  
199  C  CD2  . LEU   A 27  ? 0.124703  0.228302 0.112281  -0.00399832 -0.00156935 -0.027338   27  LEU   A CD2  
200  N  N    . ASN   A 28  ? 0.115994  0.198956 0.087345  0.0024217   0.0141335   -0.00872139 28  ASN   A N    
201  C  CA   . ASN   A 28  ? 0.11268   0.19421  0.0789532 0.00245795  0.0152067   -0.00911154 28  ASN   A CA   
202  C  C    . ASN   A 28  ? 0.117031  0.1938   0.0804964 0.0064729   0.00640754  -0.0108534  28  ASN   A C    
203  O  O    . ASN   A 28  ? 0.129903  0.201031 0.0784711 0.00045005  0.00773668  -0.0041563  28  ASN   A O    
204  C  CB   . ASN   A 28  ? 0.114208  0.202411 0.074204  0.00524744  0.00925764  -0.00469327 28  ASN   A CB   
205  C  CG   . ASN   A 28  ? 0.126361  0.213374 0.0745764 0.00720491  0.0102746   0.00141885  28  ASN   A CG   
206  O  OD1  . ASN   A 28  ? 0.158263  0.244051 0.0692331 0.0131721   0.0141539   0.00375403  28  ASN   A OD1  
207  N  ND2  . ASN   A 28  ? 0.141063  0.21883  0.0860647 0.01309     0.00703744  0.00094369  28  ASN   A ND2  
208  N  N    . GLY   A 29  ? 0.123146  0.187818 0.07984   0.00542323  -0.00170593 -0.0092912  29  GLY   A N    
209  C  CA   . GLY   A 29  ? 0.123943  0.190443 0.0845956 0.00813347  0.00271644  -0.015378   29  GLY   A CA   
210  C  C    . GLY   A 29  ? 0.114263  0.19185  0.0806096 0.00998358  0.00243666  -0.0118502  29  GLY   A C    
211  O  O    . GLY   A 29  ? 0.113407  0.205101 0.0703008 0.0104136   0.00594006  -0.00514394 29  GLY   A O    
212  N  N    . LEU   A 30  ? 0.120461  0.189087 0.0814504 0.00721751  -0.00160529 -0.0100691  30  LEU   A N    
213  C  CA   . LEU   A 30  ? 0.110897  0.192991 0.081064  0.00350543  0.00101529  -0.00422187 30  LEU   A CA   
214  C  C    . LEU   A 30  ? 0.111842  0.195637 0.0843572 0.00579646  -0.00361885 -0.00663464 30  LEU   A C    
215  O  O    . LEU   A 30  ? 0.115792  0.199752 0.0893618 0.0101529   -0.00730078 -0.00475996 30  LEU   A O    
216  C  CB   . LEU   A 30  ? 0.106018  0.197456 0.0873448 0.00605321  0.00359461  -0.00789466 30  LEU   A CB   
217  C  CG   . LEU   A 30  ? 0.110326  0.200499 0.103942  0.00238058  0.00860478  -0.00696215 30  LEU   A CG   
218  C  CD1  . LEU   A 30  ? 0.110458  0.204447 0.10632   -0.00116289 0.00736976  -0.00846998 30  LEU   A CD1  
219  C  CD2  . LEU   A 30  ? 0.105081  0.211262 0.110818  0.00122958  0.0105241   -0.0047176  30  LEU   A CD2  
220  N  N    . TRP   A 31  ? 0.0999037 0.199128 0.0789796 0.0128411   -0.00704481 -0.0079965  31  TRP   A N    
221  C  CA   . TRP   A 31  ? 0.107252  0.199904 0.0924328 0.0136267   -0.00659994 -0.0122393  31  TRP   A CA   
222  C  C    . TRP   A 31  ? 0.109122  0.200799 0.0940121 0.0125064   -0.003469   -0.0142522  31  TRP   A C    
223  O  O    . TRP   A 31  ? 0.119677  0.206929 0.0884722 0.00751496  -0.0114137  -0.0148398  31  TRP   A O    
224  C  CB   . TRP   A 31  ? 0.109294  0.202333 0.0940283 0.0152538   0.00107737  -0.0193349  31  TRP   A CB   
225  C  CG   . TRP   A 31  ? 0.119893  0.207325 0.0997777 0.016962    0.0110009   -0.021255   31  TRP   A CG   
226  C  CD1  . TRP   A 31  ? 0.122082  0.216657 0.104097  0.0183834   0.014793    -0.0210654  31  TRP   A CD1  
227  C  CD2  . TRP   A 31  ? 0.138162  0.220978 0.105394  0.0090057   0.0179769   -0.023069   31  TRP   A CD2  
228  N  NE1  . TRP   A 31  ? 0.129917  0.225845 0.115874  0.0246843   0.0167501   -0.0256453  31  TRP   A NE1  
229  C  CE2  . TRP   A 31  ? 0.152745  0.226251 0.115774  0.014192    0.0190323   -0.0223787  31  TRP   A CE2  
230  C  CE3  . TRP   A 31  ? 0.158028  0.223561 0.103637  0.0129372   0.0242584   -0.020542   31  TRP   A CE3  
231  C  CZ2  . TRP   A 31  ? 0.158095  0.234366 0.126643  0.0136839   0.0279234   -0.0305589  31  TRP   A CZ2  
232  C  CZ3  . TRP   A 31  ? 0.179762  0.232363 0.107965  0.010786    0.0247884   -0.0275755  31  TRP   A CZ3  
233  C  CH2  . TRP   A 31  ? 0.179092  0.236294 0.113763  0.00858688  0.031389    -0.0311228  31  TRP   A CH2  
234  N  N    . LEU   A 32  ? 0.119927  0.197747 0.0882676 0.0140674   -0.00729985 -0.0155001  32  LEU   A N    
235  C  CA   . LEU   A 32  ? 0.12014   0.206237 0.096769  0.00976714  -0.00178703 -0.0131563  32  LEU   A CA   
236  C  C    . LEU   A 32  ? 0.127855  0.213109 0.12807   0.0143002   -0.00637052 -0.0173038  32  LEU   A C    
237  O  O    . LEU   A 32  ? 0.126941  0.226487 0.137208  0.0212618   -0.0153143  -0.0202644  32  LEU   A O    
238  C  CB   . LEU   A 32  ? 0.126098  0.20936  0.0978487 0.0086278   0.00181619  -0.00698259 32  LEU   A CB   
239  C  CG   . LEU   A 32  ? 0.134118  0.222842 0.118105  0.0116322   0.0126133   -0.00893609 32  LEU   A CG   
240  C  CD1  . LEU   A 32  ? 0.143053  0.233704 0.119351  0.00892704  0.00873608  -0.0134599  32  LEU   A CD1  
241  C  CD2  . LEU   A 32  ? 0.141473  0.238525 0.124969  0.0145103   0.0158831   -0.00813537 32  LEU   A CD2  
242  N  N    . ASP   A 33  ? 0.133313  0.2226   0.143941  0.00860435  -0.00712745 -0.0218761  33  ASP   A N    
243  C  CA   . ASP   A 33  ? 0.142192  0.23243  0.176798  0.0132764   -5.278e-05  -0.0294384  33  ASP   A CA   
244  C  C    . ASP   A 33  ? 0.131754  0.222205 0.163832  0.0236147   0.00083597  -0.0240612  33  ASP   A C    
245  O  O    . ASP   A 33  ? 0.125644  0.240193 0.139859  0.0204363   0.00355675  -0.0130058  33  ASP   A O    
246  C  CB   . ASP   A 33  ? 0.164693  0.24404  0.220017  0.00961168  0.0029712   -0.0250028  33  ASP   A CB   
247  C  CG   . ASP   A 33  ? 0.191319  0.269349 0.282828  -0.00356044 0.00742133  -0.0304942  33  ASP   A CG   
248  O  OD1  . ASP   A 33  ? 0.249427  0.312377 0.348932  -0.0127364  -0.0117216  -0.0437591  33  ASP   A OD1  
249  O  OD2  . ASP   A 33  ? 0.230569  0.333117 0.345783  0.00356289  0.0189877   -0.0202569  33  ASP   A OD2  
250  N  N    . ASP   A 34  ? 0.130684  0.240032 0.175622  0.0250193   0.00130766  -0.0197766  34  ASP   A N    
251  C  CA   . ASP   A 34  ? 0.128628  0.244658 0.177566  0.0256303   -0.0086878  -0.0216391  34  ASP   A CA   
252  C  C    . ASP   A 34  ? 0.129222  0.240416 0.152728  0.0230911   -0.00756129 -0.0111765  34  ASP   A C    
253  O  O    . ASP   A 34  ? 0.137114  0.256892 0.153866  0.00905072  -0.00652411 -0.0190718  34  ASP   A O    
254  C  CB   . ASP   A 34  ? 0.146373  0.275667 0.222436  0.0431354   -0.00782904 -0.0264752  34  ASP   A CB   
255  C  CG   . ASP   A 34  ? 0.177943  0.2977   0.268981  0.0550139   -0.00954611 -0.0124639  34  ASP   A CG   
256  O  OD1  . ASP   A 34  ? 0.190414  0.306462 0.244786  0.0682641   -0.0231407  0.00994658  34  ASP   A OD1  
257  O  OD2  . ASP   A 34  ? 0.214834  0.350636 0.358331  0.087293    -0.00578169 -0.00967781 34  ASP   A OD2  
258  N  N    . VAL   A 35  ? 0.12032   0.230667 0.135678  0.0206448   -0.0197199  -0.0154193  35  VAL   A N    
259  C  CA   . VAL   A 35  ? 0.129829  0.23175  0.110077  0.0121985   -0.00827134 -0.00872394 35  VAL   A CA   
260  C  C    . VAL   A 35  ? 0.11735   0.223323 0.0862747 0.0047372   -0.00138793 -0.0137651  35  VAL   A C    
261  O  O    . VAL   A 35  ? 0.124353  0.223553 0.103801  0.00132864  -0.0150271  -0.0177974  35  VAL   A O    
262  C  CB   . VAL   A 35  ? 0.160188  0.234707 0.125376  0.0109228   -0.00877185 0.00057877  35  VAL   A CB   
263  C  CG1  . VAL   A 35  ? 0.178519  0.246142 0.11868   0.00791314  -0.0173147  0.00286411  35  VAL   A CG1  
264  C  CG2  . VAL   A 35  ? 0.193083  0.243721 0.141913  0.0152002   0.00134496  0.00582764  35  VAL   A CG2  
265  N  N    . VAL   A 36  ? 0.106869  0.222106 0.081312  0.00271296  -0.00297962 -0.0149986  36  VAL   A N    
266  C  CA   . VAL   A 36  ? 0.111817  0.222881 0.0817207 0.00120193  -0.00953176 -0.0160252  36  VAL   A CA   
267  C  C    . VAL   A 36  ? 0.10633   0.227016 0.0806195 0.0008717   -0.012246   -0.0182365  36  VAL   A C    
268  O  O    . VAL   A 36  ? 0.0941195 0.246113 0.0925198 0.00786324  -0.0093522  -0.0272389  36  VAL   A O    
269  C  CB   . VAL   A 36  ? 0.125452  0.225656 0.0905917 0.00054236  -0.00433074 -0.0136926  36  VAL   A CB   
270  C  CG1  . VAL   A 36  ? 0.132928  0.220444 0.0966936 -0.00246845 -0.00352185 -0.00881678 36  VAL   A CG1  
271  C  CG2  . VAL   A 36  ? 0.131126  0.231568 0.0871785 0.00533995  -0.00341429 -0.0100363  36  VAL   A CG2  
272  N  N    . TYR   A 37  ? 0.105988  0.222355 0.072655  0.00201431  -0.00905066 -0.0171178  37  TYR   A N    
273  C  CA   . TYR   A 37  ? 0.112785  0.216915 0.0702195 0.00141853  -0.00807282 -0.0108532  37  TYR   A CA   
274  C  C    . TYR   A 37  ? 0.1091    0.214091 0.0714415 -0.00066299 -0.00632376 -0.0112232  37  TYR   A C    
275  O  O    . TYR   A 37  ? 0.121041  0.21645  0.0673982 0.0069476   -0.0067366  -0.0152476  37  TYR   A O    
276  C  CB   . TYR   A 37  ? 0.110864  0.220725 0.0794162 0.00224707  -0.00906425 -0.00254293 37  TYR   A CB   
277  C  CG   . TYR   A 37  ? 0.117264  0.218357 0.0974156 0.00058658  -0.0135894  0.00264091  37  TYR   A CG   
278  C  CD1  . TYR   A 37  ? 0.124906  0.211818 0.116572  -0.00377857 -0.0129253  -0.00476787 37  TYR   A CD1  
279  C  CD2  . TYR   A 37  ? 0.134478  0.224666 0.104033  -0.00281516 -0.0193617  0.00525367  37  TYR   A CD2  
280  C  CE1  . TYR   A 37  ? 0.131275  0.216212 0.128396  -0.00403722 -0.0136017  -0.00323563 37  TYR   A CE1  
281  C  CE2  . TYR   A 37  ? 0.138403  0.223652 0.111285  -0.00575237 -0.0177887  0.0103095   37  TYR   A CE2  
282  C  CZ   . TYR   A 37  ? 0.141048  0.216853 0.137477  -0.00675435 -0.021557   -0.00053634 37  TYR   A CZ   
283  O  OH   . TYR   A 37  ? 0.179207  0.225382 0.190472  -0.01098    -0.031198   0.00644557  37  TYR   A OH   
284  N  N    . CYS   A 38  ? 0.122007  0.218967 0.0615357 -0.00301475 -0.00784287 -0.00775389 38  CYS   A N    
285  C  CA   . CYS   A 38  ? 0.119091  0.224163 0.0652937 -0.00134985 -0.0108944  -0.00812644 38  CYS   A CA   
286  C  C    . CYS   A 38  ? 0.115809  0.219828 0.0685974 0.0049135   -0.00917406 -0.0106015  38  CYS   A C    
287  O  O    . CYS   A 38  ? 0.13608   0.231669 0.0569062 0.0131545   -0.00432169 -0.0110241  38  CYS   A O    
288  C  CB   . CYS   A 38  ? 0.136193  0.233948 0.0674134 -0.0111406  -0.00833739 -0.00896475 38  CYS   A CB   
289  S  SG   . CYS   A 38  ? 0.141442  0.274758 0.0860064 -0.0259546  0.00201345  -0.0101973  38  CYS   A SG   
290  N  N    . PRO   A 39  ? 0.115364  0.213938 0.064195  0.00286567  -0.0131935  -0.0102386  39  PRO   A N    
291  C  CA   . PRO   A 39  ? 0.114602  0.218074 0.0614854 0.00241212  -0.0109108  -0.00977782 39  PRO   A CA   
292  C  C    . PRO   A 39  ? 0.114221  0.220302 0.0657808 -0.00483222 -0.0124401  -0.00787137 39  PRO   A C    
293  O  O    . PRO   A 39  ? 0.107333  0.229657 0.0724966 -0.00706603 -0.00680149 -0.00950258 39  PRO   A O    
294  C  CB   . PRO   A 39  ? 0.110454  0.214687 0.0699364 0.00356426  -0.0125167  -0.00719358 39  PRO   A CB   
295  C  CG   . PRO   A 39  ? 0.112455  0.214546 0.0788163 0.00672643  -0.0179688  -0.00893075 39  PRO   A CG   
296  C  CD   . PRO   A 39  ? 0.119598  0.215761 0.0808394 0.00512353  -0.0159284  -0.00869369 39  PRO   A CD   
297  N  N    . ARG   A 40  ? 0.112521  0.228814 0.0625595 -0.00232365 -0.0117264  -0.0115567  40  ARG   A N    
298  C  CA   . ARG   A 40  ? 0.10881   0.239322 0.0627223 0.00456953  -0.0129229  -0.00865234 40  ARG   A CA   
299  C  C    . ARG   A 40  ? 0.110372  0.242104 0.0680614 0.00261267  -0.0229969  -0.0143759  40  ARG   A C    
300  O  O    . ARG   A 40  ? 0.107952  0.249387 0.0779824 -0.00307567 -0.00963334 -0.0182756  40  ARG   A O    
301  C  CB   . ARG   A 40  ? 0.10947   0.251347 0.0657207 0.00602192  -0.016108   -0.00533553 40  ARG   A CB   
302  C  CG   . ARG   A 40  ? 0.112066  0.26607  0.0670542 0.0114208   -0.0139278  -0.00546536 40  ARG   A CG   
303  C  CD   . ARG   A 40  ? 0.108489  0.278072 0.0745547 0.0149965   -0.0173556  -0.00135845 40  ARG   A CD   
304  N  NE   . ARG   A 40  ? 0.102703  0.293539 0.0785006 0.0173322   -0.010569   -0.00326893 40  ARG   A NE   
305  C  CZ   . ARG   A 40  ? 0.111603  0.305371 0.0826386 0.019815    -0.0146393  -0.00201933 40  ARG   A CZ   
306  N  NH1  . ARG   A 40  ? 0.128149  0.303503 0.076258  0.0239553   -0.00531264 0.00507103  40  ARG   A NH1  
307  N  NH2  . ARG   A 40  ? 0.116127  0.321023 0.0799486 0.024448    -0.0162476  -0.00686193 40  ARG   A NH2  
308  N  N    . HIS   A 41  ? 0.104647  0.240723 0.0704528 0.00183075  -0.0167508  -0.0188429  41  HIS   A N    
309  C  CA   . HIS   A 41  ? 0.116031  0.241517 0.0891008 0.0100455   -0.0144714  -0.0151684  41  HIS   A CA   
310  C  C    . HIS   A 41  ? 0.121618  0.231417 0.109834  0.00121492  -0.00339955 -0.0113225  41  HIS   A C    
311  O  O    . HIS   A 41  ? 0.131152  0.232998 0.127596  0.00770447  0.00701594  -0.0163153  41  HIS   A O    
312  C  CB   . HIS   A 41  ? 0.126228  0.249555 0.0892416 0.011792    -0.00782236 -0.0168104  41  HIS   A CB   
313  C  CG   . HIS   A 41  ? 0.140543  0.256697 0.0872751 0.0163106   -0.0141969  -0.0148847  41  HIS   A CG   
314  N  ND1  . HIS   A 41  ? 0.153197  0.266687 0.108521  0.0174621   -0.0121855  -0.00674112 41  HIS   A ND1  
315  C  CD2  . HIS   A 41  ? 0.146315  0.263255 0.0866477 0.0116994   -0.00969512 -0.0112505  41  HIS   A CD2  
316  C  CE1  . HIS   A 41  ? 0.148994  0.269857 0.0942505 0.0123727   -0.0150586  0.00127566  41  HIS   A CE1  
317  N  NE2  . HIS   A 41  ? 0.135731  0.259847 0.109055  0.0147339   -0.0157131  -0.00782939 41  HIS   A NE2  
318  N  N    . VAL   A 42  ? 0.11612   0.234222 0.103475  -0.00546636 -0.00552998 -0.00621541 42  VAL   A N    
319  C  CA   . VAL   A 42  ? 0.121995  0.247155 0.113747  -0.0118391  0.00087589  -0.00715649 42  VAL   A CA   
320  C  C    . VAL   A 42  ? 0.125235  0.241384 0.12649   -0.0145667  -0.00387967 -0.00089135 42  VAL   A C    
321  O  O    . VAL   A 42  ? 0.141188  0.256713 0.130701  -0.0298967  0.0024999   0.00184746  42  VAL   A O    
322  C  CB   . VAL   A 42  ? 0.124869  0.252347 0.106906  -0.0142264  0.00760143  -0.00782955 42  VAL   A CB   
323  C  CG1  . VAL   A 42  ? 0.138193  0.252241 0.109463  -0.011949   0.0103205   -0.00989176 42  VAL   A CG1  
324  C  CG2  . VAL   A 42  ? 0.124141  0.26547  0.110775  -0.0201839  0.0118683   -0.0080934  42  VAL   A CG2  
325  N  N    . ILE   A 43  ? 0.12599   0.233705 0.116628  -0.00857357 -0.00489803 -0.0116612  43  ILE   A N    
326  C  CA   . ILE   A 43  ? 0.123495  0.245213 0.139644  -0.00634657 0.00083421  -0.0271203  43  ILE   A CA   
327  C  C    . ILE   A 43  ? 0.144265  0.255951 0.160152  -0.00818563 -0.0100392  -0.0325705  43  ILE   A C    
328  O  O    . ILE   A 43  ? 0.156241  0.288177 0.218427  -0.00735359 -0.0316647  -0.0446084  43  ILE   A O    
329  C  CB   . ILE   A 43  ? 0.131533  0.256185 0.13628   0.00111022  -0.00181002 -0.029881   43  ILE   A CB   
330  C  CG1  . ILE   A 43  ? 0.131372  0.258613 0.138391  0.00699597  -0.00301245 -0.0281593  43  ILE   A CG1  
331  C  CG2  . ILE   A 43  ? 0.151482  0.261256 0.143349  0.00749647  0.00209163  -0.0323659  43  ILE   A CG2  
332  C  CD1  . ILE   A 43  ? 0.136363  0.2673   0.141181  0.0105883   -0.0100219  -0.0311783  43  ILE   A CD1  
333  N  N    . CYS   A 44  ? 0.144917  0.272664 0.177174  -0.00440731 -0.0134781  -0.0415315  44  CYS   A N    
334  C  CA   . CYS   A 44  ? 0.172543  0.285858 0.205143  -0.00258862 -0.0133984  -0.0523393  44  CYS   A CA   
335  C  C    . CYS   A 44  ? 0.232575  0.3123   0.263912  -0.00111384 0.00206161  -0.0463661  44  CYS   A C    
336  O  O    . CYS   A 44  ? 0.283348  0.320615 0.294149  0.00202465  -0.00265212 -0.0111371  44  CYS   A O    
337  C  CB   . CYS   A 44  ? 0.181625  0.292237 0.189153  -0.00753088 -0.0200215  -0.0526766  44  CYS   A CB   
338  S  SG   . CYS   A 44  ? 0.221967  0.323862 0.175281  0.00121073  -0.0445915  -0.0508497  44  CYS   A SG   
339  N  N    . THR   A 45  ? 0.246763  0.33365  0.35097   -0.0172749  0.0279075   -0.0473105  45  THR   A N    
340  C  CA   . THR   A 45  ? 0.288254  0.341753 0.388904  -0.0138588  0.033363    -0.0589599  45  THR   A CA   
341  C  C    . THR   A 45  ? 0.242333  0.325891 0.359272  -0.0270256  0.0178528   -0.0551668  45  THR   A C    
342  O  O    . THR   A 45  ? 0.224813  0.318668 0.328707  -0.0220685  0.0266233   -0.0812341  45  THR   A O    
343  C  CB   . THR   A 45  ? 0.2979    0.368256 0.446219  -0.0186022  0.0564689   -0.0564951  45  THR   A CB   
344  O  OG1  . THR   A 45  ? 0.322612  0.418588 0.491091  -0.0305432  0.0456482   -0.0591769  45  THR   A OG1  
345  C  CG2  . THR   A 45  ? 0.329817  0.387429 0.483209  -0.00594737 0.0664735   -0.0571533  45  THR   A CG2  
346  N  N    . SER   A 46  ? 0.263619  0.323216 0.328311  -0.0288701  0.00153016  -0.055648   46  SER   A N    
347  C  CA   . SER   A 46  ? 0.280809  0.340479 0.343376  -0.0214939  -0.00587563 -0.0499421  46  SER   A CA   
348  C  C    . SER   A 46  ? 0.287677  0.358444 0.343008  -0.0177915  -0.00543166 -0.0382798  46  SER   A C    
349  O  O    . SER   A 46  ? 0.311811  0.384709 0.314838  -0.00648431 -0.0158319  -0.0751119  46  SER   A O    
350  C  CB   . SER   A 46  ? 0.308528  0.360873 0.335127  -0.0165243  -0.015147   -0.0361629  46  SER   A CB   
351  O  OG   . SER   A 46  ? 0.336079  0.388288 0.347181  -0.031656   -0.0100676  -0.0361465  46  SER   A OG   
352  N  N    . GLU   A 47  ? 0.264585  0.345846 0.327848  -0.026254   -0.0119037  -0.0313888  47  GLU   A N    
353  C  CA   . GLU   A 47  ? 0.265957  0.387999 0.335399  -0.0210545  -0.0188112  -0.0331462  47  GLU   A CA   
354  C  C    . GLU   A 47  ? 0.272458  0.401771 0.334934  -0.0197021  -0.0228325  -0.0488221  47  GLU   A C    
355  O  O    . GLU   A 47  ? 0.361691  0.485239 0.337318  -0.0196136  -0.0264848  -0.0604152  47  GLU   A O    
356  C  CB   . GLU   A 47  ? 0.278337  0.404241 0.336839  -0.0373579  -0.0174675  -0.0280966  47  GLU   A CB   
357  N  N    . ASP   A 48  ? 0.201484  0.408416 0.300558  0.00657587  -0.0190529  -0.0699646  48  ASP   A N    
358  C  CA   . ASP   A 48  ? 0.183852  0.39906  0.288036  0.0036144   -0.0203106  -0.0777924  48  ASP   A CA   
359  C  C    . ASP   A 48  ? 0.187821  0.385615 0.285161  0.00983595  -0.0162272  -0.0739043  48  ASP   A C    
360  O  O    . ASP   A 48  ? 0.16651   0.374202 0.25505   0.0144693   -0.0315959  -0.0711617  48  ASP   A O    
361  C  CB   . ASP   A 48  ? 0.185191  0.417418 0.275217  0.00497572  -0.00589913 -0.0849612  48  ASP   A CB   
362  C  CG   . ASP   A 48  ? 0.203959  0.447333 0.297827  -0.00890572 0.00528243  -0.0850196  48  ASP   A CG   
363  O  OD1  . ASP   A 48  ? 0.203187  0.456495 0.341163  -0.0143547  -0.01096    -0.0883091  48  ASP   A OD1  
364  O  OD2  . ASP   A 48  ? 0.275443  0.488742 0.326154  -0.0201314  0.0384473   -0.116895   48  ASP   A OD2  
365  N  N    . MET   A 49  ? 0.166931  0.385844 0.317893  0.00718833  -0.0202989  -0.0675633  49  MET   A N    
366  C  CA   . MET   A 49  ? 0.166601  0.37348  0.294226  0.0178116   -0.00639586 -0.0739382  49  MET   A CA   
367  C  C    . MET   A 49  ? 0.171655  0.365508 0.286247  0.0152393   -0.0332261  -0.0905859  49  MET   A C    
368  O  O    . MET   A 49  ? 0.157795  0.333995 0.252476  0.0296487   -0.0245919  -0.085951   49  MET   A O    
369  C  CB   . MET   A 49  ? 0.167335  0.381843 0.302074  0.022873    -0.00842046 -0.0707629  49  MET   A CB   
370  C  CG   . MET   A 49  ? 0.19146   0.364897 0.289077  0.0231389   -0.0108699  -0.0744641  49  MET   A CG   
371  S  SD   . MET   A 49  ? 0.199697  0.353072 0.231967  0.0197577   0.00705929  -0.0610883  49  MET   A SD   
372  C  CE   . MET   A 49  ? 0.185173  0.334096 0.258785  0.015301    -0.0207675  -0.05516    49  MET   A CE   
373  N  N    . LEU   A 50  ? 0.19471   0.379528 0.333255  0.0130154   -0.0312103  -0.120661   50  LEU   A N    
374  C  CA   . LEU   A 50  ? 0.205968  0.399974 0.311553  0.00661656  -0.0438277  -0.143439   50  LEU   A CA   
375  C  C    . LEU   A 50  ? 0.17449   0.396757 0.32276   0.0370745   -0.0798158  -0.173554   50  LEU   A C    
376  O  O    . LEU   A 50  ? 0.172652  0.396278 0.329641  0.0461269   -0.0968815  -0.196035   50  LEU   A O    
377  C  CB   . LEU   A 50  ? 0.245044  0.413278 0.293879  -0.0104976  -0.0211571  -0.139186   50  LEU   A CB   
378  C  CG   . LEU   A 50  ? 0.261788  0.419723 0.278392  -0.0313633  -0.0025495  -0.138335   50  LEU   A CG   
379  C  CD1  . LEU   A 50  ? 0.266463  0.419565 0.280654  -0.0349238  0.0109511   -0.142173   50  LEU   A CD1  
380  C  CD2  . LEU   A 50  ? 0.282885  0.409056 0.284245  -0.0356033  0.00716935  -0.132189   50  LEU   A CD2  
381  N  N    . ASN   A 51  ? 0.177928  0.413522 0.312664  0.0425101   -0.0786312  -0.180632   51  ASN   A N    
382  C  CA   . ASN   A 51  ? 0.207902  0.408696 0.266268  0.0417582   -0.075445   -0.177698   51  ASN   A CA   
383  C  C    . ASN   A 51  ? 0.178343  0.398495 0.26593   0.0418855   -0.0751045  -0.16198    51  ASN   A C    
384  O  O    . ASN   A 51  ? 0.190706  0.48759  0.354466  0.0576781   -0.0885519  -0.220326   51  ASN   A O    
385  C  CB   . ASN   A 51  ? 0.2758    0.444289 0.251317  0.030792    -0.0744227  -0.173468   51  ASN   A CB   
386  C  CG   . ASN   A 51  ? 0.322457  0.464854 0.261786  0.0322423   -0.0413872  -0.115131   51  ASN   A CG   
387  O  OD1  . ASN   A 51  ? 0.337622  0.499489 0.234147  0.0730893   -0.0607722  -0.0446838  51  ASN   A OD1  
388  N  ND2  . ASN   A 51  ? 0.320963  0.454758 0.23306   0.0382013   -0.0120629  -0.0958304  51  ASN   A ND2  
389  N  N    . PRO   A 52  ? 0.154169  0.345397 0.195064  0.0452184   -0.0370677  -0.118123   52  PRO   A N    
390  C  CA   . PRO   A 52  ? 0.136467  0.32428  0.201756  0.0409661   -0.0244494  -0.0931698  52  PRO   A CA   
391  C  C    . PRO   A 52  ? 0.135868  0.327101 0.162503  0.032963    -0.0254907  -0.0743212  52  PRO   A C    
392  O  O    . PRO   A 52  ? 0.129135  0.34575  0.199585  0.038783    -0.0238816  -0.0413169  52  PRO   A O    
393  C  CB   . PRO   A 52  ? 0.162864  0.324082 0.198086  0.0363991   -0.0288873  -0.101675   52  PRO   A CB   
394  C  CG   . PRO   A 52  ? 0.156821  0.327578 0.194528  0.0358466   -0.0393435  -0.108118   52  PRO   A CG   
395  C  CD   . PRO   A 52  ? 0.154686  0.335335 0.195558  0.0399787   -0.0467844  -0.109954   52  PRO   A CD   
396  N  N    . ASN   A 53  ? 0.134103  0.309316 0.133192  0.0221212   -0.00942642 -0.0641701  53  ASN   A N    
397  C  CA   . ASN   A 53  ? 0.143973  0.312247 0.102432  0.0235226   -0.014934   -0.0545725  53  ASN   A CA   
398  C  C    . ASN   A 53  ? 0.127797  0.286424 0.0905197 0.0156634   -0.0112211  -0.0406219  53  ASN   A C    
399  O  O    . ASN   A 53  ? 0.118306  0.267287 0.100215  0.0147927   -0.0156541  -0.035866   53  ASN   A O    
400  C  CB   . ASN   A 53  ? 0.153664  0.33434  0.0981455 0.0173803   -0.0111012  -0.055548   53  ASN   A CB   
401  C  CG   . ASN   A 53  ? 0.18265   0.360995 0.10718   0.0234707   -0.0217314  -0.0375346  53  ASN   A CG   
402  O  OD1  . ASN   A 53  ? 0.149228  0.371647 0.129183  0.00501715  -0.0317719  -0.0142128  53  ASN   A OD1  
403  N  ND2  . ASN   A 53  ? 0.246471  0.391212 0.123557  0.0278534   -0.0450451  -0.0345858  53  ASN   A ND2  
404  N  N    . TYR   A 54  ? 0.12198   0.288702 0.0871138 0.0161317   -0.00837819 -0.0322036  54  TYR   A N    
405  C  CA   . TYR   A 54  ? 0.121357  0.280462 0.0784639 0.0140937   -0.019844   -0.0225983  54  TYR   A CA   
406  C  C    . TYR   A 54  ? 0.128131  0.279955 0.079301  0.0202191   -0.00912483 -0.019783   54  TYR   A C    
407  O  O    . TYR   A 54  ? 0.127687  0.296304 0.0792388 0.0140154   -0.01044    -0.0260609  54  TYR   A O    
408  C  CB   . TYR   A 54  ? 0.124355  0.282807 0.0860163 0.0104491   -0.0127609  -0.0178799  54  TYR   A CB   
409  C  CG   . TYR   A 54  ? 0.115604  0.273422 0.0792289 0.00695292  -0.0150972  -0.0195868  54  TYR   A CG   
410  C  CD1  . TYR   A 54  ? 0.121644  0.277074 0.082471  0.00648553  -0.00927407 -0.0129945  54  TYR   A CD1  
411  C  CD2  . TYR   A 54  ? 0.119405  0.269942 0.0785329 0.0077222   -0.0152432  -0.0229452  54  TYR   A CD2  
412  C  CE1  . TYR   A 54  ? 0.129303  0.275529 0.0909662 0.0118103   -0.0119172  -0.0154864  54  TYR   A CE1  
413  C  CE2  . TYR   A 54  ? 0.122762  0.277933 0.0894819 0.0118671   -0.012348   -0.0239014  54  TYR   A CE2  
414  C  CZ   . TYR   A 54  ? 0.127702  0.277174 0.100443  0.0112097   -0.0121805  -0.0164557  54  TYR   A CZ   
415  O  OH   . TYR   A 54  ? 0.133737  0.30082  0.123211  0.0254919   -0.0147782  -0.0259585  54  TYR   A OH   
416  N  N    . GLU   A 55  ? 0.132085  0.274912 0.0811636 0.0183254   -0.00911225 -0.0134445  55  GLU   A N    
417  C  CA   . GLU   A 55  ? 0.140434  0.274395 0.0944577 0.0128978   -0.00260574 -0.0115589  55  GLU   A CA   
418  C  C    . GLU   A 55  ? 0.132415  0.259996 0.100552  0.0163619   -0.00092313 -0.0118265  55  GLU   A C    
419  O  O    . GLU   A 55  ? 0.121996  0.261045 0.106361  0.00878501  0.00396042  -0.0104746  55  GLU   A O    
420  C  CB   . GLU   A 55  ? 0.159336  0.295983 0.107456  0.00909022  -0.0165821  -0.00110618 55  GLU   A CB   
421  C  CG   . GLU   A 55  ? 0.197462  0.326012 0.154087  -0.013091   -0.00818639 0.00739222  55  GLU   A CG   
422  C  CD   . GLU   A 55  ? 0.228121  0.373412 0.214971  -0.00937936 0.00078967  0.00957873  55  GLU   A CD   
423  O  OE1  . GLU   A 55  ? 0.259097  0.397082 0.191224  -0.0314646  0.00285062  0.00933307  55  GLU   A OE1  
424  O  OE2  . GLU   A 55  ? 0.290909  0.42074  0.305743  -0.0423063  -0.00046621 0.0229514   55  GLU   A OE2  
425  N  N    . ASP   A 56  ? 0.116059  0.253786 0.0906862 0.0155322   0.00625472  -0.010744   56  ASP   A N    
426  C  CA   . ASP   A 56  ? 0.114966  0.255874 0.101519  0.0206214   0.00140603  -0.0106069  56  ASP   A CA   
427  C  C    . ASP   A 56  ? 0.113803  0.264524 0.104905  0.0272764   0.00180783  -0.00693046 56  ASP   A C    
428  O  O    . ASP   A 56  ? 0.113213  0.297755 0.110887  0.0266606   0.00321314  0.00679927  56  ASP   A O    
429  C  CB   . ASP   A 56  ? 0.134375  0.254281 0.110172  0.019136    0.00094847  -0.00956049 56  ASP   A CB   
430  C  CG   . ASP   A 56  ? 0.140105  0.264271 0.129835  0.0176626   0.00070507  -0.00683456 56  ASP   A CG   
431  O  OD1  . ASP   A 56  ? 0.161373  0.287299 0.162491  0.0239912   -0.00959108 0.00633479  56  ASP   A OD1  
432  O  OD2  . ASP   A 56  ? 0.166288  0.287944 0.185634  0.00402288  0.0100254   0.00342793  56  ASP   A OD2  
433  N  N    . LEU   A 57  ? 0.106636  0.267595 0.0869662 0.0282737   -0.00015848 -0.0088349  57  LEU   A N    
434  C  CA   . LEU   A 57  ? 0.13382   0.262112 0.0982499 0.0295723   -0.00545797 -0.00956148 57  LEU   A CA   
435  C  C    . LEU   A 57  ? 0.138236  0.259807 0.0934737 0.0176103   -0.0053501  -0.0131574  57  LEU   A C    
436  O  O    . LEU   A 57  ? 0.137877  0.269255 0.0857169 0.0148201   0.00026118  -0.0200827  57  LEU   A O    
437  C  CB   . LEU   A 57  ? 0.140713  0.267353 0.114809  0.036336    -0.0126812  -0.0120196  57  LEU   A CB   
438  C  CG   . LEU   A 57  ? 0.166987  0.278198 0.137274  0.0388836   -0.0109535  -0.0173265  57  LEU   A CG   
439  C  CD1  . LEU   A 57  ? 0.181262  0.30166  0.158512  0.049751    -0.0129346  -0.0228951  57  LEU   A CD1  
440  C  CD2  . LEU   A 57  ? 0.190864  0.286042 0.171743  0.0344894   -0.00460343 -0.0266019  57  LEU   A CD2  
441  N  N    . LEU   A 58  ? 0.133171  0.244631 0.0882889 0.0193424   -0.0105666  -0.0142006  58  LEU   A N    
442  C  CA   . LEU   A 58  ? 0.132288  0.252349 0.0921931 0.0146372   -0.00276502 -0.0219883  58  LEU   A CA   
443  C  C    . LEU   A 58  ? 0.12167   0.249554 0.0800448 0.0137522   -0.00946254 -0.0288424  58  LEU   A C    
444  O  O    . LEU   A 58  ? 0.116584  0.255706 0.0826075 0.00230643  -0.0040293  -0.0346061  58  LEU   A O    
445  C  CB   . LEU   A 58  ? 0.130295  0.264107 0.113777  0.0123621   -0.00146192 -0.022059   58  LEU   A CB   
446  C  CG   . LEU   A 58  ? 0.137944  0.266688 0.123835  0.013174    0.00887962  -0.0248196  58  LEU   A CG   
447  C  CD1  . LEU   A 58  ? 0.12256   0.274931 0.11825   0.0136296   0.00656403  -0.0244553  58  LEU   A CD1  
448  C  CD2  . LEU   A 58  ? 0.148699  0.280184 0.154427  0.00291875  0.0137464   -0.031035   58  LEU   A CD2  
449  N  N    A ILE   A 59  ? 0.121865  0.253925 0.0797565 0.0175618   -0.00644152 -0.0235268  59  ILE   A N    
450  N  N    B ILE   A 59  ? 0.119387  0.250267 0.0791212 0.0178606   -0.00667754 -0.0257108  59  ILE   A N    
451  C  CA   A ILE   A 59  ? 0.122362  0.249992 0.0860562 0.0169373   -0.00522041 -0.0185015  59  ILE   A CA   
452  C  CA   B ILE   A 59  ? 0.118424  0.244503 0.0819102 0.0170122   -0.00787532 -0.021969   59  ILE   A CA   
453  C  C    A ILE   A 59  ? 0.120621  0.244819 0.0844628 0.0146968   -0.00745384 -0.0197906  59  ILE   A C    
454  C  C    B ILE   A 59  ? 0.117734  0.24174  0.0821073 0.0147148   -0.00874376 -0.0219048  59  ILE   A C    
455  O  O    A ILE   A 59  ? 0.126608  0.247697 0.10126   0.0115222   0.00330847  -0.0227528  59  ILE   A O    
456  O  O    B ILE   A 59  ? 0.122302  0.24208  0.0969417 0.010778    0.00147467  -0.0241843  59  ILE   A O    
457  C  CB   A ILE   A 59  ? 0.12647   0.253674 0.0900089 0.0214135   -0.00353367 -0.0103246  59  ILE   A CB   
458  C  CB   B ILE   A 59  ? 0.119211  0.244446 0.0859681 0.0218661   -0.00748516 -0.017182   59  ILE   A CB   
459  C  CG1  A ILE   A 59  ? 0.131968  0.253966 0.101631  0.0216431   0.00357466  -0.0119553  59  ILE   A CG1  
460  C  CG1  B ILE   A 59  ? 0.122402  0.241999 0.0932084 0.0216675   -0.00337477 -0.0216766  59  ILE   A CG1  
461  C  CG2  A ILE   A 59  ? 0.127201  0.255028 0.0819392 0.0236244   -0.00294612 -0.00928781 59  ILE   A CG2  
462  C  CG2  B ILE   A 59  ? 0.122067  0.24422  0.0757425 0.022979    -0.00638561 -0.0172549  59  ILE   A CG2  
463  C  CD1  A ILE   A 59  ? 0.141327  0.255512 0.101595  0.0201265   0.00699761  -0.0128827  59  ILE   A CD1  
464  C  CD1  B ILE   A 59  ? 0.119057  0.243555 0.0940554 0.0224691   -0.00404943 -0.0225878  59  ILE   A CD1  
465  N  N    . ARG   A 60  ? 0.116564  0.243275 0.0842139 0.0124713   -0.0102438  -0.0207934  60  ARG   A N    
466  C  CA   . ARG   A 60  ? 0.12114   0.248687 0.0889236 0.00861304  -0.0136035  -0.0161435  60  ARG   A CA   
467  C  C    . ARG   A 60  ? 0.126179  0.253359 0.0908798 0.00148295  -0.0152154  -0.0175722  60  ARG   A C    
468  O  O    . ARG   A 60  ? 0.129523  0.25697  0.0971801 0.00048923  -0.0143762  -0.0188751  60  ARG   A O    
469  C  CB   . ARG   A 60  ? 0.12594   0.249357 0.0824029 0.00562532  -0.0209245  -0.0169575  60  ARG   A CB   
470  C  CG   . ARG   A 60  ? 0.135715  0.255836 0.0833127 0.00436535  -0.0209286  -0.0137506  60  ARG   A CG   
471  C  CD   . ARG   A 60  ? 0.135938  0.256232 0.0901739 0.00783734  -0.0203544  -0.0165275  60  ARG   A CD   
472  N  NE   . ARG   A 60  ? 0.130651  0.264618 0.0906511 0.00818942  -0.0132389  -0.0226574  60  ARG   A NE   
473  C  CZ   . ARG   A 60  ? 0.128778  0.259107 0.0911945 0.0064723   -0.00873681 -0.0226245  60  ARG   A CZ   
474  N  NH1  . ARG   A 60  ? 0.128925  0.253399 0.0907356 0.0138236   -0.00939187 -0.021989   60  ARG   A NH1  
475  N  NH2  . ARG   A 60  ? 0.140467  0.268661 0.0922695 0.00045249  -0.00849969 -0.0226988  60  ARG   A NH2  
476  N  N    . LYS   A 61  ? 0.135067  0.269052 0.0767728 -0.00250156 -0.0164382  -0.0255333  61  LYS   A N    
477  C  CA   . LYS   A 61  ? 0.149864  0.271839 0.0849603 -0.0030295  -0.0244117  -0.0303188  61  LYS   A CA   
478  C  C    . LYS   A 61  ? 0.149563  0.26731  0.0939643 -0.00087625 -0.0074548  -0.0215589  61  LYS   A C    
479  O  O    . LYS   A 61  ? 0.162661  0.269038 0.104902  0.00910718  0.00998824  -0.0233642  61  LYS   A O    
480  C  CB   . LYS   A 61  ? 0.15561   0.287585 0.115871  0.00280162  -0.0267833  -0.0312292  61  LYS   A CB   
481  C  CG   . LYS   A 61  ? 0.175016  0.308905 0.141011  0.0080057   -0.0269356  -0.0420501  61  LYS   A CG   
482  C  CD   . LYS   A 61  ? 0.199676  0.324463 0.18485   -0.00040361 -0.0234763  -0.0390753  61  LYS   A CD   
483  C  CE   . LYS   A 61  ? 0.242547  0.341155 0.232248  0.0110125   -0.0214154  -0.0363708  61  LYS   A CE   
484  N  NZ   . LYS   A 61  ? 0.289673  0.364436 0.297481  0.00644317  -0.0185372  -0.0277163  61  LYS   A NZ   
485  N  N    . SER   A 62  ? 0.143654  0.272486 0.0988425 -0.00297483 0.0025061   -0.0255699  62  SER   A N    
486  C  CA   . SER   A 62  ? 0.136292  0.286229 0.101924  0.00276576  -0.00870728 -0.0324827  62  SER   A CA   
487  C  C    . SER   A 62  ? 0.138864  0.279615 0.0972753 0.0023181   -0.0113593  -0.0309541  62  SER   A C    
488  O  O    . SER   A 62  ? 0.159148  0.300245 0.108631  0.014086    -0.020929   -0.0386539  62  SER   A O    
489  C  CB   . SER   A 62  ? 0.157862  0.306535 0.115468  -0.00328749 0.00172951  -0.0251457  62  SER   A CB   
490  O  OG   . SER   A 62  ? 0.15849   0.343999 0.134103  0.010427    0.00796451  -0.0144803  62  SER   A OG   
491  N  N    . ASN   A 63  ? 0.133469  0.281085 0.107195  0.00609868  -0.00555771 -0.0247281  63  ASN   A N    
492  C  CA   . ASN   A 63  ? 0.125311  0.279113 0.108666  0.00592379  -0.00020009 -0.0262237  63  ASN   A CA   
493  C  C    . ASN   A 63  ? 0.130163  0.281356 0.111403  0.00323053  -0.00012872 -0.0293134  63  ASN   A C    
494  O  O    . ASN   A 63  ? 0.130162  0.287648 0.111221  0.00600527  -0.014448   -0.0361085  63  ASN   A O    
495  C  CB   . ASN   A 63  ? 0.132681  0.27864  0.119451  0.00403929  0.00396013  -0.0280362  63  ASN   A CB   
496  C  CG   . ASN   A 63  ? 0.151003  0.284718 0.1477    0.00880969  0.0183917   -0.0283133  63  ASN   A CG   
497  O  OD1  . ASN   A 63  ? 0.181462  0.307915 0.159795  0.0137468   0.0416818   -0.0200484  63  ASN   A OD1  
498  N  ND2  . ASN   A 63  ? 0.151392  0.290317 0.173383  0.0155693   0.0136086   -0.0209548  63  ASN   A ND2  
499  N  N    . HIS   A 64  ? 0.128868  0.293201 0.0968579 -0.00356853 -0.00368366 -0.0172228  64  HIS   A N    
500  C  CA   . HIS   A 64  ? 0.142227  0.301887 0.107429  -0.00598838 -0.00072794 -0.00978888 64  HIS   A CA   
501  C  C    . HIS   A 64  ? 0.158928  0.299639 0.118352  -0.00975231 -0.00136271 -0.00869846 64  HIS   A C    
502  O  O    . HIS   A 64  ? 0.201959  0.317603 0.14353   -0.00107309 0.00978938  0.00418678  64  HIS   A O    
503  C  CB   . HIS   A 64  ? 0.153214  0.312673 0.0958085 -0.00119322 0.00333177  -0.012441   64  HIS   A CB   
504  C  CG   . HIS   A 64  ? 0.152765  0.330844 0.107121  -0.00230308 0.00991462  -0.0129587  64  HIS   A CG   
505  N  ND1  . HIS   A 64  ? 0.159857  0.349424 0.11517   -0.00304371 -0.00128446 -0.00613394 64  HIS   A ND1  
506  C  CD2  . HIS   A 64  ? 0.170018  0.337037 0.119001  -0.0109985  0.00127058  -0.00738216 64  HIS   A CD2  
507  C  CE1  . HIS   A 64  ? 0.165203  0.344314 0.127076  -0.00615413 -0.0110256  -0.00797382 64  HIS   A CE1  
508  N  NE2  . HIS   A 64  ? 0.169288  0.350013 0.147192  -0.0092633  -0.00770373 -0.00418841 64  HIS   A NE2  
509  N  N    . ASN   A 65  ? 0.149098  0.288929 0.106692  -0.0107461  -0.0183243  -0.0089109  65  ASN   A N    
510  C  CA   . ASN   A 65  ? 0.157569  0.285255 0.144803  -0.0184808  -0.0195267  -0.0173247  65  ASN   A CA   
511  C  C    . ASN   A 65  ? 0.155278  0.287264 0.150358  -0.00401948 -0.00925712 -0.0325028  65  ASN   A C    
512  O  O    . ASN   A 65  ? 0.177126  0.293744 0.204151  0.00721134  -0.0280657  -0.0299048  65  ASN   A O    
513  C  CB   . ASN   A 65  ? 0.18738   0.292845 0.148505  -0.0267348  -0.0163116  -0.020389   65  ASN   A CB   
514  C  CG   . ASN   A 65  ? 0.199848  0.323097 0.177884  -0.0410092  -0.014783   0.00157786  65  ASN   A CG   
515  O  OD1  . ASN   A 65  ? 0.211931  0.324072 0.155832  -0.0449318  -0.00283596 -0.00466662 65  ASN   A OD1  
516  N  ND2  . ASN   A 65  ? 0.225292  0.355204 0.211816  -0.0572375  -0.0152751  0.0240313   65  ASN   A ND2  
517  N  N    . PHE   A 66  ? 0.134265  0.292807 0.119663  -0.0047285  -0.0113931  -0.0387306  66  PHE   A N    
518  C  CA   . PHE   A 66  ? 0.137017  0.298951 0.109447  0.00471339  -0.0145854  -0.0407315  66  PHE   A CA   
519  C  C    . PHE   A 66  ? 0.15764   0.305186 0.106789  0.00808533  -0.00491827 -0.0451949  66  PHE   A C    
520  O  O    . PHE   A 66  ? 0.195123  0.315509 0.128145  0.0304169   -0.0060735  -0.044882   66  PHE   A O    
521  C  CB   . PHE   A 66  ? 0.127338  0.298316 0.117207  0.00475013  -0.0119803  -0.0407686  66  PHE   A CB   
522  C  CG   . PHE   A 66  ? 0.13583   0.307387 0.116754  -0.00028028 -0.00319879 -0.0431064  66  PHE   A CG   
523  C  CD1  . PHE   A 66  ? 0.150515  0.317385 0.121899  0.00477838  0.00246566  -0.045138   66  PHE   A CD1  
524  C  CD2  . PHE   A 66  ? 0.128881  0.317412 0.114614  -0.00359073 0.00096232  -0.0384911  66  PHE   A CD2  
525  C  CE1  . PHE   A 66  ? 0.167575  0.322393 0.117094  0.00202057  0.00848469  -0.0388392  66  PHE   A CE1  
526  C  CE2  . PHE   A 66  ? 0.152297  0.32778  0.117754  -0.00290481 -0.00400096 -0.0353321  66  PHE   A CE2  
527  C  CZ   . PHE   A 66  ? 0.151265  0.331959 0.102298  -0.00579692 0.00378634  -0.0399536  66  PHE   A CZ   
528  N  N    . LEU   A 67  ? 0.154     0.307965 0.113572  0.00880474  0.00025451  -0.0484991  67  LEU   A N    
529  C  CA   . LEU   A 67  ? 0.146367  0.333996 0.125972  0.0074942   -0.00420691 -0.0362537  67  LEU   A CA   
530  C  C    . LEU   A 67  ? 0.138065  0.320273 0.120102  0.0120232   0.00079576  -0.0385084  67  LEU   A C    
531  O  O    . LEU   A 67  ? 0.145671  0.347681 0.139505  0.01968     -0.0148218  -0.0778676  67  LEU   A O    
532  C  CB   . LEU   A 67  ? 0.201722  0.359121 0.172118  0.0108325   0.003809    -0.0209282  67  LEU   A CB   
533  C  CG   . LEU   A 67  ? 0.241581  0.395294 0.239446  -0.00408748 0.020408    -0.0147769  67  LEU   A CG   
534  C  CD1  . LEU   A 67  ? 0.288528  0.408341 0.267238  -0.00165972 0.0320002   -0.00434001 67  LEU   A CD1  
535  C  CD2  . LEU   A 67  ? 0.277082  0.417029 0.263002  -0.00081139 0.0295964   -0.0212707  67  LEU   A CD2  
536  N  N    . VAL   A 68  ? 0.136284  0.301365 0.108947  0.017968    0.0196155   -0.0198137  68  VAL   A N    
537  C  CA   . VAL   A 68  ? 0.13915   0.285423 0.089347  0.0160281   0.0228337   -0.0157194  68  VAL   A CA   
538  C  C    . VAL   A 68  ? 0.149162  0.28207  0.0866155 0.0158799   0.0233034   -0.0153216  68  VAL   A C    
539  O  O    . VAL   A 68  ? 0.165116  0.284749 0.107256  0.0321461   0.0318674   -0.00889806 68  VAL   A O    
540  C  CB   . VAL   A 68  ? 0.157556  0.289754 0.109781  0.0179389   0.0340218   -0.0103956  68  VAL   A CB   
541  C  CG1  . VAL   A 68  ? 0.175672  0.302792 0.124858  0.00866381  0.0274818   -0.00331146 68  VAL   A CG1  
542  C  CG2  . VAL   A 68  ? 0.170735  0.290771 0.114617  0.0230416   0.0369472   -0.00265042 68  VAL   A CG2  
543  N  N    . GLN   A 69  ? 0.149158  0.276286 0.0886008 0.0106268   0.0261707   -0.0239876  69  GLN   A N    
544  C  CA   . GLN   A 69  ? 0.178672  0.299215 0.103339  0.010624    0.00575088  -0.0179108  69  GLN   A CA   
545  C  C    . GLN   A 69  ? 0.179205  0.28944  0.097499  0.0128068   0.00946134  -0.0205795  69  GLN   A C    
546  O  O    . GLN   A 69  ? 0.153386  0.296048 0.0927597 0.00552997  0.00732302  -0.0237467  69  GLN   A O    
547  C  CB   . GLN   A 69  ? 0.226292  0.323324 0.160392  -0.00808718 -0.00094025 -0.0163315  69  GLN   A CB   
548  C  CG   . GLN   A 69  ? 0.289098  0.378203 0.189926  -0.0134542  -0.0148518  -0.00324957 69  GLN   A CG   
549  C  CD   . GLN   A 69  ? 0.37124   0.415403 0.263232  -0.0260934  -0.0256368  0.0094467   69  GLN   A CD   
550  O  OE1  . GLN   A 69  ? 0.414928  0.482776 0.339919  -0.0624586  -0.0384171  0.0111041   69  GLN   A OE1  
551  N  NE2  . GLN   A 69  ? 0.410923  0.457164 0.305622  -0.0149616  -0.0401571  0.0276509   69  GLN   A NE2  
552  N  N    . ALA   A 70  ? 0.204403  0.311796 0.11151   0.0139815   0.0189795   -0.0304082  70  ALA   A N    
553  C  CA   . ALA   A 70  ? 0.221906  0.335293 0.11759   0.00861788  0.00989569  -0.0274911  70  ALA   A CA   
554  C  C    . ALA   A 70  ? 0.262002  0.375186 0.13997   0.0136725   -0.00334831 -0.00766115 70  ALA   A C    
555  O  O    . ALA   A 70  ? 0.26384   0.400914 0.147424  0.00770478  0.00076088  -0.0165406  70  ALA   A O    
556  C  CB   . ALA   A 70  ? 0.231567  0.337096 0.132705  0.00391639  0.0200894   -0.0231532  70  ALA   A CB   
557  N  N    . GLY   A 71  ? 0.281449  0.40068  0.166895  0.0197868   -0.0122385  0.00802037  71  GLY   A N    
558  C  CA   . GLY   A 71  ? 0.321524  0.436383 0.187745  0.0151243   -0.0268346  0.0286919   71  GLY   A CA   
559  C  C    . GLY   A 71  ? 0.346545  0.468264 0.234552  0.00483052  -0.0216364  0.0447032   71  GLY   A C    
560  O  O    . GLY   A 71  ? 0.383797  0.443564 0.306468  -0.00508649 -0.0220799  0.0331715   71  GLY   A O    
561  N  N    . ASN   A 72  ? 0.36135   0.516925 0.228898  -0.00900003 0.00059969  0.0537689   72  ASN   A N    
562  C  CA   . ASN   A 72  ? 0.368354  0.552683 0.242184  -0.00758596 0.0179723   0.0619401   72  ASN   A CA   
563  C  C    . ASN   A 72  ? 0.354596  0.563689 0.262191  -0.0113831  0.0359766   0.0484305   72  ASN   A C    
564  O  O    . ASN   A 72  ? 0.378539  0.623012 0.296625  -0.0243193  0.082389    0.0663154   72  ASN   A O    
565  C  CB   . ASN   A 72  ? 0.410123  0.574901 0.253203  -0.0067732  0.0116703   0.0922864   72  ASN   A CB   
566  N  N    . VAL   A 73  ? 0.341353  0.543156 0.19374   0.00369184  0.014064    0.0258011   73  VAL   A N    
567  C  CA   . VAL   A 73  ? 0.338914  0.529193 0.178754  0.00751109  0.0109046   -0.0066125  73  VAL   A CA   
568  C  C    . VAL   A 73  ? 0.268491  0.495951 0.144986  0.0195955   0.0556955   -0.00970834 73  VAL   A C    
569  O  O    . VAL   A 73  ? 0.233062  0.471582 0.133675  0.0348577   0.0507694   -0.0231003  73  VAL   A O    
570  C  CB   . VAL   A 73  ? 0.384033  0.541496 0.201594  -0.00066734 -0.0349799  -0.0388928  73  VAL   A CB   
571  C  CG1  . VAL   A 73  ? 0.43108   0.544986 0.218642  0.004317    -0.0311122  -0.0493615  73  VAL   A CG1  
572  C  CG2  . VAL   A 73  ? 0.426405  0.565125 0.201216  0.00026342  -0.0371486  -0.0363521  73  VAL   A CG2  
573  N  N    . GLN   A 74  ? 0.253622  0.477179 0.188111  0.0153163   0.0856638   -0.0208514  74  GLN   A N    
574  C  CA   . GLN   A 74  ? 0.246801  0.428573 0.200126  0.0167162   0.0761813   -0.0290455  74  GLN   A CA   
575  C  C    . GLN   A 74  ? 0.23658   0.394032 0.166957  0.0155281   0.0771619   -0.0560215  74  GLN   A C    
576  O  O    . GLN   A 74  ? 0.312784  0.407361 0.189874  0.0341251   0.102785    -0.0625434  74  GLN   A O    
577  C  CB   . GLN   A 74  ? 0.265079  0.456889 0.281327  0.00914802  0.0542308   -0.0154296  74  GLN   A CB   
578  C  CG   . GLN   A 74  ? 0.318163  0.487949 0.317772  -9.22e-05   0.0494236   0.00429503  74  GLN   A CG   
579  C  CD   . GLN   A 74  ? 0.368468  0.510303 0.374546  0.021278    0.0426716   -0.00311474 74  GLN   A CD   
580  O  OE1  . GLN   A 74  ? 0.420575  0.538591 0.376396  0.00676007  0.0595311   0.0183107   74  GLN   A OE1  
581  N  NE2  . GLN   A 74  ? 0.392213  0.537309 0.420994  0.0351076   0.027347    0.00407475  74  GLN   A NE2  
582  N  N    . LEU   A 75  ? 0.167188  0.332661 0.141268  0.0134238   0.0463707   -0.0695435  75  LEU   A N    
583  C  CA   . LEU   A 75  ? 0.164989  0.330085 0.161182  0.0102442   0.0118227   -0.0639295  75  LEU   A CA   
584  C  C    . LEU   A 75  ? 0.188403  0.337071 0.159678  0.00967232  -0.00828771 -0.0699308  75  LEU   A C    
585  O  O    . LEU   A 75  ? 0.268456  0.349817 0.28574   0.00868934  -0.074826   -0.0884843  75  LEU   A O    
586  C  CB   . LEU   A 75  ? 0.169279  0.324388 0.166964  0.00745054  0.0112807   -0.0601344  75  LEU   A CB   
587  C  CG   . LEU   A 75  ? 0.167271  0.329939 0.191738  0.00719479  0.00837292  -0.047822   75  LEU   A CG   
588  C  CD1  . LEU   A 75  ? 0.162679  0.332171 0.205637  0.00021459  0.0109653   -0.0522947  75  LEU   A CD1  
589  C  CD2  . LEU   A 75  ? 0.194159  0.346764 0.201573  -0.00750646 0.00053229  -0.0475616  75  LEU   A CD2  
590  N  N    . ARG   A 76  ? 0.170382  0.335243 0.148488  0.00559741  -0.0106292  -0.0669083  76  ARG   A N    
591  C  CA   . ARG   A 76  ? 0.165978  0.354861 0.15213   0.00323104  -0.00599565 -0.0571776  76  ARG   A CA   
592  C  C    . ARG   A 76  ? 0.146522  0.318532 0.144113  0.00040167  0.0016223   -0.0647994  76  ARG   A C    
593  O  O    . ARG   A 76  ? 0.152871  0.316902 0.137462  0.00164582  0.00281885  -0.0652995  76  ARG   A O    
594  C  CB   . ARG   A 76  ? 0.187525  0.40022  0.177343  0.0140746   0.0188169   -0.0657468  76  ARG   A CB   
595  C  CG   . ARG   A 76  ? 0.209235  0.456483 0.201662  0.0245709   0.0197972   -0.05598    76  ARG   A CG   
596  C  CD   . ARG   A 76  ? 0.214464  0.513833 0.280484  0.0342278   0.0479965   -0.0606886  76  ARG   A CD   
597  N  NE   . ARG   A 76  ? 0.311556  0.565137 0.332632  0.0450385   0.0401359   -0.0438492  76  ARG   A NE   
598  C  CZ   . ARG   A 76  ? 0.38314   0.607401 0.417427  0.0441971   0.0404007   -0.0612985  76  ARG   A CZ   
599  N  NH1  . ARG   A 76  ? 0.436097  0.649214 0.428933  0.0241377   0.0555515   -0.085968   76  ARG   A NH1  
600  N  NH2  . ARG   A 76  ? 0.391534  0.644027 0.475915  0.0538204   0.0394671   -0.067609   76  ARG   A NH2  
601  N  N    . VAL   A 77  ? 0.134779  0.315221 0.141929  -0.00017892 0.00234765  -0.0591663  77  VAL   A N    
602  C  CA   . VAL   A 77  ? 0.132329  0.304729 0.138775  -0.00031874 -0.00715929 -0.0571019  77  VAL   A CA   
603  C  C    . VAL   A 77  ? 0.146059  0.302715 0.130903  0.00518375  0.00191612  -0.0599663  77  VAL   A C    
604  O  O    . VAL   A 77  ? 0.151077  0.326139 0.127041  -0.00322358 0.0101264   -0.0613067  77  VAL   A O    
605  C  CB   . VAL   A 77  ? 0.138866  0.302867 0.136186  -0.00314843 -0.0118107  -0.0546579  77  VAL   A CB   
606  C  CG1  . VAL   A 77  ? 0.135873  0.302521 0.133949  -0.00338216 -0.0160998  -0.0543635  77  VAL   A CG1  
607  C  CG2  . VAL   A 77  ? 0.14841   0.306065 0.148203  -0.00170889 -0.0181042  -0.0576444  77  VAL   A CG2  
608  N  N    . ILE   A 78  ? 0.143934  0.302545 0.143032  0.0173924   0.0110758   -0.0497723  78  ILE   A N    
609  C  CA   . ILE   A 78  ? 0.127423  0.311331 0.178388  0.0230285   0.00057767  -0.0453191  78  ILE   A CA   
610  C  C    . ILE   A 78  ? 0.140361  0.298102 0.178854  0.0329776   -0.00550532 -0.0426968  78  ILE   A C    
611  O  O    . ILE   A 78  ? 0.179194  0.306332 0.199024  0.0390878   -0.0241567  -0.0384619  78  ILE   A O    
612  C  CB   . ILE   A 78  ? 0.1506    0.321186 0.215274  0.02376     0.00335763  -0.0486384  78  ILE   A CB   
613  C  CG1  . ILE   A 78  ? 0.156185  0.326774 0.231774  0.0198354   0.00121016  -0.0581008  78  ILE   A CG1  
614  C  CG2  . ILE   A 78  ? 0.151968  0.33765  0.215497  0.0107263   0.00301664  -0.0512568  78  ILE   A CG2  
615  C  CD1  . ILE   A 78  ? 0.165021  0.328931 0.268745  0.0294533   0.004202    -0.0581282  78  ILE   A CD1  
616  N  N    . GLY   A 79  ? 0.13044   0.294513 0.156388  0.0234418   -0.00539117 -0.0310699  79  GLY   A N    
617  C  CA   . GLY   A 79  ? 0.115797  0.296204 0.159647  0.0227411   -0.0120699  -0.034353   79  GLY   A CA   
618  C  C    . GLY   A 79  ? 0.123923  0.300873 0.155343  0.0258401   -0.00952127 -0.0307748  79  GLY   A C    
619  O  O    . GLY   A 79  ? 0.114264  0.319595 0.16221   0.0236441   -0.0221011  -0.0365821  79  GLY   A O    
620  N  N    . HIS   A 80  ? 0.130334  0.317388 0.149544  0.0349078   -0.0175872  -0.0249408  80  HIS   A N    
621  C  CA   . HIS   A 80  ? 0.133184  0.334725 0.131549  0.0427266   -0.0233753  -0.0227912  80  HIS   A CA   
622  C  C    . HIS   A 80  ? 0.145609  0.351578 0.13158   0.0564888   -0.0207457  -0.0143791  80  HIS   A C    
623  O  O    . HIS   A 80  ? 0.157816  0.377111 0.122856  0.0601994   -0.0352309  -0.0119191  80  HIS   A O    
624  C  CB   . HIS   A 80  ? 0.149133  0.336381 0.123744  0.0379529   -0.0190168  -0.0304525  80  HIS   A CB   
625  C  CG   . HIS   A 80  ? 0.163759  0.351211 0.13087   0.0199127   -0.0232142  -0.0409281  80  HIS   A CG   
626  N  ND1  . HIS   A 80  ? 0.168525  0.370951 0.15372   0.0095907   -0.0137512  -0.0455561  80  HIS   A ND1  
627  C  CD2  . HIS   A 80  ? 0.192172  0.357279 0.140437  0.01065     -0.0226263  -0.0572583  80  HIS   A CD2  
628  C  CE1  . HIS   A 80  ? 0.185078  0.371424 0.164051  0.00290309  -0.0171593  -0.0581667  80  HIS   A CE1  
629  N  NE2  . HIS   A 80  ? 0.193916  0.364564 0.149119  -0.0053043  -0.0342956  -0.0643369  80  HIS   A NE2  
630  N  N    . SER   A 81  ? 0.145554  0.352796 0.125914  0.0585092   -0.0252762  -0.00449958 81  SER   A N    
631  C  CA   . SER   A 81  ? 0.172577  0.337108 0.121413  0.0584013   -0.0345195  -0.00834685 81  SER   A CA   
632  C  C    . SER   A 81  ? 0.169279  0.324668 0.123934  0.0484638   -0.0242487  -0.00415661 81  SER   A C    
633  O  O    . SER   A 81  ? 0.182164  0.338294 0.129593  0.0786278   -0.037132   -0.0297844  81  SER   A O    
634  C  CB   . SER   A 81  ? 0.210879  0.342756 0.156989  0.0641648   -0.0343435  -0.00644659 81  SER   A CB   
635  O  OG   . SER   A 81  ? 0.229168  0.357671 0.200127  0.0457721   -0.0185371  -0.0117558  81  SER   A OG   
636  N  N    . MET   A 82  ? 0.164087  0.299806 0.120515  0.0364307   -0.0203234  0.00152583  82  MET   A N    
637  C  CA   . MET   A 82  ? 0.173918  0.293489 0.147722  0.0317843   -0.00494558 0.0036871   82  MET   A CA   
638  C  C    . MET   A 82  ? 0.171457  0.281187 0.144606  0.0407717   0.00444291  0.0123462   82  MET   A C    
639  O  O    . MET   A 82  ? 0.183224  0.299319 0.166392  0.0506744   0.0296982   0.0314509   82  MET   A O    
640  C  CB   . MET   A 82  ? 0.188357  0.314649 0.191045  0.0184793   -0.0129244  -0.0035035  82  MET   A CB   
641  C  CG   . MET   A 82  ? 0.192119  0.315464 0.200367  0.025568    -0.0221178  -0.00374256 82  MET   A CG   
642  S  SD   . MET   A 82  ? 0.170972  0.338093 0.235638  0.0193689   -0.0585232  -0.0164193  82  MET   A SD   
643  C  CE   . MET   A 82  ? 0.180504  0.346066 0.251777  0.0164206   -0.0668403  -0.0157219  82  MET   A CE   
644  N  N    . GLN   A 83  ? 0.161875  0.267354 0.131212  0.0209172   0.00739554  0.0182164   83  GLN   A N    
645  C  CA   . GLN   A 83  ? 0.173338  0.27307  0.136608  0.0297221   0.00429783  0.0331906   83  GLN   A CA   
646  C  C    . GLN   A 83  ? 0.15725   0.279549 0.113617  0.0311492   0.00488962  0.033439    83  GLN   A C    
647  O  O    . GLN   A 83  ? 0.162802  0.27707  0.089747  0.0327831   -0.00390414 0.0260182   83  GLN   A O    
648  C  CB   . GLN   A 83  ? 0.179387  0.283976 0.160424  0.0260129   -0.00762864 0.0364998   83  GLN   A CB   
649  C  CG   . GLN   A 83  ? 0.181683  0.30008  0.173963  0.0226865   -0.00987353 0.0443514   83  GLN   A CG   
650  C  CD   . GLN   A 83  ? 0.20823   0.314594 0.238074  0.00974249  -0.0114453  0.0378052   83  GLN   A CD   
651  O  OE1  . GLN   A 83  ? 0.214405  0.372158 0.268982  0.0175427   -0.0359164  0.0438456   83  GLN   A OE1  
652  N  NE2  . GLN   A 83  ? 0.233514  0.3404   0.277038  -0.0036553  -0.00938291 0.0393295   83  GLN   A NE2  
653  N  N    . ASN   A 84  ? 0.162125  0.272845 0.110451  0.0265299   -0.00372195 0.0257816   84  ASN   A N    
654  C  CA   . ASN   A 84  ? 0.143639  0.283011 0.103026  0.0215548   -0.00351549 0.0202247   84  ASN   A CA   
655  C  C    . ASN   A 84  ? 0.129752  0.275169 0.0828494 0.0194374   -0.00521488 0.0117209   84  ASN   A C    
656  O  O    . ASN   A 84  ? 0.122674  0.293622 0.0964497 0.0234627   -0.00910998 0.0204928   84  ASN   A O    
657  C  CB   . ASN   A 84  ? 0.151376  0.286613 0.105893  0.0162599   -0.007841   0.0273236   84  ASN   A CB   
658  C  CG   . ASN   A 84  ? 0.165493  0.293312 0.107095  0.021333    -0.00363477 0.0338491   84  ASN   A CG   
659  O  OD1  . ASN   A 84  ? 0.195847  0.329533 0.114519  0.0275354   -0.0120549  0.04513     84  ASN   A OD1  
660  N  ND2  . ASN   A 84  ? 0.174366  0.293126 0.0981964 0.0242153   -0.00143541 0.0382446   84  ASN   A ND2  
661  N  N    . CYS   A 85  ? 0.116878  0.26727  0.065198  0.015648    -0.00021632 0.00738526  85  CYS   A N    
662  C  CA   . CYS   A 85  ? 0.120369  0.268212 0.0721388 0.0176767   -0.0154775  0.00522845  85  CYS   A CA   
663  C  C    . CYS   A 85  ? 0.10659   0.258343 0.0725957 0.0199131   -0.00693527 0.00913929  85  CYS   A C    
664  O  O    . CYS   A 85  ? 0.0989564 0.251657 0.0605518 0.0203258   -0.00928657 0.00925813  85  CYS   A O    
665  C  CB   . CYS   A 85  ? 0.138887  0.282252 0.0765517 0.0182185   -0.0126087  0.00206427  85  CYS   A CB   
666  S  SG   . CYS   A 85  ? 0.153004  0.304681 0.0842615 0.0167022   0.00385893  -0.0179185  85  CYS   A SG   
667  N  N    A VAL   A 86  ? 0.123649  0.265778 0.0701615 0.0211036   -0.0127004  0.00785823  86  VAL   A N    
668  N  N    B VAL   A 86  ? 0.121061  0.265945 0.0566783 0.0215279   -0.00899105 0.00371754  86  VAL   A N    
669  C  CA   A VAL   A 86  ? 0.143765  0.270279 0.0755766 0.0256088   -0.00651963 0.00363693  86  VAL   A CA   
670  C  CA   B VAL   A 86  ? 0.138071  0.267567 0.0610976 0.0260658   -0.00115663 -0.00404064 86  VAL   A CA   
671  C  C    A VAL   A 86  ? 0.146723  0.268284 0.0827444 0.0316179   -0.0074813  0.00644719  86  VAL   A C    
672  C  C    B VAL   A 86  ? 0.141546  0.267492 0.075225  0.0332282   -0.00462159 0.00121275  86  VAL   A C    
673  O  O    A VAL   A 86  ? 0.158409  0.266827 0.10093   0.04172     0.00088626  0.0145199   86  VAL   A O    
674  O  O    B VAL   A 86  ? 0.15577   0.266331 0.0941399 0.0428852   0.00455563  0.0113565   86  VAL   A O    
675  C  CB   A VAL   A 86  ? 0.161554  0.279634 0.0948921 0.0184978   -0.0115069  0.0036115   86  VAL   A CB   
676  C  CB   B VAL   A 86  ? 0.148516  0.273967 0.061848  0.021451    0.00122657  -0.0103023  86  VAL   A CB   
677  C  CG1  A VAL   A 86  ? 0.169821  0.28853  0.108214  0.0198141   -0.0120278  0.00483469  86  VAL   A CG1  
678  C  CG1  B VAL   A 86  ? 0.14751   0.276603 0.0669786 0.0182743   0.00163144  -0.0167236  86  VAL   A CG1  
679  C  CG2  A VAL   A 86  ? 0.162036  0.27945  0.104843  0.0153349   -0.0113114  0.00335398  86  VAL   A CG2  
680  C  CG2  B VAL   A 86  ? 0.154094  0.278659 0.0681564 0.0227991   0.00500627  -0.0121243  86  VAL   A CG2  
681  N  N    . LEU   A 87  ? 0.145885  0.25864  0.07778   0.0277308   -0.0113312  -0.0016834  87  LEU   A N    
682  C  CA   . LEU   A 87  ? 0.140374  0.268099 0.0918489 0.026313    -0.0152101  -0.00300265 87  LEU   A CA   
683  C  C    . LEU   A 87  ? 0.123215  0.265395 0.0981926 0.0245906   -0.0169024  -0.00416233 87  LEU   A C    
684  O  O    . LEU   A 87  ? 0.11974   0.265958 0.083483  0.0248902   -0.01623    -0.0115802  87  LEU   A O    
685  C  CB   . LEU   A 87  ? 0.163085  0.277326 0.134544  0.0173011   -0.0125268  -0.0103308  87  LEU   A CB   
686  C  CG   . LEU   A 87  ? 0.17673   0.296232 0.163967  0.0227051   -0.00273369 -0.0221522  87  LEU   A CG   
687  C  CD1  . LEU   A 87  ? 0.175506  0.312496 0.184421  0.0184866   -0.00362142 -0.0172222  87  LEU   A CD1  
688  C  CD2  . LEU   A 87  ? 0.171216  0.29773  0.184395  0.0204404   -0.00012064 -0.0192123  87  LEU   A CD2  
689  N  N    . LYS   A 88  ? 0.120923  0.273862 0.10195   0.0240464   -0.0195241  -0.0122595  88  LYS   A N    
690  C  CA   . LYS   A 88  ? 0.11625   0.281756 0.117211  0.0180764   -0.0179306  -0.0139655  88  LYS   A CA   
691  C  C    . LYS   A 88  ? 0.117374  0.289968 0.105515  0.0261327   -0.0150015  -0.0147571  88  LYS   A C    
692  O  O    . LYS   A 88  ? 0.115499  0.332563 0.110895  0.0370072   -0.0081601  -0.0112925  88  LYS   A O    
693  C  CB   . LYS   A 88  ? 0.141957  0.287998 0.134648  0.0107675   -0.0248452  -0.00450418 88  LYS   A CB   
694  C  CG   . LYS   A 88  ? 0.15827   0.299129 0.148403  0.00100821  -0.01886    0.00195821  88  LYS   A CG   
695  C  CD   . LYS   A 88  ? 0.20641   0.310108 0.213267  -0.0090008  -0.0122237  0.00705332  88  LYS   A CD   
696  C  CE   . LYS   A 88  ? 0.246491  0.324868 0.231565  -0.011843   -0.0051237  0.0203408   88  LYS   A CE   
697  N  NZ   . LYS   A 88  ? 0.286806  0.331759 0.272639  -0.012426   0.013103    0.0277395   88  LYS   A NZ   
698  N  N    . LEU   A 89  ? 0.097145  0.282191 0.100705  0.0205127   -0.0155989  -0.0214119  89  LEU   A N    
699  C  CA   . LEU   A 89  ? 0.0924652 0.276324 0.116442  0.0181968   -0.012424   -0.0261193  89  LEU   A CA   
700  C  C    . LEU   A 89  ? 0.102878  0.283614 0.124185  0.0189647   0.00103091  -0.0336248  89  LEU   A C    
701  O  O    . LEU   A 89  ? 0.109334  0.307419 0.147968  0.0233456   -0.00987648 -0.0474018  89  LEU   A O    
702  C  CB   . LEU   A 89  ? 0.102741  0.27359  0.119919  0.0152041   -0.00836553 -0.0247394  89  LEU   A CB   
703  C  CG   . LEU   A 89  ? 0.122176  0.260677 0.140755  0.0186733   -0.0039325  -0.0165917  89  LEU   A CG   
704  C  CD1  . LEU   A 89  ? 0.136774  0.268375 0.142146  0.0161515   -0.00053742 -0.0133303  89  LEU   A CD1  
705  C  CD2  . LEU   A 89  ? 0.134443  0.258344 0.139227  0.0114739   -0.00793173 -0.018751   89  LEU   A CD2  
706  N  N    . LYS   A 90  ? 0.124638  0.282766 0.126388  0.0227074   -0.0155319  -0.0381734  90  LYS   A N    
707  C  CA   . LYS   A 90  ? 0.125055  0.287099 0.144157  0.0138113   -0.00379663 -0.0467048  90  LYS   A CA   
708  C  C    . LYS   A 90  ? 0.121342  0.282944 0.151409  0.00746843  0.00422504  -0.0486276  90  LYS   A C    
709  O  O    . LYS   A 90  ? 0.139848  0.30104  0.135654  -0.00273693 -0.00274026 -0.0643932  90  LYS   A O    
710  C  CB   . LYS   A 90  ? 0.132948  0.3083   0.183335  0.0185221   -0.0225301  -0.0425041  90  LYS   A CB   
711  C  CG   . LYS   A 90  ? 0.199116  0.340845 0.223356  0.0156769   -0.0191612  -0.0525386  90  LYS   A CG   
712  C  CD   . LYS   A 90  ? 0.267588  0.387064 0.30183   0.0275026   -0.029212   -0.0401659  90  LYS   A CD   
713  C  CE   . LYS   A 90  ? 0.348751  0.424626 0.352965  0.0299335   -0.0260676  -0.0503038  90  LYS   A CE   
714  N  NZ   . LYS   A 90  ? 0.39291   0.47718  0.412192  0.0500618   -0.0281008  -0.0279283  90  LYS   A NZ   
715  N  N    . VAL   A 91  ? 0.114059  0.276394 0.14721   -0.00243934 0.0115818   -0.0521454  91  VAL   A N    
716  C  CA   . VAL   A 91  ? 0.125174  0.282186 0.151838  -0.00582178 0.00486161  -0.051002   91  VAL   A CA   
717  C  C    . VAL   A 91  ? 0.132354  0.291093 0.165055  -0.005024   -0.00325825 -0.0584275  91  VAL   A C    
718  O  O    . VAL   A 91  ? 0.141294  0.27811  0.154753  0.00598807  -0.00550479 -0.0601407  91  VAL   A O    
719  C  CB   . VAL   A 91  ? 0.13855   0.268598 0.15502   -0.00800737 0.00884303  -0.0469708  91  VAL   A CB   
720  C  CG1  . VAL   A 91  ? 0.147816  0.270537 0.165522  -0.0076142  0.00680743  -0.0452852  91  VAL   A CG1  
721  C  CG2  . VAL   A 91  ? 0.140198  0.271425 0.153761  -0.00704113 0.00108159  -0.0461755  91  VAL   A CG2  
722  N  N    . ASP   A 92  ? 0.134721  0.323076 0.170249  0.00310724  0.00512904  -0.0691959  92  ASP   A N    
723  C  CA   . ASP   A 92  ? 0.139884  0.363089 0.194418  0.00793264  0.0157503   -0.085436   92  ASP   A CA   
724  C  C    . ASP   A 92  ? 0.146899  0.374005 0.192651  0.0150428   0.0128348   -0.0997809  92  ASP   A C    
725  O  O    . ASP   A 92  ? 0.173914  0.419367 0.244709  0.0422013   0.013376    -0.1335     92  ASP   A O    
726  C  CB   . ASP   A 92  ? 0.155092  0.398943 0.232729  -0.00870164 0.0342027   -0.0889921  92  ASP   A CB   
727  C  CG   . ASP   A 92  ? 0.210393  0.434663 0.293308  0.00100485  0.0437929   -0.0775239  92  ASP   A CG   
728  O  OD1  . ASP   A 92  ? 0.27257   0.465322 0.356181  0.0118588   0.0435114   -0.0590941  92  ASP   A OD1  
729  O  OD2  . ASP   A 92  ? 0.237777  0.529499 0.389862  -0.0345466  0.0849997   -0.0710368  92  ASP   A OD2  
730  N  N    . THR   A 93  ? 0.145229  0.351911 0.180522  0.0162149   0.012468    -0.090239   93  THR   A N    
731  C  CA   . THR   A 93  ? 0.146296  0.342461 0.172975  0.0165335   0.0113665   -0.0744668  93  THR   A CA   
732  C  C    . THR   A 93  ? 0.144941  0.311982 0.162219  0.0182761   0.0122314   -0.0708075  93  THR   A C    
733  O  O    . THR   A 93  ? 0.150247  0.30982  0.160249  0.0123076   0.0155432   -0.0750859  93  THR   A O    
734  C  CB   . THR   A 93  ? 0.165632  0.365615 0.165928  0.00280888  0.0209638   -0.0568446  93  THR   A CB   
735  O  OG1  . THR   A 93  ? 0.17061   0.413022 0.217707  -0.0219601  0.00684081  -0.0391423  93  THR   A OG1  
736  C  CG2  . THR   A 93  ? 0.175068  0.378087 0.178876  -0.00018335 0.0171199   -0.0492579  93  THR   A CG2  
737  N  N    . ALA   A 94  ? 0.12411   0.296532 0.152511  0.0257249   0.0146037   -0.0585874  94  ALA   A N    
738  C  CA   . ALA   A 94  ? 0.126046  0.281245 0.14633   0.029411    0.0143184   -0.0518189  94  ALA   A CA   
739  C  C    . ALA   A 94  ? 0.136412  0.277352 0.139853  0.0325926   0.0170616   -0.0441025  94  ALA   A C    
740  O  O    . ALA   A 94  ? 0.146296  0.274184 0.136233  0.0344236   0.022087    -0.042057   94  ALA   A O    
741  C  CB   . ALA   A 94  ? 0.139884  0.2926   0.155428  0.0168494   0.00682318  -0.049795   94  ALA   A CB   
742  N  N    . ASN   A 95  ? 0.111442  0.250664 0.133609  0.0310316   0.00462467  -0.0333151  95  ASN   A N    
743  C  CA   . ASN   A 95  ? 0.121555  0.228889 0.129681  0.0240645   0.00264442  -0.0353838  95  ASN   A CA   
744  C  C    . ASN   A 95  ? 0.137288  0.231899 0.125561  0.0197128   -0.00193709 -0.0377834  95  ASN   A C    
745  O  O    . ASN   A 95  ? 0.140955  0.22324  0.146579  0.010008    -0.00343611 -0.0504447  95  ASN   A O    
746  C  CB   . ASN   A 95  ? 0.123806  0.221377 0.10829   0.0288888   -0.00363114 -0.0315211  95  ASN   A CB   
747  C  CG   . ASN   A 95  ? 0.134193  0.224837 0.106703  0.026819    -0.0117615  -0.0350526  95  ASN   A CG   
748  O  OD1  . ASN   A 95  ? 0.164134  0.22237  0.104414  0.0302273   -0.00936028 -0.026043   95  ASN   A OD1  
749  N  ND2  . ASN   A 95  ? 0.155893  0.231679 0.099707  0.0319927   -0.021199   -0.0465127  95  ASN   A ND2  
750  N  N    . PRO   A 96  ? 0.151889  0.249968 0.130983  0.0153902   -0.00018898 -0.0422722  96  PRO   A N    
751  C  CA   . PRO   A 96  ? 0.160596  0.257418 0.139158  0.0111282   0.00443755  -0.0374238  96  PRO   A CA   
752  C  C    . PRO   A 96  ? 0.160398  0.257865 0.148979  0.0120189   -0.00679509 -0.0392418  96  PRO   A C    
753  O  O    . PRO   A 96  ? 0.181781  0.281289 0.188128  -0.00739875 -0.0199242  -0.0497748  96  PRO   A O    
754  C  CB   . PRO   A 96  ? 0.181191  0.27285  0.131285  0.0166479   0.00911143  -0.0488436  96  PRO   A CB   
755  C  CG   . PRO   A 96  ? 0.178896  0.282547 0.137747  0.00819435  0.0104396   -0.0368728  96  PRO   A CG   
756  C  CD   . PRO   A 96  ? 0.160768  0.265875 0.138804  0.0108528   0.0065656   -0.0439641  96  PRO   A CD   
757  N  N    . LYS   A 97  ? 0.148657  0.24887  0.125093  0.0197716   -0.00088167 -0.0256143  97  LYS   A N    
758  C  CA   . LYS   A 97  ? 0.157259  0.25892  0.115918  0.0251696   -0.00120733 -0.0192107  97  LYS   A CA   
759  C  C    . LYS   A 97  ? 0.152714  0.24859  0.119777  0.0301886   0.00344777  -0.0202203  97  LYS   A C    
760  O  O    . LYS   A 97  ? 0.154398  0.25642  0.133776  0.0402801   0.0113736   -0.0108318  97  LYS   A O    
761  C  CB   . LYS   A 97  ? 0.173539  0.271831 0.130587  0.0355842   -0.00054557 -0.00477998 97  LYS   A CB   
762  C  CG   . LYS   A 97  ? 0.21094   0.299398 0.149141  0.0355412   0.00947272  0.00753999  97  LYS   A CG   
763  C  CD   . LYS   A 97  ? 0.25204   0.31628  0.189602  0.0424555   0.0200855   0.0194157   97  LYS   A CD   
764  C  CE   . LYS   A 97  ? 0.317441  0.35728  0.221524  0.0430374   0.0430496   0.0327722   97  LYS   A CE   
765  N  NZ   . LYS   A 97  ? 0.37135   0.386046 0.276722  0.0428168   0.0558895   0.0314315   97  LYS   A NZ   
766  N  N    . THR   A 98  ? 0.140359  0.234103 0.124782  0.0276326   0.00234443  -0.0245773  98  THR   A N    
767  C  CA   . THR   A 98  ? 0.137693  0.23866  0.133954  0.0175911   0.00341564  -0.0202808  98  THR   A CA   
768  C  C    . THR   A 98  ? 0.135336  0.226985 0.140758  0.0201069   0.0042296   -0.016693   98  THR   A C    
769  O  O    . THR   A 98  ? 0.150839  0.248464 0.159203  0.0106786   0.00103464  -0.0299985  98  THR   A O    
770  C  CB   . THR   A 98  ? 0.121006  0.247654 0.133121  0.0124462   -0.00016624 -0.0211149  98  THR   A CB   
771  O  OG1  . THR   A 98  ? 0.121125  0.248729 0.139338  0.00449346  0.00160414  -0.026728   98  THR   A OG1  
772  C  CG2  . THR   A 98  ? 0.127175  0.255968 0.139055  0.00630378  0.00052376  -0.0173195  98  THR   A CG2  
773  N  N    . PRO   A 99  ? 0.138575  0.225609 0.127544  0.0195609   0.00323552  -0.00947964 99  PRO   A N    
774  C  CA   . PRO   A 99  ? 0.154802  0.221286 0.136983  0.00929269  0.00183074  -0.00805876 99  PRO   A CA   
775  C  C    . PRO   A 99  ? 0.158456  0.223932 0.147544  0.004003    0.00480207  -0.00322839 99  PRO   A C    
776  O  O    . PRO   A 99  ? 0.147955  0.250982 0.145074  0.00066686  0.00809356  0.00156773  99  PRO   A O    
777  C  CB   . PRO   A 99  ? 0.150008  0.227773 0.150388  0.0134754   -0.00201026 -0.00512151 99  PRO   A CB   
778  C  CG   . PRO   A 99  ? 0.141976  0.22682  0.136637  0.016624    0.00157475  -0.00522338 99  PRO   A CG   
779  C  CD   . PRO   A 99  ? 0.132469  0.219796 0.129977  0.0210282   -0.00410205 -0.00671827 99  PRO   A CD   
780  N  N    . LYS   A 100 ? 0.167416  0.21679  0.159232  -0.00119382 0.00026395  -0.011736   100 LYS   A N    
781  C  CA   . LYS   A 100 ? 0.187923  0.21852  0.165256  0.00130375  0.00077565  -0.00838009 100 LYS   A CA   
782  C  C    . LYS   A 100 ? 0.173333  0.20774  0.159137  0.00950865  -0.00517918 -0.00181    100 LYS   A C    
783  O  O    . LYS   A 100 ? 0.185174  0.207578 0.15884   0.0149818   -0.00174637 0.00331357  100 LYS   A O    
784  C  CB   . LYS   A 100 ? 0.219937  0.242699 0.199043  -0.0144883  -0.00263635 -0.0111775  100 LYS   A CB   
785  C  CG   . LYS   A 100 ? 0.272852  0.277815 0.239752  -0.0125915  -0.00116878 -0.0280255  100 LYS   A CG   
786  C  CD   . LYS   A 100 ? 0.319866  0.332294 0.309119  -0.030532   -0.00284708 -0.0285352  100 LYS   A CD   
787  C  CE   . LYS   A 100 ? 0.379143  0.399963 0.370333  -0.00661341 -0.00980386 -0.0288824  100 LYS   A CE   
788  N  NZ   . LYS   A 100 ? 0.452719  0.457014 0.388337  0.00175346  -0.0238579  -0.0219347  100 LYS   A NZ   
789  N  N    . TYR   A 101 ? 0.170713  0.20735  0.152743  0.017719    -0.00565601 -0.00815695 101 TYR   A N    
790  C  CA   . TYR   A 101 ? 0.177456  0.198095 0.161841  0.0176381   -0.00964263 -0.00330415 101 TYR   A CA   
791  C  C    . TYR   A 101 ? 0.176782  0.201601 0.156744  0.0198435   -0.00823945 -0.00304716 101 TYR   A C    
792  O  O    . TYR   A 101 ? 0.191995  0.204446 0.150639  0.0209592   -0.00122519 0.00178297  101 TYR   A O    
793  C  CB   . TYR   A 101 ? 0.171292  0.197618 0.157591  0.0180169   -0.0100251  -0.0074023  101 TYR   A CB   
794  C  CG   . TYR   A 101 ? 0.17343   0.204806 0.169901  0.0125825   -0.0174366  -0.0106354  101 TYR   A CG   
795  C  CD1  . TYR   A 101 ? 0.179513  0.213286 0.169304  0.018638    -0.0201733  -0.0117909  101 TYR   A CD1  
796  C  CD2  . TYR   A 101 ? 0.187157  0.21625  0.176043  0.0113399   -0.0194287  -0.0186258  101 TYR   A CD2  
797  C  CE1  . TYR   A 101 ? 0.177306  0.229005 0.199948  0.0150097   -0.0217348  -0.00802875 101 TYR   A CE1  
798  C  CE2  . TYR   A 101 ? 0.187526  0.227178 0.192593  0.00883415  -0.0349955  -0.0134683  101 TYR   A CE2  
799  C  CZ   . TYR   A 101 ? 0.170732  0.236849 0.208316  0.0130781   -0.033193   -0.00618975 101 TYR   A CZ   
800  O  OH   . TYR   A 101 ? 0.167841  0.260847 0.265334  0.0107139   -0.0417746  0.00804584  101 TYR   A OH   
801  N  N    . LYS   A 102 ? 0.173205  0.206135 0.144751  0.0175658   -0.0100939  0.0076557   102 LYS   A N    
802  C  CA   . LYS   A 102 ? 0.171472  0.212229 0.150534  0.0145665   -0.0149664  0.018294    102 LYS   A CA   
803  C  C    . LYS   A 102 ? 0.146779  0.199522 0.137501  0.0170522   -0.0104431  0.0258242   102 LYS   A C    
804  O  O    . LYS   A 102 ? 0.155235  0.1977   0.133416  0.0138296   -0.0154406  0.0249258   102 LYS   A O    
805  C  CB   . LYS   A 102 ? 0.22195   0.241907 0.175567  -0.0106981  -0.0126077  0.0243495   102 LYS   A CB   
806  C  CG   . LYS   A 102 ? 0.247412  0.280276 0.211841  -0.0115085  -0.0156296  0.0203981   102 LYS   A CG   
807  C  CD   . LYS   A 102 ? 0.295398  0.327524 0.243032  -0.0257276  -0.0104395  0.0404936   102 LYS   A CD   
808  C  CE   . LYS   A 102 ? 0.330577  0.344098 0.266588  -0.0443789  -0.0130894  0.0374954   102 LYS   A CE   
809  N  NZ   . LYS   A 102 ? 0.356724  0.388041 0.300253  -0.0515964  -0.00123142 0.0498593   102 LYS   A NZ   
810  N  N    . PHE   A 103 ? 0.118805  0.18854  0.136395  0.0154514   -0.0111546  0.0381185   103 PHE   A N    
811  C  CA   . PHE   A 103 ? 0.126723  0.200708 0.135029  0.014125    -0.00716195 0.0360755   103 PHE   A CA   
812  C  C    . PHE   A 103 ? 0.145065  0.205635 0.133506  0.0152712   -0.00118416 0.0421876   103 PHE   A C    
813  O  O    . PHE   A 103 ? 0.174232  0.202287 0.167715  0.0248186   0.0104409   0.0433435   103 PHE   A O    
814  C  CB   . PHE   A 103 ? 0.134319  0.212914 0.138768  0.0123479   -0.0175996  0.0325864   103 PHE   A CB   
815  C  CG   . PHE   A 103 ? 0.134863  0.218016 0.137289  0.0152849   -0.0157074  0.0259004   103 PHE   A CG   
816  C  CD1  . PHE   A 103 ? 0.130412  0.21845  0.130696  0.0191819   -0.0129198  0.0229867   103 PHE   A CD1  
817  C  CD2  . PHE   A 103 ? 0.138796  0.236602 0.147265  0.0206266   -0.0190368  0.0249361   103 PHE   A CD2  
818  C  CE1  . PHE   A 103 ? 0.128027  0.221774 0.136557  0.0220874   -0.00915581 0.0168386   103 PHE   A CE1  
819  C  CE2  . PHE   A 103 ? 0.144903  0.241268 0.14835   0.0200057   -0.016598   0.0210587   103 PHE   A CE2  
820  C  CZ   . PHE   A 103 ? 0.135033  0.228384 0.151849  0.0236513   -0.0101905  0.0243748   103 PHE   A CZ   
821  N  N    . VAL   A 104 ? 0.14664   0.214004 0.119     0.0129831   -0.00164954 0.0436433   104 VAL   A N    
822  C  CA   . VAL   A 104 ? 0.142176  0.227821 0.137537  0.0158557   0.00207563  0.0484157   104 VAL   A CA   
823  C  C    . VAL   A 104 ? 0.154858  0.234466 0.130315  0.0210089   0.00723891  0.0467842   104 VAL   A C    
824  O  O    . VAL   A 104 ? 0.212042  0.234415 0.118318  0.0206824   0.0125665   0.0408074   104 VAL   A O    
825  C  CB   . VAL   A 104 ? 0.147664  0.249068 0.166642  0.0121894   -0.0048253  0.0465348   104 VAL   A CB   
826  C  CG1  . VAL   A 104 ? 0.15327   0.264179 0.180153  0.00809439  -0.00201564 0.0471484   104 VAL   A CG1  
827  C  CG2  . VAL   A 104 ? 0.160593  0.259409 0.175101  0.00960184  -0.0152905  0.0415154   104 VAL   A CG2  
828  N  N    . ARG   A 105 ? 0.132367  0.234195 0.126982  0.0222616   0.00682259  0.0482835   105 ARG   A N    
829  C  CA   . ARG   A 105 ? 0.117301  0.242012 0.125907  0.0173768   0.0105429   0.0494125   105 ARG   A CA   
830  C  C    . ARG   A 105 ? 0.120482  0.240738 0.125651  0.0176226   0.016631    0.0455871   105 ARG   A C    
831  O  O    . ARG   A 105 ? 0.143709  0.256572 0.194365  0.0198582   0.0242645   0.0708784   105 ARG   A O    
832  C  CB   . ARG   A 105 ? 0.130341  0.262523 0.123362  0.0171311   0.0095182   0.0498194   105 ARG   A CB   
833  C  CG   . ARG   A 105 ? 0.134698  0.271423 0.12276   0.0132863   0.0112458   0.0462562   105 ARG   A CG   
834  C  CD   . ARG   A 105 ? 0.14542   0.287703 0.129584  0.012534    0.00747083  0.0510707   105 ARG   A CD   
835  N  NE   . ARG   A 105 ? 0.156716  0.30038  0.128029  0.0122434   0.0157698   0.0541718   105 ARG   A NE   
836  C  CZ   . ARG   A 105 ? 0.148284  0.317028 0.123244  0.0103417   0.00932301  0.054477    105 ARG   A CZ   
837  N  NH1  . ARG   A 105 ? 0.151926  0.332768 0.0997286 0.00261067  0.00527867  0.05202     105 ARG   A NH1  
838  N  NH2  . ARG   A 105 ? 0.168404  0.336191 0.137416  0.006216    -0.00296633 0.0550109   105 ARG   A NH2  
839  N  N    . ILE   A 106 ? 0.112471  0.228469 0.0849589 0.0119558   0.00736679  0.0357485   106 ILE   A N    
840  C  CA   . ILE   A 106 ? 0.111736  0.224616 0.0740955 0.0109784   0.00286803  0.0254095   106 ILE   A CA   
841  C  C    . ILE   A 106 ? 0.122444  0.233852 0.0788621 0.00407937  6.405e-05   0.0167194   106 ILE   A C    
842  O  O    . ILE   A 106 ? 0.131024  0.260436 0.0811957 -0.00630964 0.00084433  0.0111305   106 ILE   A O    
843  C  CB   . ILE   A 106 ? 0.111929  0.222008 0.0770207 0.0126219   0.00416213  0.0248486   106 ILE   A CB   
844  C  CG1  . ILE   A 106 ? 0.131613  0.230939 0.0940743 0.00983376  0.00376536  0.0304483   106 ILE   A CG1  
845  C  CG2  . ILE   A 106 ? 0.114788  0.222488 0.0876995 0.00954568  0.00593236  0.0156279   106 ILE   A CG2  
846  C  CD1  . ILE   A 106 ? 0.149932  0.22751  0.103728  0.0113108   0.00848455  0.0328428   106 ILE   A CD1  
847  N  N    . GLN   A 107 ? 0.121068  0.23139  0.0718223 0.00702934  -0.00479108 0.0105832   107 GLN   A N    
848  C  CA   . GLN   A 107 ? 0.147118  0.235586 0.0757362 0.0125065   0.00236339  0.0116788   107 GLN   A CA   
849  C  C    . GLN   A 107 ? 0.14737   0.228215 0.0856335 0.0112258   0.00037807  0.0134371   107 GLN   A C    
850  O  O    . GLN   A 107 ? 0.156387  0.236267 0.0791702 0.0178144   0.00134227  0.0076539   107 GLN   A O    
851  C  CB   . GLN   A 107 ? 0.175435  0.250801 0.0834194 0.0158484   0.0193531   0.0246735   107 GLN   A CB   
852  C  CG   . GLN   A 107 ? 0.221362  0.262858 0.0924233 0.0291037   0.0319116   0.0294959   107 GLN   A CG   
853  C  CD   . GLN   A 107 ? 0.259414  0.298282 0.126422  0.0462927   0.0135761   0.0300452   107 GLN   A CD   
854  O  OE1  . GLN   A 107 ? 0.331517  0.323478 0.13226   0.0873667   -0.0186722  0.0265196   107 GLN   A OE1  
855  N  NE2  . GLN   A 107 ? 0.287434  0.323351 0.153312  0.0597326   0.0115897   0.0117912   107 GLN   A NE2  
856  N  N    . PRO   A 108 ? 0.165368  0.230272 0.0899502 0.0171455   -0.00529581 0.00857733  108 PRO   A N    
857  C  CA   . PRO   A 108 ? 0.178336  0.232141 0.099766  0.019106    0.00604256  0.00142753  108 PRO   A CA   
858  C  C    . PRO   A 108 ? 0.171452  0.221344 0.094804  0.0168329   0.0151502   0.00677519  108 PRO   A C    
859  O  O    . PRO   A 108 ? 0.187086  0.231526 0.108553  0.00704683  0.0163546   0.0135766   108 PRO   A O    
860  C  CB   . PRO   A 108 ? 0.200473  0.250757 0.111626  0.0235733   -0.00627513 -0.00866757 108 PRO   A CB   
861  C  CG   . PRO   A 108 ? 0.20827   0.269124 0.133456  0.0229685   -0.0170384  -0.0146138  108 PRO   A CG   
862  C  CD   . PRO   A 108 ? 0.185819  0.250069 0.110759  0.0217666   -0.026212   -0.00435964 108 PRO   A CD   
863  N  N    . GLY   A 109 ? 0.149323  0.219128 0.0919888 0.014232    0.0289305   0.0131374   109 GLY   A N    
864  C  CA   . GLY   A 109 ? 0.146219  0.222644 0.105966  0.0133404   0.0276315   0.00800434  109 GLY   A CA   
865  C  C    . GLY   A 109 ? 0.125385  0.210799 0.100231  0.0177574   0.016446    0.0094528   109 GLY   A C    
866  O  O    . GLY   A 109 ? 0.112842  0.245559 0.114801  0.0147356   0.00677851  -0.014295   109 GLY   A O    
867  N  N    . GLN   A 110 ? 0.11423   0.194763 0.0867662 0.0108765   0.0146845   0.00925545  110 GLN   A N    
868  C  CA   . GLN   A 110 ? 0.11712   0.177692 0.0891866 0.0060096   0.0120087   0.00961751  110 GLN   A CA   
869  C  C    . GLN   A 110 ? 0.114632  0.17727  0.0832562 0.00809289  0.00669224  0.00857211  110 GLN   A C    
870  O  O    . GLN   A 110 ? 0.134131  0.187803 0.0641919 0.0101633   -0.00062309 0.00801006  110 GLN   A O    
871  C  CB   . GLN   A 110 ? 0.119896  0.177263 0.096551  0.00607308  0.00357801  0.00864058  110 GLN   A CB   
872  C  CG   . GLN   A 110 ? 0.121441  0.174432 0.0998003 0.0053024   0.00046694  0.00857127  110 GLN   A CG   
873  C  CD   . GLN   A 110 ? 0.123139  0.177998 0.109894  0.00503373  -0.009215   0.00915287  110 GLN   A CD   
874  O  OE1  . GLN   A 110 ? 0.134548  0.181534 0.117714  0.00448252  -0.0197514  0.00948469  110 GLN   A OE1  
875  N  NE2  . GLN   A 110 ? 0.117159  0.186185 0.116436  -0.00033571 -0.0181405  0.0139841   110 GLN   A NE2  
876  N  N    . THR   A 111 ? 0.125949  0.179116 0.0787118 0.00905265  0.00709305  0.0106832   111 THR   A N    
877  C  CA   . THR   A 111 ? 0.130003  0.174206 0.0818722 0.0114966   0.00915815  0.00953468  111 THR   A CA   
878  C  C    . THR   A 111 ? 0.119718  0.176506 0.0722107 0.00844389  0.00447166  0.010926    111 THR   A C    
879  O  O    . THR   A 111 ? 0.12452   0.178717 0.0678266 0.00971106  0.0165225   0.0123854   111 THR   A O    
880  C  CB   . THR   A 111 ? 0.136084  0.178415 0.0870871 0.0173113   0.00960808  0.0121178   111 THR   A CB   
881  O  OG1  . THR   A 111 ? 0.13235   0.179772 0.0913932 0.0149271   0.0123952   0.00705386  111 THR   A OG1  
882  C  CG2  . THR   A 111 ? 0.136254  0.182638 0.0842432 0.0211903   0.00560593  0.0104504   111 THR   A CG2  
883  N  N    . PHE   A 112 ? 0.115225  0.184504 0.074407  0.00705731  0.0104977   0.00746346  112 PHE   A N    
884  C  CA   . PHE   A 112 ? 0.105777  0.187161 0.0736362 0.00585236  0.00553705  0.00384429  112 PHE   A CA   
885  C  C    . PHE   A 112 ? 0.0995323 0.176391 0.0668761 0.00516773  -0.00312245 -0.00230744 112 PHE   A C    
886  O  O    . PHE   A 112 ? 0.11161   0.180481 0.0581924 0.010061    0.00437479  -0.00631763 112 PHE   A O    
887  C  CB   . PHE   A 112 ? 0.110293  0.19643  0.0738744 -0.0003522  0.00731068  0.0028      112 PHE   A CB   
888  C  CG   . PHE   A 112 ? 0.130006  0.208933 0.0758073 -0.00820429 0.00717353  -0.00228821 112 PHE   A CG   
889  C  CD1  . PHE   A 112 ? 0.161641  0.230393 0.0809473 -0.0219992  0.0146685   -0.00670686 112 PHE   A CD1  
890  C  CD2  . PHE   A 112 ? 0.139108  0.219472 0.092284  -0.0223167  -0.00187242 -0.00742247 112 PHE   A CD2  
891  C  CE1  . PHE   A 112 ? 0.194966  0.24454  0.0889327 -0.030417   0.0124329   -0.017892   112 PHE   A CE1  
892  C  CE2  . PHE   A 112 ? 0.176205  0.228516 0.0990246 -0.034872   0.00667458  -0.0123413  112 PHE   A CE2  
893  C  CZ   . PHE   A 112 ? 0.192383  0.240767 0.096445  -0.0370601  0.00319586  -0.0211242  112 PHE   A CZ   
894  N  N    . SER   A 113 ? 0.106332  0.181459 0.0767264 -0.00063493 0.00727862  -0.0001448  113 SER   A N    
895  C  CA   . SER   A 113 ? 0.11135   0.181097 0.0814845 -0.00347889 -0.00404049 0.00150138  113 SER   A CA   
896  C  C    . SER   A 113 ? 0.110615  0.177063 0.0842556 0.00293818  -0.00142056 0.00129156  113 SER   A C    
897  O  O    . SER   A 113 ? 0.128362  0.178966 0.10508   0.0117947   -0.00752956 0.0108288   113 SER   A O    
898  C  CB   . SER   A 113 ? 0.119808  0.19076  0.081103  -0.00467412 -0.00203992 0.00042583  113 SER   A CB   
899  O  OG   . SER   A 113 ? 0.124836  0.201429 0.0848862 -0.0111462  -0.0118248  -0.00278118 113 SER   A OG   
900  N  N    . VAL   A 114 ? 0.110007  0.174852 0.0844909 0.00230625  -0.00871553 0.00562876  114 VAL   A N    
901  C  CA   . VAL   A 114 ? 0.120913  0.177925 0.0808466 0.0003744   -0.0113759  0.00973388  114 VAL   A CA   
902  C  C    . VAL   A 114 ? 0.112314  0.179813 0.0841496 0.0037874   -0.00316287 0.012961    114 VAL   A C    
903  O  O    . VAL   A 114 ? 0.1084    0.194744 0.0769053 0.00331849  0.00060878  0.0163757   114 VAL   A O    
904  C  CB   . VAL   A 114 ? 0.149281  0.185871 0.0887965 -0.0005038  -0.0153525  0.0067391   114 VAL   A CB   
905  C  CG1  . VAL   A 114 ? 0.155469  0.190966 0.100112  -0.00410722 -0.0252598  -0.00097078 114 VAL   A CG1  
906  C  CG2  . VAL   A 114 ? 0.16422   0.199801 0.0907926 -0.00166757 -0.0194588  0.00844404  114 VAL   A CG2  
907  N  N    . LEU   A 115 ? 0.113566  0.178079 0.0745252 0.00565264  -0.00128011 0.0114169   115 LEU   A N    
908  C  CA   . LEU   A 115 ? 0.116437  0.178975 0.0777982 0.0072198   0.00180579  0.0140914   115 LEU   A CA   
909  C  C    . LEU   A 115 ? 0.117486  0.180069 0.0694101 0.00564418  0.00261233  0.0120018   115 LEU   A C    
910  O  O    . LEU   A 115 ? 0.124371  0.184673 0.0729354 0.00935777  -0.00398852 0.0113022   115 LEU   A O    
911  C  CB   . LEU   A 115 ? 0.120758  0.183081 0.0862557 0.0087821   -0.00450553 0.0110132   115 LEU   A CB   
912  C  CG   . LEU   A 115 ? 0.128567  0.198175 0.0832736 0.0100966   -0.00537589 0.00683634  115 LEU   A CG   
913  C  CD1  . LEU   A 115 ? 0.134917  0.205413 0.0771205 0.0100115   -0.00738132 0.0053773   115 LEU   A CD1  
914  C  CD2  . LEU   A 115 ? 0.134522  0.204062 0.0925666 0.0154137   -0.0050292  0.00844425  115 LEU   A CD2  
915  N  N    . ALA   A 116 ? 0.114953  0.186336 0.0685398 0.00262984  0.00762381  0.00845737  116 ALA   A N    
916  C  CA   . ALA   A 116 ? 0.121119  0.201668 0.0772297 -0.00219643 0.00704737  0.0129414   116 ALA   A CA   
917  C  C    . ALA   A 116 ? 0.119851  0.214358 0.0726887 -0.0117502  0.00580298  0.0118171   116 ALA   A C    
918  O  O    . ALA   A 116 ? 0.132493  0.254742 0.0750716 -0.00711534 0.00024254  0.0164955   116 ALA   A O    
919  C  CB   . ALA   A 116 ? 0.136754  0.20485  0.0959541 -0.00259468 0.00820799  0.00872868  116 ALA   A CB   
920  N  N    . CYS   A 117 ? 0.119943  0.212966 0.0655253 -0.0108674  0.0109931   0.0128078   117 CYS   A N    
921  C  CA   . CYS   A 117 ? 0.123435  0.215804 0.0787158 -0.0139989  0.0155939   0.00429681  117 CYS   A CA   
922  C  C    . CYS   A 117 ? 0.121224  0.211907 0.0752127 -0.0108419  0.00542959  0.00508214  117 CYS   A C    
923  O  O    . CYS   A 117 ? 0.126744  0.214502 0.0761434 -0.00693021 -0.00349373 0.00941926  117 CYS   A O    
924  C  CB   . CYS   A 117 ? 0.145749  0.223084 0.0984557 -0.00784403 0.0194914   0.00409721  117 CYS   A CB   
925  S  SG   . CYS   A 117 ? 0.159751  0.24746  0.128984  -0.00732356 0.00499454  -0.00549256 117 CYS   A SG   
926  N  N    . TYR   A 118 ? 0.131678  0.218246 0.075273  -0.0112911  0.00726992  0.00950359  118 TYR   A N    
927  C  CA   . TYR   A 118 ? 0.143205  0.224003 0.0897882 -0.0125326  0.00833186  0.00488945  118 TYR   A CA   
928  C  C    . TYR   A 118 ? 0.155074  0.246418 0.0948283 -0.0114157  0.0124477   -0.00146047 118 TYR   A C    
929  O  O    . TYR   A 118 ? 0.172009  0.245379 0.0918223 -0.014677   0.0112877   -0.0113617  118 TYR   A O    
930  C  CB   . TYR   A 118 ? 0.147226  0.220862 0.097426  -0.00939142 0.00704776  0.00448506  118 TYR   A CB   
931  C  CG   . TYR   A 118 ? 0.144338  0.207125 0.105591  -0.00676606 0.00330875  -0.0021711  118 TYR   A CG   
932  C  CD1  . TYR   A 118 ? 0.145714  0.212351 0.11632   -0.0143771  -0.00724543 -0.00574493 118 TYR   A CD1  
933  C  CD2  . TYR   A 118 ? 0.146628  0.212725 0.106657  -0.00548077 -0.00180186 -0.00763095 118 TYR   A CD2  
934  C  CE1  . TYR   A 118 ? 0.149049  0.212204 0.112084  -0.00885305 -0.00728656 -0.00752348 118 TYR   A CE1  
935  C  CE2  . TYR   A 118 ? 0.132723  0.20523  0.107829  -0.00378659 -0.00445359 -0.0138409  118 TYR   A CE2  
936  C  CZ   . TYR   A 118 ? 0.14081   0.212792 0.10713   -0.00490995 -0.00119878 -0.0112618  118 TYR   A CZ   
937  O  OH   . TYR   A 118 ? 0.147789  0.229253 0.0994458 0.00090289  0.00085289  -0.0110034  118 TYR   A OH   
938  N  N    . ASN   A 119 ? 0.159911  0.268184 0.109029  -0.00831679 0.0074154   -0.00224436 119 ASN   A N    
939  C  CA   . ASN   A 119 ? 0.160712  0.283096 0.124462  -0.0105031  0.0177012   0.00524017  119 ASN   A CA   
940  C  C    . ASN   A 119 ? 0.147568  0.283241 0.115543  -0.00068553 0.0185941   0.00020183  119 ASN   A C    
941  O  O    . ASN   A 119 ? 0.167232  0.319685 0.121358  0.0020841   0.0317147   0.00778818  119 ASN   A O    
942  C  CB   . ASN   A 119 ? 0.194751  0.297637 0.15425   -0.0182049  0.0183006   0.0152657   119 ASN   A CB   
943  C  CG   . ASN   A 119 ? 0.229773  0.310745 0.197814  -0.0224753  0.0120548   0.0178996   119 ASN   A CG   
944  O  OD1  . ASN   A 119 ? 0.292773  0.317377 0.263678  -0.00080286 0.019542    0.0160929   119 ASN   A OD1  
945  N  ND2  . ASN   A 119 ? 0.254207  0.336785 0.217284  -0.0301997  -0.00793908 0.0250268   119 ASN   A ND2  
946  N  N    . GLY   A 120 ? 0.144918  0.272704 0.098447  0.00688815  0.0116955   0.00087932  120 GLY   A N    
947  C  CA   . GLY   A 120 ? 0.15185   0.274721 0.104334  0.00805143  0.0235363   -0.0003596  120 GLY   A CA   
948  C  C    . GLY   A 120 ? 0.163726  0.276949 0.103329  0.00202538  0.021622    -0.0102973  120 GLY   A C    
949  O  O    . GLY   A 120 ? 0.194813  0.287732 0.121357  -0.00990972 0.0106289   -0.0140374  120 GLY   A O    
950  N  N    . SER   A 121 ? 0.152174  0.286387 0.103172  -0.0020466  0.0107462   -0.00178106 121 SER   A N    
951  C  CA   . SER   A 121 ? 0.153893  0.302732 0.118897  -0.011014   0.00786725  -0.0107015  121 SER   A CA   
952  C  C    . SER   A 121 ? 0.158836  0.285879 0.120556  -0.0206272  0.0147154   -0.00699278 121 SER   A C    
953  O  O    . SER   A 121 ? 0.14386   0.274339 0.107315  -0.0262425  0.0138068   -0.00337676 121 SER   A O    
954  C  CB   . SER   A 121 ? 0.172062  0.331241 0.140717  -0.0115378  0.0106443   0.00453414  121 SER   A CB   
955  O  OG   . SER   A 121 ? 0.209094  0.392789 0.164535  0.00354458  0.0180425   -0.0053911  121 SER   A OG   
956  N  N    . PRO   A 122 ? 0.175466  0.302386 0.113057  -0.0381254  0.0113015   -0.00288684 122 PRO   A N    
957  C  CA   . PRO   A 122 ? 0.175135  0.307118 0.11595   -0.038886   0.00681588  0.00356351  122 PRO   A CA   
958  C  C    . PRO   A 122 ? 0.167297  0.312678 0.0962532 -0.0320028  -0.00408388 0.0254363   122 PRO   A C    
959  O  O    . PRO   A 122 ? 0.181024  0.3522   0.0983368 -0.0384154  -0.00628523 0.0420226   122 PRO   A O    
960  C  CB   . PRO   A 122 ? 0.186503  0.312516 0.1563    -0.0480227  0.0124526   0.00038273  122 PRO   A CB   
961  C  CG   . PRO   A 122 ? 0.209024  0.325327 0.15811   -0.0392811  0.0093507   -0.00217975 122 PRO   A CG   
962  C  CD   . PRO   A 122 ? 0.209204  0.318437 0.170526  -0.0426937  0.0228727   -0.0183     122 PRO   A CD   
963  N  N    . SER   A 123 ? 0.155414  0.292601 0.0928436 -0.0265433  -0.00643294 0.0383363   123 SER   A N    
964  C  CA   . SER   A 123 ? 0.171989  0.285389 0.120733  -0.0263685  -0.0069253  0.0467876   123 SER   A CA   
965  C  C    . SER   A 123 ? 0.159984  0.251972 0.102775  -0.0164292  -0.0145775  0.0476011   123 SER   A C    
966  O  O    . SER   A 123 ? 0.161171  0.265845 0.118261  -0.0102639  -0.0206291  0.0550228   123 SER   A O    
967  C  CB   . SER   A 123 ? 0.207264  0.300113 0.169971  -0.0312103  -0.0159214  0.0357638   123 SER   A CB   
968  O  OG   . SER   A 123 ? 0.29448   0.337233 0.249301  -0.0282231  -0.0331346  0.0435373   123 SER   A OG   
969  N  N    . GLY   A 124 ? 0.13788   0.22463  0.103591  -0.0114289  -0.0153384  0.0415764   124 GLY   A N    
970  C  CA   . GLY   A 124 ? 0.137862  0.21995  0.0995276 -0.00342292 -0.00776283 0.0393741   124 GLY   A CA   
971  C  C    . GLY   A 124 ? 0.126429  0.211075 0.0873801 0.00421187  -0.0179374  0.0328884   124 GLY   A C    
972  O  O    . GLY   A 124 ? 0.120572  0.228714 0.0904082 0.000964    -0.0221487  0.042015    124 GLY   A O    
973  N  N    . VAL   A 125 ? 0.126123  0.208181 0.0828813 0.00527253  -0.0252363  0.0171015   125 VAL   A N    
974  C  CA   . VAL   A 125 ? 0.130512  0.205187 0.100976  0.00903033  -0.0186033  0.016958    125 VAL   A CA   
975  C  C    . VAL   A 125 ? 0.134108  0.215515 0.0824748 0.0169841   -0.0133097  0.0226454   125 VAL   A C    
976  O  O    . VAL   A 125 ? 0.138177  0.237084 0.0851408 0.0172234   -0.0233432  0.0351767   125 VAL   A O    
977  C  CB   . VAL   A 125 ? 0.171635  0.214213 0.125313  0.00579575  -0.0182942  0.00895146  125 VAL   A CB   
978  C  CG1  . VAL   A 125 ? 0.193332  0.229581 0.152105  0.00827679  -0.0276274  0.0201009   125 VAL   A CG1  
979  C  CG2  . VAL   A 125 ? 0.171683  0.21375  0.138704  -0.00151013 -0.0115877  0.00552656  125 VAL   A CG2  
980  N  N    . TYR   A 126 ? 0.115011  0.209423 0.0735291 0.0179547   -0.007703   0.0167314   126 TYR   A N    
981  C  CA   . TYR   A 126 ? 0.109264  0.208385 0.0973888 0.0113349   -0.00026295 0.014338    126 TYR   A CA   
982  C  C    . TYR   A 126 ? 0.107108  0.202516 0.109124  0.0137507   0.0116994   0.0174414   126 TYR   A C    
983  O  O    . TYR   A 126 ? 0.11265   0.201499 0.131289  0.0120363   0.0298261   0.0358668   126 TYR   A O    
984  C  CB   . TYR   A 126 ? 0.123831  0.208366 0.0949422 0.00603257  0.00477648  0.0147773   126 TYR   A CB   
985  C  CG   . TYR   A 126 ? 0.142533  0.214204 0.0915401 0.00089282  -0.00450089 -0.00212582 126 TYR   A CG   
986  C  CD1  . TYR   A 126 ? 0.152735  0.218798 0.090994  -0.00386749 -0.00746761 -0.00600165 126 TYR   A CD1  
987  C  CD2  . TYR   A 126 ? 0.155649  0.229303 0.103806  -0.00792902 -0.0070167  -0.00317552 126 TYR   A CD2  
988  C  CE1  . TYR   A 126 ? 0.166153  0.228857 0.109546  -0.00891332 -0.0165695  -0.022994   126 TYR   A CE1  
989  C  CE2  . TYR   A 126 ? 0.154564  0.234058 0.120616  -0.00901574 -0.00559668 -0.0192156  126 TYR   A CE2  
990  C  CZ   . TYR   A 126 ? 0.166151  0.234809 0.126187  -0.00810922 -0.0219131  -0.0259785  126 TYR   A CZ   
991  O  OH   . TYR   A 126 ? 0.188488  0.24836  0.174811  -0.0024374  -0.053703   -0.0502276  126 TYR   A OH   
992  N  N    . GLN   A 127 ? 0.108803  0.211526 0.11563   0.018511    0.0123992   0.0123311   127 GLN   A N    
993  C  CA   . GLN   A 127 ? 0.127375  0.206147 0.130542  0.0100092   0.00975543  0.0108447   127 GLN   A CA   
994  C  C    . GLN   A 127 ? 0.151937  0.208082 0.127736  0.0125289   0.0183443   0.00517674  127 GLN   A C    
995  O  O    . GLN   A 127 ? 0.194208  0.21235  0.126236  0.0159346   0.0174166   0.0133308   127 GLN   A O    
996  C  CB   . GLN   A 127 ? 0.126321  0.220533 0.144904  0.0114644   0.00732981  7.354e-05   127 GLN   A CB   
997  C  CG   . GLN   A 127 ? 0.131865  0.227705 0.149921  0.0119304   -0.00668721 -0.00128107 127 GLN   A CG   
998  C  CD   . GLN   A 127 ? 0.133282  0.231739 0.141974  0.0109773   -0.0270714  -0.00010359 127 GLN   A CD   
999  O  OE1  . GLN   A 127 ? 0.133198  0.231415 0.108342  0.0159557   -0.0383788  -0.00691253 127 GLN   A OE1  
1000 N  NE2  . GLN   A 127 ? 0.148239  0.236608 0.143945  0.0139207   -0.0359749  0.0136401   127 GLN   A NE2  
1001 N  N    . CYS   A 128 ? 0.16922   0.20558  0.12929   0.0104636   0.0180866   0.00463038  128 CYS   A N    
1002 C  CA   . CYS   A 128 ? 0.19115   0.219453 0.136082  0.00470387  0.00217165  -0.00378054 128 CYS   A CA   
1003 C  C    . CYS   A 128 ? 0.20322   0.213211 0.104839  0.0058368   0.0143409   -0.0138903  128 CYS   A C    
1004 O  O    . CYS   A 128 ? 0.261331  0.228226 0.102838  -0.0119427  0.0529511   -0.0187944  128 CYS   A O    
1005 C  CB   . CYS   A 128 ? 0.212816  0.261951 0.206253  -0.0102347  -0.0146489  -0.00340959 128 CYS   A CB   
1006 S  SG   . CYS   A 128 ? 0.220497  0.320952 0.379098  -0.0181712  -0.0535148  0.021928    128 CYS   A SG   
1007 N  N    . ALA   A 129 ? 0.237617  0.215382 0.0904973 0.00685221  -0.00382761 -0.00853877 129 ALA   A N    
1008 C  CA   . ALA   A 129 ? 0.205526  0.222755 0.0733724 0.00372454  -0.0035042  -0.00727363 129 ALA   A CA   
1009 C  C    . ALA   A 129 ? 0.18203   0.219137 0.0712035 0.00248957  0.0061954   -0.00958604 129 ALA   A C    
1010 O  O    . ALA   A 129 ? 0.209044  0.229291 0.0759509 0.00048562  -0.0165127  -0.00166447 129 ALA   A O    
1011 C  CB   . ALA   A 129 ? 0.212916  0.237357 0.0734681 0.00369408  -0.00713604 -0.00201529 129 ALA   A CB   
1012 N  N    . MET   A 130 ? 0.148916  0.226416 0.0549905 0.0041147   0.00789377  -0.0140226  130 MET   A N    
1013 C  CA   . MET   A 130 ? 0.140866  0.248029 0.0527899 0.00415895  0.00909735  -0.0109512  130 MET   A CA   
1014 C  C    . MET   A 130 ? 0.132465  0.240254 0.0566352 0.00190529  0.00980919  -0.00926302 130 MET   A C    
1015 O  O    . MET   A 130 ? 0.13261   0.230195 0.0775181 0.00655807  0.0163012   -0.0114496  130 MET   A O    
1016 C  CB   . MET   A 130 ? 0.149102  0.269958 0.0622    0.00847647  0.00628019  -0.0109938  130 MET   A CB   
1017 C  CG   . MET   A 130 ? 0.151925  0.297337 0.06776   0.0151591   4.052e-05   -0.00956104 130 MET   A CG   
1018 S  SD   . MET   A 130 ? 0.154344  0.355986 0.101122  0.0148453   -0.00397237 -0.0131914  130 MET   A SD   
1019 C  CE   . MET   A 130 ? 0.124564  0.33875  0.0762862 0.0219213   -0.00634685 0.00675307  130 MET   A CE   
1020 N  N    . ARG   A 131 ? 0.122908  0.239632 0.0549125 0.00535979  0.0120073   -0.00430285 131 ARG   A N    
1021 C  CA   . ARG   A 131 ? 0.120091  0.24607  0.0654965 0.0105176   0.0122117   -0.00558746 131 ARG   A CA   
1022 C  C    . ARG   A 131 ? 0.124252  0.246536 0.0719243 0.017646    0.0130843   -0.00403463 131 ARG   A C    
1023 O  O    . ARG   A 131 ? 0.138798  0.251074 0.0607862 0.0294752   0.00838306  -0.00822529 131 ARG   A O    
1024 C  CB   . ARG   A 131 ? 0.121575  0.252019 0.0714635 0.00996766  0.0120833   -0.00551561 131 ARG   A CB   
1025 C  CG   . ARG   A 131 ? 0.114753  0.258418 0.0754784 0.00783656  0.0091224   -0.00249874 131 ARG   A CG   
1026 C  CD   . ARG   A 131 ? 0.11684   0.26876  0.0681637 0.00643867  0.00631346  -0.00623338 131 ARG   A CD   
1027 N  NE   . ARG   A 131 ? 0.119343  0.276912 0.0726841 0.00838962  0.00512589  -0.0104953  131 ARG   A NE   
1028 C  CZ   . ARG   A 131 ? 0.115997  0.273595 0.0734652 0.00864607  0.00264072  -0.00424951 131 ARG   A CZ   
1029 N  NH1  . ARG   A 131 ? 0.108503  0.27296  0.0721725 0.00910972  0.00061967  -0.00196384 131 ARG   A NH1  
1030 N  NH2  . ARG   A 131 ? 0.119637  0.289046 0.0812668 0.0134693   0.00263218  -0.00312724 131 ARG   A NH2  
1031 N  N    . PRO   A 132 ? 0.133396  0.255603 0.0710795 0.0177674   0.0198204   0.00615487  132 PRO   A N    
1032 C  CA   . PRO   A 132 ? 0.134463  0.257799 0.0673848 0.0188831   0.0187714   0.00415761  132 PRO   A CA   
1033 C  C    . PRO   A 132 ? 0.124268  0.274128 0.065824  0.024866    0.0218649   0.00429066  132 PRO   A C    
1034 O  O    . PRO   A 132 ? 0.151788  0.302446 0.0969611 0.0296327   0.00379373  0.0240701   132 PRO   A O    
1035 C  CB   . PRO   A 132 ? 0.13826   0.261407 0.0684144 0.0180888   0.0211209   0.00570406  132 PRO   A CB   
1036 C  CG   . PRO   A 132 ? 0.135436  0.259563 0.0789873 0.0197053   0.0188689   0.00499935  132 PRO   A CG   
1037 C  CD   . PRO   A 132 ? 0.13549   0.254504 0.0781862 0.0195246   0.0169567   0.00693031  132 PRO   A CD   
1038 N  N    . ASN   A 133 ? 0.125317  0.280823 0.0582803 0.0115044   0.0117911   -0.0107142  133 ASN   A N    
1039 C  CA   . ASN   A 133 ? 0.12853   0.304722 0.0606664 0.00256233  0.0096273   -0.0155485  133 ASN   A CA   
1040 C  C    . ASN   A 133 ? 0.126233  0.317672 0.0755103 -0.00119481 0.0116079   -0.00773888 133 ASN   A C    
1041 O  O    . ASN   A 133 ? 0.133496  0.341312 0.0683558 -0.0170959  -0.00225755 -0.0204174  133 ASN   A O    
1042 C  CB   . ASN   A 133 ? 0.139552  0.309099 0.0856721 0.00279272  0.0161711   -0.026424   133 ASN   A CB   
1043 C  CG   . ASN   A 133 ? 0.151219  0.300279 0.102741  -0.00227367 0.0147648   -0.0249793  133 ASN   A CG   
1044 O  OD1  . ASN   A 133 ? 0.154213  0.321648 0.0972071 0.00418015  0.0116549   -0.0289872  133 ASN   A OD1  
1045 N  ND2  . ASN   A 133 ? 0.178816  0.315297 0.124515  -0.00892917 0.0221884   -0.0396479  133 ASN   A ND2  
1046 N  N    . PHE   A 134 ? 0.121238  0.313547 0.069653  0.0101164   0.00936317  -0.00403284 134 PHE   A N    
1047 C  CA   . PHE   A 134 ? 0.125785  0.317753 0.0761351 0.0169148   0.0103477   0.0153637   134 PHE   A CA   
1048 C  C    . PHE   A 134 ? 0.128649  0.314268 0.0912104 0.0142889   0.0234431   0.0133669   134 PHE   A C    
1049 O  O    . PHE   A 134 ? 0.136175  0.342875 0.165399  0.0274558   0.034087    0.0326661   134 PHE   A O    
1050 C  CB   . PHE   A 134 ? 0.125091  0.327631 0.119931  0.0215651   -0.00354546 0.0196302   134 PHE   A CB   
1051 C  CG   . PHE   A 134 ? 0.151041  0.344272 0.17149   0.0113976   -0.0182487  0.0399639   134 PHE   A CG   
1052 C  CD1  . PHE   A 134 ? 0.196786  0.354419 0.208917  0.0125079   -0.0150824  0.0520855   134 PHE   A CD1  
1053 C  CD2  . PHE   A 134 ? 0.185637  0.365821 0.191221  0.0170897   0.00251344  0.0501199   134 PHE   A CD2  
1054 C  CE1  . PHE   A 134 ? 0.22551   0.372133 0.244484  0.00030632  -0.00999512 0.0587173   134 PHE   A CE1  
1055 C  CE2  . PHE   A 134 ? 0.202237  0.362974 0.23915   0.00912534  -0.00462398 0.0657532   134 PHE   A CE2  
1056 C  CZ   . PHE   A 134 ? 0.23796   0.368022 0.245802  0.00286216  -0.0114376  0.0620471   134 PHE   A CZ   
1057 N  N    . THR   A 135 ? 0.128438  0.287854 0.0828265 0.00217717  0.0149226   0.00228822  135 THR   A N    
1058 C  CA   . THR   A 135 ? 0.122561  0.279348 0.0802322 -0.00806117 0.00632717  0.00040493  135 THR   A CA   
1059 C  C    . THR   A 135 ? 0.1207    0.257933 0.0834404 -0.0139284  0.0135366   -0.00424979 135 THR   A C    
1060 O  O    . THR   A 135 ? 0.134659  0.264096 0.0716636 -0.0235701  0.0190873   -0.00523059 135 THR   A O    
1061 C  CB   . THR   A 135 ? 0.140628  0.288705 0.0976258 -0.0106881  -0.00495885 0.00320367  135 THR   A CB   
1062 O  OG1  . THR   A 135 ? 0.152279  0.288799 0.117869  -0.00017344 -0.00307486 -0.0102278  135 THR   A OG1  
1063 C  CG2  . THR   A 135 ? 0.1587    0.307987 0.113274  -0.0146009  -0.0172396  0.00075617  135 THR   A CG2  
1064 N  N    . ILE   A 136 ? 0.119636  0.24929  0.079526  -0.00840183 0.0179867   -0.00566397 136 ILE   A N    
1065 C  CA   . ILE   A 136 ? 0.13349   0.241825 0.0864384 -0.00773279 0.0180811   -0.0144837  136 ILE   A CA   
1066 C  C    . ILE   A 136 ? 0.133575  0.235696 0.0800595 -0.0088258  0.0193709   -0.0170721  136 ILE   A C    
1067 O  O    . ILE   A 136 ? 0.140987  0.23987  0.0878623 -0.0154566  0.00985985  -0.013035   136 ILE   A O    
1068 C  CB   . ILE   A 136 ? 0.166089  0.244111 0.101107  0.00086394  0.0275308   -0.0137861  136 ILE   A CB   
1069 C  CG1  . ILE   A 136 ? 0.164033  0.236718 0.0991698 0.00269993  0.0267826   -0.0146676  136 ILE   A CG1  
1070 C  CG2  . ILE   A 136 ? 0.195984  0.245908 0.115737  0.00253923  0.0390323   -0.0151257  136 ILE   A CG2  
1071 C  CD1  . ILE   A 136 ? 0.165774  0.237878 0.0992858 0.00299011  0.0298202   -0.0146873  136 ILE   A CD1  
1072 N  N    . LYS   A 137 ? 0.135118  0.241811 0.100146  -0.00552557 0.0130003   -0.0217449  137 LYS   A N    
1073 C  CA   . LYS   A 137 ? 0.161054  0.252179 0.119345  -0.0061125  0.00865275  -0.0199428  137 LYS   A CA   
1074 C  C    . LYS   A 137 ? 0.157879  0.242297 0.120879  -0.0139213  0.0083498   -0.0268446  137 LYS   A C    
1075 O  O    . LYS   A 137 ? 0.159161  0.268795 0.128983  -0.0179558  0.004438    -0.00060031 137 LYS   A O    
1076 C  CB   . LYS   A 137 ? 0.178361  0.274455 0.150008  0.0115234   0.0112639   -0.0244696  137 LYS   A CB   
1077 C  CG   . LYS   A 137 ? 0.227579  0.317503 0.163691  0.0201545   0.0216416   -0.0288773  137 LYS   A CG   
1078 C  CD   . LYS   A 137 ? 0.267712  0.380894 0.255389  0.0332676   0.0423632   -0.0349339  137 LYS   A CD   
1079 C  CE   . LYS   A 137 ? 0.32544   0.421213 0.296563  0.0387588   0.0469359   -0.0250708  137 LYS   A CE   
1080 N  NZ   . LYS   A 137 ? 0.364691  0.474261 0.356731  0.0470964   0.0662262   -0.0364424  137 LYS   A NZ   
1081 N  N    . GLY   A 138 ? 0.164557  0.243086 0.126127  -0.0135932  0.00827343  -0.0316922  138 GLY   A N    
1082 C  CA   . GLY   A 138 ? 0.159655  0.240161 0.129832  -0.00893739 0.00745287  -0.0312813  138 GLY   A CA   
1083 C  C    . GLY   A 138 ? 0.142948  0.226022 0.12892   -0.0012887  -0.00650616 -0.0341769  138 GLY   A C    
1084 O  O    . GLY   A 138 ? 0.161688  0.220748 0.156366  -0.00720927 0.00727711  -0.0403429  138 GLY   A O    
1085 N  N    . SER   A 139 ? 0.124699  0.214528 0.108406  -0.0003952  -0.0217473  -0.0266486  139 SER   A N    
1086 C  CA   . SER   A 139 ? 0.13019   0.219931 0.124008  0.00175498  -0.0283784  -0.0235811  139 SER   A CA   
1087 C  C    . SER   A 139 ? 0.130317  0.214706 0.10804   -0.00302965 -0.0222405  -0.0260613  139 SER   A C    
1088 O  O    . SER   A 139 ? 0.134074  0.217901 0.10278   0.00359746  -0.0332968  -0.0264637  139 SER   A O    
1089 C  CB   . SER   A 139 ? 0.13777   0.231731 0.138566  0.00376744  -0.0396095  -0.0153371  139 SER   A CB   
1090 O  OG   . SER   A 139 ? 0.173221  0.240016 0.152185  0.00709336  -0.0476805  0.00045229  139 SER   A OG   
1091 N  N    . PHE   A 140 ? 0.123486  0.211617 0.100561  -0.00798141 -0.0111807  -0.0280932  140 PHE   A N    
1092 C  CA   . PHE   A 140 ? 0.128387  0.211398 0.0993986 -0.0105433  -0.00282284 -0.0261087  140 PHE   A CA   
1093 C  C    . PHE   A 140 ? 0.141182  0.212561 0.115329  -0.00813413 -0.00393444 -0.0254108  140 PHE   A C    
1094 O  O    . PHE   A 140 ? 0.148747  0.228978 0.124578  -0.00583418 0.0166529   -0.0368851  140 PHE   A O    
1095 C  CB   . PHE   A 140 ? 0.127795  0.218256 0.104931  -0.0113271  -0.00465888 -0.0268926  140 PHE   A CB   
1096 C  CG   . PHE   A 140 ? 0.144406  0.230567 0.10593   -0.026874   -0.0201183  -0.0248724  140 PHE   A CG   
1097 C  CD1  . PHE   A 140 ? 0.156392  0.226938 0.162685  -0.0270482  0.00323811  -0.0358409  140 PHE   A CD1  
1098 C  CD2  . PHE   A 140 ? 0.184045  0.243354 0.112987  -0.0311341  -0.0139322  -0.0227754  140 PHE   A CD2  
1099 C  CE1  . PHE   A 140 ? 0.17205   0.239488 0.184058  -0.0249327  -0.0098072  -0.0256433  140 PHE   A CE1  
1100 C  CE2  . PHE   A 140 ? 0.203118  0.250663 0.118852  -0.041034   -0.0208983  -0.0104136  140 PHE   A CE2  
1101 C  CZ   . PHE   A 140 ? 0.191866  0.232472 0.15187   -0.0257232  -0.0344798  -0.0136274  140 PHE   A CZ   
1102 N  N    . LEU   A 141 ? 0.143631  0.208613 0.109196  -0.00700863 0.00039569  -0.0177638  141 LEU   A N    
1103 C  CA   . LEU   A 141 ? 0.161017  0.214496 0.128625  -0.00659803 -0.00472364 -0.00929982 141 LEU   A CA   
1104 C  C    . LEU   A 141 ? 0.156338  0.205462 0.141971  -0.00626387 0.00199854  -0.00795812 141 LEU   A C    
1105 O  O    . LEU   A 141 ? 0.138964  0.204733 0.122025  -0.00300824 -0.00944302 -0.00579368 141 LEU   A O    
1106 C  CB   . LEU   A 141 ? 0.180726  0.229058 0.142481  -0.00680193 -0.00663479 0.00228968  141 LEU   A CB   
1107 C  CG   . LEU   A 141 ? 0.189971  0.25636  0.15709   -0.00616013 -0.0123517  0.0166091   141 LEU   A CG   
1108 C  CD1  . LEU   A 141 ? 0.187464  0.271182 0.156684  -0.00713049 -0.0204967  0.0198665   141 LEU   A CD1  
1109 C  CD2  . LEU   A 141 ? 0.207286  0.269699 0.15954   -0.00060316 -0.00510651 0.0168644   141 LEU   A CD2  
1110 N  N    . ASN   A 142 ? 0.168369  0.209632 0.169952  -0.00561361 -0.0073279  -0.00775395 142 ASN   A N    
1111 C  CA   . ASN   A 142 ? 0.171067  0.225738 0.179694  -0.00991376 0.00222304  -0.0127881  142 ASN   A CA   
1112 C  C    . ASN   A 142 ? 0.162644  0.218117 0.157342  -0.00969999 0.00467254  -0.00397018 142 ASN   A C    
1113 O  O    . ASN   A 142 ? 0.180058  0.243639 0.145257  -0.0176152  0.00686914  -0.0137569  142 ASN   A O    
1114 C  CB   . ASN   A 142 ? 0.193109  0.24636  0.234098  -0.0197501  -0.00410738 -0.00959741 142 ASN   A CB   
1115 C  CG   . ASN   A 142 ? 0.208051  0.295262 0.285192  -0.0172105  0.00587455  -0.00323153 142 ASN   A CG   
1116 O  OD1  . ASN   A 142 ? 0.218412  0.326545 0.298008  -0.0200728  -0.0242406  -0.0134405  142 ASN   A OD1  
1117 N  ND2  . ASN   A 142 ? 0.248329  0.34819  0.348133  -0.0252203  0.0172761   0.0353902   142 ASN   A ND2  
1118 N  N    . GLY   A 143 ? 0.14386   0.207324 0.139214  -0.00973636 0.00027366  -0.0138517  143 GLY   A N    
1119 C  CA   . GLY   A 143 ? 0.142729  0.205056 0.139814  -0.00788268 -0.00157232 -0.0124846  143 GLY   A CA   
1120 C  C    . GLY   A 143 ? 0.127699  0.197848 0.118846  -0.00374011 -0.00448869 -0.0157358  143 GLY   A C    
1121 O  O    . GLY   A 143 ? 0.137071  0.200433 0.125254  -0.00658618 0.00112029  -0.0211246  143 GLY   A O    
1122 N  N    . SER   A 144 ? 0.124022  0.196017 0.0880616 -0.00549024 -0.0109501  -0.0157037  144 SER   A N    
1123 C  CA   . SER   A 144 ? 0.128577  0.194794 0.0861698 -0.00320392 -0.00702286 -0.0100452  144 SER   A CA   
1124 C  C    . SER   A 144 ? 0.117023  0.191161 0.0793075 -0.00325413 -0.0030296  -0.0126496  144 SER   A C    
1125 O  O    . SER   A 144 ? 0.121955  0.186947 0.0637224 -0.0033736  -0.0073089  -0.0137124  144 SER   A O    
1126 C  CB   . SER   A 144 ? 0.125733  0.197733 0.0977494 -0.00314969 -0.0077029  -0.00849371 144 SER   A CB   
1127 O  OG   . SER   A 144 ? 0.120636  0.207133 0.106763  -0.00332408 0.00025879  -0.0177903  144 SER   A OG   
1128 N  N    . CYS   A 145 ? 0.12059   0.19805  0.0857759 -0.00475799 -0.00810896 -0.0125703  145 CYS   A N    
1129 C  CA   . CYS   A 145 ? 0.114649  0.2047   0.0902688 -0.00139174 -0.007518   -0.00719712 145 CYS   A CA   
1130 C  C    . CYS   A 145 ? 0.106258  0.195467 0.0746368 -0.00354959 -0.00826398 0.00045638  145 CYS   A C    
1131 O  O    . CYS   A 145 ? 0.113986  0.201469 0.0716093 -0.0081867  -0.00175778 0.00186728  145 CYS   A O    
1132 C  CB   . CYS   A 145 ? 0.129339  0.215046 0.096485  0.00262048  -0.0214527  -0.00769779 145 CYS   A CB   
1133 S  SG   . CYS   A 145 ? 0.162109  0.25413  0.12325   0.016483    -0.02274    -0.0222716  145 CYS   A SG   
1134 N  N    . GLY   A 146 ? 0.106838  0.189522 0.0626854 -0.00726938 -0.00065071 -0.00046143 146 GLY   A N    
1135 C  CA   . GLY   A 146 ? 0.106783  0.182991 0.0749697 -0.00937758 -0.0033015  0.000699    146 GLY   A CA   
1136 C  C    . GLY   A 146 ? 0.10773   0.174277 0.0748131 -0.00699194 -0.00368664 -0.00427916 146 GLY   A C    
1137 O  O    . GLY   A 146 ? 0.111191  0.180338 0.101754  0.0014481   -0.0147168  -0.0139024  146 GLY   A O    
1138 N  N    . SER   A 147 ? 0.118645  0.173947 0.0738273 -0.00740812 -0.0151599  -8.39e-05   147 SER   A N    
1139 C  CA   . SER   A 147 ? 0.118049  0.173758 0.0753669 -0.011509   -0.0128356  0.00175261  147 SER   A CA   
1140 C  C    . SER   A 147 ? 0.122456  0.174537 0.0684154 -0.00860308 -0.0132219  0.00415692  147 SER   A C    
1141 O  O    . SER   A 147 ? 0.121074  0.19514  0.0696963 -0.00856484 -0.0162123  -0.0054394  147 SER   A O    
1142 C  CB   . SER   A 147 ? 0.13353   0.167184 0.0826617 -0.0124945  -0.00969104 0.00465079  147 SER   A CB   
1143 O  OG   . SER   A 147 ? 0.127091  0.170209 0.0882297 -0.0170234  -0.0133827  0.0113277   147 SER   A OG   
1144 N  N    . VAL   A 148 ? 0.109389  0.173118 0.0604256 -0.00475049 -0.0147194  0.00696281  148 VAL   A N    
1145 C  CA   . VAL   A 148 ? 0.110711  0.177004 0.0675284 -0.00387938 -0.0159112  0.00898965  148 VAL   A CA   
1146 C  C    . VAL   A 148 ? 0.108542  0.174305 0.0687669 -0.00028022 -0.0119972  0.00888875  148 VAL   A C    
1147 O  O    . VAL   A 148 ? 0.125628  0.177886 0.0644327 -0.00064318 -0.0112756  0.0132411   148 VAL   A O    
1148 C  CB   . VAL   A 148 ? 0.120161  0.183155 0.077968  -0.00176522 -0.00728091 0.00801211  148 VAL   A CB   
1149 C  CG1  . VAL   A 148 ? 0.120599  0.190678 0.08518   0.00572824  -0.00394039 0.00706127  148 VAL   A CG1  
1150 C  CG2  . VAL   A 148 ? 0.127639  0.192779 0.0910871 -0.00354158 -0.0154668  -0.00236319 148 VAL   A CG2  
1151 N  N    . GLY   A 149 ? 0.104925  0.176966 0.0726659 -0.00169534 -0.0150828  0.0126482   149 GLY   A N    
1152 C  CA   . GLY   A 149 ? 0.0992017 0.177716 0.069727  0.00336069  -0.00784757 0.00812043  149 GLY   A CA   
1153 C  C    . GLY   A 149 ? 0.0986354 0.178722 0.075937  0.0058083   0.00193964  0.00896596  149 GLY   A C    
1154 O  O    . GLY   A 149 ? 0.114106  0.183643 0.094134  0.00802383  0.00556772  0.018362    149 GLY   A O    
1155 N  N    . PHE   A 150 ? 0.100187  0.173981 0.0782888 0.00772252  -0.00330226 0.00656645  150 PHE   A N    
1156 C  CA   . PHE   A 150 ? 0.102687  0.180124 0.0932098 0.00356745  0.00079954  0.000943    150 PHE   A CA   
1157 C  C    . PHE   A 150 ? 0.103494  0.175977 0.085605  0.00757897  -0.00442982 -0.00372746 150 PHE   A C    
1158 O  O    . PHE   A 150 ? 0.113405  0.169999 0.0833488 0.00945347  -0.00213008 -0.00939274 150 PHE   A O    
1159 C  CB   . PHE   A 150 ? 0.117238  0.196091 0.110525  0.00490592  0.0170761   0.00264613  150 PHE   A CB   
1160 C  CG   . PHE   A 150 ? 0.13855   0.207386 0.105351  0.00495994  0.0288619   0.00659993  150 PHE   A CG   
1161 C  CD1  . PHE   A 150 ? 0.165863  0.210506 0.109239  0.00871649  0.028792    0.00819482  150 PHE   A CD1  
1162 C  CD2  . PHE   A 150 ? 0.137309  0.215453 0.101418  0.00672537  0.0290307   0.0155101   150 PHE   A CD2  
1163 C  CE1  . PHE   A 150 ? 0.182978  0.224078 0.111512  0.00454409  0.0376504   0.0142184   150 PHE   A CE1  
1164 C  CE2  . PHE   A 150 ? 0.144733  0.225269 0.10321   0.0136491   0.0425329   0.0152552   150 PHE   A CE2  
1165 C  CZ   . PHE   A 150 ? 0.173794  0.230548 0.119221  0.0146058   0.0366294   0.0158717   150 PHE   A CZ   
1166 N  N    . ASN   A 151 ? 0.106631  0.182681 0.0892691 0.00828581  -0.0104372  0.00244821  151 ASN   A N    
1167 C  CA   . ASN   A 151 ? 0.114115  0.190912 0.107654  0.00352721  -0.00784658 -0.00028881 151 ASN   A CA   
1168 C  C    . ASN   A 151 ? 0.131218  0.201978 0.103826  0.00765369  -0.0071508  -0.00367573 151 ASN   A C    
1169 O  O    . ASN   A 151 ? 0.122558  0.226828 0.116329  0.00762433  -0.0139874  -0.0151488  151 ASN   A O    
1170 C  CB   . ASN   A 151 ? 0.113343  0.198205 0.126965  0.00096583  -0.00309483 0.00255273  151 ASN   A CB   
1171 C  CG   . ASN   A 151 ? 0.1267    0.207502 0.125012  -0.00138172 -0.00090789 -0.00333073 151 ASN   A CG   
1172 O  OD1  . ASN   A 151 ? 0.143412  0.226317 0.133978  0.0218681   -0.00863182 -0.0183274  151 ASN   A OD1  
1173 N  ND2  . ASN   A 151 ? 0.137942  0.215362 0.115223  0.00621761  0.00782829  0.00082408  151 ASN   A ND2  
1174 N  N    . ILE   A 152 ? 0.138913  0.204014 0.108069  0.00712286  -0.00677528 -0.00521461 152 ILE   A N    
1175 C  CA   . ILE   A 152 ? 0.177092  0.209836 0.117031  0.00563562  -0.00742895 -0.00474073 152 ILE   A CA   
1176 C  C    . ILE   A 152 ? 0.221877  0.248924 0.166232  -0.0204542  -0.01198    -0.0152079  152 ILE   A C    
1177 O  O    . ILE   A 152 ? 0.262887  0.315879 0.196772  -0.0420973  -0.0348868  -0.00423685 152 ILE   A O    
1178 C  CB   . ILE   A 152 ? 0.186045  0.220269 0.111628  0.0218791   -0.00648477 0.0044903   152 ILE   A CB   
1179 C  CG1  . ILE   A 152 ? 0.187899  0.219192 0.0977103 0.0264067   0.0105491   0.00968944  152 ILE   A CG1  
1180 C  CG2  . ILE   A 152 ? 0.210848  0.223697 0.122378  0.0205809   -0.00358149 0.0041061   152 ILE   A CG2  
1181 C  CD1  . ILE   A 152 ? 0.193982  0.228615 0.106881  0.0210678   0.0142432   0.015733    152 ILE   A CD1  
1182 N  N    . ASP   A 153 ? 0.272866  0.275004 0.190802  -0.0348143  0.00091164  -0.0222939  153 ASP   A N    
1183 C  CA   . ASP   A 153 ? 0.302224  0.299127 0.220554  -0.0419156  0.0113068   -0.0179012  153 ASP   A CA   
1184 C  C    . ASP   A 153 ? 0.361454  0.318085 0.252355  -0.0443661  0.0303883   -0.0315044  153 ASP   A C    
1185 O  O    . ASP   A 153 ? 0.417867  0.369408 0.334737  -0.0224921  0.0593997   -0.0217976  153 ASP   A O    
1186 C  CB   . ASP   A 153 ? 0.31077   0.292068 0.198291  -0.0294942  -0.0086428  -0.0182593  153 ASP   A CB   
1187 C  CG   . ASP   A 153 ? 0.297982  0.29572  0.190453  -0.0107012  -0.0138356  -0.0131934  153 ASP   A CG   
1188 O  OD1  . ASP   A 153 ? 0.294363  0.311679 0.173581  -0.0117864  -0.0122068  0.00090178  153 ASP   A OD1  
1189 O  OD2  . ASP   A 153 ? 0.265938  0.27728  0.190424  -0.00879461 -0.0170105  -0.00810889 153 ASP   A OD2  
1190 N  N    . TYR   A 154 ? 0.37464   0.372529 0.283789  -0.0583881  0.0130527   -0.01302    154 TYR   A N    
1191 C  CA   . TYR   A 154 ? 0.381169  0.375789 0.288286  -0.050536   -0.00051015 -0.0498695  154 TYR   A CA   
1192 C  C    . TYR   A 154 ? 0.370309  0.391497 0.307628  -0.0544333  -0.0356454  -0.0483765  154 TYR   A C    
1193 O  O    . TYR   A 154 ? 0.413398  0.391293 0.390378  -0.0205147  -0.0516579  -0.0509898  154 TYR   A O    
1194 C  CB   . TYR   A 154 ? 0.397438  0.413799 0.306648  -0.0425651  0.0300355   -0.0365318  154 TYR   A CB   
1195 C  CG   . TYR   A 154 ? 0.435732  0.467675 0.317578  -0.0508997  0.0549962   -0.0224039  154 TYR   A CG   
1196 C  CD1  . TYR   A 154 ? 0.45057   0.488246 0.346643  -0.0649392  0.057156    -0.0218764  154 TYR   A CD1  
1197 C  CD2  . TYR   A 154 ? 0.450547  0.496404 0.352073  -0.0616549  0.0446178   -0.0303636  154 TYR   A CD2  
1198 C  CE1  . TYR   A 154 ? 0.448295  0.514786 0.399002  -0.0646923  0.0701701   -0.0229126  154 TYR   A CE1  
1199 C  CE2  . TYR   A 154 ? 0.467682  0.518803 0.386307  -0.0593317  0.0563395   -0.00869032 154 TYR   A CE2  
1200 C  CZ   . TYR   A 154 ? 0.468955  0.513214 0.387785  -0.0695535  0.0709466   -0.0134902  154 TYR   A CZ   
1201 O  OH   . TYR   A 154 ? 0.502695  0.527605 0.46792   -0.0722187  0.107505    -0.00820266 154 TYR   A OH   
1202 N  N    . ASP   A 155 ? 0.368466  0.398333 0.315342  -0.0618566  -0.0553672  -0.0478779  155 ASP   A N    
1203 C  CA   . ASP   A 155 ? 0.353584  0.425037 0.302391  -0.0361258  -0.0617221  -0.0481554  155 ASP   A CA   
1204 C  C    . ASP   A 155 ? 0.345974  0.419894 0.26836   -0.042939   -0.048037   -0.0471312  155 ASP   A C    
1205 O  O    . ASP   A 155 ? 0.378762  0.505237 0.259471  -0.0344151  -0.0341365  -0.0623854  155 ASP   A O    
1206 C  CB   . ASP   A 155 ? 0.38598   0.438392 0.354005  -0.0487786  -0.0552032  -0.0652077  155 ASP   A CB   
1207 N  N    . CYS   A 156 ? 0.254945  0.339472 0.253684  -0.0246188  -0.0451082  -0.017122   156 CYS   A N    
1208 C  CA   . CYS   A 156 ? 0.229027  0.272116 0.224435  -0.0108467  -0.023295   -0.0108094  156 CYS   A CA   
1209 C  C    . CYS   A 156 ? 0.168977  0.238381 0.178396  -0.00453357 -0.0200735  0.00777296  156 CYS   A C    
1210 O  O    . CYS   A 156 ? 0.152848  0.238549 0.193266  0.00014015  -0.0247043  0.0159131   156 CYS   A O    
1211 C  CB   . CYS   A 156 ? 0.257233  0.275745 0.253597  -0.00779634 -0.0253331  0.00333305  156 CYS   A CB   
1212 S  SG   . CYS   A 156 ? 0.292711  0.310241 0.273528  -0.00078397 -0.0376289  0.0395554   156 CYS   A SG   
1213 N  N    . VAL   A 157 ? 0.156249  0.219207 0.144431  0.00910894  -0.0188235  0.00815317  157 VAL   A N    
1214 C  CA   . VAL   A 157 ? 0.130997  0.205616 0.13311   0.0135544   -0.0101338  0.016685    157 VAL   A CA   
1215 C  C    . VAL   A 157 ? 0.147527  0.213744 0.130923  0.0237549   -0.00468669 0.0156006   157 VAL   A C    
1216 O  O    . VAL   A 157 ? 0.160967  0.22862  0.11782   0.0437026   -0.00545447 0.00367167  157 VAL   A O    
1217 C  CB   . VAL   A 157 ? 0.119286  0.212607 0.137449  0.0115251   -0.00643309 0.0192941   157 VAL   A CB   
1218 C  CG1  . VAL   A 157 ? 0.125732  0.216647 0.139326  0.0124799   -0.00077094 0.0215066   157 VAL   A CG1  
1219 C  CG2  . VAL   A 157 ? 0.122849  0.217167 0.131864  0.0105078   -0.00071488 0.02143     157 VAL   A CG2  
1220 N  N    . SER   A 158 ? 0.13574   0.218538 0.117738  0.0197603   -0.0101915  0.0105246   158 SER   A N    
1221 C  CA   . SER   A 158 ? 0.144102  0.221071 0.117934  0.0145688   -0.00172108 0.0173261   158 SER   A CA   
1222 C  C    . SER   A 158 ? 0.132249  0.202172 0.104149  0.0208437   -0.00234312 0.0178512   158 SER   A C    
1223 O  O    . SER   A 158 ? 0.136802  0.203544 0.151666  0.0187422   -0.00515192 0.00738979  158 SER   A O    
1224 C  CB   . SER   A 158 ? 0.162712  0.250644 0.137546  0.0103442   0.0129338   0.018011    158 SER   A CB   
1225 O  OG   . SER   A 158 ? 0.204476  0.301769 0.174427  0.0246055   0.00887341  0.0265817   158 SER   A OG   
1226 N  N    . PHE   A 159 ? 0.125799  0.185274 0.101876  0.022486    0.00325884  0.0180535   159 PHE   A N    
1227 C  CA   . PHE   A 159 ? 0.126192  0.192513 0.0909404 0.018577    0.00450968  0.0144652   159 PHE   A CA   
1228 C  C    . PHE   A 159 ? 0.132376  0.195319 0.0860627 0.0179879   0.00304979  0.021948    159 PHE   A C    
1229 O  O    . PHE   A 159 ? 0.146501  0.195947 0.101899  0.0276789   0.00416489  0.0240696   159 PHE   A O    
1230 C  CB   . PHE   A 159 ? 0.124978  0.196117 0.096669  0.0188012   0.00404457  0.0160353   159 PHE   A CB   
1231 C  CG   . PHE   A 159 ? 0.115183  0.19291  0.0993323 0.0130312   0.00485618  0.0104741   159 PHE   A CG   
1232 C  CD1  . PHE   A 159 ? 0.122486  0.194288 0.0930059 0.00884381  0.00932691  0.01106     159 PHE   A CD1  
1233 C  CD2  . PHE   A 159 ? 0.118969  0.186664 0.0988013 0.0103442   0.00144589  0.0108325   159 PHE   A CD2  
1234 C  CE1  . PHE   A 159 ? 0.125378  0.198584 0.092873  0.00323356  0.00294621  0.0124368   159 PHE   A CE1  
1235 C  CE2  . PHE   A 159 ? 0.124846  0.190074 0.098481  0.00702768  0.00378612  0.0114292   159 PHE   A CE2  
1236 C  CZ   . PHE   A 159 ? 0.117382  0.191796 0.107365  0.00641111  -0.00167515 0.0108408   159 PHE   A CZ   
1237 N  N    . CYS   A 160 ? 0.130126  0.191405 0.0671544 0.00758087  -0.00531999 0.0163172   160 CYS   A N    
1238 C  CA   . CYS   A 160 ? 0.135297  0.212488 0.0715705 0.0057799   -0.00182637 0.0107239   160 CYS   A CA   
1239 C  C    . CYS   A 160 ? 0.138425  0.207842 0.0647922 0.00066676  -0.00458562 0.0126749   160 CYS   A C    
1240 O  O    . CYS   A 160 ? 0.192067  0.240634 0.0623728 -0.00764575 -0.00335951 0.0133828   160 CYS   A O    
1241 C  CB   . CYS   A 160 ? 0.134167  0.22006  0.0959322 -0.00503488 0.00179854  0.0072846   160 CYS   A CB   
1242 S  SG   . CYS   A 160 ? 0.149049  0.239252 0.122381  0.00385053  -0.00052349 0.0135125   160 CYS   A SG   
1243 N  N    . TYR   A 161 ? 0.114779  0.20263  0.0585445 0.00094963  -0.00530857 0.0077955   161 TYR   A N    
1244 C  CA   . TYR   A 161 ? 0.112326  0.200669 0.051963  0.00276112  -0.00667789 0.0112943   161 TYR   A CA   
1245 C  C    . TYR   A 161 ? 0.106744  0.203336 0.0617212 -0.00144112 -0.010194   0.00741445  161 TYR   A C    
1246 O  O    . TYR   A 161 ? 0.104596  0.213886 0.0622649 -0.00090299 -0.0140808  0.00315972  161 TYR   A O    
1247 C  CB   . TYR   A 161 ? 0.110928  0.203004 0.048313  0.00558369  -0.00557612 0.00715841  161 TYR   A CB   
1248 C  CG   . TYR   A 161 ? 0.107793  0.206303 0.0578188 0.00266997  -0.00848847 0.00632541  161 TYR   A CG   
1249 C  CD1  . TYR   A 161 ? 0.112731  0.208818 0.0570343 0.00275752  -0.00404182 0.00457822  161 TYR   A CD1  
1250 C  CD2  . TYR   A 161 ? 0.108246  0.202012 0.0672621 0.00134758  -0.00639736 0.00805189  161 TYR   A CD2  
1251 C  CE1  . TYR   A 161 ? 0.116259  0.215101 0.0617713 -0.00028585 -0.00686366 -0.00034921 161 TYR   A CE1  
1252 C  CE2  . TYR   A 161 ? 0.110077  0.20995  0.0709357 -0.00223478 -0.0080456  0.00645343  161 TYR   A CE2  
1253 C  CZ   . TYR   A 161 ? 0.12487   0.208908 0.0790433 0.00104367  -0.00456257 -0.00176249 161 TYR   A CZ   
1254 O  OH   . TYR   A 161 ? 0.142383  0.218259 0.0781413 0.006708    -0.0079172  -0.00934802 161 TYR   A OH   
1255 N  N    . MET   A 162 ? 0.111018  0.199888 0.0566754 -0.00159927 -0.0152138  0.00314532  162 MET   A N    
1256 C  CA   . MET   A 162 ? 0.110111  0.203645 0.0616854 -0.00010559 -0.01409    0.00277461  162 MET   A CA   
1257 C  C    . MET   A 162 ? 0.105187  0.2014   0.0556904 0.00570011  -0.0107181  0.00028195  162 MET   A C    
1258 O  O    . MET   A 162 ? 0.105111  0.211116 0.0518614 -0.00219766 -0.00845413 -0.00516275 162 MET   A O    
1259 C  CB   . MET   A 162 ? 0.118194  0.206953 0.0872091 0.00323388  -0.0138794  0.00672262  162 MET   A CB   
1260 C  CG   . MET   A 162 ? 0.114852  0.229613 0.125297  -0.00575874 -0.0130548  0.0104878   162 MET   A CG   
1261 S  SD   . MET   A 162 ? 0.149898  0.290396 0.211666  0.00561964  0.0211356   0.00459035  162 MET   A SD   
1262 C  CE   . MET   A 162 ? 0.139077  0.264538 0.204261  -0.00202932 0.0375024   -0.0125674  162 MET   A CE   
1263 N  N    . HIS   A 163 ? 0.106273  0.199262 0.0499395 0.00727167  -0.00459694 -0.00135189 163 HIS   A N    
1264 C  CA   . HIS   A 163 ? 0.110199  0.202448 0.0489784 0.00810254  -0.00693406 -0.00138457 163 HIS   A CA   
1265 C  C    . HIS   A 163 ? 0.111895  0.214462 0.0644628 0.00541237  -0.00577522 -0.00864449 163 HIS   A C    
1266 O  O    . HIS   A 163 ? 0.106701  0.234633 0.0642657 0.00160614  -0.00548972 -0.00399049 163 HIS   A O    
1267 C  CB   . HIS   A 163 ? 0.112997  0.2094   0.0558448 0.0101866   -0.00502901 0.0037472   163 HIS   A CB   
1268 C  CG   . HIS   A 163 ? 0.115156  0.214118 0.0602021 0.0152424   -0.00799958 -0.00484029 163 HIS   A CG   
1269 N  ND1  . HIS   A 163 ? 0.111092  0.223923 0.0733399 0.0132415   -0.00259462 -0.00756506 163 HIS   A ND1  
1270 C  CD2  . HIS   A 163 ? 0.121272  0.219226 0.0732996 0.014489    -0.00900499 -0.00777424 163 HIS   A CD2  
1271 C  CE1  . HIS   A 163 ? 0.118558  0.223038 0.078325  0.0169583   -0.00308643 -0.0122965  163 HIS   A CE1  
1272 N  NE2  . HIS   A 163 ? 0.118731  0.223325 0.084506  0.0172236   -0.00666358 -0.00980962 163 HIS   A NE2  
1273 N  N    . HIS   A 164 ? 0.126399  0.210195 0.0700903 0.00393764  -0.0117698  -0.0156456  164 HIS   A N    
1274 C  CA   . HIS   A 164 ? 0.117603  0.214994 0.0709941 0.00206267  -0.00803551 -0.00771554 164 HIS   A CA   
1275 C  C    . HIS   A 164 ? 0.117934  0.222818 0.073974  -0.00487378 -0.0128359  -0.0170546  164 HIS   A C    
1276 O  O    . HIS   A 164 ? 0.136793  0.228308 0.10216   -0.0156035  -0.00108608 -0.015379   164 HIS   A O    
1277 C  CB   . HIS   A 164 ? 0.123991  0.218983 0.0663572 0.00169385  -0.00903282 -0.0125416  164 HIS   A CB   
1278 C  CG   . HIS   A 164 ? 0.126237  0.220656 0.0598634 0.00380815  -0.0066453  -0.0105863  164 HIS   A CG   
1279 N  ND1  . HIS   A 164 ? 0.166687  0.226243 0.0853211 0.00839822  -0.00142945 -0.017971   164 HIS   A ND1  
1280 C  CD2  . HIS   A 164 ? 0.116951  0.217049 0.0258888 0.00186271  -0.00950572 -0.0113955  164 HIS   A CD2  
1281 C  CE1  . HIS   A 164 ? 0.130571  0.224854 0.0413902 0.0107475   -0.00104423 -0.0192199  164 HIS   A CE1  
1282 N  NE2  . HIS   A 164 ? 0.146845  0.240466 0.063004  -0.00373278 0.00623219  -0.00744669 164 HIS   A NE2  
1283 N  N    . MET   A 165 ? 0.110986  0.238494 0.0822252 -0.00389603 -0.014119   -0.0158595  165 MET   A N    
1284 C  CA   . MET   A 165 ? 0.126368  0.2453   0.0961248 -0.00146201 -0.0119878  -0.0234051  165 MET   A CA   
1285 C  C    . MET   A 165 ? 0.13169   0.235026 0.0989128 -0.00267416 -0.0122911  -0.0276789  165 MET   A C    
1286 O  O    . MET   A 165 ? 0.136031  0.22993  0.0966021 -0.00431414 0.00161979  -0.0216954  165 MET   A O    
1287 C  CB   . MET   A 165 ? 0.149082  0.263362 0.105554  0.00031496  -0.0183145  -0.0271848  165 MET   A CB   
1288 C  CG   . MET   A 165 ? 0.170144  0.286689 0.108216  0.00612112  -0.0108676  -0.0282386  165 MET   A CG   
1289 S  SD   . MET   A 165 ? 0.214012  0.317286 0.111287  0.0148371   0.00690441  -0.0239395  165 MET   A SD   
1290 C  CE   . MET   A 165 ? 0.187588  0.334213 0.101551  0.0122955   -0.0249196  -0.0457251  165 MET   A CE   
1291 N  N    . GLU   A 166 ? 0.136073  0.23505  0.115943  -0.00087469 -0.0087144  -0.0230249  166 GLU   A N    
1292 C  CA   . GLU   A 166 ? 0.143339  0.235854 0.130925  0.00196856  -0.00675941 -0.0313176  166 GLU   A CA   
1293 C  C    . GLU   A 166 ? 0.156375  0.254412 0.136262  -0.0084942  -0.010622   -0.0321046  166 GLU   A C    
1294 O  O    . GLU   A 166 ? 0.162728  0.26011  0.135949  -0.01333    -0.0104713  -0.0339903  166 GLU   A O    
1295 C  CB   . GLU   A 166 ? 0.148732  0.231312 0.141078  0.0087206   -0.00696474 -0.0342022  166 GLU   A CB   
1296 C  CG   . GLU   A 166 ? 0.155477  0.232801 0.152479  0.0128927   -0.0138639  -0.0329016  166 GLU   A CG   
1297 C  CD   . GLU   A 166 ? 0.188783  0.236471 0.167671  0.0146248   -0.0191344  -0.0254366  166 GLU   A CD   
1298 O  OE1  . GLU   A 166 ? 0.169319  0.24661  0.165284  0.00085572  -0.00273203 -0.0238273  166 GLU   A OE1  
1299 O  OE2  . GLU   A 166 ? 0.252831  0.242421 0.170286  0.0211948   -0.0328729  -0.026108   166 GLU   A OE2  
1300 N  N    . LEU   A 167 ? 0.163097  0.266597 0.127648  -0.00723768 -0.00727403 -0.0426114  167 LEU   A N    
1301 C  CA   . LEU   A 167 ? 0.204824  0.294704 0.129597  -0.00751718 -0.011366   -0.0433265  167 LEU   A CA   
1302 C  C    . LEU   A 167 ? 0.23938   0.299699 0.149142  0.00839745  -0.0257708  -0.0662903  167 LEU   A C    
1303 O  O    . LEU   A 167 ? 0.243065  0.297791 0.154408  0.0206172   -0.0156669  -0.0617783  167 LEU   A O    
1304 C  CB   . LEU   A 167 ? 0.206634  0.322936 0.136104  -0.0123926  -0.00339293 -0.0318728  167 LEU   A CB   
1305 C  CG   . LEU   A 167 ? 0.227637  0.345522 0.150329  -0.0135975  -0.00422456 -0.0120759  167 LEU   A CG   
1306 C  CD1  . LEU   A 167 ? 0.231627  0.351492 0.170426  -0.0141317  -0.00751727 -0.00484431 167 LEU   A CD1  
1307 C  CD2  . LEU   A 167 ? 0.228058  0.365327 0.205697  -0.00925393 -0.0100708  0.00579042  167 LEU   A CD2  
1308 N  N    . PRO   A 168 ? 0.314569  0.318334 0.165984  0.0233488   -0.0370573  -0.090003   168 PRO   A N    
1309 C  CA   . PRO   A 168 ? 0.351954  0.329026 0.199086  0.0156779   -0.0479294  -0.0838195  168 PRO   A CA   
1310 C  C    . PRO   A 168 ? 0.349547  0.330613 0.210964  0.0119152   -0.0335901  -0.0853307  168 PRO   A C    
1311 O  O    . PRO   A 168 ? 0.375173  0.349084 0.280153  0.0004797   -0.0341244  -0.0626366  168 PRO   A O    
1312 C  CB   . PRO   A 168 ? 0.373835  0.339924 0.206675  0.0177768   -0.0552229  -0.0997953  168 PRO   A CB   
1313 C  CG   . PRO   A 168 ? 0.374311  0.347579 0.199494  0.0201471   -0.0510059  -0.0979111  168 PRO   A CG   
1314 C  CD   . PRO   A 168 ? 0.346375  0.330967 0.179545  0.0324889   -0.0461056  -0.0859992  168 PRO   A CD   
1315 N  N    . THR   A 169 ? 0.361888  0.335164 0.217369  0.00956184  -0.014496   -0.0938942  169 THR   A N    
1316 C  CA   . THR   A 169 ? 0.360321  0.360847 0.240662  0.0155779   0.0163463   -0.0840463  169 THR   A CA   
1317 C  C    . THR   A 169 ? 0.290743  0.352561 0.234364  0.0168194   0.0240266   -0.0704522  169 THR   A C    
1318 O  O    . THR   A 169 ? 0.279972  0.394127 0.296847  0.0317633   0.042502    -0.0672329  169 THR   A O    
1319 C  CB   . THR   A 169 ? 0.40922   0.404676 0.224994  0.0107949   0.0342529   -0.0790366  169 THR   A CB   
1320 O  OG1  . THR   A 169 ? 0.453504  0.433343 0.190865  0.021998    0.0467061   -0.0844819  169 THR   A OG1  
1321 C  CG2  . THR   A 169 ? 0.444007  0.424381 0.235404  0.0167702   0.0307667   -0.0902553  169 THR   A CG2  
1322 N  N    . GLY   A 170 ? 0.242837  0.30664  0.200889  0.00016384  0.0078377   -0.0579991  170 GLY   A N    
1323 C  CA   . GLY   A 170 ? 0.2243    0.292635 0.198848  -0.00275143 0.00477165  -0.0534483  170 GLY   A CA   
1324 C  C    . GLY   A 170 ? 0.229075  0.296095 0.18792   -0.00650695 0.00073204  -0.0414484  170 GLY   A C    
1325 O  O    . GLY   A 170 ? 0.305501  0.34354  0.202195  -0.0307705  -0.0260279  -0.0503633  170 GLY   A O    
1326 N  N    . VAL   A 171 ? 0.183642  0.280493 0.176329  -0.00179721 0.0108834   -0.0358428  171 VAL   A N    
1327 C  CA   . VAL   A 171 ? 0.17901   0.276718 0.168255  0.0101013   0.0133433   -0.0273267  171 VAL   A CA   
1328 C  C    . VAL   A 171 ? 0.166277  0.243244 0.131881  -0.00128555 0.0107323   -0.0188417  171 VAL   A C    
1329 O  O    . VAL   A 171 ? 0.168139  0.244879 0.128057  -0.00298954 0.00551417  -0.0299663  171 VAL   A O    
1330 C  CB   . VAL   A 171 ? 0.182097  0.300876 0.194337  0.0104359   0.0191112   -0.0269738  171 VAL   A CB   
1331 C  CG1  . VAL   A 171 ? 0.193257  0.308792 0.221583  0.0205962   0.00878014  -0.0325931  171 VAL   A CG1  
1332 C  CG2  . VAL   A 171 ? 0.202857  0.31308  0.18037   0.0120872   0.0220537   -0.0256798  171 VAL   A CG2  
1333 N  N    . HIS   A 172 ? 0.140245  0.228115 0.0991551 0.00774607  0.00861713  -0.0103094  172 HIS   A N    
1334 C  CA   . HIS   A 172 ? 0.135118  0.226284 0.0841118 0.00197957  0.00342377  -0.0180053  172 HIS   A CA   
1335 C  C    . HIS   A 172 ? 0.124332  0.234485 0.0962537 0.00885612  0.00178292  -0.00766233 172 HIS   A C    
1336 O  O    . HIS   A 172 ? 0.132344  0.250043 0.116808  0.00281278  -0.00028822 0.00846172  172 HIS   A O    
1337 C  CB   . HIS   A 172 ? 0.147729  0.22799  0.0836651 0.00229749  -0.00274612 -0.0187103  172 HIS   A CB   
1338 C  CG   . HIS   A 172 ? 0.160918  0.234395 0.0870642 -0.00376382 -0.00913441 -0.0154801  172 HIS   A CG   
1339 N  ND1  . HIS   A 172 ? 0.166333  0.226557 0.0744132 0.00313013  -0.0104429  -0.0138783  172 HIS   A ND1  
1340 C  CD2  . HIS   A 172 ? 0.174152  0.238813 0.089863  -0.00882648 -0.00416342 -0.015139   172 HIS   A CD2  
1341 C  CE1  . HIS   A 172 ? 0.177951  0.238127 0.0827872 0.00047524  -0.0160139  -0.00621611 172 HIS   A CE1  
1342 N  NE2  . HIS   A 172 ? 0.185344  0.24531  0.0957521 -0.0078492  -0.0085861  -0.0114944  172 HIS   A NE2  
1343 N  N    . ALA   A 173 ? 0.11636   0.236152 0.0930791 0.00714292  0.00595268  -0.00277661 173 ALA   A N    
1344 C  CA   . ALA   A 173 ? 0.119106  0.236437 0.0824843 0.01006     0.0048024   -0.00348885 173 ALA   A CA   
1345 C  C    . ALA   A 173 ? 0.116357  0.236298 0.0721522 0.00756258  0.00411198  -0.00060619 173 ALA   A C    
1346 O  O    . ALA   A 173 ? 0.114735  0.231863 0.0813219 0.0083542   0.0128515   0.00044451  173 ALA   A O    
1347 C  CB   . ALA   A 173 ? 0.136421  0.247253 0.0858595 0.0122649   0.00547399  -0.00903177 173 ALA   A CB   
1348 N  N    . GLY   A 174 ? 0.118203  0.239224 0.0577376 0.0089333   -0.00131626 -0.00139809 174 GLY   A N    
1349 C  CA   . GLY   A 174 ? 0.109691  0.238704 0.0611842 0.0111584   -0.00039118 0.00190556  174 GLY   A CA   
1350 C  C    . GLY   A 174 ? 0.105678  0.244909 0.0565986 0.00843848  0.00176805  0.00561477  174 GLY   A C    
1351 O  O    . GLY   A 174 ? 0.122541  0.248504 0.0551046 0.00770301  0.00728245  0.0196328   174 GLY   A O    
1352 N  N    . THR   A 175 ? 0.116137  0.237201 0.0425279 0.014247    -0.00054974 0.00326555  175 THR   A N    
1353 C  CA   . THR   A 175 ? 0.119124  0.238781 0.0535191 0.00804595  0.00477801  0.00989468  175 THR   A CA   
1354 C  C    . THR   A 175 ? 0.101149  0.235702 0.0568492 0.0134612   0.000679    0.012655    175 THR   A C    
1355 O  O    . THR   A 175 ? 0.120308  0.252099 0.0710503 0.0135533   -0.0140551  0.0256898   175 THR   A O    
1356 C  CB   . THR   A 175 ? 0.119318  0.241307 0.0594278 0.00487733  0.00330875  0.00650469  175 THR   A CB   
1357 O  OG1  . THR   A 175 ? 0.124061  0.2511   0.0616649 0.00236939  0.00439224  0.00479194  175 THR   A OG1  
1358 C  CG2  . THR   A 175 ? 0.117253  0.245403 0.072092  0.00269559  0.00652254  0.00634018  175 THR   A CG2  
1359 N  N    . ASP   A 176 ? 0.108128  0.234342 0.0573683 0.0170763   -0.00381927 0.0196243   176 ASP   A N    
1360 C  CA   . ASP   A 176 ? 0.117797  0.243192 0.083616  0.0085454   -0.00929353 0.0124977   176 ASP   A CA   
1361 C  C    . ASP   A 176 ? 0.129246  0.237838 0.0853478 0.00736977  -0.00147834 0.0111457   176 ASP   A C    
1362 O  O    . ASP   A 176 ? 0.126949  0.243474 0.0598819 0.00763117  0.00101982  0.0040055   176 ASP   A O    
1363 C  CB   . ASP   A 176 ? 0.128833  0.258686 0.0947805 0.00437566  -0.0080331  0.0166475   176 ASP   A CB   
1364 C  CG   . ASP   A 176 ? 0.132957  0.26748  0.0946618 0.00323733  -0.00354251 0.026257    176 ASP   A CG   
1365 O  OD1  . ASP   A 176 ? 0.12794   0.277007 0.120639  0.00885474  -0.00851908 0.0276954   176 ASP   A OD1  
1366 O  OD2  . ASP   A 176 ? 0.162514  0.290739 0.117632  -0.00497334 0.00878935  0.0441988   176 ASP   A OD2  
1367 N  N    . LEU   A 177 ? 0.121173  0.238212 0.0986056 0.00955634  0.00593838  0.00581784  177 LEU   A N    
1368 C  CA   . LEU   A 177 ? 0.133235  0.240448 0.0914474 0.0111371   0.00694978  0.00547736  177 LEU   A CA   
1369 C  C    . LEU   A 177 ? 0.129902  0.252959 0.10903   0.0161058   0.0101217   0.0144082   177 LEU   A C    
1370 O  O    . LEU   A 177 ? 0.125955  0.279245 0.128732  0.0231954   0.00681378  0.0182861   177 LEU   A O    
1371 C  CB   . LEU   A 177 ? 0.146467  0.240169 0.0986314 0.0110662   0.00055111  0.00017847  177 LEU   A CB   
1372 C  CG   . LEU   A 177 ? 0.163887  0.246578 0.10603   0.0116543   -0.0155399  -0.00442431 177 LEU   A CG   
1373 C  CD1  . LEU   A 177 ? 0.184577  0.255682 0.101146  0.0051982   -0.0163475  -0.00620198 177 LEU   A CD1  
1374 C  CD2  . LEU   A 177 ? 0.169734  0.245946 0.114535  0.0145911   -0.0281447  -0.00533517 177 LEU   A CD2  
1375 N  N    . GLU   A 178 ? 0.132288  0.253519 0.112494  0.0203617   0.00489374  0.0291958   178 GLU   A N    
1376 C  CA   . GLU   A 178 ? 0.150175  0.263752 0.126596  0.0232884   -0.00190219 0.0368357   178 GLU   A CA   
1377 C  C    . GLU   A 178 ? 0.13446   0.260857 0.112568  0.0232986   -0.00138399 0.035689    178 GLU   A C    
1378 O  O    . GLU   A 178 ? 0.153418  0.280004 0.106263  0.030171    -0.0134666  0.037566    178 GLU   A O    
1379 C  CB   . GLU   A 178 ? 0.181569  0.282563 0.164301  0.0162938   -0.00186339 0.0519421   178 GLU   A CB   
1380 C  CG   . GLU   A 178 ? 0.227081  0.305479 0.196043  0.0193621   -0.00410808 0.0480284   178 GLU   A CG   
1381 C  CD   . GLU   A 178 ? 0.281896  0.330694 0.252302  0.0102224   0.0131893   0.057372    178 GLU   A CD   
1382 O  OE1  . GLU   A 178 ? 0.339172  0.386123 0.293609  -0.00097266 0.0544292   0.0718545   178 GLU   A OE1  
1383 O  OE2  . GLU   A 178 ? 0.361581  0.367167 0.339506  0.0201305   0.00914831  0.0497506   178 GLU   A OE2  
1384 N  N    . GLY   A 179 ? 0.124018  0.249412 0.103893  0.0167649   0.00358841  0.0229531   179 GLY   A N    
1385 C  CA   . GLY   A 179 ? 0.11839   0.248274 0.0971305 0.0123549   0.0106452   0.0244765   179 GLY   A CA   
1386 C  C    . GLY   A 179 ? 0.127815  0.257261 0.089434  0.00512726  0.00413329  0.0246017   179 GLY   A C    
1387 O  O    . GLY   A 179 ? 0.124807  0.263244 0.106063  -0.00035767 0.00267135  0.0164472   179 GLY   A O    
1388 N  N    . ASN   A 180 ? 0.128364  0.270564 0.0725582 0.00710159  0.00355549  0.0309037   180 ASN   A N    
1389 C  CA   . ASN   A 180 ? 0.140838  0.287346 0.0744147 0.0184569   0.00070158  0.0277239   180 ASN   A CA   
1390 C  C    . ASN   A 180 ? 0.12726   0.269151 0.0656186 0.0102297   0.00055155  0.0218271   180 ASN   A C    
1391 O  O    . ASN   A 180 ? 0.12268   0.27795  0.0661175 0.0111595   -0.00416742 0.0214323   180 ASN   A O    
1392 C  CB   . ASN   A 180 ? 0.155013  0.305428 0.09054   0.0311026   0.00936459  0.043137    180 ASN   A CB   
1393 C  CG   . ASN   A 180 ? 0.192169  0.336612 0.129265  0.0470189   0.0265369   0.0450788   180 ASN   A CG   
1394 O  OD1  . ASN   A 180 ? 0.21694   0.411675 0.140903  0.0972747   0.0183792   0.0744383   180 ASN   A OD1  
1395 N  ND2  . ASN   A 180 ? 0.223426  0.33326  0.194538  0.0589598   0.0244209   0.042542    180 ASN   A ND2  
1396 N  N    . PHE   A 181 ? 0.125125  0.267412 0.0707156 0.00590504  -0.00431727 0.0225304   181 PHE   A N    
1397 C  CA   . PHE   A 181 ? 0.138594  0.258242 0.0739781 0.00448965  0.00080528  0.0163187   181 PHE   A CA   
1398 C  C    . PHE   A 181 ? 0.130544  0.264095 0.068016  0.00724208  0.00022678  0.0188839   181 PHE   A C    
1399 O  O    . PHE   A 181 ? 0.139142  0.280274 0.0662929 0.00914156  0.00155225  0.0309127   181 PHE   A O    
1400 C  CB   . PHE   A 181 ? 0.134661  0.26298  0.0769473 0.00262106  -0.00960903 0.0139656   181 PHE   A CB   
1401 C  CG   . PHE   A 181 ? 0.133511  0.259798 0.0702605 0.00042797  -0.0144024  0.0108722   181 PHE   A CG   
1402 C  CD1  . PHE   A 181 ? 0.133247  0.273053 0.0725588 -0.00413379 -0.0251209  0.0138345   181 PHE   A CD1  
1403 C  CD2  . PHE   A 181 ? 0.131815  0.260083 0.0819026 0.00070216  -0.0085214  0.0153336   181 PHE   A CD2  
1404 C  CE1  . PHE   A 181 ? 0.139327  0.266242 0.0937516 -0.00593822 -0.0198602  0.0130434   181 PHE   A CE1  
1405 C  CE2  . PHE   A 181 ? 0.135955  0.254272 0.0943738 -0.00358471 -0.0221016  0.0193324   181 PHE   A CE2  
1406 C  CZ   . PHE   A 181 ? 0.140061  0.263245 0.0863359 -0.00653825 -0.00781418 0.0150736   181 PHE   A CZ   
1407 N  N    . TYR   A 182 ? 0.124567  0.26778  0.0369545 0.00659327  0.00657592  0.0173102   182 TYR   A N    
1408 C  CA   . TYR   A 182 ? 0.117264  0.267276 0.0673818 0.00590766  0.00115079  0.0137912   182 TYR   A CA   
1409 C  C    . TYR   A 182 ? 0.134708  0.288586 0.0802109 0.00166078  0.00501199  0.00464401  182 TYR   A C    
1410 O  O    . TYR   A 182 ? 0.157752  0.284903 0.106824  -0.00146934 0.0165836   -0.0258244  182 TYR   A O    
1411 C  CB   . TYR   A 182 ? 0.117947  0.2494   0.0844556 0.00204676  -0.00701717 0.0189005   182 TYR   A CB   
1412 C  CG   . TYR   A 182 ? 0.116058  0.237109 0.0892634 0.00327651  -0.0100749  0.0195354   182 TYR   A CG   
1413 C  CD1  . TYR   A 182 ? 0.123949  0.235137 0.107224  -0.00095973 -0.01224    0.0176182   182 TYR   A CD1  
1414 C  CD2  . TYR   A 182 ? 0.117006  0.229422 0.0945611 0.00299193  -0.0087287  0.0209701   182 TYR   A CD2  
1415 C  CE1  . TYR   A 182 ? 0.123976  0.234947 0.107382  -0.00143307 -0.00618454 0.0181844   182 TYR   A CE1  
1416 C  CE2  . TYR   A 182 ? 0.118493  0.22274  0.0934986 0.00096802  -0.0195233  0.0235482   182 TYR   A CE2  
1417 C  CZ   . TYR   A 182 ? 0.117414  0.221851 0.0995782 -0.00180547 -0.012235   0.0202106   182 TYR   A CZ   
1418 O  OH   . TYR   A 182 ? 0.111818  0.216971 0.0977666 -0.00552483 -0.0130058  0.0164565   182 TYR   A OH   
1419 N  N    . GLY   A 183 ? 0.137085  0.339588 0.0829483 0.0137918   0.00710612  0.00092284  183 GLY   A N    
1420 C  CA   . GLY   A 183 ? 0.145596  0.375688 0.0913746 0.0252559   -0.00428381 -0.0107809  183 GLY   A CA   
1421 C  C    . GLY   A 183 ? 0.160053  0.416714 0.0872015 0.0233984   -0.0110601  -0.0197705  183 GLY   A C    
1422 O  O    . GLY   A 183 ? 0.177049  0.452976 0.096716  0.0432053   -0.0181351  -0.0358922  183 GLY   A O    
1423 N  N    . PRO   A 184 ? 0.176823  0.443702 0.0807581 0.0190782   -0.00426192 -0.0223869  184 PRO   A N    
1424 C  CA   . PRO   A 184 ? 0.180261  0.456121 0.0684942 0.0211786   -0.0114883  -0.0121588  184 PRO   A CA   
1425 C  C    . PRO   A 184 ? 0.206103  0.463101 0.10389   0.012246    -0.0128848  -0.00137379 184 PRO   A C    
1426 O  O    . PRO   A 184 ? 0.21406   0.503229 0.151411  0.0246056   -0.0273281  -0.0131181  184 PRO   A O    
1427 C  CB   . PRO   A 184 ? 0.200527  0.460716 0.0796552 0.0144537   0.0067146   -0.0123238  184 PRO   A CB   
1428 C  CG   . PRO   A 184 ? 0.209065  0.462296 0.09664   0.0193964   0.00209533  -0.028946   184 PRO   A CG   
1429 C  CD   . PRO   A 184 ? 0.188189  0.456874 0.0837908 0.0242769   -0.00276464 -0.022059   184 PRO   A CD   
1430 N  N    . PHE   A 185 ? 0.16851   0.423704 0.0939478 0.0268537   0.00163767  -0.0090282  185 PHE   A N    
1431 C  CA   . PHE   A 185 ? 0.155605  0.393047 0.095312  0.0378271   0.00527741  -0.00842682 185 PHE   A CA   
1432 C  C    . PHE   A 185 ? 0.15748   0.387035 0.101222  0.0345997   0.0122207   -0.0160834  185 PHE   A C    
1433 O  O    . PHE   A 185 ? 0.163738  0.398802 0.11128   0.0519049   0.0336867   -0.016113   185 PHE   A O    
1434 C  CB   . PHE   A 185 ? 0.154853  0.372844 0.0780163 0.0383417   0.00513821  -0.0219711  185 PHE   A CB   
1435 C  CG   . PHE   A 185 ? 0.153596  0.360953 0.0769062 0.0394945   -0.00114939 -0.0275947  185 PHE   A CG   
1436 C  CD1  . PHE   A 185 ? 0.160184  0.363454 0.0996529 0.0387182   -0.00890816 -0.0306019  185 PHE   A CD1  
1437 C  CD2  . PHE   A 185 ? 0.159054  0.35595  0.0967626 0.0381869   0.00205239  -0.0366268  185 PHE   A CD2  
1438 C  CE1  . PHE   A 185 ? 0.163349  0.374287 0.0960492 0.037566    -0.00679143 -0.0326911  185 PHE   A CE1  
1439 C  CE2  . PHE   A 185 ? 0.154445  0.363089 0.10986   0.0354824   -0.00938238 -0.0376426  185 PHE   A CE2  
1440 C  CZ   . PHE   A 185 ? 0.161236  0.370398 0.10634   0.0383444   -0.00434071 -0.0366441  185 PHE   A CZ   
1441 N  N    . VAL   A 186 ? 0.16653   0.377637 0.112717  0.0346427   0.0266581   -0.0194286  186 VAL   A N    
1442 C  CA   . VAL   A 186 ? 0.155137  0.370022 0.117316  0.0299181   0.013083    -0.0215841  186 VAL   A CA   
1443 C  C    . VAL   A 186 ? 0.141082  0.34159  0.109711  0.0341971   0.00406373  -0.0291564  186 VAL   A C    
1444 O  O    . VAL   A 186 ? 0.142883  0.340614 0.0948888 0.0316933   0.00541613  -0.0278603  186 VAL   A O    
1445 C  CB   . VAL   A 186 ? 0.169023  0.378799 0.125224  0.0257616   0.0126779   -0.0316946  186 VAL   A CB   
1446 C  CG1  . VAL   A 186 ? 0.186044  0.393752 0.128687  0.0270815   0.0104238   -0.0275754  186 VAL   A CG1  
1447 C  CG2  . VAL   A 186 ? 0.177791  0.385509 0.11804   0.021702    0.00934344  -0.0376976  186 VAL   A CG2  
1448 N  N    . ASP   A 187 ? 0.1242    0.326299 0.0963375 0.0290841   -0.00108516 -0.0290283  187 ASP   A N    
1449 C  CA   . ASP   A 187 ? 0.120741  0.317413 0.110969  0.0292844   0.00492118  -0.032941   187 ASP   A CA   
1450 C  C    . ASP   A 187 ? 0.129258  0.323917 0.140262  0.027688    -0.00801887 -0.0418366  187 ASP   A C    
1451 O  O    . ASP   A 187 ? 0.139773  0.321224 0.150889  0.0284749   0.0160514   -0.035822   187 ASP   A O    
1452 C  CB   . ASP   A 187 ? 0.137834  0.309769 0.111245  0.0245085   -0.00125317 -0.0351817  187 ASP   A CB   
1453 C  CG   . ASP   A 187 ? 0.133001  0.311109 0.102756  0.0290046   0.00020059  -0.0323917  187 ASP   A CG   
1454 O  OD1  . ASP   A 187 ? 0.134474  0.32876  0.104775  0.0322197   -0.00509267 -0.0242     187 ASP   A OD1  
1455 O  OD2  . ASP   A 187 ? 0.138704  0.30508  0.0901857 0.0328169   -0.00784323 -0.0257245  187 ASP   A OD2  
1456 N  N    . ARG   A 188 ? 0.136071  0.32683  0.134643  0.0405183   -0.0185813  -0.0514128  188 ARG   A N    
1457 C  CA   . ARG   A 188 ? 0.185864  0.362284 0.188048  0.0313392   -0.0462427  -0.0488899  188 ARG   A CA   
1458 C  C    . ARG   A 188 ? 0.160674  0.359653 0.156566  0.0331605   -0.046778   -0.0604557  188 ARG   A C    
1459 O  O    . ARG   A 188 ? 0.151146  0.384533 0.140279  0.0477168   -0.0419782  -0.059957   188 ARG   A O    
1460 C  CB   . ARG   A 188 ? 0.220167  0.410012 0.230772  0.0357859   -0.10252    -0.0372748  188 ARG   A CB   
1461 C  CG   . ARG   A 188 ? 0.285873  0.453026 0.262938  0.0370296   -0.0755445  -0.0110597  188 ARG   A CG   
1462 C  CD   . ARG   A 188 ? 0.276384  0.480026 0.25409   0.0590536   -0.0902829  -0.00853289 188 ARG   A CD   
1463 N  NE   . ARG   A 188 ? 0.291752  0.471432 0.200702  0.0595989   -0.043129   0.013725    188 ARG   A NE   
1464 C  CZ   . ARG   A 188 ? 0.340604  0.475854 0.201576  0.0435537   -0.0250319  0.0381484   188 ARG   A CZ   
1465 N  NH1  . ARG   A 188 ? 0.311768  0.505162 0.165796  0.0469379   0.00549072  0.0705621   188 ARG   A NH1  
1466 N  NH2  . ARG   A 188 ? 0.398221  0.463264 0.140038  0.0455544   -0.00875585 0.0314643   188 ARG   A NH2  
1467 N  N    . GLN   A 189 ? 0.184665  0.353534 0.181854  0.0396344   -0.0493651  -0.0500959  189 GLN   A N    
1468 C  CA   . GLN   A 189 ? 0.233088  0.365955 0.206621  0.0480897   -0.0360509  -0.0425236  189 GLN   A CA   
1469 C  C    . GLN   A 189 ? 0.303185  0.361184 0.216041  0.0431103   -0.0406411  -0.0490824  189 GLN   A C    
1470 O  O    . GLN   A 189 ? 0.43503   0.383003 0.192418  0.0371223   -0.0856094  -0.0512068  189 GLN   A O    
1471 C  CB   . GLN   A 189 ? 0.262492  0.391223 0.278769  0.0346286   -0.0156252  -0.0294231  189 GLN   A CB   
1472 C  CG   . GLN   A 189 ? 0.328297  0.416342 0.308074  0.0357169   -0.00200743 -0.0139692  189 GLN   A CG   
1473 C  CD   . GLN   A 189 ? 0.37267   0.455921 0.343844  0.026611    0.0118335   0.00901875  189 GLN   A CD   
1474 O  OE1  . GLN   A 189 ? 0.391139  0.48442  0.356779  0.0682632   0.0737979   0.0236289   189 GLN   A OE1  
1475 N  NE2  . GLN   A 189 ? 0.423735  0.459563 0.351258  0.0350713   -0.0110563  0.0128941   189 GLN   A NE2  
1476 N  N    . THR   A 190 ? 0.315702  0.359045 0.17126   0.0517579   -0.0249237  -0.0620478  190 THR   A N    
1477 C  CA   . THR   A 190 ? 0.275882  0.392327 0.172782  0.0497806   -0.0181126  -0.0625124  190 THR   A CA   
1478 C  C    . THR   A 190 ? 0.265519  0.414144 0.153515  0.0532056   -0.019068   -0.0781282  190 THR   A C    
1479 O  O    . THR   A 190 ? 0.249064  0.430458 0.185074  0.0597614   -0.0311138  -0.0899364  190 THR   A O    
1480 C  CB   . THR   A 190 ? 0.285145  0.405549 0.182276  0.0468904   0.00718565  -0.0514386  190 THR   A CB   
1481 O  OG1  . THR   A 190 ? 0.309156  0.454339 0.189441  0.0427185   -0.0104959  -0.0564713  190 THR   A OG1  
1482 C  CG2  . THR   A 190 ? 0.277818  0.391688 0.166624  0.0425565   0.015949    -0.05482    190 THR   A CG2  
1483 N  N    . ALA   A 191 ? 0.258877  0.430469 0.187266  0.0627224   -0.0256212  -0.0952304  191 ALA   A N    
1484 C  CA   . ALA   A 191 ? 0.259748  0.459447 0.211062  0.0598824   -0.0271489  -0.110207   191 ALA   A CA   
1485 C  C    . ALA   A 191 ? 0.228734  0.482659 0.216501  0.0470677   -0.0197608  -0.122886   191 ALA   A C    
1486 O  O    . ALA   A 191 ? 0.26595   0.536993 0.220241  0.0497376   0.00052716  -0.104366   191 ALA   A O    
1487 C  CB   . ALA   A 191 ? 0.270084  0.460304 0.231719  0.0728808   -0.0113526  -0.114213   191 ALA   A CB   
1488 N  N    . GLN   A 192 ? 0.242203  0.500248 0.27328   0.0385639   -0.0257411  -0.136267   192 GLN   A N    
1489 C  CA   . GLN   A 192 ? 0.20479   0.484913 0.281905  0.0354931   -0.00426573 -0.14875    192 GLN   A CA   
1490 C  C    . GLN   A 192 ? 0.238965  0.505874 0.297421  0.0368172   -0.0324891  -0.12961    192 GLN   A C    
1491 O  O    . GLN   A 192 ? 0.30178   0.523785 0.275972  0.0439542   -0.0188834  -0.12085    192 GLN   A O    
1492 C  CB   . GLN   A 192 ? 0.262823  0.481058 0.335555  0.0344045   0.00059182  -0.122553   192 GLN   A CB   
1493 C  CG   . GLN   A 192 ? 0.263228  0.441967 0.304062  0.0421944   0.00673249  -0.124181   192 GLN   A CG   
1494 C  CD   . GLN   A 192 ? 0.21126   0.417584 0.274194  0.0403254   0.0162426   -0.0978803  192 GLN   A CD   
1495 O  OE1  . GLN   A 192 ? 0.199956  0.39666  0.258812  0.0486985   0.0305602   -0.0934098  192 GLN   A OE1  
1496 N  NE2  . GLN   A 192 ? 0.200481  0.407614 0.245505  0.0365918   0.0127078   -0.0970626  192 GLN   A NE2  
1497 N  N    . ALA   A 193 ? 0.214419  0.506283 0.337831  0.0172405   -0.0188135  -0.137062   193 ALA   A N    
1498 C  CA   . ALA   A 193 ? 0.22033   0.515188 0.354408  0.0253781   -0.0202923  -0.148196   193 ALA   A CA   
1499 C  C    . ALA   A 193 ? 0.221272  0.531024 0.348516  0.0136646   0.00374955  -0.15587    193 ALA   A C    
1500 O  O    . ALA   A 193 ? 0.261678  0.558532 0.364419  0.00837447  0.0158208   -0.152924   193 ALA   A O    
1501 C  CB   . ALA   A 193 ? 0.220069  0.50863  0.375909  0.0305688   -0.0192877  -0.146309   193 ALA   A CB   
1502 N  N    . ALA   A 194 ? 0.209537  0.547268 0.34917   0.0174328   0.00571026  -0.168078   194 ALA   A N    
1503 C  CA   . ALA   A 194 ? 0.185222  0.531381 0.324143  0.0226656   0.0318133   -0.172284   194 ALA   A CA   
1504 C  C    . ALA   A 194 ? 0.193484  0.52744  0.298517  0.0251771   0.0165575   -0.177202   194 ALA   A C    
1505 O  O    . ALA   A 194 ? 0.184611  0.506935 0.310348  0.0389702   -0.00863342 -0.18059    194 ALA   A O    
1506 C  CB   . ALA   A 194 ? 0.222823  0.547768 0.341004  0.0157368   0.0165139   -0.164728   194 ALA   A CB   
1507 N  N    . GLY   A 195 ? 0.179398  0.551949 0.30145   0.017729    0.0324345   -0.170618   195 GLY   A N    
1508 C  CA   . GLY   A 195 ? 0.228847  0.561746 0.261254  0.0107793   0.0409201   -0.168256   195 GLY   A CA   
1509 C  C    . GLY   A 195 ? 0.199124  0.560916 0.256349  -0.00954781 0.038371    -0.166959   195 GLY   A C    
1510 O  O    . GLY   A 195 ? 0.191935  0.568126 0.256262  -0.0174457  0.0538814   -0.173795   195 GLY   A O    
1511 N  N    . THR   A 196 ? 0.212712  0.540415 0.250076  -0.0109979  0.0434647   -0.158819   196 THR   A N    
1512 C  CA   . THR   A 196 ? 0.23334   0.500338 0.272202  -0.0200566  0.0303588   -0.150797   196 THR   A CA   
1513 C  C    . THR   A 196 ? 0.206097  0.460396 0.281009  -0.0239909  0.0385932   -0.118588   196 THR   A C    
1514 O  O    . THR   A 196 ? 0.24088   0.457295 0.331896  -0.0409166  0.0356685   -0.114315   196 THR   A O    
1515 C  CB   . THR   A 196 ? 0.289132  0.532602 0.290654  -0.01154    0.0505545   -0.157443   196 THR   A CB   
1516 O  OG1  . THR   A 196 ? 0.392342  0.61746  0.404129  0.0133682   0.0421977   -0.0997924  196 THR   A OG1  
1517 C  CG2  . THR   A 196 ? 0.280476  0.530562 0.253471  -0.0105454  0.0207535   -0.185456   196 THR   A CG2  
1518 N  N    . ASP   A 197 ? 0.160726  0.411331 0.284359  -0.0301628  0.0288338   -0.129578   197 ASP   A N    
1519 C  CA   . ASP   A 197 ? 0.163669  0.391833 0.268879  -0.014316   0.0307787   -0.118186   197 ASP   A CA   
1520 C  C    . ASP   A 197 ? 0.157281  0.368727 0.225771  -0.00602184 0.0276245   -0.109635   197 ASP   A C    
1521 O  O    . ASP   A 197 ? 0.182163  0.362103 0.26385   -0.00735832 -0.00441681 -0.14093    197 ASP   A O    
1522 C  CB   . ASP   A 197 ? 0.177804  0.383679 0.265791  -0.00632271 0.0289814   -0.123165   197 ASP   A CB   
1523 C  CG   . ASP   A 197 ? 0.194672  0.374442 0.246754  0.013821    0.037505    -0.114505   197 ASP   A CG   
1524 O  OD1  . ASP   A 197 ? 0.236662  0.364738 0.248256  0.00343557  0.0581591   -0.0965071  197 ASP   A OD1  
1525 O  OD2  . ASP   A 197 ? 0.173289  0.390681 0.253005  0.0429976   -0.0157069  -0.108643   197 ASP   A OD2  
1526 N  N    . THR   A 198 ? 0.135449  0.344156 0.156182  0.009389    0.0186914   -0.0925723  198 THR   A N    
1527 C  CA   . THR   A 198 ? 0.135245  0.312606 0.11706   0.00628066  0.00172115  -0.0595601  198 THR   A CA   
1528 C  C    . THR   A 198 ? 0.12184   0.280113 0.0939788 0.00743454  0.0123428   -0.0412926  198 THR   A C    
1529 O  O    . THR   A 198 ? 0.110489  0.285288 0.0998866 0.0121572   0.00671728  -0.0422544  198 THR   A O    
1530 C  CB   . THR   A 198 ? 0.1676    0.32864  0.113042  0.0275624   -0.0116463  -0.0529953  198 THR   A CB   
1531 O  OG1  . THR   A 198 ? 0.201016  0.359179 0.130857  0.0493818   -0.0077188  -0.057816   198 THR   A OG1  
1532 C  CG2  . THR   A 198 ? 0.185744  0.347307 0.125913  0.0335939   -0.0235195  -0.0623063  198 THR   A CG2  
1533 N  N    . THR   A 199 ? 0.121276  0.255381 0.0718069 0.00201691  0.0174664   -0.029719   199 THR   A N    
1534 C  CA   . THR   A 199 ? 0.127047  0.249175 0.0599875 0.00512305  0.0200293   -0.0225719  199 THR   A CA   
1535 C  C    . THR   A 199 ? 0.131777  0.247996 0.0616453 0.00808335  0.0167683   -0.017005   199 THR   A C    
1536 O  O    . THR   A 199 ? 0.150725  0.244019 0.071154  -0.00091529 0.0109141   -0.0116912  199 THR   A O    
1537 C  CB   . THR   A 199 ? 0.134178  0.249812 0.0782733 0.00734906  0.0201679   -0.015635   199 THR   A CB   
1538 O  OG1  . THR   A 199 ? 0.154135  0.257448 0.101187  0.00650373  0.0135743   -0.0159748  199 THR   A OG1  
1539 C  CG2  . THR   A 199 ? 0.140627  0.251297 0.0913841 0.00708503  0.0179419   -0.0180806  199 THR   A CG2  
1540 N  N    . ILE   A 200 ? 0.12101   0.242657 0.0540533 0.00613494  0.0105686   -0.0125257  200 ILE   A N    
1541 C  CA   . ILE   A 200 ? 0.108201  0.235768 0.0508445 0.00568446  0.00975622  -0.00684096 200 ILE   A CA   
1542 C  C    . ILE   A 200 ? 0.107773  0.233784 0.0582016 0.00447188  0.00549772  -0.00134794 200 ILE   A C    
1543 O  O    . ILE   A 200 ? 0.102417  0.238982 0.0635454 0.0125722   -0.00214983 0.00560879  200 ILE   A O    
1544 C  CB   . ILE   A 200 ? 0.107289  0.242401 0.0548063 0.00818916  0.00856856  -0.00820002 200 ILE   A CB   
1545 C  CG1  . ILE   A 200 ? 0.108971  0.244762 0.0797367 0.0086094   0.0133561   -0.00659383 200 ILE   A CG1  
1546 C  CG2  . ILE   A 200 ? 0.111446  0.246852 0.0522655 0.00599773  0.00814956  -0.0070742  200 ILE   A CG2  
1547 C  CD1  . ILE   A 200 ? 0.104344  0.242445 0.0818685 0.0104036   0.0134709   -0.00072868 200 ILE   A CD1  
1548 N  N    . THR   A 201 ? 0.111133  0.222646 0.0602603 0.00012365  0.00323471  0.00317498  201 THR   A N    
1549 C  CA   . THR   A 201 ? 0.114628  0.21505  0.0708898 0.00045958  0.0159487   0.0110175   201 THR   A CA   
1550 C  C    . THR   A 201 ? 0.101272  0.208489 0.0576278 0.00486468  0.0111661   0.0148802   201 THR   A C    
1551 O  O    . THR   A 201 ? 0.103982  0.223456 0.0594978 0.00939229  0.00307252  0.0147673   201 THR   A O    
1552 C  CB   . THR   A 201 ? 0.132226  0.212785 0.0762271 -0.00074753 0.020883    0.0148098   201 THR   A CB   
1553 O  OG1  . THR   A 201 ? 0.127128  0.214084 0.0958151 0.00181553  0.0264089   0.00469905  201 THR   A OG1  
1554 C  CG2  . THR   A 201 ? 0.13285   0.22783  0.0731713 0.00577376  0.0263684   0.0147272   201 THR   A CG2  
1555 N  N    . VAL   A 202 ? 0.0997068 0.21092  0.0631947 0.00704143  0.00852453  0.0129049   202 VAL   A N    
1556 C  CA   . VAL   A 202 ? 0.107848  0.21257  0.0649078 0.0010929   0.014173    0.0128383   202 VAL   A CA   
1557 C  C    . VAL   A 202 ? 0.105223  0.211306 0.0617032 -0.00101203 0.00991507  0.00674215  202 VAL   A C    
1558 O  O    . VAL   A 202 ? 0.10677   0.226065 0.0572045 -0.00485144 0.00658759  0.00949764  202 VAL   A O    
1559 C  CB   . VAL   A 202 ? 0.117775  0.223745 0.0719406 0.00588322  0.0160949   0.0135508   202 VAL   A CB   
1560 C  CG1  . VAL   A 202 ? 0.117292  0.22896  0.0718645 0.0074172   0.0178077   0.0105834   202 VAL   A CG1  
1561 C  CG2  . VAL   A 202 ? 0.126393  0.235207 0.0817864 0.00725577  0.00777894  0.0109015   202 VAL   A CG2  
1562 N  N    . ASN   A 203 ? 0.101508  0.21221  0.0520129 -0.00212273 0.0073036   0.00427572  203 ASN   A N    
1563 C  CA   . ASN   A 203 ? 0.0991162 0.20526  0.0526446 0.00324814  0.0123426   0.00567197  203 ASN   A CA   
1564 C  C    . ASN   A 203 ? 0.0985154 0.206958 0.0552913 0.00397951  0.00804046  -0.00227472 203 ASN   A C    
1565 O  O    . ASN   A 203 ? 0.1003    0.220573 0.05515   0.0104475   0.00687712  -0.0110011  203 ASN   A O    
1566 C  CB   . ASN   A 203 ? 0.102311  0.199444 0.0604072 0.00421546  0.00891759  0.00757032  203 ASN   A CB   
1567 C  CG   . ASN   A 203 ? 0.103144  0.195354 0.0523684 0.00626309  0.00739621  0.00638323  203 ASN   A CG   
1568 O  OD1  . ASN   A 203 ? 0.0983841 0.196305 0.0435138 0.00758708  0.0061424   0.00116025  203 ASN   A OD1  
1569 N  ND2  . ASN   A 203 ? 0.0959548 0.201556 0.0730727 0.00956196  0.00102999  0.00423329  203 ASN   A ND2  
1570 N  N    . VAL   A 204 ? 0.0965794 0.199619 0.056584  0.011695    0.00789873  -0.0018174  204 VAL   A N    
1571 C  CA   . VAL   A 204 ? 0.104843  0.191656 0.0520745 0.0114034   0.0127011   -0.00184259 204 VAL   A CA   
1572 C  C    . VAL   A 204 ? 0.108448  0.193062 0.0533163 0.0113763   0.00543992  0.00019182  204 VAL   A C    
1573 O  O    . VAL   A 204 ? 0.106809  0.202142 0.0427064 0.0105217   0.00810194  0.009201    204 VAL   A O    
1574 C  CB   . VAL   A 204 ? 0.113891  0.190826 0.0583416 0.00747983  0.0139474   -0.00653749 204 VAL   A CB   
1575 C  CG1  . VAL   A 204 ? 0.115328  0.195167 0.0620322 0.00546868  0.0132088   -0.0087713  204 VAL   A CG1  
1576 C  CG2  . VAL   A 204 ? 0.1183    0.190403 0.0651683 0.00564951  0.0134707   -0.0125529  204 VAL   A CG2  
1577 N  N    . LEU   A 205 ? 0.104508  0.195021 0.0472434 0.00906758  0.00679031  0.00292645  205 LEU   A N    
1578 C  CA   . LEU   A 205 ? 0.108665  0.20322  0.0534367 0.00862682  0.0100623   0.00235009  205 LEU   A CA   
1579 C  C    . LEU   A 205 ? 0.10202   0.206339 0.0515881 0.00700075  0.00714838  0.00010537  205 LEU   A C    
1580 O  O    . LEU   A 205 ? 0.0985879 0.218595 0.0491732 0.00552812  0.00916437  -0.00023995 205 LEU   A O    
1581 C  CB   . LEU   A 205 ? 0.107537  0.210461 0.0582792 0.012557    0.00955225  0.00658011  205 LEU   A CB   
1582 C  CG   . LEU   A 205 ? 0.116898  0.224128 0.0582773 0.0177585   0.00587435  0.00631163  205 LEU   A CG   
1583 C  CD1  . LEU   A 205 ? 0.120321  0.23396  0.0626246 0.0189122   0.0071194   0.0147453   205 LEU   A CD1  
1584 C  CD2  . LEU   A 205 ? 0.11923   0.230111 0.0662607 0.0218175   0.00498845  0.0110948   205 LEU   A CD2  
1585 N  N    . ALA   A 206 ? 0.100809  0.209284 0.0567992 0.00586591  0.00892123  -0.00459824 206 ALA   A N    
1586 C  CA   . ALA   A 206 ? 0.110202  0.208136 0.0545256 0.00663249  0.00956215  0.00081307  206 ALA   A CA   
1587 C  C    . ALA   A 206 ? 0.101454  0.209241 0.0536047 0.00276205  0.00630757  -0.00014969 206 ALA   A C    
1588 O  O    . ALA   A 206 ? 0.0911238 0.225422 0.0549148 -0.0011217  0.012208    -0.00246092 206 ALA   A O    
1589 C  CB   . ALA   A 206 ? 0.114244  0.214578 0.0568935 0.0142427   0.0074492   0.00112022  206 ALA   A CB   
1590 N  N    . TRP   A 207 ? 0.110635  0.205426 0.0511781 0.00389266  -0.00090893 0.00104926  207 TRP   A N    
1591 C  CA   . TRP   A 207 ? 0.108435  0.206286 0.0580744 0.00725885  0.00038237  0.00063838  207 TRP   A CA   
1592 C  C    . TRP   A 207 ? 0.106551  0.214732 0.0456484 0.00759329  0.00107548  0.0025427   207 TRP   A C    
1593 O  O    . TRP   A 207 ? 0.110921  0.225487 0.0449135 0.00361793  -0.00302312 0.00081655  207 TRP   A O    
1594 C  CB   . TRP   A 207 ? 0.119078  0.209522 0.0809933 0.00584683  0.00241982  -0.0008521  207 TRP   A CB   
1595 C  CG   . TRP   A 207 ? 0.126629  0.219222 0.103739  -0.0050511  -0.00597968 0.00367778  207 TRP   A CG   
1596 C  CD1  . TRP   A 207 ? 0.138739  0.227609 0.110786  -0.00690649 -0.00186934 0.00582267  207 TRP   A CD1  
1597 C  CD2  . TRP   A 207 ? 0.128241  0.223083 0.135666  -0.00176763 -0.0147367  0.00473928  207 TRP   A CD2  
1598 N  NE1  . TRP   A 207 ? 0.149547  0.231607 0.124792  -0.00836976 -0.0231256  0.0135984   207 TRP   A NE1  
1599 C  CE2  . TRP   A 207 ? 0.137069  0.228994 0.150827  0.00376231  -0.0238855  0.00573194  207 TRP   A CE2  
1600 C  CE3  . TRP   A 207 ? 0.133884  0.233428 0.154681  -0.00236315 -0.00951826 -0.00819079 207 TRP   A CE3  
1601 C  CZ2  . TRP   A 207 ? 0.141827  0.236791 0.177662  0.00683631  -0.0252149  0.00646352  207 TRP   A CZ2  
1602 C  CZ3  . TRP   A 207 ? 0.145463  0.236908 0.180442  0.00444774  -0.0153364  -0.0039997  207 TRP   A CZ3  
1603 C  CH2  . TRP   A 207 ? 0.147975  0.232087 0.189149  0.0110508   -0.0268323  0.00010268  207 TRP   A CH2  
1604 N  N    . LEU   A 208 ? 0.105837  0.215473 0.0402416 0.00492293  -0.00209633 0.00362998  208 LEU   A N    
1605 C  CA   . LEU   A 208 ? 0.110472  0.216737 0.048804  0.00846675  0.00549876  0.00110489  208 LEU   A CA   
1606 C  C    . LEU   A 208 ? 0.102778  0.207326 0.0475811 0.00857967  0.0050247   0.00221829  208 LEU   A C    
1607 O  O    . LEU   A 208 ? 0.106812  0.212044 0.0641266 0.0167209   -0.0110468  -0.00509935 208 LEU   A O    
1608 C  CB   . LEU   A 208 ? 0.114203  0.221124 0.0523487 0.0111567   0.00929335  0.00096894  208 LEU   A CB   
1609 C  CG   . LEU   A 208 ? 0.120528  0.220621 0.0676653 0.0178547   0.00827036  -0.00124756 208 LEU   A CG   
1610 C  CD1  . LEU   A 208 ? 0.134634  0.225429 0.0694679 0.0177877   0.0100841   -0.00036384 208 LEU   A CD1  
1611 C  CD2  . LEU   A 208 ? 0.135615  0.224868 0.0761883 0.0213344   0.00751478  -0.00404375 208 LEU   A CD2  
1612 N  N    . TYR   A 209 ? 0.106839  0.200628 0.0536802 0.0068647   -0.00072258 -3.746e-05  209 TYR   A N    
1613 C  CA   . TYR   A 209 ? 0.11219   0.203467 0.0626522 -0.00328923 0.00208707  0.00149386  209 TYR   A CA   
1614 C  C    . TYR   A 209 ? 0.11795   0.20165  0.06099   -0.00516812 -0.00497784 -0.00239742 209 TYR   A C    
1615 O  O    . TYR   A 209 ? 0.113699  0.205954 0.0858301 -0.0117766  -0.00701929 -0.00623487 209 TYR   A O    
1616 C  CB   . TYR   A 209 ? 0.127301  0.210415 0.0693    0.00037163  0.00510315  0.00203458  209 TYR   A CB   
1617 C  CG   . TYR   A 209 ? 0.125667  0.210552 0.0663561 -0.00027561 0.00224564  0.00532699  209 TYR   A CG   
1618 C  CD1  . TYR   A 209 ? 0.134798  0.218472 0.073096  -0.00382133 0.00012468  0.00870327  209 TYR   A CD1  
1619 C  CD2  . TYR   A 209 ? 0.131978  0.222216 0.0684874 -0.00050544 0.00220683  0.00858487  209 TYR   A CD2  
1620 C  CE1  . TYR   A 209 ? 0.131364  0.217097 0.0759501 -0.00635292 0.00365178  0.0114541   209 TYR   A CE1  
1621 C  CE2  . TYR   A 209 ? 0.136381  0.220539 0.0658496 -0.00462268 0.0007788   0.00714075  209 TYR   A CE2  
1622 C  CZ   . TYR   A 209 ? 0.139896  0.229331 0.0674253 -0.0067264  0.00785764  0.00262736  209 TYR   A CZ   
1623 O  OH   . TYR   A 209 ? 0.15501   0.249071 0.0585634 -0.00519664 0.00662147  0.0056022   209 TYR   A OH   
1624 N  N    . ALA   A 210 ? 0.121377  0.200526 0.047973  -0.00693284 -0.0104803  -4.231e-05  210 ALA   A N    
1625 C  CA   . ALA   A 210 ? 0.127655  0.195901 0.0477829 -0.00217166 -0.00489135 -0.00552267 210 ALA   A CA   
1626 C  C    . ALA   A 210 ? 0.123647  0.196809 0.0521474 -0.00278218 -0.0137651  -0.00767441 210 ALA   A C    
1627 O  O    . ALA   A 210 ? 0.125516  0.206432 0.043772  -0.00361307 -0.00718382 -0.0105734  210 ALA   A O    
1628 C  CB   . ALA   A 210 ? 0.128114  0.196587 0.0562508 -0.00384793 -0.0105294  -0.00827221 210 ALA   A CB   
1629 N  N    . ALA   A 211 ? 0.120271  0.191349 0.057656  0.00231714  -0.0134015  -0.00026835 211 ALA   A N    
1630 C  CA   . ALA   A 211 ? 0.118598  0.192165 0.0701221 0.00457664  -0.00466464 -8.63e-05   211 ALA   A CA   
1631 C  C    . ALA   A 211 ? 0.116875  0.19878  0.0640943 0.00442866  -0.00578025 0.00043361  211 ALA   A C    
1632 O  O    . ALA   A 211 ? 0.116391  0.219838 0.059506  0.00870593  -0.004035   0.0075999   211 ALA   A O    
1633 C  CB   . ALA   A 211 ? 0.116449  0.191899 0.080712  0.00349331  0.00030566  -0.00426095 211 ALA   A CB   
1634 N  N    . VAL   A 212 ? 0.123661  0.201545 0.060333  0.00415495  -0.00402172 3.663e-05   212 VAL   A N    
1635 C  CA   . VAL   A 212 ? 0.125686  0.206603 0.0636668 0.00369106  -0.00497619 -0.00402216 212 VAL   A CA   
1636 C  C    . VAL   A 212 ? 0.120287  0.208745 0.0675928 0.00134879  -0.00835064 -0.00977165 212 VAL   A C    
1637 O  O    . VAL   A 212 ? 0.109527  0.228683 0.0772655 -0.00234039 -0.00690364 -0.00901267 212 VAL   A O    
1638 C  CB   . VAL   A 212 ? 0.133401  0.210776 0.0766125 0.00055119  0.00330704  -0.00056875 212 VAL   A CB   
1639 C  CG1  . VAL   A 212 ? 0.137136  0.219709 0.0794427 -0.00168298 0.00799598  0.00080579  212 VAL   A CG1  
1640 C  CG2  . VAL   A 212 ? 0.133884  0.214762 0.0775372 -0.00089063 0.00462437  -0.00434209 212 VAL   A CG2  
1641 N  N    . ILE   A 213 ? 0.113573  0.21543  0.0745042 0.00069047  -0.0123048  -0.021465   213 ILE   A N    
1642 C  CA   . ILE   A 213 ? 0.1248    0.219287 0.0790982 0.00712834  -0.00673284 -0.0233879  213 ILE   A CA   
1643 C  C    . ILE   A 213 ? 0.126298  0.226381 0.0831628 0.00794247  -0.00580278 -0.0228029  213 ILE   A C    
1644 O  O    . ILE   A 213 ? 0.133607  0.244266 0.0858476 0.00189383  -0.00519349 -0.0350534  213 ILE   A O    
1645 C  CB   . ILE   A 213 ? 0.135758  0.222648 0.0931614 0.0120702   0.00054771  -0.0180974  213 ILE   A CB   
1646 C  CG1  . ILE   A 213 ? 0.149107  0.227819 0.104672  0.0161582   -0.00273516 -0.0146658  213 ILE   A CG1  
1647 C  CG2  . ILE   A 213 ? 0.150567  0.224688 0.0969696 0.0170777   0.00370265  -0.016837   213 ILE   A CG2  
1648 C  CD1  . ILE   A 213 ? 0.150345  0.242217 0.119108  0.0110443   -0.00769008 -0.0115538  213 ILE   A CD1  
1649 N  N    . ASN   A 214 ? 0.126615  0.225816 0.0746408 0.0112131   0.00028352  -0.0141077  214 ASN   A N    
1650 C  CA   . ASN   A 214 ? 0.144473  0.245072 0.0882446 0.0137399   0.00030496  -0.00081635 214 ASN   A CA   
1651 C  C    . ASN   A 214 ? 0.133245  0.255159 0.0893547 0.0110629   -0.00347348 0.00844534  214 ASN   A C    
1652 O  O    . ASN   A 214 ? 0.16835   0.300472 0.0927251 0.00407837  0.00254361  0.0339265   214 ASN   A O    
1653 C  CB   . ASN   A 214 ? 0.153878  0.246991 0.0900365 0.0102531   0.00929005  0.00433215  214 ASN   A CB   
1654 C  CG   . ASN   A 214 ? 0.175944  0.258894 0.0980207 0.0164422   0.0246103   0.00768228  214 ASN   A CG   
1655 O  OD1  . ASN   A 214 ? 0.193184  0.270763 0.128396  0.00921931  0.0401322   0.0100993   214 ASN   A OD1  
1656 N  ND2  . ASN   A 214 ? 0.184609  0.277575 0.164664  0.00788909  0.0342746   0.00651333  214 ASN   A ND2  
1657 N  N    . GLY   A 215 ? 0.123996  0.254029 0.0783992 0.0148491   -0.00919845 -0.00156209 215 GLY   A N    
1658 C  CA   . GLY   A 215 ? 0.123194  0.251976 0.0862185 0.0184784   -0.0146122  -0.005998   215 GLY   A CA   
1659 C  C    . GLY   A 215 ? 0.117944  0.261716 0.0990609 0.0261836   -0.00699725 -0.0103184  215 GLY   A C    
1660 O  O    . GLY   A 215 ? 0.127613  0.3106   0.147967  0.043249    -0.0256549  -0.0234535  215 GLY   A O    
1661 N  N    . ASP   A 216 ? 0.118013  0.253168 0.0871479 0.0264447   -0.0039052  -0.00900684 216 ASP   A N    
1662 C  CA   . ASP   A 216 ? 0.144107  0.25852  0.100678  0.0276634   0.00332796  -0.00599576 216 ASP   A CA   
1663 C  C    . ASP   A 216 ? 0.135209  0.249254 0.0907284 0.0228876   0.00303221  -0.0133395  216 ASP   A C    
1664 O  O    . ASP   A 216 ? 0.159373  0.265574 0.0953287 0.0369698   -0.00535435 -0.00856086 216 ASP   A O    
1665 C  CB   . ASP   A 216 ? 0.177508  0.292121 0.143626  0.0169631   0.013175    -0.0113741  216 ASP   A CB   
1666 C  CG   . ASP   A 216 ? 0.23314   0.329226 0.182643  0.0264871   0.0173034   0.0109758   216 ASP   A CG   
1667 O  OD1  . ASP   A 216 ? 0.259588  0.379873 0.233124  0.0432073   0.0134129   0.016056    216 ASP   A OD1  
1668 O  OD2  . ASP   A 216 ? 0.259258  0.390988 0.24786   0.0232673   0.0549313   0.00329717  216 ASP   A OD2  
1669 N  N    . ARG   A 217 ? 0.129936  0.2451   0.0777233 0.0160717   0.00590836  -0.0027399  217 ARG   A N    
1670 C  CA   . ARG   A 217 ? 0.138522  0.252914 0.0744559 0.010281    0.00478473  -0.00725698 217 ARG   A CA   
1671 C  C    . ARG   A 217 ? 0.115025  0.245584 0.0670151 0.00868531  -0.00564778 -0.00515536 217 ARG   A C    
1672 O  O    . ARG   A 217 ? 0.124412  0.269751 0.0640701 0.0119895   0.00670415  -0.0105326  217 ARG   A O    
1673 C  CB   . ARG   A 217 ? 0.155292  0.256381 0.0875747 0.00246666  0.0247483   0.00350493  217 ARG   A CB   
1674 C  CG   . ARG   A 217 ? 0.169097  0.254235 0.101177  0.00010317  0.0203635   0.00678157  217 ARG   A CG   
1675 C  CD   . ARG   A 217 ? 0.16098   0.256188 0.0954943 0.00154041  0.0256294   0.00771005  217 ARG   A CD   
1676 N  NE   . ARG   A 217 ? 0.145747  0.256404 0.0995405 0.00195995  0.0262052   0.00823059  217 ARG   A NE   
1677 C  CZ   . ARG   A 217 ? 0.141808  0.248462 0.102661  -0.0026344  0.0181479   0.00648226  217 ARG   A CZ   
1678 N  NH1  . ARG   A 217 ? 0.149018  0.246821 0.0961747 0.00335561  0.0156753   0.00885661  217 ARG   A NH1  
1679 N  NH2  . ARG   A 217 ? 0.142044  0.261979 0.0933011 0.00378994  0.0138784   -0.00269272 217 ARG   A NH2  
1680 N  N    . TRP   A 218 ? 0.117542  0.246205 0.0636945 0.0151078   -0.00397368 -0.00664425 218 TRP   A N    
1681 C  CA   . TRP   A 218 ? 0.12607   0.238527 0.0795528 0.0223848   -0.00718034 -0.00613525 218 TRP   A CA   
1682 C  C    . TRP   A 218 ? 0.122367  0.236296 0.0806362 0.0226001   -0.00287536 -0.0152711  218 TRP   A C    
1683 O  O    . TRP   A 218 ? 0.118878  0.25442  0.0764467 0.0210513   0.00721922  -0.00619951 218 TRP   A O    
1684 C  CB   . TRP   A 218 ? 0.146257  0.241694 0.0815218 0.0337055   -3.733e-05  0.002191    218 TRP   A CB   
1685 C  CG   . TRP   A 218 ? 0.15254   0.256594 0.0993803 0.036135    0.0131173   0.0102785   218 TRP   A CG   
1686 C  CD1  . TRP   A 218 ? 0.157849  0.272444 0.118781  0.0415691   0.0212696   0.0103033   218 TRP   A CD1  
1687 C  CD2  . TRP   A 218 ? 0.145318  0.256031 0.131021  0.0377628   0.00173568  0.0142946   218 TRP   A CD2  
1688 N  NE1  . TRP   A 218 ? 0.168508  0.274811 0.132378  0.0417008   0.0241225   0.0122038   218 TRP   A NE1  
1689 C  CE2  . TRP   A 218 ? 0.156525  0.264811 0.150486  0.0357008   0.0069715   0.0101702   218 TRP   A CE2  
1690 C  CE3  . TRP   A 218 ? 0.158636  0.258604 0.14435   0.0302814   0.00045909  0.00518949  218 TRP   A CE3  
1691 C  CZ2  . TRP   A 218 ? 0.163411  0.265792 0.169138  0.0294629   0.00150289  0.0146555   218 TRP   A CZ2  
1692 C  CZ3  . TRP   A 218 ? 0.175261  0.26732  0.156994  0.0281559   -0.00646798 0.00379947  218 TRP   A CZ3  
1693 C  CH2  . TRP   A 218 ? 0.17229   0.265446 0.176316  0.0271202   -0.0162652  0.00800546  218 TRP   A CH2  
1694 N  N    . PHE   A 219 ? 0.113572  0.231034 0.0685618 0.0184585   -0.00285295 -0.0136479  219 PHE   A N    
1695 C  CA   . PHE   A 219 ? 0.111314  0.233006 0.0789579 0.0154333   -0.0102592  -0.0136529  219 PHE   A CA   
1696 C  C    . PHE   A 219 ? 0.111451  0.243651 0.0743645 0.0203271   -0.00439584 -0.0152116  219 PHE   A C    
1697 O  O    . PHE   A 219 ? 0.117484  0.262035 0.0710706 0.0147044   -0.0099835  -0.0103245  219 PHE   A O    
1698 C  CB   . PHE   A 219 ? 0.113399  0.23043  0.0857458 0.0127968   -0.011601   -0.00883372 219 PHE   A CB   
1699 C  CG   . PHE   A 219 ? 0.119861  0.218975 0.0905433 0.00974093  -0.00599931 -0.0033203  219 PHE   A CG   
1700 C  CD1  . PHE   A 219 ? 0.133675  0.212446 0.0926282 0.00521031  0.0041913   -0.00062898 219 PHE   A CD1  
1701 C  CD2  . PHE   A 219 ? 0.131199  0.212471 0.091305  0.0127215   -0.00326354 0.00272637  219 PHE   A CD2  
1702 C  CE1  . PHE   A 219 ? 0.134882  0.213762 0.0875107 0.00798257  0.00801866  0.00536381  219 PHE   A CE1  
1703 C  CE2  . PHE   A 219 ? 0.133388  0.212958 0.0865986 0.00997808  0.00910097  0.00083205  219 PHE   A CE2  
1704 C  CZ   . PHE   A 219 ? 0.134457  0.215248 0.0872491 0.0117678   0.0173438   0.00238938  219 PHE   A CZ   
1705 N  N    . LEU   A 220 ? 0.112936  0.245351 0.0742365 0.0197633   -0.00804986 -0.00731203 220 LEU   A N    
1706 C  CA   . LEU   A 220 ? 0.119765  0.245201 0.089141  0.0221798   -0.00464198 -0.00558238 220 LEU   A CA   
1707 C  C    . LEU   A 220 ? 0.125521  0.241723 0.0888362 0.0259783   -0.00363644 -0.00542706 220 LEU   A C    
1708 O  O    . LEU   A 220 ? 0.137206  0.239111 0.0807799 0.0296794   -0.00327876 0.00845846  220 LEU   A O    
1709 C  CB   . LEU   A 220 ? 0.129373  0.251437 0.104089  0.0182758   -0.011198   -0.00518762 220 LEU   A CB   
1710 C  CG   . LEU   A 220 ? 0.133628  0.251836 0.118331  0.0195115   -0.0150339  -0.0098051  220 LEU   A CG   
1711 C  CD1  . LEU   A 220 ? 0.152028  0.252275 0.121604  0.0192671   -0.0222344  -0.00552585 220 LEU   A CD1  
1712 C  CD2  . LEU   A 220 ? 0.132379  0.25681  0.127598  0.0168242   -0.0161817  -0.00756401 220 LEU   A CD2  
1713 N  N    . ASN   A 221 ? 0.121219  0.251479 0.0893606 0.0210801   0.00628501  -0.00205244 221 ASN   A N    
1714 C  CA   . ASN   A 221 ? 0.116662  0.252927 0.0959203 0.015405    0.0057002   -0.00521962 221 ASN   A CA   
1715 C  C    . ASN   A 221 ? 0.119065  0.259345 0.0924723 0.008423    -0.00373407 -0.00444395 221 ASN   A C    
1716 O  O    . ASN   A 221 ? 0.136303  0.273413 0.0888609 0.00991219  0.002348    -0.00115443 221 ASN   A O    
1717 C  CB   . ASN   A 221 ? 0.12316   0.247159 0.119274  0.00771241  0.00718334  -0.00997579 221 ASN   A CB   
1718 C  CG   . ASN   A 221 ? 0.138694  0.256429 0.157637  0.00771503  -0.00974349 -0.0140558  221 ASN   A CG   
1719 O  OD1  . ASN   A 221 ? 0.128394  0.25056  0.13727   -0.00169198 -0.0118795  -0.00991772 221 ASN   A OD1  
1720 N  ND2  . ASN   A 221 ? 0.177433  0.280152 0.254357  0.00965405  -0.0553865  -0.0139179  221 ASN   A ND2  
1721 N  N    . ARG   A 222 ? 0.114453  0.264546 0.0888668 0.00137999  2.879e-05   0.00257577  222 ARG   A N    
1722 C  CA   . ARG   A 222 ? 0.130974  0.275224 0.103747  -0.00596773 0.00145215  0.00793194  222 ARG   A CA   
1723 C  C    . ARG   A 222 ? 0.12493   0.281552 0.10859   -0.0001698  0.00421739  0.0127783   222 ARG   A C    
1724 O  O    . ARG   A 222 ? 0.141801  0.278378 0.153921  -0.0145574  -0.00670513 0.0187523   222 ARG   A O    
1725 C  CB   . ARG   A 222 ? 0.125881  0.293694 0.131312  -0.00739299 0.00097351  0.0128817   222 ARG   A CB   
1726 C  CG   . ARG   A 222 ? 0.133919  0.305087 0.148828  -0.00494868 0.0136775   0.00960793  222 ARG   A CG   
1727 C  CD   . ARG   A 222 ? 0.154281  0.331624 0.177317  0.00097649  0.0293374   0.0157439   222 ARG   A CD   
1728 N  NE   . ARG   A 222 ? 0.202381  0.357784 0.217021  0.00810609  0.0283127   0.0291038   222 ARG   A NE   
1729 C  CZ   . ARG   A 222 ? 0.221864  0.386253 0.215878  0.0102454   0.0555029   0.0336418   222 ARG   A CZ   
1730 N  NH1  . ARG   A 222 ? 0.236825  0.413776 0.182244  0.0275106   0.050121    0.0271647   222 ARG   A NH1  
1731 N  NH2  . ARG   A 222 ? 0.275099  0.394169 0.272268  0.00211333  0.0696356   0.0441454   222 ARG   A NH2  
1732 N  N    . PHE   A 223 ? 0.13211   0.29437  0.0879232 0.00471858  0.00212292  0.00772867  223 PHE   A N    
1733 C  CA   . PHE   A 223 ? 0.143247  0.316354 0.0939383 0.0150241   -0.00244882 0.00183563  223 PHE   A CA   
1734 C  C    . PHE   A 223 ? 0.148556  0.316137 0.103292  0.0144142   0.0012269   0.00137759  223 PHE   A C    
1735 O  O    . PHE   A 223 ? 0.142246  0.303402 0.116019  0.00913897  0.00796557  -0.0118595  223 PHE   A O    
1736 C  CB   . PHE   A 223 ? 0.167573  0.329099 0.121438  0.0197533   0.00198847  -0.0138745  223 PHE   A CB   
1737 C  CG   . PHE   A 223 ? 0.193798  0.349271 0.148082  0.0304154   0.0143347   -0.0370224  223 PHE   A CG   
1738 C  CD1  . PHE   A 223 ? 0.21647   0.376162 0.179806  0.0255086   0.0301859   -0.035826   223 PHE   A CD1  
1739 C  CD2  . PHE   A 223 ? 0.223936  0.35531  0.21417   0.0357632   0.0265029   -0.0486091  223 PHE   A CD2  
1740 C  CE1  . PHE   A 223 ? 0.231992  0.38547  0.188525  0.0359623   0.0387393   -0.0332805  223 PHE   A CE1  
1741 C  CE2  . PHE   A 223 ? 0.239772  0.367557 0.237461  0.044985    0.037429    -0.0465593  223 PHE   A CE2  
1742 C  CZ   . PHE   A 223 ? 0.243738  0.372165 0.255508  0.0429674   0.0396616   -0.037174   223 PHE   A CZ   
1743 N  N    . THR   A 224 ? 0.158218  0.342168 0.117236  0.0188489   -0.00319749 0.0122316   224 THR   A N    
1744 C  CA   . THR   A 224 ? 0.16285   0.33172  0.121689  0.0169026   -0.00851668 0.0148015   224 THR   A CA   
1745 C  C    . THR   A 224 ? 0.155313  0.307398 0.120187  0.0191741   -0.00053942 0.011811    224 THR   A C    
1746 O  O    . THR   A 224 ? 0.159813  0.307535 0.150382  0.0330745   -0.0134531  0.0111171   224 THR   A O    
1747 C  CB   . THR   A 224 ? 0.185096  0.356004 0.143209  -0.00313458 -0.0106706  0.017496    224 THR   A CB   
1748 O  OG1  . THR   A 224 ? 0.200636  0.366356 0.197985  -0.00153323 -0.0163092  0.0167381   224 THR   A OG1  
1749 C  CG2  . THR   A 224 ? 0.193207  0.364329 0.1616    -0.0159127  -0.00821263 0.0319535   224 THR   A CG2  
1750 N  N    . THR   A 225 ? 0.145966  0.28389  0.0951902 0.0144954   -0.00410691 0.00650925  225 THR   A N    
1751 C  CA   . THR   A 225 ? 0.144846  0.261235 0.0919519 0.0124114   -0.00170657 0.0065613   225 THR   A CA   
1752 C  C    . THR   A 225 ? 0.157354  0.248296 0.0906834 0.0137778   0.00222732  0.00298155  225 THR   A C    
1753 O  O    . THR   A 225 ? 0.175952  0.252227 0.0991064 0.0231269   -0.00168793 -0.00391937 225 THR   A O    
1754 C  CB   . THR   A 225 ? 0.153651  0.267048 0.0987018 0.00742643  0.00399464  0.00812214  225 THR   A CB   
1755 O  OG1  . THR   A 225 ? 0.140074  0.274806 0.11091   0.00511792  0.00677512  0.0161143   225 THR   A OG1  
1756 C  CG2  . THR   A 225 ? 0.161531  0.270032 0.0925201 -0.00163964 0.00466763  0.00898157  225 THR   A CG2  
1757 N  N    . THR   A 226 ? 0.149321  0.235325 0.0803564 0.0105124   0.00931789  0.00715809  226 THR   A N    
1758 C  CA   . THR   A 226 ? 0.151513  0.233272 0.0790124 0.012118    0.00576181  0.0152093   226 THR   A CA   
1759 C  C    . THR   A 226 ? 0.153161  0.220419 0.073093  0.00575591  0.00247119  0.00954033  226 THR   A C    
1760 O  O    . THR   A 226 ? 0.144006  0.221659 0.0767617 0.00874355  0.00900144  0.00334085  226 THR   A O    
1761 C  CB   . THR   A 226 ? 0.16912   0.238879 0.0858666 0.00653636  0.00846565  0.0263131   226 THR   A CB   
1762 O  OG1  . THR   A 226 ? 0.156996  0.250319 0.075275  0.00632692  0.00390766  0.0196805   226 THR   A OG1  
1763 C  CG2  . THR   A 226 ? 0.173626  0.243349 0.110076  0.00735427  0.0115986   0.0239539   226 THR   A CG2  
1764 N  N    . LEU   A 227 ? 0.166253  0.22301  0.0803151 0.00899116  0.00300442  0.0145778   227 LEU   A N    
1765 C  CA   . LEU   A 227 ? 0.166315  0.225758 0.0942686 0.0138762   0.0090247   0.0112323   227 LEU   A CA   
1766 C  C    . LEU   A 227 ? 0.155105  0.226295 0.0939954 0.0156426   0.0108288   0.0120702   227 LEU   A C    
1767 O  O    . LEU   A 227 ? 0.159241  0.232451 0.0868976 0.00830003  0.0147827   0.00387563  227 LEU   A O    
1768 C  CB   . LEU   A 227 ? 0.191805  0.223721 0.115453  0.0138616   0.00076361  0.00347167  227 LEU   A CB   
1769 C  CG   . LEU   A 227 ? 0.194646  0.228226 0.128409  0.0127281   -0.00177235 -0.00160371 227 LEU   A CG   
1770 C  CD1  . LEU   A 227 ? 0.200552  0.229439 0.120834  0.017774    0.00892379  -0.00469704 227 LEU   A CD1  
1771 C  CD2  . LEU   A 227 ? 0.205467  0.240433 0.154303  0.0219977   -0.00687491 -0.00941049 227 LEU   A CD2  
1772 N  N    . ASN   A 228 ? 0.160819  0.245063 0.093177  0.00678224  0.0194513   0.00829206  228 ASN   A N    
1773 C  CA   . ASN   A 228 ? 0.17718   0.261256 0.100483  0.00911375  0.0128656   0.00672367  228 ASN   A CA   
1774 C  C    . ASN   A 228 ? 0.151949  0.247693 0.0708145 0.0036615   0.0196975   0.00155565  228 ASN   A C    
1775 O  O    . ASN   A 228 ? 0.151253  0.244939 0.0803061 0.0054975   0.0184548   0.00720488  228 ASN   A O    
1776 C  CB   . ASN   A 228 ? 0.229035  0.288622 0.110975  0.0226924   -0.00639129 0.0199695   228 ASN   A CB   
1777 C  CG   . ASN   A 228 ? 0.263857  0.342316 0.174496  0.0160213   -0.0204174  0.00678506  228 ASN   A CG   
1778 O  OD1  . ASN   A 228 ? 0.315376  0.366298 0.179948  0.0388522   0.00067712  0.0113356   228 ASN   A OD1  
1779 N  ND2  . ASN   A 228 ? 0.293724  0.396824 0.199379  0.0176158   -0.0220753  -0.013395   228 ASN   A ND2  
1780 N  N    . ASP   A 229 ? 0.141291  0.248039 0.0675852 0.00123204  0.0254713   -0.00076203 229 ASP   A N    
1781 C  CA   . ASP   A 229 ? 0.135689  0.250382 0.0691914 0.00155811  0.0296545   0.00937702  229 ASP   A CA   
1782 C  C    . ASP   A 229 ? 0.131737  0.223209 0.0760067 0.00771651  0.0326121   0.00827204  229 ASP   A C    
1783 O  O    . ASP   A 229 ? 0.148735  0.226209 0.090163  0.00889894  0.0470659   5.329e-05   229 ASP   A O    
1784 C  CB   . ASP   A 229 ? 0.135308  0.271168 0.0829216 0.00874133  0.0365098   0.00983506  229 ASP   A CB   
1785 C  CG   . ASP   A 229 ? 0.156039  0.294455 0.0818048 -0.00099588 0.032054    0.0137803   229 ASP   A CG   
1786 O  OD1  . ASP   A 229 ? 0.1527    0.319116 0.101664  0.00212283  0.0255272   -0.00419968 229 ASP   A OD1  
1787 O  OD2  . ASP   A 229 ? 0.154518  0.32085  0.102018  -0.00575733 0.0266437   0.016766    229 ASP   A OD2  
1788 N  N    . PHE   A 230 ? 0.132395  0.212158 0.0811608 0.0119409   0.0253092   0.0116535   230 PHE   A N    
1789 C  CA   . PHE   A 230 ? 0.134294  0.22318  0.0838354 0.0105167   0.0189727   0.0174982   230 PHE   A CA   
1790 C  C    . PHE   A 230 ? 0.13266   0.218467 0.0808518 0.0135125   0.0276283   0.0140648   230 PHE   A C    
1791 O  O    . PHE   A 230 ? 0.139803  0.214376 0.0943426 0.00808341  0.0200044   0.0152507   230 PHE   A O    
1792 C  CB   . PHE   A 230 ? 0.133146  0.227087 0.0852618 0.0180037   0.0210763   0.0173889   230 PHE   A CB   
1793 C  CG   . PHE   A 230 ? 0.136753  0.248055 0.087402  0.0193812   0.0203836   0.0215399   230 PHE   A CG   
1794 C  CD1  . PHE   A 230 ? 0.122053  0.257343 0.0884497 0.0244226   0.0171752   0.0186005   230 PHE   A CD1  
1795 C  CD2  . PHE   A 230 ? 0.139572  0.254094 0.0908016 0.0289556   0.0149592   0.0211409   230 PHE   A CD2  
1796 C  CE1  . PHE   A 230 ? 0.139624  0.264556 0.0811346 0.0214275   0.00892736  0.0231127   230 PHE   A CE1  
1797 C  CE2  . PHE   A 230 ? 0.140189  0.26093  0.101732  0.0297166   0.0276245   0.01839     230 PHE   A CE2  
1798 C  CZ   . PHE   A 230 ? 0.151518  0.269938 0.0923617 0.027225    0.0221514   0.0193017   230 PHE   A CZ   
1799 N  N    . ASN   A 231 ? 0.132891  0.236225 0.0665254 0.0143654   0.0210921   0.0096497   231 ASN   A N    
1800 C  CA   . ASN   A 231 ? 0.137677  0.251933 0.0782072 0.0153429   0.0218678   0.00936825  231 ASN   A CA   
1801 C  C    . ASN   A 231 ? 0.135825  0.251188 0.0739715 0.00709317  0.0150981   0.0127867   231 ASN   A C    
1802 O  O    . ASN   A 231 ? 0.154649  0.267763 0.0676494 -0.00669397 0.0322846   0.00586508  231 ASN   A O    
1803 C  CB   . ASN   A 231 ? 0.131239  0.266907 0.0776033 0.0255043   0.0115808   0.00674368  231 ASN   A CB   
1804 C  CG   . ASN   A 231 ? 0.142175  0.283784 0.0839167 0.0290373   0.0174448   0.00487279  231 ASN   A CG   
1805 O  OD1  . ASN   A 231 ? 0.193669  0.303826 0.0907751 0.0469201   0.026057    0.0108545   231 ASN   A OD1  
1806 N  ND2  . ASN   A 231 ? 0.174815  0.299841 0.103779  0.031489    0.011361    0.0089628   231 ASN   A ND2  
1807 N  N    . LEU   A 232 ? 0.129856  0.244094 0.0731625 0.00856849  0.0128506   0.0146112   232 LEU   A N    
1808 C  CA   . LEU   A 232 ? 0.140836  0.2486   0.0784094 0.0147351   0.0221114   0.0114046   232 LEU   A CA   
1809 C  C    . LEU   A 232 ? 0.148778  0.237339 0.078663  0.00949349  0.0208961   0.00753308  232 LEU   A C    
1810 O  O    . LEU   A 232 ? 0.180992  0.247068 0.100933  0.00691414  -0.00249648 0.00993292  232 LEU   A O    
1811 C  CB   . LEU   A 232 ? 0.136922  0.256845 0.0830413 0.020057    0.0244626   0.0116323   232 LEU   A CB   
1812 C  CG   . LEU   A 232 ? 0.144914  0.269354 0.0892512 0.023631    0.0190011   0.0120733   232 LEU   A CG   
1813 C  CD1  . LEU   A 232 ? 0.146107  0.272313 0.0704682 0.0262251   0.0167006   0.0148372   232 LEU   A CD1  
1814 C  CD2  . LEU   A 232 ? 0.159782  0.296293 0.115032  0.0190245   0.0146395   0.00690436  232 LEU   A CD2  
1815 N  N    . VAL   A 233 ? 0.147552  0.232225 0.0823187 0.01106     0.0195052   0.00975568  233 VAL   A N    
1816 C  CA   . VAL   A 233 ? 0.159344  0.232809 0.0888029 0.00513638  0.0235222   0.010508    233 VAL   A CA   
1817 C  C    . VAL   A 233 ? 0.158488  0.229184 0.0908791 -0.00353117 0.023758    0.00485392  233 VAL   A C    
1818 O  O    . VAL   A 233 ? 0.161635  0.238754 0.0734472 -0.00793053 0.0180156   -0.00109464 233 VAL   A O    
1819 C  CB   . VAL   A 233 ? 0.164036  0.244356 0.100716  0.0013162   0.0200868   0.018505    233 VAL   A CB   
1820 C  CG1  . VAL   A 233 ? 0.178088  0.251518 0.103493  -0.0014819  0.0247096   0.0259808   233 VAL   A CG1  
1821 C  CG2  . VAL   A 233 ? 0.169964  0.250628 0.110292  0.00701464  0.0265564   0.0248969   233 VAL   A CG2  
1822 N  N    . ALA   A 234 ? 0.159153  0.237262 0.11008   -0.0200721  0.0431671   -0.00278301 234 ALA   A N    
1823 C  CA   . ALA   A 234 ? 0.17049   0.257358 0.117597  -0.0198143  0.0570814   -0.0144721  234 ALA   A CA   
1824 C  C    . ALA   A 234 ? 0.150832  0.262509 0.116489  -0.0146761  0.065677    -0.0157154  234 ALA   A C    
1825 O  O    . ALA   A 234 ? 0.15345   0.242978 0.11509   -0.0162975  0.0514126   -0.0227359  234 ALA   A O    
1826 C  CB   . ALA   A 234 ? 0.185383  0.267714 0.142233  -0.0189349  0.0609131   -0.0242719  234 ALA   A CB   
1827 N  N    . MET   A 235 ? 0.153539  0.272153 0.130297  -0.00843192 0.0724536   -0.00053447 235 MET   A N    
1828 C  CA   . MET   A 235 ? 0.154445  0.295541 0.143518  0.00243415  0.0619037   0.00028277  235 MET   A CA   
1829 C  C    . MET   A 235 ? 0.153439  0.28317  0.106265  -0.00348699 0.0418684   0.00086841  235 MET   A C    
1830 O  O    . MET   A 235 ? 0.155589  0.281344 0.118698  -0.00310071 0.0214219   0.00226952  235 MET   A O    
1831 C  CB   . MET   A 235 ? 0.179992  0.340573 0.200877  0.00442622  0.0468006   0.0240416   235 MET   A CB   
1832 C  CG   . MET   A 235 ? 0.235168  0.39201  0.263066  0.0162298   0.0589785   0.0231861   235 MET   A CG   
1833 S  SD   . MET   A 235 ? 0.36645   0.522738 0.374335  0.0645246   0.0867896   0.08944     235 MET   A SD   
1834 C  CE   . MET   A 235 ? 0.379514  0.512243 0.359472  0.0466394   0.046975    0.049631    235 MET   A CE   
1835 N  N    . LYS   A 236 ? 0.148724  0.278991 0.105714  0.00144191  0.0226436   -0.0100857  236 LYS   A N    
1836 C  CA   . LYS   A 236 ? 0.163045  0.278758 0.109772  0.00888137  0.0168249   -0.0111815  236 LYS   A CA   
1837 C  C    . LYS   A 236 ? 0.16381   0.262106 0.09913   0.00429173  0.0154917   -0.0257557  236 LYS   A C    
1838 O  O    . LYS   A 236 ? 0.224335  0.277254 0.108279  -0.00051481 0.0294943   -0.0383451  236 LYS   A O    
1839 C  CB   . LYS   A 236 ? 0.176117  0.296442 0.107566  0.0181532   0.025022    -0.0214262  236 LYS   A CB   
1840 C  CG   . LYS   A 236 ? 0.200207  0.319746 0.124129  0.0171446   0.0355285   -0.00755782 236 LYS   A CG   
1841 C  CD   . LYS   A 236 ? 0.203837  0.351187 0.161075  0.0205963   0.0314921   -0.00907828 236 LYS   A CD   
1842 C  CE   . LYS   A 236 ? 0.214322  0.37394  0.155664  0.0150719   0.0547753   -0.0102861  236 LYS   A CE   
1843 N  NZ   . LYS   A 236 ? 0.199029  0.37889  0.204766  0.0211829   0.0385088   -0.0139187  236 LYS   A NZ   
1844 N  N    . TYR   A 237 ? 0.148889  0.254053 0.0911365 0.00814684  0.0159038   -0.0228     237 TYR   A N    
1845 C  CA   . TYR   A 237 ? 0.150884  0.257316 0.083548  0.0106406   0.00702545  -0.0243103  237 TYR   A CA   
1846 C  C    . TYR   A 237 ? 0.162872  0.266474 0.0869633 0.00915559  0.0172929   -0.0270291  237 TYR   A C    
1847 O  O    . TYR   A 237 ? 0.187118  0.272606 0.0892748 0.00976472  0.018885    -0.0193118  237 TYR   A O    
1848 C  CB   . TYR   A 237 ? 0.145079  0.256071 0.0843414 0.015759    0.0100197   -0.0212694  237 TYR   A CB   
1849 C  CG   . TYR   A 237 ? 0.146663  0.251244 0.0856868 0.0195837   0.0103627   -0.0131487  237 TYR   A CG   
1850 C  CD1  . TYR   A 237 ? 0.143368  0.248444 0.0944861 0.0236885   0.00789401  0.00015438  237 TYR   A CD1  
1851 C  CD2  . TYR   A 237 ? 0.160143  0.253918 0.0923167 0.0199088   0.0091439   -0.00594889 237 TYR   A CD2  
1852 C  CE1  . TYR   A 237 ? 0.143343  0.247934 0.0690958 0.0185932   0.0242462   -0.00114716 237 TYR   A CE1  
1853 C  CE2  . TYR   A 237 ? 0.156897  0.248419 0.0895979 0.0199192   0.0158156   -0.00245264 237 TYR   A CE2  
1854 C  CZ   . TYR   A 237 ? 0.153204  0.248822 0.0889227 0.0197539   0.0202444   -0.00516981 237 TYR   A CZ   
1855 O  OH   . TYR   A 237 ? 0.161793  0.272056 0.0939857 0.0251157   0.025768    0.00124228  237 TYR   A OH   
1856 N  N    . ASN   A 238 ? 0.164281  0.268899 0.0936421 0.0112911   0.0134431   -0.0271685  238 ASN   A N    
1857 C  CA   . ASN   A 238 ? 0.163609  0.2748   0.103501  0.00211722  0.00732215  -0.0331241  238 ASN   A CA   
1858 C  C    . ASN   A 238 ? 0.139997  0.259503 0.0703522 0.00084602  0.00912184  -0.0176292  238 ASN   A C    
1859 O  O    . ASN   A 238 ? 0.134661  0.284251 0.0910733 -0.014477   0.0104737   -0.028407   238 ASN   A O    
1860 C  CB   . ASN   A 238 ? 0.191769  0.305751 0.13811   -0.00555506 0.00454992  -0.0388698  238 ASN   A CB   
1861 C  CG   . ASN   A 238 ? 0.222568  0.379984 0.211951  0.00590019  -0.0167239  -0.0289813  238 ASN   A CG   
1862 O  OD1  . ASN   A 238 ? 0.303304  0.455445 0.255465  0.00046538  -0.0558015  0.00812824  238 ASN   A OD1  
1863 N  ND2  . ASN   A 238 ? 0.257707  0.419896 0.264375  0.0156863   0.00362942  -0.0215978  238 ASN   A ND2  
1864 N  N    . TYR   A 239 ? 0.136471  0.236513 0.0655866 0.00848249  0.010475    -0.0109633  239 TYR   A N    
1865 C  CA   . TYR   A 239 ? 0.130837  0.238304 0.0568824 0.00993505  0.0176566   -0.00836074 239 TYR   A CA   
1866 C  C    . TYR   A 239 ? 0.159048  0.249783 0.0700554 0.0144739   0.011366    -0.00491636 239 TYR   A C    
1867 O  O    . TYR   A 239 ? 0.182297  0.26451  0.0649454 0.0236954   0.0129802   -0.00579453 239 TYR   A O    
1868 C  CB   . TYR   A 239 ? 0.125673  0.237889 0.0624668 0.00950574  0.0207134   -0.00674018 239 TYR   A CB   
1869 C  CG   . TYR   A 239 ? 0.114233  0.239282 0.0663224 0.010889    0.0202268   -0.00432478 239 TYR   A CG   
1870 C  CD1  . TYR   A 239 ? 0.125049  0.247645 0.0727322 0.0177959   0.0160105   -0.00744925 239 TYR   A CD1  
1871 C  CD2  . TYR   A 239 ? 0.123982  0.241927 0.078258  0.01424     0.0179075   -0.00918207 239 TYR   A CD2  
1872 C  CE1  . TYR   A 239 ? 0.124369  0.250201 0.0838586 0.016775    0.0137213   -0.00014139 239 TYR   A CE1  
1873 C  CE2  . TYR   A 239 ? 0.116071  0.255325 0.0825838 0.018837    0.016007    -0.00621594 239 TYR   A CE2  
1874 C  CZ   . TYR   A 239 ? 0.117133  0.254377 0.0746542 0.0218494   0.0108798   -0.00088886 239 TYR   A CZ   
1875 O  OH   . TYR   A 239 ? 0.123889  0.282533 0.0799687 0.0286985   0.0017283   0.00323178  239 TYR   A OH   
1876 N  N    . GLU   A 240 ? 0.163108  0.250406 0.0736148 0.01103     0.0101945   -0.00640574 240 GLU   A N    
1877 C  CA   . GLU   A 240 ? 0.177875  0.261388 0.0972405 0.0167709   0.00807768  0.00023672  240 GLU   A CA   
1878 C  C    . GLU   A 240 ? 0.182801  0.257345 0.0903572 0.0164759   0.00152384  0.00384946  240 GLU   A C    
1879 O  O    . GLU   A 240 ? 0.161551  0.251637 0.0800237 0.00557459  0.0111305   -0.00069761 240 GLU   A O    
1880 C  CB   . GLU   A 240 ? 0.200968  0.284205 0.12653   0.0271056   0.0200151   -0.00226924 240 GLU   A CB   
1881 C  CG   . GLU   A 240 ? 0.22548   0.309324 0.16989   0.0203926   0.0146769   -0.00931205 240 GLU   A CG   
1882 C  CD   . GLU   A 240 ? 0.231162  0.349968 0.212324  0.0207161   -0.00185495 -0.0130915  240 GLU   A CD   
1883 O  OE1  . GLU   A 240 ? 0.316116  0.380879 0.306538  0.010715    -0.0225283  -0.00980911 240 GLU   A OE1  
1884 O  OE2  . GLU   A 240 ? 0.300224  0.376153 0.266987  0.0095438   0.0112014   -0.0327819  240 GLU   A OE2  
1885 N  N    . PRO   A 241 ? 0.203658  0.274099 0.0737627 0.0146356   -0.0116245  -0.00036127 241 PRO   A N    
1886 C  CA   . PRO   A 241 ? 0.207701  0.272427 0.089076  0.0129482   -0.00860654 0.0108428   241 PRO   A CA   
1887 C  C    . PRO   A 241 ? 0.184951  0.260876 0.0933057 0.0141629   0.0150262   0.00815492  241 PRO   A C    
1888 O  O    . PRO   A 241 ? 0.179393  0.265678 0.139538  0.00669266  0.0317896   -0.00049486 241 PRO   A O    
1889 C  CB   . PRO   A 241 ? 0.232564  0.280946 0.0919611 0.00916549  -0.0183902  0.0156555   241 PRO   A CB   
1890 C  CG   . PRO   A 241 ? 0.225385  0.286692 0.105203  0.0101737   -0.0136976  0.00979408  241 PRO   A CG   
1891 C  CD   . PRO   A 241 ? 0.210579  0.28932  0.101543  0.0125722   -0.0159353  0.0049799   241 PRO   A CD   
1892 N  N    . LEU   A 242 ? 0.162193  0.254982 0.0876898 0.0297349   0.0202392   0.00962627  242 LEU   A N    
1893 C  CA   . LEU   A 242 ? 0.148696  0.250731 0.101945  0.0320406   0.0270327   0.00491651  242 LEU   A CA   
1894 C  C    . LEU   A 242 ? 0.156213  0.249127 0.102771  0.0382459   0.0134751   0.00096481  242 LEU   A C    
1895 O  O    . LEU   A 242 ? 0.177602  0.255098 0.120069  0.0314104   0.0368843   0.0137183   242 LEU   A O    
1896 C  CB   . LEU   A 242 ? 0.144251  0.261343 0.102694  0.0323074   0.0286755   0.0107924   242 LEU   A CB   
1897 C  CG   . LEU   A 242 ? 0.144568  0.258917 0.106487  0.033404    0.0287902   0.0133284   242 LEU   A CG   
1898 C  CD1  . LEU   A 242 ? 0.141426  0.265138 0.0993218 0.0369652   0.030091    0.00219629  242 LEU   A CD1  
1899 C  CD2  . LEU   A 242 ? 0.145688  0.272645 0.0995077 0.030805    0.0250919   0.0135706   242 LEU   A CD2  
1900 N  N    . THR   A 243 ? 0.159489  0.25034  0.0985566 0.0415684   0.0090639   -0.00042256 243 THR   A N    
1901 C  CA   . THR   A 243 ? 0.179578  0.255299 0.108322  0.0423336   0.00993578  0.00872958  243 THR   A CA   
1902 C  C    . THR   A 243 ? 0.170086  0.248368 0.114728  0.0464514   0.00544205  0.0134772   243 THR   A C    
1903 O  O    . THR   A 243 ? 0.166258  0.241852 0.108499  0.0485373   0.00729322  0.00928622  243 THR   A O    
1904 C  CB   . THR   A 243 ? 0.18097   0.260523 0.0975419 0.0414514   0.00855974  0.0174138   243 THR   A CB   
1905 O  OG1  . THR   A 243 ? 0.201915  0.283273 0.103684  0.0482189   0.00014736  0.00288732  243 THR   A OG1  
1906 C  CG2  . THR   A 243 ? 0.17944   0.265632 0.0968618 0.0404465   0.00821961  0.0190348   243 THR   A CG2  
1907 N  N    . GLN   A 244 ? 0.185875  0.252303 0.130932  0.0371408   0.00747367  0.0165833   244 GLN   A N    
1908 C  CA   . GLN   A 244 ? 0.187798  0.248567 0.146384  0.0389548   0.00376934  0.0176272   244 GLN   A CA   
1909 C  C    . GLN   A 244 ? 0.180689  0.249518 0.140282  0.039649    -0.00585509 0.0129168   244 GLN   A C    
1910 O  O    . GLN   A 244 ? 0.208134  0.269457 0.15879   0.0266376   -0.00695748 -3.15e-06   244 GLN   A O    
1911 C  CB   . GLN   A 244 ? 0.199328  0.256998 0.153293  0.0319791   0.0108861   0.0232925   244 GLN   A CB   
1912 C  CG   . GLN   A 244 ? 0.225614  0.267098 0.179017  0.0292625   0.0169259   0.0193224   244 GLN   A CG   
1913 C  CD   . GLN   A 244 ? 0.223826  0.289095 0.196218  0.0272608   0.0192983   0.00448154  244 GLN   A CD   
1914 O  OE1  . GLN   A 244 ? 0.236101  0.327174 0.209388  0.0316941   0.0248402   -0.0176391  244 GLN   A OE1  
1915 N  NE2  . GLN   A 244 ? 0.234255  0.297672 0.213818  0.0313737   0.0136983   -0.00800766 244 GLN   A NE2  
1916 N  N    . ASP   A 245 ? 0.1822    0.26246  0.124273  0.0422395   -0.0112927  0.00103409  245 ASP   A N    
1917 C  CA   . ASP   A 245 ? 0.17993   0.269186 0.137418  0.0460046   -0.00918831 -0.00344574 245 ASP   A CA   
1918 C  C    . ASP   A 245 ? 0.168321  0.254172 0.121091  0.0451448   -0.00450368 -0.00938394 245 ASP   A C    
1919 O  O    . ASP   A 245 ? 0.172884  0.273491 0.123883  0.0519958   -0.0233292  -0.0157067  245 ASP   A O    
1920 C  CB   . ASP   A 245 ? 0.182504  0.281923 0.153308  0.050896    -0.00535664 0.00044241  245 ASP   A CB   
1921 C  CG   . ASP   A 245 ? 0.200837  0.292765 0.190215  0.0594447   -0.0138546  0.0041716   245 ASP   A CG   
1922 O  OD1  . ASP   A 245 ? 0.218596  0.318548 0.204795  0.0660198   -0.0156707  0.0244957   245 ASP   A OD1  
1923 O  OD2  . ASP   A 245 ? 0.207426  0.331309 0.242038  0.0555289   -0.0351795  0.014813    245 ASP   A OD2  
1924 N  N    . HIS   A 246 ? 0.169692  0.251926 0.103599  0.0443925   -0.00058505 -0.00029689 246 HIS   A N    
1925 C  CA   . HIS   A 246 ? 0.163958  0.256534 0.0866852 0.0395576   0.0145815   0.00638602  246 HIS   A CA   
1926 C  C    . HIS   A 246 ? 0.166881  0.266866 0.0860297 0.0373621   0.00722474  8.735e-05   246 HIS   A C    
1927 O  O    . HIS   A 246 ? 0.169047  0.286416 0.0873218 0.0348661   0.00445634  0.00354995  246 HIS   A O    
1928 C  CB   . HIS   A 246 ? 0.174554  0.253236 0.103156  0.0364683   0.0131018   0.0137474   246 HIS   A CB   
1929 C  CG   . HIS   A 246 ? 0.181062  0.257653 0.10986   0.0297254   0.0159956   0.0152294   246 HIS   A CG   
1930 N  ND1  . HIS   A 246 ? 0.19399   0.259912 0.114683  0.0207871   0.016934    0.0198996   246 HIS   A ND1  
1931 C  CD2  . HIS   A 246 ? 0.181178  0.272532 0.12396   0.0252548   0.0202831   0.00429149  246 HIS   A CD2  
1932 C  CE1  . HIS   A 246 ? 0.194924  0.272102 0.139435  0.0197819   0.00889495  0.0141315   246 HIS   A CE1  
1933 N  NE2  . HIS   A 246 ? 0.188757  0.271545 0.121221  0.0157438   0.0116661   0.0120464   246 HIS   A NE2  
1934 N  N    . VAL   A 247 ? 0.152267  0.263647 0.0961021 0.0391633   0.00716774  -0.00707555 247 VAL   A N    
1935 C  CA   . VAL   A 247 ? 0.15102   0.261953 0.108574  0.0406128   -0.00031988 -0.0108775  247 VAL   A CA   
1936 C  C    . VAL   A 247 ? 0.157402  0.26699  0.128416  0.0483947   -0.00090357 -0.0179684  247 VAL   A C    
1937 O  O    . VAL   A 247 ? 0.156523  0.28556  0.129206  0.0445789   -0.0064473  -0.014865   247 VAL   A O    
1938 C  CB   . VAL   A 247 ? 0.158992  0.264972 0.109836  0.0416267   -0.00108784 -0.00628982 247 VAL   A CB   
1939 C  CG1  . VAL   A 247 ? 0.167971  0.267143 0.11142   0.0381974   0.0012923   -0.00702503 247 VAL   A CG1  
1940 C  CG2  . VAL   A 247 ? 0.16849   0.268405 0.122994  0.0367036   -0.00337393 -0.00354733 247 VAL   A CG2  
1941 N  N    . ASP   A 248 ? 0.176226  0.267842 0.131071  0.055605    -0.011518   -0.0178052  248 ASP   A N    
1942 C  CA   . ASP   A 248 ? 0.188855  0.268136 0.149419  0.0581276   -0.0155526  -0.0224342  248 ASP   A CA   
1943 C  C    . ASP   A 248 ? 0.188096  0.280604 0.136624  0.060172    -0.027918   -0.0260713  248 ASP   A C    
1944 O  O    . ASP   A 248 ? 0.182516  0.277975 0.136563  0.0607477   -0.0280633  -0.0361394  248 ASP   A O    
1945 C  CB   . ASP   A 248 ? 0.20206   0.274421 0.163818  0.0656762   -0.0228946  -0.0225895  248 ASP   A CB   
1946 C  CG   . ASP   A 248 ? 0.225102  0.278957 0.186985  0.0663974   -0.0185777  -0.0143502  248 ASP   A CG   
1947 O  OD1  . ASP   A 248 ? 0.251575  0.28807  0.210674  0.062408    0.00980019  0.00692606  248 ASP   A OD1  
1948 O  OD2  . ASP   A 248 ? 0.250027  0.308895 0.202778  0.0632049   -0.0425301  -0.00088828 248 ASP   A OD2  
1949 N  N    . ILE   A 249 ? 0.199181  0.284044 0.110869  0.0645263   -0.0229139  -0.0219759  249 ILE   A N    
1950 C  CA   . ILE   A 249 ? 0.194588  0.313501 0.133291  0.0618498   0.00378896  -0.0168473  249 ILE   A CA   
1951 C  C    . ILE   A 249 ? 0.178158  0.289888 0.119827  0.0577774   0.00527034  -0.0245259  249 ILE   A C    
1952 O  O    . ILE   A 249 ? 0.175696  0.322076 0.120823  0.0602394   0.00959902  -0.0158843  249 ILE   A O    
1953 C  CB   . ILE   A 249 ? 0.203536  0.376628 0.173914  0.0500375   0.00384944  -0.0173761  249 ILE   A CB   
1954 C  CG1  . ILE   A 249 ? 0.223902  0.396688 0.212149  0.0421633   0.0200345   -0.022848   249 ILE   A CG1  
1955 C  CG2  . ILE   A 249 ? 0.212026  0.396292 0.199146  0.0653602   -0.00181524 -0.0174728  249 ILE   A CG2  
1956 C  CD1  . ILE   A 249 ? 0.259348  0.423323 0.249716  0.0311636   0.0187898   -0.018764   249 ILE   A CD1  
1957 N  N    . LEU   A 250 ? 0.152423  0.275842 0.106456  0.0500448   0.00121056  -0.0103368  250 LEU   A N    
1958 C  CA   . LEU   A 250 ? 0.155489  0.25432  0.115481  0.0438616   -0.00040387 -0.00625381 250 LEU   A CA   
1959 C  C    . LEU   A 250 ? 0.157093  0.255622 0.128911  0.0439682   -0.00074002 -0.00917909 250 LEU   A C    
1960 O  O    . LEU   A 250 ? 0.161511  0.253945 0.149136  0.0439838   -0.0196297  -0.0140366  250 LEU   A O    
1961 C  CB   . LEU   A 250 ? 0.134938  0.244193 0.109699  0.0353079   0.00294092  -9.979e-05  250 LEU   A CB   
1962 C  CG   . LEU   A 250 ? 0.136673  0.241357 0.119399  0.0319304   0.0127345   0.00425919  250 LEU   A CG   
1963 C  CD1  . LEU   A 250 ? 0.14478   0.239571 0.130395  0.0287802   0.0120784   -0.00081933 250 LEU   A CD1  
1964 C  CD2  . LEU   A 250 ? 0.130156  0.252998 0.116827  0.0234531   0.0197739   0.00483712  250 LEU   A CD2  
1965 N  N    . GLY   A 251 ? 0.160694  0.252935 0.12779   0.0399283   -0.0121452  -0.0040037  251 GLY   A N    
1966 C  CA   . GLY   A 251 ? 0.182208  0.255512 0.146769  0.0341686   -0.0186322  -0.0101403  251 GLY   A CA   
1967 C  C    . GLY   A 251 ? 0.183347  0.250507 0.151699  0.0259008   -0.0193297  -0.0152681  251 GLY   A C    
1968 O  O    . GLY   A 251 ? 0.18828   0.239277 0.162602  0.027011    -0.0330148  -0.0135828  251 GLY   A O    
1969 N  N    . PRO   A 252 ? 0.188462  0.257487 0.166659  0.0338768   -0.0180734  -0.0211371  252 PRO   A N    
1970 C  CA   . PRO   A 252 ? 0.182327  0.260875 0.152944  0.0238244   -0.0049467  -0.0289105  252 PRO   A CA   
1971 C  C    . PRO   A 252 ? 0.165115  0.250241 0.124376  0.0156754   0.0134591   -0.0245648  252 PRO   A C    
1972 O  O    . PRO   A 252 ? 0.174673  0.247486 0.138912  0.00725429  0.00294711  -0.0317304  252 PRO   A O    
1973 C  CB   . PRO   A 252 ? 0.19148   0.26883  0.174259  0.0334423   -0.00479507 -0.0428997  252 PRO   A CB   
1974 C  CG   . PRO   A 252 ? 0.198256  0.262863 0.192304  0.0333165   -0.00833436 -0.0323999  252 PRO   A CG   
1975 C  CD   . PRO   A 252 ? 0.193267  0.270367 0.188333  0.0344582   -0.0111999  -0.0259804  252 PRO   A CD   
1976 N  N    . LEU   A 253 ? 0.152031  0.24802  0.0977069 0.0174209   0.014535    -0.0154343  253 LEU   A N    
1977 C  CA   . LEU   A 253 ? 0.145707  0.244974 0.0816584 0.0111932   0.0175473   -0.00590071 253 LEU   A CA   
1978 C  C    . LEU   A 253 ? 0.140066  0.244759 0.0929979 0.0109945   0.0114743   -0.00099444 253 LEU   A C    
1979 O  O    . LEU   A 253 ? 0.141944  0.246118 0.0953003 0.00931956  0.00173982  -0.00471081 253 LEU   A O    
1980 C  CB   . LEU   A 253 ? 0.148772  0.249502 0.0833165 0.0104747   0.0201255   -0.00409352 253 LEU   A CB   
1981 C  CG   . LEU   A 253 ? 0.148146  0.257299 0.104078  0.0099284   0.0221268   -0.00189956 253 LEU   A CG   
1982 C  CD1  . LEU   A 253 ? 0.154896  0.2636   0.116604  0.00373299  0.0228922   0.00105906  253 LEU   A CD1  
1983 C  CD2  . LEU   A 253 ? 0.16283   0.265075 0.114685  0.00596013  0.0127684   -0.00245846 253 LEU   A CD2  
1984 N  N    . SER   A 254 ? 0.134415  0.249384 0.0830999 0.0117993   0.00030374  -0.00756194 254 SER   A N    
1985 C  CA   . SER   A 254 ? 0.145469  0.261796 0.0922436 0.00696973  0.00898728  -0.00625568 254 SER   A CA   
1986 C  C    . SER   A 254 ? 0.148973  0.258127 0.107163  0.00326431  0.00021977  0.00076169  254 SER   A C    
1987 O  O    . SER   A 254 ? 0.141895  0.266549 0.135723  -0.0025774  -0.00601336 0.0050995   254 SER   A O    
1988 C  CB   . SER   A 254 ? 0.160048  0.279977 0.0898966 0.00957823  0.00545608  -0.00801705 254 SER   A CB   
1989 O  OG   . SER   A 254 ? 0.181315  0.317438 0.118262  0.00589146  0.0198912   0.00121325  254 SER   A OG   
1990 N  N    . ALA   A 255 ? 0.154295  0.260287 0.12269   -0.00055236 0.00017687  0.00053798  255 ALA   A N    
1991 C  CA   . ALA   A 255 ? 0.175728  0.262918 0.134569  -0.00862835 -0.00149067 0.00422828  255 ALA   A CA   
1992 C  C    . ALA   A 255 ? 0.168777  0.262737 0.132956  -0.00958359 0.00195636  0.00620628  255 ALA   A C    
1993 O  O    . ALA   A 255 ? 0.175803  0.287899 0.141311  -0.0319255  -0.00503012 0.0170603   255 ALA   A O    
1994 C  CB   . ALA   A 255 ? 0.195476  0.265945 0.155136  -0.00646558 -0.00294817 0.0016374   255 ALA   A CB   
1995 N  N    . GLN   A 256 ? 0.157699  0.251599 0.116559  0.00315513  -0.00023904 0.00335772  256 GLN   A N    
1996 C  CA   . GLN   A 256 ? 0.165579  0.256917 0.109496  0.00584505  -0.00074446 -0.00259591 256 GLN   A CA   
1997 C  C    . GLN   A 256 ? 0.154182  0.259644 0.10493   0.00575666  0.00610479  -0.0087804  256 GLN   A C    
1998 O  O    . GLN   A 256 ? 0.162282  0.281361 0.134805  0.00788135  -0.00722542 -0.017131   256 GLN   A O    
1999 C  CB   . GLN   A 256 ? 0.168349  0.266458 0.122809  0.0100283   0.00890206  -0.0030275  256 GLN   A CB   
2000 C  CG   . GLN   A 256 ? 0.176934  0.274676 0.126932  0.0168373   0.0122248   -0.00217739 256 GLN   A CG   
2001 C  CD   . GLN   A 256 ? 0.189495  0.287682 0.158303  0.0158592   0.0220418   0.00368062  256 GLN   A CD   
2002 O  OE1  . GLN   A 256 ? 0.195309  0.332792 0.198265  0.0332795   0.0370235   0.0267131   256 GLN   A OE1  
2003 N  NE2  . GLN   A 256 ? 0.190369  0.280277 0.150374  0.0142745   0.0238852   -8.593e-05  256 GLN   A NE2  
2004 N  N    . THR   A 257 ? 0.157842  0.242964 0.106907  0.00824004  -0.00616846 -0.00703623 257 THR   A N    
2005 C  CA   . THR   A 257 ? 0.15799   0.24675  0.0939313 0.00646375  0.00401294  -0.0039246  257 THR   A CA   
2006 C  C    . THR   A 257 ? 0.152864  0.240348 0.0997737 0.00502167  0.00134401  -0.00301551 257 THR   A C    
2007 O  O    . THR   A 257 ? 0.161105  0.239508 0.113505  0.00946686  0.00394128  0.00440585  257 THR   A O    
2008 C  CB   . THR   A 257 ? 0.152242  0.243855 0.0881411 0.00322017  0.00641644  0.0005831   257 THR   A CB   
2009 O  OG1  . THR   A 257 ? 0.150548  0.235195 0.0856537 0.00140191  0.00614266  -0.00303224 257 THR   A OG1  
2010 C  CG2  . THR   A 257 ? 0.156075  0.250214 0.0838523 0.00430894  0.00808278  -0.00488176 257 THR   A CG2  
2011 N  N    . GLY   A 258 ? 0.144565  0.24052  0.114572  -0.00018061 0.00055826  -0.00121748 258 GLY   A N    
2012 C  CA   . GLY   A 258 ? 0.151266  0.246077 0.107765  -2.016e-05  0.00050117  0.00488359  258 GLY   A CA   
2013 C  C    . GLY   A 258 ? 0.157208  0.256775 0.114338  -0.00013659 0.00682456  0.00175347  258 GLY   A C    
2014 O  O    . GLY   A 258 ? 0.184284  0.299484 0.118987  -0.0202564  0.0263197   -0.0130554  258 GLY   A O    
2015 N  N    . ILE   A 259 ? 0.145501  0.250127 0.0989149 0.00308723  0.0070344   -0.00105663 259 ILE   A N    
2016 C  CA   . ILE   A 259 ? 0.138588  0.240775 0.101901  0.00997391  0.00408963  -0.00247832 259 ILE   A CA   
2017 C  C    . ILE   A 259 ? 0.1373    0.247395 0.0962055 0.00581076  0.00514197  -0.00144388 259 ILE   A C    
2018 O  O    . ILE   A 259 ? 0.138798  0.257658 0.0973542 -0.0040178  0.00895479  3.76e-06    259 ILE   A O    
2019 C  CB   . ILE   A 259 ? 0.145779  0.235425 0.1199    0.0137822   0.00419849  -0.00853829 259 ILE   A CB   
2020 C  CG1  . ILE   A 259 ? 0.167353  0.244064 0.126943  0.0179876   -0.00430865 -0.0153175  259 ILE   A CG1  
2021 C  CG2  . ILE   A 259 ? 0.146401  0.233361 0.116299  0.00957717  0.00127921  -0.0029289  259 ILE   A CG2  
2022 C  CD1  . ILE   A 259 ? 0.176992  0.255896 0.143314  0.0169312   0.00429304  -0.0173728  259 ILE   A CD1  
2023 N  N    . ALA   A 260 ? 0.13219   0.256515 0.0966132 0.00068922  0.00370978  0.00306177  260 ALA   A N    
2024 C  CA   . ALA   A 260 ? 0.132053  0.247555 0.0908848 0.00901787  0.014183    0.00934061  260 ALA   A CA   
2025 C  C    . ALA   A 260 ? 0.132212  0.237359 0.0756129 0.0144282   0.0141532   0.0125829   260 ALA   A C    
2026 O  O    . ALA   A 260 ? 0.133507  0.241639 0.0668706 0.012775    0.0143918   0.00774767  260 ALA   A O    
2027 C  CB   . ALA   A 260 ? 0.138861  0.252922 0.0940481 -0.00052253 0.00995734  0.0165596   260 ALA   A CB   
2028 N  N    . VAL   A 261 ? 0.135792  0.237362 0.0886929 0.0228133   0.0154777   0.0171114   261 VAL   A N    
2029 C  CA   . VAL   A 261 ? 0.135303  0.239948 0.0935791 0.0264983   0.0118701   0.0105191   261 VAL   A CA   
2030 C  C    . VAL   A 261 ? 0.12301   0.221841 0.0904712 0.0167334   0.0078448   0.0126674   261 VAL   A C    
2031 O  O    . VAL   A 261 ? 0.12508   0.222126 0.0918734 0.0112655   0.00938089  0.015223    261 VAL   A O    
2032 C  CB   . VAL   A 261 ? 0.152082  0.258478 0.107646  0.0401941   0.0107245   0.012729    261 VAL   A CB   
2033 C  CG1  . VAL   A 261 ? 0.154913  0.264279 0.109468  0.0375791   0.0119112   0.00696443  261 VAL   A CG1  
2034 C  CG2  . VAL   A 261 ? 0.157721  0.266034 0.124357  0.043504    0.00974484  0.00647959  261 VAL   A CG2  
2035 N  N    . LEU   A 262 ? 0.124474  0.218709 0.0973557 0.0114138   0.0088125   0.0169487   262 LEU   A N    
2036 C  CA   . LEU   A 262 ? 0.139194  0.227087 0.093254  0.0114795   0.0115804   0.0117495   262 LEU   A CA   
2037 C  C    . LEU   A 262 ? 0.135407  0.22367  0.0956764 0.0123779   0.00929479  0.00492459  262 LEU   A C    
2038 O  O    . LEU   A 262 ? 0.138648  0.231605 0.100761  0.0162623   -0.0136661  0.00035708  262 LEU   A O    
2039 C  CB   . LEU   A 262 ? 0.157646  0.24124  0.0846016 0.00946191  0.00815938  0.00897027  262 LEU   A CB   
2040 C  CG   . LEU   A 262 ? 0.167935  0.253402 0.107513  0.0150388   0.00821663  0.0119205   262 LEU   A CG   
2041 C  CD1  . LEU   A 262 ? 0.185402  0.264688 0.105906  0.0204623   0.00994802  0.0162863   262 LEU   A CD1  
2042 C  CD2  . LEU   A 262 ? 0.175309  0.271062 0.113695  0.0118623   -0.00347684 0.00801738  262 LEU   A CD2  
2043 N  N    . ASP   A 263 ? 0.138224  0.222101 0.104355  0.00588718  0.0100105   -0.00032696 263 ASP   A N    
2044 C  CA   . ASP   A 263 ? 0.146527  0.226548 0.11221   0.00566346  0.00909806  -0.00159577 263 ASP   A CA   
2045 C  C    . ASP   A 263 ? 0.129961  0.212148 0.0987771 0.0133953   0.00159148  -0.00474113 263 ASP   A C    
2046 O  O    . ASP   A 263 ? 0.134217  0.211577 0.102262  0.0182811   0.0125103   -0.00391568 263 ASP   A O    
2047 C  CB   . ASP   A 263 ? 0.154521  0.249955 0.123588  -0.00224978 0.00382181  -0.00859632 263 ASP   A CB   
2048 C  CG   . ASP   A 263 ? 0.176522  0.280608 0.133656  -0.011379   0.0154154   -0.0120287  263 ASP   A CG   
2049 O  OD1  . ASP   A 263 ? 0.224194  0.349915 0.141624  -0.0389255  0.0196229   -0.0020809  263 ASP   A OD1  
2050 O  OD2  . ASP   A 263 ? 0.191987  0.332535 0.184962  -0.0419639  0.0390744   -0.0236377  263 ASP   A OD2  
2051 N  N    . MET   A 264 ? 0.127412  0.204393 0.0814195 0.0185144   -0.00349427 0.00211659  264 MET   A N    
2052 C  CA   . MET   A 264 ? 0.127399  0.212322 0.0860614 0.0152365   -0.00437393 0.00243231  264 MET   A CA   
2053 C  C    . MET   A 264 ? 0.12565   0.212664 0.0715326 0.012163    0.00508701  0.00513748  264 MET   A C    
2054 O  O    . MET   A 264 ? 0.146617  0.213847 0.0543145 0.0140058   -0.00204644 -0.00285465 264 MET   A O    
2055 C  CB   . MET   A 264 ? 0.127961  0.226288 0.0841968 0.0129337   -0.00292697 0.0009454   264 MET   A CB   
2056 C  CG   . MET   A 264 ? 0.128535  0.234321 0.0777892 0.00670702  -0.00568273 0.00102714  264 MET   A CG   
2057 S  SD   . MET   A 264 ? 0.137449  0.24449  0.0702853 0.0089778   0.00289845  0.0026823   264 MET   A SD   
2058 C  CE   . MET   A 264 ? 0.149514  0.245044 0.0907992 -0.00195279 -0.00291738 -0.00217282 264 MET   A CE   
2059 N  N    . CYS   A 265 ? 0.126912  0.221835 0.0732011 0.0105284   0.00045809  0.00675633  265 CYS   A N    
2060 C  CA   . CYS   A 265 ? 0.132354  0.230412 0.080332  0.00392562  0.00012006  0.00991044  265 CYS   A CA   
2061 C  C    . CYS   A 265 ? 0.126466  0.223277 0.0698477 0.00366517  -0.00185723 0.0112238   265 CYS   A C    
2062 O  O    . CYS   A 265 ? 0.118227  0.242656 0.0706202 -0.00081161 0.00676781  0.00355934  265 CYS   A O    
2063 C  CB   . CYS   A 265 ? 0.135102  0.246435 0.0825783 0.00417809  0.00286181  0.0176039   265 CYS   A CB   
2064 S  SG   . CYS   A 265 ? 0.139104  0.287602 0.0961588 0.0143604   -0.00089398 0.026767    265 CYS   A SG   
2065 N  N    . ALA   A 266 ? 0.132538  0.214852 0.082064  0.0019208   0.00132109  0.00380439  266 ALA   A N    
2066 C  CA   . ALA   A 266 ? 0.140422  0.219364 0.0867735 0.00449509  0.00649318  -0.00260888 266 ALA   A CA   
2067 C  C    . ALA   A 266 ? 0.133151  0.212374 0.0886183 0.0104852   0.0123468   -0.00689439 266 ALA   A C    
2068 O  O    . ALA   A 266 ? 0.14731   0.230378 0.0775896 0.0219163   0.0225587   -0.017466   266 ALA   A O    
2069 C  CB   . ALA   A 266 ? 0.145737  0.22186  0.0972517 0.00331136  0.00920173  -0.00245853 266 ALA   A CB   
2070 N  N    . SER   A 267 ? 0.134485  0.208521 0.0904524 0.0102739   0.0131482   -0.0138281  267 SER   A N    
2071 C  CA   . SER   A 267 ? 0.151506  0.216339 0.0857797 0.01399     0.00504626  -0.00940574 267 SER   A CA   
2072 C  C    . SER   A 267 ? 0.140435  0.205155 0.0658157 0.0192549   0.00581613  -0.00581167 267 SER   A C    
2073 O  O    . SER   A 267 ? 0.130818  0.213824 0.0693548 0.0180996   0.00475376  -0.00618062 267 SER   A O    
2074 C  CB   . SER   A 267 ? 0.175263  0.230857 0.0875477 0.0133142   0.0015343   -0.00769278 267 SER   A CB   
2075 O  OG   . SER   A 267 ? 0.180841  0.264919 0.0920584 0.0138618   -0.00591518 0.0104604   267 SER   A OG   
2076 N  N    . LEU   A 268 ? 0.140028  0.196847 0.0756117 0.0157021   -0.00047608 -0.00444099 268 LEU   A N    
2077 C  CA   . LEU   A 268 ? 0.135906  0.19791  0.0733664 0.0131105   0.00606736  -0.00182827 268 LEU   A CA   
2078 C  C    . LEU   A 268 ? 0.11746   0.196906 0.0807951 0.0154306   0.00581909  -0.0042217  268 LEU   A C    
2079 O  O    . LEU   A 268 ? 0.129741  0.200463 0.0605912 0.0146349   0.0093323   0.00052965  268 LEU   A O    
2080 C  CB   . LEU   A 268 ? 0.132731  0.205499 0.0700613 0.0130048   0.0123914   0.00134662  268 LEU   A CB   
2081 C  CG   . LEU   A 268 ? 0.134796  0.209739 0.0708021 0.00945419  0.0109079   0.00508161  268 LEU   A CG   
2082 C  CD1  . LEU   A 268 ? 0.13105   0.209772 0.072468  0.00720628  0.0109229   0.00237785  268 LEU   A CD1  
2083 C  CD2  . LEU   A 268 ? 0.135904  0.220356 0.0723294 0.0101788   0.0164066   0.00993921  268 LEU   A CD2  
2084 N  N    . LYS   A 269 ? 0.126413  0.217059 0.0892173 0.0106003   0.00447705  -0.00058286 269 LYS   A N    
2085 C  CA   . LYS   A 269 ? 0.131826  0.236529 0.102006  0.00636692  0.0128164   -0.00591611 269 LYS   A CA   
2086 C  C    . LYS   A 269 ? 0.129972  0.228249 0.0886055 -0.00064119 0.0165415   -0.00794771 269 LYS   A C    
2087 O  O    . LYS   A 269 ? 0.129957  0.229943 0.0880063 2.407e-05   0.0108121   -0.0129699  269 LYS   A O    
2088 C  CB   . LYS   A 269 ? 0.152136  0.260713 0.129075  0.00326769  0.0114963   0.0128317   269 LYS   A CB   
2089 C  CG   . LYS   A 269 ? 0.184162  0.285278 0.16714   0.0126153   0.0121761   0.0158871   269 LYS   A CG   
2090 C  CD   . LYS   A 269 ? 0.206733  0.31451  0.183412  0.0072232   0.0196527   0.0205154   269 LYS   A CD   
2091 C  CE   . LYS   A 269 ? 0.227027  0.343199 0.193494  0.00225061  0.0219692   0.00812303  269 LYS   A CE   
2092 N  NZ   . LYS   A 269 ? 0.229899  0.360286 0.176683  0.00967029  0.0252014   0.0142381   269 LYS   A NZ   
2093 N  N    . GLU   A 270 ? 0.132     0.235253 0.0823266 0.00265907  0.0130078   -0.0148649  270 GLU   A N    
2094 C  CA   . GLU   A 270 ? 0.139931  0.233939 0.09676   0.00629049  0.00925718  -0.017903   270 GLU   A CA   
2095 C  C    . GLU   A 270 ? 0.119355  0.224191 0.0926018 0.00850134  -0.00128295 -0.0177442  270 GLU   A C    
2096 O  O    . GLU   A 270 ? 0.129653  0.230917 0.10555   0.00812672  0.0162723   -0.0205737  270 GLU   A O    
2097 C  CB   . GLU   A 270 ? 0.143619  0.254225 0.129887  0.00100295  0.0111725   -0.0195186  270 GLU   A CB   
2098 C  CG   . GLU   A 270 ? 0.161344  0.272418 0.155212  0.00349501  0.00087516  -0.0209727  270 GLU   A CG   
2099 C  CD   . GLU   A 270 ? 0.170533  0.30921  0.173653  -0.0103029  -0.00346603 -0.024315   270 GLU   A CD   
2100 O  OE1  . GLU   A 270 ? 0.1981    0.349341 0.18701   -0.0274801  -0.00086425 -0.0251856  270 GLU   A OE1  
2101 O  OE2  . GLU   A 270 ? 0.183474  0.352502 0.17744   -0.0143739  -0.00739918 -0.0373674  270 GLU   A OE2  
2102 N  N    . LEU   A 271 ? 0.1226    0.221071 0.0968003 0.0114285   -0.00158725 -0.0163843  271 LEU   A N    
2103 C  CA   . LEU   A 271 ? 0.129084  0.231048 0.083084  0.0123343   0.00102295  -0.0181227  271 LEU   A CA   
2104 C  C    . LEU   A 271 ? 0.132596  0.223012 0.0771591 0.0127768   0.0110363   -0.0196865  271 LEU   A C    
2105 O  O    . LEU   A 271 ? 0.142945  0.234506 0.0737312 0.0234676   0.00587478  -0.0154049  271 LEU   A O    
2106 C  CB   . LEU   A 271 ? 0.13581   0.238141 0.0844908 0.0101448   0.00113162  -0.0248914  271 LEU   A CB   
2107 C  CG   . LEU   A 271 ? 0.14073   0.248543 0.105526  0.00741571  -0.0076872  -0.0255945  271 LEU   A CG   
2108 C  CD1  . LEU   A 271 ? 0.14459   0.259964 0.104268  0.00426593  0.00359847  -0.0294975  271 LEU   A CD1  
2109 C  CD2  . LEU   A 271 ? 0.169629  0.259152 0.116083  0.00747163  -0.0174433  -0.0247143  271 LEU   A CD2  
2110 N  N    . LEU   A 272 ? 0.126814  0.223424 0.0824644 0.00670742  0.00952759  -0.0140591  272 LEU   A N    
2111 C  CA   . LEU   A 272 ? 0.144725  0.223557 0.086219  0.00671629  0.00392958  -0.0165531  272 LEU   A CA   
2112 C  C    . LEU   A 272 ? 0.137139  0.224351 0.078729  0.00568982  0.00647255  -0.0136026  272 LEU   A C    
2113 O  O    . LEU   A 272 ? 0.143663  0.224558 0.0889123 0.00185355  0.0159585   -0.0183519  272 LEU   A O    
2114 C  CB   . LEU   A 272 ? 0.133846  0.22528  0.0897435 0.0107387   0.00128183  -0.021076   272 LEU   A CB   
2115 C  CG   . LEU   A 272 ? 0.137633  0.231206 0.0982007 0.00907169  0.0016217   -0.0258707  272 LEU   A CG   
2116 C  CD1  . LEU   A 272 ? 0.138086  0.23089  0.108409  0.0115311   0.00514762  -0.0205021  272 LEU   A CD1  
2117 C  CD2  . LEU   A 272 ? 0.140661  0.242622 0.0998182 0.0105133   0.00741121  -0.0236505  272 LEU   A CD2  
2118 N  N    . GLN   A 273 ? 0.133584  0.233067 0.0803918 0.00726023  0.00088646  -0.0127607  273 GLN   A N    
2119 C  CA   . GLN   A 273 ? 0.149031  0.242745 0.0889707 0.0154654   0.0114916   -0.003812   273 GLN   A CA   
2120 C  C    . GLN   A 273 ? 0.161876  0.237626 0.0891978 0.0162191   0.0232046   -0.0028969  273 GLN   A C    
2121 O  O    . GLN   A 273 ? 0.155766  0.231365 0.0850914 0.0130145   0.0253592   -0.00054441 273 GLN   A O    
2122 C  CB   . GLN   A 273 ? 0.160869  0.258686 0.0898747 0.0174781   0.0127328   0.00752729  273 GLN   A CB   
2123 C  CG   . GLN   A 273 ? 0.162763  0.272081 0.103962  0.0260598   0.00694932  0.0184827   273 GLN   A CG   
2124 C  CD   . GLN   A 273 ? 0.17722   0.284087 0.121485  0.0229841   0.0114365   0.0316927   273 GLN   A CD   
2125 O  OE1  . GLN   A 273 ? 0.20999   0.335717 0.139535  0.0336829   0.0337382   0.057025    273 GLN   A OE1  
2126 N  NE2  . GLN   A 273 ? 0.174296  0.288272 0.13173   0.0227283   0.00904555  0.0395476   273 GLN   A NE2  
2127 N  N    . ASN   A 274 ? 0.153546  0.235009 0.0848355 0.0241686   0.0181638   -0.00320938 274 ASN   A N    
2128 C  CA   . ASN   A 274 ? 0.164383  0.236558 0.0936065 0.0249975   0.0248443   0.00714099  274 ASN   A CA   
2129 C  C    . ASN   A 274 ? 0.186262  0.239439 0.0927448 0.0340625   0.0291474   0.0168165   274 ASN   A C    
2130 O  O    . ASN   A 274 ? 0.209632  0.250141 0.0804284 0.0383516   0.0486595   0.0367963   274 ASN   A O    
2131 C  CB   . ASN   A 274 ? 0.167732  0.244917 0.0869135 0.0224056   0.0242833   0.00310655  274 ASN   A CB   
2132 C  CG   . ASN   A 274 ? 0.180501  0.262132 0.0932505 0.0199751   0.0341174   -0.00102894 274 ASN   A CG   
2133 O  OD1  . ASN   A 274 ? 0.180317  0.297579 0.0893878 0.0128546   0.0464113   -0.00704635 274 ASN   A OD1  
2134 N  ND2  . ASN   A 274 ? 0.187868  0.264955 0.0893133 0.0139022   0.0409043   -0.00049746 274 ASN   A ND2  
2135 N  N    . GLY   A 275 ? 0.187753  0.250033 0.0901345 0.0391047   0.0292599   0.025315    275 GLY   A N    
2136 C  CA   . GLY   A 275 ? 0.205744  0.260441 0.0979163 0.0355393   0.033227    0.0331612   275 GLY   A CA   
2137 C  C    . GLY   A 275 ? 0.224525  0.279546 0.106025  0.0331929   0.0329433   0.0230134   275 GLY   A C    
2138 O  O    . GLY   A 275 ? 0.221925  0.289388 0.0931443 0.0277386   0.0336502   0.0247583   275 GLY   A O    
2139 N  N    . MET   A 276 ? 0.215353  0.278685 0.105009  0.0383787   0.039017    0.0208004   276 MET   A N    
2140 C  CA   A MET   A 276 ? 0.217753  0.289832 0.130871  0.0410872   0.0339108   0.0147295   276 MET   A CA   
2141 C  CA   B MET   A 276 ? 0.201997  0.273964 0.0885661 0.0401886   0.0459953   0.0177124   276 MET   A CA   
2142 C  C    . MET   A 276 ? 0.215167  0.287054 0.124583  0.0425288   0.0409713   0.0230638   276 MET   A C    
2143 O  O    . MET   A 276 ? 0.212232  0.280873 0.136998  0.0387021   0.0381013   0.0235165   276 MET   A O    
2144 C  CB   A MET   A 276 ? 0.216828  0.298159 0.157977  0.0367426   0.0418001   0.0134475   276 MET   A CB   
2145 C  CB   B MET   A 276 ? 0.182095  0.253805 0.0713601 0.0385116   0.0322251   0.01601     276 MET   A CB   
2146 C  CG   A MET   A 276 ? 0.223131  0.303057 0.203651  0.0361738   0.0366828   0.0105284   276 MET   A CG   
2147 C  CG   B MET   A 276 ? 0.166236  0.242194 0.0431631 0.033287    0.0335305   0.00998432  276 MET   A CG   
2148 S  SD   A MET   A 276 ? 0.232843  0.313379 0.305103  0.0110352   0.0381245   0.00124083  276 MET   A SD   
2149 S  SD   B MET   A 276 ? 0.154349  0.228006 0.0309116 0.0261736   0.0212051   0.0064073   276 MET   A SD   
2150 C  CE   A MET   A 276 ? 0.233847  0.326734 0.313473  0.00963936  0.049519    0.00433189  276 MET   A CE   
2151 C  CE   B MET   A 276 ? 0.151292  0.23393  0.0466333 0.0284697   0.0257132   0.00572525  276 MET   A CE   
2152 N  N    . ASN   A 277 ? 0.238438  0.304411 0.134502  0.0525519   0.0536974   0.0249247   277 ASN   A N    
2153 C  CA   . ASN   A 277 ? 0.274324  0.326375 0.160192  0.062839    0.0514508   0.033442    277 ASN   A CA   
2154 C  C    . ASN   A 277 ? 0.256879  0.328213 0.159882  0.058508    0.0460752   0.0368561   277 ASN   A C    
2155 O  O    . ASN   A 277 ? 0.235009  0.35684  0.172331  0.0372235   0.0389828   0.0316906   277 ASN   A O    
2156 C  CB   . ASN   A 277 ? 0.295208  0.342049 0.192404  0.067442    0.0710307   0.0349426   277 ASN   A CB   
2157 C  CG   . ASN   A 277 ? 0.358453  0.363293 0.208413  0.084412    0.103638    0.0306806   277 ASN   A CG   
2158 O  OD1  . ASN   A 277 ? 0.436789  0.386848 0.255745  0.100887    0.158559    0.0187677   277 ASN   A OD1  
2159 N  ND2  . ASN   A 277 ? 0.350176  0.382931 0.184789  0.101163    0.120627    0.0331981   277 ASN   A ND2  
2160 N  N    . GLY   A 278 ? 0.246166  0.312815 0.158588  0.0701488   0.0431978   0.0325069   278 GLY   A N    
2161 C  CA   . GLY   A 278 ? 0.272241  0.312677 0.147805  0.0676563   0.0356415   0.0328749   278 GLY   A CA   
2162 C  C    . GLY   A 278 ? 0.279977  0.311684 0.128457  0.0594496   0.0233909   0.0340785   278 GLY   A C    
2163 O  O    . GLY   A 278 ? 0.347906  0.325898 0.131231  0.0624876   0.0367238   0.0481389   278 GLY   A O    
2164 N  N    . ARG   A 279 ? 0.242431  0.309888 0.132269  0.0602569   0.0177296   0.0306827   279 ARG   A N    
2165 C  CA   . ARG   A 279 ? 0.232146  0.316339 0.123734  0.0574029   -0.00268794 0.0265299   279 ARG   A CA   
2166 C  C    . ARG   A 279 ? 0.224899  0.302272 0.107825  0.0502656   -0.0068317  0.00924224  279 ARG   A C    
2167 O  O    . ARG   A 279 ? 0.250814  0.305677 0.0919706 0.0422313   0.00393408  0.00125028  279 ARG   A O    
2168 C  CB   . ARG   A 279 ? 0.224673  0.339225 0.158027  0.0452283   -0.001835   0.0180442   279 ARG   A CB   
2169 C  CG   . ARG   A 279 ? 0.237865  0.375371 0.19838   0.0473565   -0.00408469 0.0220524   279 ARG   A CG   
2170 C  CD   . ARG   A 279 ? 0.260256  0.403565 0.24163   0.0390354   -0.0121466  0.042224    279 ARG   A CD   
2171 N  NE   . ARG   A 279 ? 0.27384   0.436419 0.261938  0.0399168   0.00314856  0.0473294   279 ARG   A NE   
2172 C  CZ   . ARG   A 279 ? 0.264933  0.465472 0.294256  0.0383998   0.0162927   0.0495534   279 ARG   A CZ   
2173 N  NH1  . ARG   A 279 ? 0.272554  0.472374 0.331536  0.0377967   0.00721071  0.0491542   279 ARG   A NH1  
2174 N  NH2  . ARG   A 279 ? 0.265165  0.468132 0.283132  0.0370705   0.0260485   0.0337689   279 ARG   A NH2  
2175 N  N    . THR   A 280 ? 0.201631  0.279931 0.113716  0.0451481   -0.0307878  0.00469525  280 THR   A N    
2176 C  CA   . THR   A 280 ? 0.18783   0.263828 0.109697  0.0364075   -0.0281745  0.00476971  280 THR   A CA   
2177 C  C    . THR   A 280 ? 0.168227  0.256665 0.1193    0.0335783   -0.0272625  -0.00138996 280 THR   A C    
2178 O  O    . THR   A 280 ? 0.168698  0.262885 0.155524  0.0315815   -0.0298355  -0.00995198 280 THR   A O    
2179 C  CB   . THR   A 280 ? 0.211561  0.287271 0.107323  0.039451    -0.0211275  0.00041371  280 THR   A CB   
2180 O  OG1  . THR   A 280 ? 0.237666  0.324083 0.121072  0.0369012   -0.036492   -0.00413815 280 THR   A OG1  
2181 C  CG2  . THR   A 280 ? 0.223091  0.297679 0.0955707 0.0353967   -0.0166087  0.00070644  280 THR   A CG2  
2182 N  N    . ILE   A 281 ? 0.149731  0.236194 0.10428   0.0215149   -0.0222644  0.00295456  281 ILE   A N    
2183 C  CA   . ILE   A 281 ? 0.150493  0.233704 0.0925819 0.0213763   -0.0224102  0.00137039  281 ILE   A CA   
2184 C  C    . ILE   A 281 ? 0.16191   0.235743 0.077658  0.0217831   -0.0162118  0.00068276  281 ILE   A C    
2185 O  O    . ILE   A 281 ? 0.167274  0.237365 0.0702788 0.0193558   -0.010107   -0.00748541 281 ILE   A O    
2186 C  CB   . ILE   A 281 ? 0.141133  0.234304 0.0941042 0.0123726   -0.0255191  0.00556461  281 ILE   A CB   
2187 C  CG1  . ILE   A 281 ? 0.140531  0.239217 0.110305  0.0135642   -0.0202449  0.0102088   281 ILE   A CG1  
2188 C  CG2  . ILE   A 281 ? 0.149353  0.240735 0.0917773 0.0081562   -0.0296803  0.00810151  281 ILE   A CG2  
2189 C  CD1  . ILE   A 281 ? 0.139437  0.239961 0.109029  0.0122835   -0.0211468  0.00880436  281 ILE   A CD1  
2190 N  N    . LEU   A 282 ? 0.184105  0.232018 0.0877501 0.0221877   -0.00508217 -0.00920851 282 LEU   A N    
2191 C  CA   . LEU   A 282 ? 0.202629  0.237296 0.081261  0.0215844   0.00402131  -0.00329017 282 LEU   A CA   
2192 C  C    . LEU   A 282 ? 0.246797  0.239589 0.0887907 0.0161221   0.00605237  -0.00088296 282 LEU   A C    
2193 O  O    . LEU   A 282 ? 0.254384  0.231642 0.0900057 0.012362    0.0332722   0.014544    282 LEU   A O    
2194 C  CB   . LEU   A 282 ? 0.18502   0.242103 0.0835273 0.020767    0.0126248   -0.00098535 282 LEU   A CB   
2195 C  CG   . LEU   A 282 ? 0.166738  0.24646  0.0918752 0.0176819   0.0222695   0.00391045  282 LEU   A CG   
2196 C  CD1  . LEU   A 282 ? 0.1603    0.250889 0.101986  0.0159329   0.0236609   0.00855472  282 LEU   A CD1  
2197 C  CD2  . LEU   A 282 ? 0.155771  0.247884 0.100226  0.0164376   0.0205369   0.00106849  282 LEU   A CD2  
2198 N  N    . GLY   A 283 ? 0.288889  0.242055 0.0833461 0.0151171   -0.00435489 0.0138774   283 GLY   A N    
2199 C  CA   . GLY   A 283 ? 0.321279  0.251561 0.0906847 0.00903241  -0.00120538 0.0172062   283 GLY   A CA   
2200 C  C    . GLY   A 283 ? 0.332481  0.25819  0.108095  -0.00439165 0.00680482  0.013636    283 GLY   A C    
2201 O  O    . GLY   A 283 ? 0.430906  0.30504  0.146641  -0.0431187  0.0168613   0.0199175   283 GLY   A O    
2202 N  N    . SER   A 284 ? 0.253535  0.248048 0.0891617 0.0162187   0.00727483  0.00308947  284 SER   A N    
2203 C  CA   . SER   A 284 ? 0.228079  0.247829 0.104089  0.022796    0.0209892   -0.0134364  284 SER   A CA   
2204 C  C    . SER   A 284 ? 0.19721   0.234719 0.0924504 0.0168292   0.0127966   -0.0105322  284 SER   A C    
2205 O  O    . SER   A 284 ? 0.197605  0.243537 0.0994383 0.00986856  0.00353352  -0.0159787  284 SER   A O    
2206 C  CB   . SER   A 284 ? 0.236563  0.270504 0.119744  0.0315655   0.00686809  -0.0104672  284 SER   A CB   
2207 O  OG   . SER   A 284 ? 0.260746  0.312155 0.157491  0.0305333   0.00504905  -0.0333557  284 SER   A OG   
2208 N  N    . ALA   A 285 ? 0.187508  0.227726 0.105044  0.016969    0.0115474   -0.00486943 285 ALA   A N    
2209 C  CA   . ALA   A 285 ? 0.197055  0.231813 0.111971  0.0142671   0.00485702  -0.0173285  285 ALA   A CA   
2210 C  C    . ALA   A 285 ? 0.19745   0.240327 0.113873  0.0120967   -0.0007404  -0.0175079  285 ALA   A C    
2211 O  O    . ALA   A 285 ? 0.222746  0.26831  0.128726  0.0293954   0.0089143   -0.0290061  285 ALA   A O    
2212 C  CB   . ALA   A 285 ? 0.216436  0.238065 0.133659  0.0128571   0.0104048   -0.0225351  285 ALA   A CB   
2213 N  N    . LEU   A 286 ? 0.198892  0.23602  0.102136  0.0143607   0.00089597  -0.00633716 286 LEU   A N    
2214 C  CA   . LEU   A 286 ? 0.205432  0.242526 0.0915254 0.00736606  -0.00109145 -0.00621323 286 LEU   A CA   
2215 C  C    . LEU   A 286 ? 0.178058  0.239077 0.0859701 0.00439401  0.00098586  -0.00798612 286 LEU   A C    
2216 O  O    . LEU   A 286 ? 0.204037  0.230532 0.0830432 0.00953796  -0.0042428  -0.0102451  286 LEU   A O    
2217 C  CB   . LEU   A 286 ? 0.232131  0.270285 0.133121  -0.00395051 -0.022345   0.00623866  286 LEU   A CB   
2218 C  CG   . LEU   A 286 ? 0.273353  0.293522 0.18171   -0.01122    -0.0355542  0.0148211   286 LEU   A CG   
2219 C  CD1  . LEU   A 286 ? 0.2729    0.323806 0.203867  -0.0144925  -0.0511315  0.0106702   286 LEU   A CD1  
2220 C  CD2  . LEU   A 286 ? 0.310728  0.307793 0.209341  -0.0138618  -0.0300297  0.00315396  286 LEU   A CD2  
2221 N  N    . LEU   A 287 ? 0.159936  0.245076 0.07626   0.00435067  0.0162495   -0.0109781  287 LEU   A N    
2222 C  CA   . LEU   A 287 ? 0.138023  0.257237 0.0969576 0.00486333  0.0157228   -0.00969601 287 LEU   A CA   
2223 C  C    . LEU   A 287 ? 0.132124  0.268945 0.120646  0.00544529  0.00669772  -0.0139064  287 LEU   A C    
2224 O  O    . LEU   A 287 ? 0.13541   0.325921 0.177828  8.947e-05   0.00183709  -0.0557946  287 LEU   A O    
2225 C  CB   . LEU   A 287 ? 0.14712   0.273138 0.10886   0.00110265  0.0256481   -0.00224101 287 LEU   A CB   
2226 C  CG   . LEU   A 287 ? 0.149423  0.296702 0.127326  0.00216174  0.0331614   -0.00306424 287 LEU   A CG   
2227 C  CD1  . LEU   A 287 ? 0.174815  0.31844  0.136804  -0.0015175  0.0309636   0.0142479   287 LEU   A CD1  
2228 C  CD2  . LEU   A 287 ? 0.162483  0.314505 0.154707  0.00456954  0.0257642   -0.011554   287 LEU   A CD2  
2229 N  N    . GLU   A 288 ? 0.115602  0.250408 0.0954063 0.00494427  -0.00880364 0.0049291   288 GLU   A N    
2230 C  CA   . GLU   A 288 ? 0.122668  0.24234  0.0970636 0.0100476   -0.0081401  0.0125771   288 GLU   A CA   
2231 C  C    . GLU   A 288 ? 0.111579  0.222807 0.0774658 0.00539856  -0.00448289 0.00244988  288 GLU   A C    
2232 O  O    . GLU   A 288 ? 0.1148    0.214894 0.0812346 0.00751605  -0.00294892 0.00078699  288 GLU   A O    
2233 C  CB   . GLU   A 288 ? 0.144611  0.259902 0.0978289 0.0108867   -0.0215531  0.0297566   288 GLU   A CB   
2234 C  CG   . GLU   A 288 ? 0.179456  0.298897 0.142032  0.020428    -0.0112534  0.0439448   288 GLU   A CG   
2235 C  CD   . GLU   A 288 ? 0.179167  0.321529 0.188936  0.022482    -0.0083786  0.0744378   288 GLU   A CD   
2236 O  OE1  . GLU   A 288 ? 0.219904  0.347607 0.233997  0.0189848   -0.0137401  0.124353    288 GLU   A OE1  
2237 O  OE2  . GLU   A 288 ? 0.170347  0.351298 0.215106  0.0453564   0.00508336  0.100465    288 GLU   A OE2  
2238 N  N    . ASP   A 289 ? 0.106189  0.222481 0.0787041 0.01169     0.00170926  0.00304545  289 ASP   A N    
2239 C  CA   . ASP   A 289 ? 0.109234  0.223388 0.0715382 0.00982967  0.00740293  0.00655131  289 ASP   A CA   
2240 C  C    . ASP   A 289 ? 0.111659  0.216837 0.0833946 0.0134902   0.00960838  0.00654841  289 ASP   A C    
2241 O  O    . ASP   A 289 ? 0.107108  0.221234 0.0976939 0.0143413   0.0110564   0.0106206   289 ASP   A O    
2242 C  CB   . ASP   A 289 ? 0.128549  0.238601 0.0713563 0.00626374  0.00621087  0.00590741  289 ASP   A CB   
2243 C  CG   . ASP   A 289 ? 0.12754   0.251209 0.0759319 0.00428264  0.0088598   0.0121366   289 ASP   A CG   
2244 O  OD1  . ASP   A 289 ? 0.14367   0.258892 0.0695825 -0.01416    0.00341366  0.0129137   289 ASP   A OD1  
2245 O  OD2  . ASP   A 289 ? 0.126949  0.276207 0.0791332 -0.00260342 0.00948923  0.00182751  289 ASP   A OD2  
2246 N  N    . GLU   A 290 ? 0.111758  0.219208 0.0765245 0.0138709   0.00932729  -0.00383692 290 GLU   A N    
2247 C  CA   . GLU   A 290 ? 0.11165   0.221704 0.0872194 0.00876234  0.0158294   0.00124114  290 GLU   A CA   
2248 C  C    . GLU   A 290 ? 0.103398  0.213508 0.0803502 0.00970493  0.0156089   0.00714623  290 GLU   A C    
2249 O  O    . GLU   A 290 ? 0.111924  0.231921 0.0880806 0.0118445   0.0193293   -0.00014085 290 GLU   A O    
2250 C  CB   . GLU   A 290 ? 0.135092  0.241868 0.102395  -0.00414662 0.0163168   -0.00140582 290 GLU   A CB   
2251 C  CG   . GLU   A 290 ? 0.154973  0.258667 0.108657  -0.00771214 0.00933714  -0.00311911 290 GLU   A CG   
2252 C  CD   . GLU   A 290 ? 0.159843  0.284676 0.119177  -0.0135741  0.00756648  -0.00020367 290 GLU   A CD   
2253 O  OE1  . GLU   A 290 ? 0.182592  0.336062 0.131611  -0.0277724  0.0237021   -0.00541408 290 GLU   A OE1  
2254 O  OE2  . GLU   A 290 ? 0.156057  0.287001 0.102904  -0.00985162 0.0137537   -0.00035423 290 GLU   A OE2  
2255 N  N    . PHE   A 291 ? 0.104001  0.205764 0.0764751 0.00593603  0.0170099   0.00289748  291 PHE   A N    
2256 C  CA   . PHE   A 291 ? 0.109593  0.211301 0.0822602 0.00330379  0.0159059   0.00395985  291 PHE   A CA   
2257 C  C    . PHE   A 291 ? 0.111218  0.205324 0.0735966 9.3e-07     0.0140333   -0.00095625 291 PHE   A C    
2258 O  O    . PHE   A 291 ? 0.119379  0.211878 0.0568758 0.0107529   0.0143527   -0.00925025 291 PHE   A O    
2259 C  CB   . PHE   A 291 ? 0.120727  0.227123 0.0892616 0.00055829  0.0124551   0.0135653   291 PHE   A CB   
2260 C  CG   . PHE   A 291 ? 0.146273  0.247601 0.0928727 0.0045864   0.0106336   0.0238305   291 PHE   A CG   
2261 C  CD1  . PHE   A 291 ? 0.162785  0.25912  0.0943636 0.0041583   0.024421    0.0328209   291 PHE   A CD1  
2262 C  CD2  . PHE   A 291 ? 0.162847  0.256215 0.10972   0.0023838   0.0163523   0.0387507   291 PHE   A CD2  
2263 C  CE1  . PHE   A 291 ? 0.1892    0.270516 0.119208  0.0020704   0.0192049   0.0444383   291 PHE   A CE1  
2264 C  CE2  . PHE   A 291 ? 0.194319  0.270389 0.127086  0.0122544   0.0165088   0.0481958   291 PHE   A CE2  
2265 C  CZ   . PHE   A 291 ? 0.182542  0.272279 0.125967  0.00410954  0.0202874   0.047997    291 PHE   A CZ   
2266 N  N    . THR   A 292 ? 0.1179    0.198664 0.066075  0.00037074  0.0122276   0.00222267  292 THR   A N    
2267 C  CA   . THR   A 292 ? 0.129854  0.196673 0.0691768 0.00174739  0.0117761   0.00519357  292 THR   A CA   
2268 C  C    . THR   A 292 ? 0.123405  0.200927 0.0639237 0.00472191  0.00551584  0.0079133   292 THR   A C    
2269 O  O    . THR   A 292 ? 0.126845  0.209561 0.056287  0.00103787  0.00619914  0.00920921  292 THR   A O    
2270 C  CB   . THR   A 292 ? 0.131253  0.203454 0.0733429 0.00724226  0.00708653  0.0060865   292 THR   A CB   
2271 O  OG1  . THR   A 292 ? 0.12144   0.19777  0.0785954 0.00830354  0.0040056   -0.00178258 292 THR   A OG1  
2272 C  CG2  . THR   A 292 ? 0.132927  0.208009 0.0731917 0.00487259  0.00188892  0.00611669  292 THR   A CG2  
2273 N  N    . PRO   A 293 ? 0.131996  0.20264  0.0641456 0.0016919   0.00222912  0.0113489   293 PRO   A N    
2274 C  CA   . PRO   A 293 ? 0.128779  0.207945 0.0755542 -0.00270642 0.00388293  0.0118686   293 PRO   A CA   
2275 C  C    . PRO   A 293 ? 0.128051  0.21181  0.088135  0.00050477  0.00097514  0.00344548  293 PRO   A C    
2276 O  O    . PRO   A 293 ? 0.116226  0.225706 0.0941169 0.00296915  -0.00044179 -0.00577016 293 PRO   A O    
2277 C  CB   . PRO   A 293 ? 0.136842  0.21303  0.0864389 -0.00170726 0.0050948   0.0185316   293 PRO   A CB   
2278 C  CG   . PRO   A 293 ? 0.138315  0.218317 0.0878742 -0.00109073 -0.00282153 0.0210515   293 PRO   A CG   
2279 C  CD   . PRO   A 293 ? 0.134816  0.219644 0.0709443 -0.00018695 -0.00409301 0.0171515   293 PRO   A CD   
2280 N  N    . PHE   A 294 ? 0.130431  0.221899 0.0989403 0.00726234  -0.0055342  -0.00390041 294 PHE   A N    
2281 C  CA   . PHE   A 294 ? 0.136577  0.227086 0.11509   0.0170502   -0.00267456 -0.00475171 294 PHE   A CA   
2282 C  C    . PHE   A 294 ? 0.126227  0.224779 0.0975307 0.0166975   0.00758162  -0.00750112 294 PHE   A C    
2283 O  O    . PHE   A 294 ? 0.1566    0.241642 0.093149  0.0236205   -0.00029626 -0.00512654 294 PHE   A O    
2284 C  CB   . PHE   A 294 ? 0.144305  0.253728 0.14592   0.0112845   -0.0145804  0.00180806  294 PHE   A CB   
2285 C  CG   . PHE   A 294 ? 0.173814  0.276445 0.169822  0.00218109  -0.01704    -0.0100629  294 PHE   A CG   
2286 C  CD1  . PHE   A 294 ? 0.198195  0.292107 0.17506   0.00310554  -0.00436244 -0.00791512 294 PHE   A CD1  
2287 C  CD2  . PHE   A 294 ? 0.199643  0.286736 0.184629  0.00243951  -0.0265404  -0.0017849  294 PHE   A CD2  
2288 C  CE1  . PHE   A 294 ? 0.201014  0.300628 0.198206  -0.00093402 -0.00819718 -0.0297662  294 PHE   A CE1  
2289 C  CE2  . PHE   A 294 ? 0.222564  0.302997 0.19671   -0.00182321 -0.0261892  -0.0179298  294 PHE   A CE2  
2290 C  CZ   . PHE   A 294 ? 0.219876  0.304893 0.201733  -0.00346728 -0.0115264  -0.0234227  294 PHE   A CZ   
2291 N  N    . ASP   A 295 ? 0.129432  0.2248   0.0806612 0.0108763   0.00962285  0.0026996   295 ASP   A N    
2292 C  CA   . ASP   A 295 ? 0.122042  0.221143 0.0717598 0.0114941   0.0131574   0.00014573  295 ASP   A CA   
2293 C  C    . ASP   A 295 ? 0.120606  0.228763 0.0742774 0.00976754  0.0163024   0.00408886  295 ASP   A C    
2294 O  O    . ASP   A 295 ? 0.130086  0.255497 0.0740784 0.00635745  0.0111644   0.00269272  295 ASP   A O    
2295 C  CB   . ASP   A 295 ? 0.131537  0.223463 0.0873595 0.0125658   0.0120641   -0.00137452 295 ASP   A CB   
2296 C  CG   . ASP   A 295 ? 0.13724   0.222844 0.103636  0.00566671  0.0124168   -0.00230374 295 ASP   A CG   
2297 O  OD1  . ASP   A 295 ? 0.138463  0.24439  0.110067  0.00605162  0.0147336   -0.0200642  295 ASP   A OD1  
2298 O  OD2  . ASP   A 295 ? 0.129455  0.229868 0.0973335 -0.00505337 0.0148609   0.00247811  295 ASP   A OD2  
2299 N  N    . VAL   A 296 ? 0.106553  0.218686 0.0841068 0.0114285   0.0149837   0.00439179  296 VAL   A N    
2300 C  CA   . VAL   A 296 ? 0.104985  0.223039 0.0861537 0.0119984   0.0147037   0.0108733   296 VAL   A CA   
2301 C  C    . VAL   A 296 ? 0.110855  0.226468 0.0971803 0.00935289  0.0114025   0.00807002  296 VAL   A C    
2302 O  O    . VAL   A 296 ? 0.122555  0.234182 0.0949598 0.00636636  0.0039062   0.00109881  296 VAL   A O    
2303 C  CB   . VAL   A 296 ? 0.107878  0.216928 0.0827107 0.015233    0.0129032   0.0168241   296 VAL   A CB   
2304 C  CG1  . VAL   A 296 ? 0.114157  0.223285 0.0951538 0.0151027   0.00799879  0.0201993   296 VAL   A CG1  
2305 C  CG2  . VAL   A 296 ? 0.110396  0.219096 0.0763841 0.0186766   0.0130695   0.0201617   296 VAL   A CG2  
2306 N  N    . VAL   A 297 ? 0.126873  0.226338 0.100608  0.00744373  0.00831349  0.00835884  297 VAL   A N    
2307 C  CA   . VAL   A 297 ? 0.148451  0.23191  0.121273  0.00292144  0.0053698   0.00029995  297 VAL   A CA   
2308 C  C    . VAL   A 297 ? 0.168973  0.234659 0.105985  -0.00079367 -0.00150313 -0.00980903 297 VAL   A C    
2309 O  O    . VAL   A 297 ? 0.199854  0.264576 0.0993512 -0.00583017 -0.00936348 -0.00697985 297 VAL   A O    
2310 C  CB   . VAL   A 297 ? 0.170026  0.238685 0.136991  -0.00203992 0.0132117   0.00125436  297 VAL   A CB   
2311 C  CG1  . VAL   A 297 ? 0.181891  0.239884 0.166858  -0.00050675 0.0103815   -0.00200739 297 VAL   A CG1  
2312 C  CG2  . VAL   A 297 ? 0.176694  0.252116 0.147695  -0.00016552 0.0175709   0.0016869   297 VAL   A CG2  
2313 N  N    . ARG   A 298 ? 0.175137  0.244133 0.0886765 0.00406376  0.00140498  -0.00788715 298 ARG   A N    
2314 C  CA   . ARG   A 298 ? 0.183183  0.242744 0.0985198 0.00250828  0.0114316   -0.0106693  298 ARG   A CA   
2315 C  C    . ARG   A 298 ? 0.185071  0.237204 0.0927433 0.00069153  0.012029    -0.0106952  298 ARG   A C    
2316 O  O    . ARG   A 298 ? 0.240353  0.248175 0.0917565 0.00540543  0.00109367  -0.0125906  298 ARG   A O    
2317 C  CB   . ARG   A 298 ? 0.182293  0.255713 0.100819  0.00583854  0.015585    -0.0114417  298 ARG   A CB   
2318 C  CG   . ARG   A 298 ? 0.19012   0.262715 0.122484  -0.00301101 0.0223502   -0.00717255 298 ARG   A CG   
2319 C  CD   . ARG   A 298 ? 0.201225  0.259524 0.127742  -0.00142876 0.00512717  -0.0174418  298 ARG   A CD   
2320 N  NE   . ARG   A 298 ? 0.212973  0.242633 0.156277  -0.00085785 0.00801257  -0.00416245 298 ARG   A NE   
2321 C  CZ   . ARG   A 298 ? 0.20448   0.24105  0.161323  0.00466602  0.00251214  -0.00524253 298 ARG   A CZ   
2322 N  NH1  . ARG   A 298 ? 0.230649  0.244323 0.1544    0.00691177  -0.00259759 0.00437853  298 ARG   A NH1  
2323 N  NH2  . ARG   A 298 ? 0.21096   0.249028 0.157065  0.0066932   -0.0020222  -0.0120209  298 ARG   A NH2  
2324 N  N    . GLN   A 299 ? 0.159393  0.234234 0.0826488 -0.0055823  0.013429    0.00145576  299 GLN   A N    
2325 C  CA   . GLN   A 299 ? 0.15262   0.240664 0.080525  -0.00488146 0.00531787  0.00702011  299 GLN   A CA   
2326 C  C    . GLN   A 299 ? 0.158015  0.254408 0.0761672 -0.0100853  -0.00769234 0.0106039   299 GLN   A C    
2327 O  O    . GLN   A 299 ? 0.1821    0.262924 0.0681322 -0.0259019  -0.0166664  0.00393562  299 GLN   A O    
2328 C  CB   . GLN   A 299 ? 0.153578  0.24335  0.089914  -0.00172496 0.00462268  0.0107016   299 GLN   A CB   
2329 C  CG   . GLN   A 299 ? 0.152089  0.237758 0.0859766 0.00281959  0.00943212  0.00969709  299 GLN   A CG   
2330 C  CD   . GLN   A 299 ? 0.150977  0.235258 0.0865168 0.00119803  0.00044396  0.00786278  299 GLN   A CD   
2331 O  OE1  . GLN   A 299 ? 0.164117  0.242109 0.0888264 0.0135123   -0.00061418 0.0036096   299 GLN   A OE1  
2332 N  NE2  . GLN   A 299 ? 0.164254  0.23886  0.0906538 0.0022155   -0.0108462  0.0148819   299 GLN   A NE2  
2333 N  N    . CYS   A 300 ? 0.154141  0.253215 0.0740127 7.328e-05   -0.00884929 0.0141774   300 CYS   A N    
2334 C  CA   . CYS   A 300 ? 0.154876  0.261266 0.0803612 0.00671272  -0.0106838  0.0123197   300 CYS   A CA   
2335 C  C    . CYS   A 300 ? 0.167793  0.249895 0.0926208 0.00382622  0.00190842  0.0155434   300 CYS   A C    
2336 O  O    . CYS   A 300 ? 0.175825  0.247251 0.100864  -0.00217356 -0.00655442 0.00669632  300 CYS   A O    
2337 C  CB   . CYS   A 300 ? 0.155751  0.282622 0.0816991 0.0194262   -0.0164046  0.00152643  300 CYS   A CB   
2338 S  SG   . CYS   A 300 ? 0.214975  0.318768 0.124573  0.0363779   -0.0328265  -0.0228263  300 CYS   A SG   
2339 N  N    . SER   A 301 ? 0.180037  0.245698 0.101104  0.00193224  0.0019842   0.0122894   301 SER   A N    
2340 C  CA   . SER   A 301 ? 0.184396  0.248673 0.121506  -0.00421229 0.0128284   0.00375495  301 SER   A CA   
2341 C  C    . SER   A 301 ? 0.186668  0.244991 0.120772  -0.0006319  0.0201591   -0.00394675 301 SER   A C    
2342 O  O    . SER   A 301 ? 0.199123  0.239296 0.121637  -0.00775421 0.0188364   -0.0147975  301 SER   A O    
2343 C  CB   . SER   A 301 ? 0.194251  0.244934 0.123249  -0.0120644  0.00184731  0.00392871  301 SER   A CB   
2344 O  OG   . SER   A 301 ? 0.20901   0.259439 0.149754  -0.0318541  0.00566216  -0.00368474 301 SER   A OG   
2345 N  N    . GLY   A 302 ? 0.187652  0.246033 0.137675  0.00539501  0.0346498   -0.00779584 302 GLY   A N    
2346 C  CA   . GLY   A 302 ? 0.193287  0.252519 0.155159  -0.00056743 0.0298713   -0.0061942  302 GLY   A CA   
2347 C  C    . GLY   A 302 ? 0.192065  0.256229 0.169381  -0.00627379 0.0317434   -0.0147466  302 GLY   A C    
2348 O  O    . GLY   A 302 ? 0.218725  0.273498 0.182029  -0.0169214  0.0344386   -0.0127033  302 GLY   A O    
2349 N  N    . VAL   A 303 ? 0.18143   0.282795 0.179529  0.007568    0.0289815   -0.0292565  303 VAL   A N    
2350 C  CA   . VAL   A 303 ? 0.188358  0.295039 0.211084  -0.00656492 0.0302122   -0.0340144  303 VAL   A CA   
2351 C  C    . VAL   A 303 ? 0.187246  0.281748 0.194659  -0.00170898 0.0378265   -0.0154208  303 VAL   A C    
2352 O  O    . VAL   A 303 ? 0.237911  0.281302 0.201504  -0.0159     0.0659062   -0.0176783  303 VAL   A O    
2353 C  CB   . VAL   A 303 ? 0.197998  0.326025 0.241766  -0.00541118 0.0133809   -0.0529281  303 VAL   A CB   
2354 C  CG1  . VAL   A 303 ? 0.205117  0.33857  0.248757  -0.0015126  -0.00304828 -0.0606739  303 VAL   A CG1  
2355 C  CG2  . VAL   A 303 ? 0.221349  0.339446 0.268902  -0.00354845 0.0140309   -0.0552545  303 VAL   A CG2  
2356 N  N    . THR   A 304 ? 0.181894  0.282827 0.181165  -0.00256344 0.0259041   -0.00932328 304 THR   A N    
2357 C  CA   . THR   A 304 ? 0.163629  0.282385 0.143871  -0.006159   0.0166781   -0.00405504 304 THR   A CA   
2358 C  C    . THR   A 304 ? 0.159331  0.275336 0.134392  -0.00398362 0.0140111   -0.0108279  304 THR   A C    
2359 O  O    . THR   A 304 ? 0.178835  0.273727 0.174239  -0.00356224 0.00100367  -0.0157019  304 THR   A O    
2360 C  CB   . THR   A 304 ? 0.164564  0.298151 0.141671  -0.00711076 0.0150025   0.00489762  304 THR   A CB   
2361 O  OG1  . THR   A 304 ? 0.177467  0.313054 0.156296  -0.00615317 0.00246964  0.00347588  304 THR   A OG1  
2362 C  CG2  . THR   A 304 ? 0.163634  0.303862 0.129659  -0.00485282 0.0180704   0.0132243   304 THR   A CG2  
2363 N  N    . PHE   A 305 ? 0.147993  0.276819 0.111086  -0.00604194 0.00535306  -0.0100244  305 PHE   A N    
2364 C  CA   . PHE   A 305 ? 0.148945  0.283973 0.125317  -0.0036845  0.00445883  -0.0113041  305 PHE   A CA   
2365 C  C    . PHE   A 305 ? 0.15182   0.288377 0.132701  0.00026937  0.00518353  -0.0173965  305 PHE   A C    
2366 O  O    . PHE   A 305 ? 0.176757  0.304015 0.11339   -0.012555   -0.00542882 -0.0151199  305 PHE   A O    
2367 C  CB   . PHE   A 305 ? 0.163459  0.286882 0.121949  -0.00329965 0.0113136   -0.00848739 305 PHE   A CB   
2368 C  CG   . PHE   A 305 ? 0.181286  0.297663 0.119432  0.00544781  0.0184005   -0.00244794 305 PHE   A CG   
2369 C  CD1  . PHE   A 305 ? 0.19794   0.308152 0.150264  -0.00232771 0.00866172  0.00378435  305 PHE   A CD1  
2370 C  CD2  . PHE   A 305 ? 0.199614  0.305707 0.138127  0.00719791  0.0163081   -0.00298135 305 PHE   A CD2  
2371 C  CE1  . PHE   A 305 ? 0.215473  0.316453 0.161094  0.0043543   0.00798932  0.00531624  305 PHE   A CE1  
2372 C  CE2  . PHE   A 305 ? 0.211529  0.317584 0.151054  0.00825677  0.0151971   0.00457633  305 PHE   A CE2  
2373 C  CZ   . PHE   A 305 ? 0.215741  0.319651 0.149125  0.00739526  0.0228605   -0.0012854  305 PHE   A CZ   
2374 N  N    . GLN   A 306 ? 0.152149  0.295095 0.145299  -0.00055212 0.00629875  -0.0213716  306 GLN   A N    
2375 C  CA   . GLN   A 306 ? 0.154559  0.327778 0.177235  0.00091445  0.0223323   -0.0168933  306 GLN   A CA   
2376 C  C    . GLN   A 306 ? 0.167996  0.340383 0.178588  0.00670738  0.0216197   -0.0191409  306 GLN   A C    
2377 O  O    . GLN   A 306 ? 0.162331  0.361336 0.166792  0.0052564   0.0285557   0.00421144  306 GLN   A O    
2378 C  CB   . GLN   A 306 ? 0.170968  0.335521 0.199466  -0.00451676 0.0322475   -0.0170664  306 GLN   A CB   
2379 C  CG   . GLN   A 306 ? 0.196786  0.35271  0.243277  0.00127022  0.0475994   -0.0146884  306 GLN   A CG   
2380 C  CD   . GLN   A 306 ? 0.245474  0.372045 0.299023  -0.00498567 0.0650344   -0.0147407  306 GLN   A CD   
2381 O  OE1  . GLN   A 306 ? 0.307068  0.430921 0.308227  -0.0121638  0.0870221   0.00282748  306 GLN   A OE1  
2382 N  NE2  . GLN   A 306 ? 0.260039  0.390194 0.326202  -0.0112462  0.0635503   -0.0280385  306 GLN   A NE2  
2383 O  OXT  . GLN   A 306 ? 0.192467  0.377916 0.18057   -0.0142907  0.0102937   -0.0221402  306 GLN   A OXT  
2384 N  N    . SER   B 1   ? 0.192903  0.26211  0.132576  0.0035452   -0.0205078  -0.0291053  1   SER   B N    
2385 C  CA   . SER   B 1   ? 0.203526  0.261065 0.144587  0.0150497   -0.0166134  -0.0224232  1   SER   B CA   
2386 C  C    . SER   B 1   ? 0.188393  0.240963 0.138934  0.0234254   -0.0133486  -0.0170522  1   SER   B C    
2387 O  O    . SER   B 1   ? 0.148325  0.226598 0.129636  0.0168886   -0.0140047  -0.013424   1   SER   B O    
2388 C  CB   . SER   B 1   ? 0.228004  0.283515 0.179735  0.0255304   0.0020259   -0.028466   1   SER   B CB   
2389 O  OG   . SER   B 1   ? 0.244852  0.320823 0.164201  0.022078    0.00424264  -0.029163   1   SER   B OG   
2390 N  N    . GLY   B 2   ? 0.197922  0.252567 0.154776  0.0268844   -0.0316268  -0.0208745  2   GLY   B N    
2391 C  CA   . GLY   B 2   ? 0.203905  0.261198 0.131637  0.0291161   -0.0350601  -0.0253369  2   GLY   B CA   
2392 C  C    . GLY   B 2   ? 0.202973  0.27941  0.120039  0.0273556   -0.0308839  -0.036314   2   GLY   B C    
2393 O  O    . GLY   B 2   ? 0.236261  0.320238 0.13302   -9.995e-05  -0.0434646  -0.0175966  2   GLY   B O    
2394 N  N    . PHE   B 3   ? 0.192404  0.297602 0.0986718 0.0392614   -0.0237987  -0.0376322  3   PHE   B N    
2395 C  CA   . PHE   B 3   ? 0.19674   0.299839 0.108035  0.0529022   -0.0303433  -0.0437231  3   PHE   B CA   
2396 C  C    . PHE   B 3   ? 0.194806  0.313354 0.118255  0.0477251   -0.0158568  -0.036633   3   PHE   B C    
2397 O  O    . PHE   B 3   ? 0.21207   0.372824 0.173423  0.0388488   0.0113723   -0.0684934  3   PHE   B O    
2398 C  CB   . PHE   B 3   ? 0.211353  0.291489 0.117022  0.0545405   -0.037108   -0.0493698  3   PHE   B CB   
2399 C  CG   . PHE   B 3   ? 0.204259  0.292348 0.123884  0.0555256   -0.038199   -0.0376492  3   PHE   B CG   
2400 C  CD1  . PHE   B 3   ? 0.197921  0.298039 0.148907  0.0531352   -0.0396277  -0.0349488  3   PHE   B CD1  
2401 C  CD2  . PHE   B 3   ? 0.205132  0.288902 0.145234  0.0450841   -0.0303988  -0.0461785  3   PHE   B CD2  
2402 C  CE1  . PHE   B 3   ? 0.200157  0.300964 0.156391  0.0516131   -0.0317955  -0.0257678  3   PHE   B CE1  
2403 C  CE2  . PHE   B 3   ? 0.200998  0.286823 0.147794  0.054742    -0.0359904  -0.0322829  3   PHE   B CE2  
2404 C  CZ   . PHE   B 3   ? 0.206175  0.295032 0.152404  0.0522042   -0.0424918  -0.0385724  3   PHE   B CZ   
2405 N  N    . ARG   B 4   ? 0.181075  0.316451 0.0949555 0.0437704   -0.0124462  -0.0267399  4   ARG   B N    
2406 C  CA   . ARG   B 4   ? 0.176991  0.319238 0.093093  0.033983    -0.0139729  -0.00638497 4   ARG   B CA   
2407 C  C    . ARG   B 4   ? 0.175203  0.292416 0.0978208 0.0253414   -0.0191285  -0.0118836  4   ARG   B C    
2408 O  O    . ARG   B 4   ? 0.179493  0.269733 0.110838  0.029433    -0.0151093  -0.0163291  4   ARG   B O    
2409 C  CB   . ARG   B 4   ? 0.181567  0.349569 0.100098  0.030659    -0.0244475  0.0155546   4   ARG   B CB   
2410 C  CG   . ARG   B 4   ? 0.195891  0.391531 0.104211  0.0263688   -0.0202115  0.0323945   4   ARG   B CG   
2411 C  CD   . ARG   B 4   ? 0.223591  0.435526 0.115489  0.00907265  -0.0145078  0.0636857   4   ARG   B CD   
2412 N  NE   . ARG   B 4   ? 0.220931  0.451093 0.150646  -0.0337194  -0.0341459  0.0849499   4   ARG   B NE   
2413 C  CZ   . ARG   B 4   ? 0.250012  0.467655 0.145716  -0.0496199  -0.0187758  0.0594535   4   ARG   B CZ   
2414 N  NH1  . ARG   B 4   ? 0.268892  0.499224 0.166636  -0.0458945  -0.0351011  0.0619401   4   ARG   B NH1  
2415 N  NH2  . ARG   B 4   ? 0.242639  0.438419 0.150203  -0.0722183  -0.0408366  0.0529782   4   ARG   B NH2  
2416 N  N    . LYS   B 5   ? 0.179105  0.296136 0.101695  0.0148335   -0.0175599  -0.0107903  5   LYS   B N    
2417 C  CA   . LYS   B 5   ? 0.182473  0.281564 0.108369  0.0065973   -0.0230408  -0.0152529  5   LYS   B CA   
2418 C  C    . LYS   B 5   ? 0.194306  0.255922 0.121636  0.00230839  -0.019837   -0.00798266 5   LYS   B C    
2419 O  O    . LYS   B 5   ? 0.254196  0.269389 0.166089  0.00862727  0.0161703   0.0148275   5   LYS   B O    
2420 C  CB   . LYS   B 5   ? 0.204835  0.31569  0.142922  -0.00734101 -0.0246134  -0.0175428  5   LYS   B CB   
2421 C  CG   . LYS   B 5   ? 0.240496  0.340114 0.160549  -0.0103713  -0.036419   -0.0263658  5   LYS   B CG   
2422 C  CD   . LYS   B 5   ? 0.253748  0.347879 0.169701  -0.00548913 -0.0387354  -0.0213135  5   LYS   B CD   
2423 C  CE   . LYS   B 5   ? 0.289169  0.354204 0.191045  -0.00394009 -0.0318112  -0.037193   5   LYS   B CE   
2424 N  NZ   . LYS   B 5   ? 0.296669  0.356832 0.216895  0.00303061  -0.0201256  -0.0429835  5   LYS   B NZ   
2425 N  N    . MET   B 6   ? 0.183742  0.230868 0.107397  0.00538847  -0.0243093  -0.00802357 6   MET   B N    
2426 C  CA   . MET   B 6   ? 0.19434   0.240124 0.106717  0.00583825  -0.0297453  -0.0191378  6   MET   B CA   
2427 C  C    . MET   B 6   ? 0.17844   0.21035  0.099731  0.0143937   -0.0334777  -0.00409001 6   MET   B C    
2428 O  O    . MET   B 6   ? 0.237557  0.20706  0.110035  0.024146    -0.0508237  -0.00863472 6   MET   B O    
2429 C  CB   . MET   B 6   ? 0.203866  0.286739 0.153546  -0.00471844 -0.0252723  -0.0278506  6   MET   B CB   
2430 C  CG   . MET   B 6   ? 0.222685  0.321375 0.197515  -0.00306673 -0.0267334  -0.042248   6   MET   B CG   
2431 S  SD   . MET   B 6   ? 0.241302  0.410903 0.309001  -0.0389954  -0.0219617  -0.0913155  6   MET   B SD   
2432 C  CE   . MET   B 6   ? 0.232171  0.361692 0.291697  -0.03524    -0.0189092  -0.0553722  6   MET   B CE   
2433 N  N    . ALA   B 7   ? 0.169707  0.203972 0.0830667 0.0163796   -0.0303684  0.00551136  7   ALA   B N    
2434 C  CA   . ALA   B 7   ? 0.167451  0.206812 0.083107  0.0211516   -0.0262059  0.00626495  7   ALA   B CA   
2435 C  C    . ALA   B 7   ? 0.160455  0.21351  0.0817124 0.0172969   -0.0300336  -0.00054922 7   ALA   B C    
2436 O  O    . ALA   B 7   ? 0.153577  0.223421 0.0819556 0.0138335   -0.0303883  0.00650976  7   ALA   B O    
2437 C  CB   . ALA   B 7   ? 0.166706  0.209069 0.0944128 0.0204763   -0.0200876  0.0157696   7   ALA   B CB   
2438 N  N    . PHE   B 8   ? 0.161698  0.217039 0.0782898 0.0187804   -0.0322002  -0.00967004 8   PHE   B N    
2439 C  CA   . PHE   B 8   ? 0.168603  0.224466 0.0735122 0.013875    -0.0300178  -0.0197259  8   PHE   B CA   
2440 C  C    . PHE   B 8   ? 0.154831  0.223155 0.084832  0.00914189  -0.0334563  -0.0149035  8   PHE   B C    
2441 O  O    . PHE   B 8   ? 0.143656  0.220043 0.106461  0.00899855  -0.0195731  -0.00541925 8   PHE   B O    
2442 C  CB   . PHE   B 8   ? 0.192656  0.228299 0.0682776 0.010589    -0.0264457  -0.0257118  8   PHE   B CB   
2443 C  CG   . PHE   B 8   ? 0.234171  0.232301 0.0576051 0.0143598   -0.0149052  -0.0318151  8   PHE   B CG   
2444 C  CD1  . PHE   B 8   ? 0.259793  0.236931 0.0853269 0.0132108   -0.0115355  -0.0275352  8   PHE   B CD1  
2445 C  CD2  . PHE   B 8   ? 0.265537  0.240897 0.0811978 0.019384    -0.0201557  -0.01945    8   PHE   B CD2  
2446 C  CE1  . PHE   B 8   ? 0.286899  0.248344 0.103047  0.00352578  -0.00048276 -0.0211     8   PHE   B CE1  
2447 C  CE2  . PHE   B 8   ? 0.295264  0.246085 0.111897  0.0137049   -0.017976   -0.0162199  8   PHE   B CE2  
2448 C  CZ   . PHE   B 8   ? 0.299419  0.247758 0.124194  0.0111828   -0.00621541 -0.0136663  8   PHE   B CZ   
2449 N  N    . PRO   B 9   ? 0.154046  0.236542 0.0970998 0.0130046   -0.0338442  -0.0100177  9   PRO   B N    
2450 C  CA   . PRO   B 9   ? 0.154766  0.234571 0.081155  0.0150311   -0.0375552  -0.0119456  9   PRO   B CA   
2451 C  C    . PRO   B 9   ? 0.159075  0.22991  0.0787668 0.011025    -0.041347   -0.00587002 9   PRO   B C    
2452 O  O    . PRO   B 9   ? 0.20927   0.262551 0.0868641 -0.00287023 -0.0288619  0.00640325  9   PRO   B O    
2453 C  CB   . PRO   B 9   ? 0.152917  0.247407 0.102691  0.0199169   -0.0338202  -0.0142904  9   PRO   B CB   
2454 C  CG   . PRO   B 9   ? 0.157835  0.256382 0.136164  0.0161266   -0.0287622  -0.0138531  9   PRO   B CG   
2455 C  CD   . PRO   B 9   ? 0.16325   0.245625 0.118869  0.0109002   -0.0351789  -0.0146042  9   PRO   B CD   
2456 N  N    . SER   B 10  ? 0.156451  0.222495 0.0680762 0.0160735   -0.0329285  0.000259    10  SER   B N    
2457 C  CA   . SER   B 10  ? 0.143549  0.221961 0.0721113 0.0168977   -0.0238241  -0.00471264 10  SER   B CA   
2458 C  C    . SER   B 10  ? 0.147405  0.222396 0.0814365 0.0194513   -0.0223731  -0.00564137 10  SER   B C    
2459 O  O    . SER   B 10  ? 0.153575  0.222603 0.0813664 0.0179562   -0.0208077  -0.00823975 10  SER   B O    
2460 C  CB   . SER   B 10  ? 0.142689  0.228637 0.0835956 0.0194702   -0.0174696  0.00077239  10  SER   B CB   
2461 O  OG   . SER   B 10  ? 0.13891   0.246234 0.0768812 0.0237558   -0.0102578  0.00583197  10  SER   B OG   
2462 N  N    . GLY   B 11  ? 0.156841  0.232649 0.0812043 0.0276281   -0.0268092  -0.0118809  11  GLY   B N    
2463 C  CA   . GLY   B 11  ? 0.152911  0.231689 0.0846014 0.0314887   -0.0257435  -0.00657359 11  GLY   B CA   
2464 C  C    . GLY   B 11  ? 0.161917  0.240188 0.0900558 0.0232626   -0.0218814  -0.0077143  11  GLY   B C    
2465 O  O    . GLY   B 11  ? 0.1744    0.234108 0.102122  0.0281185   -0.00450836 -0.0196687  11  GLY   B O    
2466 N  N    . LYS   B 12  ? 0.161164  0.246641 0.0816912 0.018798    -0.0202789  -0.00355223 12  LYS   B N    
2467 C  CA   . LYS   B 12  ? 0.166883  0.263334 0.0802197 0.018342    -0.0236049  -0.00488227 12  LYS   B CA   
2468 C  C    . LYS   B 12  ? 0.166212  0.259602 0.0698109 0.0203515   -0.0222128  -0.00812545 12  LYS   B C    
2469 O  O    . LYS   B 12  ? 0.176855  0.296774 0.068201  0.0246641   -0.0214786  -0.0215264  12  LYS   B O    
2470 C  CB   . LYS   B 12  ? 0.185411  0.28046  0.0993464 0.00329971  -0.0256883  -0.00490896 12  LYS   B CB   
2471 C  CG   . LYS   B 12  ? 0.209163  0.32187  0.148228  -0.0161704  -0.0277054  -0.00728054 12  LYS   B CG   
2472 C  CD   . LYS   B 12  ? 0.263579  0.353557 0.217057  -0.0268256  -0.0356644  0.0051346   12  LYS   B CD   
2473 C  CE   . LYS   B 12  ? 0.296742  0.408921 0.28809   -0.0385443  -0.0249468  0.00523233  12  LYS   B CE   
2474 N  NZ   . LYS   B 12  ? 0.331657  0.438229 0.335787  -0.0348555  -0.0446057  0.00773748  12  LYS   B NZ   
2475 N  N    . VAL   B 13  ? 0.155099  0.239623 0.054107  0.0238877   -0.0286484  -0.00754676 13  VAL   B N    
2476 C  CA   . VAL   B 13  ? 0.160339  0.225619 0.0636113 0.0211076   -0.0329947  -0.00526356 13  VAL   B CA   
2477 C  C    . VAL   B 13  ? 0.155876  0.221719 0.067526  0.0163529   -0.0329854  -0.00652552 13  VAL   B C    
2478 O  O    . VAL   B 13  ? 0.166156  0.218237 0.0664335 0.0170944   -0.0345831  -0.0113902  13  VAL   B O    
2479 C  CB   . VAL   B 13  ? 0.162605  0.222889 0.0719418 0.0226792   -0.0345071  -0.00089037 13  VAL   B CB   
2480 C  CG1  . VAL   B 13  ? 0.167201  0.223144 0.0675305 0.0181252   -0.0251067  0.00117451  13  VAL   B CG1  
2481 C  CG2  . VAL   B 13  ? 0.166803  0.223078 0.0920625 0.020871    -0.0397087  -0.00450931 13  VAL   B CG2  
2482 N  N    . GLU   B 14  ? 0.160075  0.219647 0.0619629 0.0134946   -0.0344807  -0.00987635 14  GLU   B N    
2483 C  CA   . GLU   B 14  ? 0.162466  0.223613 0.0687541 0.0159394   -0.0231531  -0.00603421 14  GLU   B CA   
2484 C  C    . GLU   B 14  ? 0.168982  0.224728 0.0725931 0.0199469   -0.024508   -0.00578248 14  GLU   B C    
2485 O  O    . GLU   B 14  ? 0.188078  0.229898 0.0826204 0.00881245  -0.0151076  -0.0128755  14  GLU   B O    
2486 C  CB   . GLU   B 14  ? 0.161492  0.225002 0.064239  0.0187583   -0.0158682  8.238e-05   14  GLU   B CB   
2487 C  CG   . GLU   B 14  ? 0.16162   0.227306 0.071049  0.0131401   -0.0136102  -0.00475693 14  GLU   B CG   
2488 C  CD   . GLU   B 14  ? 0.162491  0.236526 0.079809  0.0131234   -0.0174976  -0.00043309 14  GLU   B CD   
2489 O  OE1  . GLU   B 14  ? 0.157337  0.258992 0.0748339 0.0158743   -0.0265832  -0.00887059 14  GLU   B OE1  
2490 O  OE2  . GLU   B 14  ? 0.178087  0.250295 0.0915229 0.0134166   -0.019852   0.00361258  14  GLU   B OE2  
2491 N  N    . GLY   B 15  ? 0.162897  0.238556 0.0751494 0.0280885   -0.0268537  -0.0146447  15  GLY   B N    
2492 C  CA   . GLY   B 15  ? 0.174635  0.243853 0.0847848 0.0341027   -0.0236725  -0.0201916  15  GLY   B CA   
2493 C  C    . GLY   B 15  ? 0.177028  0.243336 0.0847582 0.0398587   -0.023936   -0.0218536  15  GLY   B C    
2494 O  O    . GLY   B 15  ? 0.196799  0.263162 0.0891343 0.060695    -0.0223737  -0.0305485  15  GLY   B O    
2495 N  N    . CYS   B 16  ? 0.162812  0.233472 0.058638  0.0331025   -0.0154269  -0.0144981  16  CYS   B N    
2496 C  CA   . CYS   B 16  ? 0.163951  0.235201 0.0589803 0.01539     -0.0159606  -0.00874894 16  CYS   B CA   
2497 C  C    . CYS   B 16  ? 0.159587  0.223921 0.0578655 0.018394    -0.00741505 -0.00470377 16  CYS   B C    
2498 O  O    . CYS   B 16  ? 0.159412  0.236354 0.0679019 0.0179205   -0.0133945  0.00197971  16  CYS   B O    
2499 C  CB   . CYS   B 16  ? 0.172836  0.245778 0.070972  0.00964791  -0.0224706  -0.00234653 16  CYS   B CB   
2500 S  SG   . CYS   B 16  ? 0.201055  0.287246 0.101061  -0.0235379  -0.029254   0.019981    16  CYS   B SG   
2501 N  N    . MET   B 17  ? 0.155038  0.213146 0.0557597 0.0207558   -0.0125354  0.00043512  17  MET   B N    
2502 C  CA   . MET   B 17  ? 0.163748  0.200123 0.0626582 0.0182397   -0.0138798  -0.00350338 17  MET   B CA   
2503 C  C    . MET   B 17  ? 0.166563  0.195309 0.0735499 0.0198071   -0.0131704  -0.00220404 17  MET   B C    
2504 O  O    . MET   B 17  ? 0.185785  0.200671 0.120938  0.0211442   -0.0218887  0.00972446  17  MET   B O    
2505 C  CB   . MET   B 17  ? 0.178129  0.207689 0.0700315 0.018537    -0.00134594 -0.00271462 17  MET   B CB   
2506 C  CG   . MET   B 17  ? 0.184871  0.207763 0.0722627 0.0128142   0.00031727  -0.00936764 17  MET   B CG   
2507 S  SD   . MET   B 17  ? 0.193382  0.219456 0.110712  0.0226676   -0.0026511  -0.0151374  17  MET   B SD   
2508 C  CE   . MET   B 17  ? 0.200056  0.236766 0.068265  0.0175762   -0.0125618  -0.031077   17  MET   B CE   
2509 N  N    . VAL   B 18  ? 0.172806  0.191285 0.072447  0.0158612   -0.0129215  -0.00344588 18  VAL   B N    
2510 C  CA   . VAL   B 18  ? 0.181478  0.189533 0.0693972 0.0147119   -0.00760683 -0.00246326 18  VAL   B CA   
2511 C  C    . VAL   B 18  ? 0.195283  0.184681 0.0671407 0.00920461  -0.00210605 -0.00414126 18  VAL   B C    
2512 O  O    . VAL   B 18  ? 0.195202  0.183689 0.0724376 0.0144664   -0.00122885 0.00055716  18  VAL   B O    
2513 C  CB   . VAL   B 18  ? 0.189043  0.193502 0.0754934 0.0126523   -0.00226002 -0.0100508  18  VAL   B CB   
2514 C  CG1  . VAL   B 18  ? 0.189875  0.201114 0.0856262 0.0137946   -0.00533515 -0.00989635 18  VAL   B CG1  
2515 C  CG2  . VAL   B 18  ? 0.187364  0.200582 0.0618933 0.00541313  -0.0107679  -0.0180498  18  VAL   B CG2  
2516 N  N    . GLN   B 19  ? 0.210472  0.195615 0.0952327 0.00513691  0.0118195   -0.019533   19  GLN   B N    
2517 C  CA   . GLN   B 19  ? 0.212129  0.202973 0.116026  -0.00802421 0.0130991   -0.0195963  19  GLN   B CA   
2518 C  C    . GLN   B 19  ? 0.203413  0.204839 0.12756   -0.00413542 0.0139593   -0.0282787  19  GLN   B C    
2519 O  O    . GLN   B 19  ? 0.209679  0.227176 0.124365  0.0152741   0.00604795  -0.039707   19  GLN   B O    
2520 C  CB   . GLN   B 19  ? 0.244904  0.22379  0.134901  -0.0121325  -0.00293356 -0.0128455  19  GLN   B CB   
2521 C  CG   . GLN   B 19  ? 0.278811  0.258128 0.161971  -0.0250107  0.0112425   -0.00934588 19  GLN   B CG   
2522 C  CD   . GLN   B 19  ? 0.352295  0.293849 0.209569  -0.0176444  -0.00787353 0.00722141  19  GLN   B CD   
2523 O  OE1  . GLN   B 19  ? 0.450057  0.392161 0.236456  -0.0413694  0.00118002  0.0258973   19  GLN   B OE1  
2524 N  NE2  . GLN   B 19  ? 0.38601   0.287186 0.238101  -0.00127264 -0.0387759  0.0134191   19  GLN   B NE2  
2525 N  N    . VAL   B 20  ? 0.190756  0.207419 0.130523  -0.0137645  0.0195563   -0.0318906  20  VAL   B N    
2526 C  CA   . VAL   B 20  ? 0.19472   0.208356 0.137993  -0.0176409  0.0190655   -0.0385891  20  VAL   B CA   
2527 C  C    . VAL   B 20  ? 0.203475  0.214289 0.151235  -0.0239151  0.0249191   -0.0434477  20  VAL   B C    
2528 O  O    . VAL   B 20  ? 0.215911  0.201977 0.121135  -0.0223186  0.0217627   -0.037477   20  VAL   B O    
2529 C  CB   . VAL   B 20  ? 0.194221  0.212454 0.13999   -0.0114061  0.0164832   -0.0352709  20  VAL   B CB   
2530 C  CG1  . VAL   B 20  ? 0.197532  0.229016 0.145922  -0.00907961 0.015622    -0.0312225  20  VAL   B CG1  
2531 C  CG2  . VAL   B 20  ? 0.197568  0.209147 0.142874  -0.0114168  0.00466528  -0.0299664  20  VAL   B CG2  
2532 N  N    . THR   B 21  ? 0.224642  0.227938 0.168115  -0.026215   0.0334749   -0.0596871  21  THR   B N    
2533 C  CA   . THR   B 21  ? 0.233802  0.239704 0.188615  -0.0286974  0.0278942   -0.0657293  21  THR   B CA   
2534 C  C    . THR   B 21  ? 0.228803  0.258189 0.184975  -0.0247436  0.0364864   -0.0712154  21  THR   B C    
2535 O  O    . THR   B 21  ? 0.229159  0.273324 0.185596  -0.0177741  0.0387368   -0.0901361  21  THR   B O    
2536 C  CB   . THR   B 21  ? 0.259627  0.246168 0.216404  -0.0333615  0.0219551   -0.0519709  21  THR   B CB   
2537 O  OG1  . THR   B 21  ? 0.28649   0.263828 0.221858  -0.0345538  0.0147742   -0.0396192  21  THR   B OG1  
2538 C  CG2  . THR   B 21  ? 0.277976  0.249628 0.252421  -0.0356941  0.0200172   -0.0464398  21  THR   B CG2  
2539 N  N    . CYS   B 22  ? 0.224907  0.253214 0.184495  -0.0297049  0.029308    -0.0688118  22  CYS   B N    
2540 C  CA   . CYS   B 22  ? 0.230729  0.25505  0.197     -0.0427704  0.0246907   -0.0621627  22  CYS   B CA   
2541 C  C    . CYS   B 22  ? 0.244103  0.244905 0.209152  -0.0555642  0.0150647   -0.0548316  22  CYS   B C    
2542 O  O    . CYS   B 22  ? 0.222302  0.259768 0.226278  -0.0554712  0.0129925   -0.0402316  22  CYS   B O    
2543 C  CB   . CYS   B 22  ? 0.239178  0.27186  0.183025  -0.0353112  0.0325984   -0.0597716  22  CYS   B CB   
2544 S  SG   . CYS   B 22  ? 0.244989  0.301609 0.228777  -0.0453009  0.00495952  -0.043259   22  CYS   B SG   
2545 N  N    . GLY   B 23  ? 0.269195  0.246489 0.239355  -0.0608428  0.0244482   -0.0552034  23  GLY   B N    
2546 C  CA   . GLY   B 23  ? 0.286612  0.261537 0.230575  -0.0673375  0.0244753   -0.0423124  23  GLY   B CA   
2547 C  C    . GLY   B 23  ? 0.292195  0.269093 0.231378  -0.0684534  0.0255857   -0.0366452  23  GLY   B C    
2548 O  O    . GLY   B 23  ? 0.292525  0.265157 0.269887  -0.0778298  0.0311589   -0.0380709  23  GLY   B O    
2549 N  N    . THR   B 24  ? 0.291604  0.269082 0.211104  -0.0693446  0.0163133   -0.0346009  24  THR   B N    
2550 C  CA   . THR   B 24  ? 0.289423  0.271354 0.205191  -0.0656619  0.023131    -0.0284619  24  THR   B CA   
2551 C  C    . THR   B 24  ? 0.265609  0.239721 0.171215  -0.0569647  0.021615    -0.00777654 24  THR   B C    
2552 O  O    . THR   B 24  ? 0.304902  0.240988 0.172125  -0.0640237  0.0259579   -0.0218281  24  THR   B O    
2553 C  CB   . THR   B 24  ? 0.296913  0.293645 0.233088  -0.071964   0.012298    -0.0330058  24  THR   B CB   
2554 O  OG1  . THR   B 24  ? 0.293882  0.312852 0.242471  -0.0735406  0.00612875  -0.0215669  24  THR   B OG1  
2555 C  CG2  . THR   B 24  ? 0.313044  0.307831 0.266489  -0.07837    -0.00345742 -0.0317965  24  THR   B CG2  
2556 N  N    . THR   B 25  ? 0.240624  0.232225 0.169841  -0.0465149  0.0257551   -0.0177666  25  THR   B N    
2557 C  CA   . THR   B 25  ? 0.220382  0.232066 0.159795  -0.0346385  0.0268818   -0.0181907  25  THR   B CA   
2558 C  C    . THR   B 25  ? 0.217898  0.231963 0.161001  -0.0303674  0.0319132   -0.0150857  25  THR   B C    
2559 O  O    . THR   B 25  ? 0.223535  0.256097 0.150211  -0.0307763  0.0284638   -0.0361925  25  THR   B O    
2560 C  CB   . THR   B 25  ? 0.223362  0.231557 0.155864  -0.0327856  0.015802    -0.0200588  25  THR   B CB   
2561 O  OG1  . THR   B 25  ? 0.222038  0.236522 0.165749  -0.0402233  0.00809235  -0.0166513  25  THR   B OG1  
2562 C  CG2  . THR   B 25  ? 0.228459  0.2397   0.153692  -0.0337953  0.00062548  -0.0174775  25  THR   B CG2  
2563 N  N    . THR   B 26  ? 0.210553  0.214014 0.161405  -0.0248281  0.028361    -0.0154231  26  THR   B N    
2564 C  CA   . THR   B 26  ? 0.206159  0.204717 0.155775  -0.0234095  0.0374633   -0.00528843 26  THR   B CA   
2565 C  C    . THR   B 26  ? 0.185863  0.19984  0.138857  -0.0275782  0.0373374   -0.00507743 26  THR   B C    
2566 O  O    . THR   B 26  ? 0.194355  0.207    0.156186  -0.0294599  0.0527296   -0.0155908  26  THR   B O    
2567 C  CB   . THR   B 26  ? 0.225098  0.205332 0.204273  -0.00531753 0.0285413   -0.00036871 26  THR   B CB   
2568 O  OG1  . THR   B 26  ? 0.259572  0.218293 0.244246  0.00064767  0.0183497   -0.0031719  26  THR   B OG1  
2569 C  CG2  . THR   B 26  ? 0.241886  0.21657  0.215941  -0.0137209  0.0249305   0.00567454  26  THR   B CG2  
2570 N  N    . LEU   B 27  ? 0.184607  0.189255 0.121076  -0.0282752  0.0355436   -0.015819   27  LEU   B N    
2571 C  CA   . LEU   B 27  ? 0.173854  0.192435 0.104076  -0.0241906  0.0222641   -0.0170019  27  LEU   B CA   
2572 C  C    . LEU   B 27  ? 0.169407  0.18534  0.0830752 -0.0158423  0.0170439   -0.0159294  27  LEU   B C    
2573 O  O    . LEU   B 27  ? 0.203705  0.187536 0.0984523 -0.01389    0.00845387  -0.019178   27  LEU   B O    
2574 C  CB   . LEU   B 27  ? 0.170004  0.20494  0.101686  -0.0253596  0.0181257   -0.0205355  27  LEU   B CB   
2575 C  CG   . LEU   B 27  ? 0.1736    0.20525  0.101729  -0.0222277  0.0119691   -0.0160603  27  LEU   B CG   
2576 C  CD1  . LEU   B 27  ? 0.170537  0.209757 0.108267  -0.0199632  0.00788727  -0.0185721  27  LEU   B CD1  
2577 C  CD2  . LEU   B 27  ? 0.185386  0.2171   0.111649  -0.0181669  0.015059    -0.0173346  27  LEU   B CD2  
2578 N  N    . ASN   B 28  ? 0.157218  0.183843 0.0711389 -0.00849144 0.00907026  -0.0121464  28  ASN   B N    
2579 C  CA   . ASN   B 28  ? 0.154039  0.185727 0.061975  -0.00772526 0.00139795  -0.011512   28  ASN   B CA   
2580 C  C    . ASN   B 28  ? 0.151978  0.18879  0.06711   -0.00398261 0.00348075  -0.00891507 28  ASN   B C    
2581 O  O    . ASN   B 28  ? 0.154747  0.20593  0.0681466 0.00211911  0.00068359  -0.0136912  28  ASN   B O    
2582 C  CB   . ASN   B 28  ? 0.1614    0.182436 0.0636612 -0.00642019 -0.00244934 -0.00924798 28  ASN   B CB   
2583 C  CG   . ASN   B 28  ? 0.172061  0.186981 0.0649519 0.00197783  -0.00083952 -0.00491005 28  ASN   B CG   
2584 O  OD1  . ASN   B 28  ? 0.177171  0.192511 0.0744963 0.00254867  0.00687003  0.0060249   28  ASN   B OD1  
2585 N  ND2  . ASN   B 28  ? 0.181537  0.205487 0.0573857 0.00143042  0.00029205  -0.00310379 28  ASN   B ND2  
2586 N  N    . GLY   B 29  ? 0.1489    0.190277 0.0705962 -0.00145094 -0.00232674 -0.00268138 29  GLY   B N    
2587 C  CA   . GLY   B 29  ? 0.144152  0.188799 0.0693619 -0.00368103 0.00391853  -0.00619861 29  GLY   B CA   
2588 C  C    . GLY   B 29  ? 0.140699  0.189405 0.0671738 0.00091122  -0.00233528 -0.00661698 29  GLY   B C    
2589 O  O    . GLY   B 29  ? 0.135454  0.190495 0.063218  0.00065484  -0.00033514 -0.00395843 29  GLY   B O    
2590 N  N    . LEU   B 30  ? 0.134743  0.187351 0.0619627 -0.00056514 0.00271537  -0.00796661 30  LEU   B N    
2591 C  CA   . LEU   B 30  ? 0.133663  0.197559 0.0429999 -0.000732   0.00117106  -0.0125122  30  LEU   B CA   
2592 C  C    . LEU   B 30  ? 0.136504  0.19982  0.0458797 0.0118718   -0.00134469 -0.0136662  30  LEU   B C    
2593 O  O    . LEU   B 30  ? 0.14409   0.20934  0.0533963 0.0151545   -0.0120384  -0.0126269  30  LEU   B O    
2594 C  CB   . LEU   B 30  ? 0.139967  0.197435 0.0529337 -0.00644419 0.00628174  -0.0137489  30  LEU   B CB   
2595 C  CG   . LEU   B 30  ? 0.147604  0.191539 0.0539589 -0.0106079  0.0131751   -0.0144089  30  LEU   B CG   
2596 C  CD1  . LEU   B 30  ? 0.150717  0.201281 0.0710124 -0.00917972 0.00120382  -0.0148661  30  LEU   B CD1  
2597 C  CD2  . LEU   B 30  ? 0.146053  0.191106 0.0507348 -0.0116074  0.0144123   -0.0116592  30  LEU   B CD2  
2598 N  N    . TRP   B 31  ? 0.135932  0.201749 0.0497949 0.0174307   -0.00057083 -0.0162542  31  TRP   B N    
2599 C  CA   . TRP   B 31  ? 0.133632  0.205231 0.055272  0.0195776   -0.00380244 -0.0200049  31  TRP   B CA   
2600 C  C    . TRP   B 31  ? 0.132055  0.208993 0.0633971 0.014995    -0.00479042 -0.0217423  31  TRP   B C    
2601 O  O    . TRP   B 31  ? 0.129033  0.221999 0.0676049 0.0108978   -0.00618146 -0.0155918  31  TRP   B O    
2602 C  CB   . TRP   B 31  ? 0.143845  0.208438 0.075232  0.0236573   -0.00137074 -0.0214108  31  TRP   B CB   
2603 C  CG   . TRP   B 31  ? 0.157636  0.222413 0.0861346 0.0316819   0.00213348  -0.023987   31  TRP   B CG   
2604 C  CD1  . TRP   B 31  ? 0.168138  0.22818  0.092201  0.033214    0.00231923  -0.0201974  31  TRP   B CD1  
2605 C  CD2  . TRP   B 31  ? 0.164829  0.237357 0.106862  0.0377253   0.00722223  -0.0153918  31  TRP   B CD2  
2606 N  NE1  . TRP   B 31  ? 0.171844  0.242874 0.108731  0.0381224   0.00083152  -0.022756   31  TRP   B NE1  
2607 C  CE2  . TRP   B 31  ? 0.177633  0.23937  0.116179  0.0483824   0.0132533   -0.0175907  31  TRP   B CE2  
2608 C  CE3  . TRP   B 31  ? 0.173108  0.240774 0.118482  0.0401577   0.012615    -0.00692814 31  TRP   B CE3  
2609 C  CZ2  . TRP   B 31  ? 0.173344  0.249867 0.129892  0.0537292   0.00972936  -0.0185439  31  TRP   B CZ2  
2610 C  CZ3  . TRP   B 31  ? 0.179616  0.256532 0.131406  0.0446317   0.00187956  -0.00140785 31  TRP   B CZ3  
2611 C  CH2  . TRP   B 31  ? 0.170822  0.24712  0.146303  0.0569399   0.0052711   -0.0123362  31  TRP   B CH2  
2612 N  N    . LEU   B 32  ? 0.131649  0.220177 0.06718   0.0122392   -0.00650587 -0.0206127  32  LEU   B N    
2613 C  CA   . LEU   B 32  ? 0.128775  0.227233 0.0627416 0.0139929   0.00753915  -0.01999    32  LEU   B CA   
2614 C  C    . LEU   B 32  ? 0.130986  0.244775 0.0678871 0.0166715   0.0112121   -0.0251721  32  LEU   B C    
2615 O  O    . LEU   B 32  ? 0.138143  0.242234 0.0755774 0.0161971   -0.00097892 -0.022123   32  LEU   B O    
2616 C  CB   . LEU   B 32  ? 0.140951  0.2279   0.0748567 0.0127382   0.0189935   -0.0169691  32  LEU   B CB   
2617 C  CG   . LEU   B 32  ? 0.15037   0.230638 0.08311   0.0163013   0.0261519   -0.0180485  32  LEU   B CG   
2618 C  CD1  . LEU   B 32  ? 0.14945   0.23231  0.0931262 0.0175789   0.0304068   -0.0149964  32  LEU   B CD1  
2619 C  CD2  . LEU   B 32  ? 0.1696    0.230072 0.0848757 0.0217609   0.0179457   -0.0229979  32  LEU   B CD2  
2620 N  N    . ASP   B 33  ? 0.133745  0.258614 0.0840535 0.0139127   0.00730352  -0.0369706  33  ASP   B N    
2621 C  CA   . ASP   B 33  ? 0.154623  0.26561  0.0885076 0.0221203   0.0145089   -0.0365065  33  ASP   B CA   
2622 C  C    . ASP   B 33  ? 0.162087  0.265312 0.0973943 0.0250147   0.0128738   -0.0372607  33  ASP   B C    
2623 O  O    . ASP   B 33  ? 0.168337  0.287345 0.116739  0.0327596   0.00290246  -0.0289605  33  ASP   B O    
2624 C  CB   . ASP   B 33  ? 0.177712  0.278093 0.114736  0.0115074   0.0221098   -0.0335168  33  ASP   B CB   
2625 C  CG   . ASP   B 33  ? 0.21508   0.290718 0.146518  0.0100975   0.0228906   -0.041001   33  ASP   B CG   
2626 O  OD1  . ASP   B 33  ? 0.230739  0.343878 0.252403  -0.00673331 0.0062068   -0.0452928  33  ASP   B OD1  
2627 O  OD2  . ASP   B 33  ? 0.279786  0.30839  0.161462  0.0166734   0.0259651   -0.0406958  33  ASP   B OD2  
2628 N  N    . ASP   B 34  ? 0.16533   0.26155  0.0850703 0.0166509   0.0240436   -0.033045   34  ASP   B N    
2629 C  CA   . ASP   B 34  ? 0.158768  0.249169 0.0813094 0.0177645   0.0220234   -0.037059   34  ASP   B CA   
2630 C  C    . ASP   B 34  ? 0.155336  0.232927 0.0829823 0.012247    0.0089353   -0.0396785  34  ASP   B C    
2631 O  O    . ASP   B 34  ? 0.161508  0.24122  0.101973  0.0108604   0.00384463  -0.0523053  34  ASP   B O    
2632 C  CB   . ASP   B 34  ? 0.190452  0.267354 0.0931565 0.0200357   0.0295167   -0.0471952  34  ASP   B CB   
2633 C  CG   . ASP   B 34  ? 0.21708   0.288006 0.0928627 0.0142194   0.0372101   -0.0398776  34  ASP   B CG   
2634 O  OD1  . ASP   B 34  ? 0.232906  0.292789 0.0985238 0.00983584  0.0213853   -0.0282253  34  ASP   B OD1  
2635 O  OD2  . ASP   B 34  ? 0.294835  0.328353 0.101424  0.0242942   0.048395    -0.0511527  34  ASP   B OD2  
2636 N  N    . VAL   B 35  ? 0.143018  0.215812 0.0753398 0.0103561   0.00277422  -0.0330311  35  VAL   B N    
2637 C  CA   . VAL   B 35  ? 0.145774  0.217813 0.0745155 0.00168167  0.00373211  -0.0215897  35  VAL   B CA   
2638 C  C    . VAL   B 35  ? 0.139297  0.207021 0.0726872 -0.00124381 0.00050207  -0.0230011  35  VAL   B C    
2639 O  O    . VAL   B 35  ? 0.134474  0.227754 0.0656938 -0.0018829  0.00247183  -0.0235539  35  VAL   B O    
2640 C  CB   . VAL   B 35  ? 0.158326  0.226995 0.0795658 0.00147139  0.00146795  -0.0109287  35  VAL   B CB   
2641 C  CG1  . VAL   B 35  ? 0.160144  0.230464 0.0860688 0.00399033  -0.00495773 -0.00035623 35  VAL   B CG1  
2642 C  CG2  . VAL   B 35  ? 0.174147  0.23547  0.0777007 0.00093144  9.52e-06    -0.00224243 35  VAL   B CG2  
2643 N  N    . VAL   B 36  ? 0.142025  0.204108 0.0591604 -0.00283356 4.241e-05   -0.0228808  36  VAL   B N    
2644 C  CA   . VAL   B 36  ? 0.148196  0.20078  0.0567314 -0.00210515 -0.00050753 -0.0227179  36  VAL   B CA   
2645 C  C    . VAL   B 36  ? 0.139746  0.203992 0.0662848 -0.00432662 -0.00836422 -0.0231659  36  VAL   B C    
2646 O  O    . VAL   B 36  ? 0.15219   0.222476 0.0704883 -0.00102456 -0.0177553  -0.0330203  36  VAL   B O    
2647 C  CB   . VAL   B 36  ? 0.158569  0.199667 0.062797  -0.00018224 0.0056925   -0.0239503  36  VAL   B CB   
2648 C  CG1  . VAL   B 36  ? 0.155056  0.211822 0.0679911 0.00153922  0.00738802  -0.0218516  36  VAL   B CG1  
2649 C  CG2  . VAL   B 36  ? 0.164488  0.196686 0.0653804 0.00359594  0.00943467  -0.0195375  36  VAL   B CG2  
2650 N  N    . TYR   B 37  ? 0.136598  0.195474 0.063368  -0.00098277 -0.0127456  -0.0158136  37  TYR   B N    
2651 C  CA   . TYR   B 37  ? 0.131368  0.198806 0.0566889 -0.00171921 -0.0110748  -0.00909008 37  TYR   B CA   
2652 C  C    . TYR   B 37  ? 0.125424  0.19916  0.0598622 0.00047082  -0.00833918 -0.0109899  37  TYR   B C    
2653 O  O    . TYR   B 37  ? 0.133974  0.221551 0.0649805 0.00072683  -0.0152168  -0.00023162 37  TYR   B O    
2654 C  CB   . TYR   B 37  ? 0.132925  0.195942 0.0665214 0.00045471  -0.0131191  -0.00670133 37  TYR   B CB   
2655 C  CG   . TYR   B 37  ? 0.14227   0.20556  0.0821348 -0.00669498 -0.0103315  0.00064546  37  TYR   B CG   
2656 C  CD1  . TYR   B 37  ? 0.145136  0.214124 0.0921932 -0.0114766  -0.00547398 0.00765195  37  TYR   B CD1  
2657 C  CD2  . TYR   B 37  ? 0.15052   0.229699 0.0892617 -0.00897695 -0.00348246 0.0149663   37  TYR   B CD2  
2658 C  CE1  . TYR   B 37  ? 0.145223  0.228581 0.108527  -0.0101615  0.0032232   0.0104167   37  TYR   B CE1  
2659 C  CE2  . TYR   B 37  ? 0.150914  0.239639 0.0946606 -0.0113064  0.00179244  0.0182631   37  TYR   B CE2  
2660 C  CZ   . TYR   B 37  ? 0.149566  0.239835 0.100972  -0.0142664  0.00723469  0.0151837   37  TYR   B CZ   
2661 O  OH   . TYR   B 37  ? 0.177242  0.265795 0.111273  -0.0222452  0.0211793   0.0262305   37  TYR   B OH   
2662 N  N    . CYS   B 38  ? 0.125694  0.200348 0.0506355 0.00057714  -0.00751059 -0.0077547  38  CYS   B N    
2663 C  CA   . CYS   B 38  ? 0.12377   0.197554 0.0569834 -0.00227567 -0.00474008 -0.00819179 38  CYS   B CA   
2664 C  C    . CYS   B 38  ? 0.126708  0.195146 0.0571363 0.00103433  -0.00495376 -0.00176203 38  CYS   B C    
2665 O  O    . CYS   B 38  ? 0.135685  0.20567  0.0585061 0.0013342   -0.00579016 0.00158999  38  CYS   B O    
2666 C  CB   . CYS   B 38  ? 0.143979  0.199064 0.0784106 0.00339324  -0.00041295 -0.00965493 38  CYS   B CB   
2667 S  SG   . CYS   B 38  ? 0.192585  0.210846 0.127598  -0.00950126 -0.0175536  -0.0166697  38  CYS   B SG   
2668 N  N    . PRO   B 39  ? 0.127324  0.190936 0.0477852 -0.00672966 -0.0065587  -0.00461821 39  PRO   B N    
2669 C  CA   . PRO   B 39  ? 0.126114  0.188818 0.0586923 -0.00949648 -0.00688387 -0.00668907 39  PRO   B CA   
2670 C  C    . PRO   B 39  ? 0.127758  0.18432  0.0630983 -0.00510493 -0.00672436 -0.0133159  39  PRO   B C    
2671 O  O    . PRO   B 39  ? 0.135561  0.195129 0.0768556 -0.00931509 -0.0132332  -0.0157672  39  PRO   B O    
2672 C  CB   . PRO   B 39  ? 0.128521  0.188938 0.0643388 -0.00885515 -0.00112078 -0.00775397 39  PRO   B CB   
2673 C  CG   . PRO   B 39  ? 0.137345  0.194473 0.0567827 -0.0140232  -0.00408028 -0.00782247 39  PRO   B CG   
2674 C  CD   . PRO   B 39  ? 0.138158  0.188845 0.0479438 -0.010752   -0.0104616  -0.0067947  39  PRO   B CD   
2675 N  N    . ARG   B 40  ? 0.12676   0.192094 0.0651685 -0.0103435  -0.014683   -0.0139503  40  ARG   B N    
2676 C  CA   . ARG   B 40  ? 0.134395  0.192302 0.0676258 -0.0112232  -0.0185298  -0.0142932  40  ARG   B CA   
2677 C  C    . ARG   B 40  ? 0.133045  0.197347 0.0760921 -0.0139625  -0.0153441  -0.0179983  40  ARG   B C    
2678 O  O    . ARG   B 40  ? 0.146595  0.196195 0.0951573 -0.0267733  -0.0142554  -0.0085951  40  ARG   B O    
2679 C  CB   . ARG   B 40  ? 0.133912  0.201249 0.0598734 -0.00461473 -0.0189384  -0.0123012  40  ARG   B CB   
2680 C  CG   . ARG   B 40  ? 0.135103  0.206264 0.068071  0.00055876  -0.0318302  -0.00759555 40  ARG   B CG   
2681 C  CD   . ARG   B 40  ? 0.125852  0.216896 0.064925  0.00427669  -0.0316336  -0.00998989 40  ARG   B CD   
2682 N  NE   . ARG   B 40  ? 0.130641  0.227542 0.0682263 0.00872297  -0.037769   -0.00839466 40  ARG   B NE   
2683 C  CZ   . ARG   B 40  ? 0.14329   0.24299  0.0708017 0.0192117   -0.0367239  -0.00463784 40  ARG   B CZ   
2684 N  NH1  . ARG   B 40  ? 0.15321   0.247145 0.0707672 0.021736    -0.0316927  -0.00850775 40  ARG   B NH1  
2685 N  NH2  . ARG   B 40  ? 0.147537  0.252333 0.0660635 0.0192373   -0.0390285  -0.0084388  40  ARG   B NH2  
2686 N  N    . HIS   B 41  ? 0.14302   0.19645  0.0684585 -0.023442   -0.0247416  -0.0265193  41  HIS   B N    
2687 C  CA   . HIS   B 41  ? 0.145087  0.200332 0.0747192 -0.0222671  -0.0163764  -0.0236201  41  HIS   B CA   
2688 C  C    . HIS   B 41  ? 0.151841  0.193887 0.087602  -0.0261602  -0.00969959 -0.0287788  41  HIS   B C    
2689 O  O    . HIS   B 41  ? 0.165513  0.2034   0.112071  -0.0312597  -0.00107898 -0.0123338  41  HIS   B O    
2690 C  CB   . HIS   B 41  ? 0.148437  0.208836 0.0845955 -0.0214418  -0.00754075 -0.0219335  41  HIS   B CB   
2691 C  CG   . HIS   B 41  ? 0.154542  0.218856 0.0831575 -0.0226499  -0.0058008  -0.0107857  41  HIS   B CG   
2692 N  ND1  . HIS   B 41  ? 0.163665  0.231688 0.0936883 -0.0227875  -0.0106346  -0.00906712 41  HIS   B ND1  
2693 C  CD2  . HIS   B 41  ? 0.163127  0.225307 0.0873217 -0.0279896  -0.00784066 -0.00639067 41  HIS   B CD2  
2694 C  CE1  . HIS   B 41  ? 0.174385  0.23243  0.0749157 -0.018766   -0.00553207 -0.00604387 41  HIS   B CE1  
2695 N  NE2  . HIS   B 41  ? 0.168941  0.232703 0.0854536 -0.0246134  -0.00377742 -0.00287955 41  HIS   B NE2  
2696 N  N    . VAL   B 42  ? 0.154124  0.188816 0.0826897 -0.0179223  -0.00898796 -0.0309125  42  VAL   B N    
2697 C  CA   . VAL   B 42  ? 0.163749  0.19639  0.0983898 -0.0176586  -0.00899102 -0.0266802  42  VAL   B CA   
2698 C  C    . VAL   B 42  ? 0.178489  0.203577 0.118742  -0.0226377  -0.00417281 -0.0389074  42  VAL   B C    
2699 O  O    . VAL   B 42  ? 0.214599  0.209728 0.127512  -0.026035   -0.0114811  -0.0330576  42  VAL   B O    
2700 C  CB   . VAL   B 42  ? 0.166304  0.20251  0.110425  -0.0162466  -0.0136649  -0.024813   42  VAL   B CB   
2701 C  CG1  . VAL   B 42  ? 0.17003   0.213096 0.114389  -0.0169087  -0.0100437  -0.0274302  42  VAL   B CG1  
2702 C  CG2  . VAL   B 42  ? 0.167709  0.198144 0.118145  -0.0143902  -0.0180368  -0.0257937  42  VAL   B CG2  
2703 N  N    . ILE   B 43  ? 0.175382  0.228405 0.119604  -0.0290592  -0.0163228  -0.050388   43  ILE   B N    
2704 C  CA   . ILE   B 43  ? 0.184388  0.244466 0.123507  -0.0297647  -0.0131226  -0.0589087  43  ILE   B CA   
2705 C  C    . ILE   B 43  ? 0.184792  0.261625 0.147349  -0.0381632  -0.0174429  -0.0566293  43  ILE   B C    
2706 O  O    . ILE   B 43  ? 0.186877  0.271925 0.178263  -0.0439657  -0.00813323 -0.0771592  43  ILE   B O    
2707 C  CB   . ILE   B 43  ? 0.207605  0.276823 0.118906  -0.0234489  -0.0106941  -0.0654587  43  ILE   B CB   
2708 C  CG1  . ILE   B 43  ? 0.226611  0.287591 0.119336  -0.015627   -0.0170825  -0.0693246  43  ILE   B CG1  
2709 C  CG2  . ILE   B 43  ? 0.210504  0.280692 0.124064  -0.0129759  -0.00294493 -0.0613839  43  ILE   B CG2  
2710 C  CD1  . ILE   B 43  ? 0.246243  0.303881 0.129504  -0.0180333  -0.0177251  -0.0630096  43  ILE   B CD1  
2711 N  N    . CYS   B 44  ? 0.1805    0.25889  0.149927  -0.0356395  -0.0181598  -0.0473237  44  CYS   B N    
2712 C  CA   . CYS   B 44  ? 0.184847  0.265348 0.167287  -0.0364209  -0.023798   -0.0353099  44  CYS   B CA   
2713 C  C    . CYS   B 44  ? 0.19577   0.277971 0.170195  -0.0374396  -0.0170612  -0.0323662  44  CYS   B C    
2714 O  O    . CYS   B 44  ? 0.211736  0.312619 0.16589   -0.0189539  -0.0123907  -0.0195931  44  CYS   B O    
2715 C  CB   . CYS   B 44  ? 0.202984  0.272827 0.162946  -0.0345828  -0.0226169  -0.0360899  44  CYS   B CB   
2716 S  SG   . CYS   B 44  ? 0.233329  0.287855 0.18182   -0.0258224  -0.0220295  -0.0235362  44  CYS   B SG   
2717 N  N    . THR   B 45  ? 0.215037  0.270619 0.181853  -0.0445331  -0.0195632  -0.0348359  45  THR   B N    
2718 C  CA   . THR   B 45  ? 0.218311  0.27053  0.20545   -0.0467791  -0.0259966  -0.0234206  45  THR   B CA   
2719 C  C    . THR   B 45  ? 0.206435  0.26585  0.200254  -0.0533614  -0.0159611  -0.0215222  45  THR   B C    
2720 O  O    . THR   B 45  ? 0.198966  0.262356 0.180525  -0.047843   -0.00039188 -0.0243048  45  THR   B O    
2721 C  CB   . THR   B 45  ? 0.229365  0.261483 0.23659   -0.041623   -0.0276568  -0.0321744  45  THR   B CB   
2722 O  OG1  . THR   B 45  ? 0.236497  0.263979 0.261286  -0.0299279  -0.0397421  -0.0449478  45  THR   B OG1  
2723 C  CG2  . THR   B 45  ? 0.234923  0.264923 0.250304  -0.0404282  -0.0212985  -0.0398637  45  THR   B CG2  
2724 N  N    . SER   B 46  ? 0.224931  0.288606 0.202131  -0.0490639  -0.0111605  -0.0228558  46  SER   B N    
2725 C  CA   . SER   B 46  ? 0.22429   0.312715 0.215704  -0.0485505  0.00584467  -0.0221628  46  SER   B CA   
2726 C  C    . SER   B 46  ? 0.220482  0.309229 0.202016  -0.0502598  0.0124525   -0.0228012  46  SER   B C    
2727 O  O    . SER   B 46  ? 0.216682  0.309451 0.213854  -0.0460516  0.019947    -0.015273   46  SER   B O    
2728 C  CB   . SER   B 46  ? 0.249537  0.348829 0.225426  -0.042938   0.0187892   -0.0106737  46  SER   B CB   
2729 O  OG   . SER   B 46  ? 0.311826  0.398235 0.256294  -0.0223162  0.0127232   -0.00595286 46  SER   B OG   
2730 N  N    . GLU   B 47  ? 0.214855  0.314956 0.226498  -0.0533508  0.00595092  -0.0354738  47  GLU   B N    
2731 C  CA   . GLU   B 47  ? 0.22018   0.320131 0.235972  -0.050476   -0.0111193  -0.0343183  47  GLU   B CA   
2732 C  C    . GLU   B 47  ? 0.205502  0.309982 0.221434  -0.0514974  -0.0201677  -0.0431762  47  GLU   B C    
2733 O  O    . GLU   B 47  ? 0.211747  0.324176 0.231683  -0.0384871  -0.0189829  -0.0446228  47  GLU   B O    
2734 C  CB   . GLU   B 47  ? 0.26176   0.342355 0.264578  -0.0632751  -0.0203373  -0.0394655  47  GLU   B CB   
2735 C  CG   . GLU   B 47  ? 0.279932  0.386483 0.299841  -0.062903   -0.0315941  -0.0286673  47  GLU   B CG   
2736 C  CD   . GLU   B 47  ? 0.317306  0.445151 0.353583  -0.0536864  -0.0247093  -0.0314485  47  GLU   B CD   
2737 O  OE1  . GLU   B 47  ? 0.360067  0.530873 0.440504  -0.0399393  -0.0565913  -0.0092007  47  GLU   B OE1  
2738 O  OE2  . GLU   B 47  ? 0.349423  0.457981 0.370505  -0.0639728  -0.0127888  -0.046613   47  GLU   B OE2  
2739 N  N    . ASP   B 48  ? 0.193065  0.301666 0.203981  -0.0551707  -0.0280523  -0.0371419  48  ASP   B N    
2740 C  CA   . ASP   B 48  ? 0.194107  0.301264 0.190138  -0.0558004  -0.0301333  -0.0388385  48  ASP   B CA   
2741 C  C    . ASP   B 48  ? 0.198383  0.288177 0.17013   -0.0439923  -0.0213166  -0.0276029  48  ASP   B C    
2742 O  O    . ASP   B 48  ? 0.198689  0.263846 0.179367  -0.0421986  -0.0240053  -0.0312818  48  ASP   B O    
2743 C  CB   . ASP   B 48  ? 0.202063  0.32489  0.199064  -0.0557672  -0.0263209  -0.050197   48  ASP   B CB   
2744 C  CG   . ASP   B 48  ? 0.219566  0.345878 0.209255  -0.0568165  -0.0288696  -0.0613796  48  ASP   B CG   
2745 O  OD1  . ASP   B 48  ? 0.225083  0.392951 0.205574  -0.0718613  -0.0219677  -0.0778314  48  ASP   B OD1  
2746 O  OD2  . ASP   B 48  ? 0.250367  0.355567 0.214843  -0.0501943  -0.0296479  -0.0719988  48  ASP   B OD2  
2747 N  N    . MET   B 49  ? 0.18723   0.284177 0.158673  -0.0497985  -0.0102905  -0.0116767  49  MET   B N    
2748 C  CA   . MET   B 49  ? 0.195466  0.272274 0.14436   -0.0481824  0.00686881  -0.00566341 49  MET   B CA   
2749 C  C    . MET   B 49  ? 0.197228  0.280698 0.154404  -0.0470594  0.0100802   -0.00251085 49  MET   B C    
2750 O  O    . MET   B 49  ? 0.198294  0.278807 0.148293  -0.041535   0.0195822   -0.0139448  49  MET   B O    
2751 C  CB   . MET   B 49  ? 0.189885  0.271025 0.137899  -0.0467696  0.00828293  -0.00870063 49  MET   B CB   
2752 C  CG   . MET   B 49  ? 0.181529  0.271573 0.143107  -0.0420219  0.00369329  -0.00891696 49  MET   B CG   
2753 S  SD   . MET   B 49  ? 0.179713  0.283816 0.156901  -0.0284019  0.00499631  -0.0141477  49  MET   B SD   
2754 C  CE   . MET   B 49  ? 0.175387  0.281872 0.161976  -0.0325746  -0.0164125  -0.0141549  49  MET   B CE   
2755 N  N    . LEU   B 50  ? 0.199261  0.304592 0.175515  -0.0414575  0.0093214   -0.00897585 50  LEU   B N    
2756 C  CA   . LEU   B 50  ? 0.199078  0.321092 0.191773  -0.0338409  0.01432     -0.0116361  50  LEU   B CA   
2757 C  C    . LEU   B 50  ? 0.180192  0.315664 0.190725  -0.0348852  0.00837126  -0.0133092  50  LEU   B C    
2758 O  O    . LEU   B 50  ? 0.196876  0.310254 0.198113  -0.0308051  0.0121646   -0.0096714  50  LEU   B O    
2759 C  CB   . LEU   B 50  ? 0.209226  0.334438 0.214998  -0.038759   0.0261595   -0.0105168  50  LEU   B CB   
2760 C  CG   . LEU   B 50  ? 0.219744  0.352162 0.242488  -0.0397185  0.0301107   -0.00104475 50  LEU   B CG   
2761 C  CD1  . LEU   B 50  ? 0.230646  0.357641 0.255374  -0.0430397  0.0286872   -0.00203249 50  LEU   B CD1  
2762 C  CD2  . LEU   B 50  ? 0.241226  0.364961 0.257478  -0.0470663  0.0308883   -0.00649399 50  LEU   B CD2  
2763 N  N    . ASN   B 51  ? 0.163977  0.325601 0.183298  -0.0251723  -0.00513504 -0.0160319  51  ASN   B N    
2764 C  CA   . ASN   B 51  ? 0.174691  0.341737 0.185898  -0.0322576  -0.00703094 -0.00641568 51  ASN   B CA   
2765 C  C    . ASN   B 51  ? 0.169632  0.332683 0.162469  -0.0405148  -0.0169004  -0.0168663  51  ASN   B C    
2766 O  O    . ASN   B 51  ? 0.192662  0.370387 0.175713  -0.0512314  -0.0300041  -0.0351309  51  ASN   B O    
2767 C  CB   . ASN   B 51  ? 0.177223  0.368768 0.217901  -0.0222272  -0.0111954  0.00943356  51  ASN   B CB   
2768 C  CG   . ASN   B 51  ? 0.220158  0.397817 0.25803   -0.0161027  -0.0118137  0.0345567   51  ASN   B CG   
2769 O  OD1  . ASN   B 51  ? 0.268371  0.405594 0.30934   -0.00032191 -0.0194442  0.0589344   51  ASN   B OD1  
2770 N  ND2  . ASN   B 51  ? 0.256792  0.437638 0.280837  -0.0249972  -0.0279037  0.0460263   51  ASN   B ND2  
2771 N  N    . PRO   B 52  ? 0.164738  0.307233 0.143711  -0.0366384  -0.0128612  -0.0238546  52  PRO   B N    
2772 C  CA   . PRO   B 52  ? 0.172516  0.307111 0.136669  -0.0431315  -0.0109417  -0.0219541  52  PRO   B CA   
2773 C  C    . PRO   B 52  ? 0.187406  0.303277 0.142408  -0.0372323  -0.0205213  -0.0203305  52  PRO   B C    
2774 O  O    . PRO   B 52  ? 0.20391   0.312146 0.1537    -0.0120167  -0.0238068  -0.0106161  52  PRO   B O    
2775 C  CB   . PRO   B 52  ? 0.173665  0.30504  0.13995   -0.0418525  -0.00672862 -0.0200034  52  PRO   B CB   
2776 C  CG   . PRO   B 52  ? 0.171093  0.300471 0.144261  -0.0429038  -0.00955363 -0.0267796  52  PRO   B CG   
2777 C  CD   . PRO   B 52  ? 0.178242  0.308654 0.154856  -0.0393798  -0.0109711  -0.0262715  52  PRO   B CD   
2778 N  N    . ASN   B 53  ? 0.189908  0.313616 0.133789  -0.0349905  -0.0329659  -0.0281531  53  ASN   B N    
2779 C  CA   . ASN   B 53  ? 0.194833  0.331556 0.133224  -0.0257443  -0.0338936  -0.0261212  53  ASN   B CA   
2780 C  C    . ASN   B 53  ? 0.192033  0.293442 0.121035  -0.0277645  -0.0228079  -0.0388509  53  ASN   B C    
2781 O  O    . ASN   B 53  ? 0.209108  0.290377 0.138297  -0.0315702  -0.025884   -0.0448666  53  ASN   B O    
2782 C  CB   . ASN   B 53  ? 0.203573  0.363787 0.16217   -0.0264564  -0.0512814  -0.0317793  53  ASN   B CB   
2783 C  CG   . ASN   B 53  ? 0.211181  0.408965 0.170343  -0.0227637  -0.063574   -0.0220019  53  ASN   B CG   
2784 O  OD1  . ASN   B 53  ? 0.223099  0.423912 0.184801  -0.00106597 -0.0510505  -0.0249975  53  ASN   B OD1  
2785 N  ND2  . ASN   B 53  ? 0.228776  0.443904 0.20664   -0.0191494  -0.083757   -0.0204361  53  ASN   B ND2  
2786 N  N    . TYR   B 54  ? 0.188371  0.287869 0.116424  -0.0227201  -0.0123507  -0.0351411  54  TYR   B N    
2787 C  CA   . TYR   B 54  ? 0.195028  0.294878 0.104766  -0.0139296  -0.0237828  -0.0327271  54  TYR   B CA   
2788 C  C    . TYR   B 54  ? 0.204018  0.304898 0.114693  -0.00292163 -0.027171   -0.0422478  54  TYR   B C    
2789 O  O    . TYR   B 54  ? 0.228043  0.288503 0.110117  -0.00980194 -0.0262788  -0.0398765  54  TYR   B O    
2790 C  CB   . TYR   B 54  ? 0.179433  0.289856 0.102195  -0.0174854  -0.0166059  -0.0256844  54  TYR   B CB   
2791 C  CG   . TYR   B 54  ? 0.186522  0.27731  0.100559  -0.0250177  -0.0190047  -0.0232079  54  TYR   B CG   
2792 C  CD1  . TYR   B 54  ? 0.178941  0.278469 0.0968618 -0.0259382  -0.0196039  -0.0246693  54  TYR   B CD1  
2793 C  CD2  . TYR   B 54  ? 0.173784  0.281817 0.0965079 -0.0265996  -0.0175315  -0.0206359  54  TYR   B CD2  
2794 C  CE1  . TYR   B 54  ? 0.184537  0.279198 0.0918557 -0.0230432  -0.017738   -0.0177422  54  TYR   B CE1  
2795 C  CE2  . TYR   B 54  ? 0.193271  0.278471 0.0992977 -0.0263244  -0.0133666  -0.0221517  54  TYR   B CE2  
2796 C  CZ   . TYR   B 54  ? 0.186253  0.283865 0.0891022 -0.0193298  -0.0135507  -0.0239311  54  TYR   B CZ   
2797 O  OH   . TYR   B 54  ? 0.173255  0.289974 0.0858769 -0.00704598 -0.0113896  -0.0215209  54  TYR   B OH   
2798 N  N    . GLU   B 55  ? 0.239374  0.322134 0.122599  -0.0003516  -0.0111506  -0.0395879  55  GLU   B N    
2799 C  CA   . GLU   B 55  ? 0.265582  0.34195  0.123514  0.0108446   -0.0186624  -0.0491377  55  GLU   B CA   
2800 C  C    . GLU   B 55  ? 0.269591  0.343899 0.141077  0.00869115  -0.0307419  -0.0596363  55  GLU   B C    
2801 O  O    . GLU   B 55  ? 0.302958  0.345151 0.126004  0.00900429  -0.0396691  -0.0614673  55  GLU   B O    
2802 C  CB   . GLU   B 55  ? 0.305866  0.367468 0.159669  0.0300447   -0.0334408  -0.0328005  55  GLU   B CB   
2803 C  CG   . GLU   B 55  ? 0.349178  0.382975 0.174582  0.0422245   -0.0259955  -0.0469638  55  GLU   B CG   
2804 C  CD   . GLU   B 55  ? 0.411354  0.431517 0.232155  0.0458616   -0.0247262  -0.0164079  55  GLU   B CD   
2805 O  OE1  . GLU   B 55  ? 0.435219  0.493158 0.295853  0.0514295   -0.0367886  -0.012204   55  GLU   B OE1  
2806 O  OE2  . GLU   B 55  ? 0.471856  0.527106 0.280255  0.0491456   -0.00435179 0.00216973  55  GLU   B OE2  
2807 N  N    . ASP   B 56  ? 0.2722    0.362498 0.152884  0.00439651  -0.0467247  -0.0607951  56  ASP   B N    
2808 C  CA   . ASP   B 56  ? 0.287514  0.363707 0.148205  -0.00248816 -0.0594266  -0.0716611  56  ASP   B CA   
2809 C  C    . ASP   B 56  ? 0.292251  0.333399 0.169578  -0.00861034 -0.062486   -0.0838804  56  ASP   B C    
2810 O  O    . ASP   B 56  ? 0.329518  0.341013 0.193305  -0.00051312 -0.0589536  -0.0882372  56  ASP   B O    
2811 C  CB   . ASP   B 56  ? 0.297205  0.419378 0.211601  -0.00679923 -0.0728595  -0.0629024  56  ASP   B CB   
2812 C  CG   . ASP   B 56  ? 0.365897  0.460783 0.27823   -0.0220787  -0.0595571  -0.079294   56  ASP   B CG   
2813 O  OD1  . ASP   B 56  ? 0.415792  0.572736 0.30211   -0.0211101  -0.101251   -0.108575   56  ASP   B OD1  
2814 O  OD2  . ASP   B 56  ? 0.398028  0.505897 0.3566    -0.0330991  -0.0125664  -0.0801429  56  ASP   B OD2  
2815 N  N    . LEU   B 57  ? 0.283628  0.300178 0.156861  -0.0023274  -0.059256   -0.0716673  57  LEU   B N    
2816 C  CA   . LEU   B 57  ? 0.295961  0.301534 0.163288  0.00819623  -0.0559372  -0.0640929  57  LEU   B CA   
2817 C  C    . LEU   B 57  ? 0.283027  0.307989 0.15736   0.0207765   -0.0600095  -0.0500947  57  LEU   B C    
2818 O  O    . LEU   B 57  ? 0.313251  0.323238 0.207655  0.0282622   -0.0500505  -0.0263019  57  LEU   B O    
2819 C  CB   . LEU   B 57  ? 0.305449  0.292591 0.158517  -0.0040978  -0.0569239  -0.0595029  57  LEU   B CB   
2820 C  CG   . LEU   B 57  ? 0.316408  0.296406 0.176771  -0.00581778 -0.0443789  -0.0528005  57  LEU   B CG   
2821 C  CD1  . LEU   B 57  ? 0.320404  0.299151 0.171415  -0.00263664 -0.047721   -0.0475782  57  LEU   B CD1  
2822 C  CD2  . LEU   B 57  ? 0.325999  0.305216 0.180398  -0.00851239 -0.0371934  -0.0546632  57  LEU   B CD2  
2823 N  N    . LEU   B 58  ? 0.277456  0.319319 0.128372  0.0358636   -0.0550114  -0.0323517  58  LEU   B N    
2824 C  CA   . LEU   B 58  ? 0.282012  0.331698 0.149223  0.032719    -0.0448717  -0.0424491  58  LEU   B CA   
2825 C  C    . LEU   B 58  ? 0.298336  0.343019 0.171198  0.0490816   -0.0293032  -0.0512657  58  LEU   B C    
2826 O  O    . LEU   B 58  ? 0.288817  0.31709  0.180131  0.0415776   -0.0359135  -0.0463907  58  LEU   B O    
2827 C  CB   . LEU   B 58  ? 0.269042  0.334771 0.15803   0.0247495   -0.0295865  -0.0518442  58  LEU   B CB   
2828 C  CG   . LEU   B 58  ? 0.267314  0.336434 0.156237  0.0130505   -0.0326028  -0.0540281  58  LEU   B CG   
2829 C  CD1  . LEU   B 58  ? 0.258708  0.337383 0.164478  0.00878261  -0.0349823  -0.0527325  58  LEU   B CD1  
2830 C  CD2  . LEU   B 58  ? 0.275328  0.333966 0.15851   0.00733082  -0.0181895  -0.0524092  58  LEU   B CD2  
2831 N  N    . ILE   B 59  ? 0.319867  0.367784 0.180042  0.0543313   -0.0370044  -0.0553323  59  ILE   B N    
2832 C  CA   . ILE   B 59  ? 0.346256  0.402904 0.19621   0.0494619   -0.0421526  -0.074968   59  ILE   B CA   
2833 C  C    . ILE   B 59  ? 0.317771  0.403235 0.209664  0.0296377   -0.0507577  -0.0916491  59  ILE   B C    
2834 O  O    . ILE   B 59  ? 0.333692  0.443342 0.230611  0.0461147   -0.0377732  -0.0917822  59  ILE   B O    
2835 C  CB   . ILE   B 59  ? 0.400112  0.456767 0.230428  0.0684806   -0.0457335  -0.0590712  59  ILE   B CB   
2836 C  CG1  . ILE   B 59  ? 0.454416  0.50369  0.29959   0.0543935   -0.0111707  -0.0532488  59  ILE   B CG1  
2837 C  CG2  . ILE   B 59  ? 0.418807  0.470383 0.264239  0.0767928   -0.0431337  -0.0667711  59  ILE   B CG2  
2838 C  CD1  . ILE   B 59  ? 0.454572  0.545421 0.341287  0.0460255   -0.00178012 -0.0561203  59  ILE   B CD1  
2839 N  N    . ARG   B 60  ? 0.282482  0.378413 0.242985  0.004171    -0.046946   -0.0901895  60  ARG   B N    
2840 C  CA   . ARG   B 60  ? 0.263432  0.380314 0.285664  -0.00016579 -0.0459671  -0.0708266  60  ARG   B CA   
2841 C  C    . ARG   B 60  ? 0.265282  0.355507 0.318336  -0.0137081  -0.0519159  -0.0597331  60  ARG   B C    
2842 O  O    . ARG   B 60  ? 0.288836  0.376656 0.406409  0.00501492  -0.0822497  -0.0293867  60  ARG   B O    
2843 C  CB   . ARG   B 60  ? 0.274423  0.406776 0.299193  0.00100879  -0.035424   -0.0537531  60  ARG   B CB   
2844 N  N    . LYS   B 61  ? 0.223892  0.354967 0.281684  -0.00705602 -0.041364   -0.0578365  61  LYS   B N    
2845 C  CA   . LYS   B 61  ? 0.231886  0.379517 0.26533   -0.0123788  -0.0362191  -0.0409536  61  LYS   B CA   
2846 C  C    . LYS   B 61  ? 0.248862  0.382184 0.261055  -0.0120407  -0.0256231  -0.0418525  61  LYS   B C    
2847 O  O    . LYS   B 61  ? 0.29219   0.396899 0.272331  -0.0128287  -0.0354995  -0.0247     61  LYS   B O    
2848 C  CB   . LYS   B 61  ? 0.231246  0.395189 0.262067  -0.0160792  -0.0315001  -0.0416372  61  LYS   B CB   
2849 C  CG   . LYS   B 61  ? 0.242877  0.434323 0.287697  -0.0133209  -0.0174701  -0.0310029  61  LYS   B CG   
2850 C  CD   . LYS   B 61  ? 0.247643  0.461564 0.297153  -0.0061433  -0.00895443 -0.0205656  61  LYS   B CD   
2851 C  CE   . LYS   B 61  ? 0.264836  0.485735 0.314563  0.00469036  0.00665692  -0.0163013  61  LYS   B CE   
2852 N  NZ   . LYS   B 61  ? 0.265232  0.500778 0.337896  0.0123882   0.0210491   -0.0156668  61  LYS   B NZ   
2853 N  N    . SER   B 62  ? 0.24358   0.391249 0.234445  -0.0085664  -0.0287804  -0.0556553  62  SER   B N    
2854 C  CA   . SER   B 62  ? 0.254726  0.390131 0.242357  -0.0121642  -0.0270019  -0.0684156  62  SER   B CA   
2855 C  C    . SER   B 62  ? 0.245575  0.352577 0.195299  -0.00344878 -0.00517329 -0.0766115  62  SER   B C    
2856 O  O    . SER   B 62  ? 0.242784  0.345608 0.194363  0.00832693  -0.0106115  -0.0759681  62  SER   B O    
2857 C  CB   . SER   B 62  ? 0.285484  0.393883 0.250301  -0.0223527  -0.0392268  -0.0840781  62  SER   B CB   
2858 O  OG   . SER   B 62  ? 0.344296  0.412819 0.309508  -0.0366515  -0.0332645  -0.0612473  62  SER   B OG   
2859 N  N    . ASN   B 63  ? 0.240317  0.34246  0.188162  -0.00986127 -0.00964925 -0.0641508  63  ASN   B N    
2860 C  CA   . ASN   B 63  ? 0.226091  0.30157  0.181757  -0.00842704 0.00600473  -0.0619939  63  ASN   B CA   
2861 C  C    . ASN   B 63  ? 0.228541  0.290314 0.182368  -0.0180236  0.00920809  -0.0657657  63  ASN   B C    
2862 O  O    . ASN   B 63  ? 0.246462  0.284211 0.178245  -0.0266408  0.00512861  -0.064907   63  ASN   B O    
2863 C  CB   . ASN   B 63  ? 0.233653  0.307648 0.169692  -0.00543437 0.016467    -0.0657205  63  ASN   B CB   
2864 C  CG   . ASN   B 63  ? 0.252244  0.303021 0.182757  -0.00139999 0.0193512   -0.0681036  63  ASN   B CG   
2865 O  OD1  . ASN   B 63  ? 0.272166  0.298178 0.180399  -0.00669204 0.0316476   -0.063193   63  ASN   B OD1  
2866 N  ND2  . ASN   B 63  ? 0.26837   0.333552 0.19213   -0.00909183 0.031211    -0.0731905  63  ASN   B ND2  
2867 N  N    . HIS   B 64  ? 0.237116  0.283433 0.204689  -0.00959636 0.0108747   -0.0653437  64  HIS   B N    
2868 C  CA   . HIS   B 64  ? 0.247739  0.305993 0.242086  -0.00421643 0.0239331   -0.0508627  64  HIS   B CA   
2869 C  C    . HIS   B 64  ? 0.248451  0.274822 0.231178  0.00091707  0.0222325   -0.052185   64  HIS   B C    
2870 O  O    . HIS   B 64  ? 0.241135  0.270947 0.256211  0.00640738  0.0100643   -0.0495026  64  HIS   B O    
2871 C  CB   . HIS   B 64  ? 0.272429  0.332985 0.275183  0.00758814  0.0356391   -0.0614704  64  HIS   B CB   
2872 C  CG   . HIS   B 64  ? 0.266828  0.406995 0.335513  0.0230435   0.0308432   -0.0473013  64  HIS   B CG   
2873 N  ND1  . HIS   B 64  ? 0.298187  0.478497 0.380802  0.0319562   0.0204667   -0.0460654  64  HIS   B ND1  
2874 C  CD2  . HIS   B 64  ? 0.302574  0.455086 0.354033  0.0302533   0.0385741   -0.041305   64  HIS   B CD2  
2875 C  CE1  . HIS   B 64  ? 0.280385  0.490447 0.387827  0.0329067   0.0145727   -0.0367188  64  HIS   B CE1  
2876 N  NE2  . HIS   B 64  ? 0.31067   0.508233 0.387216  0.0447164   0.0274773   -0.027582   64  HIS   B NE2  
2877 N  N    . ASN   B 65  ? 0.221482  0.286471 0.20418   -0.00854342 0.0233673   -0.0462182  65  ASN   B N    
2878 C  CA   . ASN   B 65  ? 0.245049  0.285178 0.204243  -0.0206429  0.0337377   -0.0486564  65  ASN   B CA   
2879 C  C    . ASN   B 65  ? 0.233444  0.282776 0.199287  -0.0306333  0.0380818   -0.0476218  65  ASN   B C    
2880 O  O    . ASN   B 65  ? 0.26228   0.329204 0.197723  -0.0328473  0.0460757   -0.0475711  65  ASN   B O    
2881 C  CB   . ASN   B 65  ? 0.246119  0.295002 0.2141    -0.0273546  0.0234977   -0.0478638  65  ASN   B CB   
2882 C  CG   . ASN   B 65  ? 0.283069  0.303433 0.243552  -0.0466351  0.0103287   -0.0439924  65  ASN   B CG   
2883 O  OD1  . ASN   B 65  ? 0.326587  0.358562 0.274447  -0.0417656  0.00491374  -0.0328219  65  ASN   B OD1  
2884 N  ND2  . ASN   B 65  ? 0.310819  0.321333 0.261482  -0.0521627  -0.0118638  -0.0211307  65  ASN   B ND2  
2885 N  N    . PHE   B 66  ? 0.229275  0.25221  0.168994  -0.0260708  0.0317106   -0.0509118  66  PHE   B N    
2886 C  CA   . PHE   B 66  ? 0.225341  0.263084 0.179639  -0.0220356  0.0267939   -0.0582988  66  PHE   B CA   
2887 C  C    . PHE   B 66  ? 0.242709  0.275328 0.187183  -0.00880526 0.0291848   -0.0588504  66  PHE   B C    
2888 O  O    . PHE   B 66  ? 0.265383  0.349177 0.194607  0.00875057  0.045963    -0.0394686  66  PHE   B O    
2889 C  CB   . PHE   B 66  ? 0.22622   0.252419 0.176923  -0.0126007  0.00537898  -0.0655822  66  PHE   B CB   
2890 C  CG   . PHE   B 66  ? 0.218636  0.258685 0.187767  -0.0146296  0.00313482  -0.063899   66  PHE   B CG   
2891 C  CD1  . PHE   B 66  ? 0.209673  0.240712 0.196638  -0.0183697  -0.00340159 -0.062344   66  PHE   B CD1  
2892 C  CD2  . PHE   B 66  ? 0.217089  0.253766 0.187912  -0.009275   -0.00096832 -0.0540009  66  PHE   B CD2  
2893 C  CE1  . PHE   B 66  ? 0.221075  0.255616 0.195498  -0.00910548 -0.00667642 -0.0580749  66  PHE   B CE1  
2894 C  CE2  . PHE   B 66  ? 0.216463  0.261017 0.198442  -0.0142539  -0.00678855 -0.0577612  66  PHE   B CE2  
2895 C  CZ   . PHE   B 66  ? 0.224054  0.259188 0.196894  -0.00857872 -0.00571303 -0.0544725  66  PHE   B CZ   
2896 N  N    . LEU   B 67  ? 0.243953  0.260818 0.174119  -0.00621936 0.0221935   -0.0800073  67  LEU   B N    
2897 C  CA   . LEU   B 67  ? 0.239844  0.270037 0.209612  -0.00715879 0.0182235   -0.0739006  67  LEU   B CA   
2898 C  C    . LEU   B 67  ? 0.233295  0.244864 0.197651  -0.00225613 0.0213879   -0.0665278  67  LEU   B C    
2899 O  O    . LEU   B 67  ? 0.252231  0.280512 0.21548   -0.016853   0.0229689   -0.106931   67  LEU   B O    
2900 C  CB   . LEU   B 67  ? 0.274884  0.286433 0.252585  -0.0151608  0.0188339   -0.0647206  67  LEU   B CB   
2901 C  CG   . LEU   B 67  ? 0.322028  0.31484  0.312443  -0.0352942  0.00903322  -0.0613532  67  LEU   B CG   
2902 C  CD1  . LEU   B 67  ? 0.315047  0.328408 0.342975  -0.0426301  0.0150294   -0.0516581  67  LEU   B CD1  
2903 C  CD2  . LEU   B 67  ? 0.349029  0.333116 0.336135  -0.0337665  0.012138    -0.0699557  67  LEU   B CD2  
2904 N  N    . VAL   B 68  ? 0.229879  0.239862 0.170257  0.00581889  0.0210434   -0.049025   68  VAL   B N    
2905 C  CA   . VAL   B 68  ? 0.230464  0.226095 0.154306  0.0131088   0.018282    -0.0388564  68  VAL   B CA   
2906 C  C    . VAL   B 68  ? 0.254952  0.221912 0.157705  0.0249147   0.0179037   -0.0281753  68  VAL   B C    
2907 O  O    . VAL   B 68  ? 0.250229  0.244838 0.155501  0.0370358   0.00919186  -0.0372367  68  VAL   B O    
2908 C  CB   . VAL   B 68  ? 0.224813  0.240865 0.160305  0.0170908   0.0112247   -0.0271125  68  VAL   B CB   
2909 C  CG1  . VAL   B 68  ? 0.220999  0.245195 0.169491  0.00737944  0.0130815   -0.023211   68  VAL   B CG1  
2910 C  CG2  . VAL   B 68  ? 0.226964  0.249149 0.159003  0.0230099   0.00602945  -0.0290059  68  VAL   B CG2  
2911 N  N    . GLN   B 69  ? 0.288035  0.222895 0.152978  0.0297693   0.0229249   -0.0147828  69  GLN   B N    
2912 C  CA   . GLN   B 69  ? 0.306243  0.246253 0.170467  0.0369897   0.0183814   -0.00300477 69  GLN   B CA   
2913 C  C    . GLN   B 69  ? 0.277262  0.244139 0.13045   0.0462622   0.0111776   0.00944949  69  GLN   B C    
2914 O  O    . GLN   B 69  ? 0.246421  0.247922 0.139324  0.0284152   0.00265302  -0.0150809  69  GLN   B O    
2915 C  CB   . GLN   B 69  ? 0.367371  0.270022 0.22052   0.0241241   0.0196911   0.0196619   69  GLN   B CB   
2916 C  CG   . GLN   B 69  ? 0.430198  0.325268 0.294853  0.0153285   0.0181891   0.0129772   69  GLN   B CG   
2917 C  CD   . GLN   B 69  ? 0.496209  0.368071 0.354582  0.0047984   0.0281993   0.0445816   69  GLN   B CD   
2918 O  OE1  . GLN   B 69  ? 0.575867  0.452956 0.414701  0.0152378   0.00319172  0.0281183   69  GLN   B OE1  
2919 N  NE2  . GLN   B 69  ? 0.536154  0.425748 0.410594  -0.0245938  0.0403114   0.0306249   69  GLN   B NE2  
2920 N  N    . ALA   B 70  ? 0.27556   0.267125 0.126328  0.0636129   0.0243872   0.0119875   70  ALA   B N    
2921 C  CA   . ALA   B 70  ? 0.270974  0.291914 0.15065   0.067251    0.02504     0.00738153  70  ALA   B CA   
2922 C  C    . ALA   B 70  ? 0.284138  0.308272 0.172138  0.0735167   0.0164351   0.0175565   70  ALA   B C    
2923 O  O    . ALA   B 70  ? 0.279418  0.311517 0.215189  0.0806307   0.00363016  0.00706581  70  ALA   B O    
2924 C  CB   . ALA   B 70  ? 0.281699  0.311307 0.171202  0.0583615   0.0246277   0.0150383   70  ALA   B CB   
2925 N  N    . GLY   B 71  ? 0.291477  0.3327   0.169293  0.0685218   0.0131371   0.0230646   71  GLY   B N    
2926 C  CA   . GLY   B 71  ? 0.326909  0.360303 0.199884  0.0761946   0.00189774  0.0433181   71  GLY   B CA   
2927 C  C    . GLY   B 71  ? 0.345177  0.372107 0.22279   0.0665619   0.00937625  0.0485066   71  GLY   B C    
2928 O  O    . GLY   B 71  ? 0.349156  0.399329 0.28092   0.0607567   -0.00566984 0.0697295   71  GLY   B O    
2929 N  N    . ASN   B 72  ? 0.35208   0.41553  0.233347  0.0787328   0.0395529   0.0499554   72  ASN   B N    
2930 C  CA   . ASN   B 72  ? 0.387802  0.423595 0.302254  0.0687563   0.0295114   0.0368261   72  ASN   B CA   
2931 C  C    . ASN   B 72  ? 0.372192  0.417793 0.327592  0.0784315   0.0428347   0.0241478   72  ASN   B C    
2932 O  O    . ASN   B 72  ? 0.42616   0.394853 0.39277   0.0451481   0.0454336   0.0323945   72  ASN   B O    
2933 C  CB   . ASN   B 72  ? 0.417524  0.46202  0.309941  0.0744532   0.0246368   0.0445633   72  ASN   B CB   
2934 C  CG   . ASN   B 72  ? 0.458005  0.513769 0.32561   0.0680307   0.0232238   0.0409799   72  ASN   B CG   
2935 O  OD1  . ASN   B 72  ? 0.513412  0.575082 0.355321  0.0568055   -0.0089441  0.0178622   72  ASN   B OD1  
2936 N  ND2  . ASN   B 72  ? 0.473831  0.537367 0.345132  0.0667407   0.0458403   0.0435361   72  ASN   B ND2  
2937 N  N    . VAL   B 73  ? 0.353395  0.436106 0.366092  0.0835419   0.0435042   0.0120432   73  VAL   B N    
2938 C  CA   . VAL   B 73  ? 0.325414  0.392529 0.341939  0.0943784   0.0418426   -0.00547172 73  VAL   B CA   
2939 C  C    . VAL   B 73  ? 0.312649  0.341036 0.275813  0.0799802   0.0543416   -0.0143632  73  VAL   B C    
2940 O  O    . VAL   B 73  ? 0.31775   0.316709 0.222259  0.0790393   0.0291908   -0.0123166  73  VAL   B O    
2941 C  CB   . VAL   B 73  ? 0.322357  0.430604 0.342951  0.0942994   0.0638184   -0.0173189  73  VAL   B CB   
2942 C  CG1  . VAL   B 73  ? 0.335652  0.442101 0.351021  0.0973296   0.0823809   -0.0306645  73  VAL   B CG1  
2943 C  CG2  . VAL   B 73  ? 0.344271  0.459576 0.350765  0.0979896   0.0565779   -0.023198   73  VAL   B CG2  
2944 N  N    . GLN   B 74  ? 0.32892   0.312659 0.29055   0.0665964   0.0772322   -0.0210833  74  GLN   B N    
2945 C  CA   . GLN   B 74  ? 0.315548  0.305681 0.26723   0.0565676   0.0750783   -0.0272763  74  GLN   B CA   
2946 C  C    . GLN   B 74  ? 0.292324  0.306153 0.276951  0.0429979   0.0763254   -0.0276869  74  GLN   B C    
2947 O  O    . GLN   B 74  ? 0.318623  0.353704 0.301463  0.0726078   0.0968888   -0.0127599  74  GLN   B O    
2948 C  CB   . GLN   B 74  ? 0.374656  0.312241 0.343608  0.0350987   0.0747532   -0.0245286  74  GLN   B CB   
2949 N  N    . LEU   B 75  ? 0.245641  0.298289 0.221892  0.0196032   0.0513358   -0.0348215  75  LEU   B N    
2950 C  CA   . LEU   B 75  ? 0.24194   0.319453 0.231076  -0.00418314 0.0491506   -0.0349807  75  LEU   B CA   
2951 C  C    . LEU   B 75  ? 0.276644  0.360389 0.225864  -0.0147829  0.0321532   -0.0219113  75  LEU   B C    
2952 O  O    . LEU   B 75  ? 0.294063  0.493774 0.27987   -0.0271564  0.0327036   -0.0126861  75  LEU   B O    
2953 C  CB   . LEU   B 75  ? 0.246285  0.323397 0.260547  -0.00641049 0.0521744   -0.0320756  75  LEU   B CB   
2954 C  CG   . LEU   B 75  ? 0.257444  0.328061 0.281937  -0.0117806  0.0390929   -0.0291234  75  LEU   B CG   
2955 C  CD1  . LEU   B 75  ? 0.260177  0.327135 0.294823  -0.0201127  0.0270589   -0.0348252  75  LEU   B CD1  
2956 C  CD2  . LEU   B 75  ? 0.266484  0.340843 0.301888  -0.00742252 0.0317395   -0.0257741  75  LEU   B CD2  
2957 N  N    . ARG   B 76  ? 0.281433  0.303237 0.210266  -0.00034306 0.02121     -0.0336532  76  ARG   B N    
2958 C  CA   . ARG   B 76  ? 0.309414  0.29247  0.245996  0.00274767  -0.0146814  -0.0336991  76  ARG   B CA   
2959 C  C    . ARG   B 76  ? 0.27776   0.267196 0.210356  0.00480524  -0.00460661 -0.0443772  76  ARG   B C    
2960 O  O    . ARG   B 76  ? 0.261142  0.258818 0.208039  0.0205281   -0.00267204 -0.0368805  76  ARG   B O    
2961 C  CB   . ARG   B 76  ? 0.359733  0.312339 0.293951  0.0196038   -0.0109246  -0.0456351  76  ARG   B CB   
2962 C  CG   . ARG   B 76  ? 0.405258  0.333973 0.339133  0.00325529  -0.0375006  -0.0560171  76  ARG   B CG   
2963 C  CD   . ARG   B 76  ? 0.450582  0.369807 0.410834  0.0174814   -0.0319055  -0.0623298  76  ARG   B CD   
2964 N  NE   . ARG   B 76  ? 0.483779  0.395898 0.460414  0.0186363   -0.052559   -0.0485767  76  ARG   B NE   
2965 C  CZ   . ARG   B 76  ? 0.508249  0.422049 0.489771  0.00753008  -0.0504218  -0.0498132  76  ARG   B CZ   
2966 N  NH1  . ARG   B 76  ? 0.48997   0.451189 0.512945  0.0282857   -0.0471215  -0.0311126  76  ARG   B NH1  
2967 N  NH2  . ARG   B 76  ? 0.534058  0.414286 0.50271   0.0108537   -0.0511535  -0.0632624  76  ARG   B NH2  
2968 N  N    . VAL   B 77  ? 0.262807  0.24843  0.1937    0.00458126  -0.00483185 -0.0442866  77  VAL   B N    
2969 C  CA   . VAL   B 77  ? 0.250425  0.254258 0.175639  0.00331597  0.00297647  -0.045929   77  VAL   B CA   
2970 C  C    . VAL   B 77  ? 0.242948  0.247898 0.180237  0.00601054  0.0130817   -0.0646352  77  VAL   B C    
2971 O  O    . VAL   B 77  ? 0.266963  0.249759 0.211518  -0.0117137  0.0115041   -0.0587513  77  VAL   B O    
2972 C  CB   . VAL   B 77  ? 0.250484  0.265758 0.17041   -0.00084344 0.00434432  -0.0425113  77  VAL   B CB   
2973 C  CG1  . VAL   B 77  ? 0.235881  0.269208 0.157477  -0.00141669 0.00024283  -0.0469815  77  VAL   B CG1  
2974 C  CG2  . VAL   B 77  ? 0.255951  0.285012 0.168967  0.00405722  0.00678456  -0.0340278  77  VAL   B CG2  
2975 N  N    . ILE   B 78  ? 0.218703  0.260886 0.147988  0.0026724   0.0158157   -0.0682188  78  ILE   B N    
2976 C  CA   . ILE   B 78  ? 0.233237  0.284123 0.149323  0.0083304   0.0210347   -0.0624432  78  ILE   B CA   
2977 C  C    . ILE   B 78  ? 0.230189  0.292751 0.136589  0.0121578   0.0101849   -0.0612396  78  ILE   B C    
2978 O  O    . ILE   B 78  ? 0.251655  0.327438 0.131566  0.0216339   0.0153319   -0.05075    78  ILE   B O    
2979 C  CB   . ILE   B 78  ? 0.232785  0.300012 0.165714  0.0139482   0.027788    -0.0569843  78  ILE   B CB   
2980 C  CG1  . ILE   B 78  ? 0.241654  0.318095 0.176566  0.00707527  0.0317937   -0.0504243  78  ILE   B CG1  
2981 C  CG2  . ILE   B 78  ? 0.240107  0.308612 0.193478  0.017741    0.0317624   -0.0501107  78  ILE   B CG2  
2982 C  CD1  . ILE   B 78  ? 0.245872  0.330778 0.195678  0.00369301  0.036013    -0.053632   78  ILE   B CD1  
2983 N  N    . GLY   B 79  ? 0.212515  0.288431 0.124641  0.0106965   -0.0032685  -0.0525807  79  GLY   B N    
2984 C  CA   . GLY   B 79  ? 0.22364   0.284436 0.11955   0.0082791   -0.0152512  -0.0568705  79  GLY   B CA   
2985 C  C    . GLY   B 79  ? 0.214029  0.273306 0.115594  0.0146611   -0.0249113  -0.0573671  79  GLY   B C    
2986 O  O    . GLY   B 79  ? 0.228506  0.248326 0.121272  0.00484151  -0.0394431  -0.0622502  79  GLY   B O    
2987 N  N    . HIS   B 80  ? 0.23128   0.293415 0.121251  0.0380224   -0.0338381  -0.0656944  80  HIS   B N    
2988 C  CA   . HIS   B 80  ? 0.251024  0.302142 0.133882  0.0432859   -0.0330464  -0.0778188  80  HIS   B CA   
2989 C  C    . HIS   B 80  ? 0.252714  0.309469 0.11883   0.0465254   -0.0396597  -0.0787112  80  HIS   B C    
2990 O  O    . HIS   B 80  ? 0.292066  0.338611 0.140189  0.036356    -0.0684102  -0.096117   80  HIS   B O    
2991 C  CB   . HIS   B 80  ? 0.239548  0.315189 0.15863   0.0500477   -0.0252848  -0.0796817  80  HIS   B CB   
2992 C  CG   . HIS   B 80  ? 0.239855  0.340487 0.208582  0.039387    -0.0385487  -0.0857874  80  HIS   B CG   
2993 N  ND1  . HIS   B 80  ? 0.267679  0.343019 0.228107  0.020956    -0.0566734  -0.0995069  80  HIS   B ND1  
2994 C  CD2  . HIS   B 80  ? 0.257849  0.361048 0.221506  0.0447893   -0.0601221  -0.0857075  80  HIS   B CD2  
2995 C  CE1  . HIS   B 80  ? 0.267178  0.351213 0.230414  0.0271713   -0.0660401  -0.0850436  80  HIS   B CE1  
2996 N  NE2  . HIS   B 80  ? 0.26365   0.360775 0.225789  0.0279554   -0.0519655  -0.0832412  80  HIS   B NE2  
2997 N  N    . SER   B 81  ? 0.231874  0.302587 0.0889834 0.0328903   -0.0333112  -0.0716677  81  SER   B N    
2998 C  CA   . SER   B 81  ? 0.223306  0.31713  0.0917597 0.0266586   -0.0228203  -0.0484243  81  SER   B CA   
2999 C  C    . SER   B 81  ? 0.201862  0.311282 0.0708776 0.0223923   -0.0343299  -0.0400565  81  SER   B C    
3000 O  O    . SER   B 81  ? 0.193014  0.336051 0.0759549 0.042012    -0.0416868  -0.042653   81  SER   B O    
3001 C  CB   . SER   B 81  ? 0.241893  0.343724 0.126326  0.028186    0.00048979  -0.0284707  81  SER   B CB   
3002 O  OG   . SER   B 81  ? 0.243967  0.370452 0.157009  0.0121725   0.0199992   -0.0175315  81  SER   B OG   
3003 N  N    . MET   B 82  ? 0.18806   0.314508 0.0763271 0.014041    -0.0344069  -0.0324547  82  MET   B N    
3004 C  CA   . MET   B 82  ? 0.185411  0.311601 0.0863882 0.00769051  -0.0171917  -0.0260353  82  MET   B CA   
3005 C  C    . MET   B 82  ? 0.171428  0.298887 0.0843623 0.0104498   -0.00869837 -0.0127312  82  MET   B C    
3006 O  O    . MET   B 82  ? 0.222271  0.304683 0.085993  0.010093    0.00511742  -0.00933689 82  MET   B O    
3007 C  CB   . MET   B 82  ? 0.185596  0.354528 0.121581  -0.00801952 -0.0177508  -0.0330786  82  MET   B CB   
3008 C  CG   . MET   B 82  ? 0.198207  0.40031  0.140876  -0.0293479  -0.0105209  -0.0475144  82  MET   B CG   
3009 S  SD   . MET   B 82  ? 0.20837   0.534434 0.158102  -0.0650587  0.0159943   -0.110008   82  MET   B SD   
3010 C  CE   . MET   B 82  ? 0.183774  0.496221 0.167581  -0.0583371  0.00065012  -0.109097   82  MET   B CE   
3011 N  N    . GLN   B 83  ? 0.152221  0.265146 0.0721122 0.0154146   0.00615467  0.00046813  83  GLN   B N    
3012 C  CA   . GLN   B 83  ? 0.151162  0.263047 0.0658608 0.0181919   0.0115119   0.00544414  83  GLN   B CA   
3013 C  C    . GLN   B 83  ? 0.147576  0.251002 0.0535354 0.0192714   0.0016645   0.00310554  83  GLN   B C    
3014 O  O    . GLN   B 83  ? 0.151443  0.254698 0.054251  0.0261757   -0.00381249 0.00596952  83  GLN   B O    
3015 C  CB   . GLN   B 83  ? 0.150103  0.268816 0.0760984 0.0160703   0.0286363   0.0143372   83  GLN   B CB   
3016 C  CG   . GLN   B 83  ? 0.167479  0.277423 0.0920291 0.0112987   0.0320083   0.0204636   83  GLN   B CG   
3017 C  CD   . GLN   B 83  ? 0.17635   0.284856 0.135937  0.00328594  0.0270129   0.0263905   83  GLN   B CD   
3018 O  OE1  . GLN   B 83  ? 0.19659   0.333982 0.188309  0.00593684  0.00639741  0.0363632   83  GLN   B OE1  
3019 N  NE2  . GLN   B 83  ? 0.188937  0.301235 0.160269  0.00338462  0.0312323   0.0444624   83  GLN   B NE2  
3020 N  N    . ASN   B 84  ? 0.146598  0.244749 0.0499231 0.0175903   -0.00267458 -0.00106186 84  ASN   B N    
3021 C  CA   . ASN   B 84  ? 0.132692  0.23191  0.0554    0.0168989   -0.00910582 0.00030585  84  ASN   B CA   
3022 C  C    . ASN   B 84  ? 0.136727  0.223704 0.0503656 0.00581035  -0.0177248  -0.0095773  84  ASN   B C    
3023 O  O    . ASN   B 84  ? 0.142093  0.227075 0.043276  0.00099389  -0.0140713  -0.0130946  84  ASN   B O    
3024 C  CB   . ASN   B 84  ? 0.140817  0.243907 0.0631149 0.0114415   -0.0122421  0.00169541  84  ASN   B CB   
3025 C  CG   . ASN   B 84  ? 0.156996  0.264271 0.0794447 0.00536996  -0.01892    0.0114434   84  ASN   B CG   
3026 O  OD1  . ASN   B 84  ? 0.16417   0.270508 0.0982826 0.00293303  -0.0351619  0.0173615   84  ASN   B OD1  
3027 N  ND2  . ASN   B 84  ? 0.160946  0.285554 0.0642736 -0.00163929 -0.00730411 0.0132922   84  ASN   B ND2  
3028 N  N    . CYS   B 85  ? 0.129618  0.218646 0.0495538 -0.00121184 -0.023837   -0.0103758  85  CYS   B N    
3029 C  CA   . CYS   B 85  ? 0.139271  0.226274 0.0528008 0.00504225  -0.0203261  -0.0111752  85  CYS   B CA   
3030 C  C    . CYS   B 85  ? 0.137156  0.220842 0.0584546 0.00579163  -0.0220207  -0.0117853  85  CYS   B C    
3031 O  O    . CYS   B 85  ? 0.132623  0.22269  0.057998  0.0124415   -0.0228025  -0.00472601 85  CYS   B O    
3032 C  CB   . CYS   B 85  ? 0.137278  0.227809 0.0666453 0.00925634  -0.0154825  -0.015881   85  CYS   B CB   
3033 S  SG   . CYS   B 85  ? 0.143339  0.257926 0.0790299 0.0179043   -0.0194068  -0.0133474  85  CYS   B SG   
3034 N  N    . VAL   B 86  ? 0.14325   0.229124 0.0739293 0.0165383   -0.018132   -0.00382212 86  VAL   B N    
3035 C  CA   . VAL   B 86  ? 0.151892  0.227417 0.0862811 0.0163891   -0.0188412  -0.0158492  86  VAL   B CA   
3036 C  C    . VAL   B 86  ? 0.14702   0.228405 0.0702871 0.0191354   -0.0129677  -0.0111076  86  VAL   B C    
3037 O  O    . VAL   B 86  ? 0.190111  0.233918 0.0742713 0.0315806   0.00079308  -0.00386616 86  VAL   B O    
3038 C  CB   . VAL   B 86  ? 0.163397  0.24169  0.104957  0.014066    -0.0274421  -0.0300225  86  VAL   B CB   
3039 C  CG1  . VAL   B 86  ? 0.178881  0.254157 0.157532  0.0146392   -0.0238833  -0.0262036  86  VAL   B CG1  
3040 C  CG2  . VAL   B 86  ? 0.168193  0.251163 0.0952226 0.0163257   -0.025462   -0.0296838  86  VAL   B CG2  
3041 N  N    . LEU   B 87  ? 0.142592  0.22567  0.0621575 0.00907926  -0.0101013  -0.0127465  87  LEU   B N    
3042 C  CA   . LEU   B 87  ? 0.160511  0.233837 0.0716129 0.00906131  -0.0129652  -0.0176561  87  LEU   B CA   
3043 C  C    . LEU   B 87  ? 0.163671  0.237321 0.0652139 0.0126434   -0.0160507  -0.0156075  87  LEU   B C    
3044 O  O    . LEU   B 87  ? 0.153764  0.235921 0.0727865 0.0224486   -0.0213096  -0.0225499  87  LEU   B O    
3045 C  CB   . LEU   B 87  ? 0.176533  0.244382 0.0991846 0.00113224  -0.0106354  -0.0178671  87  LEU   B CB   
3046 C  CG   . LEU   B 87  ? 0.19201   0.253836 0.1134    -0.00771349 -0.00562333 -0.023338   87  LEU   B CG   
3047 C  CD1  . LEU   B 87  ? 0.210773  0.27611  0.117767  -0.012448   -0.0094575  -0.0299117  87  LEU   B CD1  
3048 C  CD2  . LEU   B 87  ? 0.204631  0.259137 0.133022  -0.0102753  -0.00115771 -0.0191829  87  LEU   B CD2  
3049 N  N    . LYS   B 88  ? 0.175491  0.241491 0.0711814 0.0153748   -0.00653686 -0.0163891  88  LYS   B N    
3050 C  CA   . LYS   B 88  ? 0.174702  0.233923 0.0802065 0.0123464   -0.0123581  -0.0141094  88  LYS   B CA   
3051 C  C    . LYS   B 88  ? 0.180514  0.234822 0.0750046 0.00707498  -0.0157414  -0.029888   88  LYS   B C    
3052 O  O    . LYS   B 88  ? 0.212463  0.258194 0.0868633 0.0122677   -0.025575   -0.0454937  88  LYS   B O    
3053 C  CB   . LYS   B 88  ? 0.188204  0.246692 0.104516  0.01123     -0.00260953 -0.00579173 88  LYS   B CB   
3054 C  CG   . LYS   B 88  ? 0.220922  0.258453 0.135063  0.0147455   -0.00435321 -0.00728921 88  LYS   B CG   
3055 C  CD   . LYS   B 88  ? 0.28076   0.299171 0.204685  0.016438    0.00115356  0.0138819   88  LYS   B CD   
3056 C  CE   . LYS   B 88  ? 0.328603  0.361783 0.273876  0.0208441   -0.00175584 0.0274451   88  LYS   B CE   
3057 N  NZ   . LYS   B 88  ? 0.350095  0.376694 0.33574   0.0375822   -0.00477596 0.0497804   88  LYS   B NZ   
3058 N  N    . LEU   B 89  ? 0.172821  0.221235 0.0800352 0.0047377   -0.0170659  -0.0342617  89  LEU   B N    
3059 C  CA   . LEU   B 89  ? 0.175334  0.222791 0.0830405 -0.00167435 -0.0174135  -0.0376478  89  LEU   B CA   
3060 C  C    . LEU   B 89  ? 0.179248  0.23275  0.0909487 -0.0033775  -0.00698051 -0.0350706  89  LEU   B C    
3061 O  O    . LEU   B 89  ? 0.166634  0.245066 0.0884355 0.00323993  -0.00297262 -0.0292999  89  LEU   B O    
3062 C  CB   . LEU   B 89  ? 0.184048  0.235507 0.103988  -0.00193913 -0.0191664  -0.0259264  89  LEU   B CB   
3063 C  CG   . LEU   B 89  ? 0.188998  0.248077 0.112397  -0.00121287 -0.0138594  -0.0220509  89  LEU   B CG   
3064 C  CD1  . LEU   B 89  ? 0.213697  0.260891 0.129085  -0.00198979 -0.00976007 -0.0139844  89  LEU   B CD1  
3065 C  CD2  . LEU   B 89  ? 0.179752  0.257377 0.120943  -0.00260968 -0.0155031  -0.0203547  89  LEU   B CD2  
3066 N  N    . LYS   B 90  ? 0.195444  0.242054 0.092531  4.083e-05   -0.0108555  -0.0390479  90  LYS   B N    
3067 C  CA   . LYS   B 90  ? 0.200961  0.251042 0.0983166 -0.00742058 -0.00159126 -0.0368618  90  LYS   B CA   
3068 C  C    . LYS   B 90  ? 0.194835  0.243786 0.0970783 -0.00124459 0.00409006  -0.0355956  90  LYS   B C    
3069 O  O    . LYS   B 90  ? 0.193583  0.237313 0.117052  0.00304824  -0.00031502 -0.0417092  90  LYS   B O    
3070 C  CB   . LYS   B 90  ? 0.224164  0.281982 0.102704  -0.0136514  -0.00161844 -0.0310703  90  LYS   B CB   
3071 C  CG   . LYS   B 90  ? 0.248784  0.318926 0.148649  -0.0245529  0.00983892  -0.0338589  90  LYS   B CG   
3072 C  CD   . LYS   B 90  ? 0.299795  0.355615 0.206056  -0.035072   0.00230105  -0.0256527  90  LYS   B CD   
3073 C  CE   . LYS   B 90  ? 0.339957  0.395674 0.244092  -0.0383381  0.010688    0.0078824   90  LYS   B CE   
3074 N  NZ   . LYS   B 90  ? 0.37334   0.419656 0.265601  -0.0307872  -0.00432552 0.0163974   90  LYS   B NZ   
3075 N  N    . VAL   B 91  ? 0.20184   0.247368 0.132308  -0.00373174 -0.00172737 -0.0411989  91  VAL   B N    
3076 C  CA   . VAL   B 91  ? 0.209685  0.259048 0.127837  0.00832737  -0.00018615 -0.0449972  91  VAL   B CA   
3077 C  C    . VAL   B 91  ? 0.204384  0.2766   0.154827  0.0194511   -0.00774081 -0.0567733  91  VAL   B C    
3078 O  O    . VAL   B 91  ? 0.206223  0.284551 0.148678  0.0251366   -0.00556524 -0.0552681  91  VAL   B O    
3079 C  CB   . VAL   B 91  ? 0.216912  0.267297 0.128826  0.0120942   0.00651562  -0.0435342  91  VAL   B CB   
3080 C  CG1  . VAL   B 91  ? 0.222159  0.275146 0.13509   0.00552121  0.00832706  -0.0450779  91  VAL   B CG1  
3081 C  CG2  . VAL   B 91  ? 0.210231  0.272196 0.117071  0.0147276   0.00888032  -0.0454391  91  VAL   B CG2  
3082 N  N    . ASP   B 92  ? 0.232974  0.29588  0.185441  0.0284714   -0.00828301 -0.077287   92  ASP   B N    
3083 C  CA   . ASP   B 92  ? 0.230825  0.320852 0.206907  0.0372746   -0.00611149 -0.0880342  92  ASP   B CA   
3084 C  C    . ASP   B 92  ? 0.235396  0.342337 0.218401  0.0449711   -0.014009   -0.0883115  92  ASP   B C    
3085 O  O    . ASP   B 92  ? 0.22519   0.388971 0.247513  0.0452148   -0.0259393  -0.105231   92  ASP   B O    
3086 C  CB   . ASP   B 92  ? 0.267311  0.332551 0.271189  0.0289114   -0.00689169 -0.0918731  92  ASP   B CB   
3087 C  CG   . ASP   B 92  ? 0.312257  0.345995 0.320241  0.032648    -0.0078762  -0.0832019  92  ASP   B CG   
3088 O  OD1  . ASP   B 92  ? 0.377622  0.380112 0.341819  0.0386957   -0.038433   -0.0826865  92  ASP   B OD1  
3089 O  OD2  . ASP   B 92  ? 0.353623  0.361528 0.423686  0.0330372   0.00581048  -0.0941001  92  ASP   B OD2  
3090 N  N    . THR   B 93  ? 0.239038  0.33124  0.226375  0.0465714   -0.0265346  -0.0962713  93  THR   B N    
3091 C  CA   . THR   B 93  ? 0.245765  0.337552 0.242164  0.0434604   -0.0314471  -0.0823776  93  THR   B CA   
3092 C  C    . THR   B 93  ? 0.219231  0.33073  0.197551  0.047783    -0.0271334  -0.07339    93  THR   B C    
3093 O  O    . THR   B 93  ? 0.214554  0.349081 0.205279  0.0503182   -0.023552   -0.0607606  93  THR   B O    
3094 C  CB   . THR   B 93  ? 0.295038  0.349062 0.283743  0.0520089   -0.0603102  -0.0692948  93  THR   B CB   
3095 O  OG1  . THR   B 93  ? 0.34948   0.362509 0.32308   0.0542882   -0.0505014  -0.0821399  93  THR   B OG1  
3096 C  CG2  . THR   B 93  ? 0.305021  0.366483 0.310909  0.0578822   -0.0666207  -0.0629122  93  THR   B CG2  
3097 N  N    . ALA   B 94  ? 0.199837  0.32129  0.157535  0.0579211   -0.00957319 -0.06965    94  ALA   B N    
3098 C  CA   . ALA   B 94  ? 0.202287  0.318519 0.138089  0.0480936   -0.0121136  -0.0559167  94  ALA   B CA   
3099 C  C    . ALA   B 94  ? 0.188199  0.310807 0.127118  0.0552599   -0.00837701 -0.0552014  94  ALA   B C    
3100 O  O    . ALA   B 94  ? 0.206942  0.335823 0.139077  0.0736244   -0.0112698  -0.0598973  94  ALA   B O    
3101 C  CB   . ALA   B 94  ? 0.204992  0.334322 0.142557  0.0503135   -0.0029546  -0.0516796  94  ALA   B CB   
3102 N  N    . ASN   B 95  ? 0.156129  0.294777 0.106342  0.0516241   -0.0111536  -0.0387602  95  ASN   B N    
3103 C  CA   . ASN   B 95  ? 0.15761   0.287617 0.107768  0.0513158   -0.0193809  -0.0329595  95  ASN   B CA   
3104 C  C    . ASN   B 95  ? 0.159298  0.273394 0.109484  0.0465048   -0.00190748 -0.036333   95  ASN   B C    
3105 O  O    . ASN   B 95  ? 0.158184  0.270033 0.123684  0.0454429   -0.00088975 -0.0289546  95  ASN   B O    
3106 C  CB   . ASN   B 95  ? 0.152419  0.285101 0.0919384 0.0517228   -0.0215772  -0.0252063  95  ASN   B CB   
3107 C  CG   . ASN   B 95  ? 0.1616    0.285339 0.0946224 0.054302    -0.0156714  -0.0174533  95  ASN   B CG   
3108 O  OD1  . ASN   B 95  ? 0.165655  0.289172 0.105332  0.0656219   -0.0126294  -0.0185847  95  ASN   B OD1  
3109 N  ND2  . ASN   B 95  ? 0.151955  0.288117 0.093528  0.0581749   -0.0256592  -0.0188983  95  ASN   B ND2  
3110 N  N    . PRO   B 96  ? 0.167124  0.295899 0.13648   0.0497979   -0.00949301 -0.0325652  96  PRO   B N    
3111 C  CA   . PRO   B 96  ? 0.177508  0.305858 0.141855  0.0459348   -0.0151979  -0.0357084  96  PRO   B CA   
3112 C  C    . PRO   B 96  ? 0.18954   0.313207 0.133947  0.0395605   -0.0309916  -0.0320504  96  PRO   B C    
3113 O  O    . PRO   B 96  ? 0.208673  0.344547 0.163557  0.0223194   -0.0100966  -0.0402142  96  PRO   B O    
3114 C  CB   . PRO   B 96  ? 0.189407  0.310847 0.167342  0.054308    -0.0151406  -0.0354133  96  PRO   B CB   
3115 C  CG   . PRO   B 96  ? 0.193306  0.315535 0.182443  0.057877    -0.0165436  -0.0326969  96  PRO   B CG   
3116 C  CD   . PRO   B 96  ? 0.178459  0.306767 0.148026  0.0495486   -0.0141865  -0.038598   96  PRO   B CD   
3117 N  N    . LYS   B 97  ? 0.189173  0.304929 0.123882  0.0601874   -0.0338924  -0.0246095  97  LYS   B N    
3118 C  CA   . LYS   B 97  ? 0.216469  0.298031 0.125388  0.0607717   -0.0244913  -0.0218355  97  LYS   B CA   
3119 C  C    . LYS   B 97  ? 0.176103  0.297492 0.123298  0.0553543   -0.0295278  -0.0228777  97  LYS   B C    
3120 O  O    . LYS   B 97  ? 0.204657  0.295233 0.125377  0.0659319   -0.031786   -0.0172759  97  LYS   B O    
3121 C  CB   . LYS   B 97  ? 0.254221  0.323112 0.122011  0.0664278   -0.0177608  -0.0201551  97  LYS   B CB   
3122 C  CG   . LYS   B 97  ? 0.29314   0.340402 0.158306  0.0753461   -0.0192189  -0.0180421  97  LYS   B CG   
3123 C  CD   . LYS   B 97  ? 0.347564  0.378512 0.198294  0.0676091   -0.0164775  -0.00415976 97  LYS   B CD   
3124 C  CE   . LYS   B 97  ? 0.38235   0.40068  0.276337  0.0719232   -0.0242766  0.00326297  97  LYS   B CE   
3125 N  NZ   . LYS   B 97  ? 0.413995  0.453167 0.309683  0.0590251   -0.0134503  0.00362925  97  LYS   B NZ   
3126 N  N    . THR   B 98  ? 0.162932  0.272546 0.116148  0.0429735   -0.0185549  -0.0201604  98  THR   B N    
3127 C  CA   . THR   B 98  ? 0.147481  0.259599 0.109977  0.0289937   -0.00558124 -0.0210255  98  THR   B CA   
3128 C  C    . THR   B 98  ? 0.140533  0.264989 0.109033  0.0224258   -0.0134933  -0.0174809  98  THR   B C    
3129 O  O    . THR   B 98  ? 0.155861  0.269091 0.114436  0.00561177  0.00168185  -0.0282068  98  THR   B O    
3130 C  CB   . THR   B 98  ? 0.147365  0.26602  0.118653  0.0204086   -0.0185162  -0.0180891  98  THR   B CB   
3131 O  OG1  . THR   B 98  ? 0.135436  0.275213 0.128742  0.0142407   -0.0273917  -0.0194362  98  THR   B OG1  
3132 C  CG2  . THR   B 98  ? 0.146817  0.265447 0.121115  0.0176687   -0.0153778  -0.0158836  98  THR   B CG2  
3133 N  N    . PRO   B 99  ? 0.145664  0.254306 0.100049  0.0161485   -0.0166461  -0.00732036 99  PRO   B N    
3134 C  CA   . PRO   B 99  ? 0.152301  0.258876 0.110931  0.0125919   -0.0147185  -0.00863881 99  PRO   B CA   
3135 C  C    . PRO   B 99  ? 0.152605  0.257101 0.103936  0.00944043  -0.00966332 -0.00862872 99  PRO   B C    
3136 O  O    . PRO   B 99  ? 0.161206  0.269032 0.106652  0.00755312  -0.0215477  -0.00284406 99  PRO   B O    
3137 C  CB   . PRO   B 99  ? 0.162946  0.265555 0.10242   0.0118521   -0.0180468  -0.0111874  99  PRO   B CB   
3138 C  CG   . PRO   B 99  ? 0.15697   0.263707 0.103411  0.0133459   -0.00801377 -0.0037582  99  PRO   B CG   
3139 C  CD   . PRO   B 99  ? 0.146324  0.256554 0.114469  0.0135654   -0.0170006  -0.0045464  99  PRO   B CD   
3140 N  N    A LYS   B 100 ? 0.148458  0.265138 0.11419   0.00721546  -0.00981892 -0.00720314 100 LYS   B N    
3141 N  N    B LYS   B 100 ? 0.148998  0.268089 0.113761  0.00832494  -0.00798896 -0.00689001 100 LYS   B N    
3142 C  CA   A LYS   B 100 ? 0.159214  0.263516 0.119765  0.00730318  -0.00213667 -0.00691214 100 LYS   B CA   
3143 C  CA   B LYS   B 100 ? 0.160222  0.270039 0.117948  0.0109051   0.00071057  -0.00588175 100 LYS   B CA   
3144 C  C    A LYS   B 100 ? 0.155838  0.257756 0.096658  0.00906032  -0.00232515 -0.00626244 100 LYS   B C    
3145 C  C    B LYS   B 100 ? 0.155364  0.26198  0.0952562 0.0106535   -0.00080508 -0.00537418 100 LYS   B C    
3146 O  O    A LYS   B 100 ? 0.165486  0.270523 0.0913718 0.012982    -0.00060368 -0.00629766 100 LYS   B O    
3147 O  O    B LYS   B 100 ? 0.161399  0.275903 0.0891336 0.0135254   0.00291294  -0.00125341 100 LYS   B O    
3148 C  CB   A LYS   B 100 ? 0.175581  0.275233 0.15094   -0.00304304 -0.00763113 -0.00480982 100 LYS   B CB   
3149 C  CB   B LYS   B 100 ? 0.179511  0.284884 0.149348  0.00194074  -0.00338808 -0.00302571 100 LYS   B CB   
3150 C  CG   A LYS   B 100 ? 0.194481  0.282413 0.179229  -0.00815338 -0.0106061  -9.044e-05  100 LYS   B CG   
3151 C  CG   B LYS   B 100 ? 0.18971   0.304394 0.179316  0.00296478  0.00041443  -0.00267317 100 LYS   B CG   
3152 C  CD   A LYS   B 100 ? 0.215393  0.299135 0.21281   -0.0175757  -0.0123789  -0.00085731 100 LYS   B CD   
3153 C  CD   B LYS   B 100 ? 0.210016  0.327352 0.226088  -0.00476855 -0.00153377 -0.00142008 100 LYS   B CD   
3154 C  CE   A LYS   B 100 ? 0.242116  0.309984 0.241327  -0.0192683  -0.0115855  0.00218604  100 LYS   B CE   
3155 C  CE   B LYS   B 100 ? 0.215647  0.348228 0.26807   -0.00456675 0.00060317  0.00215643  100 LYS   B CE   
3156 N  NZ   A LYS   B 100 ? 0.267171  0.322888 0.272047  -0.0241228  -0.00867402 -0.00728626 100 LYS   B NZ   
3157 N  NZ   B LYS   B 100 ? 0.231002  0.36752  0.305129  -0.0107099  -0.00783342 0.00570949  100 LYS   B NZ   
3158 N  N    . TYR   B 101 ? 0.148085  0.24383  0.0878289 0.00850288  0.00373227  -0.00752721 101 TYR   B N    
3159 C  CA   . TYR   B 101 ? 0.148506  0.237226 0.0900089 0.00815326  -0.00292048 -0.00205064 101 TYR   B CA   
3160 C  C    . TYR   B 101 ? 0.149178  0.243589 0.097465  0.00627993  -0.00239476 0.00995683  101 TYR   B C    
3161 O  O    . TYR   B 101 ? 0.163907  0.267554 0.097341  0.00865224  -0.00206401 0.0110436   101 TYR   B O    
3162 C  CB   . TYR   B 101 ? 0.161168  0.22769  0.0821546 0.00905653  -0.00050103 0.00489743  101 TYR   B CB   
3163 C  CG   . TYR   B 101 ? 0.16558   0.23085  0.0773771 0.00665195  -0.0110925  0.0104047   101 TYR   B CG   
3164 C  CD1  . TYR   B 101 ? 0.174499  0.230978 0.0802838 0.00789365  -0.0160043  0.00454055  101 TYR   B CD1  
3165 C  CD2  . TYR   B 101 ? 0.158248  0.238291 0.085121  0.00240044  -0.00558773 0.00679137  101 TYR   B CD2  
3166 C  CE1  . TYR   B 101 ? 0.180368  0.237522 0.0849472 -0.00028602 -0.00888108 -0.00109686 101 TYR   B CE1  
3167 C  CE2  . TYR   B 101 ? 0.175419  0.23888  0.089423  -0.001486   -0.0154471  0.00946442  101 TYR   B CE2  
3168 C  CZ   . TYR   B 101 ? 0.184879  0.23481  0.0783082 -0.00740954 -0.0151313  0.00677898  101 TYR   B CZ   
3169 O  OH   . TYR   B 101 ? 0.209722  0.241126 0.076401  -0.0244827  -0.0271389  0.0168069   101 TYR   B OH   
3170 N  N    . LYS   B 102 ? 0.155863  0.248669 0.108694  0.0116297   -0.00813836 0.017447    102 LYS   B N    
3171 C  CA   . LYS   B 102 ? 0.151925  0.247424 0.14245   0.010746    -0.0109468  0.0262613   102 LYS   B CA   
3172 C  C    . LYS   B 102 ? 0.148514  0.234904 0.106334  0.0115262   -0.00771924 0.0239351   102 LYS   B C    
3173 O  O    . LYS   B 102 ? 0.144008  0.235528 0.0981904 0.00573133  -0.0156477  0.0210415   102 LYS   B O    
3174 C  CB   . LYS   B 102 ? 0.199477  0.260966 0.205805  0.00130814  -0.0107143  0.0483661   102 LYS   B CB   
3175 C  CG   . LYS   B 102 ? 0.247317  0.301223 0.246634  -0.0208064  0.00402487  0.0444347   102 LYS   B CG   
3176 C  CD   . LYS   B 102 ? 0.321885  0.32325  0.295118  -0.0351589  0.00753178  0.0302571   102 LYS   B CD   
3177 C  CE   . LYS   B 102 ? 0.368902  0.373759 0.35611   -0.054491   0.0225406   0.0284326   102 LYS   B CE   
3178 N  NZ   . LYS   B 102 ? 0.426842  0.4106   0.396889  -0.0539245  0.0217792   0.00368501  102 LYS   B NZ   
3179 N  N    . PHE   B 103 ? 0.136772  0.226389 0.0912275 0.0133041   0.00095562  0.0210146   103 PHE   B N    
3180 C  CA   . PHE   B 103 ? 0.137197  0.216916 0.0902426 0.0037543   0.0037232   0.0144508   103 PHE   B CA   
3181 C  C    . PHE   B 103 ? 0.150979  0.219133 0.10619   0.00043043  0.0076571   0.0189367   103 PHE   B C    
3182 O  O    . PHE   B 103 ? 0.18037   0.231293 0.120876  0.0082039   0.0174805   0.0331114   103 PHE   B O    
3183 C  CB   . PHE   B 103 ? 0.130923  0.222676 0.0903492 0.0028215   0.00275111  0.0118737   103 PHE   B CB   
3184 C  CG   . PHE   B 103 ? 0.132843  0.228047 0.0910119 0.00544572  0.00669624  0.00681616  103 PHE   B CG   
3185 C  CD1  . PHE   B 103 ? 0.144859  0.23288  0.0947019 0.0100362   0.00484293  0.00405588  103 PHE   B CD1  
3186 C  CD2  . PHE   B 103 ? 0.170389  0.234778 0.101707  0.00753403  0.00179425  0.00211842  103 PHE   B CD2  
3187 C  CE1  . PHE   B 103 ? 0.139476  0.23261  0.10199   0.0129347   0.0111217   0.00233564  103 PHE   B CE1  
3188 C  CE2  . PHE   B 103 ? 0.165978  0.24051  0.108233  0.0146166   0.00452028  0.00013701  103 PHE   B CE2  
3189 C  CZ   . PHE   B 103 ? 0.156704  0.238778 0.107162  0.0144404   0.00319559  0.00061367  103 PHE   B CZ   
3190 N  N    A VAL   B 104 ? 0.14831   0.215662 0.105337  -0.00046023 0.00789617  0.0162083   104 VAL   B N    
3191 N  N    B VAL   B 104 ? 0.142124  0.220276 0.101037  -0.00550937 0.00445147  0.0140557   104 VAL   B N    
3192 C  CA   A VAL   B 104 ? 0.159281  0.215819 0.113742  0.00320431  0.00970444  0.0123319   104 VAL   B CA   
3193 C  CA   B VAL   B 104 ? 0.148183  0.221684 0.105824  -0.00523693 0.00404487  0.00881364  104 VAL   B CA   
3194 C  C    A VAL   B 104 ? 0.165147  0.210271 0.100759  0.00098641  0.0172152   0.0140005   104 VAL   B C    
3195 C  C    B VAL   B 104 ? 0.152104  0.216311 0.0987659 -0.00703919 0.00845338  0.00803163  104 VAL   B C    
3196 O  O    A VAL   B 104 ? 0.186416  0.197345 0.0981481 0.0148591   0.020825    0.0185164   104 VAL   B O    
3197 O  O    B VAL   B 104 ? 0.146932  0.214718 0.108508  -0.0140563  -0.010046   0.00845527  104 VAL   B O    
3198 C  CB   A VAL   B 104 ? 0.170169  0.226502 0.148472  0.00358394  0.00081256  0.00611641  104 VAL   B CB   
3199 C  CB   B VAL   B 104 ? 0.157371  0.232912 0.127228  -0.00700106 0.00010159  0.00301831  104 VAL   B CB   
3200 C  CG1  A VAL   B 104 ? 0.181536  0.230685 0.167264  0.00375881  -0.00455818 0.00113215  104 VAL   B CG1  
3201 C  CG1  B VAL   B 104 ? 0.162576  0.239626 0.133779  -0.00895917 0.00332752  0.00312267  104 VAL   B CG1  
3202 C  CG2  A VAL   B 104 ? 0.176025  0.234942 0.154095  0.00394596  0.00484805  0.00667517  104 VAL   B CG2  
3203 C  CG2  B VAL   B 104 ? 0.154089  0.240219 0.121304  -0.00712564 -0.00475349 -1.103e-05  104 VAL   B CG2  
3204 N  N    . ARG   B 105 ? 0.150259  0.213379 0.0938546 -0.00426689 0.0141057   0.00887815  105 ARG   B N    
3205 C  CA   . ARG   B 105 ? 0.154272  0.213424 0.106765  -0.00564339 0.0178266   0.00676658  105 ARG   B CA   
3206 C  C    . ARG   B 105 ? 0.16892   0.205435 0.121939  -0.0177312  0.0319399   0.00115644  105 ARG   B C    
3207 O  O    . ARG   B 105 ? 0.218474  0.209229 0.143416  -0.0279469  0.0477218   -0.00767317 105 ARG   B O    
3208 C  CB   . ARG   B 105 ? 0.151929  0.227843 0.119172  -0.00169889 0.0133441   0.00697548  105 ARG   B CB   
3209 C  CG   . ARG   B 105 ? 0.154067  0.226668 0.122788  0.00305922  0.0195562   0.0116003   105 ARG   B CG   
3210 C  CD   . ARG   B 105 ? 0.15673   0.225735 0.141902  0.00416508  0.00927239  0.0184438   105 ARG   B CD   
3211 N  NE   . ARG   B 105 ? 0.152336  0.229013 0.158731  0.00563109  -0.00100654 0.0117676   105 ARG   B NE   
3212 C  CZ   . ARG   B 105 ? 0.151225  0.224169 0.132179  0.00466486  -0.00322443 0.0112331   105 ARG   B CZ   
3213 N  NH1  . ARG   B 105 ? 0.132301  0.231685 0.118359  0.00787084  -0.0112145  0.00501475  105 ARG   B NH1  
3214 N  NH2  . ARG   B 105 ? 0.154437  0.221313 0.153764  0.00415846  0.00353481  0.0110144   105 ARG   B NH2  
3215 N  N    . ILE   B 106 ? 0.180795  0.208957 0.11486   -0.0235527  0.0217454   0.00022445  106 ILE   B N    
3216 C  CA   . ILE   B 106 ? 0.204413  0.218408 0.125522  -0.0179933  0.0168414   -0.0020713  106 ILE   B CA   
3217 C  C    . ILE   B 106 ? 0.222735  0.230397 0.139555  -0.00971243 0.0112712   -0.00602024 106 ILE   B C    
3218 O  O    . ILE   B 106 ? 0.216858  0.228808 0.137105  -0.0192534  0.0177669   -0.00806927 106 ILE   B O    
3219 C  CB   . ILE   B 106 ? 0.22312   0.232999 0.133567  -0.00997174 0.00571896  0.00124153  106 ILE   B CB   
3220 C  CG1  . ILE   B 106 ? 0.231442  0.245318 0.128601  -0.00813715 0.00436321  0.00798034  106 ILE   B CG1  
3221 C  CG2  . ILE   B 106 ? 0.226797  0.234093 0.151236  -0.00588637 0.00199143  0.00282884  106 ILE   B CG2  
3222 C  CD1  . ILE   B 106 ? 0.247396  0.257452 0.135972  -0.0015749  0.00747197  0.0198537   106 ILE   B CD1  
3223 N  N    . GLN   B 107 ? 0.24108   0.24213  0.119866  -0.00431696 -0.00722155 -0.0128076  107 GLN   B N    
3224 C  CA   . GLN   B 107 ? 0.25144   0.272174 0.134556  0.0105697   -0.0119513  -0.0065664  107 GLN   B CA   
3225 C  C    . GLN   B 107 ? 0.210276  0.248039 0.132956  0.00925251  -0.0298178  0.00440147  107 GLN   B C    
3226 O  O    . GLN   B 107 ? 0.192049  0.218422 0.133508  0.0145536   -0.0310459  0.0100223   107 GLN   B O    
3227 C  CB   . GLN   B 107 ? 0.307331  0.298051 0.176833  0.0146799   0.0225653   -0.00690026 107 GLN   B CB   
3228 C  CG   . GLN   B 107 ? 0.369617  0.34981  0.201397  0.0120391   0.032223    0.007659    107 GLN   B CG   
3229 C  CD   . GLN   B 107 ? 0.435112  0.380581 0.302143  0.0134266   0.0480148   0.0225059   107 GLN   B CD   
3230 O  OE1  . GLN   B 107 ? 0.474479  0.42968  0.412112  0.0415554   0.0426049   0.0302387   107 GLN   B OE1  
3231 N  NE2  . GLN   B 107 ? 0.457062  0.44242  0.400485  0.00566179  0.05118     0.0267415   107 GLN   B NE2  
3232 N  N    . PRO   B 108 ? 0.20395   0.274429 0.143493  0.0194592   -0.0481282  0.0162308   108 PRO   B N    
3233 C  CA   . PRO   B 108 ? 0.200447  0.272788 0.158284  0.0150756   -0.0284778  0.0138348   108 PRO   B CA   
3234 C  C    . PRO   B 108 ? 0.190731  0.234055 0.139086  0.0211701   -0.011434   0.0034439   108 PRO   B C    
3235 O  O    . PRO   B 108 ? 0.213295  0.2408   0.161194  0.0160195   -0.0131848  0.0178016   108 PRO   B O    
3236 C  CB   . PRO   B 108 ? 0.199401  0.301285 0.186512  0.0160721   -0.0334093  0.0257743   108 PRO   B CB   
3237 C  CG   . PRO   B 108 ? 0.219429  0.324799 0.19437   0.021859    -0.0393575  0.0145372   108 PRO   B CG   
3238 C  CD   . PRO   B 108 ? 0.197977  0.311447 0.167327  0.0149798   -0.0569371  0.0198674   108 PRO   B CD   
3239 N  N    . GLY   B 109 ? 0.179371  0.23019  0.121328  0.0141084   6.079e-05   -0.00347865 109 GLY   B N    
3240 C  CA   . GLY   B 109 ? 0.18819   0.236744 0.123065  0.0148856   -0.00575142 -0.0174586  109 GLY   B CA   
3241 C  C    . GLY   B 109 ? 0.185372  0.240918 0.107748  0.0180291   -0.00449378 -0.0258641  109 GLY   B C    
3242 O  O    . GLY   B 109 ? 0.203293  0.293704 0.119346  0.0113421   -0.0159924  -0.0534384  109 GLY   B O    
3243 N  N    . GLN   B 110 ? 0.175669  0.221807 0.0848871 0.0245455   -0.0101318  -0.0111821  110 GLN   B N    
3244 C  CA   . GLN   B 110 ? 0.172935  0.220365 0.107421  0.0250295   -0.0184886  -0.00462985 110 GLN   B CA   
3245 C  C    . GLN   B 110 ? 0.166834  0.210883 0.1082    0.0165772   -0.0203969  -0.00812394 110 GLN   B C    
3246 O  O    . GLN   B 110 ? 0.168847  0.222956 0.104779  0.0156581   -0.0264199  0.0125912   110 GLN   B O    
3247 C  CB   . GLN   B 110 ? 0.193004  0.23045  0.117475  0.0313007   -0.00624359 -0.00191702 110 GLN   B CB   
3248 C  CG   . GLN   B 110 ? 0.235822  0.258646 0.171637  0.0232208   -0.00193501 0.0188159   110 GLN   B CG   
3249 N  N    . THR   B 111 ? 0.16779   0.201628 0.120706  0.0144938   -0.0197703  -0.00363785 111 THR   B N    
3250 C  CA   . THR   B 111 ? 0.170394  0.195847 0.115353  0.0100741   -0.0169996  -0.00192228 111 THR   B CA   
3251 C  C    . THR   B 111 ? 0.165586  0.191721 0.120532  0.0165634   -0.0145114  0.0129302   111 THR   B C    
3252 O  O    . THR   B 111 ? 0.185141  0.198393 0.134351  0.0283802   0.00863835  0.0251738   111 THR   B O    
3253 C  CB   . THR   B 111 ? 0.179913  0.208929 0.116657  0.0115286   -0.0174087  -0.00179461 111 THR   B CB   
3254 O  OG1  . THR   B 111 ? 0.176463  0.219034 0.126567  0.011236    -0.0075732  -0.008147   111 THR   B OG1  
3255 C  CG2  . THR   B 111 ? 0.182413  0.221291 0.122381  0.0123889   -0.010968   -0.00246224 111 THR   B CG2  
3256 N  N    . PHE   B 112 ? 0.147225  0.184817 0.107256  0.0135845   -0.0130826  0.0135822   112 PHE   B N    
3257 C  CA   . PHE   B 112 ? 0.14442   0.175774 0.101973  0.0102104   -0.0200022  0.0106747   112 PHE   B CA   
3258 C  C    . PHE   B 112 ? 0.128546  0.176507 0.0864134 0.00677312  -0.0134895  0.0107508   112 PHE   B C    
3259 O  O    . PHE   B 112 ? 0.116279  0.191535 0.0916558 0.0126922   -0.0190652  0.0189796   112 PHE   B O    
3260 C  CB   . PHE   B 112 ? 0.146974  0.182741 0.0932356 0.0131651   -0.0142314  0.0145482   112 PHE   B CB   
3261 C  CG   . PHE   B 112 ? 0.14368   0.193465 0.0853478 0.0183602   -0.0200165  0.0127959   112 PHE   B CG   
3262 C  CD1  . PHE   B 112 ? 0.146462  0.201268 0.119309  0.0202264   -0.0130186  0.0141663   112 PHE   B CD1  
3263 C  CD2  . PHE   B 112 ? 0.139756  0.196723 0.0839189 0.023868    -0.0144991  0.0110985   112 PHE   B CD2  
3264 C  CE1  . PHE   B 112 ? 0.143901  0.203513 0.133292  0.0187654   -0.0263545  0.0195801   112 PHE   B CE1  
3265 C  CE2  . PHE   B 112 ? 0.153275  0.201927 0.110977  0.0143057   -0.0156845  0.0150459   112 PHE   B CE2  
3266 C  CZ   . PHE   B 112 ? 0.143193  0.207909 0.129742  0.0155349   -0.0221401  0.0250362   112 PHE   B CZ   
3267 N  N    . SER   B 113 ? 0.133187  0.171269 0.0847785 0.00419938  -0.017667   0.00488549  113 SER   B N    
3268 C  CA   . SER   B 113 ? 0.140596  0.173471 0.0829324 0.00115131  -0.0123726  0.0016619   113 SER   B CA   
3269 C  C    . SER   B 113 ? 0.142422  0.176378 0.0602856 0.00199967  -0.0115185  0.0035131   113 SER   B C    
3270 O  O    . SER   B 113 ? 0.147925  0.203745 0.0582162 -0.0122083  -0.0107034  -0.00611537 113 SER   B O    
3271 C  CB   . SER   B 113 ? 0.143873  0.180474 0.100654  -0.00407038 -0.0302226  -0.00394902 113 SER   B CB   
3272 O  OG   . SER   B 113 ? 0.152559  0.20014  0.129347  -0.00876043 -0.046099   -0.0161262  113 SER   B OG   
3273 N  N    . VAL   B 114 ? 0.144315  0.187846 0.0677549 0.00387532  -0.00079607 0.00028893  114 VAL   B N    
3274 C  CA   . VAL   B 114 ? 0.141493  0.187447 0.0580403 0.00684897  0.00271646  -0.00023835 114 VAL   B CA   
3275 C  C    . VAL   B 114 ? 0.143421  0.189508 0.0562151 0.00800547  -0.00702397 -0.00280532 114 VAL   B C    
3276 O  O    . VAL   B 114 ? 0.160663  0.19712  0.0550703 0.0122263   -0.0159152  -0.00768966 114 VAL   B O    
3277 C  CB   . VAL   B 114 ? 0.142665  0.20204  0.0806184 0.0135848   0.00840178  0.00454827  114 VAL   B CB   
3278 C  CG1  . VAL   B 114 ? 0.141775  0.210832 0.0945309 0.0118716   0.011397    0.00362115  114 VAL   B CG1  
3279 C  CG2  . VAL   B 114 ? 0.146329  0.207992 0.0972679 0.0161376   0.0104515   0.00971892  114 VAL   B CG2  
3280 N  N    . LEU   B 115 ? 0.145966  0.183794 0.0597849 0.00405137  -0.00986441 -0.0040431  115 LEU   B N    
3281 C  CA   . LEU   B 115 ? 0.142748  0.185633 0.055409  0.00297178  -0.00723227 -0.00729928 115 LEU   B CA   
3282 C  C    . LEU   B 115 ? 0.143196  0.19366  0.0648097 -0.00224976 -0.00580985 -0.00804658 115 LEU   B C    
3283 O  O    . LEU   B 115 ? 0.146418  0.209013 0.08119   -0.0119286  -0.0114805  -0.0190389  115 LEU   B O    
3284 C  CB   . LEU   B 115 ? 0.142177  0.189623 0.0666283 0.00409901  -0.00899652 -0.0112775  115 LEU   B CB   
3285 C  CG   . LEU   B 115 ? 0.153054  0.196061 0.0760337 0.0038222   -0.0151859  -0.00847378 115 LEU   B CG   
3286 C  CD1  . LEU   B 115 ? 0.151079  0.205009 0.0804665 0.00361957  -0.0188479  -0.0112371  115 LEU   B CD1  
3287 C  CD2  . LEU   B 115 ? 0.164855  0.20456  0.087593  0.00529472  -0.0105964  -0.011458   115 LEU   B CD2  
3288 N  N    . ALA   B 116 ? 0.145384  0.200073 0.0627547 -0.00515908 -0.00537485 -0.00920799 116 ALA   B N    
3289 C  CA   . ALA   B 116 ? 0.154512  0.197401 0.0644289 -0.00896932 -0.00558349 -0.00451967 116 ALA   B CA   
3290 C  C    . ALA   B 116 ? 0.156206  0.203034 0.0709005 -0.00180766 -0.0124081  -0.00393024 116 ALA   B C    
3291 O  O    . ALA   B 116 ? 0.18179   0.199884 0.0942097 0.0103558   -0.0415949  -0.007355   116 ALA   B O    
3292 C  CB   . ALA   B 116 ? 0.159305  0.203837 0.0709413 -0.011702   0.00052976  -0.00818175 116 ALA   B CB   
3293 N  N    A CYS   B 117 ? 0.141537  0.189643 0.0663898 -0.00237474 -0.00594581 -0.00515486 117 CYS   B N    
3294 N  N    B CYS   B 117 ? 0.165427  0.215578 0.0828349 -0.00753451 -0.0159764  -0.00381548 117 CYS   B N    
3295 C  CA   A CYS   B 117 ? 0.146264  0.1856   0.0537996 -0.00543878 -0.00272211 -0.00557908 117 CYS   B CA   
3296 C  CA   B CYS   B 117 ? 0.189697  0.223947 0.0929017 -0.00549641 -0.0122706  0.00133043  117 CYS   B CA   
3297 C  C    A CYS   B 117 ? 0.153954  0.188026 0.057304  -0.00704978 0.00184863  -0.00370972 117 CYS   B C    
3298 C  C    B CYS   B 117 ? 0.182462  0.207293 0.0749365 -0.00303459 -0.00115198 0.00215178  117 CYS   B C    
3299 O  O    A CYS   B 117 ? 0.15207   0.188434 0.0585018 -0.00501912 0.00189551  -0.00651316 117 CYS   B O    
3300 O  O    B CYS   B 117 ? 0.17792   0.211804 0.0763949 -0.00283378 0.00081501  -0.00176921 117 CYS   B O    
3301 C  CB   A CYS   B 117 ? 0.136147  0.171907 0.0546925 -0.00679469 -0.00048052 -0.0110533  117 CYS   B CB   
3302 C  CB   B CYS   B 117 ? 0.22336   0.253048 0.105179  -0.00864275 -0.00168431 0.0063834   117 CYS   B CB   
3303 S  SG   A CYS   B 117 ? 0.124347  0.165927 0.0445555 -0.00918853 0.00110825  -0.0161803  117 CYS   B SG   
3304 S  SG   B CYS   B 117 ? 0.292425  0.324735 0.197262  0.0170295   0.00827264  0.0117623   117 CYS   B SG   
3305 N  N    . TYR   B 118 ? 0.17332   0.200805 0.0736167 -0.00412308 0.00421969  0.00190543  118 TYR   B N    
3306 C  CA   . TYR   B 118 ? 0.186869  0.193747 0.0818353 -0.00873042 0.00132857  -0.00342054 118 TYR   B CA   
3307 C  C    . TYR   B 118 ? 0.199748  0.202948 0.0913321 0.00042516  0.00898543  0.00065118  118 TYR   B C    
3308 O  O    . TYR   B 118 ? 0.209993  0.199351 0.0943576 0.00718781  0.00721987  -0.00874513 118 TYR   B O    
3309 C  CB   . TYR   B 118 ? 0.185294  0.205897 0.0893948 -0.0138866  0.0079537   -0.00145382 118 TYR   B CB   
3310 C  CG   . TYR   B 118 ? 0.189576  0.206932 0.084948  -0.0170594  0.0041897   -0.00408911 118 TYR   B CG   
3311 C  CD1  . TYR   B 118 ? 0.19093   0.208339 0.0728009 -0.0195154  -0.00013903 -0.00417089 118 TYR   B CD1  
3312 C  CD2  . TYR   B 118 ? 0.188915  0.216617 0.0767399 -0.0146735  -0.00235884 -0.00342203 118 TYR   B CD2  
3313 C  CE1  . TYR   B 118 ? 0.195061  0.209359 0.071961  -0.0181975  0.00534964  -0.00376021 118 TYR   B CE1  
3314 C  CE2  . TYR   B 118 ? 0.18837   0.22123  0.0739249 -0.0136435  0.00358603  -0.00486338 118 TYR   B CE2  
3315 C  CZ   . TYR   B 118 ? 0.18802   0.214366 0.0729627 -0.0157982  0.00201411  -0.00412199 118 TYR   B CZ   
3316 O  OH   . TYR   B 118 ? 0.189174  0.218518 0.0807085 -0.014651   0.0129396   -0.0138446  118 TYR   B OH   
3317 N  N    . ASN   B 119 ? 0.221262  0.200958 0.125922  -0.0045553  -0.00245285 -0.00563652 119 ASN   B N    
3318 C  CA   . ASN   B 119 ? 0.249301  0.215166 0.143608  -0.00168269 -0.00475071 -0.0127938  119 ASN   B CA   
3319 C  C    . ASN   B 119 ? 0.248509  0.212865 0.117636  0.0085983   -0.0018833  -0.0176424  119 ASN   B C    
3320 O  O    . ASN   B 119 ? 0.275826  0.219742 0.131628  0.0200568   0.00371165  -0.0146561  119 ASN   B O    
3321 C  CB   . ASN   B 119 ? 0.292584  0.244862 0.183345  -0.002057   -0.00298321 0.00153897  119 ASN   B CB   
3322 C  CG   . ASN   B 119 ? 0.334356  0.319332 0.264602  -0.0126274  0.0101975   0.00375312  119 ASN   B CG   
3323 O  OD1  . ASN   B 119 ? 0.407819  0.41793  0.347469  -0.0234171  -0.0281495  -0.00746234 119 ASN   B OD1  
3324 N  ND2  . ASN   B 119 ? 0.386218  0.394489 0.300456  -0.016869   0.0238417   0.0121161   119 ASN   B ND2  
3325 N  N    . GLY   B 120 ? 0.218286  0.202984 0.0995209 0.00884545  -0.0106857  -0.0242511  120 GLY   B N    
3326 C  CA   . GLY   B 120 ? 0.215497  0.215475 0.0943505 0.00867931  -0.000934   -0.0241768  120 GLY   B CA   
3327 C  C    . GLY   B 120 ? 0.215344  0.238613 0.124061  0.00333606  -0.00224122 -0.0231294  120 GLY   B C    
3328 O  O    . GLY   B 120 ? 0.229279  0.283094 0.141319  -0.0012169  0.0214411   -0.0166866  120 GLY   B O    
3329 N  N    . SER   B 121 ? 0.205509  0.245973 0.119946  0.00151468  -0.00862252 -0.0181163  121 SER   B N    
3330 C  CA   . SER   B 121 ? 0.227121  0.255294 0.134721  0.00162939  -0.0198526  -0.0203048  121 SER   B CA   
3331 C  C    . SER   B 121 ? 0.201754  0.234527 0.135034  0.00996191  -0.00948628 -0.00623064 121 SER   B C    
3332 O  O    . SER   B 121 ? 0.200148  0.233825 0.138042  0.0124788   -0.00362932 -0.015788   121 SER   B O    
3333 C  CB   . SER   B 121 ? 0.268158  0.285934 0.147709  0.00215851  -0.0318505  -0.0104484  121 SER   B CB   
3334 O  OG   . SER   B 121 ? 0.326252  0.363278 0.235943  0.00304867  -0.0740084  -0.0356731  121 SER   B OG   
3335 N  N    . PRO   B 122 ? 0.2135    0.224617 0.114455  0.0131449   -0.00012827 -0.0108729  122 PRO   B N    
3336 C  CA   . PRO   B 122 ? 0.220299  0.224577 0.107039  0.0179298   -0.0128789  -0.0106756  122 PRO   B CA   
3337 C  C    . PRO   B 122 ? 0.22477   0.216884 0.10921   0.0232607   -0.013868   -0.00603599 122 PRO   B C    
3338 O  O    . PRO   B 122 ? 0.241254  0.224195 0.136482  0.0461205   -0.018742   -0.00145728 122 PRO   B O    
3339 C  CB   . PRO   B 122 ? 0.230476  0.236499 0.0981933 0.00930388  -0.0142652  -0.00520407 122 PRO   B CB   
3340 C  CG   . PRO   B 122 ? 0.228077  0.248882 0.113042  0.00338779  -0.00492346 -0.0148128  122 PRO   B CG   
3341 C  CD   . PRO   B 122 ? 0.221823  0.243658 0.114652  0.00618554  -0.0009541  -0.0101983  122 PRO   B CD   
3342 N  N    . SER   B 123 ? 0.208179  0.21198  0.104829  0.0210635   -0.0140599  -0.00540706 123 SER   B N    
3343 C  CA   . SER   B 123 ? 0.213492  0.219111 0.110432  0.00611097  -0.0084127  -0.00331363 123 SER   B CA   
3344 C  C    . SER   B 123 ? 0.178363  0.207258 0.0948019 0.00447484  -0.00896407 0.00685791  123 SER   B C    
3345 O  O    . SER   B 123 ? 0.182791  0.218791 0.0916457 0.00478753  -0.0100611  0.00217101  123 SER   B O    
3346 C  CB   . SER   B 123 ? 0.241369  0.264188 0.162848  -0.0250923  -0.00554865 -0.0125762  123 SER   B CB   
3347 O  OG   . SER   B 123 ? 0.328483  0.349664 0.23748   -0.0352108  0.0278591   0.0122837   123 SER   B OG   
3348 N  N    . GLY   B 124 ? 0.156375  0.204192 0.0647037 0.00194853  -0.0056402  -0.00023713 124 GLY   B N    
3349 C  CA   . GLY   B 124 ? 0.155459  0.194176 0.0895116 0.00205049  -0.0146296  0.00399172  124 GLY   B CA   
3350 C  C    . GLY   B 124 ? 0.145963  0.195519 0.0579038 0.00088028  -0.0184112  -0.00086573 124 GLY   B C    
3351 O  O    . GLY   B 124 ? 0.160663  0.196038 0.0620411 -0.00677913 -0.0383586  -0.00148109 124 GLY   B O    
3352 N  N    . VAL   B 125 ? 0.145107  0.198738 0.0694732 -0.00101351 -0.0276919  -0.00552384 125 VAL   B N    
3353 C  CA   . VAL   B 125 ? 0.154025  0.200689 0.0820581 -0.00139324 -0.0267217  -0.00725358 125 VAL   B CA   
3354 C  C    . VAL   B 125 ? 0.157347  0.203081 0.0597543 0.00723659  -0.0303478  -0.00699048 125 VAL   B C    
3355 O  O    . VAL   B 125 ? 0.186413  0.216136 0.0597966 0.0130641   -0.0502518  -0.0149061  125 VAL   B O    
3356 C  CB   . VAL   B 125 ? 0.17141   0.224129 0.14278   -0.00939265 -0.0135087  0.00193639  125 VAL   B CB   
3357 C  CG1  . VAL   B 125 ? 0.193252  0.244855 0.161091  -0.00725351 -0.0189596  -0.00302529 125 VAL   B CG1  
3358 C  CG2  . VAL   B 125 ? 0.176395  0.220911 0.154175  -0.0113677  -0.00271432 0.00181591  125 VAL   B CG2  
3359 N  N    . TYR   B 126 ? 0.162085  0.198151 0.0491187 0.0118774   -0.0235628  -0.0106722  126 TYR   B N    
3360 C  CA   . TYR   B 126 ? 0.157478  0.202267 0.0732332 0.0133491   -0.0166473  -0.0126251  126 TYR   B CA   
3361 C  C    . TYR   B 126 ? 0.165989  0.20593  0.0548006 0.014146    -0.0106083  -0.0155236  126 TYR   B C    
3362 O  O    . TYR   B 126 ? 0.192705  0.21004  0.0512048 -6.2e-06    0.00620705  -0.00848897 126 TYR   B O    
3363 C  CB   . TYR   B 126 ? 0.171932  0.219341 0.0761608 0.0137965   0.00324914  -0.00576496 126 TYR   B CB   
3364 C  CG   . TYR   B 126 ? 0.156562  0.226086 0.102595  0.00492669  0.0180729   -0.014784   126 TYR   B CG   
3365 C  CD1  . TYR   B 126 ? 0.151649  0.242444 0.110955  -0.00456974 0.0217871   -0.0128096  126 TYR   B CD1  
3366 C  CD2  . TYR   B 126 ? 0.178343  0.242958 0.143463  -0.00192993 0.0101073   -0.0236202  126 TYR   B CD2  
3367 C  CE1  . TYR   B 126 ? 0.157455  0.264711 0.102226  -0.00727939 0.0272371   -0.0256917  126 TYR   B CE1  
3368 C  CE2  . TYR   B 126 ? 0.180007  0.255241 0.142019  -0.00333354 0.0207346   -0.0416093  126 TYR   B CE2  
3369 C  CZ   . TYR   B 126 ? 0.163714  0.273718 0.114427  -0.0103999  0.0233477   -0.039611   126 TYR   B CZ   
3370 O  OH   . TYR   B 126 ? 0.170771  0.351994 0.134449  -0.0296055  0.0299646   -0.0687807  126 TYR   B OH   
3371 N  N    . GLN   B 127 ? 0.193256  0.219956 0.0697292 0.0242092   -0.0170049  -0.0235612  127 GLN   B N    
3372 C  CA   . GLN   B 127 ? 0.20162   0.226376 0.090908  0.0288114   -0.00866877 -0.0232119  127 GLN   B CA   
3373 C  C    . GLN   B 127 ? 0.195405  0.239851 0.114624  0.030317    0.00525146  -0.00213758 127 GLN   B C    
3374 O  O    . GLN   B 127 ? 0.217584  0.261227 0.113869  0.0455156   0.0162916   0.00637638  127 GLN   B O    
3375 C  CB   . GLN   B 127 ? 0.23232   0.259772 0.0985034 0.0197957   -0.011687   -0.0408286  127 GLN   B CB   
3376 C  CG   . GLN   B 127 ? 0.243308  0.291198 0.118571  0.0138365   -0.0231709  -0.0405742  127 GLN   B CG   
3377 C  CD   . GLN   B 127 ? 0.206366  0.303596 0.126794  0.0192783   -0.0316794  -0.0513832  127 GLN   B CD   
3378 O  OE1  . GLN   B 127 ? 0.173168  0.329927 0.119405  0.0278813   -0.0479549  -0.0550057  127 GLN   B OE1  
3379 N  NE2  . GLN   B 127 ? 0.212929  0.315134 0.138198  0.0326199   -0.0356431  -0.0446712  127 GLN   B NE2  
3380 N  N    . CYS   B 128 ? 0.193272  0.251511 0.130583  0.0373121   -0.00268857 0.0195493   128 CYS   B N    
3381 C  CA   . CYS   B 128 ? 0.190734  0.27367  0.15259   0.0359862   -0.0178537  0.0259658   128 CYS   B CA   
3382 C  C    . CYS   B 128 ? 0.164333  0.258049 0.12866   0.0364396   -0.00232391 0.022601    128 CYS   B C    
3383 O  O    . CYS   B 128 ? 0.182732  0.270603 0.20149   0.0429897   0.018757    0.0487816   128 CYS   B O    
3384 C  CB   . CYS   B 128 ? 0.176112  0.315861 0.208177  0.0195055   -0.0366099  0.0240307   128 CYS   B CB   
3385 S  SG   . CYS   B 128 ? 0.352164  0.421506 0.289673  -0.0120781  -0.00474334 0.0131658   128 CYS   B SG   
3386 N  N    . ALA   B 129 ? 0.161219  0.267764 0.119596  0.0376905   -0.00893816 0.0420678   129 ALA   B N    
3387 C  CA   . ALA   B 129 ? 0.158264  0.251273 0.123359  0.0303617   -0.0269248  0.0278434   129 ALA   B CA   
3388 C  C    . ALA   B 129 ? 0.15753   0.231651 0.120319  0.018012    -0.0226815  0.0179677   129 ALA   B C    
3389 O  O    . ALA   B 129 ? 0.164098  0.236783 0.134175  0.0153082   -0.00787138 0.0198472   129 ALA   B O    
3390 C  CB   . ALA   B 129 ? 0.176696  0.261163 0.115527  0.020486    -0.0311323  0.0260442   129 ALA   B CB   
3391 N  N    . MET   B 130 ? 0.143591  0.217573 0.109019  0.0199261   -0.0284092  0.00843522  130 MET   B N    
3392 C  CA   . MET   B 130 ? 0.152253  0.210941 0.111263  0.0116649   -0.0374299  -0.00501575 130 MET   B CA   
3393 C  C    . MET   B 130 ? 0.144807  0.189378 0.100305  0.00667297  -0.0448625  -0.00545747 130 MET   B C    
3394 O  O    . MET   B 130 ? 0.158433  0.195284 0.117432  -0.00053873 -0.0394725  -0.0136732  130 MET   B O    
3395 C  CB   . MET   B 130 ? 0.171175  0.21627  0.118804  0.021683    -0.0295177  -0.0083274  130 MET   B CB   
3396 C  CG   . MET   B 130 ? 0.170046  0.227235 0.145334  0.0357961   -0.035895   -0.00742763 130 MET   B CG   
3397 S  SD   . MET   B 130 ? 0.197775  0.256867 0.137441  0.0227262   -0.03972    -0.0216569  130 MET   B SD   
3398 C  CE   . MET   B 130 ? 0.204186  0.239265 0.125444  0.0213098   -0.0560322  -0.0311055  130 MET   B CE   
3399 N  N    . ARG   B 131 ? 0.146914  0.188265 0.106064  0.00702998  -0.0407754  -0.0121592  131 ARG   B N    
3400 C  CA   . ARG   B 131 ? 0.147708  0.192001 0.0988135 0.00915155  -0.0389705  -0.015307   131 ARG   B CA   
3401 C  C    . ARG   B 131 ? 0.13954   0.194212 0.0859497 0.00600345  -0.037737   -0.0193343  131 ARG   B C    
3402 O  O    . ARG   B 131 ? 0.131112  0.195911 0.081364  0.00804664  -0.0242077  -0.0168578  131 ARG   B O    
3403 C  CB   . ARG   B 131 ? 0.150918  0.198903 0.10243   0.0100318   -0.0369316  -0.0160545  131 ARG   B CB   
3404 C  CG   . ARG   B 131 ? 0.155535  0.2036   0.0978497 0.00970988  -0.041411   -0.0188512  131 ARG   B CG   
3405 C  CD   . ARG   B 131 ? 0.157597  0.20788  0.107658  0.0111245   -0.0474231  -0.0215477  131 ARG   B CD   
3406 N  NE   . ARG   B 131 ? 0.155772  0.210399 0.103266  0.0133984   -0.0465064  -0.0265311  131 ARG   B NE   
3407 C  CZ   . ARG   B 131 ? 0.159596  0.205755 0.118651  0.0151009   -0.0378036  -0.0374712  131 ARG   B CZ   
3408 N  NH1  . ARG   B 131 ? 0.162898  0.204826 0.117593  0.0217325   -0.0358776  -0.0408787  131 ARG   B NH1  
3409 N  NH2  . ARG   B 131 ? 0.160218  0.214664 0.130769  0.0177069   -0.0467125  -0.0426979  131 ARG   B NH2  
3410 N  N    . PRO   B 132 ? 0.146927  0.198102 0.0864461 0.0119046   -0.0364235  -0.0168258  132 PRO   B N    
3411 C  CA   . PRO   B 132 ? 0.152516  0.196567 0.096634  0.0160242   -0.0325345  -0.016224   132 PRO   B CA   
3412 C  C    . PRO   B 132 ? 0.157635  0.188503 0.0754574 0.0138673   -0.0334727  -0.0109534  132 PRO   B C    
3413 O  O    . PRO   B 132 ? 0.194117  0.193404 0.0788269 0.0142722   -0.0225429  0.0082027   132 PRO   B O    
3414 C  CB   . PRO   B 132 ? 0.16005   0.201788 0.102989  0.0162465   -0.0336692  -0.0205324  132 PRO   B CB   
3415 C  CG   . PRO   B 132 ? 0.164589  0.207953 0.110029  0.0129606   -0.0375799  -0.019402   132 PRO   B CG   
3416 C  CD   . PRO   B 132 ? 0.155441  0.203453 0.0932417 0.0156705   -0.0343489  -0.0217651  132 PRO   B CD   
3417 N  N    . ASN   B 133 ? 0.150493  0.205141 0.0768217 0.00820101  -0.0312687  -0.0110415  133 ASN   B N    
3418 C  CA   . ASN   B 133 ? 0.144664  0.208467 0.0757563 0.00932423  -0.0277676  -0.0110454  133 ASN   B CA   
3419 C  C    . ASN   B 133 ? 0.151609  0.199713 0.0756555 0.00612903  -0.0243324  -0.00923057 133 ASN   B C    
3420 O  O    . ASN   B 133 ? 0.152826  0.232434 0.074691  -0.0012738  -0.0294616  -0.0124857  133 ASN   B O    
3421 C  CB   . ASN   B 133 ? 0.147256  0.214983 0.0812704 0.0124721   -0.0164682  -0.0139335  133 ASN   B CB   
3422 C  CG   . ASN   B 133 ? 0.147429  0.221852 0.0802977 0.0150441   -0.0069076  -0.0126418  133 ASN   B CG   
3423 O  OD1  . ASN   B 133 ? 0.144149  0.223307 0.0732697 0.0171459   -0.0182358  -0.0136435  133 ASN   B OD1  
3424 N  ND2  . ASN   B 133 ? 0.155941  0.238931 0.0885916 0.0144589   0.00118679  -0.00480868 133 ASN   B ND2  
3425 N  N    . PHE   B 134 ? 0.151621  0.198945 0.06658   0.00888303  -0.0236304  -0.0111162  134 PHE   B N    
3426 C  CA   . PHE   B 134 ? 0.164797  0.197273 0.0686531 0.0105881   -0.0195779  -0.0116463  134 PHE   B CA   
3427 C  C    . PHE   B 134 ? 0.179127  0.19639  0.0781038 0.00734457  -0.01014    -0.0147261  134 PHE   B C    
3428 O  O    . PHE   B 134 ? 0.260195  0.200481 0.100262  0.0197303   0.0240216   -0.0109761  134 PHE   B O    
3429 C  CB   . PHE   B 134 ? 0.173029  0.20573  0.0699141 0.0094376   -0.0222991  -0.0110816  134 PHE   B CB   
3430 C  CG   . PHE   B 134 ? 0.199825  0.207474 0.090844  0.00878146  -0.0144059  -0.00686255 134 PHE   B CG   
3431 C  CD1  . PHE   B 134 ? 0.208181  0.216434 0.109493  0.00310421  -0.0105661  0.00940773  134 PHE   B CD1  
3432 C  CD2  . PHE   B 134 ? 0.219503  0.217444 0.116754  0.0106929   -0.00526187 0.00546994  134 PHE   B CD2  
3433 C  CE1  . PHE   B 134 ? 0.220983  0.234413 0.133611  0.00469554  0.00762824  0.0224898   134 PHE   B CE1  
3434 C  CE2  . PHE   B 134 ? 0.226363  0.225286 0.133149  0.00969137  -0.00684856 0.0157578   134 PHE   B CE2  
3435 C  CZ   . PHE   B 134 ? 0.239016  0.223645 0.134942  0.00365993  0.00417991  0.0294343   134 PHE   B CZ   
3436 N  N    . THR   B 135 ? 0.162741  0.189247 0.0720964 0.00572861  -0.0116146  -0.0115954  135 THR   B N    
3437 C  CA   . THR   B 135 ? 0.152398  0.194109 0.0916297 0.00045393  -0.0112035  -0.0109732  135 THR   B CA   
3438 C  C    . THR   B 135 ? 0.147368  0.193708 0.080276  -0.00161791 -0.00667988 -0.0161249  135 THR   B C    
3439 O  O    . THR   B 135 ? 0.150356  0.203098 0.0915775 -0.00617983 -0.0174874  -0.0204596  135 THR   B O    
3440 C  CB   . THR   B 135 ? 0.162376  0.203549 0.0993123 0.00394006  -0.00724166 -0.0110388  135 THR   B CB   
3441 O  OG1  . THR   B 135 ? 0.167851  0.205131 0.0962123 0.0011433   -0.00395853 -0.00877771 135 THR   B OG1  
3442 C  CG2  . THR   B 135 ? 0.160844  0.216075 0.118488  0.00923059  -0.00903386 -0.0112788  135 THR   B CG2  
3443 N  N    . ILE   B 136 ? 0.153268  0.199573 0.0820292 -0.00701944 -0.00702046 -0.0154014  136 ILE   B N    
3444 C  CA   . ILE   B 136 ? 0.15829   0.208047 0.0869284 -0.00524143 -0.00708285 -0.00583297 136 ILE   B CA   
3445 C  C    . ILE   B 136 ? 0.159667  0.201356 0.0868094 -0.00223628 -0.00454835 -0.00632634 136 ILE   B C    
3446 O  O    . ILE   B 136 ? 0.160526  0.20854  0.0769644 -0.00415126 -0.00561874 -0.00935441 136 ILE   B O    
3447 C  CB   . ILE   B 136 ? 0.192107  0.234317 0.119506  -0.00146366 0.0163171   -0.0153278  136 ILE   B CB   
3448 C  CG1  . ILE   B 136 ? 0.190638  0.23566  0.121153  -0.0119037  0.0155408   -0.0218844  136 ILE   B CG1  
3449 C  CG2  . ILE   B 136 ? 0.204742  0.248047 0.152055  -0.00141845 0.0334209   -0.00228383 136 ILE   B CG2  
3450 C  CD1  . ILE   B 136 ? 0.196784  0.235609 0.124671  -0.00981246 0.0188822   -0.028113   136 ILE   B CD1  
3451 N  N    . LYS   B 137 ? 0.163807  0.211544 0.0971135 -0.00434639 -0.015841   -0.00542158 137 LYS   B N    
3452 C  CA   . LYS   B 137 ? 0.179738  0.224086 0.099878  -0.00309495 -0.00844716 -0.00562559 137 LYS   B CA   
3453 C  C    . LYS   B 137 ? 0.16962   0.216671 0.103161  -0.00921415 -0.00373362 -0.00753754 137 LYS   B C    
3454 O  O    . LYS   B 137 ? 0.188625  0.229567 0.109398  -0.00784746 -0.0278791  -0.00213361 137 LYS   B O    
3455 C  CB   . LYS   B 137 ? 0.204515  0.246001 0.121479  0.00797441  -0.00879885 -0.0189658  137 LYS   B CB   
3456 C  CG   . LYS   B 137 ? 0.236097  0.273327 0.157168  0.0240671   -0.0169514  -0.0196823  137 LYS   B CG   
3457 C  CD   . LYS   B 137 ? 0.284066  0.314105 0.194756  0.0335343   -0.00229636 -0.0355161  137 LYS   B CD   
3458 C  CE   . LYS   B 137 ? 0.345703  0.355535 0.24221   0.0432326   0.00331672  -0.0199241  137 LYS   B CE   
3459 N  NZ   . LYS   B 137 ? 0.397596  0.401722 0.25394   0.0392239   0.00527459  -0.0279456  137 LYS   B NZ   
3460 N  N    . GLY   B 138 ? 0.149096  0.213889 0.0920928 -0.00777136 0.00646815  -0.00879286 138 GLY   B N    
3461 C  CA   . GLY   B 138 ? 0.161327  0.211481 0.103437  -0.0085156  0.00787103  -0.005733   138 GLY   B CA   
3462 C  C    . GLY   B 138 ? 0.143976  0.211973 0.0809237 -0.00275132 0.0101778   -0.0104191  138 GLY   B C    
3463 O  O    . GLY   B 138 ? 0.144749  0.230971 0.112108  0.00116273  0.0284164   -0.016783   138 GLY   B O    
3464 N  N    . SER   B 139 ? 0.130319  0.208454 0.0653317 -0.00341453 -0.00059116 -0.00765761 139 SER   B N    
3465 C  CA   . SER   B 139 ? 0.126585  0.212421 0.0760206 -0.00459274 -0.00706328 -0.00198015 139 SER   B CA   
3466 C  C    . SER   B 139 ? 0.122311  0.215242 0.0690943 -0.00055791 0.00320633  -0.00202341 139 SER   B C    
3467 O  O    . SER   B 139 ? 0.124265  0.223617 0.0817776 0.00287229  0.00353894  -0.00321186 139 SER   B O    
3468 C  CB   . SER   B 139 ? 0.134646  0.218004 0.0832359 -0.0101431  -0.0148314  0.00048624  139 SER   B CB   
3469 O  OG   . SER   B 139 ? 0.159536  0.231154 0.085171  -0.0141445  -0.012972   0.0138908   139 SER   B OG   
3470 N  N    . PHE   B 140 ? 0.132146  0.210351 0.0681854 -0.00653007 0.00276586  -0.00934359 140 PHE   B N    
3471 C  CA   . PHE   B 140 ? 0.141553  0.210859 0.0732813 -0.00823839 0.00183035  -0.00800839 140 PHE   B CA   
3472 C  C    . PHE   B 140 ? 0.151768  0.213083 0.0624226 -0.010246   0.00952442  -0.00801428 140 PHE   B C    
3473 O  O    . PHE   B 140 ? 0.148354  0.232615 0.101249  -0.00958375 0.00055631  -0.00293554 140 PHE   B O    
3474 C  CB   . PHE   B 140 ? 0.139396  0.210307 0.0794346 -0.011244   -0.0011033  -0.00442607 140 PHE   B CB   
3475 C  CG   . PHE   B 140 ? 0.140379  0.21249  0.0827645 -0.017286   -0.00108194 -0.00705898 140 PHE   B CG   
3476 C  CD1  . PHE   B 140 ? 0.149896  0.215759 0.113485  -0.0173914  -0.00244585 -0.00782895 140 PHE   B CD1  
3477 C  CD2  . PHE   B 140 ? 0.137267  0.225855 0.108001  -0.00992334 -0.00510993 0.00790623  140 PHE   B CD2  
3478 C  CE1  . PHE   B 140 ? 0.147618  0.23626  0.107777  -0.0197014  0.00065325  -0.0066218  140 PHE   B CE1  
3479 C  CE2  . PHE   B 140 ? 0.153695  0.237235 0.11697   -0.0143094  -0.0148144  0.018135    140 PHE   B CE2  
3480 C  CZ   . PHE   B 140 ? 0.161808  0.238322 0.106858  -0.0272185  0.00351081  0.00639817  140 PHE   B CZ   
3481 N  N    . LEU   B 141 ? 0.168372  0.219827 0.0654783 -0.0108726  0.0232421   -0.00012322 141 LEU   B N    
3482 C  CA   . LEU   B 141 ? 0.181648  0.212153 0.0738646 -0.015977   0.017564    -0.00806373 141 LEU   B CA   
3483 C  C    . LEU   B 141 ? 0.182389  0.205824 0.0707251 -0.0262181  0.0240245   -0.00535326 141 LEU   B C    
3484 O  O    . LEU   B 141 ? 0.169622  0.186503 0.0772941 -0.0305115  0.0204316   0.0063447   141 LEU   B O    
3485 C  CB   . LEU   B 141 ? 0.20142   0.220046 0.0877593 -0.0150789  0.0175268   -0.00196227 141 LEU   B CB   
3486 C  CG   . LEU   B 141 ? 0.224681  0.24092  0.0921867 -0.0128921  0.0178871   -0.00126481 141 LEU   B CG   
3487 C  CD1  . LEU   B 141 ? 0.23842   0.256181 0.113326  -0.00500814 0.0130765   0.00131274  141 LEU   B CD1  
3488 C  CD2  . LEU   B 141 ? 0.24619   0.253247 0.104067  -0.00562395 0.0232487   -0.00180232 141 LEU   B CD2  
3489 N  N    . ASN   B 142 ? 0.187492  0.215098 0.0885686 -0.0266978  0.031245    0.00434679  142 ASN   B N    
3490 C  CA   . ASN   B 142 ? 0.208557  0.218094 0.110564  -0.0276546  0.015807    -0.00285159 142 ASN   B CA   
3491 C  C    . ASN   B 142 ? 0.201107  0.210652 0.0990017 -0.0263117  0.0100295   0.00534787  142 ASN   B C    
3492 O  O    . ASN   B 142 ? 0.217327  0.225694 0.0937679 -0.0181263  0.00872487  0.0151733   142 ASN   B O    
3493 C  CB   . ASN   B 142 ? 0.242047  0.244831 0.164297  -0.0437732  0.0248962   0.00396197  142 ASN   B CB   
3494 C  CG   . ASN   B 142 ? 0.306894  0.288832 0.217418  -0.0520295  0.0167137   -0.0122031  142 ASN   B CG   
3495 O  OD1  . ASN   B 142 ? 0.371318  0.353228 0.24369   -0.0732263  0.0194174   0.0132064   142 ASN   B OD1  
3496 N  ND2  . ASN   B 142 ? 0.378903  0.317393 0.27317   -0.0444633  0.0255474   -0.00596753 142 ASN   B ND2  
3497 N  N    . GLY   B 143 ? 0.188936  0.199417 0.0958797 -0.0267872  0.00954549  -0.00486795 143 GLY   B N    
3498 C  CA   . GLY   B 143 ? 0.192004  0.18564  0.0910224 -0.0198994  0.00289256  -0.00706944 143 GLY   B CA   
3499 C  C    . GLY   B 143 ? 0.185168  0.181522 0.0762344 -0.018901   -0.00521535 -0.00678936 143 GLY   B C    
3500 O  O    . GLY   B 143 ? 0.201699  0.186045 0.0948901 -0.0161949  -0.00388274 -0.018301   143 GLY   B O    
3501 N  N    . SER   B 144 ? 0.169896  0.184287 0.0548865 -0.0189564  -0.00509897 -0.00803845 144 SER   B N    
3502 C  CA   . SER   B 144 ? 0.162475  0.179803 0.0554723 -0.0186494  -0.00175553 -0.00870388 144 SER   B CA   
3503 C  C    . SER   B 144 ? 0.148429  0.174756 0.0599417 -0.0221619  0.00393968  -0.00637475 144 SER   B C    
3504 O  O    . SER   B 144 ? 0.140495  0.177565 0.0620259 -0.0242111  0.0022434   -0.00602982 144 SER   B O    
3505 C  CB   . SER   B 144 ? 0.173991  0.183519 0.0542462 -0.0187339  0.00590375  -0.00969534 144 SER   B CB   
3506 O  OG   . SER   B 144 ? 0.183129  0.192116 0.0593653 -0.0119624  0.0148138   -0.0124451  144 SER   B OG   
3507 N  N    . CYS   B 145 ? 0.137345  0.186165 0.0595331 -0.0211977  0.0029329   -0.00223692 145 CYS   B N    
3508 C  CA   . CYS   B 145 ? 0.14725   0.190709 0.0603138 -0.0164207  0.0009241   -0.00301382 145 CYS   B CA   
3509 C  C    . CYS   B 145 ? 0.14442   0.177438 0.0599954 -0.0136181  -0.00745964 -0.00507272 145 CYS   B C    
3510 O  O    . CYS   B 145 ? 0.152307  0.181453 0.0637946 -0.00291226 -0.00477721 -0.00610435 145 CYS   B O    
3511 C  CB   . CYS   B 145 ? 0.152981  0.216616 0.0552316 -0.0191235  0.0029851   -0.0049747  145 CYS   B CB   
3512 S  SG   . CYS   B 145 ? 0.155804  0.269315 0.0920767 -0.0171874  0.00410533  -0.00295218 145 CYS   B SG   
3513 N  N    . GLY   B 146 ? 0.128334  0.166281 0.0532763 -0.0101823  -0.0101439  -0.00432326 146 GLY   B N    
3514 C  CA   . GLY   B 146 ? 0.131024  0.174241 0.058817  -0.0160015  -0.00529895 -0.00585321 146 GLY   B CA   
3515 C  C    . GLY   B 146 ? 0.133216  0.168779 0.0639303 -0.0180096  -0.00503051 -0.00700947 146 GLY   B C    
3516 O  O    . GLY   B 146 ? 0.132302  0.194961 0.080046  -0.02104    -0.003171   -0.0144691  146 GLY   B O    
3517 N  N    . SER   B 147 ? 0.136107  0.166043 0.0610825 -0.0181583  -0.00536413 0.00037711  147 SER   B N    
3518 C  CA   . SER   B 147 ? 0.130374  0.16795  0.0654944 -0.0131671  -0.0102098  0.00048475  147 SER   B CA   
3519 C  C    . SER   B 147 ? 0.129365  0.16924  0.0690289 -0.00838991 -0.00743184 0.00048323  147 SER   B C    
3520 O  O    . SER   B 147 ? 0.123999  0.181411 0.0907632 -0.00725513 -0.0128997  0.0127217   147 SER   B O    
3521 C  CB   . SER   B 147 ? 0.1384    0.166017 0.0649292 -0.0136232  -0.0148323  -0.00332128 147 SER   B CB   
3522 O  OG   . SER   B 147 ? 0.150338  0.177111 0.0677338 -0.0182219  -0.0189664  0.00813823  147 SER   B OG   
3523 N  N    . VAL   B 148 ? 0.132027  0.180346 0.0729376 -0.00931671 -0.008879   0.000382    148 VAL   B N    
3524 C  CA   . VAL   B 148 ? 0.135582  0.181751 0.0820794 -0.0114144  -0.00423722 -0.00669504 148 VAL   B CA   
3525 C  C    . VAL   B 148 ? 0.140815  0.182836 0.0657104 -0.00698118 -0.00791413 -0.00192991 148 VAL   B C    
3526 O  O    . VAL   B 148 ? 0.159356  0.193683 0.0667531 -0.0004053  -0.0160627  -0.00192734 148 VAL   B O    
3527 C  CB   . VAL   B 148 ? 0.148888  0.201033 0.0937513 -0.0118219  0.00330784  -0.0241326  148 VAL   B CB   
3528 C  CG1  . VAL   B 148 ? 0.147459  0.215969 0.0926814 -0.0186962  0.00839118  -0.0300122  148 VAL   B CG1  
3529 C  CG2  . VAL   B 148 ? 0.16056   0.22042  0.114491  -0.00813054 0.00027784  -0.0278522  148 VAL   B CG2  
3530 N  N    . GLY   B 149 ? 0.139285  0.179513 0.0631175 -0.00642282 -0.0126463  -0.00049849 149 GLY   B N    
3531 C  CA   . GLY   B 149 ? 0.138495  0.186189 0.0631994 -0.00677809 -0.0119935  -0.00332557 149 GLY   B CA   
3532 C  C    . GLY   B 149 ? 0.137283  0.190082 0.0525794 -0.00840581 -0.0128514  -0.00393749 149 GLY   B C    
3533 O  O    . GLY   B 149 ? 0.138436  0.191092 0.0503302 -0.0104491  -0.0176495  -0.00454789 149 GLY   B O    
3534 N  N    . PHE   B 150 ? 0.134567  0.196524 0.0545096 -0.0123864  -0.0107732  -0.00759368 150 PHE   B N    
3535 C  CA   . PHE   B 150 ? 0.136576  0.193921 0.0708212 -0.0126018  -0.0115322  -0.00375772 150 PHE   B CA   
3536 C  C    . PHE   B 150 ? 0.135993  0.204789 0.076684  -0.0171507  -0.0089394  -0.00646753 150 PHE   B C    
3537 O  O    . PHE   B 150 ? 0.129728  0.199471 0.0728017 -0.0128024  -0.00835113 -0.00881775 150 PHE   B O    
3538 C  CB   . PHE   B 150 ? 0.147498  0.195704 0.0906499 -0.00599549 -0.00850185 -0.00976707 150 PHE   B CB   
3539 C  CG   . PHE   B 150 ? 0.164737  0.198273 0.114398  0.0138718   -0.0135885  -0.00593063 150 PHE   B CG   
3540 C  CD1  . PHE   B 150 ? 0.180873  0.199074 0.121433  0.0180707   -0.018867   0.00134931  150 PHE   B CD1  
3541 C  CD2  . PHE   B 150 ? 0.173317  0.200559 0.1362    0.0204384   -0.0173175  -0.00347486 150 PHE   B CD2  
3542 C  CE1  . PHE   B 150 ? 0.193079  0.207161 0.132972  0.0257572   -0.0202129  0.00517025  150 PHE   B CE1  
3543 C  CE2  . PHE   B 150 ? 0.185104  0.209    0.14564   0.0269111   -0.0201066  -0.00029313 150 PHE   B CE2  
3544 C  CZ   . PHE   B 150 ? 0.194826  0.208934 0.147831  0.029983    -0.0233141  0.0113081   150 PHE   B CZ   
3545 N  N    . ASN   B 151 ? 0.130042  0.21084  0.0746075 -0.0209201  -0.0110392  -0.00684071 151 ASN   B N    
3546 C  CA   . ASN   B 151 ? 0.141966  0.223204 0.0938062 -0.0250656  -0.00972215 -0.0215287  151 ASN   B CA   
3547 C  C    . ASN   B 151 ? 0.144181  0.233144 0.0924244 -0.0266457  0.00081081  -0.0272001  151 ASN   B C    
3548 O  O    . ASN   B 151 ? 0.147742  0.247666 0.0949261 -0.0207471  -0.00831904 -0.0338993  151 ASN   B O    
3549 C  CB   . ASN   B 151 ? 0.157365  0.233507 0.11721   -0.0228866  -0.0128255  -0.0184792  151 ASN   B CB   
3550 C  CG   . ASN   B 151 ? 0.188352  0.263655 0.133398  -0.01207    -0.00064938 -0.022701   151 ASN   B CG   
3551 O  OD1  . ASN   B 151 ? 0.224309  0.348224 0.150546  0.00094172  0.00838456  -0.0479379  151 ASN   B OD1  
3552 N  ND2  . ASN   B 151 ? 0.190015  0.274608 0.13894   -0.0102859  0.00203918  -0.0233166  151 ASN   B ND2  
3553 N  N    . ILE   B 152 ? 0.134414  0.257888 0.0924831 -0.0280405  0.00530676  -0.0271749  152 ILE   B N    
3554 C  CA   . ILE   B 152 ? 0.159537  0.299682 0.116378  -0.0250764  0.0267335   -0.0394347  152 ILE   B CA   
3555 C  C    . ILE   B 152 ? 0.214     0.317148 0.164665  -0.0466047  0.0352157   -0.0606171  152 ILE   B C    
3556 O  O    . ILE   B 152 ? 0.226595  0.332723 0.202646  -0.0659924  0.0548025   -0.0848657  152 ILE   B O    
3557 C  CB   . ILE   B 152 ? 0.164965  0.338458 0.149768  -0.00326503 0.0188432   -0.0295126  152 ILE   B CB   
3558 C  CG1  . ILE   B 152 ? 0.184777  0.351666 0.160593  0.00810775  0.00958943  0.00558425  152 ILE   B CG1  
3559 C  CG2  . ILE   B 152 ? 0.1678    0.362552 0.182436  0.00157627  0.022613    -0.027768   152 ILE   B CG2  
3560 C  CD1  . ILE   B 152 ? 0.217857  0.376943 0.197355  0.0226303   0.0165135   0.0187676   152 ILE   B CD1  
3561 N  N    . ASP   B 153 ? 0.267555  0.365622 0.209639  -0.0613666  0.0729129   -0.0751084  153 ASP   B N    
3562 C  CA   . ASP   B 153 ? 0.316283  0.403283 0.271833  -0.0827144  0.0369577   -0.0887635  153 ASP   B CA   
3563 C  C    . ASP   B 153 ? 0.317388  0.459393 0.255649  -0.0916989  0.0518913   -0.113791   153 ASP   B C    
3564 O  O    . ASP   B 153 ? 0.33994   0.46294  0.26505   -0.111252   0.0564748   -0.135622   153 ASP   B O    
3565 C  CB   . ASP   B 153 ? 0.373437  0.420318 0.333866  -0.075166   0.02697     -0.0620248  153 ASP   B CB   
3566 C  CG   . ASP   B 153 ? 0.401289  0.483771 0.411145  -0.0677547  0.0193458   -0.0638896  153 ASP   B CG   
3567 O  OD1  . ASP   B 153 ? 0.448262  0.520785 0.478941  -0.0834738  0.00270607  -0.0877452  153 ASP   B OD1  
3568 O  OD2  . ASP   B 153 ? 0.494998  0.510348 0.535086  -0.0796739  -0.0367143  -0.0886759  153 ASP   B OD2  
3569 N  N    . TYR   B 154 ? 0.32058   0.520752 0.306784  -0.0939362  0.031771    -0.115623   154 TYR   B N    
3570 C  CA   . TYR   B 154 ? 0.346558  0.550712 0.335056  -0.0679844  0.0331686   -0.11067    154 TYR   B CA   
3571 C  C    . TYR   B 154 ? 0.35265   0.573273 0.364422  -0.0558239  0.0110069   -0.104354   154 TYR   B C    
3572 O  O    . TYR   B 154 ? 0.362729  0.617356 0.394249  -0.0643934  0.0364865   -0.0884626  154 TYR   B O    
3573 C  CB   . TYR   B 154 ? 0.35312   0.574566 0.377666  -0.0651296  0.051386    -0.0928623  154 TYR   B CB   
3574 N  N    . ASP   B 155 ? 0.319148  0.567677 0.372035  -0.0392653  -0.0269538  -0.116269   155 ASP   B N    
3575 C  CA   . ASP   B 155 ? 0.284551  0.558386 0.365784  -0.010381   -0.0439333  -0.0852771  155 ASP   B CA   
3576 C  C    . ASP   B 155 ? 0.2562    0.485481 0.322328  0.00751228  -0.0425515  -0.0828868  155 ASP   B C    
3577 O  O    . ASP   B 155 ? 0.271952  0.50332  0.330212  0.0775419   -0.045066   -0.0781145  155 ASP   B O    
3578 C  CB   . ASP   B 155 ? 0.291034  0.608348 0.411555  0.0039233   -0.0274298  -0.064973   155 ASP   B CB   
3579 C  CG   . ASP   B 155 ? 0.313069  0.658343 0.460221  -0.00194661 -0.00278808 -0.0392936  155 ASP   B CG   
3580 O  OD1  . ASP   B 155 ? 0.277736  0.694807 0.492033  -0.0221892  -0.00147042 -0.00426684 155 ASP   B OD1  
3581 O  OD2  . ASP   B 155 ? 0.374038  0.696795 0.505237  0.0179328   0.0350707   -0.023228   155 ASP   B OD2  
3582 N  N    . CYS   B 156 ? 0.235465  0.407    0.211838  -0.0151809  -0.0187044  -0.076649   156 CYS   B N    
3583 C  CA   . CYS   B 156 ? 0.176641  0.350849 0.180039  -0.0190144  0.0189175   -0.0500588  156 CYS   B CA   
3584 C  C    . CYS   B 156 ? 0.172344  0.295665 0.150612  -0.00864229 0.017448    -0.0376245  156 CYS   B C    
3585 O  O    . CYS   B 156 ? 0.183501  0.293464 0.166804  -0.0227853  0.03143     -0.0441657  156 CYS   B O    
3586 C  CB   . CYS   B 156 ? 0.232672  0.362958 0.216202  -0.0196358  0.0549468   -0.0323047  156 CYS   B CB   
3587 S  SG   . CYS   B 156 ? 0.302782  0.373027 0.237055  -0.0309226  0.0571511   0.0120667   156 CYS   B SG   
3588 N  N    . VAL   B 157 ? 0.137892  0.273202 0.10558   -0.00317895 0.00617541  -0.0191575  157 VAL   B N    
3589 C  CA   . VAL   B 157 ? 0.128177  0.25283  0.0999304 0.00777525  -0.0105758  -0.0129103  157 VAL   B CA   
3590 C  C    . VAL   B 157 ? 0.130358  0.240592 0.0877534 0.00057851  -0.0179848  -0.0144196  157 VAL   B C    
3591 O  O    . VAL   B 157 ? 0.17177   0.267408 0.099246  0.0151244   -0.00917577 -0.0291997  157 VAL   B O    
3592 C  CB   . VAL   B 157 ? 0.148582  0.25636  0.10016   0.0115977   -0.0159823  -0.0082846  157 VAL   B CB   
3593 C  CG1  . VAL   B 157 ? 0.149859  0.252833 0.104031  0.0131004   -0.0164186  -0.00711357 157 VAL   B CG1  
3594 C  CG2  . VAL   B 157 ? 0.163359  0.261929 0.109567  0.0234628   -0.0146747  -0.00395068 157 VAL   B CG2  
3595 N  N    . SER   B 158 ? 0.128587  0.218686 0.0873574 -0.00757263 -0.0234439  -0.0112319  158 SER   B N    
3596 C  CA   . SER   B 158 ? 0.129235  0.220914 0.0847253 -0.0115608  -0.0202112  -0.00536175 158 SER   B CA   
3597 C  C    . SER   B 158 ? 0.123501  0.206008 0.0735463 -0.0102507  -0.016153   -0.00225067 158 SER   B C    
3598 O  O    . SER   B 158 ? 0.149426  0.222984 0.0834733 -0.0216879  -0.00087035 -0.0171131  158 SER   B O    
3599 C  CB   . SER   B 158 ? 0.148912  0.230158 0.116071  -0.0173847  -0.0146297  -0.00675003 158 SER   B CB   
3600 O  OG   . SER   B 158 ? 0.182085  0.274118 0.151973  -0.0323628  -0.00968267 0.010431    158 SER   B OG   
3601 N  N    . PHE   B 159 ? 0.122863  0.196414 0.0717466 -0.0101039  -0.0084572  0.00039488  159 PHE   B N    
3602 C  CA   . PHE   B 159 ? 0.126553  0.193695 0.0751981 -0.00561139 -0.0119182  0.00942597  159 PHE   B CA   
3603 C  C    . PHE   B 159 ? 0.119634  0.20606  0.0729597 -0.00598256 -0.021122   0.0177715   159 PHE   B C    
3604 O  O    . PHE   B 159 ? 0.131183  0.234671 0.0764176 0.00173965  -0.0213046  0.0314779   159 PHE   B O    
3605 C  CB   . PHE   B 159 ? 0.134788  0.189001 0.0853331 -0.00836554 -0.0128661  0.00942624  159 PHE   B CB   
3606 C  CG   . PHE   B 159 ? 0.149091  0.182009 0.0839907 -0.00482982 -0.0119161  0.0103398   159 PHE   B CG   
3607 C  CD1  . PHE   B 159 ? 0.152876  0.180082 0.0894047 -0.00577118 -0.0039762  0.0125798   159 PHE   B CD1  
3608 C  CD2  . PHE   B 159 ? 0.151011  0.193156 0.0915058 -0.00171663 -0.0119462  0.0135926   159 PHE   B CD2  
3609 C  CE1  . PHE   B 159 ? 0.152642  0.1823   0.0912542 -0.0077332  -0.0114722  0.0140664   159 PHE   B CE1  
3610 C  CE2  . PHE   B 159 ? 0.153162  0.189663 0.0963158 -0.00254622 -0.0126765  0.00660216  159 PHE   B CE2  
3611 C  CZ   . PHE   B 159 ? 0.150808  0.187474 0.097702  -0.00221382 -0.0173561  0.00976088  159 PHE   B CZ   
3612 N  N    . CYS   B 160 ? 0.109634  0.201882 0.0777055 -0.00425099 -0.0238888  0.0138313   160 CYS   B N    
3613 C  CA   . CYS   B 160 ? 0.125846  0.198512 0.0907551 2.867e-05   -0.0148655  0.0112407   160 CYS   B CA   
3614 C  C    . CYS   B 160 ? 0.125208  0.194232 0.0848623 -0.0020065  -0.0120986  0.00726436  160 CYS   B C    
3615 O  O    . CYS   B 160 ? 0.127853  0.215968 0.10842   -0.00194074 -0.0111045  0.0303593   160 CYS   B O    
3616 C  CB   . CYS   B 160 ? 0.1345    0.199581 0.102049  0.00011731  -0.0187961  0.00387299  160 CYS   B CB   
3617 S  SG   . CYS   B 160 ? 0.181587  0.214081 0.104207  0.00318948  -0.0227616  -0.00774718 160 CYS   B SG   
3618 N  N    . TYR   B 161 ? 0.110113  0.188097 0.0685484 -0.00652427 -0.0155483  0.00236425  161 TYR   B N    
3619 C  CA   . TYR   B 161 ? 0.115951  0.191034 0.0521935 -0.00504821 -0.0134442  0.00278134  161 TYR   B CA   
3620 C  C    . TYR   B 161 ? 0.114408  0.18697  0.0467183 -0.00896493 -0.0125347  0.00453476  161 TYR   B C    
3621 O  O    . TYR   B 161 ? 0.120271  0.185547 0.0557901 -0.00996561 -0.0167049  0.0101025   161 TYR   B O    
3622 C  CB   . TYR   B 161 ? 0.121014  0.186529 0.0529002 -0.00268822 -0.0157548  -0.00142754 161 TYR   B CB   
3623 C  CG   . TYR   B 161 ? 0.119089  0.186933 0.0549492 -0.00120054 -0.015754   -0.00278626 161 TYR   B CG   
3624 C  CD1  . TYR   B 161 ? 0.119295  0.192663 0.0587204 -0.00082687 -0.0119762  -0.00128376 161 TYR   B CD1  
3625 C  CD2  . TYR   B 161 ? 0.115932  0.184198 0.0530896 -0.00051952 -0.0122341  -0.00192159 161 TYR   B CD2  
3626 C  CE1  . TYR   B 161 ? 0.123027  0.189167 0.0634859 -0.00419979 -0.00850347 -0.00585859 161 TYR   B CE1  
3627 C  CE2  . TYR   B 161 ? 0.126802  0.186519 0.0404615 -0.00251192 -0.00566431 -0.00108885 161 TYR   B CE2  
3628 C  CZ   . TYR   B 161 ? 0.121594  0.188431 0.052187  -0.00472136 -0.00472424 -0.00739089 161 TYR   B CZ   
3629 O  OH   . TYR   B 161 ? 0.13129   0.192842 0.0611444 -0.0114213  -0.00153534 -0.00724391 161 TYR   B OH   
3630 N  N    . MET   B 162 ? 0.116627  0.177937 0.0444937 -0.0079454  -0.0154098  -0.00361241 162 MET   B N    
3631 C  CA   . MET   B 162 ? 0.122525  0.182128 0.0462793 -0.00717233 -0.0107187  -0.00827575 162 MET   B CA   
3632 C  C    . MET   B 162 ? 0.120815  0.170762 0.0515059 -0.00401479 -0.00836923 -0.00617333 162 MET   B C    
3633 O  O    . MET   B 162 ? 0.122459  0.176619 0.0507854 -0.00206994 -0.0151469  -0.00457384 162 MET   B O    
3634 C  CB   . MET   B 162 ? 0.150402  0.196159 0.0533691 -0.00992921 0.00063492  -0.0154968  162 MET   B CB   
3635 C  CG   . MET   B 162 ? 0.174397  0.208706 0.06452   -0.028136   0.00291195  -0.0145628  162 MET   B CG   
3636 S  SD   . MET   B 162 ? 0.256769  0.248573 0.125906  -0.022936   0.0343911   -0.0296516  162 MET   B SD   
3637 C  CE   . MET   B 162 ? 0.201582  0.221376 0.073318  -0.0285816  0.0627796   -0.035773   162 MET   B CE   
3638 N  N    . HIS   B 163 ? 0.110522  0.170334 0.0528902 -0.00369939 -0.00947197 -0.00103987 163 HIS   B N    
3639 C  CA   . HIS   B 163 ? 0.115993  0.174462 0.0486543 -0.00348188 -0.00657205 -0.00268404 163 HIS   B CA   
3640 C  C    . HIS   B 163 ? 0.125741  0.166211 0.0445341 -0.00476446 -0.00508634 -0.00568254 163 HIS   B C    
3641 O  O    . HIS   B 163 ? 0.131281  0.16273  0.0569305 -0.0089565  -0.0157787  -0.0136017  163 HIS   B O    
3642 C  CB   . HIS   B 163 ? 0.121524  0.17528  0.0493829 -0.00206487 -0.00501329 -0.00049258 163 HIS   B CB   
3643 C  CG   . HIS   B 163 ? 0.118065  0.174629 0.0578294 -0.00447221 -0.00782379 0.00015096  163 HIS   B CG   
3644 N  ND1  . HIS   B 163 ? 0.130764  0.179472 0.0655819 -0.00489775 -0.0100091  0.00075688  163 HIS   B ND1  
3645 C  CD2  . HIS   B 163 ? 0.129078  0.176856 0.079264  -0.0029703  -0.00275438 0.00229742  163 HIS   B CD2  
3646 C  CE1  . HIS   B 163 ? 0.123343  0.179574 0.0712776 0.00244126  -0.00166876 -0.00416884 163 HIS   B CE1  
3647 N  NE2  . HIS   B 163 ? 0.13292   0.184729 0.0733929 0.00042411  -0.00573877 -0.00431209 163 HIS   B NE2  
3648 N  N    . HIS   B 164 ? 0.119617  0.182104 0.0457503 -0.00998723 -3.908e-05  -0.0146152  164 HIS   B N    
3649 C  CA   . HIS   B 164 ? 0.124641  0.191851 0.0518028 -0.0167608  -0.00036218 -0.0157772  164 HIS   B CA   
3650 C  C    . HIS   B 164 ? 0.128422  0.201878 0.0634497 -0.0230964  0.00371507  -0.0146171  164 HIS   B C    
3651 O  O    . HIS   B 164 ? 0.144062  0.217557 0.0755403 -0.0371444  0.0127559   -0.0157389  164 HIS   B O    
3652 C  CB   . HIS   B 164 ? 0.124008  0.192566 0.051257  -0.0130217  -0.00479573 -0.0195279  164 HIS   B CB   
3653 C  CG   . HIS   B 164 ? 0.131068  0.191891 0.0463091 -0.00883764 -0.00660304 -0.0179139  164 HIS   B CG   
3654 N  ND1  . HIS   B 164 ? 0.140568  0.193665 0.05185   -0.00668303 -0.00753585 -0.022995   164 HIS   B ND1  
3655 C  CD2  . HIS   B 164 ? 0.143343  0.195871 0.0434285 -0.010392   -0.00719076 -0.0216379  164 HIS   B CD2  
3656 C  CE1  . HIS   B 164 ? 0.135868  0.19591  0.0498555 -0.00311714 -0.00586369 -0.026478   164 HIS   B CE1  
3657 N  NE2  . HIS   B 164 ? 0.148408  0.204888 0.0447942 -0.00256243 -0.00881961 -0.027947   164 HIS   B NE2  
3658 N  N    . MET   B 165 ? 0.124396  0.209695 0.0728532 -0.0197154  0.00695609  -0.0145751  165 MET   B N    
3659 C  CA   . MET   B 165 ? 0.130656  0.238526 0.0797915 -0.0233826  0.00831467  -0.0213174  165 MET   B CA   
3660 C  C    . MET   B 165 ? 0.128203  0.223671 0.0885541 -0.0214572  0.0164592   -0.0186906  165 MET   B C    
3661 O  O    . MET   B 165 ? 0.13932   0.201795 0.0832836 -0.015522   0.0162294   -0.00864544 165 MET   B O    
3662 C  CB   . MET   B 165 ? 0.147123  0.274909 0.088709  -0.0210819  0.00117378  -0.0323353  165 MET   B CB   
3663 C  CG   . MET   B 165 ? 0.174975  0.301471 0.112067  -0.00513923 -0.0236585  -0.0244046  165 MET   B CG   
3664 S  SD   . MET   B 165 ? 0.225646  0.359331 0.184199  -0.0155769  -0.00303414 -0.0133416  165 MET   B SD   
3665 C  CE   . MET   B 165 ? 0.152765  0.361195 0.158039  -0.0178933  -0.0628239  -0.0504822  165 MET   B CE   
3666 N  N    . GLU   B 166 ? 0.136221  0.23865  0.0979651 -0.0294056  0.0160696   -0.0120167  166 GLU   B N    
3667 C  CA   . GLU   B 166 ? 0.130329  0.241581 0.0913632 -0.0227172  0.013813    -0.00686801 166 GLU   B CA   
3668 C  C    . GLU   B 166 ? 0.13154   0.259405 0.0952659 -0.026358   0.00820844  0.00161337  166 GLU   B C    
3669 O  O    . GLU   B 166 ? 0.13563   0.283747 0.119917  -0.0255654  -0.00029723 -0.0181375  166 GLU   B O    
3670 C  CB   . GLU   B 166 ? 0.13134   0.246118 0.102576  -0.0203074  0.0132378   -0.00036432 166 GLU   B CB   
3671 C  CG   . GLU   B 166 ? 0.134392  0.253347 0.109079  -0.0186577  0.0119598   -0.00522518 166 GLU   B CG   
3672 C  CD   . GLU   B 166 ? 0.144055  0.268444 0.108816  -0.0189607  0.0182481   -0.00141546 166 GLU   B CD   
3673 O  OE1  . GLU   B 166 ? 0.153025  0.297837 0.13342   -0.0208553  0.0301717   0.00203276  166 GLU   B OE1  
3674 O  OE2  . GLU   B 166 ? 0.137998  0.26646  0.0996758 -0.0186558  0.0296105   -0.00511943 166 GLU   B OE2  
3675 N  N    . LEU   B 167 ? 0.138141  0.265493 0.104586  -0.0218859  -0.00980718 0.00352776  167 LEU   B N    
3676 C  CA   . LEU   B 167 ? 0.143465  0.287749 0.126157  -0.0190044  -0.012397   0.0120795   167 LEU   B CA   
3677 C  C    . LEU   B 167 ? 0.148761  0.321644 0.149283  -0.0103699  -0.00235937 0.0265933   167 LEU   B C    
3678 O  O    . LEU   B 167 ? 0.155029  0.310947 0.147431  -0.0016846  0.00422437  0.0280856   167 LEU   B O    
3679 C  CB   . LEU   B 167 ? 0.158752  0.290784 0.130732  -0.0146169  -0.0242639  0.0215483   167 LEU   B CB   
3680 C  CG   . LEU   B 167 ? 0.17284   0.298381 0.142211  -0.0237435  -0.017925   0.0197749   167 LEU   B CG   
3681 C  CD1  . LEU   B 167 ? 0.173565  0.295788 0.144209  -0.0230696  -0.0239867  0.024999    167 LEU   B CD1  
3682 C  CD2  . LEU   B 167 ? 0.212783  0.322251 0.15006   -0.0350807  -0.0303207  0.0220154   167 LEU   B CD2  
3683 N  N    . PRO   B 168 ? 0.147109  0.369284 0.176102  -0.0084059  0.00570042  0.0373169   168 PRO   B N    
3684 C  CA   . PRO   B 168 ? 0.163622  0.39276  0.194545  -0.00645403 0.0202862   0.0505109   168 PRO   B CA   
3685 C  C    . PRO   B 168 ? 0.171776  0.388362 0.188309  -0.00063471 0.0456588   0.0448561   168 PRO   B C    
3686 O  O    . PRO   B 168 ? 0.217916  0.417905 0.220107  -0.0145129  0.0603036   0.0816808   168 PRO   B O    
3687 C  CB   . PRO   B 168 ? 0.16865   0.413005 0.225792  -0.00679006 0.0108245   0.0404977   168 PRO   B CB   
3688 C  CG   . PRO   B 168 ? 0.174256  0.420516 0.225982  -0.00842802 -0.00060702 0.0478399   168 PRO   B CG   
3689 C  CD   . PRO   B 168 ? 0.164729  0.395161 0.211929  -0.00131399 -0.00880814 0.0452853   168 PRO   B CD   
3690 N  N    . THR   B 169 ? 0.16863   0.366693 0.178833  0.0111556   0.029405    0.0338727   169 THR   B N    
3691 C  CA   . THR   B 169 ? 0.190417  0.351679 0.166651  0.0282389   0.0345175   0.0227786   169 THR   B CA   
3692 C  C    . THR   B 169 ? 0.202396  0.322997 0.124184  0.0258598   0.0175721   0.00474047  169 THR   B C    
3693 O  O    . THR   B 169 ? 0.247359  0.34826  0.12445   0.0283439   0.0032634   -0.00793937 169 THR   B O    
3694 C  CB   . THR   B 169 ? 0.207866  0.36545  0.217892  0.0366391   0.0256075   0.0292738   169 THR   B CB   
3695 O  OG1  . THR   B 169 ? 0.193178  0.369903 0.195393  0.0389718   0.00347312  0.0391343   169 THR   B OG1  
3696 C  CG2  . THR   B 169 ? 0.231921  0.373945 0.253352  0.0528506   0.0250447   0.0341265   169 THR   B CG2  
3697 N  N    . GLY   B 170 ? 0.180054  0.3021   0.101098  0.0180626   0.0114279   0.0139692   170 GLY   B N    
3698 C  CA   . GLY   B 170 ? 0.167617  0.2871   0.0942344 0.0187086   0.0247209   0.00829892  170 GLY   B CA   
3699 C  C    . GLY   B 170 ? 0.168097  0.273411 0.0892974 0.0156009   0.013887    0.012488    170 GLY   B C    
3700 O  O    . GLY   B 170 ? 0.173002  0.304883 0.14211   0.0107435   -0.00155663 0.044133    170 GLY   B O    
3701 N  N    . VAL   B 171 ? 0.147878  0.247183 0.0787431 0.0187367   0.0114934   0.0044473   171 VAL   B N    
3702 C  CA   . VAL   B 171 ? 0.154269  0.22907  0.0667728 0.00733998  0.00888422  -0.00277681 171 VAL   B CA   
3703 C  C    . VAL   B 171 ? 0.150912  0.209351 0.0706887 -0.00307201 0.00123389  -0.00706519 171 VAL   B C    
3704 O  O    . VAL   B 171 ? 0.136755  0.21472  0.0930313 -0.0109179  0.00623392  -0.00459878 171 VAL   B O    
3705 C  CB   . VAL   B 171 ? 0.159018  0.230169 0.0679185 0.00929218  0.0142424   -0.00318681 171 VAL   B CB   
3706 C  CG1  . VAL   B 171 ? 0.18138   0.234638 0.0777612 0.015757    0.01268     -0.0137597  171 VAL   B CG1  
3707 C  CG2  . VAL   B 171 ? 0.159044  0.227864 0.0788463 0.00942276  0.0142438   0.0082656   171 VAL   B CG2  
3708 N  N    . HIS   B 172 ? 0.15661   0.19676  0.0639284 -0.00579773 0.002505    -0.00667972 172 HIS   B N    
3709 C  CA   . HIS   B 172 ? 0.151944  0.186001 0.0712775 -0.00650365 0.00592007  -0.00519796 172 HIS   B CA   
3710 C  C    . HIS   B 172 ? 0.146401  0.189552 0.0709376 -0.0125193  0.00402439  -0.00611013 172 HIS   B C    
3711 O  O    . HIS   B 172 ? 0.166241  0.199802 0.0501591 -0.0106874  -0.00262946 -0.00438138 172 HIS   B O    
3712 C  CB   . HIS   B 172 ? 0.146438  0.184324 0.0757148 -0.00588701 0.00852284  0.00059774  172 HIS   B CB   
3713 C  CG   . HIS   B 172 ? 0.150328  0.188927 0.0761681 -0.00197104 0.015844    0.00427228  172 HIS   B CG   
3714 N  ND1  . HIS   B 172 ? 0.156527  0.193846 0.0858989 -0.00116237 0.00638687  0.00871058  172 HIS   B ND1  
3715 C  CD2  . HIS   B 172 ? 0.158229  0.196573 0.0721842 -0.00262948 0.0118049   0.0058002   172 HIS   B CD2  
3716 C  CE1  . HIS   B 172 ? 0.157796  0.194104 0.0867926 -0.00657467 0.00900131  0.00664421  172 HIS   B CE1  
3717 N  NE2  . HIS   B 172 ? 0.159184  0.205369 0.0706334 -0.00370105 0.0119483   0.00368766  172 HIS   B NE2  
3718 N  N    . ALA   B 173 ? 0.15046   0.192508 0.0715498 -0.0137192  0.00739319  -0.00719455 173 ALA   B N    
3719 C  CA   . ALA   B 173 ? 0.153047  0.195679 0.0750389 -0.00738045 0.0103415   -0.00617932 173 ALA   B CA   
3720 C  C    . ALA   B 173 ? 0.135231  0.186376 0.0644939 -0.007923   -0.00027291 -0.00400215 173 ALA   B C    
3721 O  O    . ALA   B 173 ? 0.148055  0.184233 0.0551992 -0.00748709 0.00876375  -0.0115319  173 ALA   B O    
3722 C  CB   . ALA   B 173 ? 0.157944  0.215039 0.0794741 -0.00105536 0.0129501   -0.00884593 173 ALA   B CB   
3723 N  N    . GLY   B 174 ? 0.133702  0.192596 0.0634168 -0.00639227 -0.00349325 -0.00062708 174 GLY   B N    
3724 C  CA   . GLY   B 174 ? 0.129211  0.189313 0.062708  -0.00456599 -0.00710454 -0.00278561 174 GLY   B CA   
3725 C  C    . GLY   B 174 ? 0.126407  0.179886 0.0590642 -0.00223126 -0.00611198 -0.0033542  174 GLY   B C    
3726 O  O    . GLY   B 174 ? 0.125711  0.193837 0.0623217 0.00278029  0.013673    -0.00492043 174 GLY   B O    
3727 N  N    . THR   B 175 ? 0.124763  0.180429 0.0620618 -0.00087548 -0.00599505 0.00662781  175 THR   B N    
3728 C  CA   . THR   B 175 ? 0.126578  0.184915 0.0541709 -0.00034182 -0.0118434  0.00591595  175 THR   B CA   
3729 C  C    . THR   B 175 ? 0.122905  0.182308 0.057936  0.00272304  -0.00945629 0.0122554   175 THR   B C    
3730 O  O    . THR   B 175 ? 0.119629  0.186415 0.0584199 -0.00299167 -0.0177254  0.0154222   175 THR   B O    
3731 C  CB   . THR   B 175 ? 0.138901  0.1904   0.0575329 -0.00107064 -0.0132858  0.00155112  175 THR   B CB   
3732 O  OG1  . THR   B 175 ? 0.153913  0.186295 0.0488596 0.00239446  -0.0163763  -0.00049978 175 THR   B OG1  
3733 C  CG2  . THR   B 175 ? 0.13813   0.201023 0.0531074 -0.00024918 -0.0210057  -0.0011069  175 THR   B CG2  
3734 N  N    . ASP   B 176 ? 0.118055  0.176453 0.066549  0.00347789  -0.00496012 0.0149224   176 ASP   B N    
3735 C  CA   . ASP   B 176 ? 0.119806  0.186696 0.0837185 0.00306563  -0.00104503 0.00939583  176 ASP   B CA   
3736 C  C    . ASP   B 176 ? 0.122649  0.185429 0.0709639 -0.00072379 0.00176756  0.00792488  176 ASP   B C    
3737 O  O    . ASP   B 176 ? 0.13751   0.196227 0.0663605 -0.00885053 0.0105993   -0.00078698 176 ASP   B O    
3738 C  CB   . ASP   B 176 ? 0.128918  0.191112 0.0919887 0.0027184   0.0003111   0.0100343   176 ASP   B CB   
3739 C  CG   . ASP   B 176 ? 0.143188  0.193199 0.0959374 0.00179857  -9.914e-05  0.011868    176 ASP   B CG   
3740 O  OD1  . ASP   B 176 ? 0.168769  0.206629 0.0885114 0.00579288  0.00380358  0.00532752  176 ASP   B OD1  
3741 O  OD2  . ASP   B 176 ? 0.165967  0.203141 0.115205  0.00260164  -0.00188508 0.022545    176 ASP   B OD2  
3742 N  N    . LEU   B 177 ? 0.11946   0.199225 0.0729451 0.00236336  0.00137529  0.00094215  177 LEU   B N    
3743 C  CA   . LEU   B 177 ? 0.132977  0.210577 0.0863937 0.0117332   -0.00597058 0.00104039  177 LEU   B CA   
3744 C  C    . LEU   B 177 ? 0.149724  0.2254   0.0903123 0.0171094   -0.0074139  -0.0123608  177 LEU   B C    
3745 O  O    . LEU   B 177 ? 0.191768  0.234659 0.110005  0.0363899   -0.0247784  -0.0365749  177 LEU   B O    
3746 C  CB   . LEU   B 177 ? 0.130532  0.221993 0.101056  0.0138606   -0.00441569 0.00288722  177 LEU   B CB   
3747 C  CG   . LEU   B 177 ? 0.133305  0.232648 0.103917  0.0141624   -0.00803396 0.00288663  177 LEU   B CG   
3748 C  CD1  . LEU   B 177 ? 0.152166  0.238922 0.128333  0.0136716   -0.0120779  0.0137304   177 LEU   B CD1  
3749 C  CD2  . LEU   B 177 ? 0.135022  0.250704 0.104147  0.0177385   -0.00711971 0.00185337  177 LEU   B CD2  
3750 N  N    . GLU   B 178 ? 0.147989  0.246827 0.0722476 0.0227203   -0.0107506  -0.00672305 178 GLU   B N    
3751 C  CA   . GLU   B 178 ? 0.164573  0.267361 0.0774867 0.0196485   -0.0160741  -0.00760853 178 GLU   B CA   
3752 C  C    . GLU   B 178 ? 0.163314  0.259555 0.0690911 0.0216779   -0.0181318  -0.010614   178 GLU   B C    
3753 O  O    . GLU   B 178 ? 0.180423  0.282092 0.0668599 0.0307509   -0.022561   -0.0189625  178 GLU   B O    
3754 C  CB   . GLU   B 178 ? 0.194686  0.295186 0.094148  0.0175517   -0.0127451  0.00962406  178 GLU   B CB   
3755 C  CG   . GLU   B 178 ? 0.218733  0.329037 0.127216  0.0102738   -0.00465212 0.0115982   178 GLU   B CG   
3756 C  CD   . GLU   B 178 ? 0.279908  0.361802 0.188881  0.00305731  0.00235433  0.0319312   178 GLU   B CD   
3757 O  OE1  . GLU   B 178 ? 0.346798  0.382353 0.268788  0.0145841   0.0239797   0.0418836   178 GLU   B OE1  
3758 O  OE2  . GLU   B 178 ? 0.341096  0.445673 0.213504  -0.0289497  0.0273405   0.0472418   178 GLU   B OE2  
3759 N  N    . GLY   B 179 ? 0.144805  0.256863 0.0688316 0.0184916   -0.0177971  -0.0150637  179 GLY   B N    
3760 C  CA   . GLY   B 179 ? 0.153824  0.236593 0.0697054 0.0119746   -0.0192605  -0.015789   179 GLY   B CA   
3761 C  C    . GLY   B 179 ? 0.145815  0.224536 0.0685239 0.00480018  -0.015576   -0.0101302  179 GLY   B C    
3762 O  O    . GLY   B 179 ? 0.136021  0.229041 0.0589163 0.00563369  -0.016848   -0.015441   179 GLY   B O    
3763 N  N    . ASN   B 180 ? 0.142034  0.217027 0.0587977 0.00660971  -0.0124995  -0.00635657 180 ASN   B N    
3764 C  CA   . ASN   B 180 ? 0.151407  0.22326  0.0628048 0.00856853  -0.0146043  -0.0116437  180 ASN   B CA   
3765 C  C    . ASN   B 180 ? 0.13643   0.216979 0.0655798 0.00592038  -0.00625357 -0.00438498 180 ASN   B C    
3766 O  O    . ASN   B 180 ? 0.131753  0.205467 0.0661199 0.00493335  -0.00483513 0.00088353  180 ASN   B O    
3767 C  CB   . ASN   B 180 ? 0.167625  0.240319 0.0793652 0.0106974   -0.0166268  -0.0070617  180 ASN   B CB   
3768 C  CG   . ASN   B 180 ? 0.198454  0.282157 0.0870968 0.00960383  -0.010074   -0.00466555 180 ASN   B CG   
3769 O  OD1  . ASN   B 180 ? 0.248099  0.35124  0.0908791 0.0149809   -0.0399044  -0.01651    180 ASN   B OD1  
3770 N  ND2  . ASN   B 180 ? 0.20079   0.300658 0.102258  0.00635679  -0.0116352  -8.666e-05  180 ASN   B ND2  
3771 N  N    . PHE   B 181 ? 0.127522  0.221761 0.0577952 0.00967398  -0.0172526  -0.00842753 181 PHE   B N    
3772 C  CA   . PHE   B 181 ? 0.122071  0.2165   0.0635565 0.00570878  -0.00860627 -0.00403071 181 PHE   B CA   
3773 C  C    . PHE   B 181 ? 0.122066  0.206298 0.0745114 0.0111138   -0.0101442  0.00031742  181 PHE   B C    
3774 O  O    . PHE   B 181 ? 0.133608  0.203356 0.0788838 0.0163435   -0.00382287 0.00405928  181 PHE   B O    
3775 C  CB   . PHE   B 181 ? 0.125491  0.220519 0.0716263 -0.00335765 -0.0128112  -0.00748441 181 PHE   B CB   
3776 C  CG   . PHE   B 181 ? 0.127538  0.217989 0.0751124 -0.0125336  -0.0124688  -0.00972883 181 PHE   B CG   
3777 C  CD1  . PHE   B 181 ? 0.137115  0.226    0.0753405 -0.0155002  -0.00978891 -0.0144447  181 PHE   B CD1  
3778 C  CD2  . PHE   B 181 ? 0.130831  0.220391 0.0741597 -0.0181969  -0.0174595  -0.00869126 181 PHE   B CD2  
3779 C  CE1  . PHE   B 181 ? 0.129507  0.223193 0.0717539 -0.0212103  -0.0065096  -0.00994297 181 PHE   B CE1  
3780 C  CE2  . PHE   B 181 ? 0.140809  0.222472 0.0765776 -0.021498   -0.0195602  -0.00819984 181 PHE   B CE2  
3781 C  CZ   . PHE   B 181 ? 0.155261  0.225251 0.0785785 -0.0213728  -0.00862188 -0.00808304 181 PHE   B CZ   
3782 N  N    . TYR   B 182 ? 0.119499  0.195368 0.0715243 0.0132044   -0.0109705  -0.00251795 182 TYR   B N    
3783 C  CA   . TYR   B 182 ? 0.121489  0.199431 0.0729661 0.0144519   -0.0141659  -0.00704567 182 TYR   B CA   
3784 C  C    . TYR   B 182 ? 0.129907  0.202172 0.0795264 0.00819226  -0.00543711 -0.0137543  182 TYR   B C    
3785 O  O    . TYR   B 182 ? 0.142852  0.213787 0.109226  0.00385864  -0.00922105 -0.00882526 182 TYR   B O    
3786 C  CB   . TYR   B 182 ? 0.114522  0.196668 0.078911  0.013218    -0.0150728  -0.00827799 182 TYR   B CB   
3787 C  CG   . TYR   B 182 ? 0.111989  0.187312 0.0684585 0.0137253   -0.0135109  -0.00509775 182 TYR   B CG   
3788 C  CD1  . TYR   B 182 ? 0.112242  0.184121 0.0761063 0.0174063   -0.0142353  -0.00013967 182 TYR   B CD1  
3789 C  CD2  . TYR   B 182 ? 0.114565  0.186471 0.0661502 0.0131997   -0.0104255  -0.00561192 182 TYR   B CD2  
3790 C  CE1  . TYR   B 182 ? 0.118765  0.188312 0.0798049 0.0107559   -0.00337977 0.00215672  182 TYR   B CE1  
3791 C  CE2  . TYR   B 182 ? 0.117667  0.190093 0.0693329 0.0121238   -0.00295949 -0.00250766 182 TYR   B CE2  
3792 C  CZ   . TYR   B 182 ? 0.119394  0.189294 0.0709805 0.0119503   -0.00610209 -0.00326523 182 TYR   B CZ   
3793 O  OH   . TYR   B 182 ? 0.12019   0.193208 0.081542  0.00148764  -0.00473915 -0.0016737  182 TYR   B OH   
3794 N  N    . GLY   B 183 ? 0.125869  0.208685 0.080459  0.00955581  -0.00572157 -0.0131502  183 GLY   B N    
3795 C  CA   . GLY   B 183 ? 0.120113  0.214985 0.0916255 0.00966834  -0.0184402  -0.0149363  183 GLY   B CA   
3796 C  C    . GLY   B 183 ? 0.126712  0.2208   0.0960703 0.0143179   -0.0216757  -0.0208866  183 GLY   B C    
3797 O  O    . GLY   B 183 ? 0.126533  0.232553 0.0846306 0.00406002  -0.0157198  -0.0223624  183 GLY   B O    
3798 N  N    . PRO   B 184 ? 0.117056  0.228002 0.101659  0.0146465   -0.0224374  -0.0115839  184 PRO   B N    
3799 C  CA   . PRO   B 184 ? 0.124705  0.241373 0.118271  0.0114871   -0.0278122  -0.00911809 184 PRO   B CA   
3800 C  C    . PRO   B 184 ? 0.145246  0.237209 0.128053  0.00799766  -0.0230098  -0.0113219  184 PRO   B C    
3801 O  O    . PRO   B 184 ? 0.156901  0.248012 0.237482  0.0150465   -0.0200108  0.00260224  184 PRO   B O    
3802 C  CB   . PRO   B 184 ? 0.137322  0.24968  0.144158  0.0167381   -0.0236281  -0.00325157 184 PRO   B CB   
3803 C  CG   . PRO   B 184 ? 0.13373   0.245943 0.138801  0.0185507   -0.0117873  -0.00695221 184 PRO   B CG   
3804 C  CD   . PRO   B 184 ? 0.13252   0.238121 0.116275  0.0208857   -0.0174909  -0.0116517  184 PRO   B CD   
3805 N  N    . PHE   B 185 ? 0.123181  0.236299 0.0857417 5.145e-05   -0.0118025  -0.00866358 185 PHE   B N    
3806 C  CA   . PHE   B 185 ? 0.1266    0.233379 0.0868398 -0.0015536  -0.0127212  -0.0103738  185 PHE   B CA   
3807 C  C    . PHE   B 185 ? 0.144328  0.236207 0.0862681 0.00098322  -0.00524854 -0.00843426 185 PHE   B C    
3808 O  O    . PHE   B 185 ? 0.158841  0.256104 0.0987636 -0.00074414 0.00931105  -0.00915776 185 PHE   B O    
3809 C  CB   . PHE   B 185 ? 0.131651  0.240943 0.0886333 -0.00252352 -0.0070693  0.00364525  185 PHE   B CB   
3810 C  CG   . PHE   B 185 ? 0.136206  0.2434   0.0877503 -0.0026264  -0.0169428  0.00265352  185 PHE   B CG   
3811 C  CD1  . PHE   B 185 ? 0.139666  0.259179 0.0904887 -0.00095718 -0.0135247  -0.00050151 185 PHE   B CD1  
3812 C  CD2  . PHE   B 185 ? 0.147839  0.246371 0.0974454 -0.0103147  -0.0132409  -0.00287046 185 PHE   B CD2  
3813 C  CE1  . PHE   B 185 ? 0.149258  0.263894 0.095349  0.00163497  -0.00887337 -0.00272561 185 PHE   B CE1  
3814 C  CE2  . PHE   B 185 ? 0.158571  0.25438  0.0818548 -0.00384202 -0.0188056  0.00420322  185 PHE   B CE2  
3815 C  CZ   . PHE   B 185 ? 0.163628  0.254717 0.0819369 -2.136e-05  -0.0177665  0.00149929  185 PHE   B CZ   
3816 N  N    . VAL   B 186 ? 0.137239  0.23818  0.0725458 -0.00036773 -0.0103625  -0.00315409 186 VAL   B N    
3817 C  CA   . VAL   B 186 ? 0.14406   0.238845 0.0816563 0.0062356   -0.00614451 -0.00789838 186 VAL   B CA   
3818 C  C    . VAL   B 186 ? 0.133349  0.233979 0.077489  0.00697561  0.00090605  -0.00733375 186 VAL   B C    
3819 O  O    . VAL   B 186 ? 0.133203  0.246808 0.0747683 0.00984293  0.00703726  -0.00768532 186 VAL   B O    
3820 C  CB   . VAL   B 186 ? 0.160905  0.253159 0.093377  0.0113805   -0.0182479  0.00095325  186 VAL   B CB   
3821 C  CG1  . VAL   B 186 ? 0.176621  0.264754 0.10026   0.0157327   -0.0112813  0.0068181   186 VAL   B CG1  
3822 C  CG2  . VAL   B 186 ? 0.162304  0.261526 0.0959447 0.00668722  -0.0269206  0.00469005  186 VAL   B CG2  
3823 N  N    . ASP   B 187 ? 0.144838  0.224205 0.0857769 0.0108639   0.00864388  -0.0105999  187 ASP   B N    
3824 C  CA   . ASP   B 187 ? 0.147303  0.221918 0.0832879 0.00892265  0.00343287  -0.015012   187 ASP   B CA   
3825 C  C    . ASP   B 187 ? 0.15312   0.228485 0.107321  0.00307035  0.00706148  -0.0211302  187 ASP   B C    
3826 O  O    . ASP   B 187 ? 0.159052  0.22147  0.101792  -0.00450926 0.010932    -0.0117051  187 ASP   B O    
3827 C  CB   . ASP   B 187 ? 0.144536  0.230891 0.0937255 0.0105546   -0.00668432 -0.0149233  187 ASP   B CB   
3828 C  CG   . ASP   B 187 ? 0.144236  0.235897 0.0933798 0.0166128   -0.0101852  -0.0163208  187 ASP   B CG   
3829 O  OD1  . ASP   B 187 ? 0.150052  0.253141 0.101506  0.0151866   -0.0145697  -0.011707   187 ASP   B OD1  
3830 O  OD2  . ASP   B 187 ? 0.145515  0.245558 0.0785556 0.0239583   -0.0104095  -0.0229967  187 ASP   B OD2  
3831 N  N    . ARG   B 188 ? 0.156945  0.248492 0.134575  -0.00624777 0.0154651   -0.025845   188 ARG   B N    
3832 C  CA   . ARG   B 188 ? 0.169421  0.267926 0.14471   -0.0154127  0.0127743   -0.030989   188 ARG   B CA   
3833 C  C    . ARG   B 188 ? 0.167197  0.280901 0.149036  -0.0157321  0.0144408   -0.0335632  188 ARG   B C    
3834 O  O    . ARG   B 188 ? 0.179686  0.269396 0.173007  -0.0247235  0.00280256  -0.0295762  188 ARG   B O    
3835 C  CB   . ARG   B 188 ? 0.190728  0.295738 0.165786  -0.0101466  0.00657209  -0.031645   188 ARG   B CB   
3836 C  CG   . ARG   B 188 ? 0.215384  0.330164 0.177802  -0.0199412  -0.00434825 -0.0252221  188 ARG   B CG   
3837 C  CD   . ARG   B 188 ? 0.289284  0.396128 0.215116  -0.00887921 -0.0207993  -0.0142434  188 ARG   B CD   
3838 N  NE   . ARG   B 188 ? 0.343404  0.436754 0.223331  0.037349    -0.0268054  -0.0226955  188 ARG   B NE   
3839 C  CZ   . ARG   B 188 ? 0.390918  0.451443 0.268809  0.0559795   0.0184218   0.00580328  188 ARG   B CZ   
3840 N  NH1  . ARG   B 188 ? 0.397893  0.500825 0.313894  0.071173    0.0384556   0.00189686  188 ARG   B NH1  
3841 N  NH2  . ARG   B 188 ? 0.394575  0.438416 0.221355  0.0859278   0.0192272   -0.00572238 188 ARG   B NH2  
3842 N  N    . GLN   B 189 ? 0.180373  0.303791 0.154751  -0.0220251  0.0233177   -0.0325909  189 GLN   B N    
3843 C  CA   . GLN   B 189 ? 0.181155  0.331496 0.188171  -0.0241981  0.0449452   -0.0407581  189 GLN   B CA   
3844 C  C    . GLN   B 189 ? 0.173529  0.331433 0.232835  -0.0293429  0.0549056   -0.0534937  189 GLN   B C    
3845 O  O    . GLN   B 189 ? 0.217098  0.343747 0.248681  -0.0402782  0.0406379   -0.0611992  189 GLN   B O    
3846 C  CB   . GLN   B 189 ? 0.212416  0.350715 0.196395  -0.0291146  0.0447514   -0.0267368  189 GLN   B CB   
3847 C  CG   . GLN   B 189 ? 0.250496  0.389774 0.209437  -0.0272748  0.0538539   -0.0158423  189 GLN   B CG   
3848 C  CD   . GLN   B 189 ? 0.306286  0.42212  0.243071  -0.0286026  0.0270671   -0.00541864 189 GLN   B CD   
3849 O  OE1  . GLN   B 189 ? 0.331404  0.468597 0.300726  -0.0265691  0.0215325   0.0391407   189 GLN   B OE1  
3850 N  NE2  . GLN   B 189 ? 0.339211  0.450512 0.240334  -0.0084151  0.0533348   -0.0090695  189 GLN   B NE2  
3851 N  N    . THR   B 190 ? 0.180673  0.340401 0.291655  -0.026265   0.0617616   -0.0827946  190 THR   B N    
3852 C  CA   . THR   B 190 ? 0.182656  0.36204  0.333497  -0.0259633  0.0518219   -0.0998785  190 THR   B CA   
3853 C  C    . THR   B 190 ? 0.178854  0.364627 0.318402  -0.0384795  0.0659053   -0.100766   190 THR   B C    
3854 O  O    . THR   B 190 ? 0.175111  0.39458  0.294881  -0.0476105  0.0866147   -0.101372   190 THR   B O    
3855 C  CB   . THR   B 190 ? 0.195608  0.362836 0.36707   -0.0222714  0.0457993   -0.103518   190 THR   B CB   
3856 O  OG1  . THR   B 190 ? 0.218375  0.381438 0.400551  0.0037815   0.0265161   -0.116555   190 THR   B OG1  
3857 C  CG2  . THR   B 190 ? 0.227947  0.365203 0.389856  -0.0247173  0.0387938   -0.106953   190 THR   B CG2  
3858 N  N    . ALA   B 191 ? 0.19533   0.364369 0.347592  -0.0386114  0.068068    -0.111445   191 ALA   B N    
3859 C  CA   . ALA   B 191 ? 0.204602  0.362021 0.30335   -0.0219173  0.0688287   -0.0945512  191 ALA   B CA   
3860 C  C    . ALA   B 191 ? 0.183504  0.339416 0.234543  -0.0134567  0.0422752   -0.0716709  191 ALA   B C    
3861 O  O    . ALA   B 191 ? 0.178588  0.373016 0.247289  -0.00369812 -0.00529908 -0.0645343  191 ALA   B O    
3862 C  CB   . ALA   B 191 ? 0.21253   0.372562 0.344658  -0.0192661  0.0754468   -0.0984131  191 ALA   B CB   
3863 N  N    . GLN   B 192 ? 0.189978  0.316521 0.180491  -0.0171561  0.045102    -0.052618   192 GLN   B N    
3864 C  CA   . GLN   B 192 ? 0.180305  0.307879 0.141999  -0.0134989  0.0270709   -0.0463722  192 GLN   B CA   
3865 C  C    . GLN   B 192 ? 0.194017  0.329883 0.141924  -0.0120209  0.0220279   -0.0511531  192 GLN   B C    
3866 O  O    . GLN   B 192 ? 0.251665  0.354836 0.144556  0.00233173  0.00748361  -0.0344395  192 GLN   B O    
3867 C  CB   . GLN   B 192 ? 0.175825  0.287665 0.122018  -0.0123058  0.0201657   -0.0346228  192 GLN   B CB   
3868 C  CG   . GLN   B 192 ? 0.161952  0.282668 0.123384  -0.0154455  0.0072374   -0.0317797  192 GLN   B CG   
3869 C  CD   . GLN   B 192 ? 0.149701  0.261859 0.116888  -0.0185181  0.00047568  -0.0261816  192 GLN   B CD   
3870 O  OE1  . GLN   B 192 ? 0.157726  0.256933 0.105329  -0.0165274  -0.00429563 -0.0202002  192 GLN   B OE1  
3871 N  NE2  . GLN   B 192 ? 0.154952  0.272936 0.136276  -0.0130632  0.00812116  -0.0175549  192 GLN   B NE2  
3872 N  N    . ALA   B 193 ? 0.184989  0.340699 0.126236  -0.0280297  0.0265389   -0.0759967  193 ALA   B N    
3873 C  CA   . ALA   B 193 ? 0.212707  0.368663 0.142759  -0.0274228  0.0196781   -0.0919762  193 ALA   B CA   
3874 C  C    . ALA   B 193 ? 0.223747  0.381649 0.207561  -0.0255442  0.0273069   -0.108094   193 ALA   B C    
3875 O  O    . ALA   B 193 ? 0.253964  0.376117 0.226389  -0.0585907  0.0675426   -0.113593   193 ALA   B O    
3876 C  CB   . ALA   B 193 ? 0.209174  0.38295  0.152407  -0.0307772  0.0302864   -0.0848075  193 ALA   B CB   
3877 N  N    . ALA   B 194 ? 0.222601  0.397411 0.260939  -0.00667617 0.00444263  -0.136205   194 ALA   B N    
3878 C  CA   . ALA   B 194 ? 0.227825  0.405541 0.32806   0.00611071  -0.011285   -0.143965   194 ALA   B CA   
3879 C  C    . ALA   B 194 ? 0.198666  0.401513 0.28661   0.0112094   -0.0265385  -0.142469   194 ALA   B C    
3880 O  O    . ALA   B 194 ? 0.20021   0.418832 0.303097  0.0354515   -0.0131036  -0.155183   194 ALA   B O    
3881 C  CB   . ALA   B 194 ? 0.230939  0.426531 0.372898  0.0156277   -0.0304317  -0.141768   194 ALA   B CB   
3882 N  N    . GLY   B 195 ? 0.200334  0.390469 0.276269  0.0295539   -0.0322941  -0.122496   195 GLY   B N    
3883 C  CA   . GLY   B 195 ? 0.171322  0.369333 0.22444   0.0325397   -0.0457395  -0.101412   195 GLY   B CA   
3884 C  C    . GLY   B 195 ? 0.171264  0.339567 0.207508  0.0331606   -0.0386253  -0.0843336  195 GLY   B C    
3885 O  O    . GLY   B 195 ? 0.159576  0.321398 0.239671  0.0342496   -0.0452756  -0.091244   195 GLY   B O    
3886 N  N    A THR   B 196 ? 0.18501   0.332481 0.204683  0.0339421   -0.041823   -0.0706337  196 THR   B N    
3887 N  N    B THR   B 196 ? 0.165752  0.327941 0.192354  0.0324235   -0.0406334  -0.071324   196 THR   B N    
3888 C  CA   A THR   B 196 ? 0.201185  0.340809 0.202645  0.0215257   -0.037607   -0.0655073  196 THR   B CA   
3889 C  CA   B THR   B 196 ? 0.165512  0.326115 0.187502  0.0274468   -0.030619   -0.0697205  196 THR   B CA   
3890 C  C    A THR   B 196 ? 0.189413  0.327965 0.18642   0.0249914   -0.0308421  -0.0502211  196 THR   B C    
3891 C  C    B THR   B 196 ? 0.16723   0.319357 0.183003  0.0239144   -0.0256221  -0.0522325  196 THR   B C    
3892 O  O    A THR   B 196 ? 0.215016  0.349985 0.230227  0.0235934   -0.0361492  -0.0131204  196 THR   B O    
3893 O  O    B THR   B 196 ? 0.190781  0.338766 0.221575  0.022713    -0.0303792  -0.0125018  196 THR   B O    
3894 C  CB   A THR   B 196 ? 0.224705  0.350922 0.22215   0.0245425   -0.0350711  -0.0676368  196 THR   B CB   
3895 C  CB   B THR   B 196 ? 0.161738  0.328654 0.187963  0.0267585   -0.0306708  -0.0726798  196 THR   B CB   
3896 O  OG1  A THR   B 196 ? 0.270077  0.369793 0.236341  0.0149204   -0.0404043  -0.0620305  196 THR   B OG1  
3897 O  OG1  B THR   B 196 ? 0.152786  0.325997 0.172842  0.0280355   -0.0241416  -0.0815068  196 THR   B OG1  
3898 C  CG2  A THR   B 196 ? 0.219902  0.351551 0.211266  0.0218021   -0.0382836  -0.0717547  196 THR   B CG2  
3899 C  CG2  B THR   B 196 ? 0.152708  0.329827 0.184482  0.0298483   -0.0279953  -0.0764609  196 THR   B CG2  
3900 N  N    . ASP   B 197 ? 0.163619  0.309836 0.175514  0.0137748   -0.0230391  -0.0539187  197 ASP   B N    
3901 C  CA   . ASP   B 197 ? 0.164435  0.290768 0.174973  0.0109778   -0.0108612  -0.0597247  197 ASP   B CA   
3902 C  C    . ASP   B 197 ? 0.166272  0.282496 0.184125  0.0125459   -0.0140863  -0.0633711  197 ASP   B C    
3903 O  O    . ASP   B 197 ? 0.176663  0.306117 0.204653  0.0163614   -0.0128737  -0.0758586  197 ASP   B O    
3904 C  CB   . ASP   B 197 ? 0.16142   0.297362 0.172774  0.0100308   -0.00796058 -0.0527592  197 ASP   B CB   
3905 C  CG   . ASP   B 197 ? 0.161318  0.297983 0.150236  0.0221338   -0.00551175 -0.0445513  197 ASP   B CG   
3906 O  OD1  . ASP   B 197 ? 0.168562  0.257755 0.145007  0.00997459  -0.0210366  -0.0386143  197 ASP   B OD1  
3907 O  OD2  . ASP   B 197 ? 0.166662  0.328324 0.152407  0.0307035   -0.0179086  -0.0421203  197 ASP   B OD2  
3908 N  N    . THR   B 198 ? 0.160897  0.253063 0.168051  0.0145921   -0.0202027  -0.0671644  198 THR   B N    
3909 C  CA   . THR   B 198 ? 0.159924  0.244197 0.17146   0.0244869   -0.0316159  -0.0543473  198 THR   B CA   
3910 C  C    . THR   B 198 ? 0.157449  0.222456 0.148939  0.0228148   -0.0325138  -0.047725   198 THR   B C    
3911 O  O    . THR   B 198 ? 0.172899  0.234039 0.143326  0.0288347   -0.0473993  -0.0522935  198 THR   B O    
3912 C  CB   . THR   B 198 ? 0.193661  0.267942 0.189754  0.0378301   -0.0310229  -0.0487757  198 THR   B CB   
3913 O  OG1  . THR   B 198 ? 0.234457  0.279499 0.170688  0.0529062   -0.0257437  -0.026394   198 THR   B OG1  
3914 C  CG2  . THR   B 198 ? 0.195517  0.274585 0.207632  0.0398146   -0.0333985  -0.0514037  198 THR   B CG2  
3915 N  N    . THR   B 199 ? 0.149915  0.218682 0.139864  0.0215408   -0.0226715  -0.0454753  199 THR   B N    
3916 C  CA   . THR   B 199 ? 0.14817   0.215191 0.133098  0.01158     -0.024609   -0.0374541  199 THR   B CA   
3917 C  C    . THR   B 199 ? 0.151478  0.205491 0.130456  0.0131099   -0.0281733  -0.0276861  199 THR   B C    
3918 O  O    . THR   B 199 ? 0.148615  0.203211 0.147707  0.00889247  -0.0287937  -0.0156067  199 THR   B O    
3919 C  CB   . THR   B 199 ? 0.154122  0.230733 0.1366    0.0125362   -0.0165843  -0.035835   199 THR   B CB   
3920 O  OG1  . THR   B 199 ? 0.174921  0.247212 0.141249  0.00710852  -0.00864275 -0.0311649  199 THR   B OG1  
3921 C  CG2  . THR   B 199 ? 0.159862  0.244241 0.140256  0.0132623   -0.0169641  -0.0393208  199 THR   B CG2  
3922 N  N    . ILE   B 200 ? 0.149056  0.205418 0.109161  0.00824098  -0.0308323  -0.0229742  200 ILE   B N    
3923 C  CA   . ILE   B 200 ? 0.157814  0.203468 0.0945111 0.00555464  -0.0302586  -0.0186551  200 ILE   B CA   
3924 C  C    . ILE   B 200 ? 0.149965  0.201053 0.0918505 0.00456093  -0.0279382  -0.0111497  200 ILE   B C    
3925 O  O    . ILE   B 200 ? 0.155558  0.200077 0.0906572 0.0124716   -0.0262975  -0.00071688 200 ILE   B O    
3926 C  CB   . ILE   B 200 ? 0.164455  0.207119 0.0962634 0.00396299  -0.0300206  -0.0182953  200 ILE   B CB   
3927 C  CG1  . ILE   B 200 ? 0.177511  0.211869 0.099179  0.00070799  -0.0226794  -0.0207982  200 ILE   B CG1  
3928 C  CG2  . ILE   B 200 ? 0.166747  0.216298 0.0761386 0.00207458  -0.0368601  -0.0160421  200 ILE   B CG2  
3929 C  CD1  . ILE   B 200 ? 0.179812  0.206919 0.100684  0.00038755  -0.0192381  -0.0181064  200 ILE   B CD1  
3930 N  N    . THR   B 201 ? 0.158308  0.195953 0.0925007 0.00055666  -0.0296473  -0.00763157 201 THR   B N    
3931 C  CA   . THR   B 201 ? 0.153565  0.198536 0.0841127 0.00127735  -0.0197334  -0.0078523  201 THR   B CA   
3932 C  C    . THR   B 201 ? 0.154416  0.201122 0.0913735 -0.00183208 -0.0245276  -0.00340686 201 THR   B C    
3933 O  O    . THR   B 201 ? 0.141507  0.205475 0.093732  0.00612566  -0.0255725  -0.00293958 201 THR   B O    
3934 C  CB   . THR   B 201 ? 0.16277   0.203295 0.0963163 -0.00377708 -0.0254034  -0.00101215 201 THR   B CB   
3935 O  OG1  . THR   B 201 ? 0.160546  0.220746 0.10973   -0.00734987 -0.0306464  -0.00994901 201 THR   B OG1  
3936 C  CG2  . THR   B 201 ? 0.180927  0.207432 0.107398  -0.00023956 -0.0295086  0.00156611  201 THR   B CG2  
3937 N  N    . VAL   B 202 ? 0.142455  0.208537 0.0957214 -0.00258336 -0.0183273  0.00023576  202 VAL   B N    
3938 C  CA   . VAL   B 202 ? 0.143896  0.207384 0.0931257 -0.00471061 -0.018895   0.00641251  202 VAL   B CA   
3939 C  C    . VAL   B 202 ? 0.135321  0.201849 0.0883809 -0.00542133 -0.0188817  0.0004009   202 VAL   B C    
3940 O  O    . VAL   B 202 ? 0.142483  0.219069 0.0707595 -0.00876644 -0.024      0.0077337   202 VAL   B O    
3941 C  CB   . VAL   B 202 ? 0.161208  0.223627 0.0984732 -0.00103442 -0.0135041  0.0152452   202 VAL   B CB   
3942 C  CG1  . VAL   B 202 ? 0.174979  0.232452 0.0930575 0.00177135  -0.00311707 0.0115625   202 VAL   B CG1  
3943 C  CG2  . VAL   B 202 ? 0.166424  0.233871 0.103934  0.00301346  -0.0131275  0.0226803   202 VAL   B CG2  
3944 N  N    . ASN   B 203 ? 0.133814  0.192837 0.0753583 -1.578e-05  -0.0266373  -0.00339674 203 ASN   B N    
3945 C  CA   . ASN   B 203 ? 0.144538  0.192403 0.0844485 0.00239878  -0.018431   6.969e-05   203 ASN   B CA   
3946 C  C    . ASN   B 203 ? 0.137768  0.184368 0.0807879 0.0027283   -0.020227   -0.00124439 203 ASN   B C    
3947 O  O    . ASN   B 203 ? 0.12942   0.185277 0.0879191 -0.00300386 -0.0169652  0.0159611   203 ASN   B O    
3948 C  CB   . ASN   B 203 ? 0.132914  0.193596 0.0739175 0.00105234  -0.0173492  -0.0062634  203 ASN   B CB   
3949 C  CG   . ASN   B 203 ? 0.13448   0.201778 0.0769428 0.00058921  -0.0155133  -0.00413082 203 ASN   B CG   
3950 O  OD1  . ASN   B 203 ? 0.148785  0.222432 0.0710768 -0.00206615 -0.0164304  0.00385723  203 ASN   B OD1  
3951 N  ND2  . ASN   B 203 ? 0.136974  0.198098 0.0753632 -0.00215627 -0.00669711 -0.00263965 203 ASN   B ND2  
3952 N  N    . VAL   B 204 ? 0.14465   0.177777 0.0722105 0.0006814   -0.026672   -0.00631686 204 VAL   B N    
3953 C  CA   . VAL   B 204 ? 0.155031  0.169258 0.0746114 0.00152429  -0.0226204  -0.00601991 204 VAL   B CA   
3954 C  C    . VAL   B 204 ? 0.153587  0.168502 0.0738304 -0.00105633 -0.0302094  0.0011078   204 VAL   B C    
3955 O  O    . VAL   B 204 ? 0.15717   0.175437 0.0670419 -0.00767481 -0.0298242  0.00356174  204 VAL   B O    
3956 C  CB   . VAL   B 204 ? 0.160128  0.171993 0.0849693 0.00569966  -0.0202508  -0.00888411 204 VAL   B CB   
3957 C  CG1  . VAL   B 204 ? 0.162739  0.177417 0.0831246 0.00387023  -0.016964   -0.00744986 204 VAL   B CG1  
3958 C  CG2  . VAL   B 204 ? 0.161315  0.172418 0.0887539 0.00794263  -0.0202904  -0.0162013  204 VAL   B CG2  
3959 N  N    . LEU   B 205 ? 0.1643    0.17302  0.0669603 -0.00212012 -0.0338263  0.00669993  205 LEU   B N    
3960 C  CA   . LEU   B 205 ? 0.159781  0.175075 0.0750365 -0.00182133 -0.0308693  0.00598258  205 LEU   B CA   
3961 C  C    . LEU   B 205 ? 0.154058  0.189645 0.0891309 -0.00401926 -0.032617   0.00475731  205 LEU   B C    
3962 O  O    . LEU   B 205 ? 0.14852   0.197562 0.0877592 -0.00791339 -0.0326523  0.00132294  205 LEU   B O    
3963 C  CB   . LEU   B 205 ? 0.173546  0.174734 0.0879288 -0.00636981 -0.0348685  0.0109437   205 LEU   B CB   
3964 C  CG   . LEU   B 205 ? 0.189406  0.180077 0.0908202 0.00042978  -0.0317758  0.0108568   205 LEU   B CG   
3965 C  CD1  . LEU   B 205 ? 0.189428  0.191987 0.0933513 0.00373774  -0.0321681  0.0157013   205 LEU   B CD1  
3966 C  CD2  . LEU   B 205 ? 0.202943  0.181428 0.104552  0.00693697  -0.0238379  0.00577315  205 LEU   B CD2  
3967 N  N    . ALA   B 206 ? 0.146368  0.195874 0.0810676 -0.00773902 -0.0311035  0.00093754  206 ALA   B N    
3968 C  CA   . ALA   B 206 ? 0.139966  0.199544 0.0881676 -0.0050446  -0.0274437  0.00491961  206 ALA   B CA   
3969 C  C    . ALA   B 206 ? 0.133265  0.195746 0.0881003 -0.00593558 -0.025141   0.00328885  206 ALA   B C    
3970 O  O    . ALA   B 206 ? 0.126313  0.218619 0.0910394 -0.00818039 -0.0217665  0.00189596  206 ALA   B O    
3971 C  CB   . ALA   B 206 ? 0.13723   0.202922 0.0959824 0.00029957  -0.0248226  0.00553038  206 ALA   B CB   
3972 N  N    . TRP   B 207 ? 0.13483   0.187759 0.079962  -0.00667474 -0.0249633  0.00248933  207 TRP   B N    
3973 C  CA   . TRP   B 207 ? 0.142463  0.187462 0.0797004 -0.00668346 -0.028691   0.00266167  207 TRP   B CA   
3974 C  C    . TRP   B 207 ? 0.137793  0.181946 0.0758938 -0.00972416 -0.0326945  0.00408746  207 TRP   B C    
3975 O  O    . TRP   B 207 ? 0.142041  0.191664 0.0781884 -0.00406021 -0.0346727  0.00746734  207 TRP   B O    
3976 C  CB   . TRP   B 207 ? 0.157972  0.195478 0.0789824 -0.0136288  -0.0313776  0.00415263  207 TRP   B CB   
3977 C  CG   . TRP   B 207 ? 0.173066  0.202054 0.0846609 -0.0192159  -0.0256386  0.00619177  207 TRP   B CG   
3978 C  CD1  . TRP   B 207 ? 0.178387  0.216359 0.0915464 -0.0138982  -0.0299539  0.00816163  207 TRP   B CD1  
3979 C  CD2  . TRP   B 207 ? 0.179221  0.223699 0.0903744 -0.0269285  -0.0236196  0.00397873  207 TRP   B CD2  
3980 N  NE1  . TRP   B 207 ? 0.20203   0.233439 0.0928783 -0.0216727  -0.0294061  0.013652    207 TRP   B NE1  
3981 C  CE2  . TRP   B 207 ? 0.196329  0.232065 0.0935445 -0.0283028  -0.0232585  0.00353904  207 TRP   B CE2  
3982 C  CE3  . TRP   B 207 ? 0.197062  0.230704 0.0983053 -0.0295146  -0.0129811  -0.00826176 207 TRP   B CE3  
3983 C  CZ2  . TRP   B 207 ? 0.207107  0.254112 0.101733  -0.0322569  -0.0160694  -0.00519349 207 TRP   B CZ2  
3984 C  CZ3  . TRP   B 207 ? 0.20658   0.252196 0.122024  -0.0277177  -0.00531263 -0.0117852  207 TRP   B CZ3  
3985 C  CH2  . TRP   B 207 ? 0.212051  0.261543 0.100479  -0.0302233  -0.0120899  -0.0109378  207 TRP   B CH2  
3986 N  N    . LEU   B 208 ? 0.152627  0.176912 0.0641136 -0.0138385  -0.0324536  0.00201348  208 LEU   B N    
3987 C  CA   . LEU   B 208 ? 0.162668  0.181752 0.0780771 -0.0159114  -0.031816   -0.00083636 208 LEU   B CA   
3988 C  C    . LEU   B 208 ? 0.161732  0.189874 0.0878799 -0.0205547  -0.0350049  -0.00123148 208 LEU   B C    
3989 O  O    . LEU   B 208 ? 0.166299  0.194265 0.0997802 -0.0185709  -0.045139   -0.00665162 208 LEU   B O    
3990 C  CB   . LEU   B 208 ? 0.16312   0.192597 0.0728136 -0.0102775  -0.0316693  0.00332929  208 LEU   B CB   
3991 C  CG   . LEU   B 208 ? 0.163675  0.196994 0.0798889 -0.00909869 -0.0270971  0.00471008  208 LEU   B CG   
3992 C  CD1  . LEU   B 208 ? 0.169577  0.209036 0.0864702 -0.00162177 -0.015678   0.00965904  208 LEU   B CD1  
3993 C  CD2  . LEU   B 208 ? 0.165751  0.203398 0.0895427 -0.011979   -0.0269997  0.00981523  208 LEU   B CD2  
3994 N  N    . TYR   B 209 ? 0.15317   0.20003  0.0981617 -0.0217242  -0.0361074  0.0010564   209 TYR   B N    
3995 C  CA   . TYR   B 209 ? 0.156104  0.20381  0.104302  -0.0321038  -0.0298151  0.00865876  209 TYR   B CA   
3996 C  C    . TYR   B 209 ? 0.139881  0.207751 0.10829   -0.0292677  -0.0285347  0.00904936  209 TYR   B C    
3997 O  O    . TYR   B 209 ? 0.154757  0.229813 0.112605  -0.021577   -0.0478446  0.00947595  209 TYR   B O    
3998 C  CB   . TYR   B 209 ? 0.151548  0.215456 0.108794  -0.0369692  -0.0251895  0.00694775  209 TYR   B CB   
3999 C  CG   . TYR   B 209 ? 0.17256   0.217584 0.125881  -0.041227   -0.0167997  0.0132182   209 TYR   B CG   
4000 C  CD1  . TYR   B 209 ? 0.178341  0.2214   0.136853  -0.0478868  -0.0184627  0.0158326   209 TYR   B CD1  
4001 C  CD2  . TYR   B 209 ? 0.173214  0.214822 0.127602  -0.0434037  -0.021677   0.0096883   209 TYR   B CD2  
4002 C  CE1  . TYR   B 209 ? 0.185755  0.22441  0.141333  -0.0450719  -0.0215625  0.0162426   209 TYR   B CE1  
4003 C  CE2  . TYR   B 209 ? 0.196337  0.217147 0.133487  -0.0479596  -0.0132419  0.0179497   209 TYR   B CE2  
4004 C  CZ   . TYR   B 209 ? 0.197476  0.225204 0.151126  -0.0497451  -0.027304   0.0163667   209 TYR   B CZ   
4005 O  OH   . TYR   B 209 ? 0.232375  0.237619 0.181557  -0.0421559  -0.03098    0.0240892   209 TYR   B OH   
4006 N  N    . ALA   B 210 ? 0.143422  0.214373 0.0994842 -0.0215362  -0.0371283  0.0074116   210 ALA   B N    
4007 C  CA   . ALA   B 210 ? 0.148373  0.214455 0.102939  -0.011978   -0.0283568  0.007089    210 ALA   B CA   
4008 C  C    . ALA   B 210 ? 0.150551  0.203674 0.0995509 -0.00424342 -0.0440141  0.00540255  210 ALA   B C    
4009 O  O    . ALA   B 210 ? 0.151515  0.214982 0.0988056 -0.00022265 -0.045386   0.00778031  210 ALA   B O    
4010 C  CB   . ALA   B 210 ? 0.135398  0.216656 0.0995232 -0.00501443 -0.0299665  0.00821996  210 ALA   B CB   
4011 N  N    . ALA   B 211 ? 0.149355  0.195994 0.0907418 -0.00709581 -0.0522902  -0.00030145 211 ALA   B N    
4012 C  CA   . ALA   B 211 ? 0.174224  0.198641 0.0961611 -0.00460161 -0.047899   0.0015892   211 ALA   B CA   
4013 C  C    . ALA   B 211 ? 0.180679  0.196371 0.114995  -0.0086969  -0.0577881  0.00753981  211 ALA   B C    
4014 O  O    . ALA   B 211 ? 0.204197  0.209936 0.116207  -0.00392763 -0.0721028  -0.0157929  211 ALA   B O    
4015 C  CB   . ALA   B 211 ? 0.172595  0.203109 0.100265  -0.00303158 -0.0501419  0.00294038  211 ALA   B CB   
4016 N  N    . VAL   B 212 ? 0.193736  0.193488 0.13505   -0.0151308  -0.0746415  0.0120561   212 VAL   B N    
4017 C  CA   . VAL   B 212 ? 0.210635  0.200587 0.147994  -0.0199549  -0.0769537  0.00351384  212 VAL   B CA   
4018 C  C    . VAL   B 212 ? 0.206991  0.228715 0.174031  -0.0227561  -0.088387   0.00023063  212 VAL   B C    
4019 O  O    . VAL   B 212 ? 0.221405  0.25736  0.180271  -0.0227524  -0.105171   -0.00077519 212 VAL   B O    
4020 C  CB   . VAL   B 212 ? 0.225696  0.1998   0.165237  -0.0237512  -0.0736721  0.00641213  212 VAL   B CB   
4021 C  CG1  . VAL   B 212 ? 0.229915  0.204525 0.186884  -0.027886   -0.0735039  0.00462615  212 VAL   B CG1  
4022 C  CG2  . VAL   B 212 ? 0.232935  0.20107  0.144963  -0.0202405  -0.0726285  0.00234248  212 VAL   B CG2  
4023 N  N    . ILE   B 213 ? 0.191619  0.240486 0.173554  -0.0193522  -0.088789   0.00198057  213 ILE   B N    
4024 C  CA   . ILE   B 213 ? 0.194077  0.260404 0.19761   -0.0150397  -0.0741933  0.0134362   213 ILE   B CA   
4025 C  C    . ILE   B 213 ? 0.199503  0.261323 0.198255  -0.00218365 -0.0837246  0.011467    213 ILE   B C    
4026 O  O    . ILE   B 213 ? 0.203878  0.291975 0.222899  -0.00622811 -0.0968035  0.0298414   213 ILE   B O    
4027 C  CB   . ILE   B 213 ? 0.189153  0.293146 0.209209  -0.0148901  -0.062558   0.0155925   213 ILE   B CB   
4028 C  CG1  . ILE   B 213 ? 0.199199  0.308    0.231787  -0.0257226  -0.0483681  0.0323505   213 ILE   B CG1  
4029 C  CG2  . ILE   B 213 ? 0.186883  0.317194 0.227759  -0.0131406  -0.0495685  0.0185838   213 ILE   B CG2  
4030 C  CD1  . ILE   B 213 ? 0.215375  0.316492 0.233496  -0.0293122  -0.0426463  0.033062    213 ILE   B CD1  
4031 N  N    . ASN   B 214 ? 0.206479  0.236199 0.180882  0.0037549   -0.0920797  0.00870223  214 ASN   B N    
4032 C  CA   . ASN   B 214 ? 0.234688  0.252116 0.186518  0.01755     -0.0925229  0.00826613  214 ASN   B CA   
4033 C  C    . ASN   B 214 ? 0.245132  0.271885 0.181872  0.0201335   -0.0861956  0.0125338   214 ASN   B C    
4034 O  O    . ASN   B 214 ? 0.283112  0.29093  0.198177  0.0233484   -0.0631152  0.0308407   214 ASN   B O    
4035 C  CB   . ASN   B 214 ? 0.244763  0.26073  0.202108  0.0183973   -0.0990336  -0.00126592 214 ASN   B CB   
4036 C  CG   . ASN   B 214 ? 0.263367  0.27796  0.252292  0.0401974   -0.10959    -0.0137242  214 ASN   B CG   
4037 O  OD1  . ASN   B 214 ? 0.333279  0.304676 0.311282  0.066606    -0.144693   -0.0145991  214 ASN   B OD1  
4038 N  ND2  . ASN   B 214 ? 0.266538  0.288072 0.253532  0.0442719   -0.097644   -0.0229387  214 ASN   B ND2  
4039 N  N    . GLY   B 215 ? 0.261665  0.279939 0.163271  0.0137725   -0.0991654  -0.00897189 215 GLY   B N    
4040 C  CA   . GLY   B 215 ? 0.288092  0.311576 0.162889  0.0214741   -0.104606   -0.0191429  215 GLY   B CA   
4041 C  C    . GLY   B 215 ? 0.308582  0.334187 0.145411  0.0160392   -0.101623   -0.031589   215 GLY   B C    
4042 O  O    . GLY   B 215 ? 0.351426  0.378628 0.159417  0.0319848   -0.105535   -0.0543374  215 GLY   B O    
4043 N  N    . ASP   B 216 ? 0.323984  0.338103 0.123668  0.0128184   -0.102335   -0.0196767  216 ASP   B N    
4044 C  CA   . ASP   B 216 ? 0.344625  0.360564 0.135655  0.00334143  -0.0923699  -0.00832822 216 ASP   B CA   
4045 C  C    . ASP   B 216 ? 0.344054  0.373304 0.147068  0.0162419   -0.0818641  0.0177882   216 ASP   B C    
4046 O  O    . ASP   B 216 ? 0.35304   0.415473 0.137955  0.0620897   -0.0558195  0.0165362   216 ASP   B O    
4047 C  CB   . ASP   B 216 ? 0.383164  0.389306 0.1848    -0.0208534  -0.0804666  -0.0197485  216 ASP   B CB   
4048 C  CG   . ASP   B 216 ? 0.415895  0.421643 0.244109  -0.0457449  -0.0737775  -0.0248456  216 ASP   B CG   
4049 O  OD1  . ASP   B 216 ? 0.474236  0.488395 0.271448  -0.0419998  -0.0587309  -0.0366745  216 ASP   B OD1  
4050 O  OD2  . ASP   B 216 ? 0.419692  0.435505 0.317773  -0.0674307  -0.0907284  -0.0374856  216 ASP   B OD2  
4051 N  N    . ARG   B 217 ? 0.340229  0.320607 0.199785  -0.00065829 -0.0900061  0.0279442   217 ARG   B N    
4052 C  CA   . ARG   B 217 ? 0.334299  0.326593 0.239295  -0.0114437  -0.108179   0.0339695   217 ARG   B CA   
4053 C  C    . ARG   B 217 ? 0.306999  0.286159 0.198193  -0.0189849  -0.110141   0.0368564   217 ARG   B C    
4054 O  O    . ARG   B 217 ? 0.305497  0.280979 0.24452   -0.0335124  -0.111489   0.0450653   217 ARG   B O    
4055 C  CB   . ARG   B 217 ? 0.357663  0.356746 0.298757  -0.0260468  -0.111735   0.0352128   217 ARG   B CB   
4056 C  CG   . ARG   B 217 ? 0.349093  0.386615 0.328601  -0.0258789  -0.124792   0.0444951   217 ARG   B CG   
4057 C  CD   . ARG   B 217 ? 0.360312  0.393562 0.364307  -0.0338975  -0.124611   0.0480951   217 ARG   B CD   
4058 N  NE   . ARG   B 217 ? 0.352099  0.403483 0.381306  -0.040026   -0.117162   0.0525571   217 ARG   B NE   
4059 C  CZ   . ARG   B 217 ? 0.320602  0.384837 0.388378  -0.0524206  -0.124337   0.048717    217 ARG   B CZ   
4060 N  NH1  . ARG   B 217 ? 0.275739  0.381062 0.391423  -0.063936   -0.135857   0.0314201   217 ARG   B NH1  
4061 N  NH2  . ARG   B 217 ? 0.345816  0.373925 0.412156  -0.0435095  -0.117446   0.0518153   217 ARG   B NH2  
4062 N  N    . TRP   B 218 ? 0.307646  0.256464 0.167856  -0.00703669 -0.0950537  0.0169387   218 TRP   B N    
4063 C  CA   . TRP   B 218 ? 0.315905  0.239283 0.160058  -0.00097496 -0.0761152  0.00263148  218 TRP   B CA   
4064 C  C    . TRP   B 218 ? 0.32469   0.230417 0.14052   0.0140269   -0.0672953  -0.00935641 218 TRP   B C    
4065 O  O    . TRP   B 218 ? 0.362252  0.253562 0.153437  0.0174013   -0.0508102  -0.0114491  218 TRP   B O    
4066 C  CB   . TRP   B 218 ? 0.313659  0.245666 0.141892  0.00528645  -0.0599312  -0.00109852 218 TRP   B CB   
4067 C  CG   . TRP   B 218 ? 0.300764  0.242943 0.131084  0.00778656  -0.0298356  -0.0113318  218 TRP   B CG   
4068 C  CD1  . TRP   B 218 ? 0.300922  0.247172 0.138237  0.00896737  -0.022777   -0.0146178  218 TRP   B CD1  
4069 C  CD2  . TRP   B 218 ? 0.290997  0.268608 0.110032  0.0132468   -0.0128629  -0.0171727  218 TRP   B CD2  
4070 N  NE1  . TRP   B 218 ? 0.293299  0.256549 0.117886  0.00502072  -0.0106295  -0.00777714 218 TRP   B NE1  
4071 C  CE2  . TRP   B 218 ? 0.291172  0.272584 0.111298  0.0118091   -0.00547402 -0.0184021  218 TRP   B CE2  
4072 C  CE3  . TRP   B 218 ? 0.294818  0.284755 0.123278  0.0192478   -0.00599896 -0.0232484  218 TRP   B CE3  
4073 C  CZ2  . TRP   B 218 ? 0.293858  0.276352 0.100795  0.00847533  0.00628493  -0.0224962  218 TRP   B CZ2  
4074 C  CZ3  . TRP   B 218 ? 0.289674  0.291958 0.126902  0.0198869   -0.00426493 -0.0261371  218 TRP   B CZ3  
4075 C  CH2  . TRP   B 218 ? 0.27813   0.297225 0.110512  0.0125919   0.00344837  -0.0175433  218 TRP   B CH2  
4076 N  N    . PHE   B 219 ? 0.285761  0.200646 0.14072   0.026409    -0.0616161  -0.0187659  219 PHE   B N    
4077 C  CA   . PHE   B 219 ? 0.271244  0.188548 0.143686  0.0295198   -0.0628578  -0.0254851  219 PHE   B CA   
4078 C  C    . PHE   B 219 ? 0.275575  0.189327 0.146509  0.0328087   -0.0639712  -0.0211768  219 PHE   B C    
4079 O  O    . PHE   B 219 ? 0.273907  0.199023 0.153017  0.0468995   -0.0610948  -0.033494   219 PHE   B O    
4080 C  CB   . PHE   B 219 ? 0.258939  0.193349 0.128314  0.0254168   -0.074103   -0.0191652  219 PHE   B CB   
4081 C  CG   . PHE   B 219 ? 0.247271  0.199044 0.132613  0.0235529   -0.0696813  -0.016474   219 PHE   B CG   
4082 C  CD1  . PHE   B 219 ? 0.243737  0.199597 0.143074  0.0256288   -0.0597597  -0.013641   219 PHE   B CD1  
4083 C  CD2  . PHE   B 219 ? 0.243464  0.190057 0.136812  0.0214565   -0.0634228  -0.018503   219 PHE   B CD2  
4084 C  CE1  . PHE   B 219 ? 0.24201   0.203689 0.140073  0.0243108   -0.0642119  -0.0182329  219 PHE   B CE1  
4085 C  CE2  . PHE   B 219 ? 0.245486  0.201936 0.134252  0.027928    -0.0643658  -0.0189849  219 PHE   B CE2  
4086 C  CZ   . PHE   B 219 ? 0.237057  0.199383 0.158855  0.0242189   -0.0563909  -0.0187117  219 PHE   B CZ   
4087 N  N    . LEU   B 220 ? 0.277598  0.191612 0.150594  0.0395668   -0.073038   -0.0155303  220 LEU   B N    
4088 C  CA   . LEU   B 220 ? 0.285801  0.205964 0.140173  0.0323259   -0.0713693  -0.0122361  220 LEU   B CA   
4089 C  C    . LEU   B 220 ? 0.284453  0.209478 0.140743  0.0277548   -0.0552923  -0.0101316  220 LEU   B C    
4090 O  O    . LEU   B 220 ? 0.309661  0.221118 0.157822  0.0189182   -0.0392261  -0.00976796 220 LEU   B O    
4091 C  CB   . LEU   B 220 ? 0.294171  0.219562 0.148506  0.0397948   -0.0713431  -0.0125792  220 LEU   B CB   
4092 C  CG   . LEU   B 220 ? 0.29187   0.232418 0.16147   0.0486502   -0.0784424  -0.00839265 220 LEU   B CG   
4093 C  CD1  . LEU   B 220 ? 0.300413  0.248465 0.193439  0.0418324   -0.0721973  -0.00509039 220 LEU   B CD1  
4094 C  CD2  . LEU   B 220 ? 0.294584  0.231456 0.159029  0.0405815   -0.0745822  -0.00860227 220 LEU   B CD2  
4095 N  N    . ASN   B 221 ? 0.277357  0.208377 0.137451  0.0194257   -0.0486735  -0.015867   221 ASN   B N    
4096 C  CA   . ASN   B 221 ? 0.253606  0.203983 0.133905  0.00866791  -0.0404667  -0.0145117  221 ASN   B CA   
4097 C  C    . ASN   B 221 ? 0.220773  0.202942 0.126957  0.00991917  -0.0367266  -0.0219061  221 ASN   B C    
4098 O  O    . ASN   B 221 ? 0.210654  0.23456  0.149522  0.02093     -0.0297239  -0.0299208  221 ASN   B O    
4099 C  CB   . ASN   B 221 ? 0.261326  0.206657 0.145303  -0.0128914  -0.0444653  -0.0114763  221 ASN   B CB   
4100 C  CG   . ASN   B 221 ? 0.269059  0.221802 0.146792  -0.0218092  -0.0464476  0.00358978  221 ASN   B CG   
4101 O  OD1  . ASN   B 221 ? 0.251836  0.22713  0.131908  -0.0309898  -0.0549463  0.00633465  221 ASN   B OD1  
4102 N  ND2  . ASN   B 221 ? 0.286632  0.238393 0.16069   -0.0345577  -0.0510151  0.00289045  221 ASN   B ND2  
4103 N  N    . ARG   B 222 ? 0.197671  0.189957 0.115067  0.00250787  -0.0314993  -0.0195809  222 ARG   B N    
4104 C  CA   . ARG   B 222 ? 0.185347  0.191325 0.122095  -0.00283504 -0.0255666  -0.0235527  222 ARG   B CA   
4105 C  C    . ARG   B 222 ? 0.178807  0.182294 0.125976  -0.00155299 -0.0233363  -0.0214289  222 ARG   B C    
4106 O  O    . ARG   B 222 ? 0.168283  0.178676 0.144455  -0.003197   -0.0328236  -0.0166419  222 ARG   B O    
4107 C  CB   . ARG   B 222 ? 0.196007  0.195099 0.121126  -0.00962009 -0.0197123  -0.0254118  222 ARG   B CB   
4108 C  CG   . ARG   B 222 ? 0.207331  0.194605 0.121326  -0.00939625 -0.0131058  -0.0259264  222 ARG   B CG   
4109 C  CD   . ARG   B 222 ? 0.221834  0.206751 0.134958  -0.00922693 -0.00708708 -0.0294047  222 ARG   B CD   
4110 N  NE   . ARG   B 222 ? 0.229424  0.218608 0.130336  -0.0100085  -0.00513143 -0.0278947  222 ARG   B NE   
4111 C  CZ   . ARG   B 222 ? 0.221708  0.206448 0.129938  -0.00683238 -0.0122143  -0.032413   222 ARG   B CZ   
4112 N  NH1  . ARG   B 222 ? 0.200787  0.202351 0.0947467 -0.00823749 -0.0252714  -0.0366853  222 ARG   B NH1  
4113 N  NH2  . ARG   B 222 ? 0.245677  0.23976  0.141467  -0.00318259 -0.020123   -0.0269848  222 ARG   B NH2  
4114 N  N    . PHE   B 223 ? 0.190157  0.179601 0.113144  -0.00331107 -0.0249136  -0.0247833  223 PHE   B N    
4115 C  CA   . PHE   B 223 ? 0.19673   0.195796 0.117257  0.00733186  -0.0269361  -0.0184528  223 PHE   B CA   
4116 C  C    . PHE   B 223 ? 0.231513  0.192503 0.114504  0.0208172   -0.0294501  -0.0172672  223 PHE   B C    
4117 O  O    . PHE   B 223 ? 0.253338  0.198805 0.0852803 0.0332699   -0.0249154  -0.015327   223 PHE   B O    
4118 C  CB   . PHE   B 223 ? 0.186718  0.207939 0.124598  0.00760555  -0.02759    -0.0110291  223 PHE   B CB   
4119 C  CG   . PHE   B 223 ? 0.175409  0.224313 0.128686  0.00294708  -0.0172419  -0.0027204  223 PHE   B CG   
4120 C  CD1  . PHE   B 223 ? 0.160704  0.225328 0.128273  0.00789007  -0.0101171  0.00301644  223 PHE   B CD1  
4121 C  CD2  . PHE   B 223 ? 0.17289   0.230332 0.144777  0.00208811  -0.0222974  0.00336431  223 PHE   B CD2  
4122 C  CE1  . PHE   B 223 ? 0.164296  0.236208 0.141635  0.00896956  -0.00051969 0.00607774  223 PHE   B CE1  
4123 C  CE2  . PHE   B 223 ? 0.169871  0.246393 0.154535  -2.938e-05  -0.00071158 0.00834862  223 PHE   B CE2  
4124 C  CZ   . PHE   B 223 ? 0.161286  0.245215 0.14382   0.00822662  0.00313233  0.00905092  223 PHE   B CZ   
4125 N  N    . THR   B 224 ? 0.263774  0.217718 0.112375  0.0270987   -0.0486744  -0.0267427  224 THR   B N    
4126 C  CA   . THR   B 224 ? 0.284619  0.233666 0.12835   0.0167814   -0.0552234  -0.0428547  224 THR   B CA   
4127 C  C    . THR   B 224 ? 0.287659  0.24862  0.137406  0.0255713   -0.0663437  -0.0409187  224 THR   B C    
4128 O  O    . THR   B 224 ? 0.29223   0.271216 0.159101  0.0328193   -0.0817844  -0.0688996  224 THR   B O    
4129 C  CB   . THR   B 224 ? 0.307366  0.243426 0.152969  0.00367578  -0.0456394  -0.0385711  224 THR   B CB   
4130 O  OG1  . THR   B 224 ? 0.311149  0.27491  0.169058  0.00791206  -0.018818   -0.0463889  224 THR   B OG1  
4131 C  CG2  . THR   B 224 ? 0.315553  0.244868 0.159233  0.00775079  -0.0558701  -0.0334503  224 THR   B CG2  
4132 N  N    . THR   B 225 ? 0.311695  0.249418 0.13585   0.0176244   -0.0695622  -0.033143   225 THR   B N    
4133 C  CA   . THR   B 225 ? 0.322375  0.26945  0.133507  0.0134248   -0.0851445  -0.0142761  225 THR   B CA   
4134 C  C    . THR   B 225 ? 0.340172  0.279885 0.138174  -0.00806118 -0.0803707  0.00236339  225 THR   B C    
4135 O  O    . THR   B 225 ? 0.352915  0.299556 0.142105  -0.0359327  -0.0803926  0.0211664   225 THR   B O    
4136 C  CB   . THR   B 225 ? 0.305058  0.295102 0.146052  0.00809658  -0.0945826  -0.00932868 225 THR   B CB   
4137 O  OG1  . THR   B 225 ? 0.318317  0.332992 0.169865  0.0328895   -0.101213   -0.00146116 225 THR   B OG1  
4138 C  CG2  . THR   B 225 ? 0.300638  0.284653 0.148614  0.00590225  -0.092388   -0.00864771 225 THR   B CG2  
4139 N  N    . THR   B 226 ? 0.365617  0.290389 0.127581  -0.00937694 -0.0922954  0.00094549  226 THR   B N    
4140 C  CA   . THR   B 226 ? 0.398581  0.28782  0.13147   -0.0176698  -0.086622   0.00443999  226 THR   B CA   
4141 C  C    . THR   B 226 ? 0.402222  0.272853 0.124877  -0.0179834  -0.0916309  0.0282276   226 THR   B C    
4142 O  O    . THR   B 226 ? 0.381949  0.266749 0.135023  -0.022112   -0.0960702  0.0335304   226 THR   B O    
4143 C  CB   . THR   B 226 ? 0.431126  0.272915 0.168342  -0.0234526  -0.0857323  0.00368095  226 THR   B CB   
4144 O  OG1  . THR   B 226 ? 0.441204  0.264588 0.170138  -0.025426   -0.0735833  -0.00286225 226 THR   B OG1  
4145 C  CG2  . THR   B 226 ? 0.445244  0.280903 0.202564  -0.0259521  -0.0841056  -0.00856723 226 THR   B CG2  
4146 N  N    . LEU   B 227 ? 0.416693  0.26446  0.12751   -0.0170178  -0.0927036  0.0218259   227 LEU   B N    
4147 C  CA   . LEU   B 227 ? 0.441996  0.275973 0.138451  -0.0156941  -0.0815603  0.0121299   227 LEU   B CA   
4148 C  C    . LEU   B 227 ? 0.450375  0.273419 0.15969   -0.00508511 -0.0990986  0.00523009  227 LEU   B C    
4149 O  O    . LEU   B 227 ? 0.444058  0.257231 0.170101  -0.012242   -0.10264    0.00459439  227 LEU   B O    
4150 C  CB   . LEU   B 227 ? 0.461744  0.304588 0.153319  -0.0203314  -0.064425   0.0185747   227 LEU   B CB   
4151 C  CG   . LEU   B 227 ? 0.492748  0.320205 0.186677  -0.0226978  -0.0493203  0.0134516   227 LEU   B CG   
4152 C  CD1  . LEU   B 227 ? 0.500064  0.317166 0.197808  -0.0132679  -0.0410238  0.0150839   227 LEU   B CD1  
4153 C  CD2  . LEU   B 227 ? 0.507661  0.343633 0.212193  -0.020649   -0.0303901  0.00021451  227 LEU   B CD2  
4154 N  N    A ASN   B 228 ? 0.457431  0.272209 0.141828  -0.0058422  -0.105556   0.00240162  228 ASN   B N    
4155 N  N    B ASN   B 228 ? 0.451915  0.279417 0.151343  0.0006418   -0.108472   0.00155628  228 ASN   B N    
4156 C  CA   A ASN   B 228 ? 0.458001  0.285374 0.17748   0.00287818  -0.103278   -0.00036366 228 ASN   B CA   
4157 C  CA   B ASN   B 228 ? 0.451498  0.299054 0.195108  0.013994    -0.10742    -0.0033338  228 ASN   B CA   
4158 C  C    A ASN   B 228 ? 0.443127  0.282018 0.180339  0.0101713   -0.108556   0.00107511  228 ASN   B C    
4159 C  C    B ASN   B 228 ? 0.440105  0.285731 0.193129  0.0165991   -0.110535   -0.00493565 228 ASN   B C    
4160 O  O    A ASN   B 228 ? 0.445525  0.285855 0.165622  0.00584399  -0.128591   -0.00562167 228 ASN   B O    
4161 O  O    B ASN   B 228 ? 0.445281  0.285869 0.208464  0.014399    -0.11586    -0.0127347  228 ASN   B O    
4162 C  CB   A ASN   B 228 ? 0.470405  0.291451 0.184953  0.00270207  -0.099306   0.00724063  228 ASN   B CB   
4163 C  CB   B ASN   B 228 ? 0.460483  0.316844 0.214158  0.026322    -0.110735   0.00641266  228 ASN   B CB   
4164 C  CG   A ASN   B 228 ? 0.485917  0.307495 0.196959  0.00501175  -0.0861167  0.0118376   228 ASN   B CG   
4165 C  CG   B ASN   B 228 ? 0.472395  0.342025 0.251494  0.0406824   -0.107671   0.00660636  228 ASN   B CG   
4166 O  OD1  A ASN   B 228 ? 0.513886  0.307692 0.206808  0.00290021  -0.0913888  0.00752227  228 ASN   B OD1  
4167 O  OD1  B ASN   B 228 ? 0.476682  0.363679 0.267644  0.0441525   -0.113842   0.00351859  228 ASN   B OD1  
4168 N  ND2  A ASN   B 228 ? 0.494465  0.31919  0.220231  0.00575035  -0.0747554  0.0253929   228 ASN   B ND2  
4169 N  ND2  B ASN   B 228 ? 0.478891  0.347476 0.27372   0.0553241   -0.110259   0.00711041  228 ASN   B ND2  
4170 N  N    . ASP   B 229 ? 0.43727   0.280157 0.198226  0.0204777   -0.104666   -0.010961   229 ASP   B N    
4171 C  CA   . ASP   B 229 ? 0.411228  0.27625  0.227721  0.0310128   -0.0977813  -0.00779458 229 ASP   B CA   
4172 C  C    . ASP   B 229 ? 0.374663  0.276766 0.217055  0.0235986   -0.0886468  -0.00248417 229 ASP   B C    
4173 O  O    . ASP   B 229 ? 0.3365    0.27622  0.246927  0.0307718   -0.0785098  0.0061376   229 ASP   B O    
4174 C  CB   . ASP   B 229 ? 0.446705  0.290785 0.266365  0.0389655   -0.104603   -0.0343936  229 ASP   B CB   
4175 C  CG   . ASP   B 229 ? 0.490127  0.317622 0.327525  0.049212    -0.115155   -0.0381523  229 ASP   B CG   
4176 O  OD1  . ASP   B 229 ? 0.506592  0.339636 0.402239  0.0882636   -0.138818   -0.0222498  229 ASP   B OD1  
4177 O  OD2  . ASP   B 229 ? 0.520014  0.351714 0.37321   0.0498381   -0.117655   -0.0765491  229 ASP   B OD2  
4178 N  N    . PHE   B 230 ? 0.35461   0.245138 0.18314   0.0194858   -0.10001    0.000659    230 PHE   B N    
4179 C  CA   . PHE   B 230 ? 0.334342  0.242051 0.175735  -0.00135403 -0.103399   0.0036291   230 PHE   B CA   
4180 C  C    . PHE   B 230 ? 0.315797  0.236972 0.181779  -0.00295492 -0.100075   0.0123198   230 PHE   B C    
4181 O  O    . PHE   B 230 ? 0.302417  0.279423 0.177978  -0.0167315  -0.0920515  0.0113511   230 PHE   B O    
4182 C  CB   . PHE   B 230 ? 0.339277  0.240936 0.173321  -0.00010368 -0.110246   0.00450882  230 PHE   B CB   
4183 C  CG   . PHE   B 230 ? 0.334727  0.245295 0.200715  -0.00891023 -0.11265    0.0114043   230 PHE   B CG   
4184 C  CD1  . PHE   B 230 ? 0.338658  0.256141 0.21226   -0.00233683 -0.115202   0.0173796   230 PHE   B CD1  
4185 C  CD2  . PHE   B 230 ? 0.355402  0.248846 0.24293   0.00476585  -0.0931357  0.00884912  230 PHE   B CD2  
4186 C  CE1  . PHE   B 230 ? 0.338996  0.25904  0.205089  -0.0138911  -0.118896   0.0291931   230 PHE   B CE1  
4187 C  CE2  . PHE   B 230 ? 0.373869  0.254982 0.255224  0.0021697   -0.0971652  0.0180711   230 PHE   B CE2  
4188 C  CZ   . PHE   B 230 ? 0.360202  0.260167 0.255826  -0.00237492 -0.0978392  0.0262533   230 PHE   B CZ   
4189 N  N    . ASN   B 231 ? 0.299263  0.239771 0.180332  0.00760997  -0.0962369  0.0116456   231 ASN   B N    
4190 C  CA   . ASN   B 231 ? 0.301782  0.246813 0.219587  0.00639087  -0.0952842  0.0163259   231 ASN   B CA   
4191 C  C    . ASN   B 231 ? 0.303502  0.253749 0.23429   0.0176867   -0.0971673  0.0246655   231 ASN   B C    
4192 O  O    . ASN   B 231 ? 0.310257  0.264574 0.26002   0.00988758  -0.101826   0.0233682   231 ASN   B O    
4193 C  CB   . ASN   B 231 ? 0.309713  0.269195 0.230563  0.0154699   -0.0880788  0.0176475   231 ASN   B CB   
4194 C  CG   . ASN   B 231 ? 0.318784  0.282559 0.269941  0.0172249   -0.0631925  0.0278683   231 ASN   B CG   
4195 O  OD1  . ASN   B 231 ? 0.324989  0.283822 0.394698  0.035868    -0.0110522  0.0482671   231 ASN   B OD1  
4196 N  ND2  . ASN   B 231 ? 0.341332  0.279939 0.246834  0.0134066   -0.0583779  0.0185211   231 ASN   B ND2  
4197 N  N    . LEU   B 232 ? 0.323384  0.2617   0.259341  0.02174     -0.0992444  0.00873382  232 LEU   B N    
4198 C  CA   . LEU   B 232 ? 0.338641  0.288407 0.291871  0.0257446   -0.0912006  -0.0137033  232 LEU   B CA   
4199 C  C    . LEU   B 232 ? 0.336814  0.304636 0.26214   0.018241    -0.104585   -0.0270338  232 LEU   B C    
4200 O  O    . LEU   B 232 ? 0.34463   0.333447 0.264553  0.00937533  -0.116962   -0.0384303  232 LEU   B O    
4201 C  CB   . LEU   B 232 ? 0.350907  0.300917 0.337622  0.0439195   -0.0814089  -0.011313   232 LEU   B CB   
4202 C  CG   . LEU   B 232 ? 0.402272  0.328994 0.37513   0.0432961   -0.0706785  -0.00437866 232 LEU   B CG   
4203 C  CD1  . LEU   B 232 ? 0.408975  0.329632 0.396484  0.0485864   -0.0644239  -0.00926921 232 LEU   B CD1  
4204 C  CD2  . LEU   B 232 ? 0.412819  0.359185 0.399625  0.0430361   -0.0804304  -0.00343164 232 LEU   B CD2  
4205 N  N    . VAL   B 233 ? 0.324661  0.292537 0.255823  0.0170632   -0.10101    -0.0268719  233 VAL   B N    
4206 C  CA   . VAL   B 233 ? 0.31453   0.286649 0.236822  0.0159808   -0.0991112  -0.026956   233 VAL   B CA   
4207 C  C    . VAL   B 233 ? 0.280872  0.285143 0.23126   0.0161117   -0.0947339  -0.0176521  233 VAL   B C    
4208 O  O    . VAL   B 233 ? 0.278256  0.290169 0.224528  0.00682654  -0.0920998  -0.0166078  233 VAL   B O    
4209 C  CB   . VAL   B 233 ? 0.327982  0.296562 0.259429  0.0178351   -0.108113   -0.0327566  233 VAL   B CB   
4210 C  CG1  . VAL   B 233 ? 0.339394  0.293502 0.255232  0.0135425   -0.100849   -0.0386153  233 VAL   B CG1  
4211 C  CG2  . VAL   B 233 ? 0.331385  0.303652 0.235385  0.0251024   -0.107778   -0.0337604  233 VAL   B CG2  
4212 N  N    . ALA   B 234 ? 0.263309  0.279414 0.254824  0.0149793   -0.086037   -0.0128544  234 ALA   B N    
4213 C  CA   . ALA   B 234 ? 0.259721  0.288837 0.267611  0.0211312   -0.0729239  -0.0221706  234 ALA   B CA   
4214 C  C    . ALA   B 234 ? 0.244639  0.31114  0.287083  0.0360221   -0.0663932  -0.0204757  234 ALA   B C    
4215 O  O    . ALA   B 234 ? 0.230095  0.300199 0.292395  0.0498693   -0.0444563  -0.0251283  234 ALA   B O    
4216 C  CB   . ALA   B 234 ? 0.272356  0.292854 0.285305  0.0182109   -0.0691128  -0.0204645  234 ALA   B CB   
4217 N  N    . MET   B 235 ? 0.258797  0.33983  0.285283  0.0373476   -0.072142   -0.0191674  235 MET   B N    
4218 C  CA   . MET   B 235 ? 0.263534  0.361211 0.312306  0.0298554   -0.0720739  -0.0224855  235 MET   B CA   
4219 C  C    . MET   B 235 ? 0.262737  0.333015 0.279477  0.0361311   -0.0764108  -0.0292829  235 MET   B C    
4220 O  O    . MET   B 235 ? 0.266022  0.321325 0.284478  0.028513    -0.0655857  -0.00960059 235 MET   B O    
4221 C  CB   . MET   B 235 ? 0.292706  0.410814 0.341594  0.0368931   -0.0899796  -0.00128008 235 MET   B CB   
4222 C  CG   . MET   B 235 ? 0.311199  0.478623 0.397446  0.0318897   -0.104926   0.0157729   235 MET   B CG   
4223 S  SD   . MET   B 235 ? 0.385106  0.617796 0.456215  0.0351069   -0.14159    0.062149    235 MET   B SD   
4224 C  CE   . MET   B 235 ? 0.386697  0.619252 0.442147  0.0418711   -0.146774   0.053494    235 MET   B CE   
4225 N  N    . LYS   B 236 ? 0.24977   0.327167 0.265552  0.0362696   -0.0574659  -0.0326238  236 LYS   B N    
4226 C  CA   . LYS   B 236 ? 0.230458  0.334777 0.290251  0.0508948   -0.0372972  -0.0462814  236 LYS   B CA   
4227 C  C    . LYS   B 236 ? 0.203749  0.322167 0.270311  0.0401232   -0.00941717 -0.0562345  236 LYS   B C    
4228 O  O    . LYS   B 236 ? 0.176572  0.361838 0.309663  0.0358925   -0.00897044 -0.0693739  236 LYS   B O    
4229 C  CB   . LYS   B 236 ? 0.272034  0.359357 0.308939  0.0490318   -0.0259626  -0.0588982  236 LYS   B CB   
4230 C  CG   . LYS   B 236 ? 0.327236  0.390238 0.332413  0.0425562   -0.0118668  -0.0737179  236 LYS   B CG   
4231 C  CD   . LYS   B 236 ? 0.376812  0.414107 0.372662  0.0409007   -0.0023697  -0.0987749  236 LYS   B CD   
4232 C  CE   . LYS   B 236 ? 0.431712  0.453897 0.397908  0.0273679   0.0100377   -0.103681   236 LYS   B CE   
4233 N  NZ   . LYS   B 236 ? 0.476572  0.469902 0.441962  0.0270175   0.0195603   -0.118116   236 LYS   B NZ   
4234 N  N    . TYR   B 237 ? 0.185688  0.284704 0.229046  0.035864    0.00504693  -0.0636161  237 TYR   B N    
4235 C  CA   . TYR   B 237 ? 0.193266  0.290897 0.215083  0.0276492   -1.427e-05  -0.058209   237 TYR   B CA   
4236 C  C    . TYR   B 237 ? 0.192385  0.279032 0.210936  0.0297341   -0.00324661 -0.0518667  237 TYR   B C    
4237 O  O    . TYR   B 237 ? 0.17842   0.281694 0.208254  0.028939    0.00356107  -0.0520469  237 TYR   B O    
4238 C  CB   . TYR   B 237 ? 0.196285  0.292389 0.219468  0.0258854   -0.00427294 -0.0651289  237 TYR   B CB   
4239 C  CG   . TYR   B 237 ? 0.211273  0.30232  0.218062  0.0263235   -0.0115311  -0.0715749  237 TYR   B CG   
4240 C  CD1  . TYR   B 237 ? 0.226112  0.311825 0.237877  0.0230937   -0.002544   -0.0721197  237 TYR   B CD1  
4241 C  CD2  . TYR   B 237 ? 0.229727  0.311908 0.223182  0.0207289   -0.0193515  -0.0774986  237 TYR   B CD2  
4242 C  CE1  . TYR   B 237 ? 0.235234  0.329085 0.23496   0.0168786   -0.00677598 -0.0832717  237 TYR   B CE1  
4243 C  CE2  . TYR   B 237 ? 0.250414  0.325224 0.240836  0.0238542   -0.00600046 -0.0827826  237 TYR   B CE2  
4244 C  CZ   . TYR   B 237 ? 0.229333  0.33055  0.237916  0.0299505   -0.00151082 -0.0844942  237 TYR   B CZ   
4245 O  OH   . TYR   B 237 ? 0.268406  0.365392 0.234558  0.0303839   -0.00740394 -0.0990583  237 TYR   B OH   
4246 N  N    . ASN   B 238 ? 0.163808  0.272511 0.215421  0.0302489   -0.0184987  -0.0495772  238 ASN   B N    
4247 C  CA   . ASN   B 238 ? 0.175726  0.278984 0.229398  0.0328755   -0.0273863  -0.0551178  238 ASN   B CA   
4248 C  C    . ASN   B 238 ? 0.171024  0.247824 0.179958  0.0251886   -0.0267248  -0.0509572  238 ASN   B C    
4249 O  O    . ASN   B 238 ? 0.170387  0.241745 0.181919  0.0207085   -0.0265601  -0.0534609  238 ASN   B O    
4250 C  CB   . ASN   B 238 ? 0.214009  0.305213 0.288147  0.0274994   -0.0201389  -0.0512105  238 ASN   B CB   
4251 C  CG   . ASN   B 238 ? 0.264787  0.376481 0.390472  0.013633    -0.05618    -0.0534898  238 ASN   B CG   
4252 O  OD1  . ASN   B 238 ? 0.310801  0.397308 0.459739  0.0301414   -0.0360969  -0.076543   238 ASN   B OD1  
4253 N  ND2  . ASN   B 238 ? 0.351475  0.408685 0.44625   0.00383957  -0.0703107  -0.0666796  238 ASN   B ND2  
4254 N  N    . TYR   B 239 ? 0.168263  0.241267 0.157127  0.0240263   -0.0292316  -0.0357448  239 TYR   B N    
4255 C  CA   . TYR   B 239 ? 0.170686  0.236446 0.13521   0.0229331   -0.0267534  -0.0246239  239 TYR   B CA   
4256 C  C    . TYR   B 239 ? 0.195846  0.247288 0.142345  0.0250225   -0.0279285  -0.016554   239 TYR   B C    
4257 O  O    . TYR   B 239 ? 0.208541  0.262185 0.136055  0.0339522   -0.0241293  -0.00353361 239 TYR   B O    
4258 C  CB   . TYR   B 239 ? 0.177549  0.22395  0.128745  0.0265171   -0.0319393  -0.0222638  239 TYR   B CB   
4259 C  CG   . TYR   B 239 ? 0.179361  0.219247 0.129474  0.0286217   -0.0323832  -0.0137148  239 TYR   B CG   
4260 C  CD1  . TYR   B 239 ? 0.189215  0.213699 0.130256  0.0277245   -0.0422842  -0.00962875 239 TYR   B CD1  
4261 C  CD2  . TYR   B 239 ? 0.19138   0.229466 0.127659  0.0259322   -0.0407409  -0.0115046  239 TYR   B CD2  
4262 C  CE1  . TYR   B 239 ? 0.205345  0.216247 0.126392  0.0307499   -0.0359923  -0.00955483 239 TYR   B CE1  
4263 C  CE2  . TYR   B 239 ? 0.200314  0.229054 0.138679  0.0361787   -0.0445426  -0.0123541  239 TYR   B CE2  
4264 C  CZ   . TYR   B 239 ? 0.211183  0.220697 0.128702  0.0353901   -0.0446737  -0.0113957  239 TYR   B CZ   
4265 O  OH   . TYR   B 239 ? 0.248445  0.236061 0.130335  0.0416477   -0.0475367  -0.0161441  239 TYR   B OH   
4266 N  N    . GLU   B 240 ? 0.185975  0.261457 0.123901  0.0179071   -0.0288268  -0.00692766 240 GLU   B N    
4267 C  CA   . GLU   B 240 ? 0.206986  0.27414  0.130684  0.0127178   -0.0331176  0.0006582   240 GLU   B CA   
4268 C  C    . GLU   B 240 ? 0.202824  0.273906 0.129621  0.00607093  -0.0447845  0.00519527  240 GLU   B C    
4269 O  O    . GLU   B 240 ? 0.195413  0.247019 0.141825  0.0103058   -0.0486473  -0.00095621 240 GLU   B O    
4270 C  CB   . GLU   B 240 ? 0.233886  0.298539 0.142997  0.0160885   -0.0255318  -0.00473575 240 GLU   B CB   
4271 C  CG   . GLU   B 240 ? 0.269001  0.309317 0.159786  0.00179958  -0.0238072  -0.00240834 240 GLU   B CG   
4272 C  CD   . GLU   B 240 ? 0.312642  0.352494 0.179657  -0.013258   -0.0412791  -0.00927155 240 GLU   B CD   
4273 O  OE1  . GLU   B 240 ? 0.389011  0.417977 0.212869  -0.0368879  -0.0290572  0.00380877  240 GLU   B OE1  
4274 O  OE2  . GLU   B 240 ? 0.332377  0.376121 0.234523  0.00446831  -0.0306097  -0.00246761 240 GLU   B OE2  
4275 N  N    . PRO   B 241 ? 0.222825  0.284726 0.149238  -0.0120085  -0.0695209  0.0193099   241 PRO   B N    
4276 C  CA   . PRO   B 241 ? 0.247798  0.287831 0.159573  -0.0133845  -0.0716858  0.0245681   241 PRO   B CA   
4277 C  C    . PRO   B 241 ? 0.252324  0.283239 0.165425  -0.0142861  -0.0607379  0.0125115   241 PRO   B C    
4278 O  O    . PRO   B 241 ? 0.244587  0.297678 0.141301  -0.0193102  -0.0524115  -0.00526725 241 PRO   B O    
4279 C  CB   . PRO   B 241 ? 0.253731  0.304678 0.164916  -0.0158108  -0.0771259  0.0344233   241 PRO   B CB   
4280 C  CG   . PRO   B 241 ? 0.252205  0.297416 0.175298  -0.0173413  -0.080796   0.026039    241 PRO   B CG   
4281 C  CD   . PRO   B 241 ? 0.237929  0.295491 0.160849  -0.0132663  -0.0848365  0.0213973   241 PRO   B CD   
4282 N  N    . LEU   B 242 ? 0.259914  0.282884 0.154602  -0.0231005  -0.0538484  0.0219682   242 LEU   B N    
4283 C  CA   . LEU   B 242 ? 0.263197  0.281392 0.123664  -0.0246752  -0.0469568  0.0315019   242 LEU   B CA   
4284 C  C    . LEU   B 242 ? 0.274062  0.274906 0.131668  -0.0195407  -0.0501798  0.0394549   242 LEU   B C    
4285 O  O    . LEU   B 242 ? 0.301292  0.285252 0.138663  -0.00751659 -0.0400553  0.0423635   242 LEU   B O    
4286 C  CB   . LEU   B 242 ? 0.277918  0.280367 0.118325  -0.0273607  -0.0397172  0.0247687   242 LEU   B CB   
4287 C  CG   . LEU   B 242 ? 0.283009  0.286865 0.108308  -0.0295794  -0.0476447  0.0180144   242 LEU   B CG   
4288 C  CD1  . LEU   B 242 ? 0.284204  0.293132 0.107906  -0.0256347  -0.0444337  0.0193744   242 LEU   B CD1  
4289 C  CD2  . LEU   B 242 ? 0.297971  0.291282 0.124678  -0.0299223  -0.063088   0.0137536   242 LEU   B CD2  
4290 N  N    . THR   B 243 ? 0.272963  0.288467 0.137545  -0.0122944  -0.0438709  0.0510988   243 THR   B N    
4291 C  CA   . THR   B 243 ? 0.290116  0.29921  0.14458   -0.0133754  -0.0352556  0.0629897   243 THR   B CA   
4292 C  C    . THR   B 243 ? 0.291875  0.291693 0.147454  -0.016783   -0.0334112  0.0736592   243 THR   B C    
4293 O  O    . THR   B 243 ? 0.291625  0.303445 0.138048  -0.00632448 -0.0238954  0.0710047   243 THR   B O    
4294 C  CB   . THR   B 243 ? 0.29495   0.312817 0.151387  -0.0222268  -0.0425578  0.0509999   243 THR   B CB   
4295 O  OG1  . THR   B 243 ? 0.304198  0.308852 0.153656  -0.0232847  -0.0328482  0.0662141   243 THR   B OG1  
4296 C  CG2  . THR   B 243 ? 0.305945  0.32356  0.156847  -0.0286933  -0.0392792  0.0468811   243 THR   B CG2  
4297 N  N    . GLN   B 244 ? 0.304741  0.295043 0.155913  -0.021598   -0.0438617  0.0869462   244 GLN   B N    
4298 C  CA   . GLN   B 244 ? 0.324295  0.312157 0.176702  -0.0357241  -0.0457594  0.0860519   244 GLN   B CA   
4299 C  C    . GLN   B 244 ? 0.310942  0.321731 0.167955  -0.0470931  -0.0271941  0.0897195   244 GLN   B C    
4300 O  O    . GLN   B 244 ? 0.309925  0.346611 0.151166  -0.0495086  -0.0260507  0.0696326   244 GLN   B O    
4301 C  CB   . GLN   B 244 ? 0.354685  0.318056 0.185455  -0.0288614  -0.0498205  0.0966308   244 GLN   B CB   
4302 C  CG   . GLN   B 244 ? 0.365693  0.320754 0.204573  -0.0342255  -0.0457875  0.0972088   244 GLN   B CG   
4303 C  CD   . GLN   B 244 ? 0.372915  0.329491 0.224812  -0.035363   -0.0392972  0.0748214   244 GLN   B CD   
4304 O  OE1  . GLN   B 244 ? 0.380597  0.34657  0.230738  -0.0454759  -0.0394503  0.0467326   244 GLN   B OE1  
4305 N  NE2  . GLN   B 244 ? 0.380866  0.35963  0.272953  -0.0359932  -0.0311665  0.067289    244 GLN   B NE2  
4306 N  N    . ASP   B 245 ? 0.30216   0.334756 0.15181   -0.0536383  -0.0329842  0.0884545   245 ASP   B N    
4307 C  CA   . ASP   B 245 ? 0.303438  0.361973 0.182066  -0.0456581  -0.0148553  0.0850998   245 ASP   B CA   
4308 C  C    . ASP   B 245 ? 0.256444  0.351319 0.158448  -0.0320426  -0.00633232 0.0662698   245 ASP   B C    
4309 O  O    . ASP   B 245 ? 0.236052  0.377373 0.164449  -0.0269449  0.0141807   0.0628706   245 ASP   B O    
4310 C  CB   . ASP   B 245 ? 0.354395  0.393389 0.19338   -0.0547698  -0.0131851  0.0855024   245 ASP   B CB   
4311 C  CG   . ASP   B 245 ? 0.401465  0.435634 0.297186  -0.0516644  0.00386216  0.0801614   245 ASP   B CG   
4312 O  OD1  . ASP   B 245 ? 0.450183  0.51023  0.384184  -0.0721045  0.0504864   0.0708599   245 ASP   B OD1  
4313 O  OD2  . ASP   B 245 ? 0.482089  0.453248 0.403605  -0.0418474  0.0191171   0.0957529   245 ASP   B OD2  
4314 N  N    . HIS   B 246 ? 0.237701  0.331953 0.146481  -0.0359847  -0.0201261  0.0643752   246 HIS   B N    
4315 C  CA   . HIS   B 246 ? 0.241188  0.326445 0.133248  -0.0327519  -0.0183323  0.0539031   246 HIS   B CA   
4316 C  C    . HIS   B 246 ? 0.238703  0.322013 0.131727  -0.0364228  -0.0151623  0.0533006   246 HIS   B C    
4317 O  O    . HIS   B 246 ? 0.254541  0.34     0.135751  -0.0367626  -0.0222622  0.0626111   246 HIS   B O    
4318 C  CB   . HIS   B 246 ? 0.230418  0.317159 0.123154  -0.0297057  -0.0206143  0.0493365   246 HIS   B CB   
4319 C  CG   . HIS   B 246 ? 0.239156  0.323102 0.130893  -0.0269369  -0.0152346  0.0348821   246 HIS   B CG   
4320 N  ND1  . HIS   B 246 ? 0.235218  0.330072 0.144299  -0.0328219  -0.0254459  0.0273427   246 HIS   B ND1  
4321 C  CD2  . HIS   B 246 ? 0.243449  0.338    0.1173    -0.0224741  -0.0178057  0.0291403   246 HIS   B CD2  
4322 C  CE1  . HIS   B 246 ? 0.240783  0.332468 0.126186  -0.0243652  -0.0160398  0.0193534   246 HIS   B CE1  
4323 N  NE2  . HIS   B 246 ? 0.241143  0.338231 0.139697  -0.0247742  -0.00910299 0.0252363   246 HIS   B NE2  
4324 N  N    . VAL   B 247 ? 0.266685  0.332292 0.13848   -0.0352417  -0.0205746  0.0637932   247 VAL   B N    
4325 C  CA   . VAL   B 247 ? 0.286609  0.331814 0.138475  -0.0343659  -0.0220625  0.0617691   247 VAL   B CA   
4326 C  C    . VAL   B 247 ? 0.297726  0.364764 0.156637  -0.0348263  -0.0251927  0.0644796   247 VAL   B C    
4327 O  O    . VAL   B 247 ? 0.303573  0.355517 0.12825   -0.026842   -0.0229392  0.0567363   247 VAL   B O    
4328 C  CB   . VAL   B 247 ? 0.308624  0.329857 0.159722  -0.0294099  -0.0311964  0.0602388   247 VAL   B CB   
4329 C  CG1  . VAL   B 247 ? 0.311299  0.330233 0.173781  -0.0299211  -0.044655   0.0639963   247 VAL   B CG1  
4330 C  CG2  . VAL   B 247 ? 0.299848  0.335041 0.178322  -0.020494   -0.034201   0.0549738   247 VAL   B CG2  
4331 N  N    . ASP   B 248 ? 0.284834  0.383374 0.162333  -0.0421307  -0.00276974 0.0535925   248 ASP   B N    
4332 C  CA   . ASP   B 248 ? 0.295696  0.386076 0.175754  -0.0446978  0.0187406   0.0572108   248 ASP   B CA   
4333 C  C    . ASP   B 248 ? 0.265896  0.368937 0.161314  -0.0389918  0.032034    0.0431173   248 ASP   B C    
4334 O  O    . ASP   B 248 ? 0.274491  0.376942 0.151707  -0.0428309  0.0186033   0.0453877   248 ASP   B O    
4335 C  CB   . ASP   B 248 ? 0.313432  0.414672 0.179089  -0.0542408  0.0281937   0.0591903   248 ASP   B CB   
4336 C  CG   . ASP   B 248 ? 0.348845  0.42332  0.19417   -0.0480789  0.0328092   0.0633178   248 ASP   B CG   
4337 O  OD1  . ASP   B 248 ? 0.411246  0.433704 0.214596  -0.0534362  0.0361953   0.0660618   248 ASP   B OD1  
4338 O  OD2  . ASP   B 248 ? 0.401484  0.467368 0.191681  -0.0480653  0.0417868   0.0779438   248 ASP   B OD2  
4339 N  N    . ILE   B 249 ? 0.277642  0.36216  0.16763   -0.0234812  0.0281055   0.0271929   249 ILE   B N    
4340 C  CA   . ILE   B 249 ? 0.301149  0.370339 0.154461  -0.00626304 0.036585    0.0184324   249 ILE   B CA   
4341 C  C    . ILE   B 249 ? 0.279331  0.356947 0.153814  0.00680252  0.0265297   -0.00046543 249 ILE   B C    
4342 O  O    . ILE   B 249 ? 0.26634   0.36214  0.194018  0.0136446   0.0353999   -0.0131707  249 ILE   B O    
4343 C  CB   . ILE   B 249 ? 0.34549   0.369158 0.167527  -0.0113705  0.0331929   0.00151417  249 ILE   B CB   
4344 C  CG1  . ILE   B 249 ? 0.385841  0.404471 0.188467  -0.0169785  0.00854608  0.00403406  249 ILE   B CG1  
4345 C  CG2  . ILE   B 249 ? 0.363086  0.389466 0.19161   -0.00136552 0.0346704   0.00924774  249 ILE   B CG2  
4346 C  CD1  . ILE   B 249 ? 0.407597  0.414458 0.201638  -0.0244442  0.00211491  0.00439494  249 ILE   B CD1  
4347 N  N    . LEU   B 250 ? 0.239672  0.364424 0.134064  -0.00361064 0.0339016   0.0250598   250 LEU   B N    
4348 C  CA   . LEU   B 250 ? 0.264014  0.350836 0.139459  -0.0133189  0.0233086   0.0259754   250 LEU   B CA   
4349 C  C    . LEU   B 250 ? 0.244904  0.376467 0.153297  -0.0197481  0.035984    0.0167296   250 LEU   B C    
4350 O  O    . LEU   B 250 ? 0.224487  0.39241  0.163207  -0.0298594  0.0173483   0.023641    250 LEU   B O    
4351 C  CB   . LEU   B 250 ? 0.264065  0.322027 0.134211  -0.0199409  0.0280696   0.0254225   250 LEU   B CB   
4352 C  CG   . LEU   B 250 ? 0.270631  0.293772 0.13351   -0.0148321  0.0269516   0.0226727   250 LEU   B CG   
4353 C  CD1  . LEU   B 250 ? 0.271403  0.291631 0.141497  -0.0133089  0.0313345   0.0179888   250 LEU   B CD1  
4354 C  CD2  . LEU   B 250 ? 0.276317  0.290713 0.127096  -0.0153013  0.0221209   0.0173832   250 LEU   B CD2  
4355 N  N    . GLY   B 251 ? 0.268462  0.359494 0.163803  -0.0185731  0.0257349   0.0169334   251 GLY   B N    
4356 C  CA   . GLY   B 251 ? 0.278705  0.345977 0.176036  -0.0137417  0.0238197   -0.00250258 251 GLY   B CA   
4357 C  C    . GLY   B 251 ? 0.267253  0.336144 0.165687  -0.0182373  0.0289599   -0.0244901  251 GLY   B C    
4358 O  O    . GLY   B 251 ? 0.280623  0.329541 0.152736  0.00324705  0.0493159   -0.0421112  251 GLY   B O    
4359 N  N    . PRO   B 252 ? 0.259674  0.336898 0.169014  -0.0231355  0.0387842   -0.0352712  252 PRO   B N    
4360 C  CA   . PRO   B 252 ? 0.27095   0.345179 0.19732   -0.0319539  0.0299644   -0.0349592  252 PRO   B CA   
4361 C  C    . PRO   B 252 ? 0.248092  0.344532 0.201264  -0.0400273  0.0327255   -0.0284842  252 PRO   B C    
4362 O  O    . PRO   B 252 ? 0.225399  0.370601 0.243633  -0.0618968  0.0384694   -0.0341079  252 PRO   B O    
4363 C  CB   . PRO   B 252 ? 0.287086  0.354628 0.199521  -0.0165031  0.029509    -0.0394892  252 PRO   B CB   
4364 C  CG   . PRO   B 252 ? 0.299406  0.355799 0.198427  -0.0226621  0.0352137   -0.0481777  252 PRO   B CG   
4365 C  CD   . PRO   B 252 ? 0.268387  0.346329 0.183428  -0.0367038  0.0308365   -0.0479369  252 PRO   B CD   
4366 N  N    . LEU   B 253 ? 0.235293  0.324148 0.189125  -0.036134   0.0121262   -0.0193383  253 LEU   B N    
4367 C  CA   . LEU   B 253 ? 0.215118  0.296267 0.192113  -0.0196151  0.025991    -0.0135849  253 LEU   B CA   
4368 C  C    . LEU   B 253 ? 0.228733  0.290425 0.203897  -0.0259957  0.0152947   -0.00844331 253 LEU   B C    
4369 O  O    . LEU   B 253 ? 0.23186   0.300329 0.220772  -0.0312894  -0.0106934  -0.00313973 253 LEU   B O    
4370 C  CB   . LEU   B 253 ? 0.23752   0.301199 0.16978   -0.0147738  0.00682111  -0.00363791 253 LEU   B CB   
4371 C  CG   . LEU   B 253 ? 0.250269  0.304217 0.160183  -0.00034242 0.00476489  0.00249557  253 LEU   B CG   
4372 C  CD1  . LEU   B 253 ? 0.25492   0.319088 0.16816   0.0045665   0.00444713  0.00210964  253 LEU   B CD1  
4373 C  CD2  . LEU   B 253 ? 0.265758  0.323239 0.182169  0.00455532  -0.00504904 0.00725141  253 LEU   B CD2  
4374 N  N    . SER   B 254 ? 0.229819  0.264362 0.199805  -0.0234518  0.0100966   -0.0130284  254 SER   B N    
4375 C  CA   . SER   B 254 ? 0.230986  0.273016 0.203676  -0.0125434  0.00477642  -0.0135868  254 SER   B CA   
4376 C  C    . SER   B 254 ? 0.242589  0.275745 0.225841  -0.02008    0.00133098  -0.0309774  254 SER   B C    
4377 O  O    . SER   B 254 ? 0.248689  0.260621 0.245371  -0.0258268  -0.0127272  -0.0316645  254 SER   B O    
4378 C  CB   . SER   B 254 ? 0.243618  0.266777 0.203329  -0.00818622 -0.0043337  -0.0128515  254 SER   B CB   
4379 O  OG   . SER   B 254 ? 0.274996  0.301336 0.202387  0.00889717  0.0170308   -0.025577   254 SER   B OG   
4380 N  N    . ALA   B 255 ? 0.220509  0.306005 0.263427  -0.018836   0.00375314  -0.0547881  255 ALA   B N    
4381 C  CA   . ALA   B 255 ? 0.220767  0.31172  0.267049  -0.0195991  0.00138744  -0.0444705  255 ALA   B CA   
4382 C  C    . ALA   B 255 ? 0.232439  0.323666 0.277521  -0.025111   -0.00665078 -0.0349131  255 ALA   B C    
4383 O  O    . ALA   B 255 ? 0.249369  0.320386 0.301813  -0.0428711  -0.0154241  -0.0365807  255 ALA   B O    
4384 C  CB   . ALA   B 255 ? 0.237808  0.329406 0.278345  -0.0184553  0.00502897  -0.0398354  255 ALA   B CB   
4385 N  N    . GLN   B 256 ? 0.23234   0.322769 0.281655  -0.00775785 -0.0169373  -0.0287381  256 GLN   B N    
4386 C  CA   . GLN   B 256 ? 0.240929  0.348415 0.273573  -0.0124843  -0.0131829  -0.0154256  256 GLN   B CA   
4387 C  C    . GLN   B 256 ? 0.248865  0.352332 0.258461  -0.00630281 -0.0323027  -0.0160414  256 GLN   B C    
4388 O  O    . GLN   B 256 ? 0.252338  0.392002 0.258677  0.00137884  -0.0328158  -0.00707696 256 GLN   B O    
4389 C  CB   . GLN   B 256 ? 0.251352  0.344223 0.2907    -0.0115301  -0.0087601  -0.00991046 256 GLN   B CB   
4390 C  CG   . GLN   B 256 ? 0.286175  0.370242 0.322575  -0.00989224 -0.00084575 0.00346193  256 GLN   B CG   
4391 C  CD   . GLN   B 256 ? 0.335535  0.38933  0.376123  -0.0266688  -0.0109593  0.00730633  256 GLN   B CD   
4392 O  OE1  . GLN   B 256 ? 0.420419  0.444192 0.395099  -0.0422346  0.00697199  -0.0204188  256 GLN   B OE1  
4393 N  NE2  . GLN   B 256 ? 0.347394  0.415402 0.40763   -0.029811   -0.0193466  0.0264699   256 GLN   B NE2  
4394 N  N    . THR   B 257 ? 0.231625  0.340404 0.204482  -0.0159575  -0.0380987  -0.0142506  257 THR   B N    
4395 C  CA   . THR   B 257 ? 0.243109  0.301913 0.199827  -0.0152809  -0.0447457  -0.00350434 257 THR   B CA   
4396 C  C    . THR   B 257 ? 0.25499   0.279577 0.181125  -0.0340008  -0.0404901  -0.0132687  257 THR   B C    
4397 O  O    . THR   B 257 ? 0.268276  0.303395 0.185804  -0.018471   -0.0381554  -0.0139982  257 THR   B O    
4398 C  CB   . THR   B 257 ? 0.241521  0.298121 0.184831  -0.0258626  -0.0593536  -0.00148077 257 THR   B CB   
4399 O  OG1  . THR   B 257 ? 0.225665  0.286921 0.206773  -0.0428968  -0.0634101  0.0130205   257 THR   B OG1  
4400 C  CG2  . THR   B 257 ? 0.249564  0.305792 0.201321  -0.0229056  -0.0683558  -0.00438625 257 THR   B CG2  
4401 N  N    . GLY   B 258 ? 0.247533  0.259701 0.190821  -0.0277127  -0.036715   -0.016438   258 GLY   B N    
4402 C  CA   . GLY   B 258 ? 0.262305  0.251892 0.211007  -0.024755   -0.018688   -0.0107694  258 GLY   B CA   
4403 C  C    . GLY   B 258 ? 0.262087  0.247433 0.231098  -0.0236423  -0.00905847 -0.0131939  258 GLY   B C    
4404 O  O    . GLY   B 258 ? 0.286515  0.250175 0.22672   -0.0191502  0.00443823  -0.0168059  258 GLY   B O    
4405 N  N    . ILE   B 259 ? 0.252977  0.247876 0.251616  -0.0201912  -0.00398452 -0.0137422  259 ILE   B N    
4406 C  CA   . ILE   B 259 ? 0.250274  0.258397 0.22022   -0.0148748  -0.010068   -0.00901681 259 ILE   B CA   
4407 C  C    . ILE   B 259 ? 0.260434  0.249449 0.215661  -0.0230692  -0.00894483 -0.00640438 259 ILE   B C    
4408 O  O    . ILE   B 259 ? 0.263523  0.253678 0.200557  -0.0326066  -0.0199365  -0.0104891  259 ILE   B O    
4409 C  CB   . ILE   B 259 ? 0.250265  0.265748 0.248704  -0.0058076  -0.00553587 -0.0062562  259 ILE   B CB   
4410 C  CG1  . ILE   B 259 ? 0.278053  0.305773 0.260944  0.00249369  -0.00652128 0.0080905   259 ILE   B CG1  
4411 C  CG2  . ILE   B 259 ? 0.254558  0.273344 0.236668  -0.00626119 0.00342183  -0.00949391 259 ILE   B CG2  
4412 C  CD1  . ILE   B 259 ? 0.315808  0.318717 0.279866  0.00375248  -0.0173551  -0.00251941 259 ILE   B CD1  
4413 N  N    . ALA   B 260 ? 0.258933  0.242275 0.18597   -0.0274138  -0.0168969  -0.0110836  260 ALA   B N    
4414 C  CA   . ALA   B 260 ? 0.265465  0.247697 0.191416  -0.0339634  -0.0261554  -0.00158115 260 ALA   B CA   
4415 C  C    . ALA   B 260 ? 0.27074   0.240584 0.157024  -0.0420914  -0.0209013  -0.00193614 260 ALA   B C    
4416 O  O    . ALA   B 260 ? 0.261324  0.241619 0.140376  -0.037397   -0.0341721  0.00229904  260 ALA   B O    
4417 C  CB   . ALA   B 260 ? 0.27913   0.245552 0.204452  -0.0377701  -0.0186802  -0.00028829 260 ALA   B CB   
4418 N  N    . VAL   B 261 ? 0.289538  0.230114 0.160633  -0.0473018  -0.0405582  0.00701037  261 VAL   B N    
4419 C  CA   . VAL   B 261 ? 0.28822   0.228325 0.149908  -0.040252   -0.0431063  -0.00592683 261 VAL   B CA   
4420 C  C    . VAL   B 261 ? 0.277846  0.217729 0.147249  -0.0372265  -0.0556871  -0.00446901 261 VAL   B C    
4421 O  O    . VAL   B 261 ? 0.269856  0.209733 0.122697  -0.0360608  -0.0520753  -0.0170557  261 VAL   B O    
4422 C  CB   . VAL   B 261 ? 0.300197  0.235194 0.147674  -0.0445281  -0.042127   -0.0004024  261 VAL   B CB   
4423 C  CG1  . VAL   B 261 ? 0.306999  0.239369 0.143246  -0.0433338  -0.0575991  -0.0149341  261 VAL   B CG1  
4424 C  CG2  . VAL   B 261 ? 0.296316  0.238428 0.151603  -0.0514614  -0.0428127  -0.00298595 261 VAL   B CG2  
4425 N  N    . LEU   B 262 ? 0.288208  0.216303 0.160636  -0.0216304  -0.0539593  -0.00584019 262 LEU   B N    
4426 C  CA   . LEU   B 262 ? 0.303188  0.228294 0.157208  -0.0122442  -0.0420436  0.00392519  262 LEU   B CA   
4427 C  C    . LEU   B 262 ? 0.272089  0.244063 0.155436  -0.00718653 -0.0349484  -0.00269235 262 LEU   B C    
4428 O  O    . LEU   B 262 ? 0.271376  0.273453 0.163221  -0.00558445 -0.0287515  -0.00663952 262 LEU   B O    
4429 C  CB   . LEU   B 262 ? 0.330807  0.22514  0.163499  -0.00454387 -0.05195    0.00658594  262 LEU   B CB   
4430 C  CG   . LEU   B 262 ? 0.362074  0.23835  0.168029  0.00307912  -0.0539566  0.00670745  262 LEU   B CG   
4431 C  CD1  . LEU   B 262 ? 0.374033  0.235719 0.194694  0.0113856   -0.0522311  0.00648877  262 LEU   B CD1  
4432 C  CD2  . LEU   B 262 ? 0.37236   0.239593 0.142505  0.00186504  -0.0620008  0.00084798  262 LEU   B CD2  
4433 N  N    . ASP   B 263 ? 0.294     0.263421 0.161185  -0.00869283 -0.0360915  -0.00113078 263 ASP   B N    
4434 C  CA   . ASP   B 263 ? 0.28788   0.273963 0.166518  0.00057709  -0.0449538  -0.0029523  263 ASP   B CA   
4435 C  C    . ASP   B 263 ? 0.255517  0.244248 0.124447  0.00609393  -0.0576288  -0.00161245 263 ASP   B C    
4436 O  O    . ASP   B 263 ? 0.279001  0.257406 0.154516  0.00637291  -0.0403457  -0.0122912  263 ASP   B O    
4437 C  CB   . ASP   B 263 ? 0.295177  0.313974 0.224814  0.00103281  -0.0465774  -0.00487543 263 ASP   B CB   
4438 C  CG   . ASP   B 263 ? 0.3277    0.350375 0.259598  -0.0101337  -0.0416419  0.00403803  263 ASP   B CG   
4439 O  OD1  . ASP   B 263 ? 0.33304   0.358473 0.341985  0.00395466  -0.042197   -0.00110159 263 ASP   B OD1  
4440 O  OD2  . ASP   B 263 ? 0.33594   0.427086 0.328527  -0.0216394  -0.046469   -0.0296186  263 ASP   B OD2  
4441 N  N    . MET   B 264 ? 0.271043  0.235629 0.140017  0.00621327  -0.0733721  0.00955751  264 MET   B N    
4442 C  CA   . MET   B 264 ? 0.264068  0.215425 0.124994  0.00976285  -0.0697291  0.00557814  264 MET   B CA   
4443 C  C    . MET   B 264 ? 0.267691  0.211971 0.127935  -0.0004155  -0.0670316  0.00447139  264 MET   B C    
4444 O  O    . MET   B 264 ? 0.27366   0.210604 0.132941  0.00277434  -0.0603265  0.00143169  264 MET   B O    
4445 C  CB   . MET   B 264 ? 0.263158  0.220684 0.133171  -0.0002572  -0.0604871  -0.0009511  264 MET   B CB   
4446 C  CG   . MET   B 264 ? 0.254271  0.218346 0.128376  -0.00220926 -0.062293   0.00112944  264 MET   B CG   
4447 S  SD   . MET   B 264 ? 0.271717  0.223089 0.13163   -0.0114317  -0.0640768  0.00661406  264 MET   B SD   
4448 C  CE   . MET   B 264 ? 0.276097  0.241899 0.123013  -0.0187408  -0.0593689  0.00680572  264 MET   B CE   
4449 N  N    . CYS   B 265 ? 0.277623  0.212849 0.134078  0.00073231  -0.0721877  0.00663644  265 CYS   B N    
4450 C  CA   . CYS   B 265 ? 0.288606  0.212259 0.124789  -0.00185427 -0.0820318  0.00415856  265 CYS   B CA   
4451 C  C    . CYS   B 265 ? 0.275886  0.200115 0.130434  -0.00872537 -0.0790781  0.00151773  265 CYS   B C    
4452 O  O    . CYS   B 265 ? 0.286108  0.205321 0.146329  -0.0113187  -0.0747428  -0.0224481  265 CYS   B O    
4453 C  CB   . CYS   B 265 ? 0.293686  0.207866 0.123749  0.00101927  -0.0941502  0.00125898  265 CYS   B CB   
4454 S  SG   . CYS   B 265 ? 0.314826  0.234611 0.137591  0.00188353  -0.0923263  -0.00870868 265 CYS   B SG   
4455 N  N    . ALA   B 266 ? 0.292393  0.200862 0.149491  -0.00432198 -0.0608005  -0.011073   266 ALA   B N    
4456 C  CA   . ALA   B 266 ? 0.295362  0.214004 0.150494  0.00238675  -0.0580941  -0.00840045 266 ALA   B CA   
4457 C  C    . ALA   B 266 ? 0.283178  0.219157 0.129337  0.00716042  -0.0574928  -0.0153437  266 ALA   B C    
4458 O  O    . ALA   B 266 ? 0.300861  0.260133 0.147132  0.0156056   -0.0443426  -0.0305875  266 ALA   B O    
4459 C  CB   . ALA   B 266 ? 0.292762  0.211148 0.150071  0.00364252  -0.0553693  -0.00999402 266 ALA   B CB   
4460 N  N    . SER   B 267 ? 0.286346  0.225874 0.130816  0.00325144  -0.0712592  -0.0212675  267 SER   B N    
4461 C  CA   . SER   B 267 ? 0.272032  0.223025 0.144965  0.00610941  -0.0624209  -0.0114279  267 SER   B CA   
4462 C  C    . SER   B 267 ? 0.259091  0.20368  0.140062  0.0152651   -0.0598457  -0.0167953  267 SER   B C    
4463 O  O    . SER   B 267 ? 0.256802  0.213804 0.151094  0.015064    -0.0588032  -0.0194825  267 SER   B O    
4464 C  CB   . SER   B 267 ? 0.277134  0.237226 0.154213  0.00427292  -0.0674552  -0.00863848 267 SER   B CB   
4465 O  OG   . SER   B 267 ? 0.297705  0.266124 0.158332  -0.0156147  -0.073547   0.00150525  267 SER   B OG   
4466 N  N    . LEU   B 268 ? 0.27017   0.201512 0.151949  0.0132      -0.0600075  -0.0188967  268 LEU   B N    
4467 C  CA   . LEU   B 268 ? 0.264642  0.202459 0.142172  0.0133577   -0.0578208  -0.0303578  268 LEU   B CA   
4468 C  C    . LEU   B 268 ? 0.265617  0.212481 0.1486    0.0127392   -0.0623568  -0.0396183  268 LEU   B C    
4469 O  O    . LEU   B 268 ? 0.267077  0.216313 0.145255  0.0214271   -0.0518987  -0.0455278  268 LEU   B O    
4470 C  CB   . LEU   B 268 ? 0.256888  0.189631 0.137831  0.00642475  -0.0523299  -0.0210271  268 LEU   B CB   
4471 C  CG   . LEU   B 268 ? 0.251001  0.190723 0.131989  0.00204159  -0.0491709  -0.020096   268 LEU   B CG   
4472 C  CD1  . LEU   B 268 ? 0.242434  0.18631  0.138908  0.00203598  -0.0442637  -0.0188295  268 LEU   B CD1  
4473 C  CD2  . LEU   B 268 ? 0.259736  0.20631  0.138124  -0.00219181 -0.0527923  -0.0277963  268 LEU   B CD2  
4474 N  N    . LYS   B 269 ? 0.275254  0.231613 0.181553  0.0315536   -0.0618804  -0.0446661  269 LYS   B N    
4475 C  CA   . LYS   B 269 ? 0.293645  0.257635 0.215028  0.041757    -0.0617632  -0.0472986  269 LYS   B CA   
4476 C  C    . LYS   B 269 ? 0.266915  0.251145 0.215661  0.0422312   -0.0574938  -0.0624843  269 LYS   B C    
4477 O  O    . LYS   B 269 ? 0.2749    0.249322 0.233298  0.047299    -0.0654827  -0.0731378  269 LYS   B O    
4478 C  CB   . LYS   B 269 ? 0.324401  0.273619 0.23679   0.0405518   -0.060466   -0.0389096  269 LYS   B CB   
4479 C  CG   . LYS   B 269 ? 0.364652  0.300123 0.277679  0.0509988   -0.0410748  -0.0417423  269 LYS   B CG   
4480 C  CD   . LYS   B 269 ? 0.393778  0.316522 0.310926  0.0382519   -0.0205453  -0.0337679  269 LYS   B CD   
4481 C  CE   . LYS   B 269 ? 0.401043  0.320129 0.3383    0.035973    0.00595812  -0.0455089  269 LYS   B CE   
4482 N  NZ   . LYS   B 269 ? 0.414738  0.338537 0.369168  0.0368188   0.0372553   -0.0289147  269 LYS   B NZ   
4483 N  N    . GLU   B 270 ? 0.267519  0.257748 0.211164  0.0518496   -0.0512598  -0.0594477  270 GLU   B N    
4484 C  CA   . GLU   B 270 ? 0.268021  0.270419 0.20347   0.0491312   -0.0444618  -0.0689682  270 GLU   B CA   
4485 C  C    . GLU   B 270 ? 0.245799  0.258717 0.169255  0.0419602   -0.0280527  -0.0694599  270 GLU   B C    
4486 O  O    . GLU   B 270 ? 0.247125  0.277995 0.199997  0.050372    -0.00810029 -0.0698032  270 GLU   B O    
4487 C  CB   . GLU   B 270 ? 0.280461  0.292553 0.203481  0.0404817   -0.0446671  -0.0764265  270 GLU   B CB   
4488 C  CG   . GLU   B 270 ? 0.302012  0.311026 0.230782  0.0486557   -0.0478283  -0.0781167  270 GLU   B CG   
4489 C  CD   . GLU   B 270 ? 0.311852  0.344652 0.255626  0.0530091   -0.0360894  -0.0720001  270 GLU   B CD   
4490 O  OE1  . GLU   B 270 ? 0.37492   0.393876 0.264124  0.0372642   -0.0200448  -0.0590637  270 GLU   B OE1  
4491 O  OE2  . GLU   B 270 ? 0.329829  0.351479 0.295244  0.0445298   -0.0402037  -0.0633923  270 GLU   B OE2  
4492 N  N    . LEU   B 271 ? 0.248391  0.259503 0.163703  0.0452635   -0.0238281  -0.0574155  271 LEU   B N    
4493 C  CA   . LEU   B 271 ? 0.232408  0.26158  0.168501  0.0452637   -0.0247871  -0.0552589  271 LEU   B CA   
4494 C  C    . LEU   B 271 ? 0.219759  0.271394 0.184632  0.0452451   -0.0154217  -0.0576728  271 LEU   B C    
4495 O  O    . LEU   B 271 ? 0.226805  0.313586 0.215402  0.0291128   -0.0173801  -0.0491952  271 LEU   B O    
4496 C  CB   . LEU   B 271 ? 0.226444  0.26748  0.170043  0.0490563   -0.0251704  -0.0363609  271 LEU   B CB   
4497 C  CG   . LEU   B 271 ? 0.224193  0.276907 0.180032  0.04891     -0.0295139  -0.0207178  271 LEU   B CG   
4498 C  CD1  . LEU   B 271 ? 0.226037  0.273958 0.184975  0.0550317   -0.0314497  -0.0115315  271 LEU   B CD1  
4499 C  CD2  . LEU   B 271 ? 0.22595   0.300202 0.194655  0.0440698   -0.0295797  -0.00953801 271 LEU   B CD2  
4500 N  N    . LEU   B 272 ? 0.239397  0.281543 0.192966  0.0462424   -0.0194712  -0.0684307  272 LEU   B N    
4501 C  CA   . LEU   B 272 ? 0.235253  0.295042 0.214457  0.0356546   -0.0150047  -0.0724405  272 LEU   B CA   
4502 C  C    . LEU   B 272 ? 0.236046  0.305276 0.236107  0.0411538   -0.011394   -0.0775529  272 LEU   B C    
4503 O  O    . LEU   B 272 ? 0.240312  0.331874 0.255869  0.0333734   -0.0174125  -0.0872252  272 LEU   B O    
4504 C  CB   . LEU   B 272 ? 0.233088  0.287752 0.218419  0.0365949   -0.0242009  -0.0691544  272 LEU   B CB   
4505 C  CG   . LEU   B 272 ? 0.245217  0.28183  0.197351  0.0375814   -0.0345125  -0.071606   272 LEU   B CG   
4506 C  CD1  . LEU   B 272 ? 0.255103  0.286817 0.202383  0.0382158   -0.0392042  -0.0740914  272 LEU   B CD1  
4507 C  CD2  . LEU   B 272 ? 0.247786  0.282034 0.193489  0.0372368   -0.035491   -0.0697086  272 LEU   B CD2  
4508 N  N    . GLN   B 273 ? 0.259354  0.32486  0.265837  0.0451869   -0.00107324 -0.0958476  273 GLN   B N    
4509 C  CA   . GLN   B 273 ? 0.282157  0.338372 0.286978  0.0536968   0.00882375  -0.0971671  273 GLN   B CA   
4510 C  C    . GLN   B 273 ? 0.283909  0.378799 0.281262  0.053733    0.0323394   -0.0925127  273 GLN   B C    
4511 O  O    . GLN   B 273 ? 0.278459  0.449387 0.332733  0.0754672   0.0332757   -0.072639   273 GLN   B O    
4512 C  CB   . GLN   B 273 ? 0.309291  0.334151 0.319553  0.0574215   -0.00801964 -0.104198   273 GLN   B CB   
4513 C  CG   . GLN   B 273 ? 0.321875  0.315957 0.330715  0.0590094   -0.0286816  -0.112323   273 GLN   B CG   
4514 C  CD   . GLN   B 273 ? 0.337275  0.306902 0.344111  0.0436792   -0.0445634  -0.130837   273 GLN   B CD   
4515 O  OE1  . GLN   B 273 ? 0.399973  0.31669  0.382301  0.0480638   -0.0414082  -0.170818   273 GLN   B OE1  
4516 N  NE2  . GLN   B 273 ? 0.34483   0.296194 0.354299  0.0318618   -0.0589393  -0.123839   273 GLN   B NE2  
4517 N  N    . ASN   B 274 ? 0.2957    0.369586 0.261502  0.0610511   0.046068    -0.0874392  274 ASN   B N    
4518 C  CA   . ASN   B 274 ? 0.305137  0.38589  0.261673  0.0524414   0.052336    -0.0853931  274 ASN   B CA   
4519 C  C    . ASN   B 274 ? 0.310339  0.379168 0.260725  0.0355943   0.0730676   -0.0703939  274 ASN   B C    
4520 O  O    . ASN   B 274 ? 0.358024  0.438494 0.28593   0.0251729   0.0850915   -0.048254   274 ASN   B O    
4521 C  CB   . ASN   B 274 ? 0.334118  0.39458  0.281744  0.0560373   0.0480228   -0.101123   274 ASN   B CB   
4522 C  CG   . ASN   B 274 ? 0.350001  0.408163 0.30511   0.0672639   0.0373779   -0.103481   274 ASN   B CG   
4523 O  OD1  . ASN   B 274 ? 0.386785  0.450944 0.372367  0.0803039   0.0776706   -0.0883548  274 ASN   B OD1  
4524 N  ND2  . ASN   B 274 ? 0.364086  0.403114 0.318684  0.0667357   0.0256988   -0.101552   274 ASN   B ND2  
4525 N  N    . GLY   B 275 ? 0.30741   0.359676 0.238998  0.0226807   0.0710241   -0.0622115  275 GLY   B N    
4526 C  CA   . GLY   B 275 ? 0.305449  0.354888 0.233189  0.0189468   0.0745033   -0.0512516  275 GLY   B CA   
4527 C  C    . GLY   B 275 ? 0.295252  0.336504 0.230975  0.0115581   0.0737038   -0.0535282  275 GLY   B C    
4528 O  O    . GLY   B 275 ? 0.286262  0.338458 0.228104  0.0109833   0.0431444   -0.0619695  275 GLY   B O    
4529 N  N    . MET   B 276 ? 0.29255   0.340346 0.232939  0.0125867   0.075124    -0.0525875  276 MET   B N    
4530 C  CA   . MET   B 276 ? 0.298882  0.358572 0.251503  0.00670409  0.0640642   -0.0405555  276 MET   B CA   
4531 C  C    . MET   B 276 ? 0.297385  0.383149 0.235638  -0.00391651 0.0730616   -0.0203694  276 MET   B C    
4532 O  O    . MET   B 276 ? 0.306951  0.390193 0.218003  -0.00155615 0.0885305   -0.0186331  276 MET   B O    
4533 C  CB   . MET   B 276 ? 0.292829  0.34787  0.253343  0.00251999  0.0362757   -0.0274886  276 MET   B CB   
4534 C  CG   . MET   B 276 ? 0.295415  0.34475  0.243401  0.00374013  0.006074    -0.0240498  276 MET   B CG   
4535 S  SD   . MET   B 276 ? 0.268473  0.346376 0.209617  9.117e-05   -0.00215074 -0.0201913  276 MET   B SD   
4536 C  CE   . MET   B 276 ? 0.301422  0.322746 0.205865  -0.00334788 -0.00410517 -0.013036   276 MET   B CE   
4537 N  N    . ASN   B 277 ? 0.306714  0.427909 0.232726  0.00399516  0.0760508   -0.0317448  277 ASN   B N    
4538 C  CA   . ASN   B 277 ? 0.32208   0.4551   0.237769  -0.0045798  0.0978166   -0.0281983  277 ASN   B CA   
4539 C  C    . ASN   B 277 ? 0.323699  0.450666 0.205041  -0.00651491 0.0924396   -0.0337009  277 ASN   B C    
4540 O  O    . ASN   B 277 ? 0.363135  0.480154 0.231283  -0.0145943  0.0771031   -0.0445244  277 ASN   B O    
4541 C  CB   . ASN   B 277 ? 0.357218  0.479318 0.280055  -0.00642881 0.0917021   -0.0210545  277 ASN   B CB   
4542 C  CG   . ASN   B 277 ? 0.392371  0.52659  0.362404  0.0056941   0.0696088   -0.0125673  277 ASN   B CG   
4543 O  OD1  . ASN   B 277 ? 0.466298  0.558234 0.407637  -0.0261841  0.0374111   0.0166829   277 ASN   B OD1  
4544 N  ND2  . ASN   B 277 ? 0.395158  0.548611 0.408957  0.0171772   0.0601667   -0.0149784  277 ASN   B ND2  
4545 N  N    . GLY   B 278 ? 0.324915  0.440135 0.209975  -0.0108943  0.103992    0.00016793  278 GLY   B N    
4546 C  CA   . GLY   B 278 ? 0.332523  0.432643 0.203986  -0.00883448 0.0956714   0.00363563  278 GLY   B CA   
4547 C  C    . GLY   B 278 ? 0.333783  0.414809 0.183615  -0.00878261 0.0772899   0.0158742   278 GLY   B C    
4548 O  O    . GLY   B 278 ? 0.36344   0.435111 0.197837  -0.0143836  0.0639536   0.0464955   278 GLY   B O    
4549 N  N    . ARG   B 279 ? 0.344909  0.399991 0.160585  -0.00432125 0.06674     0.0171209   279 ARG   B N    
4550 C  CA   . ARG   B 279 ? 0.328949  0.3673   0.150207  -0.00236651 0.0421524   0.00797712  279 ARG   B CA   
4551 C  C    . ARG   B 279 ? 0.274342  0.351421 0.137812  0.00247986  0.0230393   0.0103482   279 ARG   B C    
4552 O  O    . ARG   B 279 ? 0.262972  0.351847 0.184998  0.0224463   0.0141933   -0.00422164 279 ARG   B O    
4553 C  CB   . ARG   B 279 ? 0.381576  0.374826 0.171548  -0.00222437 0.0523817   0.0101356   279 ARG   B CB   
4554 C  CG   . ARG   B 279 ? 0.421249  0.377561 0.19182   0.00074659  0.0623783   -0.0088089  279 ARG   B CG   
4555 C  CD   . ARG   B 279 ? 0.453526  0.396964 0.218731  -0.00154595 0.0658599   0.0010397   279 ARG   B CD   
4556 N  NE   . ARG   B 279 ? 0.482911  0.398206 0.226652  0.00305856  0.06422     -0.00429101 279 ARG   B NE   
4557 C  CZ   . ARG   B 279 ? 0.506044  0.406713 0.286574  0.00734209  0.0589483   -0.0167277  279 ARG   B CZ   
4558 N  NH1  . ARG   B 279 ? 0.519327  0.401953 0.304805  -0.00552114 0.0624217   -0.0330554  279 ARG   B NH1  
4559 N  NH2  . ARG   B 279 ? 0.502759  0.415036 0.33216   0.0189557   0.0553191   -0.0242623  279 ARG   B NH2  
4560 N  N    . THR   B 280 ? 0.248306  0.319251 0.0957303 -0.0114278  0.0081009   0.0112726   280 THR   B N    
4561 C  CA   . THR   B 280 ? 0.231039  0.296878 0.100487  -0.0193764  -0.00384019 0.00563047  280 THR   B CA   
4562 C  C    . THR   B 280 ? 0.226513  0.272548 0.0969203 -0.0275295  -0.010975   -0.00089363 280 THR   B C    
4563 O  O    . THR   B 280 ? 0.234037  0.276234 0.0871113 -0.0304378  -0.0203238  0.00397814  280 THR   B O    
4564 C  CB   . THR   B 280 ? 0.257469  0.298259 0.111161  -0.0273546  -0.00630007 0.0161514   280 THR   B CB   
4565 O  OG1  . THR   B 280 ? 0.273049  0.309521 0.130435  -0.0158073  -0.017371   0.0208593   280 THR   B OG1  
4566 C  CG2  . THR   B 280 ? 0.277781  0.305792 0.129971  -0.0326722  0.00268614  0.027134    280 THR   B CG2  
4567 N  N    . ILE   B 281 ? 0.193201  0.253286 0.0865911 -0.0169411  -0.0247676  0.00641937  281 ILE   B N    
4568 C  CA   . ILE   B 281 ? 0.185253  0.245946 0.1039    -0.0118352  -0.0236472  0.0095293   281 ILE   B CA   
4569 C  C    . ILE   B 281 ? 0.176918  0.241826 0.110472  -0.00688992 -0.0184078  0.0240824   281 ILE   B C    
4570 O  O    . ILE   B 281 ? 0.185141  0.237063 0.120858  -0.00750219 -0.0175621  0.0208665   281 ILE   B O    
4571 C  CB   . ILE   B 281 ? 0.187176  0.244503 0.100177  -0.0109551  -0.0199446  0.00532504  281 ILE   B CB   
4572 C  CG1  . ILE   B 281 ? 0.192117  0.240192 0.11336   -0.00991591 -0.0262753  0.00364941  281 ILE   B CG1  
4573 C  CG2  . ILE   B 281 ? 0.189293  0.248437 0.095721  -0.0110268  -0.0152311  0.00201739  281 ILE   B CG2  
4574 C  CD1  . ILE   B 281 ? 0.192613  0.236949 0.133156  -0.00264983 -0.0219457  0.00797727  281 ILE   B CD1  
4575 N  N    . LEU   B 282 ? 0.176713  0.254565 0.123149  -0.00382932 -0.0165593  0.0278192   282 LEU   B N    
4576 C  CA   . LEU   B 282 ? 0.18911   0.251478 0.138184  0.00462842  -0.0192108  0.0324115   282 LEU   B CA   
4577 C  C    . LEU   B 282 ? 0.200717  0.270475 0.177973  0.0061182   -0.00919548 0.0491319   282 LEU   B C    
4578 O  O    . LEU   B 282 ? 0.213077  0.258498 0.200855  0.00291262  0.00817862  0.0513795   282 LEU   B O    
4579 C  CB   . LEU   B 282 ? 0.197856  0.238859 0.133155  0.00363579  -0.0192381  0.0218612   282 LEU   B CB   
4580 C  CG   . LEU   B 282 ? 0.209961  0.241819 0.125575  -0.00145603 -0.00904306 0.00835282  282 LEU   B CG   
4581 C  CD1  . LEU   B 282 ? 0.222967  0.241413 0.127173  0.00152525  -0.00563671 0.00949989  282 LEU   B CD1  
4582 C  CD2  . LEU   B 282 ? 0.210369  0.240692 0.121441  -0.00299675 -0.0097649  0.00391675  282 LEU   B CD2  
4583 N  N    . GLY   B 283 ? 0.197173  0.284617 0.182477  0.0147841   -0.0117967  0.0691751   283 GLY   B N    
4584 C  CA   . GLY   B 283 ? 0.202364  0.292512 0.216689  0.0125881   -0.00997497 0.0901634   283 GLY   B CA   
4585 C  C    . GLY   B 283 ? 0.208354  0.294406 0.227783  0.0104231   -0.00834431 0.0932076   283 GLY   B C    
4586 O  O    . GLY   B 283 ? 0.226167  0.310547 0.342928  -0.00296663 -0.00936483 0.131329    283 GLY   B O    
4587 N  N    . SER   B 284 ? 0.195351  0.273123 0.162113  0.0130656   0.0037982   0.0663801   284 SER   B N    
4588 C  CA   . SER   B 284 ? 0.201196  0.272928 0.13824   0.00748456  0.00794583  0.0421258   284 SER   B CA   
4589 C  C    . SER   B 284 ? 0.196803  0.25117  0.121234  0.00034645  -0.00130488 0.0317524   284 SER   B C    
4590 O  O    . SER   B 284 ? 0.182553  0.260916 0.139566  -0.00960751 -0.00183802 0.0171885   284 SER   B O    
4591 C  CB   . SER   B 284 ? 0.216954  0.287112 0.13303   0.0134868   0.0087499   0.0321501   284 SER   B CB   
4592 O  OG   . SER   B 284 ? 0.234696  0.313187 0.157995  0.0287819   0.0113452   -0.00200212 284 SER   B OG   
4593 N  N    . ALA   B 285 ? 0.205849  0.250466 0.136679  -0.00657728 0.00330795  0.0327607   285 ALA   B N    
4594 C  CA   . ALA   B 285 ? 0.207297  0.264102 0.133064  -0.0084804  0.0128813   0.0166003   285 ALA   B CA   
4595 C  C    . ALA   B 285 ? 0.215479  0.267907 0.132333  0.00434033  0.0112113   0.00716273  285 ALA   B C    
4596 O  O    . ALA   B 285 ? 0.232019  0.295735 0.16778   0.01227     0.0180816   -0.0275278  285 ALA   B O    
4597 C  CB   . ALA   B 285 ? 0.216498  0.28042  0.146822  -0.0125704  0.0210901   0.0181695   285 ALA   B CB   
4598 N  N    . LEU   B 286 ? 0.19661   0.249495 0.120822  -0.00341337 0.0136787   0.0149885   286 LEU   B N    
4599 C  CA   . LEU   B 286 ? 0.21207   0.256059 0.136627  -0.00675376 0.00155963  0.0230096   286 LEU   B CA   
4600 C  C    . LEU   B 286 ? 0.192677  0.237221 0.121992  0.00077579  0.00409611  0.00268488  286 LEU   B C    
4601 O  O    . LEU   B 286 ? 0.195283  0.252811 0.127758  0.00175046  0.0115615   0.0174463   286 LEU   B O    
4602 C  CB   . LEU   B 286 ? 0.239126  0.283824 0.141105  -0.0232809  -0.00883523 0.0296909   286 LEU   B CB   
4603 C  CG   . LEU   B 286 ? 0.263282  0.312137 0.17727   -0.0298433  -0.00498627 0.0490596   286 LEU   B CG   
4604 C  CD1  . LEU   B 286 ? 0.277187  0.324159 0.19248   -0.0366779  -0.0150682  0.0529517   286 LEU   B CD1  
4605 C  CD2  . LEU   B 286 ? 0.272896  0.338547 0.202792  -0.0224534  -0.00434516 0.0544343   286 LEU   B CD2  
4606 N  N    . LEU   B 287 ? 0.177324  0.209927 0.116457  -0.00023811 0.00440226  -0.0100556  287 LEU   B N    
4607 C  CA   . LEU   B 287 ? 0.185938  0.207643 0.116696  -0.00069258 0.00083587  -0.0237834  287 LEU   B CA   
4608 C  C    . LEU   B 287 ? 0.184218  0.209179 0.107595  -0.00143799 -0.0127744  -0.0271278  287 LEU   B C    
4609 O  O    . LEU   B 287 ? 0.19769   0.260878 0.158153  0.00849256  -0.0320493  -0.0727344  287 LEU   B O    
4610 C  CB   . LEU   B 287 ? 0.209356  0.209523 0.121404  0.00231812  -0.00608934 -0.022561   287 LEU   B CB   
4611 C  CG   . LEU   B 287 ? 0.236648  0.219524 0.126776  0.00716547  -0.00611923 -0.0264436  287 LEU   B CG   
4612 C  CD1  . LEU   B 287 ? 0.261604  0.221775 0.142363  0.0116453   -0.0144261  -0.0287706  287 LEU   B CD1  
4613 C  CD2  . LEU   B 287 ? 0.253671  0.234666 0.155348  0.00480192  -0.00921953 -0.036304   287 LEU   B CD2  
4614 N  N    . GLU   B 288 ? 0.181974  0.20343  0.0829491 -0.0090604  -0.0212113  -0.0145596  288 GLU   B N    
4615 C  CA   . GLU   B 288 ? 0.19043   0.20366  0.0797699 -0.00906489 -0.0158241  -0.0116     288 GLU   B CA   
4616 C  C    . GLU   B 288 ? 0.168131  0.188961 0.0742099 -0.01021    -0.0204713  -0.0154731  288 GLU   B C    
4617 O  O    . GLU   B 288 ? 0.164824  0.192365 0.0579966 -0.015799   -0.0191273  -0.0217674  288 GLU   B O    
4618 C  CB   . GLU   B 288 ? 0.214706  0.226374 0.0903118 -0.0069307  -0.0270335  -0.00135501 288 GLU   B CB   
4619 C  CG   . GLU   B 288 ? 0.255614  0.249182 0.112379  0.00390234  -0.0304631  -0.00162861 288 GLU   B CG   
4620 C  CD   . GLU   B 288 ? 0.312874  0.271685 0.146697  -0.0131143  -0.0236943  0.00576873  288 GLU   B CD   
4621 O  OE1  . GLU   B 288 ? 0.324368  0.264664 0.123155  -0.00123448 -0.00702864 0.0143466   288 GLU   B OE1  
4622 O  OE2  . GLU   B 288 ? 0.388282  0.291436 0.167471  -0.012329   -0.0186947  0.0226039   288 GLU   B OE2  
4623 N  N    . ASP   B 289 ? 0.165754  0.189573 0.070075  -0.00900342 -0.0163763  -0.0171729  289 ASP   B N    
4624 C  CA   . ASP   B 289 ? 0.161102  0.183088 0.0727243 0.00046473  -0.0236519  -0.0162208  289 ASP   B CA   
4625 C  C    . ASP   B 289 ? 0.162475  0.182116 0.0719458 0.00776989  -0.0188963  -0.00844259 289 ASP   B C    
4626 O  O    . ASP   B 289 ? 0.164455  0.194708 0.0722566 -0.00033407 -0.0338743  -0.00830773 289 ASP   B O    
4627 C  CB   . ASP   B 289 ? 0.16447   0.195218 0.0820572 0.00176283  -0.0257309  -0.0219972  289 ASP   B CB   
4628 C  CG   . ASP   B 289 ? 0.167072  0.198997 0.0926019 0.00443532  -0.0311989  -0.0266931  289 ASP   B CG   
4629 O  OD1  . ASP   B 289 ? 0.177326  0.208906 0.101333  0.00256757  -0.0442479  -0.0230586  289 ASP   B OD1  
4630 O  OD2  . ASP   B 289 ? 0.167782  0.223603 0.117242  0.0113548   -0.0409034  -0.0329314  289 ASP   B OD2  
4631 N  N    . GLU   B 290 ? 0.16455   0.179026 0.0702855 0.00863407  -0.0195307  -0.00919575 290 GLU   B N    
4632 C  CA   . GLU   B 290 ? 0.162507  0.188295 0.0871252 0.0145468   -0.0143964  -0.00932572 290 GLU   B CA   
4633 C  C    . GLU   B 290 ? 0.164943  0.194587 0.0838908 0.0157251   -0.0177683  -0.0128304  290 GLU   B C    
4634 O  O    . GLU   B 290 ? 0.179573  0.21572  0.113605  0.023352    -0.00840321 -0.0273949  290 GLU   B O    
4635 C  CB   . GLU   B 290 ? 0.183038  0.195409 0.0975425 0.0150548   -0.0124492  -0.00920652 290 GLU   B CB   
4636 C  CG   . GLU   B 290 ? 0.182796  0.211293 0.111547  0.0109754   -0.0075412  -0.0133343  290 GLU   B CG   
4637 C  CD   . GLU   B 290 ? 0.187791  0.213772 0.118173  0.0163618   -0.0171834  -0.0210875  290 GLU   B CD   
4638 O  OE1  . GLU   B 290 ? 0.181378  0.221923 0.134537  0.0129151   -0.0155709  -0.0193576  290 GLU   B OE1  
4639 O  OE2  . GLU   B 290 ? 0.195077  0.216316 0.147759  0.0197925   -0.042839   -0.0289032  290 GLU   B OE2  
4640 N  N    . PHE   B 291 ? 0.148192  0.198001 0.0818769 0.0119924   -0.0188634  -0.0113714  291 PHE   B N    
4641 C  CA   . PHE   B 291 ? 0.150525  0.2016   0.0996488 0.0134514   -0.0205473  -0.0142904  291 PHE   B CA   
4642 C  C    . PHE   B 291 ? 0.148513  0.199823 0.103086  0.00694045  -0.0208187  -0.0167244  291 PHE   B C    
4643 O  O    . PHE   B 291 ? 0.153602  0.198916 0.102545  0.0155341   -0.0155509  -0.0145859  291 PHE   B O    
4644 C  CB   . PHE   B 291 ? 0.160824  0.209884 0.0986772 0.0151912   -0.0189387  -0.0181673  291 PHE   B CB   
4645 C  CG   . PHE   B 291 ? 0.171076  0.223292 0.0987744 0.0221068   -0.0228267  -0.0157002  291 PHE   B CG   
4646 C  CD1  . PHE   B 291 ? 0.179024  0.233811 0.101532  0.0281211   -0.0133577  -0.0201059  291 PHE   B CD1  
4647 C  CD2  . PHE   B 291 ? 0.173536  0.236458 0.11581   0.0293744   -0.0156821  -0.0203007  291 PHE   B CD2  
4648 C  CE1  . PHE   B 291 ? 0.18012   0.229869 0.119464  0.0292928   -0.0189009  -0.0147899  291 PHE   B CE1  
4649 C  CE2  . PHE   B 291 ? 0.194179  0.242236 0.123724  0.0347477   -0.00522535 -0.00876657 291 PHE   B CE2  
4650 C  CZ   . PHE   B 291 ? 0.193271  0.243915 0.1144    0.0325879   -0.0181844  -0.00946355 291 PHE   B CZ   
4651 N  N    . THR   B 292 ? 0.157897  0.21265  0.101681  0.0028828   -0.0206544  -0.0124458  292 THR   B N    
4652 C  CA   . THR   B 292 ? 0.156012  0.230918 0.10671   -0.0025263  -0.0138377  -0.00718952 292 THR   B CA   
4653 C  C    . THR   B 292 ? 0.147439  0.24385  0.0917673 -0.0055347  -0.0136729  -0.0039478  292 THR   B C    
4654 O  O    . THR   B 292 ? 0.144931  0.24543  0.0953131 -0.00778548 -0.0118853  0.0038709   292 THR   B O    
4655 C  CB   . THR   B 292 ? 0.167903  0.249236 0.118462  0.00563962  -0.0173416  -0.0214844  292 THR   B CB   
4656 O  OG1  . THR   B 292 ? 0.160051  0.281362 0.125779  0.00278538  -0.0103433  -0.0292137  292 THR   B OG1  
4657 C  CG2  . THR   B 292 ? 0.173925  0.250798 0.123134  0.00943652  -0.0159712  -0.0282384  292 THR   B CG2  
4658 N  N    . PRO   B 293 ? 0.151182  0.257747 0.0869448 -0.012118   -0.0157019  0.00408041  293 PRO   B N    
4659 C  CA   . PRO   B 293 ? 0.155274  0.270713 0.0944109 -0.0180657  -0.0161669  0.00690897  293 PRO   B CA   
4660 C  C    . PRO   B 293 ? 0.162181  0.289073 0.109686  -0.0150453  -0.0119906  -0.00237586 293 PRO   B C    
4661 O  O    . PRO   B 293 ? 0.154846  0.311764 0.116482  -0.0131127  -0.0166496  0.00790496  293 PRO   B O    
4662 C  CB   . PRO   B 293 ? 0.169957  0.266613 0.11382   -0.013408   -0.0156873  0.00542204  293 PRO   B CB   
4663 C  CG   . PRO   B 293 ? 0.169432  0.263469 0.108517  -0.0133638  -0.0115931  0.00613566  293 PRO   B CG   
4664 C  CD   . PRO   B 293 ? 0.164098  0.257902 0.0961443 -0.00950293 -0.0140485  0.00917213  293 PRO   B CD   
4665 N  N    . PHE   B 294 ? 0.161672  0.310928 0.104116  -0.0108857  -0.00979699 -0.0110754  294 PHE   B N    
4666 C  CA   . PHE   B 294 ? 0.185777  0.328191 0.141798  -0.00361271 -0.00214892 -0.0222467  294 PHE   B CA   
4667 C  C    . PHE   B 294 ? 0.168957  0.314332 0.137371  -0.00097198 -0.00951976 -0.0283969  294 PHE   B C    
4668 O  O    . PHE   B 294 ? 0.170886  0.353249 0.14932   -4.04e-06   -0.0125275  -0.0379797  294 PHE   B O    
4669 C  CB   . PHE   B 294 ? 0.220543  0.349117 0.160784  -0.00351538 0.00618875  -0.0357124  294 PHE   B CB   
4670 C  CG   . PHE   B 294 ? 0.2811    0.388401 0.285335  0.0211967   0.00895679  -0.0294707  294 PHE   B CG   
4671 C  CD1  . PHE   B 294 ? 0.322425  0.421324 0.348466  0.021459    0.0442293   -0.0189209  294 PHE   B CD1  
4672 C  CD2  . PHE   B 294 ? 0.332056  0.402461 0.356161  0.0245742   0.00744391  -0.0363959  294 PHE   B CD2  
4673 C  CE1  . PHE   B 294 ? 0.344535  0.422158 0.404736  0.0354911   0.0308944   -0.033712   294 PHE   B CE1  
4674 C  CE2  . PHE   B 294 ? 0.347766  0.411945 0.365489  0.0383425   0.00474055  -0.0383521  294 PHE   B CE2  
4675 C  CZ   . PHE   B 294 ? 0.36143   0.41515  0.383943  0.0343114   0.0210756   -0.0362648  294 PHE   B CZ   
4676 N  N    . ASP   B 295 ? 0.156813  0.309901 0.126323  0.00727386  -0.0184792  -0.0289487  295 ASP   B N    
4677 C  CA   . ASP   B 295 ? 0.170622  0.302947 0.133554  0.0182476   -0.0275664  -0.0309932  295 ASP   B CA   
4678 C  C    . ASP   B 295 ? 0.17339   0.301242 0.129691  0.0193849   -0.0385547  -0.0166624  295 ASP   B C    
4679 O  O    . ASP   B 295 ? 0.18672   0.303389 0.172271  0.0334443   -0.051811   -0.019465   295 ASP   B O    
4680 C  CB   . ASP   B 295 ? 0.164709  0.301599 0.126319  0.0288409   -0.0263612  -0.030053   295 ASP   B CB   
4681 C  CG   . ASP   B 295 ? 0.173967  0.304851 0.130259  0.0346026   -0.0277079  -0.035958   295 ASP   B CG   
4682 O  OD1  . ASP   B 295 ? 0.172937  0.328156 0.176213  0.0445607   -0.01321    -0.0530468  295 ASP   B OD1  
4683 O  OD2  . ASP   B 295 ? 0.16524   0.296308 0.130521  0.0357002   -0.0473828  -0.0369942  295 ASP   B OD2  
4684 N  N    . VAL   B 296 ? 0.156056  0.300028 0.0980809 0.0142846   -0.0362001  -0.0135157  296 VAL   B N    
4685 C  CA   . VAL   B 296 ? 0.163961  0.326054 0.102452  0.00337779  -0.048537   -0.00474069 296 VAL   B CA   
4686 C  C    . VAL   B 296 ? 0.170103  0.356339 0.12271   -0.0103227  -0.0419439  0.0134366   296 VAL   B C    
4687 O  O    . VAL   B 296 ? 0.165379  0.392985 0.149312  -0.0107031  -0.0594523  0.0199399   296 VAL   B O    
4688 C  CB   . VAL   B 296 ? 0.173447  0.316329 0.110411  -0.00042151 -0.0414764  -0.0128287  296 VAL   B CB   
4689 C  CG1  . VAL   B 296 ? 0.177814  0.326457 0.125736  -0.0148829  -0.0357625  -0.0204448  296 VAL   B CG1  
4690 C  CG2  . VAL   B 296 ? 0.166725  0.293009 0.125609  0.00483399  -0.0392935  -0.0123575  296 VAL   B CG2  
4691 N  N    . VAL   B 297 ? 0.161542  0.383965 0.144155  -0.0203441  -0.0326383  0.0222538   297 VAL   B N    
4692 C  CA   . VAL   B 297 ? 0.170739  0.416163 0.195094  -0.0225926  -0.0198966  0.0266579   297 VAL   B CA   
4693 C  C    . VAL   B 297 ? 0.154906  0.437399 0.19519   -0.0027592  -0.0284613  0.0343612   297 VAL   B C    
4694 O  O    . VAL   B 297 ? 0.165707  0.475331 0.171253  -0.00679489 -0.03531    0.0215755   297 VAL   B O    
4695 C  CB   . VAL   B 297 ? 0.180905  0.413866 0.219034  -0.0187754  -0.0183459  0.0393506   297 VAL   B CB   
4696 C  CG1  . VAL   B 297 ? 0.186084  0.427693 0.236706  -0.0250388  -0.0166148  0.0409939   297 VAL   B CG1  
4697 C  CG2  . VAL   B 297 ? 0.200274  0.426129 0.24457   -0.0196113  -0.00887833 0.0376252   297 VAL   B CG2  
4698 N  N    . ARG   B 298 ? 0.182127  0.449254 0.204352  0.00685663  -0.0370714  0.028403    298 ARG   B N    
4699 C  CA   . ARG   B 298 ? 0.202024  0.476258 0.241624  0.0333135   -0.037322   0.0275347   298 ARG   B CA   
4700 C  C    . ARG   B 298 ? 0.158909  0.478185 0.22894   0.0268762   -0.0170402  0.0273736   298 ARG   B C    
4701 O  O    . ARG   B 298 ? 0.171905  0.52138  0.233752  0.0434132   -0.0257744  0.0373858   298 ARG   B O    
4702 C  CB   . ARG   B 298 ? 0.288862  0.495519 0.307676  0.0379428   -0.0459701  0.00859077  298 ARG   B CB   
4703 C  CG   . ARG   B 298 ? 0.398161  0.529522 0.384605  0.0567138   -0.0259685  0.00872409  298 ARG   B CG   
4704 C  CD   . ARG   B 298 ? 0.465182  0.57947  0.416663  0.0588273   -0.00741565 -0.0234747  298 ARG   B CD   
4705 N  NE   . ARG   B 298 ? 0.51671   0.617692 0.433439  0.0674328   0.0718703   -0.0213268  298 ARG   B NE   
4706 C  CZ   . ARG   B 298 ? 0.533562  0.610394 0.400188  0.108288    0.0963131   -0.0303287  298 ARG   B CZ   
4707 N  NH1  . ARG   B 298 ? 0.543119  0.616771 0.351016  0.112885    0.182064    0.00445351  298 ARG   B NH1  
4708 N  NH2  . ARG   B 298 ? 0.511442  0.640999 0.371271  0.144943    0.124663    -0.082418   298 ARG   B NH2  
4709 N  N    . GLN   B 299 ? 0.151445  0.427483 0.206906  0.0132395   -0.0190734  0.0234601   299 GLN   B N    
4710 C  CA   . GLN   B 299 ? 0.170589  0.394354 0.211481  0.00205293  -0.027357   0.0232237   299 GLN   B CA   
4711 C  C    . GLN   B 299 ? 0.179924  0.412452 0.219879  -0.0167238  -0.0492541  0.0427131   299 GLN   B C    
4712 O  O    . GLN   B 299 ? 0.211568  0.446014 0.303408  -0.0334154  -0.111155   0.0577933   299 GLN   B O    
4713 C  CB   . GLN   B 299 ? 0.167353  0.352474 0.16936   0.0076755   -0.02814    0.0117472   299 GLN   B CB   
4714 C  CG   . GLN   B 299 ? 0.167628  0.325435 0.154227  0.0117261   -0.0183141  0.00475513  299 GLN   B CG   
4715 C  CD   . GLN   B 299 ? 0.158326  0.310031 0.140602  0.0208807   -0.0122382  -0.00299668 299 GLN   B CD   
4716 O  OE1  . GLN   B 299 ? 0.162212  0.28518  0.122966  0.0234616   -0.0227553  -0.0101689  299 GLN   B OE1  
4717 N  NE2  . GLN   B 299 ? 0.161611  0.308373 0.145786  0.0168317   -0.0145559  0.00103545  299 GLN   B NE2  
4718 N  N    . CYS   B 300 ? 0.202266  0.4237   0.241093  -0.00467313 -0.0694294  0.0330879   300 CYS   B N    
4719 C  CA   . CYS   B 300 ? 0.23828   0.453789 0.242692  -0.00904172 -0.0808819  0.0167531   300 CYS   B CA   
4720 C  C    . CYS   B 300 ? 0.244419  0.456648 0.228193  -0.0249059  -0.0697638  0.0106799   300 CYS   B C    
4721 O  O    . CYS   B 300 ? 0.26758   0.460262 0.223568  -0.00874934 -0.0915121  0.00306702  300 CYS   B O    
4722 C  CB   . CYS   B 300 ? 0.269593  0.486846 0.280169  -0.00040913 -0.0789641  -0.0133605  300 CYS   B CB   
4723 S  SG   . CYS   B 300 ? 0.301473  0.568765 0.275807  -0.00277347 -0.0882803  -0.0698921  300 CYS   B SG   
4724 N  N    . SER   B 301 ? 0.254664  0.464288 0.235486  -0.0396081  -0.0585528  0.0187643   301 SER   B N    
4725 C  CA   . SER   B 301 ? 0.252401  0.464436 0.238204  -0.0416693  -0.0481637  0.0299842   301 SER   B CA   
4726 C  C    . SER   B 301 ? 0.253573  0.451251 0.247933  -0.0431976  -0.036927   0.0242932   301 SER   B C    
4727 O  O    . SER   B 301 ? 0.256349  0.421043 0.289872  -0.021047   -0.0215971  0.0128045   301 SER   B O    
4728 C  CB   . SER   B 301 ? 0.279558  0.503672 0.248624  -0.056077   -0.0305326  0.0346347   301 SER   B CB   
4729 O  OG   . SER   B 301 ? 0.30807   0.550808 0.215982  -0.0542824  -0.00615784 0.0360636   301 SER   B OG   
4730 N  N    . GLY   B 302 ? 0.257705  0.432251 0.227664  -0.0290442  -0.0471553  0.0299405   302 GLY   B N    
4731 C  CA   . GLY   B 302 ? 0.275155  0.433153 0.212854  -0.0261412  -0.0304428  0.029311    302 GLY   B CA   
4732 C  C    . GLY   B 302 ? 0.279103  0.436864 0.2177    -0.0191951  -0.0318439  0.0209374   302 GLY   B C    
4733 O  O    . GLY   B 302 ? 0.270026  0.447402 0.208727  -0.011729   -0.0417771  0.0187256   302 GLY   B O    
4734 N  N    . VAL   B 303 ? 0.271326  0.44866  0.203274  -0.0261325  -0.0248148  0.0186778   303 VAL   B N    
4735 C  CA   . VAL   B 303 ? 0.291747  0.445676 0.199687  -0.0281834  -0.0224905  0.0246221   303 VAL   B CA   
4736 C  C    . VAL   B 303 ? 0.283457  0.432021 0.19906   -0.0304797  -0.0165966  0.0425736   303 VAL   B C    
4737 O  O    . VAL   B 303 ? 0.272615  0.438791 0.242662  -0.0392547  0.0051643   0.0429307   303 VAL   B O    
4738 C  CB   . VAL   B 303 ? 0.293806  0.44374  0.210708  -0.030447   -0.01669    0.0276758   303 VAL   B CB   
4739 C  CG1  . VAL   B 303 ? 0.312211  0.459602 0.217655  -0.033137   -0.0227883  0.0203275   303 VAL   B CG1  
4740 C  CG2  . VAL   B 303 ? 0.310297  0.443321 0.210983  -0.0405715  -0.0161864  0.0331297   303 VAL   B CG2  
4741 N  N    . THR   B 304 ? 0.275977  0.414729 0.179417  -0.0201912  -0.0242637  0.0514443   304 THR   B N    
4742 C  CA   . THR   B 304 ? 0.288626  0.423814 0.16887   -0.0269516  -0.0265073  0.0490453   304 THR   B CA   
4743 C  C    . THR   B 304 ? 0.310843  0.446559 0.174989  -0.024304   -0.0449573  0.041959    304 THR   B C    
4744 O  O    . THR   B 304 ? 0.314205  0.44081  0.195886  -0.0477178  -0.0397256  0.0508182   304 THR   B O    
4745 C  CB   . THR   B 304 ? 0.278822  0.411691 0.182361  -0.0216312  -0.0146156  0.0606688   304 THR   B CB   
4746 O  OG1  . THR   B 304 ? 0.284964  0.427612 0.201441  -0.015801   -0.00124152 0.0707204   304 THR   B OG1  
4747 C  CG2  . THR   B 304 ? 0.263454  0.401521 0.178219  -0.0227756  -0.0162746  0.0496385   304 THR   B CG2  
4748 N  N    . PHE   B 305 ? 0.330418  0.464643 0.163781  -0.0155277  -0.0653784  0.0297731   305 PHE   B N    
4749 C  CA   . PHE   B 305 ? 0.358897  0.505748 0.168335  -0.00359894 -0.0781542  0.0200659   305 PHE   B CA   
4750 C  C    . PHE   B 305 ? 0.402696  0.527862 0.208198  0.0111557   -0.0814208  -0.00655988 305 PHE   B C    
4751 O  O    . PHE   B 305 ? 0.439135  0.557273 0.332776  0.0228557   -0.114406   0.0365345   305 PHE   B O    
4752 C  CB   . PHE   B 305 ? 0.3562    0.516576 0.214663  -0.00043994 -0.0690193  0.0230794   305 PHE   B CB   
4753 C  CG   . PHE   B 305 ? 0.325365  0.530903 0.229696  0.0092721   -0.078538   0.0359502   305 PHE   B CG   
4754 C  CD1  . PHE   B 305 ? 0.34227   0.540903 0.241121  0.00757105  -0.0748901  0.040405    305 PHE   B CD1  
4755 C  CD2  . PHE   B 305 ? 0.295288  0.540204 0.22643   0.0156062   -0.0830074  0.0469477   305 PHE   B CD2  
4756 C  CE1  . PHE   B 305 ? 0.335682  0.535591 0.260282  0.0131617   -0.0802636  0.0487882   305 PHE   B CE1  
4757 C  CE2  . PHE   B 305 ? 0.326481  0.544033 0.270939  0.0189705   -0.0805364  0.0551407   305 PHE   B CE2  
4758 C  CZ   . PHE   B 305 ? 0.349679  0.538801 0.267786  0.0119017   -0.0665735  0.0566171   305 PHE   B CZ   
4759 C  C4   . A1ITJ C .   ? 0.157828  0.359562 0.146547  -0.00865882 -0.0159976  -0.0445561  401 A1ITJ A C4   
4760 C  C5   . A1ITJ C .   ? 0.157433  0.330457 0.150362  -0.00720247 -0.0145283  -0.0349825  401 A1ITJ A C5   
4761 C  C7   . A1ITJ C .   ? 0.144701  0.291559 0.134315  -0.0141186  -0.00999106 -0.0243094  401 A1ITJ A C7   
4762 C  C8   . A1ITJ C .   ? 0.142794  0.287734 0.136457  -0.00898127 -0.00509007 -0.0271228  401 A1ITJ A C8   
4763 C  C10  . A1ITJ C .   ? 0.139146  0.296005 0.136195  -0.0141832  0.00070513  -0.029867   401 A1ITJ A C10  
4764 C  C13  . A1ITJ C .   ? 0.134249  0.25946  0.121964  -0.00147147 -0.00833065 -0.022705   401 A1ITJ A C13  
4765 C  C17  . A1ITJ C .   ? 0.150166  0.256363 0.137291  -0.00387479 -0.00628803 -0.0195725  401 A1ITJ A C17  
4766 C  C21  . A1ITJ C .   ? 0.14421   0.312893 0.14572   -0.0150102  -0.00903731 -0.0322749  401 A1ITJ A C21  
4767 C  C22  . A1ITJ C .   ? 0.161914  0.33784  0.171592  -0.015971   -0.0297491  -0.0376745  401 A1ITJ A C22  
4768 C  C24  . A1ITJ C .   ? 0.174167  0.385331 0.189034  -0.0143415  -0.0424535  -0.0186977  401 A1ITJ A C24  
4769 C  C28  . A1ITJ C .   ? 0.216225  0.380622 0.165761  -0.00528675 -0.0053943  -0.0532976  401 A1ITJ A C28  
4770 C  C1   . A1ITJ C .   ? 0.209916  0.41423  0.14959   0.0331989   0.0120538   -0.0473343  401 A1ITJ A C1   
4771 C  C2   . A1ITJ C .   ? 0.213091  0.411723 0.150791  0.0159505   0.00082139  -0.0379205  401 A1ITJ A C2   
4772 C  C3   . A1ITJ C .   ? 0.192556  0.390698 0.165145  0.00024429  -0.00683583 -0.0372995  401 A1ITJ A C3   
4773 N  N6   . A1ITJ C .   ? 0.147373  0.307568 0.147994  -0.0161978  -0.0088232  -0.0358371  401 A1ITJ A N6   
4774 N  N9   . A1ITJ C .   ? 0.1298    0.282955 0.132143  -0.0121879  -0.0097321  -0.0332536  401 A1ITJ A N9   
4775 C  C11  . A1ITJ C .   ? 0.142886  0.303532 0.15612   -0.0145878  -0.00689446 -0.0293046  401 A1ITJ A C11  
4776 C  C12  . A1ITJ C .   ? 0.136459  0.277176 0.122012  -0.00117286 -0.00672023 -0.0308682  401 A1ITJ A C12  
4777 C  C14  . A1ITJ C .   ? 0.14641   0.247434 0.118875  -0.00217334 -0.0116421  -0.0254108  401 A1ITJ A C14  
4778 N  N15  . A1ITJ C .   ? 0.141299  0.249709 0.123251  -0.00240718 -0.0127931  -0.0224105  401 A1ITJ A N15  
4779 C  C16  . A1ITJ C .   ? 0.132874  0.257359 0.124215  0.00155685  -0.00518942 -0.0272337  401 A1ITJ A C16  
4780 CL CL18 . A1ITJ C .   ? 0.198859  0.278753 0.28042   -0.00680997 0.00415486  -0.0259085  401 A1ITJ A CL18 
4781 C  C19  . A1ITJ C .   ? 0.15023   0.25924  0.147047  -0.00758948 -0.00708702 -0.0215303  401 A1ITJ A C19  
4782 O  O20  . A1ITJ C .   ? 0.143511  0.265239 0.120841  0.00220944  -0.00145536 -0.0319793  401 A1ITJ A O20  
4783 N  N23  . A1ITJ C .   ? 0.168665  0.370808 0.183443  -0.0040645  -0.0383653  -0.0298846  401 A1ITJ A N23  
4784 C  C25  . A1ITJ C .   ? 0.177015  0.393487 0.20846   -0.0120564  -0.0344665  -0.0128986  401 A1ITJ A C25  
4785 O  O26  . A1ITJ C .   ? 0.174566  0.341264 0.206466  -0.0353079  -0.0263822  -0.0526381  401 A1ITJ A O26  
4786 C  C27  . A1ITJ C .   ? 0.198141  0.361392 0.154146  -0.00465699 -0.0112546  -0.0512466  401 A1ITJ A C27  
4787 C  C29  . A1ITJ C .   ? 0.228048  0.395636 0.137413  -0.0060961  -0.0209078  -0.0596835  401 A1ITJ A C29  
4788 BR BR30 . A1ITJ C .   ? 0.236004  0.459283 0.167798  0.0153594   -0.0151927  -0.0772759  401 A1ITJ A BR30 
4789 C  C31  . A1ITJ C .   ? 0.199169  0.400036 0.120711  -0.00254283 -0.0225482  -0.0460267  401 A1ITJ A C31  
4790 C  C4   . A1ITJ D .   ? 0.226428  0.285692 0.162288  -0.0289904  -0.0129398  -0.0155915  401 A1ITJ B C4   
4791 C  C5   . A1ITJ D .   ? 0.20623   0.27717  0.13452   -0.0351431  -0.0116032  -0.0166076  401 A1ITJ B C5   
4792 C  C7   . A1ITJ D .   ? 0.190572  0.25306  0.101827  -0.0228444  -0.00525458 -0.0235248  401 A1ITJ B C7   
4793 C  C8   . A1ITJ D .   ? 0.18942   0.241894 0.095644  -0.0121761  -0.00250053 -0.030472   401 A1ITJ B C8   
4794 C  C10  . A1ITJ D .   ? 0.181421  0.239849 0.110923  -0.0161178  -0.00615223 -0.0206035  401 A1ITJ B C10  
4795 C  C13  . A1ITJ D .   ? 0.18174   0.22085  0.0915262 -0.0189733  0.00519286  -0.00913774 401 A1ITJ B C13  
4796 C  C17  . A1ITJ D .   ? 0.194375  0.24189  0.0833298 -0.0285522  0.020498    -0.0140906  401 A1ITJ B C17  
4797 C  C21  . A1ITJ D .   ? 0.191012  0.259896 0.119579  -0.0335535  -0.0150627  -0.0199806  401 A1ITJ B C21  
4798 C  C22  . A1ITJ D .   ? 0.194688  0.280868 0.146494  -0.0456332  -0.0187386  -0.0271091  401 A1ITJ B C22  
4799 C  C24  . A1ITJ D .   ? 0.222148  0.29034  0.155761  -0.0519433  -0.0238022  -0.0375259  401 A1ITJ B C24  
4800 C  C28  . A1ITJ D .   ? 0.253049  0.313394 0.203127  -0.0231428  0.00719202  -0.00399433 401 A1ITJ B C28  
4801 C  C1   . A1ITJ D .   ? 0.244055  0.320693 0.137519  -0.0203419  -0.0255294  -0.00886958 401 A1ITJ B C1   
4802 C  C2   . A1ITJ D .   ? 0.250434  0.310396 0.164714  -0.0204961  -0.0304637  -0.00497445 401 A1ITJ B C2   
4803 C  C3   . A1ITJ D .   ? 0.239868  0.298269 0.169574  -0.0294551  -0.0251915  -0.0124019  401 A1ITJ B C3   
4804 N  N6   . A1ITJ D .   ? 0.1858    0.262377 0.126887  -0.0341915  -0.00498115 -0.0205292  401 A1ITJ B N6   
4805 N  N9   . A1ITJ D .   ? 0.185586  0.234824 0.100912  -0.018705   -0.00480305 -0.0201792  401 A1ITJ B N9   
4806 C  C11  . A1ITJ D .   ? 0.185013  0.248559 0.113722  -0.0260804  -0.00959082 -0.018208   401 A1ITJ B C11  
4807 C  C12  . A1ITJ D .   ? 0.179554  0.224386 0.0947693 -0.0075213  0.00475171  -0.0106081  401 A1ITJ B C12  
4808 C  C14  . A1ITJ D .   ? 0.175532  0.222199 0.0900434 -0.0202295  0.013751    -0.00688103 401 A1ITJ B C14  
4809 N  N15  . A1ITJ D .   ? 0.179518  0.227408 0.0858067 -0.0195886  0.0209845   -0.00878191 401 A1ITJ B N15  
4810 C  C16  . A1ITJ D .   ? 0.183137  0.23844  0.0799391 -0.0233911  0.0171085   -0.0146114  401 A1ITJ B C16  
4811 CL CL18 . A1ITJ D .   ? 0.260564  0.317279 0.123287  -0.0573155  0.0619303   -0.0221731  401 A1ITJ B CL18 
4812 C  C19  . A1ITJ D .   ? 0.181972  0.226371 0.11086   -0.0306411  0.0235626   -0.0126854  401 A1ITJ B C19  
4813 O  O20  . A1ITJ D .   ? 0.189249  0.221196 0.0971798 -0.00034781 -0.00125764 -0.00215523 401 A1ITJ B O20  
4814 N  N23  . A1ITJ D .   ? 0.201612  0.287614 0.150377  -0.0474249  -0.0243704  -0.0333618  401 A1ITJ B N23  
4815 C  C25  . A1ITJ D .   ? 0.234073  0.288739 0.151618  -0.0500694  -0.017454   -0.0430711  401 A1ITJ B C25  
4816 O  O26  . A1ITJ D .   ? 0.197493  0.318168 0.180982  -0.0591469  -0.0178137  -0.0321636  401 A1ITJ B O26  
4817 C  C27  . A1ITJ D .   ? 0.22656   0.304009 0.169356  -0.0261317  -0.00487963 -0.00576194 401 A1ITJ B C27  
4818 C  C29  . A1ITJ D .   ? 0.235244  0.319446 0.20714   -0.00636615 -0.00650982 0.00162472  401 A1ITJ B C29  
4819 BR BR30 . A1ITJ D .   ? 0.279541  0.360762 0.213952  0.0335927   0.0381076   0.00952516  401 A1ITJ B BR30 
4820 C  C31  . A1ITJ D .   ? 0.245157  0.295407 0.179102  -0.0160565  -0.0320443  -0.0114947  401 A1ITJ B C31  
4821 S  S    . DMS   E .   ? 0.224786  0.321983 0.144636  -0.00202445 -0.0282398  -0.0204054  402 DMS   B S    
4822 O  O    . DMS   E .   ? 0.221201  0.322158 0.169999  0.0151227   -0.00987457 -0.023632   402 DMS   B O    
4823 C  C1   . DMS   E .   ? 0.242777  0.322076 0.144181  0.00585804  -0.0241978  -0.0185724  402 DMS   B C1   
4824 C  C2   . DMS   E .   ? 0.238739  0.342044 0.11393   0.00275619  -0.0223943  -0.016394   402 DMS   B C2   
4825 CL CL   . CL    F .   ? 0.152542  0.221197 0.0852093 0.00374384  -0.00556145 -0.0259226  403 CL    B CL   
4826 O  O    . HOH   G .   ? 0.408437  0.41011  0.493444  -0.00918609 0.0635065   -0.0616332  501 HOH   A O    
4827 O  O    . HOH   G .   ? 0.233224  0.523487 0.096908  0.0952152   0.0878084   0.0638335   502 HOH   A O    
4828 O  O    . HOH   G .   ? 0.243577  0.351559 0.976213  0.051863    -0.100862   -0.090281   503 HOH   A O    
4829 O  O    . HOH   G .   ? 0.356583  1.01018  0.382752  -0.061239   -0.0941024  0.0619814   504 HOH   A O    
4830 O  O    . HOH   G .   ? 0.2103    0.47161  0.373617  -0.0582828  0.123017    -0.22079    505 HOH   A O    
4831 O  O    . HOH   G .   ? 0.380542  0.377049 0.297261  0.0293494   -0.0228752  0.0490961   506 HOH   A O    
4832 O  O    . HOH   G .   ? 0.302308  0.319845 0.272493  -0.0241554  0.0848372   0.00994167  507 HOH   A O    
4833 O  O    . HOH   G .   ? 0.531025  0.684064 0.371894  -0.1815     0.22623     -0.104902   508 HOH   A O    
4834 O  O    . HOH   G .   ? 0.409226  0.36457  0.231652  -0.0852638  -0.138355   0.0844434   509 HOH   A O    
4835 O  O    . HOH   G .   ? 0.211694  0.359115 0.382145  -0.041356   -0.0135954  0.0242044   510 HOH   A O    
4836 O  O    . HOH   G .   ? 0.298767  0.70861  0.486455  0.0735302   -0.0506615  0.0830404   511 HOH   A O    
4837 O  O    . HOH   G .   ? 0.447943  0.400774 0.271738  -0.0155611  -0.0380599  0.0671225   512 HOH   A O    
4838 O  O    . HOH   G .   ? 0.422654  0.465863 0.377685  0.155438    0.00051618  -0.0101643  513 HOH   A O    
4839 O  O    . HOH   G .   ? 0.253788  0.33114  0.536792  0.100698    -0.121675   -0.0968308  514 HOH   A O    
4840 O  O    . HOH   G .   ? 0.330654  0.449379 0.388447  -0.0550476  -0.0187341  0.0803772   515 HOH   A O    
4841 O  O    . HOH   G .   ? 0.44659   0.543548 0.238726  -0.0521176  0.037552    0.025245    516 HOH   A O    
4842 O  O    . HOH   G .   ? 0.447079  0.417082 0.302052  0.0272257   0.0885017   0.0346055   517 HOH   A O    
4843 O  O    . HOH   G .   ? 0.345161  0.315476 0.269341  0.0534514   -0.0154093  -0.0278585  518 HOH   A O    
4844 O  O    . HOH   G .   ? 0.195861  0.359591 0.462976  0.0452145   -0.0357657  -0.00835795 519 HOH   A O    
4845 O  O    . HOH   G .   ? 0.520522  0.477572 0.371039  0.137967    0.279462    0.0717574   520 HOH   A O    
4846 O  O    . HOH   G .   ? 0.145397  0.398871 0.170814  0.032465    0.0341858   0.0205228   521 HOH   A O    
4847 O  O    . HOH   G .   ? 0.175776  0.252317 0.166995  -0.0142857  -0.00046816 -0.0167195  522 HOH   A O    
4848 O  O    . HOH   G .   ? 0.298461  0.349614 0.156856  -0.04568    0.0621721   -0.013029   523 HOH   A O    
4849 O  O    . HOH   G .   ? 0.247     0.721852 0.138133  0.129189    -0.0222767  -0.0309449  524 HOH   A O    
4850 O  O    . HOH   G .   ? 0.415346  0.560007 0.151356  -0.0254255  -0.0941169  0.0541593   525 HOH   A O    
4851 O  O    . HOH   G .   ? 0.371605  0.561898 0.35299   -0.115241   -0.108644   0.129281    526 HOH   A O    
4852 O  O    . HOH   G .   ? 0.460685  0.431322 0.273508  -0.0906542  0.0261099   -0.0429095  527 HOH   A O    
4853 O  O    . HOH   G .   ? 0.229998  0.629147 0.347636  -0.0539817  -0.0637679  0.0220588   528 HOH   A O    
4854 O  O    . HOH   G .   ? 0.373361  0.374502 0.493245  0.038639    -0.0269811  -0.0794912  529 HOH   A O    
4855 O  O    . HOH   G .   ? 0.220056  0.354709 0.202385  0.00799046  -0.0424046  -0.0026931  530 HOH   A O    
4856 O  O    . HOH   G .   ? 0.219583  0.293947 0.132469  0.00250304  -0.0218961  -0.0106955  531 HOH   A O    
4857 O  O    . HOH   G .   ? 0.392621  0.363752 0.212254  0.0125703   0.0960863   0.00551076  532 HOH   A O    
4858 O  O    . HOH   G .   ? 0.185542  0.308275 0.392477  0.0122417   0.0599315   -0.0581126  533 HOH   A O    
4859 O  O    . HOH   G .   ? 0.533106  0.407677 0.280986  0.188793    -0.206323   -0.11357    534 HOH   A O    
4860 O  O    . HOH   G .   ? 0.361475  0.679655 0.270073  -0.093211   0.101952    -0.177608   535 HOH   A O    
4861 O  O    . HOH   G .   ? 0.35487   0.418126 0.560253  0.152697    -0.0874381  0.0213013   536 HOH   A O    
4862 O  O    . HOH   G .   ? 0.542277  0.463087 0.6436    0.00197668  0.0504891   0.190015    537 HOH   A O    
4863 O  O    . HOH   G .   ? 0.299017  0.507326 0.416061  0.0563358   0.143549    0.0549651   538 HOH   A O    
4864 O  O    . HOH   G .   ? 0.351373  0.363152 0.4344    -0.0967696  0.154733    -0.0684819  539 HOH   A O    
4865 O  O    . HOH   G .   ? 0.168124  0.257399 0.114749  -0.0131815  -0.00050477 -0.0214292  540 HOH   A O    
4866 O  O    . HOH   G .   ? 0.142618  0.252918 0.0927675 0.0349533   -0.0168593  0.0107462   541 HOH   A O    
4867 O  O    . HOH   G .   ? 0.16183   0.231445 0.147159  0.0145544   0.0144068   0.0109374   542 HOH   A O    
4868 O  O    . HOH   G .   ? 0.3311    0.593784 0.376641  -0.163787   0.0273308   0.131622    543 HOH   A O    
4869 O  O    . HOH   G .   ? 0.18907   0.324757 0.289415  -0.0429629  0.0601816   -0.0573353  544 HOH   A O    
4870 O  O    . HOH   G .   ? 0.221863  0.266    0.105304  0.0230634   0.0483764   0.0103418   545 HOH   A O    
4871 O  O    . HOH   G .   ? 0.279593  0.324402 0.264728  0.00017507  -0.0461509  0.0209605   546 HOH   A O    
4872 O  O    . HOH   G .   ? 0.367618  0.407349 0.241891  0.00038968  0.146696    -0.0737934  547 HOH   A O    
4873 O  O    . HOH   G .   ? 0.292915  0.723521 0.273205  0.00063298  -0.0441635  -0.159949   548 HOH   A O    
4874 O  O    . HOH   G .   ? 0.189442  0.275822 0.141601  0.0304408   0.0401785   -0.00091841 549 HOH   A O    
4875 O  O    . HOH   G .   ? 0.289425  0.508736 0.228569  0.00402907  0.0208842   -0.131186   550 HOH   A O    
4876 O  O    . HOH   G .   ? 0.317027  0.488199 0.477832  0.141661    0.17531     0.185077    551 HOH   A O    
4877 O  O    . HOH   G .   ? 0.429479  0.338024 0.199943  0.0354911   -0.0450697  -0.090287   552 HOH   A O    
4878 O  O    . HOH   G .   ? 0.164564  0.222969 0.113051  0.00687384  -0.0052106  -0.00519616 553 HOH   A O    
4879 O  O    . HOH   G .   ? 0.438022  0.384935 0.337004  -0.0149484  0.0641521   0.00021362  554 HOH   A O    
4880 O  O    . HOH   G .   ? 0.229489  0.407006 0.158059  0.11274     -0.00932851 -0.0211081  555 HOH   A O    
4881 O  O    . HOH   G .   ? 0.260553  0.630792 0.546459  -0.0108573  -0.0278429  0.140247    556 HOH   A O    
4882 O  O    . HOH   G .   ? 0.388081  0.383227 0.101492  -0.109571   0.121728    -0.049654   557 HOH   A O    
4883 O  O    . HOH   G .   ? 0.197187  0.36912  0.122981  0.106603    0.014888    0.0107923   558 HOH   A O    
4884 O  O    . HOH   G .   ? 0.242457  0.440056 0.193162  -0.0610036  -0.011952   -0.0254878  559 HOH   A O    
4885 O  O    . HOH   G .   ? 0.244812  0.377855 0.467544  -0.0491386  0.0140602   -0.0535336  560 HOH   A O    
4886 O  O    . HOH   G .   ? 0.298841  0.326896 0.20208   0.0215034   0.0569923   -0.0775115  561 HOH   A O    
4887 O  O    . HOH   G .   ? 0.251714  0.392915 0.224074  0.0296122   0.028454    -0.0384629  562 HOH   A O    
4888 O  O    . HOH   G .   ? 0.347103  0.388876 0.437663  -0.0103822  -0.0520838  -0.17147    563 HOH   A O    
4889 O  O    . HOH   G .   ? 0.187296  0.323075 0.156914  0.00260177  0.0183183   -0.0281626  564 HOH   A O    
4890 O  O    . HOH   G .   ? 0.229621  0.365447 0.237653  -0.0135839  -0.00888483 -0.00022164 565 HOH   A O    
4891 O  O    . HOH   G .   ? 0.24797   0.533744 0.362083  0.0277219   -0.0249243  -0.130021   566 HOH   A O    
4892 O  O    . HOH   G .   ? 0.138005  0.34318  0.135652  -0.00951825 0.00607475  -0.0290405  567 HOH   A O    
4893 O  O    . HOH   G .   ? 0.264301  0.339036 0.132887  0.0407456   -0.0424791  -0.0295496  568 HOH   A O    
4894 O  O    . HOH   G .   ? 0.364343  0.72065  0.167395  0.199933    0.016708    0.0592375   569 HOH   A O    
4895 O  O    . HOH   G .   ? 0.255749  0.317532 0.129707  0.0389769   0.0214307   0.0123768   570 HOH   A O    
4896 O  O    . HOH   G .   ? 0.168955  0.435664 0.422991  0.0483254   0.0574605   -0.0773317  571 HOH   A O    
4897 O  O    . HOH   G .   ? 0.211417  0.353837 0.241752  0.0319978   0.020655    0.0404532   572 HOH   A O    
4898 O  O    . HOH   G .   ? 0.127094  0.237181 0.256464  0.0107199   -0.0463858  0.0124683   573 HOH   A O    
4899 O  O    . HOH   G .   ? 0.469058  0.486474 0.502602  0.129477    -0.122361   -0.0912107  574 HOH   A O    
4900 O  O    . HOH   G .   ? 0.197333  0.504928 0.15485   -0.024819   -0.00894134 -0.112584   575 HOH   A O    
4901 O  O    . HOH   G .   ? 0.241601  0.406351 0.303539  0.0162265   0.0220829   0.0170243   576 HOH   A O    
4902 O  O    . HOH   G .   ? 0.218467  0.360744 0.115801  0.0108438   0.0439709   0.00272984  577 HOH   A O    
4903 O  O    . HOH   G .   ? 0.182831  0.30263  0.10104   0.0181229   -0.0296912  0.0312018   578 HOH   A O    
4904 O  O    . HOH   G .   ? 0.151838  0.333986 0.190114  0.0628602   0.052021    0.0607044   579 HOH   A O    
4905 O  O    . HOH   G .   ? 0.139702  0.247145 0.109139  0.0081217   -0.0066271  0.0271496   580 HOH   A O    
4906 O  O    . HOH   G .   ? 0.340834  0.404983 0.493884  -0.0264796  0.0579792   0.0950624   581 HOH   A O    
4907 O  O    . HOH   G .   ? 0.288548  0.36344  0.280363  0.0695229   0.0126485   -0.0327353  582 HOH   A O    
4908 O  O    . HOH   G .   ? 0.254796  0.367904 0.288549  -0.066804   0.0302594   -0.00999121 583 HOH   A O    
4909 O  O    . HOH   G .   ? 0.358788  0.405143 0.266239  -0.0070243  0.0842702   0.133489    584 HOH   A O    
4910 O  O    . HOH   G .   ? 0.272753  0.355251 0.144859  0.067681    0.0369939   -0.0188752  585 HOH   A O    
4911 O  O    . HOH   G .   ? 0.275778  0.523394 0.794933  -0.049213   -0.082978   -0.204987   586 HOH   A O    
4912 O  O    . HOH   G .   ? 0.163252  0.702131 0.300411  0.0413098   0.0095438   0.183838    587 HOH   A O    
4913 O  O    . HOH   G .   ? 0.308134  0.489009 0.405966  0.0743902   -0.00789706 0.12322     588 HOH   A O    
4914 O  O    . HOH   G .   ? 0.328997  0.218401 0.146004  0.0267744   -0.0262441  0.00654363  589 HOH   A O    
4915 O  O    . HOH   G .   ? 0.226673  0.375797 0.114003  0.0514586   0.0682734   0.000785    590 HOH   A O    
4916 O  O    . HOH   G .   ? 0.334682  0.328842 0.215233  -0.0480329  -0.121564   -0.00750149 591 HOH   A O    
4917 O  O    . HOH   G .   ? 0.182919  0.402987 0.252874  0.0444306   0.0317884   -0.0375945  592 HOH   A O    
4918 O  O    . HOH   G .   ? 0.251763  0.278936 0.150639  0.0120724   0.0210645   -0.0093101  593 HOH   A O    
4919 O  O    . HOH   G .   ? 0.229949  0.44353  0.309099  -0.0226323  0.000555    0.0148356   594 HOH   A O    
4920 O  O    . HOH   G .   ? 0.2693    0.345733 0.175605  -0.0266419  -0.0328435  0.0295793   595 HOH   A O    
4921 O  O    . HOH   G .   ? 0.327851  0.48904  0.461955  -0.0943164  0.0676582   0.00266609  596 HOH   A O    
4922 O  O    . HOH   G .   ? 0.215059  0.322755 0.249442  -0.0196199  0.0872818   0.0150805   597 HOH   A O    
4923 O  O    . HOH   G .   ? 0.120597  0.321228 0.22764   -0.00276234 -0.0140517  0.0137659   598 HOH   A O    
4924 O  O    . HOH   G .   ? 0.302416  0.89461  0.141602  -0.020528   0.0663246   0.0128736   599 HOH   A O    
4925 O  O    . HOH   G .   ? 0.668209  0.443404 0.359334  0.077781    0.0860928   0.0542102   600 HOH   A O    
4926 O  O    . HOH   G .   ? 0.269276  0.440282 0.59674   -0.079495   -0.205897   0.103686    601 HOH   A O    
4927 O  O    . HOH   G .   ? 0.362104  0.331226 0.226357  -0.046352   -0.0541777  0.0475738   602 HOH   A O    
4928 O  O    . HOH   G .   ? 0.282991  0.457504 0.581445  0.0772628   0.113451    0.239463    603 HOH   A O    
4929 O  O    . HOH   G .   ? 0.219242  0.318222 0.166456  -0.0498701  0.0186519   0.0133816   604 HOH   A O    
4930 O  O    . HOH   G .   ? 0.236688  0.360939 0.129931  -0.00551419 0.0258976   -0.044546   605 HOH   A O    
4931 O  O    . HOH   G .   ? 0.280295  0.410011 0.172278  0.00593976  0.0297801   0.0610665   606 HOH   A O    
4932 O  O    . HOH   G .   ? 0.289592  0.292972 0.182254  0.0627175   0.0182088   0.0361458   607 HOH   A O    
4933 O  O    . HOH   G .   ? 0.478332  0.48035  0.392915  0.210862    0.277209    0.132806    608 HOH   A O    
4934 O  O    . HOH   G .   ? 0.332108  0.556301 0.153382  -0.145303   -0.0058462  -0.0911704  609 HOH   A O    
4935 O  O    . HOH   G .   ? 0.152364  0.315507 0.0921246 0.00173699  0.0229442   -0.0103504  610 HOH   A O    
4936 O  O    . HOH   G .   ? 0.505381  0.54906  0.335782  0.0624189   0.0479592   -0.0560566  611 HOH   A O    
4937 O  O    . HOH   G .   ? 0.671004  0.425834 0.246275  0.00451772  0.0597576   0.00032753  612 HOH   A O    
4938 O  O    . HOH   G .   ? 0.203449  0.503405 0.180991  -0.0290589  -0.0298776  0.0061335   613 HOH   A O    
4939 O  O    . HOH   G .   ? 0.185473  0.330041 0.162169  0.063397    -0.00739242 0.00966239  614 HOH   A O    
4940 O  O    . HOH   G .   ? 0.168651  0.391903 0.299682  0.00313717  0.00875779  0.0312004   615 HOH   A O    
4941 O  O    . HOH   G .   ? 0.347901  0.46152  0.207734  0.0628645   0.116815    0.0864823   616 HOH   A O    
4942 O  O    . HOH   G .   ? 0.598359  0.413031 0.377383  0.0670951   -0.227515   0.075853    617 HOH   A O    
4943 O  O    . HOH   G .   ? 0.604295  0.885201 0.360782  0.170821    0.0119844   0.299393    618 HOH   A O    
4944 O  O    . HOH   G .   ? 0.241831  0.360924 0.261724  0.00317324  -0.00711251 -0.0339564  619 HOH   A O    
4945 O  O    . HOH   G .   ? 0.192225  0.267695 0.113752  0.0100448   0.00845446  0.00289398  620 HOH   A O    
4946 O  O    . HOH   G .   ? 0.228489  0.316989 0.0734275 0.0354272   -0.00646425 0.0344309   621 HOH   A O    
4947 O  O    . HOH   G .   ? 0.174201  0.301108 0.145707  0.00291895  0.0305055   0.0271245   622 HOH   A O    
4948 O  O    . HOH   G .   ? 0.183749  0.388571 0.232672  0.00023707  -0.0894426  0.0264374   623 HOH   A O    
4949 O  O    . HOH   G .   ? 0.48075   0.523036 0.437192  -0.0580299  0.0646052   -0.111228   624 HOH   A O    
4950 O  O    . HOH   G .   ? 0.136679  0.32705  0.0981133 -0.00326221 0.0252433   0.0153137   625 HOH   A O    
4951 O  O    . HOH   G .   ? 0.285949  0.319194 0.272157  -0.0398535  -0.103207   -0.0427818  626 HOH   A O    
4952 O  O    . HOH   G .   ? 0.200977  0.288262 0.12013   0.0086361   0.058905    -0.00745926 627 HOH   A O    
4953 O  O    . HOH   G .   ? 0.227568  0.387355 0.186881  -0.0403393  -0.0179046  -0.0821052  628 HOH   A O    
4954 O  O    . HOH   G .   ? 0.320087  0.442171 0.364977  -0.0449619  0.0233685   0.0174071   629 HOH   A O    
4955 O  O    . HOH   G .   ? 0.107009  0.216066 0.0604146 0.00849001  0.00793921  0.00420375  630 HOH   A O    
4956 O  O    . HOH   G .   ? 0.266611  0.229354 0.187031  -0.0107427  -0.0503676  0.0131593   631 HOH   A O    
4957 O  O    . HOH   G .   ? 0.26293   0.400569 0.250657  -0.0169955  -0.0498088  -0.00105938 632 HOH   A O    
4958 O  O    . HOH   G .   ? 0.284775  0.401316 0.217679  0.0468369   0.0561843   -0.0153821  633 HOH   A O    
4959 O  O    . HOH   G .   ? 0.298998  0.318777 0.344954  -0.00756142 -0.000129   0.0206058   634 HOH   A O    
4960 O  O    . HOH   G .   ? 0.183001  0.266386 0.107707  0.00226574  -0.0268902  -0.0174885  635 HOH   A O    
4961 O  O    . HOH   G .   ? 0.362438  0.515001 0.267533  -0.037765   -0.042938   0.0117054   636 HOH   A O    
4962 O  O    . HOH   G .   ? 1.14243   0.334798 0.326605  0.0778245   0.0027913   0.0299713   637 HOH   A O    
4963 O  O    . HOH   G .   ? 0.339228  0.355672 0.453469  -0.0333616  -0.0111268  -0.124099   638 HOH   A O    
4964 O  O    . HOH   G .   ? 0.205297  0.320007 0.238542  -0.0216164  0.0448428   -0.0795625  639 HOH   A O    
4965 O  O    . HOH   G .   ? 0.394921  0.630597 0.291239  -0.023917   0.0824457   -0.0701179  640 HOH   A O    
4966 O  O    . HOH   G .   ? 0.32689   0.49581  0.207694  0.0267159   0.00179889  -0.0588876  641 HOH   A O    
4967 O  O    . HOH   G .   ? 0.5578    0.579185 0.250856  0.257877    -0.139514   -0.0425793  642 HOH   A O    
4968 O  O    . HOH   G .   ? 0.44012   0.546252 0.371575  -0.0743624  -0.0252062  -0.168431   643 HOH   A O    
4969 O  O    . HOH   G .   ? 0.187375  0.349178 0.186611  0.0494076   0.016602    -0.0359108  644 HOH   A O    
4970 O  O    . HOH   G .   ? 0.177047  0.276536 0.105415  -0.00485234 0.0147011   0.00295446  645 HOH   A O    
4971 O  O    . HOH   G .   ? 0.170884  0.386349 0.17967   0.00520884  -0.0210729  0.0265991   646 HOH   A O    
4972 O  O    . HOH   G .   ? 0.169238  0.315941 0.154438  -0.0285842  0.00311545  -0.0193238  647 HOH   A O    
4973 O  O    . HOH   G .   ? 0.189079  0.567469 0.119073  0.00767371  -0.0157441  -0.0377243  648 HOH   A O    
4974 O  O    . HOH   G .   ? 0.371959  0.443813 0.278695  -0.0970989  -0.0151169  -0.0302548  649 HOH   A O    
4975 O  O    . HOH   G .   ? 0.49866   0.457182 0.453736  -0.00300512 -0.0220266  0.197031    650 HOH   A O    
4976 O  O    . HOH   G .   ? 0.347907  0.564882 0.283114  -0.0467636  0.024991    0.0256826   651 HOH   A O    
4977 O  O    . HOH   G .   ? 0.421396  0.578274 0.182343  -0.0351254  -0.0700012  0.0754856   652 HOH   A O    
4978 O  O    . HOH   G .   ? 0.110291  0.276694 0.0896415 0.00517033  0.00091136  -0.0106037  653 HOH   A O    
4979 O  O    . HOH   G .   ? 0.379518  0.549499 0.183965  0.132334    0.0458654   0.0413437   654 HOH   A O    
4980 O  O    . HOH   G .   ? 0.399768  0.305808 0.146315  0.0142165   0.0711497   0.0336753   655 HOH   A O    
4981 O  O    . HOH   G .   ? 0.373535  0.58689  0.243628  0.0436466   -0.00994934 -0.0093482  656 HOH   A O    
4982 O  O    . HOH   G .   ? 0.414599  0.446989 0.232528  0.0528079   0.0618658   0.0243774   657 HOH   A O    
4983 O  O    . HOH   G .   ? 0.222656  0.301447 0.189907  -0.00178318 0.0488652   -0.0404927  658 HOH   A O    
4984 O  O    . HOH   G .   ? 0.373559  0.503695 0.592133  -0.0792715  0.0300594   0.0194077   659 HOH   A O    
4985 O  O    . HOH   G .   ? 0.211093  0.343543 0.266886  0.0249829   -0.0833545  -0.0434837  660 HOH   A O    
4986 O  O    . HOH   G .   ? 0.146449  0.284368 0.161898  -0.00812322 0.00577129  -0.0688992  661 HOH   A O    
4987 O  O    . HOH   G .   ? 0.452248  0.669467 0.275468  -0.0308973  0.036218    -0.0127442  662 HOH   A O    
4988 O  O    . HOH   G .   ? 0.333586  0.32916  0.279971  -0.0206835  -0.0876746  -0.016293   663 HOH   A O    
4989 O  O    . HOH   G .   ? 0.258696  0.46808  0.354476  -0.082862   -0.0393904  -0.0254159  664 HOH   A O    
4990 O  O    . HOH   G .   ? 0.249487  0.293413 0.259491  0.0407763   -0.0356758  -0.0381162  665 HOH   A O    
4991 O  O    . HOH   G .   ? 0.222727  0.265183 0.166312  0.00171308  0.00339849  0.0273366   666 HOH   A O    
4992 O  O    . HOH   G .   ? 0.255613  0.485089 0.463986  -0.0345991  -0.0164573  0.0440469   667 HOH   A O    
4993 O  O    . HOH   G .   ? 0.548634  0.373437 0.262792  0.100877    0.00525147  0.0565656   668 HOH   A O    
4994 O  O    . HOH   G .   ? 0.189621  0.395206 0.13237   0.0402894   -0.0174528  -0.0238201  669 HOH   A O    
4995 O  O    . HOH   G .   ? 0.229701  0.433896 0.247414  -0.0517242  0.0163311   -0.016646   670 HOH   A O    
4996 O  O    . HOH   G .   ? 0.472835  0.353307 0.270567  -0.0449809  0.119011    -0.00134006 671 HOH   A O    
4997 O  O    . HOH   G .   ? 0.201727  0.377476 0.197015  0.012203    -0.0987072  0.0405024   672 HOH   A O    
4998 O  O    . HOH   G .   ? 0.242753  0.365367 0.159985  0.00386848  0.0634286   -0.00351294 673 HOH   A O    
4999 O  O    . HOH   G .   ? 0.62579   0.535509 0.582302  -0.0429997  0.397401    -0.157398   674 HOH   A O    
5000 O  O    . HOH   G .   ? 0.308722  0.335529 0.171595  -0.040901   -0.0127309  0.0846284   675 HOH   A O    
5001 O  O    . HOH   G .   ? 0.40616   0.411267 0.441189  -0.0128094  -0.228798   0.0897632   676 HOH   A O    
5002 O  O    . HOH   G .   ? 0.292501  0.280568 0.320714  0.0428762   0.0329579   -0.0350433  677 HOH   A O    
5003 O  O    . HOH   G .   ? 0.25991   0.427222 0.377932  -0.0127162  0.0230312   -0.138223   678 HOH   A O    
5004 O  O    . HOH   G .   ? 0.313361  0.480425 0.244164  0.0164608   0.0183141   0.0294033   679 HOH   A O    
5005 O  O    . HOH   G .   ? 0.313756  0.595406 0.170383  0.201255    0.0733703   0.13734     680 HOH   A O    
5006 O  O    . HOH   G .   ? 0.290039  0.502183 0.346739  0.052135    0.0536805   0.0542511   681 HOH   A O    
5007 O  O    . HOH   G .   ? 0.989392  0.618355 0.45142   0.0051906   -0.0712141  -0.121614   682 HOH   A O    
5008 O  O    . HOH   G .   ? 0.535886  0.775777 0.248988  0.162202    0.0187493   -0.146718   683 HOH   A O    
5009 O  O    . HOH   G .   ? 0.278106  0.362815 0.390752  -0.0691705  0.0535146   0.0178585   684 HOH   A O    
5010 O  O    . HOH   G .   ? 0.169562  0.385512 0.150632  0.00874492  -0.00912099 -0.00811484 685 HOH   A O    
5011 O  O    . HOH   G .   ? 0.441603  0.386627 0.226983  -0.118761   -0.0250807  -0.0395075  686 HOH   A O    
5012 O  O    . HOH   G .   ? 0.338018  0.32856  0.162361  -0.0487186  0.0475202   -0.0377848  687 HOH   A O    
5013 O  O    . HOH   G .   ? 0.175856  0.321159 0.0881286 -0.029735   -0.00670274 0.0284184   688 HOH   A O    
5014 O  O    . HOH   G .   ? 0.170594  0.91512  0.173558  0.0750534   0.0162327   0.0936141   689 HOH   A O    
5015 O  O    . HOH   G .   ? 0.354079  0.542225 0.338458  -0.0559422  0.0209939   0.156411    690 HOH   A O    
5016 O  O    . HOH   G .   ? 0.427652  0.605653 0.244084  0.193072    -0.133208   0.0657488   691 HOH   A O    
5017 O  O    . HOH   G .   ? 0.820854  0.596883 0.123479  0.387952    -0.0619276  -0.0349512  692 HOH   A O    
5018 O  O    . HOH   G .   ? 0.281531  0.269516 0.148111  0.00960477  0.0410557   0.0148048   693 HOH   A O    
5019 O  O    . HOH   G .   ? 0.433644  0.543331 0.559884  0.189432    0.142976    -0.0628634  694 HOH   A O    
5020 O  O    . HOH   G .   ? 0.306751  0.390181 0.181859  0.0285374   0.0117165   0.0496581   695 HOH   A O    
5021 O  O    . HOH   G .   ? 0.230634  0.480969 0.426843  -0.00207152 -0.00698187 -0.161363   696 HOH   A O    
5022 O  O    . HOH   G .   ? 0.443457  0.523272 0.261345  0.154804    0.05401     -0.0884555  697 HOH   A O    
5023 O  O    . HOH   G .   ? 0.34827   0.308164 0.109944  -0.0403978  0.00774976  -0.0166912  698 HOH   A O    
5024 O  O    . HOH   G .   ? 0.377034  0.484571 0.201002  0.107514    0.0466948   0.0541677   699 HOH   A O    
5025 O  O    . HOH   G .   ? 0.371826  0.836112 0.282083  0.0219641   0.106301    -0.0374862  700 HOH   A O    
5026 O  O    . HOH   G .   ? 0.293156  0.39138  0.0850463 0.0583059   0.00877371  0.0357999   701 HOH   A O    
5027 O  O    . HOH   G .   ? 0.30242   0.380084 0.207589  -0.00109115 0.124291    0.0146487   702 HOH   A O    
5028 O  O    . HOH   G .   ? 0.541434  0.424777 0.124856  -0.137596   -0.113508   0.0857495   703 HOH   A O    
5029 O  O    . HOH   G .   ? 0.261251  0.289569 0.234619  0.0396988   -0.0366537  0.074806    704 HOH   A O    
5030 O  O    . HOH   G .   ? 0.189207  0.421344 0.239195  0.0896985   -0.00176676 0.00755399  705 HOH   A O    
5031 O  O    . HOH   G .   ? 0.199272  0.350553 0.181155  -0.0610049  -0.0834722  0.11305     706 HOH   A O    
5032 O  O    . HOH   G .   ? 0.468837  0.464639 0.286465  0.0405984   -0.0671939  0.0734588   707 HOH   A O    
5033 O  O    . HOH   G .   ? 0.323659  0.266328 0.209448  0.0528155   0.00373853  0.0600103   708 HOH   A O    
5034 O  O    . HOH   G .   ? 0.202991  0.406561 0.279173  -0.0370758  -0.0834771  -0.0278678  709 HOH   A O    
5035 O  O    . HOH   G .   ? 0.211442  0.298995 0.176789  0.027588    0.00914253  0.0375235   710 HOH   A O    
5036 O  O    . HOH   G .   ? 0.230557  0.379692 0.335103  0.0158678   -0.0119004  -0.0342016  711 HOH   A O    
5037 O  O    . HOH   G .   ? 0.438347  0.597131 0.373331  -0.0779115  -0.154146   -0.111194   712 HOH   A O    
5038 O  O    . HOH   G .   ? 0.398411  0.558973 0.36726   0.058196    -0.12602    -0.0253962  713 HOH   A O    
5039 O  O    . HOH   G .   ? 0.392538  1.05601  0.538351  0.258616    -0.185187   -0.424322   714 HOH   A O    
5040 O  O    . HOH   G .   ? 0.185516  0.277666 0.123384  0.0450001   -0.027668   -0.0104343  715 HOH   A O    
5041 O  O    . HOH   G .   ? 0.267005  0.362908 0.176475  0.0727491   0.0120693   0.0162144   716 HOH   A O    
5042 O  O    . HOH   G .   ? 0.15246   0.282745 0.101268  0.0128526   0.0185615   -0.0237094  717 HOH   A O    
5043 O  O    . HOH   G .   ? 0.184806  0.350972 0.214819  0.0331094   0.0158096   -0.0660275  718 HOH   A O    
5044 O  O    . HOH   G .   ? 0.229561  0.256154 0.263388  -0.00589783 -0.0304185  -0.0409923  719 HOH   A O    
5045 O  O    . HOH   G .   ? 0.714994  0.345949 0.542015  0.107442    0.213513    0.131619    720 HOH   A O    
5046 O  O    . HOH   G .   ? 0.257001  0.247561 0.122463  -0.00769747 -0.00152686 0.031645    721 HOH   A O    
5047 O  O    . HOH   G .   ? 0.214905  0.315886 0.219241  0.0275878   -0.00724177 -0.0691797  722 HOH   A O    
5048 O  O    . HOH   G .   ? 0.38267   0.613995 0.520507  -0.127677   0.213481    -0.0586246  723 HOH   A O    
5049 O  O    . HOH   G .   ? 0.256373  0.499446 0.240169  0.0989117   -0.0776982  0.0381747   724 HOH   A O    
5050 O  O    . HOH   G .   ? 0.2665    0.354223 0.114394  -0.0139208  -0.00554068 0.012373    725 HOH   A O    
5051 O  O    . HOH   G .   ? 0.218875  0.413993 0.331091  -0.0499632  -0.0117372  -0.0905267  726 HOH   A O    
5052 O  O    . HOH   G .   ? 0.283756  0.255494 0.107202  0.00499061  0.0193835   0.0252458   727 HOH   A O    
5053 O  O    . HOH   G .   ? 0.216683  0.411907 0.353411  0.0360426   -0.0095038  -0.0395546  728 HOH   A O    
5054 O  O    . HOH   G .   ? 0.498322  0.354165 0.779372  -0.107477   0.158219    -0.102641   729 HOH   A O    
5055 O  O    . HOH   G .   ? 0.365541  0.345685 0.64912   0.0430647   0.251076    0.150711    730 HOH   A O    
5056 O  O    . HOH   G .   ? 0.309507  0.755676 0.115938  -0.0900252  -0.085171   0.0703165   731 HOH   A O    
5057 O  O    . HOH   G .   ? 0.21111   0.533187 0.122409  -0.0179843  -0.0253569  0.0251546   732 HOH   A O    
5058 O  O    . HOH   G .   ? 0.324243  0.78718  0.118269  0.208151    0.100189    0.104235    733 HOH   A O    
5059 O  O    . HOH   G .   ? 0.226969  0.470832 0.211034  -0.00680135 0.015021    -0.117256   734 HOH   A O    
5060 O  O    . HOH   G .   ? 0.238783  0.505411 0.190786  0.00095325  0.0210922   0.0890004   735 HOH   A O    
5061 O  O    . HOH   G .   ? 0.353946  0.275877 0.48438   0.051518    -0.0476989  -0.0765845  736 HOH   A O    
5062 O  O    . HOH   G .   ? 0.307544  0.344665 0.111038  0.0008102   0.0264882   -0.0119367  737 HOH   A O    
5063 O  O    . HOH   G .   ? 0.30346   0.259452 0.364895  0.08739     0.0175166   -0.0100338  738 HOH   A O    
5064 O  O    . HOH   G .   ? 0.286287  0.497754 0.349394  0.03989     -0.12004    -0.134298   739 HOH   A O    
5065 O  O    . HOH   G .   ? 0.273219  0.316409 0.216765  0.0493682   -0.0240473  0.0223129   740 HOH   A O    
5066 O  O    . HOH   G .   ? 0.706689  0.656562 0.39647   0.236764    -0.226244   -0.170713   741 HOH   A O    
5067 O  O    . HOH   G .   ? 0.920163  0.455182 0.370081  -0.170914   -0.174995   0.0135206   742 HOH   A O    
5068 O  O    . HOH   G .   ? 0.215732  0.452849 0.391681  0.0295832   -0.00434949 0.0649711   743 HOH   A O    
5069 O  O    . HOH   G .   ? 0.310322  0.376945 0.26614   -0.0143768  -0.0247349  0.0433306   744 HOH   A O    
5070 O  O    . HOH   G .   ? 0.262057  0.393142 0.243413  -0.0369035  0.112119    -0.101011   745 HOH   A O    
5071 O  O    . HOH   G .   ? 0.332629  0.344976 0.228672  0.0966452   -0.0591056  0.00921966  746 HOH   A O    
5072 O  O    . HOH   G .   ? 0.220763  0.497705 0.223351  -0.0216084  0.0286032   -0.074891   747 HOH   A O    
5073 O  O    . HOH   G .   ? 0.671144  0.769754 0.28377   -0.0659263  -0.144303   0.00994188  748 HOH   A O    
5074 O  O    . HOH   G .   ? 0.825537  0.417094 0.375432  -0.0957003  0.0890381   0.144938    749 HOH   A O    
5075 O  O    . HOH   G .   ? 0.625132  0.54438  0.350111  -0.117795   -0.123834   0.103704    750 HOH   A O    
5076 O  O    . HOH   G .   ? 0.536656  0.61945  0.207327  -0.100118   -0.0351689  0.0862276   751 HOH   A O    
5077 O  O    . HOH   G .   ? 0.384033  0.495663 0.188762  0.0208524   0.0233369   0.0148103   752 HOH   A O    
5078 O  O    . HOH   G .   ? 0.46157   0.636249 0.601519  -0.175228   0.00586529  0.151283    753 HOH   A O    
5079 O  O    . HOH   G .   ? 0.334905  0.415919 0.22068   -0.0329351  -0.0272486  0.0251227   754 HOH   A O    
5080 O  O    . HOH   G .   ? 0.504944  0.715929 0.383919  0.221391    -0.158171   -0.00657906 755 HOH   A O    
5081 O  O    . HOH   G .   ? 0.442113  0.627898 0.453009  -0.145367   -0.0665739  0.17161     756 HOH   A O    
5082 O  O    . HOH   G .   ? 0.433139  0.691287 0.375451  -0.0997609  0.00437057  -0.184794   757 HOH   A O    
5083 O  O    . HOH   G .   ? 0.305872  0.544844 0.30294   0.0474927   -0.0494128  -0.0621005  758 HOH   A O    
5084 O  O    . HOH   G .   ? 0.156566  0.142719 0.126357  -0.0340338  0.023433    0.0225044   759 HOH   A O    
5085 O  O    . HOH   G .   ? 0.539228  0.386571 0.397056  -0.0977098  0.145201    -0.0277829  760 HOH   A O    
5086 O  O    . HOH   G .   ? 0.571384  0.441102 0.557809  -0.0967231  -0.327124   0.178329    761 HOH   A O    
5087 O  O    . HOH   G .   ? 0.409667  0.465909 0.519137  -0.218396   -0.0963397  0.119359    762 HOH   A O    
5088 O  O    . HOH   G .   ? 0.166313  0.224961 0.130353  0.0170892   -0.0715838  -0.0229183  763 HOH   A O    
5089 O  O    . HOH   G .   ? 0.332951  0.591798 0.144453  0.153146    -0.0498676  -0.0156653  764 HOH   A O    
5090 O  O    . HOH   G .   ? 0.275979  0.516081 0.264297  -0.0636023  -0.0322388  0.104553    765 HOH   A O    
5091 O  O    . HOH   G .   ? 0.276758  0.375591 0.211497  -0.0146125  -0.038943   0.0223226   766 HOH   A O    
5092 O  O    . HOH   G .   ? 0.416194  0.552152 0.66171   0.0361707   0.0482654   0.158897    767 HOH   A O    
5093 O  O    . HOH   G .   ? 0.356608  0.651222 0.232988  0.0798163   0.140282    -0.0448523  768 HOH   A O    
5094 O  O    . HOH   G .   ? 0.41661   0.737988 0.722957  0.247794    -0.175982   -0.0369506  769 HOH   A O    
5095 O  O    . HOH   G .   ? 0.249869  0.42606  0.43638   0.0428323   -0.0276865  -0.0341436  770 HOH   A O    
5096 O  O    . HOH   G .   ? 0.431395  0.401414 0.539277  -0.0179571  0.0705701   -0.164165   771 HOH   A O    
5097 O  O    . HOH   G .   ? 0.402883  0.487483 0.281227  0.0879857   0.118296    0.00664596  772 HOH   A O    
5098 O  O    . HOH   G .   ? 0.228033  0.743198 0.220736  0.149223    0.038932    0.168814    773 HOH   A O    
5099 O  O    . HOH   G .   ? 0.221417  0.608039 0.207705  -0.0187699  -0.0352006  0.0227212   774 HOH   A O    
5100 O  O    . HOH   G .   ? 0.298     0.432998 0.266339  0.0685862   0.0957462   0.015143    775 HOH   A O    
5101 O  O    . HOH   G .   ? 0.210445  0.453512 0.213436  0.0104465   0.030358    0.0585315   776 HOH   A O    
5102 O  O    . HOH   G .   ? 0.31664   0.648177 0.565396  -0.022503   0.0436653   0.18658     777 HOH   A O    
5103 O  O    . HOH   G .   ? 0.35305   0.868076 0.349757  0.00918502  0.0438836   -0.118912   778 HOH   A O    
5104 O  O    . HOH   G .   ? 0.27869   0.375748 0.231667  0.0874412   0.0252316   0.00235912  779 HOH   A O    
5105 O  O    . HOH   G .   ? 0.611486  0.574414 0.22835   -0.0566917  -0.13961    0.0128071   780 HOH   A O    
5106 O  O    . HOH   G .   ? 0.353734  0.425054 0.308725  0.0385678   0.0219575   0.0180236   781 HOH   A O    
5107 O  O    . HOH   G .   ? 0.532143  0.48364  0.326486  0.0771377   0.121586    0.113749    782 HOH   A O    
5108 O  O    . HOH   G .   ? 0.635578  0.746808 0.470833  -0.113695   -0.222577   -0.163322   783 HOH   A O    
5109 O  O    . HOH   G .   ? 0.703606  0.354404 0.260575  0.130178    -0.0885976  -0.110458   784 HOH   A O    
5110 O  O    . HOH   G .   ? 0.327181  0.469953 0.388984  0.0556544   0.0637687   -0.00087195 785 HOH   A O    
5111 O  O    . HOH   G .   ? 0.268743  0.450763 0.327735  -0.0287322  0.0238106   0.034828    786 HOH   A O    
5112 O  O    . HOH   G .   ? 0.313152  0.594134 0.342717  -0.0489847  -0.0632816  0.00319786  787 HOH   A O    
5113 O  O    . HOH   G .   ? 0.474414  0.688378 0.24594   0.0756816   0.0889199   -0.0780893  788 HOH   A O    
5114 O  O    . HOH   G .   ? 0.240903  0.358721 0.432733  -0.00923858 -0.155119   -0.0208618  789 HOH   A O    
5115 O  O    . HOH   G .   ? 0.228941  0.431157 0.19155   -0.0230439  -0.00673924 -0.0600238  790 HOH   A O    
5116 O  O    . HOH   G .   ? 0.409696  0.440847 0.473303  0.162883    0.0239321   0.153601    791 HOH   A O    
5117 O  O    . HOH   G .   ? 0.413451  0.463479 0.281155  0.0696401   0.0582735   -0.0280696  792 HOH   A O    
5118 O  O    . HOH   G .   ? 0.596525  0.671043 0.268645  0.125175    -0.102247   0.0968372   793 HOH   A O    
5119 O  O    . HOH   G .   ? 0.301395  0.349458 0.267224  0.029026    -0.0201687  0.0622077   794 HOH   A O    
5120 O  O    . HOH   G .   ? 0.337742  0.480267 0.3472    0.0119133   -0.128283   0.118175    795 HOH   A O    
5121 O  O    . HOH   G .   ? 0.520927  0.646987 0.263729  0.252143    -0.0923849  -0.142077   796 HOH   A O    
5122 O  O    . HOH   G .   ? 0.248658  0.373949 0.185795  0.0305785   0.038159    -0.0679468  797 HOH   A O    
5123 O  O    . HOH   G .   ? 0.322568  0.534694 0.517472  -0.0621741  -0.0312761  0.0145199   798 HOH   A O    
5124 O  O    . HOH   G .   ? 0.565439  0.550172 0.193821  0.121147    0.0787583   0.0478954   799 HOH   A O    
5125 O  O    . HOH   G .   ? 0.276171  0.400192 0.196029  0.0587677   -0.00428315 0.021754    800 HOH   A O    
5126 O  O    . HOH   G .   ? 0.253115  0.366369 0.19563   0.0109027   0.0105273   0.0519282   801 HOH   A O    
5127 O  O    . HOH   G .   ? 0.517984  0.667397 0.42193   0.221526    0.170334    0.125055    802 HOH   A O    
5128 O  O    . HOH   G .   ? 0.407402  0.399044 0.478571  -0.0849263  -0.108555   0.0832957   803 HOH   A O    
5129 O  O    . HOH   G .   ? 0.373244  0.394965 0.408242  0.0856634   -0.116638   0.0391596   804 HOH   A O    
5130 O  O    . HOH   G .   ? 0.422058  0.708145 0.425025  -0.0960588  0.136381    -0.171456   805 HOH   A O    
5131 O  O    . HOH   G .   ? 0.347159  0.65766  0.521405  0.013342    0.207217    -0.163994   806 HOH   A O    
5132 O  O    . HOH   G .   ? 0.170605  0.420849 0.319332  -0.0310146  0.0516703   -0.02877    807 HOH   A O    
5133 O  O    . HOH   G .   ? 0.337352  0.631451 0.347253  0.0888026   -0.0362948  0.0678136   808 HOH   A O    
5134 O  O    . HOH   G .   ? 0.363624  0.348872 0.273074  -0.0281219  -0.0260345  0.00662061  809 HOH   A O    
5135 O  O    . HOH   G .   ? 0.335381  0.428492 0.766349  -0.0235055  -0.00537539 0.045029    810 HOH   A O    
5136 O  O    . HOH   G .   ? 0.32668   0.387453 0.210462  0.0506755   0.0113478   -0.0178761  811 HOH   A O    
5137 O  O    . HOH   G .   ? 0.232772  0.73075  0.267947  -0.0429166  -0.0296685  0.246553    812 HOH   A O    
5138 O  O    . HOH   G .   ? 0.223002  0.521701 0.202635  -0.00010695 0.0191335   -0.0132991  813 HOH   A O    
5139 O  O    . HOH   G .   ? 0.528211  0.431852 0.255632  0.0710453   -0.125918   0.090171    814 HOH   A O    
5140 O  O    . HOH   G .   ? 0.484828  0.419772 0.228455  0.0680858   -0.0438199  -0.00197539 815 HOH   A O    
5141 O  O    . HOH   G .   ? 0.483895  0.510668 0.49458   -0.00849731 0.12445     0.0439435   816 HOH   A O    
5142 O  O    . HOH   G .   ? 0.306009  0.366878 0.133369  0.0221702   0.032875    0.0153867   817 HOH   A O    
5143 O  O    . HOH   G .   ? 0.356264  0.599218 0.342884  -0.110771   0.078384    -0.11122    818 HOH   A O    
5144 O  O    . HOH   G .   ? 0.480496  0.673997 0.236268  -0.0359197  -0.0256879  -0.0330964  819 HOH   A O    
5145 O  O    . HOH   G .   ? 0.329512  0.490831 0.307967  0.0533358   0.0671327   -0.00568888 820 HOH   A O    
5146 O  O    . HOH   G .   ? 0.35868   0.68753  0.325266  -0.106106   -0.017045   -0.223313   821 HOH   A O    
5147 O  O    . HOH   G .   ? 0.33624   0.381761 0.613791  -0.0269109  0.183553    0.00813387  822 HOH   A O    
5148 O  O    . HOH   G .   ? 0.600096  0.509316 0.260817  0.243161    -0.170578   -0.11222    823 HOH   A O    
5149 O  O    . HOH   G .   ? 0.225933  0.589199 0.310344  0.050006    -0.0378081  0.0301974   824 HOH   A O    
5150 O  O    . HOH   G .   ? 0.433298  0.669275 0.253823  -0.0277516  0.0238416   0.0280038   825 HOH   A O    
5151 O  O    . HOH   G .   ? 0.350278  0.615483 0.421158  -0.015586   0.072226    -0.172427   826 HOH   A O    
5152 O  O    . HOH   G .   ? 0.370672  0.412597 0.296688  -0.0146245  -0.0505086  -0.0112104  827 HOH   A O    
5153 O  O    . HOH   G .   ? 0.460912  0.729902 0.670099  0.156283    0.145945    0.338707    828 HOH   A O    
5154 O  O    . HOH   G .   ? 0.312486  0.353732 0.302143  -0.0402511  0.0302791   0.0370925   829 HOH   A O    
5155 O  O    . HOH   G .   ? 0.253955  0.295395 0.131974  0.0133562   0.0589547   0.0201066   830 HOH   A O    
5156 O  O    . HOH   G .   ? 0.336804  0.325662 0.617829  0.0188785   -0.0495983  0.01255     831 HOH   A O    
5157 O  O    . HOH   G .   ? 0.248128  0.299549 0.852819  -0.00791795 -0.00104328 0.145486    832 HOH   A O    
5158 O  O    . HOH   G .   ? 0.317599  0.570631 0.39677   0.0790733   -0.099015   -0.136986   833 HOH   A O    
5159 O  O    . HOH   G .   ? 0.388712  0.442632 0.2625    -0.141776   0.0931773   -0.00388348 834 HOH   A O    
5160 O  O    . HOH   G .   ? 0.52856   0.466067 0.458992  0.0997119   -0.30083    -0.203121   835 HOH   A O    
5161 O  O    . HOH   G .   ? 0.314895  0.576398 0.469454  0.0263397   -0.0954608  0.108972    836 HOH   A O    
5162 O  O    . HOH   G .   ? 0.231887  0.436442 0.415261  0.00910711  0.102225    0.00669321  837 HOH   A O    
5163 O  O    . HOH   G .   ? 0.195229  0.357019 0.246236  0.00951044  0.0324157   0.0117205   838 HOH   A O    
5164 O  O    . HOH   G .   ? 0.234565  0.449049 0.304338  0.0136859   0.0480639   0.0484646   839 HOH   A O    
5165 O  O    . HOH   G .   ? 0.405316  0.545587 0.479205  0.0436247   0.174105    0.0330991   840 HOH   A O    
5166 O  O    . HOH   G .   ? 0.718085  0.513983 0.355929  0.244646    -0.122047   0.0405972   841 HOH   A O    
5167 O  O    . HOH   G .   ? 0.413276  0.358952 0.320228  0.0398675   -0.0260862  0.0963097   842 HOH   A O    
5168 O  O    . HOH   G .   ? 0.55996   0.751202 0.41907   -0.0426959  0.193025    0.0471415   843 HOH   A O    
5169 O  O    . HOH   G .   ? 0.447481  0.454913 0.368155  -0.020398   0.117522    0.0567084   844 HOH   A O    
5170 O  O    . HOH   G .   ? 0.456125  0.446454 0.416757  0.0091026   0.231091    0.0928064   845 HOH   A O    
5171 O  O    . HOH   G .   ? 0.29862   0.668964 0.478087  0.015837    -0.0457049  0.192506    846 HOH   A O    
5172 O  O    . HOH   H .   ? 0.386346  0.250938 0.161938  0.109798    -0.0590729  -0.0137168  501 HOH   B O    
5173 O  O    . HOH   H .   ? 0.330621  0.353056 0.2316    0.0205867   0.0399277   -0.136417   502 HOH   B O    
5174 O  O    . HOH   H .   ? 0.22596   0.357474 0.291834  0.0307673   -0.0608797  -0.0641357  503 HOH   B O    
5175 O  O    . HOH   H .   ? 0.303408  0.443654 0.302355  -0.0617079  -0.0743708  -0.0195114  504 HOH   B O    
5176 O  O    . HOH   H .   ? 0.561514  0.778663 0.412296  0.423118    -0.0804119  -0.0322218  505 HOH   B O    
5177 O  O    . HOH   H .   ? 0.350643  0.544049 0.640025  -0.146664   0.0350555   0.0524068   506 HOH   B O    
5178 O  O    . HOH   H .   ? 0.62339   0.456955 0.357186  0.038659    0.156839    0.0288861   507 HOH   B O    
5179 O  O    . HOH   H .   ? 0.11243   0.242592 0.249547  -0.0116788  0.0102956   -0.0304979  508 HOH   B O    
5180 O  O    . HOH   H .   ? 0.349355  0.466868 0.339977  -0.0756122  0.00496034  -0.00828128 509 HOH   B O    
5181 O  O    . HOH   H .   ? 0.395746  0.478021 0.422371  -0.0144741  0.133993    -0.00981684 510 HOH   B O    
5182 O  O    . HOH   H .   ? 0.37732   0.396681 0.32166   -0.097194   0.129972    -0.00337183 511 HOH   B O    
5183 O  O    . HOH   H .   ? 0.529277  0.41713  0.378124  -0.00595012 -0.120798   -0.0112745  512 HOH   B O    
5184 O  O    . HOH   H .   ? 0.333744  0.474318 0.203844  0.0281047   0.108727    -0.0625019  513 HOH   B O    
5185 O  O    . HOH   H .   ? 0.26593   0.466514 0.234398  -0.058453   0.0947757   0.05075     514 HOH   B O    
5186 O  O    . HOH   H .   ? 0.229586  0.258956 0.133405  -0.0420545  0.00263899  -0.0202266  515 HOH   B O    
5187 O  O    . HOH   H .   ? 0.484355  0.747246 0.830634  -0.106749   -0.188197   0.447764    516 HOH   B O    
5188 O  O    . HOH   H .   ? 0.368261  0.458166 0.233359  -0.0263227  -0.0382661  -0.0195781  517 HOH   B O    
5189 O  O    . HOH   H .   ? 0.279299  0.355829 0.260205  0.0167091   -0.0381144  -0.0732555  518 HOH   B O    
5190 O  O    . HOH   H .   ? 0.291131  0.447054 0.374767  -0.0565636  0.0896085   0.0889316   519 HOH   B O    
5191 O  O    . HOH   H .   ? 0.280122  0.583333 0.398047  0.120601    0.0336563   -0.167657   520 HOH   B O    
5192 O  O    . HOH   H .   ? 0.45688   0.527101 0.545223  -0.0895374  0.105698    -0.21211    521 HOH   B O    
5193 O  O    . HOH   H .   ? 0.297134  0.503003 0.194053  -0.0738977  0.0477805   -0.0477747  522 HOH   B O    
5194 O  O    . HOH   H .   ? 0.647494  0.44998  0.430972  -0.150771   0.0139354   0.0770865   523 HOH   B O    
5195 O  O    . HOH   H .   ? 0.320763  0.551947 0.13155   0.210555    -0.0562196  -0.0941103  524 HOH   B O    
5196 O  O    . HOH   H .   ? 0.648472  0.469992 0.18786   0.0994467   -0.0424799  -0.0625149  525 HOH   B O    
5197 O  O    . HOH   H .   ? 0.659183  0.480365 0.324109  -0.247335   0.0660151   0.0489616   526 HOH   B O    
5198 O  O    . HOH   H .   ? 0.425192  0.365736 0.211939  -0.0750496  0.0807646   -0.0585896  527 HOH   B O    
5199 O  O    . HOH   H .   ? 0.275779  0.415599 0.714741  0.0429019   0.0824258   0.0663199   528 HOH   B O    
5200 O  O    . HOH   H .   ? 0.344361  0.502594 0.40044   0.0637959   -0.0629937  -0.0540527  529 HOH   B O    
5201 O  O    . HOH   H .   ? 0.629593  0.418309 0.311967  0.168066    0.0169481   0.140228    530 HOH   B O    
5202 O  O    . HOH   H .   ? 0.173656  0.319705 0.190829  -0.00744457 0.00198915  0.0420051   531 HOH   B O    
5203 O  O    . HOH   H .   ? 0.37644   0.411253 0.324015  0.012446    -0.128808   -0.0329851  532 HOH   B O    
5204 O  O    . HOH   H .   ? 0.210557  0.447783 0.305021  -0.0234481  0.00749168  -0.116881   533 HOH   B O    
5205 O  O    . HOH   H .   ? 0.622563  0.315211 0.37251   -0.0146033  -0.183021   -0.0676387  534 HOH   B O    
5206 O  O    . HOH   H .   ? 0.734399  0.346621 0.245995  0.0131234   0.04694     0.0170053   535 HOH   B O    
5207 O  O    . HOH   H .   ? 0.323946  0.389426 0.349464  0.116708    0.0557889   -0.0101097  536 HOH   B O    
5208 O  O    . HOH   H .   ? 0.559995  0.462782 0.280124  0.0689169   -0.0987602  -0.0272179  537 HOH   B O    
5209 O  O    . HOH   H .   ? 0.415257  0.577201 0.359173  0.0514239   -0.02762    -0.177289   538 HOH   B O    
5210 O  O    . HOH   H .   ? 0.499319  0.621774 0.46555   -0.176975   0.135997    0.0798091   539 HOH   B O    
5211 O  O    . HOH   H .   ? 0.32569   0.555382 0.248708  0.0465348   0.0395736   0.0583211   540 HOH   B O    
5212 O  O    . HOH   H .   ? 0.286949  0.500275 0.155556  0.0757905   -0.0320171  -0.0339102  541 HOH   B O    
5213 O  O    . HOH   H .   ? 0.226707  0.257344 0.135254  0.0159093   -0.0264646  -0.0328855  542 HOH   B O    
5214 O  O    . HOH   H .   ? 0.339414  0.380575 0.269156  -0.0707662  -0.0713997  -0.0395985  543 HOH   B O    
5215 O  O    . HOH   H .   ? 0.541446  0.490799 0.262346  -0.0141684  -0.127704   0.0363113   544 HOH   B O    
5216 O  O    . HOH   H .   ? 0.171373  0.450815 0.345284  0.0542668   -0.0635881  -0.236977   545 HOH   B O    
5217 O  O    . HOH   H .   ? 0.271187  0.306252 0.234838  0.0058634   0.00786448  -0.050382   546 HOH   B O    
5218 O  O    . HOH   H .   ? 0.240416  0.36661  0.204964  0.0228836   0.0297003   0.124366    547 HOH   B O    
5219 O  O    . HOH   H .   ? 0.213388  0.258807 0.199457  0.0172076   -0.0106436  -0.0301982  548 HOH   B O    
5220 O  O    . HOH   H .   ? 0.204194  0.415226 0.323864  -0.0116012  0.0485679   0.0649847   549 HOH   B O    
5221 O  O    . HOH   H .   ? 0.328144  0.721702 0.478435  -0.222591   0.0657627   -0.24147    550 HOH   B O    
5222 O  O    . HOH   H .   ? 0.485926  0.342876 0.468044  0.0732294   0.191575    -0.079006   551 HOH   B O    
5223 O  O    . HOH   H .   ? 0.20719   0.51251  0.442152  0.068776    0.0730243   0.131369    552 HOH   B O    
5224 O  O    . HOH   H .   ? 0.24565   0.331944 0.176671  0.0181537   0.0174706   -0.0226354  553 HOH   B O    
5225 O  O    . HOH   H .   ? 0.229376  0.443102 0.205717  0.0155283   0.00949022  0.0824475   554 HOH   B O    
5226 O  O    . HOH   H .   ? 0.310468  0.39436  0.310093  0.00944032  -0.121251   -0.0513149  555 HOH   B O    
5227 O  O    . HOH   H .   ? 0.466711  0.403059 0.423994  0.00589944  -0.0885353  0.019987    556 HOH   B O    
5228 O  O    . HOH   H .   ? 0.478199  0.389116 0.185706  0.0448915   0.0550204   -0.0477288  557 HOH   B O    
5229 O  O    . HOH   H .   ? 0.372066  0.453132 0.560337  0.0723869   -0.223989   -0.0417043  558 HOH   B O    
5230 O  O    . HOH   H .   ? 0.410248  0.361674 0.251779  0.0677055   -0.158245   -0.0186909  559 HOH   B O    
5231 O  O    . HOH   H .   ? 0.507627  0.888729 0.302753  0.179498    -0.136916   -0.214691   560 HOH   B O    
5232 O  O    . HOH   H .   ? 0.345629  0.421636 0.401036  0.0170949   0.00504064  -0.00717605 561 HOH   B O    
5233 O  O    . HOH   H .   ? 0.254172  0.682458 0.184536  0.0319476   0.00312788  0.0511018   562 HOH   B O    
5234 O  O    . HOH   H .   ? 0.378492  0.440585 0.182184  -0.0713894  -0.0670498  -0.035093   563 HOH   B O    
5235 O  O    . HOH   H .   ? 0.367093  0.334696 0.382987  -0.0319397  0.0229328   -0.0567599  564 HOH   B O    
5236 O  O    . HOH   H .   ? 0.219601  0.270036 0.108302  0.0351459   -0.0374197  -0.0227618  565 HOH   B O    
5237 O  O    . HOH   H .   ? 0.232277  0.199444 0.167581  0.00665563  -0.0153133  -0.0241087  566 HOH   B O    
5238 O  O    . HOH   H .   ? 0.306738  0.400506 0.260869  0.00142489  -0.106715   -0.00151185 567 HOH   B O    
5239 O  O    . HOH   H .   ? 0.275668  0.341583 0.210147  0.00662877  0.0184526   0.0255008   568 HOH   B O    
5240 O  O    . HOH   H .   ? 0.214292  0.288691 0.166574  -0.0142996  -0.0417023  -0.0765617  569 HOH   B O    
5241 O  O    . HOH   H .   ? 0.302931  0.485445 0.351535  -0.0160505  0.150017    -0.0581978  570 HOH   B O    
5242 O  O    . HOH   H .   ? 0.410735  0.448264 0.37694   -0.0892309  0.0460842   -0.11016    571 HOH   B O    
5243 O  O    . HOH   H .   ? 0.194442  0.214246 0.126289  -0.0287749  -0.00251942 -0.0134193  572 HOH   B O    
5244 O  O    . HOH   H .   ? 0.313614  0.407893 0.246906  -0.00809821 0.120732    -0.075699   573 HOH   B O    
5245 O  O    . HOH   H .   ? 0.195586  0.387322 0.180892  0.0722521   -0.0699507  -0.0614476  574 HOH   B O    
5246 O  O    . HOH   H .   ? 0.293227  0.496037 0.201388  0.0190637   0.075999    -0.00561752 575 HOH   B O    
5247 O  O    . HOH   H .   ? 0.266386  0.587362 0.432557  -0.124516   0.0640619   -0.0928539  576 HOH   B O    
5248 O  O    . HOH   H .   ? 0.167933  0.344442 0.0916838 -0.0124347  -0.0233249  0.0105713   577 HOH   B O    
5249 O  O    . HOH   H .   ? 0.432     0.384887 0.204244  -0.0606638  -0.0693319  0.0124332   578 HOH   B O    
5250 O  O    . HOH   H .   ? 0.347447  0.38096  0.166056  0.0134215   -0.102555   0.012558    579 HOH   B O    
5251 O  O    . HOH   H .   ? 0.142819  0.262281 0.115022  0.0226018   -0.0157699  0.0154982   580 HOH   B O    
5252 O  O    . HOH   H .   ? 0.279565  0.459854 0.438636  -0.0381525  -0.0403275  -0.144667   581 HOH   B O    
5253 O  O    . HOH   H .   ? 0.490625  0.598298 0.48723   0.00195736  0.130424    -0.137303   582 HOH   B O    
5254 O  O    . HOH   H .   ? 0.363014  0.342271 0.237314  0.00050019  -0.0419671  -0.0196867  583 HOH   B O    
5255 O  O    . HOH   H .   ? 0.463519  0.446111 0.809558  -0.121618   -0.356943   0.213326    584 HOH   B O    
5256 O  O    . HOH   H .   ? 0.4667    0.639917 0.278728  0.298672    -0.102839   -0.0818575  585 HOH   B O    
5257 O  O    . HOH   H .   ? 0.414998  0.701133 0.355003  -0.0853861  -0.14257    0.0475836   586 HOH   B O    
5258 O  O    . HOH   H .   ? 0.216645  0.217646 0.160826  -0.0407583  0.0511302   -0.0227658  587 HOH   B O    
5259 O  O    . HOH   H .   ? 0.258791  0.36363  0.236319  -0.00251389 -0.0481553  0.0359135   588 HOH   B O    
5260 O  O    . HOH   H .   ? 0.623772  0.296239 0.0684603 -0.145081   -0.0313723  0.00270063  589 HOH   B O    
5261 O  O    . HOH   H .   ? 0.480098  0.499675 0.350703  -0.00576942 0.212299    -0.114586   590 HOH   B O    
5262 O  O    . HOH   H .   ? 0.257669  0.483743 0.208751  0.0301749   0.00592505  0.0991649   591 HOH   B O    
5263 O  O    . HOH   H .   ? 0.315491  0.231521 0.116249  -0.00159979 -0.0612085  -0.00672144 592 HOH   B O    
5264 O  O    . HOH   H .   ? 0.244542  0.459029 0.209992  0.0768785   -0.00014833 0.00115712  593 HOH   B O    
5265 O  O    . HOH   H .   ? 0.419004  0.418393 0.652253  -0.151883   -0.142169   0.216774    594 HOH   B O    
5266 O  O    . HOH   H .   ? 0.429508  0.31921  0.279396  -0.03051    -0.0572499  -0.063682   595 HOH   B O    
5267 O  O    . HOH   H .   ? 0.411655  0.536213 0.22327   -0.0147134  -0.0238637  0.0358556   596 HOH   B O    
5268 O  O    . HOH   H .   ? 0.591693  0.415275 0.384586  -0.125591   0.075405    -0.0540135  597 HOH   B O    
5269 O  O    . HOH   H .   ? 0.60288   0.529942 0.504543  -0.0222421  -0.032979   0.277724    598 HOH   B O    
5270 O  O    . HOH   H .   ? 0.416944  0.589301 0.450059  -0.208129   0.100459    -0.191621   599 HOH   B O    
5271 O  O    . HOH   H .   ? 0.45437   0.402492 0.316698  -0.0453841  -0.0738399  0.110029    600 HOH   B O    
5272 O  O    . HOH   H .   ? 0.295928  0.616153 0.31606   -0.0845352  -0.0336165  0.0301075   601 HOH   B O    
5273 O  O    . HOH   H .   ? 0.362266  0.395652 0.502245  -0.0767337  -0.0264066  -0.0159194  602 HOH   B O    
5274 O  O    . HOH   H .   ? 0.264635  0.547252 0.350777  -0.0643445  0.0107395   -0.0114991  603 HOH   B O    
5275 O  O    . HOH   H .   ? 0.177698  0.189004 0.111626  0.00014132  -0.0502078  -0.0127119  604 HOH   B O    
5276 O  O    . HOH   H .   ? 0.266364  0.943517 0.196935  -0.0377089  -0.0506429  0.064229    605 HOH   B O    
5277 O  O    . HOH   H .   ? 0.412355  0.509239 0.255986  0.0900258   -0.122763   0.0277743   606 HOH   B O    
5278 O  O    . HOH   H .   ? 0.376248  0.339475 0.403674  -0.0329843  0.00324739  -0.0898154  607 HOH   B O    
5279 O  O    . HOH   H .   ? 0.316234  0.692553 0.325656  -0.0179452  0.0593262   -0.0720669  608 HOH   B O    
5280 O  O    . HOH   H .   ? 0.339316  0.363767 0.228411  0.0654195   0.0408764   0.00885746  609 HOH   B O    
5281 O  O    . HOH   H .   ? 0.644423  0.416194 0.327292  -0.103182   0.140438    0.0815454   610 HOH   B O    
5282 O  O    . HOH   H .   ? 0.23334   0.683882 0.652177  -0.0315743  0.114976    -0.183408   611 HOH   B O    
5283 O  O    . HOH   H .   ? 0.390391  0.403604 0.311961  -0.0170111  -0.151829   0.0896057   612 HOH   B O    
5284 O  O    . HOH   H .   ? 0.320162  0.257742 0.233144  -0.0146265  -0.0117822  0.0767369   613 HOH   B O    
5285 O  O    . HOH   H .   ? 0.372073  0.304545 0.0911865 0.0471797   0.00314984  0.0196369   614 HOH   B O    
5286 O  O    . HOH   H .   ? 0.484772  0.444676 0.382175  0.042187    0.127636    0.059609    615 HOH   B O    
5287 O  O    . HOH   H .   ? 0.381603  0.394416 0.347038  -0.0384947  -0.0569772  0.00617002  616 HOH   B O    
5288 O  O    . HOH   H .   ? 0.566517  0.519721 0.248935  -0.0341505  0.0892084   -0.141425   617 HOH   B O    
5289 O  O    . HOH   H .   ? 0.216277  0.290464 0.122802  -0.0571251  -0.0112682  -0.00312826 618 HOH   B O    
5290 O  O    . HOH   H .   ? 0.260328  0.395324 0.256755  -0.0417896  -0.0475476  -0.00131415 619 HOH   B O    
5291 O  O    . HOH   H .   ? 0.284787  0.594282 0.267191  0.109662    0.109595    0.169492    620 HOH   B O    
5292 O  O    . HOH   H .   ? 0.181621  0.190481 0.10904   0.0105636   0.0249766   -0.00050414 621 HOH   B O    
5293 O  O    . HOH   H .   ? 0.313217  0.322883 0.543626  0.00850533  -0.0760422  -0.0672097  622 HOH   B O    
5294 O  O    . HOH   H .   ? 0.466966  0.38826  0.357476  0.115269    0.0683433   0.0828986   623 HOH   B O    
5295 O  O    . HOH   H .   ? 0.485369  0.388416 0.60723   -0.0327454  -0.263973   0.061335    624 HOH   B O    
5296 O  O    . HOH   H .   ? 0.240004  0.615397 0.180779  0.0314746   -0.0432217  -0.0258304  625 HOH   B O    
5297 O  O    . HOH   H .   ? 0.51336   0.423067 0.416515  0.0799964   0.0239235   -0.0163721  626 HOH   B O    
5298 O  O    . HOH   H .   ? 0.509043  0.435853 0.306706  0.0367046   -0.0881181  0.0544198   627 HOH   B O    
5299 O  O    . HOH   H .   ? 0.424591  0.293748 0.298054  -0.029437   0.0235293   -0.0138836  628 HOH   B O    
5300 O  O    . HOH   H .   ? 0.306212  0.632033 0.456621  0.0233153   0.184827    0.0938252   629 HOH   B O    
5301 O  O    . HOH   H .   ? 0.351931  0.470241 0.276205  0.0589771   -0.0499408  -0.0530691  630 HOH   B O    
5302 O  O    . HOH   H .   ? 0.235513  0.376059 0.296299  0.0134187   -0.0119114  -0.00282117 631 HOH   B O    
5303 O  O    . HOH   H .   ? 0.589101  0.523432 0.378654  -0.256287   0.0599851   0.0124913   632 HOH   B O    
5304 O  O    . HOH   H .   ? 0.292957  0.727543 0.442154  0.00471388  -0.0305095  -0.283593   633 HOH   B O    
5305 O  O    . HOH   H .   ? 0.14737   0.220765 0.0974416 -0.00987793 -0.0127616  -0.0234858  634 HOH   B O    
5306 O  O    . HOH   H .   ? 0.218008  0.262328 0.111815  0.00612007  -0.0672608  0.0167065   635 HOH   B O    
5307 O  O    . HOH   H .   ? 0.334048  0.318834 0.190871  -0.0601987  0.015192    -0.11164    636 HOH   B O    
5308 O  O    . HOH   H .   ? 0.582101  0.521007 0.241151  0.0941304   -0.0266473  -0.0622739  637 HOH   B O    
5309 O  O    . HOH   H .   ? 0.376764  0.307889 0.124192  0.0554839   0.0600088   0.0455917   638 HOH   B O    
5310 O  O    . HOH   H .   ? 0.322419  0.409119 0.32789   -0.0551936  -0.00573187 -0.0552429  639 HOH   B O    
5311 O  O    . HOH   H .   ? 0.487281  0.366222 0.495998  0.0851407   -0.243147   -0.108769   640 HOH   B O    
5312 O  O    . HOH   H .   ? 0.197046  0.213273 0.105997  0.00610805  -0.00919555 -0.00905293 641 HOH   B O    
5313 O  O    . HOH   H .   ? 0.460333  0.524953 0.440235  -0.00784095 0.102034    -0.13506    642 HOH   B O    
5314 O  O    . HOH   H .   ? 0.297471  0.305876 0.145658  -0.0131692  -0.00360898 0.0049358   643 HOH   B O    
5315 O  O    . HOH   H .   ? 0.195461  0.353127 0.104462  0.0415504   -0.0144881  0.0263362   644 HOH   B O    
5316 O  O    . HOH   H .   ? 0.285557  0.445376 0.260506  0.086378    0.0807776   0.139475    645 HOH   B O    
5317 O  O    . HOH   H .   ? 0.467404  0.762683 0.344145  0.111472    0.00843241  0.0171346   646 HOH   B O    
5318 O  O    . HOH   H .   ? 0.169141  0.180332 0.0880693 -0.0219773  -0.0421302  -0.00957718 647 HOH   B O    
5319 O  O    . HOH   H .   ? 0.285179  0.368975 0.355016  -0.0665283  0.0514219   -0.0913871  648 HOH   B O    
5320 O  O    . HOH   H .   ? 0.23345   0.253392 0.216128  0.0180727   0.00844249  -0.0442555  649 HOH   B O    
5321 O  O    . HOH   H .   ? 0.277856  0.512155 0.128759  0.0672867   0.0391251   -0.0167372  650 HOH   B O    
5322 O  O    . HOH   H .   ? 0.307078  0.455049 0.563801  -0.0421376  -0.0184138  -0.0985536  651 HOH   B O    
5323 O  O    . HOH   H .   ? 0.396824  0.589165 0.392158  0.0127567   -0.190994   -0.0580971  652 HOH   B O    
5324 O  O    . HOH   H .   ? 0.189461  0.382091 0.259604  -0.0317301  -0.0204909  -0.0227026  653 HOH   B O    
5325 O  O    . HOH   H .   ? 0.301724  0.399012 0.26615   -0.0217031  -0.0112901  -0.0473627  654 HOH   B O    
5326 O  O    . HOH   H .   ? 0.276784  0.371675 0.169453  -0.0695031  0.0197075   0.0375669   655 HOH   B O    
5327 O  O    . HOH   H .   ? 0.161292  0.29328  0.159175  0.0302956   0.00571944  0.0456712   656 HOH   B O    
5328 O  O    . HOH   H .   ? 0.782587  0.596947 0.261054  -0.0199305  0.0998855   -0.0874841  657 HOH   B O    
5329 O  O    . HOH   H .   ? 0.469389  0.364571 0.280541  -0.0574058  -0.0680241  -0.0267878  658 HOH   B O    
5330 O  O    . HOH   H .   ? 0.237943  0.383878 0.211346  0.0835026   -0.0139822  -0.0794267  659 HOH   B O    
5331 O  O    . HOH   H .   ? 0.707244  0.400721 0.350357  0.180958    -0.0324266  -0.0530821  660 HOH   B O    
5332 O  O    . HOH   H .   ? 0.41932   0.531552 0.233634  -0.0643046  -0.0166305  0.00064601  661 HOH   B O    
5333 O  O    . HOH   H .   ? 0.217083  0.260967 0.246312  -0.0453457  0.0192919   -0.0675785  662 HOH   B O    
5334 O  O    . HOH   H .   ? 0.280681  0.369347 0.219772  0.0459616   -0.0642913  -0.0856307  663 HOH   B O    
5335 O  O    . HOH   H .   ? 0.407346  0.426085 0.287683  0.0400873   0.0114292   0.0788246   664 HOH   B O    
5336 O  O    . HOH   H .   ? 0.42443   0.387729 0.441199  -0.0595503  -0.136295   -0.0874711  665 HOH   B O    
5337 O  O    . HOH   H .   ? 0.554892  0.518286 0.293586  -0.0665785  -0.00704624 0.142182    666 HOH   B O    
5338 O  O    . HOH   H .   ? 0.322758  0.530081 0.2391    0.0696028   -0.0404889  0.0269874   667 HOH   B O    
5339 O  O    . HOH   H .   ? 0.477346  0.419761 0.263966  -0.0522545  -0.0905963  0.136799    668 HOH   B O    
5340 O  O    . HOH   H .   ? 0.339574  0.555063 0.271546  0.221708    0.0935955   0.178106    669 HOH   B O    
5341 O  O    . HOH   H .   ? 0.28885   0.322596 0.214166  -0.0543027  -0.0373806  0.0844518   670 HOH   B O    
5342 O  O    . HOH   H .   ? 0.212483  0.656901 0.617504  -0.0971273  0.0717274   -0.231187   671 HOH   B O    
5343 O  O    . HOH   H .   ? 0.301163  0.228183 0.307317  -0.00367948 0.0111984   0.00088297  672 HOH   B O    
5344 O  O    . HOH   H .   ? 0.301602  0.535853 0.220216  0.164292    -0.0376582  -0.0256239  673 HOH   B O    
5345 O  O    . HOH   H .   ? 0.289288  0.63141  0.426545  0.0500838   0.101048    -0.283101   674 HOH   B O    
5346 O  O    . HOH   H .   ? 0.27965   0.450503 0.122691  0.0709884   0.0796789   0.0612996   675 HOH   B O    
5347 O  O    . HOH   H .   ? 0.27866   0.325316 0.301401  -0.00115556 -0.176174   -0.0236978  676 HOH   B O    
5348 O  O    . HOH   H .   ? 0.238758  0.745456 0.406692  0.0239481   -0.0306489  0.0625034   677 HOH   B O    
5349 O  O    . HOH   H .   ? 0.386042  0.453832 0.173139  0.0718099   -0.17948    -0.0310737  678 HOH   B O    
5350 O  O    . HOH   H .   ? 0.537418  0.407661 0.459585  -0.044576   -0.109583   0.0958811   679 HOH   B O    
5351 O  O    . HOH   H .   ? 0.414479  0.526048 0.143601  0.110012    -0.0858118  -0.121833   680 HOH   B O    
5352 O  O    . HOH   H .   ? 0.441145  0.426568 0.350268  -0.0156949  -0.140508   0.152312    681 HOH   B O    
5353 O  O    . HOH   H .   ? 0.173294  0.291913 0.0982387 0.0256028   0.0173039   -0.0245003  682 HOH   B O    
5354 O  O    . HOH   H .   ? 0.216576  0.434008 0.182455  -0.0655566  0.0355315   0.00888144  683 HOH   B O    
5355 O  O    . HOH   H .   ? 0.93225   0.508373 0.216112  -0.0709697  -0.010342   -0.101414   684 HOH   B O    
5356 O  O    . HOH   H .   ? 0.17407   0.276617 0.20155   -0.00531447 0.0160587   0.044003    685 HOH   B O    
5357 O  O    . HOH   H .   ? 0.381984  0.608763 0.401007  -0.190486   -0.064973   0.11884     686 HOH   B O    
5358 O  O    . HOH   H .   ? 0.160502  0.327441 0.1795    0.0129584   -0.03269    -0.0122359  687 HOH   B O    
5359 O  O    . HOH   H .   ? 0.377693  0.416171 0.245275  -0.00218812 0.0177012   -0.0357675  688 HOH   B O    
5360 O  O    . HOH   H .   ? 0.548558  0.560194 0.58042   -0.100005   0.165129    -0.140672   689 HOH   B O    
5361 O  O    . HOH   H .   ? 0.587933  0.682462 0.251743  -0.0875495  0.0723557   -0.037738   690 HOH   B O    
5362 O  O    . HOH   H .   ? 0.461367  0.424582 0.297656  -0.0423165  0.0231215   -0.0659372  691 HOH   B O    
5363 O  O    . HOH   H .   ? 0.42623   0.298225 0.309337  0.0354409   -0.147278   -0.0222044  692 HOH   B O    
5364 O  O    . HOH   H .   ? 0.3797    0.430806 0.499424  0.0661967   -0.148413   -0.0412921  693 HOH   B O    
5365 O  O    . HOH   H .   ? 0.297332  0.317102 0.149381  -0.0763419  -0.0626081  0.00396496  694 HOH   B O    
5366 O  O    . HOH   H .   ? 0.278268  0.307795 0.273041  -0.0134676  0.122675    0.0929489   695 HOH   B O    
5367 O  O    . HOH   H .   ? 0.506092  0.505544 0.188339  0.165442    -0.0196919  0.0424667   696 HOH   B O    
5368 O  O    . HOH   H .   ? 0.328426  0.75868  0.254755  -0.146766   -0.0919802  0.0777804   697 HOH   B O    
5369 O  O    . HOH   H .   ? 0.443838  0.460973 0.201177  0.0865441   0.0110647   -0.0412222  698 HOH   B O    
5370 O  O    . HOH   H .   ? 0.473176  0.451517 0.348728  0.0762231   0.117108    0.142084    699 HOH   B O    
5371 O  O    . HOH   H .   ? 0.241442  0.820015 0.505151  -0.0766791  0.0214092   0.21044     700 HOH   B O    
5372 O  O    . HOH   H .   ? 0.284796  0.406664 0.242502  0.0261326   0.0544326   0.019254    701 HOH   B O    
5373 O  O    . HOH   H .   ? 0.358414  0.555465 0.469079  0.136445    -0.0841537  -0.134268   702 HOH   B O    
5374 O  O    . HOH   H .   ? 0.408745  0.474249 0.287842  0.0249576   -0.0518153  0.156962    703 HOH   B O    
5375 O  O    . HOH   H .   ? 0.493265  0.355122 0.272671  -0.083051   -0.130171   0.0420674   704 HOH   B O    
5376 O  O    . HOH   H .   ? 0.343037  0.396914 0.330487  -0.0247004  -0.0160918  0.0620173   705 HOH   B O    
5377 O  O    . HOH   H .   ? 0.191155  0.364782 0.144509  0.023865    -0.0162885  0.0138507   706 HOH   B O    
5378 O  O    . HOH   H .   ? 0.243052  0.466042 0.155679  -0.107417   0.0402183   0.0185258   707 HOH   B O    
5379 O  O    . HOH   H .   ? 0.220119  0.385929 0.0744268 0.018169    -0.0217962  -0.0194666  708 HOH   B O    
5380 O  O    . HOH   H .   ? 0.418229  0.368043 0.56381   0.0620223   -0.0564399  -0.0200854  709 HOH   B O    
5381 O  O    . HOH   H .   ? 0.372109  0.586203 0.474525  -0.0848759  0.0126425   0.104668    710 HOH   B O    
5382 O  O    . HOH   H .   ? 0.379521  0.561924 0.130935  -0.0732381  -0.062668   0.115111    711 HOH   B O    
5383 O  O    . HOH   H .   ? 0.473026  0.327115 0.16699   -0.0643944  -0.0878936  0.042321    712 HOH   B O    
5384 O  O    . HOH   H .   ? 0.207149  0.305214 0.0812869 0.00288149  -0.0218252  0.00967007  713 HOH   B O    
5385 O  O    . HOH   H .   ? 0.307569  0.763378 0.234933  -0.131922   0.0630758   -0.174665   714 HOH   B O    
5386 O  O    . HOH   H .   ? 0.279037  0.383494 0.247188  0.00241473  0.0284244   0.0762871   715 HOH   B O    
5387 O  O    . HOH   H .   ? 0.906794  0.36113  0.281223  0.133809    0.0526497   0.0252909   716 HOH   B O    
5388 O  O    . HOH   H .   ? 0.564823  0.511889 0.20447   0.122669    -0.0163026  -0.0360588  717 HOH   B O    
5389 O  O    . HOH   H .   ? 0.270267  0.43836  0.136057  0.0471486   0.0699067   0.0446104   718 HOH   B O    
5390 O  O    . HOH   H .   ? 0.220688  0.560034 0.473471  0.0823529   -0.00279305 -0.165884   719 HOH   B O    
5391 O  O    . HOH   H .   ? 0.53824   0.336445 0.802863  0.152932    0.100539    0.0351577   720 HOH   B O    
5392 O  O    . HOH   H .   ? 0.398961  0.323191 0.551473  -0.0671534  -0.0683695  -0.0839061  721 HOH   B O    
5393 O  O    . HOH   H .   ? 0.450179  0.544027 0.223168  -0.0740522  -0.060971   0.081029    722 HOH   B O    
5394 O  O    . HOH   H .   ? 0.313906  0.713576 0.394013  -0.0628347  0.046987    0.0918109   723 HOH   B O    
5395 O  O    . HOH   H .   ? 0.30402   0.492677 0.116702  -0.0814217  -0.0256147  0.0136325   724 HOH   B O    
5396 O  O    . HOH   H .   ? 0.535611  0.60718  0.197859  0.176772    -0.127074   -0.113128   725 HOH   B O    
5397 O  O    . HOH   H .   ? 0.585674  0.32554  0.174596  -0.060677   0.00348847  -0.0267053  726 HOH   B O    
5398 O  O    . HOH   H .   ? 0.350376  0.293059 0.615474  -0.0590585  0.0765222   0.087243    727 HOH   B O    
5399 O  O    . HOH   H .   ? 0.524582  0.444642 0.40145   0.0235585   -0.0194448  -0.0732995  728 HOH   B O    
5400 O  O    . HOH   H .   ? 0.607001  0.554524 0.409974  -0.0932064  -0.218771   -0.0340766  729 HOH   B O    
5401 O  O    . HOH   H .   ? 0.229265  0.715648 0.271605  0.00762053  -0.0220799  0.131783    730 HOH   B O    
5402 O  O    . HOH   H .   ? 0.247845  0.515923 0.370806  0.0618477   -0.0542704  -0.00202971 731 HOH   B O    
5403 O  O    . HOH   H .   ? 0.411423  0.655143 0.723687  0.196838    -0.0318817  0.168726    732 HOH   B O    
5404 O  O    . HOH   H .   ? 0.369633  0.788215 0.489548  0.165413    -0.044656   -0.20024    733 HOH   B O    
5405 O  O    . HOH   H .   ? 0.245422  0.882137 0.964288  -0.00742995 0.0843612   -0.0203074  734 HOH   B O    
5406 O  O    . HOH   H .   ? 0.622128  0.371412 0.725559  -0.0847373  -0.248232   0.110698    735 HOH   B O    
5407 O  O    . HOH   H .   ? 0.587519  0.411167 0.18261   0.0619853   -0.101299   0.00188028  736 HOH   B O    
5408 O  O    . HOH   H .   ? 0.39663   0.518787 0.322181  -0.0121355  0.0548686   -0.110246   737 HOH   B O    
5409 O  O    . HOH   H .   ? 0.283131  0.407343 0.118064  0.0369927   0.0178519   -0.00585069 738 HOH   B O    
5410 O  O    . HOH   H .   ? 0.291934  0.410703 0.291311  -0.0790389  0.0260041   -0.0123023  739 HOH   B O    
5411 O  O    . HOH   H .   ? 0.257612  0.402024 0.402357  -0.0331987  0.0167312   -0.0495183  740 HOH   B O    
5412 O  O    . HOH   H .   ? 0.560562  0.373088 0.79736   -0.018397   -0.104614   0.0461647   741 HOH   B O    
5413 O  O    . HOH   H .   ? 0.324994  0.512034 0.231881  0.0926689   -0.057398   0.0514901   742 HOH   B O    
5414 O  O    . HOH   H .   ? 0.652064  0.480714 0.229696  -0.00471811 -0.0124636  0.0789552   743 HOH   B O    
5415 O  O    . HOH   H .   ? 0.530871  0.45227  0.297464  0.0855292   -0.108571   0.0139648   744 HOH   B O    
5416 O  O    . HOH   H .   ? 0.482712  0.434499 0.281024  0.0589257   0.0540767   -0.030024   745 HOH   B O    
5417 O  O    . HOH   H .   ? 0.43936   0.392337 0.304424  0.0127069   -0.0749896  -0.0243384  746 HOH   B O    
5418 O  O    . HOH   H .   ? 0.539059  0.755973 0.473287  0.268374    0.239989    0.210688    747 HOH   B O    
5419 O  O    . HOH   H .   ? 0.484178  0.424284 0.415776  0.0270576   -0.150012   -0.0254838  748 HOH   B O    
5420 O  O    . HOH   H .   ? 0.309971  0.370368 0.23928   0.0686395   -0.00673335 0.0992647   749 HOH   B O    
5421 O  O    . HOH   H .   ? 0.468816  0.466376 0.332095  -0.00406505 -0.0682931  0.00183959  750 HOH   B O    
5422 O  O    . HOH   H .   ? 0.552267  0.438774 0.280866  0.0132754   -0.00848677 0.0714906   751 HOH   B O    
5423 O  O    . HOH   H .   ? 0.42866   0.519242 0.283253  -0.0903743  0.0182839   0.0318843   752 HOH   B O    
5424 O  O    . HOH   H .   ? 0.553309  0.57105  0.249625  -0.101357   0.217015    -0.0574173  753 HOH   B O    
5425 O  O    . HOH   H .   ? 0.568904  0.469402 0.282833  -0.0942766  -0.181267   0.0810656   754 HOH   B O    
5426 O  O    . HOH   H .   ? 0.445069  0.455691 0.390567  -0.104242   -0.0801242  0.0404796   755 HOH   B O    
5427 O  O    . HOH   H .   ? 0.274793  0.504669 0.316071  0.0964071   0.0151653   0.00554603  756 HOH   B O    
5428 O  O    . HOH   H .   ? 0.250806  0.347725 0.159257  -0.0126252  0.0381293   -0.0652549  757 HOH   B O    
5429 O  O    . HOH   H .   ? 0.495622  0.611233 0.280046  0.218964    0.00194665  0.0851868   758 HOH   B O    
5430 O  O    . HOH   H .   ? 0.490574  0.307021 0.21832   -0.0760982  -0.111314   0.00939737  759 HOH   B O    
5431 O  O    . HOH   H .   ? 0.502659  0.495128 0.285997  0.162967    0.0451516   0.0986539   760 HOH   B O    
5432 O  O    . HOH   H .   ? 0.574365  0.446251 0.342769  -0.0637966  0.084434    0.16326     761 HOH   B O    
5433 O  O    . HOH   H .   ? 0.826633  0.5928   0.305919  -0.231236   -0.11655    0.0448598   762 HOH   B O    
5434 O  O    . HOH   H .   ? 0.345854  0.495072 0.196332  -0.0454752  0.0738994   -0.0706359  763 HOH   B O    
5435 O  O    . HOH   H .   ? 0.4802    0.438987 0.3905    0.0494468   -0.22928    -0.0107232  764 HOH   B O    
5436 O  O    . HOH   H .   ? 0.571421  0.511089 0.383902  0.0458888   -0.124966   -0.127429   765 HOH   B O    
5437 O  O    . HOH   H .   ? 0.327902  0.52329  0.211546  0.00047377  0.0789971   -0.0210448  766 HOH   B O    
5438 O  O    . HOH   H .   ? 0.361746  0.618684 0.496424  -0.053973   -0.167004   0.0552031   767 HOH   B O    
5439 O  O    . HOH   H .   ? 0.369674  0.611033 0.355008  -0.060987   0.0347159   0.0900437   768 HOH   B O    
5440 O  O    . HOH   H .   ? 0.622564  0.752221 0.478759  0.14652     0.0766689   0.0190095   769 HOH   B O    
5441 O  O    . HOH   H .   ? 0.652814  0.534151 0.722961  -0.0157367  0.320763    -0.17513    770 HOH   B O    
5442 O  O    . HOH   H .   ? 0.761729  0.596408 0.418305  0.283496    -0.0561562  0.0939789   771 HOH   B O    
5443 O  O    . HOH   H .   ? 0.496424  0.403113 0.251483  0.0406258   -0.127117   0.0293035   772 HOH   B O    
5444 O  O    . HOH   H .   ? 0.266918  0.707898 0.34914   0.0740085   0.0650722   0.015162    773 HOH   B O    
5445 O  O    . HOH   H .   ? 0.2242    0.400455 0.264613  -0.0412797  0.0108257   -0.0170294  774 HOH   B O    
5446 O  O    . HOH   H .   ? 0.651222  0.399707 0.343233  0.0440628   -0.0967869  -0.0538138  775 HOH   B O    
5447 O  O    . HOH   H .   ? 0.482496  0.369278 0.20145   -0.0779535  -0.00516551 -0.0134153  776 HOH   B O    
5448 O  O    . HOH   H .   ? 0.339879  0.547983 0.422294  0.138476    0.0385445   0.0359367   777 HOH   B O    
5449 O  O    . HOH   H .   ? 0.483749  0.566461 0.2896    -0.105133   0.059946    -0.0123135  778 HOH   B O    
5450 O  O    . HOH   H .   ? 0.368102  0.645721 0.547238  -0.073482   -0.0213331  0.277471    779 HOH   B O    
5451 O  O    . HOH   H .   ? 0.37863   0.385848 0.322846  0.0161859   -0.135715   0.0928869   780 HOH   B O    
5452 O  O    . HOH   H .   ? 0.456828  0.448917 0.454828  0.0020078   0.18771     0.117092    781 HOH   B O    
5453 O  O    . HOH   H .   ? 0.4684    0.53394  0.170667  0.110895    0.0216923   -0.0598716  782 HOH   B O    
5454 O  O    . HOH   H .   ? 0.563894  0.385666 0.231985  0.0419773   0.0959933   0.0198502   783 HOH   B O    
5455 O  O    . HOH   H .   ? 0.314765  0.406046 0.49745   -0.041747   0.175174    -0.0861437  784 HOH   B O    
5456 O  O    . HOH   H .   ? 0.602615  0.577894 0.173325  0.0173912   -0.12511    0.0140932   785 HOH   B O    
5457 O  O    . HOH   H .   ? 0.601858  0.648784 0.995695  0.168656    0.337978    0.240276    786 HOH   B O    
5458 O  O    . HOH   H .   ? 0.287136  0.880008 0.306956  -0.118984   -0.0736799  -0.0970907  787 HOH   B O    
5459 O  O    . HOH   H .   ? 0.464733  0.639966 0.481818  0.128535    0.218003    0.0245238   788 HOH   B O    
5460 O  O    . HOH   H .   ? 0.227403  0.495981 0.23705   -0.0244158  0.0289404   0.00267853  789 HOH   B O    
5461 O  O    . HOH   H .   ? 0.538231  0.7391   0.317987  -0.150047   -0.184455   0.0557229   790 HOH   B O    
5462 O  O    . HOH   H .   ? 0.342184  0.562993 0.300801  0.0670357   0.0795322   -0.0235774  791 HOH   B O    
5463 O  O    . HOH   H .   ? 0.476403  0.434485 0.377974  -0.0359116  -0.0243619  -0.0736651  792 HOH   B O    
5464 O  O    . HOH   H .   ? 0.297298  0.389403 0.296194  -0.0172215  0.0773974   -0.00491019 793 HOH   B O    
5465 O  O    . HOH   H .   ? 0.398411  0.514152 0.25368   -0.0430657  -0.117153   0.0456029   794 HOH   B O    
5466 O  O    . HOH   H .   ? 0.332721  0.5501   0.492943  -0.0462459  0.00919737  -0.0955592  795 HOH   B O    
5467 O  O    . HOH   H .   ? 0.491325  0.547363 0.302947  -0.0997361  -0.0831924  -0.0371106  796 HOH   B O    
5468 O  O    . HOH   H .   ? 0.332416  0.850615 0.2826    0.0212361   0.112159    0.0527571   797 HOH   B O    
5469 O  O    . HOH   H .   ? 0.572618  0.723659 0.254651  0.211947    -0.0677034  0.059248    798 HOH   B O    
# 
