data_9EDQ
# 
_entry.id   9EDQ 
# 
_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   9EDQ         pdb_00009edq 10.2210/pdb9edq/pdb 
WWPDB D_1000290196 ?            ?                   
# 
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 2025-03-19 ? 
3 'Structure model' 1 2 2025-04-23 ? 
# 
_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        
# 
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.page_first'              
7  2 'Structure model' '_citation.page_last'               
8  2 'Structure model' '_citation.pdbx_database_id_DOI'    
9  2 'Structure model' '_citation.pdbx_database_id_PubMed' 
10 2 'Structure model' '_citation.title'                   
11 2 'Structure model' '_citation.year'                    
12 3 'Structure model' '_citation.journal_volume'          
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9EDQ 
_pdbx_database_status.recvd_initial_deposition_date   2024-11-17 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 3 
_pdbx_contact_author.email              g.hansman@griffith.edu.au 
_pdbx_contact_author.name_first         Grant 
_pdbx_contact_author.name_last          Hansman 
_pdbx_contact_author.name_mi            S. 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-8735-4618 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Holroyd, D.L.' 1 0009-0002-2830-6020 
'Kumar, A.'     2 0000-0001-7540-6177 
'Bruning, J.B.' 3 0000-0002-6919-1824 
'Hansman, G.S.' 4 0000-0001-8735-4618 
# 
_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.Virol. 
_citation.journal_id_ASTM           JOVIAM 
_citation.journal_id_CSD            0825 
_citation.journal_id_ISSN           1098-5514 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            99 
_citation.language                  ? 
_citation.page_first                e0197124 
_citation.page_last                 e0197124 
_citation.title                     'Antigenic structural analysis of bat and human norovirus protruding (P) domains.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1128/jvi.01971-24 
_citation.pdbx_database_id_PubMed   40062838 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Holroyd, D.L.'    1 0009-0002-2830-6020 
primary 'Kumar, A.'        2 0000-0001-7540-6177 
primary 'Vasquez, E.'      3 ?                   
primary 'Masic, V.'        4 ?                   
primary 'von Itzstein, M.' 5 0000-0001-6302-7524 
primary 'Bruning, J.B.'    6 0000-0002-6919-1824 
primary 'Hansman, G.S.'    7 0000-0001-8735-4618 
# 
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 VP1           32288.195 2   ? ? 'protruding domain' ? 
2 non-polymer syn 'SULFATE ION' 96.063    4   ? ? ?                   ? 
3 water       nat water         18.015    862 ? ? ?                   ? 
# 
_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       
;EPFSLPNLQTDEMSSSRWPNPLATLFADPNVAVAPQWQNGRCTLEGELLGTTPRNASWLNRFRGVSTAAVANQVLHLTLY
EPDGSVFNPLSGAPAPEGFPDFTAQEYHLRAAGKVANTTGGGEIKSTDYTPALGGVKITAWDATGPSAGVEMTGQIESIG
MENNTDFDVLPDYNGSAFDGSLNLAPPIVPLLPGETLLRFGTVPITTRRQSDPIRIISCALPQEWITWFLTHNFTALGDA
ALLRYRNQATGQLLFECKLYRSGFVVVNGVNVRTEFPMSGVFEFVSWVPNFFQLAPV
;
_entity_poly.pdbx_seq_one_letter_code_can   
;EPFSLPNLQTDEMSSSRWPNPLATLFADPNVAVAPQWQNGRCTLEGELLGTTPRNASWLNRFRGVSTAAVANQVLHLTLY
EPDGSVFNPLSGAPAPEGFPDFTAQEYHLRAAGKVANTTGGGEIKSTDYTPALGGVKITAWDATGPSAGVEMTGQIESIG
MENNTDFDVLPDYNGSAFDGSLNLAPPIVPLLPGETLLRFGTVPITTRRQSDPIRIISCALPQEWITWFLTHNFTALGDA
ALLRYRNQATGQLLFECKLYRSGFVVVNGVNVRTEFPMSGVFEFVSWVPNFFQLAPV
;
_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 'SULFATE ION' SO4 
3 water         HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLU n 
1 2   PRO n 
1 3   PHE n 
1 4   SER n 
1 5   LEU n 
1 6   PRO n 
1 7   ASN n 
1 8   LEU n 
1 9   GLN n 
1 10  THR n 
1 11  ASP n 
1 12  GLU n 
1 13  MET n 
1 14  SER n 
1 15  SER n 
1 16  SER n 
1 17  ARG n 
1 18  TRP n 
1 19  PRO n 
1 20  ASN n 
1 21  PRO n 
1 22  LEU n 
1 23  ALA n 
1 24  THR n 
1 25  LEU n 
1 26  PHE n 
1 27  ALA n 
1 28  ASP n 
1 29  PRO n 
1 30  ASN n 
1 31  VAL n 
1 32  ALA n 
1 33  VAL n 
1 34  ALA n 
1 35  PRO n 
1 36  GLN n 
1 37  TRP n 
1 38  GLN n 
1 39  ASN n 
1 40  GLY n 
1 41  ARG n 
1 42  CYS n 
1 43  THR n 
1 44  LEU n 
1 45  GLU n 
1 46  GLY n 
1 47  GLU n 
1 48  LEU n 
1 49  LEU n 
1 50  GLY n 
1 51  THR n 
1 52  THR n 
1 53  PRO n 
1 54  ARG n 
1 55  ASN n 
1 56  ALA n 
1 57  SER n 
1 58  TRP n 
1 59  LEU n 
1 60  ASN n 
1 61  ARG n 
1 62  PHE n 
1 63  ARG n 
1 64  GLY n 
1 65  VAL n 
1 66  SER n 
1 67  THR n 
1 68  ALA n 
1 69  ALA n 
1 70  VAL n 
1 71  ALA n 
1 72  ASN n 
1 73  GLN n 
1 74  VAL n 
1 75  LEU n 
1 76  HIS n 
1 77  LEU n 
1 78  THR n 
1 79  LEU n 
1 80  TYR n 
1 81  GLU n 
1 82  PRO n 
1 83  ASP n 
1 84  GLY n 
1 85  SER n 
1 86  VAL n 
1 87  PHE n 
1 88  ASN n 
1 89  PRO n 
1 90  LEU n 
1 91  SER n 
1 92  GLY n 
1 93  ALA n 
1 94  PRO n 
1 95  ALA n 
1 96  PRO n 
1 97  GLU n 
1 98  GLY n 
1 99  PHE n 
1 100 PRO n 
1 101 ASP n 
1 102 PHE n 
1 103 THR n 
1 104 ALA n 
1 105 GLN n 
1 106 GLU n 
1 107 TYR n 
1 108 HIS n 
1 109 LEU n 
1 110 ARG n 
1 111 ALA n 
1 112 ALA n 
1 113 GLY n 
1 114 LYS n 
1 115 VAL n 
1 116 ALA n 
1 117 ASN n 
1 118 THR n 
1 119 THR n 
1 120 GLY n 
1 121 GLY n 
1 122 GLY n 
1 123 GLU n 
1 124 ILE n 
1 125 LYS n 
1 126 SER n 
1 127 THR n 
1 128 ASP n 
1 129 TYR n 
1 130 THR n 
1 131 PRO n 
1 132 ALA n 
1 133 LEU n 
1 134 GLY n 
1 135 GLY n 
1 136 VAL n 
1 137 LYS n 
1 138 ILE n 
1 139 THR n 
1 140 ALA n 
1 141 TRP n 
1 142 ASP n 
1 143 ALA n 
1 144 THR n 
1 145 GLY n 
1 146 PRO n 
1 147 SER n 
1 148 ALA n 
1 149 GLY n 
1 150 VAL n 
1 151 GLU n 
1 152 MET n 
1 153 THR n 
1 154 GLY n 
1 155 GLN n 
1 156 ILE n 
1 157 GLU n 
1 158 SER n 
1 159 ILE n 
1 160 GLY n 
1 161 MET n 
1 162 GLU n 
1 163 ASN n 
1 164 ASN n 
1 165 THR n 
1 166 ASP n 
1 167 PHE n 
1 168 ASP n 
1 169 VAL n 
1 170 LEU n 
1 171 PRO n 
1 172 ASP n 
1 173 TYR n 
1 174 ASN n 
1 175 GLY n 
1 176 SER n 
1 177 ALA n 
1 178 PHE n 
1 179 ASP n 
1 180 GLY n 
1 181 SER n 
1 182 LEU n 
1 183 ASN n 
1 184 LEU n 
1 185 ALA n 
1 186 PRO n 
1 187 PRO n 
1 188 ILE n 
1 189 VAL n 
1 190 PRO n 
1 191 LEU n 
1 192 LEU n 
1 193 PRO n 
1 194 GLY n 
1 195 GLU n 
1 196 THR n 
1 197 LEU n 
1 198 LEU n 
1 199 ARG n 
1 200 PHE n 
1 201 GLY n 
1 202 THR n 
1 203 VAL n 
1 204 PRO n 
1 205 ILE n 
1 206 THR n 
1 207 THR n 
1 208 ARG n 
1 209 ARG n 
1 210 GLN n 
1 211 SER n 
1 212 ASP n 
1 213 PRO n 
1 214 ILE n 
1 215 ARG n 
1 216 ILE n 
1 217 ILE n 
1 218 SER n 
1 219 CYS n 
1 220 ALA n 
1 221 LEU n 
1 222 PRO n 
1 223 GLN n 
1 224 GLU n 
1 225 TRP n 
1 226 ILE n 
1 227 THR n 
1 228 TRP n 
1 229 PHE n 
1 230 LEU n 
1 231 THR n 
1 232 HIS n 
1 233 ASN n 
1 234 PHE n 
1 235 THR n 
1 236 ALA n 
1 237 LEU n 
1 238 GLY n 
1 239 ASP n 
1 240 ALA n 
1 241 ALA n 
1 242 LEU n 
1 243 LEU n 
1 244 ARG n 
1 245 TYR n 
1 246 ARG n 
1 247 ASN n 
1 248 GLN n 
1 249 ALA n 
1 250 THR n 
1 251 GLY n 
1 252 GLN n 
1 253 LEU n 
1 254 LEU n 
1 255 PHE n 
1 256 GLU n 
1 257 CYS n 
1 258 LYS n 
1 259 LEU n 
1 260 TYR n 
1 261 ARG n 
1 262 SER n 
1 263 GLY n 
1 264 PHE n 
1 265 VAL n 
1 266 VAL n 
1 267 VAL n 
1 268 ASN n 
1 269 GLY n 
1 270 VAL n 
1 271 ASN n 
1 272 VAL n 
1 273 ARG n 
1 274 THR n 
1 275 GLU n 
1 276 PHE n 
1 277 PRO n 
1 278 MET n 
1 279 SER n 
1 280 GLY n 
1 281 VAL n 
1 282 PHE n 
1 283 GLU n 
1 284 PHE n 
1 285 VAL n 
1 286 SER n 
1 287 TRP n 
1 288 VAL n 
1 289 PRO n 
1 290 ASN n 
1 291 PHE n 
1 292 PHE n 
1 293 GLN n 
1 294 LEU n 
1 295 ALA n 
1 296 PRO n 
1 297 VAL n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   297 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ORF2 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    GX/NPIH26 
_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      'Bat norovirus' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     1514709 
_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 
ALA 'L-peptide linking' y ALANINE         ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE        ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE       ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE       ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER           ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE      ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE      ? 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE   ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE         ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE          ? 'C3 H7 N O3'     105.093 
SO4 non-polymer         . 'SULFATE ION'   ? 'O4 S -2'        96.063  
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   GLU 1   226 226 GLU GLU A . n 
A 1 2   PRO 2   227 227 PRO PRO A . n 
A 1 3   PHE 3   228 228 PHE PHE A . n 
A 1 4   SER 4   229 229 SER SER A . n 
A 1 5   LEU 5   230 230 LEU LEU A . n 
A 1 6   PRO 6   231 231 PRO PRO A . n 
A 1 7   ASN 7   232 232 ASN ASN A . n 
A 1 8   LEU 8   233 233 LEU LEU A . n 
A 1 9   GLN 9   234 234 GLN GLN A . n 
A 1 10  THR 10  235 235 THR THR A . n 
A 1 11  ASP 11  236 236 ASP ASP A . n 
A 1 12  GLU 12  237 237 GLU GLU A . n 
A 1 13  MET 13  238 238 MET MET A . n 
A 1 14  SER 14  239 239 SER SER A . n 
A 1 15  SER 15  240 240 SER SER A . n 
A 1 16  SER 16  241 241 SER SER A . n 
A 1 17  ARG 17  242 242 ARG ARG A . n 
A 1 18  TRP 18  243 243 TRP TRP A . n 
A 1 19  PRO 19  244 244 PRO PRO A . n 
A 1 20  ASN 20  245 245 ASN ASN A . n 
A 1 21  PRO 21  246 246 PRO PRO A . n 
A 1 22  LEU 22  247 247 LEU LEU A . n 
A 1 23  ALA 23  248 248 ALA ALA A . n 
A 1 24  THR 24  249 249 THR THR A . n 
A 1 25  LEU 25  250 250 LEU LEU A . n 
A 1 26  PHE 26  251 251 PHE PHE A . n 
A 1 27  ALA 27  252 252 ALA ALA A . n 
A 1 28  ASP 28  253 253 ASP ASP A . n 
A 1 29  PRO 29  254 254 PRO PRO A . n 
A 1 30  ASN 30  255 255 ASN ASN A . n 
A 1 31  VAL 31  256 256 VAL VAL A . n 
A 1 32  ALA 32  257 257 ALA ALA A . n 
A 1 33  VAL 33  258 258 VAL VAL A . n 
A 1 34  ALA 34  259 259 ALA ALA A . n 
A 1 35  PRO 35  260 260 PRO PRO A . n 
A 1 36  GLN 36  261 261 GLN GLN A . n 
A 1 37  TRP 37  262 262 TRP TRP A . n 
A 1 38  GLN 38  263 263 GLN GLN A . n 
A 1 39  ASN 39  264 264 ASN ASN A . n 
A 1 40  GLY 40  265 265 GLY GLY A . n 
A 1 41  ARG 41  266 266 ARG ARG A . n 
A 1 42  CYS 42  267 267 CYS CYS A . n 
A 1 43  THR 43  268 268 THR THR A . n 
A 1 44  LEU 44  269 269 LEU LEU A . n 
A 1 45  GLU 45  270 270 GLU GLU A . n 
A 1 46  GLY 46  271 271 GLY GLY A . n 
A 1 47  GLU 47  272 272 GLU GLU A . n 
A 1 48  LEU 48  273 273 LEU LEU A . n 
A 1 49  LEU 49  274 274 LEU LEU A . n 
A 1 50  GLY 50  275 275 GLY GLY A . n 
A 1 51  THR 51  276 276 THR THR A . n 
A 1 52  THR 52  277 277 THR THR A . n 
A 1 53  PRO 53  278 278 PRO PRO A . n 
A 1 54  ARG 54  279 279 ARG ARG A . n 
A 1 55  ASN 55  280 280 ASN ASN A . n 
A 1 56  ALA 56  281 281 ALA ALA A . n 
A 1 57  SER 57  282 282 SER SER A . n 
A 1 58  TRP 58  283 283 TRP TRP A . n 
A 1 59  LEU 59  284 284 LEU LEU A . n 
A 1 60  ASN 60  285 285 ASN ASN A . n 
A 1 61  ARG 61  286 286 ARG ARG A . n 
A 1 62  PHE 62  287 287 PHE PHE A . n 
A 1 63  ARG 63  288 288 ARG ARG A . n 
A 1 64  GLY 64  289 289 GLY GLY A . n 
A 1 65  VAL 65  290 290 VAL VAL A . n 
A 1 66  SER 66  291 291 SER SER A . n 
A 1 67  THR 67  292 292 THR THR A . n 
A 1 68  ALA 68  293 293 ALA ALA A . n 
A 1 69  ALA 69  294 294 ALA ALA A . n 
A 1 70  VAL 70  295 295 VAL VAL A . n 
A 1 71  ALA 71  296 296 ALA ALA A . n 
A 1 72  ASN 72  297 297 ASN ASN A . n 
A 1 73  GLN 73  298 298 GLN GLN A . n 
A 1 74  VAL 74  299 299 VAL VAL A . n 
A 1 75  LEU 75  300 300 LEU LEU A . n 
A 1 76  HIS 76  301 301 HIS HIS A . n 
A 1 77  LEU 77  302 302 LEU LEU A . n 
A 1 78  THR 78  303 303 THR THR A . n 
A 1 79  LEU 79  304 304 LEU LEU A . n 
A 1 80  TYR 80  305 305 TYR TYR A . n 
A 1 81  GLU 81  306 306 GLU GLU A . n 
A 1 82  PRO 82  307 307 PRO PRO A . n 
A 1 83  ASP 83  308 308 ASP ASP A . n 
A 1 84  GLY 84  309 309 GLY GLY A . n 
A 1 85  SER 85  310 310 SER SER A . n 
A 1 86  VAL 86  311 311 VAL VAL A . n 
A 1 87  PHE 87  312 312 PHE PHE A . n 
A 1 88  ASN 88  313 313 ASN ASN A . n 
A 1 89  PRO 89  314 314 PRO PRO A . n 
A 1 90  LEU 90  315 315 LEU LEU A . n 
A 1 91  SER 91  316 316 SER SER A . n 
A 1 92  GLY 92  317 317 GLY GLY A . n 
A 1 93  ALA 93  318 318 ALA ALA A . n 
A 1 94  PRO 94  319 319 PRO PRO A . n 
A 1 95  ALA 95  320 320 ALA ALA A . n 
A 1 96  PRO 96  321 321 PRO PRO A . n 
A 1 97  GLU 97  322 322 GLU GLU A . n 
A 1 98  GLY 98  323 323 GLY GLY A . n 
A 1 99  PHE 99  324 324 PHE PHE A . n 
A 1 100 PRO 100 325 325 PRO PRO A . n 
A 1 101 ASP 101 326 326 ASP ASP A . n 
A 1 102 PHE 102 327 327 PHE PHE A . n 
A 1 103 THR 103 328 328 THR THR A . n 
A 1 104 ALA 104 329 329 ALA ALA A . n 
A 1 105 GLN 105 330 330 GLN GLN A . n 
A 1 106 GLU 106 331 331 GLU GLU A . n 
A 1 107 TYR 107 332 332 TYR TYR A . n 
A 1 108 HIS 108 333 333 HIS HIS A . n 
A 1 109 LEU 109 334 334 LEU LEU A . n 
A 1 110 ARG 110 335 335 ARG ARG A . n 
A 1 111 ALA 111 336 336 ALA ALA A . n 
A 1 112 ALA 112 337 337 ALA ALA A . n 
A 1 113 GLY 113 338 338 GLY GLY A . n 
A 1 114 LYS 114 339 339 LYS LYS A . n 
A 1 115 VAL 115 340 340 VAL VAL A . n 
A 1 116 ALA 116 341 341 ALA ALA A . n 
A 1 117 ASN 117 342 342 ASN ASN A . n 
A 1 118 THR 118 343 343 THR THR A . n 
A 1 119 THR 119 344 344 THR THR A . n 
A 1 120 GLY 120 345 345 GLY GLY A . n 
A 1 121 GLY 121 346 346 GLY GLY A . n 
A 1 122 GLY 122 347 347 GLY GLY A . n 
A 1 123 GLU 123 348 348 GLU GLU A . n 
A 1 124 ILE 124 349 349 ILE ILE A . n 
A 1 125 LYS 125 350 350 LYS LYS A . n 
A 1 126 SER 126 351 351 SER SER A . n 
A 1 127 THR 127 352 352 THR THR A . n 
A 1 128 ASP 128 353 353 ASP ASP A . n 
A 1 129 TYR 129 354 354 TYR TYR A . n 
A 1 130 THR 130 355 355 THR THR A . n 
A 1 131 PRO 131 356 356 PRO PRO A . n 
A 1 132 ALA 132 357 357 ALA ALA A . n 
A 1 133 LEU 133 358 358 LEU LEU A . n 
A 1 134 GLY 134 359 359 GLY GLY A . n 
A 1 135 GLY 135 360 360 GLY GLY A . n 
A 1 136 VAL 136 361 361 VAL VAL A . n 
A 1 137 LYS 137 362 362 LYS LYS A . n 
A 1 138 ILE 138 363 363 ILE ILE A . n 
A 1 139 THR 139 364 364 THR THR A . n 
A 1 140 ALA 140 365 365 ALA ALA A . n 
A 1 141 TRP 141 366 366 TRP TRP A . n 
A 1 142 ASP 142 367 367 ASP ASP A . n 
A 1 143 ALA 143 368 368 ALA ALA A . n 
A 1 144 THR 144 369 369 THR THR A . n 
A 1 145 GLY 145 370 370 GLY GLY A . n 
A 1 146 PRO 146 371 371 PRO PRO A . n 
A 1 147 SER 147 372 372 SER SER A . n 
A 1 148 ALA 148 373 373 ALA ALA A . n 
A 1 149 GLY 149 374 374 GLY GLY A . n 
A 1 150 VAL 150 375 375 VAL VAL A . n 
A 1 151 GLU 151 376 376 GLU GLU A . n 
A 1 152 MET 152 377 377 MET MET A . n 
A 1 153 THR 153 378 378 THR THR A . n 
A 1 154 GLY 154 379 379 GLY GLY A . n 
A 1 155 GLN 155 380 380 GLN GLN A . n 
A 1 156 ILE 156 381 381 ILE ILE A . n 
A 1 157 GLU 157 382 382 GLU GLU A . n 
A 1 158 SER 158 383 383 SER SER A . n 
A 1 159 ILE 159 384 384 ILE ILE A . n 
A 1 160 GLY 160 385 385 GLY GLY A . n 
A 1 161 MET 161 386 386 MET MET A . n 
A 1 162 GLU 162 387 387 GLU GLU A . n 
A 1 163 ASN 163 388 388 ASN ASN A . n 
A 1 164 ASN 164 389 389 ASN ASN A . n 
A 1 165 THR 165 390 390 THR THR A . n 
A 1 166 ASP 166 391 391 ASP ASP A . n 
A 1 167 PHE 167 392 392 PHE PHE A . n 
A 1 168 ASP 168 393 393 ASP ASP A . n 
A 1 169 VAL 169 394 394 VAL VAL A . n 
A 1 170 LEU 170 395 395 LEU LEU A . n 
A 1 171 PRO 171 396 396 PRO PRO A . n 
A 1 172 ASP 172 397 397 ASP ASP A . n 
A 1 173 TYR 173 398 398 TYR TYR A . n 
A 1 174 ASN 174 399 399 ASN ASN A . n 
A 1 175 GLY 175 400 400 GLY GLY A . n 
A 1 176 SER 176 401 401 SER SER A . n 
A 1 177 ALA 177 402 402 ALA ALA A . n 
A 1 178 PHE 178 403 403 PHE PHE A . n 
A 1 179 ASP 179 404 404 ASP ASP A . n 
A 1 180 GLY 180 405 405 GLY GLY A . n 
A 1 181 SER 181 406 406 SER SER A . n 
A 1 182 LEU 182 407 407 LEU LEU A . n 
A 1 183 ASN 183 408 408 ASN ASN A . n 
A 1 184 LEU 184 409 409 LEU LEU A . n 
A 1 185 ALA 185 410 410 ALA ALA A . n 
A 1 186 PRO 186 411 411 PRO PRO A . n 
A 1 187 PRO 187 412 412 PRO PRO A . n 
A 1 188 ILE 188 413 413 ILE ILE A . n 
A 1 189 VAL 189 414 414 VAL VAL A . n 
A 1 190 PRO 190 415 415 PRO PRO A . n 
A 1 191 LEU 191 416 416 LEU LEU A . n 
A 1 192 LEU 192 417 417 LEU LEU A . n 
A 1 193 PRO 193 418 418 PRO PRO A . n 
A 1 194 GLY 194 419 419 GLY GLY A . n 
A 1 195 GLU 195 420 420 GLU GLU A . n 
A 1 196 THR 196 421 421 THR THR A . n 
A 1 197 LEU 197 422 422 LEU LEU A . n 
A 1 198 LEU 198 423 423 LEU LEU A . n 
A 1 199 ARG 199 424 424 ARG ARG A . n 
A 1 200 PHE 200 425 425 PHE PHE A . n 
A 1 201 GLY 201 426 426 GLY GLY A . n 
A 1 202 THR 202 427 427 THR THR A . n 
A 1 203 VAL 203 428 428 VAL VAL A . n 
A 1 204 PRO 204 429 429 PRO PRO A . n 
A 1 205 ILE 205 430 430 ILE ILE A . n 
A 1 206 THR 206 431 431 THR THR A . n 
A 1 207 THR 207 432 432 THR THR A . n 
A 1 208 ARG 208 433 433 ARG ARG A . n 
A 1 209 ARG 209 434 434 ARG ARG A . n 
A 1 210 GLN 210 435 435 GLN GLN A . n 
A 1 211 SER 211 436 436 SER SER A . n 
A 1 212 ASP 212 437 437 ASP ASP A . n 
A 1 213 PRO 213 438 438 PRO PRO A . n 
A 1 214 ILE 214 439 439 ILE ILE A . n 
A 1 215 ARG 215 440 440 ARG ARG A . n 
A 1 216 ILE 216 441 441 ILE ILE A . n 
A 1 217 ILE 217 442 442 ILE ILE A . n 
A 1 218 SER 218 443 443 SER SER A . n 
A 1 219 CYS 219 444 444 CYS CYS A . n 
A 1 220 ALA 220 445 445 ALA ALA A . n 
A 1 221 LEU 221 446 446 LEU LEU A . n 
A 1 222 PRO 222 447 447 PRO PRO A . n 
A 1 223 GLN 223 448 448 GLN GLN A . n 
A 1 224 GLU 224 449 449 GLU GLU A . n 
A 1 225 TRP 225 450 450 TRP TRP A . n 
A 1 226 ILE 226 451 451 ILE ILE A . n 
A 1 227 THR 227 452 452 THR THR A . n 
A 1 228 TRP 228 453 453 TRP TRP A . n 
A 1 229 PHE 229 454 454 PHE PHE A . n 
A 1 230 LEU 230 455 455 LEU LEU A . n 
A 1 231 THR 231 456 456 THR THR A . n 
A 1 232 HIS 232 457 457 HIS HIS A . n 
A 1 233 ASN 233 458 458 ASN ASN A . n 
A 1 234 PHE 234 459 459 PHE PHE A . n 
A 1 235 THR 235 460 460 THR THR A . n 
A 1 236 ALA 236 461 461 ALA ALA A . n 
A 1 237 LEU 237 462 462 LEU LEU A . n 
A 1 238 GLY 238 463 463 GLY GLY A . n 
A 1 239 ASP 239 464 464 ASP ASP A . n 
A 1 240 ALA 240 465 465 ALA ALA A . n 
A 1 241 ALA 241 466 466 ALA ALA A . n 
A 1 242 LEU 242 467 467 LEU LEU A . n 
A 1 243 LEU 243 468 468 LEU LEU A . n 
A 1 244 ARG 244 469 469 ARG ARG A . n 
A 1 245 TYR 245 470 470 TYR TYR A . n 
A 1 246 ARG 246 471 471 ARG ARG A . n 
A 1 247 ASN 247 472 472 ASN ASN A . n 
A 1 248 GLN 248 473 473 GLN GLN A . n 
A 1 249 ALA 249 474 474 ALA ALA A . n 
A 1 250 THR 250 475 475 THR THR A . n 
A 1 251 GLY 251 476 476 GLY GLY A . n 
A 1 252 GLN 252 477 477 GLN GLN A . n 
A 1 253 LEU 253 478 478 LEU LEU A . n 
A 1 254 LEU 254 479 479 LEU LEU A . n 
A 1 255 PHE 255 480 480 PHE PHE A . n 
A 1 256 GLU 256 481 481 GLU GLU A . n 
A 1 257 CYS 257 482 482 CYS CYS A . n 
A 1 258 LYS 258 483 483 LYS LYS A . n 
A 1 259 LEU 259 484 484 LEU LEU A . n 
A 1 260 TYR 260 485 485 TYR TYR A . n 
A 1 261 ARG 261 486 486 ARG ARG A . n 
A 1 262 SER 262 487 487 SER SER A . n 
A 1 263 GLY 263 488 488 GLY GLY A . n 
A 1 264 PHE 264 489 489 PHE PHE A . n 
A 1 265 VAL 265 490 490 VAL VAL A . n 
A 1 266 VAL 266 491 491 VAL VAL A . n 
A 1 267 VAL 267 492 492 VAL VAL A . n 
A 1 268 ASN 268 493 493 ASN ASN A . n 
A 1 269 GLY 269 494 494 GLY GLY A . n 
A 1 270 VAL 270 495 495 VAL VAL A . n 
A 1 271 ASN 271 496 496 ASN ASN A . n 
A 1 272 VAL 272 497 497 VAL VAL A . n 
A 1 273 ARG 273 498 498 ARG ARG A . n 
A 1 274 THR 274 499 499 THR THR A . n 
A 1 275 GLU 275 500 500 GLU GLU A . n 
A 1 276 PHE 276 501 501 PHE PHE A . n 
A 1 277 PRO 277 502 502 PRO PRO A . n 
A 1 278 MET 278 503 503 MET MET A . n 
A 1 279 SER 279 504 504 SER SER A . n 
A 1 280 GLY 280 505 505 GLY GLY A . n 
A 1 281 VAL 281 506 506 VAL VAL A . n 
A 1 282 PHE 282 507 507 PHE PHE A . n 
A 1 283 GLU 283 508 508 GLU GLU A . n 
A 1 284 PHE 284 509 509 PHE PHE A . n 
A 1 285 VAL 285 510 510 VAL VAL A . n 
A 1 286 SER 286 511 511 SER SER A . n 
A 1 287 TRP 287 512 512 TRP TRP A . n 
A 1 288 VAL 288 513 513 VAL VAL A . n 
A 1 289 PRO 289 514 514 PRO PRO A . n 
A 1 290 ASN 290 515 515 ASN ASN A . n 
A 1 291 PHE 291 516 516 PHE PHE A . n 
A 1 292 PHE 292 517 517 PHE PHE A . n 
A 1 293 GLN 293 518 518 GLN GLN A . n 
A 1 294 LEU 294 519 519 LEU LEU A . n 
A 1 295 ALA 295 520 520 ALA ALA A . n 
A 1 296 PRO 296 521 521 PRO PRO A . n 
A 1 297 VAL 297 522 522 VAL VAL A . n 
B 1 1   GLU 1   226 226 GLU GLU B . n 
B 1 2   PRO 2   227 227 PRO PRO B . n 
B 1 3   PHE 3   228 228 PHE PHE B . n 
B 1 4   SER 4   229 229 SER SER B . n 
B 1 5   LEU 5   230 230 LEU LEU B . n 
B 1 6   PRO 6   231 231 PRO PRO B . n 
B 1 7   ASN 7   232 232 ASN ASN B . n 
B 1 8   LEU 8   233 233 LEU LEU B . n 
B 1 9   GLN 9   234 234 GLN GLN B . n 
B 1 10  THR 10  235 235 THR THR B . n 
B 1 11  ASP 11  236 236 ASP ASP B . n 
B 1 12  GLU 12  237 237 GLU GLU B . n 
B 1 13  MET 13  238 238 MET MET B . n 
B 1 14  SER 14  239 239 SER SER B . n 
B 1 15  SER 15  240 240 SER SER B . n 
B 1 16  SER 16  241 241 SER SER B . n 
B 1 17  ARG 17  242 242 ARG ARG B . n 
B 1 18  TRP 18  243 243 TRP TRP B . n 
B 1 19  PRO 19  244 244 PRO PRO B . n 
B 1 20  ASN 20  245 245 ASN ASN B . n 
B 1 21  PRO 21  246 246 PRO PRO B . n 
B 1 22  LEU 22  247 247 LEU LEU B . n 
B 1 23  ALA 23  248 248 ALA ALA B . n 
B 1 24  THR 24  249 249 THR THR B . n 
B 1 25  LEU 25  250 250 LEU LEU B . n 
B 1 26  PHE 26  251 251 PHE PHE B . n 
B 1 27  ALA 27  252 252 ALA ALA B . n 
B 1 28  ASP 28  253 253 ASP ASP B . n 
B 1 29  PRO 29  254 254 PRO PRO B . n 
B 1 30  ASN 30  255 255 ASN ASN B . n 
B 1 31  VAL 31  256 256 VAL VAL B . n 
B 1 32  ALA 32  257 257 ALA ALA B . n 
B 1 33  VAL 33  258 258 VAL VAL B . n 
B 1 34  ALA 34  259 259 ALA ALA B . n 
B 1 35  PRO 35  260 260 PRO PRO B . n 
B 1 36  GLN 36  261 261 GLN GLN B . n 
B 1 37  TRP 37  262 262 TRP TRP B . n 
B 1 38  GLN 38  263 263 GLN GLN B . n 
B 1 39  ASN 39  264 264 ASN ASN B . n 
B 1 40  GLY 40  265 265 GLY GLY B . n 
B 1 41  ARG 41  266 266 ARG ARG B . n 
B 1 42  CYS 42  267 267 CYS CYS B . n 
B 1 43  THR 43  268 268 THR THR B . n 
B 1 44  LEU 44  269 269 LEU LEU B . n 
B 1 45  GLU 45  270 270 GLU GLU B . n 
B 1 46  GLY 46  271 271 GLY GLY B . n 
B 1 47  GLU 47  272 272 GLU GLU B . n 
B 1 48  LEU 48  273 273 LEU LEU B . n 
B 1 49  LEU 49  274 274 LEU LEU B . n 
B 1 50  GLY 50  275 275 GLY GLY B . n 
B 1 51  THR 51  276 276 THR THR B . n 
B 1 52  THR 52  277 277 THR THR B . n 
B 1 53  PRO 53  278 278 PRO PRO B . n 
B 1 54  ARG 54  279 279 ARG ARG B . n 
B 1 55  ASN 55  280 280 ASN ASN B . n 
B 1 56  ALA 56  281 281 ALA ALA B . n 
B 1 57  SER 57  282 282 SER SER B . n 
B 1 58  TRP 58  283 283 TRP TRP B . n 
B 1 59  LEU 59  284 284 LEU LEU B . n 
B 1 60  ASN 60  285 285 ASN ASN B . n 
B 1 61  ARG 61  286 286 ARG ARG B . n 
B 1 62  PHE 62  287 287 PHE PHE B . n 
B 1 63  ARG 63  288 288 ARG ARG B . n 
B 1 64  GLY 64  289 289 GLY GLY B . n 
B 1 65  VAL 65  290 290 VAL VAL B . n 
B 1 66  SER 66  291 291 SER SER B . n 
B 1 67  THR 67  292 292 THR THR B . n 
B 1 68  ALA 68  293 293 ALA ALA B . n 
B 1 69  ALA 69  294 294 ALA ALA B . n 
B 1 70  VAL 70  295 295 VAL VAL B . n 
B 1 71  ALA 71  296 296 ALA ALA B . n 
B 1 72  ASN 72  297 297 ASN ASN B . n 
B 1 73  GLN 73  298 298 GLN GLN B . n 
B 1 74  VAL 74  299 299 VAL VAL B . n 
B 1 75  LEU 75  300 300 LEU LEU B . n 
B 1 76  HIS 76  301 301 HIS HIS B . n 
B 1 77  LEU 77  302 302 LEU LEU B . n 
B 1 78  THR 78  303 303 THR THR B . n 
B 1 79  LEU 79  304 304 LEU LEU B . n 
B 1 80  TYR 80  305 305 TYR TYR B . n 
B 1 81  GLU 81  306 306 GLU GLU B . n 
B 1 82  PRO 82  307 307 PRO PRO B . n 
B 1 83  ASP 83  308 308 ASP ASP B . n 
B 1 84  GLY 84  309 309 GLY GLY B . n 
B 1 85  SER 85  310 310 SER SER B . n 
B 1 86  VAL 86  311 311 VAL VAL B . n 
B 1 87  PHE 87  312 312 PHE PHE B . n 
B 1 88  ASN 88  313 313 ASN ASN B . n 
B 1 89  PRO 89  314 314 PRO PRO B . n 
B 1 90  LEU 90  315 315 LEU LEU B . n 
B 1 91  SER 91  316 316 SER SER B . n 
B 1 92  GLY 92  317 317 GLY GLY B . n 
B 1 93  ALA 93  318 318 ALA ALA B . n 
B 1 94  PRO 94  319 319 PRO PRO B . n 
B 1 95  ALA 95  320 320 ALA ALA B . n 
B 1 96  PRO 96  321 321 PRO PRO B . n 
B 1 97  GLU 97  322 322 GLU GLU B . n 
B 1 98  GLY 98  323 323 GLY GLY B . n 
B 1 99  PHE 99  324 324 PHE PHE B . n 
B 1 100 PRO 100 325 325 PRO PRO B . n 
B 1 101 ASP 101 326 326 ASP ASP B . n 
B 1 102 PHE 102 327 327 PHE PHE B . n 
B 1 103 THR 103 328 328 THR THR B . n 
B 1 104 ALA 104 329 329 ALA ALA B . n 
B 1 105 GLN 105 330 330 GLN GLN B . n 
B 1 106 GLU 106 331 331 GLU GLU B . n 
B 1 107 TYR 107 332 332 TYR TYR B . n 
B 1 108 HIS 108 333 333 HIS HIS B . n 
B 1 109 LEU 109 334 334 LEU LEU B . n 
B 1 110 ARG 110 335 335 ARG ARG B . n 
B 1 111 ALA 111 336 336 ALA ALA B . n 
B 1 112 ALA 112 337 337 ALA ALA B . n 
B 1 113 GLY 113 338 338 GLY GLY B . n 
B 1 114 LYS 114 339 339 LYS LYS B . n 
B 1 115 VAL 115 340 340 VAL VAL B . n 
B 1 116 ALA 116 341 341 ALA ALA B . n 
B 1 117 ASN 117 342 342 ASN ASN B . n 
B 1 118 THR 118 343 343 THR THR B . n 
B 1 119 THR 119 344 344 THR THR B . n 
B 1 120 GLY 120 345 345 GLY GLY B . n 
B 1 121 GLY 121 346 346 GLY GLY B . n 
B 1 122 GLY 122 347 347 GLY GLY B . n 
B 1 123 GLU 123 348 348 GLU GLU B . n 
B 1 124 ILE 124 349 349 ILE ILE B . n 
B 1 125 LYS 125 350 350 LYS LYS B . n 
B 1 126 SER 126 351 351 SER SER B . n 
B 1 127 THR 127 352 352 THR THR B . n 
B 1 128 ASP 128 353 353 ASP ASP B . n 
B 1 129 TYR 129 354 354 TYR TYR B . n 
B 1 130 THR 130 355 355 THR THR B . n 
B 1 131 PRO 131 356 356 PRO PRO B . n 
B 1 132 ALA 132 357 357 ALA ALA B . n 
B 1 133 LEU 133 358 358 LEU LEU B . n 
B 1 134 GLY 134 359 359 GLY GLY B . n 
B 1 135 GLY 135 360 360 GLY GLY B . n 
B 1 136 VAL 136 361 361 VAL VAL B . n 
B 1 137 LYS 137 362 362 LYS LYS B . n 
B 1 138 ILE 138 363 363 ILE ILE B . n 
B 1 139 THR 139 364 364 THR THR B . n 
B 1 140 ALA 140 365 365 ALA ALA B . n 
B 1 141 TRP 141 366 366 TRP TRP B . n 
B 1 142 ASP 142 367 367 ASP ASP B . n 
B 1 143 ALA 143 368 368 ALA ALA B . n 
B 1 144 THR 144 369 369 THR THR B . n 
B 1 145 GLY 145 370 370 GLY GLY B . n 
B 1 146 PRO 146 371 371 PRO PRO B . n 
B 1 147 SER 147 372 372 SER SER B . n 
B 1 148 ALA 148 373 373 ALA ALA B . n 
B 1 149 GLY 149 374 374 GLY GLY B . n 
B 1 150 VAL 150 375 375 VAL VAL B . n 
B 1 151 GLU 151 376 376 GLU GLU B . n 
B 1 152 MET 152 377 377 MET MET B . n 
B 1 153 THR 153 378 378 THR THR B . n 
B 1 154 GLY 154 379 379 GLY GLY B . n 
B 1 155 GLN 155 380 380 GLN GLN B . n 
B 1 156 ILE 156 381 381 ILE ILE B . n 
B 1 157 GLU 157 382 382 GLU GLU B . n 
B 1 158 SER 158 383 383 SER SER B . n 
B 1 159 ILE 159 384 384 ILE ILE B . n 
B 1 160 GLY 160 385 385 GLY GLY B . n 
B 1 161 MET 161 386 386 MET MET B . n 
B 1 162 GLU 162 387 387 GLU GLU B . n 
B 1 163 ASN 163 388 388 ASN ASN B . n 
B 1 164 ASN 164 389 389 ASN ASN B . n 
B 1 165 THR 165 390 390 THR THR B . n 
B 1 166 ASP 166 391 391 ASP ASP B . n 
B 1 167 PHE 167 392 392 PHE PHE B . n 
B 1 168 ASP 168 393 393 ASP ASP B . n 
B 1 169 VAL 169 394 394 VAL VAL B . n 
B 1 170 LEU 170 395 395 LEU LEU B . n 
B 1 171 PRO 171 396 396 PRO PRO B . n 
B 1 172 ASP 172 397 397 ASP ASP B . n 
B 1 173 TYR 173 398 398 TYR TYR B . n 
B 1 174 ASN 174 399 399 ASN ASN B . n 
B 1 175 GLY 175 400 400 GLY GLY B . n 
B 1 176 SER 176 401 401 SER SER B . n 
B 1 177 ALA 177 402 402 ALA ALA B . n 
B 1 178 PHE 178 403 403 PHE PHE B . n 
B 1 179 ASP 179 404 404 ASP ASP B . n 
B 1 180 GLY 180 405 405 GLY GLY B . n 
B 1 181 SER 181 406 406 SER SER B . n 
B 1 182 LEU 182 407 407 LEU LEU B . n 
B 1 183 ASN 183 408 408 ASN ASN B . n 
B 1 184 LEU 184 409 409 LEU LEU B . n 
B 1 185 ALA 185 410 410 ALA ALA B . n 
B 1 186 PRO 186 411 411 PRO PRO B . n 
B 1 187 PRO 187 412 412 PRO PRO B . n 
B 1 188 ILE 188 413 413 ILE ILE B . n 
B 1 189 VAL 189 414 414 VAL VAL B . n 
B 1 190 PRO 190 415 415 PRO PRO B . n 
B 1 191 LEU 191 416 416 LEU LEU B . n 
B 1 192 LEU 192 417 417 LEU LEU B . n 
B 1 193 PRO 193 418 418 PRO PRO B . n 
B 1 194 GLY 194 419 419 GLY GLY B . n 
B 1 195 GLU 195 420 420 GLU GLU B . n 
B 1 196 THR 196 421 421 THR THR B . n 
B 1 197 LEU 197 422 422 LEU LEU B . n 
B 1 198 LEU 198 423 423 LEU LEU B . n 
B 1 199 ARG 199 424 424 ARG ARG B . n 
B 1 200 PHE 200 425 425 PHE PHE B . n 
B 1 201 GLY 201 426 426 GLY GLY B . n 
B 1 202 THR 202 427 427 THR THR B . n 
B 1 203 VAL 203 428 428 VAL VAL B . n 
B 1 204 PRO 204 429 429 PRO PRO B . n 
B 1 205 ILE 205 430 430 ILE ILE B . n 
B 1 206 THR 206 431 431 THR THR B . n 
B 1 207 THR 207 432 432 THR THR B . n 
B 1 208 ARG 208 433 433 ARG ARG B . n 
B 1 209 ARG 209 434 434 ARG ARG B . n 
B 1 210 GLN 210 435 435 GLN GLN B . n 
B 1 211 SER 211 436 436 SER SER B . n 
B 1 212 ASP 212 437 437 ASP ASP B . n 
B 1 213 PRO 213 438 438 PRO PRO B . n 
B 1 214 ILE 214 439 439 ILE ILE B . n 
B 1 215 ARG 215 440 440 ARG ARG B . n 
B 1 216 ILE 216 441 441 ILE ILE B . n 
B 1 217 ILE 217 442 442 ILE ILE B . n 
B 1 218 SER 218 443 443 SER SER B . n 
B 1 219 CYS 219 444 444 CYS CYS B . n 
B 1 220 ALA 220 445 445 ALA ALA B . n 
B 1 221 LEU 221 446 446 LEU LEU B . n 
B 1 222 PRO 222 447 447 PRO PRO B . n 
B 1 223 GLN 223 448 448 GLN GLN B . n 
B 1 224 GLU 224 449 449 GLU GLU B . n 
B 1 225 TRP 225 450 450 TRP TRP B . n 
B 1 226 ILE 226 451 451 ILE ILE B . n 
B 1 227 THR 227 452 452 THR THR B . n 
B 1 228 TRP 228 453 453 TRP TRP B . n 
B 1 229 PHE 229 454 454 PHE PHE B . n 
B 1 230 LEU 230 455 455 LEU LEU B . n 
B 1 231 THR 231 456 456 THR THR B . n 
B 1 232 HIS 232 457 457 HIS HIS B . n 
B 1 233 ASN 233 458 458 ASN ASN B . n 
B 1 234 PHE 234 459 459 PHE PHE B . n 
B 1 235 THR 235 460 460 THR THR B . n 
B 1 236 ALA 236 461 461 ALA ALA B . n 
B 1 237 LEU 237 462 462 LEU LEU B . n 
B 1 238 GLY 238 463 463 GLY GLY B . n 
B 1 239 ASP 239 464 464 ASP ASP B . n 
B 1 240 ALA 240 465 465 ALA ALA B . n 
B 1 241 ALA 241 466 466 ALA ALA B . n 
B 1 242 LEU 242 467 467 LEU LEU B . n 
B 1 243 LEU 243 468 468 LEU LEU B . n 
B 1 244 ARG 244 469 469 ARG ARG B . n 
B 1 245 TYR 245 470 470 TYR TYR B . n 
B 1 246 ARG 246 471 471 ARG ARG B . n 
B 1 247 ASN 247 472 472 ASN ASN B . n 
B 1 248 GLN 248 473 473 GLN GLN B . n 
B 1 249 ALA 249 474 474 ALA ALA B . n 
B 1 250 THR 250 475 475 THR THR B . n 
B 1 251 GLY 251 476 476 GLY GLY B . n 
B 1 252 GLN 252 477 477 GLN GLN B . n 
B 1 253 LEU 253 478 478 LEU LEU B . n 
B 1 254 LEU 254 479 479 LEU LEU B . n 
B 1 255 PHE 255 480 480 PHE PHE B . n 
B 1 256 GLU 256 481 481 GLU GLU B . n 
B 1 257 CYS 257 482 482 CYS CYS B . n 
B 1 258 LYS 258 483 483 LYS LYS B . n 
B 1 259 LEU 259 484 484 LEU LEU B . n 
B 1 260 TYR 260 485 485 TYR TYR B . n 
B 1 261 ARG 261 486 486 ARG ARG B . n 
B 1 262 SER 262 487 487 SER SER B . n 
B 1 263 GLY 263 488 488 GLY GLY B . n 
B 1 264 PHE 264 489 489 PHE PHE B . n 
B 1 265 VAL 265 490 490 VAL VAL B . n 
B 1 266 VAL 266 491 491 VAL VAL B . n 
B 1 267 VAL 267 492 492 VAL VAL B . n 
B 1 268 ASN 268 493 493 ASN ASN B . n 
B 1 269 GLY 269 494 494 GLY GLY B . n 
B 1 270 VAL 270 495 495 VAL VAL B . n 
B 1 271 ASN 271 496 496 ASN ASN B . n 
B 1 272 VAL 272 497 497 VAL VAL B . n 
B 1 273 ARG 273 498 498 ARG ARG B . n 
B 1 274 THR 274 499 499 THR THR B . n 
B 1 275 GLU 275 500 500 GLU GLU B . n 
B 1 276 PHE 276 501 501 PHE PHE B . n 
B 1 277 PRO 277 502 502 PRO PRO B . n 
B 1 278 MET 278 503 503 MET MET B . n 
B 1 279 SER 279 504 504 SER SER B . n 
B 1 280 GLY 280 505 505 GLY GLY B . n 
B 1 281 VAL 281 506 506 VAL VAL B . n 
B 1 282 PHE 282 507 507 PHE PHE B . n 
B 1 283 GLU 283 508 508 GLU GLU B . n 
B 1 284 PHE 284 509 509 PHE PHE B . n 
B 1 285 VAL 285 510 510 VAL VAL B . n 
B 1 286 SER 286 511 511 SER SER B . n 
B 1 287 TRP 287 512 512 TRP TRP B . n 
B 1 288 VAL 288 513 513 VAL VAL B . n 
B 1 289 PRO 289 514 514 PRO PRO B . n 
B 1 290 ASN 290 515 515 ASN ASN B . n 
B 1 291 PHE 291 516 516 PHE PHE B . n 
B 1 292 PHE 292 517 517 PHE PHE B . n 
B 1 293 GLN 293 518 518 GLN GLN B . n 
B 1 294 LEU 294 519 519 LEU LEU B . n 
B 1 295 ALA 295 520 520 ALA ALA B . n 
B 1 296 PRO 296 521 521 PRO PRO B . n 
B 1 297 VAL 297 522 522 VAL VAL B . n 
# 
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 SO4 1   601  1   SO4 SO4 A . 
D 2 SO4 1   602  3   SO4 SO4 A . 
E 2 SO4 1   601  2   SO4 SO4 B . 
F 2 SO4 1   602  4   SO4 SO4 B . 
G 3 HOH 1   701  678 HOH HOH A . 
G 3 HOH 2   702  200 HOH HOH A . 
G 3 HOH 3   703  812 HOH HOH A . 
G 3 HOH 4   704  373 HOH HOH A . 
G 3 HOH 5   705  51  HOH HOH A . 
G 3 HOH 6   706  430 HOH HOH A . 
G 3 HOH 7   707  790 HOH HOH A . 
G 3 HOH 8   708  661 HOH HOH A . 
G 3 HOH 9   709  475 HOH HOH A . 
G 3 HOH 10  710  228 HOH HOH A . 
G 3 HOH 11  711  850 HOH HOH A . 
G 3 HOH 12  712  800 HOH HOH A . 
G 3 HOH 13  713  802 HOH HOH A . 
G 3 HOH 14  714  178 HOH HOH A . 
G 3 HOH 15  715  290 HOH HOH A . 
G 3 HOH 16  716  367 HOH HOH A . 
G 3 HOH 17  717  411 HOH HOH A . 
G 3 HOH 18  718  603 HOH HOH A . 
G 3 HOH 19  719  608 HOH HOH A . 
G 3 HOH 20  720  552 HOH HOH A . 
G 3 HOH 21  721  195 HOH HOH A . 
G 3 HOH 22  722  466 HOH HOH A . 
G 3 HOH 23  723  640 HOH HOH A . 
G 3 HOH 24  724  299 HOH HOH A . 
G 3 HOH 25  725  423 HOH HOH A . 
G 3 HOH 26  726  932 HOH HOH A . 
G 3 HOH 27  727  435 HOH HOH A . 
G 3 HOH 28  728  288 HOH HOH A . 
G 3 HOH 29  729  495 HOH HOH A . 
G 3 HOH 30  730  101 HOH HOH A . 
G 3 HOH 31  731  98  HOH HOH A . 
G 3 HOH 32  732  123 HOH HOH A . 
G 3 HOH 33  733  160 HOH HOH A . 
G 3 HOH 34  734  233 HOH HOH A . 
G 3 HOH 35  735  560 HOH HOH A . 
G 3 HOH 36  736  833 HOH HOH A . 
G 3 HOH 37  737  838 HOH HOH A . 
G 3 HOH 38  738  499 HOH HOH A . 
G 3 HOH 39  739  313 HOH HOH A . 
G 3 HOH 40  740  53  HOH HOH A . 
G 3 HOH 41  741  197 HOH HOH A . 
G 3 HOH 42  742  854 HOH HOH A . 
G 3 HOH 43  743  234 HOH HOH A . 
G 3 HOH 44  744  75  HOH HOH A . 
G 3 HOH 45  745  318 HOH HOH A . 
G 3 HOH 46  746  330 HOH HOH A . 
G 3 HOH 47  747  251 HOH HOH A . 
G 3 HOH 48  748  573 HOH HOH A . 
G 3 HOH 49  749  49  HOH HOH A . 
G 3 HOH 50  750  130 HOH HOH A . 
G 3 HOH 51  751  339 HOH HOH A . 
G 3 HOH 52  752  81  HOH HOH A . 
G 3 HOH 53  753  29  HOH HOH A . 
G 3 HOH 54  754  431 HOH HOH A . 
G 3 HOH 55  755  86  HOH HOH A . 
G 3 HOH 56  756  32  HOH HOH A . 
G 3 HOH 57  757  26  HOH HOH A . 
G 3 HOH 58  758  422 HOH HOH A . 
G 3 HOH 59  759  623 HOH HOH A . 
G 3 HOH 60  760  21  HOH HOH A . 
G 3 HOH 61  761  658 HOH HOH A . 
G 3 HOH 62  762  568 HOH HOH A . 
G 3 HOH 63  763  140 HOH HOH A . 
G 3 HOH 64  764  637 HOH HOH A . 
G 3 HOH 65  765  410 HOH HOH A . 
G 3 HOH 66  766  453 HOH HOH A . 
G 3 HOH 67  767  390 HOH HOH A . 
G 3 HOH 68  768  436 HOH HOH A . 
G 3 HOH 69  769  597 HOH HOH A . 
G 3 HOH 70  770  443 HOH HOH A . 
G 3 HOH 71  771  105 HOH HOH A . 
G 3 HOH 72  772  515 HOH HOH A . 
G 3 HOH 73  773  633 HOH HOH A . 
G 3 HOH 74  774  115 HOH HOH A . 
G 3 HOH 75  775  15  HOH HOH A . 
G 3 HOH 76  776  97  HOH HOH A . 
G 3 HOH 77  777  52  HOH HOH A . 
G 3 HOH 78  778  113 HOH HOH A . 
G 3 HOH 79  779  84  HOH HOH A . 
G 3 HOH 80  780  719 HOH HOH A . 
G 3 HOH 81  781  168 HOH HOH A . 
G 3 HOH 82  782  469 HOH HOH A . 
G 3 HOH 83  783  229 HOH HOH A . 
G 3 HOH 84  784  761 HOH HOH A . 
G 3 HOH 85  785  85  HOH HOH A . 
G 3 HOH 86  786  328 HOH HOH A . 
G 3 HOH 87  787  370 HOH HOH A . 
G 3 HOH 88  788  567 HOH HOH A . 
G 3 HOH 89  789  420 HOH HOH A . 
G 3 HOH 90  790  71  HOH HOH A . 
G 3 HOH 91  791  576 HOH HOH A . 
G 3 HOH 92  792  136 HOH HOH A . 
G 3 HOH 93  793  175 HOH HOH A . 
G 3 HOH 94  794  510 HOH HOH A . 
G 3 HOH 95  795  22  HOH HOH A . 
G 3 HOH 96  796  904 HOH HOH A . 
G 3 HOH 97  797  521 HOH HOH A . 
G 3 HOH 98  798  117 HOH HOH A . 
G 3 HOH 99  799  275 HOH HOH A . 
G 3 HOH 100 800  76  HOH HOH A . 
G 3 HOH 101 801  245 HOH HOH A . 
G 3 HOH 102 802  445 HOH HOH A . 
G 3 HOH 103 803  118 HOH HOH A . 
G 3 HOH 104 804  575 HOH HOH A . 
G 3 HOH 105 805  268 HOH HOH A . 
G 3 HOH 106 806  504 HOH HOH A . 
G 3 HOH 107 807  108 HOH HOH A . 
G 3 HOH 108 808  291 HOH HOH A . 
G 3 HOH 109 809  12  HOH HOH A . 
G 3 HOH 110 810  37  HOH HOH A . 
G 3 HOH 111 811  432 HOH HOH A . 
G 3 HOH 112 812  227 HOH HOH A . 
G 3 HOH 113 813  378 HOH HOH A . 
G 3 HOH 114 814  28  HOH HOH A . 
G 3 HOH 115 815  259 HOH HOH A . 
G 3 HOH 116 816  87  HOH HOH A . 
G 3 HOH 117 817  17  HOH HOH A . 
G 3 HOH 118 818  722 HOH HOH A . 
G 3 HOH 119 819  239 HOH HOH A . 
G 3 HOH 120 820  580 HOH HOH A . 
G 3 HOH 121 821  222 HOH HOH A . 
G 3 HOH 122 822  157 HOH HOH A . 
G 3 HOH 123 823  50  HOH HOH A . 
G 3 HOH 124 824  67  HOH HOH A . 
G 3 HOH 125 825  527 HOH HOH A . 
G 3 HOH 126 826  237 HOH HOH A . 
G 3 HOH 127 827  66  HOH HOH A . 
G 3 HOH 128 828  376 HOH HOH A . 
G 3 HOH 129 829  7   HOH HOH A . 
G 3 HOH 130 830  356 HOH HOH A . 
G 3 HOH 131 831  264 HOH HOH A . 
G 3 HOH 132 832  216 HOH HOH A . 
G 3 HOH 133 833  636 HOH HOH A . 
G 3 HOH 134 834  185 HOH HOH A . 
G 3 HOH 135 835  340 HOH HOH A . 
G 3 HOH 136 836  13  HOH HOH A . 
G 3 HOH 137 837  301 HOH HOH A . 
G 3 HOH 138 838  44  HOH HOH A . 
G 3 HOH 139 839  30  HOH HOH A . 
G 3 HOH 140 840  5   HOH HOH A . 
G 3 HOH 141 841  624 HOH HOH A . 
G 3 HOH 142 842  276 HOH HOH A . 
G 3 HOH 143 843  440 HOH HOH A . 
G 3 HOH 144 844  302 HOH HOH A . 
G 3 HOH 145 845  599 HOH HOH A . 
G 3 HOH 146 846  374 HOH HOH A . 
G 3 HOH 147 847  380 HOH HOH A . 
G 3 HOH 148 848  148 HOH HOH A . 
G 3 HOH 149 849  231 HOH HOH A . 
G 3 HOH 150 850  710 HOH HOH A . 
G 3 HOH 151 851  372 HOH HOH A . 
G 3 HOH 152 852  36  HOH HOH A . 
G 3 HOH 153 853  63  HOH HOH A . 
G 3 HOH 154 854  54  HOH HOH A . 
G 3 HOH 155 855  57  HOH HOH A . 
G 3 HOH 156 856  321 HOH HOH A . 
G 3 HOH 157 857  20  HOH HOH A . 
G 3 HOH 158 858  558 HOH HOH A . 
G 3 HOH 159 859  365 HOH HOH A . 
G 3 HOH 160 860  186 HOH HOH A . 
G 3 HOH 161 861  4   HOH HOH A . 
G 3 HOH 162 862  129 HOH HOH A . 
G 3 HOH 163 863  111 HOH HOH A . 
G 3 HOH 164 864  708 HOH HOH A . 
G 3 HOH 165 865  655 HOH HOH A . 
G 3 HOH 166 866  355 HOH HOH A . 
G 3 HOH 167 867  96  HOH HOH A . 
G 3 HOH 168 868  351 HOH HOH A . 
G 3 HOH 169 869  133 HOH HOH A . 
G 3 HOH 170 870  82  HOH HOH A . 
G 3 HOH 171 871  666 HOH HOH A . 
G 3 HOH 172 872  56  HOH HOH A . 
G 3 HOH 173 873  817 HOH HOH A . 
G 3 HOH 174 874  821 HOH HOH A . 
G 3 HOH 175 875  256 HOH HOH A . 
G 3 HOH 176 876  782 HOH HOH A . 
G 3 HOH 177 877  138 HOH HOH A . 
G 3 HOH 178 878  83  HOH HOH A . 
G 3 HOH 179 879  856 HOH HOH A . 
G 3 HOH 180 880  319 HOH HOH A . 
G 3 HOH 181 881  65  HOH HOH A . 
G 3 HOH 182 882  347 HOH HOH A . 
G 3 HOH 183 883  400 HOH HOH A . 
G 3 HOH 184 884  219 HOH HOH A . 
G 3 HOH 185 885  765 HOH HOH A . 
G 3 HOH 186 886  88  HOH HOH A . 
G 3 HOH 187 887  224 HOH HOH A . 
G 3 HOH 188 888  847 HOH HOH A . 
G 3 HOH 189 889  502 HOH HOH A . 
G 3 HOH 190 890  465 HOH HOH A . 
G 3 HOH 191 891  269 HOH HOH A . 
G 3 HOH 192 892  530 HOH HOH A . 
G 3 HOH 193 893  342 HOH HOH A . 
G 3 HOH 194 894  206 HOH HOH A . 
G 3 HOH 195 895  116 HOH HOH A . 
G 3 HOH 196 896  480 HOH HOH A . 
G 3 HOH 197 897  213 HOH HOH A . 
G 3 HOH 198 898  150 HOH HOH A . 
G 3 HOH 199 899  45  HOH HOH A . 
G 3 HOH 200 900  218 HOH HOH A . 
G 3 HOH 201 901  329 HOH HOH A . 
G 3 HOH 202 902  728 HOH HOH A . 
G 3 HOH 203 903  359 HOH HOH A . 
G 3 HOH 204 904  663 HOH HOH A . 
G 3 HOH 205 905  255 HOH HOH A . 
G 3 HOH 206 906  212 HOH HOH A . 
G 3 HOH 207 907  512 HOH HOH A . 
G 3 HOH 208 908  194 HOH HOH A . 
G 3 HOH 209 909  103 HOH HOH A . 
G 3 HOH 210 910  307 HOH HOH A . 
G 3 HOH 211 911  460 HOH HOH A . 
G 3 HOH 212 912  820 HOH HOH A . 
G 3 HOH 213 913  729 HOH HOH A . 
G 3 HOH 214 914  801 HOH HOH A . 
G 3 HOH 215 915  210 HOH HOH A . 
G 3 HOH 216 916  165 HOH HOH A . 
G 3 HOH 217 917  364 HOH HOH A . 
G 3 HOH 218 918  709 HOH HOH A . 
G 3 HOH 219 919  642 HOH HOH A . 
G 3 HOH 220 920  94  HOH HOH A . 
G 3 HOH 221 921  73  HOH HOH A . 
G 3 HOH 222 922  126 HOH HOH A . 
G 3 HOH 223 923  221 HOH HOH A . 
G 3 HOH 224 924  482 HOH HOH A . 
G 3 HOH 225 925  304 HOH HOH A . 
G 3 HOH 226 926  695 HOH HOH A . 
G 3 HOH 227 927  508 HOH HOH A . 
G 3 HOH 228 928  747 HOH HOH A . 
G 3 HOH 229 929  294 HOH HOH A . 
G 3 HOH 230 930  262 HOH HOH A . 
G 3 HOH 231 931  736 HOH HOH A . 
G 3 HOH 232 932  402 HOH HOH A . 
G 3 HOH 233 933  371 HOH HOH A . 
G 3 HOH 234 934  40  HOH HOH A . 
G 3 HOH 235 935  794 HOH HOH A . 
G 3 HOH 236 936  773 HOH HOH A . 
G 3 HOH 237 937  187 HOH HOH A . 
G 3 HOH 238 938  638 HOH HOH A . 
G 3 HOH 239 939  688 HOH HOH A . 
G 3 HOH 240 940  724 HOH HOH A . 
G 3 HOH 241 941  164 HOH HOH A . 
G 3 HOH 242 942  295 HOH HOH A . 
G 3 HOH 243 943  501 HOH HOH A . 
G 3 HOH 244 944  639 HOH HOH A . 
G 3 HOH 245 945  407 HOH HOH A . 
G 3 HOH 246 946  672 HOH HOH A . 
G 3 HOH 247 947  181 HOH HOH A . 
G 3 HOH 248 948  929 HOH HOH A . 
G 3 HOH 249 949  861 HOH HOH A . 
G 3 HOH 250 950  298 HOH HOH A . 
G 3 HOH 251 951  871 HOH HOH A . 
G 3 HOH 252 952  232 HOH HOH A . 
G 3 HOH 253 953  191 HOH HOH A . 
G 3 HOH 254 954  826 HOH HOH A . 
G 3 HOH 255 955  878 HOH HOH A . 
G 3 HOH 256 956  417 HOH HOH A . 
G 3 HOH 257 957  252 HOH HOH A . 
G 3 HOH 258 958  585 HOH HOH A . 
G 3 HOH 259 959  386 HOH HOH A . 
G 3 HOH 260 960  161 HOH HOH A . 
G 3 HOH 261 961  79  HOH HOH A . 
G 3 HOH 262 962  586 HOH HOH A . 
G 3 HOH 263 963  617 HOH HOH A . 
G 3 HOH 264 964  860 HOH HOH A . 
G 3 HOH 265 965  912 HOH HOH A . 
G 3 HOH 266 966  615 HOH HOH A . 
G 3 HOH 267 967  645 HOH HOH A . 
G 3 HOH 268 968  183 HOH HOH A . 
G 3 HOH 269 969  459 HOH HOH A . 
G 3 HOH 270 970  429 HOH HOH A . 
G 3 HOH 271 971  855 HOH HOH A . 
G 3 HOH 272 972  785 HOH HOH A . 
G 3 HOH 273 973  705 HOH HOH A . 
G 3 HOH 274 974  769 HOH HOH A . 
G 3 HOH 275 975  754 HOH HOH A . 
G 3 HOH 276 976  884 HOH HOH A . 
G 3 HOH 277 977  866 HOH HOH A . 
G 3 HOH 278 978  543 HOH HOH A . 
G 3 HOH 279 979  717 HOH HOH A . 
G 3 HOH 280 980  751 HOH HOH A . 
G 3 HOH 281 981  632 HOH HOH A . 
G 3 HOH 282 982  565 HOH HOH A . 
G 3 HOH 283 983  591 HOH HOH A . 
G 3 HOH 284 984  449 HOH HOH A . 
G 3 HOH 285 985  845 HOH HOH A . 
G 3 HOH 286 986  616 HOH HOH A . 
G 3 HOH 287 987  483 HOH HOH A . 
G 3 HOH 288 988  744 HOH HOH A . 
G 3 HOH 289 989  907 HOH HOH A . 
G 3 HOH 290 990  561 HOH HOH A . 
G 3 HOH 291 991  611 HOH HOH A . 
G 3 HOH 292 992  781 HOH HOH A . 
G 3 HOH 293 993  601 HOH HOH A . 
G 3 HOH 294 994  190 HOH HOH A . 
G 3 HOH 295 995  734 HOH HOH A . 
G 3 HOH 296 996  776 HOH HOH A . 
G 3 HOH 297 997  831 HOH HOH A . 
G 3 HOH 298 998  270 HOH HOH A . 
G 3 HOH 299 999  621 HOH HOH A . 
G 3 HOH 300 1000 819 HOH HOH A . 
G 3 HOH 301 1001 441 HOH HOH A . 
G 3 HOH 302 1002 803 HOH HOH A . 
G 3 HOH 303 1003 456 HOH HOH A . 
G 3 HOH 304 1004 835 HOH HOH A . 
G 3 HOH 305 1005 424 HOH HOH A . 
G 3 HOH 306 1006 917 HOH HOH A . 
G 3 HOH 307 1007 203 HOH HOH A . 
G 3 HOH 308 1008 706 HOH HOH A . 
G 3 HOH 309 1009 698 HOH HOH A . 
G 3 HOH 310 1010 726 HOH HOH A . 
G 3 HOH 311 1011 902 HOH HOH A . 
G 3 HOH 312 1012 476 HOH HOH A . 
G 3 HOH 313 1013 815 HOH HOH A . 
G 3 HOH 314 1014 764 HOH HOH A . 
G 3 HOH 315 1015 913 HOH HOH A . 
G 3 HOH 316 1016 746 HOH HOH A . 
G 3 HOH 317 1017 566 HOH HOH A . 
G 3 HOH 318 1018 647 HOH HOH A . 
G 3 HOH 319 1019 667 HOH HOH A . 
G 3 HOH 320 1020 474 HOH HOH A . 
G 3 HOH 321 1021 925 HOH HOH A . 
G 3 HOH 322 1022 771 HOH HOH A . 
G 3 HOH 323 1023 538 HOH HOH A . 
G 3 HOH 324 1024 918 HOH HOH A . 
G 3 HOH 325 1025 198 HOH HOH A . 
G 3 HOH 326 1026 755 HOH HOH A . 
G 3 HOH 327 1027 906 HOH HOH A . 
G 3 HOH 328 1028 911 HOH HOH A . 
G 3 HOH 329 1029 836 HOH HOH A . 
G 3 HOH 330 1030 634 HOH HOH A . 
G 3 HOH 331 1031 158 HOH HOH A . 
G 3 HOH 332 1032 915 HOH HOH A . 
G 3 HOH 333 1033 426 HOH HOH A . 
G 3 HOH 334 1034 752 HOH HOH A . 
G 3 HOH 335 1035 553 HOH HOH A . 
G 3 HOH 336 1036 312 HOH HOH A . 
G 3 HOH 337 1037 683 HOH HOH A . 
G 3 HOH 338 1038 759 HOH HOH A . 
G 3 HOH 339 1039 681 HOH HOH A . 
G 3 HOH 340 1040 572 HOH HOH A . 
G 3 HOH 341 1041 903 HOH HOH A . 
G 3 HOH 342 1042 563 HOH HOH A . 
G 3 HOH 343 1043 718 HOH HOH A . 
G 3 HOH 344 1044 657 HOH HOH A . 
G 3 HOH 345 1045 798 HOH HOH A . 
G 3 HOH 346 1046 922 HOH HOH A . 
G 3 HOH 347 1047 676 HOH HOH A . 
G 3 HOH 348 1048 331 HOH HOH A . 
G 3 HOH 349 1049 841 HOH HOH A . 
G 3 HOH 350 1050 690 HOH HOH A . 
G 3 HOH 351 1051 758 HOH HOH A . 
G 3 HOH 352 1052 778 HOH HOH A . 
G 3 HOH 353 1053 425 HOH HOH A . 
G 3 HOH 354 1054 451 HOH HOH A . 
G 3 HOH 355 1055 522 HOH HOH A . 
G 3 HOH 356 1056 651 HOH HOH A . 
G 3 HOH 357 1057 694 HOH HOH A . 
G 3 HOH 358 1058 354 HOH HOH A . 
G 3 HOH 359 1059 592 HOH HOH A . 
G 3 HOH 360 1060 293 HOH HOH A . 
G 3 HOH 361 1061 248 HOH HOH A . 
G 3 HOH 362 1062 128 HOH HOH A . 
G 3 HOH 363 1063 524 HOH HOH A . 
G 3 HOH 364 1064 405 HOH HOH A . 
G 3 HOH 365 1065 686 HOH HOH A . 
G 3 HOH 366 1066 334 HOH HOH A . 
G 3 HOH 367 1067 652 HOH HOH A . 
G 3 HOH 368 1068 760 HOH HOH A . 
G 3 HOH 369 1069 541 HOH HOH A . 
G 3 HOH 370 1070 324 HOH HOH A . 
G 3 HOH 371 1071 600 HOH HOH A . 
G 3 HOH 372 1072 421 HOH HOH A . 
G 3 HOH 373 1073 872 HOH HOH A . 
G 3 HOH 374 1074 881 HOH HOH A . 
G 3 HOH 375 1075 489 HOH HOH A . 
G 3 HOH 376 1076 531 HOH HOH A . 
G 3 HOH 377 1077 892 HOH HOH A . 
G 3 HOH 378 1078 408 HOH HOH A . 
G 3 HOH 379 1079 682 HOH HOH A . 
G 3 HOH 380 1080 788 HOH HOH A . 
G 3 HOH 381 1081 908 HOH HOH A . 
G 3 HOH 382 1082 852 HOH HOH A . 
G 3 HOH 383 1083 473 HOH HOH A . 
G 3 HOH 384 1084 863 HOH HOH A . 
G 3 HOH 385 1085 840 HOH HOH A . 
G 3 HOH 386 1086 828 HOH HOH A . 
G 3 HOH 387 1087 578 HOH HOH A . 
G 3 HOH 388 1088 607 HOH HOH A . 
G 3 HOH 389 1089 184 HOH HOH A . 
G 3 HOH 390 1090 626 HOH HOH A . 
G 3 HOH 391 1091 547 HOH HOH A . 
G 3 HOH 392 1092 711 HOH HOH A . 
G 3 HOH 393 1093 296 HOH HOH A . 
G 3 HOH 394 1094 145 HOH HOH A . 
G 3 HOH 395 1095 910 HOH HOH A . 
G 3 HOH 396 1096 450 HOH HOH A . 
G 3 HOH 397 1097 757 HOH HOH A . 
G 3 HOH 398 1098 409 HOH HOH A . 
G 3 HOH 399 1099 927 HOH HOH A . 
G 3 HOH 400 1100 679 HOH HOH A . 
G 3 HOH 401 1101 654 HOH HOH A . 
G 3 HOH 402 1102 772 HOH HOH A . 
G 3 HOH 403 1103 791 HOH HOH A . 
G 3 HOH 404 1104 673 HOH HOH A . 
G 3 HOH 405 1105 447 HOH HOH A . 
G 3 HOH 406 1106 931 HOH HOH A . 
G 3 HOH 407 1107 767 HOH HOH A . 
G 3 HOH 408 1108 877 HOH HOH A . 
G 3 HOH 409 1109 891 HOH HOH A . 
G 3 HOH 410 1110 921 HOH HOH A . 
G 3 HOH 411 1111 653 HOH HOH A . 
G 3 HOH 412 1112 265 HOH HOH A . 
G 3 HOH 413 1113 865 HOH HOH A . 
G 3 HOH 414 1114 914 HOH HOH A . 
G 3 HOH 415 1115 674 HOH HOH A . 
G 3 HOH 416 1116 687 HOH HOH A . 
G 3 HOH 417 1117 797 HOH HOH A . 
G 3 HOH 418 1118 875 HOH HOH A . 
G 3 HOH 419 1119 243 HOH HOH A . 
G 3 HOH 420 1120 829 HOH HOH A . 
G 3 HOH 421 1121 919 HOH HOH A . 
G 3 HOH 422 1122 692 HOH HOH A . 
G 3 HOH 423 1123 896 HOH HOH A . 
G 3 HOH 424 1124 179 HOH HOH A . 
G 3 HOH 425 1125 920 HOH HOH A . 
G 3 HOH 426 1126 887 HOH HOH A . 
G 3 HOH 427 1127 888 HOH HOH A . 
G 3 HOH 428 1128 749 HOH HOH A . 
G 3 HOH 429 1129 876 HOH HOH A . 
G 3 HOH 430 1130 665 HOH HOH A . 
H 3 HOH 1   701  193 HOH HOH B . 
H 3 HOH 2   702  266 HOH HOH B . 
H 3 HOH 3   703  810 HOH HOH B . 
H 3 HOH 4   704  280 HOH HOH B . 
H 3 HOH 5   705  641 HOH HOH B . 
H 3 HOH 6   706  300 HOH HOH B . 
H 3 HOH 7   707  434 HOH HOH B . 
H 3 HOH 8   708  799 HOH HOH B . 
H 3 HOH 9   709  756 HOH HOH B . 
H 3 HOH 10  710  806 HOH HOH B . 
H 3 HOH 11  711  91  HOH HOH B . 
H 3 HOH 12  712  895 HOH HOH B . 
H 3 HOH 13  713  816 HOH HOH B . 
H 3 HOH 14  714  874 HOH HOH B . 
H 3 HOH 15  715  389 HOH HOH B . 
H 3 HOH 16  716  689 HOH HOH B . 
H 3 HOH 17  717  589 HOH HOH B . 
H 3 HOH 18  718  352 HOH HOH B . 
H 3 HOH 19  719  520 HOH HOH B . 
H 3 HOH 20  720  385 HOH HOH B . 
H 3 HOH 21  721  488 HOH HOH B . 
H 3 HOH 22  722  263 HOH HOH B . 
H 3 HOH 23  723  322 HOH HOH B . 
H 3 HOH 24  724  170 HOH HOH B . 
H 3 HOH 25  725  416 HOH HOH B . 
H 3 HOH 26  726  808 HOH HOH B . 
H 3 HOH 27  727  327 HOH HOH B . 
H 3 HOH 28  728  392 HOH HOH B . 
H 3 HOH 29  729  335 HOH HOH B . 
H 3 HOH 30  730  242 HOH HOH B . 
H 3 HOH 31  731  163 HOH HOH B . 
H 3 HOH 32  732  202 HOH HOH B . 
H 3 HOH 33  733  267 HOH HOH B . 
H 3 HOH 34  734  458 HOH HOH B . 
H 3 HOH 35  735  395 HOH HOH B . 
H 3 HOH 36  736  214 HOH HOH B . 
H 3 HOH 37  737  362 HOH HOH B . 
H 3 HOH 38  738  375 HOH HOH B . 
H 3 HOH 39  739  427 HOH HOH B . 
H 3 HOH 40  740  464 HOH HOH B . 
H 3 HOH 41  741  492 HOH HOH B . 
H 3 HOH 42  742  470 HOH HOH B . 
H 3 HOH 43  743  39  HOH HOH B . 
H 3 HOH 44  744  738 HOH HOH B . 
H 3 HOH 45  745  696 HOH HOH B . 
H 3 HOH 46  746  506 HOH HOH B . 
H 3 HOH 47  747  394 HOH HOH B . 
H 3 HOH 48  748  155 HOH HOH B . 
H 3 HOH 49  749  61  HOH HOH B . 
H 3 HOH 50  750  238 HOH HOH B . 
H 3 HOH 51  751  779 HOH HOH B . 
H 3 HOH 52  752  99  HOH HOH B . 
H 3 HOH 53  753  16  HOH HOH B . 
H 3 HOH 54  754  38  HOH HOH B . 
H 3 HOH 55  755  680 HOH HOH B . 
H 3 HOH 56  756  143 HOH HOH B . 
H 3 HOH 57  757  125 HOH HOH B . 
H 3 HOH 58  758  201 HOH HOH B . 
H 3 HOH 59  759  156 HOH HOH B . 
H 3 HOH 60  760  9   HOH HOH B . 
H 3 HOH 61  761  177 HOH HOH B . 
H 3 HOH 62  762  46  HOH HOH B . 
H 3 HOH 63  763  162 HOH HOH B . 
H 3 HOH 64  764  77  HOH HOH B . 
H 3 HOH 65  765  261 HOH HOH B . 
H 3 HOH 66  766  455 HOH HOH B . 
H 3 HOH 67  767  209 HOH HOH B . 
H 3 HOH 68  768  595 HOH HOH B . 
H 3 HOH 69  769  146 HOH HOH B . 
H 3 HOH 70  770  832 HOH HOH B . 
H 3 HOH 71  771  742 HOH HOH B . 
H 3 HOH 72  772  827 HOH HOH B . 
H 3 HOH 73  773  851 HOH HOH B . 
H 3 HOH 74  774  444 HOH HOH B . 
H 3 HOH 75  775  247 HOH HOH B . 
H 3 HOH 76  776  2   HOH HOH B . 
H 3 HOH 77  777  297 HOH HOH B . 
H 3 HOH 78  778  60  HOH HOH B . 
H 3 HOH 79  779  310 HOH HOH B . 
H 3 HOH 80  780  323 HOH HOH B . 
H 3 HOH 81  781  671 HOH HOH B . 
H 3 HOH 82  782  618 HOH HOH B . 
H 3 HOH 83  783  31  HOH HOH B . 
H 3 HOH 84  784  732 HOH HOH B . 
H 3 HOH 85  785  338 HOH HOH B . 
H 3 HOH 86  786  192 HOH HOH B . 
H 3 HOH 87  787  254 HOH HOH B . 
H 3 HOH 88  788  249 HOH HOH B . 
H 3 HOH 89  789  223 HOH HOH B . 
H 3 HOH 90  790  109 HOH HOH B . 
H 3 HOH 91  791  89  HOH HOH B . 
H 3 HOH 92  792  43  HOH HOH B . 
H 3 HOH 93  793  35  HOH HOH B . 
H 3 HOH 94  794  792 HOH HOH B . 
H 3 HOH 95  795  644 HOH HOH B . 
H 3 HOH 96  796  144 HOH HOH B . 
H 3 HOH 97  797  121 HOH HOH B . 
H 3 HOH 98  798  142 HOH HOH B . 
H 3 HOH 99  799  139 HOH HOH B . 
H 3 HOH 100 800  11  HOH HOH B . 
H 3 HOH 101 801  398 HOH HOH B . 
H 3 HOH 102 802  64  HOH HOH B . 
H 3 HOH 103 803  18  HOH HOH B . 
H 3 HOH 104 804  587 HOH HOH B . 
H 3 HOH 105 805  58  HOH HOH B . 
H 3 HOH 106 806  509 HOH HOH B . 
H 3 HOH 107 807  205 HOH HOH B . 
H 3 HOH 108 808  897 HOH HOH B . 
H 3 HOH 109 809  124 HOH HOH B . 
H 3 HOH 110 810  68  HOH HOH B . 
H 3 HOH 111 811  933 HOH HOH B . 
H 3 HOH 112 812  41  HOH HOH B . 
H 3 HOH 113 813  3   HOH HOH B . 
H 3 HOH 114 814  42  HOH HOH B . 
H 3 HOH 115 815  507 HOH HOH B . 
H 3 HOH 116 816  19  HOH HOH B . 
H 3 HOH 117 817  278 HOH HOH B . 
H 3 HOH 118 818  27  HOH HOH B . 
H 3 HOH 119 819  93  HOH HOH B . 
H 3 HOH 120 820  25  HOH HOH B . 
H 3 HOH 121 821  24  HOH HOH B . 
H 3 HOH 122 822  873 HOH HOH B . 
H 3 HOH 123 823  14  HOH HOH B . 
H 3 HOH 124 824  320 HOH HOH B . 
H 3 HOH 125 825  106 HOH HOH B . 
H 3 HOH 126 826  631 HOH HOH B . 
H 3 HOH 127 827  289 HOH HOH B . 
H 3 HOH 128 828  381 HOH HOH B . 
H 3 HOH 129 829  159 HOH HOH B . 
H 3 HOH 130 830  292 HOH HOH B . 
H 3 HOH 131 831  285 HOH HOH B . 
H 3 HOH 132 832  171 HOH HOH B . 
H 3 HOH 133 833  377 HOH HOH B . 
H 3 HOH 134 834  337 HOH HOH B . 
H 3 HOH 135 835  345 HOH HOH B . 
H 3 HOH 136 836  107 HOH HOH B . 
H 3 HOH 137 837  199 HOH HOH B . 
H 3 HOH 138 838  10  HOH HOH B . 
H 3 HOH 139 839  244 HOH HOH B . 
H 3 HOH 140 840  554 HOH HOH B . 
H 3 HOH 141 841  457 HOH HOH B . 
H 3 HOH 142 842  220 HOH HOH B . 
H 3 HOH 143 843  236 HOH HOH B . 
H 3 HOH 144 844  6   HOH HOH B . 
H 3 HOH 145 845  535 HOH HOH B . 
H 3 HOH 146 846  314 HOH HOH B . 
H 3 HOH 147 847  368 HOH HOH B . 
H 3 HOH 148 848  735 HOH HOH B . 
H 3 HOH 149 849  152 HOH HOH B . 
H 3 HOH 150 850  613 HOH HOH B . 
H 3 HOH 151 851  241 HOH HOH B . 
H 3 HOH 152 852  485 HOH HOH B . 
H 3 HOH 153 853  169 HOH HOH B . 
H 3 HOH 154 854  382 HOH HOH B . 
H 3 HOH 155 855  95  HOH HOH B . 
H 3 HOH 156 856  114 HOH HOH B . 
H 3 HOH 157 857  8   HOH HOH B . 
H 3 HOH 158 858  481 HOH HOH B . 
H 3 HOH 159 859  78  HOH HOH B . 
H 3 HOH 160 860  793 HOH HOH B . 
H 3 HOH 161 861  467 HOH HOH B . 
H 3 HOH 162 862  104 HOH HOH B . 
H 3 HOH 163 863  154 HOH HOH B . 
H 3 HOH 164 864  120 HOH HOH B . 
H 3 HOH 165 865  1   HOH HOH B . 
H 3 HOH 166 866  74  HOH HOH B . 
H 3 HOH 167 867  258 HOH HOH B . 
H 3 HOH 168 868  537 HOH HOH B . 
H 3 HOH 169 869  208 HOH HOH B . 
H 3 HOH 170 870  72  HOH HOH B . 
H 3 HOH 171 871  306 HOH HOH B . 
H 3 HOH 172 872  725 HOH HOH B . 
H 3 HOH 173 873  132 HOH HOH B . 
H 3 HOH 174 874  69  HOH HOH B . 
H 3 HOH 175 875  533 HOH HOH B . 
H 3 HOH 176 876  23  HOH HOH B . 
H 3 HOH 177 877  166 HOH HOH B . 
H 3 HOH 178 878  406 HOH HOH B . 
H 3 HOH 179 879  272 HOH HOH B . 
H 3 HOH 180 880  598 HOH HOH B . 
H 3 HOH 181 881  442 HOH HOH B . 
H 3 HOH 182 882  122 HOH HOH B . 
H 3 HOH 183 883  173 HOH HOH B . 
H 3 HOH 184 884  446 HOH HOH B . 
H 3 HOH 185 885  516 HOH HOH B . 
H 3 HOH 186 886  100 HOH HOH B . 
H 3 HOH 187 887  557 HOH HOH B . 
H 3 HOH 188 888  277 HOH HOH B . 
H 3 HOH 189 889  217 HOH HOH B . 
H 3 HOH 190 890  119 HOH HOH B . 
H 3 HOH 191 891  849 HOH HOH B . 
H 3 HOH 192 892  505 HOH HOH B . 
H 3 HOH 193 893  701 HOH HOH B . 
H 3 HOH 194 894  196 HOH HOH B . 
H 3 HOH 195 895  463 HOH HOH B . 
H 3 HOH 196 896  590 HOH HOH B . 
H 3 HOH 197 897  230 HOH HOH B . 
H 3 HOH 198 898  517 HOH HOH B . 
H 3 HOH 199 899  733 HOH HOH B . 
H 3 HOH 200 900  858 HOH HOH B . 
H 3 HOH 201 901  346 HOH HOH B . 
H 3 HOH 202 902  730 HOH HOH B . 
H 3 HOH 203 903  303 HOH HOH B . 
H 3 HOH 204 904  70  HOH HOH B . 
H 3 HOH 205 905  668 HOH HOH B . 
H 3 HOH 206 906  923 HOH HOH B . 
H 3 HOH 207 907  59  HOH HOH B . 
H 3 HOH 208 908  842 HOH HOH B . 
H 3 HOH 209 909  151 HOH HOH B . 
H 3 HOH 210 910  514 HOH HOH B . 
H 3 HOH 211 911  33  HOH HOH B . 
H 3 HOH 212 912  727 HOH HOH B . 
H 3 HOH 213 913  619 HOH HOH B . 
H 3 HOH 214 914  737 HOH HOH B . 
H 3 HOH 215 915  305 HOH HOH B . 
H 3 HOH 216 916  62  HOH HOH B . 
H 3 HOH 217 917  271 HOH HOH B . 
H 3 HOH 218 918  396 HOH HOH B . 
H 3 HOH 219 919  141 HOH HOH B . 
H 3 HOH 220 920  149 HOH HOH B . 
H 3 HOH 221 921  174 HOH HOH B . 
H 3 HOH 222 922  609 HOH HOH B . 
H 3 HOH 223 923  439 HOH HOH B . 
H 3 HOH 224 924  379 HOH HOH B . 
H 3 HOH 225 925  862 HOH HOH B . 
H 3 HOH 226 926  207 HOH HOH B . 
H 3 HOH 227 927  325 HOH HOH B . 
H 3 HOH 228 928  415 HOH HOH B . 
H 3 HOH 229 929  326 HOH HOH B . 
H 3 HOH 230 930  780 HOH HOH B . 
H 3 HOH 231 931  484 HOH HOH B . 
H 3 HOH 232 932  528 HOH HOH B . 
H 3 HOH 233 933  766 HOH HOH B . 
H 3 HOH 234 934  80  HOH HOH B . 
H 3 HOH 235 935  172 HOH HOH B . 
H 3 HOH 236 936  92  HOH HOH B . 
H 3 HOH 237 937  491 HOH HOH B . 
H 3 HOH 238 938  204 HOH HOH B . 
H 3 HOH 239 939  518 HOH HOH B . 
H 3 HOH 240 940  433 HOH HOH B . 
H 3 HOH 241 941  110 HOH HOH B . 
H 3 HOH 242 942  55  HOH HOH B . 
H 3 HOH 243 943  235 HOH HOH B . 
H 3 HOH 244 944  90  HOH HOH B . 
H 3 HOH 245 945  167 HOH HOH B . 
H 3 HOH 246 946  699 HOH HOH B . 
H 3 HOH 247 947  477 HOH HOH B . 
H 3 HOH 248 948  879 HOH HOH B . 
H 3 HOH 249 949  454 HOH HOH B . 
H 3 HOH 250 950  47  HOH HOH B . 
H 3 HOH 251 951  281 HOH HOH B . 
H 3 HOH 252 952  577 HOH HOH B . 
H 3 HOH 253 953  284 HOH HOH B . 
H 3 HOH 254 954  361 HOH HOH B . 
H 3 HOH 255 955  795 HOH HOH B . 
H 3 HOH 256 956  574 HOH HOH B . 
H 3 HOH 257 957  890 HOH HOH B . 
H 3 HOH 258 958  403 HOH HOH B . 
H 3 HOH 259 959  814 HOH HOH B . 
H 3 HOH 260 960  620 HOH HOH B . 
H 3 HOH 261 961  545 HOH HOH B . 
H 3 HOH 262 962  48  HOH HOH B . 
H 3 HOH 263 963  556 HOH HOH B . 
H 3 HOH 264 964  813 HOH HOH B . 
H 3 HOH 265 965  604 HOH HOH B . 
H 3 HOH 266 966  487 HOH HOH B . 
H 3 HOH 267 967  357 HOH HOH B . 
H 3 HOH 268 968  811 HOH HOH B . 
H 3 HOH 269 969  240 HOH HOH B . 
H 3 HOH 270 970  282 HOH HOH B . 
H 3 HOH 271 971  783 HOH HOH B . 
H 3 HOH 272 972  804 HOH HOH B . 
H 3 HOH 273 973  659 HOH HOH B . 
H 3 HOH 274 974  134 HOH HOH B . 
H 3 HOH 275 975  176 HOH HOH B . 
H 3 HOH 276 976  582 HOH HOH B . 
H 3 HOH 277 977  260 HOH HOH B . 
H 3 HOH 278 978  770 HOH HOH B . 
H 3 HOH 279 979  823 HOH HOH B . 
H 3 HOH 280 980  857 HOH HOH B . 
H 3 HOH 281 981  344 HOH HOH B . 
H 3 HOH 282 982  399 HOH HOH B . 
H 3 HOH 283 983  188 HOH HOH B . 
H 3 HOH 284 984  901 HOH HOH B . 
H 3 HOH 285 985  606 HOH HOH B . 
H 3 HOH 286 986  768 HOH HOH B . 
H 3 HOH 287 987  428 HOH HOH B . 
H 3 HOH 288 988  393 HOH HOH B . 
H 3 HOH 289 989  226 HOH HOH B . 
H 3 HOH 290 990  471 HOH HOH B . 
H 3 HOH 291 991  748 HOH HOH B . 
H 3 HOH 292 992  397 HOH HOH B . 
H 3 HOH 293 993  885 HOH HOH B . 
H 3 HOH 294 994  511 HOH HOH B . 
H 3 HOH 295 995  740 HOH HOH B . 
H 3 HOH 296 996  333 HOH HOH B . 
H 3 HOH 297 997  412 HOH HOH B . 
H 3 HOH 298 998  693 HOH HOH B . 
H 3 HOH 299 999  787 HOH HOH B . 
H 3 HOH 300 1000 274 HOH HOH B . 
H 3 HOH 301 1001 859 HOH HOH B . 
H 3 HOH 302 1002 894 HOH HOH B . 
H 3 HOH 303 1003 629 HOH HOH B . 
H 3 HOH 304 1004 805 HOH HOH B . 
H 3 HOH 305 1005 685 HOH HOH B . 
H 3 HOH 306 1006 147 HOH HOH B . 
H 3 HOH 307 1007 529 HOH HOH B . 
H 3 HOH 308 1008 279 HOH HOH B . 
H 3 HOH 309 1009 704 HOH HOH B . 
H 3 HOH 310 1010 834 HOH HOH B . 
H 3 HOH 311 1011 848 HOH HOH B . 
H 3 HOH 312 1012 387 HOH HOH B . 
H 3 HOH 313 1013 596 HOH HOH B . 
H 3 HOH 314 1014 628 HOH HOH B . 
H 3 HOH 315 1015 523 HOH HOH B . 
H 3 HOH 316 1016 763 HOH HOH B . 
H 3 HOH 317 1017 656 HOH HOH B . 
H 3 HOH 318 1018 404 HOH HOH B . 
H 3 HOH 319 1019 700 HOH HOH B . 
H 3 HOH 320 1020 898 HOH HOH B . 
H 3 HOH 321 1021 697 HOH HOH B . 
H 3 HOH 322 1022 720 HOH HOH B . 
H 3 HOH 323 1023 343 HOH HOH B . 
H 3 HOH 324 1024 702 HOH HOH B . 
H 3 HOH 325 1025 745 HOH HOH B . 
H 3 HOH 326 1026 526 HOH HOH B . 
H 3 HOH 327 1027 664 HOH HOH B . 
H 3 HOH 328 1028 534 HOH HOH B . 
H 3 HOH 329 1029 843 HOH HOH B . 
H 3 HOH 330 1030 287 HOH HOH B . 
H 3 HOH 331 1031 225 HOH HOH B . 
H 3 HOH 332 1032 211 HOH HOH B . 
H 3 HOH 333 1033 660 HOH HOH B . 
H 3 HOH 334 1034 870 HOH HOH B . 
H 3 HOH 335 1035 715 HOH HOH B . 
H 3 HOH 336 1036 739 HOH HOH B . 
H 3 HOH 337 1037 273 HOH HOH B . 
H 3 HOH 338 1038 880 HOH HOH B . 
H 3 HOH 339 1039 414 HOH HOH B . 
H 3 HOH 340 1040 853 HOH HOH B . 
H 3 HOH 341 1041 401 HOH HOH B . 
H 3 HOH 342 1042 928 HOH HOH B . 
H 3 HOH 343 1043 703 HOH HOH B . 
H 3 HOH 344 1044 648 HOH HOH B . 
H 3 HOH 345 1045 883 HOH HOH B . 
H 3 HOH 346 1046 102 HOH HOH B . 
H 3 HOH 347 1047 627 HOH HOH B . 
H 3 HOH 348 1048 594 HOH HOH B . 
H 3 HOH 349 1049 34  HOH HOH B . 
H 3 HOH 350 1050 714 HOH HOH B . 
H 3 HOH 351 1051 584 HOH HOH B . 
H 3 HOH 352 1052 869 HOH HOH B . 
H 3 HOH 353 1053 332 HOH HOH B . 
H 3 HOH 354 1054 494 HOH HOH B . 
H 3 HOH 355 1055 131 HOH HOH B . 
H 3 HOH 356 1056 315 HOH HOH B . 
H 3 HOH 357 1057 646 HOH HOH B . 
H 3 HOH 358 1058 650 HOH HOH B . 
H 3 HOH 359 1059 916 HOH HOH B . 
H 3 HOH 360 1060 490 HOH HOH B . 
H 3 HOH 361 1061 369 HOH HOH B . 
H 3 HOH 362 1062 899 HOH HOH B . 
H 3 HOH 363 1063 479 HOH HOH B . 
H 3 HOH 364 1064 649 HOH HOH B . 
H 3 HOH 365 1065 837 HOH HOH B . 
H 3 HOH 366 1066 349 HOH HOH B . 
H 3 HOH 367 1067 419 HOH HOH B . 
H 3 HOH 368 1068 353 HOH HOH B . 
H 3 HOH 369 1069 774 HOH HOH B . 
H 3 HOH 370 1070 643 HOH HOH B . 
H 3 HOH 371 1071 513 HOH HOH B . 
H 3 HOH 372 1072 180 HOH HOH B . 
H 3 HOH 373 1073 555 HOH HOH B . 
H 3 HOH 374 1074 712 HOH HOH B . 
H 3 HOH 375 1075 677 HOH HOH B . 
H 3 HOH 376 1076 743 HOH HOH B . 
H 3 HOH 377 1077 900 HOH HOH B . 
H 3 HOH 378 1078 622 HOH HOH B . 
H 3 HOH 379 1079 610 HOH HOH B . 
H 3 HOH 380 1080 713 HOH HOH B . 
H 3 HOH 381 1081 360 HOH HOH B . 
H 3 HOH 382 1082 581 HOH HOH B . 
H 3 HOH 383 1083 753 HOH HOH B . 
H 3 HOH 384 1084 716 HOH HOH B . 
H 3 HOH 385 1085 532 HOH HOH B . 
H 3 HOH 386 1086 669 HOH HOH B . 
H 3 HOH 387 1087 824 HOH HOH B . 
H 3 HOH 388 1088 246 HOH HOH B . 
H 3 HOH 389 1089 662 HOH HOH B . 
H 3 HOH 390 1090 311 HOH HOH B . 
H 3 HOH 391 1091 723 HOH HOH B . 
H 3 HOH 392 1092 257 HOH HOH B . 
H 3 HOH 393 1093 741 HOH HOH B . 
H 3 HOH 394 1094 775 HOH HOH B . 
H 3 HOH 395 1095 750 HOH HOH B . 
H 3 HOH 396 1096 486 HOH HOH B . 
H 3 HOH 397 1097 383 HOH HOH B . 
H 3 HOH 398 1098 438 HOH HOH B . 
H 3 HOH 399 1099 583 HOH HOH B . 
H 3 HOH 400 1100 789 HOH HOH B . 
H 3 HOH 401 1101 625 HOH HOH B . 
H 3 HOH 402 1102 822 HOH HOH B . 
H 3 HOH 403 1103 542 HOH HOH B . 
H 3 HOH 404 1104 926 HOH HOH B . 
H 3 HOH 405 1105 309 HOH HOH B . 
H 3 HOH 406 1106 358 HOH HOH B . 
H 3 HOH 407 1107 562 HOH HOH B . 
H 3 HOH 408 1108 830 HOH HOH B . 
H 3 HOH 409 1109 893 HOH HOH B . 
H 3 HOH 410 1110 350 HOH HOH B . 
H 3 HOH 411 1111 864 HOH HOH B . 
H 3 HOH 412 1112 413 HOH HOH B . 
H 3 HOH 413 1113 384 HOH HOH B . 
H 3 HOH 414 1114 905 HOH HOH B . 
H 3 HOH 415 1115 731 HOH HOH B . 
H 3 HOH 416 1116 250 HOH HOH B . 
H 3 HOH 417 1117 525 HOH HOH B . 
H 3 HOH 418 1118 909 HOH HOH B . 
H 3 HOH 419 1119 882 HOH HOH B . 
H 3 HOH 420 1120 363 HOH HOH B . 
H 3 HOH 421 1121 519 HOH HOH B . 
H 3 HOH 422 1122 846 HOH HOH B . 
H 3 HOH 423 1123 391 HOH HOH B . 
H 3 HOH 424 1124 868 HOH HOH B . 
H 3 HOH 425 1125 818 HOH HOH B . 
H 3 HOH 426 1126 707 HOH HOH B . 
H 3 HOH 427 1127 844 HOH HOH B . 
H 3 HOH 428 1128 825 HOH HOH B . 
H 3 HOH 429 1129 930 HOH HOH B . 
H 3 HOH 430 1130 924 HOH HOH B . 
H 3 HOH 431 1131 886 HOH HOH B . 
H 3 HOH 432 1132 889 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 ARG 288 ? NH1 ? A ARG 63  NH1 
2  1 Y 1 A ARG 288 ? NH2 ? A ARG 63  NH2 
3  1 Y 1 A ASN 458 ? CG  ? A ASN 233 CG  
4  1 Y 1 A ASN 458 ? OD1 ? A ASN 233 OD1 
5  1 Y 1 A ASN 458 ? ND2 ? A ASN 233 ND2 
6  1 Y 1 A ARG 471 ? CZ  ? A ARG 246 CZ  
7  1 Y 1 A ARG 471 ? NH1 ? A ARG 246 NH1 
8  1 Y 1 A ARG 471 ? NH2 ? A ARG 246 NH2 
9  1 Y 1 A LEU 478 ? CD1 ? A LEU 253 CD1 
10 1 Y 1 A LEU 478 ? CD2 ? A LEU 253 CD2 
11 1 Y 1 A GLU 508 ? CG  ? A GLU 283 CG  
12 1 Y 1 A GLU 508 ? CD  ? A GLU 283 CD  
13 1 Y 1 A GLU 508 ? OE1 ? A GLU 283 OE1 
14 1 Y 1 A GLU 508 ? OE2 ? A GLU 283 OE2 
15 1 Y 1 B VAL 311 ? CG1 ? B VAL 86  CG1 
16 1 Y 1 B ASN 458 ? CG  ? B ASN 233 CG  
17 1 Y 1 B ASN 458 ? OD1 ? B ASN 233 OD1 
18 1 Y 1 B ASN 458 ? ND2 ? B ASN 233 ND2 
19 1 Y 1 B ARG 471 ? CZ  ? B ARG 246 CZ  
20 1 Y 1 B ARG 471 ? NH1 ? B ARG 246 NH1 
21 1 Y 1 B ARG 471 ? NH2 ? B ARG 246 NH2 
22 1 Y 1 B LEU 478 ? CD1 ? B LEU 253 CD1 
23 1 Y 1 B LEU 478 ? CD2 ? B LEU 253 CD2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? 1.20.1_4487 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .           2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .           4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  120.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9EDQ 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     67.490 
_cell.length_a_esd                 ? 
_cell.length_b                     67.490 
_cell.length_b_esd                 ? 
_cell.length_c                     238.760 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        12 
_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                         9EDQ 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                154 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 32 2 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9EDQ 
_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             2.07 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          40.48 
_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    
;1.6 M magnesium sulfate heptahydrate,
0.1 M MES (pH 6.5)
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            291.15 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER2 S 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-06-19 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.95372 
_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                        'AUSTRALIAN SYNCHROTRON BEAMLINE MX1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.95372 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   MX1 
_diffrn_source.pdbx_synchrotron_site       'Australian Synchrotron' 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9EDQ 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.63 
_reflns.d_resolution_low                               47.75 
_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                                     79732 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.9 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                13.4 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          11.1 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.57 
_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                                0.151 
_reflns.pdbx_Rpim_I_all                                0.041 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       1071388 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.145 
_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                                    1.63 
_reflns_shell.d_res_low                                     1.66 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           49582 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             3791 
_reflns_shell.percent_possible_obs                          97.5 
_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                               13.1 
_reflns_shell.pdbx_chi_squared                              0.52 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     1.3 
_reflns_shell.pdbx_Rrim_I_all                               1.721 
_reflns_shell.pdbx_Rpim_I_all                               0.467 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.639 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  1.654 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9EDQ 
_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                            1.63 
_refine.ls_d_res_low                             47.11 
_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                     79483 
_refine.ls_number_reflns_R_free                  3975 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.88 
_refine.ls_percent_reflns_R_free                 5.00 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1639 
_refine.ls_R_factor_R_free                       0.1938 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1624 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_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       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_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                 18.24 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.17 
_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                       1.63 
_refine_hist.d_res_low                        47.11 
_refine_hist.number_atoms_solvent             862 
_refine_hist.number_atoms_total               5421 
_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        4539 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         20 
_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' ? 0.006  ? 4959 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.796  ? 6838 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 11.148 ? 1762 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.057  ? 749  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.007  ? 917  ? f_plane_restr      ? ? 
# 
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' 1.63 1.65  . . 137 2610 98.00  . . . . 0.2421 . . . . . . . . . . . 0.2325 
'X-RAY DIFFRACTION' 1.65 1.67  . . 139 2635 100.00 . . . . 0.2486 . . . . . . . . . . . 0.2802 
'X-RAY DIFFRACTION' 1.67 1.70  . . 141 2671 100.00 . . . . 0.2301 . . . . . . . . . . . 0.2872 
'X-RAY DIFFRACTION' 1.70 1.72  . . 140 2666 100.00 . . . . 0.2267 . . . . . . . . . . . 0.2726 
'X-RAY DIFFRACTION' 1.72 1.74  . . 139 2636 100.00 . . . . 0.2168 . . . . . . . . . . . 0.2459 
'X-RAY DIFFRACTION' 1.74 1.77  . . 142 2705 100.00 . . . . 0.2021 . . . . . . . . . . . 0.2457 
'X-RAY DIFFRACTION' 1.77 1.80  . . 138 2628 100.00 . . . . 0.1877 . . . . . . . . . . . 0.2293 
'X-RAY DIFFRACTION' 1.80 1.83  . . 143 2701 100.00 . . . . 0.1824 . . . . . . . . . . . 0.2449 
'X-RAY DIFFRACTION' 1.83 1.86  . . 138 2631 100.00 . . . . 0.1753 . . . . . . . . . . . 0.1980 
'X-RAY DIFFRACTION' 1.86 1.89  . . 140 2663 100.00 . . . . 0.1840 . . . . . . . . . . . 0.2384 
'X-RAY DIFFRACTION' 1.89 1.93  . . 142 2687 100.00 . . . . 0.1843 . . . . . . . . . . . 0.2221 
'X-RAY DIFFRACTION' 1.93 1.97  . . 140 2666 100.00 . . . . 0.1839 . . . . . . . . . . . 0.2291 
'X-RAY DIFFRACTION' 1.97 2.01  . . 140 2651 100.00 . . . . 0.1716 . . . . . . . . . . . 0.1831 
'X-RAY DIFFRACTION' 2.01 2.06  . . 141 2683 100.00 . . . . 0.1536 . . . . . . . . . . . 0.2127 
'X-RAY DIFFRACTION' 2.06 2.11  . . 143 2715 100.00 . . . . 0.1591 . . . . . . . . . . . 0.2173 
'X-RAY DIFFRACTION' 2.11 2.17  . . 140 2667 100.00 . . . . 0.1532 . . . . . . . . . . . 0.1964 
'X-RAY DIFFRACTION' 2.17 2.23  . . 141 2677 100.00 . . . . 0.1585 . . . . . . . . . . . 0.1953 
'X-RAY DIFFRACTION' 2.23 2.30  . . 140 2668 100.00 . . . . 0.1541 . . . . . . . . . . . 0.1931 
'X-RAY DIFFRACTION' 2.30 2.38  . . 144 2734 100.00 . . . . 0.1566 . . . . . . . . . . . 0.1849 
'X-RAY DIFFRACTION' 2.38 2.48  . . 142 2685 100.00 . . . . 0.1582 . . . . . . . . . . . 0.2026 
'X-RAY DIFFRACTION' 2.48 2.59  . . 143 2721 100.00 . . . . 0.1602 . . . . . . . . . . . 0.2095 
'X-RAY DIFFRACTION' 2.59 2.73  . . 141 2679 100.00 . . . . 0.1671 . . . . . . . . . . . 0.2122 
'X-RAY DIFFRACTION' 2.73 2.90  . . 143 2714 100.00 . . . . 0.1614 . . . . . . . . . . . 0.1852 
'X-RAY DIFFRACTION' 2.90 3.12  . . 144 2748 100.00 . . . . 0.1655 . . . . . . . . . . . 0.1608 
'X-RAY DIFFRACTION' 3.12 3.44  . . 145 2749 100.00 . . . . 0.1502 . . . . . . . . . . . 0.1940 
'X-RAY DIFFRACTION' 3.44 3.93  . . 144 2760 100.00 . . . . 0.1334 . . . . . . . . . . . 0.1750 
'X-RAY DIFFRACTION' 3.93 4.96  . . 148 2808 100.00 . . . . 0.1246 . . . . . . . . . . . 0.1232 
'X-RAY DIFFRACTION' 4.96 47.11 . . 157 2950 99.00  . . . . 0.1732 . . . . . . . . . . . 0.1974 
# 
_struct.entry_id                     9EDQ 
_struct.title                        'GX/NPIH26 bat norovirus protruding domain' 
_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        9EDQ 
_struct_keywords.text            'norovirus, P domain, VIRAL PROTEIN' 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN' 
# 
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 2 ? 
F N N 2 ? 
G N N 3 ? 
H N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A0A2S1TZT6_9CALI 
_struct_ref.pdbx_db_accession          A0A2S1TZT6 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;EPFSLPNLQTDEMSSSRWPNPLATLFADPNVAVAPQWQNGRCTLEGELLGTTPRNASWLNRFRGVSTAAVANQVLHLTLY
EPDGSVFNPLSGAPAPEGFPDFTAQEYHLRAAGKVANTTGGGEIKSTDYTPALGGVKITAWDATGPSAGVEMTGQIESIG
MENNTDFDVLPDYNGSAFDGSLNLAPPIVPLLPGETLLRFGTVPITTRRQSDPIRIISCALPQEWITWFLTHNFTALGDA
ALLRYRNQATGQLLFECKLYRSGFVVVNGVNVRTEFPMSGVFEFVSWVPNFFQLAPV
;
_struct_ref.pdbx_align_begin           227 
# 
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 9EDQ A 1 ? 297 ? A0A2S1TZT6 227 ? 523 ? 226 522 
2 1 9EDQ B 1 ? 297 ? A0A2S1TZT6 227 ? 523 ? 226 522 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 4290  ? 
1 MORE         -70   ? 
1 'SSA (A^2)'  22330 ? 
# 
_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   none 
_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 GLN A 9   ? MET A 13  ? GLN A 234 MET A 238 5 ? 5  
HELX_P HELX_P2  AA2 ASN A 55  ? LEU A 59  ? ASN A 280 LEU A 284 5 ? 5  
HELX_P HELX_P3  AA3 ASN A 88  ? GLY A 92  ? ASN A 313 GLY A 317 5 ? 5  
HELX_P HELX_P4  AA4 THR A 127 ? TYR A 129 ? THR A 352 TYR A 354 5 ? 3  
HELX_P HELX_P5  AA5 THR A 130 ? LEU A 133 ? THR A 355 LEU A 358 5 ? 4  
HELX_P HELX_P6  AA6 ASN A 163 ? VAL A 169 ? ASN A 388 VAL A 394 5 ? 7  
HELX_P HELX_P7  AA7 PRO A 222 ? THR A 231 ? PRO A 447 THR A 456 1 ? 10 
HELX_P HELX_P8  AA8 GLN B 9   ? MET B 13  ? GLN B 234 MET B 238 5 ? 5  
HELX_P HELX_P9  AA9 ASN B 55  ? LEU B 59  ? ASN B 280 LEU B 284 5 ? 5  
HELX_P HELX_P10 AB1 THR B 127 ? TYR B 129 ? THR B 352 TYR B 354 5 ? 3  
HELX_P HELX_P11 AB2 THR B 130 ? LEU B 133 ? THR B 355 LEU B 358 5 ? 4  
HELX_P HELX_P12 AB3 ASN B 163 ? VAL B 169 ? ASN B 388 VAL B 394 5 ? 7  
HELX_P HELX_P13 AB4 PRO B 222 ? THR B 231 ? PRO B 447 THR B 456 1 ? 10 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 GLY 145 A . ? GLY 370 A PRO 146 A ? PRO 371 A 1 4.98 
2 GLY 145 B . ? GLY 370 B PRO 146 B ? PRO 371 B 1 5.09 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 6 ? 
AA3 ? 6 ? 
AA4 ? 4 ? 
AA5 ? 4 ? 
AA6 ? 6 ? 
AA7 ? 6 ? 
AA8 ? 4 ? 
# 
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 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA3 5 6 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? parallel      
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA6 3 4 ? anti-parallel 
AA6 4 5 ? anti-parallel 
AA6 5 6 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA7 2 3 ? anti-parallel 
AA7 3 4 ? anti-parallel 
AA7 4 5 ? anti-parallel 
AA7 5 6 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA8 2 3 ? anti-parallel 
AA8 3 4 ? 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 ILE A 217 ? CYS A 219 ? ILE A 442 CYS A 444 
AA1 2 GLU A 195 ? THR A 202 ? GLU A 420 THR A 427 
AA1 3 THR A 24  ? ALA A 27  ? THR A 249 ALA A 252 
AA1 4 THR A 274 ? GLU A 275 ? THR A 499 GLU A 500 
AA2 1 ILE A 217 ? CYS A 219 ? ILE A 442 CYS A 444 
AA2 2 GLU A 195 ? THR A 202 ? GLU A 420 THR A 427 
AA2 3 PHE A 264 ? ASN A 268 ? PHE A 489 ASN A 493 
AA2 4 LEU A 253 ? TYR A 260 ? LEU A 478 TYR A 485 
AA2 5 ALA A 240 ? ARG A 246 ? ALA A 465 ARG A 471 
AA2 6 VAL A 281 ? VAL A 288 ? VAL A 506 VAL A 513 
AA3 1 GLY A 120 ? LYS A 125 ? GLY A 345 LYS A 350 
AA3 2 GLU A 106 ? GLY A 113 ? GLU A 331 GLY A 338 
AA3 3 GLU A 151 ? GLY A 160 ? GLU A 376 GLY A 385 
AA3 4 ARG A 61  ? SER A 66  ? ARG A 286 SER A 291 
AA3 5 LEU A 75  ? TYR A 80  ? LEU A 300 TYR A 305 
AA3 6 GLY A 135 ? ILE A 138 ? GLY A 360 ILE A 363 
AA4 1 GLY A 120 ? LYS A 125 ? GLY A 345 LYS A 350 
AA4 2 GLU A 106 ? GLY A 113 ? GLU A 331 GLY A 338 
AA4 3 GLU A 151 ? GLY A 160 ? GLU A 376 GLY A 385 
AA4 4 THR A 206 ? THR A 207 ? THR A 431 THR A 432 
AA5 1 ILE B 217 ? CYS B 219 ? ILE B 442 CYS B 444 
AA5 2 GLU B 195 ? THR B 202 ? GLU B 420 THR B 427 
AA5 3 THR B 24  ? ALA B 27  ? THR B 249 ALA B 252 
AA5 4 THR B 274 ? GLU B 275 ? THR B 499 GLU B 500 
AA6 1 ILE B 217 ? CYS B 219 ? ILE B 442 CYS B 444 
AA6 2 GLU B 195 ? THR B 202 ? GLU B 420 THR B 427 
AA6 3 PHE B 264 ? ASN B 268 ? PHE B 489 ASN B 493 
AA6 4 LEU B 253 ? TYR B 260 ? LEU B 478 TYR B 485 
AA6 5 ALA B 240 ? ARG B 246 ? ALA B 465 ARG B 471 
AA6 6 VAL B 281 ? VAL B 288 ? VAL B 506 VAL B 513 
AA7 1 GLY B 120 ? LYS B 125 ? GLY B 345 LYS B 350 
AA7 2 GLU B 106 ? GLY B 113 ? GLU B 331 GLY B 338 
AA7 3 GLU B 151 ? GLY B 160 ? GLU B 376 GLY B 385 
AA7 4 ARG B 61  ? SER B 66  ? ARG B 286 SER B 291 
AA7 5 LEU B 75  ? TYR B 80  ? LEU B 300 TYR B 305 
AA7 6 GLY B 135 ? ILE B 138 ? GLY B 360 ILE B 363 
AA8 1 GLY B 120 ? LYS B 125 ? GLY B 345 LYS B 350 
AA8 2 GLU B 106 ? GLY B 113 ? GLU B 331 GLY B 338 
AA8 3 GLU B 151 ? GLY B 160 ? GLU B 376 GLY B 385 
AA8 4 THR B 206 ? THR B 207 ? THR B 431 THR B 432 
# 
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 ILE A 217 ? O ILE A 442 N THR A 202 ? N THR A 427 
AA1 2 3 O ARG A 199 ? O ARG A 424 N PHE A 26  ? N PHE A 251 
AA1 3 4 N ALA A 27  ? N ALA A 252 O THR A 274 ? O THR A 499 
AA2 1 2 O ILE A 217 ? O ILE A 442 N THR A 202 ? N THR A 427 
AA2 2 3 N LEU A 198 ? N LEU A 423 O VAL A 265 ? O VAL A 490 
AA2 3 4 O PHE A 264 ? O PHE A 489 N TYR A 260 ? N TYR A 485 
AA2 4 5 O PHE A 255 ? O PHE A 480 N TYR A 245 ? N TYR A 470 
AA2 5 6 N LEU A 242 ? N LEU A 467 O SER A 286 ? O SER A 511 
AA3 1 2 O GLY A 122 ? O GLY A 347 N LEU A 109 ? N LEU A 334 
AA3 2 3 N ARG A 110 ? N ARG A 335 O GLN A 155 ? O GLN A 380 
AA3 3 4 O MET A 152 ? O MET A 377 N GLY A 64  ? N GLY A 289 
AA3 4 5 N ARG A 63  ? N ARG A 288 O TYR A 80  ? O TYR A 305 
AA3 5 6 N LEU A 75  ? N LEU A 300 O ILE A 138 ? O ILE A 363 
AA4 1 2 O GLY A 122 ? O GLY A 347 N LEU A 109 ? N LEU A 334 
AA4 2 3 N ARG A 110 ? N ARG A 335 O GLN A 155 ? O GLN A 380 
AA4 3 4 N ILE A 159 ? N ILE A 384 O THR A 207 ? O THR A 432 
AA5 1 2 O ILE B 217 ? O ILE B 442 N THR B 202 ? N THR B 427 
AA5 2 3 O ARG B 199 ? O ARG B 424 N PHE B 26  ? N PHE B 251 
AA5 3 4 N ALA B 27  ? N ALA B 252 O THR B 274 ? O THR B 499 
AA6 1 2 O ILE B 217 ? O ILE B 442 N THR B 202 ? N THR B 427 
AA6 2 3 N LEU B 198 ? N LEU B 423 O VAL B 265 ? O VAL B 490 
AA6 3 4 O PHE B 264 ? O PHE B 489 N TYR B 260 ? N TYR B 485 
AA6 4 5 O LEU B 254 ? O LEU B 479 N TYR B 245 ? N TYR B 470 
AA6 5 6 N ARG B 244 ? N ARG B 469 O GLU B 283 ? O GLU B 508 
AA7 1 2 O GLY B 122 ? O GLY B 347 N LEU B 109 ? N LEU B 334 
AA7 2 3 N GLU B 106 ? N GLU B 331 O GLY B 160 ? O GLY B 385 
AA7 3 4 O GLY B 154 ? O GLY B 379 N PHE B 62  ? N PHE B 287 
AA7 4 5 N VAL B 65  ? N VAL B 290 O THR B 78  ? O THR B 303 
AA7 5 6 N LEU B 75  ? N LEU B 300 O ILE B 138 ? O ILE B 363 
AA8 1 2 O GLY B 122 ? O GLY B 347 N LEU B 109 ? N LEU B 334 
AA8 2 3 N GLU B 106 ? N GLU B 331 O GLY B 160 ? O GLY B 385 
AA8 3 4 N ILE B 159 ? N ILE B 384 O THR B 207 ? O THR B 432 
# 
_pdbx_entry_details.entry_id                   9EDQ 
_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     N 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASN A 458 ? ? -106.80 68.76  
2 1 VAL A 510 ? ? -109.82 -64.67 
3 1 PHE B 403 ? ? 53.67   82.84  
4 1 ASN B 458 ? ? -103.59 77.61  
5 1 VAL B 510 ? ? -107.70 -60.36 
# 
_pdbx_refine_tls.id               1 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           refined 
_pdbx_refine_tls.origin_x         14.6964 
_pdbx_refine_tls.origin_y         -25.2550 
_pdbx_refine_tls.origin_z         20.1292 
_pdbx_refine_tls.T[1][1]          0.0849 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          -0.0144 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          -0.0116 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.1260 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          0.0018 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.0850 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          0.4910 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          0.0022 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          -0.1458 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          0.5303 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          -0.1421 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          0.6984 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          0.0207 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          -0.0036 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          -0.0093 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          -0.0128 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          0.0139 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          0.0296 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          0.0111 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          -0.0311 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          -0.0273 
_pdbx_refine_tls.S[3][3]_esd      ? 
# 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.refine_tls_id       1 
_pdbx_refine_tls_group.beg_label_asym_id   ? 
_pdbx_refine_tls_group.beg_label_seq_id    ? 
_pdbx_refine_tls_group.beg_auth_asym_id    ? 
_pdbx_refine_tls_group.beg_auth_seq_id     ? 
_pdbx_refine_tls_group.beg_PDB_ins_code    ? 
_pdbx_refine_tls_group.end_label_asym_id   ? 
_pdbx_refine_tls_group.end_label_seq_id    ? 
_pdbx_refine_tls_group.end_auth_asym_id    ? 
_pdbx_refine_tls_group.end_auth_seq_id     ? 
_pdbx_refine_tls_group.end_PDB_ins_code    ? 
_pdbx_refine_tls_group.selection           ? 
_pdbx_refine_tls_group.selection_details   all 
# 
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 1122 ? 5.87 . 
2  1 O ? A HOH 1123 ? 5.87 . 
3  1 O ? A HOH 1124 ? 5.95 . 
4  1 O ? A HOH 1125 ? 6.14 . 
5  1 O ? A HOH 1126 ? 6.18 . 
6  1 O ? A HOH 1127 ? 6.19 . 
7  1 O ? A HOH 1128 ? 6.39 . 
8  1 O ? A HOH 1129 ? 6.67 . 
9  1 O ? A HOH 1130 ? 6.96 . 
10 1 O ? B HOH 1122 ? 5.86 . 
11 1 O ? B HOH 1123 ? 5.91 . 
12 1 O ? B HOH 1124 ? 5.98 . 
13 1 O ? B HOH 1125 ? 6.03 . 
14 1 O ? B HOH 1126 ? 6.27 . 
15 1 O A B HOH 1127 ? 6.29 . 
16 1 O ? B HOH 1128 ? 6.40 . 
17 1 O ? B HOH 1129 ? 6.91 . 
18 1 O ? B HOH 1130 ? 7.28 . 
19 1 O ? B HOH 1131 ? 7.95 . 
20 1 O ? B HOH 1132 ? 8.18 . 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
GLN N    N N N 88  
GLN CA   C N S 89  
GLN C    C N N 90  
GLN O    O N N 91  
GLN CB   C N N 92  
GLN CG   C N N 93  
GLN CD   C N N 94  
GLN OE1  O N N 95  
GLN NE2  N N N 96  
GLN OXT  O N N 97  
GLN H    H N N 98  
GLN H2   H N N 99  
GLN HA   H N N 100 
GLN HB2  H N N 101 
GLN HB3  H N N 102 
GLN HG2  H N N 103 
GLN HG3  H N N 104 
GLN HE21 H N N 105 
GLN HE22 H N N 106 
GLN HXT  H N N 107 
GLU N    N N N 108 
GLU CA   C N S 109 
GLU C    C N N 110 
GLU O    O N N 111 
GLU CB   C N N 112 
GLU CG   C N N 113 
GLU CD   C N N 114 
GLU OE1  O N N 115 
GLU OE2  O N N 116 
GLU OXT  O N N 117 
GLU H    H N N 118 
GLU H2   H N N 119 
GLU HA   H N N 120 
GLU HB2  H N N 121 
GLU HB3  H N N 122 
GLU HG2  H N N 123 
GLU HG3  H N N 124 
GLU HE2  H N N 125 
GLU HXT  H N N 126 
GLY N    N N N 127 
GLY CA   C N N 128 
GLY C    C N N 129 
GLY O    O N N 130 
GLY OXT  O N N 131 
GLY H    H N N 132 
GLY H2   H N N 133 
GLY HA2  H N N 134 
GLY HA3  H N N 135 
GLY HXT  H N N 136 
HIS N    N N N 137 
HIS CA   C N S 138 
HIS C    C N N 139 
HIS O    O N N 140 
HIS CB   C N N 141 
HIS CG   C Y N 142 
HIS ND1  N Y N 143 
HIS CD2  C Y N 144 
HIS CE1  C Y N 145 
HIS NE2  N Y N 146 
HIS OXT  O N N 147 
HIS H    H N N 148 
HIS H2   H N N 149 
HIS HA   H N N 150 
HIS HB2  H N N 151 
HIS HB3  H N N 152 
HIS HD1  H N N 153 
HIS HD2  H N N 154 
HIS HE1  H N N 155 
HIS HE2  H N N 156 
HIS HXT  H N N 157 
HOH O    O N N 158 
HOH H1   H N N 159 
HOH H2   H N N 160 
ILE N    N N N 161 
ILE CA   C N S 162 
ILE C    C N N 163 
ILE O    O N N 164 
ILE CB   C N S 165 
ILE CG1  C N N 166 
ILE CG2  C N N 167 
ILE CD1  C N N 168 
ILE OXT  O N N 169 
ILE H    H N N 170 
ILE H2   H N N 171 
ILE HA   H N N 172 
ILE HB   H N N 173 
ILE HG12 H N N 174 
ILE HG13 H N N 175 
ILE HG21 H N N 176 
ILE HG22 H N N 177 
ILE HG23 H N N 178 
ILE HD11 H N N 179 
ILE HD12 H N N 180 
ILE HD13 H N N 181 
ILE HXT  H N N 182 
LEU N    N N N 183 
LEU CA   C N S 184 
LEU C    C N N 185 
LEU O    O N N 186 
LEU CB   C N N 187 
LEU CG   C N N 188 
LEU CD1  C N N 189 
LEU CD2  C N N 190 
LEU OXT  O N N 191 
LEU H    H N N 192 
LEU H2   H N N 193 
LEU HA   H N N 194 
LEU HB2  H N N 195 
LEU HB3  H N N 196 
LEU HG   H N N 197 
LEU HD11 H N N 198 
LEU HD12 H N N 199 
LEU HD13 H N N 200 
LEU HD21 H N N 201 
LEU HD22 H N N 202 
LEU HD23 H N N 203 
LEU HXT  H N N 204 
LYS N    N N N 205 
LYS CA   C N S 206 
LYS C    C N N 207 
LYS O    O N N 208 
LYS CB   C N N 209 
LYS CG   C N N 210 
LYS CD   C N N 211 
LYS CE   C N N 212 
LYS NZ   N N N 213 
LYS OXT  O N N 214 
LYS H    H N N 215 
LYS H2   H N N 216 
LYS HA   H N N 217 
LYS HB2  H N N 218 
LYS HB3  H N N 219 
LYS HG2  H N N 220 
LYS HG3  H N N 221 
LYS HD2  H N N 222 
LYS HD3  H N N 223 
LYS HE2  H N N 224 
LYS HE3  H N N 225 
LYS HZ1  H N N 226 
LYS HZ2  H N N 227 
LYS HZ3  H N N 228 
LYS HXT  H N N 229 
MET N    N N N 230 
MET CA   C N S 231 
MET C    C N N 232 
MET O    O N N 233 
MET CB   C N N 234 
MET CG   C N N 235 
MET SD   S N N 236 
MET CE   C N N 237 
MET OXT  O N N 238 
MET H    H N N 239 
MET H2   H N N 240 
MET HA   H N N 241 
MET HB2  H N N 242 
MET HB3  H N N 243 
MET HG2  H N N 244 
MET HG3  H N N 245 
MET HE1  H N N 246 
MET HE2  H N N 247 
MET HE3  H N N 248 
MET HXT  H N N 249 
PHE N    N N N 250 
PHE CA   C N S 251 
PHE C    C N N 252 
PHE O    O N N 253 
PHE CB   C N N 254 
PHE CG   C Y N 255 
PHE CD1  C Y N 256 
PHE CD2  C Y N 257 
PHE CE1  C Y N 258 
PHE CE2  C Y N 259 
PHE CZ   C Y N 260 
PHE OXT  O N N 261 
PHE H    H N N 262 
PHE H2   H N N 263 
PHE HA   H N N 264 
PHE HB2  H N N 265 
PHE HB3  H N N 266 
PHE HD1  H N N 267 
PHE HD2  H N N 268 
PHE HE1  H N N 269 
PHE HE2  H N N 270 
PHE HZ   H N N 271 
PHE HXT  H N N 272 
PRO N    N N N 273 
PRO CA   C N S 274 
PRO C    C N N 275 
PRO O    O N N 276 
PRO CB   C N N 277 
PRO CG   C N N 278 
PRO CD   C N N 279 
PRO OXT  O N N 280 
PRO H    H N N 281 
PRO HA   H N N 282 
PRO HB2  H N N 283 
PRO HB3  H N N 284 
PRO HG2  H N N 285 
PRO HG3  H N N 286 
PRO HD2  H N N 287 
PRO HD3  H N N 288 
PRO HXT  H N N 289 
SER N    N N N 290 
SER CA   C N S 291 
SER C    C N N 292 
SER O    O N N 293 
SER CB   C N N 294 
SER OG   O N N 295 
SER OXT  O N N 296 
SER H    H N N 297 
SER H2   H N N 298 
SER HA   H N N 299 
SER HB2  H N N 300 
SER HB3  H N N 301 
SER HG   H N N 302 
SER HXT  H N N 303 
SO4 S    S N N 304 
SO4 O1   O N N 305 
SO4 O2   O N N 306 
SO4 O3   O N N 307 
SO4 O4   O N N 308 
THR N    N N N 309 
THR CA   C N S 310 
THR C    C N N 311 
THR O    O N N 312 
THR CB   C N R 313 
THR OG1  O N N 314 
THR CG2  C N N 315 
THR OXT  O N N 316 
THR H    H N N 317 
THR H2   H N N 318 
THR HA   H N N 319 
THR HB   H N N 320 
THR HG1  H N N 321 
THR HG21 H N N 322 
THR HG22 H N N 323 
THR HG23 H N N 324 
THR HXT  H N N 325 
TRP N    N N N 326 
TRP CA   C N S 327 
TRP C    C N N 328 
TRP O    O N N 329 
TRP CB   C N N 330 
TRP CG   C Y N 331 
TRP CD1  C Y N 332 
TRP CD2  C Y N 333 
TRP NE1  N Y N 334 
TRP CE2  C Y N 335 
TRP CE3  C Y N 336 
TRP CZ2  C Y N 337 
TRP CZ3  C Y N 338 
TRP CH2  C Y N 339 
TRP OXT  O N N 340 
TRP H    H N N 341 
TRP H2   H N N 342 
TRP HA   H N N 343 
TRP HB2  H N N 344 
TRP HB3  H N N 345 
TRP HD1  H N N 346 
TRP HE1  H N N 347 
TRP HE3  H N N 348 
TRP HZ2  H N N 349 
TRP HZ3  H N N 350 
TRP HH2  H N N 351 
TRP HXT  H N N 352 
TYR N    N N N 353 
TYR CA   C N S 354 
TYR C    C N N 355 
TYR O    O N N 356 
TYR CB   C N N 357 
TYR CG   C Y N 358 
TYR CD1  C Y N 359 
TYR CD2  C Y N 360 
TYR CE1  C Y N 361 
TYR CE2  C Y N 362 
TYR CZ   C Y N 363 
TYR OH   O N N 364 
TYR OXT  O N N 365 
TYR H    H N N 366 
TYR H2   H N N 367 
TYR HA   H N N 368 
TYR HB2  H N N 369 
TYR HB3  H N N 370 
TYR HD1  H N N 371 
TYR HD2  H N N 372 
TYR HE1  H N N 373 
TYR HE2  H N N 374 
TYR HH   H N N 375 
TYR HXT  H N N 376 
VAL N    N N N 377 
VAL CA   C N S 378 
VAL C    C N N 379 
VAL O    O N N 380 
VAL CB   C N N 381 
VAL CG1  C N N 382 
VAL CG2  C N N 383 
VAL OXT  O N N 384 
VAL H    H N N 385 
VAL H2   H N N 386 
VAL HA   H N N 387 
VAL HB   H N N 388 
VAL HG11 H N N 389 
VAL HG12 H N N 390 
VAL HG13 H N N 391 
VAL HG21 H N N 392 
VAL HG22 H N N 393 
VAL HG23 H N N 394 
VAL HXT  H N N 395 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LYS N   CA   sing N N 194 
LYS N   H    sing N N 195 
LYS N   H2   sing N N 196 
LYS CA  C    sing N N 197 
LYS CA  CB   sing N N 198 
LYS CA  HA   sing N N 199 
LYS C   O    doub N N 200 
LYS C   OXT  sing N N 201 
LYS CB  CG   sing N N 202 
LYS CB  HB2  sing N N 203 
LYS CB  HB3  sing N N 204 
LYS CG  CD   sing N N 205 
LYS CG  HG2  sing N N 206 
LYS CG  HG3  sing N N 207 
LYS CD  CE   sing N N 208 
LYS CD  HD2  sing N N 209 
LYS CD  HD3  sing N N 210 
LYS CE  NZ   sing N N 211 
LYS CE  HE2  sing N N 212 
LYS CE  HE3  sing N N 213 
LYS NZ  HZ1  sing N N 214 
LYS NZ  HZ2  sing N N 215 
LYS NZ  HZ3  sing N N 216 
LYS OXT HXT  sing N N 217 
MET N   CA   sing N N 218 
MET N   H    sing N N 219 
MET N   H2   sing N N 220 
MET CA  C    sing N N 221 
MET CA  CB   sing N N 222 
MET CA  HA   sing N N 223 
MET C   O    doub N N 224 
MET C   OXT  sing N N 225 
MET CB  CG   sing N N 226 
MET CB  HB2  sing N N 227 
MET CB  HB3  sing N N 228 
MET CG  SD   sing N N 229 
MET CG  HG2  sing N N 230 
MET CG  HG3  sing N N 231 
MET SD  CE   sing N N 232 
MET CE  HE1  sing N N 233 
MET CE  HE2  sing N N 234 
MET CE  HE3  sing N N 235 
MET OXT HXT  sing N N 236 
PHE N   CA   sing N N 237 
PHE N   H    sing N N 238 
PHE N   H2   sing N N 239 
PHE CA  C    sing N N 240 
PHE CA  CB   sing N N 241 
PHE CA  HA   sing N N 242 
PHE C   O    doub N N 243 
PHE C   OXT  sing N N 244 
PHE CB  CG   sing N N 245 
PHE CB  HB2  sing N N 246 
PHE CB  HB3  sing N N 247 
PHE CG  CD1  doub Y N 248 
PHE CG  CD2  sing Y N 249 
PHE CD1 CE1  sing Y N 250 
PHE CD1 HD1  sing N N 251 
PHE CD2 CE2  doub Y N 252 
PHE CD2 HD2  sing N N 253 
PHE CE1 CZ   doub Y N 254 
PHE CE1 HE1  sing N N 255 
PHE CE2 CZ   sing Y N 256 
PHE CE2 HE2  sing N N 257 
PHE CZ  HZ   sing N N 258 
PHE OXT HXT  sing N N 259 
PRO N   CA   sing N N 260 
PRO N   CD   sing N N 261 
PRO N   H    sing N N 262 
PRO CA  C    sing N N 263 
PRO CA  CB   sing N N 264 
PRO CA  HA   sing N N 265 
PRO C   O    doub N N 266 
PRO C   OXT  sing N N 267 
PRO CB  CG   sing N N 268 
PRO CB  HB2  sing N N 269 
PRO CB  HB3  sing N N 270 
PRO CG  CD   sing N N 271 
PRO CG  HG2  sing N N 272 
PRO CG  HG3  sing N N 273 
PRO CD  HD2  sing N N 274 
PRO CD  HD3  sing N N 275 
PRO OXT HXT  sing N N 276 
SER N   CA   sing N N 277 
SER N   H    sing N N 278 
SER N   H2   sing N N 279 
SER CA  C    sing N N 280 
SER CA  CB   sing N N 281 
SER CA  HA   sing N N 282 
SER C   O    doub N N 283 
SER C   OXT  sing N N 284 
SER CB  OG   sing N N 285 
SER CB  HB2  sing N N 286 
SER CB  HB3  sing N N 287 
SER OG  HG   sing N N 288 
SER OXT HXT  sing N N 289 
SO4 S   O1   doub N N 290 
SO4 S   O2   doub N N 291 
SO4 S   O3   sing N N 292 
SO4 S   O4   sing N N 293 
THR N   CA   sing N N 294 
THR N   H    sing N N 295 
THR N   H2   sing N N 296 
THR CA  C    sing N N 297 
THR CA  CB   sing N N 298 
THR CA  HA   sing N N 299 
THR C   O    doub N N 300 
THR C   OXT  sing N N 301 
THR CB  OG1  sing N N 302 
THR CB  CG2  sing N N 303 
THR CB  HB   sing N N 304 
THR OG1 HG1  sing N N 305 
THR CG2 HG21 sing N N 306 
THR CG2 HG22 sing N N 307 
THR CG2 HG23 sing N N 308 
THR OXT HXT  sing N N 309 
TRP N   CA   sing N N 310 
TRP N   H    sing N N 311 
TRP N   H2   sing N N 312 
TRP CA  C    sing N N 313 
TRP CA  CB   sing N N 314 
TRP CA  HA   sing N N 315 
TRP C   O    doub N N 316 
TRP C   OXT  sing N N 317 
TRP CB  CG   sing N N 318 
TRP CB  HB2  sing N N 319 
TRP CB  HB3  sing N N 320 
TRP CG  CD1  doub Y N 321 
TRP CG  CD2  sing Y N 322 
TRP CD1 NE1  sing Y N 323 
TRP CD1 HD1  sing N N 324 
TRP CD2 CE2  doub Y N 325 
TRP CD2 CE3  sing Y N 326 
TRP NE1 CE2  sing Y N 327 
TRP NE1 HE1  sing N N 328 
TRP CE2 CZ2  sing Y N 329 
TRP CE3 CZ3  doub Y N 330 
TRP CE3 HE3  sing N N 331 
TRP CZ2 CH2  doub Y N 332 
TRP CZ2 HZ2  sing N N 333 
TRP CZ3 CH2  sing Y N 334 
TRP CZ3 HZ3  sing N N 335 
TRP CH2 HH2  sing N N 336 
TRP OXT HXT  sing N N 337 
TYR N   CA   sing N N 338 
TYR N   H    sing N N 339 
TYR N   H2   sing N N 340 
TYR CA  C    sing N N 341 
TYR CA  CB   sing N N 342 
TYR CA  HA   sing N N 343 
TYR C   O    doub N N 344 
TYR C   OXT  sing N N 345 
TYR CB  CG   sing N N 346 
TYR CB  HB2  sing N N 347 
TYR CB  HB3  sing N N 348 
TYR CG  CD1  doub Y N 349 
TYR CG  CD2  sing Y N 350 
TYR CD1 CE1  sing Y N 351 
TYR CD1 HD1  sing N N 352 
TYR CD2 CE2  doub Y N 353 
TYR CD2 HD2  sing N N 354 
TYR CE1 CZ   doub Y N 355 
TYR CE1 HE1  sing N N 356 
TYR CE2 CZ   sing Y N 357 
TYR CE2 HE2  sing N N 358 
TYR CZ  OH   sing N N 359 
TYR OH  HH   sing N N 360 
TYR OXT HXT  sing N N 361 
VAL N   CA   sing N N 362 
VAL N   H    sing N N 363 
VAL N   H2   sing N N 364 
VAL CA  C    sing N N 365 
VAL CA  CB   sing N N 366 
VAL CA  HA   sing N N 367 
VAL C   O    doub N N 368 
VAL C   OXT  sing N N 369 
VAL CB  CG1  sing N N 370 
VAL CB  CG2  sing N N 371 
VAL CB  HB   sing N N 372 
VAL CG1 HG11 sing N N 373 
VAL CG1 HG12 sing N N 374 
VAL CG1 HG13 sing N N 375 
VAL CG2 HG21 sing N N 376 
VAL CG2 HG22 sing N N 377 
VAL CG2 HG23 sing N N 378 
VAL OXT HXT  sing N N 379 
# 
_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      PDB 
_pdbx_initial_refinement_model.accession_code   6H6M 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9EDQ 
_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]   0.014817 
_atom_sites.fract_transf_matrix[1][2]   0.008555 
_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]   0.017109 
_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]   0.004188 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
MG 
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . GLU A 1 1   ? -1.223  -3.582  26.808  1.00 47.45  ? 226  GLU A N   1 
ATOM   2    C CA  . GLU A 1 1   ? -1.257  -3.646  25.349  1.00 52.05  ? 226  GLU A CA  1 
ATOM   3    C C   . GLU A 1 1   ? -2.368  -4.575  24.864  1.00 44.85  ? 226  GLU A C   1 
ATOM   4    O O   . GLU A 1 1   ? -2.645  -5.592  25.501  1.00 37.63  ? 226  GLU A O   1 
ATOM   5    C CB  . GLU A 1 1   ? 0.099   -4.100  24.808  1.00 56.32  ? 226  GLU A CB  1 
ATOM   6    C CG  . GLU A 1 1   ? 0.760   -5.195  25.628  1.00 44.65  ? 226  GLU A CG  1 
ATOM   7    C CD  . GLU A 1 1   ? 2.261   -5.254  25.407  1.00 54.12  ? 226  GLU A CD  1 
ATOM   8    O OE1 . GLU A 1 1   ? 2.728   -4.817  24.332  1.00 55.93  ? 226  GLU A OE1 1 
ATOM   9    O OE2 . GLU A 1 1   ? 2.976   -5.723  26.317  1.00 39.59  ? 226  GLU A OE2 1 
ATOM   10   N N   . PRO A 1 2   ? -3.008  -4.217  23.747  1.00 36.50  ? 227  PRO A N   1 
ATOM   11   C CA  . PRO A 1 2   ? -4.110  -5.041  23.232  1.00 32.33  ? 227  PRO A CA  1 
ATOM   12   C C   . PRO A 1 2   ? -3.617  -6.415  22.798  1.00 29.54  ? 227  PRO A C   1 
ATOM   13   O O   . PRO A 1 2   ? -2.490  -6.575  22.325  1.00 25.86  ? 227  PRO A O   1 
ATOM   14   C CB  . PRO A 1 2   ? -4.634  -4.232  22.042  1.00 35.56  ? 227  PRO A CB  1 
ATOM   15   C CG  . PRO A 1 2   ? -3.466  -3.417  21.605  1.00 45.98  ? 227  PRO A CG  1 
ATOM   16   C CD  . PRO A 1 2   ? -2.710  -3.077  22.863  1.00 44.81  ? 227  PRO A CD  1 
ATOM   17   N N   . PHE A 1 3   ? -4.484  -7.411  22.972  1.00 24.88  ? 228  PHE A N   1 
ATOM   18   C CA  . PHE A 1 3   ? -4.101  -8.790  22.711  1.00 20.38  ? 228  PHE A CA  1 
ATOM   19   C C   . PHE A 1 3   ? -3.763  -8.996  21.240  1.00 16.79  ? 228  PHE A C   1 
ATOM   20   O O   . PHE A 1 3   ? -4.396  -8.421  20.351  1.00 21.26  ? 228  PHE A O   1 
ATOM   21   C CB  . PHE A 1 3   ? -5.222  -9.746  23.124  1.00 20.14  ? 228  PHE A CB  1 
ATOM   22   C CG  . PHE A 1 3   ? -4.825  -11.192 23.031  1.00 20.36  ? 228  PHE A CG  1 
ATOM   23   C CD1 . PHE A 1 3   ? -4.022  -11.763 24.006  1.00 17.92  ? 228  PHE A CD1 1 
ATOM   24   C CD2 . PHE A 1 3   ? -5.214  -11.966 21.947  1.00 18.26  ? 228  PHE A CD2 1 
ATOM   25   C CE1 . PHE A 1 3   ? -3.632  -13.093 23.911  1.00 20.05  ? 228  PHE A CE1 1 
ATOM   26   C CE2 . PHE A 1 3   ? -4.833  -13.287 21.843  1.00 16.29  ? 228  PHE A CE2 1 
ATOM   27   C CZ  . PHE A 1 3   ? -4.039  -13.858 22.825  1.00 17.91  ? 228  PHE A CZ  1 
ATOM   28   N N   . SER A 1 4   ? -2.755  -9.832  20.994  1.00 16.96  ? 229  SER A N   1 
ATOM   29   C CA  . SER A 1 4   ? -2.350  -10.199 19.646  1.00 19.56  ? 229  SER A CA  1 
ATOM   30   C C   . SER A 1 4   ? -1.649  -11.547 19.704  1.00 15.71  ? 229  SER A C   1 
ATOM   31   O O   . SER A 1 4   ? -1.274  -12.032 20.775  1.00 16.76  ? 229  SER A O   1 
ATOM   32   C CB  . SER A 1 4   ? -1.418  -9.155  19.024  1.00 19.48  ? 229  SER A CB  1 
ATOM   33   O OG  . SER A 1 4   ? -0.134  -9.187  19.639  1.00 18.73  ? 229  SER A OG  1 
ATOM   34   N N   . LEU A 1 5   ? -1.470  -12.144 18.528  1.00 16.90  ? 230  LEU A N   1 
ATOM   35   C CA  . LEU A 1 5   ? -0.655  -13.328 18.328  1.00 18.34  ? 230  LEU A CA  1 
ATOM   36   C C   . LEU A 1 5   ? 0.417   -13.017 17.290  1.00 15.06  ? 230  LEU A C   1 
ATOM   37   O O   . LEU A 1 5   ? 0.219   -12.144 16.442  1.00 18.54  ? 230  LEU A O   1 
ATOM   38   C CB  . LEU A 1 5   ? -1.506  -14.513 17.858  1.00 19.59  ? 230  LEU A CB  1 
ATOM   39   C CG  . LEU A 1 5   ? -2.482  -15.034 18.916  1.00 18.31  ? 230  LEU A CG  1 
ATOM   40   C CD1 . LEU A 1 5   ? -3.465  -16.007 18.296  1.00 17.27  ? 230  LEU A CD1 1 
ATOM   41   C CD2 . LEU A 1 5   ? -1.708  -15.676 20.066  1.00 18.17  ? 230  LEU A CD2 1 
ATOM   42   N N   . PRO A 1 6   ? 1.558   -13.692 17.335  1.00 13.62  ? 231  PRO A N   1 
ATOM   43   C CA  . PRO A 1 6   ? 2.627   -13.379 16.374  1.00 16.41  ? 231  PRO A CA  1 
ATOM   44   C C   . PRO A 1 6   ? 2.235   -13.751 14.952  1.00 20.24  ? 231  PRO A C   1 
ATOM   45   O O   . PRO A 1 6   ? 1.572   -14.765 14.706  1.00 20.63  ? 231  PRO A O   1 
ATOM   46   C CB  . PRO A 1 6   ? 3.815   -14.221 16.862  1.00 17.54  ? 231  PRO A CB  1 
ATOM   47   C CG  . PRO A 1 6   ? 3.218   -15.285 17.736  1.00 15.19  ? 231  PRO A CG  1 
ATOM   48   C CD  . PRO A 1 6   ? 1.947   -14.708 18.323  1.00 13.86  ? 231  PRO A CD  1 
ATOM   49   N N   . ASN A 1 7   ? 2.688   -12.924 14.004  1.00 18.74  ? 232  ASN A N   1 
ATOM   50   C CA  . ASN A 1 7   ? 2.349   -13.076 12.590  1.00 15.48  ? 232  ASN A CA  1 
ATOM   51   C C   . ASN A 1 7   ? 3.237   -14.139 11.932  1.00 20.49  ? 232  ASN A C   1 
ATOM   52   O O   . ASN A 1 7   ? 3.982   -13.881 10.988  1.00 32.22  ? 232  ASN A O   1 
ATOM   53   C CB  . ASN A 1 7   ? 2.489   -11.726 11.893  1.00 15.35  ? 232  ASN A CB  1 
ATOM   54   C CG  . ASN A 1 7   ? 2.134   -11.782 10.421  1.00 45.11  ? 232  ASN A CG  1 
ATOM   55   O OD1 . ASN A 1 7   ? 1.273   -12.554 10.007  1.00 45.74  ? 232  ASN A OD1 1 
ATOM   56   N ND2 . ASN A 1 7   ? 2.814   -10.969 9.619   1.00 46.71  ? 232  ASN A ND2 1 
ATOM   57   N N   . LEU A 1 8   ? 3.182   -15.349 12.485  1.00 16.64  ? 233  LEU A N   1 
ATOM   58   C CA  . LEU A 1 8   ? 3.928   -16.488 11.971  1.00 17.04  ? 233  LEU A CA  1 
ATOM   59   C C   . LEU A 1 8   ? 2.949   -17.541 11.472  1.00 18.34  ? 233  LEU A C   1 
ATOM   60   O O   . LEU A 1 8   ? 1.924   -17.801 12.111  1.00 18.02  ? 233  LEU A O   1 
ATOM   61   C CB  . LEU A 1 8   ? 4.839   -17.105 13.058  1.00 14.49  ? 233  LEU A CB  1 
ATOM   62   C CG  . LEU A 1 8   ? 5.989   -16.247 13.585  1.00 15.71  ? 233  LEU A CG  1 
ATOM   63   C CD1 . LEU A 1 8   ? 6.645   -16.935 14.821  1.00 14.42  ? 233  LEU A CD1 1 
ATOM   64   C CD2 . LEU A 1 8   ? 6.997   -15.992 12.474  1.00 21.58  ? 233  LEU A CD2 1 
ATOM   65   N N   . GLN A 1 9   ? 3.266   -18.146 10.330  1.00 14.64  ? 234  GLN A N   1 
ATOM   66   C CA  . GLN A 1 9   ? 2.501   -19.294 9.873   1.00 13.86  ? 234  GLN A CA  1 
ATOM   67   C C   . GLN A 1 9   ? 2.718   -20.474 10.813  1.00 13.49  ? 234  GLN A C   1 
ATOM   68   O O   . GLN A 1 9   ? 3.742   -20.583 11.483  1.00 14.01  ? 234  GLN A O   1 
ATOM   69   C CB  . GLN A 1 9   ? 2.912   -19.682 8.451   1.00 19.11  ? 234  GLN A CB  1 
ATOM   70   C CG  . GLN A 1 9   ? 2.665   -18.582 7.426   1.00 21.71  ? 234  GLN A CG  1 
ATOM   71   C CD  . GLN A 1 9   ? 3.157   -18.944 6.039   1.00 30.76  ? 234  GLN A CD  1 
ATOM   72   O OE1 . GLN A 1 9   ? 3.703   -20.024 5.813   1.00 27.73  ? 234  GLN A OE1 1 
ATOM   73   N NE2 . GLN A 1 9   ? 2.969   -18.033 5.104   1.00 25.52  ? 234  GLN A NE2 1 
ATOM   74   N N   . THR A 1 10  ? 1.736   -21.377 10.840  1.00 14.32  ? 235  THR A N   1 
ATOM   75   C CA  . THR A 1 10  ? 1.861   -22.568 11.674  1.00 13.59  ? 235  THR A CA  1 
ATOM   76   C C   . THR A 1 10  ? 3.153   -23.321 11.360  1.00 18.44  ? 235  THR A C   1 
ATOM   77   O O   . THR A 1 10  ? 3.866   -23.740 12.272  1.00 14.36  ? 235  THR A O   1 
ATOM   78   C CB  . THR A 1 10  ? 0.641   -23.479 11.499  1.00 13.51  ? 235  THR A CB  1 
ATOM   79   O OG1 . THR A 1 10  ? -0.558  -22.699 11.582  1.00 16.52  ? 235  THR A OG1 1 
ATOM   80   C CG2 . THR A 1 10  ? 0.620   -24.530 12.614  1.00 18.33  ? 235  THR A CG2 1 
ATOM   81   N N   . ASP A 1 11  ? 3.498   -23.465 10.075  1.00 13.66  ? 236  ASP A N   1 
ATOM   82   C CA  . ASP A 1 11  ? 4.721   -24.185 9.731   1.00 11.36  ? 236  ASP A CA  1 
ATOM   83   C C   . ASP A 1 11  ? 5.994   -23.370 9.965   1.00 14.19  ? 236  ASP A C   1 
ATOM   84   O O   . ASP A 1 11  ? 7.089   -23.899 9.740   1.00 14.55  ? 236  ASP A O   1 
ATOM   85   C CB  . ASP A 1 11  ? 4.660   -24.677 8.271   1.00 18.55  ? 236  ASP A CB  1 
ATOM   86   C CG  . ASP A 1 11  ? 4.513   -23.553 7.260   1.00 24.17  ? 236  ASP A CG  1 
ATOM   87   O OD1 . ASP A 1 11  ? 4.617   -22.358 7.618   1.00 19.25  ? 236  ASP A OD1 1 
ATOM   88   O OD2 . ASP A 1 11  ? 4.286   -23.873 6.071   1.00 30.13  ? 236  ASP A OD2 1 
ATOM   89   N N   . GLU A 1 12  ? 5.886   -22.123 10.428  1.00 13.68  ? 237  GLU A N   1 
ATOM   90   C CA  . GLU A 1 12  ? 7.034   -21.332 10.860  1.00 14.30  ? 237  GLU A CA  1 
ATOM   91   C C   . GLU A 1 12  ? 7.227   -21.377 12.367  1.00 12.61  ? 237  GLU A C   1 
ATOM   92   O O   . GLU A 1 12  ? 8.119   -20.699 12.890  1.00 13.93  ? 237  GLU A O   1 
ATOM   93   C CB  . GLU A 1 12  ? 6.888   -19.880 10.384  1.00 13.40  ? 237  GLU A CB  1 
ATOM   94   C CG  . GLU A 1 12  ? 6.902   -19.755 8.856   1.00 14.34  ? 237  GLU A CG  1 
ATOM   95   C CD  . GLU A 1 12  ? 6.539   -18.362 8.353   1.00 23.39  ? 237  GLU A CD  1 
ATOM   96   O OE1 . GLU A 1 12  ? 5.804   -17.626 9.049   1.00 19.20  ? 237  GLU A OE1 1 
ATOM   97   O OE2 . GLU A 1 12  ? 6.988   -18.012 7.238   1.00 26.96  ? 237  GLU A OE2 1 
ATOM   98   N N   . MET A 1 13  ? 6.440   -22.189 13.073  1.00 13.13  ? 238  MET A N   1 
ATOM   99   C CA  . MET A 1 13  ? 6.486   -22.248 14.526  1.00 12.77  ? 238  MET A CA  1 
ATOM   100  C C   . MET A 1 13  ? 6.887   -23.644 14.996  1.00 12.40  ? 238  MET A C   1 
ATOM   101  O O   . MET A 1 13  ? 7.045   -24.589 14.211  1.00 12.04  ? 238  MET A O   1 
ATOM   102  C CB  . MET A 1 13  ? 5.143   -21.817 15.128  1.00 12.77  ? 238  MET A CB  1 
ATOM   103  C CG  . MET A 1 13  ? 4.858   -20.327 14.926  1.00 11.67  ? 238  MET A CG  1 
ATOM   104  S SD  . MET A 1 13  ? 3.405   -19.718 15.823  1.00 14.30  ? 238  MET A SD  1 
ATOM   105  C CE  . MET A 1 13  ? 2.072   -20.414 14.851  1.00 14.69  ? 238  MET A CE  1 
ATOM   106  N N   . SER A 1 14  ? 7.040   -23.757 16.310  1.00 11.93  ? 239  SER A N   1 
ATOM   107  C CA  . SER A 1 14  ? 7.682   -24.890 16.949  1.00 10.08  ? 239  SER A CA  1 
ATOM   108  C C   . SER A 1 14  ? 6.744   -25.534 17.957  1.00 11.05  ? 239  SER A C   1 
ATOM   109  O O   . SER A 1 14  ? 5.938   -24.857 18.602  1.00 12.13  ? 239  SER A O   1 
ATOM   110  C CB  . SER A 1 14  ? 8.943   -24.437 17.683  1.00 10.88  ? 239  SER A CB  1 
ATOM   111  O OG  . SER A 1 14  ? 9.768   -23.654 16.833  1.00 15.94  ? 239  SER A OG  1 
ATOM   112  N N   . SER A 1 15  ? 6.875   -26.848 18.113  1.00 10.83  ? 240  SER A N   1 
ATOM   113  C CA  . SER A 1 15  ? 6.172   -27.519 19.196  1.00 11.10  ? 240  SER A CA  1 
ATOM   114  C C   . SER A 1 15  ? 6.724   -27.081 20.553  1.00 12.79  ? 240  SER A C   1 
ATOM   115  O O   . SER A 1 15  ? 7.923   -26.818 20.715  1.00 13.72  ? 240  SER A O   1 
ATOM   116  C CB  . SER A 1 15  ? 6.292   -29.038 19.042  1.00 13.25  ? 240  SER A CB  1 
ATOM   117  O OG  . SER A 1 15  ? 5.825   -29.714 20.199  1.00 12.30  ? 240  SER A OG  1 
ATOM   118  N N   . SER A 1 16  ? 5.827   -27.004 21.540  1.00 12.32  ? 241  SER A N   1 
ATOM   119  C CA  . SER A 1 16  ? 6.197   -26.731 22.920  1.00 10.97  ? 241  SER A CA  1 
ATOM   120  C C   . SER A 1 16  ? 6.224   -27.995 23.771  1.00 10.92  ? 241  SER A C   1 
ATOM   121  O O   . SER A 1 16  ? 6.465   -27.913 24.976  1.00 13.49  ? 241  SER A O   1 
ATOM   122  C CB  . SER A 1 16  ? 5.239   -25.704 23.531  1.00 10.42  ? 241  SER A CB  1 
ATOM   123  O OG  . SER A 1 16  ? 3.906   -26.176 23.451  1.00 10.72  ? 241  SER A OG  1 
ATOM   124  N N   . ARG A 1 17  ? 6.008   -29.170 23.167  1.00 10.86  ? 242  ARG A N   1 
ATOM   125  C CA  . ARG A 1 17  ? 6.177   -30.425 23.893  1.00 10.36  ? 242  ARG A CA  1 
ATOM   126  C C   . ARG A 1 17  ? 7.273   -31.323 23.327  1.00 12.71  ? 242  ARG A C   1 
ATOM   127  O O   . ARG A 1 17  ? 7.668   -32.272 24.004  1.00 13.09  ? 242  ARG A O   1 
ATOM   128  C CB  . ARG A 1 17  ? 4.852   -31.208 23.954  1.00 13.85  ? 242  ARG A CB  1 
ATOM   129  C CG  . ARG A 1 17  ? 3.832   -30.600 24.927  1.00 11.55  ? 242  ARG A CG  1 
ATOM   130  C CD  . ARG A 1 17  ? 2.587   -31.467 25.115  1.00 11.50  ? 242  ARG A CD  1 
ATOM   131  N NE  . ARG A 1 17  ? 2.865   -32.735 25.785  1.00 11.78  ? 242  ARG A NE  1 
ATOM   132  C CZ  . ARG A 1 17  ? 2.513   -33.923 25.307  1.00 12.18  ? 242  ARG A CZ  1 
ATOM   133  N NH1 . ARG A 1 17  ? 1.874   -34.048 24.151  1.00 13.29  ? 242  ARG A NH1 1 
ATOM   134  N NH2 . ARG A 1 17  ? 2.771   -35.014 26.026  1.00 13.46  ? 242  ARG A NH2 1 
ATOM   135  N N   . TRP A 1 18  ? 7.813   -31.031 22.143  1.00 10.64  ? 243  TRP A N   1 
ATOM   136  C CA  . TRP A 1 18  ? 8.962   -31.759 21.627  1.00 12.75  ? 243  TRP A CA  1 
ATOM   137  C C   . TRP A 1 18  ? 9.699   -30.769 20.735  1.00 10.88  ? 243  TRP A C   1 
ATOM   138  O O   . TRP A 1 18  ? 9.072   -30.176 19.845  1.00 17.06  ? 243  TRP A O   1 
ATOM   139  C CB  . TRP A 1 18  ? 8.588   -33.013 20.826  1.00 10.94  ? 243  TRP A CB  1 
ATOM   140  C CG  . TRP A 1 18  ? 9.791   -33.883 20.573  1.00 11.14  ? 243  TRP A CG  1 
ATOM   141  C CD1 . TRP A 1 18  ? 10.618  -33.834 19.498  1.00 13.37  ? 243  TRP A CD1 1 
ATOM   142  C CD2 . TRP A 1 18  ? 10.315  -34.894 21.444  1.00 10.43  ? 243  TRP A CD2 1 
ATOM   143  N NE1 . TRP A 1 18  ? 11.629  -34.763 19.629  1.00 14.36  ? 243  TRP A NE1 1 
ATOM   144  C CE2 . TRP A 1 18  ? 11.459  -35.433 20.815  1.00 9.88   ? 243  TRP A CE2 1 
ATOM   145  C CE3 . TRP A 1 18  ? 9.917   -35.412 22.687  1.00 12.18  ? 243  TRP A CE3 1 
ATOM   146  C CZ2 . TRP A 1 18  ? 12.225  -36.455 21.394  1.00 10.12  ? 243  TRP A CZ2 1 
ATOM   147  C CZ3 . TRP A 1 18  ? 10.671  -36.423 23.262  1.00 14.21  ? 243  TRP A CZ3 1 
ATOM   148  C CH2 . TRP A 1 18  ? 11.819  -36.932 22.618  1.00 14.10  ? 243  TRP A CH2 1 
ATOM   149  N N   . PRO A 1 19  ? 10.989  -30.552 20.943  1.00 11.55  ? 244  PRO A N   1 
ATOM   150  C CA  . PRO A 1 19  ? 11.684  -29.535 20.144  1.00 14.66  ? 244  PRO A CA  1 
ATOM   151  C C   . PRO A 1 19  ? 11.783  -29.950 18.689  1.00 20.89  ? 244  PRO A C   1 
ATOM   152  O O   . PRO A 1 19  ? 12.617  -30.787 18.328  1.00 20.13  ? 244  PRO A O   1 
ATOM   153  C CB  . PRO A 1 19  ? 13.070  -29.439 20.802  1.00 16.37  ? 244  PRO A CB  1 
ATOM   154  C CG  . PRO A 1 19  ? 12.961  -30.186 22.117  1.00 18.69  ? 244  PRO A CG  1 
ATOM   155  C CD  . PRO A 1 19  ? 11.892  -31.235 21.886  1.00 12.35  ? 244  PRO A CD  1 
ATOM   156  N N   . ASN A 1 20  ? 10.915  -29.390 17.858  1.00 11.59  ? 245  ASN A N   1 
ATOM   157  C CA  . ASN A 1 20  ? 10.901  -29.667 16.429  1.00 10.23  ? 245  ASN A CA  1 
ATOM   158  C C   . ASN A 1 20  ? 9.877   -28.740 15.782  1.00 14.73  ? 245  ASN A C   1 
ATOM   159  O O   . ASN A 1 20  ? 8.982   -28.231 16.466  1.00 13.08  ? 245  ASN A O   1 
ATOM   160  C CB  . ASN A 1 20  ? 10.544  -31.138 16.140  1.00 16.72  ? 245  ASN A CB  1 
ATOM   161  C CG  . ASN A 1 20  ? 11.756  -31.963 15.736  1.00 20.15  ? 245  ASN A CG  1 
ATOM   162  O OD1 . ASN A 1 20  ? 12.780  -31.416 15.335  1.00 18.55  ? 245  ASN A OD1 1 
ATOM   163  N ND2 . ASN A 1 20  ? 11.642  -33.287 15.840  1.00 20.05  ? 245  ASN A ND2 1 
ATOM   164  N N   . PRO A 1 21  ? 9.987   -28.506 14.475  1.00 13.15  ? 246  PRO A N   1 
ATOM   165  C CA  . PRO A 1 21  ? 8.994   -27.664 13.795  1.00 10.40  ? 246  PRO A CA  1 
ATOM   166  C C   . PRO A 1 21  ? 7.622   -28.310 13.786  1.00 13.54  ? 246  PRO A C   1 
ATOM   167  O O   . PRO A 1 21  ? 7.480   -29.525 13.641  1.00 15.21  ? 246  PRO A O   1 
ATOM   168  C CB  . PRO A 1 21  ? 9.533   -27.548 12.358  1.00 13.34  ? 246  PRO A CB  1 
ATOM   169  C CG  . PRO A 1 21  ? 10.951  -27.991 12.435  1.00 20.30  ? 246  PRO A CG  1 
ATOM   170  C CD  . PRO A 1 21  ? 11.056  -28.954 13.565  1.00 14.77  ? 246  PRO A CD  1 
ATOM   171  N N   . LEU A 1 22  ? 6.597   -27.473 13.896  1.00 12.51  ? 247  LEU A N   1 
ATOM   172  C CA  . LEU A 1 22  ? 5.242   -27.986 13.726  1.00 13.02  ? 247  LEU A CA  1 
ATOM   173  C C   . LEU A 1 22  ? 5.067   -28.521 12.313  1.00 16.24  ? 247  LEU A C   1 
ATOM   174  O O   . LEU A 1 22  ? 5.471   -27.881 11.339  1.00 16.73  ? 247  LEU A O   1 
ATOM   175  C CB  . LEU A 1 22  ? 4.209   -26.895 13.994  1.00 13.39  ? 247  LEU A CB  1 
ATOM   176  C CG  . LEU A 1 22  ? 4.202   -26.395 15.435  1.00 11.22  ? 247  LEU A CG  1 
ATOM   177  C CD1 . LEU A 1 22  ? 3.184   -25.264 15.598  1.00 14.54  ? 247  LEU A CD1 1 
ATOM   178  C CD2 . LEU A 1 22  ? 3.918   -27.543 16.392  1.00 13.47  ? 247  LEU A CD2 1 
ATOM   179  N N   . ALA A 1 23  ? 4.452   -29.704 12.208  1.00 12.25  ? 248  ALA A N   1 
ATOM   180  C CA  . ALA A 1 23  ? 4.218   -30.341 10.916  1.00 16.65  ? 248  ALA A CA  1 
ATOM   181  C C   . ALA A 1 23  ? 2.752   -30.597 10.602  1.00 18.04  ? 248  ALA A C   1 
ATOM   182  O O   . ALA A 1 23  ? 2.412   -30.730 9.418   1.00 18.74  ? 248  ALA A O   1 
ATOM   183  C CB  . ALA A 1 23  ? 4.973   -31.679 10.829  1.00 19.39  ? 248  ALA A CB  1 
ATOM   184  N N   A THR A 1 24  ? 1.882   -30.700 11.606  0.66 16.18  ? 249  THR A N   1 
ATOM   185  N N   B THR A 1 24  ? 1.878   -30.649 11.605  0.34 16.19  ? 249  THR A N   1 
ATOM   186  C CA  A THR A 1 24  ? 0.461   -30.906 11.364  0.66 15.08  ? 249  THR A CA  1 
ATOM   187  C CA  B THR A 1 24  ? 0.469   -30.926 11.382  0.34 15.10  ? 249  THR A CA  1 
ATOM   188  C C   A THR A 1 24  ? -0.351  -29.995 12.270  0.66 16.95  ? 249  THR A C   1 
ATOM   189  C C   B THR A 1 24  ? -0.377  -30.063 12.307  0.34 16.91  ? 249  THR A C   1 
ATOM   190  O O   A THR A 1 24  ? 0.124   -29.506 13.302  0.66 15.30  ? 249  THR A O   1 
ATOM   191  O O   B THR A 1 24  ? 0.056   -29.673 13.396  0.34 15.78  ? 249  THR A O   1 
ATOM   192  C CB  A THR A 1 24  ? 0.016   -32.371 11.570  0.66 17.18  ? 249  THR A CB  1 
ATOM   193  C CB  B THR A 1 24  ? 0.140   -32.410 11.600  0.34 17.19  ? 249  THR A CB  1 
ATOM   194  O OG1 A THR A 1 24  ? 0.345   -32.813 12.894  0.66 15.96  ? 249  THR A OG1 1 
ATOM   195  O OG1 B THR A 1 24  ? 1.125   -33.216 10.945  0.34 26.68  ? 249  THR A OG1 1 
ATOM   196  C CG2 A THR A 1 24  ? 0.659   -33.283 10.537  0.66 23.90  ? 249  THR A CG2 1 
ATOM   197  C CG2 B THR A 1 24  ? -1.225  -32.740 11.021  0.34 13.09  ? 249  THR A CG2 1 
ATOM   198  N N   . LEU A 1 25  ? -1.589  -29.764 11.847  1.00 16.47  ? 250  LEU A N   1 
ATOM   199  C CA  . LEU A 1 25  ? -2.563  -28.980 12.595  1.00 14.60  ? 250  LEU A CA  1 
ATOM   200  C C   . LEU A 1 25  ? -3.879  -29.716 12.425  1.00 17.30  ? 250  LEU A C   1 
ATOM   201  O O   . LEU A 1 25  ? -4.379  -29.826 11.302  1.00 17.93  ? 250  LEU A O   1 
ATOM   202  C CB  . LEU A 1 25  ? -2.644  -27.552 12.052  1.00 17.33  ? 250  LEU A CB  1 
ATOM   203  C CG  . LEU A 1 25  ? -3.669  -26.613 12.685  1.00 17.13  ? 250  LEU A CG  1 
ATOM   204  C CD1 . LEU A 1 25  ? -3.271  -26.347 14.131  1.00 17.68  ? 250  LEU A CD1 1 
ATOM   205  C CD2 . LEU A 1 25  ? -3.720  -25.313 11.891  1.00 17.32  ? 250  LEU A CD2 1 
ATOM   206  N N   . PHE A 1 26  ? -4.426  -30.268 13.505  1.00 15.81  ? 251  PHE A N   1 
ATOM   207  C CA  . PHE A 1 26  ? -5.566  -31.150 13.312  1.00 16.26  ? 251  PHE A CA  1 
ATOM   208  C C   . PHE A 1 26  ? -6.433  -31.174 14.563  1.00 17.59  ? 251  PHE A C   1 
ATOM   209  O O   . PHE A 1 26  ? -6.004  -30.789 15.657  1.00 16.36  ? 251  PHE A O   1 
ATOM   210  C CB  . PHE A 1 26  ? -5.107  -32.567 12.933  1.00 20.00  ? 251  PHE A CB  1 
ATOM   211  C CG  . PHE A 1 26  ? -4.364  -33.283 14.026  1.00 18.14  ? 251  PHE A CG  1 
ATOM   212  C CD1 . PHE A 1 26  ? -3.019  -33.016 14.263  1.00 22.46  ? 251  PHE A CD1 1 
ATOM   213  C CD2 . PHE A 1 26  ? -5.005  -34.233 14.813  1.00 16.83  ? 251  PHE A CD2 1 
ATOM   214  C CE1 . PHE A 1 26  ? -2.326  -33.678 15.274  1.00 18.07  ? 251  PHE A CE1 1 
ATOM   215  C CE2 . PHE A 1 26  ? -4.317  -34.892 15.821  1.00 22.04  ? 251  PHE A CE2 1 
ATOM   216  C CZ  . PHE A 1 26  ? -2.976  -34.617 16.047  1.00 17.10  ? 251  PHE A CZ  1 
ATOM   217  N N   . ALA A 1 27  ? -7.674  -31.617 14.374  1.00 19.34  ? 252  ALA A N   1 
ATOM   218  C CA  . ALA A 1 27  ? -8.618  -31.818 15.463  1.00 20.36  ? 252  ALA A CA  1 
ATOM   219  C C   . ALA A 1 27  ? -9.111  -33.251 15.382  1.00 21.45  ? 252  ALA A C   1 
ATOM   220  O O   . ALA A 1 27  ? -9.608  -33.672 14.333  1.00 22.36  ? 252  ALA A O   1 
ATOM   221  C CB  . ALA A 1 27  ? -9.789  -30.838 15.370  1.00 21.32  ? 252  ALA A CB  1 
ATOM   222  N N   . ASP A 1 28  ? -8.963  -33.997 16.475  1.00 21.68  ? 253  ASP A N   1 
ATOM   223  C CA  . ASP A 1 28  ? -9.411  -35.390 16.544  1.00 20.05  ? 253  ASP A CA  1 
ATOM   224  C C   . ASP A 1 28  ? -10.462 -35.527 17.635  1.00 19.62  ? 253  ASP A C   1 
ATOM   225  O O   . ASP A 1 28  ? -10.121 -35.593 18.831  1.00 23.06  ? 253  ASP A O   1 
ATOM   226  C CB  . ASP A 1 28  ? -8.243  -36.343 16.805  1.00 24.29  ? 253  ASP A CB  1 
ATOM   227  C CG  . ASP A 1 28  ? -8.636  -37.822 16.636  1.00 23.31  ? 253  ASP A CG  1 
ATOM   228  O OD1 . ASP A 1 28  ? -9.843  -38.145 16.708  1.00 35.09  ? 253  ASP A OD1 1 
ATOM   229  O OD2 . ASP A 1 28  ? -7.726  -38.654 16.442  1.00 44.62  ? 253  ASP A OD2 1 
ATOM   230  N N   . PRO A 1 29  ? -11.743 -35.606 17.278  1.00 24.42  ? 254  PRO A N   1 
ATOM   231  C CA  . PRO A 1 29  ? -12.798 -35.664 18.295  1.00 24.30  ? 254  PRO A CA  1 
ATOM   232  C C   . PRO A 1 29  ? -12.976 -37.027 18.945  1.00 29.55  ? 254  PRO A C   1 
ATOM   233  O O   . PRO A 1 29  ? -13.805 -37.146 19.852  1.00 32.34  ? 254  PRO A O   1 
ATOM   234  C CB  . PRO A 1 29  ? -14.051 -35.275 17.503  1.00 26.48  ? 254  PRO A CB  1 
ATOM   235  C CG  . PRO A 1 29  ? -13.778 -35.788 16.115  1.00 25.58  ? 254  PRO A CG  1 
ATOM   236  C CD  . PRO A 1 29  ? -12.276 -35.654 15.905  1.00 23.85  ? 254  PRO A CD  1 
ATOM   237  N N   . ASN A 1 30  ? -12.232 -38.052 18.522  1.00 22.07  ? 255  ASN A N   1 
ATOM   238  C CA  . ASN A 1 30  ? -12.418 -39.409 19.026  1.00 26.00  ? 255  ASN A CA  1 
ATOM   239  C C   . ASN A 1 30  ? -11.220 -39.921 19.821  1.00 28.09  ? 255  ASN A C   1 
ATOM   240  O O   . ASN A 1 30  ? -10.958 -41.126 19.843  1.00 36.31  ? 255  ASN A O   1 
ATOM   241  C CB  . ASN A 1 30  ? -12.714 -40.373 17.882  1.00 27.98  ? 255  ASN A CB  1 
ATOM   242  C CG  . ASN A 1 30  ? -13.927 -39.972 17.089  1.00 31.84  ? 255  ASN A CG  1 
ATOM   243  O OD1 . ASN A 1 30  ? -13.878 -39.892 15.862  1.00 46.03  ? 255  ASN A OD1 1 
ATOM   244  N ND2 . ASN A 1 30  ? -15.023 -39.705 17.781  1.00 29.65  ? 255  ASN A ND2 1 
ATOM   245  N N   . VAL A 1 31  ? -10.485 -39.036 20.477  1.00 27.07  ? 256  VAL A N   1 
ATOM   246  C CA  . VAL A 1 31  ? -9.397  -39.480 21.339  1.00 27.57  ? 256  VAL A CA  1 
ATOM   247  C C   . VAL A 1 31  ? -9.986  -40.027 22.630  1.00 29.88  ? 256  VAL A C   1 
ATOM   248  O O   . VAL A 1 31  ? -10.990 -39.516 23.138  1.00 33.98  ? 256  VAL A O   1 
ATOM   249  C CB  . VAL A 1 31  ? -8.406  -38.330 21.590  1.00 19.67  ? 256  VAL A CB  1 
ATOM   250  C CG1 . VAL A 1 31  ? -7.240  -38.804 22.447  1.00 29.26  ? 256  VAL A CG1 1 
ATOM   251  C CG2 . VAL A 1 31  ? -7.898  -37.807 20.259  1.00 23.84  ? 256  VAL A CG2 1 
ATOM   252  N N   . ALA A 1 32  ? -9.362  -41.085 23.162  1.00 30.68  ? 257  ALA A N   1 
ATOM   253  C CA  . ALA A 1 32  ? -9.980  -41.849 24.242  1.00 32.62  ? 257  ALA A CA  1 
ATOM   254  C C   . ALA A 1 32  ? -10.154 -41.011 25.504  1.00 29.39  ? 257  ALA A C   1 
ATOM   255  O O   . ALA A 1 32  ? -11.198 -41.083 26.161  1.00 38.60  ? 257  ALA A O   1 
ATOM   256  C CB  . ALA A 1 32  ? -9.156  -43.102 24.539  1.00 39.94  ? 257  ALA A CB  1 
ATOM   257  N N   . VAL A 1 33  ? -9.154  -40.205 25.859  1.00 31.85  ? 258  VAL A N   1 
ATOM   258  C CA  . VAL A 1 33  ? -9.197  -39.447 27.102  1.00 29.70  ? 258  VAL A CA  1 
ATOM   259  C C   . VAL A 1 33  ? -8.578  -38.071 26.863  1.00 21.51  ? 258  VAL A C   1 
ATOM   260  O O   . VAL A 1 33  ? -7.803  -37.866 25.924  1.00 28.82  ? 258  VAL A O   1 
ATOM   261  C CB  . VAL A 1 33  ? -8.499  -40.231 28.245  1.00 46.58  ? 258  VAL A CB  1 
ATOM   262  C CG1 . VAL A 1 33  ? -7.154  -40.774 27.783  1.00 44.28  ? 258  VAL A CG1 1 
ATOM   263  C CG2 . VAL A 1 33  ? -8.388  -39.414 29.538  1.00 41.09  ? 258  VAL A CG2 1 
ATOM   264  N N   . ALA A 1 34  ? -9.002  -37.107 27.680  1.00 22.43  ? 259  ALA A N   1 
ATOM   265  C CA  . ALA A 1 34  ? -8.493  -35.750 27.567  1.00 21.82  ? 259  ALA A CA  1 
ATOM   266  C C   . ALA A 1 34  ? -7.021  -35.704 27.968  1.00 21.34  ? 259  ALA A C   1 
ATOM   267  O O   . ALA A 1 34  ? -6.600  -36.404 28.893  1.00 20.79  ? 259  ALA A O   1 
ATOM   268  C CB  . ALA A 1 34  ? -9.301  -34.795 28.450  1.00 24.06  ? 259  ALA A CB  1 
ATOM   269  N N   . PRO A 1 35  ? -6.217  -34.897 27.297  1.00 15.03  ? 260  PRO A N   1 
ATOM   270  C CA  . PRO A 1 35  ? -4.800  -34.822 27.648  1.00 13.56  ? 260  PRO A CA  1 
ATOM   271  C C   . PRO A 1 35  ? -4.593  -33.965 28.883  1.00 16.74  ? 260  PRO A C   1 
ATOM   272  O O   . PRO A 1 35  ? -5.356  -33.037 29.162  1.00 15.46  ? 260  PRO A O   1 
ATOM   273  C CB  . PRO A 1 35  ? -4.173  -34.167 26.415  1.00 18.81  ? 260  PRO A CB  1 
ATOM   274  C CG  . PRO A 1 35  ? -5.258  -33.254 25.924  1.00 17.11  ? 260  PRO A CG  1 
ATOM   275  C CD  . PRO A 1 35  ? -6.559  -33.990 26.185  1.00 19.34  ? 260  PRO A CD  1 
ATOM   276  N N   . GLN A 1 36  ? -3.546  -34.294 29.628  1.00 14.13  ? 261  GLN A N   1 
ATOM   277  C CA  . GLN A 1 36  ? -3.142  -33.526 30.810  1.00 15.01  ? 261  GLN A CA  1 
ATOM   278  C C   . GLN A 1 36  ? -1.665  -33.153 30.714  1.00 12.68  ? 261  GLN A C   1 
ATOM   279  O O   . GLN A 1 36  ? -0.886  -33.301 31.661  1.00 15.97  ? 261  GLN A O   1 
ATOM   280  C CB  . GLN A 1 36  ? -3.438  -34.281 32.108  1.00 19.56  ? 261  GLN A CB  1 
ATOM   281  C CG  . GLN A 1 36  ? -3.427  -33.371 33.322  1.00 19.26  ? 261  GLN A CG  1 
ATOM   282  C CD  . GLN A 1 36  ? -3.816  -34.064 34.614  1.00 18.61  ? 261  GLN A CD  1 
ATOM   283  O OE1 . GLN A 1 36  ? -4.130  -35.258 34.635  1.00 21.28  ? 261  GLN A OE1 1 
ATOM   284  N NE2 . GLN A 1 36  ? -3.811  -33.306 35.706  1.00 18.84  ? 261  GLN A NE2 1 
ATOM   285  N N   . TRP A 1 37  ? -1.284  -32.637 29.539  1.00 13.53  ? 262  TRP A N   1 
ATOM   286  C CA  . TRP A 1 37  ? 0.086   -32.223 29.254  1.00 12.82  ? 262  TRP A CA  1 
ATOM   287  C C   . TRP A 1 37  ? 0.605   -31.266 30.319  1.00 11.89  ? 262  TRP A C   1 
ATOM   288  O O   . TRP A 1 37  ? -0.120  -30.393 30.809  1.00 14.80  ? 262  TRP A O   1 
ATOM   289  C CB  . TRP A 1 37  ? 0.143   -31.555 27.868  1.00 13.09  ? 262  TRP A CB  1 
ATOM   290  C CG  . TRP A 1 37  ? -0.396  -32.442 26.762  1.00 14.37  ? 262  TRP A CG  1 
ATOM   291  C CD1 . TRP A 1 37  ? -0.340  -33.812 26.709  1.00 14.06  ? 262  TRP A CD1 1 
ATOM   292  C CD2 . TRP A 1 37  ? -1.086  -32.025 25.572  1.00 12.32  ? 262  TRP A CD2 1 
ATOM   293  N NE1 . TRP A 1 37  ? -0.953  -34.266 25.561  1.00 15.32  ? 262  TRP A NE1 1 
ATOM   294  C CE2 . TRP A 1 37  ? -1.415  -33.191 24.846  1.00 13.88  ? 262  TRP A CE2 1 
ATOM   295  C CE3 . TRP A 1 37  ? -1.466  -30.781 25.053  1.00 13.41  ? 262  TRP A CE3 1 
ATOM   296  C CZ2 . TRP A 1 37  ? -2.093  -33.149 23.622  1.00 18.00  ? 262  TRP A CZ2 1 
ATOM   297  C CZ3 . TRP A 1 37  ? -2.148  -30.745 23.833  1.00 13.12  ? 262  TRP A CZ3 1 
ATOM   298  C CH2 . TRP A 1 37  ? -2.451  -31.920 23.138  1.00 14.92  ? 262  TRP A CH2 1 
ATOM   299  N N   . GLN A 1 38  ? 1.864   -31.458 30.703  1.00 10.97  ? 263  GLN A N   1 
ATOM   300  C CA  . GLN A 1 38  ? 2.485   -30.581 31.680  1.00 14.88  ? 263  GLN A CA  1 
ATOM   301  C C   . GLN A 1 38  ? 3.430   -29.573 31.054  1.00 10.41  ? 263  GLN A C   1 
ATOM   302  O O   . GLN A 1 38  ? 3.759   -28.581 31.709  1.00 10.90  ? 263  GLN A O   1 
ATOM   303  C CB  . GLN A 1 38  ? 3.249   -31.396 32.731  1.00 12.23  ? 263  GLN A CB  1 
ATOM   304  C CG  . GLN A 1 38  ? 2.329   -32.299 33.543  1.00 13.77  ? 263  GLN A CG  1 
ATOM   305  C CD  . GLN A 1 38  ? 1.235   -31.509 34.252  1.00 13.93  ? 263  GLN A CD  1 
ATOM   306  O OE1 . GLN A 1 38  ? 1.520   -30.639 35.081  1.00 12.58  ? 263  GLN A OE1 1 
ATOM   307  N NE2 . GLN A 1 38  ? -0.019  -31.809 33.932  1.00 12.86  ? 263  GLN A NE2 1 
ATOM   308  N N   . ASN A 1 39  ? 3.876   -29.808 29.821  1.00 10.20  ? 264  ASN A N   1 
ATOM   309  C CA  . ASN A 1 39  ? 4.635   -28.828 29.058  1.00 10.73  ? 264  ASN A CA  1 
ATOM   310  C C   . ASN A 1 39  ? 3.734   -28.180 28.008  1.00 12.21  ? 264  ASN A C   1 
ATOM   311  O O   . ASN A 1 39  ? 2.682   -28.708 27.651  1.00 13.59  ? 264  ASN A O   1 
ATOM   312  C CB  . ASN A 1 39  ? 5.841   -29.491 28.390  1.00 12.74  ? 264  ASN A CB  1 
ATOM   313  C CG  . ASN A 1 39  ? 6.879   -29.937 29.402  1.00 13.16  ? 264  ASN A CG  1 
ATOM   314  O OD1 . ASN A 1 39  ? 7.128   -29.235 30.374  1.00 13.14  ? 264  ASN A OD1 1 
ATOM   315  N ND2 . ASN A 1 39  ? 7.476   -31.102 29.184  1.00 13.43  ? 264  ASN A ND2 1 
ATOM   316  N N   . GLY A 1 40  ? 4.162   -27.016 27.517  1.00 10.35  ? 265  GLY A N   1 
ATOM   317  C CA  . GLY A 1 40  ? 3.362   -26.298 26.543  1.00 12.80  ? 265  GLY A CA  1 
ATOM   318  C C   . GLY A 1 40  ? 2.101   -25.691 27.118  1.00 14.95  ? 265  GLY A C   1 
ATOM   319  O O   . GLY A 1 40  ? 1.102   -25.567 26.404  1.00 13.37  ? 265  GLY A O   1 
ATOM   320  N N   . ARG A 1 41  ? 2.120   -25.312 28.397  1.00 11.50  ? 266  ARG A N   1 
ATOM   321  C CA  . ARG A 1 41  ? 0.937   -24.822 29.095  1.00 10.72  ? 266  ARG A CA  1 
ATOM   322  C C   . ARG A 1 41  ? 1.218   -23.420 29.619  1.00 13.17  ? 266  ARG A C   1 
ATOM   323  O O   . ARG A 1 41  ? 2.164   -23.220 30.391  1.00 13.03  ? 266  ARG A O   1 
ATOM   324  C CB  . ARG A 1 41  ? 0.560   -25.748 30.262  1.00 13.22  ? 266  ARG A CB  1 
ATOM   325  C CG  . ARG A 1 41  ? 0.343   -27.223 29.883  1.00 15.81  ? 266  ARG A CG  1 
ATOM   326  C CD  . ARG A 1 41  ? -0.944  -27.432 29.100  1.00 14.87  ? 266  ARG A CD  1 
ATOM   327  N NE  . ARG A 1 41  ? -2.129  -26.985 29.830  1.00 14.48  ? 266  ARG A NE  1 
ATOM   328  C CZ  . ARG A 1 41  ? -2.853  -27.743 30.639  1.00 15.78  ? 266  ARG A CZ  1 
ATOM   329  N NH1 . ARG A 1 41  ? -2.521  -29.002 30.891  1.00 15.56  ? 266  ARG A NH1 1 
ATOM   330  N NH2 . ARG A 1 41  ? -3.943  -27.226 31.206  1.00 16.73  ? 266  ARG A NH2 1 
ATOM   331  N N   . CYS A 1 42  ? 0.376   -22.464 29.231  1.00 14.12  ? 267  CYS A N   1 
ATOM   332  C CA  . CYS A 1 42  ? 0.571   -21.069 29.611  1.00 13.03  ? 267  CYS A CA  1 
ATOM   333  C C   . CYS A 1 42  ? -0.760  -20.348 29.448  1.00 16.59  ? 267  CYS A C   1 
ATOM   334  O O   . CYS A 1 42  ? -1.468  -20.587 28.468  1.00 13.56  ? 267  CYS A O   1 
ATOM   335  C CB  . CYS A 1 42  ? 1.641   -20.407 28.732  1.00 13.15  ? 267  CYS A CB  1 
ATOM   336  S SG  . CYS A 1 42  ? 2.172   -18.747 29.251  1.00 14.74  ? 267  CYS A SG  1 
ATOM   337  N N   . THR A 1 43  ? -1.103  -19.479 30.400  1.00 11.87  ? 268  THR A N   1 
ATOM   338  C CA  . THR A 1 43  ? -2.308  -18.674 30.238  1.00 12.38  ? 268  THR A CA  1 
ATOM   339  C C   . THR A 1 43  ? -2.027  -17.492 29.309  1.00 14.89  ? 268  THR A C   1 
ATOM   340  O O   . THR A 1 43  ? -0.876  -17.135 29.049  1.00 15.22  ? 268  THR A O   1 
ATOM   341  C CB  . THR A 1 43  ? -2.809  -18.146 31.582  1.00 15.20  ? 268  THR A CB  1 
ATOM   342  O OG1 . THR A 1 43  ? -1.891  -17.144 32.057  1.00 15.43  ? 268  THR A OG1 1 
ATOM   343  C CG2 . THR A 1 43  ? -2.914  -19.274 32.600  1.00 13.85  ? 268  THR A CG2 1 
ATOM   344  N N   . LEU A 1 44  ? -3.101  -16.860 28.828  1.00 15.99  ? 269  LEU A N   1 
ATOM   345  C CA  . LEU A 1 44  ? -2.928  -15.732 27.918  1.00 14.67  ? 269  LEU A CA  1 
ATOM   346  C C   . LEU A 1 44  ? -2.245  -14.562 28.608  1.00 16.85  ? 269  LEU A C   1 
ATOM   347  O O   . LEU A 1 44  ? -1.579  -13.753 27.945  1.00 17.22  ? 269  LEU A O   1 
ATOM   348  C CB  . LEU A 1 44  ? -4.279  -15.300 27.346  1.00 16.23  ? 269  LEU A CB  1 
ATOM   349  C CG  . LEU A 1 44  ? -5.071  -16.415 26.659  1.00 22.24  ? 269  LEU A CG  1 
ATOM   350  C CD1 . LEU A 1 44  ? -6.272  -15.853 25.888  1.00 19.07  ? 269  LEU A CD1 1 
ATOM   351  C CD2 . LEU A 1 44  ? -4.194  -17.275 25.760  1.00 20.15  ? 269  LEU A CD2 1 
ATOM   352  N N   . GLU A 1 45  ? -2.388  -14.463 29.928  1.00 17.89  ? 270  GLU A N   1 
ATOM   353  C CA  . GLU A 1 45  ? -1.738  -13.427 30.720  1.00 16.16  ? 270  GLU A CA  1 
ATOM   354  C C   . GLU A 1 45  ? -0.299  -13.785 31.105  1.00 18.72  ? 270  GLU A C   1 
ATOM   355  O O   . GLU A 1 45  ? 0.286   -13.097 31.948  1.00 23.51  ? 270  GLU A O   1 
ATOM   356  C CB  . GLU A 1 45  ? -2.574  -13.127 31.972  1.00 19.44  ? 270  GLU A CB  1 
ATOM   357  C CG  . GLU A 1 45  ? -4.000  -12.662 31.634  1.00 17.18  ? 270  GLU A CG  1 
ATOM   358  C CD  . GLU A 1 45  ? -4.763  -12.117 32.831  1.00 20.79  ? 270  GLU A CD  1 
ATOM   359  O OE1 . GLU A 1 45  ? -4.341  -12.350 33.986  1.00 34.54  ? 270  GLU A OE1 1 
ATOM   360  O OE2 . GLU A 1 45  ? -5.788  -11.445 32.611  1.00 24.24  ? 270  GLU A OE2 1 
ATOM   361  N N   . GLY A 1 46  ? 0.279   -14.831 30.508  1.00 16.00  ? 271  GLY A N   1 
ATOM   362  C CA  . GLY A 1 46  ? 1.693   -15.126 30.672  1.00 12.24  ? 271  GLY A CA  1 
ATOM   363  C C   . GLY A 1 46  ? 2.069   -15.918 31.900  1.00 16.55  ? 271  GLY A C   1 
ATOM   364  O O   . GLY A 1 46  ? 3.214   -15.834 32.351  1.00 15.22  ? 271  GLY A O   1 
ATOM   365  N N   . GLU A 1 47  ? 1.154   -16.693 32.460  1.00 12.56  ? 272  GLU A N   1 
ATOM   366  C CA  . GLU A 1 47  ? 1.473   -17.530 33.606  1.00 12.85  ? 272  GLU A CA  1 
ATOM   367  C C   . GLU A 1 47  ? 1.749   -18.948 33.122  1.00 11.51  ? 272  GLU A C   1 
ATOM   368  O O   . GLU A 1 47  ? 0.850   -19.622 32.604  1.00 14.07  ? 272  GLU A O   1 
ATOM   369  C CB  . GLU A 1 47  ? 0.339   -17.509 34.623  1.00 17.08  ? 272  GLU A CB  1 
ATOM   370  C CG  . GLU A 1 47  ? 0.146   -16.126 35.201  1.00 17.36  ? 272  GLU A CG  1 
ATOM   371  C CD  . GLU A 1 47  ? -0.825  -16.127 36.337  1.00 39.10  ? 272  GLU A CD  1 
ATOM   372  O OE1 . GLU A 1 47  ? -0.622  -16.931 37.273  1.00 47.09  ? 272  GLU A OE1 1 
ATOM   373  O OE2 . GLU A 1 47  ? -1.792  -15.340 36.278  1.00 22.25  ? 272  GLU A OE2 1 
ATOM   374  N N   . LEU A 1 48  ? 2.979   -19.408 33.329  1.00 11.96  ? 273  LEU A N   1 
ATOM   375  C CA  . LEU A 1 48  ? 3.338   -20.760 32.926  1.00 13.29  ? 273  LEU A CA  1 
ATOM   376  C C   . LEU A 1 48  ? 2.701   -21.780 33.864  1.00 14.42  ? 273  LEU A C   1 
ATOM   377  O O   . LEU A 1 48  ? 2.613   -21.569 35.076  1.00 15.49  ? 273  LEU A O   1 
ATOM   378  C CB  . LEU A 1 48  ? 4.855   -20.925 32.934  1.00 15.31  ? 273  LEU A CB  1 
ATOM   379  C CG  . LEU A 1 48  ? 5.598   -20.015 31.957  1.00 12.01  ? 273  LEU A CG  1 
ATOM   380  C CD1 . LEU A 1 48  ? 7.086   -20.041 32.287  1.00 15.60  ? 273  LEU A CD1 1 
ATOM   381  C CD2 . LEU A 1 48  ? 5.341   -20.435 30.510  1.00 13.84  ? 273  LEU A CD2 1 
ATOM   382  N N   . LEU A 1 49  ? 2.258   -22.893 33.300  1.00 14.81  ? 274  LEU A N   1 
ATOM   383  C CA  . LEU A 1 49  ? 1.644   -23.951 34.078  1.00 11.86  ? 274  LEU A CA  1 
ATOM   384  C C   . LEU A 1 49  ? 2.468   -25.224 33.960  1.00 14.27  ? 274  LEU A C   1 
ATOM   385  O O   . LEU A 1 49  ? 3.186   -25.438 32.984  1.00 14.13  ? 274  LEU A O   1 
ATOM   386  C CB  . LEU A 1 49  ? 0.205   -24.219 33.617  1.00 11.61  ? 274  LEU A CB  1 
ATOM   387  C CG  . LEU A 1 49  ? -0.706  -23.005 33.396  1.00 15.24  ? 274  LEU A CG  1 
ATOM   388  C CD1 . LEU A 1 49  ? -2.073  -23.464 32.898  1.00 17.24  ? 274  LEU A CD1 1 
ATOM   389  C CD2 . LEU A 1 49  ? -0.862  -22.152 34.653  1.00 17.05  ? 274  LEU A CD2 1 
ATOM   390  N N   . GLY A 1 50  ? 2.338   -26.088 34.962  1.00 15.76  ? 275  GLY A N   1 
ATOM   391  C CA  . GLY A 1 50  ? 2.983   -27.376 34.864  1.00 11.64  ? 275  GLY A CA  1 
ATOM   392  C C   . GLY A 1 50  ? 4.495   -27.242 34.892  1.00 14.79  ? 275  GLY A C   1 
ATOM   393  O O   . GLY A 1 50  ? 5.059   -26.402 35.603  1.00 13.86  ? 275  GLY A O   1 
ATOM   394  N N   . THR A 1 51  ? 5.169   -28.070 34.094  1.00 13.36  ? 276  THR A N   1 
ATOM   395  C CA  . THR A 1 51  ? 6.622   -28.025 34.002  1.00 11.20  ? 276  THR A CA  1 
ATOM   396  C C   . THR A 1 51  ? 7.106   -27.183 32.821  1.00 12.96  ? 276  THR A C   1 
ATOM   397  O O   . THR A 1 51  ? 8.301   -27.187 32.520  1.00 11.57  ? 276  THR A O   1 
ATOM   398  C CB  . THR A 1 51  ? 7.198   -29.441 33.903  1.00 14.70  ? 276  THR A CB  1 
ATOM   399  O OG1 . THR A 1 51  ? 6.594   -30.125 32.796  1.00 14.21  ? 276  THR A OG1 1 
ATOM   400  C CG2 . THR A 1 51  ? 6.939   -30.236 35.200  1.00 14.20  ? 276  THR A CG2 1 
ATOM   401  N N   . THR A 1 52  ? 6.204   -26.439 32.172  1.00 12.75  ? 277  THR A N   1 
ATOM   402  C CA  . THR A 1 52  ? 6.531   -25.620 31.008  1.00 12.17  ? 277  THR A CA  1 
ATOM   403  C C   . THR A 1 52  ? 7.715   -24.704 31.300  1.00 10.76  ? 277  THR A C   1 
ATOM   404  O O   . THR A 1 52  ? 7.619   -23.839 32.182  1.00 12.32  ? 277  THR A O   1 
ATOM   405  C CB  . THR A 1 52  ? 5.317   -24.780 30.626  1.00 10.23  ? 277  THR A CB  1 
ATOM   406  O OG1 . THR A 1 52  ? 4.187   -25.642 30.455  1.00 10.79  ? 277  THR A OG1 1 
ATOM   407  C CG2 . THR A 1 52  ? 5.569   -23.992 29.339  1.00 12.37  ? 277  THR A CG2 1 
ATOM   408  N N   . PRO A 1 53  ? 8.817   -24.829 30.569  1.00 14.16  ? 278  PRO A N   1 
ATOM   409  C CA  . PRO A 1 53  ? 9.986   -23.993 30.863  1.00 18.38  ? 278  PRO A CA  1 
ATOM   410  C C   . PRO A 1 53  ? 9.816   -22.568 30.361  1.00 18.92  ? 278  PRO A C   1 
ATOM   411  O O   . PRO A 1 53  ? 9.232   -22.324 29.304  1.00 15.41  ? 278  PRO A O   1 
ATOM   412  C CB  . PRO A 1 53  ? 11.125  -24.704 30.120  1.00 13.60  ? 278  PRO A CB  1 
ATOM   413  C CG  . PRO A 1 53  ? 10.454  -25.534 29.058  1.00 14.01  ? 278  PRO A CG  1 
ATOM   414  C CD  . PRO A 1 53  ? 9.111   -25.922 29.623  1.00 12.77  ? 278  PRO A CD  1 
ATOM   415  N N   A ARG A 1 54  ? 10.338  -21.622 31.143  0.44 13.17  ? 279  ARG A N   1 
ATOM   416  N N   B ARG A 1 54  ? 10.352  -21.622 31.136  0.56 13.15  ? 279  ARG A N   1 
ATOM   417  C CA  A ARG A 1 54  ? 10.348  -20.229 30.712  0.44 13.29  ? 279  ARG A CA  1 
ATOM   418  C CA  B ARG A 1 54  ? 10.338  -20.229 30.707  0.56 13.28  ? 279  ARG A CA  1 
ATOM   419  C C   A ARG A 1 54  ? 11.272  -20.031 29.518  0.44 13.08  ? 279  ARG A C   1 
ATOM   420  C C   B ARG A 1 54  ? 11.297  -19.989 29.549  0.56 13.01  ? 279  ARG A C   1 
ATOM   421  O O   A ARG A 1 54  ? 10.955  -19.272 28.595  0.44 16.01  ? 279  ARG A O   1 
ATOM   422  O O   B ARG A 1 54  ? 11.027  -19.149 28.684  0.56 15.76  ? 279  ARG A O   1 
ATOM   423  C CB  A ARG A 1 54  ? 10.764  -19.337 31.877  0.44 14.94  ? 279  ARG A CB  1 
ATOM   424  C CB  B ARG A 1 54  ? 10.681  -19.323 31.886  0.56 14.94  ? 279  ARG A CB  1 
ATOM   425  C CG  A ARG A 1 54  ? 10.922  -17.869 31.538  0.44 16.80  ? 279  ARG A CG  1 
ATOM   426  C CG  B ARG A 1 54  ? 10.366  -17.863 31.644  0.56 16.84  ? 279  ARG A CG  1 
ATOM   427  C CD  A ARG A 1 54  ? 11.045  -17.063 32.827  0.44 22.44  ? 279  ARG A CD  1 
ATOM   428  C CD  B ARG A 1 54  ? 10.694  -17.012 32.869  0.56 22.29  ? 279  ARG A CD  1 
ATOM   429  N NE  A ARG A 1 54  ? 9.877   -17.270 33.671  0.44 21.55  ? 279  ARG A NE  1 
ATOM   430  N NE  B ARG A 1 54  ? 10.361  -15.618 32.620  0.56 25.92  ? 279  ARG A NE  1 
ATOM   431  C CZ  A ARG A 1 54  ? 8.758   -16.566 33.575  0.44 21.18  ? 279  ARG A CZ  1 
ATOM   432  C CZ  B ARG A 1 54  ? 9.134   -15.122 32.698  0.56 20.31  ? 279  ARG A CZ  1 
ATOM   433  N NH1 A ARG A 1 54  ? 8.643   -15.571 32.710  0.44 21.89  ? 279  ARG A NH1 1 
ATOM   434  N NH1 B ARG A 1 54  ? 8.108   -15.871 33.066  0.56 31.12  ? 279  ARG A NH1 1 
ATOM   435  N NH2 A ARG A 1 54  ? 7.730   -16.872 34.361  0.44 19.69  ? 279  ARG A NH2 1 
ATOM   436  N NH2 B ARG A 1 54  ? 8.932   -13.842 32.402  0.56 36.65  ? 279  ARG A NH2 1 
ATOM   437  N N   . ASN A 1 55  ? 12.415  -20.707 29.516  1.00 11.20  ? 280  ASN A N   1 
ATOM   438  C CA  . ASN A 1 55  ? 13.333  -20.676 28.383  1.00 11.66  ? 280  ASN A CA  1 
ATOM   439  C C   . ASN A 1 55  ? 12.910  -21.765 27.404  1.00 11.41  ? 280  ASN A C   1 
ATOM   440  O O   . ASN A 1 55  ? 12.888  -22.948 27.765  1.00 12.39  ? 280  ASN A O   1 
ATOM   441  C CB  . ASN A 1 55  ? 14.768  -20.902 28.851  1.00 8.81   ? 280  ASN A CB  1 
ATOM   442  C CG  . ASN A 1 55  ? 15.790  -20.650 27.757  1.00 13.17  ? 280  ASN A CG  1 
ATOM   443  O OD1 . ASN A 1 55  ? 15.528  -20.877 26.583  1.00 14.69  ? 280  ASN A OD1 1 
ATOM   444  N ND2 . ASN A 1 55  ? 16.966  -20.163 28.144  1.00 10.74  ? 280  ASN A ND2 1 
ATOM   445  N N   . ALA A 1 56  ? 12.566  -21.369 26.176  1.00 12.91  ? 281  ALA A N   1 
ATOM   446  C CA  . ALA A 1 56  ? 12.145  -22.341 25.166  1.00 13.34  ? 281  ALA A CA  1 
ATOM   447  C C   . ALA A 1 56  ? 13.133  -23.497 25.034  1.00 14.92  ? 281  ALA A C   1 
ATOM   448  O O   . ALA A 1 56  ? 12.732  -24.654 24.844  1.00 14.73  ? 281  ALA A O   1 
ATOM   449  C CB  . ALA A 1 56  ? 11.978  -21.642 23.813  1.00 12.17  ? 281  ALA A CB  1 
ATOM   450  N N   A SER A 1 57  ? 14.426  -23.209 25.147  0.50 13.61  ? 282  SER A N   1 
ATOM   451  N N   B SER A 1 57  ? 14.428  -23.212 25.129  0.50 13.59  ? 282  SER A N   1 
ATOM   452  C CA  A SER A 1 57  ? 15.440  -24.212 24.854  0.50 10.69  ? 282  SER A CA  1 
ATOM   453  C CA  B SER A 1 57  ? 15.440  -24.234 24.899  0.50 10.64  ? 282  SER A CA  1 
ATOM   454  C C   A SER A 1 57  ? 15.737  -25.151 26.012  0.50 12.83  ? 282  SER A C   1 
ATOM   455  C C   B SER A 1 57  ? 15.767  -25.054 26.145  0.50 13.06  ? 282  SER A C   1 
ATOM   456  O O   A SER A 1 57  ? 16.596  -26.026 25.858  0.50 14.30  ? 282  SER A O   1 
ATOM   457  O O   B SER A 1 57  ? 16.734  -25.825 26.125  0.50 15.29  ? 282  SER A O   1 
ATOM   458  C CB  A SER A 1 57  ? 16.732  -23.531 24.408  0.50 12.23  ? 282  SER A CB  1 
ATOM   459  C CB  B SER A 1 57  ? 16.712  -23.595 24.328  0.50 12.20  ? 282  SER A CB  1 
ATOM   460  O OG  A SER A 1 57  ? 16.606  -23.112 23.072  0.50 19.40  ? 282  SER A OG  1 
ATOM   461  O OG  B SER A 1 57  ? 17.166  -22.532 25.143  0.50 11.34  ? 282  SER A OG  1 
ATOM   462  N N   A TRP A 1 58  ? 15.086  -24.998 27.160  0.50 9.54   ? 283  TRP A N   1 
ATOM   463  N N   B TRP A 1 58  ? 14.995  -24.905 27.227  0.50 9.70   ? 283  TRP A N   1 
ATOM   464  C CA  A TRP A 1 58  ? 15.229  -25.976 28.230  0.50 10.52  ? 283  TRP A CA  1 
ATOM   465  C CA  B TRP A 1 58  ? 15.061  -25.840 28.345  0.50 10.94  ? 283  TRP A CA  1 
ATOM   466  C C   A TRP A 1 58  ? 14.227  -27.116 28.112  0.50 11.12  ? 283  TRP A C   1 
ATOM   467  C C   B TRP A 1 58  ? 14.254  -27.106 28.090  0.50 11.11  ? 283  TRP A C   1 
ATOM   468  O O   A TRP A 1 58  ? 14.233  -28.019 28.956  0.50 12.03  ? 283  TRP A O   1 
ATOM   469  O O   B TRP A 1 58  ? 14.424  -28.087 28.821  0.50 11.70  ? 283  TRP A O   1 
ATOM   470  C CB  A TRP A 1 58  ? 15.103  -25.302 29.605  0.50 11.73  ? 283  TRP A CB  1 
ATOM   471  C CB  B TRP A 1 58  ? 14.540  -25.202 29.640  0.50 12.25  ? 283  TRP A CB  1 
ATOM   472  C CG  A TRP A 1 58  ? 16.439  -24.853 30.154  0.50 13.80  ? 283  TRP A CG  1 
ATOM   473  C CG  B TRP A 1 58  ? 15.412  -24.153 30.271  0.50 18.31  ? 283  TRP A CG  1 
ATOM   474  C CD1 A TRP A 1 58  ? 16.947  -23.584 30.155  0.50 15.65  ? 283  TRP A CD1 1 
ATOM   475  C CD1 B TRP A 1 58  ? 16.759  -24.004 30.123  0.50 13.71  ? 283  TRP A CD1 1 
ATOM   476  C CD2 A TRP A 1 58  ? 17.436  -25.685 30.758  0.50 13.86  ? 283  TRP A CD2 1 
ATOM   477  C CD2 B TRP A 1 58  ? 14.986  -23.112 31.164  0.50 24.08  ? 283  TRP A CD2 1 
ATOM   478  N NE1 A TRP A 1 58  ? 18.199  -23.573 30.731  0.50 11.60  ? 283  TRP A NE1 1 
ATOM   479  N NE1 B TRP A 1 58  ? 17.201  -22.927 30.861  0.50 15.56  ? 283  TRP A NE1 1 
ATOM   480  C CE2 A TRP A 1 58  ? 18.520  -24.852 31.110  0.50 11.75  ? 283  TRP A CE2 1 
ATOM   481  C CE2 B TRP A 1 58  ? 16.132  -22.359 31.502  0.50 19.89  ? 283  TRP A CE2 1 
ATOM   482  C CE3 A TRP A 1 58  ? 17.514  -27.051 31.046  0.50 19.42  ? 283  TRP A CE3 1 
ATOM   483  C CE3 B TRP A 1 58  ? 13.743  -22.727 31.687  0.50 8.90   ? 283  TRP A CE3 1 
ATOM   484  C CZ2 A TRP A 1 58  ? 19.670  -25.344 31.723  0.50 14.97  ? 283  TRP A CZ2 1 
ATOM   485  C CZ2 B TRP A 1 58  ? 16.078  -21.259 32.362  0.50 14.27  ? 283  TRP A CZ2 1 
ATOM   486  C CZ3 A TRP A 1 58  ? 18.656  -27.536 31.653  0.50 16.36  ? 283  TRP A CZ3 1 
ATOM   487  C CZ3 B TRP A 1 58  ? 13.694  -21.638 32.538  0.50 17.62  ? 283  TRP A CZ3 1 
ATOM   488  C CH2 A TRP A 1 58  ? 19.716  -26.684 31.990  0.50 19.48  ? 283  TRP A CH2 1 
ATOM   489  C CH2 B TRP A 1 58  ? 14.858  -20.910 32.860  0.50 16.01  ? 283  TRP A CH2 1 
ATOM   490  N N   . LEU A 1 59  ? 13.368  -27.094 27.097  1.00 12.06  ? 284  LEU A N   1 
ATOM   491  C CA  . LEU A 1 59  ? 12.515  -28.244 26.826  1.00 11.50  ? 284  LEU A CA  1 
ATOM   492  C C   . LEU A 1 59  ? 13.372  -29.432 26.410  1.00 10.99  ? 284  LEU A C   1 
ATOM   493  O O   . LEU A 1 59  ? 14.219  -29.318 25.522  1.00 11.05  ? 284  LEU A O   1 
ATOM   494  C CB  . LEU A 1 59  ? 11.507  -27.908 25.726  1.00 12.75  ? 284  LEU A CB  1 
ATOM   495  C CG  . LEU A 1 59  ? 10.539  -29.019 25.317  1.00 12.66  ? 284  LEU A CG  1 
ATOM   496  C CD1 . LEU A 1 59  ? 9.612   -29.383 26.483  1.00 13.93  ? 284  LEU A CD1 1 
ATOM   497  C CD2 . LEU A 1 59  ? 9.757   -28.591 24.075  1.00 14.35  ? 284  LEU A CD2 1 
ATOM   498  N N   . ASN A 1 60  ? 13.156  -30.573 27.074  1.00 11.32  ? 285  ASN A N   1 
ATOM   499  C CA  . ASN A 1 60  ? 13.907  -31.808 26.870  1.00 9.88   ? 285  ASN A CA  1 
ATOM   500  C C   . ASN A 1 60  ? 15.371  -31.678 27.269  1.00 12.64  ? 285  ASN A C   1 
ATOM   501  O O   . ASN A 1 60  ? 16.180  -32.532 26.892  1.00 20.19  ? 285  ASN A O   1 
ATOM   502  C CB  . ASN A 1 60  ? 13.808  -32.322 25.425  1.00 10.55  ? 285  ASN A CB  1 
ATOM   503  C CG  . ASN A 1 60  ? 12.605  -33.226 25.224  1.00 14.91  ? 285  ASN A CG  1 
ATOM   504  O OD1 . ASN A 1 60  ? 11.780  -33.367 26.128  1.00 17.52  ? 285  ASN A OD1 1 
ATOM   505  N ND2 . ASN A 1 60  ? 12.510  -33.856 24.058  1.00 15.50  ? 285  ASN A ND2 1 
ATOM   506  N N   . ARG A 1 61  ? 15.738  -30.649 28.027  1.00 9.04   ? 286  ARG A N   1 
ATOM   507  C CA  . ARG A 1 61  ? 17.074  -30.570 28.600  1.00 9.69   ? 286  ARG A CA  1 
ATOM   508  C C   . ARG A 1 61  ? 17.017  -30.912 30.088  1.00 12.80  ? 286  ARG A C   1 
ATOM   509  O O   . ARG A 1 61  ? 15.965  -30.827 30.725  1.00 13.51  ? 286  ARG A O   1 
ATOM   510  C CB  . ARG A 1 61  ? 17.674  -29.170 28.395  1.00 11.08  ? 286  ARG A CB  1 
ATOM   511  C CG  . ARG A 1 61  ? 18.329  -28.933 27.036  1.00 16.40  ? 286  ARG A CG  1 
ATOM   512  C CD  . ARG A 1 61  ? 17.347  -29.007 25.891  1.00 19.71  ? 286  ARG A CD  1 
ATOM   513  N NE  . ARG A 1 61  ? 17.934  -28.510 24.652  1.00 21.68  ? 286  ARG A NE  1 
ATOM   514  C CZ  . ARG A 1 61  ? 17.229  -28.016 23.642  1.00 23.15  ? 286  ARG A CZ  1 
ATOM   515  N NH1 . ARG A 1 61  ? 15.898  -27.999 23.662  1.00 17.33  ? 286  ARG A NH1 1 
ATOM   516  N NH2 . ARG A 1 61  ? 17.874  -27.493 22.601  1.00 20.45  ? 286  ARG A NH2 1 
ATOM   517  N N   . PHE A 1 62  ? 18.161  -31.324 30.638  1.00 11.53  ? 287  PHE A N   1 
ATOM   518  C CA  . PHE A 1 62  ? 18.250  -31.649 32.054  1.00 13.02  ? 287  PHE A CA  1 
ATOM   519  C C   . PHE A 1 62  ? 19.651  -31.322 32.546  1.00 16.07  ? 287  PHE A C   1 
ATOM   520  O O   . PHE A 1 62  ? 20.614  -31.280 31.774  1.00 12.72  ? 287  PHE A O   1 
ATOM   521  C CB  . PHE A 1 62  ? 17.920  -33.132 32.337  1.00 12.88  ? 287  PHE A CB  1 
ATOM   522  C CG  . PHE A 1 62  ? 18.812  -34.108 31.601  1.00 13.01  ? 287  PHE A CG  1 
ATOM   523  C CD1 . PHE A 1 62  ? 20.012  -34.526 32.153  1.00 15.48  ? 287  PHE A CD1 1 
ATOM   524  C CD2 . PHE A 1 62  ? 18.441  -34.607 30.361  1.00 13.16  ? 287  PHE A CD2 1 
ATOM   525  C CE1 . PHE A 1 62  ? 20.849  -35.420 31.461  1.00 17.71  ? 287  PHE A CE1 1 
ATOM   526  C CE2 . PHE A 1 62  ? 19.264  -35.495 29.666  1.00 14.70  ? 287  PHE A CE2 1 
ATOM   527  C CZ  . PHE A 1 62  ? 20.471  -35.907 30.227  1.00 15.68  ? 287  PHE A CZ  1 
ATOM   528  N N   . ARG A 1 63  ? 19.746  -31.108 33.854  1.00 14.75  ? 288  ARG A N   1 
ATOM   529  C CA  . ARG A 1 63  ? 20.968  -30.733 34.544  1.00 15.45  ? 288  ARG A CA  1 
ATOM   530  C C   . ARG A 1 63  ? 20.979  -31.481 35.866  1.00 13.87  ? 288  ARG A C   1 
ATOM   531  O O   . ARG A 1 63  ? 19.927  -31.649 36.495  1.00 15.45  ? 288  ARG A O   1 
ATOM   532  C CB  . ARG A 1 63  ? 21.002  -29.207 34.783  1.00 19.75  ? 288  ARG A CB  1 
ATOM   533  C CG  . ARG A 1 63  ? 22.336  -28.582 35.142  1.00 45.86  ? 288  ARG A CG  1 
ATOM   534  C CD  . ARG A 1 63  ? 22.085  -27.178 35.700  1.00 34.69  ? 288  ARG A CD  1 
ATOM   535  N NE  . ARG A 1 63  ? 23.226  -26.281 35.577  1.00 47.84  ? 288  ARG A NE  1 
ATOM   536  C CZ  . ARG A 1 63  ? 23.219  -25.163 34.865  1.00 46.64  ? 288  ARG A CZ  1 
ATOM   537  N N   . GLY A 1 64  ? 22.148  -31.958 36.271  1.00 13.26  ? 289  GLY A N   1 
ATOM   538  C CA  . GLY A 1 64  ? 22.238  -32.588 37.573  1.00 13.44  ? 289  GLY A CA  1 
ATOM   539  C C   . GLY A 1 64  ? 23.680  -32.787 37.977  1.00 16.91  ? 289  GLY A C   1 
ATOM   540  O O   . GLY A 1 64  ? 24.597  -32.251 37.352  1.00 20.89  ? 289  GLY A O   1 
ATOM   541  N N   A VAL A 1 65  ? 23.874  -33.584 39.028  0.52 12.79  ? 290  VAL A N   1 
ATOM   542  N N   B VAL A 1 65  ? 23.865  -33.545 39.055  0.48 12.80  ? 290  VAL A N   1 
ATOM   543  C CA  A VAL A 1 65  ? 25.207  -33.908 39.526  0.52 12.18  ? 290  VAL A CA  1 
ATOM   544  C CA  B VAL A 1 65  ? 25.191  -33.928 39.523  0.48 12.18  ? 290  VAL A CA  1 
ATOM   545  C C   A VAL A 1 65  ? 25.282  -35.404 39.791  0.52 12.77  ? 290  VAL A C   1 
ATOM   546  C C   B VAL A 1 65  ? 25.231  -35.436 39.686  0.48 12.81  ? 290  VAL A C   1 
ATOM   547  O O   A VAL A 1 65  ? 24.377  -35.978 40.406  0.52 14.79  ? 290  VAL A O   1 
ATOM   548  O O   B VAL A 1 65  ? 24.254  -36.051 40.128  0.48 15.59  ? 290  VAL A O   1 
ATOM   549  C CB  A VAL A 1 65  ? 25.557  -33.104 40.794  0.52 14.53  ? 290  VAL A CB  1 
ATOM   550  C CB  B VAL A 1 65  ? 25.576  -33.234 40.847  0.48 14.68  ? 290  VAL A CB  1 
ATOM   551  C CG1 A VAL A 1 65  ? 26.850  -33.606 41.420  0.52 14.63  ? 290  VAL A CG1 1 
ATOM   552  C CG1 B VAL A 1 65  ? 25.850  -31.770 40.605  0.48 25.25  ? 290  VAL A CG1 1 
ATOM   553  C CG2 A VAL A 1 65  ? 25.715  -31.654 40.437  0.52 25.51  ? 290  VAL A CG2 1 
ATOM   554  C CG2 B VAL A 1 65  ? 24.492  -33.426 41.894  0.48 12.77  ? 290  VAL A CG2 1 
ATOM   555  N N   . SER A 1 66  ? 26.364  -36.034 39.331  1.00 13.52  ? 291  SER A N   1 
ATOM   556  C CA  . SER A 1 66  ? 26.517  -37.474 39.491  1.00 15.59  ? 291  SER A CA  1 
ATOM   557  C C   . SER A 1 66  ? 26.608  -37.838 40.969  1.00 16.05  ? 291  SER A C   1 
ATOM   558  O O   . SER A 1 66  ? 27.330  -37.202 41.743  1.00 18.55  ? 291  SER A O   1 
ATOM   559  C CB  . SER A 1 66  ? 27.759  -37.956 38.738  1.00 15.12  ? 291  SER A CB  1 
ATOM   560  O OG  . SER A 1 66  ? 28.920  -37.278 39.183  1.00 17.08  ? 291  SER A OG  1 
ATOM   561  N N   . THR A 1 67  ? 25.866  -38.863 41.366  1.00 14.87  ? 292  THR A N   1 
ATOM   562  C CA  . THR A 1 67  ? 25.880  -39.299 42.761  1.00 15.28  ? 292  THR A CA  1 
ATOM   563  C C   . THR A 1 67  ? 26.983  -40.305 43.067  1.00 19.55  ? 292  THR A C   1 
ATOM   564  O O   . THR A 1 67  ? 27.312  -40.521 44.242  1.00 20.74  ? 292  THR A O   1 
ATOM   565  C CB  . THR A 1 67  ? 24.527  -39.897 43.114  1.00 22.86  ? 292  THR A CB  1 
ATOM   566  O OG1 . THR A 1 67  ? 24.375  -41.134 42.426  1.00 28.35  ? 292  THR A OG1 1 
ATOM   567  C CG2 . THR A 1 67  ? 23.436  -38.970 42.657  1.00 25.35  ? 292  THR A CG2 1 
ATOM   568  N N   . ALA A 1 68  ? 27.557  -40.917 42.038  1.00 18.71  ? 293  ALA A N   1 
ATOM   569  C CA  . ALA A 1 68  ? 28.622  -41.894 42.184  1.00 16.60  ? 293  ALA A CA  1 
ATOM   570  C C   . ALA A 1 68  ? 29.324  -41.956 40.843  1.00 18.12  ? 293  ALA A C   1 
ATOM   571  O O   . ALA A 1 68  ? 28.791  -41.489 39.836  1.00 18.37  ? 293  ALA A O   1 
ATOM   572  C CB  . ALA A 1 68  ? 28.089  -43.275 42.585  1.00 20.00  ? 293  ALA A CB  1 
ATOM   573  N N   . ALA A 1 69  ? 30.525  -42.523 40.836  1.00 18.19  ? 294  ALA A N   1 
ATOM   574  C CA  . ALA A 1 69  ? 31.220  -42.681 39.570  1.00 19.10  ? 294  ALA A CA  1 
ATOM   575  C C   . ALA A 1 69  ? 30.480  -43.686 38.703  1.00 16.90  ? 294  ALA A C   1 
ATOM   576  O O   . ALA A 1 69  ? 29.868  -44.644 39.201  1.00 21.17  ? 294  ALA A O   1 
ATOM   577  C CB  . ALA A 1 69  ? 32.660  -43.142 39.794  1.00 24.55  ? 294  ALA A CB  1 
ATOM   578  N N   . VAL A 1 70  ? 30.537  -43.449 37.391  1.00 19.96  ? 295  VAL A N   1 
ATOM   579  C CA  . VAL A 1 70  ? 29.994  -44.384 36.419  1.00 19.54  ? 295  VAL A CA  1 
ATOM   580  C C   . VAL A 1 70  ? 30.583  -45.765 36.651  1.00 22.49  ? 295  VAL A C   1 
ATOM   581  O O   . VAL A 1 70  ? 31.791  -45.919 36.861  1.00 24.19  ? 295  VAL A O   1 
ATOM   582  C CB  . VAL A 1 70  ? 30.283  -43.882 34.993  1.00 20.76  ? 295  VAL A CB  1 
ATOM   583  C CG1 . VAL A 1 70  ? 30.006  -44.983 33.973  1.00 21.42  ? 295  VAL A CG1 1 
ATOM   584  C CG2 . VAL A 1 70  ? 29.451  -42.645 34.700  1.00 20.42  ? 295  VAL A CG2 1 
ATOM   585  N N   . ALA A 1 71  ? 29.718  -46.774 36.624  1.00 22.58  ? 296  ALA A N   1 
ATOM   586  C CA  . ALA A 1 71  ? 30.126  -48.167 36.668  1.00 24.19  ? 296  ALA A CA  1 
ATOM   587  C C   . ALA A 1 71  ? 29.023  -48.998 36.032  1.00 27.97  ? 296  ALA A C   1 
ATOM   588  O O   . ALA A 1 71  ? 27.839  -48.704 36.216  1.00 23.92  ? 296  ALA A O   1 
ATOM   589  C CB  . ALA A 1 71  ? 30.394  -48.630 38.103  1.00 26.27  ? 296  ALA A CB  1 
ATOM   590  N N   . ASN A 1 72  ? 29.420  -50.018 35.271  1.00 25.95  ? 297  ASN A N   1 
ATOM   591  C CA  . ASN A 1 72  ? 28.480  -50.937 34.623  1.00 25.38  ? 297  ASN A CA  1 
ATOM   592  C C   . ASN A 1 72  ? 27.477  -50.202 33.736  1.00 20.06  ? 297  ASN A C   1 
ATOM   593  O O   . ASN A 1 72  ? 26.308  -50.580 33.648  1.00 19.54  ? 297  ASN A O   1 
ATOM   594  C CB  . ASN A 1 72  ? 27.753  -51.793 35.659  1.00 30.13  ? 297  ASN A CB  1 
ATOM   595  C CG  . ASN A 1 72  ? 28.706  -52.587 36.522  1.00 55.90  ? 297  ASN A CG  1 
ATOM   596  O OD1 . ASN A 1 72  ? 28.561  -52.636 37.743  1.00 59.38  ? 297  ASN A OD1 1 
ATOM   597  N ND2 . ASN A 1 72  ? 29.701  -53.204 35.892  1.00 44.88  ? 297  ASN A ND2 1 
ATOM   598  N N   . GLN A 1 73  ? 27.947  -49.142 33.070  1.00 19.71  ? 298  GLN A N   1 
ATOM   599  C CA  . GLN A 1 73  ? 27.147  -48.347 32.132  1.00 22.08  ? 298  GLN A CA  1 
ATOM   600  C C   . GLN A 1 73  ? 25.972  -47.657 32.819  1.00 19.27  ? 298  GLN A C   1 
ATOM   601  O O   . GLN A 1 73  ? 24.948  -47.376 32.190  1.00 19.04  ? 298  GLN A O   1 
ATOM   602  C CB  . GLN A 1 73  ? 26.654  -49.194 30.955  1.00 19.56  ? 298  GLN A CB  1 
ATOM   603  C CG  . GLN A 1 73  ? 27.775  -49.809 30.143  1.00 23.84  ? 298  GLN A CG  1 
ATOM   604  C CD  . GLN A 1 73  ? 27.409  -49.912 28.677  1.00 46.14  ? 298  GLN A CD  1 
ATOM   605  O OE1 . GLN A 1 73  ? 26.268  -50.220 28.336  1.00 34.37  ? 298  GLN A OE1 1 
ATOM   606  N NE2 . GLN A 1 73  ? 28.369  -49.628 27.800  1.00 51.32  ? 298  GLN A NE2 1 
ATOM   607  N N   . VAL A 1 74  ? 26.115  -47.356 34.108  1.00 19.13  ? 299  VAL A N   1 
ATOM   608  C CA  . VAL A 1 74  ? 25.077  -46.685 34.883  1.00 14.46  ? 299  VAL A CA  1 
ATOM   609  C C   . VAL A 1 74  ? 25.614  -45.344 35.354  1.00 19.59  ? 299  VAL A C   1 
ATOM   610  O O   . VAL A 1 74  ? 26.712  -45.272 35.919  1.00 17.37  ? 299  VAL A O   1 
ATOM   611  C CB  . VAL A 1 74  ? 24.626  -47.524 36.091  1.00 20.10  ? 299  VAL A CB  1 
ATOM   612  C CG1 . VAL A 1 74  ? 23.630  -46.733 36.957  1.00 20.43  ? 299  VAL A CG1 1 
ATOM   613  C CG2 . VAL A 1 74  ? 24.023  -48.839 35.635  1.00 18.19  ? 299  VAL A CG2 1 
ATOM   614  N N   . LEU A 1 75  ? 24.829  -44.296 35.142  1.00 15.75  ? 300  LEU A N   1 
ATOM   615  C CA  . LEU A 1 75  ? 25.121  -42.962 35.652  1.00 17.02  ? 300  LEU A CA  1 
ATOM   616  C C   . LEU A 1 75  ? 23.890  -42.482 36.406  1.00 14.79  ? 300  LEU A C   1 
ATOM   617  O O   . LEU A 1 75  ? 22.826  -42.325 35.804  1.00 16.84  ? 300  LEU A O   1 
ATOM   618  C CB  . LEU A 1 75  ? 25.455  -41.999 34.506  1.00 15.58  ? 300  LEU A CB  1 
ATOM   619  C CG  . LEU A 1 75  ? 25.501  -40.498 34.824  1.00 14.48  ? 300  LEU A CG  1 
ATOM   620  C CD1 . LEU A 1 75  ? 26.573  -40.178 35.881  1.00 16.54  ? 300  LEU A CD1 1 
ATOM   621  C CD2 . LEU A 1 75  ? 25.728  -39.677 33.553  1.00 16.87  ? 300  LEU A CD2 1 
ATOM   622  N N   A HIS A 1 76  ? 24.036  -42.278 37.718  0.44 16.38  ? 301  HIS A N   1 
ATOM   623  N N   B HIS A 1 76  ? 24.011  -42.262 37.710  0.56 16.44  ? 301  HIS A N   1 
ATOM   624  C CA  A HIS A 1 76  ? 22.978  -41.724 38.562  0.44 14.71  ? 301  HIS A CA  1 
ATOM   625  C CA  B HIS A 1 76  ? 22.880  -41.731 38.461  0.56 14.55  ? 301  HIS A CA  1 
ATOM   626  C C   A HIS A 1 76  ? 23.159  -40.211 38.664  0.44 16.09  ? 301  HIS A C   1 
ATOM   627  C C   B HIS A 1 76  ? 23.096  -40.253 38.742  0.56 15.99  ? 301  HIS A C   1 
ATOM   628  O O   A HIS A 1 76  ? 24.256  -39.742 38.982  0.44 14.96  ? 301  HIS A O   1 
ATOM   629  O O   B HIS A 1 76  ? 24.151  -39.860 39.246  0.56 14.93  ? 301  HIS A O   1 
ATOM   630  C CB  A HIS A 1 76  ? 23.026  -42.323 39.972  0.44 15.03  ? 301  HIS A CB  1 
ATOM   631  C CB  B HIS A 1 76  ? 22.633  -42.472 39.773  0.56 15.75  ? 301  HIS A CB  1 
ATOM   632  C CG  A HIS A 1 76  ? 22.706  -43.787 40.056  0.44 17.14  ? 301  HIS A CG  1 
ATOM   633  C CG  B HIS A 1 76  ? 21.380  -42.022 40.459  0.56 22.46  ? 301  HIS A CG  1 
ATOM   634  N ND1 A HIS A 1 76  ? 21.428  -44.259 40.269  0.44 19.68  ? 301  HIS A ND1 1 
ATOM   635  N ND1 B HIS A 1 76  ? 21.356  -40.970 41.349  0.56 26.06  ? 301  HIS A ND1 1 
ATOM   636  C CD2 A HIS A 1 76  ? 23.507  -44.879 40.027  0.44 24.12  ? 301  HIS A CD2 1 
ATOM   637  C CD2 B HIS A 1 76  ? 20.098  -42.441 40.339  0.56 15.93  ? 301  HIS A CD2 1 
ATOM   638  C CE1 A HIS A 1 76  ? 21.451  -45.577 40.338  0.44 14.74  ? 301  HIS A CE1 1 
ATOM   639  C CE1 B HIS A 1 76  ? 20.117  -40.774 41.763  0.56 14.07  ? 301  HIS A CE1 1 
ATOM   640  N NE2 A HIS A 1 76  ? 22.700  -45.980 40.194  0.44 15.02  ? 301  HIS A NE2 1 
ATOM   641  N NE2 B HIS A 1 76  ? 19.335  -41.653 41.164  0.56 19.65  ? 301  HIS A NE2 1 
ATOM   642  N N   . LEU A 1 77  ? 22.095  -39.447 38.412  1.00 14.54  ? 302  LEU A N   1 
ATOM   643  C CA  . LEU A 1 77  ? 22.131  -37.999 38.597  1.00 16.65  ? 302  LEU A CA  1 
ATOM   644  C C   . LEU A 1 77  ? 21.149  -37.579 39.680  1.00 17.84  ? 302  LEU A C   1 
ATOM   645  O O   . LEU A 1 77  ? 19.978  -37.971 39.644  1.00 21.13  ? 302  LEU A O   1 
ATOM   646  C CB  . LEU A 1 77  ? 21.783  -37.261 37.308  1.00 16.68  ? 302  LEU A CB  1 
ATOM   647  C CG  . LEU A 1 77  ? 22.692  -37.483 36.107  1.00 15.66  ? 302  LEU A CG  1 
ATOM   648  C CD1 . LEU A 1 77  ? 22.206  -36.632 34.949  1.00 19.15  ? 302  LEU A CD1 1 
ATOM   649  C CD2 . LEU A 1 77  ? 24.138  -37.157 36.468  1.00 18.56  ? 302  LEU A CD2 1 
ATOM   650  N N   . THR A 1 78  ? 21.618  -36.764 40.621  1.00 14.83  ? 303  THR A N   1 
ATOM   651  C CA  . THR A 1 78  ? 20.716  -35.932 41.401  1.00 12.74  ? 303  THR A CA  1 
ATOM   652  C C   . THR A 1 78  ? 20.327  -34.730 40.552  1.00 14.86  ? 303  THR A C   1 
ATOM   653  O O   . THR A 1 78  ? 21.199  -34.057 39.996  1.00 14.77  ? 303  THR A O   1 
ATOM   654  C CB  . THR A 1 78  ? 21.384  -35.475 42.693  1.00 18.97  ? 303  THR A CB  1 
ATOM   655  O OG1 . THR A 1 78  ? 21.670  -36.620 43.502  1.00 23.07  ? 303  THR A OG1 1 
ATOM   656  C CG2 . THR A 1 78  ? 20.463  -34.539 43.458  1.00 21.43  ? 303  THR A CG2 1 
ATOM   657  N N   . LEU A 1 79  ? 19.025  -34.469 40.420  1.00 13.64  ? 304  LEU A N   1 
ATOM   658  C CA  . LEU A 1 79  ? 18.553  -33.489 39.452  1.00 11.37  ? 304  LEU A CA  1 
ATOM   659  C C   . LEU A 1 79  ? 18.589  -32.064 39.994  1.00 13.53  ? 304  LEU A C   1 
ATOM   660  O O   . LEU A 1 79  ? 18.363  -31.827 41.188  1.00 17.57  ? 304  LEU A O   1 
ATOM   661  C CB  . LEU A 1 79  ? 17.133  -33.824 38.999  1.00 14.53  ? 304  LEU A CB  1 
ATOM   662  C CG  . LEU A 1 79  ? 17.062  -35.055 38.095  1.00 18.56  ? 304  LEU A CG  1 
ATOM   663  C CD1 . LEU A 1 79  ? 15.613  -35.446 37.911  1.00 21.84  ? 304  LEU A CD1 1 
ATOM   664  C CD2 . LEU A 1 79  ? 17.742  -34.784 36.749  1.00 17.69  ? 304  LEU A CD2 1 
ATOM   665  N N   . TYR A 1 80  ? 18.899  -31.126 39.102  1.00 12.34  ? 305  TYR A N   1 
ATOM   666  C CA  . TYR A 1 80  ? 18.805  -29.694 39.344  1.00 12.08  ? 305  TYR A CA  1 
ATOM   667  C C   . TYR A 1 80  ? 17.708  -29.099 38.467  1.00 14.79  ? 305  TYR A C   1 
ATOM   668  O O   . TYR A 1 80  ? 17.257  -29.709 37.493  1.00 15.77  ? 305  TYR A O   1 
ATOM   669  C CB  . TYR A 1 80  ? 20.125  -28.983 39.023  1.00 14.85  ? 305  TYR A CB  1 
ATOM   670  C CG  . TYR A 1 80  ? 21.280  -29.229 39.964  1.00 17.53  ? 305  TYR A CG  1 
ATOM   671  C CD1 . TYR A 1 80  ? 21.161  -30.074 41.047  1.00 19.11  ? 305  TYR A CD1 1 
ATOM   672  C CD2 . TYR A 1 80  ? 22.504  -28.599 39.756  1.00 35.57  ? 305  TYR A CD2 1 
ATOM   673  C CE1 . TYR A 1 80  ? 22.229  -30.291 41.916  1.00 22.54  ? 305  TYR A CE1 1 
ATOM   674  C CE2 . TYR A 1 80  ? 23.571  -28.806 40.611  1.00 35.68  ? 305  TYR A CE2 1 
ATOM   675  C CZ  . TYR A 1 80  ? 23.422  -29.644 41.695  1.00 32.08  ? 305  TYR A CZ  1 
ATOM   676  O OH  . TYR A 1 80  ? 24.477  -29.857 42.553  1.00 42.15  ? 305  TYR A OH  1 
ATOM   677  N N   . GLU A 1 81  ? 17.310  -27.874 38.800  1.00 21.60  ? 306  GLU A N   1 
ATOM   678  C CA  . GLU A 1 81  ? 16.482  -27.090 37.899  1.00 17.11  ? 306  GLU A CA  1 
ATOM   679  C C   . GLU A 1 81  ? 17.347  -26.417 36.834  1.00 19.19  ? 306  GLU A C   1 
ATOM   680  O O   . GLU A 1 81  ? 18.574  -26.361 36.958  1.00 25.91  ? 306  GLU A O   1 
ATOM   681  C CB  . GLU A 1 81  ? 15.695  -26.038 38.679  1.00 23.21  ? 306  GLU A CB  1 
ATOM   682  C CG  . GLU A 1 81  ? 14.593  -26.595 39.585  1.00 24.21  ? 306  GLU A CG  1 
ATOM   683  C CD  . GLU A 1 81  ? 13.346  -27.074 38.832  1.00 31.51  ? 306  GLU A CD  1 
ATOM   684  O OE1 . GLU A 1 81  ? 13.289  -26.979 37.583  1.00 22.63  ? 306  GLU A OE1 1 
ATOM   685  O OE2 . GLU A 1 81  ? 12.410  -27.555 39.503  1.00 35.29  ? 306  GLU A OE2 1 
ATOM   686  N N   . PRO A 1 82  ? 16.730  -25.930 35.753  1.00 21.85  ? 307  PRO A N   1 
ATOM   687  C CA  . PRO A 1 82  ? 17.485  -25.126 34.773  1.00 20.19  ? 307  PRO A CA  1 
ATOM   688  C C   . PRO A 1 82  ? 18.287  -23.981 35.370  1.00 26.29  ? 307  PRO A C   1 
ATOM   689  O O   . PRO A 1 82  ? 19.377  -23.677 34.866  1.00 25.53  ? 307  PRO A O   1 
ATOM   690  C CB  . PRO A 1 82  ? 16.375  -24.605 33.850  1.00 22.27  ? 307  PRO A CB  1 
ATOM   691  C CG  . PRO A 1 82  ? 15.366  -25.723 33.839  1.00 22.04  ? 307  PRO A CG  1 
ATOM   692  C CD  . PRO A 1 82  ? 15.398  -26.316 35.238  1.00 23.39  ? 307  PRO A CD  1 
ATOM   693  N N   . ASP A 1 83  ? 17.799  -23.341 36.435  1.00 26.67  ? 308  ASP A N   1 
ATOM   694  C CA  . ASP A 1 83  ? 18.560  -22.240 37.017  1.00 43.03  ? 308  ASP A CA  1 
ATOM   695  C C   . ASP A 1 83  ? 19.790  -22.709 37.779  1.00 50.13  ? 308  ASP A C   1 
ATOM   696  O O   . ASP A 1 83  ? 20.537  -21.867 38.288  1.00 50.04  ? 308  ASP A O   1 
ATOM   697  C CB  . ASP A 1 83  ? 17.665  -21.390 37.928  1.00 36.40  ? 308  ASP A CB  1 
ATOM   698  C CG  . ASP A 1 83  ? 17.080  -22.174 39.102  1.00 62.61  ? 308  ASP A CG  1 
ATOM   699  O OD1 . ASP A 1 83  ? 17.614  -23.245 39.466  1.00 41.23  ? 308  ASP A OD1 1 
ATOM   700  O OD2 . ASP A 1 83  ? 16.065  -21.709 39.664  1.00 61.41  ? 308  ASP A OD2 1 
ATOM   701  N N   . GLY A 1 84  ? 20.022  -24.018 37.870  1.00 37.30  ? 309  GLY A N   1 
ATOM   702  C CA  . GLY A 1 84  ? 21.156  -24.548 38.585  1.00 31.95  ? 309  GLY A CA  1 
ATOM   703  C C   . GLY A 1 84  ? 20.911  -24.830 40.050  1.00 26.68  ? 309  GLY A C   1 
ATOM   704  O O   . GLY A 1 84  ? 21.779  -25.428 40.698  1.00 31.32  ? 309  GLY A O   1 
ATOM   705  N N   . SER A 1 85  ? 19.770  -24.413 40.594  1.00 30.71  ? 310  SER A N   1 
ATOM   706  C CA  . SER A 1 85  ? 19.421  -24.788 41.956  1.00 30.75  ? 310  SER A CA  1 
ATOM   707  C C   . SER A 1 85  ? 18.978  -26.244 41.995  1.00 32.01  ? 310  SER A C   1 
ATOM   708  O O   . SER A 1 85  ? 18.546  -26.813 40.987  1.00 26.92  ? 310  SER A O   1 
ATOM   709  C CB  . SER A 1 85  ? 18.305  -23.900 42.507  1.00 39.21  ? 310  SER A CB  1 
ATOM   710  O OG  . SER A 1 85  ? 17.080  -24.146 41.834  1.00 45.89  ? 310  SER A OG  1 
ATOM   711  N N   A VAL A 1 86  ? 19.084  -26.849 43.180  0.47 28.22  ? 311  VAL A N   1 
ATOM   712  N N   B VAL A 1 86  ? 19.082  -26.844 43.183  0.53 28.19  ? 311  VAL A N   1 
ATOM   713  C CA  A VAL A 1 86  ? 18.721  -28.253 43.321  0.47 24.41  ? 311  VAL A CA  1 
ATOM   714  C CA  B VAL A 1 86  ? 18.705  -28.243 43.347  0.53 24.37  ? 311  VAL A CA  1 
ATOM   715  C C   A VAL A 1 86  ? 17.210  -28.400 43.183  0.47 27.40  ? 311  VAL A C   1 
ATOM   716  C C   B VAL A 1 86  ? 17.200  -28.386 43.169  0.53 27.37  ? 311  VAL A C   1 
ATOM   717  O O   A VAL A 1 86  ? 16.434  -27.555 43.648  0.47 29.56  ? 311  VAL A O   1 
ATOM   718  O O   B VAL A 1 86  ? 16.416  -27.536 43.609  0.53 29.53  ? 311  VAL A O   1 
ATOM   719  C CB  A VAL A 1 86  ? 19.235  -28.821 44.657  0.47 39.97  ? 311  VAL A CB  1 
ATOM   720  C CB  B VAL A 1 86  ? 19.159  -28.771 44.719  0.53 40.06  ? 311  VAL A CB  1 
ATOM   721  C CG1 A VAL A 1 86  ? 18.542  -28.159 45.843  0.47 29.44  ? 311  VAL A CG1 1 
ATOM   722  C CG1 B VAL A 1 86  ? 18.944  -30.279 44.812  0.53 40.54  ? 311  VAL A CG1 1 
ATOM   723  C CG2 A VAL A 1 86  ? 19.063  -30.338 44.699  0.47 40.17  ? 311  VAL A CG2 1 
ATOM   724  C CG2 B VAL A 1 86  ? 20.616  -28.423 44.971  0.53 32.42  ? 311  VAL A CG2 1 
ATOM   725  N N   . PHE A 1 87  ? 16.786  -29.458 42.504  1.00 23.60  ? 312  PHE A N   1 
ATOM   726  C CA  . PHE A 1 87  ? 15.370  -29.746 42.366  1.00 21.70  ? 312  PHE A CA  1 
ATOM   727  C C   . PHE A 1 87  ? 14.856  -30.310 43.683  1.00 19.09  ? 312  PHE A C   1 
ATOM   728  O O   . PHE A 1 87  ? 15.434  -31.258 44.220  1.00 25.71  ? 312  PHE A O   1 
ATOM   729  C CB  . PHE A 1 87  ? 15.146  -30.738 41.228  1.00 20.33  ? 312  PHE A CB  1 
ATOM   730  C CG  . PHE A 1 87  ? 13.742  -31.250 41.153  1.00 16.52  ? 312  PHE A CG  1 
ATOM   731  C CD1 . PHE A 1 87  ? 12.738  -30.465 40.608  1.00 21.29  ? 312  PHE A CD1 1 
ATOM   732  C CD2 . PHE A 1 87  ? 13.421  -32.505 41.634  1.00 24.43  ? 312  PHE A CD2 1 
ATOM   733  C CE1 . PHE A 1 87  ? 11.439  -30.937 40.547  1.00 17.53  ? 312  PHE A CE1 1 
ATOM   734  C CE2 . PHE A 1 87  ? 12.126  -32.976 41.564  1.00 27.22  ? 312  PHE A CE2 1 
ATOM   735  C CZ  . PHE A 1 87  ? 11.139  -32.187 41.021  1.00 18.30  ? 312  PHE A CZ  1 
ATOM   736  N N   . ASN A 1 88  ? 13.788  -29.723 44.215  1.00 18.25  ? 313  ASN A N   1 
ATOM   737  C CA  . ASN A 1 88  ? 13.285  -30.150 45.514  1.00 21.07  ? 313  ASN A CA  1 
ATOM   738  C C   . ASN A 1 88  ? 12.017  -30.974 45.352  1.00 16.78  ? 313  ASN A C   1 
ATOM   739  O O   . ASN A 1 88  ? 10.953  -30.414 45.045  1.00 24.62  ? 313  ASN A O   1 
ATOM   740  C CB  . ASN A 1 88  ? 13.023  -28.955 46.428  1.00 29.78  ? 313  ASN A CB  1 
ATOM   741  C CG  . ASN A 1 88  ? 12.845  -29.373 47.879  1.00 46.03  ? 313  ASN A CG  1 
ATOM   742  O OD1 . ASN A 1 88  ? 12.697  -30.564 48.189  1.00 30.22  ? 313  ASN A OD1 1 
ATOM   743  N ND2 . ASN A 1 88  ? 12.864  -28.397 48.780  1.00 64.76  ? 313  ASN A ND2 1 
ATOM   744  N N   . PRO A 1 89  ? 12.077  -32.288 45.573  1.00 20.32  ? 314  PRO A N   1 
ATOM   745  C CA  . PRO A 1 89  ? 10.863  -33.109 45.447  1.00 17.01  ? 314  PRO A CA  1 
ATOM   746  C C   . PRO A 1 89  ? 9.730   -32.623 46.332  1.00 20.63  ? 314  PRO A C   1 
ATOM   747  O O   . PRO A 1 89  ? 8.559   -32.730 45.942  1.00 28.93  ? 314  PRO A O   1 
ATOM   748  C CB  . PRO A 1 89  ? 11.342  -34.506 45.872  1.00 22.18  ? 314  PRO A CB  1 
ATOM   749  C CG  . PRO A 1 89  ? 12.806  -34.500 45.634  1.00 27.90  ? 314  PRO A CG  1 
ATOM   750  C CD  . PRO A 1 89  ? 13.263  -33.093 45.908  1.00 30.02  ? 314  PRO A CD  1 
ATOM   751  N N   . LEU A 1 90  ? 10.048  -32.053 47.493  1.00 21.13  ? 315  LEU A N   1 
ATOM   752  C CA  . LEU A 1 90  ? 9.008   -31.643 48.431  1.00 20.65  ? 315  LEU A CA  1 
ATOM   753  C C   . LEU A 1 90  ? 8.155   -30.503 47.889  1.00 22.24  ? 315  LEU A C   1 
ATOM   754  O O   . LEU A 1 90  ? 7.071   -30.257 48.424  1.00 26.97  ? 315  LEU A O   1 
ATOM   755  C CB  . LEU A 1 90  ? 9.637   -31.241 49.769  1.00 20.96  ? 315  LEU A CB  1 
ATOM   756  C CG  . LEU A 1 90  ? 10.287  -32.370 50.570  1.00 28.69  ? 315  LEU A CG  1 
ATOM   757  C CD1 . LEU A 1 90  ? 10.963  -31.812 51.816  1.00 35.55  ? 315  LEU A CD1 1 
ATOM   758  C CD2 . LEU A 1 90  ? 9.259   -33.430 50.938  1.00 29.86  ? 315  LEU A CD2 1 
ATOM   759  N N   . SER A 1 91  ? 8.613   -29.812 46.847  1.00 22.81  ? 316  SER A N   1 
ATOM   760  C CA  . SER A 1 91  ? 7.860   -28.694 46.286  1.00 29.29  ? 316  SER A CA  1 
ATOM   761  C C   . SER A 1 91  ? 6.539   -29.125 45.661  1.00 27.02  ? 316  SER A C   1 
ATOM   762  O O   . SER A 1 91  ? 5.664   -28.278 45.447  1.00 27.62  ? 316  SER A O   1 
ATOM   763  C CB  . SER A 1 91  ? 8.689   -27.977 45.226  1.00 30.02  ? 316  SER A CB  1 
ATOM   764  O OG  . SER A 1 91  ? 8.827   -28.793 44.068  1.00 27.95  ? 316  SER A OG  1 
ATOM   765  N N   . GLY A 1 92  ? 6.382   -30.407 45.346  1.00 19.92  ? 317  GLY A N   1 
ATOM   766  C CA  . GLY A 1 92  ? 5.210   -30.878 44.642  1.00 19.85  ? 317  GLY A CA  1 
ATOM   767  C C   . GLY A 1 92  ? 5.341   -30.923 43.134  1.00 17.45  ? 317  GLY A C   1 
ATOM   768  O O   . GLY A 1 92  ? 4.430   -31.423 42.466  1.00 18.00  ? 317  GLY A O   1 
ATOM   769  N N   . ALA A 1 93  ? 6.441   -30.437 42.576  1.00 14.89  ? 318  ALA A N   1 
ATOM   770  C CA  . ALA A 1 93  ? 6.620   -30.517 41.136  1.00 14.75  ? 318  ALA A CA  1 
ATOM   771  C C   . ALA A 1 93  ? 6.867   -31.965 40.719  1.00 14.94  ? 318  ALA A C   1 
ATOM   772  O O   . ALA A 1 93  ? 7.548   -32.708 41.438  1.00 19.21  ? 318  ALA A O   1 
ATOM   773  C CB  . ALA A 1 93  ? 7.791   -29.646 40.696  1.00 16.00  ? 318  ALA A CB  1 
ATOM   774  N N   . PRO A 1 94  ? 6.330   -32.397 39.569  1.00 16.80  ? 319  PRO A N   1 
ATOM   775  C CA  . PRO A 1 94  ? 6.544   -33.787 39.136  1.00 14.34  ? 319  PRO A CA  1 
ATOM   776  C C   . PRO A 1 94  ? 7.931   -34.033 38.580  1.00 13.71  ? 319  PRO A C   1 
ATOM   777  O O   . PRO A 1 94  ? 8.338   -35.201 38.478  1.00 13.41  ? 319  PRO A O   1 
ATOM   778  C CB  . PRO A 1 94  ? 5.481   -33.979 38.038  1.00 16.05  ? 319  PRO A CB  1 
ATOM   779  C CG  . PRO A 1 94  ? 5.334   -32.618 37.444  1.00 16.18  ? 319  PRO A CG  1 
ATOM   780  C CD  . PRO A 1 94  ? 5.464   -31.657 38.631  1.00 15.87  ? 319  PRO A CD  1 
ATOM   781  N N   . ALA A 1 95  ? 8.653   -32.980 38.212  1.00 12.47  ? 320  ALA A N   1 
ATOM   782  C CA  . ALA A 1 95  ? 9.932   -33.088 37.524  1.00 13.17  ? 320  ALA A CA  1 
ATOM   783  C C   . ALA A 1 95  ? 10.522  -31.691 37.398  1.00 13.74  ? 320  ALA A C   1 
ATOM   784  O O   . ALA A 1 95  ? 9.794   -30.696 37.534  1.00 15.99  ? 320  ALA A O   1 
ATOM   785  C CB  . ALA A 1 95  ? 9.765   -33.720 36.129  1.00 12.54  ? 320  ALA A CB  1 
ATOM   786  N N   . PRO A 1 96  ? 11.824  -31.583 37.128  1.00 15.62  ? 321  PRO A N   1 
ATOM   787  C CA  . PRO A 1 96  ? 12.374  -30.277 36.754  1.00 10.78  ? 321  PRO A CA  1 
ATOM   788  C C   . PRO A 1 96  ? 11.675  -29.747 35.508  1.00 11.47  ? 321  PRO A C   1 
ATOM   789  O O   . PRO A 1 96  ? 11.168  -30.518 34.684  1.00 13.17  ? 321  PRO A O   1 
ATOM   790  C CB  . PRO A 1 96  ? 13.856  -30.576 36.478  1.00 14.76  ? 321  PRO A CB  1 
ATOM   791  C CG  . PRO A 1 96  ? 14.131  -31.832 37.264  1.00 11.82  ? 321  PRO A CG  1 
ATOM   792  C CD  . PRO A 1 96  ? 12.863  -32.629 37.185  1.00 16.03  ? 321  PRO A CD  1 
ATOM   793  N N   . GLU A 1 97  ? 11.662  -28.416 35.373  1.00 12.83  ? 322  GLU A N   1 
ATOM   794  C CA  . GLU A 1 97  ? 11.090  -27.775 34.189  1.00 14.38  ? 322  GLU A CA  1 
ATOM   795  C C   . GLU A 1 97  ? 11.669  -28.374 32.914  1.00 14.90  ? 322  GLU A C   1 
ATOM   796  O O   . GLU A 1 97  ? 12.878  -28.586 32.805  1.00 17.44  ? 322  GLU A O   1 
ATOM   797  C CB  . GLU A 1 97  ? 11.376  -26.267 34.191  1.00 21.07  ? 322  GLU A CB  1 
ATOM   798  C CG  . GLU A 1 97  ? 10.714  -25.463 35.275  1.00 34.50  ? 322  GLU A CG  1 
ATOM   799  C CD  . GLU A 1 97  ? 10.971  -23.964 35.121  1.00 26.03  ? 322  GLU A CD  1 
ATOM   800  O OE1 . GLU A 1 97  ? 11.476  -23.530 34.051  1.00 33.18  ? 322  GLU A OE1 1 
ATOM   801  O OE2 . GLU A 1 97  ? 10.652  -23.222 36.064  1.00 42.37  ? 322  GLU A OE2 1 
ATOM   802  N N   . GLY A 1 98  ? 10.797  -28.633 31.938  1.00 12.00  ? 323  GLY A N   1 
ATOM   803  C CA  . GLY A 1 98  ? 11.226  -29.109 30.646  1.00 12.06  ? 323  GLY A CA  1 
ATOM   804  C C   . GLY A 1 98  ? 11.302  -30.614 30.493  1.00 10.74  ? 323  GLY A C   1 
ATOM   805  O O   . GLY A 1 98  ? 11.503  -31.093 29.367  1.00 13.79  ? 323  GLY A O   1 
ATOM   806  N N   . PHE A 1 99  ? 11.147  -31.378 31.578  1.00 11.86  ? 324  PHE A N   1 
ATOM   807  C CA  . PHE A 1 99  ? 11.216  -32.830 31.475  1.00 10.91  ? 324  PHE A CA  1 
ATOM   808  C C   . PHE A 1 99  ? 10.026  -33.384 30.688  1.00 10.93  ? 324  PHE A C   1 
ATOM   809  O O   . PHE A 1 99  ? 8.902   -32.879 30.799  1.00 12.09  ? 324  PHE A O   1 
ATOM   810  C CB  . PHE A 1 99  ? 11.239  -33.478 32.859  1.00 9.77   ? 324  PHE A CB  1 
ATOM   811  C CG  . PHE A 1 99  ? 12.609  -33.901 33.316  1.00 10.92  ? 324  PHE A CG  1 
ATOM   812  C CD1 . PHE A 1 99  ? 13.599  -32.957 33.546  1.00 13.67  ? 324  PHE A CD1 1 
ATOM   813  C CD2 . PHE A 1 99  ? 12.902  -35.246 33.534  1.00 15.77  ? 324  PHE A CD2 1 
ATOM   814  C CE1 . PHE A 1 99  ? 14.851  -33.336 33.978  1.00 13.04  ? 324  PHE A CE1 1 
ATOM   815  C CE2 . PHE A 1 99  ? 14.174  -35.634 33.959  1.00 15.54  ? 324  PHE A CE2 1 
ATOM   816  C CZ  . PHE A 1 99  ? 15.143  -34.677 34.179  1.00 14.68  ? 324  PHE A CZ  1 
ATOM   817  N N   . PRO A 1 100 ? 10.242  -34.450 29.921  1.00 11.53  ? 325  PRO A N   1 
ATOM   818  C CA  . PRO A 1 100 ? 9.134   -35.116 29.218  1.00 14.30  ? 325  PRO A CA  1 
ATOM   819  C C   . PRO A 1 100 ? 7.932   -35.420 30.114  1.00 11.91  ? 325  PRO A C   1 
ATOM   820  O O   . PRO A 1 100 ? 8.070   -35.850 31.266  1.00 14.30  ? 325  PRO A O   1 
ATOM   821  C CB  . PRO A 1 100 ? 9.784   -36.402 28.691  1.00 16.08  ? 325  PRO A CB  1 
ATOM   822  C CG  . PRO A 1 100 ? 11.214  -35.992 28.450  1.00 16.90  ? 325  PRO A CG  1 
ATOM   823  C CD  . PRO A 1 100 ? 11.543  -35.076 29.625  1.00 14.41  ? 325  PRO A CD  1 
ATOM   824  N N   . ASP A 1 101 ? 6.738   -35.199 29.553  1.00 11.47  ? 326  ASP A N   1 
ATOM   825  C CA  . ASP A 1 101 ? 5.460   -35.275 30.255  1.00 11.95  ? 326  ASP A CA  1 
ATOM   826  C C   . ASP A 1 101 ? 4.569   -36.369 29.667  1.00 14.11  ? 326  ASP A C   1 
ATOM   827  O O   . ASP A 1 101 ? 3.336   -36.242 29.605  1.00 14.85  ? 326  ASP A O   1 
ATOM   828  C CB  . ASP A 1 101 ? 4.749   -33.923 30.214  1.00 12.50  ? 326  ASP A CB  1 
ATOM   829  C CG  . ASP A 1 101 ? 4.318   -33.539 28.805  1.00 14.58  ? 326  ASP A CG  1 
ATOM   830  O OD1 . ASP A 1 101 ? 4.850   -34.133 27.846  1.00 13.19  ? 326  ASP A OD1 1 
ATOM   831  O OD2 . ASP A 1 101 ? 3.458   -32.640 28.657  1.00 14.43  ? 326  ASP A OD2 1 
ATOM   832  N N   . PHE A 1 102 ? 5.175   -37.467 29.224  1.00 11.00  ? 327  PHE A N   1 
ATOM   833  C CA  . PHE A 1 102 ? 4.403   -38.558 28.642  1.00 11.40  ? 327  PHE A CA  1 
ATOM   834  C C   . PHE A 1 102 ? 5.114   -39.879 28.901  1.00 15.33  ? 327  PHE A C   1 
ATOM   835  O O   . PHE A 1 102 ? 6.280   -39.917 29.308  1.00 15.44  ? 327  PHE A O   1 
ATOM   836  C CB  . PHE A 1 102 ? 4.196   -38.344 27.147  1.00 14.28  ? 327  PHE A CB  1 
ATOM   837  C CG  . PHE A 1 102 ? 5.477   -38.299 26.370  1.00 13.51  ? 327  PHE A CG  1 
ATOM   838  C CD1 . PHE A 1 102 ? 6.154   -37.099 26.175  1.00 14.83  ? 327  PHE A CD1 1 
ATOM   839  C CD2 . PHE A 1 102 ? 6.012   -39.460 25.831  1.00 14.18  ? 327  PHE A CD2 1 
ATOM   840  C CE1 . PHE A 1 102 ? 7.343   -37.064 25.454  1.00 15.51  ? 327  PHE A CE1 1 
ATOM   841  C CE2 . PHE A 1 102 ? 7.201   -39.436 25.125  1.00 13.78  ? 327  PHE A CE2 1 
ATOM   842  C CZ  . PHE A 1 102 ? 7.866   -38.231 24.929  1.00 15.32  ? 327  PHE A CZ  1 
ATOM   843  N N   . THR A 1 103 ? 4.392   -40.966 28.617  1.00 15.21  ? 328  THR A N   1 
ATOM   844  C CA  . THR A 1 103 ? 4.855   -42.330 28.851  1.00 14.24  ? 328  THR A CA  1 
ATOM   845  C C   . THR A 1 103 ? 5.591   -42.866 27.629  1.00 15.52  ? 328  THR A C   1 
ATOM   846  O O   . THR A 1 103 ? 5.123   -42.709 26.497  1.00 14.69  ? 328  THR A O   1 
ATOM   847  C CB  . THR A 1 103 ? 3.656   -43.224 29.196  1.00 16.04  ? 328  THR A CB  1 
ATOM   848  O OG1 . THR A 1 103 ? 3.057   -42.765 30.414  1.00 19.15  ? 328  THR A OG1 1 
ATOM   849  C CG2 . THR A 1 103 ? 4.076   -44.691 29.365  1.00 18.76  ? 328  THR A CG2 1 
ATOM   850  N N   . ALA A 1 104 ? 6.752   -43.480 27.862  1.00 15.34  ? 329  ALA A N   1 
ATOM   851  C CA  . ALA A 1 104 ? 7.556   -44.104 26.819  1.00 15.83  ? 329  ALA A CA  1 
ATOM   852  C C   . ALA A 1 104 ? 8.298   -45.271 27.452  1.00 17.95  ? 329  ALA A C   1 
ATOM   853  O O   . ALA A 1 104 ? 8.415   -45.345 28.674  1.00 17.00  ? 329  ALA A O   1 
ATOM   854  C CB  . ALA A 1 104 ? 8.545   -43.111 26.192  1.00 13.35  ? 329  ALA A CB  1 
ATOM   855  N N   . GLN A 1 105 ? 8.798   -46.190 26.617  1.00 16.53  ? 330  GLN A N   1 
ATOM   856  C CA  . GLN A 1 105 ? 9.564   -47.315 27.152  1.00 13.29  ? 330  GLN A CA  1 
ATOM   857  C C   . GLN A 1 105 ? 10.987  -46.910 27.496  1.00 17.68  ? 330  GLN A C   1 
ATOM   858  O O   . GLN A 1 105 ? 11.574  -47.455 28.437  1.00 16.00  ? 330  GLN A O   1 
ATOM   859  C CB  . GLN A 1 105 ? 9.588   -48.487 26.166  1.00 15.69  ? 330  GLN A CB  1 
ATOM   860  C CG  . GLN A 1 105 ? 8.245   -49.200 26.043  1.00 19.84  ? 330  GLN A CG  1 
ATOM   861  C CD  . GLN A 1 105 ? 7.247   -48.384 25.248  1.00 22.55  ? 330  GLN A CD  1 
ATOM   862  O OE1 . GLN A 1 105 ? 7.535   -47.973 24.134  1.00 18.20  ? 330  GLN A OE1 1 
ATOM   863  N NE2 . GLN A 1 105 ? 6.081   -48.126 25.828  1.00 19.41  ? 330  GLN A NE2 1 
ATOM   864  N N   A GLU A 1 106 ? 11.552  -45.979 26.729  0.68 15.47  ? 331  GLU A N   1 
ATOM   865  N N   B GLU A 1 106 ? 11.554  -45.959 26.769  0.32 15.47  ? 331  GLU A N   1 
ATOM   866  C CA  A GLU A 1 106 ? 12.896  -45.458 26.937  0.68 14.88  ? 331  GLU A CA  1 
ATOM   867  C CA  B GLU A 1 106 ? 12.849  -45.430 27.160  0.32 14.51  ? 331  GLU A CA  1 
ATOM   868  C C   A GLU A 1 106 ? 12.887  -43.986 26.569  0.68 13.41  ? 331  GLU A C   1 
ATOM   869  C C   B GLU A 1 106 ? 13.016  -44.062 26.530  0.32 13.74  ? 331  GLU A C   1 
ATOM   870  O O   A GLU A 1 106 ? 12.144  -43.567 25.676  0.68 14.53  ? 331  GLU A O   1 
ATOM   871  O O   B GLU A 1 106 ? 12.503  -43.794 25.440  0.32 12.32  ? 331  GLU A O   1 
ATOM   872  C CB  A GLU A 1 106 ? 13.947  -46.171 26.073  0.68 16.76  ? 331  GLU A CB  1 
ATOM   873  C CB  B GLU A 1 106 ? 14.001  -46.357 26.759  0.32 18.83  ? 331  GLU A CB  1 
ATOM   874  C CG  A GLU A 1 106 ? 14.221  -47.618 26.427  0.68 15.50  ? 331  GLU A CG  1 
ATOM   875  C CG  B GLU A 1 106 ? 13.947  -46.843 25.330  0.32 17.99  ? 331  GLU A CG  1 
ATOM   876  C CD  A GLU A 1 106 ? 13.290  -48.582 25.727  0.68 18.86  ? 331  GLU A CD  1 
ATOM   877  C CD  B GLU A 1 106 ? 13.194  -48.150 25.184  0.32 19.79  ? 331  GLU A CD  1 
ATOM   878  O OE1 A GLU A 1 106 ? 12.751  -48.221 24.659  0.68 20.52  ? 331  GLU A OE1 1 
ATOM   879  O OE1 B GLU A 1 106 ? 13.149  -48.928 26.160  0.32 23.98  ? 331  GLU A OE1 1 
ATOM   880  O OE2 A GLU A 1 106 ? 13.094  -49.698 26.253  0.68 20.63  ? 331  GLU A OE2 1 
ATOM   881  O OE2 B GLU A 1 106 ? 12.647  -48.400 24.090  0.32 25.05  ? 331  GLU A OE2 1 
ATOM   882  N N   . TYR A 1 107 ? 13.731  -43.206 27.244  1.00 13.43  ? 332  TYR A N   1 
ATOM   883  C CA  . TYR A 1 107 ? 13.999  -41.833 26.847  1.00 13.02  ? 332  TYR A CA  1 
ATOM   884  C C   . TYR A 1 107 ? 15.483  -41.777 26.512  1.00 15.86  ? 332  TYR A C   1 
ATOM   885  O O   . TYR A 1 107 ? 16.323  -41.898 27.412  1.00 15.36  ? 332  TYR A O   1 
ATOM   886  C CB  . TYR A 1 107 ? 13.633  -40.855 27.966  1.00 11.51  ? 332  TYR A CB  1 
ATOM   887  C CG  . TYR A 1 107 ? 12.221  -41.016 28.494  1.00 11.72  ? 332  TYR A CG  1 
ATOM   888  C CD1 . TYR A 1 107 ? 11.918  -42.011 29.404  1.00 15.25  ? 332  TYR A CD1 1 
ATOM   889  C CD2 . TYR A 1 107 ? 11.190  -40.169 28.073  1.00 15.41  ? 332  TYR A CD2 1 
ATOM   890  C CE1 . TYR A 1 107 ? 10.633  -42.171 29.888  1.00 13.35  ? 332  TYR A CE1 1 
ATOM   891  C CE2 . TYR A 1 107 ? 9.900   -40.320 28.559  1.00 12.50  ? 332  TYR A CE2 1 
ATOM   892  C CZ  . TYR A 1 107 ? 9.633   -41.324 29.466  1.00 15.80  ? 332  TYR A CZ  1 
ATOM   893  O OH  . TYR A 1 107 ? 8.361   -41.509 29.962  1.00 13.99  ? 332  TYR A OH  1 
ATOM   894  N N   . HIS A 1 108 ? 15.806  -41.633 25.222  1.00 11.60  ? 333  HIS A N   1 
ATOM   895  C CA  . HIS A 1 108 ? 17.200  -41.659 24.786  1.00 14.66  ? 333  HIS A CA  1 
ATOM   896  C C   . HIS A 1 108 ? 17.831  -40.293 24.975  1.00 12.53  ? 333  HIS A C   1 
ATOM   897  O O   . HIS A 1 108 ? 17.185  -39.264 24.751  1.00 12.86  ? 333  HIS A O   1 
ATOM   898  C CB  . HIS A 1 108 ? 17.310  -42.048 23.313  1.00 14.35  ? 333  HIS A CB  1 
ATOM   899  C CG  . HIS A 1 108 ? 16.596  -43.312 22.965  1.00 15.74  ? 333  HIS A CG  1 
ATOM   900  N ND1 . HIS A 1 108 ? 15.687  -43.384 21.933  1.00 17.90  ? 333  HIS A ND1 1 
ATOM   901  C CD2 . HIS A 1 108 ? 16.667  -44.555 23.498  1.00 17.92  ? 333  HIS A CD2 1 
ATOM   902  C CE1 . HIS A 1 108 ? 15.220  -44.618 21.850  1.00 17.88  ? 333  HIS A CE1 1 
ATOM   903  N NE2 . HIS A 1 108 ? 15.798  -45.348 22.786  1.00 16.50  ? 333  HIS A NE2 1 
ATOM   904  N N   . LEU A 1 109 ? 19.107  -40.274 25.359  1.00 10.97  ? 334  LEU A N   1 
ATOM   905  C CA  . LEU A 1 109 ? 19.703  -38.992 25.706  1.00 12.51  ? 334  LEU A CA  1 
ATOM   906  C C   . LEU A 1 109 ? 21.172  -38.939 25.310  1.00 14.21  ? 334  LEU A C   1 
ATOM   907  O O   . LEU A 1 109 ? 21.802  -39.951 24.982  1.00 12.99  ? 334  LEU A O   1 
ATOM   908  C CB  . LEU A 1 109 ? 19.520  -38.697 27.203  1.00 11.15  ? 334  LEU A CB  1 
ATOM   909  C CG  . LEU A 1 109 ? 20.109  -39.683 28.225  1.00 13.66  ? 334  LEU A CG  1 
ATOM   910  C CD1 . LEU A 1 109 ? 21.608  -39.491 28.461  1.00 13.38  ? 334  LEU A CD1 1 
ATOM   911  C CD2 . LEU A 1 109 ? 19.370  -39.571 29.543  1.00 12.71  ? 334  LEU A CD2 1 
ATOM   912  N N   . ARG A 1 110 ? 21.695  -37.713 25.318  1.00 12.14  ? 335  ARG A N   1 
ATOM   913  C CA  . ARG A 1 110 ? 23.121  -37.428 25.287  1.00 10.74  ? 335  ARG A CA  1 
ATOM   914  C C   . ARG A 1 110 ? 23.403  -36.440 26.404  1.00 13.24  ? 335  ARG A C   1 
ATOM   915  O O   . ARG A 1 110 ? 22.545  -35.625 26.750  1.00 12.89  ? 335  ARG A O   1 
ATOM   916  C CB  . ARG A 1 110 ? 23.584  -36.804 23.964  1.00 14.67  ? 335  ARG A CB  1 
ATOM   917  C CG  . ARG A 1 110 ? 23.653  -37.729 22.764  1.00 21.06  ? 335  ARG A CG  1 
ATOM   918  C CD  . ARG A 1 110 ? 24.181  -36.936 21.538  1.00 16.61  ? 335  ARG A CD  1 
ATOM   919  N NE  . ARG A 1 110 ? 23.807  -37.575 20.288  1.00 23.42  ? 335  ARG A NE  1 
ATOM   920  C CZ  . ARG A 1 110 ? 24.613  -38.367 19.604  1.00 23.50  ? 335  ARG A CZ  1 
ATOM   921  N NH1 . ARG A 1 110 ? 25.843  -38.617 20.020  1.00 20.09  ? 335  ARG A NH1 1 
ATOM   922  N NH2 . ARG A 1 110 ? 24.178  -38.919 18.474  1.00 40.96  ? 335  ARG A NH2 1 
ATOM   923  N N   . ALA A 1 111 ? 24.607  -36.502 26.961  1.00 12.13  ? 336  ALA A N   1 
ATOM   924  C CA  . ALA A 1 111 ? 24.961  -35.585 28.034  1.00 12.04  ? 336  ALA A CA  1 
ATOM   925  C C   . ALA A 1 111 ? 26.466  -35.380 28.049  1.00 15.11  ? 336  ALA A C   1 
ATOM   926  O O   . ALA A 1 111 ? 27.220  -36.159 27.463  1.00 13.83  ? 336  ALA A O   1 
ATOM   927  C CB  . ALA A 1 111 ? 24.477  -36.109 29.397  1.00 10.12  ? 336  ALA A CB  1 
ATOM   928  N N   . ALA A 1 112 ? 26.894  -34.322 28.742  1.00 12.59  ? 337  ALA A N   1 
ATOM   929  C CA  . ALA A 1 112 ? 28.310  -34.008 28.885  1.00 10.41  ? 337  ALA A CA  1 
ATOM   930  C C   . ALA A 1 112 ? 28.495  -33.142 30.125  1.00 15.84  ? 337  ALA A C   1 
ATOM   931  O O   . ALA A 1 112 ? 27.581  -32.418 30.530  1.00 15.28  ? 337  ALA A O   1 
ATOM   932  C CB  . ALA A 1 112 ? 28.853  -33.265 27.655  1.00 13.38  ? 337  ALA A CB  1 
ATOM   933  N N   . GLY A 1 113 ? 29.696  -33.202 30.700  1.00 15.01  ? 338  GLY A N   1 
ATOM   934  C CA  . GLY A 1 113 ? 30.119  -32.287 31.735  1.00 16.34  ? 338  GLY A CA  1 
ATOM   935  C C   . GLY A 1 113 ? 31.228  -31.367 31.242  1.00 17.76  ? 338  GLY A C   1 
ATOM   936  O O   . GLY A 1 113 ? 31.611  -31.365 30.077  1.00 16.60  ? 338  GLY A O   1 
ATOM   937  N N   . LYS A 1 114 ? 31.744  -30.562 32.169  1.00 18.65  ? 339  LYS A N   1 
ATOM   938  C CA  . LYS A 1 114 ? 32.761  -29.578 31.823  1.00 20.53  ? 339  LYS A CA  1 
ATOM   939  C C   . LYS A 1 114 ? 34.174  -30.148 31.857  1.00 25.34  ? 339  LYS A C   1 
ATOM   940  O O   . LYS A 1 114 ? 35.136  -29.392 31.678  1.00 25.65  ? 339  LYS A O   1 
ATOM   941  C CB  . LYS A 1 114 ? 32.661  -28.376 32.763  1.00 28.88  ? 339  LYS A CB  1 
ATOM   942  C CG  . LYS A 1 114 ? 31.251  -27.827 32.848  1.00 55.22  ? 339  LYS A CG  1 
ATOM   943  C CD  . LYS A 1 114 ? 31.128  -26.723 33.872  1.00 46.35  ? 339  LYS A CD  1 
ATOM   944  C CE  . LYS A 1 114 ? 31.216  -27.250 35.288  1.00 41.13  ? 339  LYS A CE  1 
ATOM   945  N NZ  . LYS A 1 114 ? 30.940  -26.164 36.271  1.00 52.57  ? 339  LYS A NZ  1 
ATOM   946  N N   . VAL A 1 115 ? 34.325  -31.452 32.091  1.00 20.01  ? 340  VAL A N   1 
ATOM   947  C CA  . VAL A 1 115 ? 35.632  -32.090 32.138  1.00 18.81  ? 340  VAL A CA  1 
ATOM   948  C C   . VAL A 1 115 ? 35.663  -33.214 31.115  1.00 18.76  ? 340  VAL A C   1 
ATOM   949  O O   . VAL A 1 115 ? 34.635  -33.626 30.569  1.00 17.94  ? 340  VAL A O   1 
ATOM   950  C CB  . VAL A 1 115 ? 35.990  -32.628 33.538  1.00 20.47  ? 340  VAL A CB  1 
ATOM   951  C CG1 . VAL A 1 115 ? 36.084  -31.484 34.528  1.00 24.41  ? 340  VAL A CG1 1 
ATOM   952  C CG2 . VAL A 1 115 ? 34.966  -33.655 33.989  1.00 22.92  ? 340  VAL A CG2 1 
ATOM   953  N N   . ALA A 1 116 ? 36.868  -33.708 30.862  1.00 22.10  ? 341  ALA A N   1 
ATOM   954  C CA  . ALA A 1 116 ? 37.076  -34.680 29.807  1.00 26.37  ? 341  ALA A CA  1 
ATOM   955  C C   . ALA A 1 116 ? 36.437  -36.015 30.171  1.00 21.35  ? 341  ALA A C   1 
ATOM   956  O O   . ALA A 1 116 ? 36.222  -36.333 31.342  1.00 20.51  ? 341  ALA A O   1 
ATOM   957  C CB  . ALA A 1 116 ? 38.569  -34.874 29.549  1.00 29.87  ? 341  ALA A CB  1 
ATOM   958  N N   . ASN A 1 117 ? 36.130  -36.791 29.131  1.00 18.31  ? 342  ASN A N   1 
ATOM   959  C CA  . ASN A 1 117 ? 35.619  -38.158 29.249  1.00 18.84  ? 342  ASN A CA  1 
ATOM   960  C C   . ASN A 1 117 ? 34.247  -38.201 29.910  1.00 15.20  ? 342  ASN A C   1 
ATOM   961  O O   . ASN A 1 117 ? 33.898  -39.170 30.588  1.00 20.32  ? 342  ASN A O   1 
ATOM   962  C CB  . ASN A 1 117 ? 36.604  -39.069 29.979  1.00 22.73  ? 342  ASN A CB  1 
ATOM   963  C CG  . ASN A 1 117 ? 37.791  -39.414 29.121  1.00 41.41  ? 342  ASN A CG  1 
ATOM   964  O OD1 . ASN A 1 117 ? 37.667  -40.161 28.149  1.00 41.73  ? 342  ASN A OD1 1 
ATOM   965  N ND2 . ASN A 1 117 ? 38.945  -38.856 29.454  1.00 34.93  ? 342  ASN A ND2 1 
ATOM   966  N N   . THR A 1 118 ? 33.440  -37.166 29.692  1.00 15.18  ? 343  THR A N   1 
ATOM   967  C CA  . THR A 1 118 ? 32.080  -37.151 30.205  1.00 17.78  ? 343  THR A CA  1 
ATOM   968  C C   . THR A 1 118 ? 31.017  -37.046 29.124  1.00 16.36  ? 343  THR A C   1 
ATOM   969  O O   . THR A 1 118 ? 29.831  -37.087 29.455  1.00 15.63  ? 343  THR A O   1 
ATOM   970  C CB  . THR A 1 118 ? 31.884  -36.010 31.219  1.00 15.75  ? 343  THR A CB  1 
ATOM   971  O OG1 . THR A 1 118 ? 32.173  -34.748 30.605  1.00 14.83  ? 343  THR A OG1 1 
ATOM   972  C CG2 . THR A 1 118 ? 32.781  -36.198 32.427  1.00 15.90  ? 343  THR A CG2 1 
ATOM   973  N N   . THR A 1 119 ? 31.389  -36.906 27.848  1.00 11.64  ? 344  THR A N   1 
ATOM   974  C CA  . THR A 1 119 ? 30.394  -36.901 26.783  1.00 12.30  ? 344  THR A CA  1 
ATOM   975  C C   . THR A 1 119 ? 29.937  -38.324 26.517  1.00 15.05  ? 344  THR A C   1 
ATOM   976  O O   . THR A 1 119 ? 30.753  -39.204 26.234  1.00 14.06  ? 344  THR A O   1 
ATOM   977  C CB  . THR A 1 119 ? 30.968  -36.302 25.502  1.00 14.67  ? 344  THR A CB  1 
ATOM   978  O OG1 . THR A 1 119 ? 31.222  -34.907 25.696  1.00 16.48  ? 344  THR A OG1 1 
ATOM   979  C CG2 . THR A 1 119 ? 30.002  -36.483 24.340  1.00 14.29  ? 344  THR A CG2 1 
ATOM   980  N N   . GLY A 1 120 ? 28.634  -38.548 26.590  1.00 14.89  ? 345  GLY A N   1 
ATOM   981  C CA  . GLY A 1 120 ? 28.173  -39.892 26.316  1.00 14.29  ? 345  GLY A CA  1 
ATOM   982  C C   . GLY A 1 120 ? 26.731  -39.895 25.874  1.00 14.78  ? 345  GLY A C   1 
ATOM   983  O O   . GLY A 1 120 ? 26.035  -38.876 25.885  1.00 12.87  ? 345  GLY A O   1 
ATOM   984  N N   . GLY A 1 121 ? 26.305  -41.079 25.466  1.00 13.56  ? 346  GLY A N   1 
ATOM   985  C CA  . GLY A 1 121 ? 24.902  -41.330 25.233  1.00 16.54  ? 346  GLY A CA  1 
ATOM   986  C C   . GLY A 1 121 ? 24.393  -42.372 26.205  1.00 14.95  ? 346  GLY A C   1 
ATOM   987  O O   . GLY A 1 121 ? 25.168  -43.185 26.726  1.00 13.97  ? 346  GLY A O   1 
ATOM   988  N N   . GLY A 1 122 ? 23.101  -42.344 26.473  1.00 16.27  ? 347  GLY A N   1 
ATOM   989  C CA  . GLY A 1 122 ? 22.490  -43.362 27.297  1.00 13.17  ? 347  GLY A CA  1 
ATOM   990  C C   . GLY A 1 122 ? 20.989  -43.256 27.189  1.00 14.01  ? 347  GLY A C   1 
ATOM   991  O O   . GLY A 1 122 ? 20.458  -42.679 26.241  1.00 13.15  ? 347  GLY A O   1 
ATOM   992  N N   . GLU A 1 123 ? 20.296  -43.828 28.163  1.00 12.31  ? 348  GLU A N   1 
ATOM   993  C CA  . GLU A 1 123 ? 18.845  -43.731 28.140  1.00 12.59  ? 348  GLU A CA  1 
ATOM   994  C C   . GLU A 1 123 ? 18.312  -43.837 29.559  1.00 14.88  ? 348  GLU A C   1 
ATOM   995  O O   . GLU A 1 123 ? 18.999  -44.307 30.469  1.00 15.08  ? 348  GLU A O   1 
ATOM   996  C CB  . GLU A 1 123 ? 18.222  -44.820 27.260  1.00 14.88  ? 348  GLU A CB  1 
ATOM   997  C CG  . GLU A 1 123 ? 18.438  -46.227 27.803  1.00 15.59  ? 348  GLU A CG  1 
ATOM   998  C CD  . GLU A 1 123 ? 18.046  -47.306 26.811  1.00 23.24  ? 348  GLU A CD  1 
ATOM   999  O OE1 . GLU A 1 123 ? 17.933  -46.998 25.604  1.00 24.47  ? 348  GLU A OE1 1 
ATOM   1000 O OE2 . GLU A 1 123 ? 17.846  -48.458 27.242  1.00 22.89  ? 348  GLU A OE2 1 
ATOM   1001 N N   . ILE A 1 124 ? 17.073  -43.396 29.739  1.00 13.48  ? 349  ILE A N   1 
ATOM   1002 C CA  . ILE A 1 124 ? 16.336  -43.631 30.977  1.00 13.58  ? 349  ILE A CA  1 
ATOM   1003 C C   . ILE A 1 124 ? 15.226  -44.615 30.652  1.00 14.60  ? 349  ILE A C   1 
ATOM   1004 O O   . ILE A 1 124 ? 14.303  -44.293 29.896  1.00 15.47  ? 349  ILE A O   1 
ATOM   1005 C CB  . ILE A 1 124 ? 15.767  -42.335 31.570  1.00 13.86  ? 349  ILE A CB  1 
ATOM   1006 C CG1 . ILE A 1 124 ? 16.886  -41.314 31.757  1.00 11.55  ? 349  ILE A CG1 1 
ATOM   1007 C CG2 . ILE A 1 124 ? 15.090  -42.621 32.933  1.00 13.49  ? 349  ILE A CG2 1 
ATOM   1008 C CD1 . ILE A 1 124 ? 16.391  -39.919 32.053  1.00 17.43  ? 349  ILE A CD1 1 
ATOM   1009 N N   . LYS A 1 125 ? 15.316  -45.823 31.201  1.00 13.01  ? 350  LYS A N   1 
ATOM   1010 C CA  . LYS A 1 125 ? 14.242  -46.792 31.023  1.00 15.39  ? 350  LYS A CA  1 
ATOM   1011 C C   . LYS A 1 125 ? 12.996  -46.313 31.761  1.00 16.10  ? 350  LYS A C   1 
ATOM   1012 O O   . LYS A 1 125 ? 13.085  -45.606 32.768  1.00 15.96  ? 350  LYS A O   1 
ATOM   1013 C CB  . LYS A 1 125 ? 14.698  -48.162 31.532  1.00 17.80  ? 350  LYS A CB  1 
ATOM   1014 C CG  . LYS A 1 125 ? 15.859  -48.726 30.697  1.00 23.09  ? 350  LYS A CG  1 
ATOM   1015 C CD  . LYS A 1 125 ? 16.434  -50.035 31.237  1.00 31.41  ? 350  LYS A CD  1 
ATOM   1016 C CE  . LYS A 1 125 ? 17.461  -50.627 30.247  1.00 33.61  ? 350  LYS A CE  1 
ATOM   1017 N NZ  . LYS A 1 125 ? 18.487  -49.623 29.742  1.00 23.83  ? 350  LYS A NZ  1 
ATOM   1018 N N   . SER A 1 126 ? 11.821  -46.692 31.242  1.00 15.86  ? 351  SER A N   1 
ATOM   1019 C CA  . SER A 1 126 ? 10.557  -46.254 31.842  1.00 13.13  ? 351  SER A CA  1 
ATOM   1020 C C   . SER A 1 126 ? 10.534  -46.461 33.354  1.00 19.13  ? 351  SER A C   1 
ATOM   1021 O O   . SER A 1 126 ? 10.159  -45.557 34.107  1.00 17.08  ? 351  SER A O   1 
ATOM   1022 C CB  . SER A 1 126 ? 9.376   -46.988 31.199  1.00 16.69  ? 351  SER A CB  1 
ATOM   1023 O OG  . SER A 1 126 ? 8.155   -46.454 31.688  1.00 16.54  ? 351  SER A OG  1 
ATOM   1024 N N   . THR A 1 127 ? 10.937  -47.647 33.822  1.00 17.21  ? 352  THR A N   1 
ATOM   1025 C CA  . THR A 1 127 ? 10.882  -47.934 35.250  1.00 17.26  ? 352  THR A CA  1 
ATOM   1026 C C   . THR A 1 127 ? 11.782  -46.999 36.051  1.00 16.16  ? 352  THR A C   1 
ATOM   1027 O O   . THR A 1 127 ? 11.539  -46.789 37.242  1.00 19.64  ? 352  THR A O   1 
ATOM   1028 C CB  . THR A 1 127 ? 11.254  -49.406 35.500  1.00 20.55  ? 352  THR A CB  1 
ATOM   1029 O OG1 . THR A 1 127 ? 11.094  -49.726 36.889  1.00 29.42  ? 352  THR A OG1 1 
ATOM   1030 C CG2 . THR A 1 127 ? 12.682  -49.666 35.094  1.00 19.55  ? 352  THR A CG2 1 
ATOM   1031 N N   . ASP A 1 128 ? 12.806  -46.422 35.415  1.00 14.31  ? 353  ASP A N   1 
ATOM   1032 C CA  . ASP A 1 128 ? 13.711  -45.470 36.041  1.00 13.93  ? 353  ASP A CA  1 
ATOM   1033 C C   . ASP A 1 128 ? 13.297  -44.018 35.833  1.00 16.86  ? 353  ASP A C   1 
ATOM   1034 O O   . ASP A 1 128 ? 13.943  -43.118 36.388  1.00 15.26  ? 353  ASP A O   1 
ATOM   1035 C CB  . ASP A 1 128 ? 15.139  -45.671 35.501  1.00 14.02  ? 353  ASP A CB  1 
ATOM   1036 C CG  . ASP A 1 128 ? 15.727  -47.016 35.879  1.00 18.75  ? 353  ASP A CG  1 
ATOM   1037 O OD1 . ASP A 1 128 ? 15.479  -47.476 37.015  1.00 18.96  ? 353  ASP A OD1 1 
ATOM   1038 O OD2 . ASP A 1 128 ? 16.448  -47.617 35.046  1.00 19.92  ? 353  ASP A OD2 1 
ATOM   1039 N N   . TYR A 1 129 ? 12.249  -43.759 35.049  1.00 13.82  ? 354  TYR A N   1 
ATOM   1040 C CA  . TYR A 1 129 ? 11.820  -42.384 34.794  1.00 15.53  ? 354  TYR A CA  1 
ATOM   1041 C C   . TYR A 1 129 ? 10.924  -41.951 35.950  1.00 13.87  ? 354  TYR A C   1 
ATOM   1042 O O   . TYR A 1 129 ? 9.691   -41.927 35.867  1.00 16.60  ? 354  TYR A O   1 
ATOM   1043 C CB  . TYR A 1 129 ? 11.114  -42.261 33.449  1.00 14.50  ? 354  TYR A CB  1 
ATOM   1044 C CG  . TYR A 1 129 ? 10.894  -40.826 33.057  1.00 16.41  ? 354  TYR A CG  1 
ATOM   1045 C CD1 . TYR A 1 129 ? 11.951  -40.053 32.599  1.00 17.56  ? 354  TYR A CD1 1 
ATOM   1046 C CD2 . TYR A 1 129 ? 9.638   -40.234 33.155  1.00 13.96  ? 354  TYR A CD2 1 
ATOM   1047 C CE1 . TYR A 1 129 ? 11.770  -38.729 32.234  1.00 16.56  ? 354  TYR A CE1 1 
ATOM   1048 C CE2 . TYR A 1 129 ? 9.448   -38.902 32.798  1.00 15.51  ? 354  TYR A CE2 1 
ATOM   1049 C CZ  . TYR A 1 129 ? 10.521  -38.159 32.351  1.00 17.37  ? 354  TYR A CZ  1 
ATOM   1050 O OH  . TYR A 1 129 ? 10.356  -36.843 31.983  1.00 16.26  ? 354  TYR A OH  1 
ATOM   1051 N N   . THR A 1 130 ? 11.563  -41.640 37.072  1.00 14.27  ? 355  THR A N   1 
ATOM   1052 C CA  . THR A 1 130 ? 10.851  -41.223 38.281  1.00 13.57  ? 355  THR A CA  1 
ATOM   1053 C C   . THR A 1 130 ? 11.452  -39.934 38.822  1.00 12.76  ? 355  THR A C   1 
ATOM   1054 O O   . THR A 1 130 ? 11.871  -39.864 39.983  1.00 15.73  ? 355  THR A O   1 
ATOM   1055 C CB  . THR A 1 130 ? 10.864  -42.332 39.332  1.00 15.96  ? 355  THR A CB  1 
ATOM   1056 O OG1 . THR A 1 130 ? 12.208  -42.758 39.580  1.00 17.52  ? 355  THR A OG1 1 
ATOM   1057 C CG2 . THR A 1 130 ? 10.073  -43.524 38.834  1.00 16.42  ? 355  THR A CG2 1 
ATOM   1058 N N   . PRO A 1 131 ? 11.437  -38.860 38.018  1.00 15.64  ? 356  PRO A N   1 
ATOM   1059 C CA  . PRO A 1 131 ? 12.153  -37.636 38.409  1.00 14.69  ? 356  PRO A CA  1 
ATOM   1060 C C   . PRO A 1 131 ? 11.562  -36.945 39.616  1.00 16.91  ? 356  PRO A C   1 
ATOM   1061 O O   . PRO A 1 131 ? 12.276  -36.180 40.280  1.00 16.48  ? 356  PRO A O   1 
ATOM   1062 C CB  . PRO A 1 131 ? 12.045  -36.753 37.161  1.00 13.22  ? 356  PRO A CB  1 
ATOM   1063 C CG  . PRO A 1 131 ? 10.776  -37.218 36.489  1.00 14.15  ? 356  PRO A CG  1 
ATOM   1064 C CD  . PRO A 1 131 ? 10.766  -38.708 36.713  1.00 14.03  ? 356  PRO A CD  1 
ATOM   1065 N N   . ALA A 1 132 ? 10.291  -37.183 39.929  1.00 14.26  ? 357  ALA A N   1 
ATOM   1066 C CA  . ALA A 1 132 ? 9.738   -36.572 41.130  1.00 16.87  ? 357  ALA A CA  1 
ATOM   1067 C C   . ALA A 1 132 ? 10.485  -37.004 42.379  1.00 22.16  ? 357  ALA A C   1 
ATOM   1068 O O   . ALA A 1 132 ? 10.386  -36.325 43.404  1.00 19.91  ? 357  ALA A O   1 
ATOM   1069 C CB  . ALA A 1 132 ? 8.253   -36.908 41.280  1.00 15.94  ? 357  ALA A CB  1 
ATOM   1070 N N   . LEU A 1 133 ? 11.229  -38.115 42.323  1.00 14.43  ? 358  LEU A N   1 
ATOM   1071 C CA  . LEU A 1 133 ? 11.964  -38.566 43.495  1.00 17.62  ? 358  LEU A CA  1 
ATOM   1072 C C   . LEU A 1 133 ? 13.262  -37.801 43.701  1.00 21.14  ? 358  LEU A C   1 
ATOM   1073 O O   . LEU A 1 133 ? 13.881  -37.951 44.760  1.00 22.99  ? 358  LEU A O   1 
ATOM   1074 C CB  . LEU A 1 133 ? 12.249  -40.067 43.396  1.00 20.94  ? 358  LEU A CB  1 
ATOM   1075 C CG  . LEU A 1 133 ? 10.991  -40.932 43.258  1.00 24.16  ? 358  LEU A CG  1 
ATOM   1076 C CD1 . LEU A 1 133 ? 11.343  -42.407 43.216  1.00 21.04  ? 358  LEU A CD1 1 
ATOM   1077 C CD2 . LEU A 1 133 ? 9.993   -40.643 44.388  1.00 19.66  ? 358  LEU A CD2 1 
ATOM   1078 N N   . GLY A 1 134 ? 13.683  -36.992 42.725  1.00 18.32  ? 359  GLY A N   1 
ATOM   1079 C CA  . GLY A 1 134 ? 14.834  -36.121 42.874  1.00 19.30  ? 359  GLY A CA  1 
ATOM   1080 C C   . GLY A 1 134 ? 16.046  -36.510 42.054  1.00 18.33  ? 359  GLY A C   1 
ATOM   1081 O O   . GLY A 1 134 ? 17.039  -35.771 42.065  1.00 18.71  ? 359  GLY A O   1 
ATOM   1082 N N   . GLY A 1 135 ? 15.996  -37.634 41.343  1.00 16.96  ? 360  GLY A N   1 
ATOM   1083 C CA  . GLY A 1 135 ? 17.124  -38.093 40.559  1.00 20.67  ? 360  GLY A CA  1 
ATOM   1084 C C   . GLY A 1 135 ? 16.655  -38.992 39.436  1.00 16.45  ? 360  GLY A C   1 
ATOM   1085 O O   . GLY A 1 135 ? 15.484  -39.368 39.364  1.00 18.49  ? 360  GLY A O   1 
ATOM   1086 N N   . VAL A 1 136 ? 17.582  -39.342 38.549  1.00 18.67  ? 361  VAL A N   1 
ATOM   1087 C CA  . VAL A 1 136 ? 17.304  -40.331 37.510  1.00 16.25  ? 361  VAL A CA  1 
ATOM   1088 C C   . VAL A 1 136 ? 18.505  -41.247 37.343  1.00 15.20  ? 361  VAL A C   1 
ATOM   1089 O O   . VAL A 1 136 ? 19.658  -40.800 37.359  1.00 17.33  ? 361  VAL A O   1 
ATOM   1090 C CB  . VAL A 1 136 ? 16.935  -39.714 36.141  1.00 18.53  ? 361  VAL A CB  1 
ATOM   1091 C CG1 . VAL A 1 136 ? 15.481  -39.203 36.128  1.00 20.34  ? 361  VAL A CG1 1 
ATOM   1092 C CG2 . VAL A 1 136 ? 17.918  -38.632 35.737  1.00 19.66  ? 361  VAL A CG2 1 
ATOM   1093 N N   . LYS A 1 137 ? 18.218  -42.533 37.152  1.00 14.16  ? 362  LYS A N   1 
ATOM   1094 C CA  . LYS A 1 137 ? 19.226  -43.537 36.843  1.00 13.73  ? 362  LYS A CA  1 
ATOM   1095 C C   . LYS A 1 137 ? 19.317  -43.667 35.327  1.00 17.19  ? 362  LYS A C   1 
ATOM   1096 O O   . LYS A 1 137 ? 18.353  -44.085 34.672  1.00 15.68  ? 362  LYS A O   1 
ATOM   1097 C CB  . LYS A 1 137 ? 18.861  -44.872 37.491  1.00 14.41  ? 362  LYS A CB  1 
ATOM   1098 C CG  . LYS A 1 137 ? 19.825  -45.999 37.189  1.00 15.98  ? 362  LYS A CG  1 
ATOM   1099 C CD  . LYS A 1 137 ? 19.288  -47.306 37.753  1.00 21.96  ? 362  LYS A CD  1 
ATOM   1100 C CE  . LYS A 1 137 ? 20.216  -48.467 37.456  1.00 28.51  ? 362  LYS A CE  1 
ATOM   1101 N NZ  . LYS A 1 137 ? 19.588  -49.766 37.845  1.00 26.46  ? 362  LYS A NZ  1 
ATOM   1102 N N   . ILE A 1 138 ? 20.463  -43.286 34.766  1.00 13.22  ? 363  ILE A N   1 
ATOM   1103 C CA  . ILE A 1 138 ? 20.714  -43.387 33.332  1.00 13.38  ? 363  ILE A CA  1 
ATOM   1104 C C   . ILE A 1 138 ? 21.438  -44.704 33.091  1.00 16.24  ? 363  ILE A C   1 
ATOM   1105 O O   . ILE A 1 138 ? 22.432  -45.007 33.763  1.00 18.35  ? 363  ILE A O   1 
ATOM   1106 C CB  . ILE A 1 138 ? 21.534  -42.185 32.821  1.00 11.85  ? 363  ILE A CB  1 
ATOM   1107 C CG1 . ILE A 1 138 ? 20.772  -40.876 33.053  1.00 15.10  ? 363  ILE A CG1 1 
ATOM   1108 C CG2 . ILE A 1 138 ? 21.885  -42.377 31.343  1.00 11.70  ? 363  ILE A CG2 1 
ATOM   1109 C CD1 . ILE A 1 138 ? 21.612  -39.579 32.793  1.00 14.54  ? 363  ILE A CD1 1 
ATOM   1110 N N   . THR A 1 139 ? 20.913  -45.510 32.178  1.00 14.79  ? 364  THR A N   1 
ATOM   1111 C CA  . THR A 1 139 ? 21.518  -46.792 31.856  1.00 15.69  ? 364  THR A CA  1 
ATOM   1112 C C   . THR A 1 139 ? 21.994  -46.768 30.409  1.00 15.48  ? 364  THR A C   1 
ATOM   1113 O O   . THR A 1 139 ? 21.744  -45.813 29.660  1.00 15.57  ? 364  THR A O   1 
ATOM   1114 C CB  . THR A 1 139 ? 20.537  -47.947 32.113  1.00 17.71  ? 364  THR A CB  1 
ATOM   1115 O OG1 . THR A 1 139 ? 19.314  -47.703 31.410  1.00 17.18  ? 364  THR A OG1 1 
ATOM   1116 C CG2 . THR A 1 139 ? 20.232  -48.070 33.606  1.00 21.39  ? 364  THR A CG2 1 
ATOM   1117 N N   . ALA A 1 140 ? 22.718  -47.825 30.031  1.00 16.51  ? 365  ALA A N   1 
ATOM   1118 C CA  . ALA A 1 140 ? 23.401  -47.897 28.735  1.00 15.60  ? 365  ALA A CA  1 
ATOM   1119 C C   . ALA A 1 140 ? 24.281  -46.667 28.506  1.00 16.29  ? 365  ALA A C   1 
ATOM   1120 O O   . ALA A 1 140 ? 24.497  -46.231 27.376  1.00 18.55  ? 365  ALA A O   1 
ATOM   1121 C CB  . ALA A 1 140 ? 22.399  -48.082 27.586  1.00 17.73  ? 365  ALA A CB  1 
ATOM   1122 N N   . TRP A 1 141 ? 24.798  -46.097 29.591  1.00 14.08  ? 366  TRP A N   1 
ATOM   1123 C CA  . TRP A 1 141 ? 25.660  -44.927 29.497  1.00 15.82  ? 366  TRP A CA  1 
ATOM   1124 C C   . TRP A 1 141 ? 27.042  -45.353 29.016  1.00 16.79  ? 366  TRP A C   1 
ATOM   1125 O O   . TRP A 1 141 ? 27.663  -46.232 29.614  1.00 19.91  ? 366  TRP A O   1 
ATOM   1126 C CB  . TRP A 1 141 ? 25.748  -44.237 30.858  1.00 15.95  ? 366  TRP A CB  1 
ATOM   1127 C CG  . TRP A 1 141 ? 26.709  -43.086 30.888  1.00 12.91  ? 366  TRP A CG  1 
ATOM   1128 C CD1 . TRP A 1 141 ? 27.957  -43.082 31.449  1.00 14.28  ? 366  TRP A CD1 1 
ATOM   1129 C CD2 . TRP A 1 141 ? 26.520  -41.788 30.317  1.00 13.38  ? 366  TRP A CD2 1 
ATOM   1130 N NE1 . TRP A 1 141 ? 28.550  -41.858 31.268  1.00 14.91  ? 366  TRP A NE1 1 
ATOM   1131 C CE2 . TRP A 1 141 ? 27.689  -41.043 30.582  1.00 16.50  ? 366  TRP A CE2 1 
ATOM   1132 C CE3 . TRP A 1 141 ? 25.473  -41.176 29.622  1.00 13.86  ? 366  TRP A CE3 1 
ATOM   1133 C CZ2 . TRP A 1 141 ? 27.840  -39.714 30.171  1.00 18.04  ? 366  TRP A CZ2 1 
ATOM   1134 C CZ3 . TRP A 1 141 ? 25.625  -39.856 29.212  1.00 15.99  ? 366  TRP A CZ3 1 
ATOM   1135 C CH2 . TRP A 1 141 ? 26.802  -39.143 29.485  1.00 14.94  ? 366  TRP A CH2 1 
ATOM   1136 N N   . ASP A 1 142 ? 27.532  -44.721 27.944  1.00 15.74  ? 367  ASP A N   1 
ATOM   1137 C CA  . ASP A 1 142 ? 28.677  -45.261 27.215  1.00 17.54  ? 367  ASP A CA  1 
ATOM   1138 C C   . ASP A 1 142 ? 29.967  -44.457 27.378  1.00 22.82  ? 367  ASP A C   1 
ATOM   1139 O O   . ASP A 1 142 ? 30.929  -44.708 26.643  1.00 22.50  ? 367  ASP A O   1 
ATOM   1140 C CB  . ASP A 1 142 ? 28.334  -45.428 25.726  1.00 15.52  ? 367  ASP A CB  1 
ATOM   1141 C CG  . ASP A 1 142 ? 28.072  -44.109 25.002  1.00 19.61  ? 367  ASP A CG  1 
ATOM   1142 O OD1 . ASP A 1 142 ? 28.428  -43.018 25.506  1.00 15.86  ? 367  ASP A OD1 1 
ATOM   1143 O OD2 . ASP A 1 142 ? 27.498  -44.177 23.894  1.00 20.49  ? 367  ASP A OD2 1 
ATOM   1144 N N   . ALA A 1 143 ? 30.032  -43.522 28.321  1.00 15.85  ? 368  ALA A N   1 
ATOM   1145 C CA  . ALA A 1 143 ? 31.282  -42.826 28.604  1.00 15.04  ? 368  ALA A CA  1 
ATOM   1146 C C   . ALA A 1 143 ? 31.936  -43.397 29.858  1.00 18.34  ? 368  ALA A C   1 
ATOM   1147 O O   . ALA A 1 143 ? 31.280  -44.011 30.705  1.00 18.39  ? 368  ALA A O   1 
ATOM   1148 C CB  . ALA A 1 143 ? 31.053  -41.323 28.772  1.00 16.46  ? 368  ALA A CB  1 
ATOM   1149 N N   . THR A 1 144 ? 33.255  -43.194 29.962  1.00 17.80  ? 369  THR A N   1 
ATOM   1150 C CA  . THR A 1 144 ? 33.988  -43.733 31.105  1.00 16.95  ? 369  THR A CA  1 
ATOM   1151 C C   . THR A 1 144 ? 33.753  -42.911 32.359  1.00 21.39  ? 369  THR A C   1 
ATOM   1152 O O   . THR A 1 144 ? 33.780  -43.456 33.469  1.00 23.39  ? 369  THR A O   1 
ATOM   1153 C CB  . THR A 1 144 ? 35.487  -43.807 30.795  1.00 23.49  ? 369  THR A CB  1 
ATOM   1154 O OG1 . THR A 1 144 ? 35.999  -42.488 30.579  1.00 26.45  ? 369  THR A OG1 1 
ATOM   1155 C CG2 . THR A 1 144 ? 35.715  -44.630 29.541  1.00 24.24  ? 369  THR A CG2 1 
ATOM   1156 N N   . GLY A 1 145 ? 33.535  -41.613 32.197  1.00 17.56  ? 370  GLY A N   1 
ATOM   1157 C CA  . GLY A 1 145 ? 33.171  -40.740 33.284  1.00 16.26  ? 370  GLY A CA  1 
ATOM   1158 C C   . GLY A 1 145 ? 31.718  -40.327 33.180  1.00 19.69  ? 370  GLY A C   1 
ATOM   1159 O O   . GLY A 1 145 ? 30.999  -40.736 32.263  1.00 15.91  ? 370  GLY A O   1 
ATOM   1160 N N   . PRO A 1 146 ? 31.262  -39.472 34.108  1.00 15.02  ? 371  PRO A N   1 
ATOM   1161 C CA  . PRO A 1 146 ? 32.026  -38.796 35.172  1.00 14.89  ? 371  PRO A CA  1 
ATOM   1162 C C   . PRO A 1 146 ? 32.296  -39.603 36.428  1.00 16.38  ? 371  PRO A C   1 
ATOM   1163 O O   . PRO A 1 146 ? 31.694  -40.645 36.698  1.00 18.16  ? 371  PRO A O   1 
ATOM   1164 C CB  . PRO A 1 146 ? 31.114  -37.612 35.523  1.00 17.65  ? 371  PRO A CB  1 
ATOM   1165 C CG  . PRO A 1 146 ? 29.726  -38.219 35.379  1.00 14.47  ? 371  PRO A CG  1 
ATOM   1166 C CD  . PRO A 1 146 ? 29.835  -39.092 34.140  1.00 13.91  ? 371  PRO A CD  1 
ATOM   1167 N N   . SER A 1 147 ? 33.233  -39.100 37.227  1.00 18.61  ? 372  SER A N   1 
ATOM   1168 C CA  . SER A 1 147 ? 33.324  -39.504 38.616  1.00 16.10  ? 372  SER A CA  1 
ATOM   1169 C C   . SER A 1 147 ? 32.156  -38.903 39.397  1.00 16.19  ? 372  SER A C   1 
ATOM   1170 O O   . SER A 1 147 ? 31.309  -38.194 38.849  1.00 17.63  ? 372  SER A O   1 
ATOM   1171 C CB  . SER A 1 147 ? 34.663  -39.067 39.204  1.00 28.91  ? 372  SER A CB  1 
ATOM   1172 O OG  . SER A 1 147 ? 35.737  -39.603 38.457  1.00 34.85  ? 372  SER A OG  1 
ATOM   1173 N N   . ALA A 1 148 ? 32.110  -39.180 40.699  1.00 17.53  ? 373  ALA A N   1 
ATOM   1174 C CA  . ALA A 1 148 ? 31.057  -38.614 41.534  1.00 16.66  ? 373  ALA A CA  1 
ATOM   1175 C C   . ALA A 1 148 ? 31.207  -37.100 41.668  1.00 18.99  ? 373  ALA A C   1 
ATOM   1176 O O   . ALA A 1 148 ? 32.313  -36.549 41.633  1.00 15.85  ? 373  ALA A O   1 
ATOM   1177 C CB  . ALA A 1 148 ? 31.080  -39.244 42.927  1.00 17.08  ? 373  ALA A CB  1 
ATOM   1178 N N   . GLY A 1 149 ? 30.075  -36.429 41.847  1.00 17.21  ? 374  GLY A N   1 
ATOM   1179 C CA  . GLY A 1 149 ? 30.082  -35.025 42.198  1.00 16.00  ? 374  GLY A CA  1 
ATOM   1180 C C   . GLY A 1 149 ? 30.271  -34.071 41.045  1.00 16.89  ? 374  GLY A C   1 
ATOM   1181 O O   . GLY A 1 149 ? 30.538  -32.889 41.281  1.00 18.02  ? 374  GLY A O   1 
ATOM   1182 N N   . VAL A 1 150 ? 30.123  -34.542 39.817  1.00 13.57  ? 375  VAL A N   1 
ATOM   1183 C CA  . VAL A 1 150 ? 30.388  -33.754 38.620  1.00 13.47  ? 375  VAL A CA  1 
ATOM   1184 C C   . VAL A 1 150 ? 29.062  -33.299 38.019  1.00 15.03  ? 375  VAL A C   1 
ATOM   1185 O O   . VAL A 1 150 ? 28.132  -34.103 37.852  1.00 14.06  ? 375  VAL A O   1 
ATOM   1186 C CB  . VAL A 1 150 ? 31.209  -34.571 37.603  1.00 19.26  ? 375  VAL A CB  1 
ATOM   1187 C CG1 . VAL A 1 150 ? 31.316  -33.837 36.269  1.00 15.50  ? 375  VAL A CG1 1 
ATOM   1188 C CG2 . VAL A 1 150 ? 32.586  -34.893 38.175  1.00 21.52  ? 375  VAL A CG2 1 
ATOM   1189 N N   . GLU A 1 151 ? 28.980  -32.017 37.667  1.00 14.70  ? 376  GLU A N   1 
ATOM   1190 C CA  . GLU A 1 151 ? 27.784  -31.495 37.015  1.00 13.63  ? 376  GLU A CA  1 
ATOM   1191 C C   . GLU A 1 151 ? 27.664  -32.033 35.596  1.00 15.25  ? 376  GLU A C   1 
ATOM   1192 O O   . GLU A 1 151 ? 28.627  -31.991 34.826  1.00 17.57  ? 376  GLU A O   1 
ATOM   1193 C CB  . GLU A 1 151 ? 27.817  -29.969 36.970  1.00 19.47  ? 376  GLU A CB  1 
ATOM   1194 C CG  . GLU A 1 151 ? 27.389  -29.287 38.247  1.00 39.90  ? 376  GLU A CG  1 
ATOM   1195 C CD  . GLU A 1 151 ? 26.748  -27.924 38.002  1.00 40.65  ? 376  GLU A CD  1 
ATOM   1196 O OE1 . GLU A 1 151 ? 26.142  -27.725 36.927  1.00 52.97  ? 376  GLU A OE1 1 
ATOM   1197 O OE2 . GLU A 1 151 ? 26.860  -27.050 38.885  1.00 59.79  ? 376  GLU A OE2 1 
ATOM   1198 N N   . MET A 1 152 ? 26.472  -32.511 35.243  1.00 12.22  ? 377  MET A N   1 
ATOM   1199 C CA  . MET A 1 152 ? 26.180  -33.001 33.902  1.00 13.88  ? 377  MET A CA  1 
ATOM   1200 C C   . MET A 1 152 ? 24.982  -32.251 33.344  1.00 14.04  ? 377  MET A C   1 
ATOM   1201 O O   . MET A 1 152 ? 24.027  -31.964 34.072  1.00 15.35  ? 377  MET A O   1 
ATOM   1202 C CB  . MET A 1 152 ? 25.900  -34.519 33.910  1.00 12.82  ? 377  MET A CB  1 
ATOM   1203 C CG  . MET A 1 152 ? 27.063  -35.362 34.415  1.00 12.66  ? 377  MET A CG  1 
ATOM   1204 S SD  . MET A 1 152 ? 28.409  -35.393 33.210  1.00 14.84  ? 377  MET A SD  1 
ATOM   1205 C CE  . MET A 1 152 ? 27.677  -36.344 31.869  1.00 13.85  ? 377  MET A CE  1 
ATOM   1206 N N   A THR A 1 153 ? 25.036  -31.935 32.051  0.68 11.85  ? 378  THR A N   1 
ATOM   1207 N N   B THR A 1 153 ? 25.055  -31.886 32.068  0.32 11.99  ? 378  THR A N   1 
ATOM   1208 C CA  A THR A 1 153 ? 23.907  -31.345 31.347  0.68 11.18  ? 378  THR A CA  1 
ATOM   1209 C CA  B THR A 1 153 ? 23.909  -31.361 31.340  0.32 11.34  ? 378  THR A CA  1 
ATOM   1210 C C   A THR A 1 153 ? 23.661  -32.143 30.080  0.68 11.14  ? 378  THR A C   1 
ATOM   1211 C C   B THR A 1 153 ? 23.652  -32.255 30.141  0.32 11.10  ? 378  THR A C   1 
ATOM   1212 O O   A THR A 1 153 ? 24.610  -32.546 29.403  0.68 12.30  ? 378  THR A O   1 
ATOM   1213 O O   B THR A 1 153 ? 24.580  -32.844 29.580  0.32 12.92  ? 378  THR A O   1 
ATOM   1214 C CB  A THR A 1 153 ? 24.156  -29.880 30.976  0.68 17.47  ? 378  THR A CB  1 
ATOM   1215 C CB  B THR A 1 153 ? 24.120  -29.918 30.851  0.32 17.42  ? 378  THR A CB  1 
ATOM   1216 O OG1 A THR A 1 153 ? 24.652  -29.179 32.118  0.68 24.60  ? 378  THR A OG1 1 
ATOM   1217 O OG1 B THR A 1 153 ? 25.391  -29.806 30.201  0.32 15.98  ? 378  THR A OG1 1 
ATOM   1218 C CG2 A THR A 1 153 ? 22.861  -29.236 30.512  0.68 12.29  ? 378  THR A CG2 1 
ATOM   1219 C CG2 B THR A 1 153 ? 24.040  -28.936 31.999  0.32 23.61  ? 378  THR A CG2 1 
ATOM   1220 N N   . GLY A 1 154 ? 22.392  -32.352 29.743  1.00 11.45  ? 379  GLY A N   1 
ATOM   1221 C CA  . GLY A 1 154 ? 22.095  -33.191 28.606  1.00 12.58  ? 379  GLY A CA  1 
ATOM   1222 C C   . GLY A 1 154 ? 20.788  -32.849 27.938  1.00 15.73  ? 379  GLY A C   1 
ATOM   1223 O O   . GLY A 1 154 ? 20.100  -31.892 28.308  1.00 11.42  ? 379  GLY A O   1 
ATOM   1224 N N   A GLN A 1 155 ? 20.459  -33.644 26.924  0.48 12.48  ? 380  GLN A N   1 
ATOM   1225 N N   B GLN A 1 155 ? 20.436  -33.682 26.958  0.52 12.41  ? 380  GLN A N   1 
ATOM   1226 C CA  A GLN A 1 155 ? 19.242  -33.449 26.156  0.48 10.78  ? 380  GLN A CA  1 
ATOM   1227 C CA  B GLN A 1 155 ? 19.289  -33.457 26.089  0.52 10.77  ? 380  GLN A CA  1 
ATOM   1228 C C   A GLN A 1 155 ? 18.638  -34.805 25.843  0.48 12.06  ? 380  GLN A C   1 
ATOM   1229 C C   B GLN A 1 155 ? 18.641  -34.800 25.787  0.52 12.10  ? 380  GLN A C   1 
ATOM   1230 O O   A GLN A 1 155 ? 19.356  -35.768 25.554  0.48 11.50  ? 380  GLN A O   1 
ATOM   1231 O O   B GLN A 1 155 ? 19.340  -35.764 25.459  0.52 11.56  ? 380  GLN A O   1 
ATOM   1232 C CB  A GLN A 1 155 ? 19.507  -32.681 24.858  0.48 12.09  ? 380  GLN A CB  1 
ATOM   1233 C CB  B GLN A 1 155 ? 19.731  -32.757 24.793  0.52 11.03  ? 380  GLN A CB  1 
ATOM   1234 C CG  A GLN A 1 155 ? 18.240  -32.358 24.080  0.48 8.39   ? 380  GLN A CG  1 
ATOM   1235 C CG  B GLN A 1 155 ? 21.080  -33.246 24.282  0.52 15.99  ? 380  GLN A CG  1 
ATOM   1236 C CD  A GLN A 1 155 ? 18.510  -31.450 22.905  0.48 9.57   ? 380  GLN A CD  1 
ATOM   1237 C CD  B GLN A 1 155 ? 21.695  -32.365 23.188  0.52 17.76  ? 380  GLN A CD  1 
ATOM   1238 O OE1 A GLN A 1 155 ? 19.626  -30.947 22.744  0.48 10.83  ? 380  GLN A OE1 1 
ATOM   1239 O OE1 B GLN A 1 155 ? 22.106  -31.214 23.441  0.52 15.21  ? 380  GLN A OE1 1 
ATOM   1240 N NE2 A GLN A 1 155 ? 17.488  -31.226 22.077  0.48 10.12  ? 380  GLN A NE2 1 
ATOM   1241 N NE2 B GLN A 1 155 ? 21.792  -32.918 21.972  0.52 13.03  ? 380  GLN A NE2 1 
ATOM   1242 N N   . ILE A 1 156 ? 17.316  -34.874 25.918  1.00 11.38  ? 381  ILE A N   1 
ATOM   1243 C CA  . ILE A 1 156 ? 16.573  -36.065 25.533  1.00 12.45  ? 381  ILE A CA  1 
ATOM   1244 C C   . ILE A 1 156 ? 16.268  -35.909 24.050  1.00 9.14   ? 381  ILE A C   1 
ATOM   1245 O O   . ILE A 1 156 ? 15.672  -34.910 23.632  1.00 13.57  ? 381  ILE A O   1 
ATOM   1246 C CB  . ILE A 1 156 ? 15.308  -36.233 26.392  1.00 15.69  ? 381  ILE A CB  1 
ATOM   1247 C CG1 . ILE A 1 156 ? 15.748  -36.625 27.814  1.00 18.91  ? 381  ILE A CG1 1 
ATOM   1248 C CG2 . ILE A 1 156 ? 14.371  -37.283 25.787  1.00 12.99  ? 381  ILE A CG2 1 
ATOM   1249 C CD1 . ILE A 1 156 ? 14.656  -36.661 28.837  1.00 21.84  ? 381  ILE A CD1 1 
ATOM   1250 N N   A GLU A 1 157 ? 16.715  -36.872 23.241  0.44 11.77  ? 382  GLU A N   1 
ATOM   1251 N N   B GLU A 1 157 ? 16.717  -36.889 23.259  0.56 11.78  ? 382  GLU A N   1 
ATOM   1252 C CA  A GLU A 1 157 ? 16.745  -36.701 21.794  0.44 12.26  ? 382  GLU A CA  1 
ATOM   1253 C CA  B GLU A 1 157 ? 16.837  -36.797 21.808  0.56 12.59  ? 382  GLU A CA  1 
ATOM   1254 C C   A GLU A 1 157 ? 15.729  -37.540 21.043  0.44 12.42  ? 382  GLU A C   1 
ATOM   1255 C C   B GLU A 1 157 ? 15.751  -37.542 21.058  0.56 12.44  ? 382  GLU A C   1 
ATOM   1256 O O   A GLU A 1 157 ? 15.430  -37.221 19.887  0.44 12.85  ? 382  GLU A O   1 
ATOM   1257 O O   B GLU A 1 157 ? 15.428  -37.167 19.924  0.56 12.79  ? 382  GLU A O   1 
ATOM   1258 C CB  A GLU A 1 157 ? 18.136  -37.047 21.251  0.44 13.42  ? 382  GLU A CB  1 
ATOM   1259 C CB  B GLU A 1 157 ? 18.189  -37.370 21.357  0.56 9.36   ? 382  GLU A CB  1 
ATOM   1260 C CG  A GLU A 1 157 ? 19.241  -36.228 21.879  0.44 9.45   ? 382  GLU A CG  1 
ATOM   1261 C CG  B GLU A 1 157 ? 19.414  -36.797 22.085  0.56 9.97   ? 382  GLU A CG  1 
ATOM   1262 C CD  A GLU A 1 157 ? 20.607  -36.669 21.438  0.44 10.29  ? 382  GLU A CD  1 
ATOM   1263 C CD  B GLU A 1 157 ? 19.779  -35.406 21.618  0.56 15.38  ? 382  GLU A CD  1 
ATOM   1264 O OE1 A GLU A 1 157 ? 20.790  -37.868 21.138  0.44 16.36  ? 382  GLU A OE1 1 
ATOM   1265 O OE1 B GLU A 1 157 ? 18.918  -34.722 21.041  0.56 16.66  ? 382  GLU A OE1 1 
ATOM   1266 O OE2 A GLU A 1 157 ? 21.497  -35.805 21.379  0.44 12.27  ? 382  GLU A OE2 1 
ATOM   1267 O OE2 B GLU A 1 157 ? 20.940  -34.998 21.826  0.56 14.85  ? 382  GLU A OE2 1 
ATOM   1268 N N   . SER A 1 158 ? 15.223  -38.607 21.655  1.00 13.64  ? 383  SER A N   1 
ATOM   1269 C CA  . SER A 1 158 ? 14.312  -39.536 20.999  1.00 12.07  ? 383  SER A CA  1 
ATOM   1270 C C   . SER A 1 158 ? 13.767  -40.438 22.094  1.00 12.67  ? 383  SER A C   1 
ATOM   1271 O O   . SER A 1 158 ? 14.206  -40.365 23.243  1.00 14.79  ? 383  SER A O   1 
ATOM   1272 C CB  . SER A 1 158 ? 15.018  -40.338 19.896  1.00 15.54  ? 383  SER A CB  1 
ATOM   1273 O OG  . SER A 1 158 ? 16.159  -41.002 20.408  1.00 16.94  ? 383  SER A OG  1 
ATOM   1274 N N   . ILE A 1 159 ? 12.776  -41.259 21.747  1.00 14.10  ? 384  ILE A N   1 
ATOM   1275 C CA  . ILE A 1 159 ? 12.164  -42.149 22.728  1.00 13.21  ? 384  ILE A CA  1 
ATOM   1276 C C   . ILE A 1 159 ? 11.958  -43.513 22.106  1.00 12.78  ? 384  ILE A C   1 
ATOM   1277 O O   . ILE A 1 159 ? 11.827  -43.644 20.889  1.00 15.57  ? 384  ILE A O   1 
ATOM   1278 C CB  . ILE A 1 159 ? 10.803  -41.637 23.269  1.00 16.70  ? 384  ILE A CB  1 
ATOM   1279 C CG1 . ILE A 1 159 ? 9.835   -41.304 22.120  1.00 16.21  ? 384  ILE A CG1 1 
ATOM   1280 C CG2 . ILE A 1 159 ? 11.011  -40.497 24.270  1.00 12.84  ? 384  ILE A CG2 1 
ATOM   1281 C CD1 . ILE A 1 159 ? 9.758   -39.846 21.764  1.00 20.48  ? 384  ILE A CD1 1 
ATOM   1282 N N   . GLY A 1 160 ? 11.937  -44.535 22.956  1.00 15.65  ? 385  GLY A N   1 
ATOM   1283 C CA  . GLY A 1 160 ? 11.373  -45.813 22.563  1.00 16.65  ? 385  GLY A CA  1 
ATOM   1284 C C   . GLY A 1 160 ? 9.878   -45.714 22.768  1.00 15.56  ? 385  GLY A C   1 
ATOM   1285 O O   . GLY A 1 160 ? 9.434   -45.420 23.880  1.00 15.22  ? 385  GLY A O   1 
ATOM   1286 N N   . MET A 1 161 ? 9.087   -45.907 21.708  1.00 16.39  ? 386  MET A N   1 
ATOM   1287 C CA  . MET A 1 161 ? 7.675   -45.523 21.773  1.00 14.74  ? 386  MET A CA  1 
ATOM   1288 C C   . MET A 1 161 ? 6.860   -46.514 20.940  1.00 19.43  ? 386  MET A C   1 
ATOM   1289 O O   . MET A 1 161 ? 6.649   -46.308 19.744  1.00 18.19  ? 386  MET A O   1 
ATOM   1290 C CB  . MET A 1 161 ? 7.488   -44.097 21.276  1.00 17.22  ? 386  MET A CB  1 
ATOM   1291 C CG  . MET A 1 161 ? 6.140   -43.500 21.600  1.00 15.88  ? 386  MET A CG  1 
ATOM   1292 S SD  . MET A 1 161 ? 5.937   -43.279 23.380  1.00 16.21  ? 386  MET A SD  1 
ATOM   1293 C CE  . MET A 1 161 ? 4.501   -42.198 23.357  1.00 15.91  ? 386  MET A CE  1 
ATOM   1294 N N   . GLU A 1 162 ? 6.372   -47.558 21.597  1.00 17.23  ? 387  GLU A N   1 
ATOM   1295 C CA  . GLU A 1 162 ? 5.647   -48.593 20.876  1.00 15.17  ? 387  GLU A CA  1 
ATOM   1296 C C   . GLU A 1 162 ? 4.229   -48.181 20.503  1.00 20.77  ? 387  GLU A C   1 
ATOM   1297 O O   . GLU A 1 162 ? 3.664   -48.761 19.567  1.00 20.44  ? 387  GLU A O   1 
ATOM   1298 C CB  . GLU A 1 162 ? 5.601   -49.879 21.702  1.00 20.68  ? 387  GLU A CB  1 
ATOM   1299 C CG  . GLU A 1 162 ? 4.767   -49.762 22.954  1.00 34.85  ? 387  GLU A CG  1 
ATOM   1300 C CD  . GLU A 1 162 ? 4.899   -50.976 23.847  1.00 57.67  ? 387  GLU A CD  1 
ATOM   1301 O OE1 . GLU A 1 162 ? 5.684   -51.884 23.493  1.00 42.50  ? 387  GLU A OE1 1 
ATOM   1302 O OE2 . GLU A 1 162 ? 4.222   -51.016 24.900  1.00 45.86  ? 387  GLU A OE2 1 
ATOM   1303 N N   . ASN A 1 163 ? 3.660   -47.180 21.180  1.00 22.59  ? 388  ASN A N   1 
ATOM   1304 C CA  . ASN A 1 163 ? 2.236   -46.859 21.062  1.00 19.80  ? 388  ASN A CA  1 
ATOM   1305 C C   . ASN A 1 163 ? 2.067   -45.344 21.034  1.00 17.86  ? 388  ASN A C   1 
ATOM   1306 O O   . ASN A 1 163 ? 2.343   -44.667 22.033  1.00 18.53  ? 388  ASN A O   1 
ATOM   1307 C CB  . ASN A 1 163 ? 1.456   -47.472 22.227  1.00 20.22  ? 388  ASN A CB  1 
ATOM   1308 C CG  . ASN A 1 163 ? -0.041  -47.387 22.047  1.00 25.50  ? 388  ASN A CG  1 
ATOM   1309 O OD1 . ASN A 1 163 ? -0.545  -46.648 21.193  1.00 24.01  ? 388  ASN A OD1 1 
ATOM   1310 N ND2 . ASN A 1 163 ? -0.771  -48.155 22.856  1.00 25.94  ? 388  ASN A ND2 1 
ATOM   1311 N N   . ASN A 1 164 ? 1.575   -44.809 19.910  1.00 18.41  ? 389  ASN A N   1 
ATOM   1312 C CA  . ASN A 1 164 ? 1.453   -43.355 19.798  1.00 19.61  ? 389  ASN A CA  1 
ATOM   1313 C C   . ASN A 1 164 ? 0.500   -42.758 20.837  1.00 17.40  ? 389  ASN A C   1 
ATOM   1314 O O   . ASN A 1 164 ? 0.668   -41.595 21.226  1.00 18.55  ? 389  ASN A O   1 
ATOM   1315 C CB  . ASN A 1 164 ? 0.993   -42.966 18.392  1.00 17.77  ? 389  ASN A CB  1 
ATOM   1316 C CG  . ASN A 1 164 ? 1.298   -41.506 18.070  1.00 18.43  ? 389  ASN A CG  1 
ATOM   1317 O OD1 . ASN A 1 164 ? 2.448   -41.146 17.847  1.00 17.00  ? 389  ASN A OD1 1 
ATOM   1318 N ND2 . ASN A 1 164 ? 0.270   -40.665 18.056  1.00 20.40  ? 389  ASN A ND2 1 
ATOM   1319 N N   . THR A 1 165 ? -0.504  -43.516 21.296  1.00 18.03  ? 390  THR A N   1 
ATOM   1320 C CA  . THR A 1 165 ? -1.452  -42.966 22.270  1.00 19.39  ? 390  THR A CA  1 
ATOM   1321 C C   . THR A 1 165 ? -0.792  -42.632 23.609  1.00 20.16  ? 390  THR A C   1 
ATOM   1322 O O   . THR A 1 165 ? -1.353  -41.852 24.389  1.00 17.57  ? 390  THR A O   1 
ATOM   1323 C CB  . THR A 1 165 ? -2.641  -43.925 22.499  1.00 19.23  ? 390  THR A CB  1 
ATOM   1324 O OG1 . THR A 1 165 ? -2.186  -45.180 23.026  1.00 21.44  ? 390  THR A OG1 1 
ATOM   1325 C CG2 . THR A 1 165 ? -3.397  -44.176 21.200  1.00 26.62  ? 390  THR A CG2 1 
ATOM   1326 N N   . ASP A 1 166 ? 0.394   -43.180 23.889  1.00 19.79  ? 391  ASP A N   1 
ATOM   1327 C CA  . ASP A 1 166 ? 1.065   -42.893 25.149  1.00 18.36  ? 391  ASP A CA  1 
ATOM   1328 C C   . ASP A 1 166 ? 1.591   -41.462 25.232  1.00 15.38  ? 391  ASP A C   1 
ATOM   1329 O O   . ASP A 1 166 ? 1.975   -41.020 26.321  1.00 15.46  ? 391  ASP A O   1 
ATOM   1330 C CB  . ASP A 1 166 ? 2.209   -43.887 25.371  1.00 18.34  ? 391  ASP A CB  1 
ATOM   1331 C CG  . ASP A 1 166 ? 1.722   -45.237 25.873  1.00 26.81  ? 391  ASP A CG  1 
ATOM   1332 O OD1 . ASP A 1 166 ? 0.654   -45.278 26.526  1.00 21.69  ? 391  ASP A OD1 1 
ATOM   1333 O OD2 . ASP A 1 166 ? 2.406   -46.254 25.620  1.00 22.17  ? 391  ASP A OD2 1 
ATOM   1334 N N   . PHE A 1 167 ? 1.624   -40.721 24.124  1.00 15.62  ? 392  PHE A N   1 
ATOM   1335 C CA  . PHE A 1 167 ? 1.984   -39.310 24.221  1.00 12.69  ? 392  PHE A CA  1 
ATOM   1336 C C   . PHE A 1 167 ? 0.996   -38.523 25.071  1.00 12.98  ? 392  PHE A C   1 
ATOM   1337 O O   . PHE A 1 167 ? 1.351   -37.451 25.578  1.00 14.97  ? 392  PHE A O   1 
ATOM   1338 C CB  . PHE A 1 167 ? 2.077   -38.680 22.825  1.00 13.67  ? 392  PHE A CB  1 
ATOM   1339 C CG  . PHE A 1 167 ? 3.336   -39.036 22.079  1.00 12.17  ? 392  PHE A CG  1 
ATOM   1340 C CD1 . PHE A 1 167 ? 4.582   -38.711 22.599  1.00 13.91  ? 392  PHE A CD1 1 
ATOM   1341 C CD2 . PHE A 1 167 ? 3.269   -39.672 20.843  1.00 14.22  ? 392  PHE A CD2 1 
ATOM   1342 C CE1 . PHE A 1 167 ? 5.759   -39.024 21.911  1.00 11.84  ? 392  PHE A CE1 1 
ATOM   1343 C CE2 . PHE A 1 167 ? 4.443   -39.997 20.147  1.00 14.60  ? 392  PHE A CE2 1 
ATOM   1344 C CZ  . PHE A 1 167 ? 5.682   -39.673 20.678  1.00 14.90  ? 392  PHE A CZ  1 
ATOM   1345 N N   . ASP A 1 168 ? -0.233  -39.024 25.224  1.00 16.14  ? 393  ASP A N   1 
ATOM   1346 C CA  . ASP A 1 168 ? -1.265  -38.388 26.029  1.00 15.42  ? 393  ASP A CA  1 
ATOM   1347 C C   . ASP A 1 168 ? -1.479  -39.086 27.369  1.00 15.30  ? 393  ASP A C   1 
ATOM   1348 O O   . ASP A 1 168 ? -2.520  -38.894 28.004  1.00 20.90  ? 393  ASP A O   1 
ATOM   1349 C CB  . ASP A 1 168 ? -2.578  -38.338 25.248  1.00 13.67  ? 393  ASP A CB  1 
ATOM   1350 C CG  . ASP A 1 168 ? -2.527  -37.371 24.075  1.00 15.79  ? 393  ASP A CG  1 
ATOM   1351 O OD1 . ASP A 1 168 ? -1.635  -36.493 24.045  1.00 17.56  ? 393  ASP A OD1 1 
ATOM   1352 O OD2 . ASP A 1 168 ? -3.407  -37.488 23.188  1.00 18.11  ? 393  ASP A OD2 1 
ATOM   1353 N N   . VAL A 1 169 ? -0.515  -39.879 27.823  1.00 14.48  ? 394  VAL A N   1 
ATOM   1354 C CA  . VAL A 1 169 ? -0.611  -40.575 29.106  1.00 14.31  ? 394  VAL A CA  1 
ATOM   1355 C C   . VAL A 1 169 ? 0.540   -40.096 29.978  1.00 17.92  ? 394  VAL A C   1 
ATOM   1356 O O   . VAL A 1 169 ? 1.708   -40.367 29.669  1.00 14.63  ? 394  VAL A O   1 
ATOM   1357 C CB  . VAL A 1 169 ? -0.572  -42.100 28.941  1.00 16.78  ? 394  VAL A CB  1 
ATOM   1358 C CG1 . VAL A 1 169 ? -0.644  -42.758 30.306  1.00 18.86  ? 394  VAL A CG1 1 
ATOM   1359 C CG2 . VAL A 1 169 ? -1.730  -42.584 28.073  1.00 17.83  ? 394  VAL A CG2 1 
ATOM   1360 N N   . LEU A 1 170 ? 0.225   -39.391 31.068  1.00 13.84  ? 395  LEU A N   1 
ATOM   1361 C CA  . LEU A 1 170 ? 1.284   -38.894 31.940  1.00 14.53  ? 395  LEU A CA  1 
ATOM   1362 C C   . LEU A 1 170 ? 2.128   -40.055 32.466  1.00 16.39  ? 395  LEU A C   1 
ATOM   1363 O O   . LEU A 1 170 ? 1.587   -41.126 32.782  1.00 18.44  ? 395  LEU A O   1 
ATOM   1364 C CB  . LEU A 1 170 ? 0.704   -38.111 33.119  1.00 17.43  ? 395  LEU A CB  1 
ATOM   1365 C CG  . LEU A 1 170 ? 0.150   -36.716 32.807  1.00 17.28  ? 395  LEU A CG  1 
ATOM   1366 C CD1 . LEU A 1 170 ? -0.386  -36.063 34.070  1.00 19.95  ? 395  LEU A CD1 1 
ATOM   1367 C CD2 . LEU A 1 170 ? 1.227   -35.860 32.163  1.00 17.80  ? 395  LEU A CD2 1 
ATOM   1368 N N   . PRO A 1 171 ? 3.440   -39.872 32.595  1.00 14.74  ? 396  PRO A N   1 
ATOM   1369 C CA  . PRO A 1 171 ? 4.281   -40.910 33.202  1.00 16.57  ? 396  PRO A CA  1 
ATOM   1370 C C   . PRO A 1 171 ? 4.051   -40.985 34.704  1.00 17.76  ? 396  PRO A C   1 
ATOM   1371 O O   . PRO A 1 171 ? 3.462   -40.098 35.322  1.00 18.49  ? 396  PRO A O   1 
ATOM   1372 C CB  . PRO A 1 171 ? 5.700   -40.429 32.886  1.00 15.06  ? 396  PRO A CB  1 
ATOM   1373 C CG  . PRO A 1 171 ? 5.569   -38.922 32.937  1.00 15.53  ? 396  PRO A CG  1 
ATOM   1374 C CD  . PRO A 1 171 ? 4.187   -38.617 32.373  1.00 16.50  ? 396  PRO A CD  1 
ATOM   1375 N N   . ASP A 1 172 ? 4.539   -42.078 35.297  1.00 13.19  ? 397  ASP A N   1 
ATOM   1376 C CA  . ASP A 1 172 ? 4.477   -42.269 36.749  1.00 19.71  ? 397  ASP A CA  1 
ATOM   1377 C C   . ASP A 1 172 ? 5.664   -41.538 37.379  1.00 18.18  ? 397  ASP A C   1 
ATOM   1378 O O   . ASP A 1 172 ? 6.654   -42.127 37.827  1.00 17.08  ? 397  ASP A O   1 
ATOM   1379 C CB  . ASP A 1 172 ? 4.463   -43.752 37.099  1.00 14.49  ? 397  ASP A CB  1 
ATOM   1380 C CG  . ASP A 1 172 ? 3.127   -44.430 36.781  1.00 21.17  ? 397  ASP A CG  1 
ATOM   1381 O OD1 . ASP A 1 172 ? 2.140   -43.734 36.456  1.00 23.06  ? 397  ASP A OD1 1 
ATOM   1382 O OD2 . ASP A 1 172 ? 3.067   -45.674 36.866  1.00 29.02  ? 397  ASP A OD2 1 
ATOM   1383 N N   . TYR A 1 173 ? 5.538   -40.210 37.410  1.00 15.22  ? 398  TYR A N   1 
ATOM   1384 C CA  . TYR A 1 173 ? 6.640   -39.338 37.813  1.00 14.04  ? 398  TYR A CA  1 
ATOM   1385 C C   . TYR A 1 173 ? 7.260   -39.731 39.149  1.00 16.43  ? 398  TYR A C   1 
ATOM   1386 O O   . TYR A 1 173 ? 8.465   -39.543 39.357  1.00 15.35  ? 398  TYR A O   1 
ATOM   1387 C CB  . TYR A 1 173 ? 6.157   -37.903 37.939  1.00 14.20  ? 398  TYR A CB  1 
ATOM   1388 C CG  . TYR A 1 173 ? 5.837   -37.124 36.688  1.00 15.46  ? 398  TYR A CG  1 
ATOM   1389 C CD1 . TYR A 1 173 ? 6.848   -36.564 35.904  1.00 17.46  ? 398  TYR A CD1 1 
ATOM   1390 C CD2 . TYR A 1 173 ? 4.518   -36.842 36.358  1.00 13.62  ? 398  TYR A CD2 1 
ATOM   1391 C CE1 . TYR A 1 173 ? 6.538   -35.784 34.787  1.00 16.62  ? 398  TYR A CE1 1 
ATOM   1392 C CE2 . TYR A 1 173 ? 4.201   -36.066 35.244  1.00 14.30  ? 398  TYR A CE2 1 
ATOM   1393 C CZ  . TYR A 1 173 ? 5.215   -35.540 34.475  1.00 16.65  ? 398  TYR A CZ  1 
ATOM   1394 O OH  . TYR A 1 173 ? 4.898   -34.756 33.390  1.00 14.66  ? 398  TYR A OH  1 
ATOM   1395 N N   . ASN A 1 174 ? 6.449   -40.198 40.096  1.00 15.96  ? 399  ASN A N   1 
ATOM   1396 C CA  . ASN A 1 174 ? 6.956   -40.546 41.415  1.00 16.17  ? 399  ASN A CA  1 
ATOM   1397 C C   . ASN A 1 174 ? 7.087   -42.053 41.604  1.00 19.03  ? 399  ASN A C   1 
ATOM   1398 O O   . ASN A 1 174 ? 7.299   -42.512 42.731  1.00 22.18  ? 399  ASN A O   1 
ATOM   1399 C CB  . ASN A 1 174 ? 6.075   -39.925 42.509  1.00 17.59  ? 399  ASN A CB  1 
ATOM   1400 C CG  . ASN A 1 174 ? 4.652   -40.491 42.530  1.00 20.29  ? 399  ASN A CG  1 
ATOM   1401 O OD1 . ASN A 1 174 ? 4.390   -41.593 42.047  1.00 23.34  ? 399  ASN A OD1 1 
ATOM   1402 N ND2 . ASN A 1 174 ? 3.733   -39.735 43.119  1.00 21.76  ? 399  ASN A ND2 1 
ATOM   1403 N N   . GLY A 1 175 ? 6.985   -42.829 40.524  1.00 16.71  ? 400  GLY A N   1 
ATOM   1404 C CA  . GLY A 1 175 ? 7.162   -44.266 40.622  1.00 17.58  ? 400  GLY A CA  1 
ATOM   1405 C C   . GLY A 1 175 ? 5.948   -45.021 41.093  1.00 20.29  ? 400  GLY A C   1 
ATOM   1406 O O   . GLY A 1 175 ? 6.053   -46.221 41.377  1.00 29.09  ? 400  GLY A O   1 
ATOM   1407 N N   . SER A 1 176 ? 4.797   -44.359 41.180  1.00 22.74  ? 401  SER A N   1 
ATOM   1408 C CA  . SER A 1 176 ? 3.565   -44.982 41.634  1.00 23.18  ? 401  SER A CA  1 
ATOM   1409 C C   . SER A 1 176 ? 2.423   -44.531 40.742  1.00 20.77  ? 401  SER A C   1 
ATOM   1410 O O   . SER A 1 176 ? 2.550   -43.585 39.958  1.00 25.10  ? 401  SER A O   1 
ATOM   1411 C CB  . SER A 1 176 ? 3.251   -44.627 43.089  1.00 24.04  ? 401  SER A CB  1 
ATOM   1412 O OG  . SER A 1 176 ? 2.621   -43.357 43.167  1.00 22.81  ? 401  SER A OG  1 
ATOM   1413 N N   . ALA A 1 177 ? 1.286   -45.205 40.897  1.00 27.41  ? 402  ALA A N   1 
ATOM   1414 C CA  . ALA A 1 177 ? 0.067   -44.837 40.191  1.00 34.96  ? 402  ALA A CA  1 
ATOM   1415 C C   . ALA A 1 177 ? -0.692  -43.700 40.863  1.00 34.77  ? 402  ALA A C   1 
ATOM   1416 O O   . ALA A 1 177 ? -1.771  -43.334 40.384  1.00 34.59  ? 402  ALA A O   1 
ATOM   1417 C CB  . ALA A 1 177 ? -0.851  -46.060 40.065  1.00 35.78  ? 402  ALA A CB  1 
ATOM   1418 N N   . PHE A 1 178 ? -0.167  -43.129 41.947  1.00 19.84  ? 403  PHE A N   1 
ATOM   1419 C CA  . PHE A 1 178 ? -0.891  -42.141 42.746  1.00 24.43  ? 403  PHE A CA  1 
ATOM   1420 C C   . PHE A 1 178 ? -0.195  -40.790 42.629  1.00 25.50  ? 403  PHE A C   1 
ATOM   1421 O O   . PHE A 1 178 ? 0.900   -40.596 43.168  1.00 34.36  ? 403  PHE A O   1 
ATOM   1422 C CB  . PHE A 1 178 ? -1.003  -42.610 44.197  1.00 21.31  ? 403  PHE A CB  1 
ATOM   1423 C CG  . PHE A 1 178 ? -1.815  -43.851 44.343  1.00 22.99  ? 403  PHE A CG  1 
ATOM   1424 C CD1 . PHE A 1 178 ? -1.239  -45.098 44.177  1.00 24.69  ? 403  PHE A CD1 1 
ATOM   1425 C CD2 . PHE A 1 178 ? -3.171  -43.776 44.608  1.00 18.58  ? 403  PHE A CD2 1 
ATOM   1426 C CE1 . PHE A 1 178 ? -1.994  -46.244 44.282  1.00 20.43  ? 403  PHE A CE1 1 
ATOM   1427 C CE2 . PHE A 1 178 ? -3.933  -44.922 44.718  1.00 23.99  ? 403  PHE A CE2 1 
ATOM   1428 C CZ  . PHE A 1 178 ? -3.341  -46.158 44.557  1.00 26.27  ? 403  PHE A CZ  1 
ATOM   1429 N N   . ASP A 1 179 ? -0.838  -39.860 41.931  1.00 22.16  ? 404  ASP A N   1 
ATOM   1430 C CA  . ASP A 1 179 ? -0.268  -38.544 41.660  1.00 21.35  ? 404  ASP A CA  1 
ATOM   1431 C C   . ASP A 1 179 ? -0.904  -37.452 42.510  1.00 29.42  ? 404  ASP A C   1 
ATOM   1432 O O   . ASP A 1 179 ? -0.720  -36.267 42.220  1.00 26.43  ? 404  ASP A O   1 
ATOM   1433 C CB  . ASP A 1 179 ? -0.403  -38.209 40.168  1.00 26.76  ? 404  ASP A CB  1 
ATOM   1434 C CG  . ASP A 1 179 ? -1.848  -38.201 39.692  1.00 36.08  ? 404  ASP A CG  1 
ATOM   1435 O OD1 . ASP A 1 179 ? -2.752  -38.504 40.501  1.00 59.77  ? 404  ASP A OD1 1 
ATOM   1436 O OD2 . ASP A 1 179 ? -2.089  -37.883 38.506  1.00 47.60  ? 404  ASP A OD2 1 
ATOM   1437 N N   . GLY A 1 180 ? -1.634  -37.829 43.564  1.00 31.17  ? 405  GLY A N   1 
ATOM   1438 C CA  . GLY A 1 180 ? -2.390  -36.858 44.337  1.00 32.76  ? 405  GLY A CA  1 
ATOM   1439 C C   . GLY A 1 180 ? -1.556  -35.756 44.964  1.00 28.78  ? 405  GLY A C   1 
ATOM   1440 O O   . GLY A 1 180 ? -2.039  -34.635 45.128  1.00 36.39  ? 405  GLY A O   1 
ATOM   1441 N N   . SER A 1 181 ? -0.308  -36.048 45.335  1.00 23.13  ? 406  SER A N   1 
ATOM   1442 C CA  . SER A 1 181 ? 0.533   -35.026 45.949  1.00 23.21  ? 406  SER A CA  1 
ATOM   1443 C C   . SER A 1 181 ? 1.234   -34.138 44.931  1.00 27.17  ? 406  SER A C   1 
ATOM   1444 O O   . SER A 1 181 ? 1.899   -33.174 45.328  1.00 25.62  ? 406  SER A O   1 
ATOM   1445 C CB  . SER A 1 181 ? 1.586   -35.665 46.852  1.00 31.83  ? 406  SER A CB  1 
ATOM   1446 O OG  . SER A 1 181 ? 0.985   -36.215 48.009  1.00 45.95  ? 406  SER A OG  1 
ATOM   1447 N N   . LEU A 1 182 ? 1.107   -34.431 43.642  1.00 20.52  ? 407  LEU A N   1 
ATOM   1448 C CA  . LEU A 1 182 ? 1.805   -33.682 42.612  1.00 14.60  ? 407  LEU A CA  1 
ATOM   1449 C C   . LEU A 1 182 ? 0.980   -32.484 42.158  1.00 21.49  ? 407  LEU A C   1 
ATOM   1450 O O   . LEU A 1 182 ? -0.239  -32.576 42.002  1.00 19.64  ? 407  LEU A O   1 
ATOM   1451 C CB  . LEU A 1 182 ? 2.114   -34.583 41.416  1.00 19.33  ? 407  LEU A CB  1 
ATOM   1452 C CG  . LEU A 1 182 ? 3.019   -35.771 41.750  1.00 16.44  ? 407  LEU A CG  1 
ATOM   1453 C CD1 . LEU A 1 182 ? 3.261   -36.628 40.512  1.00 18.80  ? 407  LEU A CD1 1 
ATOM   1454 C CD2 . LEU A 1 182 ? 4.347   -35.267 42.363  1.00 20.02  ? 407  LEU A CD2 1 
ATOM   1455 N N   . ASN A 1 183 ? 1.661   -31.362 41.946  1.00 14.42  ? 408  ASN A N   1 
ATOM   1456 C CA  . ASN A 1 183 ? 1.044   -30.118 41.483  1.00 16.31  ? 408  ASN A CA  1 
ATOM   1457 C C   . ASN A 1 183 ? 1.051   -30.147 39.960  1.00 15.77  ? 408  ASN A C   1 
ATOM   1458 O O   . ASN A 1 183 ? 2.023   -29.749 39.313  1.00 16.71  ? 408  ASN A O   1 
ATOM   1459 C CB  . ASN A 1 183 ? 1.808   -28.920 42.035  1.00 16.42  ? 408  ASN A CB  1 
ATOM   1460 C CG  . ASN A 1 183 ? 1.263   -27.589 41.555  1.00 22.39  ? 408  ASN A CG  1 
ATOM   1461 O OD1 . ASN A 1 183 ? 0.100   -27.475 41.178  1.00 18.43  ? 408  ASN A OD1 1 
ATOM   1462 N ND2 . ASN A 1 183 ? 2.106   -26.566 41.590  1.00 22.56  ? 408  ASN A ND2 1 
ATOM   1463 N N   . LEU A 1 184 ? -0.038  -30.657 39.390  1.00 15.01  ? 409  LEU A N   1 
ATOM   1464 C CA  . LEU A 1 184 ? -0.165  -30.901 37.959  1.00 12.80  ? 409  LEU A CA  1 
ATOM   1465 C C   . LEU A 1 184 ? -1.128  -29.899 37.332  1.00 15.30  ? 409  LEU A C   1 
ATOM   1466 O O   . LEU A 1 184 ? -2.219  -29.665 37.863  1.00 19.22  ? 409  LEU A O   1 
ATOM   1467 C CB  . LEU A 1 184 ? -0.688  -32.316 37.703  1.00 13.98  ? 409  LEU A CB  1 
ATOM   1468 C CG  . LEU A 1 184 ? 0.201   -33.482 38.147  1.00 17.28  ? 409  LEU A CG  1 
ATOM   1469 C CD1 . LEU A 1 184 ? -0.527  -34.805 37.908  1.00 17.71  ? 409  LEU A CD1 1 
ATOM   1470 C CD2 . LEU A 1 184 ? 1.529   -33.448 37.395  1.00 23.03  ? 409  LEU A CD2 1 
ATOM   1471 N N   . ALA A 1 185 ? -0.733  -29.333 36.189  1.00 13.39  ? 410  ALA A N   1 
ATOM   1472 C CA  . ALA A 1 185 ? -1.677  -28.555 35.396  1.00 14.15  ? 410  ALA A CA  1 
ATOM   1473 C C   . ALA A 1 185 ? -2.891  -29.423 35.063  1.00 13.00  ? 410  ALA A C   1 
ATOM   1474 O O   . ALA A 1 185 ? -2.760  -30.638 34.891  1.00 14.52  ? 410  ALA A O   1 
ATOM   1475 C CB  . ALA A 1 185 ? -1.011  -28.053 34.114  1.00 15.46  ? 410  ALA A CB  1 
ATOM   1476 N N   . PRO A 1 186 ? -4.083  -28.833 34.965  1.00 17.90  ? 411  PRO A N   1 
ATOM   1477 C CA  . PRO A 1 186 ? -5.310  -29.635 34.865  1.00 23.30  ? 411  PRO A CA  1 
ATOM   1478 C C   . PRO A 1 186 ? -5.513  -30.198 33.468  1.00 14.62  ? 411  PRO A C   1 
ATOM   1479 O O   . PRO A 1 186 ? -4.904  -29.730 32.494  1.00 15.63  ? 411  PRO A O   1 
ATOM   1480 C CB  . PRO A 1 186 ? -6.413  -28.627 35.224  1.00 22.59  ? 411  PRO A CB  1 
ATOM   1481 C CG  . PRO A 1 186 ? -5.874  -27.338 34.800  1.00 15.76  ? 411  PRO A CG  1 
ATOM   1482 C CD  . PRO A 1 186 ? -4.371  -27.388 34.996  1.00 18.55  ? 411  PRO A CD  1 
ATOM   1483 N N   . PRO A 1 187 ? -6.378  -31.202 33.327  1.00 14.27  ? 412  PRO A N   1 
ATOM   1484 C CA  . PRO A 1 187 ? -6.688  -31.729 31.992  1.00 18.16  ? 412  PRO A CA  1 
ATOM   1485 C C   . PRO A 1 187 ? -7.309  -30.652 31.112  1.00 17.85  ? 412  PRO A C   1 
ATOM   1486 O O   . PRO A 1 187 ? -7.966  -29.723 31.593  1.00 18.33  ? 412  PRO A O   1 
ATOM   1487 C CB  . PRO A 1 187 ? -7.684  -32.866 32.274  1.00 19.88  ? 412  PRO A CB  1 
ATOM   1488 C CG  . PRO A 1 187 ? -7.521  -33.188 33.739  1.00 21.39  ? 412  PRO A CG  1 
ATOM   1489 C CD  . PRO A 1 187 ? -7.109  -31.904 34.397  1.00 14.83  ? 412  PRO A CD  1 
ATOM   1490 N N   . ILE A 1 188 ? -7.092  -30.795 29.809  1.00 16.12  ? 413  ILE A N   1 
ATOM   1491 C CA  . ILE A 1 188 ? -7.544  -29.845 28.801  1.00 17.43  ? 413  ILE A CA  1 
ATOM   1492 C C   . ILE A 1 188 ? -8.861  -30.365 28.240  1.00 18.75  ? 413  ILE A C   1 
ATOM   1493 O O   . ILE A 1 188 ? -8.890  -31.381 27.541  1.00 21.34  ? 413  ILE A O   1 
ATOM   1494 C CB  . ILE A 1 188 ? -6.499  -29.672 27.692  1.00 15.28  ? 413  ILE A CB  1 
ATOM   1495 C CG1 . ILE A 1 188 ? -5.182  -29.135 28.272  1.00 18.58  ? 413  ILE A CG1 1 
ATOM   1496 C CG2 . ILE A 1 188 ? -7.051  -28.785 26.581  1.00 19.17  ? 413  ILE A CG2 1 
ATOM   1497 C CD1 . ILE A 1 188 ? -4.031  -29.129 27.271  1.00 19.15  ? 413  ILE A CD1 1 
ATOM   1498 N N   . VAL A 1 189 ? -9.965  -29.688 28.555  1.00 18.75  ? 414  VAL A N   1 
ATOM   1499 C CA  . VAL A 1 189 ? -11.291 -30.137 28.164  1.00 20.79  ? 414  VAL A CA  1 
ATOM   1500 C C   . VAL A 1 189 ? -12.051 -28.946 27.590  1.00 26.38  ? 414  VAL A C   1 
ATOM   1501 O O   . VAL A 1 189 ? -12.208 -27.930 28.274  1.00 27.14  ? 414  VAL A O   1 
ATOM   1502 C CB  . VAL A 1 189 ? -12.072 -30.753 29.337  1.00 21.67  ? 414  VAL A CB  1 
ATOM   1503 C CG1 . VAL A 1 189 ? -13.398 -31.343 28.850  1.00 22.05  ? 414  VAL A CG1 1 
ATOM   1504 C CG2 . VAL A 1 189 ? -11.248 -31.825 30.023  1.00 27.12  ? 414  VAL A CG2 1 
ATOM   1505 N N   . PRO A 1 190 ? -12.524 -29.011 26.350  1.00 21.36  ? 415  PRO A N   1 
ATOM   1506 C CA  . PRO A 1 190 ? -13.293 -27.888 25.799  1.00 22.99  ? 415  PRO A CA  1 
ATOM   1507 C C   . PRO A 1 190 ? -14.493 -27.553 26.671  1.00 26.01  ? 415  PRO A C   1 
ATOM   1508 O O   . PRO A 1 190 ? -15.121 -28.430 27.269  1.00 22.39  ? 415  PRO A O   1 
ATOM   1509 C CB  . PRO A 1 190 ? -13.725 -28.396 24.420  1.00 21.71  ? 415  PRO A CB  1 
ATOM   1510 C CG  . PRO A 1 190 ? -12.677 -29.398 24.044  1.00 25.54  ? 415  PRO A CG  1 
ATOM   1511 C CD  . PRO A 1 190 ? -12.277 -30.064 25.352  1.00 27.00  ? 415  PRO A CD  1 
ATOM   1512 N N   . LEU A 1 191 ? -14.815 -26.260 26.733  1.00 24.25  ? 416  LEU A N   1 
ATOM   1513 C CA  . LEU A 1 191 ? -15.915 -25.814 27.588  1.00 25.27  ? 416  LEU A CA  1 
ATOM   1514 C C   . LEU A 1 191 ? -17.289 -26.089 26.978  1.00 32.46  ? 416  LEU A C   1 
ATOM   1515 O O   . LEU A 1 191 ? -18.250 -26.318 27.719  1.00 29.95  ? 416  LEU A O   1 
ATOM   1516 C CB  . LEU A 1 191 ? -15.767 -24.323 27.905  1.00 27.59  ? 416  LEU A CB  1 
ATOM   1517 C CG  . LEU A 1 191 ? -14.760 -23.920 28.998  1.00 33.51  ? 416  LEU A CG  1 
ATOM   1518 C CD1 . LEU A 1 191 ? -15.058 -24.633 30.322  1.00 38.12  ? 416  LEU A CD1 1 
ATOM   1519 C CD2 . LEU A 1 191 ? -13.307 -24.149 28.584  1.00 33.22  ? 416  LEU A CD2 1 
ATOM   1520 N N   . LEU A 1 192 ? -17.415 -26.069 25.644  1.00 25.96  ? 417  LEU A N   1 
ATOM   1521 C CA  . LEU A 1 192 ? -18.678 -26.428 25.014  1.00 27.24  ? 417  LEU A CA  1 
ATOM   1522 C C   . LEU A 1 192 ? -18.610 -27.852 24.468  1.00 36.77  ? 417  LEU A C   1 
ATOM   1523 O O   . LEU A 1 192 ? -17.544 -28.326 24.069  1.00 31.74  ? 417  LEU A O   1 
ATOM   1524 C CB  . LEU A 1 192 ? -19.024 -25.463 23.874  1.00 27.07  ? 417  LEU A CB  1 
ATOM   1525 C CG  . LEU A 1 192 ? -19.658 -24.111 24.220  1.00 32.42  ? 417  LEU A CG  1 
ATOM   1526 C CD1 . LEU A 1 192 ? -19.866 -23.285 22.957  1.00 25.24  ? 417  LEU A CD1 1 
ATOM   1527 C CD2 . LEU A 1 192 ? -20.985 -24.280 24.953  1.00 33.45  ? 417  LEU A CD2 1 
ATOM   1528 N N   . PRO A 1 193 ? -19.730 -28.572 24.429  1.00 40.87  ? 418  PRO A N   1 
ATOM   1529 C CA  . PRO A 1 193 ? -19.646 -30.014 24.142  1.00 38.64  ? 418  PRO A CA  1 
ATOM   1530 C C   . PRO A 1 193 ? -19.329 -30.352 22.689  1.00 37.65  ? 418  PRO A C   1 
ATOM   1531 O O   . PRO A 1 193 ? -18.704 -31.392 22.440  1.00 36.54  ? 418  PRO A O   1 
ATOM   1532 C CB  . PRO A 1 193 ? -21.030 -30.523 24.554  1.00 48.75  ? 418  PRO A CB  1 
ATOM   1533 C CG  . PRO A 1 193 ? -21.931 -29.325 24.353  1.00 39.41  ? 418  PRO A CG  1 
ATOM   1534 C CD  . PRO A 1 193 ? -21.106 -28.135 24.728  1.00 46.14  ? 418  PRO A CD  1 
ATOM   1535 N N   . GLY A 1 194 ? -19.745 -29.529 21.723  1.00 27.64  ? 419  GLY A N   1 
ATOM   1536 C CA  . GLY A 1 194 ? -19.393 -29.777 20.337  1.00 26.25  ? 419  GLY A CA  1 
ATOM   1537 C C   . GLY A 1 194 ? -18.016 -29.314 19.917  1.00 33.31  ? 419  GLY A C   1 
ATOM   1538 O O   . GLY A 1 194 ? -17.647 -29.441 18.742  1.00 28.48  ? 419  GLY A O   1 
ATOM   1539 N N   . GLU A 1 195 ? -17.236 -28.773 20.847  1.00 24.98  ? 420  GLU A N   1 
ATOM   1540 C CA  . GLU A 1 195 ? -15.901 -28.283 20.543  1.00 19.68  ? 420  GLU A CA  1 
ATOM   1541 C C   . GLU A 1 195 ? -14.881 -29.407 20.633  1.00 25.32  ? 420  GLU A C   1 
ATOM   1542 O O   . GLU A 1 195 ? -15.050 -30.373 21.380  1.00 23.67  ? 420  GLU A O   1 
ATOM   1543 C CB  . GLU A 1 195 ? -15.520 -27.145 21.487  1.00 19.28  ? 420  GLU A CB  1 
ATOM   1544 C CG  . GLU A 1 195 ? -16.258 -25.850 21.171  1.00 22.28  ? 420  GLU A CG  1 
ATOM   1545 C CD  . GLU A 1 195 ? -15.987 -24.764 22.180  1.00 24.27  ? 420  GLU A CD  1 
ATOM   1546 O OE1 . GLU A 1 195 ? -15.397 -25.072 23.238  1.00 20.56  ? 420  GLU A OE1 1 
ATOM   1547 O OE2 . GLU A 1 195 ? -16.349 -23.602 21.905  1.00 22.31  ? 420  GLU A OE2 1 
ATOM   1548 N N   . THR A 1 196 ? -13.814 -29.268 19.853  1.00 20.48  ? 421  THR A N   1 
ATOM   1549 C CA  . THR A 1 196 ? -12.743 -30.247 19.799  1.00 17.80  ? 421  THR A CA  1 
ATOM   1550 C C   . THR A 1 196 ? -11.425 -29.508 19.927  1.00 19.09  ? 421  THR A C   1 
ATOM   1551 O O   . THR A 1 196 ? -11.241 -28.457 19.311  1.00 18.72  ? 421  THR A O   1 
ATOM   1552 C CB  . THR A 1 196 ? -12.775 -31.043 18.487  1.00 21.88  ? 421  THR A CB  1 
ATOM   1553 O OG1 . THR A 1 196 ? -14.044 -31.700 18.365  1.00 24.53  ? 421  THR A OG1 1 
ATOM   1554 C CG2 . THR A 1 196 ? -11.659 -32.082 18.452  1.00 24.31  ? 421  THR A CG2 1 
ATOM   1555 N N   . LEU A 1 197 ? -10.526 -30.052 20.742  1.00 18.52  ? 422  LEU A N   1 
ATOM   1556 C CA  . LEU A 1 197 ? -9.209  -29.460 20.916  1.00 16.36  ? 422  LEU A CA  1 
ATOM   1557 C C   . LEU A 1 197 ? -8.467  -29.399 19.588  1.00 19.12  ? 422  LEU A C   1 
ATOM   1558 O O   . LEU A 1 197 ? -8.387  -30.394 18.858  1.00 17.07  ? 422  LEU A O   1 
ATOM   1559 C CB  . LEU A 1 197 ? -8.408  -30.281 21.929  1.00 20.26  ? 422  LEU A CB  1 
ATOM   1560 C CG  . LEU A 1 197 ? -6.946  -29.907 22.194  1.00 18.29  ? 422  LEU A CG  1 
ATOM   1561 C CD1 . LEU A 1 197 ? -6.795  -28.522 22.821  1.00 18.16  ? 422  LEU A CD1 1 
ATOM   1562 C CD2 . LEU A 1 197 ? -6.276  -30.965 23.070  1.00 18.93  ? 422  LEU A CD2 1 
ATOM   1563 N N   . LEU A 1 198 ? -7.918  -28.232 19.270  1.00 15.56  ? 423  LEU A N   1 
ATOM   1564 C CA  . LEU A 1 198 ? -7.083  -28.082 18.086  1.00 14.54  ? 423  LEU A CA  1 
ATOM   1565 C C   . LEU A 1 198 ? -5.645  -28.412 18.469  1.00 15.37  ? 423  LEU A C   1 
ATOM   1566 O O   . LEU A 1 198 ? -5.074  -27.784 19.372  1.00 17.28  ? 423  LEU A O   1 
ATOM   1567 C CB  . LEU A 1 198 ? -7.193  -26.667 17.516  1.00 15.82  ? 423  LEU A CB  1 
ATOM   1568 C CG  . LEU A 1 198 ? -6.483  -26.460 16.171  1.00 18.69  ? 423  LEU A CG  1 
ATOM   1569 C CD1 . LEU A 1 198 ? -7.152  -27.290 15.055  1.00 14.77  ? 423  LEU A CD1 1 
ATOM   1570 C CD2 . LEU A 1 198 ? -6.427  -24.970 15.827  1.00 17.34  ? 423  LEU A CD2 1 
ATOM   1571 N N   . ARG A 1 199 ? -5.070  -29.410 17.807  1.00 14.89  ? 424  ARG A N   1 
ATOM   1572 C CA  . ARG A 1 199 ? -3.758  -29.935 18.163  1.00 12.94  ? 424  ARG A CA  1 
ATOM   1573 C C   . ARG A 1 199 ? -2.681  -29.434 17.206  1.00 17.80  ? 424  ARG A C   1 
ATOM   1574 O O   . ARG A 1 199 ? -2.820  -29.567 15.986  1.00 16.50  ? 424  ARG A O   1 
ATOM   1575 C CB  . ARG A 1 199 ? -3.789  -31.461 18.168  1.00 15.32  ? 424  ARG A CB  1 
ATOM   1576 C CG  . ARG A 1 199 ? -4.705  -32.022 19.255  1.00 16.04  ? 424  ARG A CG  1 
ATOM   1577 C CD  . ARG A 1 199 ? -4.859  -33.548 19.207  1.00 19.26  ? 424  ARG A CD  1 
ATOM   1578 N NE  . ARG A 1 199 ? -5.738  -34.000 20.282  1.00 19.01  ? 424  ARG A NE  1 
ATOM   1579 C CZ  . ARG A 1 199 ? -5.360  -34.753 21.308  1.00 23.33  ? 424  ARG A CZ  1 
ATOM   1580 N NH1 . ARG A 1 199 ? -4.137  -35.253 21.391  1.00 16.99  ? 424  ARG A NH1 1 
ATOM   1581 N NH2 . ARG A 1 199 ? -6.233  -35.015 22.277  1.00 20.65  ? 424  ARG A NH2 1 
ATOM   1582 N N   . PHE A 1 200 ? -1.605  -28.876 17.770  1.00 13.26  ? 425  PHE A N   1 
ATOM   1583 C CA  . PHE A 1 200 ? -0.417  -28.483 17.018  1.00 12.44  ? 425  PHE A CA  1 
ATOM   1584 C C   . PHE A 1 200 ? 0.571   -29.647 17.090  1.00 15.47  ? 425  PHE A C   1 
ATOM   1585 O O   . PHE A 1 200 ? 1.127   -29.923 18.154  1.00 14.58  ? 425  PHE A O   1 
ATOM   1586 C CB  . PHE A 1 200 ? 0.198   -27.207 17.610  1.00 12.80  ? 425  PHE A CB  1 
ATOM   1587 C CG  . PHE A 1 200 ? -0.727  -26.010 17.572  1.00 13.52  ? 425  PHE A CG  1 
ATOM   1588 C CD1 . PHE A 1 200 ? -0.753  -25.172 16.461  1.00 13.03  ? 425  PHE A CD1 1 
ATOM   1589 C CD2 . PHE A 1 200 ? -1.575  -25.733 18.634  1.00 15.43  ? 425  PHE A CD2 1 
ATOM   1590 C CE1 . PHE A 1 200 ? -1.610  -24.072 16.409  1.00 14.45  ? 425  PHE A CE1 1 
ATOM   1591 C CE2 . PHE A 1 200 ? -2.440  -24.644 18.599  1.00 16.00  ? 425  PHE A CE2 1 
ATOM   1592 C CZ  . PHE A 1 200 ? -2.461  -23.805 17.476  1.00 16.29  ? 425  PHE A CZ  1 
ATOM   1593 N N   . GLY A 1 201 ? 0.812   -30.320 15.964  1.00 14.71  ? 426  GLY A N   1 
ATOM   1594 C CA  . GLY A 1 201 ? 1.552   -31.575 15.959  1.00 12.95  ? 426  GLY A CA  1 
ATOM   1595 C C   . GLY A 1 201 ? 2.956   -31.478 15.383  1.00 15.35  ? 426  GLY A C   1 
ATOM   1596 O O   . GLY A 1 201 ? 3.228   -30.660 14.501  1.00 13.48  ? 426  GLY A O   1 
ATOM   1597 N N   . THR A 1 202 ? 3.860   -32.316 15.901  1.00 14.39  ? 427  THR A N   1 
ATOM   1598 C CA  . THR A 1 202 ? 5.189   -32.494 15.320  1.00 10.89  ? 427  THR A CA  1 
ATOM   1599 C C   . THR A 1 202 ? 5.568   -33.968 15.399  1.00 17.45  ? 427  THR A C   1 
ATOM   1600 O O   . THR A 1 202 ? 4.881   -34.774 16.035  1.00 15.00  ? 427  THR A O   1 
ATOM   1601 C CB  . THR A 1 202 ? 6.253   -31.623 16.009  1.00 14.40  ? 427  THR A CB  1 
ATOM   1602 O OG1 . THR A 1 202 ? 7.436   -31.634 15.203  1.00 16.32  ? 427  THR A OG1 1 
ATOM   1603 C CG2 . THR A 1 202 ? 6.582   -32.187 17.370  1.00 15.09  ? 427  THR A CG2 1 
ATOM   1604 N N   . VAL A 1 203 ? 6.669   -34.324 14.739  1.00 14.53  ? 428  VAL A N   1 
ATOM   1605 C CA  . VAL A 1 203 ? 7.107   -35.711 14.632  1.00 15.34  ? 428  VAL A CA  1 
ATOM   1606 C C   . VAL A 1 203 ? 8.396   -35.873 15.437  1.00 13.39  ? 428  VAL A C   1 
ATOM   1607 O O   . VAL A 1 203 ? 9.452   -35.362 15.029  1.00 16.05  ? 428  VAL A O   1 
ATOM   1608 C CB  . VAL A 1 203 ? 7.323   -36.128 13.174  1.00 17.37  ? 428  VAL A CB  1 
ATOM   1609 C CG1 . VAL A 1 203 ? 7.817   -37.569 13.132  1.00 13.97  ? 428  VAL A CG1 1 
ATOM   1610 C CG2 . VAL A 1 203 ? 6.044   -35.959 12.375  1.00 19.94  ? 428  VAL A CG2 1 
ATOM   1611 N N   . PRO A 1 204 ? 8.366   -36.580 16.563  1.00 12.78  ? 429  PRO A N   1 
ATOM   1612 C CA  . PRO A 1 204 ? 9.606   -36.926 17.261  1.00 11.48  ? 429  PRO A CA  1 
ATOM   1613 C C   . PRO A 1 204 ? 10.232  -38.164 16.644  1.00 12.03  ? 429  PRO A C   1 
ATOM   1614 O O   . PRO A 1 204 ? 9.554   -39.000 16.052  1.00 13.33  ? 429  PRO A O   1 
ATOM   1615 C CB  . PRO A 1 204 ? 9.128   -37.212 18.688  1.00 11.49  ? 429  PRO A CB  1 
ATOM   1616 C CG  . PRO A 1 204 ? 7.754   -37.811 18.474  1.00 12.25  ? 429  PRO A CG  1 
ATOM   1617 C CD  . PRO A 1 204 ? 7.180   -37.182 17.203  1.00 12.52  ? 429  PRO A CD  1 
ATOM   1618 N N   . ILE A 1 205 ? 11.546  -38.287 16.792  1.00 11.59  ? 430  ILE A N   1 
ATOM   1619 C CA  . ILE A 1 205 ? 12.208  -39.531 16.403  1.00 13.66  ? 430  ILE A CA  1 
ATOM   1620 C C   . ILE A 1 205 ? 11.931  -40.593 17.461  1.00 12.13  ? 430  ILE A C   1 
ATOM   1621 O O   . ILE A 1 205 ? 12.169  -40.372 18.654  1.00 13.08  ? 430  ILE A O   1 
ATOM   1622 C CB  . ILE A 1 205 ? 13.719  -39.313 16.215  1.00 14.37  ? 430  ILE A CB  1 
ATOM   1623 C CG1 . ILE A 1 205 ? 13.975  -38.391 15.021  1.00 14.93  ? 430  ILE A CG1 1 
ATOM   1624 C CG2 . ILE A 1 205 ? 14.401  -40.650 15.995  1.00 14.63  ? 430  ILE A CG2 1 
ATOM   1625 C CD1 . ILE A 1 205 ? 15.452  -37.995 14.831  1.00 12.78  ? 430  ILE A CD1 1 
ATOM   1626 N N   . THR A 1 206 ? 11.392  -41.749 17.043  1.00 13.41  ? 431  THR A N   1 
ATOM   1627 C CA  . THR A 1 206 ? 11.208  -42.834 17.997  1.00 13.05  ? 431  THR A CA  1 
ATOM   1628 C C   . THR A 1 206 ? 11.625  -44.168 17.394  1.00 14.71  ? 431  THR A C   1 
ATOM   1629 O O   . THR A 1 206 ? 11.630  -44.354 16.169  1.00 16.57  ? 431  THR A O   1 
ATOM   1630 C CB  . THR A 1 206 ? 9.757   -42.977 18.548  1.00 13.64  ? 431  THR A CB  1 
ATOM   1631 O OG1 . THR A 1 206 ? 9.026   -43.968 17.809  1.00 16.90  ? 431  THR A OG1 1 
ATOM   1632 C CG2 . THR A 1 206 ? 8.997   -41.660 18.547  1.00 14.54  ? 431  THR A CG2 1 
ATOM   1633 N N   . THR A 1 207 ? 11.999  -45.082 18.288  1.00 16.14  ? 432  THR A N   1 
ATOM   1634 C CA  . THR A 1 207 ? 12.145  -46.496 17.986  1.00 14.43  ? 432  THR A CA  1 
ATOM   1635 C C   . THR A 1 207 ? 10.859  -47.230 18.369  1.00 16.94  ? 432  THR A C   1 
ATOM   1636 O O   . THR A 1 207 ? 9.885   -46.626 18.826  1.00 18.11  ? 432  THR A O   1 
ATOM   1637 C CB  . THR A 1 207 ? 13.352  -47.094 18.713  1.00 18.06  ? 432  THR A CB  1 
ATOM   1638 O OG1 . THR A 1 207 ? 13.211  -46.891 20.123  1.00 16.78  ? 432  THR A OG1 1 
ATOM   1639 C CG2 . THR A 1 207 ? 14.662  -46.456 18.229  1.00 17.89  ? 432  THR A CG2 1 
ATOM   1640 N N   . ARG A 1 208 ? 10.868  -48.557 18.187  1.00 16.91  ? 433  ARG A N   1 
ATOM   1641 C CA  . ARG A 1 208 ? 9.727   -49.433 18.495  1.00 21.22  ? 433  ARG A CA  1 
ATOM   1642 C C   . ARG A 1 208 ? 8.527   -49.133 17.600  1.00 20.94  ? 433  ARG A C   1 
ATOM   1643 O O   . ARG A 1 208 ? 7.381   -49.119 18.055  1.00 19.34  ? 433  ARG A O   1 
ATOM   1644 C CB  . ARG A 1 208 ? 9.329   -49.342 19.966  1.00 17.76  ? 433  ARG A CB  1 
ATOM   1645 C CG  . ARG A 1 208 ? 10.447  -49.720 20.927  1.00 16.34  ? 433  ARG A CG  1 
ATOM   1646 C CD  . ARG A 1 208 ? 9.943   -49.801 22.354  1.00 19.10  ? 433  ARG A CD  1 
ATOM   1647 N NE  . ARG A 1 208 ? 11.023  -50.122 23.279  1.00 23.52  ? 433  ARG A NE  1 
ATOM   1648 C CZ  . ARG A 1 208 ? 11.204  -51.311 23.838  1.00 34.08  ? 433  ARG A CZ  1 
ATOM   1649 N NH1 . ARG A 1 208 ? 10.383  -52.320 23.599  1.00 35.90  ? 433  ARG A NH1 1 
ATOM   1650 N NH2 . ARG A 1 208 ? 12.234  -51.490 24.659  1.00 35.26  ? 433  ARG A NH2 1 
ATOM   1651 N N   . ARG A 1 209 ? 8.787   -48.922 16.310  1.00 20.89  ? 434  ARG A N   1 
ATOM   1652 C CA  . ARG A 1 209 ? 7.748   -48.584 15.347  1.00 23.83  ? 434  ARG A CA  1 
ATOM   1653 C C   . ARG A 1 209 ? 7.375   -49.769 14.460  1.00 35.25  ? 434  ARG A C   1 
ATOM   1654 O O   . ARG A 1 209 ? 6.940   -49.588 13.320  1.00 26.55  ? 434  ARG A O   1 
ATOM   1655 C CB  . ARG A 1 209 ? 8.190   -47.389 14.503  1.00 18.41  ? 434  ARG A CB  1 
ATOM   1656 C CG  . ARG A 1 209 ? 8.411   -46.157 15.354  1.00 18.68  ? 434  ARG A CG  1 
ATOM   1657 C CD  . ARG A 1 209 ? 8.606   -44.885 14.552  1.00 19.51  ? 434  ARG A CD  1 
ATOM   1658 N NE  . ARG A 1 209 ? 9.835   -44.877 13.777  1.00 21.82  ? 434  ARG A NE  1 
ATOM   1659 C CZ  . ARG A 1 209 ? 9.887   -44.613 12.479  1.00 24.91  ? 434  ARG A CZ  1 
ATOM   1660 N NH1 . ARG A 1 209 ? 8.788   -44.376 11.777  1.00 20.47  ? 434  ARG A NH1 1 
ATOM   1661 N NH2 . ARG A 1 209 ? 11.070  -44.564 11.876  1.00 20.45  ? 434  ARG A NH2 1 
ATOM   1662 N N   . GLN A 1 210 ? 7.529   -50.991 14.974  1.00 26.23  ? 435  GLN A N   1 
ATOM   1663 C CA  . GLN A 1 210 ? 7.200   -52.165 14.170  1.00 31.62  ? 435  GLN A CA  1 
ATOM   1664 C C   . GLN A 1 210 ? 5.691   -52.336 14.020  1.00 33.24  ? 435  GLN A C   1 
ATOM   1665 O O   . GLN A 1 210 ? 5.217   -52.766 12.963  1.00 45.99  ? 435  GLN A O   1 
ATOM   1666 C CB  . GLN A 1 210 ? 7.825   -53.417 14.786  1.00 29.95  ? 435  GLN A CB  1 
ATOM   1667 C CG  . GLN A 1 210 ? 9.349   -53.383 14.844  1.00 46.71  ? 435  GLN A CG  1 
ATOM   1668 C CD  . GLN A 1 210 ? 9.993   -53.290 13.469  1.00 63.33  ? 435  GLN A CD  1 
ATOM   1669 O OE1 . GLN A 1 210 ? 9.576   -53.966 12.527  1.00 64.09  ? 435  GLN A OE1 1 
ATOM   1670 N NE2 . GLN A 1 210 ? 11.015  -52.447 13.349  1.00 55.21  ? 435  GLN A NE2 1 
ATOM   1671 N N   A SER A 1 211 ? 4.925   -52.013 15.065  0.49 45.74  ? 436  SER A N   1 
ATOM   1672 N N   B SER A 1 211 ? 4.921   -52.008 15.061  0.51 45.73  ? 436  SER A N   1 
ATOM   1673 C CA  A SER A 1 211 ? 3.474   -52.156 14.988  0.49 54.27  ? 436  SER A CA  1 
ATOM   1674 C CA  B SER A 1 211 ? 3.470   -52.161 14.977  0.51 54.29  ? 436  SER A CA  1 
ATOM   1675 C C   A SER A 1 211 ? 2.879   -51.174 13.985  0.49 60.60  ? 436  SER A C   1 
ATOM   1676 C C   B SER A 1 211 ? 2.868   -51.170 13.986  0.51 60.62  ? 436  SER A C   1 
ATOM   1677 O O   A SER A 1 211 ? 2.174   -51.575 13.052  0.49 55.44  ? 436  SER A O   1 
ATOM   1678 O O   B SER A 1 211 ? 2.144   -51.561 13.063  0.51 55.46  ? 436  SER A O   1 
ATOM   1679 C CB  A SER A 1 211 ? 2.848   -51.963 16.371  0.49 45.89  ? 436  SER A CB  1 
ATOM   1680 C CB  B SER A 1 211 ? 2.835   -51.999 16.361  0.51 45.89  ? 436  SER A CB  1 
ATOM   1681 O OG  A SER A 1 211 ? 1.433   -51.987 16.301  0.49 38.37  ? 436  SER A OG  1 
ATOM   1682 O OG  B SER A 1 211 ? 2.968   -53.180 17.136  0.51 35.78  ? 436  SER A OG  1 
ATOM   1683 N N   . ASP A 1 212 ? 3.157   -49.880 14.162  1.00 47.81  ? 437  ASP A N   1 
ATOM   1684 C CA  . ASP A 1 212 ? 2.684   -48.849 13.251  1.00 43.64  ? 437  ASP A CA  1 
ATOM   1685 C C   . ASP A 1 212 ? 3.689   -47.708 13.321  1.00 29.52  ? 437  ASP A C   1 
ATOM   1686 O O   . ASP A 1 212 ? 4.082   -47.297 14.422  1.00 39.79  ? 437  ASP A O   1 
ATOM   1687 C CB  . ASP A 1 212 ? 1.272   -48.374 13.605  1.00 61.13  ? 437  ASP A CB  1 
ATOM   1688 C CG  . ASP A 1 212 ? 1.236   -47.535 14.868  1.00 58.41  ? 437  ASP A CG  1 
ATOM   1689 O OD1 . ASP A 1 212 ? 1.700   -48.021 15.922  1.00 57.38  ? 437  ASP A OD1 1 
ATOM   1690 O OD2 . ASP A 1 212 ? 0.767   -46.377 14.799  1.00 57.59  ? 437  ASP A OD2 1 
ATOM   1691 N N   . PRO A 1 213 ? 4.152   -47.188 12.183  1.00 24.70  ? 438  PRO A N   1 
ATOM   1692 C CA  . PRO A 1 213 ? 5.325   -46.310 12.202  1.00 25.97  ? 438  PRO A CA  1 
ATOM   1693 C C   . PRO A 1 213 ? 5.060   -44.820 12.364  1.00 22.30  ? 438  PRO A C   1 
ATOM   1694 O O   . PRO A 1 213 ? 6.030   -44.078 12.553  1.00 23.18  ? 438  PRO A O   1 
ATOM   1695 C CB  . PRO A 1 213 ? 5.966   -46.593 10.836  1.00 26.51  ? 438  PRO A CB  1 
ATOM   1696 C CG  . PRO A 1 213 ? 4.806   -46.897 9.958   1.00 24.31  ? 438  PRO A CG  1 
ATOM   1697 C CD  . PRO A 1 213 ? 3.784   -47.589 10.816  1.00 22.23  ? 438  PRO A CD  1 
ATOM   1698 N N   . ILE A 1 214 ? 3.818   -44.349 12.302  1.00 16.69  ? 439  ILE A N   1 
ATOM   1699 C CA  . ILE A 1 214 ? 3.574   -42.908 12.377  1.00 16.95  ? 439  ILE A CA  1 
ATOM   1700 C C   . ILE A 1 214 ? 3.592   -42.451 13.833  1.00 17.69  ? 439  ILE A C   1 
ATOM   1701 O O   . ILE A 1 214 ? 2.838   -42.957 14.671  1.00 17.13  ? 439  ILE A O   1 
ATOM   1702 C CB  . ILE A 1 214 ? 2.251   -42.528 11.701  1.00 24.23  ? 439  ILE A CB  1 
ATOM   1703 C CG1 . ILE A 1 214 ? 2.342   -42.781 10.194  1.00 23.82  ? 439  ILE A CG1 1 
ATOM   1704 C CG2 . ILE A 1 214 ? 1.947   -41.055 11.953  1.00 26.36  ? 439  ILE A CG2 1 
ATOM   1705 C CD1 . ILE A 1 214 ? 3.522   -42.084 9.528   1.00 19.14  ? 439  ILE A CD1 1 
ATOM   1706 N N   . ARG A 1 215 ? 4.438   -41.472 14.131  1.00 16.54  ? 440  ARG A N   1 
ATOM   1707 C CA  . ARG A 1 215 ? 4.539   -40.907 15.471  1.00 14.75  ? 440  ARG A CA  1 
ATOM   1708 C C   . ARG A 1 215 ? 4.232   -39.419 15.409  1.00 17.23  ? 440  ARG A C   1 
ATOM   1709 O O   . ARG A 1 215 ? 4.861   -38.685 14.640  1.00 16.82  ? 440  ARG A O   1 
ATOM   1710 C CB  . ARG A 1 215 ? 5.936   -41.143 16.059  1.00 17.23  ? 440  ARG A CB  1 
ATOM   1711 C CG  . ARG A 1 215 ? 6.232   -42.611 16.369  1.00 18.43  ? 440  ARG A CG  1 
ATOM   1712 C CD  . ARG A 1 215 ? 5.350   -43.115 17.497  1.00 18.11  ? 440  ARG A CD  1 
ATOM   1713 N NE  . ARG A 1 215 ? 5.498   -44.551 17.709  1.00 19.49  ? 440  ARG A NE  1 
ATOM   1714 C CZ  . ARG A 1 215 ? 4.777   -45.472 17.083  1.00 25.07  ? 440  ARG A CZ  1 
ATOM   1715 N NH1 . ARG A 1 215 ? 3.843   -45.139 16.205  1.00 24.94  ? 440  ARG A NH1 1 
ATOM   1716 N NH2 . ARG A 1 215 ? 5.002   -46.759 17.337  1.00 23.33  ? 440  ARG A NH2 1 
ATOM   1717 N N   . ILE A 1 216 ? 3.267   -38.975 16.214  1.00 15.83  ? 441  ILE A N   1 
ATOM   1718 C CA  . ILE A 1 216 ? 2.869   -37.568 16.256  1.00 15.99  ? 441  ILE A CA  1 
ATOM   1719 C C   . ILE A 1 216 ? 2.630   -37.193 17.711  1.00 12.67  ? 441  ILE A C   1 
ATOM   1720 O O   . ILE A 1 216 ? 1.842   -37.849 18.397  1.00 16.40  ? 441  ILE A O   1 
ATOM   1721 C CB  . ILE A 1 216 ? 1.602   -37.287 15.431  1.00 16.05  ? 441  ILE A CB  1 
ATOM   1722 C CG1 . ILE A 1 216 ? 1.857   -37.524 13.938  1.00 21.13  ? 441  ILE A CG1 1 
ATOM   1723 C CG2 . ILE A 1 216 ? 1.135   -35.859 15.664  1.00 19.40  ? 441  ILE A CG2 1 
ATOM   1724 C CD1 . ILE A 1 216 ? 0.584   -37.544 13.108  1.00 25.12  ? 441  ILE A CD1 1 
ATOM   1725 N N   . ILE A 1 217 ? 3.312   -36.152 18.184  1.00 12.30  ? 442  ILE A N   1 
ATOM   1726 C CA  . ILE A 1 217 ? 3.082   -35.594 19.511  1.00 12.86  ? 442  ILE A CA  1 
ATOM   1727 C C   . ILE A 1 217 ? 2.485   -34.204 19.333  1.00 13.78  ? 442  ILE A C   1 
ATOM   1728 O O   . ILE A 1 217 ? 2.956   -33.423 18.497  1.00 13.92  ? 442  ILE A O   1 
ATOM   1729 C CB  . ILE A 1 217 ? 4.381   -35.565 20.339  1.00 13.12  ? 442  ILE A CB  1 
ATOM   1730 C CG1 . ILE A 1 217 ? 4.103   -35.043 21.746  1.00 14.08  ? 442  ILE A CG1 1 
ATOM   1731 C CG2 . ILE A 1 217 ? 5.460   -34.716 19.669  1.00 14.10  ? 442  ILE A CG2 1 
ATOM   1732 C CD1 . ILE A 1 217 ? 5.286   -35.173 22.665  1.00 13.92  ? 442  ILE A CD1 1 
ATOM   1733 N N   . SER A 1 218 ? 1.430   -33.909 20.088  1.00 14.40  ? 443  SER A N   1 
ATOM   1734 C CA  . SER A 1 218 ? 0.691   -32.660 19.950  1.00 12.45  ? 443  SER A CA  1 
ATOM   1735 C C   . SER A 1 218 ? 0.925   -31.749 21.148  1.00 14.36  ? 443  SER A C   1 
ATOM   1736 O O   . SER A 1 218 ? 1.326   -32.192 22.227  1.00 15.37  ? 443  SER A O   1 
ATOM   1737 C CB  . SER A 1 218 ? -0.813  -32.918 19.802  1.00 19.15  ? 443  SER A CB  1 
ATOM   1738 O OG  . SER A 1 218 ? -1.090  -33.666 18.628  1.00 17.62  ? 443  SER A OG  1 
ATOM   1739 N N   . CYS A 1 219 ? 0.668   -30.455 20.949  1.00 12.92  ? 444  CYS A N   1 
ATOM   1740 C CA  . CYS A 1 219 ? 0.746   -29.503 22.047  1.00 12.91  ? 444  CYS A CA  1 
ATOM   1741 C C   . CYS A 1 219 ? -0.387  -28.496 21.911  1.00 15.53  ? 444  CYS A C   1 
ATOM   1742 O O   . CYS A 1 219 ? -1.006  -28.366 20.852  1.00 13.77  ? 444  CYS A O   1 
ATOM   1743 C CB  . CYS A 1 219 ? 2.118   -28.801 22.104  1.00 13.05  ? 444  CYS A CB  1 
ATOM   1744 S SG  . CYS A 1 219 ? 2.503   -27.744 20.665  1.00 12.76  ? 444  CYS A SG  1 
ATOM   1745 N N   . ALA A 1 220 ? -0.653  -27.783 23.009  1.00 11.66  ? 445  ALA A N   1 
ATOM   1746 C CA  . ALA A 1 220 ? -1.795  -26.875 23.047  1.00 11.53  ? 445  ALA A CA  1 
ATOM   1747 C C   . ALA A 1 220 ? -1.469  -25.512 22.458  1.00 12.06  ? 445  ALA A C   1 
ATOM   1748 O O   . ALA A 1 220 ? -2.367  -24.832 21.944  1.00 13.17  ? 445  ALA A O   1 
ATOM   1749 C CB  . ALA A 1 220 ? -2.283  -26.707 24.492  1.00 14.93  ? 445  ALA A CB  1 
ATOM   1750 N N   . LEU A 1 221 ? -0.205  -25.092 22.540  1.00 13.99  ? 446  LEU A N   1 
ATOM   1751 C CA  . LEU A 1 221 ? 0.249   -23.782 22.089  1.00 10.60  ? 446  LEU A CA  1 
ATOM   1752 C C   . LEU A 1 221 ? 1.597   -23.931 21.398  1.00 12.17  ? 446  LEU A C   1 
ATOM   1753 O O   . LEU A 1 221 ? 2.507   -24.562 21.963  1.00 11.79  ? 446  LEU A O   1 
ATOM   1754 C CB  . LEU A 1 221 ? 0.398   -22.826 23.276  1.00 10.94  ? 446  LEU A CB  1 
ATOM   1755 C CG  . LEU A 1 221 ? -0.808  -22.591 24.164  1.00 13.20  ? 446  LEU A CG  1 
ATOM   1756 C CD1 . LEU A 1 221 ? -0.307  -21.963 25.450  1.00 13.58  ? 446  LEU A CD1 1 
ATOM   1757 C CD2 . LEU A 1 221 ? -1.828  -21.691 23.449  1.00 13.82  ? 446  LEU A CD2 1 
ATOM   1758 N N   . PRO A 1 222 ? 1.788   -23.327 20.224  1.00 11.72  ? 447  PRO A N   1 
ATOM   1759 C CA  . PRO A 1 222 ? 3.152   -23.224 19.687  1.00 13.42  ? 447  PRO A CA  1 
ATOM   1760 C C   . PRO A 1 222 ? 4.058   -22.539 20.698  1.00 12.31  ? 447  PRO A C   1 
ATOM   1761 O O   . PRO A 1 222 ? 3.630   -21.645 21.427  1.00 11.80  ? 447  PRO A O   1 
ATOM   1762 C CB  . PRO A 1 222 ? 2.979   -22.372 18.425  1.00 10.72  ? 447  PRO A CB  1 
ATOM   1763 C CG  . PRO A 1 222 ? 1.501   -22.544 18.047  1.00 11.72  ? 447  PRO A CG  1 
ATOM   1764 C CD  . PRO A 1 222 ? 0.793   -22.634 19.386  1.00 11.86  ? 447  PRO A CD  1 
ATOM   1765 N N   . GLN A 1 223 ? 5.320   -22.966 20.745  1.00 11.53  ? 448  GLN A N   1 
ATOM   1766 C CA  . GLN A 1 223 ? 6.254   -22.322 21.662  1.00 13.89  ? 448  GLN A CA  1 
ATOM   1767 C C   . GLN A 1 223 ? 6.285   -20.812 21.443  1.00 13.63  ? 448  GLN A C   1 
ATOM   1768 O O   . GLN A 1 223 ? 6.374   -20.041 22.410  1.00 11.13  ? 448  GLN A O   1 
ATOM   1769 C CB  . GLN A 1 223 ? 7.657   -22.915 21.496  1.00 10.59  ? 448  GLN A CB  1 
ATOM   1770 C CG  . GLN A 1 223 ? 8.738   -22.166 22.275  1.00 11.40  ? 448  GLN A CG  1 
ATOM   1771 C CD  . GLN A 1 223 ? 8.514   -22.230 23.787  1.00 14.36  ? 448  GLN A CD  1 
ATOM   1772 O OE1 . GLN A 1 223 ? 8.450   -23.315 24.363  1.00 16.49  ? 448  GLN A OE1 1 
ATOM   1773 N NE2 . GLN A 1 223 ? 8.391   -21.067 24.430  1.00 13.07  ? 448  GLN A NE2 1 
ATOM   1774 N N   . GLU A 1 224 ? 6.210   -20.368 20.179  1.00 13.18  ? 449  GLU A N   1 
ATOM   1775 C CA  . GLU A 1 224 ? 6.325   -18.936 19.910  1.00 10.13  ? 449  GLU A CA  1 
ATOM   1776 C C   . GLU A 1 224 ? 5.152   -18.151 20.486  1.00 11.29  ? 449  GLU A C   1 
ATOM   1777 O O   . GLU A 1 224 ? 5.310   -16.966 20.807  1.00 11.49  ? 449  GLU A O   1 
ATOM   1778 C CB  . GLU A 1 224 ? 6.457   -18.679 18.410  1.00 12.54  ? 449  GLU A CB  1 
ATOM   1779 C CG  . GLU A 1 224 ? 7.799   -19.145 17.815  1.00 10.77  ? 449  GLU A CG  1 
ATOM   1780 C CD  . GLU A 1 224 ? 7.894   -20.643 17.531  1.00 11.53  ? 449  GLU A CD  1 
ATOM   1781 O OE1 . GLU A 1 224 ? 6.927   -21.395 17.793  1.00 11.00  ? 449  GLU A OE1 1 
ATOM   1782 O OE2 . GLU A 1 224 ? 8.968   -21.080 17.040  1.00 14.76  ? 449  GLU A OE2 1 
ATOM   1783 N N   . TRP A 1 225 ? 3.975   -18.782 20.632  1.00 12.65  ? 450  TRP A N   1 
ATOM   1784 C CA  . TRP A 1 225 ? 2.870   -18.113 21.319  1.00 10.17  ? 450  TRP A CA  1 
ATOM   1785 C C   . TRP A 1 225 ? 3.151   -17.995 22.810  1.00 10.92  ? 450  TRP A C   1 
ATOM   1786 O O   . TRP A 1 225 ? 2.859   -16.963 23.421  1.00 11.95  ? 450  TRP A O   1 
ATOM   1787 C CB  . TRP A 1 225 ? 1.555   -18.869 21.125  1.00 11.34  ? 450  TRP A CB  1 
ATOM   1788 C CG  . TRP A 1 225 ? 0.948   -18.809 19.758  1.00 11.87  ? 450  TRP A CG  1 
ATOM   1789 C CD1 . TRP A 1 225 ? 1.529   -18.356 18.613  1.00 17.80  ? 450  TRP A CD1 1 
ATOM   1790 C CD2 . TRP A 1 225 ? -0.376  -19.215 19.411  1.00 13.78  ? 450  TRP A CD2 1 
ATOM   1791 N NE1 . TRP A 1 225 ? 0.647   -18.471 17.564  1.00 15.10  ? 450  TRP A NE1 1 
ATOM   1792 C CE2 . TRP A 1 225 ? -0.531  -18.996 18.031  1.00 13.94  ? 450  TRP A CE2 1 
ATOM   1793 C CE3 . TRP A 1 225 ? -1.438  -19.760 20.135  1.00 15.40  ? 450  TRP A CE3 1 
ATOM   1794 C CZ2 . TRP A 1 225 ? -1.716  -19.299 17.357  1.00 18.51  ? 450  TRP A CZ2 1 
ATOM   1795 C CZ3 . TRP A 1 225 ? -2.625  -20.051 19.471  1.00 13.73  ? 450  TRP A CZ3 1 
ATOM   1796 C CH2 . TRP A 1 225 ? -2.744  -19.831 18.085  1.00 15.87  ? 450  TRP A CH2 1 
ATOM   1797 N N   . ILE A 1 226 ? 3.688   -19.055 23.424  1.00 10.55  ? 451  ILE A N   1 
ATOM   1798 C CA  . ILE A 1 226 ? 4.002   -18.995 24.852  1.00 11.05  ? 451  ILE A CA  1 
ATOM   1799 C C   . ILE A 1 226 ? 4.967   -17.853 25.122  1.00 12.38  ? 451  ILE A C   1 
ATOM   1800 O O   . ILE A 1 226 ? 4.733   -17.012 25.999  1.00 12.45  ? 451  ILE A O   1 
ATOM   1801 C CB  . ILE A 1 226 ? 4.569   -20.341 25.342  1.00 9.88   ? 451  ILE A CB  1 
ATOM   1802 C CG1 . ILE A 1 226 ? 3.519   -21.444 25.169  1.00 10.76  ? 451  ILE A CG1 1 
ATOM   1803 C CG2 . ILE A 1 226 ? 5.081   -20.197 26.788  1.00 11.80  ? 451  ILE A CG2 1 
ATOM   1804 C CD1 . ILE A 1 226 ? 4.036   -22.845 25.518  1.00 13.79  ? 451  ILE A CD1 1 
ATOM   1805 N N   . THR A 1 227 ? 6.049   -17.785 24.345  1.00 11.26  ? 452  THR A N   1 
ATOM   1806 C CA  . THR A 1 227 ? 6.989   -16.680 24.504  1.00 11.72  ? 452  THR A CA  1 
ATOM   1807 C C   . THR A 1 227 ? 6.308   -15.338 24.264  1.00 12.95  ? 452  THR A C   1 
ATOM   1808 O O   . THR A 1 227 ? 6.595   -14.364 24.963  1.00 14.01  ? 452  THR A O   1 
ATOM   1809 C CB  . THR A 1 227 ? 8.179   -16.873 23.566  1.00 11.62  ? 452  THR A CB  1 
ATOM   1810 O OG1 . THR A 1 227 ? 8.813   -18.121 23.880  1.00 12.70  ? 452  THR A OG1 1 
ATOM   1811 C CG2 . THR A 1 227 ? 9.181   -15.731 23.725  1.00 13.95  ? 452  THR A CG2 1 
ATOM   1812 N N   . TRP A 1 228 ? 5.386   -15.278 23.294  1.00 11.57  ? 453  TRP A N   1 
ATOM   1813 C CA  . TRP A 1 228 ? 4.612   -14.059 23.061  1.00 12.33  ? 453  TRP A CA  1 
ATOM   1814 C C   . TRP A 1 228 ? 3.864   -13.625 24.318  1.00 14.02  ? 453  TRP A C   1 
ATOM   1815 O O   . TRP A 1 228 ? 3.827   -12.437 24.651  1.00 13.94  ? 453  TRP A O   1 
ATOM   1816 C CB  . TRP A 1 228 ? 3.633   -14.297 21.912  1.00 11.22  ? 453  TRP A CB  1 
ATOM   1817 C CG  . TRP A 1 228 ? 3.091   -13.053 21.232  1.00 12.72  ? 453  TRP A CG  1 
ATOM   1818 C CD1 . TRP A 1 228 ? 1.819   -12.563 21.302  1.00 12.12  ? 453  TRP A CD1 1 
ATOM   1819 C CD2 . TRP A 1 228 ? 3.808   -12.180 20.342  1.00 14.15  ? 453  TRP A CD2 1 
ATOM   1820 N NE1 . TRP A 1 228 ? 1.698   -11.431 20.508  1.00 14.84  ? 453  TRP A NE1 1 
ATOM   1821 C CE2 . TRP A 1 228 ? 2.906   -11.181 19.911  1.00 15.63  ? 453  TRP A CE2 1 
ATOM   1822 C CE3 . TRP A 1 228 ? 5.123   -12.154 19.869  1.00 13.18  ? 453  TRP A CE3 1 
ATOM   1823 C CZ2 . TRP A 1 228 ? 3.285   -10.156 19.028  1.00 16.75  ? 453  TRP A CZ2 1 
ATOM   1824 C CZ3 . TRP A 1 228 ? 5.499   -11.137 18.987  1.00 15.95  ? 453  TRP A CZ3 1 
ATOM   1825 C CH2 . TRP A 1 228 ? 4.585   -10.151 18.586  1.00 18.05  ? 453  TRP A CH2 1 
ATOM   1826 N N   . PHE A 1 229 ? 3.249   -14.573 25.025  1.00 14.20  ? 454  PHE A N   1 
ATOM   1827 C CA  . PHE A 1 229 ? 2.526   -14.216 26.246  1.00 11.12  ? 454  PHE A CA  1 
ATOM   1828 C C   . PHE A 1 229 ? 3.467   -13.765 27.351  1.00 14.11  ? 454  PHE A C   1 
ATOM   1829 O O   . PHE A 1 229 ? 3.069   -12.969 28.209  1.00 15.10  ? 454  PHE A O   1 
ATOM   1830 C CB  . PHE A 1 229 ? 1.691   -15.397 26.735  1.00 13.15  ? 454  PHE A CB  1 
ATOM   1831 C CG  . PHE A 1 229 ? 0.740   -15.945 25.706  1.00 15.88  ? 454  PHE A CG  1 
ATOM   1832 C CD1 . PHE A 1 229 ? 0.186   -15.126 24.732  1.00 16.63  ? 454  PHE A CD1 1 
ATOM   1833 C CD2 . PHE A 1 229 ? 0.389   -17.285 25.731  1.00 16.92  ? 454  PHE A CD2 1 
ATOM   1834 C CE1 . PHE A 1 229 ? -0.687  -15.641 23.794  1.00 15.22  ? 454  PHE A CE1 1 
ATOM   1835 C CE2 . PHE A 1 229 ? -0.483  -17.804 24.798  1.00 12.30  ? 454  PHE A CE2 1 
ATOM   1836 C CZ  . PHE A 1 229 ? -1.017  -16.992 23.827  1.00 15.73  ? 454  PHE A CZ  1 
ATOM   1837 N N   . LEU A 1 230 ? 4.692   -14.305 27.379  1.00 13.21  ? 455  LEU A N   1 
ATOM   1838 C CA  . LEU A 1 230 ? 5.671   -13.918 28.393  1.00 12.50  ? 455  LEU A CA  1 
ATOM   1839 C C   . LEU A 1 230 ? 6.241   -12.527 28.132  1.00 14.51  ? 455  LEU A C   1 
ATOM   1840 O O   . LEU A 1 230 ? 6.669   -11.846 29.075  1.00 19.46  ? 455  LEU A O   1 
ATOM   1841 C CB  . LEU A 1 230 ? 6.812   -14.939 28.436  1.00 11.80  ? 455  LEU A CB  1 
ATOM   1842 C CG  . LEU A 1 230 ? 6.476   -16.387 28.796  1.00 12.43  ? 455  LEU A CG  1 
ATOM   1843 C CD1 . LEU A 1 230 ? 7.749   -17.239 28.794  1.00 13.66  ? 455  LEU A CD1 1 
ATOM   1844 C CD2 . LEU A 1 230 ? 5.793   -16.455 30.163  1.00 19.77  ? 455  LEU A CD2 1 
ATOM   1845 N N   . THR A 1 231 ? 6.263   -12.092 26.872  1.00 12.04  ? 456  THR A N   1 
ATOM   1846 C CA  . THR A 1 231 ? 6.902   -10.839 26.489  1.00 14.62  ? 456  THR A CA  1 
ATOM   1847 C C   . THR A 1 231 ? 5.903   -9.710  26.282  1.00 20.20  ? 456  THR A C   1 
ATOM   1848 O O   . THR A 1 231 ? 6.295   -8.612  25.870  1.00 19.25  ? 456  THR A O   1 
ATOM   1849 C CB  . THR A 1 231 ? 7.744   -11.046 25.224  1.00 12.68  ? 456  THR A CB  1 
ATOM   1850 O OG1 . THR A 1 231 ? 6.928   -11.585 24.180  1.00 15.37  ? 456  THR A OG1 1 
ATOM   1851 C CG2 . THR A 1 231 ? 8.889   -12.022 25.512  1.00 16.81  ? 456  THR A CG2 1 
ATOM   1852 N N   . HIS A 1 232 ? 4.627   -9.953  26.561  1.00 17.78  ? 457  HIS A N   1 
ATOM   1853 C CA  . HIS A 1 232 ? 3.600   -8.926  26.523  1.00 17.06  ? 457  HIS A CA  1 
ATOM   1854 C C   . HIS A 1 232 ? 2.844   -8.952  27.841  1.00 20.93  ? 457  HIS A C   1 
ATOM   1855 O O   . HIS A 1 232 ? 2.832   -9.960  28.552  1.00 22.72  ? 457  HIS A O   1 
ATOM   1856 C CB  . HIS A 1 232 ? 2.639   -9.135  25.353  1.00 18.18  ? 457  HIS A CB  1 
ATOM   1857 C CG  . HIS A 1 232 ? 3.273   -8.966  24.008  1.00 18.10  ? 457  HIS A CG  1 
ATOM   1858 N ND1 . HIS A 1 232 ? 4.027   -9.949  23.405  1.00 14.34  ? 457  HIS A ND1 1 
ATOM   1859 C CD2 . HIS A 1 232 ? 3.263   -7.920  23.148  1.00 23.78  ? 457  HIS A CD2 1 
ATOM   1860 C CE1 . HIS A 1 232 ? 4.459   -9.516  22.234  1.00 17.45  ? 457  HIS A CE1 1 
ATOM   1861 N NE2 . HIS A 1 232 ? 4.006   -8.286  22.053  1.00 17.41  ? 457  HIS A NE2 1 
ATOM   1862 N N   . ASN A 1 233 ? 2.216   -7.830  28.171  1.00 21.01  ? 458  ASN A N   1 
ATOM   1863 C CA  . ASN A 1 233 ? 1.464   -7.708  29.417  1.00 31.78  ? 458  ASN A CA  1 
ATOM   1864 C C   . ASN A 1 233 ? -0.026  -7.722  29.093  1.00 27.25  ? 458  ASN A C   1 
ATOM   1865 O O   . ASN A 1 233 ? -0.723  -6.717  29.222  1.00 31.89  ? 458  ASN A O   1 
ATOM   1866 C CB  . ASN A 1 233 ? 1.875   -6.430  30.172  1.00 29.49  ? 458  ASN A CB  1 
ATOM   1867 N N   . PHE A 1 234 ? -0.510  -8.882  28.649  1.00 20.95  ? 459  PHE A N   1 
ATOM   1868 C CA  . PHE A 1 234 ? -1.893  -8.996  28.211  1.00 19.70  ? 459  PHE A CA  1 
ATOM   1869 C C   . PHE A 1 234 ? -2.822  -9.187  29.398  1.00 20.60  ? 459  PHE A C   1 
ATOM   1870 O O   . PHE A 1 234 ? -2.490  -9.880  30.365  1.00 21.03  ? 459  PHE A O   1 
ATOM   1871 C CB  . PHE A 1 234 ? -2.083  -10.176 27.261  1.00 15.89  ? 459  PHE A CB  1 
ATOM   1872 C CG  . PHE A 1 234 ? -1.368  -10.040 25.944  1.00 13.59  ? 459  PHE A CG  1 
ATOM   1873 C CD1 . PHE A 1 234 ? -1.266  -8.811  25.307  1.00 24.82  ? 459  PHE A CD1 1 
ATOM   1874 C CD2 . PHE A 1 234 ? -0.835  -11.157 25.321  1.00 16.13  ? 459  PHE A CD2 1 
ATOM   1875 C CE1 . PHE A 1 234 ? -0.620  -8.701  24.078  1.00 16.27  ? 459  PHE A CE1 1 
ATOM   1876 C CE2 . PHE A 1 234 ? -0.189  -11.054 24.108  1.00 20.32  ? 459  PHE A CE2 1 
ATOM   1877 C CZ  . PHE A 1 234 ? -0.079  -9.826  23.480  1.00 23.20  ? 459  PHE A CZ  1 
ATOM   1878 N N   . THR A 1 235 ? -4.003  -8.590  29.299  1.00 20.29  ? 460  THR A N   1 
ATOM   1879 C CA  . THR A 1 235 ? -5.097  -8.829  30.225  1.00 22.23  ? 460  THR A CA  1 
ATOM   1880 C C   . THR A 1 235 ? -6.179  -9.601  29.484  1.00 26.24  ? 460  THR A C   1 
ATOM   1881 O O   . THR A 1 235 ? -6.646  -9.159  28.432  1.00 29.55  ? 460  THR A O   1 
ATOM   1882 C CB  . THR A 1 235 ? -5.661  -7.510  30.768  1.00 32.62  ? 460  THR A CB  1 
ATOM   1883 O OG1 . THR A 1 235 ? -4.631  -6.788  31.457  1.00 30.11  ? 460  THR A OG1 1 
ATOM   1884 C CG2 . THR A 1 235 ? -6.830  -7.774  31.723  1.00 27.48  ? 460  THR A CG2 1 
ATOM   1885 N N   . ALA A 1 236 ? -6.572  -10.751 30.026  1.00 22.86  ? 461  ALA A N   1 
ATOM   1886 C CA  . ALA A 1 236 ? -7.660  -11.525 29.432  1.00 29.80  ? 461  ALA A CA  1 
ATOM   1887 C C   . ALA A 1 236 ? -8.967  -10.798 29.715  1.00 27.56  ? 461  ALA A C   1 
ATOM   1888 O O   . ALA A 1 236 ? -9.505  -10.865 30.821  1.00 32.13  ? 461  ALA A O   1 
ATOM   1889 C CB  . ALA A 1 236 ? -7.681  -12.945 29.987  1.00 25.45  ? 461  ALA A CB  1 
ATOM   1890 N N   . LEU A 1 237 ? -9.477  -10.083 28.714  1.00 22.06  ? 462  LEU A N   1 
ATOM   1891 C CA  . LEU A 1 237 ? -10.699 -9.308  28.882  1.00 23.44  ? 462  LEU A CA  1 
ATOM   1892 C C   . LEU A 1 237 ? -11.958 -10.145 28.705  1.00 23.91  ? 462  LEU A C   1 
ATOM   1893 O O   . LEU A 1 237 ? -13.061 -9.628  28.920  1.00 31.47  ? 462  LEU A O   1 
ATOM   1894 C CB  . LEU A 1 237 ? -10.716 -8.131  27.901  1.00 30.76  ? 462  LEU A CB  1 
ATOM   1895 C CG  . LEU A 1 237 ? -9.616  -7.088  28.130  1.00 32.24  ? 462  LEU A CG  1 
ATOM   1896 C CD1 . LEU A 1 237 ? -9.629  -6.020  27.042  1.00 36.54  ? 462  LEU A CD1 1 
ATOM   1897 C CD2 . LEU A 1 237 ? -9.762  -6.454  29.507  1.00 34.82  ? 462  LEU A CD2 1 
ATOM   1898 N N   . GLY A 1 238 ? -11.820 -11.414 28.325  1.00 26.36  ? 463  GLY A N   1 
ATOM   1899 C CA  . GLY A 1 238 ? -12.948 -12.311 28.206  1.00 20.60  ? 463  GLY A CA  1 
ATOM   1900 C C   . GLY A 1 238 ? -12.494 -13.735 28.459  1.00 21.64  ? 463  GLY A C   1 
ATOM   1901 O O   . GLY A 1 238 ? -11.307 -14.010 28.661  1.00 20.92  ? 463  GLY A O   1 
ATOM   1902 N N   . ASP A 1 239 ? -13.468 -14.649 28.434  1.00 21.76  ? 464  ASP A N   1 
ATOM   1903 C CA  . ASP A 1 239 ? -13.182 -16.062 28.660  1.00 19.61  ? 464  ASP A CA  1 
ATOM   1904 C C   . ASP A 1 239 ? -12.282 -16.646 27.580  1.00 22.74  ? 464  ASP A C   1 
ATOM   1905 O O   . ASP A 1 239 ? -11.507 -17.574 27.844  1.00 18.61  ? 464  ASP A O   1 
ATOM   1906 C CB  . ASP A 1 239 ? -14.489 -16.848 28.715  1.00 18.44  ? 464  ASP A CB  1 
ATOM   1907 C CG  . ASP A 1 239 ? -15.327 -16.505 29.928  1.00 26.04  ? 464  ASP A CG  1 
ATOM   1908 O OD1 . ASP A 1 239 ? -14.749 -16.074 30.947  1.00 25.93  ? 464  ASP A OD1 1 
ATOM   1909 O OD2 . ASP A 1 239 ? -16.564 -16.678 29.857  1.00 27.10  ? 464  ASP A OD2 1 
ATOM   1910 N N   . ALA A 1 240 ? -12.388 -16.145 26.356  1.00 20.38  ? 465  ALA A N   1 
ATOM   1911 C CA  . ALA A 1 240 ? -11.632 -16.712 25.257  1.00 17.71  ? 465  ALA A CA  1 
ATOM   1912 C C   . ALA A 1 240 ? -11.354 -15.620 24.241  1.00 19.52  ? 465  ALA A C   1 
ATOM   1913 O O   . ALA A 1 240 ? -12.116 -14.652 24.121  1.00 19.10  ? 465  ALA A O   1 
ATOM   1914 C CB  . ALA A 1 240 ? -12.387 -17.875 24.590  1.00 18.34  ? 465  ALA A CB  1 
ATOM   1915 N N   . ALA A 1 241 ? -10.243 -15.781 23.532  1.00 16.87  ? 466  ALA A N   1 
ATOM   1916 C CA  . ALA A 1 241 ? -9.928  -14.950 22.380  1.00 17.30  ? 466  ALA A CA  1 
ATOM   1917 C C   . ALA A 1 241 ? -10.473 -15.637 21.132  1.00 17.97  ? 466  ALA A C   1 
ATOM   1918 O O   . ALA A 1 241 ? -10.058 -16.752 20.803  1.00 19.32  ? 466  ALA A O   1 
ATOM   1919 C CB  . ALA A 1 241 ? -8.419  -14.720 22.263  1.00 15.16  ? 466  ALA A CB  1 
ATOM   1920 N N   . LEU A 1 242 ? -11.418 -14.984 20.463  1.00 21.66  ? 467  LEU A N   1 
ATOM   1921 C CA  . LEU A 1 242 ? -11.873 -15.447 19.159  1.00 17.02  ? 467  LEU A CA  1 
ATOM   1922 C C   . LEU A 1 242 ? -10.794 -15.149 18.125  1.00 17.70  ? 467  LEU A C   1 
ATOM   1923 O O   . LEU A 1 242 ? -10.335 -14.008 18.008  1.00 19.98  ? 467  LEU A O   1 
ATOM   1924 C CB  . LEU A 1 242 ? -13.183 -14.755 18.780  1.00 21.42  ? 467  LEU A CB  1 
ATOM   1925 C CG  . LEU A 1 242 ? -13.768 -15.095 17.414  1.00 21.54  ? 467  LEU A CG  1 
ATOM   1926 C CD1 . LEU A 1 242 ? -14.205 -16.546 17.381  1.00 22.79  ? 467  LEU A CD1 1 
ATOM   1927 C CD2 . LEU A 1 242 ? -14.937 -14.169 17.105  1.00 19.30  ? 467  LEU A CD2 1 
ATOM   1928 N N   . LEU A 1 243 ? -10.368 -16.180 17.397  1.00 19.00  ? 468  LEU A N   1 
ATOM   1929 C CA  . LEU A 1 243 ? -9.327  -16.061 16.387  1.00 18.38  ? 468  LEU A CA  1 
ATOM   1930 C C   . LEU A 1 243 ? -9.868  -16.485 15.033  1.00 19.82  ? 468  LEU A C   1 
ATOM   1931 O O   . LEU A 1 243 ? -10.793 -17.292 14.941  1.00 19.57  ? 468  LEU A O   1 
ATOM   1932 C CB  . LEU A 1 243 ? -8.112  -16.947 16.699  1.00 21.38  ? 468  LEU A CB  1 
ATOM   1933 C CG  . LEU A 1 243 ? -7.572  -17.023 18.121  1.00 15.31  ? 468  LEU A CG  1 
ATOM   1934 C CD1 . LEU A 1 243 ? -6.447  -18.040 18.150  1.00 15.40  ? 468  LEU A CD1 1 
ATOM   1935 C CD2 . LEU A 1 243 ? -7.101  -15.647 18.573  1.00 20.69  ? 468  LEU A CD2 1 
ATOM   1936 N N   . ARG A 1 244 ? -9.249  -15.964 13.975  1.00 19.99  ? 469  ARG A N   1 
ATOM   1937 C CA  . ARG A 1 244 ? -9.460  -16.470 12.628  1.00 19.78  ? 469  ARG A CA  1 
ATOM   1938 C C   . ARG A 1 244 ? -8.158  -17.064 12.121  1.00 20.75  ? 469  ARG A C   1 
ATOM   1939 O O   . ARG A 1 244 ? -7.084  -16.485 12.323  1.00 21.81  ? 469  ARG A O   1 
ATOM   1940 C CB  . ARG A 1 244 ? -9.940  -15.373 11.673  1.00 20.31  ? 469  ARG A CB  1 
ATOM   1941 C CG  . ARG A 1 244 ? -11.428 -15.108 11.790  1.00 34.10  ? 469  ARG A CG  1 
ATOM   1942 C CD  . ARG A 1 244 ? -11.820 -13.786 11.163  1.00 42.17  ? 469  ARG A CD  1 
ATOM   1943 N NE  . ARG A 1 244 ? -13.170 -13.402 11.561  1.00 39.45  ? 469  ARG A NE  1 
ATOM   1944 C CZ  . ARG A 1 244 ? -13.603 -12.149 11.611  1.00 46.54  ? 469  ARG A CZ  1 
ATOM   1945 N NH1 . ARG A 1 244 ? -12.823 -11.137 11.270  1.00 39.09  ? 469  ARG A NH1 1 
ATOM   1946 N NH2 . ARG A 1 244 ? -14.844 -11.906 12.027  1.00 48.37  ? 469  ARG A NH2 1 
ATOM   1947 N N   . TYR A 1 245 ? -8.252  -18.227 11.486  1.00 20.58  ? 470  TYR A N   1 
ATOM   1948 C CA  . TYR A 1 245 ? -7.108  -18.863 10.839  1.00 17.89  ? 470  TYR A CA  1 
ATOM   1949 C C   . TYR A 1 245 ? -7.218  -18.576 9.342   1.00 19.77  ? 470  TYR A C   1 
ATOM   1950 O O   . TYR A 1 245 ? -8.133  -19.069 8.677   1.00 24.50  ? 470  TYR A O   1 
ATOM   1951 C CB  . TYR A 1 245 ? -7.084  -20.362 11.120  1.00 21.27  ? 470  TYR A CB  1 
ATOM   1952 C CG  . TYR A 1 245 ? -5.828  -21.054 10.651  1.00 20.69  ? 470  TYR A CG  1 
ATOM   1953 C CD1 . TYR A 1 245 ? -4.577  -20.645 11.100  1.00 13.92  ? 470  TYR A CD1 1 
ATOM   1954 C CD2 . TYR A 1 245 ? -5.891  -22.125 9.766   1.00 23.56  ? 470  TYR A CD2 1 
ATOM   1955 C CE1 . TYR A 1 245 ? -3.415  -21.294 10.681  1.00 18.55  ? 470  TYR A CE1 1 
ATOM   1956 C CE2 . TYR A 1 245 ? -4.751  -22.768 9.333   1.00 19.37  ? 470  TYR A CE2 1 
ATOM   1957 C CZ  . TYR A 1 245 ? -3.512  -22.354 9.795   1.00 16.74  ? 470  TYR A CZ  1 
ATOM   1958 O OH  . TYR A 1 245 ? -2.372  -22.995 9.372   1.00 16.24  ? 470  TYR A OH  1 
ATOM   1959 N N   . ARG A 1 246 ? -6.290  -17.781 8.818   1.00 19.73  ? 471  ARG A N   1 
ATOM   1960 C CA  . ARG A 1 246 ? -6.381  -17.266 7.458   1.00 24.77  ? 471  ARG A CA  1 
ATOM   1961 C C   . ARG A 1 246 ? -5.128  -17.639 6.673   1.00 26.08  ? 471  ARG A C   1 
ATOM   1962 O O   . ARG A 1 246 ? -4.010  -17.520 7.180   1.00 23.06  ? 471  ARG A O   1 
ATOM   1963 C CB  . ARG A 1 246 ? -6.566  -15.742 7.485   1.00 23.60  ? 471  ARG A CB  1 
ATOM   1964 C CG  . ARG A 1 246 ? -6.808  -15.082 6.137   1.00 37.73  ? 471  ARG A CG  1 
ATOM   1965 C CD  . ARG A 1 246 ? -6.739  -13.561 6.265   1.00 51.08  ? 471  ARG A CD  1 
ATOM   1966 N NE  . ARG A 1 246 ? -7.673  -13.042 7.259   1.00 45.56  ? 471  ARG A NE  1 
ATOM   1967 N N   . ASN A 1 247 ? -5.316  -18.107 5.438   1.00 24.63  ? 472  ASN A N   1 
ATOM   1968 C CA  . ASN A 1 247 ? -4.189  -18.283 4.523   1.00 26.46  ? 472  ASN A CA  1 
ATOM   1969 C C   . ASN A 1 247 ? -3.864  -16.919 3.935   1.00 30.45  ? 472  ASN A C   1 
ATOM   1970 O O   . ASN A 1 247 ? -4.603  -16.420 3.083   1.00 31.02  ? 472  ASN A O   1 
ATOM   1971 C CB  . ASN A 1 247 ? -4.525  -19.293 3.428   1.00 39.58  ? 472  ASN A CB  1 
ATOM   1972 C CG  . ASN A 1 247 ? -3.344  -19.570 2.504   1.00 52.51  ? 472  ASN A CG  1 
ATOM   1973 O OD1 . ASN A 1 247 ? -2.720  -18.649 1.969   1.00 44.05  ? 472  ASN A OD1 1 
ATOM   1974 N ND2 . ASN A 1 247 ? -3.026  -20.847 2.324   1.00 42.17  ? 472  ASN A ND2 1 
ATOM   1975 N N   . GLN A 1 248 ? -2.762  -16.310 4.380   1.00 36.62  ? 473  GLN A N   1 
ATOM   1976 C CA  . GLN A 1 248 ? -2.488  -14.928 3.993   1.00 46.05  ? 473  GLN A CA  1 
ATOM   1977 C C   . GLN A 1 248 ? -2.088  -14.810 2.528   1.00 49.80  ? 473  GLN A C   1 
ATOM   1978 O O   . GLN A 1 248 ? -2.349  -13.777 1.901   1.00 49.11  ? 473  GLN A O   1 
ATOM   1979 C CB  . GLN A 1 248 ? -1.408  -14.325 4.888   1.00 39.83  ? 473  GLN A CB  1 
ATOM   1980 C CG  . GLN A 1 248 ? -1.858  -14.126 6.330   1.00 50.08  ? 473  GLN A CG  1 
ATOM   1981 C CD  . GLN A 1 248 ? -0.838  -13.376 7.159   1.00 60.79  ? 473  GLN A CD  1 
ATOM   1982 O OE1 . GLN A 1 248 ? 0.343   -13.325 6.813   1.00 58.47  ? 473  GLN A OE1 1 
ATOM   1983 N NE2 . GLN A 1 248 ? -1.290  -12.781 8.260   1.00 48.67  ? 473  GLN A NE2 1 
ATOM   1984 N N   . ALA A 1 249 ? -1.464  -15.844 1.963   1.00 30.23  ? 474  ALA A N   1 
ATOM   1985 C CA  . ALA A 1 249 ? -1.150  -15.806 0.538   1.00 33.72  ? 474  ALA A CA  1 
ATOM   1986 C C   . ALA A 1 249 ? -2.423  -15.799 -0.306  1.00 44.74  ? 474  ALA A C   1 
ATOM   1987 O O   . ALA A 1 249 ? -2.596  -14.942 -1.181  1.00 46.82  ? 474  ALA A O   1 
ATOM   1988 C CB  . ALA A 1 249 ? -0.259  -16.989 0.162   1.00 40.10  ? 474  ALA A CB  1 
ATOM   1989 N N   . THR A 1 250 ? -3.333  -16.740 -0.046  1.00 44.45  ? 475  THR A N   1 
ATOM   1990 C CA  . THR A 1 250 ? -4.528  -16.924 -0.864  1.00 50.30  ? 475  THR A CA  1 
ATOM   1991 C C   . THR A 1 250 ? -5.742  -16.162 -0.350  1.00 41.63  ? 475  THR A C   1 
ATOM   1992 O O   . THR A 1 250 ? -6.777  -16.164 -1.024  1.00 57.68  ? 475  THR A O   1 
ATOM   1993 C CB  . THR A 1 250 ? -4.888  -18.411 -0.954  1.00 56.30  ? 475  THR A CB  1 
ATOM   1994 O OG1 . THR A 1 250 ? -5.440  -18.845 0.297   1.00 48.09  ? 475  THR A OG1 1 
ATOM   1995 C CG2 . THR A 1 250 ? -3.651  -19.243 -1.276  1.00 51.68  ? 475  THR A CG2 1 
ATOM   1996 N N   . GLY A 1 251 ? -5.653  -15.530 0.822   1.00 59.18  ? 476  GLY A N   1 
ATOM   1997 C CA  . GLY A 1 251 ? -6.755  -14.782 1.392   1.00 63.41  ? 476  GLY A CA  1 
ATOM   1998 C C   . GLY A 1 251 ? -7.855  -15.609 2.025   1.00 61.76  ? 476  GLY A C   1 
ATOM   1999 O O   . GLY A 1 251 ? -8.649  -15.063 2.801   1.00 59.46  ? 476  GLY A O   1 
ATOM   2000 N N   . GLN A 1 252 ? -7.922  -16.907 1.733   1.00 42.79  ? 477  GLN A N   1 
ATOM   2001 C CA  . GLN A 1 252 ? -9.026  -17.747 2.180   1.00 39.56  ? 477  GLN A CA  1 
ATOM   2002 C C   . GLN A 1 252 ? -9.091  -17.809 3.706   1.00 50.61  ? 477  GLN A C   1 
ATOM   2003 O O   . GLN A 1 252 ? -8.122  -18.198 4.366   1.00 32.77  ? 477  GLN A O   1 
ATOM   2004 C CB  . GLN A 1 252 ? -8.861  -19.151 1.592   1.00 48.07  ? 477  GLN A CB  1 
ATOM   2005 C CG  . GLN A 1 252 ? -10.125 -20.003 1.566   1.00 53.71  ? 477  GLN A CG  1 
ATOM   2006 C CD  . GLN A 1 252 ? -9.842  -21.462 1.221   1.00 64.98  ? 477  GLN A CD  1 
ATOM   2007 O OE1 . GLN A 1 252 ? -8.686  -21.893 1.174   1.00 56.24  ? 477  GLN A OE1 1 
ATOM   2008 N NE2 . GLN A 1 252 ? -10.901 -22.228 0.979   1.00 58.55  ? 477  GLN A NE2 1 
ATOM   2009 N N   . LEU A 1 253 ? -10.229 -17.408 4.268   1.00 45.55  ? 478  LEU A N   1 
ATOM   2010 C CA  . LEU A 1 253 ? -10.504 -17.673 5.675   1.00 26.66  ? 478  LEU A CA  1 
ATOM   2011 C C   . LEU A 1 253 ? -10.793 -19.158 5.839   1.00 34.47  ? 478  LEU A C   1 
ATOM   2012 O O   . LEU A 1 253 ? -11.732 -19.683 5.233   1.00 35.91  ? 478  LEU A O   1 
ATOM   2013 C CB  . LEU A 1 253 ? -11.684 -16.831 6.157   1.00 36.69  ? 478  LEU A CB  1 
ATOM   2014 C CG  . LEU A 1 253 ? -12.068 -16.939 7.634   1.00 37.56  ? 478  LEU A CG  1 
ATOM   2015 N N   . LEU A 1 254 ? -9.980  -19.844 6.639   1.00 24.51  ? 479  LEU A N   1 
ATOM   2016 C CA  . LEU A 1 254 ? -10.119 -21.290 6.767   1.00 26.63  ? 479  LEU A CA  1 
ATOM   2017 C C   . LEU A 1 254 ? -11.112 -21.669 7.862   1.00 27.68  ? 479  LEU A C   1 
ATOM   2018 O O   . LEU A 1 254 ? -12.034 -22.454 7.618   1.00 31.06  ? 479  LEU A O   1 
ATOM   2019 C CB  . LEU A 1 254 ? -8.751  -21.927 7.029   1.00 27.02  ? 479  LEU A CB  1 
ATOM   2020 C CG  . LEU A 1 254 ? -7.756  -21.740 5.875   1.00 33.04  ? 479  LEU A CG  1 
ATOM   2021 C CD1 . LEU A 1 254 ? -6.390  -22.295 6.236   1.00 24.21  ? 479  LEU A CD1 1 
ATOM   2022 C CD2 . LEU A 1 254 ? -8.273  -22.388 4.594   1.00 37.55  ? 479  LEU A CD2 1 
ATOM   2023 N N   . PHE A 1 255 ? -10.955 -21.116 9.064   1.00 24.67  ? 480  PHE A N   1 
ATOM   2024 C CA  . PHE A 1 255 ? -11.933 -21.350 10.122  1.00 21.26  ? 480  PHE A CA  1 
ATOM   2025 C C   . PHE A 1 255 ? -11.750 -20.293 11.201  1.00 21.08  ? 480  PHE A C   1 
ATOM   2026 O O   . PHE A 1 255 ? -10.749 -19.575 11.228  1.00 23.76  ? 480  PHE A O   1 
ATOM   2027 C CB  . PHE A 1 255 ? -11.802 -22.761 10.715  1.00 21.51  ? 480  PHE A CB  1 
ATOM   2028 C CG  . PHE A 1 255 ? -10.429 -23.082 11.246  1.00 20.00  ? 480  PHE A CG  1 
ATOM   2029 C CD1 . PHE A 1 255 ? -10.024 -22.654 12.509  1.00 20.76  ? 480  PHE A CD1 1 
ATOM   2030 C CD2 . PHE A 1 255 ? -9.555  -23.842 10.493  1.00 26.38  ? 480  PHE A CD2 1 
ATOM   2031 C CE1 . PHE A 1 255 ? -8.757  -22.960 12.985  1.00 19.99  ? 480  PHE A CE1 1 
ATOM   2032 C CE2 . PHE A 1 255 ? -8.293  -24.156 10.969  1.00 27.86  ? 480  PHE A CE2 1 
ATOM   2033 C CZ  . PHE A 1 255 ? -7.895  -23.715 12.215  1.00 27.63  ? 480  PHE A CZ  1 
ATOM   2034 N N   . GLU A 1 256 ? -12.734 -20.205 12.092  1.00 21.26  ? 481  GLU A N   1 
ATOM   2035 C CA  . GLU A 1 256 ? -12.582 -19.447 13.324  1.00 23.79  ? 481  GLU A CA  1 
ATOM   2036 C C   . GLU A 1 256 ? -12.478 -20.424 14.487  1.00 22.40  ? 481  GLU A C   1 
ATOM   2037 O O   . GLU A 1 256 ? -12.908 -21.574 14.399  1.00 19.48  ? 481  GLU A O   1 
ATOM   2038 C CB  . GLU A 1 256 ? -13.736 -18.457 13.540  1.00 22.69  ? 481  GLU A CB  1 
ATOM   2039 C CG  . GLU A 1 256 ? -15.126 -19.066 13.640  1.00 39.92  ? 481  GLU A CG  1 
ATOM   2040 C CD  . GLU A 1 256 ? -16.194 -18.028 13.965  1.00 43.44  ? 481  GLU A CD  1 
ATOM   2041 O OE1 . GLU A 1 256 ? -15.979 -16.829 13.670  1.00 31.35  ? 481  GLU A OE1 1 
ATOM   2042 O OE2 . GLU A 1 256 ? -17.246 -18.412 14.525  1.00 24.44  ? 481  GLU A OE2 1 
ATOM   2043 N N   . CYS A 1 257 ? -11.856 -19.970 15.570  1.00 18.67  ? 482  CYS A N   1 
ATOM   2044 C CA  . CYS A 1 257 ? -11.589 -20.854 16.692  1.00 17.56  ? 482  CYS A CA  1 
ATOM   2045 C C   . CYS A 1 257 ? -11.541 -20.012 17.957  1.00 19.85  ? 482  CYS A C   1 
ATOM   2046 O O   . CYS A 1 257 ? -11.525 -18.780 17.908  1.00 18.82  ? 482  CYS A O   1 
ATOM   2047 C CB  . CYS A 1 257 ? -10.288 -21.640 16.481  1.00 15.99  ? 482  CYS A CB  1 
ATOM   2048 S SG  . CYS A 1 257 ? -8.820  -20.611 16.205  1.00 18.26  ? 482  CYS A SG  1 
ATOM   2049 N N   . LYS A 1 258 ? -11.545 -20.687 19.103  1.00 16.65  ? 483  LYS A N   1 
ATOM   2050 C CA  . LYS A 1 258 ? -11.484 -20.015 20.394  1.00 17.61  ? 483  LYS A CA  1 
ATOM   2051 C C   . LYS A 1 258 ? -10.202 -20.413 21.106  1.00 15.37  ? 483  LYS A C   1 
ATOM   2052 O O   . LYS A 1 258 ? -9.907  -21.603 21.247  1.00 17.56  ? 483  LYS A O   1 
ATOM   2053 C CB  . LYS A 1 258 ? -12.709 -20.356 21.256  1.00 16.80  ? 483  LYS A CB  1 
ATOM   2054 C CG  . LYS A 1 258 ? -13.937 -19.502 20.943  1.00 17.63  ? 483  LYS A CG  1 
ATOM   2055 C CD  . LYS A 1 258 ? -15.221 -20.220 21.317  1.00 20.77  ? 483  LYS A CD  1 
ATOM   2056 C CE  . LYS A 1 258 ? -15.321 -20.426 22.815  1.00 23.21  ? 483  LYS A CE  1 
ATOM   2057 N NZ  . LYS A 1 258 ? -16.587 -21.138 23.193  1.00 23.88  ? 483  LYS A NZ  1 
ATOM   2058 N N   . LEU A 1 259 ? -9.432  -19.415 21.522  1.00 15.03  ? 484  LEU A N   1 
ATOM   2059 C CA  . LEU A 1 259 ? -8.259  -19.610 22.366  1.00 14.39  ? 484  LEU A CA  1 
ATOM   2060 C C   . LEU A 1 259 ? -8.689  -19.277 23.795  1.00 18.08  ? 484  LEU A C   1 
ATOM   2061 O O   . LEU A 1 259 ? -8.833  -18.108 24.155  1.00 15.87  ? 484  LEU A O   1 
ATOM   2062 C CB  . LEU A 1 259 ? -7.111  -18.740 21.866  1.00 15.55  ? 484  LEU A CB  1 
ATOM   2063 C CG  . LEU A 1 259 ? -5.914  -18.528 22.791  1.00 14.33  ? 484  LEU A CG  1 
ATOM   2064 C CD1 . LEU A 1 259 ? -5.259  -19.866 23.172  1.00 15.96  ? 484  LEU A CD1 1 
ATOM   2065 C CD2 . LEU A 1 259 ? -4.893  -17.594 22.126  1.00 13.92  ? 484  LEU A CD2 1 
ATOM   2066 N N   . TYR A 1 260 ? -8.952  -20.310 24.594  1.00 15.62  ? 485  TYR A N   1 
ATOM   2067 C CA  . TYR A 1 260 ? -9.413  -20.088 25.958  1.00 15.94  ? 485  TYR A CA  1 
ATOM   2068 C C   . TYR A 1 260 ? -8.301  -19.470 26.795  1.00 14.61  ? 485  TYR A C   1 
ATOM   2069 O O   . TYR A 1 260 ? -7.113  -19.693 26.554  1.00 16.46  ? 485  TYR A O   1 
ATOM   2070 C CB  . TYR A 1 260 ? -9.882  -21.398 26.591  1.00 15.16  ? 485  TYR A CB  1 
ATOM   2071 C CG  . TYR A 1 260 ? -11.238 -21.865 26.107  1.00 17.26  ? 485  TYR A CG  1 
ATOM   2072 C CD1 . TYR A 1 260 ? -12.397 -21.225 26.524  1.00 19.08  ? 485  TYR A CD1 1 
ATOM   2073 C CD2 . TYR A 1 260 ? -11.360 -22.958 25.253  1.00 17.13  ? 485  TYR A CD2 1 
ATOM   2074 C CE1 . TYR A 1 260 ? -13.652 -21.647 26.093  1.00 21.58  ? 485  TYR A CE1 1 
ATOM   2075 C CE2 . TYR A 1 260 ? -12.616 -23.395 24.818  1.00 16.82  ? 485  TYR A CE2 1 
ATOM   2076 C CZ  . TYR A 1 260 ? -13.748 -22.733 25.242  1.00 19.19  ? 485  TYR A CZ  1 
ATOM   2077 O OH  . TYR A 1 260 ? -14.992 -23.156 24.824  1.00 21.32  ? 485  TYR A OH  1 
ATOM   2078 N N   . ARG A 1 261 ? -8.691  -18.672 27.783  1.00 15.70  ? 486  ARG A N   1 
ATOM   2079 C CA  . ARG A 1 261 ? -7.674  -17.938 28.522  1.00 18.53  ? 486  ARG A CA  1 
ATOM   2080 C C   . ARG A 1 261 ? -6.739  -18.851 29.305  1.00 14.97  ? 486  ARG A C   1 
ATOM   2081 O O   . ARG A 1 261 ? -5.635  -18.416 29.652  1.00 17.34  ? 486  ARG A O   1 
ATOM   2082 C CB  . ARG A 1 261 ? -8.315  -16.916 29.448  1.00 22.23  ? 486  ARG A CB  1 
ATOM   2083 C CG  . ARG A 1 261 ? -9.149  -17.512 30.536  1.00 20.63  ? 486  ARG A CG  1 
ATOM   2084 C CD  . ARG A 1 261 ? -9.695  -16.419 31.444  1.00 44.16  ? 486  ARG A CD  1 
ATOM   2085 N NE  . ARG A 1 261 ? -8.641  -15.731 32.184  1.00 35.89  ? 486  ARG A NE  1 
ATOM   2086 C CZ  . ARG A 1 261 ? -8.844  -14.665 32.949  1.00 51.75  ? 486  ARG A CZ  1 
ATOM   2087 N NH1 . ARG A 1 261 ? -10.043 -14.121 33.067  1.00 36.25  ? 486  ARG A NH1 1 
ATOM   2088 N NH2 . ARG A 1 261 ? -7.817  -14.129 33.611  1.00 26.22  ? 486  ARG A NH2 1 
ATOM   2089 N N   . SER A 1 262 ? -7.124  -20.099 29.569  1.00 14.14  ? 487  SER A N   1 
ATOM   2090 C CA  . SER A 1 262 ? -6.221  -21.008 30.261  1.00 16.40  ? 487  SER A CA  1 
ATOM   2091 C C   . SER A 1 262 ? -5.180  -21.619 29.331  1.00 16.71  ? 487  SER A C   1 
ATOM   2092 O O   . SER A 1 262 ? -4.323  -22.378 29.806  1.00 16.93  ? 487  SER A O   1 
ATOM   2093 C CB  . SER A 1 262 ? -7.019  -22.109 30.975  1.00 19.36  ? 487  SER A CB  1 
ATOM   2094 O OG  . SER A 1 262 ? -7.629  -23.003 30.063  1.00 20.44  ? 487  SER A OG  1 
ATOM   2095 N N   . GLY A 1 263 ? -5.235  -21.313 28.033  1.00 16.88  ? 488  GLY A N   1 
ATOM   2096 C CA  . GLY A 1 263 ? -4.168  -21.648 27.106  1.00 14.78  ? 488  GLY A CA  1 
ATOM   2097 C C   . GLY A 1 263 ? -4.383  -22.853 26.206  1.00 16.14  ? 488  GLY A C   1 
ATOM   2098 O O   . GLY A 1 263 ? -3.516  -23.729 26.146  1.00 15.35  ? 488  GLY A O   1 
ATOM   2099 N N   . PHE A 1 264 ? -5.513  -22.923 25.503  1.00 14.33  ? 489  PHE A N   1 
ATOM   2100 C CA  . PHE A 1 264 ? -5.662  -23.928 24.459  1.00 16.48  ? 489  PHE A CA  1 
ATOM   2101 C C   . PHE A 1 264 ? -6.718  -23.454 23.469  1.00 14.50  ? 489  PHE A C   1 
ATOM   2102 O O   . PHE A 1 264 ? -7.509  -22.549 23.758  1.00 15.86  ? 489  PHE A O   1 
ATOM   2103 C CB  . PHE A 1 264 ? -5.999  -25.318 25.038  1.00 13.37  ? 489  PHE A CB  1 
ATOM   2104 C CG  . PHE A 1 264 ? -7.347  -25.419 25.701  1.00 13.72  ? 489  PHE A CG  1 
ATOM   2105 C CD1 . PHE A 1 264 ? -7.519  -25.055 27.029  1.00 16.52  ? 489  PHE A CD1 1 
ATOM   2106 C CD2 . PHE A 1 264 ? -8.438  -25.922 25.003  1.00 16.93  ? 489  PHE A CD2 1 
ATOM   2107 C CE1 . PHE A 1 264 ? -8.769  -25.173 27.649  1.00 20.73  ? 489  PHE A CE1 1 
ATOM   2108 C CE2 . PHE A 1 264 ? -9.682  -26.041 25.606  1.00 17.25  ? 489  PHE A CE2 1 
ATOM   2109 C CZ  . PHE A 1 264 ? -9.853  -25.662 26.935  1.00 21.93  ? 489  PHE A CZ  1 
ATOM   2110 N N   . VAL A 1 265 ? -6.708  -24.075 22.290  1.00 16.11  ? 490  VAL A N   1 
ATOM   2111 C CA  . VAL A 1 265 ? -7.542  -23.673 21.160  1.00 13.85  ? 490  VAL A CA  1 
ATOM   2112 C C   . VAL A 1 265 ? -8.534  -24.782 20.834  1.00 16.27  ? 490  VAL A C   1 
ATOM   2113 O O   . VAL A 1 265 ? -8.204  -25.969 20.911  1.00 16.98  ? 490  VAL A O   1 
ATOM   2114 C CB  . VAL A 1 265 ? -6.674  -23.347 19.924  1.00 14.57  ? 490  VAL A CB  1 
ATOM   2115 C CG1 . VAL A 1 265 ? -7.538  -22.799 18.805  1.00 18.59  ? 490  VAL A CG1 1 
ATOM   2116 C CG2 . VAL A 1 265 ? -5.553  -22.368 20.299  1.00 16.61  ? 490  VAL A CG2 1 
ATOM   2117 N N   . VAL A 1 266 ? -9.746  -24.395 20.442  1.00 16.17  ? 491  VAL A N   1 
ATOM   2118 C CA  . VAL A 1 266 ? -10.765 -25.355 20.041  1.00 15.60  ? 491  VAL A CA  1 
ATOM   2119 C C   . VAL A 1 266 ? -11.405 -24.899 18.737  1.00 17.52  ? 491  VAL A C   1 
ATOM   2120 O O   . VAL A 1 266 ? -11.450 -23.705 18.426  1.00 18.70  ? 491  VAL A O   1 
ATOM   2121 C CB  . VAL A 1 266 ? -11.853 -25.553 21.124  1.00 17.29  ? 491  VAL A CB  1 
ATOM   2122 C CG1 . VAL A 1 266 ? -11.223 -26.070 22.407  1.00 17.35  ? 491  VAL A CG1 1 
ATOM   2123 C CG2 . VAL A 1 266 ? -12.616 -24.252 21.364  1.00 18.58  ? 491  VAL A CG2 1 
ATOM   2124 N N   . VAL A 1 267 ? -11.925 -25.867 17.986  1.00 18.15  ? 492  VAL A N   1 
ATOM   2125 C CA  . VAL A 1 267 ? -12.762 -25.616 16.820  1.00 18.69  ? 492  VAL A CA  1 
ATOM   2126 C C   . VAL A 1 267 ? -14.081 -26.347 17.033  1.00 21.11  ? 492  VAL A C   1 
ATOM   2127 O O   . VAL A 1 267 ? -14.193 -27.234 17.876  1.00 20.55  ? 492  VAL A O   1 
ATOM   2128 C CB  . VAL A 1 267 ? -12.099 -26.073 15.505  1.00 18.32  ? 492  VAL A CB  1 
ATOM   2129 C CG1 . VAL A 1 267 ? -10.903 -25.192 15.168  1.00 17.38  ? 492  VAL A CG1 1 
ATOM   2130 C CG2 . VAL A 1 267 ? -11.683 -27.532 15.610  1.00 21.11  ? 492  VAL A CG2 1 
ATOM   2131 N N   . ASN A 1 268 ? -15.076 -25.982 16.230  1.00 19.71  ? 493  ASN A N   1 
ATOM   2132 C CA  . ASN A 1 268 ? -16.417 -26.535 16.334  1.00 21.90  ? 493  ASN A CA  1 
ATOM   2133 C C   . ASN A 1 268 ? -16.765 -27.299 15.064  1.00 20.77  ? 493  ASN A C   1 
ATOM   2134 O O   . ASN A 1 268 ? -16.227 -27.021 13.989  1.00 26.91  ? 493  ASN A O   1 
ATOM   2135 C CB  . ASN A 1 268 ? -17.437 -25.414 16.571  1.00 20.16  ? 493  ASN A CB  1 
ATOM   2136 C CG  . ASN A 1 268 ? -18.836 -25.939 16.857  1.00 26.78  ? 493  ASN A CG  1 
ATOM   2137 O OD1 . ASN A 1 268 ? -19.011 -27.053 17.352  1.00 33.05  ? 493  ASN A OD1 1 
ATOM   2138 N ND2 . ASN A 1 268 ? -19.832 -25.129 16.557  1.00 28.64  ? 493  ASN A ND2 1 
ATOM   2139 N N   . GLY A 1 269 ? -17.669 -28.267 15.195  1.00 26.84  ? 494  GLY A N   1 
ATOM   2140 C CA  . GLY A 1 269 ? -18.201 -28.948 14.030  1.00 29.03  ? 494  GLY A CA  1 
ATOM   2141 C C   . GLY A 1 269 ? -17.310 -30.018 13.449  1.00 35.69  ? 494  GLY A C   1 
ATOM   2142 O O   . GLY A 1 269 ? -17.438 -30.339 12.263  1.00 29.40  ? 494  GLY A O   1 
ATOM   2143 N N   . VAL A 1 270 ? -16.410 -30.584 14.244  1.00 26.57  ? 495  VAL A N   1 
ATOM   2144 C CA  . VAL A 1 270 ? -15.518 -31.642 13.793  1.00 23.41  ? 495  VAL A CA  1 
ATOM   2145 C C   . VAL A 1 270 ? -16.065 -32.968 14.298  1.00 27.85  ? 495  VAL A C   1 
ATOM   2146 O O   . VAL A 1 270 ? -16.181 -33.177 15.511  1.00 30.38  ? 495  VAL A O   1 
ATOM   2147 C CB  . VAL A 1 270 ? -14.085 -31.400 14.287  1.00 24.87  ? 495  VAL A CB  1 
ATOM   2148 C CG1 . VAL A 1 270 ? -13.228 -32.620 14.037  1.00 28.88  ? 495  VAL A CG1 1 
ATOM   2149 C CG2 . VAL A 1 270 ? -13.505 -30.175 13.592  1.00 29.54  ? 495  VAL A CG2 1 
ATOM   2150 N N   . ASN A 1 271 ? -16.422 -33.860 13.369  1.00 31.64  ? 496  ASN A N   1 
ATOM   2151 C CA  . ASN A 1 271 ? -16.961 -35.167 13.718  1.00 35.10  ? 496  ASN A CA  1 
ATOM   2152 C C   . ASN A 1 271 ? -15.988 -36.309 13.479  1.00 41.43  ? 496  ASN A C   1 
ATOM   2153 O O   . ASN A 1 271 ? -16.156 -37.376 14.076  1.00 36.01  ? 496  ASN A O   1 
ATOM   2154 C CB  . ASN A 1 271 ? -18.254 -35.445 12.932  1.00 39.37  ? 496  ASN A CB  1 
ATOM   2155 C CG  . ASN A 1 271 ? -19.308 -34.371 13.147  1.00 53.14  ? 496  ASN A CG  1 
ATOM   2156 O OD1 . ASN A 1 271 ? -19.761 -33.730 12.198  1.00 56.80  ? 496  ASN A OD1 1 
ATOM   2157 N ND2 . ASN A 1 271 ? -19.696 -34.165 14.401  1.00 46.75  ? 496  ASN A ND2 1 
ATOM   2158 N N   . VAL A 1 272 ? -14.984 -36.113 12.623  1.00 31.48  ? 497  VAL A N   1 
ATOM   2159 C CA  . VAL A 1 272 ? -13.934 -37.091 12.380  1.00 33.11  ? 497  VAL A CA  1 
ATOM   2160 C C   . VAL A 1 272 ? -12.609 -36.350 12.415  1.00 25.61  ? 497  VAL A C   1 
ATOM   2161 O O   . VAL A 1 272 ? -12.564 -35.121 12.332  1.00 28.65  ? 497  VAL A O   1 
ATOM   2162 C CB  . VAL A 1 272 ? -14.106 -37.817 11.029  1.00 29.77  ? 497  VAL A CB  1 
ATOM   2163 C CG1 . VAL A 1 272 ? -15.424 -38.589 10.997  1.00 35.77  ? 497  VAL A CG1 1 
ATOM   2164 C CG2 . VAL A 1 272 ? -14.039 -36.810 9.888   1.00 29.70  ? 497  VAL A CG2 1 
ATOM   2165 N N   . ARG A 1 273 ? -11.522 -37.110 12.534  1.00 24.54  ? 498  ARG A N   1 
ATOM   2166 C CA  . ARG A 1 273 ? -10.198 -36.501 12.563  1.00 22.74  ? 498  ARG A CA  1 
ATOM   2167 C C   . ARG A 1 273 ? -9.978  -35.673 11.306  1.00 32.34  ? 498  ARG A C   1 
ATOM   2168 O O   . ARG A 1 273 ? -10.131 -36.169 10.187  1.00 27.94  ? 498  ARG A O   1 
ATOM   2169 C CB  . ARG A 1 273 ? -9.114  -37.571 12.689  1.00 24.86  ? 498  ARG A CB  1 
ATOM   2170 C CG  . ARG A 1 273 ? -7.721  -37.003 12.954  1.00 25.83  ? 498  ARG A CG  1 
ATOM   2171 C CD  . ARG A 1 273 ? -6.691  -38.126 13.024  1.00 24.94  ? 498  ARG A CD  1 
ATOM   2172 N NE  . ARG A 1 273 ? -5.374  -37.682 13.474  1.00 25.10  ? 498  ARG A NE  1 
ATOM   2173 C CZ  . ARG A 1 273 ? -4.486  -37.063 12.709  1.00 27.21  ? 498  ARG A CZ  1 
ATOM   2174 N NH1 . ARG A 1 273 ? -4.761  -36.731 11.458  1.00 34.72  ? 498  ARG A NH1 1 
ATOM   2175 N NH2 . ARG A 1 273 ? -3.288  -36.769 13.213  1.00 27.86  ? 498  ARG A NH2 1 
ATOM   2176 N N   . THR A 1 274 ? -9.629  -34.402 11.497  1.00 23.95  ? 499  THR A N   1 
ATOM   2177 C CA  . THR A 1 274 ? -9.608  -33.418 10.421  1.00 22.30  ? 499  THR A CA  1 
ATOM   2178 C C   . THR A 1 274 ? -8.290  -32.658 10.462  1.00 24.80  ? 499  THR A C   1 
ATOM   2179 O O   . THR A 1 274 ? -7.951  -32.063 11.490  1.00 20.75  ? 499  THR A O   1 
ATOM   2180 C CB  . THR A 1 274 ? -10.785 -32.446 10.552  1.00 24.57  ? 499  THR A CB  1 
ATOM   2181 O OG1 . THR A 1 274 ? -12.024 -33.169 10.469  1.00 26.95  ? 499  THR A OG1 1 
ATOM   2182 C CG2 . THR A 1 274 ? -10.736 -31.389 9.460   1.00 27.16  ? 499  THR A CG2 1 
ATOM   2183 N N   . GLU A 1 275 ? -7.555  -32.672 9.352   1.00 25.85  ? 500  GLU A N   1 
ATOM   2184 C CA  . GLU A 1 275 ? -6.301  -31.937 9.236   1.00 31.90  ? 500  GLU A CA  1 
ATOM   2185 C C   . GLU A 1 275 ? -6.529  -30.618 8.508   1.00 22.25  ? 500  GLU A C   1 
ATOM   2186 O O   . GLU A 1 275 ? -7.409  -30.511 7.652   1.00 23.02  ? 500  GLU A O   1 
ATOM   2187 C CB  . GLU A 1 275 ? -5.243  -32.759 8.494   1.00 25.42  ? 500  GLU A CB  1 
ATOM   2188 C CG  . GLU A 1 275 ? -4.781  -33.993 9.244   1.00 39.50  ? 500  GLU A CG  1 
ATOM   2189 C CD  . GLU A 1 275 ? -3.591  -34.659 8.591   1.00 68.82  ? 500  GLU A CD  1 
ATOM   2190 O OE1 . GLU A 1 275 ? -3.214  -34.247 7.472   1.00 70.12  ? 500  GLU A OE1 1 
ATOM   2191 O OE2 . GLU A 1 275 ? -3.030  -35.593 9.199   1.00 75.86  ? 500  GLU A OE2 1 
ATOM   2192 N N   . PHE A 1 276 ? -5.728  -29.612 8.854   1.00 22.06  ? 501  PHE A N   1 
ATOM   2193 C CA  . PHE A 1 276 ? -5.874  -28.270 8.318   1.00 22.15  ? 501  PHE A CA  1 
ATOM   2194 C C   . PHE A 1 276 ? -4.583  -27.811 7.649   1.00 22.23  ? 501  PHE A C   1 
ATOM   2195 O O   . PHE A 1 276 ? -3.498  -28.321 7.955   1.00 19.84  ? 501  PHE A O   1 
ATOM   2196 C CB  . PHE A 1 276 ? -6.271  -27.288 9.433   1.00 23.02  ? 501  PHE A CB  1 
ATOM   2197 C CG  . PHE A 1 276 ? -7.577  -27.637 10.107  1.00 22.72  ? 501  PHE A CG  1 
ATOM   2198 C CD1 . PHE A 1 276 ? -8.787  -27.339 9.499   1.00 21.43  ? 501  PHE A CD1 1 
ATOM   2199 C CD2 . PHE A 1 276 ? -7.594  -28.268 11.342  1.00 18.91  ? 501  PHE A CD2 1 
ATOM   2200 C CE1 . PHE A 1 276 ? -9.985  -27.656 10.102  1.00 23.18  ? 501  PHE A CE1 1 
ATOM   2201 C CE2 . PHE A 1 276 ? -8.804  -28.593 11.953  1.00 18.89  ? 501  PHE A CE2 1 
ATOM   2202 C CZ  . PHE A 1 276 ? -9.994  -28.283 11.332  1.00 19.90  ? 501  PHE A CZ  1 
ATOM   2203 N N   . PRO A 1 277 ? -4.664  -26.858 6.720   1.00 20.33  ? 502  PRO A N   1 
ATOM   2204 C CA  . PRO A 1 277 ? -3.446  -26.364 6.064   1.00 18.18  ? 502  PRO A CA  1 
ATOM   2205 C C   . PRO A 1 277 ? -2.490  -25.730 7.056   1.00 20.50  ? 502  PRO A C   1 
ATOM   2206 O O   . PRO A 1 277 ? -2.901  -25.110 8.038   1.00 19.62  ? 502  PRO A O   1 
ATOM   2207 C CB  . PRO A 1 277 ? -3.974  -25.321 5.072   1.00 20.33  ? 502  PRO A CB  1 
ATOM   2208 C CG  . PRO A 1 277 ? -5.369  -25.739 4.799   1.00 23.49  ? 502  PRO A CG  1 
ATOM   2209 C CD  . PRO A 1 277 ? -5.884  -26.321 6.090   1.00 21.49  ? 502  PRO A CD  1 
ATOM   2210 N N   . MET A 1 278 ? -1.194  -25.871 6.770   1.00 19.14  ? 503  MET A N   1 
ATOM   2211 C CA  . MET A 1 278 ? -0.159  -25.376 7.664   1.00 19.35  ? 503  MET A CA  1 
ATOM   2212 C C   . MET A 1 278 ? 0.323   -23.975 7.314   1.00 16.90  ? 503  MET A C   1 
ATOM   2213 O O   . MET A 1 278 ? 1.083   -23.389 8.094   1.00 17.79  ? 503  MET A O   1 
ATOM   2214 C CB  . MET A 1 278 ? 1.038   -26.338 7.662   1.00 19.20  ? 503  MET A CB  1 
ATOM   2215 C CG  . MET A 1 278 ? 0.743   -27.683 8.304   1.00 20.79  ? 503  MET A CG  1 
ATOM   2216 S SD  . MET A 1 278 ? 0.621   -27.546 10.103  1.00 18.96  ? 503  MET A SD  1 
ATOM   2217 C CE  . MET A 1 278 ? 2.309   -27.089 10.504  1.00 17.18  ? 503  MET A CE  1 
ATOM   2218 N N   A SER A 1 279 ? -0.086  -23.416 6.175   0.63 19.36  ? 504  SER A N   1 
ATOM   2219 N N   B SER A 1 279 ? -0.099  -23.430 6.171   0.37 19.41  ? 504  SER A N   1 
ATOM   2220 C CA  A SER A 1 279 ? 0.441   -22.133 5.727   0.63 22.86  ? 504  SER A CA  1 
ATOM   2221 C CA  B SER A 1 279 ? 0.380   -22.144 5.679   0.37 22.92  ? 504  SER A CA  1 
ATOM   2222 C C   A SER A 1 279 ? -0.424  -20.950 6.153   0.63 23.32  ? 504  SER A C   1 
ATOM   2223 C C   B SER A 1 279 ? -0.546  -20.994 6.052   0.37 23.68  ? 504  SER A C   1 
ATOM   2224 O O   A SER A 1 279 ? -0.293  -19.861 5.583   0.63 30.02  ? 504  SER A O   1 
ATOM   2225 O O   B SER A 1 279 ? -0.590  -19.978 5.350   0.37 27.84  ? 504  SER A O   1 
ATOM   2226 C CB  A SER A 1 279 ? 0.611   -22.140 4.208   0.63 24.94  ? 504  SER A CB  1 
ATOM   2227 C CB  B SER A 1 279 ? 0.568   -22.200 4.164   0.37 24.85  ? 504  SER A CB  1 
ATOM   2228 O OG  A SER A 1 279 ? -0.615  -22.443 3.580   0.63 24.06  ? 504  SER A OG  1 
ATOM   2229 O OG  B SER A 1 279 ? 1.440   -23.254 3.807   0.37 21.80  ? 504  SER A OG  1 
ATOM   2230 N N   . GLY A 1 280 ? -1.302  -21.133 7.140   1.00 19.13  ? 505  GLY A N   1 
ATOM   2231 C CA  . GLY A 1 280 ? -2.157  -20.069 7.608   1.00 18.44  ? 505  GLY A CA  1 
ATOM   2232 C C   . GLY A 1 280 ? -1.560  -19.385 8.823   1.00 17.15  ? 505  GLY A C   1 
ATOM   2233 O O   . GLY A 1 280 ? -0.624  -19.878 9.439   1.00 19.12  ? 505  GLY A O   1 
ATOM   2234 N N   . VAL A 1 281 ? -2.138  -18.234 9.160   1.00 15.53  ? 506  VAL A N   1 
ATOM   2235 C CA  . VAL A 1 281 ? -1.773  -17.469 10.346  1.00 17.15  ? 506  VAL A CA  1 
ATOM   2236 C C   . VAL A 1 281 ? -3.018  -17.267 11.199  1.00 16.12  ? 506  VAL A C   1 
ATOM   2237 O O   . VAL A 1 281 ? -4.100  -16.987 10.673  1.00 22.07  ? 506  VAL A O   1 
ATOM   2238 C CB  . VAL A 1 281 ? -1.152  -16.106 9.974   1.00 20.44  ? 506  VAL A CB  1 
ATOM   2239 C CG1 . VAL A 1 281 ? -0.837  -15.288 11.234  1.00 18.82  ? 506  VAL A CG1 1 
ATOM   2240 C CG2 . VAL A 1 281 ? 0.094   -16.307 9.122   1.00 17.19  ? 506  VAL A CG2 1 
ATOM   2241 N N   . PHE A 1 282 ? -2.861  -17.414 12.518  1.00 17.23  ? 507  PHE A N   1 
ATOM   2242 C CA  . PHE A 1 282 ? -3.924  -17.099 13.464  1.00 17.47  ? 507  PHE A CA  1 
ATOM   2243 C C   . PHE A 1 282 ? -3.918  -15.609 13.802  1.00 19.87  ? 507  PHE A C   1 
ATOM   2244 O O   . PHE A 1 282 ? -2.880  -15.057 14.186  1.00 21.84  ? 507  PHE A O   1 
ATOM   2245 C CB  . PHE A 1 282 ? -3.741  -17.911 14.748  1.00 15.73  ? 507  PHE A CB  1 
ATOM   2246 C CG  . PHE A 1 282 ? -3.937  -19.398 14.583  1.00 15.09  ? 507  PHE A CG  1 
ATOM   2247 C CD1 . PHE A 1 282 ? -2.878  -20.224 14.233  1.00 17.05  ? 507  PHE A CD1 1 
ATOM   2248 C CD2 . PHE A 1 282 ? -5.185  -19.970 14.824  1.00 17.86  ? 507  PHE A CD2 1 
ATOM   2249 C CE1 . PHE A 1 282 ? -3.067  -21.601 14.107  1.00 17.80  ? 507  PHE A CE1 1 
ATOM   2250 C CE2 . PHE A 1 282 ? -5.385  -21.336 14.699  1.00 15.68  ? 507  PHE A CE2 1 
ATOM   2251 C CZ  . PHE A 1 282 ? -4.328  -22.156 14.343  1.00 14.78  ? 507  PHE A CZ  1 
ATOM   2252 N N   A GLU A 1 283 ? -5.083  -14.971 13.694  0.51 18.74  ? 508  GLU A N   1 
ATOM   2253 N N   B GLU A 1 283 ? -5.083  -14.971 13.694  0.49 18.75  ? 508  GLU A N   1 
ATOM   2254 C CA  A GLU A 1 283 ? -5.239  -13.543 13.945  0.51 18.41  ? 508  GLU A CA  1 
ATOM   2255 C CA  B GLU A 1 283 ? -5.238  -13.543 13.945  0.49 18.42  ? 508  GLU A CA  1 
ATOM   2256 C C   A GLU A 1 283 ? -6.327  -13.318 14.987  0.51 25.49  ? 508  GLU A C   1 
ATOM   2257 C C   B GLU A 1 283 ? -6.326  -13.318 14.988  0.49 25.48  ? 508  GLU A C   1 
ATOM   2258 O O   A GLU A 1 283 ? -7.403  -13.918 14.906  0.51 21.02  ? 508  GLU A O   1 
ATOM   2259 O O   B GLU A 1 283 ? -7.402  -13.919 14.907  0.49 21.02  ? 508  GLU A O   1 
ATOM   2260 C CB  A GLU A 1 283 ? -5.587  -12.794 12.652  0.51 23.09  ? 508  GLU A CB  1 
ATOM   2261 C CB  B GLU A 1 283 ? -5.586  -12.793 12.653  0.49 23.09  ? 508  GLU A CB  1 
ATOM   2262 N N   . PHE A 1 284 ? -6.046  -12.450 15.957  1.00 20.56  ? 509  PHE A N   1 
ATOM   2263 C CA  . PHE A 1 284 ? -7.035  -12.105 16.971  1.00 17.80  ? 509  PHE A CA  1 
ATOM   2264 C C   . PHE A 1 284 ? -8.186  -11.314 16.360  1.00 20.62  ? 509  PHE A C   1 
ATOM   2265 O O   . PHE A 1 284 ? -7.980  -10.438 15.518  1.00 24.25  ? 509  PHE A O   1 
ATOM   2266 C CB  . PHE A 1 284 ? -6.371  -11.289 18.082  1.00 23.30  ? 509  PHE A CB  1 
ATOM   2267 C CG  . PHE A 1 284 ? -7.319  -10.782 19.132  1.00 23.60  ? 509  PHE A CG  1 
ATOM   2268 C CD1 . PHE A 1 284 ? -8.001  -11.663 19.968  1.00 19.35  ? 509  PHE A CD1 1 
ATOM   2269 C CD2 . PHE A 1 284 ? -7.503  -9.419  19.311  1.00 27.70  ? 509  PHE A CD2 1 
ATOM   2270 C CE1 . PHE A 1 284 ? -8.856  -11.185 20.940  1.00 23.08  ? 509  PHE A CE1 1 
ATOM   2271 C CE2 . PHE A 1 284 ? -8.363  -8.936  20.288  1.00 26.01  ? 509  PHE A CE2 1 
ATOM   2272 C CZ  . PHE A 1 284 ? -9.035  -9.820  21.100  1.00 24.84  ? 509  PHE A CZ  1 
ATOM   2273 N N   . VAL A 1 285 ? -9.404  -11.628 16.797  1.00 17.75  ? 510  VAL A N   1 
ATOM   2274 C CA  . VAL A 1 285 ? -10.607 -10.889 16.420  1.00 20.97  ? 510  VAL A CA  1 
ATOM   2275 C C   . VAL A 1 285 ? -11.152 -10.100 17.605  1.00 27.42  ? 510  VAL A C   1 
ATOM   2276 O O   . VAL A 1 285 ? -11.165 -8.867  17.590  1.00 27.78  ? 510  VAL A O   1 
ATOM   2277 C CB  . VAL A 1 285 ? -11.683 -11.835 15.841  1.00 25.28  ? 510  VAL A CB  1 
ATOM   2278 C CG1 . VAL A 1 285 ? -12.930 -11.046 15.449  1.00 24.62  ? 510  VAL A CG1 1 
ATOM   2279 C CG2 . VAL A 1 285 ? -11.123 -12.630 14.667  1.00 21.01  ? 510  VAL A CG2 1 
ATOM   2280 N N   . SER A 1 286 ? -11.596 -10.796 18.650  1.00 22.71  ? 511  SER A N   1 
ATOM   2281 C CA  . SER A 1 286 ? -12.210 -10.149 19.803  1.00 24.88  ? 511  SER A CA  1 
ATOM   2282 C C   . SER A 1 286 ? -12.296 -11.152 20.943  1.00 23.53  ? 511  SER A C   1 
ATOM   2283 O O   . SER A 1 286 ? -12.030 -12.342 20.771  1.00 22.30  ? 511  SER A O   1 
ATOM   2284 C CB  . SER A 1 286 ? -13.598 -9.614  19.455  1.00 26.28  ? 511  SER A CB  1 
ATOM   2285 O OG  . SER A 1 286 ? -14.428 -10.684 19.050  1.00 28.65  ? 511  SER A OG  1 
ATOM   2286 N N   . TRP A 1 287 ? -12.686 -10.650 22.113  1.00 19.95  ? 512  TRP A N   1 
ATOM   2287 C CA  . TRP A 1 287 ? -12.919 -11.469 23.294  1.00 24.04  ? 512  TRP A CA  1 
ATOM   2288 C C   . TRP A 1 287 ? -14.366 -11.947 23.334  1.00 19.81  ? 512  TRP A C   1 
ATOM   2289 O O   . TRP A 1 287 ? -15.293 -11.174 23.077  1.00 25.00  ? 512  TRP A O   1 
ATOM   2290 C CB  . TRP A 1 287 ? -12.601 -10.670 24.558  1.00 20.17  ? 512  TRP A CB  1 
ATOM   2291 C CG  . TRP A 1 287 ? -11.142 -10.314 24.697  1.00 23.54  ? 512  TRP A CG  1 
ATOM   2292 C CD1 . TRP A 1 287 ? -10.554 -9.111  24.411  1.00 25.59  ? 512  TRP A CD1 1 
ATOM   2293 C CD2 . TRP A 1 287 ? -10.101 -11.167 25.168  1.00 21.55  ? 512  TRP A CD2 1 
ATOM   2294 N NE1 . TRP A 1 287 ? -9.208  -9.169  24.671  1.00 23.12  ? 512  TRP A NE1 1 
ATOM   2295 C CE2 . TRP A 1 287 ? -8.901  -10.422 25.133  1.00 19.70  ? 512  TRP A CE2 1 
ATOM   2296 C CE3 . TRP A 1 287 ? -10.060 -12.495 25.609  1.00 18.83  ? 512  TRP A CE3 1 
ATOM   2297 C CZ2 . TRP A 1 287 ? -7.683  -10.955 25.529  1.00 19.72  ? 512  TRP A CZ2 1 
ATOM   2298 C CZ3 . TRP A 1 287 ? -8.844  -13.029 25.999  1.00 19.28  ? 512  TRP A CZ3 1 
ATOM   2299 C CH2 . TRP A 1 287 ? -7.670  -12.260 25.956  1.00 24.64  ? 512  TRP A CH2 1 
ATOM   2300 N N   . VAL A 1 288 ? -14.560 -13.221 23.669  1.00 21.54  ? 513  VAL A N   1 
ATOM   2301 C CA  . VAL A 1 288 ? -15.901 -13.814 23.699  1.00 21.89  ? 513  VAL A CA  1 
ATOM   2302 C C   . VAL A 1 288 ? -16.060 -14.651 24.962  1.00 26.92  ? 513  VAL A C   1 
ATOM   2303 O O   . VAL A 1 288 ? -15.077 -15.093 25.565  1.00 23.20  ? 513  VAL A O   1 
ATOM   2304 C CB  . VAL A 1 288 ? -16.178 -14.684 22.452  1.00 25.18  ? 513  VAL A CB  1 
ATOM   2305 C CG1 . VAL A 1 288 ? -16.212 -13.831 21.201  1.00 22.77  ? 513  VAL A CG1 1 
ATOM   2306 C CG2 . VAL A 1 288 ? -15.138 -15.788 22.322  1.00 22.12  ? 513  VAL A CG2 1 
ATOM   2307 N N   . PRO A 1 289 ? -17.302 -14.877 25.387  1.00 24.27  ? 514  PRO A N   1 
ATOM   2308 C CA  . PRO A 1 289 ? -17.540 -15.698 26.580  1.00 24.61  ? 514  PRO A CA  1 
ATOM   2309 C C   . PRO A 1 289 ? -17.349 -17.184 26.299  1.00 22.16  ? 514  PRO A C   1 
ATOM   2310 O O   . PRO A 1 289 ? -17.239 -17.621 25.152  1.00 26.10  ? 514  PRO A O   1 
ATOM   2311 C CB  . PRO A 1 289 ? -18.999 -15.381 26.933  1.00 25.77  ? 514  PRO A CB  1 
ATOM   2312 C CG  . PRO A 1 289 ? -19.610 -14.972 25.643  1.00 26.43  ? 514  PRO A CG  1 
ATOM   2313 C CD  . PRO A 1 289 ? -18.537 -14.236 24.903  1.00 22.23  ? 514  PRO A CD  1 
ATOM   2314 N N   . ASN A 1 290 ? -17.293 -17.961 27.393  1.00 22.40  ? 515  ASN A N   1 
ATOM   2315 C CA  . ASN A 1 290 ? -17.057 -19.401 27.298  1.00 23.47  ? 515  ASN A CA  1 
ATOM   2316 C C   . ASN A 1 290 ? -18.071 -20.085 26.391  1.00 23.86  ? 515  ASN A C   1 
ATOM   2317 O O   . ASN A 1 290 ? -17.736 -21.057 25.704  1.00 28.14  ? 515  ASN A O   1 
ATOM   2318 C CB  . ASN A 1 290 ? -17.114 -20.048 28.687  1.00 24.95  ? 515  ASN A CB  1 
ATOM   2319 C CG  . ASN A 1 290 ? -15.757 -20.124 29.370  1.00 27.24  ? 515  ASN A CG  1 
ATOM   2320 O OD1 . ASN A 1 290 ? -14.710 -20.049 28.726  1.00 30.68  ? 515  ASN A OD1 1 
ATOM   2321 N ND2 . ASN A 1 290 ? -15.774 -20.297 30.685  1.00 39.95  ? 515  ASN A ND2 1 
ATOM   2322 N N   . PHE A 1 291 ? -19.313 -19.616 26.393  1.00 22.26  ? 516  PHE A N   1 
ATOM   2323 C CA  . PHE A 1 291 ? -20.380 -20.260 25.641  1.00 26.92  ? 516  PHE A CA  1 
ATOM   2324 C C   . PHE A 1 291 ? -20.620 -19.615 24.282  1.00 27.12  ? 516  PHE A C   1 
ATOM   2325 O O   . PHE A 1 291 ? -21.655 -19.878 23.657  1.00 27.28  ? 516  PHE A O   1 
ATOM   2326 C CB  . PHE A 1 291 ? -21.662 -20.279 26.473  1.00 32.33  ? 516  PHE A CB  1 
ATOM   2327 C CG  . PHE A 1 291 ? -21.584 -21.188 27.674  1.00 37.10  ? 516  PHE A CG  1 
ATOM   2328 C CD1 . PHE A 1 291 ? -20.565 -22.124 27.784  1.00 42.04  ? 516  PHE A CD1 1 
ATOM   2329 C CD2 . PHE A 1 291 ? -22.524 -21.110 28.689  1.00 52.10  ? 516  PHE A CD2 1 
ATOM   2330 C CE1 . PHE A 1 291 ? -20.478 -22.962 28.882  1.00 54.02  ? 516  PHE A CE1 1 
ATOM   2331 C CE2 . PHE A 1 291 ? -22.447 -21.947 29.792  1.00 51.41  ? 516  PHE A CE2 1 
ATOM   2332 C CZ  . PHE A 1 291 ? -21.423 -22.875 29.888  1.00 52.19  ? 516  PHE A CZ  1 
ATOM   2333 N N   . PHE A 1 292 ? -19.686 -18.789 23.806  1.00 23.82  ? 517  PHE A N   1 
ATOM   2334 C CA  . PHE A 1 292 ? -19.732 -18.308 22.433  1.00 24.60  ? 517  PHE A CA  1 
ATOM   2335 C C   . PHE A 1 292 ? -19.613 -19.489 21.480  1.00 27.56  ? 517  PHE A C   1 
ATOM   2336 O O   . PHE A 1 292 ? -18.653 -20.265 21.554  1.00 23.88  ? 517  PHE A O   1 
ATOM   2337 C CB  . PHE A 1 292 ? -18.606 -17.305 22.180  1.00 28.55  ? 517  PHE A CB  1 
ATOM   2338 C CG  . PHE A 1 292 ? -18.616 -16.723 20.791  1.00 23.44  ? 517  PHE A CG  1 
ATOM   2339 C CD1 . PHE A 1 292 ? -19.326 -15.569 20.517  1.00 27.92  ? 517  PHE A CD1 1 
ATOM   2340 C CD2 . PHE A 1 292 ? -17.915 -17.333 19.762  1.00 24.11  ? 517  PHE A CD2 1 
ATOM   2341 C CE1 . PHE A 1 292 ? -19.343 -15.035 19.238  1.00 29.55  ? 517  PHE A CE1 1 
ATOM   2342 C CE2 . PHE A 1 292 ? -17.925 -16.805 18.484  1.00 26.11  ? 517  PHE A CE2 1 
ATOM   2343 C CZ  . PHE A 1 292 ? -18.637 -15.656 18.223  1.00 28.79  ? 517  PHE A CZ  1 
ATOM   2344 N N   . GLN A 1 293 ? -20.588 -19.632 20.591  1.00 27.22  ? 518  GLN A N   1 
ATOM   2345 C CA  . GLN A 1 293 ? -20.638 -20.781 19.700  1.00 24.25  ? 518  GLN A CA  1 
ATOM   2346 C C   . GLN A 1 293 ? -19.961 -20.435 18.380  1.00 25.46  ? 518  GLN A C   1 
ATOM   2347 O O   . GLN A 1 293 ? -20.349 -19.473 17.706  1.00 25.95  ? 518  GLN A O   1 
ATOM   2348 C CB  . GLN A 1 293 ? -22.078 -21.224 19.468  1.00 23.47  ? 518  GLN A CB  1 
ATOM   2349 C CG  . GLN A 1 293 ? -22.173 -22.524 18.707  1.00 27.76  ? 518  GLN A CG  1 
ATOM   2350 C CD  . GLN A 1 293 ? -23.611 -22.926 18.492  1.00 31.89  ? 518  GLN A CD  1 
ATOM   2351 O OE1 . GLN A 1 293 ? -24.292 -23.332 19.431  1.00 33.87  ? 518  GLN A OE1 1 
ATOM   2352 N NE2 . GLN A 1 293 ? -24.090 -22.790 17.259  1.00 29.18  ? 518  GLN A NE2 1 
ATOM   2353 N N   . LEU A 1 294 ? -18.954 -21.226 18.017  1.00 23.93  ? 519  LEU A N   1 
ATOM   2354 C CA  . LEU A 1 294 ? -18.176 -21.001 16.810  1.00 21.79  ? 519  LEU A CA  1 
ATOM   2355 C C   . LEU A 1 294 ? -18.912 -21.491 15.575  1.00 26.30  ? 519  LEU A C   1 
ATOM   2356 O O   . LEU A 1 294 ? -19.713 -22.425 15.635  1.00 23.41  ? 519  LEU A O   1 
ATOM   2357 C CB  . LEU A 1 294 ? -16.840 -21.734 16.895  1.00 19.73  ? 519  LEU A CB  1 
ATOM   2358 C CG  . LEU A 1 294 ? -15.815 -21.231 17.897  1.00 19.42  ? 519  LEU A CG  1 
ATOM   2359 C CD1 . LEU A 1 294 ? -14.808 -22.319 18.174  1.00 20.97  ? 519  LEU A CD1 1 
ATOM   2360 C CD2 . LEU A 1 294 ? -15.142 -20.019 17.290  1.00 19.39  ? 519  LEU A CD2 1 
ATOM   2361 N N   . ALA A 1 295 ? -18.604 -20.866 14.442  1.00 24.42  ? 520  ALA A N   1 
ATOM   2362 C CA  . ALA A 1 295 ? -19.016 -21.418 13.163  1.00 25.26  ? 520  ALA A CA  1 
ATOM   2363 C C   . ALA A 1 295 ? -18.303 -22.747 12.931  1.00 24.58  ? 520  ALA A C   1 
ATOM   2364 O O   . ALA A 1 295 ? -17.090 -22.846 13.149  1.00 23.51  ? 520  ALA A O   1 
ATOM   2365 C CB  . ALA A 1 295 ? -18.691 -20.450 12.024  1.00 26.81  ? 520  ALA A CB  1 
ATOM   2366 N N   . PRO A 1 296 ? -19.017 -23.776 12.481  1.00 23.39  ? 521  PRO A N   1 
ATOM   2367 C CA  . PRO A 1 296 ? -18.367 -25.067 12.226  1.00 21.58  ? 521  PRO A CA  1 
ATOM   2368 C C   . PRO A 1 296 ? -17.299 -24.930 11.153  1.00 25.08  ? 521  PRO A C   1 
ATOM   2369 O O   . PRO A 1 296 ? -17.409 -24.103 10.246  1.00 27.76  ? 521  PRO A O   1 
ATOM   2370 C CB  . PRO A 1 296 ? -19.520 -25.963 11.754  1.00 30.47  ? 521  PRO A CB  1 
ATOM   2371 C CG  . PRO A 1 296 ? -20.766 -25.259 12.176  1.00 32.28  ? 521  PRO A CG  1 
ATOM   2372 C CD  . PRO A 1 296 ? -20.447 -23.801 12.129  1.00 29.82  ? 521  PRO A CD  1 
ATOM   2373 N N   . VAL A 1 297 ? -16.250 -25.744 11.272  1.00 25.87  ? 522  VAL A N   1 
ATOM   2374 C CA  . VAL A 1 297 ? -15.164 -25.727 10.297  1.00 21.40  ? 522  VAL A CA  1 
ATOM   2375 C C   . VAL A 1 297 ? -15.688 -26.099 8.918   1.00 33.36  ? 522  VAL A C   1 
ATOM   2376 O O   . VAL A 1 297 ? -15.143 -25.651 7.911   1.00 33.45  ? 522  VAL A O   1 
ATOM   2377 C CB  . VAL A 1 297 ? -14.011 -26.674 10.708  1.00 25.14  ? 522  VAL A CB  1 
ATOM   2378 C CG1 . VAL A 1 297 ? -13.473 -26.295 12.073  1.00 23.71  ? 522  VAL A CG1 1 
ATOM   2379 C CG2 . VAL A 1 297 ? -14.481 -28.117 10.700  1.00 33.15  ? 522  VAL A CG2 1 
ATOM   2380 O OXT . VAL A 1 297 ? -16.664 -26.840 8.789   1.00 31.76  ? 522  VAL A OXT 1 
ATOM   2381 N N   . GLU B 1 1   ? 5.358   0.376   14.614  1.00 48.43  ? 226  GLU B N   1 
ATOM   2382 C CA  . GLU B 1 1   ? 5.568   0.174   16.045  1.00 43.68  ? 226  GLU B CA  1 
ATOM   2383 C C   . GLU B 1 1   ? 6.970   0.621   16.467  1.00 35.86  ? 226  GLU B C   1 
ATOM   2384 O O   . GLU B 1 1   ? 7.946   0.352   15.765  1.00 39.74  ? 226  GLU B O   1 
ATOM   2385 C CB  . GLU B 1 1   ? 5.340   -1.295  16.411  1.00 53.36  ? 226  GLU B CB  1 
ATOM   2386 C CG  . GLU B 1 1   ? 5.803   -1.671  17.815  1.00 51.05  ? 226  GLU B CG  1 
ATOM   2387 C CD  . GLU B 1 1   ? 4.932   -2.734  18.460  1.00 58.04  ? 226  GLU B CD  1 
ATOM   2388 O OE1 . GLU B 1 1   ? 3.765   -2.883  18.041  1.00 71.67  ? 226  GLU B OE1 1 
ATOM   2389 O OE2 . GLU B 1 1   ? 5.415   -3.420  19.388  1.00 45.76  ? 226  GLU B OE2 1 
ATOM   2390 N N   . PRO B 1 2   ? 7.069   1.324   17.597  1.00 40.72  ? 227  PRO B N   1 
ATOM   2391 C CA  . PRO B 1 2   ? 8.387   1.761   18.078  1.00 33.69  ? 227  PRO B CA  1 
ATOM   2392 C C   . PRO B 1 2   ? 9.278   0.577   18.429  1.00 35.32  ? 227  PRO B C   1 
ATOM   2393 O O   . PRO B 1 2   ? 8.810   -0.464  18.898  1.00 22.70  ? 227  PRO B O   1 
ATOM   2394 C CB  . PRO B 1 2   ? 8.055   2.600   19.318  1.00 35.03  ? 227  PRO B CB  1 
ATOM   2395 C CG  . PRO B 1 2   ? 6.673   2.180   19.715  1.00 40.40  ? 227  PRO B CG  1 
ATOM   2396 C CD  . PRO B 1 2   ? 5.975   1.836   18.437  1.00 41.73  ? 227  PRO B CD  1 
ATOM   2397 N N   . PHE B 1 3   ? 10.580  0.748   18.195  1.00 25.08  ? 228  PHE B N   1 
ATOM   2398 C CA  . PHE B 1 3   ? 11.518  -0.353  18.375  1.00 22.04  ? 228  PHE B CA  1 
ATOM   2399 C C   . PHE B 1 3   ? 11.550  -0.802  19.831  1.00 22.50  ? 228  PHE B C   1 
ATOM   2400 O O   . PHE B 1 3   ? 11.423  0.006   20.756  1.00 22.33  ? 228  PHE B O   1 
ATOM   2401 C CB  . PHE B 1 3   ? 12.927  0.049   17.917  1.00 20.14  ? 228  PHE B CB  1 
ATOM   2402 C CG  . PHE B 1 3   ? 13.916  -1.094  17.931  1.00 15.70  ? 228  PHE B CG  1 
ATOM   2403 C CD1 . PHE B 1 3   ? 13.930  -2.028  16.911  1.00 16.49  ? 228  PHE B CD1 1 
ATOM   2404 C CD2 . PHE B 1 3   ? 14.802  -1.249  18.982  1.00 17.97  ? 228  PHE B CD2 1 
ATOM   2405 C CE1 . PHE B 1 3   ? 14.820  -3.094  16.931  1.00 17.63  ? 228  PHE B CE1 1 
ATOM   2406 C CE2 . PHE B 1 3   ? 15.695  -2.292  19.010  1.00 19.38  ? 228  PHE B CE2 1 
ATOM   2407 C CZ  . PHE B 1 3   ? 15.712  -3.222  17.992  1.00 17.94  ? 228  PHE B CZ  1 
ATOM   2408 N N   . SER B 1 4   ? 11.712  -2.109  20.026  1.00 18.87  ? 229  SER B N   1 
ATOM   2409 C CA  . SER B 1 4   ? 11.871  -2.687  21.349  1.00 17.24  ? 229  SER B CA  1 
ATOM   2410 C C   . SER B 1 4   ? 12.581  -4.020  21.198  1.00 17.87  ? 229  SER B C   1 
ATOM   2411 O O   . SER B 1 4   ? 12.692  -4.570  20.098  1.00 16.81  ? 229  SER B O   1 
ATOM   2412 C CB  . SER B 1 4   ? 10.524  -2.887  22.045  1.00 22.18  ? 229  SER B CB  1 
ATOM   2413 O OG  . SER B 1 4   ? 9.837   -3.966  21.435  1.00 22.30  ? 229  SER B OG  1 
ATOM   2414 N N   . LEU B 1 5   ? 13.048  -4.537  22.328  1.00 16.73  ? 230  LEU B N   1 
ATOM   2415 C CA  . LEU B 1 5   ? 13.543  -5.897  22.448  1.00 13.19  ? 230  LEU B CA  1 
ATOM   2416 C C   . LEU B 1 5   ? 12.682  -6.632  23.467  1.00 16.71  ? 230  LEU B C   1 
ATOM   2417 O O   . LEU B 1 5   ? 12.138  -6.000  24.379  1.00 19.37  ? 230  LEU B O   1 
ATOM   2418 C CB  . LEU B 1 5   ? 15.007  -5.916  22.905  1.00 20.19  ? 230  LEU B CB  1 
ATOM   2419 C CG  . LEU B 1 5   ? 15.979  -5.334  21.884  1.00 16.55  ? 230  LEU B CG  1 
ATOM   2420 C CD1 . LEU B 1 5   ? 17.366  -5.253  22.488  1.00 18.73  ? 230  LEU B CD1 1 
ATOM   2421 C CD2 . LEU B 1 5   ? 15.975  -6.203  20.623  1.00 15.56  ? 230  LEU B CD2 1 
ATOM   2422 N N   . PRO B 1 6   ? 12.529  -7.949  23.346  1.00 13.79  ? 231  PRO B N   1 
ATOM   2423 C CA  . PRO B 1 6   ? 11.711  -8.671  24.332  1.00 13.03  ? 231  PRO B CA  1 
ATOM   2424 C C   . PRO B 1 6   ? 12.321  -8.574  25.725  1.00 20.81  ? 231  PRO B C   1 
ATOM   2425 O O   . PRO B 1 6   ? 13.536  -8.452  25.891  1.00 20.37  ? 231  PRO B O   1 
ATOM   2426 C CB  . PRO B 1 6   ? 11.708  -10.111 23.810  1.00 17.49  ? 231  PRO B CB  1 
ATOM   2427 C CG  . PRO B 1 6   ? 12.946  -10.219 22.966  1.00 18.30  ? 231  PRO B CG  1 
ATOM   2428 C CD  . PRO B 1 6   ? 13.141  -8.849  22.352  1.00 13.06  ? 231  PRO B CD  1 
ATOM   2429 N N   A ASN B 1 7   ? 11.474  -8.672  26.752  0.52 17.77  ? 232  ASN B N   1 
ATOM   2430 N N   B ASN B 1 7   ? 11.432  -8.586  26.718  0.48 17.65  ? 232  ASN B N   1 
ATOM   2431 C CA  A ASN B 1 7   ? 11.906  -8.414  28.126  0.52 15.44  ? 232  ASN B CA  1 
ATOM   2432 C CA  B ASN B 1 7   ? 11.801  -8.531  28.130  0.48 15.74  ? 232  ASN B CA  1 
ATOM   2433 C C   A ASN B 1 7   ? 12.538  -9.629  28.813  0.52 17.40  ? 232  ASN B C   1 
ATOM   2434 C C   B ASN B 1 7   ? 12.104  -9.939  28.645  0.48 16.25  ? 232  ASN B C   1 
ATOM   2435 O O   A ASN B 1 7   ? 12.519  -9.715  30.049  0.52 20.28  ? 232  ASN B O   1 
ATOM   2436 O O   B ASN B 1 7   ? 11.429  -10.484 29.519  0.48 15.97  ? 232  ASN B O   1 
ATOM   2437 C CB  A ASN B 1 7   ? 10.723  -7.896  28.944  0.52 19.33  ? 232  ASN B CB  1 
ATOM   2438 C CB  B ASN B 1 7   ? 10.682  -7.866  28.924  0.48 19.31  ? 232  ASN B CB  1 
ATOM   2439 C CG  A ASN B 1 7   ? 9.649   -8.939  29.132  0.52 22.53  ? 232  ASN B CG  1 
ATOM   2440 C CG  B ASN B 1 7   ? 11.003  -7.729  30.402  0.48 25.46  ? 232  ASN B CG  1 
ATOM   2441 O OD1 A ASN B 1 7   ? 9.650   -9.979  28.470  0.52 22.09  ? 232  ASN B OD1 1 
ATOM   2442 O OD1 B ASN B 1 7   ? 12.103  -7.331  30.782  0.48 26.35  ? 232  ASN B OD1 1 
ATOM   2443 N ND2 A ASN B 1 7   ? 8.722   -8.671  30.039  0.52 26.71  ? 232  ASN B ND2 1 
ATOM   2444 N ND2 B ASN B 1 7   ? 10.036  -8.070  31.246  0.48 29.76  ? 232  ASN B ND2 1 
ATOM   2445 N N   . LEU B 1 8   ? 13.125  -10.547 28.052  1.00 15.10  ? 233  LEU B N   1 
ATOM   2446 C CA  . LEU B 1 8   ? 13.675  -11.792 28.565  1.00 12.95  ? 233  LEU B CA  1 
ATOM   2447 C C   . LEU B 1 8   ? 15.107  -11.570 29.037  1.00 16.37  ? 233  LEU B C   1 
ATOM   2448 O O   . LEU B 1 8   ? 15.880  -10.858 28.388  1.00 13.90  ? 233  LEU B O   1 
ATOM   2449 C CB  . LEU B 1 8   ? 13.650  -12.880 27.480  1.00 12.51  ? 233  LEU B CB  1 
ATOM   2450 C CG  . LEU B 1 8   ? 12.268  -13.159 26.880  1.00 15.27  ? 233  LEU B CG  1 
ATOM   2451 C CD1 . LEU B 1 8   ? 12.399  -14.060 25.640  1.00 17.88  ? 233  LEU B CD1 1 
ATOM   2452 C CD2 . LEU B 1 8   ? 11.432  -13.830 27.945  1.00 18.88  ? 233  LEU B CD2 1 
ATOM   2453 N N   . GLN B 1 9   ? 15.453  -12.167 30.177  1.00 14.35  ? 234  GLN B N   1 
ATOM   2454 C CA  . GLN B 1 9   ? 16.853  -12.186 30.595  1.00 13.49  ? 234  GLN B CA  1 
ATOM   2455 C C   . GLN B 1 9   ? 17.690  -13.020 29.628  1.00 13.88  ? 234  GLN B C   1 
ATOM   2456 O O   . GLN B 1 9   ? 17.185  -13.893 28.917  1.00 13.62  ? 234  GLN B O   1 
ATOM   2457 C CB  . GLN B 1 9   ? 16.990  -12.757 32.006  1.00 15.88  ? 234  GLN B CB  1 
ATOM   2458 C CG  . GLN B 1 9   ? 16.210  -11.977 33.059  1.00 16.72  ? 234  GLN B CG  1 
ATOM   2459 C CD  . GLN B 1 9   ? 16.182  -12.652 34.419  1.00 22.81  ? 234  GLN B CD  1 
ATOM   2460 O OE1 . GLN B 1 9   ? 16.794  -13.702 34.632  1.00 26.44  ? 234  GLN B OE1 1 
ATOM   2461 N NE2 . GLN B 1 9   ? 15.473  -12.042 35.353  1.00 23.29  ? 234  GLN B NE2 1 
ATOM   2462 N N   . THR B 1 10  ? 19.001  -12.757 29.616  1.00 11.74  ? 235  THR B N   1 
ATOM   2463 C CA  . THR B 1 10  ? 19.853  -13.497 28.688  1.00 11.16  ? 235  THR B CA  1 
ATOM   2464 C C   . THR B 1 10  ? 19.751  -14.997 28.931  1.00 12.04  ? 235  THR B C   1 
ATOM   2465 O O   . THR B 1 10  ? 19.710  -15.785 27.976  1.00 12.97  ? 235  THR B O   1 
ATOM   2466 C CB  . THR B 1 10  ? 21.297  -13.027 28.815  1.00 10.18  ? 235  THR B CB  1 
ATOM   2467 O OG1 . THR B 1 10  ? 21.310  -11.596 28.804  1.00 14.68  ? 235  THR B OG1 1 
ATOM   2468 C CG2 . THR B 1 10  ? 22.121  -13.547 27.638  1.00 12.30  ? 235  THR B CG2 1 
ATOM   2469 N N   . ASP B 1 11  ? 19.709  -15.410 30.204  1.00 11.53  ? 236  ASP B N   1 
ATOM   2470 C CA  . ASP B 1 11  ? 19.606  -16.830 30.514  1.00 15.16  ? 236  ASP B CA  1 
ATOM   2471 C C   . ASP B 1 11  ? 18.212  -17.395 30.273  1.00 16.12  ? 236  ASP B C   1 
ATOM   2472 O O   . ASP B 1 11  ? 18.023  -18.607 30.456  1.00 14.16  ? 236  ASP B O   1 
ATOM   2473 C CB  . ASP B 1 11  ? 20.050  -17.098 31.965  1.00 15.37  ? 236  ASP B CB  1 
ATOM   2474 C CG  . ASP B 1 11  ? 19.245  -16.329 33.008  1.00 19.34  ? 236  ASP B CG  1 
ATOM   2475 O OD1 . ASP B 1 11  ? 18.192  -15.735 32.694  1.00 16.63  ? 236  ASP B OD1 1 
ATOM   2476 O OD2 . ASP B 1 11  ? 19.686  -16.319 34.189  1.00 26.10  ? 236  ASP B OD2 1 
ATOM   2477 N N   . GLU B 1 12  ? 17.249  -16.567 29.867  1.00 10.60  ? 237  GLU B N   1 
ATOM   2478 C CA  . GLU B 1 12  ? 15.928  -17.039 29.464  1.00 10.51  ? 237  GLU B CA  1 
ATOM   2479 C C   . GLU B 1 12  ? 15.811  -17.178 27.955  1.00 13.58  ? 237  GLU B C   1 
ATOM   2480 O O   . GLU B 1 12  ? 14.733  -17.511 27.451  1.00 11.47  ? 237  GLU B O   1 
ATOM   2481 C CB  . GLU B 1 12  ? 14.828  -16.090 29.982  1.00 13.71  ? 237  GLU B CB  1 
ATOM   2482 C CG  . GLU B 1 12  ? 14.718  -16.096 31.505  1.00 12.43  ? 237  GLU B CG  1 
ATOM   2483 C CD  . GLU B 1 12  ? 13.840  -14.977 32.055  1.00 23.41  ? 237  GLU B CD  1 
ATOM   2484 O OE1 . GLU B 1 12  ? 13.537  -14.016 31.324  1.00 20.45  ? 237  GLU B OE1 1 
ATOM   2485 O OE2 . GLU B 1 12  ? 13.453  -15.067 33.242  1.00 24.11  ? 237  GLU B OE2 1 
ATOM   2486 N N   . MET B 1 13  ? 16.899  -16.945 27.224  1.00 11.65  ? 238  MET B N   1 
ATOM   2487 C CA  . MET B 1 13  ? 16.893  -16.991 25.767  1.00 11.82  ? 238  MET B CA  1 
ATOM   2488 C C   . MET B 1 13  ? 17.818  -18.095 25.254  1.00 10.76  ? 238  MET B C   1 
ATOM   2489 O O   . MET B 1 13  ? 18.545  -18.751 26.016  1.00 11.19  ? 238  MET B O   1 
ATOM   2490 C CB  . MET B 1 13  ? 17.284  -15.628 25.188  1.00 11.40  ? 238  MET B CB  1 
ATOM   2491 C CG  . MET B 1 13  ? 16.220  -14.565 25.443  1.00 15.26  ? 238  MET B CG  1 
ATOM   2492 S SD  . MET B 1 13  ? 16.490  -12.987 24.617  1.00 13.33  ? 238  MET B SD  1 
ATOM   2493 C CE  . MET B 1 13  ? 17.903  -12.353 25.533  1.00 11.28  ? 238  MET B CE  1 
ATOM   2494 N N   . SER B 1 14  ? 17.793  -18.263 23.933  1.00 10.65  ? 239  SER B N   1 
ATOM   2495 C CA  . SER B 1 14  ? 18.374  -19.402 23.236  1.00 10.34  ? 239  SER B CA  1 
ATOM   2496 C C   . SER B 1 14  ? 19.404  -18.941 22.218  1.00 11.66  ? 239  SER B C   1 
ATOM   2497 O O   . SER B 1 14  ? 19.283  -17.860 21.638  1.00 12.95  ? 239  SER B O   1 
ATOM   2498 C CB  . SER B 1 14  ? 17.304  -20.176 22.492  1.00 11.81  ? 239  SER B CB  1 
ATOM   2499 O OG  . SER B 1 14  ? 16.174  -20.433 23.302  1.00 13.84  ? 239  SER B OG  1 
ATOM   2500 N N   . SER B 1 15  ? 20.404  -19.784 21.983  1.00 10.06  ? 240  SER B N   1 
ATOM   2501 C CA  . SER B 1 15  ? 21.336  -19.527 20.894  1.00 10.02  ? 240  SER B CA  1 
ATOM   2502 C C   . SER B 1 15  ? 20.637  -19.724 19.559  1.00 11.68  ? 240  SER B C   1 
ATOM   2503 O O   . SER B 1 15  ? 19.761  -20.586 19.413  1.00 12.35  ? 240  SER B O   1 
ATOM   2504 C CB  . SER B 1 15  ? 22.539  -20.462 20.990  1.00 14.17  ? 240  SER B CB  1 
ATOM   2505 O OG  . SER B 1 15  ? 23.354  -20.397 19.830  1.00 12.02  ? 240  SER B OG  1 
ATOM   2506 N N   . SER B 1 16  ? 21.045  -18.915 18.573  1.00 10.95  ? 241  SER B N   1 
ATOM   2507 C CA  . SER B 1 16  ? 20.593  -19.034 17.196  1.00 9.55   ? 241  SER B CA  1 
ATOM   2508 C C   . SER B 1 16  ? 21.601  -19.753 16.312  1.00 9.78   ? 241  SER B C   1 
ATOM   2509 O O   . SER B 1 16  ? 21.386  -19.839 15.098  1.00 11.65  ? 241  SER B O   1 
ATOM   2510 C CB  . SER B 1 16  ? 20.294  -17.640 16.617  1.00 11.53  ? 241  SER B CB  1 
ATOM   2511 O OG  . SER B 1 16  ? 21.459  -16.814 16.677  1.00 10.74  ? 241  SER B OG  1 
ATOM   2512 N N   . ARG B 1 17  ? 22.703  -20.256 16.882  1.00 10.13  ? 242  ARG B N   1 
ATOM   2513 C CA  . ARG B 1 17  ? 23.649  -21.059 16.122  1.00 10.00  ? 242  ARG B CA  1 
ATOM   2514 C C   . ARG B 1 17  ? 23.784  -22.492 16.634  1.00 13.13  ? 242  ARG B C   1 
ATOM   2515 O O   . ARG B 1 17  ? 24.312  -23.341 15.902  1.00 13.37  ? 242  ARG B O   1 
ATOM   2516 C CB  . ARG B 1 17  ? 25.029  -20.372 16.079  1.00 10.33  ? 242  ARG B CB  1 
ATOM   2517 C CG  . ARG B 1 17  ? 25.068  -19.159 15.128  1.00 9.51   ? 242  ARG B CG  1 
ATOM   2518 C CD  . ARG B 1 17  ? 26.490  -18.618 14.932  1.00 10.34  ? 242  ARG B CD  1 
ATOM   2519 N NE  . ARG B 1 17  ? 27.348  -19.583 14.245  1.00 10.73  ? 242  ARG B NE  1 
ATOM   2520 C CZ  . ARG B 1 17  ? 28.526  -20.007 14.681  1.00 13.18  ? 242  ARG B CZ  1 
ATOM   2521 N NH1 . ARG B 1 17  ? 29.063  -19.551 15.809  1.00 12.41  ? 242  ARG B NH1 1 
ATOM   2522 N NH2 . ARG B 1 17  ? 29.203  -20.889 13.947  1.00 12.80  ? 242  ARG B NH2 1 
ATOM   2523 N N   . TRP B 1 18  ? 23.303  -22.800 17.843  1.00 11.46  ? 243  TRP B N   1 
ATOM   2524 C CA  . TRP B 1 18  ? 23.203  -24.188 18.307  1.00 11.32  ? 243  TRP B CA  1 
ATOM   2525 C C   . TRP B 1 18  ? 21.973  -24.241 19.202  1.00 12.48  ? 243  TRP B C   1 
ATOM   2526 O O   . TRP B 1 18  ? 21.854  -23.406 20.105  1.00 14.02  ? 243  TRP B O   1 
ATOM   2527 C CB  . TRP B 1 18  ? 24.440  -24.650 19.076  1.00 12.44  ? 243  TRP B CB  1 
ATOM   2528 C CG  . TRP B 1 18  ? 24.440  -26.140 19.300  1.00 11.17  ? 243  TRP B CG  1 
ATOM   2529 C CD1 . TRP B 1 18  ? 23.904  -26.805 20.367  1.00 14.31  ? 243  TRP B CD1 1 
ATOM   2530 C CD2 . TRP B 1 18  ? 24.969  -27.144 18.419  1.00 12.59  ? 243  TRP B CD2 1 
ATOM   2531 N NE1 . TRP B 1 18  ? 24.081  -28.163 20.215  1.00 12.39  ? 243  TRP B NE1 1 
ATOM   2532 C CE2 . TRP B 1 18  ? 24.726  -28.398 19.025  1.00 10.63  ? 243  TRP B CE2 1 
ATOM   2533 C CE3 . TRP B 1 18  ? 25.627  -27.103 17.178  1.00 11.88  ? 243  TRP B CE3 1 
ATOM   2534 C CZ2 . TRP B 1 18  ? 25.120  -29.606 18.436  1.00 13.53  ? 243  TRP B CZ2 1 
ATOM   2535 C CZ3 . TRP B 1 18  ? 26.017  -28.316 16.583  1.00 12.36  ? 243  TRP B CZ3 1 
ATOM   2536 C CH2 . TRP B 1 18  ? 25.767  -29.548 17.223  1.00 11.34  ? 243  TRP B CH2 1 
ATOM   2537 N N   . PRO B 1 19  ? 21.035  -25.163 18.977  1.00 12.71  ? 244  PRO B N   1 
ATOM   2538 C CA  . PRO B 1 19  ? 19.816  -25.158 19.796  1.00 14.83  ? 244  PRO B CA  1 
ATOM   2539 C C   . PRO B 1 19  ? 20.131  -25.529 21.232  1.00 16.47  ? 244  PRO B C   1 
ATOM   2540 O O   . PRO B 1 19  ? 20.370  -26.701 21.539  1.00 18.76  ? 244  PRO B O   1 
ATOM   2541 C CB  . PRO B 1 19  ? 18.920  -26.209 19.121  1.00 17.04  ? 244  PRO B CB  1 
ATOM   2542 C CG  . PRO B 1 19  ? 19.552  -26.496 17.789  1.00 17.50  ? 244  PRO B CG  1 
ATOM   2543 C CD  . PRO B 1 19  ? 21.017  -26.227 17.956  1.00 14.21  ? 244  PRO B CD  1 
ATOM   2544 N N   . ASN B 1 20  ? 20.169  -24.531 22.105  1.00 10.94  ? 245  ASN B N   1 
ATOM   2545 C CA  . ASN B 1 20  ? 20.430  -24.717 23.527  1.00 10.93  ? 245  ASN B CA  1 
ATOM   2546 C C   . ASN B 1 20  ? 20.273  -23.362 24.220  1.00 11.78  ? 245  ASN B C   1 
ATOM   2547 O O   . ASN B 1 20  ? 20.371  -22.315 23.568  1.00 13.96  ? 245  ASN B O   1 
ATOM   2548 C CB  . ASN B 1 20  ? 21.840  -25.295 23.781  1.00 12.54  ? 245  ASN B CB  1 
ATOM   2549 C CG  . ASN B 1 20  ? 21.813  -26.793 24.107  1.00 18.66  ? 245  ASN B CG  1 
ATOM   2550 O OD1 . ASN B 1 20  ? 20.778  -27.338 24.502  1.00 19.25  ? 245  ASN B OD1 1 
ATOM   2551 N ND2 . ASN B 1 20  ? 22.947  -27.459 23.937  1.00 18.83  ? 245  ASN B ND2 1 
ATOM   2552 N N   . PRO B 1 21  ? 20.050  -23.362 25.531  1.00 12.38  ? 246  PRO B N   1 
ATOM   2553 C CA  . PRO B 1 21  ? 19.930  -22.099 26.264  1.00 12.53  ? 246  PRO B CA  1 
ATOM   2554 C C   . PRO B 1 21  ? 21.246  -21.345 26.286  1.00 11.97  ? 246  PRO B C   1 
ATOM   2555 O O   . PRO B 1 21  ? 22.321  -21.945 26.388  1.00 14.06  ? 246  PRO B O   1 
ATOM   2556 C CB  . PRO B 1 21  ? 19.542  -22.541 27.681  1.00 16.57  ? 246  PRO B CB  1 
ATOM   2557 C CG  . PRO B 1 21  ? 19.147  -23.973 27.569  1.00 19.83  ? 246  PRO B CG  1 
ATOM   2558 C CD  . PRO B 1 21  ? 19.888  -24.533 26.412  1.00 16.17  ? 246  PRO B CD  1 
ATOM   2559 N N   . LEU B 1 22  ? 21.156  -20.019 26.204  1.00 12.25  ? 247  LEU B N   1 
ATOM   2560 C CA  . LEU B 1 22  ? 22.348  -19.202 26.384  1.00 10.71  ? 247  LEU B CA  1 
ATOM   2561 C C   . LEU B 1 22  ? 22.909  -19.411 27.781  1.00 16.54  ? 247  LEU B C   1 
ATOM   2562 O O   . LEU B 1 22  ? 22.166  -19.449 28.766  1.00 14.27  ? 247  LEU B O   1 
ATOM   2563 C CB  . LEU B 1 22  ? 22.036  -17.718 26.164  1.00 10.55  ? 247  LEU B CB  1 
ATOM   2564 C CG  . LEU B 1 22  ? 21.594  -17.401 24.727  1.00 11.63  ? 247  LEU B CG  1 
ATOM   2565 C CD1 . LEU B 1 22  ? 21.276  -15.920 24.587  1.00 15.09  ? 247  LEU B CD1 1 
ATOM   2566 C CD2 . LEU B 1 22  ? 22.663  -17.789 23.712  1.00 12.44  ? 247  LEU B CD2 1 
ATOM   2567 N N   . ALA B 1 23  ? 24.236  -19.540 27.855  1.00 11.19  ? 248  ALA B N   1 
ATOM   2568 C CA  . ALA B 1 23  ? 24.938  -19.813 29.101  1.00 15.85  ? 248  ALA B CA  1 
ATOM   2569 C C   . ALA B 1 23  ? 25.993  -18.783 29.458  1.00 15.04  ? 248  ALA B C   1 
ATOM   2570 O O   . ALA B 1 23  ? 26.328  -18.664 30.640  1.00 15.06  ? 248  ALA B O   1 
ATOM   2571 C CB  . ALA B 1 23  ? 25.614  -21.192 29.047  1.00 18.16  ? 248  ALA B CB  1 
ATOM   2572 N N   A THR B 1 24  ? 26.557  -18.071 28.482  0.60 11.78  ? 249  THR B N   1 
ATOM   2573 N N   B THR B 1 24  ? 26.493  -18.019 28.489  0.40 11.79  ? 249  THR B N   1 
ATOM   2574 C CA  A THR B 1 24  ? 27.559  -17.050 28.750  0.60 12.08  ? 249  THR B CA  1 
ATOM   2575 C CA  B THR B 1 24  ? 27.565  -17.067 28.726  0.40 12.22  ? 249  THR B CA  1 
ATOM   2576 C C   A THR B 1 24  ? 27.282  -15.839 27.876  0.60 13.75  ? 249  THR B C   1 
ATOM   2577 C C   B THR B 1 24  ? 27.347  -15.852 27.838  0.40 13.67  ? 249  THR B C   1 
ATOM   2578 O O   A THR B 1 24  ? 26.619  -15.925 26.836  0.60 13.32  ? 249  THR B O   1 
ATOM   2579 O O   B THR B 1 24  ? 26.778  -15.952 26.746  0.40 13.52  ? 249  THR B O   1 
ATOM   2580 C CB  A THR B 1 24  ? 28.999  -17.544 28.501  0.60 15.61  ? 249  THR B CB  1 
ATOM   2581 C CB  B THR B 1 24  ? 28.934  -17.704 28.453  0.40 15.73  ? 249  THR B CB  1 
ATOM   2582 O OG1 A THR B 1 24  ? 29.114  -18.102 27.181  0.60 13.87  ? 249  THR B OG1 1 
ATOM   2583 O OG1 B THR B 1 24  ? 29.060  -18.906 29.221  0.40 26.15  ? 249  THR B OG1 1 
ATOM   2584 C CG2 A THR B 1 24  ? 29.410  -18.581 29.541  0.60 24.02  ? 249  THR B CG2 1 
ATOM   2585 C CG2 B THR B 1 24  ? 30.052  -16.759 28.831  0.40 10.80  ? 249  THR B CG2 1 
ATOM   2586 N N   . LEU B 1 25  ? 27.794  -14.699 28.328  1.00 14.09  ? 250  LEU B N   1 
ATOM   2587 C CA  . LEU B 1 25  ? 27.673  -13.433 27.619  1.00 14.12  ? 250  LEU B CA  1 
ATOM   2588 C C   . LEU B 1 25  ? 29.005  -12.730 27.800  1.00 14.76  ? 250  LEU B C   1 
ATOM   2589 O O   . LEU B 1 25  ? 29.411  -12.470 28.940  1.00 15.59  ? 250  LEU B O   1 
ATOM   2590 C CB  . LEU B 1 25  ? 26.518  -12.597 28.184  1.00 13.89  ? 250  LEU B CB  1 
ATOM   2591 C CG  . LEU B 1 25  ? 26.357  -11.172 27.641  1.00 13.88  ? 250  LEU B CG  1 
ATOM   2592 C CD1 . LEU B 1 25  ? 25.980  -11.209 26.174  1.00 13.63  ? 250  LEU B CD1 1 
ATOM   2593 C CD2 . LEU B 1 25  ? 25.292  -10.407 28.459  1.00 13.39  ? 250  LEU B CD2 1 
ATOM   2594 N N   . PHE B 1 26  ? 29.713  -12.469 26.703  1.00 13.13  ? 251  PHE B N   1 
ATOM   2595 C CA  . PHE B 1 26  ? 31.099  -12.043 26.866  1.00 14.74  ? 251  PHE B CA  1 
ATOM   2596 C C   . PHE B 1 26  ? 31.576  -11.317 25.622  1.00 14.38  ? 251  PHE B C   1 
ATOM   2597 O O   . PHE B 1 26  ? 31.008  -11.454 24.537  1.00 14.43  ? 251  PHE B O   1 
ATOM   2598 C CB  . PHE B 1 26  ? 32.017  -13.238 27.177  1.00 15.28  ? 251  PHE B CB  1 
ATOM   2599 C CG  . PHE B 1 26  ? 32.185  -14.199 26.020  1.00 13.26  ? 251  PHE B CG  1 
ATOM   2600 C CD1 . PHE B 1 26  ? 31.229  -15.170 25.762  1.00 16.51  ? 251  PHE B CD1 1 
ATOM   2601 C CD2 . PHE B 1 26  ? 33.314  -14.125 25.192  1.00 16.43  ? 251  PHE B CD2 1 
ATOM   2602 C CE1 . PHE B 1 26  ? 31.382  -16.054 24.705  1.00 15.76  ? 251  PHE B CE1 1 
ATOM   2603 C CE2 . PHE B 1 26  ? 33.477  -15.006 24.142  1.00 17.94  ? 251  PHE B CE2 1 
ATOM   2604 C CZ  . PHE B 1 26  ? 32.506  -15.968 23.889  1.00 15.93  ? 251  PHE B CZ  1 
ATOM   2605 N N   . ALA B 1 27  ? 32.628  -10.527 25.804  1.00 14.95  ? 252  ALA B N   1 
ATOM   2606 C CA  . ALA B 1 27  ? 33.283  -9.824  24.713  1.00 15.72  ? 252  ALA B CA  1 
ATOM   2607 C C   . ALA B 1 27  ? 34.750  -10.211 24.731  1.00 18.82  ? 252  ALA B C   1 
ATOM   2608 O O   . ALA B 1 27  ? 35.408  -10.105 25.773  1.00 18.39  ? 252  ALA B O   1 
ATOM   2609 C CB  . ALA B 1 27  ? 33.119  -8.307  24.845  1.00 19.39  ? 252  ALA B CB  1 
ATOM   2610 N N   . ASP B 1 28  ? 35.246  -10.694 23.600  1.00 17.73  ? 253  ASP B N   1 
ATOM   2611 C CA  . ASP B 1 28  ? 36.653  -11.083 23.487  1.00 18.00  ? 253  ASP B CA  1 
ATOM   2612 C C   . ASP B 1 28  ? 37.330  -10.198 22.454  1.00 17.90  ? 253  ASP B C   1 
ATOM   2613 O O   . ASP B 1 28  ? 37.124  -10.396 21.241  1.00 23.17  ? 253  ASP B O   1 
ATOM   2614 C CB  . ASP B 1 28  ? 36.790  -12.558 23.105  1.00 21.63  ? 253  ASP B CB  1 
ATOM   2615 C CG  . ASP B 1 28  ? 38.226  -13.055 23.227  1.00 25.96  ? 253  ASP B CG  1 
ATOM   2616 O OD1 . ASP B 1 28  ? 39.129  -12.215 23.398  1.00 30.46  ? 253  ASP B OD1 1 
ATOM   2617 O OD2 . ASP B 1 28  ? 38.448  -14.278 23.158  1.00 29.45  ? 253  ASP B OD2 1 
ATOM   2618 N N   . PRO B 1 29  ? 38.164  -9.244  22.872  1.00 18.21  ? 254  PRO B N   1 
ATOM   2619 C CA  . PRO B 1 29  ? 38.786  -8.322  21.916  1.00 20.78  ? 254  PRO B CA  1 
ATOM   2620 C C   . PRO B 1 29  ? 40.003  -8.889  21.209  1.00 35.65  ? 254  PRO B C   1 
ATOM   2621 O O   . PRO B 1 29  ? 40.584  -8.198  20.364  1.00 31.41  ? 254  PRO B O   1 
ATOM   2622 C CB  . PRO B 1 29  ? 39.179  -7.141  22.807  1.00 20.24  ? 254  PRO B CB  1 
ATOM   2623 C CG  . PRO B 1 29  ? 39.531  -7.795  24.120  1.00 26.24  ? 254  PRO B CG  1 
ATOM   2624 C CD  . PRO B 1 29  ? 38.563  -8.951  24.262  1.00 19.18  ? 254  PRO B CD  1 
ATOM   2625 N N   . ASN B 1 30  ? 40.411  -10.114 21.531  1.00 22.43  ? 255  ASN B N   1 
ATOM   2626 C CA  . ASN B 1 30  ? 41.631  -10.693 20.984  1.00 30.14  ? 255  ASN B CA  1 
ATOM   2627 C C   . ASN B 1 30  ? 41.347  -11.847 20.025  1.00 36.88  ? 255  ASN B C   1 
ATOM   2628 O O   . ASN B 1 30  ? 42.163  -12.762 19.882  1.00 31.69  ? 255  ASN B O   1 
ATOM   2629 C CB  . ASN B 1 30  ? 42.550  -11.139 22.118  1.00 29.27  ? 255  ASN B CB  1 
ATOM   2630 C CG  . ASN B 1 30  ? 43.053  -9.972  22.938  1.00 35.75  ? 255  ASN B CG  1 
ATOM   2631 O OD1 . ASN B 1 30  ? 43.377  -8.916  22.393  1.00 42.06  ? 255  ASN B OD1 1 
ATOM   2632 N ND2 . ASN B 1 30  ? 43.103  -10.145 24.253  1.00 37.78  ? 255  ASN B ND2 1 
ATOM   2633 N N   . VAL B 1 31  ? 40.194  -11.817 19.361  1.00 29.26  ? 256  VAL B N   1 
ATOM   2634 C CA  . VAL B 1 31  ? 39.909  -12.732 18.264  1.00 28.32  ? 256  VAL B CA  1 
ATOM   2635 C C   . VAL B 1 31  ? 40.465  -12.108 16.992  1.00 26.82  ? 256  VAL B C   1 
ATOM   2636 O O   . VAL B 1 31  ? 40.042  -11.019 16.589  1.00 33.77  ? 256  VAL B O   1 
ATOM   2637 C CB  . VAL B 1 31  ? 38.403  -13.007 18.140  1.00 30.62  ? 256  VAL B CB  1 
ATOM   2638 C CG1 . VAL B 1 31  ? 38.145  -14.008 17.031  1.00 35.74  ? 256  VAL B CG1 1 
ATOM   2639 C CG2 . VAL B 1 31  ? 37.851  -13.524 19.469  1.00 27.07  ? 256  VAL B CG2 1 
ATOM   2640 N N   . ALA B 1 32  ? 41.422  -12.795 16.362  1.00 27.19  ? 257  ALA B N   1 
ATOM   2641 C CA  . ALA B 1 32  ? 42.186  -12.183 15.281  1.00 34.81  ? 257  ALA B CA  1 
ATOM   2642 C C   . ALA B 1 32  ? 41.353  -11.995 14.021  1.00 35.51  ? 257  ALA B C   1 
ATOM   2643 O O   . ALA B 1 32  ? 41.561  -11.024 13.285  1.00 31.46  ? 257  ALA B O   1 
ATOM   2644 C CB  . ALA B 1 32  ? 43.425  -13.025 14.969  1.00 31.09  ? 257  ALA B CB  1 
ATOM   2645 N N   . VAL B 1 33  ? 40.418  -12.900 13.746  1.00 24.20  ? 258  VAL B N   1 
ATOM   2646 C CA  . VAL B 1 33  ? 39.666  -12.884 12.497  1.00 17.85  ? 258  VAL B CA  1 
ATOM   2647 C C   . VAL B 1 33  ? 38.178  -12.780 12.811  1.00 18.30  ? 258  VAL B C   1 
ATOM   2648 O O   . VAL B 1 33  ? 37.675  -13.478 13.697  1.00 21.49  ? 258  VAL B O   1 
ATOM   2649 C CB  . VAL B 1 33  ? 39.963  -14.128 11.642  1.00 17.96  ? 258  VAL B CB  1 
ATOM   2650 C CG1 . VAL B 1 33  ? 39.158  -14.076 10.344  1.00 23.49  ? 258  VAL B CG1 1 
ATOM   2651 C CG2 . VAL B 1 33  ? 41.467  -14.207 11.345  1.00 23.01  ? 258  VAL B CG2 1 
ATOM   2652 N N   . ALA B 1 34  ? 37.482  -11.906 12.087  1.00 20.24  ? 259  ALA B N   1 
ATOM   2653 C CA  . ALA B 1 34  ? 36.067  -11.683 12.341  1.00 18.35  ? 259  ALA B CA  1 
ATOM   2654 C C   . ALA B 1 34  ? 35.256  -12.927 11.992  1.00 15.19  ? 259  ALA B C   1 
ATOM   2655 O O   . ALA B 1 34  ? 35.601  -13.663 11.065  1.00 18.50  ? 259  ALA B O   1 
ATOM   2656 C CB  . ALA B 1 34  ? 35.560  -10.499 11.524  1.00 19.05  ? 259  ALA B CB  1 
ATOM   2657 N N   . PRO B 1 35  ? 34.174  -13.183 12.718  1.00 13.39  ? 260  PRO B N   1 
ATOM   2658 C CA  . PRO B 1 35  ? 33.320  -14.324 12.385  1.00 12.78  ? 260  PRO B CA  1 
ATOM   2659 C C   . PRO B 1 35  ? 32.474  -14.032 11.158  1.00 14.60  ? 260  PRO B C   1 
ATOM   2660 O O   . PRO B 1 35  ? 32.127  -12.885 10.863  1.00 13.64  ? 260  PRO B O   1 
ATOM   2661 C CB  . PRO B 1 35  ? 32.447  -14.484 13.635  1.00 16.87  ? 260  PRO B CB  1 
ATOM   2662 C CG  . PRO B 1 35  ? 32.353  -13.094 14.184  1.00 15.33  ? 260  PRO B CG  1 
ATOM   2663 C CD  . PRO B 1 35  ? 33.692  -12.457 13.906  1.00 14.40  ? 260  PRO B CD  1 
ATOM   2664 N N   . GLN B 1 36  ? 32.158  -15.094 10.426  1.00 12.10  ? 261  GLN B N   1 
ATOM   2665 C CA  . GLN B 1 36  ? 31.323  -14.988 9.235   1.00 11.94  ? 261  GLN B CA  1 
ATOM   2666 C C   . GLN B 1 36  ? 30.178  -15.990 9.315   1.00 16.53  ? 261  GLN B C   1 
ATOM   2667 O O   . GLN B 1 36  ? 29.867  -16.709 8.365   1.00 14.25  ? 261  GLN B O   1 
ATOM   2668 C CB  . GLN B 1 36  ? 32.144  -15.184 7.967   1.00 11.12  ? 261  GLN B CB  1 
ATOM   2669 C CG  . GLN B 1 36  ? 31.414  -14.650 6.729   1.00 14.36  ? 261  GLN B CG  1 
ATOM   2670 C CD  . GLN B 1 36  ? 32.206  -14.770 5.438   1.00 18.69  ? 261  GLN B CD  1 
ATOM   2671 O OE1 . GLN B 1 36  ? 33.382  -15.154 5.426   1.00 16.57  ? 261  GLN B OE1 1 
ATOM   2672 N NE2 . GLN B 1 36  ? 31.550  -14.436 4.332   1.00 15.34  ? 261  GLN B NE2 1 
ATOM   2673 N N   . TRP B 1 37  ? 29.551  -16.031 10.487  1.00 12.47  ? 262  TRP B N   1 
ATOM   2674 C CA  . TRP B 1 37  ? 28.451  -16.950 10.763  1.00 11.48  ? 262  TRP B CA  1 
ATOM   2675 C C   . TRP B 1 37  ? 27.354  -16.823 9.718   1.00 13.71  ? 262  TRP B C   1 
ATOM   2676 O O   . TRP B 1 37  ? 26.992  -15.715 9.307   1.00 12.52  ? 262  TRP B O   1 
ATOM   2677 C CB  . TRP B 1 37  ? 27.888  -16.648 12.153  1.00 12.15  ? 262  TRP B CB  1 
ATOM   2678 C CG  . TRP B 1 37  ? 28.923  -16.702 13.244  1.00 11.72  ? 262  TRP B CG  1 
ATOM   2679 C CD1 . TRP B 1 37  ? 30.011  -17.531 13.294  1.00 15.42  ? 262  TRP B CD1 1 
ATOM   2680 C CD2 . TRP B 1 37  ? 28.967  -15.908 14.443  1.00 10.83  ? 262  TRP B CD2 1 
ATOM   2681 N NE1 . TRP B 1 37  ? 30.723  -17.310 14.452  1.00 13.92  ? 262  TRP B NE1 1 
ATOM   2682 C CE2 . TRP B 1 37  ? 30.105  -16.322 15.178  1.00 9.82   ? 262  TRP B CE2 1 
ATOM   2683 C CE3 . TRP B 1 37  ? 28.158  -14.892 14.971  1.00 12.42  ? 262  TRP B CE3 1 
ATOM   2684 C CZ2 . TRP B 1 37  ? 30.461  -15.747 16.404  1.00 12.39  ? 262  TRP B CZ2 1 
ATOM   2685 C CZ3 . TRP B 1 37  ? 28.518  -14.320 16.202  1.00 11.36  ? 262  TRP B CZ3 1 
ATOM   2686 C CH2 . TRP B 1 37  ? 29.653  -14.752 16.896  1.00 11.67  ? 262  TRP B CH2 1 
ATOM   2687 N N   . GLN B 1 38  ? 26.805  -17.969 9.301   1.00 11.14  ? 263  GLN B N   1 
ATOM   2688 C CA  . GLN B 1 38  ? 25.713  -17.969 8.336   1.00 9.47   ? 263  GLN B CA  1 
ATOM   2689 C C   . GLN B 1 38  ? 24.346  -18.171 8.976   1.00 9.19   ? 263  GLN B C   1 
ATOM   2690 O O   . GLN B 1 38  ? 23.340  -17.797 8.365   1.00 12.21  ? 263  GLN B O   1 
ATOM   2691 C CB  . GLN B 1 38  ? 25.944  -19.044 7.269   1.00 12.31  ? 263  GLN B CB  1 
ATOM   2692 C CG  . GLN B 1 38  ? 27.219  -18.789 6.449   1.00 12.78  ? 263  GLN B CG  1 
ATOM   2693 C CD  . GLN B 1 38  ? 27.180  -17.462 5.724   1.00 14.64  ? 263  GLN B CD  1 
ATOM   2694 O OE1 . GLN B 1 38  ? 26.308  -17.231 4.879   1.00 13.26  ? 263  GLN B OE1 1 
ATOM   2695 N NE2 . GLN B 1 38  ? 28.137  -16.579 6.039   1.00 11.83  ? 263  GLN B NE2 1 
ATOM   2696 N N   . ASN B 1 39  ? 24.282  -18.724 10.191  1.00 9.60   ? 264  ASN B N   1 
ATOM   2697 C CA  . ASN B 1 39  ? 23.047  -18.775 10.962  1.00 11.24  ? 264  ASN B CA  1 
ATOM   2698 C C   . ASN B 1 39  ? 23.030  -17.660 12.006  1.00 9.63   ? 264  ASN B C   1 
ATOM   2699 O O   . ASN B 1 39  ? 24.053  -17.039 12.292  1.00 12.84  ? 264  ASN B O   1 
ATOM   2700 C CB  . ASN B 1 39  ? 22.891  -20.146 11.624  1.00 11.05  ? 264  ASN B CB  1 
ATOM   2701 C CG  . ASN B 1 39  ? 22.699  -21.247 10.603  1.00 10.70  ? 264  ASN B CG  1 
ATOM   2702 O OD1 . ASN B 1 39  ? 21.961  -21.076 9.628   1.00 11.44  ? 264  ASN B OD1 1 
ATOM   2703 N ND2 . ASN B 1 39  ? 23.372  -22.377 10.810  1.00 11.07  ? 264  ASN B ND2 1 
ATOM   2704 N N   . GLY B 1 40  ? 21.848  -17.399 12.566  1.00 8.60   ? 265  GLY B N   1 
ATOM   2705 C CA  . GLY B 1 40  ? 21.731  -16.334 13.542  1.00 11.76  ? 265  GLY B CA  1 
ATOM   2706 C C   . GLY B 1 40  ? 21.932  -14.945 12.977  1.00 14.75  ? 265  GLY B C   1 
ATOM   2707 O O   . GLY B 1 40  ? 22.413  -14.060 13.691  1.00 12.22  ? 265  GLY B O   1 
ATOM   2708 N N   . ARG B 1 41  ? 21.574  -14.724 11.713  1.00 10.37  ? 266  ARG B N   1 
ATOM   2709 C CA  . ARG B 1 41  ? 21.821  -13.456 11.022  1.00 10.75  ? 266  ARG B CA  1 
ATOM   2710 C C   . ARG B 1 41  ? 20.491  -12.846 10.592  1.00 11.62  ? 266  ARG B C   1 
ATOM   2711 O O   . ARG B 1 41  ? 19.746  -13.456 9.817   1.00 13.01  ? 266  ARG B O   1 
ATOM   2712 C CB  . ARG B 1 41  ? 22.724  -13.658 9.801   1.00 11.99  ? 266  ARG B CB  1 
ATOM   2713 C CG  . ARG B 1 41  ? 24.089  -14.328 10.090  1.00 15.24  ? 266  ARG B CG  1 
ATOM   2714 C CD  . ARG B 1 41  ? 25.025  -13.411 10.889  1.00 11.82  ? 266  ARG B CD  1 
ATOM   2715 N NE  . ARG B 1 41  ? 25.313  -12.150 10.203  1.00 12.92  ? 266  ARG B NE  1 
ATOM   2716 C CZ  . ARG B 1 41  ? 26.314  -11.962 9.354   1.00 13.39  ? 266  ARG B CZ  1 
ATOM   2717 N NH1 . ARG B 1 41  ? 27.149  -12.940 9.037   1.00 13.76  ? 266  ARG B NH1 1 
ATOM   2718 N NH2 . ARG B 1 41  ? 26.487  -10.756 8.816   1.00 14.89  ? 266  ARG B NH2 1 
ATOM   2719 N N   . CYS B 1 42  ? 20.196  -11.644 11.091  1.00 10.24  ? 267  CYS B N   1 
ATOM   2720 C CA  . CYS B 1 42  ? 18.915  -10.999 10.822  1.00 13.16  ? 267  CYS B CA  1 
ATOM   2721 C C   . CYS B 1 42  ? 19.062  -9.499  11.042  1.00 14.47  ? 267  CYS B C   1 
ATOM   2722 O O   . CYS B 1 42  ? 19.645  -9.090  12.050  1.00 14.67  ? 267  CYS B O   1 
ATOM   2723 C CB  . CYS B 1 42  ? 17.828  -11.570 11.744  1.00 13.12  ? 267  CYS B CB  1 
ATOM   2724 S SG  . CYS B 1 42  ? 16.154  -10.952 11.355  1.00 14.97  ? 267  CYS B SG  1 
ATOM   2725 N N   . THR B 1 43  ? 18.557  -8.685  10.104  1.00 12.17  ? 268  THR B N   1 
ATOM   2726 C CA  . THR B 1 43  ? 18.577  -7.241  10.302  1.00 11.61  ? 268  THR B CA  1 
ATOM   2727 C C   . THR B 1 43  ? 17.469  -6.828  11.265  1.00 10.89  ? 268  THR B C   1 
ATOM   2728 O O   . THR B 1 43  ? 16.519  -7.576  11.515  1.00 12.73  ? 268  THR B O   1 
ATOM   2729 C CB  . THR B 1 43  ? 18.409  -6.487  8.978   1.00 11.26  ? 268  THR B CB  1 
ATOM   2730 O OG1 . THR B 1 43  ? 17.056  -6.614  8.508   1.00 16.07  ? 268  THR B OG1 1 
ATOM   2731 C CG2 . THR B 1 43  ? 19.350  -7.055  7.917   1.00 16.96  ? 268  THR B CG2 1 
ATOM   2732 N N   . LEU B 1 44  ? 17.590  -5.609  11.803  1.00 15.31  ? 269  LEU B N   1 
ATOM   2733 C CA  . LEU B 1 44  ? 16.566  -5.128  12.729  1.00 15.05  ? 269  LEU B CA  1 
ATOM   2734 C C   . LEU B 1 44  ? 15.209  -4.967  12.048  1.00 14.73  ? 269  LEU B C   1 
ATOM   2735 O O   . LEU B 1 44  ? 14.173  -5.052  12.720  1.00 16.83  ? 269  LEU B O   1 
ATOM   2736 C CB  . LEU B 1 44  ? 17.003  -3.808  13.365  1.00 15.76  ? 269  LEU B CB  1 
ATOM   2737 C CG  . LEU B 1 44  ? 18.337  -3.846  14.115  1.00 24.70  ? 269  LEU B CG  1 
ATOM   2738 C CD1 . LEU B 1 44  ? 18.528  -2.571  14.942  1.00 18.08  ? 269  LEU B CD1 1 
ATOM   2739 C CD2 . LEU B 1 44  ? 18.468  -5.096  14.985  1.00 18.67  ? 269  LEU B CD2 1 
ATOM   2740 N N   . GLU B 1 45  ? 15.190  -4.774  10.733  1.00 14.59  ? 270  GLU B N   1 
ATOM   2741 C CA  . GLU B 1 45  ? 13.935  -4.725  9.989   1.00 17.69  ? 270  GLU B CA  1 
ATOM   2742 C C   . GLU B 1 45  ? 13.378  -6.113  9.664   1.00 18.15  ? 270  GLU B C   1 
ATOM   2743 O O   . GLU B 1 45  ? 12.374  -6.210  8.947   1.00 20.71  ? 270  GLU B O   1 
ATOM   2744 C CB  . GLU B 1 45  ? 14.124  -3.888  8.721   1.00 24.21  ? 270  GLU B CB  1 
ATOM   2745 C CG  . GLU B 1 45  ? 14.521  -2.457  9.077   1.00 30.61  ? 270  GLU B CG  1 
ATOM   2746 C CD  . GLU B 1 45  ? 14.525  -1.505  7.897   1.00 55.32  ? 270  GLU B CD  1 
ATOM   2747 O OE1 . GLU B 1 45  ? 14.554  -1.973  6.737   1.00 60.99  ? 270  GLU B OE1 1 
ATOM   2748 O OE2 . GLU B 1 45  ? 14.498  -0.280  8.145   1.00 45.15  ? 270  GLU B OE2 1 
ATOM   2749 N N   . GLY B 1 46  ? 13.989  -7.170  10.195  1.00 14.29  ? 271  GLY B N   1 
ATOM   2750 C CA  . GLY B 1 46  ? 13.448  -8.508  10.080  1.00 15.00  ? 271  GLY B CA  1 
ATOM   2751 C C   . GLY B 1 46  ? 13.752  -9.221  8.780   1.00 20.84  ? 271  GLY B C   1 
ATOM   2752 O O   . GLY B 1 46  ? 12.936  -10.023 8.315   1.00 19.32  ? 271  GLY B O   1 
ATOM   2753 N N   . GLU B 1 47  ? 14.897  -8.950  8.165   1.00 14.53  ? 272  GLU B N   1 
ATOM   2754 C CA  . GLU B 1 47  ? 15.306  -9.664  6.959   1.00 16.57  ? 272  GLU B CA  1 
ATOM   2755 C C   . GLU B 1 47  ? 16.440  -10.624 7.297   1.00 16.30  ? 272  GLU B C   1 
ATOM   2756 O O   . GLU B 1 47  ? 17.479  -10.211 7.833   1.00 12.84  ? 272  GLU B O   1 
ATOM   2757 C CB  . GLU B 1 47  ? 15.709  -8.683  5.865   1.00 18.21  ? 272  GLU B CB  1 
ATOM   2758 C CG  . GLU B 1 47  ? 14.596  -7.697  5.572   1.00 23.34  ? 272  GLU B CG  1 
ATOM   2759 C CD  . GLU B 1 47  ? 14.561  -7.283  4.127   1.00 28.57  ? 272  GLU B CD  1 
ATOM   2760 O OE1 . GLU B 1 47  ? 15.408  -7.773  3.355   1.00 35.32  ? 272  GLU B OE1 1 
ATOM   2761 O OE2 . GLU B 1 47  ? 13.676  -6.481  3.765   1.00 29.38  ? 272  GLU B OE2 1 
ATOM   2762 N N   . LEU B 1 48  ? 16.225  -11.904 7.006   1.00 13.99  ? 273  LEU B N   1 
ATOM   2763 C CA  . LEU B 1 48  ? 17.194  -12.940 7.333   1.00 14.98  ? 273  LEU B CA  1 
ATOM   2764 C C   . LEU B 1 48  ? 18.360  -12.933 6.353   1.00 13.98  ? 273  LEU B C   1 
ATOM   2765 O O   . LEU B 1 48  ? 18.198  -12.645 5.162   1.00 14.39  ? 273  LEU B O   1 
ATOM   2766 C CB  . LEU B 1 48  ? 16.523  -14.308 7.313   1.00 12.66  ? 273  LEU B CB  1 
ATOM   2767 C CG  . LEU B 1 48  ? 15.358  -14.479 8.279   1.00 15.95  ? 273  LEU B CG  1 
ATOM   2768 C CD1 . LEU B 1 48  ? 14.704  -15.839 8.048   1.00 19.61  ? 273  LEU B CD1 1 
ATOM   2769 C CD2 . LEU B 1 48  ? 15.841  -14.342 9.726   1.00 14.55  ? 273  LEU B CD2 1 
ATOM   2770 N N   . LEU B 1 49  ? 19.547  -13.251 6.870   1.00 12.42  ? 274  LEU B N   1 
ATOM   2771 C CA  . LEU B 1 49  ? 20.744  -13.378 6.052   1.00 12.10  ? 274  LEU B CA  1 
ATOM   2772 C C   . LEU B 1 49  ? 21.280  -14.802 6.124   1.00 12.14  ? 274  LEU B C   1 
ATOM   2773 O O   . LEU B 1 49  ? 21.030  -15.531 7.083   1.00 12.45  ? 274  LEU B O   1 
ATOM   2774 C CB  . LEU B 1 49  ? 21.845  -12.410 6.510   1.00 13.02  ? 274  LEU B CB  1 
ATOM   2775 C CG  . LEU B 1 49  ? 21.427  -11.003 6.934   1.00 15.33  ? 274  LEU B CG  1 
ATOM   2776 C CD1 . LEU B 1 49  ? 22.653  -10.231 7.418   1.00 19.94  ? 274  LEU B CD1 1 
ATOM   2777 C CD2 . LEU B 1 49  ? 20.769  -10.292 5.777   1.00 14.03  ? 274  LEU B CD2 1 
ATOM   2778 N N   . GLY B 1 50  ? 22.041  -15.189 5.102   1.00 11.87  ? 275  GLY B N   1 
ATOM   2779 C CA  . GLY B 1 50  ? 22.747  -16.466 5.165   1.00 11.24  ? 275  GLY B CA  1 
ATOM   2780 C C   . GLY B 1 50  ? 21.789  -17.646 5.132   1.00 13.28  ? 275  GLY B C   1 
ATOM   2781 O O   . GLY B 1 50  ? 20.773  -17.639 4.426   1.00 14.64  ? 275  GLY B O   1 
ATOM   2782 N N   . THR B 1 51  ? 22.111  -18.676 5.910   1.00 10.75  ? 276  THR B N   1 
ATOM   2783 C CA  . THR B 1 51  ? 21.261  -19.859 6.009   1.00 11.52  ? 276  THR B CA  1 
ATOM   2784 C C   . THR B 1 51  ? 20.297  -19.791 7.192   1.00 11.94  ? 276  THR B C   1 
ATOM   2785 O O   . THR B 1 51  ? 19.653  -20.796 7.512   1.00 12.72  ? 276  THR B O   1 
ATOM   2786 C CB  . THR B 1 51  ? 22.124  -21.132 6.099   1.00 11.79  ? 276  THR B CB  1 
ATOM   2787 O OG1 . THR B 1 51  ? 23.104  -21.000 7.142   1.00 11.85  ? 276  THR B OG1 1 
ATOM   2788 C CG2 . THR B 1 51  ? 22.854  -21.401 4.758   1.00 11.23  ? 276  THR B CG2 1 
ATOM   2789 N N   . THR B 1 52  ? 20.163  -18.626 7.825   1.00 11.10  ? 277  THR B N   1 
ATOM   2790 C CA  . THR B 1 52  ? 19.333  -18.467 9.012   1.00 11.86  ? 277  THR B CA  1 
ATOM   2791 C C   . THR B 1 52  ? 17.900  -18.911 8.744   1.00 9.72   ? 277  THR B C   1 
ATOM   2792 O O   . THR B 1 52  ? 17.243  -18.349 7.857   1.00 14.54  ? 277  THR B O   1 
ATOM   2793 C CB  . THR B 1 52  ? 19.344  -17.007 9.457   1.00 11.45  ? 277  THR B CB  1 
ATOM   2794 O OG1 . THR B 1 52  ? 20.701  -16.585 9.643   1.00 10.52  ? 277  THR B OG1 1 
ATOM   2795 C CG2 . THR B 1 52  ? 18.568  -16.828 10.751  1.00 12.09  ? 277  THR B CG2 1 
ATOM   2796 N N   . PRO B 1 53  ? 17.383  -19.896 9.476   1.00 13.20  ? 278  PRO B N   1 
ATOM   2797 C CA  . PRO B 1 53  ? 16.027  -20.374 9.209   1.00 15.34  ? 278  PRO B CA  1 
ATOM   2798 C C   . PRO B 1 53  ? 14.973  -19.449 9.792   1.00 13.56  ? 278  PRO B C   1 
ATOM   2799 O O   . PRO B 1 53  ? 15.129  -18.886 10.880  1.00 15.97  ? 278  PRO B O   1 
ATOM   2800 C CB  . PRO B 1 53  ? 15.999  -21.750 9.890   1.00 15.15  ? 278  PRO B CB  1 
ATOM   2801 C CG  . PRO B 1 53  ? 17.017  -21.666 10.950  1.00 15.69  ? 278  PRO B CG  1 
ATOM   2802 C CD  . PRO B 1 53  ? 18.115  -20.780 10.396  1.00 14.01  ? 278  PRO B CD  1 
ATOM   2803 N N   . ARG B 1 54  ? 13.872  -19.330 9.059   1.00 14.31  ? 279  ARG B N   1 
ATOM   2804 C CA  . ARG B 1 54  ? 12.737  -18.541 9.523   1.00 15.60  ? 279  ARG B CA  1 
ATOM   2805 C C   . ARG B 1 54  ? 12.065  -19.191 10.724  1.00 17.71  ? 279  ARG B C   1 
ATOM   2806 O O   . ARG B 1 54  ? 11.640  -18.502 11.663  1.00 15.65  ? 279  ARG B O   1 
ATOM   2807 C CB  . ARG B 1 54  ? 11.753  -18.390 8.370   1.00 17.68  ? 279  ARG B CB  1 
ATOM   2808 C CG  . ARG B 1 54  ? 10.676  -17.403 8.608   1.00 27.14  ? 279  ARG B CG  1 
ATOM   2809 C CD  . ARG B 1 54  ? 10.046  -16.970 7.291   1.00 24.99  ? 279  ARG B CD  1 
ATOM   2810 N NE  . ARG B 1 54  ? 9.093   -15.915 7.580   1.00 29.17  ? 279  ARG B NE  1 
ATOM   2811 C CZ  . ARG B 1 54  ? 9.398   -14.627 7.592   1.00 25.51  ? 279  ARG B CZ  1 
ATOM   2812 N NH1 . ARG B 1 54  ? 10.579  -14.194 7.176   1.00 35.04  ? 279  ARG B NH1 1 
ATOM   2813 N NH2 . ARG B 1 54  ? 8.493   -13.753 8.024   1.00 34.00  ? 279  ARG B NH2 1 
ATOM   2814 N N   . ASN B 1 55  ? 11.963  -20.512 10.708  1.00 11.80  ? 280  ASN B N   1 
ATOM   2815 C CA  . ASN B 1 55  ? 11.445  -21.288 11.827  1.00 12.72  ? 280  ASN B CA  1 
ATOM   2816 C C   . ASN B 1 55  ? 12.606  -21.588 12.763  1.00 12.18  ? 280  ASN B C   1 
ATOM   2817 O O   . ASN B 1 55  ? 13.585  -22.218 12.351  1.00 13.23  ? 280  ASN B O   1 
ATOM   2818 C CB  . ASN B 1 55  ? 10.808  -22.581 11.310  1.00 13.27  ? 280  ASN B CB  1 
ATOM   2819 C CG  . ASN B 1 55  ? 10.087  -23.363 12.387  1.00 14.09  ? 280  ASN B CG  1 
ATOM   2820 O OD1 . ASN B 1 55  ? 10.482  -23.365 13.546  1.00 15.03  ? 280  ASN B OD1 1 
ATOM   2821 N ND2 . ASN B 1 55  ? 9.014   -24.043 11.995  1.00 11.01  ? 280  ASN B ND2 1 
ATOM   2822 N N   . ALA B 1 56  ? 12.505  -21.116 14.007  1.00 11.58  ? 281  ALA B N   1 
ATOM   2823 C CA  . ALA B 1 56  ? 13.571  -21.325 14.984  1.00 14.59  ? 281  ALA B CA  1 
ATOM   2824 C C   . ALA B 1 56  ? 13.981  -22.790 15.095  1.00 16.41  ? 281  ALA B C   1 
ATOM   2825 O O   . ALA B 1 56  ? 15.170  -23.097 15.279  1.00 15.20  ? 281  ALA B O   1 
ATOM   2826 C CB  . ALA B 1 56  ? 13.121  -20.815 16.354  1.00 13.34  ? 281  ALA B CB  1 
ATOM   2827 N N   A SER B 1 57  ? 13.018  -23.707 15.008  0.54 12.53  ? 282  SER B N   1 
ATOM   2828 N N   B SER B 1 57  ? 13.028  -23.707 14.941  0.46 12.49  ? 282  SER B N   1 
ATOM   2829 C CA  A SER B 1 57  ? 13.283  -25.113 15.289  0.54 12.13  ? 282  SER B CA  1 
ATOM   2830 C CA  B SER B 1 57  ? 13.293  -25.130 15.101  0.46 11.81  ? 282  SER B CA  1 
ATOM   2831 C C   A SER B 1 57  ? 13.802  -25.888 14.082  0.54 13.82  ? 282  SER B C   1 
ATOM   2832 C C   B SER B 1 57  ? 13.748  -25.810 13.814  0.46 12.75  ? 282  SER B C   1 
ATOM   2833 O O   A SER B 1 57  ? 13.990  -27.103 14.188  0.54 15.22  ? 282  SER B O   1 
ATOM   2834 O O   B SER B 1 57  ? 13.831  -27.040 13.781  0.46 11.53  ? 282  SER B O   1 
ATOM   2835 C CB  A SER B 1 57  ? 12.023  -25.788 15.848  0.54 13.56  ? 282  SER B CB  1 
ATOM   2836 C CB  B SER B 1 57  ? 12.057  -25.830 15.664  0.46 14.43  ? 282  SER B CB  1 
ATOM   2837 O OG  A SER B 1 57  ? 10.925  -25.642 14.969  0.54 12.16  ? 282  SER B OG  1 
ATOM   2838 O OG  B SER B 1 57  ? 11.803  -25.366 16.973  0.46 15.74  ? 282  SER B OG  1 
ATOM   2839 N N   A TRP B 1 58  ? 14.050  -25.230 12.948  0.54 12.36  ? 283  TRP B N   1 
ATOM   2840 N N   B TRP B 1 58  ? 14.044  -25.053 12.758  0.46 11.58  ? 283  TRP B N   1 
ATOM   2841 C CA  A TRP B 1 58  ? 14.743  -25.893 11.847  0.54 10.05  ? 283  TRP B CA  1 
ATOM   2842 C CA  B TRP B 1 58  ? 14.771  -25.648 11.642  0.46 10.76  ? 283  TRP B CA  1 
ATOM   2843 C C   A TRP B 1 58  ? 16.260  -25.797 11.959  0.54 9.56   ? 283  TRP B C   1 
ATOM   2844 C C   B TRP B 1 58  ? 16.270  -25.730 11.903  0.46 9.70   ? 283  TRP B C   1 
ATOM   2845 O O   A TRP B 1 58  ? 16.963  -26.410 11.147  0.54 11.30  ? 283  TRP B O   1 
ATOM   2846 O O   B TRP B 1 58  ? 16.972  -26.422 11.156  0.46 11.32  ? 283  TRP B O   1 
ATOM   2847 C CB  A TRP B 1 58  ? 14.289  -25.325 10.495  0.54 14.69  ? 283  TRP B CB  1 
ATOM   2848 C CB  B TRP B 1 58  ? 14.538  -24.862 10.346  0.46 12.22  ? 283  TRP B CB  1 
ATOM   2849 C CG  A TRP B 1 58  ? 13.155  -26.104 9.917   0.54 10.94  ? 283  TRP B CG  1 
ATOM   2850 C CG  B TRP B 1 58  ? 13.169  -24.985 9.765   0.46 15.66  ? 283  TRP B CG  1 
ATOM   2851 C CD1 A TRP B 1 58  ? 11.832  -25.760 9.917   0.54 13.23  ? 283  TRP B CD1 1 
ATOM   2852 C CD1 B TRP B 1 58  ? 12.299  -26.020 9.930   0.46 15.78  ? 283  TRP B CD1 1 
ATOM   2853 C CD2 A TRP B 1 58  ? 13.238  -27.385 9.281   0.54 14.19  ? 283  TRP B CD2 1 
ATOM   2854 C CD2 B TRP B 1 58  ? 12.508  -24.036 8.916   0.46 22.95  ? 283  TRP B CD2 1 
ATOM   2855 N NE1 A TRP B 1 58  ? 11.089  -26.746 9.311   0.54 14.58  ? 283  TRP B NE1 1 
ATOM   2856 N NE1 B TRP B 1 58  ? 11.135  -25.776 9.244   0.46 18.94  ? 283  TRP B NE1 1 
ATOM   2857 C CE2 A TRP B 1 58  ? 11.930  -27.751 8.905   0.54 12.77  ? 283  TRP B CE2 1 
ATOM   2858 C CE2 B TRP B 1 58  ? 11.237  -24.564 8.613   0.46 17.93  ? 283  TRP B CE2 1 
ATOM   2859 C CE3 A TRP B 1 58  ? 14.296  -28.248 8.975   0.54 19.70  ? 283  TRP B CE3 1 
ATOM   2860 C CE3 B TRP B 1 58  ? 12.861  -22.782 8.399   0.46 12.70  ? 283  TRP B CE3 1 
ATOM   2861 C CZ2 A TRP B 1 58  ? 11.649  -28.945 8.249   0.54 20.64  ? 283  TRP B CZ2 1 
ATOM   2862 C CZ2 B TRP B 1 58  ? 10.319  -23.892 7.804   0.46 18.01  ? 283  TRP B CZ2 1 
ATOM   2863 C CZ3 A TRP B 1 58  ? 14.014  -29.436 8.325   0.54 16.59  ? 283  TRP B CZ3 1 
ATOM   2864 C CZ3 B TRP B 1 58  ? 11.950  -22.120 7.597   0.46 26.05  ? 283  TRP B CZ3 1 
ATOM   2865 C CH2 A TRP B 1 58  ? 12.703  -29.773 7.971   0.54 21.19  ? 283  TRP B CH2 1 
ATOM   2866 C CH2 B TRP B 1 58  ? 10.691  -22.675 7.309   0.46 21.24  ? 283  TRP B CH2 1 
ATOM   2867 N N   . LEU B 1 59  ? 16.776  -25.033 12.924  1.00 11.34  ? 284  LEU B N   1 
ATOM   2868 C CA  . LEU B 1 59  ? 18.211  -25.036 13.196  1.00 11.04  ? 284  LEU B CA  1 
ATOM   2869 C C   . LEU B 1 59  ? 18.671  -26.448 13.549  1.00 11.63  ? 284  LEU B C   1 
ATOM   2870 O O   . LEU B 1 59  ? 18.080  -27.107 14.411  1.00 12.41  ? 284  LEU B O   1 
ATOM   2871 C CB  . LEU B 1 59  ? 18.528  -24.074 14.345  1.00 9.68   ? 284  LEU B CB  1 
ATOM   2872 C CG  . LEU B 1 59  ? 20.010  -23.946 14.711  1.00 10.11  ? 284  LEU B CG  1 
ATOM   2873 C CD1 . LEU B 1 59  ? 20.796  -23.373 13.534  1.00 11.28  ? 284  LEU B CD1 1 
ATOM   2874 C CD2 . LEU B 1 59  ? 20.182  -23.073 15.948  1.00 11.90  ? 284  LEU B CD2 1 
ATOM   2875 N N   . ASN B 1 60  ? 19.712  -26.921 12.855  1.00 12.54  ? 285  ASN B N   1 
ATOM   2876 C CA  . ASN B 1 60  ? 20.291  -28.251 13.058  1.00 10.45  ? 285  ASN B CA  1 
ATOM   2877 C C   . ASN B 1 60  ? 19.338  -29.377 12.674  1.00 13.75  ? 285  ASN B C   1 
ATOM   2878 O O   . ASN B 1 60  ? 19.565  -30.529 13.045  1.00 18.19  ? 285  ASN B O   1 
ATOM   2879 C CB  . ASN B 1 60  ? 20.762  -28.443 14.508  1.00 10.42  ? 285  ASN B CB  1 
ATOM   2880 C CG  . ASN B 1 60  ? 22.165  -27.941 14.723  1.00 14.87  ? 285  ASN B CG  1 
ATOM   2881 O OD1 . ASN B 1 60  ? 22.713  -27.251 13.874  1.00 16.67  ? 285  ASN B OD1 1 
ATOM   2882 N ND2 . ASN B 1 60  ? 22.769  -28.314 15.848  1.00 14.68  ? 285  ASN B ND2 1 
ATOM   2883 N N   . ARG B 1 61  ? 18.275  -29.078 11.932  1.00 10.47  ? 286  ARG B N   1 
ATOM   2884 C CA  . ARG B 1 61  ? 17.416  -30.115 11.379  1.00 10.52  ? 286  ARG B CA  1 
ATOM   2885 C C   . ARG B 1 61  ? 17.680  -30.243 9.882   1.00 15.01  ? 286  ARG B C   1 
ATOM   2886 O O   . ARG B 1 61  ? 18.134  -29.305 9.229   1.00 15.39  ? 286  ARG B O   1 
ATOM   2887 C CB  . ARG B 1 61  ? 15.933  -29.802 11.583  1.00 11.33  ? 286  ARG B CB  1 
ATOM   2888 C CG  . ARG B 1 61  ? 15.434  -29.486 12.997  1.00 24.57  ? 286  ARG B CG  1 
ATOM   2889 C CD  . ARG B 1 61  ? 16.227  -30.011 14.154  1.00 31.33  ? 286  ARG B CD  1 
ATOM   2890 N NE  . ARG B 1 61  ? 15.415  -30.023 15.372  1.00 25.99  ? 286  ARG B NE  1 
ATOM   2891 C CZ  . ARG B 1 61  ? 15.383  -29.065 16.296  1.00 39.44  ? 286  ARG B CZ  1 
ATOM   2892 N NH1 . ARG B 1 61  ? 16.125  -27.964 16.201  1.00 25.42  ? 286  ARG B NH1 1 
ATOM   2893 N NH2 . ARG B 1 61  ? 14.587  -29.217 17.352  1.00 35.26  ? 286  ARG B NH2 1 
ATOM   2894 N N   . PHE B 1 62  ? 17.374  -31.414 9.328   1.00 12.68  ? 287  PHE B N   1 
ATOM   2895 C CA  . PHE B 1 62  ? 17.560  -31.613 7.903   1.00 12.30  ? 287  PHE B CA  1 
ATOM   2896 C C   . PHE B 1 62  ? 16.490  -32.567 7.402   1.00 14.41  ? 287  PHE B C   1 
ATOM   2897 O O   . PHE B 1 62  ? 15.896  -33.330 8.169   1.00 13.32  ? 287  PHE B O   1 
ATOM   2898 C CB  . PHE B 1 62  ? 18.970  -32.150 7.586   1.00 13.11  ? 287  PHE B CB  1 
ATOM   2899 C CG  . PHE B 1 62  ? 19.289  -33.448 8.271   1.00 12.22  ? 287  PHE B CG  1 
ATOM   2900 C CD1 . PHE B 1 62  ? 18.940  -34.657 7.690   1.00 14.15  ? 287  PHE B CD1 1 
ATOM   2901 C CD2 . PHE B 1 62  ? 19.941  -33.453 9.499   1.00 12.86  ? 287  PHE B CD2 1 
ATOM   2902 C CE1 . PHE B 1 62  ? 19.222  -35.861 8.338   1.00 13.42  ? 287  PHE B CE1 1 
ATOM   2903 C CE2 . PHE B 1 62  ? 20.237  -34.647 10.154  1.00 16.11  ? 287  PHE B CE2 1 
ATOM   2904 C CZ  . PHE B 1 62  ? 19.875  -35.849 9.578   1.00 14.38  ? 287  PHE B CZ  1 
ATOM   2905 N N   . ARG B 1 63  ? 16.254  -32.520 6.097   1.00 13.93  ? 288  ARG B N   1 
ATOM   2906 C CA  . ARG B 1 63  ? 15.365  -33.494 5.490   1.00 11.57  ? 288  ARG B CA  1 
ATOM   2907 C C   . ARG B 1 63  ? 15.803  -33.739 4.058   1.00 13.02  ? 288  ARG B C   1 
ATOM   2908 O O   . ARG B 1 63  ? 16.457  -32.899 3.436   1.00 15.03  ? 288  ARG B O   1 
ATOM   2909 C CB  . ARG B 1 63  ? 13.903  -33.045 5.569   1.00 18.00  ? 288  ARG B CB  1 
ATOM   2910 C CG  . ARG B 1 63  ? 13.574  -31.828 4.764   1.00 21.14  ? 288  ARG B CG  1 
ATOM   2911 C CD  . ARG B 1 63  ? 12.069  -31.540 4.864   1.00 21.67  ? 288  ARG B CD  1 
ATOM   2912 N NE  . ARG B 1 63  ? 11.260  -32.606 4.279   1.00 29.56  ? 288  ARG B NE  1 
ATOM   2913 C CZ  . ARG B 1 63  ? 9.939   -32.568 4.164   1.00 41.35  ? 288  ARG B CZ  1 
ATOM   2914 N NH1 . ARG B 1 63  ? 9.235   -31.545 4.619   1.00 36.63  ? 288  ARG B NH1 1 
ATOM   2915 N NH2 . ARG B 1 63  ? 9.310   -33.581 3.573   1.00 48.46  ? 288  ARG B NH2 1 
ATOM   2916 N N   . GLY B 1 64  ? 15.481  -34.920 3.563   1.00 14.08  ? 289  GLY B N   1 
ATOM   2917 C CA  . GLY B 1 64  ? 15.907  -35.295 2.238   1.00 12.01  ? 289  GLY B CA  1 
ATOM   2918 C C   . GLY B 1 64  ? 15.303  -36.619 1.859   1.00 12.62  ? 289  GLY B C   1 
ATOM   2919 O O   . GLY B 1 64  ? 14.335  -37.070 2.473   1.00 15.18  ? 289  GLY B O   1 
ATOM   2920 N N   . VAL B 1 65  ? 15.884  -37.235 0.836   1.00 13.51  ? 290  VAL B N   1 
ATOM   2921 C CA  . VAL B 1 65  ? 15.416  -38.521 0.339   1.00 15.64  ? 290  VAL B CA  1 
ATOM   2922 C C   . VAL B 1 65  ? 16.627  -39.411 0.085   1.00 16.93  ? 290  VAL B C   1 
ATOM   2923 O O   . VAL B 1 65  ? 17.647  -38.957 -0.445  1.00 14.10  ? 290  VAL B O   1 
ATOM   2924 C CB  . VAL B 1 65  ? 14.553  -38.354 -0.935  1.00 14.12  ? 290  VAL B CB  1 
ATOM   2925 C CG1 . VAL B 1 65  ? 15.358  -37.700 -2.067  1.00 14.80  ? 290  VAL B CG1 1 
ATOM   2926 C CG2 . VAL B 1 65  ? 13.995  -39.698 -1.389  1.00 15.44  ? 290  VAL B CG2 1 
ATOM   2927 N N   . SER B 1 66  ? 16.525  -40.680 0.478   1.00 14.73  ? 291  SER B N   1 
ATOM   2928 C CA  . SER B 1 66  ? 17.629  -41.602 0.250   1.00 14.57  ? 291  SER B CA  1 
ATOM   2929 C C   . SER B 1 66  ? 17.840  -41.819 -1.243  1.00 17.98  ? 291  SER B C   1 
ATOM   2930 O O   . SER B 1 66  ? 16.888  -42.040 -1.995  1.00 17.32  ? 291  SER B O   1 
ATOM   2931 C CB  . SER B 1 66  ? 17.354  -42.938 0.939   1.00 14.85  ? 291  SER B CB  1 
ATOM   2932 O OG  . SER B 1 66  ? 16.190  -43.537 0.398   1.00 15.36  ? 291  SER B OG  1 
ATOM   2933 N N   . THR B 1 67  ? 19.103  -41.761 -1.672  1.00 19.22  ? 292  THR B N   1 
ATOM   2934 C CA  . THR B 1 67  ? 19.458  -41.997 -3.067  1.00 24.76  ? 292  THR B CA  1 
ATOM   2935 C C   . THR B 1 67  ? 19.706  -43.469 -3.363  1.00 25.10  ? 292  THR B C   1 
ATOM   2936 O O   . THR B 1 67  ? 19.641  -43.882 -4.528  1.00 27.31  ? 292  THR B O   1 
ATOM   2937 C CB  . THR B 1 67  ? 20.709  -41.192 -3.427  1.00 23.47  ? 292  THR B CB  1 
ATOM   2938 O OG1 . THR B 1 67  ? 21.860  -41.874 -2.925  1.00 36.32  ? 292  THR B OG1 1 
ATOM   2939 C CG2 . THR B 1 67  ? 20.657  -39.836 -2.772  1.00 28.56  ? 292  THR B CG2 1 
ATOM   2940 N N   . ALA B 1 68  ? 19.974  -44.263 -2.331  1.00 24.80  ? 293  ALA B N   1 
ATOM   2941 C CA  . ALA B 1 68  ? 20.181  -45.694 -2.450  1.00 19.05  ? 293  ALA B CA  1 
ATOM   2942 C C   . ALA B 1 68  ? 19.754  -46.342 -1.145  1.00 23.87  ? 293  ALA B C   1 
ATOM   2943 O O   . ALA B 1 68  ? 19.654  -45.682 -0.108  1.00 25.14  ? 293  ALA B O   1 
ATOM   2944 C CB  . ALA B 1 68  ? 21.643  -46.027 -2.767  1.00 20.28  ? 293  ALA B CB  1 
ATOM   2945 N N   . ALA B 1 69  ? 19.490  -47.639 -1.203  1.00 23.53  ? 294  ALA B N   1 
ATOM   2946 C CA  . ALA B 1 69  ? 19.252  -48.379 0.023   1.00 25.02  ? 294  ALA B CA  1 
ATOM   2947 C C   . ALA B 1 69  ? 20.505  -48.357 0.885   1.00 23.62  ? 294  ALA B C   1 
ATOM   2948 O O   . ALA B 1 69  ? 21.632  -48.298 0.382   1.00 23.39  ? 294  ALA B O   1 
ATOM   2949 C CB  . ALA B 1 69  ? 18.849  -49.822 -0.283  1.00 30.36  ? 294  ALA B CB  1 
ATOM   2950 N N   . VAL B 1 70  ? 20.295  -48.390 2.201   1.00 21.16  ? 295  VAL B N   1 
ATOM   2951 C CA  . VAL B 1 70  ? 21.413  -48.407 3.133   1.00 18.26  ? 295  VAL B CA  1 
ATOM   2952 C C   . VAL B 1 70  ? 22.257  -49.651 2.898   1.00 23.79  ? 295  VAL B C   1 
ATOM   2953 O O   . VAL B 1 70  ? 21.736  -50.755 2.682   1.00 25.58  ? 295  VAL B O   1 
ATOM   2954 C CB  . VAL B 1 70  ? 20.894  -48.350 4.580   1.00 18.65  ? 295  VAL B CB  1 
ATOM   2955 C CG1 . VAL B 1 70  ? 21.987  -48.717 5.560   1.00 23.07  ? 295  VAL B CG1 1 
ATOM   2956 C CG2 . VAL B 1 70  ? 20.354  -46.963 4.887   1.00 22.63  ? 295  VAL B CG2 1 
ATOM   2957 N N   . ALA B 1 71  ? 23.573  -49.467 2.916   1.00 20.72  ? 296  ALA B N   1 
ATOM   2958 C CA  . ALA B 1 71  ? 24.504  -50.572 2.757   1.00 25.63  ? 296  ALA B CA  1 
ATOM   2959 C C   . ALA B 1 71  ? 25.815  -50.197 3.427   1.00 25.71  ? 296  ALA B C   1 
ATOM   2960 O O   . ALA B 1 71  ? 26.280  -49.062 3.291   1.00 21.48  ? 296  ALA B O   1 
ATOM   2961 C CB  . ALA B 1 71  ? 24.734  -50.905 1.275   1.00 27.65  ? 296  ALA B CB  1 
ATOM   2962 N N   . ASN B 1 72  ? 26.399  -51.156 4.152   1.00 22.89  ? 297  ASN B N   1 
ATOM   2963 C CA  . ASN B 1 72  ? 27.690  -50.965 4.815   1.00 21.48  ? 297  ASN B CA  1 
ATOM   2964 C C   . ASN B 1 72  ? 27.684  -49.722 5.702   1.00 17.75  ? 297  ASN B C   1 
ATOM   2965 O O   . ASN B 1 72  ? 28.635  -48.938 5.714   1.00 22.37  ? 297  ASN B O   1 
ATOM   2966 C CB  . ASN B 1 72  ? 28.823  -50.887 3.795   1.00 24.88  ? 297  ASN B CB  1 
ATOM   2967 C CG  . ASN B 1 72  ? 28.758  -52.000 2.775   1.00 49.98  ? 297  ASN B CG  1 
ATOM   2968 O OD1 . ASN B 1 72  ? 28.643  -53.172 3.131   1.00 56.50  ? 297  ASN B OD1 1 
ATOM   2969 N ND2 . ASN B 1 72  ? 28.813  -51.638 1.493   1.00 45.81  ? 297  ASN B ND2 1 
ATOM   2970 N N   . GLN B 1 73  ? 26.582  -49.533 6.435   1.00 18.07  ? 298  GLN B N   1 
ATOM   2971 C CA  . GLN B 1 73  ? 26.409  -48.418 7.369   1.00 19.14  ? 298  GLN B CA  1 
ATOM   2972 C C   . GLN B 1 73  ? 26.547  -47.060 6.684   1.00 20.53  ? 298  GLN B C   1 
ATOM   2973 O O   . GLN B 1 73  ? 26.940  -46.073 7.310   1.00 17.04  ? 298  GLN B O   1 
ATOM   2974 C CB  . GLN B 1 73  ? 27.378  -48.526 8.552   1.00 21.16  ? 298  GLN B CB  1 
ATOM   2975 C CG  . GLN B 1 73  ? 27.236  -49.839 9.306   1.00 19.12  ? 298  GLN B CG  1 
ATOM   2976 C CD  . GLN B 1 73  ? 27.775  -49.773 10.722  1.00 40.25  ? 298  GLN B CD  1 
ATOM   2977 O OE1 . GLN B 1 73  ? 28.544  -48.877 11.068  1.00 35.53  ? 298  GLN B OE1 1 
ATOM   2978 N NE2 . GLN B 1 73  ? 27.358  -50.719 11.556  1.00 69.47  ? 298  GLN B NE2 1 
ATOM   2979 N N   . VAL B 1 74  ? 26.185  -46.979 5.406   1.00 18.29  ? 299  VAL B N   1 
ATOM   2980 C CA  . VAL B 1 74  ? 26.202  -45.722 4.669   1.00 17.09  ? 299  VAL B CA  1 
ATOM   2981 C C   . VAL B 1 74  ? 24.787  -45.400 4.209   1.00 17.29  ? 299  VAL B C   1 
ATOM   2982 O O   . VAL B 1 74  ? 24.112  -46.256 3.621   1.00 18.57  ? 299  VAL B O   1 
ATOM   2983 C CB  . VAL B 1 74  ? 27.151  -45.786 3.464   1.00 19.93  ? 299  VAL B CB  1 
ATOM   2984 C CG1 . VAL B 1 74  ? 26.990  -44.540 2.594   1.00 18.92  ? 299  VAL B CG1 1 
ATOM   2985 C CG2 . VAL B 1 74  ? 28.590  -45.963 3.939   1.00 19.72  ? 299  VAL B CG2 1 
ATOM   2986 N N   . LEU B 1 75  ? 24.361  -44.160 4.457   1.00 17.11  ? 300  LEU B N   1 
ATOM   2987 C CA  . LEU B 1 75  ? 23.087  -43.622 3.985   1.00 16.21  ? 300  LEU B CA  1 
ATOM   2988 C C   . LEU B 1 75  ? 23.377  -42.334 3.225   1.00 16.70  ? 300  LEU B C   1 
ATOM   2989 O O   . LEU B 1 75  ? 23.869  -41.368 3.817   1.00 16.17  ? 300  LEU B O   1 
ATOM   2990 C CB  . LEU B 1 75  ? 22.139  -43.346 5.164   1.00 14.72  ? 300  LEU B CB  1 
ATOM   2991 C CG  . LEU B 1 75  ? 20.849  -42.537 4.893   1.00 16.17  ? 300  LEU B CG  1 
ATOM   2992 C CD1 . LEU B 1 75  ? 19.955  -43.214 3.853   1.00 18.41  ? 300  LEU B CD1 1 
ATOM   2993 C CD2 . LEU B 1 75  ? 20.073  -42.310 6.181   1.00 12.95  ? 300  LEU B CD2 1 
ATOM   2994 N N   A HIS B 1 76  ? 23.096  -42.305 1.924   0.51 16.24  ? 301  HIS B N   1 
ATOM   2995 N N   B HIS B 1 76  ? 23.072  -42.332 1.924   0.49 16.13  ? 301  HIS B N   1 
ATOM   2996 C CA  A HIS B 1 76  ? 23.259  -41.066 1.170   0.51 15.80  ? 301  HIS B CA  1 
ATOM   2997 C CA  B HIS B 1 76  ? 23.182  -41.148 1.077   0.49 16.23  ? 301  HIS B CA  1 
ATOM   2998 C C   A HIS B 1 76  ? 21.901  -40.419 0.955   0.51 14.54  ? 301  HIS B C   1 
ATOM   2999 C C   B HIS B 1 76  ? 21.829  -40.447 1.024   0.49 14.55  ? 301  HIS B C   1 
ATOM   3000 O O   A HIS B 1 76  ? 20.972  -41.057 0.448   0.51 14.76  ? 301  HIS B O   1 
ATOM   3001 O O   B HIS B 1 76  ? 20.821  -41.076 0.690   0.49 15.55  ? 301  HIS B O   1 
ATOM   3002 C CB  A HIS B 1 76  ? 23.950  -41.264 -0.181  0.51 21.26  ? 301  HIS B CB  1 
ATOM   3003 C CB  B HIS B 1 76  ? 23.608  -41.525 -0.348  0.49 18.48  ? 301  HIS B CB  1 
ATOM   3004 C CG  A HIS B 1 76  ? 24.387  -39.972 -0.807  0.51 21.70  ? 301  HIS B CG  1 
ATOM   3005 C CG  B HIS B 1 76  ? 24.967  -42.151 -0.452  0.49 19.85  ? 301  HIS B CG  1 
ATOM   3006 N ND1 A HIS B 1 76  ? 23.528  -39.161 -1.518  0.51 27.47  ? 301  HIS B ND1 1 
ATOM   3007 N ND1 B HIS B 1 76  ? 26.102  -41.421 -0.739  0.49 19.94  ? 301  HIS B ND1 1 
ATOM   3008 C CD2 A HIS B 1 76  ? 25.577  -39.324 -0.782  0.51 25.17  ? 301  HIS B CD2 1 
ATOM   3009 C CD2 B HIS B 1 76  ? 25.367  -43.441 -0.356  0.49 20.57  ? 301  HIS B CD2 1 
ATOM   3010 C CE1 A HIS B 1 76  ? 24.173  -38.081 -1.921  0.51 16.04  ? 301  HIS B CE1 1 
ATOM   3011 C CE1 B HIS B 1 76  ? 27.144  -42.232 -0.789  0.49 15.65  ? 301  HIS B CE1 1 
ATOM   3012 N NE2 A HIS B 1 76  ? 25.420  -38.157 -1.489  0.51 27.55  ? 301  HIS B NE2 1 
ATOM   3013 N NE2 B HIS B 1 76  ? 26.726  -43.463 -0.560  0.49 19.60  ? 301  HIS B NE2 1 
ATOM   3014 N N   . LEU B 1 77  ? 21.803  -39.153 1.339   1.00 13.33  ? 302  LEU B N   1 
ATOM   3015 C CA  . LEU B 1 77  ? 20.581  -38.364 1.247   1.00 15.55  ? 302  LEU B CA  1 
ATOM   3016 C C   . LEU B 1 77  ? 20.755  -37.256 0.224   1.00 21.09  ? 302  LEU B C   1 
ATOM   3017 O O   . LEU B 1 77  ? 21.717  -36.484 0.296   1.00 20.16  ? 302  LEU B O   1 
ATOM   3018 C CB  . LEU B 1 77  ? 20.208  -37.718 2.577   1.00 16.40  ? 302  LEU B CB  1 
ATOM   3019 C CG  . LEU B 1 77  ? 19.633  -38.560 3.714   1.00 21.89  ? 302  LEU B CG  1 
ATOM   3020 C CD1 . LEU B 1 77  ? 19.307  -37.644 4.882   1.00 22.74  ? 302  LEU B CD1 1 
ATOM   3021 C CD2 . LEU B 1 77  ? 18.396  -39.322 3.241   1.00 23.60  ? 302  LEU B CD2 1 
ATOM   3022 N N   . THR B 1 78  ? 19.819  -37.170 -0.706  1.00 14.91  ? 303  THR B N   1 
ATOM   3023 C CA  . THR B 1 78  ? 19.652  -35.960 -1.500  1.00 13.34  ? 303  THR B CA  1 
ATOM   3024 C C   . THR B 1 78  ? 18.843  -34.972 -0.673  1.00 13.60  ? 303  THR B C   1 
ATOM   3025 O O   . THR B 1 78  ? 17.792  -35.326 -0.143  1.00 14.78  ? 303  THR B O   1 
ATOM   3026 C CB  . THR B 1 78  ? 18.939  -36.282 -2.806  1.00 15.16  ? 303  THR B CB  1 
ATOM   3027 O OG1 . THR B 1 78  ? 19.797  -37.096 -3.619  1.00 19.71  ? 303  THR B OG1 1 
ATOM   3028 C CG2 . THR B 1 78  ? 18.588  -34.999 -3.568  1.00 16.63  ? 303  THR B CG2 1 
ATOM   3029 N N   . LEU B 1 79  ? 19.332  -33.742 -0.541  1.00 13.69  ? 304  LEU B N   1 
ATOM   3030 C CA  . LEU B 1 79  ? 18.761  -32.834 0.442   1.00 13.44  ? 304  LEU B CA  1 
ATOM   3031 C C   . LEU B 1 79  ? 17.577  -32.040 -0.105  1.00 12.07  ? 304  LEU B C   1 
ATOM   3032 O O   . LEU B 1 79  ? 17.540  -31.664 -1.277  1.00 13.27  ? 304  LEU B O   1 
ATOM   3033 C CB  . LEU B 1 79  ? 19.826  -31.860 0.950   1.00 13.30  ? 304  LEU B CB  1 
ATOM   3034 C CG  . LEU B 1 79  ? 20.897  -32.496 1.826   1.00 17.71  ? 304  LEU B CG  1 
ATOM   3035 C CD1 . LEU B 1 79  ? 22.074  -31.530 2.008   1.00 15.85  ? 304  LEU B CD1 1 
ATOM   3036 C CD2 . LEU B 1 79  ? 20.291  -32.911 3.174   1.00 14.01  ? 304  LEU B CD2 1 
ATOM   3037 N N   . TYR B 1 80  ? 16.615  -31.789 0.780   1.00 12.27  ? 305  TYR B N   1 
ATOM   3038 C CA  . TYR B 1 80  ? 15.519  -30.849 0.583   1.00 11.69  ? 305  TYR B CA  1 
ATOM   3039 C C   . TYR B 1 80  ? 15.725  -29.620 1.472   1.00 14.37  ? 305  TYR B C   1 
ATOM   3040 O O   . TYR B 1 80  ? 16.537  -29.628 2.397   1.00 14.71  ? 305  TYR B O   1 
ATOM   3041 C CB  . TYR B 1 80  ? 14.171  -31.490 0.945   1.00 15.39  ? 305  TYR B CB  1 
ATOM   3042 C CG  . TYR B 1 80  ? 13.737  -32.664 0.100   1.00 17.33  ? 305  TYR B CG  1 
ATOM   3043 C CD1 . TYR B 1 80  ? 14.366  -32.963 -1.101  1.00 12.89  ? 305  TYR B CD1 1 
ATOM   3044 C CD2 . TYR B 1 80  ? 12.676  -33.462 0.502   1.00 22.57  ? 305  TYR B CD2 1 
ATOM   3045 C CE1 . TYR B 1 80  ? 13.941  -34.046 -1.884  1.00 20.79  ? 305  TYR B CE1 1 
ATOM   3046 C CE2 . TYR B 1 80  ? 12.249  -34.528 -0.259  1.00 21.08  ? 305  TYR B CE2 1 
ATOM   3047 C CZ  . TYR B 1 80  ? 12.878  -34.819 -1.441  1.00 20.88  ? 305  TYR B CZ  1 
ATOM   3048 O OH  . TYR B 1 80  ? 12.426  -35.888 -2.189  1.00 20.89  ? 305  TYR B OH  1 
ATOM   3049 N N   A GLU B 1 81  ? 15.001  -28.546 1.170   0.59 15.18  ? 306  GLU B N   1 
ATOM   3050 N N   B GLU B 1 81  ? 14.982  -28.556 1.158   0.41 15.27  ? 306  GLU B N   1 
ATOM   3051 C CA  A GLU B 1 81  ? 14.913  -27.435 2.107   0.59 18.04  ? 306  GLU B CA  1 
ATOM   3052 C CA  B GLU B 1 81  ? 14.849  -27.415 2.050   0.41 18.19  ? 306  GLU B CA  1 
ATOM   3053 C C   A GLU B 1 81  ? 13.874  -27.771 3.163   0.59 24.20  ? 306  GLU B C   1 
ATOM   3054 C C   B GLU B 1 81  ? 13.839  -27.754 3.142   0.41 24.15  ? 306  GLU B C   1 
ATOM   3055 O O   A GLU B 1 81  ? 13.110  -28.730 3.013   0.59 23.56  ? 306  GLU B O   1 
ATOM   3056 O O   B GLU B 1 81  ? 13.066  -28.707 3.000   0.41 23.50  ? 306  GLU B O   1 
ATOM   3057 C CB  A GLU B 1 81  ? 14.558  -26.135 1.382   0.59 17.35  ? 306  GLU B CB  1 
ATOM   3058 C CB  B GLU B 1 81  ? 14.403  -26.176 1.267   0.41 17.88  ? 306  GLU B CB  1 
ATOM   3059 C CG  A GLU B 1 81  ? 15.691  -25.517 0.563   0.59 23.88  ? 306  GLU B CG  1 
ATOM   3060 C CG  B GLU B 1 81  ? 15.272  -25.849 0.036   0.41 19.33  ? 306  GLU B CG  1 
ATOM   3061 C CD  A GLU B 1 81  ? 16.634  -24.602 1.359   0.59 19.35  ? 306  GLU B CD  1 
ATOM   3062 C CD  B GLU B 1 81  ? 14.900  -24.529 -0.641  0.41 27.16  ? 306  GLU B CD  1 
ATOM   3063 O OE1 A GLU B 1 81  ? 16.574  -24.544 2.605   0.59 14.26  ? 306  GLU B OE1 1 
ATOM   3064 O OE1 B GLU B 1 81  ? 13.847  -23.955 -0.294  0.41 26.75  ? 306  GLU B OE1 1 
ATOM   3065 O OE2 A GLU B 1 81  ? 17.459  -23.934 0.708   0.59 28.40  ? 306  GLU B OE2 1 
ATOM   3066 O OE2 B GLU B 1 81  ? 15.663  -24.066 -1.523  0.41 19.97  ? 306  GLU B OE2 1 
ATOM   3067 N N   . PRO B 1 82  ? 13.849  -27.017 4.264   1.00 24.81  ? 307  PRO B N   1 
ATOM   3068 C CA  . PRO B 1 82  ? 12.818  -27.243 5.297   1.00 28.54  ? 307  PRO B CA  1 
ATOM   3069 C C   . PRO B 1 82  ? 11.387  -27.362 4.790   1.00 26.71  ? 307  PRO B C   1 
ATOM   3070 O O   . PRO B 1 82  ? 10.622  -28.167 5.334   1.00 31.74  ? 307  PRO B O   1 
ATOM   3071 C CB  . PRO B 1 82  ? 12.983  -26.012 6.193   1.00 22.91  ? 307  PRO B CB  1 
ATOM   3072 C CG  . PRO B 1 82  ? 14.453  -25.731 6.154   1.00 20.47  ? 307  PRO B CG  1 
ATOM   3073 C CD  . PRO B 1 82  ? 14.920  -26.124 4.753   1.00 24.65  ? 307  PRO B CD  1 
ATOM   3074 N N   . ASP B 1 83  ? 10.995  -26.598 3.769   1.00 29.90  ? 308  ASP B N   1 
ATOM   3075 C CA  . ASP B 1 83  ? 9.618   -26.654 3.300   1.00 40.86  ? 308  ASP B CA  1 
ATOM   3076 C C   . ASP B 1 83  ? 9.341   -27.863 2.413   1.00 50.01  ? 308  ASP B C   1 
ATOM   3077 O O   . ASP B 1 83  ? 8.280   -27.922 1.782   1.00 43.79  ? 308  ASP B O   1 
ATOM   3078 C CB  . ASP B 1 83  ? 9.250   -25.361 2.562   1.00 36.27  ? 308  ASP B CB  1 
ATOM   3079 C CG  . ASP B 1 83  ? 10.043  -25.158 1.276   1.00 56.08  ? 308  ASP B CG  1 
ATOM   3080 O OD1 . ASP B 1 83  ? 10.973  -25.944 0.992   1.00 44.38  ? 308  ASP B OD1 1 
ATOM   3081 O OD2 . ASP B 1 83  ? 9.730   -24.196 0.543   1.00 63.11  ? 308  ASP B OD2 1 
ATOM   3082 N N   . GLY B 1 84  ? 10.262  -28.825 2.350   1.00 40.07  ? 309  GLY B N   1 
ATOM   3083 C CA  . GLY B 1 84  ? 10.095  -29.987 1.512   1.00 25.83  ? 309  GLY B CA  1 
ATOM   3084 C C   . GLY B 1 84  ? 10.390  -29.772 0.046   1.00 30.83  ? 309  GLY B C   1 
ATOM   3085 O O   . GLY B 1 84  ? 10.387  -30.749 -0.711  1.00 30.50  ? 309  GLY B O   1 
ATOM   3086 N N   . SER B 1 85  ? 10.629  -28.534 -0.384  1.00 32.63  ? 310  SER B N   1 
ATOM   3087 C CA  . SER B 1 85  ? 11.111  -28.298 -1.736  1.00 29.13  ? 310  SER B CA  1 
ATOM   3088 C C   . SER B 1 85  ? 12.545  -28.797 -1.880  1.00 30.84  ? 310  SER B C   1 
ATOM   3089 O O   . SER B 1 85  ? 13.293  -28.913 -0.904  1.00 23.80  ? 310  SER B O   1 
ATOM   3090 C CB  . SER B 1 85  ? 11.035  -26.813 -2.098  1.00 33.58  ? 310  SER B CB  1 
ATOM   3091 O OG  . SER B 1 85  ? 11.778  -26.013 -1.198  1.00 46.26  ? 310  SER B OG  1 
ATOM   3092 N N   . VAL B 1 86  ? 12.921  -29.101 -3.114  1.00 28.90  ? 311  VAL B N   1 
ATOM   3093 C CA  . VAL B 1 86  ? 14.244  -29.648 -3.389  1.00 24.98  ? 311  VAL B CA  1 
ATOM   3094 C C   . VAL B 1 86  ? 15.279  -28.537 -3.283  1.00 24.49  ? 311  VAL B C   1 
ATOM   3095 O O   . VAL B 1 86  ? 15.060  -27.408 -3.729  1.00 30.89  ? 311  VAL B O   1 
ATOM   3096 C CB  . VAL B 1 86  ? 14.278  -30.327 -4.768  1.00 35.57  ? 311  VAL B CB  1 
ATOM   3097 C CG2 . VAL B 1 86  ? 13.607  -31.697 -4.689  1.00 25.37  ? 311  VAL B CG2 1 
ATOM   3098 N N   . PHE B 1 87  ? 16.395  -28.850 -2.644  1.00 22.87  ? 312  PHE B N   1 
ATOM   3099 C CA  . PHE B 1 87  ? 17.508  -27.918 -2.523  1.00 18.36  ? 312  PHE B CA  1 
ATOM   3100 C C   . PHE B 1 87  ? 18.314  -27.977 -3.812  1.00 19.96  ? 312  PHE B C   1 
ATOM   3101 O O   . PHE B 1 87  ? 18.851  -29.033 -4.154  1.00 21.22  ? 312  PHE B O   1 
ATOM   3102 C CB  . PHE B 1 87  ? 18.365  -28.304 -1.319  1.00 15.88  ? 312  PHE B CB  1 
ATOM   3103 C CG  . PHE B 1 87  ? 19.613  -27.487 -1.174  1.00 13.02  ? 312  PHE B CG  1 
ATOM   3104 C CD1 . PHE B 1 87  ? 19.558  -26.210 -0.633  1.00 17.62  ? 312  PHE B CD1 1 
ATOM   3105 C CD2 . PHE B 1 87  ? 20.837  -27.994 -1.571  1.00 18.60  ? 312  PHE B CD2 1 
ATOM   3106 C CE1 . PHE B 1 87  ? 20.709  -25.454 -0.509  1.00 14.17  ? 312  PHE B CE1 1 
ATOM   3107 C CE2 . PHE B 1 87  ? 21.983  -27.247 -1.449  1.00 19.02  ? 312  PHE B CE2 1 
ATOM   3108 C CZ  . PHE B 1 87  ? 21.924  -25.978 -0.901  1.00 15.27  ? 312  PHE B CZ  1 
ATOM   3109 N N   . ASN B 1 88  ? 18.387  -26.859 -4.541  1.00 20.76  ? 313  ASN B N   1 
ATOM   3110 C CA  . ASN B 1 88  ? 19.063  -26.848 -5.831  1.00 15.44  ? 313  ASN B CA  1 
ATOM   3111 C C   . ASN B 1 88  ? 20.538  -26.541 -5.619  1.00 16.14  ? 313  ASN B C   1 
ATOM   3112 O O   . ASN B 1 88  ? 20.877  -25.403 -5.260  1.00 19.14  ? 313  ASN B O   1 
ATOM   3113 C CB  . ASN B 1 88  ? 18.432  -25.821 -6.766  1.00 21.15  ? 313  ASN B CB  1 
ATOM   3114 C CG  . ASN B 1 88  ? 18.989  -25.896 -8.179  1.00 21.05  ? 313  ASN B CG  1 
ATOM   3115 O OD1 . ASN B 1 88  ? 20.010  -26.542 -8.435  1.00 22.49  ? 313  ASN B OD1 1 
ATOM   3116 N ND2 . ASN B 1 88  ? 18.311  -25.233 -9.114  1.00 35.68  ? 313  ASN B ND2 1 
ATOM   3117 N N   . PRO B 1 89  ? 21.443  -27.503 -5.826  1.00 18.34  ? 314  PRO B N   1 
ATOM   3118 C CA  . PRO B 1 89  ? 22.862  -27.273 -5.533  1.00 16.50  ? 314  PRO B CA  1 
ATOM   3119 C C   . PRO B 1 89  ? 23.560  -26.403 -6.547  1.00 22.27  ? 314  PRO B C   1 
ATOM   3120 O O   . PRO B 1 89  ? 24.727  -26.051 -6.334  1.00 25.25  ? 314  PRO B O   1 
ATOM   3121 C CB  . PRO B 1 89  ? 23.448  -28.689 -5.550  1.00 19.27  ? 314  PRO B CB  1 
ATOM   3122 C CG  . PRO B 1 89  ? 22.594  -29.408 -6.533  1.00 25.02  ? 314  PRO B CG  1 
ATOM   3123 C CD  . PRO B 1 89  ? 21.203  -28.870 -6.327  1.00 21.67  ? 314  PRO B CD  1 
ATOM   3124 N N   . LEU B 1 90  ? 22.904  -26.073 -7.652  1.00 19.27  ? 315  LEU B N   1 
ATOM   3125 C CA  . LEU B 1 90  ? 23.465  -25.172 -8.638  1.00 19.56  ? 315  LEU B CA  1 
ATOM   3126 C C   . LEU B 1 90  ? 23.152  -23.712 -8.338  1.00 30.66  ? 315  LEU B C   1 
ATOM   3127 O O   . LEU B 1 90  ? 23.623  -22.835 -9.062  1.00 32.26  ? 315  LEU B O   1 
ATOM   3128 C CB  . LEU B 1 90  ? 22.956  -25.549 -10.037 1.00 19.59  ? 315  LEU B CB  1 
ATOM   3129 C CG  . LEU B 1 90  ? 23.303  -26.988 -10.442 1.00 29.50  ? 315  LEU B CG  1 
ATOM   3130 C CD1 . LEU B 1 90  ? 22.777  -27.301 -11.823 1.00 25.18  ? 315  LEU B CD1 1 
ATOM   3131 C CD2 . LEU B 1 90  ? 24.804  -27.218 -10.381 1.00 26.65  ? 315  LEU B CD2 1 
ATOM   3132 N N   . SER B 1 91  ? 22.412  -23.429 -7.271  1.00 23.30  ? 316  SER B N   1 
ATOM   3133 C CA  . SER B 1 91  ? 21.938  -22.075 -7.008  1.00 22.17  ? 316  SER B CA  1 
ATOM   3134 C C   . SER B 1 91  ? 22.950  -21.192 -6.283  1.00 20.83  ? 316  SER B C   1 
ATOM   3135 O O   . SER B 1 91  ? 22.753  -19.973 -6.236  1.00 29.51  ? 316  SER B O   1 
ATOM   3136 C CB  . SER B 1 91  ? 20.656  -22.115 -6.176  1.00 21.70  ? 316  SER B CB  1 
ATOM   3137 O OG  . SER B 1 91  ? 20.930  -22.566 -4.856  1.00 37.25  ? 316  SER B OG  1 
ATOM   3138 N N   . GLY B 1 92  ? 24.006  -21.756 -5.704  1.00 20.26  ? 317  GLY B N   1 
ATOM   3139 C CA  . GLY B 1 92  ? 24.981  -20.969 -4.971  1.00 17.68  ? 317  GLY B CA  1 
ATOM   3140 C C   . GLY B 1 92  ? 24.760  -20.906 -3.474  1.00 14.78  ? 317  GLY B C   1 
ATOM   3141 O O   . GLY B 1 92  ? 25.578  -20.298 -2.768  1.00 18.18  ? 317  GLY B O   1 
ATOM   3142 N N   . ALA B 1 93  ? 23.685  -21.492 -2.966  1.00 15.98  ? 318  ALA B N   1 
ATOM   3143 C CA  . ALA B 1 93  ? 23.502  -21.532 -1.525  1.00 14.13  ? 318  ALA B CA  1 
ATOM   3144 C C   . ALA B 1 93  ? 24.503  -22.507 -0.910  1.00 14.66  ? 318  ALA B C   1 
ATOM   3145 O O   . ALA B 1 93  ? 24.804  -23.545 -1.508  1.00 15.56  ? 318  ALA B O   1 
ATOM   3146 C CB  . ALA B 1 93  ? 22.071  -21.937 -1.166  1.00 16.94  ? 318  ALA B CB  1 
ATOM   3147 N N   . PRO B 1 94  ? 25.054  -22.194 0.269   1.00 15.03  ? 319  PRO B N   1 
ATOM   3148 C CA  . PRO B 1 94  ? 26.035  -23.106 0.877   1.00 15.86  ? 319  PRO B CA  1 
ATOM   3149 C C   . PRO B 1 94  ? 25.429  -24.386 1.424   1.00 15.05  ? 319  PRO B C   1 
ATOM   3150 O O   . PRO B 1 94  ? 26.136  -25.398 1.513   1.00 13.80  ? 319  PRO B O   1 
ATOM   3151 C CB  . PRO B 1 94  ? 26.651  -22.262 2.007   1.00 17.08  ? 319  PRO B CB  1 
ATOM   3152 C CG  . PRO B 1 94  ? 25.607  -21.235 2.330   1.00 14.53  ? 319  PRO B CG  1 
ATOM   3153 C CD  . PRO B 1 94  ? 24.935  -20.923 1.005   1.00 12.37  ? 319  PRO B CD  1 
ATOM   3154 N N   . ALA B 1 95  ? 24.154  -24.373 1.789   1.00 13.27  ? 320  ALA B N   1 
ATOM   3155 C CA  . ALA B 1 95  ? 23.503  -25.491 2.461   1.00 12.65  ? 320  ALA B CA  1 
ATOM   3156 C C   . ALA B 1 95  ? 22.022  -25.168 2.578   1.00 14.13  ? 320  ALA B C   1 
ATOM   3157 O O   . ALA B 1 95  ? 21.630  -24.009 2.418   1.00 12.90  ? 320  ALA B O   1 
ATOM   3158 C CB  . ALA B 1 95  ? 24.102  -25.731 3.860   1.00 10.24  ? 320  ALA B CB  1 
ATOM   3159 N N   . PRO B 1 96  ? 21.184  -26.168 2.859   1.00 12.15  ? 321  PRO B N   1 
ATOM   3160 C CA  . PRO B 1 96  ? 19.798  -25.862 3.224   1.00 11.38  ? 321  PRO B CA  1 
ATOM   3161 C C   . PRO B 1 96  ? 19.761  -25.025 4.490   1.00 11.78  ? 321  PRO B C   1 
ATOM   3162 O O   . PRO B 1 96  ? 20.674  -25.077 5.320   1.00 14.21  ? 321  PRO B O   1 
ATOM   3163 C CB  . PRO B 1 96  ? 19.169  -27.241 3.449   1.00 14.70  ? 321  PRO B CB  1 
ATOM   3164 C CG  . PRO B 1 96  ? 20.032  -28.191 2.659   1.00 15.37  ? 321  PRO B CG  1 
ATOM   3165 C CD  . PRO B 1 96  ? 21.425  -27.622 2.771   1.00 14.68  ? 321  PRO B CD  1 
ATOM   3166 N N   . GLU B 1 97  ? 18.690  -24.247 4.639   1.00 12.56  ? 322  GLU B N   1 
ATOM   3167 C CA  . GLU B 1 97  ? 18.553  -23.414 5.833   1.00 12.28  ? 322  GLU B CA  1 
ATOM   3168 C C   . GLU B 1 97  ? 18.711  -24.244 7.105   1.00 12.55  ? 322  GLU B C   1 
ATOM   3169 O O   . GLU B 1 97  ? 18.215  -25.366 7.199   1.00 15.35  ? 322  GLU B O   1 
ATOM   3170 C CB  . GLU B 1 97  ? 17.192  -22.716 5.837   1.00 15.35  ? 322  GLU B CB  1 
ATOM   3171 C CG  . GLU B 1 97  ? 16.990  -21.736 4.715   1.00 26.20  ? 322  GLU B CG  1 
ATOM   3172 C CD  . GLU B 1 97  ? 15.596  -21.126 4.738   1.00 38.61  ? 322  GLU B CD  1 
ATOM   3173 O OE1 . GLU B 1 97  ? 14.925  -21.192 5.797   1.00 40.26  ? 322  GLU B OE1 1 
ATOM   3174 O OE2 . GLU B 1 97  ? 15.172  -20.587 3.696   1.00 44.73  ? 322  GLU B OE2 1 
ATOM   3175 N N   . GLY B 1 98  ? 19.414  -23.684 8.093   1.00 10.40  ? 323  GLY B N   1 
ATOM   3176 C CA  . GLY B 1 98  ? 19.587  -24.339 9.374   1.00 11.51  ? 323  GLY B CA  1 
ATOM   3177 C C   . GLY B 1 98  ? 20.775  -25.274 9.489   1.00 11.74  ? 323  GLY B C   1 
ATOM   3178 O O   . GLY B 1 98  ? 21.069  -25.745 10.599  1.00 12.80  ? 323  GLY B O   1 
ATOM   3179 N N   . PHE B 1 99  ? 21.468  -25.573 8.397   1.00 11.87  ? 324  PHE B N   1 
ATOM   3180 C CA  . PHE B 1 99  ? 22.632  -26.445 8.498   1.00 12.32  ? 324  PHE B CA  1 
ATOM   3181 C C   . PHE B 1 99  ? 23.767  -25.782 9.281   1.00 11.97  ? 324  PHE B C   1 
ATOM   3182 O O   . PHE B 1 99  ? 23.962  -24.564 9.199   1.00 11.96  ? 324  PHE B O   1 
ATOM   3183 C CB  . PHE B 1 99  ? 23.152  -26.814 7.116   1.00 9.58   ? 324  PHE B CB  1 
ATOM   3184 C CG  . PHE B 1 99  ? 22.672  -28.159 6.638   1.00 13.52  ? 324  PHE B CG  1 
ATOM   3185 C CD1 . PHE B 1 99  ? 21.326  -28.380 6.397   1.00 11.43  ? 324  PHE B CD1 1 
ATOM   3186 C CD2 . PHE B 1 99  ? 23.567  -29.198 6.467   1.00 13.72  ? 324  PHE B CD2 1 
ATOM   3187 C CE1 . PHE B 1 99  ? 20.888  -29.632 5.968   1.00 13.74  ? 324  PHE B CE1 1 
ATOM   3188 C CE2 . PHE B 1 99  ? 23.140  -30.447 6.035   1.00 14.55  ? 324  PHE B CE2 1 
ATOM   3189 C CZ  . PHE B 1 99  ? 21.795  -30.660 5.792   1.00 15.43  ? 324  PHE B CZ  1 
ATOM   3190 N N   . PRO B 1 100 ? 24.544  -26.570 10.030  1.00 10.90  ? 325  PRO B N   1 
ATOM   3191 C CA  . PRO B 1 100 ? 25.696  -26.012 10.750  1.00 10.80  ? 325  PRO B CA  1 
ATOM   3192 C C   . PRO B 1 100 ? 26.620  -25.206 9.840   1.00 12.59  ? 325  PRO B C   1 
ATOM   3193 O O   . PRO B 1 100 ? 26.885  -25.570 8.683   1.00 12.09  ? 325  PRO B O   1 
ATOM   3194 C CB  . PRO B 1 100 ? 26.398  -27.255 11.312  1.00 11.75  ? 325  PRO B CB  1 
ATOM   3195 C CG  . PRO B 1 100 ? 25.243  -28.219 11.528  1.00 16.51  ? 325  PRO B CG  1 
ATOM   3196 C CD  . PRO B 1 100 ? 24.318  -27.990 10.361  1.00 14.33  ? 325  PRO B CD  1 
ATOM   3197 N N   . ASP B 1 101 ? 27.109  -24.095 10.389  1.00 10.36  ? 326  ASP B N   1 
ATOM   3198 C CA  . ASP B 1 101 ? 27.925  -23.119 9.681   1.00 9.38   ? 326  ASP B CA  1 
ATOM   3199 C C   . ASP B 1 101 ? 29.331  -23.047 10.274  1.00 10.51  ? 326  ASP B C   1 
ATOM   3200 O O   . ASP B 1 101 ? 29.928  -21.973 10.383  1.00 12.48  ? 326  ASP B O   1 
ATOM   3201 C CB  . ASP B 1 101 ? 27.262  -21.745 9.723   1.00 11.64  ? 326  ASP B CB  1 
ATOM   3202 C CG  . ASP B 1 101 ? 27.151  -21.198 11.137  1.00 12.90  ? 326  ASP B CG  1 
ATOM   3203 O OD1 . ASP B 1 101 ? 27.399  -21.963 12.100  1.00 12.63  ? 326  ASP B OD1 1 
ATOM   3204 O OD2 . ASP B 1 101 ? 26.831  -19.994 11.274  1.00 10.77  ? 326  ASP B OD2 1 
ATOM   3205 N N   . PHE B 1 102 ? 29.895  -24.193 10.653  1.00 12.15  ? 327  PHE B N   1 
ATOM   3206 C CA  . PHE B 1 102 ? 31.247  -24.187 11.197  1.00 11.02  ? 327  PHE B CA  1 
ATOM   3207 C C   . PHE B 1 102 ? 31.925  -25.519 10.897  1.00 10.90  ? 327  PHE B C   1 
ATOM   3208 O O   . PHE B 1 102 ? 31.294  -26.486 10.453  1.00 15.38  ? 327  PHE B O   1 
ATOM   3209 C CB  . PHE B 1 102 ? 31.236  -23.906 12.708  1.00 10.93  ? 327  PHE B CB  1 
ATOM   3210 C CG  . PHE B 1 102 ? 30.474  -24.930 13.508  1.00 12.48  ? 327  PHE B CG  1 
ATOM   3211 C CD1 . PHE B 1 102 ? 29.114  -24.788 13.711  1.00 12.08  ? 327  PHE B CD1 1 
ATOM   3212 C CD2 . PHE B 1 102 ? 31.122  -26.035 14.033  1.00 11.83  ? 327  PHE B CD2 1 
ATOM   3213 C CE1 . PHE B 1 102 ? 28.408  -25.742 14.440  1.00 11.19  ? 327  PHE B CE1 1 
ATOM   3214 C CE2 . PHE B 1 102 ? 30.437  -26.980 14.771  1.00 12.16  ? 327  PHE B CE2 1 
ATOM   3215 C CZ  . PHE B 1 102 ? 29.075  -26.840 14.962  1.00 12.52  ? 327  PHE B CZ  1 
ATOM   3216 N N   . THR B 1 103 ? 33.220  -25.556 11.180  1.00 10.91  ? 328  THR B N   1 
ATOM   3217 C CA  . THR B 1 103 ? 34.072  -26.704 10.899  1.00 12.33  ? 328  THR B CA  1 
ATOM   3218 C C   . THR B 1 103 ? 34.115  -27.636 12.108  1.00 15.20  ? 328  THR B C   1 
ATOM   3219 O O   . THR B 1 103 ? 34.263  -27.177 13.244  1.00 14.06  ? 328  THR B O   1 
ATOM   3220 C CB  . THR B 1 103 ? 35.470  -26.203 10.539  1.00 13.34  ? 328  THR B CB  1 
ATOM   3221 O OG1 . THR B 1 103 ? 35.374  -25.372 9.376   1.00 12.42  ? 328  THR B OG1 1 
ATOM   3222 C CG2 . THR B 1 103 ? 36.443  -27.359 10.265  1.00 12.41  ? 328  THR B CG2 1 
ATOM   3223 N N   . ALA B 1 104 ? 33.966  -28.940 11.859  1.00 13.52  ? 329  ALA B N   1 
ATOM   3224 C CA  . ALA B 1 104 ? 34.056  -29.961 12.903  1.00 12.04  ? 329  ALA B CA  1 
ATOM   3225 C C   . ALA B 1 104 ? 34.568  -31.238 12.257  1.00 13.88  ? 329  ALA B C   1 
ATOM   3226 O O   . ALA B 1 104 ? 34.481  -31.403 11.042  1.00 16.17  ? 329  ALA B O   1 
ATOM   3227 C CB  . ALA B 1 104 ? 32.704  -30.213 13.586  1.00 15.21  ? 329  ALA B CB  1 
ATOM   3228 N N   . GLN B 1 105 ? 35.096  -32.154 13.079  1.00 12.21  ? 330  GLN B N   1 
ATOM   3229 C CA  . GLN B 1 105 ? 35.573  -33.419 12.515  1.00 17.34  ? 330  GLN B CA  1 
ATOM   3230 C C   . GLN B 1 105 ? 34.425  -34.360 12.167  1.00 15.98  ? 330  GLN B C   1 
ATOM   3231 O O   . GLN B 1 105 ? 34.517  -35.108 11.184  1.00 15.81  ? 330  GLN B O   1 
ATOM   3232 C CB  . GLN B 1 105 ? 36.533  -34.111 13.483  1.00 16.03  ? 330  GLN B CB  1 
ATOM   3233 C CG  . GLN B 1 105 ? 37.868  -33.412 13.617  1.00 17.77  ? 330  GLN B CG  1 
ATOM   3234 C CD  . GLN B 1 105 ? 37.762  -32.154 14.450  1.00 24.54  ? 330  GLN B CD  1 
ATOM   3235 O OE1 . GLN B 1 105 ? 37.171  -32.167 15.529  1.00 21.30  ? 330  GLN B OE1 1 
ATOM   3236 N NE2 . GLN B 1 105 ? 38.312  -31.057 13.947  1.00 18.88  ? 330  GLN B NE2 1 
ATOM   3237 N N   . GLU B 1 106 ? 33.361  -34.336 12.964  1.00 15.64  ? 331  GLU B N   1 
ATOM   3238 C CA  . GLU B 1 106 ? 32.160  -35.136 12.753  1.00 15.08  ? 331  GLU B CA  1 
ATOM   3239 C C   . GLU B 1 106 ? 30.955  -34.321 13.199  1.00 13.21  ? 331  GLU B C   1 
ATOM   3240 O O   . GLU B 1 106 ? 31.026  -33.562 14.171  1.00 13.32  ? 331  GLU B O   1 
ATOM   3241 C CB  . GLU B 1 106 ? 32.176  -36.450 13.559  1.00 16.59  ? 331  GLU B CB  1 
ATOM   3242 C CG  . GLU B 1 106 ? 33.275  -37.412 13.199  1.00 22.87  ? 331  GLU B CG  1 
ATOM   3243 C CD  . GLU B 1 106 ? 34.542  -37.158 13.974  1.00 19.02  ? 331  GLU B CD  1 
ATOM   3244 O OE1 . GLU B 1 106 ? 34.459  -36.602 15.097  1.00 19.52  ? 331  GLU B OE1 1 
ATOM   3245 O OE2 . GLU B 1 106 ? 35.613  -37.525 13.464  1.00 23.10  ? 331  GLU B OE2 1 
ATOM   3246 N N   . TYR B 1 107 ? 29.834  -34.508 12.502  1.00 11.88  ? 332  TYR B N   1 
ATOM   3247 C CA  . TYR B 1 107 ? 28.542  -33.962 12.910  1.00 12.18  ? 332  TYR B CA  1 
ATOM   3248 C C   . TYR B 1 107 ? 27.645  -35.158 13.226  1.00 14.07  ? 332  TYR B C   1 
ATOM   3249 O O   . TYR B 1 107 ? 27.248  -35.890 12.312  1.00 14.97  ? 332  TYR B O   1 
ATOM   3250 C CB  . TYR B 1 107 ? 27.940  -33.081 11.811  1.00 14.16  ? 332  TYR B CB  1 
ATOM   3251 C CG  . TYR B 1 107 ? 28.872  -31.989 11.293  1.00 14.84  ? 332  TYR B CG  1 
ATOM   3252 C CD1 . TYR B 1 107 ? 29.880  -32.285 10.384  1.00 10.85  ? 332  TYR B CD1 1 
ATOM   3253 C CD2 . TYR B 1 107 ? 28.721  -30.663 11.694  1.00 16.05  ? 332  TYR B CD2 1 
ATOM   3254 C CE1 . TYR B 1 107 ? 30.727  -31.302 9.904   1.00 13.00  ? 332  TYR B CE1 1 
ATOM   3255 C CE2 . TYR B 1 107 ? 29.563  -29.666 11.215  1.00 10.31  ? 332  TYR B CE2 1 
ATOM   3256 C CZ  . TYR B 1 107 ? 30.569  -29.996 10.320  1.00 13.44  ? 332  TYR B CZ  1 
ATOM   3257 O OH  . TYR B 1 107 ? 31.430  -29.037 9.834   1.00 13.27  ? 332  TYR B OH  1 
ATOM   3258 N N   . HIS B 1 108 ? 27.365  -35.380 14.517  1.00 11.30  ? 333  HIS B N   1 
ATOM   3259 C CA  . HIS B 1 108 ? 26.598  -36.547 14.946  1.00 12.34  ? 333  HIS B CA  1 
ATOM   3260 C C   . HIS B 1 108 ? 25.115  -36.281 14.764  1.00 13.65  ? 333  HIS B C   1 
ATOM   3261 O O   . HIS B 1 108 ? 24.642  -35.162 14.990  1.00 11.99  ? 333  HIS B O   1 
ATOM   3262 C CB  . HIS B 1 108 ? 26.868  -36.867 16.416  1.00 11.76  ? 333  HIS B CB  1 
ATOM   3263 C CG  . HIS B 1 108 ? 28.318  -37.002 16.747  1.00 15.26  ? 333  HIS B CG  1 
ATOM   3264 N ND1 . HIS B 1 108 ? 28.916  -36.300 17.772  1.00 16.33  ? 333  HIS B ND1 1 
ATOM   3265 C CD2 . HIS B 1 108 ? 29.286  -37.773 16.200  1.00 20.30  ? 333  HIS B CD2 1 
ATOM   3266 C CE1 . HIS B 1 108 ? 30.195  -36.622 17.831  1.00 17.28  ? 333  HIS B CE1 1 
ATOM   3267 N NE2 . HIS B 1 108 ? 30.446  -37.513 16.888  1.00 20.48  ? 333  HIS B NE2 1 
ATOM   3268 N N   . LEU B 1 109 ? 24.370  -37.308 14.368  1.00 10.13  ? 334  LEU B N   1 
ATOM   3269 C CA  . LEU B 1 109 ? 22.971  -37.070 14.061  1.00 9.95   ? 334  LEU B CA  1 
ATOM   3270 C C   . LEU B 1 109 ? 22.108  -38.278 14.396  1.00 11.64  ? 334  LEU B C   1 
ATOM   3271 O O   . LEU B 1 109 ? 22.597  -39.380 14.670  1.00 12.54  ? 334  LEU B O   1 
ATOM   3272 C CB  . LEU B 1 109 ? 22.800  -36.693 12.578  1.00 11.67  ? 334  LEU B CB  1 
ATOM   3273 C CG  . LEU B 1 109 ? 23.300  -37.698 11.525  1.00 15.28  ? 334  LEU B CG  1 
ATOM   3274 C CD1 . LEU B 1 109 ? 22.288  -38.836 11.254  1.00 14.00  ? 334  LEU B CD1 1 
ATOM   3275 C CD2 . LEU B 1 109 ? 23.618  -36.956 10.247  1.00 12.75  ? 334  LEU B CD2 1 
ATOM   3276 N N   A ARG B 1 110 ? 20.798  -38.035 14.376  0.73 11.42  ? 335  ARG B N   1 
ATOM   3277 N N   B ARG B 1 110 ? 20.796  -38.032 14.382  0.27 11.50  ? 335  ARG B N   1 
ATOM   3278 C CA  A ARG B 1 110 ? 19.756  -39.051 14.414  0.73 11.22  ? 335  ARG B CA  1 
ATOM   3279 C CA  B ARG B 1 110 ? 19.744  -39.038 14.428  0.27 11.35  ? 335  ARG B CA  1 
ATOM   3280 C C   A ARG B 1 110 ? 18.771  -38.713 13.309  0.73 14.55  ? 335  ARG B C   1 
ATOM   3281 C C   B ARG B 1 110 ? 18.753  -38.708 13.321  0.27 14.48  ? 335  ARG B C   1 
ATOM   3282 O O   A ARG B 1 110 ? 18.578  -37.539 12.989  0.73 13.45  ? 335  ARG B O   1 
ATOM   3283 O O   B ARG B 1 110 ? 18.537  -37.535 13.010  0.27 13.41  ? 335  ARG B O   1 
ATOM   3284 C CB  A ARG B 1 110 ? 19.012  -39.076 15.760  0.73 15.89  ? 335  ARG B CB  1 
ATOM   3285 C CB  B ARG B 1 110 ? 19.011  -39.047 15.786  0.27 15.80  ? 335  ARG B CB  1 
ATOM   3286 C CG  A ARG B 1 110 ? 19.793  -39.605 16.945  0.73 20.38  ? 335  ARG B CG  1 
ATOM   3287 C CG  B ARG B 1 110 ? 19.510  -40.054 16.817  0.27 24.26  ? 335  ARG B CG  1 
ATOM   3288 C CD  A ARG B 1 110 ? 18.864  -39.695 18.170  0.73 15.29  ? 335  ARG B CD  1 
ATOM   3289 C CD  B ARG B 1 110 ? 18.675  -39.961 18.101  0.27 18.13  ? 335  ARG B CD  1 
ATOM   3290 N NE  A ARG B 1 110 ? 19.600  -39.888 19.410  0.73 16.44  ? 335  ARG B NE  1 
ATOM   3291 N NE  B ARG B 1 110 ? 18.993  -41.007 19.066  0.27 23.68  ? 335  ARG B NE  1 
ATOM   3292 C CZ  A ARG B 1 110 ? 19.713  -41.050 20.030  0.73 26.68  ? 335  ARG B CZ  1 
ATOM   3293 C CZ  B ARG B 1 110 ? 19.900  -40.893 20.027  0.27 26.04  ? 335  ARG B CZ  1 
ATOM   3294 N NH1 A ARG B 1 110 ? 19.162  -42.144 19.539  0.73 19.44  ? 335  ARG B NH1 1 
ATOM   3295 N NH1 B ARG B 1 110 ? 20.615  -39.791 20.176  0.27 11.11  ? 335  ARG B NH1 1 
ATOM   3296 N NH2 A ARG B 1 110 ? 20.397  -41.114 21.171  0.73 37.10  ? 335  ARG B NH2 1 
ATOM   3297 N NH2 B ARG B 1 110 ? 20.096  -41.912 20.860  0.27 31.30  ? 335  ARG B NH2 1 
ATOM   3298 N N   . ALA B 1 111 ? 18.152  -39.737 12.719  1.00 14.46  ? 336  ALA B N   1 
ATOM   3299 C CA  . ALA B 1 111 ? 17.157  -39.505 11.674  1.00 13.37  ? 336  ALA B CA  1 
ATOM   3300 C C   . ALA B 1 111 ? 16.140  -40.637 11.660  1.00 16.03  ? 336  ALA B C   1 
ATOM   3301 O O   . ALA B 1 111 ? 16.362  -41.700 12.237  1.00 14.89  ? 336  ALA B O   1 
ATOM   3302 C CB  . ALA B 1 111 ? 17.803  -39.356 10.293  1.00 14.15  ? 336  ALA B CB  1 
ATOM   3303 N N   . ALA B 1 112 ? 15.016  -40.396 10.982  1.00 13.41  ? 337  ALA B N   1 
ATOM   3304 C CA  . ALA B 1 112 ? 13.966  -41.401 10.837  1.00 12.48  ? 337  ALA B CA  1 
ATOM   3305 C C   . ALA B 1 112 ? 13.104  -41.059 9.635   1.00 18.88  ? 337  ALA B C   1 
ATOM   3306 O O   . ALA B 1 112 ? 12.983  -39.897 9.241   1.00 14.82  ? 337  ALA B O   1 
ATOM   3307 C CB  . ALA B 1 112 ? 13.081  -41.511 12.087  1.00 12.95  ? 337  ALA B CB  1 
ATOM   3308 N N   . GLY B 1 113 ? 12.480  -42.095 9.082   1.00 14.12  ? 338  GLY B N   1 
ATOM   3309 C CA  . GLY B 1 113 ? 11.526  -41.937 8.005   1.00 16.98  ? 338  GLY B CA  1 
ATOM   3310 C C   . GLY B 1 113 ? 10.141  -42.354 8.437   1.00 15.72  ? 338  GLY B C   1 
ATOM   3311 O O   . GLY B 1 113 ? 9.911   -42.663 9.618   1.00 18.88  ? 338  GLY B O   1 
ATOM   3312 N N   . LYS B 1 114 ? 9.208   -42.387 7.483   1.00 16.44  ? 339  LYS B N   1 
ATOM   3313 C CA  . LYS B 1 114 ? 7.823   -42.714 7.782   1.00 21.53  ? 339  LYS B CA  1 
ATOM   3314 C C   . LYS B 1 114 ? 7.598   -44.201 8.008   1.00 23.75  ? 339  LYS B C   1 
ATOM   3315 O O   . LYS B 1 114 ? 6.492   -44.585 8.405   1.00 34.00  ? 339  LYS B O   1 
ATOM   3316 C CB  . LYS B 1 114 ? 6.902   -42.255 6.642   1.00 22.37  ? 339  LYS B CB  1 
ATOM   3317 C CG  . LYS B 1 114 ? 6.936   -40.777 6.306   1.00 30.41  ? 339  LYS B CG  1 
ATOM   3318 C CD  . LYS B 1 114 ? 6.219   -40.528 4.981   1.00 36.03  ? 339  LYS B CD  1 
ATOM   3319 C CE  . LYS B 1 114 ? 6.380   -39.089 4.525   1.00 60.75  ? 339  LYS B CE  1 
ATOM   3320 N NZ  . LYS B 1 114 ? 5.779   -38.870 3.182   1.00 57.52  ? 339  LYS B NZ  1 
ATOM   3321 N N   . VAL B 1 115 ? 8.591   -45.051 7.736   1.00 16.86  ? 340  VAL B N   1 
ATOM   3322 C CA  . VAL B 1 115 ? 8.405   -46.488 7.783   1.00 16.36  ? 340  VAL B CA  1 
ATOM   3323 C C   . VAL B 1 115 ? 9.350   -47.064 8.829   1.00 22.88  ? 340  VAL B C   1 
ATOM   3324 O O   . VAL B 1 115 ? 10.314  -46.428 9.263   1.00 18.84  ? 340  VAL B O   1 
ATOM   3325 C CB  . VAL B 1 115 ? 8.616   -47.158 6.404   1.00 26.31  ? 340  VAL B CB  1 
ATOM   3326 C CG1 . VAL B 1 115 ? 7.614   -46.609 5.393   1.00 28.17  ? 340  VAL B CG1 1 
ATOM   3327 C CG2 . VAL B 1 115 ? 10.035  -46.938 5.898   1.00 31.35  ? 340  VAL B CG2 1 
ATOM   3328 N N   . ALA B 1 116 ? 9.047   -48.282 9.245   1.00 27.41  ? 341  ALA B N   1 
ATOM   3329 C CA  . ALA B 1 116 ? 9.826   -48.900 10.301  1.00 26.59  ? 341  ALA B CA  1 
ATOM   3330 C C   . ALA B 1 116 ? 11.241  -49.221 9.823   1.00 32.20  ? 341  ALA B C   1 
ATOM   3331 O O   . ALA B 1 116 ? 11.530  -49.297 8.623   1.00 24.92  ? 341  ALA B O   1 
ATOM   3332 C CB  . ALA B 1 116 ? 9.144   -50.173 10.796  1.00 31.75  ? 341  ALA B CB  1 
ATOM   3333 N N   . ASN B 1 117 ? 12.122  -49.415 10.802  1.00 18.79  ? 342  ASN B N   1 
ATOM   3334 C CA  . ASN B 1 117 ? 13.532  -49.740 10.610  1.00 22.52  ? 342  ASN B CA  1 
ATOM   3335 C C   . ASN B 1 117 ? 14.293  -48.635 9.907   1.00 20.62  ? 342  ASN B C   1 
ATOM   3336 O O   . ASN B 1 117 ? 15.316  -48.895 9.272   1.00 19.41  ? 342  ASN B O   1 
ATOM   3337 C CB  . ASN B 1 117 ? 13.705  -51.068 9.869   1.00 26.45  ? 342  ASN B CB  1 
ATOM   3338 C CG  . ASN B 1 117 ? 13.529  -52.254 10.795  1.00 38.67  ? 342  ASN B CG  1 
ATOM   3339 O OD1 . ASN B 1 117 ? 12.481  -52.892 10.806  1.00 42.69  ? 342  ASN B OD1 1 
ATOM   3340 N ND2 . ASN B 1 117 ? 14.549  -52.528 11.609  1.00 41.02  ? 342  ASN B ND2 1 
ATOM   3341 N N   . THR B 1 118 ? 13.820  -47.396 10.022  1.00 16.97  ? 343  THR B N   1 
ATOM   3342 C CA  . THR B 1 118 ? 14.562  -46.258 9.503   1.00 14.05  ? 343  THR B CA  1 
ATOM   3343 C C   . THR B 1 118 ? 15.055  -45.321 10.592  1.00 14.93  ? 343  THR B C   1 
ATOM   3344 O O   . THR B 1 118 ? 15.715  -44.328 10.273  1.00 15.45  ? 343  THR B O   1 
ATOM   3345 C CB  . THR B 1 118 ? 13.718  -45.460 8.497   1.00 13.89  ? 343  THR B CB  1 
ATOM   3346 O OG1 . THR B 1 118 ? 12.548  -44.951 9.146   1.00 17.22  ? 343  THR B OG1 1 
ATOM   3347 C CG2 . THR B 1 118 ? 13.320  -46.309 7.300   1.00 16.60  ? 343  THR B CG2 1 
ATOM   3348 N N   . THR B 1 119 ? 14.758  -45.589 11.864  1.00 18.32  ? 344  THR B N   1 
ATOM   3349 C CA  . THR B 1 119 ? 15.313  -44.774 12.941  1.00 15.95  ? 344  THR B CA  1 
ATOM   3350 C C   . THR B 1 119 ? 16.739  -45.219 13.209  1.00 19.27  ? 344  THR B C   1 
ATOM   3351 O O   . THR B 1 119 ? 16.980  -46.387 13.537  1.00 17.70  ? 344  THR B O   1 
ATOM   3352 C CB  . THR B 1 119 ? 14.475  -44.887 14.210  1.00 15.37  ? 344  THR B CB  1 
ATOM   3353 O OG1 . THR B 1 119 ? 13.188  -44.317 13.961  1.00 17.31  ? 344  THR B OG1 1 
ATOM   3354 C CG2 . THR B 1 119 ? 15.137  -44.138 15.374  1.00 15.76  ? 344  THR B CG2 1 
ATOM   3355 N N   . GLY B 1 120 ? 17.683  -44.291 13.070  1.00 15.62  ? 345  GLY B N   1 
ATOM   3356 C CA  . GLY B 1 120 ? 19.066  -44.630 13.321  1.00 14.53  ? 345  GLY B CA  1 
ATOM   3357 C C   . GLY B 1 120 ? 19.861  -43.430 13.785  1.00 16.05  ? 345  GLY B C   1 
ATOM   3358 O O   . GLY B 1 120 ? 19.400  -42.288 13.751  1.00 15.23  ? 345  GLY B O   1 
ATOM   3359 N N   . GLY B 1 121 ? 21.074  -43.718 14.230  1.00 14.08  ? 346  GLY B N   1 
ATOM   3360 C CA  . GLY B 1 121 ? 22.063  -42.691 14.472  1.00 12.60  ? 346  GLY B CA  1 
ATOM   3361 C C   . GLY B 1 121 ? 23.173  -42.846 13.457  1.00 13.38  ? 346  GLY B C   1 
ATOM   3362 O O   . GLY B 1 121 ? 23.347  -43.920 12.865  1.00 13.85  ? 346  GLY B O   1 
ATOM   3363 N N   . GLY B 1 122 ? 23.902  -41.773 13.222  1.00 12.31  ? 347  GLY B N   1 
ATOM   3364 C CA  . GLY B 1 122 ? 25.031  -41.812 12.320  1.00 13.21  ? 347  GLY B CA  1 
ATOM   3365 C C   . GLY B 1 122 ? 25.762  -40.502 12.447  1.00 11.50  ? 347  GLY B C   1 
ATOM   3366 O O   . GLY B 1 122 ? 25.559  -39.765 13.412  1.00 13.75  ? 347  GLY B O   1 
ATOM   3367 N N   . GLU B 1 123 ? 26.622  -40.220 11.473  1.00 12.46  ? 348  GLU B N   1 
ATOM   3368 C CA  . GLU B 1 123 ? 27.382  -38.978 11.518  1.00 13.84  ? 348  GLU B CA  1 
ATOM   3369 C C   . GLU B 1 123 ? 27.766  -38.577 10.106  1.00 15.66  ? 348  GLU B C   1 
ATOM   3370 O O   . GLU B 1 123 ? 27.821  -39.405 9.195   1.00 15.22  ? 348  GLU B O   1 
ATOM   3371 C CB  . GLU B 1 123 ? 28.646  -39.125 12.382  1.00 15.05  ? 348  GLU B CB  1 
ATOM   3372 C CG  . GLU B 1 123 ? 29.647  -40.145 11.838  1.00 18.77  ? 348  GLU B CG  1 
ATOM   3373 C CD  . GLU B 1 123 ? 30.799  -40.398 12.797  1.00 26.88  ? 348  GLU B CD  1 
ATOM   3374 O OE1 . GLU B 1 123 ? 30.654  -40.082 13.990  1.00 23.76  ? 348  GLU B OE1 1 
ATOM   3375 O OE2 . GLU B 1 123 ? 31.849  -40.905 12.355  1.00 22.92  ? 348  GLU B OE2 1 
ATOM   3376 N N   . ILE B 1 124 ? 28.055  -37.293 9.937   1.00 14.60  ? 349  ILE B N   1 
ATOM   3377 C CA  . ILE B 1 124 ? 28.674  -36.790 8.717   1.00 13.16  ? 349  ILE B CA  1 
ATOM   3378 C C   . ILE B 1 124 ? 30.117  -36.435 9.058   1.00 12.42  ? 349  ILE B C   1 
ATOM   3379 O O   . ILE B 1 124 ? 30.365  -35.526 9.861   1.00 14.68  ? 349  ILE B O   1 
ATOM   3380 C CB  . ILE B 1 124 ? 27.922  -35.574 8.158   1.00 12.55  ? 349  ILE B CB  1 
ATOM   3381 C CG1 . ILE B 1 124 ? 26.437  -35.897 7.984   1.00 12.91  ? 349  ILE B CG1 1 
ATOM   3382 C CG2 . ILE B 1 124 ? 28.538  -35.125 6.840   1.00 12.55  ? 349  ILE B CG2 1 
ATOM   3383 C CD1 . ILE B 1 124 ? 25.579  -34.666 7.769   1.00 15.54  ? 349  ILE B CD1 1 
ATOM   3384 N N   . LYS B 1 125 ? 31.067  -37.162 8.471   1.00 14.43  ? 350  LYS B N   1 
ATOM   3385 C CA  . LYS B 1 125 ? 32.471  -36.826 8.647   1.00 14.13  ? 350  LYS B CA  1 
ATOM   3386 C C   . LYS B 1 125 ? 32.776  -35.523 7.919   1.00 13.96  ? 350  LYS B C   1 
ATOM   3387 O O   . LYS B 1 125 ? 32.097  -35.154 6.959   1.00 14.93  ? 350  LYS B O   1 
ATOM   3388 C CB  . LYS B 1 125 ? 33.356  -37.969 8.135   1.00 18.25  ? 350  LYS B CB  1 
ATOM   3389 C CG  . LYS B 1 125 ? 33.247  -39.219 8.992   1.00 22.09  ? 350  LYS B CG  1 
ATOM   3390 C CD  . LYS B 1 125 ? 33.792  -40.453 8.286   1.00 34.23  ? 350  LYS B CD  1 
ATOM   3391 C CE  . LYS B 1 125 ? 33.829  -41.665 9.229   1.00 37.12  ? 350  LYS B CE  1 
ATOM   3392 N NZ  . LYS B 1 125 ? 32.507  -41.970 9.887   1.00 24.75  ? 350  LYS B NZ  1 
ATOM   3393 N N   . SER B 1 126 ? 33.791  -34.802 8.401   1.00 14.24  ? 351  SER B N   1 
ATOM   3394 C CA  . SER B 1 126 ? 34.093  -33.489 7.824   1.00 14.54  ? 351  SER B CA  1 
ATOM   3395 C C   . SER B 1 126 ? 34.260  -33.552 6.311   1.00 16.44  ? 351  SER B C   1 
ATOM   3396 O O   . SER B 1 126 ? 33.727  -32.703 5.581   1.00 16.00  ? 351  SER B O   1 
ATOM   3397 C CB  . SER B 1 126 ? 35.351  -32.903 8.464   1.00 15.25  ? 351  SER B CB  1 
ATOM   3398 O OG  . SER B 1 126 ? 35.555  -31.567 8.019   1.00 14.71  ? 351  SER B OG  1 
ATOM   3399 N N   A THR B 1 127 ? 35.001  -34.553 5.819   0.69 15.19  ? 352  THR B N   1 
ATOM   3400 N N   B THR B 1 127 ? 34.999  -34.551 5.817   0.31 15.32  ? 352  THR B N   1 
ATOM   3401 C CA  A THR B 1 127 ? 35.222  -34.678 4.381   0.69 17.60  ? 352  THR B CA  1 
ATOM   3402 C CA  B THR B 1 127 ? 35.208  -34.672 4.376   0.31 17.59  ? 352  THR B CA  1 
ATOM   3403 C C   A THR B 1 127 ? 33.917  -34.886 3.616   0.69 17.59  ? 352  THR B C   1 
ATOM   3404 C C   B THR B 1 127 ? 33.891  -34.830 3.626   0.31 17.50  ? 352  THR B C   1 
ATOM   3405 O O   A THR B 1 127 ? 33.855  -34.575 2.423   0.69 18.48  ? 352  THR B O   1 
ATOM   3406 O O   B THR B 1 127 ? 33.790  -34.438 2.459   0.31 18.33  ? 352  THR B O   1 
ATOM   3407 C CB  A THR B 1 127 ? 36.206  -35.823 4.087   0.69 16.90  ? 352  THR B CB  1 
ATOM   3408 C CB  B THR B 1 127 ? 36.140  -35.848 4.069   0.31 16.96  ? 352  THR B CB  1 
ATOM   3409 O OG1 A THR B 1 127 ? 36.665  -35.727 2.732   0.69 19.73  ? 352  THR B OG1 1 
ATOM   3410 O OG1 B THR B 1 127 ? 35.655  -37.033 4.712   0.31 21.35  ? 352  THR B OG1 1 
ATOM   3411 C CG2 A THR B 1 127 ? 35.552  -37.176 4.292   0.69 23.52  ? 352  THR B CG2 1 
ATOM   3412 C CG2 B THR B 1 127 ? 37.545  -35.550 4.558   0.31 16.29  ? 352  THR B CG2 1 
ATOM   3413 N N   . ASP B 1 128 ? 32.874  -35.388 4.276   1.00 13.66  ? 353  ASP B N   1 
ATOM   3414 C CA  . ASP B 1 128 ? 31.573  -35.585 3.658   1.00 14.69  ? 353  ASP B CA  1 
ATOM   3415 C C   . ASP B 1 128 ? 30.614  -34.433 3.922   1.00 15.50  ? 353  ASP B C   1 
ATOM   3416 O O   . ASP B 1 128 ? 29.487  -34.451 3.416   1.00 15.97  ? 353  ASP B O   1 
ATOM   3417 C CB  . ASP B 1 128 ? 30.955  -36.886 4.157   1.00 13.86  ? 353  ASP B CB  1 
ATOM   3418 C CG  . ASP B 1 128 ? 31.764  -38.105 3.755   1.00 15.86  ? 353  ASP B CG  1 
ATOM   3419 O OD1 . ASP B 1 128 ? 32.280  -38.152 2.613   1.00 19.11  ? 353  ASP B OD1 1 
ATOM   3420 O OD2 . ASP B 1 128 ? 31.894  -39.027 4.588   1.00 18.57  ? 353  ASP B OD2 1 
ATOM   3421 N N   . TYR B 1 129 ? 31.025  -33.439 4.708   1.00 14.10  ? 354  TYR B N   1 
ATOM   3422 C CA  . TYR B 1 129 ? 30.145  -32.311 5.008   1.00 13.54  ? 354  TYR B CA  1 
ATOM   3423 C C   . TYR B 1 129 ? 30.245  -31.312 3.863   1.00 14.81  ? 354  TYR B C   1 
ATOM   3424 O O   . TYR B 1 129 ? 30.861  -30.246 3.964   1.00 14.82  ? 354  TYR B O   1 
ATOM   3425 C CB  . TYR B 1 129 ? 30.490  -31.669 6.345   1.00 12.01  ? 354  TYR B CB  1 
ATOM   3426 C CG  . TYR B 1 129 ? 29.428  -30.689 6.777   1.00 10.77  ? 354  TYR B CG  1 
ATOM   3427 C CD1 . TYR B 1 129 ? 28.191  -31.144 7.230   1.00 13.56  ? 354  TYR B CD1 1 
ATOM   3428 C CD2 . TYR B 1 129 ? 29.636  -29.320 6.716   1.00 10.95  ? 354  TYR B CD2 1 
ATOM   3429 C CE1 . TYR B 1 129 ? 27.197  -30.263 7.616   1.00 14.01  ? 354  TYR B CE1 1 
ATOM   3430 C CE2 . TYR B 1 129 ? 28.636  -28.423 7.113   1.00 11.04  ? 354  TYR B CE2 1 
ATOM   3431 C CZ  . TYR B 1 129 ? 27.426  -28.905 7.560   1.00 13.70  ? 354  TYR B CZ  1 
ATOM   3432 O OH  . TYR B 1 129 ? 26.424  -28.032 7.950   1.00 13.40  ? 354  TYR B OH  1 
ATOM   3433 N N   . THR B 1 130 ? 29.608  -31.665 2.750   1.00 12.90  ? 355  THR B N   1 
ATOM   3434 C CA  . THR B 1 130 ? 29.599  -30.826 1.552   1.00 14.80  ? 355  THR B CA  1 
ATOM   3435 C C   . THR B 1 130 ? 28.164  -30.611 1.073   1.00 13.92  ? 355  THR B C   1 
ATOM   3436 O O   . THR B 1 130 ? 27.823  -30.937 -0.071  1.00 13.89  ? 355  THR B O   1 
ATOM   3437 C CB  . THR B 1 130 ? 30.470  -31.446 0.458   1.00 18.59  ? 355  THR B CB  1 
ATOM   3438 O OG1 . THR B 1 130 ? 30.026  -32.783 0.168   1.00 16.87  ? 355  THR B OG1 1 
ATOM   3439 C CG2 . THR B 1 130 ? 31.954  -31.495 0.900   1.00 17.41  ? 355  THR B CG2 1 
ATOM   3440 N N   . PRO B 1 131 ? 27.307  -30.008 1.918   1.00 12.00  ? 356  PRO B N   1 
ATOM   3441 C CA  . PRO B 1 131 ? 25.874  -29.907 1.576   1.00 11.38  ? 356  PRO B CA  1 
ATOM   3442 C C   . PRO B 1 131 ? 25.590  -29.002 0.395   1.00 15.90  ? 356  PRO B C   1 
ATOM   3443 O O   . PRO B 1 131 ? 24.520  -29.128 -0.219  1.00 14.92  ? 356  PRO B O   1 
ATOM   3444 C CB  . PRO B 1 131 ? 25.242  -29.344 2.857   1.00 10.85  ? 356  PRO B CB  1 
ATOM   3445 C CG  . PRO B 1 131 ? 26.379  -28.526 3.489   1.00 12.94  ? 356  PRO B CG  1 
ATOM   3446 C CD  . PRO B 1 131 ? 27.607  -29.361 3.214   1.00 13.83  ? 356  PRO B CD  1 
ATOM   3447 N N   . ALA B 1 132 ? 26.509  -28.104 0.044   1.00 13.31  ? 357  ALA B N   1 
ATOM   3448 C CA  . ALA B 1 132 ? 26.278  -27.260 -1.123  1.00 14.14  ? 357  ALA B CA  1 
ATOM   3449 C C   . ALA B 1 132 ? 26.145  -28.085 -2.393  1.00 16.97  ? 357  ALA B C   1 
ATOM   3450 O O   . ALA B 1 132 ? 25.547  -27.608 -3.367  1.00 17.09  ? 357  ALA B O   1 
ATOM   3451 C CB  . ALA B 1 132 ? 27.408  -26.235 -1.282  1.00 14.52  ? 357  ALA B CB  1 
ATOM   3452 N N   . LEU B 1 133 ? 26.658  -29.322 -2.390  1.00 12.69  ? 358  LEU B N   1 
ATOM   3453 C CA  . LEU B 1 133 ? 26.556  -30.218 -3.537  1.00 17.47  ? 358  LEU B CA  1 
ATOM   3454 C C   . LEU B 1 133 ? 25.180  -30.859 -3.658  1.00 15.92  ? 358  LEU B C   1 
ATOM   3455 O O   . LEU B 1 133 ? 24.910  -31.528 -4.662  1.00 19.04  ? 358  LEU B O   1 
ATOM   3456 C CB  . LEU B 1 133 ? 27.633  -31.304 -3.449  1.00 21.33  ? 358  LEU B CB  1 
ATOM   3457 C CG  . LEU B 1 133 ? 29.088  -30.812 -3.459  1.00 15.90  ? 358  LEU B CG  1 
ATOM   3458 C CD1 . LEU B 1 133 ? 30.084  -31.973 -3.421  1.00 18.71  ? 358  LEU B CD1 1 
ATOM   3459 C CD2 . LEU B 1 133 ? 29.343  -29.930 -4.680  1.00 19.80  ? 358  LEU B CD2 1 
ATOM   3460 N N   . GLY B 1 134 ? 24.304  -30.649 -2.684  1.00 15.94  ? 359  GLY B N   1 
ATOM   3461 C CA  . GLY B 1 134 ? 22.931  -31.084 -2.783  1.00 18.66  ? 359  GLY B CA  1 
ATOM   3462 C C   . GLY B 1 134 ? 22.623  -32.358 -2.046  1.00 20.32  ? 359  GLY B C   1 
ATOM   3463 O O   . GLY B 1 134 ? 21.462  -32.788 -2.045  1.00 15.84  ? 359  GLY B O   1 
ATOM   3464 N N   . GLY B 1 135 ? 23.624  -32.975 -1.423  1.00 16.87  ? 360  GLY B N   1 
ATOM   3465 C CA  . GLY B 1 135 ? 23.419  -34.199 -0.676  1.00 15.40  ? 360  GLY B CA  1 
ATOM   3466 C C   . GLY B 1 135 ? 24.487  -34.355 0.382   1.00 18.48  ? 360  GLY B C   1 
ATOM   3467 O O   . GLY B 1 135 ? 25.467  -33.609 0.418   1.00 16.31  ? 360  GLY B O   1 
ATOM   3468 N N   . VAL B 1 136 ? 24.284  -35.324 1.270   1.00 16.09  ? 361  VAL B N   1 
ATOM   3469 C CA  . VAL B 1 136 ? 25.297  -35.652 2.272   1.00 12.27  ? 361  VAL B CA  1 
ATOM   3470 C C   . VAL B 1 136 ? 25.377  -37.163 2.425   1.00 15.68  ? 361  VAL B C   1 
ATOM   3471 O O   . VAL B 1 136 ? 24.355  -37.860 2.442   1.00 17.33  ? 361  VAL B O   1 
ATOM   3472 C CB  . VAL B 1 136 ? 25.035  -34.991 3.647   1.00 16.99  ? 361  VAL B CB  1 
ATOM   3473 C CG1 . VAL B 1 136 ? 25.386  -33.495 3.619   1.00 22.15  ? 361  VAL B CG1 1 
ATOM   3474 C CG2 . VAL B 1 136 ? 23.594  -35.201 4.085   1.00 20.71  ? 361  VAL B CG2 1 
ATOM   3475 N N   . LYS B 1 137 ? 26.602  -37.667 2.527   1.00 14.85  ? 362  LYS B N   1 
ATOM   3476 C CA  . LYS B 1 137 ? 26.859  -39.073 2.814   1.00 14.14  ? 362  LYS B CA  1 
ATOM   3477 C C   . LYS B 1 137 ? 26.958  -39.236 4.325   1.00 17.25  ? 362  LYS B C   1 
ATOM   3478 O O   . LYS B 1 137 ? 27.869  -38.686 4.956   1.00 17.18  ? 362  LYS B O   1 
ATOM   3479 C CB  . LYS B 1 137 ? 28.139  -39.531 2.115   1.00 17.01  ? 362  LYS B CB  1 
ATOM   3480 C CG  . LYS B 1 137 ? 28.595  -40.936 2.462   1.00 14.34  ? 362  LYS B CG  1 
ATOM   3481 C CD  . LYS B 1 137 ? 29.966  -41.216 1.850   1.00 20.51  ? 362  LYS B CD  1 
ATOM   3482 C CE  . LYS B 1 137 ? 30.444  -42.621 2.155   1.00 30.77  ? 362  LYS B CE  1 
ATOM   3483 N NZ  . LYS B 1 137 ? 31.743  -42.903 1.490   1.00 30.77  ? 362  LYS B NZ  1 
ATOM   3484 N N   . ILE B 1 138 ? 26.001  -39.958 4.906   1.00 13.19  ? 363  ILE B N   1 
ATOM   3485 C CA  . ILE B 1 138 ? 25.980  -40.236 6.336   1.00 12.62  ? 363  ILE B CA  1 
ATOM   3486 C C   . ILE B 1 138 ? 26.656  -41.579 6.552   1.00 14.58  ? 363  ILE B C   1 
ATOM   3487 O O   . ILE B 1 138 ? 26.323  -42.562 5.882   1.00 17.23  ? 363  ILE B O   1 
ATOM   3488 C CB  . ILE B 1 138 ? 24.539  -40.246 6.877   1.00 13.28  ? 363  ILE B CB  1 
ATOM   3489 C CG1 . ILE B 1 138 ? 23.876  -38.886 6.628   1.00 12.82  ? 363  ILE B CG1 1 
ATOM   3490 C CG2 . ILE B 1 138 ? 24.513  -40.621 8.369   1.00 13.30  ? 363  ILE B CG2 1 
ATOM   3491 C CD1 . ILE B 1 138 ? 22.370  -38.879 6.904   1.00 18.20  ? 363  ILE B CD1 1 
ATOM   3492 N N   . THR B 1 139 ? 27.630  -41.616 7.455   1.00 13.35  ? 364  THR B N   1 
ATOM   3493 C CA  . THR B 1 139 ? 28.347  -42.846 7.751   1.00 13.86  ? 364  THR B CA  1 
ATOM   3494 C C   . THR B 1 139 ? 28.091  -43.250 9.199   1.00 13.42  ? 364  THR B C   1 
ATOM   3495 O O   . THR B 1 139 ? 27.479  -42.513 9.975   1.00 15.60  ? 364  THR B O   1 
ATOM   3496 C CB  . THR B 1 139 ? 29.849  -42.692 7.473   1.00 16.30  ? 364  THR B CB  1 
ATOM   3497 O OG1 . THR B 1 139 ? 30.347  -41.514 8.119   1.00 16.80  ? 364  THR B OG1 1 
ATOM   3498 C CG2 . THR B 1 139 ? 30.088  -42.582 5.971   1.00 17.04  ? 364  THR B CG2 1 
ATOM   3499 N N   . ALA B 1 140 ? 28.553  -44.455 9.549   1.00 18.99  ? 365  ALA B N   1 
ATOM   3500 C CA  . ALA B 1 140 ? 28.244  -45.074 10.841  1.00 17.87  ? 365  ALA B CA  1 
ATOM   3501 C C   . ALA B 1 140 ? 26.737  -45.126 11.088  1.00 13.59  ? 365  ALA B C   1 
ATOM   3502 O O   . ALA B 1 140 ? 26.278  -45.065 12.231  1.00 15.72  ? 365  ALA B O   1 
ATOM   3503 C CB  . ALA B 1 140 ? 28.949  -44.360 11.998  1.00 15.04  ? 365  ALA B CB  1 
ATOM   3504 N N   . TRP B 1 141 ? 25.958  -45.257 10.010  1.00 15.38  ? 366  TRP B N   1 
ATOM   3505 C CA  . TRP B 1 141 ? 24.505  -45.338 10.109  1.00 17.00  ? 366  TRP B CA  1 
ATOM   3506 C C   . TRP B 1 141 ? 24.102  -46.720 10.608  1.00 16.81  ? 366  TRP B C   1 
ATOM   3507 O O   . TRP B 1 141 ? 24.512  -47.731 10.030  1.00 17.23  ? 366  TRP B O   1 
ATOM   3508 C CB  . TRP B 1 141 ? 23.876  -45.056 8.742   1.00 15.36  ? 366  TRP B CB  1 
ATOM   3509 C CG  . TRP B 1 141 ? 22.391  -45.179 8.731   1.00 14.25  ? 366  TRP B CG  1 
ATOM   3510 C CD1 . TRP B 1 141 ? 21.658  -46.185 8.172   1.00 16.17  ? 366  TRP B CD1 1 
ATOM   3511 C CD2 . TRP B 1 141 ? 21.451  -44.269 9.315   1.00 13.01  ? 366  TRP B CD2 1 
ATOM   3512 N NE1 . TRP B 1 141 ? 20.314  -45.957 8.367   1.00 17.05  ? 366  TRP B NE1 1 
ATOM   3513 C CE2 . TRP B 1 141 ? 20.159  -44.788 9.064   1.00 15.32  ? 366  TRP B CE2 1 
ATOM   3514 C CE3 . TRP B 1 141 ? 21.573  -43.065 10.028  1.00 15.69  ? 366  TRP B CE3 1 
ATOM   3515 C CZ2 . TRP B 1 141 ? 18.995  -44.149 9.505   1.00 15.81  ? 366  TRP B CZ2 1 
ATOM   3516 C CZ3 . TRP B 1 141 ? 20.410  -42.420 10.467  1.00 15.81  ? 366  TRP B CZ3 1 
ATOM   3517 C CH2 . TRP B 1 141 ? 19.138  -42.965 10.199  1.00 13.76  ? 366  TRP B CH2 1 
ATOM   3518 N N   . ASP B 1 142 ? 23.299  -46.773 11.677  1.00 13.76  ? 367  ASP B N   1 
ATOM   3519 C CA  . ASP B 1 142 ? 23.108  -48.036 12.395  1.00 16.53  ? 367  ASP B CA  1 
ATOM   3520 C C   . ASP B 1 142 ? 21.718  -48.653 12.238  1.00 20.45  ? 367  ASP B C   1 
ATOM   3521 O O   . ASP B 1 142 ? 21.407  -49.637 12.926  1.00 17.27  ? 367  ASP B O   1 
ATOM   3522 C CB  . ASP B 1 142 ? 23.457  -47.857 13.882  1.00 18.37  ? 367  ASP B CB  1 
ATOM   3523 C CG  . ASP B 1 142 ? 22.567  -46.858 14.605  1.00 20.37  ? 367  ASP B CG  1 
ATOM   3524 O OD1 . ASP B 1 142 ? 21.471  -46.521 14.113  1.00 15.50  ? 367  ASP B OD1 1 
ATOM   3525 O OD2 . ASP B 1 142 ? 22.966  -46.420 15.714  1.00 22.94  ? 367  ASP B OD2 1 
ATOM   3526 N N   . ALA B 1 143 ? 20.883  -48.133 11.345  1.00 17.43  ? 368  ALA B N   1 
ATOM   3527 C CA  . ALA B 1 143 ? 19.595  -48.758 11.058  1.00 15.08  ? 368  ALA B CA  1 
ATOM   3528 C C   . ALA B 1 143 ? 19.693  -49.573 9.775   1.00 15.27  ? 368  ALA B C   1 
ATOM   3529 O O   . ALA B 1 143 ? 20.543  -49.318 8.922   1.00 21.81  ? 368  ALA B O   1 
ATOM   3530 C CB  . ALA B 1 143 ? 18.489  -47.704 10.938  1.00 17.83  ? 368  ALA B CB  1 
ATOM   3531 N N   . THR B 1 144 ? 18.817  -50.578 9.650   1.00 16.93  ? 369  THR B N   1 
ATOM   3532 C CA  . THR B 1 144 ? 18.882  -51.452 8.481   1.00 17.75  ? 369  THR B CA  1 
ATOM   3533 C C   . THR B 1 144 ? 18.296  -50.787 7.246   1.00 20.20  ? 369  THR B C   1 
ATOM   3534 O O   . THR B 1 144 ? 18.707  -51.107 6.123   1.00 22.91  ? 369  THR B O   1 
ATOM   3535 C CB  . THR B 1 144 ? 18.149  -52.765 8.740   1.00 27.17  ? 369  THR B CB  1 
ATOM   3536 O OG1 . THR B 1 144 ? 16.775  -52.481 9.007   1.00 22.69  ? 369  THR B OG1 1 
ATOM   3537 C CG2 . THR B 1 144 ? 18.756  -53.493 9.928   1.00 26.46  ? 369  THR B CG2 1 
ATOM   3538 N N   . GLY B 1 145 ? 17.324  -49.896 7.428   1.00 20.29  ? 370  GLY B N   1 
ATOM   3539 C CA  . GLY B 1 145 ? 16.809  -49.091 6.343   1.00 20.13  ? 370  GLY B CA  1 
ATOM   3540 C C   . GLY B 1 145 ? 17.274  -47.653 6.451   1.00 17.78  ? 370  GLY B C   1 
ATOM   3541 O O   . GLY B 1 145 ? 18.026  -47.282 7.361   1.00 17.67  ? 370  GLY B O   1 
ATOM   3542 N N   . PRO B 1 146 ? 16.784  -46.796 5.552   1.00 15.05  ? 371  PRO B N   1 
ATOM   3543 C CA  . PRO B 1 146 ? 15.764  -47.060 4.528   1.00 15.54  ? 371  PRO B CA  1 
ATOM   3544 C C   . PRO B 1 146 ? 16.269  -47.692 3.249   1.00 20.14  ? 371  PRO B C   1 
ATOM   3545 O O   . PRO B 1 146 ? 17.470  -47.729 2.972   1.00 18.51  ? 371  PRO B O   1 
ATOM   3546 C CB  . PRO B 1 146 ? 15.237  -45.653 4.220   1.00 15.04  ? 371  PRO B CB  1 
ATOM   3547 C CG  . PRO B 1 146 ? 16.444  -44.788 4.382   1.00 14.52  ? 371  PRO B CG  1 
ATOM   3548 C CD  . PRO B 1 146 ? 17.138  -45.365 5.602   1.00 14.44  ? 371  PRO B CD  1 
ATOM   3549 N N   A SER B 1 147 ? 15.345  -48.188 2.432   0.35 16.81  ? 372  SER B N   1 
ATOM   3550 N N   B SER B 1 147 ? 15.343  -48.203 2.437   0.65 16.82  ? 372  SER B N   1 
ATOM   3551 C CA  A SER B 1 147 ? 15.655  -48.521 1.051   0.35 17.45  ? 372  SER B CA  1 
ATOM   3552 C CA  B SER B 1 147 ? 15.649  -48.508 1.050   0.65 17.44  ? 372  SER B CA  1 
ATOM   3553 C C   A SER B 1 147 ? 15.765  -47.218 0.261   0.35 17.29  ? 372  SER B C   1 
ATOM   3554 C C   B SER B 1 147 ? 15.748  -47.203 0.261   0.65 17.28  ? 372  SER B C   1 
ATOM   3555 O O   A SER B 1 147 ? 15.704  -46.118 0.820   0.35 17.07  ? 372  SER B O   1 
ATOM   3556 O O   B SER B 1 147 ? 15.669  -46.103 0.818   0.65 16.89  ? 372  SER B O   1 
ATOM   3557 C CB  A SER B 1 147 ? 14.605  -49.473 0.484   0.35 25.08  ? 372  SER B CB  1 
ATOM   3558 C CB  B SER B 1 147 ? 14.597  -49.449 0.462   0.65 25.23  ? 372  SER B CB  1 
ATOM   3559 O OG  A SER B 1 147 ? 14.533  -50.660 1.254   0.35 23.22  ? 372  SER B OG  1 
ATOM   3560 O OG  B SER B 1 147 ? 13.287  -48.930 0.624   0.65 25.40  ? 372  SER B OG  1 
ATOM   3561 N N   . ALA B 1 148 ? 15.930  -47.325 -1.053  1.00 21.23  ? 373  ALA B N   1 
ATOM   3562 C CA  . ALA B 1 148 ? 16.143  -46.150 -1.885  1.00 18.78  ? 373  ALA B CA  1 
ATOM   3563 C C   . ALA B 1 148 ? 14.839  -45.397 -2.125  1.00 17.28  ? 373  ALA B C   1 
ATOM   3564 O O   . ALA B 1 148 ? 13.759  -45.991 -2.206  1.00 17.71  ? 373  ALA B O   1 
ATOM   3565 C CB  . ALA B 1 148 ? 16.764  -46.549 -3.223  1.00 25.16  ? 373  ALA B CB  1 
ATOM   3566 N N   . GLY B 1 149 ? 14.962  -44.075 -2.266  1.00 18.01  ? 374  GLY B N   1 
ATOM   3567 C CA  . GLY B 1 149 ? 13.833  -43.220 -2.599  1.00 16.65  ? 374  GLY B CA  1 
ATOM   3568 C C   . GLY B 1 149 ? 12.930  -42.878 -1.438  1.00 16.66  ? 374  GLY B C   1 
ATOM   3569 O O   . GLY B 1 149 ? 11.789  -42.460 -1.661  1.00 18.50  ? 374  GLY B O   1 
ATOM   3570 N N   . VAL B 1 150 ? 13.418  -43.016 -0.208  1.00 15.66  ? 375  VAL B N   1 
ATOM   3571 C CA  . VAL B 1 150 ? 12.615  -42.875 1.001   1.00 15.25  ? 375  VAL B CA  1 
ATOM   3572 C C   . VAL B 1 150 ? 12.927  -41.535 1.649   1.00 14.46  ? 375  VAL B C   1 
ATOM   3573 O O   . VAL B 1 150 ? 14.100  -41.183 1.825   1.00 14.13  ? 375  VAL B O   1 
ATOM   3574 C CB  . VAL B 1 150 ? 12.898  -44.034 1.974   1.00 17.59  ? 375  VAL B CB  1 
ATOM   3575 C CG1 . VAL B 1 150 ? 12.240  -43.796 3.333   1.00 17.42  ? 375  VAL B CG1 1 
ATOM   3576 C CG2 . VAL B 1 150 ? 12.459  -45.365 1.337   1.00 18.62  ? 375  VAL B CG2 1 
ATOM   3577 N N   . GLU B 1 151 ? 11.885  -40.786 2.008   1.00 14.21  ? 376  GLU B N   1 
ATOM   3578 C CA  . GLU B 1 151 ? 12.095  -39.523 2.710   1.00 13.51  ? 376  GLU B CA  1 
ATOM   3579 C C   . GLU B 1 151 ? 12.615  -39.768 4.122   1.00 13.10  ? 376  GLU B C   1 
ATOM   3580 O O   . GLU B 1 151 ? 12.146  -40.668 4.827   1.00 17.01  ? 376  GLU B O   1 
ATOM   3581 C CB  . GLU B 1 151 ? 10.802  -38.717 2.808   1.00 17.11  ? 376  GLU B CB  1 
ATOM   3582 C CG  . GLU B 1 151 ? 10.235  -38.244 1.497   1.00 30.88  ? 376  GLU B CG  1 
ATOM   3583 C CD  . GLU B 1 151 ? 9.272   -37.079 1.674   1.00 35.32  ? 376  GLU B CD  1 
ATOM   3584 O OE1 . GLU B 1 151 ? 9.218   -36.512 2.788   1.00 53.80  ? 376  GLU B OE1 1 
ATOM   3585 O OE2 . GLU B 1 151 ? 8.572   -36.737 0.702   1.00 49.04  ? 376  GLU B OE2 1 
ATOM   3586 N N   . MET B 1 152 ? 13.580  -38.958 4.532   1.00 12.56  ? 377  MET B N   1 
ATOM   3587 C CA  . MET B 1 152 ? 14.140  -39.000 5.879   1.00 12.41  ? 377  MET B CA  1 
ATOM   3588 C C   . MET B 1 152 ? 14.200  -37.597 6.462   1.00 15.24  ? 377  MET B C   1 
ATOM   3589 O O   . MET B 1 152 ? 14.453  -36.632 5.739   1.00 15.91  ? 377  MET B O   1 
ATOM   3590 C CB  . MET B 1 152 ? 15.557  -39.591 5.869   1.00 14.41  ? 377  MET B CB  1 
ATOM   3591 C CG  . MET B 1 152 ? 15.630  -41.011 5.332   1.00 16.74  ? 377  MET B CG  1 
ATOM   3592 S SD  . MET B 1 152 ? 14.963  -42.189 6.531   1.00 14.55  ? 377  MET B SD  1 
ATOM   3593 C CE  . MET B 1 152 ? 16.167  -42.069 7.856   1.00 14.64  ? 377  MET B CE  1 
ATOM   3594 N N   A THR B 1 153 ? 13.986  -37.496 7.779   0.61 11.31  ? 378  THR B N   1 
ATOM   3595 N N   B THR B 1 153 ? 13.947  -37.482 7.763   0.39 11.38  ? 378  THR B N   1 
ATOM   3596 C CA  A THR B 1 153 ? 14.134  -36.240 8.511   0.61 11.53  ? 378  THR B CA  1 
ATOM   3597 C CA  B THR B 1 153 ? 14.190  -36.238 8.482   0.39 11.52  ? 378  THR B CA  1 
ATOM   3598 C C   A THR B 1 153 ? 14.967  -36.481 9.761   0.61 13.27  ? 378  THR B C   1 
ATOM   3599 C C   B THR B 1 153 ? 15.068  -36.530 9.685   0.39 13.25  ? 378  THR B C   1 
ATOM   3600 O O   A THR B 1 153 ? 14.795  -37.497 10.441  0.61 14.26  ? 378  THR B O   1 
ATOM   3601 O O   B THR B 1 153 ? 15.035  -37.627 10.247  0.39 13.43  ? 378  THR B O   1 
ATOM   3602 C CB  A THR B 1 153 ? 12.771  -35.661 8.899   0.61 16.34  ? 378  THR B CB  1 
ATOM   3603 C CB  B THR B 1 153 ? 12.893  -35.561 8.942   0.39 16.78  ? 378  THR B CB  1 
ATOM   3604 O OG1 A THR B 1 153 ? 11.902  -35.710 7.767   0.61 23.55  ? 378  THR B OG1 1 
ATOM   3605 O OG1 B THR B 1 153 ? 12.144  -36.458 9.769   0.39 15.79  ? 378  THR B OG1 1 
ATOM   3606 C CG2 A THR B 1 153 ? 12.910  -34.215 9.348   0.61 11.70  ? 378  THR B CG2 1 
ATOM   3607 C CG2 B THR B 1 153 ? 12.061  -35.159 7.752   0.39 18.50  ? 378  THR B CG2 1 
ATOM   3608 N N   . GLY B 1 154 ? 15.862  -35.544 10.075  1.00 10.27  ? 379  GLY B N   1 
ATOM   3609 C CA  . GLY B 1 154 ? 16.738  -35.764 11.199  1.00 14.77  ? 379  GLY B CA  1 
ATOM   3610 C C   . GLY B 1 154 ? 17.230  -34.511 11.881  1.00 12.36  ? 379  GLY B C   1 
ATOM   3611 O O   . GLY B 1 154 ? 16.825  -33.392 11.546  1.00 12.05  ? 379  GLY B O   1 
ATOM   3612 N N   A GLN B 1 155 ? 18.128  -34.702 12.846  0.57 11.72  ? 380  GLN B N   1 
ATOM   3613 N N   B GLN B 1 155 ? 18.122  -34.723 12.846  0.43 11.71  ? 380  GLN B N   1 
ATOM   3614 C CA  A GLN B 1 155 ? 18.594  -33.632 13.711  0.57 11.82  ? 380  GLN B CA  1 
ATOM   3615 C CA  B GLN B 1 155 ? 18.658  -33.644 13.657  0.43 11.77  ? 380  GLN B CA  1 
ATOM   3616 C C   A GLN B 1 155 ? 20.084  -33.805 13.961  0.57 13.79  ? 380  GLN B C   1 
ATOM   3617 C C   B GLN B 1 155 ? 20.111  -33.951 13.984  0.43 13.22  ? 380  GLN B C   1 
ATOM   3618 O O   A GLN B 1 155 ? 20.558  -34.927 14.153  0.57 11.78  ? 380  GLN B O   1 
ATOM   3619 O O   B GLN B 1 155 ? 20.450  -35.086 14.326  0.43 11.99  ? 380  GLN B O   1 
ATOM   3620 C CB  A GLN B 1 155 ? 17.811  -33.628 15.042  0.57 10.84  ? 380  GLN B CB  1 
ATOM   3621 C CB  B GLN B 1 155 ? 17.847  -33.461 14.947  0.43 11.51  ? 380  GLN B CB  1 
ATOM   3622 C CG  A GLN B 1 155 ? 17.699  -34.998 15.711  0.57 11.37  ? 380  GLN B CG  1 
ATOM   3623 C CG  B GLN B 1 155 ? 18.386  -32.375 15.858  0.43 9.57   ? 380  GLN B CG  1 
ATOM   3624 C CD  A GLN B 1 155 ? 16.548  -35.088 16.716  0.57 20.94  ? 380  GLN B CD  1 
ATOM   3625 C CD  B GLN B 1 155 ? 17.435  -32.033 16.982  0.43 14.14  ? 380  GLN B CD  1 
ATOM   3626 O OE1 A GLN B 1 155 ? 15.380  -34.814 16.383  0.57 15.66  ? 380  GLN B OE1 1 
ATOM   3627 O OE1 B GLN B 1 155 ? 16.348  -32.607 17.090  0.43 10.36  ? 380  GLN B OE1 1 
ATOM   3628 N NE2 A GLN B 1 155 ? 16.873  -35.485 17.952  0.57 13.82  ? 380  GLN B NE2 1 
ATOM   3629 N NE2 B GLN B 1 155 ? 17.840  -31.089 17.832  0.43 16.49  ? 380  GLN B NE2 1 
ATOM   3630 N N   A ILE B 1 156 ? 20.818  -32.694 13.914  0.57 12.24  ? 381  ILE B N   1 
ATOM   3631 N N   B ILE B 1 156 ? 20.958  -32.936 13.855  0.43 12.71  ? 381  ILE B N   1 
ATOM   3632 C CA  A ILE B 1 156 ? 22.217  -32.667 14.327  0.57 15.74  ? 381  ILE B CA  1 
ATOM   3633 C CA  B ILE B 1 156 ? 22.354  -33.020 14.264  0.43 12.62  ? 381  ILE B CA  1 
ATOM   3634 C C   A ILE B 1 156 ? 22.234  -32.457 15.836  0.57 11.49  ? 381  ILE B C   1 
ATOM   3635 C C   B ILE B 1 156 ? 22.412  -32.684 15.749  0.43 12.40  ? 381  ILE B C   1 
ATOM   3636 O O   A ILE B 1 156 ? 21.654  -31.489 16.342  0.57 10.62  ? 381  ILE B O   1 
ATOM   3637 O O   B ILE B 1 156 ? 21.978  -31.603 16.164  0.43 13.12  ? 381  ILE B O   1 
ATOM   3638 C CB  A ILE B 1 156 ? 22.993  -31.560 13.595  0.57 13.71  ? 381  ILE B CB  1 
ATOM   3639 C CB  B ILE B 1 156 ? 23.231  -32.074 13.431  0.43 10.06  ? 381  ILE B CB  1 
ATOM   3640 C CG1 A ILE B 1 156 ? 22.876  -31.727 12.080  0.57 15.24  ? 381  ILE B CG1 1 
ATOM   3641 C CG1 B ILE B 1 156 ? 23.196  -32.500 11.960  0.43 10.73  ? 381  ILE B CG1 1 
ATOM   3642 C CG2 A ILE B 1 156 ? 24.453  -31.570 14.003  0.57 9.02   ? 381  ILE B CG2 1 
ATOM   3643 C CG2 B ILE B 1 156 ? 24.647  -32.043 13.967  0.43 11.51  ? 381  ILE B CG2 1 
ATOM   3644 C CD1 A ILE B 1 156 ? 23.573  -32.952 11.566  0.57 14.97  ? 381  ILE B CD1 1 
ATOM   3645 C CD1 B ILE B 1 156 ? 23.863  -31.515 11.013  0.43 9.29   ? 381  ILE B CD1 1 
ATOM   3646 N N   A GLU B 1 157 ? 22.886  -33.371 16.562  0.57 11.96  ? 382  GLU B N   1 
ATOM   3647 N N   B GLU B 1 157 ? 22.938  -33.616 16.548  0.43 11.36  ? 382  GLU B N   1 
ATOM   3648 C CA  A GLU B 1 157 ? 22.785  -33.410 18.016  0.57 10.43  ? 382  GLU B CA  1 
ATOM   3649 C CA  B GLU B 1 157 ? 22.812  -33.588 18.002  0.43 10.74  ? 382  GLU B CA  1 
ATOM   3650 C C   A GLU B 1 157 ? 24.071  -33.070 18.749  0.57 10.24  ? 382  GLU B C   1 
ATOM   3651 C C   B GLU B 1 157 ? 24.054  -33.084 18.719  0.43 10.28  ? 382  GLU B C   1 
ATOM   3652 O O   A GLU B 1 157 ? 24.004  -32.643 19.907  0.57 11.92  ? 382  GLU B O   1 
ATOM   3653 O O   B GLU B 1 157 ? 23.945  -32.543 19.825  0.43 12.30  ? 382  GLU B O   1 
ATOM   3654 C CB  A GLU B 1 157 ? 22.331  -34.801 18.476  0.57 12.99  ? 382  GLU B CB  1 
ATOM   3655 C CB  B GLU B 1 157 ? 22.498  -34.995 18.527  0.43 11.90  ? 382  GLU B CB  1 
ATOM   3656 C CG  A GLU B 1 157 ? 20.969  -35.188 17.955  0.57 9.15   ? 382  GLU B CG  1 
ATOM   3657 C CG  B GLU B 1 157 ? 21.447  -35.750 17.723  0.43 11.08  ? 382  GLU B CG  1 
ATOM   3658 C CD  A GLU B 1 157 ? 20.570  -36.583 18.372  0.57 14.44  ? 382  GLU B CD  1 
ATOM   3659 C CD  B GLU B 1 157 ? 20.035  -35.315 18.054  0.43 18.99  ? 382  GLU B CD  1 
ATOM   3660 O OE1 A GLU B 1 157 ? 21.460  -37.413 18.643  0.57 17.77  ? 382  GLU B OE1 1 
ATOM   3661 O OE1 B GLU B 1 157 ? 19.874  -34.234 18.660  0.43 17.32  ? 382  GLU B OE1 1 
ATOM   3662 O OE2 A GLU B 1 157 ? 19.359  -36.842 18.436  0.57 16.93  ? 382  GLU B OE2 1 
ATOM   3663 O OE2 B GLU B 1 157 ? 19.086  -36.060 17.721  0.43 17.02  ? 382  GLU B OE2 1 
ATOM   3664 N N   . SER B 1 158 ? 25.224  -33.273 18.125  1.00 12.78  ? 383  SER B N   1 
ATOM   3665 C CA  . SER B 1 158 ? 26.502  -33.017 18.773  1.00 10.90  ? 383  SER B CA  1 
ATOM   3666 C C   . SER B 1 158 ? 27.540  -33.043 17.664  1.00 10.92  ? 383  SER B C   1 
ATOM   3667 O O   . SER B 1 158 ? 27.226  -33.351 16.513  1.00 14.12  ? 383  SER B O   1 
ATOM   3668 C CB  . SER B 1 158 ? 26.796  -34.049 19.865  1.00 15.57  ? 383  SER B CB  1 
ATOM   3669 O OG  . SER B 1 158 ? 26.668  -35.366 19.368  1.00 16.36  ? 383  SER B OG  1 
ATOM   3670 N N   A ILE B 1 159 ? 28.781  -32.736 18.026  0.27 10.64  ? 384  ILE B N   1 
ATOM   3671 N N   B ILE B 1 159 ? 28.772  -32.667 18.005  0.73 10.52  ? 384  ILE B N   1 
ATOM   3672 C CA  A ILE B 1 159 ? 29.876  -32.694 17.070  0.27 11.35  ? 384  ILE B CA  1 
ATOM   3673 C CA  B ILE B 1 159 ? 29.872  -32.661 17.045  0.73 11.27  ? 384  ILE B CA  1 
ATOM   3674 C C   A ILE B 1 159 ? 31.114  -33.333 17.679  0.27 14.23  ? 384  ILE B C   1 
ATOM   3675 C C   B ILE B 1 159 ? 31.120  -33.273 17.666  0.73 14.28  ? 384  ILE B C   1 
ATOM   3676 O O   A ILE B 1 159 ? 31.267  -33.422 18.898  0.27 15.08  ? 384  ILE B O   1 
ATOM   3677 O O   B ILE B 1 159 ? 31.290  -33.290 18.889  0.73 14.98  ? 384  ILE B O   1 
ATOM   3678 C CB  A ILE B 1 159 ? 30.201  -31.254 16.630  0.27 13.03  ? 384  ILE B CB  1 
ATOM   3679 C CB  B ILE B 1 159 ? 30.196  -31.241 16.512  0.73 13.03  ? 384  ILE B CB  1 
ATOM   3680 C CG1 A ILE B 1 159 ? 30.279  -30.355 17.862  0.27 14.71  ? 384  ILE B CG1 1 
ATOM   3681 C CG1 B ILE B 1 159 ? 30.480  -30.257 17.661  0.73 14.36  ? 384  ILE B CG1 1 
ATOM   3682 C CG2 A ILE B 1 159 ? 29.169  -30.756 15.625  0.27 12.96  ? 384  ILE B CG2 1 
ATOM   3683 C CG2 B ILE B 1 159 ? 29.086  -30.759 15.570  0.73 12.95  ? 384  ILE B CG2 1 
ATOM   3684 C CD1 A ILE B 1 159 ? 30.679  -28.958 17.561  0.27 11.90  ? 384  ILE B CD1 1 
ATOM   3685 C CD1 B ILE B 1 159 ? 29.265  -29.461 18.138  0.73 15.56  ? 384  ILE B CD1 1 
ATOM   3686 N N   . GLY B 1 160 ? 31.994  -33.789 16.801  1.00 12.75  ? 385  GLY B N   1 
ATOM   3687 C CA  . GLY B 1 160 ? 33.353  -34.094 17.178  1.00 15.88  ? 385  GLY B CA  1 
ATOM   3688 C C   . GLY B 1 160 ? 34.109  -32.803 16.947  1.00 19.65  ? 385  GLY B C   1 
ATOM   3689 O O   . GLY B 1 160 ? 34.111  -32.282 15.828  1.00 15.93  ? 385  GLY B O   1 
ATOM   3690 N N   . MET B 1 161 ? 34.714  -32.240 17.985  1.00 16.73  ? 386  MET B N   1 
ATOM   3691 C CA  . MET B 1 161 ? 35.191  -30.855 17.903  1.00 15.81  ? 386  MET B CA  1 
ATOM   3692 C C   . MET B 1 161 ? 36.527  -30.748 18.631  1.00 17.75  ? 386  MET B C   1 
ATOM   3693 O O   . MET B 1 161 ? 36.567  -30.495 19.839  1.00 20.51  ? 386  MET B O   1 
ATOM   3694 C CB  . MET B 1 161 ? 34.151  -29.903 18.481  1.00 13.53  ? 386  MET B CB  1 
ATOM   3695 C CG  . MET B 1 161 ? 34.419  -28.455 18.156  1.00 15.99  ? 386  MET B CG  1 
ATOM   3696 S SD  . MET B 1 161 ? 34.292  -28.179 16.379  1.00 14.79  ? 386  MET B SD  1 
ATOM   3697 C CE  . MET B 1 161 ? 34.211  -26.382 16.371  1.00 11.44  ? 386  MET B CE  1 
ATOM   3698 N N   . GLU B 1 162 ? 37.612  -30.920 17.874  1.00 14.72  ? 387  GLU B N   1 
ATOM   3699 C CA  . GLU B 1 162 ? 38.950  -30.896 18.459  1.00 16.73  ? 387  GLU B CA  1 
ATOM   3700 C C   . GLU B 1 162 ? 39.323  -29.505 18.965  1.00 23.13  ? 387  GLU B C   1 
ATOM   3701 O O   . GLU B 1 162 ? 40.029  -29.378 19.974  1.00 22.59  ? 387  GLU B O   1 
ATOM   3702 C CB  . GLU B 1 162 ? 39.968  -31.380 17.427  1.00 19.12  ? 387  GLU B CB  1 
ATOM   3703 C CG  . GLU B 1 162 ? 41.321  -31.746 18.023  1.00 35.52  ? 387  GLU B CG  1 
ATOM   3704 C CD  . GLU B 1 162 ? 41.278  -33.050 18.801  1.00 56.39  ? 387  GLU B CD  1 
ATOM   3705 O OE1 . GLU B 1 162 ? 40.765  -34.054 18.254  1.00 45.92  ? 387  GLU B OE1 1 
ATOM   3706 O OE2 . GLU B 1 162 ? 41.749  -33.068 19.959  1.00 49.48  ? 387  GLU B OE2 1 
ATOM   3707 N N   . ASN B 1 163 ? 38.889  -28.450 18.267  1.00 18.02  ? 388  ASN B N   1 
ATOM   3708 C CA  . ASN B 1 163 ? 39.359  -27.095 18.550  1.00 19.81  ? 388  ASN B CA  1 
ATOM   3709 C C   . ASN B 1 163 ? 38.186  -26.136 18.641  1.00 17.43  ? 388  ASN B C   1 
ATOM   3710 O O   . ASN B 1 163 ? 37.409  -26.011 17.686  1.00 14.67  ? 388  ASN B O   1 
ATOM   3711 C CB  . ASN B 1 163 ? 40.346  -26.628 17.477  1.00 21.02  ? 388  ASN B CB  1 
ATOM   3712 C CG  . ASN B 1 163 ? 41.644  -27.413 17.511  1.00 24.77  ? 388  ASN B CG  1 
ATOM   3713 O OD1 . ASN B 1 163 ? 42.397  -27.344 18.484  1.00 39.63  ? 388  ASN B OD1 1 
ATOM   3714 N ND2 . ASN B 1 163 ? 41.905  -28.170 16.455  1.00 30.84  ? 388  ASN B ND2 1 
ATOM   3715 N N   . ASN B 1 164 ? 38.067  -25.444 19.781  1.00 17.78  ? 389  ASN B N   1 
ATOM   3716 C CA  . ASN B 1 164 ? 36.958  -24.509 19.949  1.00 16.31  ? 389  ASN B CA  1 
ATOM   3717 C C   . ASN B 1 164 ? 37.006  -23.396 18.909  1.00 14.22  ? 389  ASN B C   1 
ATOM   3718 O O   . ASN B 1 164 ? 35.959  -22.868 18.515  1.00 15.09  ? 389  ASN B O   1 
ATOM   3719 C CB  . ASN B 1 164 ? 36.961  -23.914 21.363  1.00 16.17  ? 389  ASN B CB  1 
ATOM   3720 C CG  . ASN B 1 164 ? 35.591  -23.359 21.761  1.00 15.68  ? 389  ASN B CG  1 
ATOM   3721 O OD1 . ASN B 1 164 ? 34.655  -24.115 21.991  1.00 15.90  ? 389  ASN B OD1 1 
ATOM   3722 N ND2 . ASN B 1 164 ? 35.466  -22.032 21.799  1.00 18.46  ? 389  ASN B ND2 1 
ATOM   3723 N N   . THR B 1 165 ? 38.202  -23.027 18.448  1.00 16.42  ? 390  THR B N   1 
ATOM   3724 C CA  . THR B 1 165 ? 38.294  -21.943 17.480  1.00 12.49  ? 390  THR B CA  1 
ATOM   3725 C C   . THR B 1 165 ? 37.602  -22.281 16.168  1.00 14.70  ? 390  THR B C   1 
ATOM   3726 O O   . THR B 1 165 ? 37.258  -21.366 15.408  1.00 14.88  ? 390  THR B O   1 
ATOM   3727 C CB  . THR B 1 165 ? 39.756  -21.586 17.222  1.00 18.59  ? 390  THR B CB  1 
ATOM   3728 O OG1 . THR B 1 165 ? 40.486  -22.770 16.871  1.00 18.16  ? 390  THR B OG1 1 
ATOM   3729 C CG2 . THR B 1 165 ? 40.361  -20.956 18.472  1.00 16.16  ? 390  THR B CG2 1 
ATOM   3730 N N   . ASP B 1 166 ? 37.363  -23.567 15.897  1.00 13.61  ? 391  ASP B N   1 
ATOM   3731 C CA  . ASP B 1 166 ? 36.721  -23.931 14.641  1.00 15.74  ? 391  ASP B CA  1 
ATOM   3732 C C   . ASP B 1 166 ? 35.246  -23.555 14.603  1.00 13.32  ? 391  ASP B C   1 
ATOM   3733 O O   . ASP B 1 166 ? 34.645  -23.593 13.521  1.00 11.95  ? 391  ASP B O   1 
ATOM   3734 C CB  . ASP B 1 166 ? 36.893  -25.425 14.375  1.00 13.48  ? 391  ASP B CB  1 
ATOM   3735 C CG  . ASP B 1 166 ? 38.238  -25.754 13.726  1.00 18.01  ? 391  ASP B CG  1 
ATOM   3736 O OD1 . ASP B 1 166 ? 38.814  -24.873 13.040  1.00 16.24  ? 391  ASP B OD1 1 
ATOM   3737 O OD2 . ASP B 1 166 ? 38.707  -26.899 13.879  1.00 19.94  ? 391  ASP B OD2 1 
ATOM   3738 N N   . PHE B 1 167 ? 34.647  -23.165 15.732  1.00 12.53  ? 392  PHE B N   1 
ATOM   3739 C CA  . PHE B 1 167 ? 33.279  -22.666 15.653  1.00 12.71  ? 392  PHE B CA  1 
ATOM   3740 C C   . PHE B 1 167 ? 33.189  -21.399 14.812  1.00 12.97  ? 392  PHE B C   1 
ATOM   3741 O O   . PHE B 1 167 ? 32.111  -21.095 14.288  1.00 13.59  ? 392  PHE B O   1 
ATOM   3742 C CB  . PHE B 1 167 ? 32.695  -22.393 17.040  1.00 13.89  ? 392  PHE B CB  1 
ATOM   3743 C CG  . PHE B 1 167 ? 32.330  -23.637 17.807  1.00 10.50  ? 392  PHE B CG  1 
ATOM   3744 C CD1 . PHE B 1 167 ? 31.318  -24.473 17.351  1.00 12.67  ? 392  PHE B CD1 1 
ATOM   3745 C CD2 . PHE B 1 167 ? 32.971  -23.945 19.007  1.00 14.90  ? 392  PHE B CD2 1 
ATOM   3746 C CE1 . PHE B 1 167 ? 30.968  -25.620 18.067  1.00 12.89  ? 392  PHE B CE1 1 
ATOM   3747 C CE2 . PHE B 1 167 ? 32.622  -25.085 19.724  1.00 14.20  ? 392  PHE B CE2 1 
ATOM   3748 C CZ  . PHE B 1 167 ? 31.624  -25.926 19.253  1.00 14.85  ? 392  PHE B CZ  1 
ATOM   3749 N N   . ASP B 1 168 ? 34.292  -20.659 14.664  1.00 13.33  ? 393  ASP B N   1 
ATOM   3750 C CA  . ASP B 1 168 ? 34.309  -19.440 13.868  1.00 11.62  ? 393  ASP B CA  1 
ATOM   3751 C C   . ASP B 1 168 ? 34.981  -19.630 12.505  1.00 12.30  ? 393  ASP B C   1 
ATOM   3752 O O   . ASP B 1 168 ? 35.355  -18.642 11.865  1.00 13.43  ? 393  ASP B O   1 
ATOM   3753 C CB  . ASP B 1 168 ? 35.004  -18.313 14.638  1.00 14.02  ? 393  ASP B CB  1 
ATOM   3754 C CG  . ASP B 1 168 ? 34.201  -17.826 15.831  1.00 16.03  ? 393  ASP B CG  1 
ATOM   3755 O OD1 . ASP B 1 168 ? 32.979  -18.089 15.891  1.00 15.01  ? 393  ASP B OD1 1 
ATOM   3756 O OD2 . ASP B 1 168 ? 34.794  -17.157 16.707  1.00 17.23  ? 393  ASP B OD2 1 
ATOM   3757 N N   . VAL B 1 169 ? 35.152  -20.875 12.053  1.00 12.34  ? 394  VAL B N   1 
ATOM   3758 C CA  . VAL B 1 169 ? 35.754  -21.184 10.757  1.00 11.31  ? 394  VAL B CA  1 
ATOM   3759 C C   . VAL B 1 169 ? 34.674  -21.820 9.887   1.00 13.31  ? 394  VAL B C   1 
ATOM   3760 O O   . VAL B 1 169 ? 34.198  -22.928 10.176  1.00 12.86  ? 394  VAL B O   1 
ATOM   3761 C CB  . VAL B 1 169 ? 36.970  -22.112 10.901  1.00 12.27  ? 394  VAL B CB  1 
ATOM   3762 C CG1 . VAL B 1 169 ? 37.539  -22.458 9.550   1.00 14.71  ? 394  VAL B CG1 1 
ATOM   3763 C CG2 . VAL B 1 169 ? 38.043  -21.458 11.768  1.00 13.58  ? 394  VAL B CG2 1 
ATOM   3764 N N   . LEU B 1 170 ? 34.274  -21.129 8.826   1.00 12.37  ? 395  LEU B N   1 
ATOM   3765 C CA  . LEU B 1 170 ? 33.243  -21.673 7.951   1.00 12.17  ? 395  LEU B CA  1 
ATOM   3766 C C   . LEU B 1 170 ? 33.709  -23.007 7.373   1.00 11.89  ? 395  LEU B C   1 
ATOM   3767 O O   . LEU B 1 170 ? 34.894  -23.167 7.051   1.00 13.36  ? 395  LEU B O   1 
ATOM   3768 C CB  . LEU B 1 170 ? 32.934  -20.708 6.803   1.00 11.63  ? 395  LEU B CB  1 
ATOM   3769 C CG  . LEU B 1 170 ? 32.126  -19.458 7.134   1.00 12.45  ? 395  LEU B CG  1 
ATOM   3770 C CD1 . LEU B 1 170 ? 31.964  -18.643 5.844   1.00 13.98  ? 395  LEU B CD1 1 
ATOM   3771 C CD2 . LEU B 1 170 ? 30.785  -19.849 7.748   1.00 11.67  ? 395  LEU B CD2 1 
ATOM   3772 N N   . PRO B 1 171 ? 32.813  -23.971 7.206   1.00 14.09  ? 396  PRO B N   1 
ATOM   3773 C CA  . PRO B 1 171 ? 33.190  -25.243 6.584   1.00 12.88  ? 396  PRO B CA  1 
ATOM   3774 C C   . PRO B 1 171 ? 33.316  -25.094 5.074   1.00 14.07  ? 396  PRO B C   1 
ATOM   3775 O O   . PRO B 1 171 ? 32.879  -24.110 4.474   1.00 16.59  ? 396  PRO B O   1 
ATOM   3776 C CB  . PRO B 1 171 ? 32.010  -26.148 6.950   1.00 13.75  ? 396  PRO B CB  1 
ATOM   3777 C CG  . PRO B 1 171 ? 30.841  -25.184 6.873   1.00 10.50  ? 396  PRO B CG  1 
ATOM   3778 C CD  . PRO B 1 171 ? 31.365  -23.905 7.485   1.00 10.47  ? 396  PRO B CD  1 
ATOM   3779 N N   . ASP B 1 172 ? 33.946  -26.100 4.459   1.00 14.68  ? 397  ASP B N   1 
ATOM   3780 C CA  . ASP B 1 172 ? 34.110  -26.144 3.002   1.00 15.75  ? 397  ASP B CA  1 
ATOM   3781 C C   . ASP B 1 172 ? 32.831  -26.735 2.412   1.00 15.26  ? 397  ASP B C   1 
ATOM   3782 O O   . ASP B 1 172 ? 32.774  -27.892 1.993   1.00 15.54  ? 397  ASP B O   1 
ATOM   3783 C CB  . ASP B 1 172 ? 35.335  -26.962 2.633   1.00 13.33  ? 397  ASP B CB  1 
ATOM   3784 C CG  . ASP B 1 172 ? 35.633  -26.930 1.146   1.00 33.27  ? 397  ASP B CG  1 
ATOM   3785 O OD1 . ASP B 1 172 ? 35.120  -26.028 0.447   1.00 25.00  ? 397  ASP B OD1 1 
ATOM   3786 O OD2 . ASP B 1 172 ? 36.379  -27.815 0.679   1.00 37.97  ? 397  ASP B OD2 1 
ATOM   3787 N N   . TYR B 1 173 ? 31.788  -25.899 2.384   1.00 15.02  ? 398  TYR B N   1 
ATOM   3788 C CA  . TYR B 1 173 ? 30.440  -26.357 2.050   1.00 12.03  ? 398  TYR B CA  1 
ATOM   3789 C C   . TYR B 1 173 ? 30.348  -27.093 0.713   1.00 15.39  ? 398  TYR B C   1 
ATOM   3790 O O   . TYR B 1 173 ? 29.474  -27.951 0.548   1.00 15.16  ? 398  TYR B O   1 
ATOM   3791 C CB  . TYR B 1 173 ? 29.491  -25.179 1.970   1.00 11.85  ? 398  TYR B CB  1 
ATOM   3792 C CG  . TYR B 1 173 ? 29.080  -24.475 3.245   1.00 11.52  ? 398  TYR B CG  1 
ATOM   3793 C CD1 . TYR B 1 173 ? 28.071  -24.984 4.068   1.00 10.53  ? 398  TYR B CD1 1 
ATOM   3794 C CD2 . TYR B 1 173 ? 29.606  -23.232 3.547   1.00 12.24  ? 398  TYR B CD2 1 
ATOM   3795 C CE1 . TYR B 1 173 ? 27.640  -24.280 5.199   1.00 11.35  ? 398  TYR B CE1 1 
ATOM   3796 C CE2 . TYR B 1 173 ? 29.188  -22.524 4.658   1.00 12.27  ? 398  TYR B CE2 1 
ATOM   3797 C CZ  . TYR B 1 173 ? 28.206  -23.043 5.470   1.00 11.82  ? 398  TYR B CZ  1 
ATOM   3798 O OH  . TYR B 1 173 ? 27.790  -22.303 6.556   1.00 12.30  ? 398  TYR B OH  1 
ATOM   3799 N N   . ASN B 1 174 ? 31.174  -26.733 -0.273  1.00 18.31  ? 399  ASN B N   1 
ATOM   3800 C CA  . ASN B 1 174 ? 31.093  -27.370 -1.588  1.00 16.99  ? 399  ASN B CA  1 
ATOM   3801 C C   . ASN B 1 174 ? 32.276  -28.281 -1.883  1.00 17.01  ? 399  ASN B C   1 
ATOM   3802 O O   . ASN B 1 174 ? 32.440  -28.709 -3.037  1.00 18.38  ? 399  ASN B O   1 
ATOM   3803 C CB  . ASN B 1 174 ? 30.950  -26.328 -2.701  1.00 17.59  ? 399  ASN B CB  1 
ATOM   3804 C CG  . ASN B 1 174 ? 32.181  -25.445 -2.857  1.00 19.11  ? 399  ASN B CG  1 
ATOM   3805 O OD1 . ASN B 1 174 ? 33.212  -25.648 -2.218  1.00 26.45  ? 399  ASN B OD1 1 
ATOM   3806 N ND2 . ASN B 1 174 ? 32.075  -24.460 -3.743  1.00 31.61  ? 399  ASN B ND2 1 
ATOM   3807 N N   . GLY B 1 175 ? 33.097  -28.585 -0.877  1.00 17.37  ? 400  GLY B N   1 
ATOM   3808 C CA  . GLY B 1 175 ? 34.218  -29.484 -1.035  1.00 19.12  ? 400  GLY B CA  1 
ATOM   3809 C C   . GLY B 1 175 ? 35.289  -29.016 -1.989  1.00 35.47  ? 400  GLY B C   1 
ATOM   3810 O O   . GLY B 1 175 ? 36.123  -29.829 -2.397  1.00 34.83  ? 400  GLY B O   1 
ATOM   3811 N N   . SER B 1 176 ? 35.303  -27.732 -2.353  1.00 26.87  ? 401  SER B N   1 
ATOM   3812 C CA  . SER B 1 176 ? 36.192  -27.218 -3.387  1.00 32.01  ? 401  SER B CA  1 
ATOM   3813 C C   . SER B 1 176 ? 37.370  -26.442 -2.821  1.00 41.69  ? 401  SER B C   1 
ATOM   3814 O O   . SER B 1 176 ? 38.013  -25.688 -3.560  1.00 48.70  ? 401  SER B O   1 
ATOM   3815 C CB  . SER B 1 176 ? 35.421  -26.321 -4.354  1.00 32.95  ? 401  SER B CB  1 
ATOM   3816 O OG  . SER B 1 176 ? 35.115  -25.079 -3.739  1.00 41.45  ? 401  SER B OG  1 
ATOM   3817 N N   . ALA B 1 177 ? 37.661  -26.606 -1.532  1.00 37.32  ? 402  ALA B N   1 
ATOM   3818 C CA  . ALA B 1 177 ? 38.672  -25.801 -0.842  1.00 39.72  ? 402  ALA B CA  1 
ATOM   3819 C C   . ALA B 1 177 ? 38.374  -24.307 -0.990  1.00 42.99  ? 402  ALA B C   1 
ATOM   3820 O O   . ALA B 1 177 ? 39.231  -23.512 -1.384  1.00 43.50  ? 402  ALA B O   1 
ATOM   3821 C CB  . ALA B 1 177 ? 40.085  -26.142 -1.331  1.00 42.67  ? 402  ALA B CB  1 
ATOM   3822 N N   . PHE B 1 178 ? 37.129  -23.935 -0.681  1.00 48.78  ? 403  PHE B N   1 
ATOM   3823 C CA  . PHE B 1 178 ? 36.685  -22.544 -0.619  1.00 53.47  ? 403  PHE B CA  1 
ATOM   3824 C C   . PHE B 1 178 ? 36.991  -21.778 -1.903  1.00 55.59  ? 403  PHE B C   1 
ATOM   3825 O O   . PHE B 1 178 ? 37.995  -21.060 -1.964  1.00 62.28  ? 403  PHE B O   1 
ATOM   3826 C CB  . PHE B 1 178 ? 37.336  -21.831 0.573   1.00 48.29  ? 403  PHE B CB  1 
ATOM   3827 C CG  . PHE B 1 178 ? 37.298  -22.618 1.862   1.00 55.88  ? 403  PHE B CG  1 
ATOM   3828 C CD1 . PHE B 1 178 ? 36.197  -22.553 2.703   1.00 33.32  ? 403  PHE B CD1 1 
ATOM   3829 C CD2 . PHE B 1 178 ? 38.374  -23.406 2.244   1.00 42.41  ? 403  PHE B CD2 1 
ATOM   3830 C CE1 . PHE B 1 178 ? 36.167  -23.270 3.890   1.00 29.99  ? 403  PHE B CE1 1 
ATOM   3831 C CE2 . PHE B 1 178 ? 38.346  -24.123 3.426   1.00 40.80  ? 403  PHE B CE2 1 
ATOM   3832 C CZ  . PHE B 1 178 ? 37.240  -24.053 4.250   1.00 39.73  ? 403  PHE B CZ  1 
ATOM   3833 N N   . ASP B 1 179 ? 36.138  -21.895 -2.925  1.00 41.17  ? 404  ASP B N   1 
ATOM   3834 C CA  . ASP B 1 179 ? 36.426  -21.273 -4.214  1.00 47.47  ? 404  ASP B CA  1 
ATOM   3835 C C   . ASP B 1 179 ? 35.733  -19.929 -4.424  1.00 62.08  ? 404  ASP B C   1 
ATOM   3836 O O   . ASP B 1 179 ? 36.011  -19.262 -5.428  1.00 52.31  ? 404  ASP B O   1 
ATOM   3837 C CB  . ASP B 1 179 ? 36.075  -22.228 -5.371  1.00 46.03  ? 404  ASP B CB  1 
ATOM   3838 C CG  . ASP B 1 179 ? 34.585  -22.534 -5.473  1.00 59.80  ? 404  ASP B CG  1 
ATOM   3839 O OD1 . ASP B 1 179 ? 33.784  -22.010 -4.668  1.00 46.73  ? 404  ASP B OD1 1 
ATOM   3840 O OD2 . ASP B 1 179 ? 34.219  -23.317 -6.378  1.00 40.68  ? 404  ASP B OD2 1 
ATOM   3841 N N   . GLY B 1 180 ? 34.848  -19.512 -3.517  1.00 41.64  ? 405  GLY B N   1 
ATOM   3842 C CA  . GLY B 1 180 ? 34.255  -18.191 -3.596  1.00 33.52  ? 405  GLY B CA  1 
ATOM   3843 C C   . GLY B 1 180 ? 33.041  -18.059 -4.491  1.00 39.88  ? 405  GLY B C   1 
ATOM   3844 O O   . GLY B 1 180 ? 32.602  -16.933 -4.747  1.00 43.48  ? 405  GLY B O   1 
ATOM   3845 N N   . SER B 1 181 ? 32.483  -19.167 -4.981  1.00 27.66  ? 406  SER B N   1 
ATOM   3846 C CA  . SER B 1 181 ? 31.248  -19.120 -5.752  1.00 22.08  ? 406  SER B CA  1 
ATOM   3847 C C   . SER B 1 181 ? 30.003  -19.085 -4.875  1.00 21.97  ? 406  SER B C   1 
ATOM   3848 O O   . SER B 1 181 ? 28.903  -18.859 -5.396  1.00 25.59  ? 406  SER B O   1 
ATOM   3849 C CB  . SER B 1 181 ? 31.156  -20.333 -6.677  1.00 26.80  ? 406  SER B CB  1 
ATOM   3850 O OG  . SER B 1 181 ? 31.129  -21.529 -5.917  1.00 40.85  ? 406  SER B OG  1 
ATOM   3851 N N   . LEU B 1 182 ? 30.136  -19.304 -3.569  1.00 19.06  ? 407  LEU B N   1 
ATOM   3852 C CA  . LEU B 1 182 ? 28.966  -19.453 -2.721  1.00 18.20  ? 407  LEU B CA  1 
ATOM   3853 C C   . LEU B 1 182 ? 28.443  -18.099 -2.248  1.00 15.59  ? 407  LEU B C   1 
ATOM   3854 O O   . LEU B 1 182 ? 29.195  -17.140 -2.058  1.00 17.07  ? 407  LEU B O   1 
ATOM   3855 C CB  . LEU B 1 182 ? 29.276  -20.341 -1.518  1.00 16.34  ? 407  LEU B CB  1 
ATOM   3856 C CG  . LEU B 1 182 ? 29.622  -21.783 -1.913  1.00 17.65  ? 407  LEU B CG  1 
ATOM   3857 C CD1 . LEU B 1 182 ? 29.884  -22.632 -0.681  1.00 23.27  ? 407  LEU B CD1 1 
ATOM   3858 C CD2 . LEU B 1 182 ? 28.501  -22.374 -2.754  1.00 23.12  ? 407  LEU B CD2 1 
ATOM   3859 N N   . ASN B 1 183 ? 27.130  -18.036 -2.090  1.00 14.91  ? 408  ASN B N   1 
ATOM   3860 C CA  . ASN B 1 183 ? 26.430  -16.846 -1.609  1.00 13.92  ? 408  ASN B CA  1 
ATOM   3861 C C   . ASN B 1 183 ? 26.475  -16.853 -0.082  1.00 14.02  ? 408  ASN B C   1 
ATOM   3862 O O   . ASN B 1 183 ? 25.670  -17.523 0.572   1.00 15.20  ? 408  ASN B O   1 
ATOM   3863 C CB  . ASN B 1 183 ? 25.001  -16.869 -2.148  1.00 16.75  ? 408  ASN B CB  1 
ATOM   3864 C CG  . ASN B 1 183 ? 24.189  -15.676 -1.720  1.00 28.02  ? 408  ASN B CG  1 
ATOM   3865 O OD1 . ASN B 1 183 ? 24.734  -14.666 -1.300  1.00 22.65  ? 408  ASN B OD1 1 
ATOM   3866 N ND2 . ASN B 1 183 ? 22.867  -15.789 -1.829  1.00 23.47  ? 408  ASN B ND2 1 
ATOM   3867 N N   . LEU B 1 184 ? 27.430  -16.118 0.501   1.00 13.29  ? 409  LEU B N   1 
ATOM   3868 C CA  . LEU B 1 184 ? 27.648  -16.098 1.947   1.00 14.30  ? 409  LEU B CA  1 
ATOM   3869 C C   . LEU B 1 184 ? 27.350  -14.724 2.531   1.00 14.46  ? 409  LEU B C   1 
ATOM   3870 O O   . LEU B 1 184 ? 27.760  -13.702 1.971   1.00 16.49  ? 409  LEU B O   1 
ATOM   3871 C CB  . LEU B 1 184 ? 29.091  -16.466 2.288   1.00 15.23  ? 409  LEU B CB  1 
ATOM   3872 C CG  . LEU B 1 184 ? 29.581  -17.836 1.831   1.00 14.94  ? 409  LEU B CG  1 
ATOM   3873 C CD1 . LEU B 1 184 ? 31.072  -17.966 2.042   1.00 16.12  ? 409  LEU B CD1 1 
ATOM   3874 C CD2 . LEU B 1 184 ? 28.869  -18.905 2.626   1.00 16.42  ? 409  LEU B CD2 1 
ATOM   3875 N N   . ALA B 1 185 ? 26.665  -14.710 3.675   1.00 13.59  ? 410  ALA B N   1 
ATOM   3876 C CA  . ALA B 1 185 ? 26.489  -13.472 4.423   1.00 11.26  ? 410  ALA B CA  1 
ATOM   3877 C C   . ALA B 1 185 ? 27.851  -12.936 4.860   1.00 13.00  ? 410  ALA B C   1 
ATOM   3878 O O   . ALA B 1 185 ? 28.785  -13.704 5.103   1.00 14.88  ? 410  ALA B O   1 
ATOM   3879 C CB  . ALA B 1 185 ? 25.601  -13.707 5.646   1.00 12.47  ? 410  ALA B CB  1 
ATOM   3880 N N   . PRO B 1 186 ? 27.997  -11.621 4.967   1.00 13.33  ? 411  PRO B N   1 
ATOM   3881 C CA  . PRO B 1 186 ? 29.331  -11.030 5.132   1.00 16.39  ? 411  PRO B CA  1 
ATOM   3882 C C   . PRO B 1 186 ? 29.848  -11.166 6.553   1.00 11.53  ? 411  PRO B C   1 
ATOM   3883 O O   . PRO B 1 186 ? 29.083  -11.470 7.481   1.00 13.76  ? 411  PRO B O   1 
ATOM   3884 C CB  . PRO B 1 186 ? 29.107  -9.555  4.761   1.00 19.85  ? 411  PRO B CB  1 
ATOM   3885 C CG  . PRO B 1 186 ? 27.681  -9.306  5.064   1.00 20.88  ? 411  PRO B CG  1 
ATOM   3886 C CD  . PRO B 1 186 ? 26.946  -10.607 4.762   1.00 16.82  ? 411  PRO B CD  1 
ATOM   3887 N N   . PRO B 1 187 ? 31.148  -10.948 6.755   1.00 12.40  ? 412  PRO B N   1 
ATOM   3888 C CA  . PRO B 1 187 ? 31.711  -10.973 8.113   1.00 15.28  ? 412  PRO B CA  1 
ATOM   3889 C C   . PRO B 1 187 ? 31.094  -9.913  9.017   1.00 14.04  ? 412  PRO B C   1 
ATOM   3890 O O   . PRO B 1 187 ? 30.647  -8.851  8.568   1.00 16.28  ? 412  PRO B O   1 
ATOM   3891 C CB  . PRO B 1 187 ? 33.204  -10.700 7.883   1.00 15.82  ? 412  PRO B CB  1 
ATOM   3892 C CG  . PRO B 1 187 ? 33.450  -11.069 6.451   1.00 16.57  ? 412  PRO B CG  1 
ATOM   3893 C CD  . PRO B 1 187 ? 32.183  -10.701 5.737   1.00 13.40  ? 412  PRO B CD  1 
ATOM   3894 N N   . ILE B 1 188 ? 31.085  -10.218 10.312  1.00 13.12  ? 413  ILE B N   1 
ATOM   3895 C CA  . ILE B 1 188 ? 30.536  -9.339  11.336  1.00 12.44  ? 413  ILE B CA  1 
ATOM   3896 C C   . ILE B 1 188 ? 31.687  -8.520  11.914  1.00 15.25  ? 413  ILE B C   1 
ATOM   3897 O O   . ILE B 1 188 ? 32.550  -9.061  12.610  1.00 16.12  ? 413  ILE B O   1 
ATOM   3898 C CB  . ILE B 1 188 ? 29.835  -10.149 12.430  1.00 13.37  ? 413  ILE B CB  1 
ATOM   3899 C CG1 . ILE B 1 188 ? 28.687  -10.965 11.827  1.00 13.96  ? 413  ILE B CG1 1 
ATOM   3900 C CG2 . ILE B 1 188 ? 29.348  -9.220  13.533  1.00 14.70  ? 413  ILE B CG2 1 
ATOM   3901 C CD1 . ILE B 1 188 ? 28.128  -12.012 12.788  1.00 19.61  ? 413  ILE B CD1 1 
ATOM   3902 N N   . VAL B 1 189 ? 31.705  -7.219  11.627  1.00 12.61  ? 414  VAL B N   1 
ATOM   3903 C CA  . VAL B 1 189 ? 32.812  -6.352  12.032  1.00 15.70  ? 414  VAL B CA  1 
ATOM   3904 C C   . VAL B 1 189 ? 32.264  -5.094  12.699  1.00 18.32  ? 414  VAL B C   1 
ATOM   3905 O O   . VAL B 1 189 ? 31.474  -4.376  12.071  1.00 19.72  ? 414  VAL B O   1 
ATOM   3906 C CB  . VAL B 1 189 ? 33.684  -5.965  10.823  1.00 20.43  ? 414  VAL B CB  1 
ATOM   3907 C CG1 . VAL B 1 189 ? 34.913  -5.169  11.283  1.00 21.69  ? 414  VAL B CG1 1 
ATOM   3908 C CG2 . VAL B 1 189 ? 34.076  -7.197  10.004  1.00 16.87  ? 414  VAL B CG2 1 
ATOM   3909 N N   . PRO B 1 190 ? 32.670  -4.764  13.929  1.00 17.90  ? 415  PRO B N   1 
ATOM   3910 C CA  . PRO B 1 190 ? 32.225  -3.495  14.530  1.00 17.48  ? 415  PRO B CA  1 
ATOM   3911 C C   . PRO B 1 190 ? 32.613  -2.311  13.663  1.00 16.90  ? 415  PRO B C   1 
ATOM   3912 O O   . PRO B 1 190 ? 33.694  -2.274  13.074  1.00 16.78  ? 415  PRO B O   1 
ATOM   3913 C CB  . PRO B 1 190 ? 32.956  -3.454  15.876  1.00 16.65  ? 415  PRO B CB  1 
ATOM   3914 C CG  . PRO B 1 190 ? 33.238  -4.875  16.203  1.00 17.91  ? 415  PRO B CG  1 
ATOM   3915 C CD  . PRO B 1 190 ? 33.514  -5.538  14.856  1.00 16.87  ? 415  PRO B CD  1 
ATOM   3916 N N   . LEU B 1 191 ? 31.730  -1.320  13.604  1.00 17.26  ? 416  LEU B N   1 
ATOM   3917 C CA  . LEU B 1 191 ? 31.993  -0.192  12.720  1.00 16.21  ? 416  LEU B CA  1 
ATOM   3918 C C   . LEU B 1 191 ? 32.986  0.813   13.304  1.00 15.94  ? 416  LEU B C   1 
ATOM   3919 O O   . LEU B 1 191 ? 33.548  1.620   12.548  1.00 19.72  ? 416  LEU B O   1 
ATOM   3920 C CB  . LEU B 1 191 ? 30.674  0.490   12.354  1.00 19.30  ? 416  LEU B CB  1 
ATOM   3921 C CG  . LEU B 1 191 ? 29.698  -0.418  11.586  1.00 22.60  ? 416  LEU B CG  1 
ATOM   3922 C CD1 . LEU B 1 191 ? 28.489  0.383   11.156  1.00 21.68  ? 416  LEU B CD1 1 
ATOM   3923 C CD2 . LEU B 1 191 ? 30.373  -1.043  10.382  1.00 31.88  ? 416  LEU B CD2 1 
ATOM   3924 N N   . LEU B 1 192 ? 33.251  0.771   14.636  1.00 18.91  ? 417  LEU B N   1 
ATOM   3925 C CA  . LEU B 1 192 ? 34.308  1.595   15.210  1.00 18.46  ? 417  LEU B CA  1 
ATOM   3926 C C   . LEU B 1 192 ? 35.450  0.728   15.734  1.00 18.03  ? 417  LEU B C   1 
ATOM   3927 O O   . LEU B 1 192 ? 35.204  -0.349  16.284  1.00 18.40  ? 417  LEU B O   1 
ATOM   3928 C CB  . LEU B 1 192 ? 33.779  2.474   16.353  1.00 17.25  ? 417  LEU B CB  1 
ATOM   3929 C CG  . LEU B 1 192 ? 32.617  3.412   16.033  1.00 20.45  ? 417  LEU B CG  1 
ATOM   3930 C CD1 . LEU B 1 192 ? 32.310  4.295   17.237  1.00 18.33  ? 417  LEU B CD1 1 
ATOM   3931 C CD2 . LEU B 1 192 ? 32.959  4.273   14.833  1.00 20.77  ? 417  LEU B CD2 1 
ATOM   3932 N N   . PRO B 1 193 ? 36.701  1.174   15.585  1.00 21.88  ? 418  PRO B N   1 
ATOM   3933 C CA  . PRO B 1 193 ? 37.843  0.307   15.950  1.00 20.94  ? 418  PRO B CA  1 
ATOM   3934 C C   . PRO B 1 193 ? 37.950  -0.028  17.437  1.00 27.65  ? 418  PRO B C   1 
ATOM   3935 O O   . PRO B 1 193 ? 38.520  -1.074  17.777  1.00 28.47  ? 418  PRO B O   1 
ATOM   3936 C CB  . PRO B 1 193 ? 39.056  1.120   15.473  1.00 27.41  ? 418  PRO B CB  1 
ATOM   3937 C CG  . PRO B 1 193 ? 38.558  2.546   15.417  1.00 23.48  ? 418  PRO B CG  1 
ATOM   3938 C CD  . PRO B 1 193 ? 37.138  2.424   14.945  1.00 19.59  ? 418  PRO B CD  1 
ATOM   3939 N N   . GLY B 1 194 ? 37.447  0.813   18.335  1.00 22.23  ? 419  GLY B N   1 
ATOM   3940 C CA  . GLY B 1 194 ? 37.504  0.474   19.747  1.00 22.48  ? 419  GLY B CA  1 
ATOM   3941 C C   . GLY B 1 194 ? 36.409  -0.448  20.235  1.00 23.40  ? 419  GLY B C   1 
ATOM   3942 O O   . GLY B 1 194 ? 36.374  -0.814  21.417  1.00 23.95  ? 419  GLY B O   1 
ATOM   3943 N N   . GLU B 1 195 ? 35.507  -0.846  19.346  1.00 16.23  ? 420  GLU B N   1 
ATOM   3944 C CA  . GLU B 1 195 ? 34.379  -1.679  19.722  1.00 15.31  ? 420  GLU B CA  1 
ATOM   3945 C C   . GLU B 1 195 ? 34.728  -3.155  19.591  1.00 17.35  ? 420  GLU B C   1 
ATOM   3946 O O   . GLU B 1 195 ? 35.584  -3.543  18.789  1.00 16.96  ? 420  GLU B O   1 
ATOM   3947 C CB  . GLU B 1 195 ? 33.157  -1.338  18.866  1.00 15.12  ? 420  GLU B CB  1 
ATOM   3948 C CG  . GLU B 1 195 ? 32.579  0.031   19.206  1.00 15.76  ? 420  GLU B CG  1 
ATOM   3949 C CD  . GLU B 1 195 ? 31.497  0.483   18.240  1.00 18.46  ? 420  GLU B CD  1 
ATOM   3950 O OE1 . GLU B 1 195 ? 31.416  -0.070  17.120  1.00 17.38  ? 420  GLU B OE1 1 
ATOM   3951 O OE2 . GLU B 1 195 ? 30.732  1.408   18.607  1.00 18.50  ? 420  GLU B OE2 1 
ATOM   3952 N N   . THR B 1 196 ? 34.053  -3.978  20.402  1.00 14.32  ? 421  THR B N   1 
ATOM   3953 C CA  . THR B 1 196 ? 34.243  -5.423  20.423  1.00 15.52  ? 421  THR B CA  1 
ATOM   3954 C C   . THR B 1 196 ? 32.887  -6.105  20.307  1.00 14.72  ? 421  THR B C   1 
ATOM   3955 O O   . THR B 1 196 ? 31.921  -5.696  20.959  1.00 15.09  ? 421  THR B O   1 
ATOM   3956 C CB  . THR B 1 196 ? 34.951  -5.884  21.724  1.00 15.32  ? 421  THR B CB  1 
ATOM   3957 O OG1 . THR B 1 196 ? 36.228  -5.254  21.826  1.00 17.85  ? 421  THR B OG1 1 
ATOM   3958 C CG2 . THR B 1 196 ? 35.131  -7.411  21.749  1.00 15.43  ? 421  THR B CG2 1 
ATOM   3959 N N   . LEU B 1 197 ? 32.812  -7.135  19.460  1.00 12.79  ? 422  LEU B N   1 
ATOM   3960 C CA  . LEU B 1 197 ? 31.580  -7.894  19.301  1.00 13.39  ? 422  LEU B CA  1 
ATOM   3961 C C   . LEU B 1 197 ? 31.140  -8.503  20.631  1.00 16.87  ? 422  LEU B C   1 
ATOM   3962 O O   . LEU B 1 197 ? 31.937  -9.134  21.332  1.00 15.01  ? 422  LEU B O   1 
ATOM   3963 C CB  . LEU B 1 197 ? 31.789  -8.991  18.249  1.00 13.99  ? 422  LEU B CB  1 
ATOM   3964 C CG  . LEU B 1 197 ? 30.645  -9.982  18.036  1.00 12.94  ? 422  LEU B CG  1 
ATOM   3965 C CD1 . LEU B 1 197 ? 29.413  -9.302  17.437  1.00 14.49  ? 422  LEU B CD1 1 
ATOM   3966 C CD2 . LEU B 1 197 ? 31.114  -11.143 17.162  1.00 14.27  ? 422  LEU B CD2 1 
ATOM   3967 N N   . LEU B 1 198 ? 29.864  -8.318  20.980  1.00 13.36  ? 423  LEU B N   1 
ATOM   3968 C CA  . LEU B 1 198 ? 29.295  -8.951  22.164  1.00 11.45  ? 423  LEU B CA  1 
ATOM   3969 C C   . LEU B 1 198 ? 28.729  -10.311 21.764  1.00 11.72  ? 423  LEU B C   1 
ATOM   3970 O O   . LEU B 1 198 ? 27.866  -10.403 20.881  1.00 14.92  ? 423  LEU B O   1 
ATOM   3971 C CB  . LEU B 1 198 ? 28.218  -8.071  22.803  1.00 11.98  ? 423  LEU B CB  1 
ATOM   3972 C CG  . LEU B 1 198 ? 27.654  -8.590  24.129  1.00 14.62  ? 423  LEU B CG  1 
ATOM   3973 C CD1 . LEU B 1 198 ? 28.737  -8.562  25.224  1.00 14.57  ? 423  LEU B CD1 1 
ATOM   3974 C CD2 . LEU B 1 198 ? 26.424  -7.771  24.531  1.00 14.36  ? 423  LEU B CD2 1 
ATOM   3975 N N   . ARG B 1 199 ? 29.243  -11.368 22.391  1.00 10.89  ? 424  ARG B N   1 
ATOM   3976 C CA  . ARG B 1 199 ? 28.945  -12.740 21.993  1.00 12.27  ? 424  ARG B CA  1 
ATOM   3977 C C   . ARG B 1 199 ? 27.955  -13.372 22.961  1.00 11.55  ? 424  ARG B C   1 
ATOM   3978 O O   . ARG B 1 199 ? 28.154  -13.327 24.180  1.00 13.49  ? 424  ARG B O   1 
ATOM   3979 C CB  . ARG B 1 199 ? 30.231  -13.568 21.931  1.00 12.13  ? 424  ARG B CB  1 
ATOM   3980 C CG  . ARG B 1 199 ? 31.137  -13.131 20.769  1.00 11.39  ? 424  ARG B CG  1 
ATOM   3981 C CD  . ARG B 1 199 ? 32.479  -13.860 20.751  1.00 14.32  ? 424  ARG B CD  1 
ATOM   3982 N NE  . ARG B 1 199 ? 33.316  -13.425 19.633  1.00 15.17  ? 424  ARG B NE  1 
ATOM   3983 C CZ  . ARG B 1 199 ? 33.677  -14.203 18.620  1.00 15.39  ? 424  ARG B CZ  1 
ATOM   3984 N NH1 . ARG B 1 199 ? 33.367  -15.488 18.594  1.00 17.49  ? 424  ARG B NH1 1 
ATOM   3985 N NH2 . ARG B 1 199 ? 34.369  -13.677 17.613  1.00 19.16  ? 424  ARG B NH2 1 
ATOM   3986 N N   . PHE B 1 200 ? 26.888  -13.950 22.406  1.00 9.72   ? 425  PHE B N   1 
ATOM   3987 C CA  . PHE B 1 200 ? 25.912  -14.736 23.157  1.00 12.33  ? 425  PHE B CA  1 
ATOM   3988 C C   . PHE B 1 200 ? 26.304  -16.201 23.016  1.00 14.51  ? 425  PHE B C   1 
ATOM   3989 O O   . PHE B 1 200 ? 26.194  -16.760 21.924  1.00 13.62  ? 425  PHE B O   1 
ATOM   3990 C CB  . PHE B 1 200 ? 24.505  -14.502 22.609  1.00 9.93   ? 425  PHE B CB  1 
ATOM   3991 C CG  . PHE B 1 200 ? 24.036  -13.068 22.714  1.00 9.66   ? 425  PHE B CG  1 
ATOM   3992 C CD1 . PHE B 1 200 ? 24.276  -12.157 21.687  1.00 12.37  ? 425  PHE B CD1 1 
ATOM   3993 C CD2 . PHE B 1 200 ? 23.347  -12.644 23.839  1.00 13.24  ? 425  PHE B CD2 1 
ATOM   3994 C CE1 . PHE B 1 200 ? 23.834  -10.832 21.783  1.00 13.25  ? 425  PHE B CE1 1 
ATOM   3995 C CE2 . PHE B 1 200 ? 22.901  -11.321 23.958  1.00 13.43  ? 425  PHE B CE2 1 
ATOM   3996 C CZ  . PHE B 1 200 ? 23.143  -10.412 22.931  1.00 12.56  ? 425  PHE B CZ  1 
ATOM   3997 N N   . GLY B 1 201 ? 26.748  -16.829 24.105  1.00 12.92  ? 426  GLY B N   1 
ATOM   3998 C CA  . GLY B 1 201 ? 27.377  -18.141 24.035  1.00 11.08  ? 426  GLY B CA  1 
ATOM   3999 C C   . GLY B 1 201 ? 26.505  -19.246 24.607  1.00 14.50  ? 426  GLY B C   1 
ATOM   4000 O O   . GLY B 1 201 ? 25.686  -19.010 25.499  1.00 12.59  ? 426  GLY B O   1 
ATOM   4001 N N   . THR B 1 202 ? 26.675  -20.461 24.076  1.00 11.83  ? 427  THR B N   1 
ATOM   4002 C CA  . THR B 1 202 ? 26.028  -21.646 24.629  1.00 12.19  ? 427  THR B CA  1 
ATOM   4003 C C   . THR B 1 202 ? 27.001  -22.808 24.518  1.00 13.69  ? 427  THR B C   1 
ATOM   4004 O O   . THR B 1 202 ? 28.039  -22.715 23.859  1.00 13.54  ? 427  THR B O   1 
ATOM   4005 C CB  . THR B 1 202 ? 24.705  -21.993 23.929  1.00 14.70  ? 427  THR B CB  1 
ATOM   4006 O OG1 . THR B 1 202 ? 24.013  -23.015 24.680  1.00 15.92  ? 427  THR B OG1 1 
ATOM   4007 C CG2 . THR B 1 202 ? 24.962  -22.499 22.528  1.00 14.12  ? 427  THR B CG2 1 
ATOM   4008 N N   . VAL B 1 203 ? 26.667  -23.907 25.182  1.00 13.56  ? 428  VAL B N   1 
ATOM   4009 C CA  . VAL B 1 203 ? 27.548  -25.067 25.252  1.00 13.76  ? 428  VAL B CA  1 
ATOM   4010 C C   . VAL B 1 203 ? 26.914  -26.175 24.416  1.00 15.21  ? 428  VAL B C   1 
ATOM   4011 O O   . VAL B 1 203 ? 25.876  -26.722 24.806  1.00 14.64  ? 428  VAL B O   1 
ATOM   4012 C CB  . VAL B 1 203 ? 27.774  -25.533 26.698  1.00 15.96  ? 428  VAL B CB  1 
ATOM   4013 C CG1 . VAL B 1 203 ? 28.658  -26.778 26.694  1.00 16.27  ? 428  VAL B CG1 1 
ATOM   4014 C CG2 . VAL B 1 203 ? 28.426  -24.429 27.544  1.00 14.65  ? 428  VAL B CG2 1 
ATOM   4015 N N   . PRO B 1 204 ? 27.476  -26.528 23.267  1.00 12.61  ? 429  PRO B N   1 
ATOM   4016 C CA  . PRO B 1 204 ? 27.016  -27.721 22.561  1.00 12.37  ? 429  PRO B CA  1 
ATOM   4017 C C   . PRO B 1 204 ? 27.694  -28.942 23.145  1.00 11.96  ? 429  PRO B C   1 
ATOM   4018 O O   . PRO B 1 204 ? 28.781  -28.862 23.717  1.00 14.03  ? 429  PRO B O   1 
ATOM   4019 C CB  . PRO B 1 204 ? 27.486  -27.481 21.123  1.00 12.54  ? 429  PRO B CB  1 
ATOM   4020 C CG  . PRO B 1 204 ? 28.796  -26.737 21.320  1.00 13.35  ? 429  PRO B CG  1 
ATOM   4021 C CD  . PRO B 1 204 ? 28.631  -25.899 22.602  1.00 13.54  ? 429  PRO B CD  1 
ATOM   4022 N N   . ILE B 1 205 ? 27.039  -30.089 22.996  1.00 12.22  ? 430  ILE B N   1 
ATOM   4023 C CA  . ILE B 1 205 ? 27.687  -31.338 23.378  1.00 11.80  ? 430  ILE B CA  1 
ATOM   4024 C C   . ILE B 1 205 ? 28.698  -31.685 22.298  1.00 13.57  ? 430  ILE B C   1 
ATOM   4025 O O   . ILE B 1 205 ? 28.358  -31.708 21.109  1.00 12.56  ? 430  ILE B O   1 
ATOM   4026 C CB  . ILE B 1 205 ? 26.656  -32.464 23.551  1.00 12.31  ? 430  ILE B CB  1 
ATOM   4027 C CG1 . ILE B 1 205 ? 25.717  -32.146 24.716  1.00 12.22  ? 430  ILE B CG1 1 
ATOM   4028 C CG2 . ILE B 1 205 ? 27.365  -33.807 23.727  1.00 13.96  ? 430  ILE B CG2 1 
ATOM   4029 C CD1 . ILE B 1 205 ? 24.570  -33.147 24.864  1.00 11.05  ? 430  ILE B CD1 1 
ATOM   4030 N N   . THR B 1 206 ? 29.954  -31.916 22.693  1.00 13.60  ? 431  THR B N   1 
ATOM   4031 C CA  . THR B 1 206 ? 30.962  -32.344 21.729  1.00 13.00  ? 431  THR B CA  1 
ATOM   4032 C C   . THR B 1 206 ? 31.844  -33.444 22.313  1.00 14.66  ? 431  THR B C   1 
ATOM   4033 O O   . THR B 1 206 ? 32.044  -33.541 23.527  1.00 16.84  ? 431  THR B O   1 
ATOM   4034 C CB  . THR B 1 206 ? 31.880  -31.195 21.204  1.00 17.59  ? 431  THR B CB  1 
ATOM   4035 O OG1 . THR B 1 206 ? 33.128  -31.188 21.898  1.00 20.48  ? 431  THR B OG1 1 
ATOM   4036 C CG2 . THR B 1 206 ? 31.230  -29.820 21.337  1.00 14.36  ? 431  THR B CG2 1 
ATOM   4037 N N   . THR B 1 207 ? 32.362  -34.278 21.412  1.00 15.17  ? 432  THR B N   1 
ATOM   4038 C CA  . THR B 1 207 ? 33.448  -35.203 21.699  1.00 15.25  ? 432  THR B CA  1 
ATOM   4039 C C   . THR B 1 207 ? 34.776  -34.555 21.318  1.00 15.04  ? 432  THR B C   1 
ATOM   4040 O O   . THR B 1 207 ? 34.831  -33.402 20.879  1.00 16.92  ? 432  THR B O   1 
ATOM   4041 C CB  . THR B 1 207 ? 33.262  -36.512 20.936  1.00 20.82  ? 432  THR B CB  1 
ATOM   4042 O OG1 . THR B 1 207 ? 33.188  -36.237 19.530  1.00 19.52  ? 432  THR B OG1 1 
ATOM   4043 C CG2 . THR B 1 207 ? 31.997  -37.211 21.382  1.00 22.93  ? 432  THR B CG2 1 
ATOM   4044 N N   . ARG B 1 208 ? 35.861  -35.316 21.475  1.00 18.00  ? 433  ARG B N   1 
ATOM   4045 C CA  . ARG B 1 208 ? 37.225  -34.848 21.215  1.00 21.60  ? 433  ARG B CA  1 
ATOM   4046 C C   . ARG B 1 208 ? 37.619  -33.715 22.162  1.00 25.68  ? 433  ARG B C   1 
ATOM   4047 O O   . ARG B 1 208 ? 38.364  -32.806 21.787  1.00 20.25  ? 433  ARG B O   1 
ATOM   4048 C CB  . ARG B 1 208 ? 37.411  -34.430 19.748  1.00 20.96  ? 433  ARG B CB  1 
ATOM   4049 C CG  . ARG B 1 208 ? 37.025  -35.515 18.744  1.00 18.58  ? 433  ARG B CG  1 
ATOM   4050 C CD  . ARG B 1 208 ? 37.354  -35.103 17.327  1.00 20.86  ? 433  ARG B CD  1 
ATOM   4051 N NE  . ARG B 1 208 ? 37.090  -36.175 16.376  1.00 23.21  ? 433  ARG B NE  1 
ATOM   4052 C CZ  . ARG B 1 208 ? 37.995  -37.048 15.960  1.00 38.92  ? 433  ARG B CZ  1 
ATOM   4053 N NH1 . ARG B 1 208 ? 39.240  -37.020 16.408  1.00 37.67  ? 433  ARG B NH1 1 
ATOM   4054 N NH2 . ARG B 1 208 ? 37.641  -37.975 15.075  1.00 35.28  ? 433  ARG B NH2 1 
ATOM   4055 N N   . ARG B 1 209 ? 37.114  -33.778 23.395  1.00 21.56  ? 434  ARG B N   1 
ATOM   4056 C CA  . ARG B 1 209 ? 37.369  -32.787 24.432  1.00 26.52  ? 434  ARG B CA  1 
ATOM   4057 C C   . ARG B 1 209 ? 38.417  -33.238 25.439  1.00 27.37  ? 434  ARG B C   1 
ATOM   4058 O O   . ARG B 1 209 ? 38.539  -32.623 26.503  1.00 29.45  ? 434  ARG B O   1 
ATOM   4059 C CB  . ARG B 1 209 ? 36.073  -32.458 25.174  1.00 20.73  ? 434  ARG B CB  1 
ATOM   4060 C CG  . ARG B 1 209 ? 35.014  -31.854 24.302  1.00 19.80  ? 434  ARG B CG  1 
ATOM   4061 C CD  . ARG B 1 209 ? 33.868  -31.292 25.115  1.00 18.38  ? 434  ARG B CD  1 
ATOM   4062 N NE  . ARG B 1 209 ? 33.154  -32.326 25.855  1.00 19.69  ? 434  ARG B NE  1 
ATOM   4063 C CZ  . ARG B 1 209 ? 33.203  -32.482 27.172  1.00 20.88  ? 434  ARG B CZ  1 
ATOM   4064 N NH1 . ARG B 1 209 ? 33.870  -31.642 27.944  1.00 20.44  ? 434  ARG B NH1 1 
ATOM   4065 N NH2 . ARG B 1 209 ? 32.546  -33.493 27.729  1.00 17.09  ? 434  ARG B NH2 1 
ATOM   4066 N N   . GLN B 1 210 ? 39.166  -34.300 25.137  1.00 22.90  ? 435  GLN B N   1 
ATOM   4067 C CA  . GLN B 1 210 ? 40.052  -34.889 26.141  1.00 34.17  ? 435  GLN B CA  1 
ATOM   4068 C C   . GLN B 1 210 ? 41.106  -33.901 26.614  1.00 44.52  ? 435  GLN B C   1 
ATOM   4069 O O   . GLN B 1 210 ? 41.572  -33.987 27.756  1.00 37.76  ? 435  GLN B O   1 
ATOM   4070 C CB  . GLN B 1 210 ? 40.735  -36.143 25.585  1.00 32.76  ? 435  GLN B CB  1 
ATOM   4071 C CG  . GLN B 1 210 ? 39.785  -37.204 25.049  1.00 53.14  ? 435  GLN B CG  1 
ATOM   4072 C CD  . GLN B 1 210 ? 39.490  -37.036 23.567  1.00 60.58  ? 435  GLN B CD  1 
ATOM   4073 O OE1 . GLN B 1 210 ? 39.836  -36.017 22.958  1.00 55.02  ? 435  GLN B OE1 1 
ATOM   4074 N NE2 . GLN B 1 210 ? 38.855  -38.044 22.975  1.00 48.51  ? 435  GLN B NE2 1 
ATOM   4075 N N   . SER B 1 211 ? 41.482  -32.954 25.760  1.00 24.77  ? 436  SER B N   1 
ATOM   4076 C CA  . SER B 1 211 ? 42.606  -32.061 25.998  1.00 40.42  ? 436  SER B CA  1 
ATOM   4077 C C   . SER B 1 211 ? 42.190  -30.680 26.490  1.00 33.06  ? 436  SER B C   1 
ATOM   4078 O O   . SER B 1 211 ? 42.889  -30.078 27.315  1.00 26.94  ? 436  SER B O   1 
ATOM   4079 C CB  . SER B 1 211 ? 43.412  -31.930 24.706  1.00 49.69  ? 436  SER B CB  1 
ATOM   4080 O OG  . SER B 1 211 ? 43.956  -33.176 24.306  1.00 40.50  ? 436  SER B OG  1 
ATOM   4081 N N   . ASP B 1 212 ? 41.080  -30.155 25.975  1.00 25.80  ? 437  ASP B N   1 
ATOM   4082 C CA  . ASP B 1 212 ? 40.537  -28.863 26.388  1.00 22.92  ? 437  ASP B CA  1 
ATOM   4083 C C   . ASP B 1 212 ? 39.030  -29.055 26.441  1.00 21.63  ? 437  ASP B C   1 
ATOM   4084 O O   . ASP B 1 212 ? 38.360  -29.062 25.395  1.00 27.62  ? 437  ASP B O   1 
ATOM   4085 C CB  . ASP B 1 212 ? 40.916  -27.739 25.425  1.00 31.54  ? 437  ASP B CB  1 
ATOM   4086 C CG  . ASP B 1 212 ? 40.156  -26.444 25.697  1.00 34.95  ? 437  ASP B CG  1 
ATOM   4087 O OD1 . ASP B 1 212 ? 39.662  -26.245 26.829  1.00 48.54  ? 437  ASP B OD1 1 
ATOM   4088 O OD2 . ASP B 1 212 ? 40.042  -25.618 24.765  1.00 56.84  ? 437  ASP B OD2 1 
ATOM   4089 N N   . PRO B 1 213 ? 38.464  -29.231 27.635  1.00 22.41  ? 438  PRO B N   1 
ATOM   4090 C CA  . PRO B 1 213 ? 37.067  -29.676 27.735  1.00 19.49  ? 438  PRO B CA  1 
ATOM   4091 C C   . PRO B 1 213 ? 36.020  -28.589 27.579  1.00 18.26  ? 438  PRO B C   1 
ATOM   4092 O O   . PRO B 1 213 ? 34.830  -28.928 27.534  1.00 21.62  ? 438  PRO B O   1 
ATOM   4093 C CB  . PRO B 1 213 ? 37.000  -30.282 29.140  1.00 20.39  ? 438  PRO B CB  1 
ATOM   4094 C CG  . PRO B 1 213 ? 38.070  -29.562 29.905  1.00 19.69  ? 438  PRO B CG  1 
ATOM   4095 C CD  . PRO B 1 213 ? 39.178  -29.317 28.918  1.00 24.49  ? 438  PRO B CD  1 
ATOM   4096 N N   . ILE B 1 214 ? 36.389  -27.312 27.505  1.00 19.67  ? 439  ILE B N   1 
ATOM   4097 C CA  . ILE B 1 214 ? 35.395  -26.242 27.430  1.00 16.24  ? 439  ILE B CA  1 
ATOM   4098 C C   . ILE B 1 214 ? 35.062  -25.998 25.967  1.00 19.02  ? 439  ILE B C   1 
ATOM   4099 O O   . ILE B 1 214 ? 35.958  -25.716 25.164  1.00 16.19  ? 439  ILE B O   1 
ATOM   4100 C CB  . ILE B 1 214 ? 35.905  -24.956 28.098  1.00 21.95  ? 439  ILE B CB  1 
ATOM   4101 C CG1 . ILE B 1 214 ? 36.074  -25.181 29.603  1.00 20.50  ? 439  ILE B CG1 1 
ATOM   4102 C CG2 . ILE B 1 214 ? 34.966  -23.800 27.820  1.00 22.62  ? 439  ILE B CG2 1 
ATOM   4103 C CD1 . ILE B 1 214 ? 34.816  -25.746 30.266  1.00 23.35  ? 439  ILE B CD1 1 
ATOM   4104 N N   . ARG B 1 215 ? 33.779  -26.108 25.621  1.00 14.08  ? 440  ARG B N   1 
ATOM   4105 C CA  . ARG B 1 215 ? 33.296  -25.804 24.280  1.00 14.37  ? 440  ARG B CA  1 
ATOM   4106 C C   . ARG B 1 215 ? 32.205  -24.750 24.361  1.00 17.23  ? 440  ARG B C   1 
ATOM   4107 O O   . ARG B 1 215 ? 31.211  -24.922 25.079  1.00 14.88  ? 440  ARG B O   1 
ATOM   4108 C CB  . ARG B 1 215 ? 32.777  -27.052 23.569  1.00 16.76  ? 440  ARG B CB  1 
ATOM   4109 C CG  . ARG B 1 215 ? 33.850  -28.054 23.221  1.00 18.74  ? 440  ARG B CG  1 
ATOM   4110 C CD  . ARG B 1 215 ? 34.739  -27.586 22.085  1.00 16.99  ? 440  ARG B CD  1 
ATOM   4111 N NE  . ARG B 1 215 ? 35.797  -28.559 21.839  1.00 16.46  ? 440  ARG B NE  1 
ATOM   4112 C CZ  . ARG B 1 215 ? 36.920  -28.602 22.540  1.00 20.28  ? 440  ARG B CZ  1 
ATOM   4113 N NH1 . ARG B 1 215 ? 37.170  -27.710 23.487  1.00 23.23  ? 440  ARG B NH1 1 
ATOM   4114 N NH2 . ARG B 1 215 ? 37.807  -29.564 22.291  1.00 20.47  ? 440  ARG B NH2 1 
ATOM   4115 N N   . ILE B 1 216 ? 32.393  -23.659 23.622  1.00 13.25  ? 441  ILE B N   1 
ATOM   4116 C CA  . ILE B 1 216 ? 31.453  -22.542 23.610  1.00 12.60  ? 441  ILE B CA  1 
ATOM   4117 C C   . ILE B 1 216 ? 31.272  -22.103 22.168  1.00 11.36  ? 441  ILE B C   1 
ATOM   4118 O O   . ILE B 1 216 ? 32.258  -21.794 21.488  1.00 14.76  ? 441  ILE B O   1 
ATOM   4119 C CB  . ILE B 1 216 ? 31.953  -21.354 24.452  1.00 13.87  ? 441  ILE B CB  1 
ATOM   4120 C CG1 . ILE B 1 216 ? 32.069  -21.762 25.921  1.00 16.86  ? 441  ILE B CG1 1 
ATOM   4121 C CG2 . ILE B 1 216 ? 31.011  -20.188 24.266  1.00 15.16  ? 441  ILE B CG2 1 
ATOM   4122 C CD1 . ILE B 1 216 ? 32.868  -20.787 26.772  1.00 26.03  ? 441  ILE B CD1 1 
ATOM   4123 N N   . ILE B 1 217 ? 30.024  -22.076 21.700  1.00 10.66  ? 442  ILE B N   1 
ATOM   4124 C CA  . ILE B 1 217 ? 29.687  -21.549 20.382  1.00 11.00  ? 442  ILE B CA  1 
ATOM   4125 C C   . ILE B 1 217 ? 28.900  -20.264 20.604  1.00 15.32  ? 442  ILE B C   1 
ATOM   4126 O O   . ILE B 1 217 ? 28.016  -20.217 21.468  1.00 14.04  ? 442  ILE B O   1 
ATOM   4127 C CB  . ILE B 1 217 ? 28.902  -22.576 19.530  1.00 11.35  ? 442  ILE B CB  1 
ATOM   4128 C CG1 . ILE B 1 217 ? 28.680  -22.038 18.105  1.00 13.60  ? 442  ILE B CG1 1 
ATOM   4129 C CG2 . ILE B 1 217 ? 27.558  -22.975 20.181  1.00 12.23  ? 442  ILE B CG2 1 
ATOM   4130 C CD1 . ILE B 1 217 ? 27.946  -23.033 17.161  1.00 13.05  ? 442  ILE B CD1 1 
ATOM   4131 N N   . SER B 1 218 ? 29.242  -19.218 19.850  1.00 14.16  ? 443  SER B N   1 
ATOM   4132 C CA  . SER B 1 218 ? 28.653  -17.896 20.020  1.00 12.04  ? 443  SER B CA  1 
ATOM   4133 C C   . SER B 1 218 ? 27.718  -17.551 18.873  1.00 15.59  ? 443  SER B C   1 
ATOM   4134 O O   . SER B 1 218 ? 27.801  -18.119 17.784  1.00 14.50  ? 443  SER B O   1 
ATOM   4135 C CB  . SER B 1 218 ? 29.737  -16.824 20.112  1.00 12.11  ? 443  SER B CB  1 
ATOM   4136 O OG  . SER B 1 218 ? 30.498  -16.976 21.294  1.00 16.96  ? 443  SER B OG  1 
ATOM   4137 N N   . CYS B 1 219 ? 26.834  -16.583 19.115  1.00 10.69  ? 444  CYS B N   1 
ATOM   4138 C CA  . CYS B 1 219 ? 25.957  -16.106 18.048  1.00 9.20   ? 444  CYS B CA  1 
ATOM   4139 C C   . CYS B 1 219 ? 25.742  -14.610 18.235  1.00 14.15  ? 444  CYS B C   1 
ATOM   4140 O O   . CYS B 1 219 ? 26.032  -14.058 19.298  1.00 13.23  ? 444  CYS B O   1 
ATOM   4141 C CB  . CYS B 1 219 ? 24.626  -16.883 18.018  1.00 8.68   ? 444  CYS B CB  1 
ATOM   4142 S SG  . CYS B 1 219 ? 23.610  -16.654 19.507  1.00 12.08  ? 444  CYS B SG  1 
ATOM   4143 N N   . ALA B 1 220 ? 25.264  -13.947 17.170  1.00 11.42  ? 445  ALA B N   1 
ATOM   4144 C CA  . ALA B 1 220 ? 25.175  -12.487 17.180  1.00 11.69  ? 445  ALA B CA  1 
ATOM   4145 C C   . ALA B 1 220 ? 23.892  -11.996 17.830  1.00 11.21  ? 445  ALA B C   1 
ATOM   4146 O O   . ALA B 1 220 ? 23.859  -10.882 18.371  1.00 11.80  ? 445  ALA B O   1 
ATOM   4147 C CB  . ALA B 1 220 ? 25.263  -11.940 15.749  1.00 14.68  ? 445  ALA B CB  1 
ATOM   4148 N N   . LEU B 1 221 ? 22.828  -12.792 17.753  1.00 13.01  ? 446  LEU B N   1 
ATOM   4149 C CA  . LEU B 1 221 ? 21.516  -12.448 18.264  1.00 10.02  ? 446  LEU B CA  1 
ATOM   4150 C C   . LEU B 1 221 ? 20.906  -13.683 18.913  1.00 12.55  ? 446  LEU B C   1 
ATOM   4151 O O   . LEU B 1 221 ? 20.985  -14.781 18.342  1.00 11.21  ? 446  LEU B O   1 
ATOM   4152 C CB  . LEU B 1 221 ? 20.587  -11.971 17.143  1.00 11.49  ? 446  LEU B CB  1 
ATOM   4153 C CG  . LEU B 1 221 ? 21.067  -10.795 16.287  1.00 10.98  ? 446  LEU B CG  1 
ATOM   4154 C CD1 . LEU B 1 221 ? 20.220  -10.720 15.009  1.00 14.78  ? 446  LEU B CD1 1 
ATOM   4155 C CD2 . LEU B 1 221 ? 20.948  -9.508  17.080  1.00 11.56  ? 446  LEU B CD2 1 
ATOM   4156 N N   . PRO B 1 222 ? 20.280  -13.546 20.081  1.00 8.87   ? 447  PRO B N   1 
ATOM   4157 C CA  . PRO B 1 222 ? 19.462  -14.653 20.585  1.00 10.86  ? 447  PRO B CA  1 
ATOM   4158 C C   . PRO B 1 222 ? 18.377  -14.971 19.575  1.00 8.90   ? 447  PRO B C   1 
ATOM   4159 O O   . PRO B 1 222 ? 17.863  -14.077 18.890  1.00 11.40  ? 447  PRO B O   1 
ATOM   4160 C CB  . PRO B 1 222 ? 18.863  -14.109 21.885  1.00 8.88   ? 447  PRO B CB  1 
ATOM   4161 C CG  . PRO B 1 222 ? 19.780  -12.965 22.289  1.00 11.81  ? 447  PRO B CG  1 
ATOM   4162 C CD  . PRO B 1 222 ? 20.285  -12.387 20.995  1.00 10.46  ? 447  PRO B CD  1 
ATOM   4163 N N   . GLN B 1 223 ? 18.000  -16.254 19.512  1.00 9.85   ? 448  GLN B N   1 
ATOM   4164 C CA  . GLN B 1 223 ? 16.926  -16.641 18.608  1.00 9.46   ? 448  GLN B CA  1 
ATOM   4165 C C   . GLN B 1 223 ? 15.670  -15.829 18.884  1.00 11.41  ? 448  GLN B C   1 
ATOM   4166 O O   . GLN B 1 223 ? 14.960  -15.428 17.949  1.00 11.49  ? 448  GLN B O   1 
ATOM   4167 C CB  . GLN B 1 223 ? 16.624  -18.141 18.736  1.00 10.57  ? 448  GLN B CB  1 
ATOM   4168 C CG  . GLN B 1 223 ? 15.360  -18.558 17.960  1.00 9.93   ? 448  GLN B CG  1 
ATOM   4169 C CD  . GLN B 1 223 ? 15.490  -18.353 16.443  1.00 12.82  ? 448  GLN B CD  1 
ATOM   4170 O OE1 . GLN B 1 223 ? 14.677  -17.650 15.810  1.00 17.46  ? 448  GLN B OE1 1 
ATOM   4171 N NE2 . GLN B 1 223 ? 16.486  -18.984 15.853  1.00 11.13  ? 448  GLN B NE2 1 
ATOM   4172 N N   . GLU B 1 224 ? 15.382  -15.563 20.162  1.00 10.94  ? 449  GLU B N   1 
ATOM   4173 C CA  . GLU B 1 224 ? 14.151  -14.847 20.481  1.00 10.44  ? 449  GLU B CA  1 
ATOM   4174 C C   . GLU B 1 224 ? 14.163  -13.425 19.935  1.00 11.36  ? 449  GLU B C   1 
ATOM   4175 O O   . GLU B 1 224 ? 13.099  -12.863 19.657  1.00 11.86  ? 449  GLU B O   1 
ATOM   4176 C CB  . GLU B 1 224 ? 13.912  -14.851 21.998  1.00 11.49  ? 449  GLU B CB  1 
ATOM   4177 C CG  . GLU B 1 224 ? 13.540  -16.240 22.569  1.00 10.22  ? 449  GLU B CG  1 
ATOM   4178 C CD  . GLU B 1 224 ? 14.734  -17.172 22.801  1.00 13.11  ? 449  GLU B CD  1 
ATOM   4179 O OE1 . GLU B 1 224 ? 15.885  -16.800 22.481  1.00 12.60  ? 449  GLU B OE1 1 
ATOM   4180 O OE2 . GLU B 1 224 ? 14.514  -18.297 23.306  1.00 14.61  ? 449  GLU B OE2 1 
ATOM   4181 N N   . TRP B 1 225 ? 15.343  -12.819 19.770  1.00 11.40  ? 450  TRP B N   1 
ATOM   4182 C CA  . TRP B 1 225 ? 15.392  -11.497 19.146  1.00 9.28   ? 450  TRP B CA  1 
ATOM   4183 C C   . TRP B 1 225 ? 15.139  -11.591 17.647  1.00 11.89  ? 450  TRP B C   1 
ATOM   4184 O O   . TRP B 1 225 ? 14.480  -10.718 17.069  1.00 12.58  ? 450  TRP B O   1 
ATOM   4185 C CB  . TRP B 1 225 ? 16.746  -10.814 19.394  1.00 10.70  ? 450  TRP B CB  1 
ATOM   4186 C CG  . TRP B 1 225 ? 17.021  -10.344 20.798  1.00 9.98   ? 450  TRP B CG  1 
ATOM   4187 C CD1 . TRP B 1 225 ? 16.317  -10.628 21.938  1.00 12.95  ? 450  TRP B CD1 1 
ATOM   4188 C CD2 . TRP B 1 225 ? 18.108  -9.510  21.187  1.00 12.26  ? 450  TRP B CD2 1 
ATOM   4189 N NE1 . TRP B 1 225 ? 16.916  -10.011 23.023  1.00 13.59  ? 450  TRP B NE1 1 
ATOM   4190 C CE2 . TRP B 1 225 ? 18.018  -9.319  22.581  1.00 10.32  ? 450  TRP B CE2 1 
ATOM   4191 C CE3 . TRP B 1 225 ? 19.154  -8.900  20.483  1.00 13.45  ? 450  TRP B CE3 1 
ATOM   4192 C CZ2 . TRP B 1 225 ? 18.935  -8.544  23.282  1.00 13.64  ? 450  TRP B CZ2 1 
ATOM   4193 C CZ3 . TRP B 1 225 ? 20.059  -8.128  21.180  1.00 15.32  ? 450  TRP B CZ3 1 
ATOM   4194 C CH2 . TRP B 1 225 ? 19.947  -7.966  22.568  1.00 13.33  ? 450  TRP B CH2 1 
ATOM   4195 N N   . ILE B 1 226 ? 15.674  -12.627 16.993  1.00 11.24  ? 451  ILE B N   1 
ATOM   4196 C CA  . ILE B 1 226 ? 15.396  -12.817 15.570  1.00 10.93  ? 451  ILE B CA  1 
ATOM   4197 C C   . ILE B 1 226 ? 13.896  -12.947 15.343  1.00 11.48  ? 451  ILE B C   1 
ATOM   4198 O O   . ILE B 1 226 ? 13.315  -12.256 14.498  1.00 12.75  ? 451  ILE B O   1 
ATOM   4199 C CB  . ILE B 1 226 ? 16.166  -14.037 15.035  1.00 11.52  ? 451  ILE B CB  1 
ATOM   4200 C CG1 . ILE B 1 226 ? 17.664  -13.752 15.104  1.00 10.54  ? 451  ILE B CG1 1 
ATOM   4201 C CG2 . ILE B 1 226 ? 15.752  -14.377 13.602  1.00 10.59  ? 451  ILE B CG2 1 
ATOM   4202 C CD1 . ILE B 1 226 ? 18.534  -14.944 14.721  1.00 10.55  ? 451  ILE B CD1 1 
ATOM   4203 N N   . THR B 1 227 ? 13.239  -13.801 16.131  1.00 11.59  ? 452  THR B N   1 
ATOM   4204 C CA  . THR B 1 227 ? 11.794  -13.948 15.993  1.00 12.67  ? 452  THR B CA  1 
ATOM   4205 C C   . THR B 1 227 ? 11.074  -12.643 16.303  1.00 12.97  ? 452  THR B C   1 
ATOM   4206 O O   . THR B 1 227 ? 10.099  -12.295 15.627  1.00 12.82  ? 452  THR B O   1 
ATOM   4207 C CB  . THR B 1 227 ? 11.289  -15.074 16.888  1.00 10.97  ? 452  THR B CB  1 
ATOM   4208 O OG1 . THR B 1 227 ? 11.963  -16.291 16.538  1.00 14.21  ? 452  THR B OG1 1 
ATOM   4209 C CG2 . THR B 1 227 ? 9.770   -15.265 16.712  1.00 12.75  ? 452  THR B CG2 1 
ATOM   4210 N N   . TRP B 1 228 ? 11.565  -11.891 17.297  1.00 12.30  ? 453  TRP B N   1 
ATOM   4211 C CA  . TRP B 1 228 ? 11.004  -10.570 17.574  1.00 9.97   ? 453  TRP B CA  1 
ATOM   4212 C C   . TRP B 1 228 ? 11.079  -9.675  16.341  1.00 13.16  ? 453  TRP B C   1 
ATOM   4213 O O   . TRP B 1 228 ? 10.111  -8.985  16.004  1.00 12.96  ? 453  TRP B O   1 
ATOM   4214 C CB  . TRP B 1 228 ? 11.760  -9.937  18.744  1.00 14.29  ? 453  TRP B CB  1 
ATOM   4215 C CG  . TRP B 1 228 ? 11.081  -8.799  19.440  1.00 12.97  ? 453  TRP B CG  1 
ATOM   4216 C CD1 . TRP B 1 228 ? 11.427  -7.484  19.391  1.00 14.46  ? 453  TRP B CD1 1 
ATOM   4217 C CD2 . TRP B 1 228 ? 9.992   -8.893  20.366  1.00 12.51  ? 453  TRP B CD2 1 
ATOM   4218 N NE1 . TRP B 1 228 ? 10.603  -6.742  20.206  1.00 17.32  ? 453  TRP B NE1 1 
ATOM   4219 C CE2 . TRP B 1 228 ? 9.712   -7.589  20.815  1.00 18.34  ? 453  TRP B CE2 1 
ATOM   4220 C CE3 . TRP B 1 228 ? 9.213   -9.954  20.838  1.00 17.38  ? 453  TRP B CE3 1 
ATOM   4221 C CZ2 . TRP B 1 228 ? 8.688   -7.314  21.717  1.00 15.52  ? 453  TRP B CZ2 1 
ATOM   4222 C CZ3 . TRP B 1 228 ? 8.197   -9.681  21.736  1.00 17.14  ? 453  TRP B CZ3 1 
ATOM   4223 C CH2 . TRP B 1 228 ? 7.942   -8.371  22.165  1.00 17.25  ? 453  TRP B CH2 1 
ATOM   4224 N N   . PHE B 1 229 ? 12.211  -9.689  15.633  1.00 11.54  ? 454  PHE B N   1 
ATOM   4225 C CA  . PHE B 1 229 ? 12.311  -8.804  14.478  1.00 11.22  ? 454  PHE B CA  1 
ATOM   4226 C C   . PHE B 1 229 ? 11.415  -9.275  13.344  1.00 12.02  ? 454  PHE B C   1 
ATOM   4227 O O   . PHE B 1 229 ? 10.940  -8.450  12.556  1.00 14.28  ? 454  PHE B O   1 
ATOM   4228 C CB  . PHE B 1 229 ? 13.756  -8.692  13.977  1.00 12.64  ? 454  PHE B CB  1 
ATOM   4229 C CG  . PHE B 1 229 ? 14.751  -8.239  15.030  1.00 12.78  ? 454  PHE B CG  1 
ATOM   4230 C CD1 . PHE B 1 229 ? 14.359  -7.410  16.076  1.00 15.86  ? 454  PHE B CD1 1 
ATOM   4231 C CD2 . PHE B 1 229 ? 16.082  -8.649  14.959  1.00 15.60  ? 454  PHE B CD2 1 
ATOM   4232 C CE1 . PHE B 1 229 ? 15.281  -7.001  17.048  1.00 15.24  ? 454  PHE B CE1 1 
ATOM   4233 C CE2 . PHE B 1 229 ? 17.005  -8.241  15.914  1.00 14.29  ? 454  PHE B CE2 1 
ATOM   4234 C CZ  . PHE B 1 229 ? 16.606  -7.419  16.959  1.00 14.99  ? 454  PHE B CZ  1 
ATOM   4235 N N   . LEU B 1 230 ? 11.173  -10.586 13.243  1.00 13.52  ? 455  LEU B N   1 
ATOM   4236 C CA  . LEU B 1 230 ? 10.297  -11.104 12.194  1.00 12.31  ? 455  LEU B CA  1 
ATOM   4237 C C   . LEU B 1 230 ? 8.822   -10.828 12.462  1.00 19.34  ? 455  LEU B C   1 
ATOM   4238 O O   . LEU B 1 230 ? 8.016   -10.848 11.518  1.00 19.09  ? 455  LEU B O   1 
ATOM   4239 C CB  . LEU B 1 230 ? 10.473  -12.610 12.053  1.00 11.33  ? 455  LEU B CB  1 
ATOM   4240 C CG  . LEU B 1 230 ? 11.842  -13.111 11.623  1.00 13.82  ? 455  LEU B CG  1 
ATOM   4241 C CD1 . LEU B 1 230 ? 11.852  -14.634 11.689  1.00 17.41  ? 455  LEU B CD1 1 
ATOM   4242 C CD2 . LEU B 1 230 ? 12.196  -12.611 10.225  1.00 16.15  ? 455  LEU B CD2 1 
ATOM   4243 N N   . THR B 1 231 ? 8.446   -10.619 13.723  1.00 13.23  ? 456  THR B N   1 
ATOM   4244 C CA  . THR B 1 231 ? 7.053   -10.465 14.127  1.00 14.43  ? 456  THR B CA  1 
ATOM   4245 C C   . THR B 1 231 ? 6.697   -9.022  14.450  1.00 19.98  ? 456  THR B C   1 
ATOM   4246 O O   . THR B 1 231 ? 5.603   -8.762  14.961  1.00 20.78  ? 456  THR B O   1 
ATOM   4247 C CB  . THR B 1 231 ? 6.758   -11.349 15.338  1.00 17.00  ? 456  THR B CB  1 
ATOM   4248 O OG1 . THR B 1 231 ? 7.663   -11.022 16.398  1.00 15.21  ? 456  THR B OG1 1 
ATOM   4249 C CG2 . THR B 1 231 ? 6.929   -12.814 14.988  1.00 13.62  ? 456  THR B CG2 1 
ATOM   4250 N N   . HIS B 1 232 ? 7.603   -8.084  14.194  1.00 15.64  ? 457  HIS B N   1 
ATOM   4251 C CA  . HIS B 1 232 ? 7.327   -6.665  14.311  1.00 14.77  ? 457  HIS B CA  1 
ATOM   4252 C C   . HIS B 1 232 ? 7.687   -5.984  12.998  1.00 17.80  ? 457  HIS B C   1 
ATOM   4253 O O   . HIS B 1 232 ? 8.503   -6.486  12.225  1.00 20.59  ? 457  HIS B O   1 
ATOM   4254 C CB  . HIS B 1 232 ? 8.111   -6.047  15.481  1.00 16.85  ? 457  HIS B CB  1 
ATOM   4255 C CG  . HIS B 1 232 ? 7.639   -6.512  16.823  1.00 17.16  ? 457  HIS B CG  1 
ATOM   4256 N ND1 . HIS B 1 232 ? 7.990   -7.735  17.353  1.00 16.60  ? 457  HIS B ND1 1 
ATOM   4257 C CD2 . HIS B 1 232 ? 6.812   -5.932  17.725  1.00 19.82  ? 457  HIS B CD2 1 
ATOM   4258 C CE1 . HIS B 1 232 ? 7.413   -7.881  18.534  1.00 16.44  ? 457  HIS B CE1 1 
ATOM   4259 N NE2 . HIS B 1 232 ? 6.683   -6.805  18.779  1.00 15.59  ? 457  HIS B NE2 1 
ATOM   4260 N N   . ASN B 1 233 ? 7.047   -4.848  12.735  1.00 27.25  ? 458  ASN B N   1 
ATOM   4261 C CA  . ASN B 1 233 ? 7.351   -4.053  11.548  1.00 45.02  ? 458  ASN B CA  1 
ATOM   4262 C C   . ASN B 1 233 ? 8.183   -2.862  12.013  1.00 50.66  ? 458  ASN B C   1 
ATOM   4263 O O   . ASN B 1 233 ? 7.693   -1.746  12.174  1.00 46.22  ? 458  ASN B O   1 
ATOM   4264 C CB  . ASN B 1 233 ? 6.070   -3.626  10.835  1.00 34.47  ? 458  ASN B CB  1 
ATOM   4265 N N   . PHE B 1 234 ? 9.462   -3.123  12.265  1.00 35.28  ? 459  PHE B N   1 
ATOM   4266 C CA  . PHE B 1 234 ? 10.351  -2.090  12.770  1.00 37.93  ? 459  PHE B CA  1 
ATOM   4267 C C   . PHE B 1 234 ? 10.957  -1.302  11.620  1.00 35.06  ? 459  PHE B C   1 
ATOM   4268 O O   . PHE B 1 234 ? 11.239  -1.843  10.547  1.00 33.03  ? 459  PHE B O   1 
ATOM   4269 C CB  . PHE B 1 234 ? 11.477  -2.687  13.615  1.00 28.05  ? 459  PHE B CB  1 
ATOM   4270 C CG  . PHE B 1 234 ? 11.034  -3.199  14.948  1.00 18.57  ? 459  PHE B CG  1 
ATOM   4271 C CD1 . PHE B 1 234 ? 10.008  -2.581  15.643  1.00 21.76  ? 459  PHE B CD1 1 
ATOM   4272 C CD2 . PHE B 1 234 ? 11.644  -4.308  15.510  1.00 16.52  ? 459  PHE B CD2 1 
ATOM   4273 C CE1 . PHE B 1 234 ? 9.600   -3.056  16.880  1.00 24.02  ? 459  PHE B CE1 1 
ATOM   4274 C CE2 . PHE B 1 234 ? 11.236  -4.788  16.744  1.00 17.74  ? 459  PHE B CE2 1 
ATOM   4275 C CZ  . PHE B 1 234 ? 10.219  -4.154  17.433  1.00 22.86  ? 459  PHE B CZ  1 
ATOM   4276 N N   . THR B 1 235 ? 11.164  -0.014  11.863  1.00 37.24  ? 460  THR B N   1 
ATOM   4277 C CA  . THR B 1 235 ? 11.936  0.849   10.980  1.00 36.22  ? 460  THR B CA  1 
ATOM   4278 C C   . THR B 1 235 ? 13.111  1.403   11.771  1.00 40.41  ? 460  THR B C   1 
ATOM   4279 O O   . THR B 1 235 ? 12.916  2.130   12.753  1.00 35.00  ? 460  THR B O   1 
ATOM   4280 C CB  . THR B 1 235 ? 11.077  1.983   10.424  1.00 42.17  ? 460  THR B CB  1 
ATOM   4281 O OG1 . THR B 1 235 ? 9.970   1.428   9.702   1.00 56.66  ? 460  THR B OG1 1 
ATOM   4282 C CG2 . THR B 1 235 ? 11.903  2.867   9.495   1.00 38.66  ? 460  THR B CG2 1 
ATOM   4283 N N   . ALA B 1 236 ? 14.325  1.049   11.356  1.00 30.18  ? 461  ALA B N   1 
ATOM   4284 C CA  . ALA B 1 236 ? 15.519  1.563   12.015  1.00 38.18  ? 461  ALA B CA  1 
ATOM   4285 C C   . ALA B 1 236 ? 15.641  3.055   11.735  1.00 32.23  ? 461  ALA B C   1 
ATOM   4286 O O   . ALA B 1 236 ? 15.946  3.462   10.610  1.00 37.87  ? 461  ALA B O   1 
ATOM   4287 C CB  . ALA B 1 236 ? 16.754  0.810   11.533  1.00 33.87  ? 461  ALA B CB  1 
ATOM   4288 N N   . LEU B 1 237 ? 15.385  3.876   12.745  1.00 40.60  ? 462  LEU B N   1 
ATOM   4289 C CA  . LEU B 1 237 ? 15.505  5.319   12.596  1.00 52.12  ? 462  LEU B CA  1 
ATOM   4290 C C   . LEU B 1 237 ? 16.934  5.804   12.797  1.00 50.48  ? 462  LEU B C   1 
ATOM   4291 O O   . LEU B 1 237 ? 17.165  7.016   12.879  1.00 46.98  ? 462  LEU B O   1 
ATOM   4292 C CB  . LEU B 1 237 ? 14.558  6.027   13.570  1.00 38.40  ? 462  LEU B CB  1 
ATOM   4293 C CG  . LEU B 1 237 ? 13.112  5.507   13.591  1.00 44.40  ? 462  LEU B CG  1 
ATOM   4294 C CD1 . LEU B 1 237 ? 12.246  6.345   14.524  1.00 36.86  ? 462  LEU B CD1 1 
ATOM   4295 C CD2 . LEU B 1 237 ? 12.507  5.460   12.191  1.00 47.32  ? 462  LEU B CD2 1 
ATOM   4296 N N   . GLY B 1 238 ? 17.890  4.880   12.882  1.00 39.69  ? 463  GLY B N   1 
ATOM   4297 C CA  . GLY B 1 238 ? 19.289  5.225   13.045  1.00 28.80  ? 463  GLY B CA  1 
ATOM   4298 C C   . GLY B 1 238 ? 20.149  4.046   12.652  1.00 23.21  ? 463  GLY B C   1 
ATOM   4299 O O   . GLY B 1 238 ? 19.659  2.943   12.413  1.00 27.18  ? 463  GLY B O   1 
ATOM   4300 N N   . ASP B 1 239 ? 21.451  4.308   12.581  1.00 27.09  ? 464  ASP B N   1 
ATOM   4301 C CA  . ASP B 1 239 ? 22.405  3.260   12.247  1.00 21.14  ? 464  ASP B CA  1 
ATOM   4302 C C   . ASP B 1 239 ? 22.417  2.156   13.295  1.00 24.71  ? 464  ASP B C   1 
ATOM   4303 O O   . ASP B 1 239 ? 22.745  1.005   12.986  1.00 19.72  ? 464  ASP B O   1 
ATOM   4304 C CB  . ASP B 1 239 ? 23.800  3.862   12.120  1.00 27.96  ? 464  ASP B CB  1 
ATOM   4305 C CG  . ASP B 1 239 ? 23.914  4.881   10.999  1.00 36.33  ? 464  ASP B CG  1 
ATOM   4306 O OD1 . ASP B 1 239 ? 23.258  4.705   9.950   1.00 31.62  ? 464  ASP B OD1 1 
ATOM   4307 O OD2 . ASP B 1 239 ? 24.687  5.852   11.164  1.00 23.90  ? 464  ASP B OD2 1 
ATOM   4308 N N   . ALA B 1 240 ? 22.090  2.484   14.539  1.00 18.98  ? 465  ALA B N   1 
ATOM   4309 C CA  . ALA B 1 240 ? 22.257  1.514   15.611  1.00 15.46  ? 465  ALA B CA  1 
ATOM   4310 C C   . ALA B 1 240 ? 21.316  1.866   16.746  1.00 19.77  ? 465  ALA B C   1 
ATOM   4311 O O   . ALA B 1 240 ? 21.031  3.040   16.988  1.00 18.83  ? 465  ALA B O   1 
ATOM   4312 C CB  . ALA B 1 240 ? 23.701  1.485   16.123  1.00 17.94  ? 465  ALA B CB  1 
ATOM   4313 N N   . ALA B 1 241 ? 20.859  0.834   17.444  1.00 17.15  ? 466  ALA B N   1 
ATOM   4314 C CA  . ALA B 1 241 ? 20.024  0.998   18.623  1.00 15.38  ? 466  ALA B CA  1 
ATOM   4315 C C   . ALA B 1 241 ? 20.920  0.998   19.855  1.00 16.23  ? 466  ALA B C   1 
ATOM   4316 O O   . ALA B 1 241 ? 21.640  0.020   20.103  1.00 16.78  ? 466  ALA B O   1 
ATOM   4317 C CB  . ALA B 1 241 ? 18.990  -0.125  18.703  1.00 15.40  ? 466  ALA B CB  1 
ATOM   4318 N N   . LEU B 1 242 ? 20.912  2.107   20.594  1.00 15.99  ? 467  LEU B N   1 
ATOM   4319 C CA  . LEU B 1 242 ? 21.574  2.158   21.891  1.00 17.28  ? 467  LEU B CA  1 
ATOM   4320 C C   . LEU B 1 242 ? 20.761  1.352   22.896  1.00 15.79  ? 467  LEU B C   1 
ATOM   4321 O O   . LEU B 1 242 ? 19.562  1.602   23.083  1.00 18.67  ? 467  LEU B O   1 
ATOM   4322 C CB  . LEU B 1 242 ? 21.722  3.609   22.351  1.00 15.48  ? 467  LEU B CB  1 
ATOM   4323 C CG  . LEU B 1 242 ? 22.406  3.846   23.693  1.00 16.40  ? 467  LEU B CG  1 
ATOM   4324 C CD1 . LEU B 1 242 ? 23.860  3.443   23.601  1.00 20.31  ? 467  LEU B CD1 1 
ATOM   4325 C CD2 . LEU B 1 242 ? 22.281  5.314   24.110  1.00 19.22  ? 467  LEU B CD2 1 
ATOM   4326 N N   . LEU B 1 243 ? 21.402  0.382   23.538  1.00 17.78  ? 468  LEU B N   1 
ATOM   4327 C CA  . LEU B 1 243 ? 20.743  -0.441  24.537  1.00 14.32  ? 468  LEU B CA  1 
ATOM   4328 C C   . LEU B 1 243 ? 21.453  -0.277  25.870  1.00 18.09  ? 468  LEU B C   1 
ATOM   4329 O O   . LEU B 1 243 ? 22.651  0.002   25.921  1.00 18.10  ? 468  LEU B O   1 
ATOM   4330 C CB  . LEU B 1 243 ? 20.769  -1.922  24.161  1.00 15.13  ? 468  LEU B CB  1 
ATOM   4331 C CG  . LEU B 1 243 ? 20.490  -2.299  22.708  1.00 15.28  ? 468  LEU B CG  1 
ATOM   4332 C CD1 . LEU B 1 243 ? 20.675  -3.809  22.522  1.00 13.54  ? 468  LEU B CD1 1 
ATOM   4333 C CD2 . LEU B 1 243 ? 19.076  -1.852  22.310  1.00 17.75  ? 468  LEU B CD2 1 
ATOM   4334 N N   . ARG B 1 244 ? 20.710  -0.491  26.952  1.00 16.00  ? 469  ARG B N   1 
ATOM   4335 C CA  . ARG B 1 244 ? 21.307  -0.654  28.267  1.00 19.35  ? 469  ARG B CA  1 
ATOM   4336 C C   . ARG B 1 244 ? 21.033  -2.070  28.748  1.00 15.93  ? 469  ARG B C   1 
ATOM   4337 O O   . ARG B 1 244 ? 19.943  -2.616  28.537  1.00 19.10  ? 469  ARG B O   1 
ATOM   4338 C CB  . ARG B 1 244 ? 20.780  0.379   29.276  1.00 21.25  ? 469  ARG B CB  1 
ATOM   4339 C CG  . ARG B 1 244 ? 19.275  0.380   29.473  1.00 34.85  ? 469  ARG B CG  1 
ATOM   4340 C CD  . ARG B 1 244 ? 18.900  1.318   30.610  1.00 42.78  ? 469  ARG B CD  1 
ATOM   4341 N NE  . ARG B 1 244 ? 17.496  1.707   30.585  1.00 57.16  ? 469  ARG B NE  1 
ATOM   4342 C CZ  . ARG B 1 244 ? 16.950  2.570   31.432  1.00 59.53  ? 469  ARG B CZ  1 
ATOM   4343 N NH1 . ARG B 1 244 ? 17.660  3.132   32.396  1.00 64.33  ? 469  ARG B NH1 1 
ATOM   4344 N NH2 . ARG B 1 244 ? 15.663  2.878   31.307  1.00 72.38  ? 469  ARG B NH2 1 
ATOM   4345 N N   . TYR B 1 245 ? 22.047  -2.679  29.346  1.00 18.08  ? 470  TYR B N   1 
ATOM   4346 C CA  . TYR B 1 245 ? 21.942  -4.026  29.888  1.00 17.76  ? 470  TYR B CA  1 
ATOM   4347 C C   . TYR B 1 245 ? 21.821  -3.862  31.389  1.00 18.70  ? 470  TYR B C   1 
ATOM   4348 O O   . TYR B 1 245 ? 22.751  -3.371  32.036  1.00 18.66  ? 470  TYR B O   1 
ATOM   4349 C CB  . TYR B 1 245 ? 23.158  -4.867  29.528  1.00 13.47  ? 470  TYR B CB  1 
ATOM   4350 C CG  . TYR B 1 245 ? 23.024  -6.323  29.920  1.00 15.02  ? 470  TYR B CG  1 
ATOM   4351 C CD1 . TYR B 1 245 ? 21.978  -7.097  29.432  1.00 13.66  ? 470  TYR B CD1 1 
ATOM   4352 C CD2 . TYR B 1 245 ? 23.942  -6.923  30.778  1.00 14.64  ? 470  TYR B CD2 1 
ATOM   4353 C CE1 . TYR B 1 245 ? 21.849  -8.427  29.779  1.00 14.24  ? 470  TYR B CE1 1 
ATOM   4354 C CE2 . TYR B 1 245 ? 23.823  -8.276  31.118  1.00 12.36  ? 470  TYR B CE2 1 
ATOM   4355 C CZ  . TYR B 1 245 ? 22.777  -9.011  30.612  1.00 11.71  ? 470  TYR B CZ  1 
ATOM   4356 O OH  . TYR B 1 245 ? 22.645  -10.349 30.948  1.00 13.66  ? 470  TYR B OH  1 
ATOM   4357 N N   . ARG B 1 246 ? 20.667  -4.235  31.933  1.00 14.98  ? 471  ARG B N   1 
ATOM   4358 C CA  . ARG B 1 246 ? 20.327  -3.909  33.310  1.00 18.18  ? 471  ARG B CA  1 
ATOM   4359 C C   . ARG B 1 246 ? 19.918  -5.169  34.052  1.00 21.11  ? 471  ARG B C   1 
ATOM   4360 O O   . ARG B 1 246 ? 19.163  -5.992  33.526  1.00 18.13  ? 471  ARG B O   1 
ATOM   4361 C CB  . ARG B 1 246 ? 19.184  -2.884  33.366  1.00 24.18  ? 471  ARG B CB  1 
ATOM   4362 C CG  . ARG B 1 246 ? 18.714  -2.559  34.791  1.00 30.99  ? 471  ARG B CG  1 
ATOM   4363 C CD  . ARG B 1 246 ? 17.313  -1.954  34.800  1.00 45.07  ? 471  ARG B CD  1 
ATOM   4364 N NE  . ARG B 1 246 ? 17.241  -0.723  34.024  1.00 43.49  ? 471  ARG B NE  1 
ATOM   4365 N N   . ASN B 1 247 ? 20.400  -5.314  35.285  1.00 20.19  ? 472  ASN B N   1 
ATOM   4366 C CA  . ASN B 1 247 ? 19.805  -6.286  36.199  1.00 27.29  ? 472  ASN B CA  1 
ATOM   4367 C C   . ASN B 1 247 ? 18.504  -5.686  36.725  1.00 35.79  ? 472  ASN B C   1 
ATOM   4368 O O   . ASN B 1 247 ? 18.526  -4.713  37.482  1.00 34.79  ? 472  ASN B O   1 
ATOM   4369 C CB  . ASN B 1 247 ? 20.768  -6.620  37.331  1.00 38.03  ? 472  ASN B CB  1 
ATOM   4370 C CG  . ASN B 1 247 ? 20.302  -7.797  38.161  1.00 57.40  ? 472  ASN B CG  1 
ATOM   4371 O OD1 . ASN B 1 247 ? 19.127  -7.896  38.525  1.00 46.36  ? 472  ASN B OD1 1 
ATOM   4372 N ND2 . ASN B 1 247 ? 21.222  -8.706  38.457  1.00 47.47  ? 472  ASN B ND2 1 
ATOM   4373 N N   . GLN B 1 248 ? 17.363  -6.243  36.305  1.00 40.53  ? 473  GLN B N   1 
ATOM   4374 C CA  . GLN B 1 248 ? 16.084  -5.634  36.666  1.00 49.81  ? 473  GLN B CA  1 
ATOM   4375 C C   . GLN B 1 248 ? 15.743  -5.853  38.135  1.00 48.61  ? 473  GLN B C   1 
ATOM   4376 O O   . GLN B 1 248 ? 15.017  -5.045  38.727  1.00 43.09  ? 473  GLN B O   1 
ATOM   4377 C CB  . GLN B 1 248 ? 14.965  -6.179  35.775  1.00 49.56  ? 473  GLN B CB  1 
ATOM   4378 C CG  . GLN B 1 248 ? 15.026  -5.712  34.321  1.00 44.69  ? 473  GLN B CG  1 
ATOM   4379 C CD  . GLN B 1 248 ? 13.852  -6.224  33.497  1.00 67.10  ? 473  GLN B CD  1 
ATOM   4380 O OE1 . GLN B 1 248 ? 13.235  -7.236  33.838  1.00 60.80  ? 473  GLN B OE1 1 
ATOM   4381 N NE2 . GLN B 1 248 ? 13.534  -5.522  32.411  1.00 41.35  ? 473  GLN B NE2 1 
ATOM   4382 N N   . ALA B 1 249 ? 16.252  -6.931  38.738  1.00 37.39  ? 474  ALA B N   1 
ATOM   4383 C CA  . ALA B 1 249 ? 15.986  -7.194  40.149  1.00 54.10  ? 474  ALA B CA  1 
ATOM   4384 C C   . ALA B 1 249 ? 16.654  -6.151  41.039  1.00 52.88  ? 474  ALA B C   1 
ATOM   4385 O O   . ALA B 1 249 ? 16.003  -5.535  41.892  1.00 38.31  ? 474  ALA B O   1 
ATOM   4386 C CB  . ALA B 1 249 ? 16.461  -8.601  40.516  1.00 50.98  ? 474  ALA B CB  1 
ATOM   4387 N N   . THR B 1 250 ? 17.957  -5.943  40.856  1.00 49.46  ? 475  THR B N   1 
ATOM   4388 C CA  . THR B 1 250 ? 18.716  -4.985  41.648  1.00 34.71  ? 475  THR B CA  1 
ATOM   4389 C C   . THR B 1 250 ? 18.681  -3.578  41.074  1.00 44.30  ? 475  THR B C   1 
ATOM   4390 O O   . THR B 1 250 ? 19.058  -2.631  41.777  1.00 33.22  ? 475  THR B O   1 
ATOM   4391 C CB  . THR B 1 250 ? 20.174  -5.438  41.762  1.00 31.26  ? 475  THR B CB  1 
ATOM   4392 O OG1 . THR B 1 250 ? 20.797  -5.362  40.474  1.00 41.18  ? 475  THR B OG1 1 
ATOM   4393 C CG2 . THR B 1 250 ? 20.248  -6.873  42.261  1.00 38.85  ? 475  THR B CG2 1 
ATOM   4394 N N   . GLY B 1 251 ? 18.242  -3.419  39.825  1.00 38.03  ? 476  GLY B N   1 
ATOM   4395 C CA  . GLY B 1 251 ? 18.290  -2.141  39.152  1.00 41.96  ? 476  GLY B CA  1 
ATOM   4396 C C   . GLY B 1 251 ? 19.655  -1.753  38.637  1.00 32.84  ? 476  GLY B C   1 
ATOM   4397 O O   . GLY B 1 251 ? 19.800  -0.655  38.081  1.00 51.28  ? 476  GLY B O   1 
ATOM   4398 N N   . GLN B 1 252 ? 20.664  -2.608  38.799  1.00 26.84  ? 477  GLN B N   1 
ATOM   4399 C CA  . GLN B 1 252 ? 22.028  -2.224  38.459  1.00 26.68  ? 477  GLN B CA  1 
ATOM   4400 C C   . GLN B 1 252 ? 22.195  -2.169  36.946  1.00 28.32  ? 477  GLN B C   1 
ATOM   4401 O O   . GLN B 1 252 ? 22.020  -3.179  36.261  1.00 23.69  ? 477  GLN B O   1 
ATOM   4402 C CB  . GLN B 1 252 ? 23.028  -3.208  39.064  1.00 33.89  ? 477  GLN B CB  1 
ATOM   4403 C CG  . GLN B 1 252 ? 24.485  -2.903  38.719  1.00 37.97  ? 477  GLN B CG  1 
ATOM   4404 C CD  . GLN B 1 252 ? 25.454  -3.986  39.187  1.00 57.01  ? 477  GLN B CD  1 
ATOM   4405 O OE1 . GLN B 1 252 ? 25.043  -5.047  39.671  1.00 39.87  ? 477  GLN B OE1 1 
ATOM   4406 N NE2 . GLN B 1 252 ? 26.750  -3.721  39.037  1.00 44.11  ? 477  GLN B NE2 1 
ATOM   4407 N N   . LEU B 1 253 ? 22.547  -0.998  36.425  1.00 22.16  ? 478  LEU B N   1 
ATOM   4408 C CA  . LEU B 1 253 ? 22.947  -0.905  35.026  1.00 21.64  ? 478  LEU B CA  1 
ATOM   4409 C C   . LEU B 1 253 ? 24.363  -1.442  34.881  1.00 25.65  ? 478  LEU B C   1 
ATOM   4410 O O   . LEU B 1 253 ? 25.276  -1.002  35.583  1.00 31.65  ? 478  LEU B O   1 
ATOM   4411 C CB  . LEU B 1 253 ? 22.872  0.539   34.535  1.00 23.92  ? 478  LEU B CB  1 
ATOM   4412 C CG  . LEU B 1 253 ? 22.957  0.695   33.013  1.00 39.69  ? 478  LEU B CG  1 
ATOM   4413 N N   . LEU B 1 254 ? 24.543  -2.407  33.983  1.00 18.76  ? 479  LEU B N   1 
ATOM   4414 C CA  . LEU B 1 254 ? 25.830  -3.069  33.826  1.00 17.07  ? 479  LEU B CA  1 
ATOM   4415 C C   . LEU B 1 254 ? 26.679  -2.459  32.720  1.00 21.12  ? 479  LEU B C   1 
ATOM   4416 O O   . LEU B 1 254 ? 27.882  -2.270  32.913  1.00 26.63  ? 479  LEU B O   1 
ATOM   4417 C CB  . LEU B 1 254 ? 25.622  -4.564  33.569  1.00 19.36  ? 479  LEU B CB  1 
ATOM   4418 C CG  . LEU B 1 254 ? 24.973  -5.326  34.738  1.00 23.99  ? 479  LEU B CG  1 
ATOM   4419 C CD1 . LEU B 1 254 ? 24.643  -6.753  34.337  1.00 28.39  ? 479  LEU B CD1 1 
ATOM   4420 C CD2 . LEU B 1 254 ? 25.883  -5.308  35.955  1.00 34.22  ? 479  LEU B CD2 1 
ATOM   4421 N N   . PHE B 1 255 ? 26.088  -2.136  31.573  1.00 17.07  ? 480  PHE B N   1 
ATOM   4422 C CA  . PHE B 1 255 ? 26.811  -1.447  30.505  1.00 18.80  ? 480  PHE B CA  1 
ATOM   4423 C C   . PHE B 1 255 ? 25.799  -0.935  29.491  1.00 19.44  ? 480  PHE B C   1 
ATOM   4424 O O   . PHE B 1 255 ? 24.627  -1.317  29.513  1.00 18.82  ? 480  PHE B O   1 
ATOM   4425 C CB  . PHE B 1 255 ? 27.854  -2.350  29.824  1.00 18.11  ? 480  PHE B CB  1 
ATOM   4426 C CG  . PHE B 1 255 ? 27.293  -3.629  29.246  1.00 16.86  ? 480  PHE B CG  1 
ATOM   4427 C CD1 . PHE B 1 255 ? 26.692  -3.644  27.993  1.00 14.32  ? 480  PHE B CD1 1 
ATOM   4428 C CD2 . PHE B 1 255 ? 27.398  -4.822  29.937  1.00 18.02  ? 480  PHE B CD2 1 
ATOM   4429 C CE1 . PHE B 1 255 ? 26.170  -4.819  27.458  1.00 12.95  ? 480  PHE B CE1 1 
ATOM   4430 C CE2 . PHE B 1 255 ? 26.889  -5.999  29.411  1.00 19.43  ? 480  PHE B CE2 1 
ATOM   4431 C CZ  . PHE B 1 255 ? 26.281  -6.003  28.165  1.00 19.89  ? 480  PHE B CZ  1 
ATOM   4432 N N   . GLU B 1 256 ? 26.268  -0.064  28.596  1.00 16.87  ? 481  GLU B N   1 
ATOM   4433 C CA  . GLU B 1 256 ? 25.507  0.274   27.401  1.00 16.16  ? 481  GLU B CA  1 
ATOM   4434 C C   . GLU B 1 256 ? 26.207  -0.321  26.187  1.00 17.22  ? 481  GLU B C   1 
ATOM   4435 O O   . GLU B 1 256 ? 27.417  -0.564  26.205  1.00 18.89  ? 481  GLU B O   1 
ATOM   4436 C CB  . GLU B 1 256 ? 25.321  1.794   27.244  1.00 19.98  ? 481  GLU B CB  1 
ATOM   4437 C CG  . GLU B 1 256 ? 26.594  2.632   27.176  1.00 24.43  ? 481  GLU B CG  1 
ATOM   4438 C CD  . GLU B 1 256 ? 26.296  4.105   26.889  1.00 33.70  ? 481  GLU B CD  1 
ATOM   4439 O OE1 . GLU B 1 256 ? 25.166  4.564   27.184  1.00 27.67  ? 481  GLU B OE1 1 
ATOM   4440 O OE2 . GLU B 1 256 ? 27.186  4.803   26.362  1.00 24.50  ? 481  GLU B OE2 1 
ATOM   4441 N N   . CYS B 1 257 ? 25.431  -0.585  25.141  1.00 16.51  ? 482  CYS B N   1 
ATOM   4442 C CA  . CYS B 1 257 ? 25.964  -1.229  23.947  1.00 15.14  ? 482  CYS B CA  1 
ATOM   4443 C C   . CYS B 1 257 ? 25.203  -0.718  22.732  1.00 16.98  ? 482  CYS B C   1 
ATOM   4444 O O   . CYS B 1 257 ? 24.162  -0.074  22.856  1.00 16.13  ? 482  CYS B O   1 
ATOM   4445 C CB  . CYS B 1 257 ? 25.864  -2.757  24.058  1.00 14.16  ? 482  CYS B CB  1 
ATOM   4446 S SG  . CYS B 1 257 ? 24.178  -3.398  24.360  1.00 15.72  ? 482  CYS B SG  1 
ATOM   4447 N N   . LYS B 1 258 ? 25.733  -1.018  21.545  1.00 16.02  ? 483  LYS B N   1 
ATOM   4448 C CA  . LYS B 1 258 ? 25.094  -0.652  20.282  1.00 14.50  ? 483  LYS B CA  1 
ATOM   4449 C C   . LYS B 1 258 ? 24.668  -1.903  19.528  1.00 14.65  ? 483  LYS B C   1 
ATOM   4450 O O   . LYS B 1 258 ? 25.490  -2.791  19.277  1.00 14.31  ? 483  LYS B O   1 
ATOM   4451 C CB  . LYS B 1 258 ? 26.032  0.171   19.397  1.00 14.05  ? 483  LYS B CB  1 
ATOM   4452 C CG  . LYS B 1 258 ? 26.058  1.640   19.731  1.00 14.78  ? 483  LYS B CG  1 
ATOM   4453 C CD  . LYS B 1 258 ? 27.400  2.254   19.329  1.00 16.96  ? 483  LYS B CD  1 
ATOM   4454 C CE  . LYS B 1 258 ? 27.482  2.552   17.830  1.00 15.37  ? 483  LYS B CE  1 
ATOM   4455 N NZ  . LYS B 1 258 ? 28.852  3.032   17.452  1.00 16.22  ? 483  LYS B NZ  1 
ATOM   4456 N N   . LEU B 1 259 ? 23.384  -1.961  19.161  1.00 12.72  ? 484  LEU B N   1 
ATOM   4457 C CA  . LEU B 1 259 ? 22.844  -3.017  18.303  1.00 12.19  ? 484  LEU B CA  1 
ATOM   4458 C C   . LEU B 1 259 ? 22.775  -2.454  16.885  1.00 13.66  ? 484  LEU B C   1 
ATOM   4459 O O   . LEU B 1 259 ? 21.901  -1.641  16.567  1.00 14.50  ? 484  LEU B O   1 
ATOM   4460 C CB  . LEU B 1 259 ? 21.480  -3.466  18.813  1.00 11.91  ? 484  LEU B CB  1 
ATOM   4461 C CG  . LEU B 1 259 ? 20.624  -4.345  17.903  1.00 11.94  ? 484  LEU B CG  1 
ATOM   4462 C CD1 . LEU B 1 259 ? 21.354  -5.621  17.502  1.00 13.65  ? 484  LEU B CD1 1 
ATOM   4463 C CD2 . LEU B 1 259 ? 19.299  -4.660  18.631  1.00 14.61  ? 484  LEU B CD2 1 
ATOM   4464 N N   . TYR B 1 260 ? 23.738  -2.840  16.048  1.00 13.39  ? 485  TYR B N   1 
ATOM   4465 C CA  . TYR B 1 260 ? 23.795  -2.320  14.690  1.00 12.56  ? 485  TYR B CA  1 
ATOM   4466 C C   . TYR B 1 260 ? 22.634  -2.862  13.857  1.00 14.79  ? 485  TYR B C   1 
ATOM   4467 O O   . TYR B 1 260 ? 22.153  -3.975  14.075  1.00 17.51  ? 485  TYR B O   1 
ATOM   4468 C CB  . TYR B 1 260 ? 25.138  -2.667  14.036  1.00 14.88  ? 485  TYR B CB  1 
ATOM   4469 C CG  . TYR B 1 260 ? 26.291  -1.768  14.476  1.00 14.70  ? 485  TYR B CG  1 
ATOM   4470 C CD1 . TYR B 1 260 ? 26.354  -0.432  14.081  1.00 14.84  ? 485  TYR B CD1 1 
ATOM   4471 C CD2 . TYR B 1 260 ? 27.328  -2.259  15.275  1.00 14.46  ? 485  TYR B CD2 1 
ATOM   4472 C CE1 . TYR B 1 260 ? 27.414  0.401   14.481  1.00 17.41  ? 485  TYR B CE1 1 
ATOM   4473 C CE2 . TYR B 1 260 ? 28.405  -1.435  15.662  1.00 15.04  ? 485  TYR B CE2 1 
ATOM   4474 C CZ  . TYR B 1 260 ? 28.435  -0.106  15.265  1.00 15.28  ? 485  TYR B CZ  1 
ATOM   4475 O OH  . TYR B 1 260 ? 29.474  0.734   15.627  1.00 15.37  ? 485  TYR B OH  1 
ATOM   4476 N N   A ARG B 1 261 ? 22.197  -2.051  12.889  0.60 15.77  ? 486  ARG B N   1 
ATOM   4477 N N   B ARG B 1 261 ? 22.180  -2.040  12.900  0.40 15.74  ? 486  ARG B N   1 
ATOM   4478 C CA  A ARG B 1 261 ? 21.033  -2.387  12.074  0.60 15.97  ? 486  ARG B CA  1 
ATOM   4479 C CA  B ARG B 1 261 ? 21.043  -2.400  12.052  0.40 16.09  ? 486  ARG B CA  1 
ATOM   4480 C C   A ARG B 1 261 ? 21.198  -3.718  11.338  0.60 16.53  ? 486  ARG B C   1 
ATOM   4481 C C   B ARG B 1 261 ? 21.211  -3.775  11.422  0.40 16.51  ? 486  ARG B C   1 
ATOM   4482 O O   A ARG B 1 261 ? 20.204  -4.404  11.069  0.60 15.11  ? 486  ARG B O   1 
ATOM   4483 O O   B ARG B 1 261 ? 20.239  -4.526  11.278  0.40 16.36  ? 486  ARG B O   1 
ATOM   4484 C CB  A ARG B 1 261 ? 20.770  -1.240  11.091  0.60 21.95  ? 486  ARG B CB  1 
ATOM   4485 C CB  B ARG B 1 261 ? 20.864  -1.370  10.935  0.40 22.90  ? 486  ARG B CB  1 
ATOM   4486 C CG  A ARG B 1 261 ? 20.239  -1.663  9.741   0.60 26.96  ? 486  ARG B CG  1 
ATOM   4487 C CG  B ARG B 1 261 ? 20.343  -0.023  11.343  0.40 29.61  ? 486  ARG B CG  1 
ATOM   4488 C CD  A ARG B 1 261 ? 20.538  -0.624  8.682   0.60 38.01  ? 486  ARG B CD  1 
ATOM   4489 C CD  B ARG B 1 261 ? 20.333  0.871   10.124  0.40 31.56  ? 486  ARG B CD  1 
ATOM   4490 N NE  A ARG B 1 261 ? 20.012  0.684   9.045   0.60 40.77  ? 486  ARG B NE  1 
ATOM   4491 N NE  B ARG B 1 261 ? 19.487  0.329   9.067   0.40 34.93  ? 486  ARG B NE  1 
ATOM   4492 C CZ  A ARG B 1 261 ? 18.808  1.128   8.709   0.60 53.91  ? 486  ARG B CZ  1 
ATOM   4493 C CZ  B ARG B 1 261 ? 18.467  0.976   8.521   0.40 52.34  ? 486  ARG B CZ  1 
ATOM   4494 N NH1 A ARG B 1 261 ? 17.965  0.383   8.011   0.60 51.37  ? 486  ARG B NH1 1 
ATOM   4495 N NH1 B ARG B 1 261 ? 18.157  2.209   8.886   0.40 54.38  ? 486  ARG B NH1 1 
ATOM   4496 N NH2 A ARG B 1 261 ? 18.441  2.350   9.083   0.60 54.66  ? 486  ARG B NH2 1 
ATOM   4497 N NH2 B ARG B 1 261 ? 17.744  0.374   7.581   0.40 47.31  ? 486  ARG B NH2 1 
ATOM   4498 N N   . SER B 1 262 ? 22.432  -4.109  11.006  1.00 11.98  ? 487  SER B N   1 
ATOM   4499 C CA  . SER B 1 262 ? 22.648  -5.368  10.306  1.00 13.07  ? 487  SER B CA  1 
ATOM   4500 C C   . SER B 1 262 ? 22.592  -6.579  11.235  1.00 16.53  ? 487  SER B C   1 
ATOM   4501 O O   . SER B 1 262 ? 22.717  -7.713  10.753  1.00 16.12  ? 487  SER B O   1 
ATOM   4502 C CB  . SER B 1 262 ? 23.983  -5.334  9.552   1.00 20.20  ? 487  SER B CB  1 
ATOM   4503 O OG  . SER B 1 262 ? 25.075  -5.324  10.455  1.00 20.81  ? 487  SER B OG  1 
ATOM   4504 N N   . GLY B 1 263 ? 22.408  -6.381  12.542  1.00 13.42  ? 488  GLY B N   1 
ATOM   4505 C CA  . GLY B 1 263 ? 22.093  -7.490  13.425  1.00 12.61  ? 488  GLY B CA  1 
ATOM   4506 C C   . GLY B 1 263 ? 23.204  -8.046  14.300  1.00 12.87  ? 488  GLY B C   1 
ATOM   4507 O O   . GLY B 1 263 ? 23.399  -9.266  14.343  1.00 12.45  ? 488  GLY B O   1 
ATOM   4508 N N   . PHE B 1 264 ? 23.940  -7.182  14.999  1.00 12.24  ? 489  PHE B N   1 
ATOM   4509 C CA  . PHE B 1 264 ? 24.879  -7.656  16.006  1.00 11.68  ? 489  PHE B CA  1 
ATOM   4510 C C   . PHE B 1 264 ? 25.111  -6.530  17.007  1.00 12.13  ? 489  PHE B C   1 
ATOM   4511 O O   . PHE B 1 264 ? 24.814  -5.363  16.733  1.00 12.82  ? 489  PHE B O   1 
ATOM   4512 C CB  . PHE B 1 264 ? 26.191  -8.137  15.372  1.00 13.12  ? 489  PHE B CB  1 
ATOM   4513 C CG  . PHE B 1 264 ? 26.995  -7.042  14.697  1.00 13.56  ? 489  PHE B CG  1 
ATOM   4514 C CD1 . PHE B 1 264 ? 26.691  -6.622  13.413  1.00 15.48  ? 489  PHE B CD1 1 
ATOM   4515 C CD2 . PHE B 1 264 ? 28.082  -6.453  15.342  1.00 12.74  ? 489  PHE B CD2 1 
ATOM   4516 C CE1 . PHE B 1 264 ? 27.448  -5.622  12.787  1.00 14.87  ? 489  PHE B CE1 1 
ATOM   4517 C CE2 . PHE B 1 264 ? 28.843  -5.451  14.718  1.00 15.70  ? 489  PHE B CE2 1 
ATOM   4518 C CZ  . PHE B 1 264 ? 28.522  -5.036  13.441  1.00 17.04  ? 489  PHE B CZ  1 
ATOM   4519 N N   . VAL B 1 265 ? 25.631  -6.904  18.184  1.00 12.93  ? 490  VAL B N   1 
ATOM   4520 C CA  . VAL B 1 265 ? 25.799  -5.991  19.316  1.00 11.51  ? 490  VAL B CA  1 
ATOM   4521 C C   . VAL B 1 265 ? 27.286  -5.806  19.603  1.00 12.16  ? 490  VAL B C   1 
ATOM   4522 O O   . VAL B 1 265 ? 28.062  -6.760  19.508  1.00 12.38  ? 490  VAL B O   1 
ATOM   4523 C CB  . VAL B 1 265 ? 25.082  -6.535  20.572  1.00 13.42  ? 490  VAL B CB  1 
ATOM   4524 C CG1 . VAL B 1 265 ? 25.180  -5.544  21.737  1.00 13.47  ? 490  VAL B CG1 1 
ATOM   4525 C CG2 . VAL B 1 265 ? 23.623  -6.897  20.269  1.00 13.18  ? 490  VAL B CG2 1 
ATOM   4526 N N   . VAL B 1 266 ? 27.681  -4.585  19.971  1.00 12.74  ? 491  VAL B N   1 
ATOM   4527 C CA  . VAL B 1 266 ? 29.068  -4.288  20.331  1.00 13.18  ? 491  VAL B CA  1 
ATOM   4528 C C   . VAL B 1 266 ? 29.113  -3.526  21.651  1.00 13.95  ? 491  VAL B C   1 
ATOM   4529 O O   . VAL B 1 266 ? 28.179  -2.801  22.013  1.00 14.68  ? 491  VAL B O   1 
ATOM   4530 C CB  . VAL B 1 266 ? 29.826  -3.476  19.242  1.00 17.09  ? 491  VAL B CB  1 
ATOM   4531 C CG1 . VAL B 1 266 ? 29.811  -4.213  17.893  1.00 14.64  ? 491  VAL B CG1 1 
ATOM   4532 C CG2 . VAL B 1 266 ? 29.264  -2.066  19.113  1.00 13.67  ? 491  VAL B CG2 1 
ATOM   4533 N N   . VAL B 1 267 ? 30.229  -3.685  22.362  1.00 15.53  ? 492  VAL B N   1 
ATOM   4534 C CA  . VAL B 1 267 ? 30.551  -2.885  23.536  1.00 14.08  ? 492  VAL B CA  1 
ATOM   4535 C C   . VAL B 1 267 ? 31.881  -2.183  23.280  1.00 14.71  ? 492  VAL B C   1 
ATOM   4536 O O   . VAL B 1 267 ? 32.625  -2.534  22.366  1.00 17.63  ? 492  VAL B O   1 
ATOM   4537 C CB  . VAL B 1 267 ? 30.620  -3.728  24.824  1.00 15.45  ? 492  VAL B CB  1 
ATOM   4538 C CG1 . VAL B 1 267 ? 29.223  -4.169  25.250  1.00 14.03  ? 492  VAL B CG1 1 
ATOM   4539 C CG2 . VAL B 1 267 ? 31.511  -4.935  24.602  1.00 16.23  ? 492  VAL B CG2 1 
ATOM   4540 N N   . ASN B 1 268 ? 32.188  -1.199  24.129  1.00 17.32  ? 493  ASN B N   1 
ATOM   4541 C CA  . ASN B 1 268 ? 33.355  -0.349  23.961  1.00 20.51  ? 493  ASN B CA  1 
ATOM   4542 C C   . ASN B 1 268 ? 34.278  -0.477  25.170  1.00 19.16  ? 493  ASN B C   1 
ATOM   4543 O O   . ASN B 1 268 ? 33.828  -0.759  26.284  1.00 19.18  ? 493  ASN B O   1 
ATOM   4544 C CB  . ASN B 1 268 ? 32.921  1.114   23.778  1.00 18.36  ? 493  ASN B CB  1 
ATOM   4545 C CG  . ASN B 1 268 ? 34.071  2.037   23.427  1.00 19.65  ? 493  ASN B CG  1 
ATOM   4546 O OD1 . ASN B 1 268 ? 35.031  1.638   22.763  1.00 22.84  ? 493  ASN B OD1 1 
ATOM   4547 N ND2 . ASN B 1 268 ? 33.974  3.284   23.865  1.00 26.93  ? 493  ASN B ND2 1 
ATOM   4548 N N   . GLY B 1 269 ? 35.576  -0.286  24.939  1.00 19.52  ? 494  GLY B N   1 
ATOM   4549 C CA  . GLY B 1 269 ? 36.523  -0.247  26.040  1.00 23.98  ? 494  GLY B CA  1 
ATOM   4550 C C   . GLY B 1 269 ? 36.874  -1.585  26.656  1.00 31.99  ? 494  GLY B C   1 
ATOM   4551 O O   . GLY B 1 269 ? 37.254  -1.636  27.832  1.00 30.25  ? 494  GLY B O   1 
ATOM   4552 N N   . VAL B 1 270 ? 36.769  -2.672  25.898  1.00 20.95  ? 495  VAL B N   1 
ATOM   4553 C CA  . VAL B 1 270 ? 37.110  -4.007  26.375  1.00 23.93  ? 495  VAL B CA  1 
ATOM   4554 C C   . VAL B 1 270 ? 38.538  -4.313  25.947  1.00 27.80  ? 495  VAL B C   1 
ATOM   4555 O O   . VAL B 1 270 ? 38.833  -4.382  24.747  1.00 24.39  ? 495  VAL B O   1 
ATOM   4556 C CB  . VAL B 1 270 ? 36.137  -5.062  25.829  1.00 25.14  ? 495  VAL B CB  1 
ATOM   4557 C CG1 . VAL B 1 270 ? 36.477  -6.430  26.374  1.00 26.80  ? 495  VAL B CG1 1 
ATOM   4558 C CG2 . VAL B 1 270 ? 34.701  -4.688  26.168  1.00 26.77  ? 495  VAL B CG2 1 
ATOM   4559 N N   . ASN B 1 271 ? 39.428  -4.515  26.921  1.00 26.10  ? 496  ASN B N   1 
ATOM   4560 C CA  . ASN B 1 271 ? 40.831  -4.767  26.622  1.00 36.69  ? 496  ASN B CA  1 
ATOM   4561 C C   . ASN B 1 271 ? 41.266  -6.202  26.875  1.00 43.91  ? 496  ASN B C   1 
ATOM   4562 O O   . ASN B 1 271 ? 42.301  -6.618  26.344  1.00 32.20  ? 496  ASN B O   1 
ATOM   4563 C CB  . ASN B 1 271 ? 41.718  -3.817  27.437  1.00 33.86  ? 496  ASN B CB  1 
ATOM   4564 C CG  . ASN B 1 271 ? 41.338  -2.363  27.235  1.00 52.72  ? 496  ASN B CG  1 
ATOM   4565 O OD1 . ASN B 1 271 ? 41.043  -1.647  28.191  1.00 53.72  ? 496  ASN B OD1 1 
ATOM   4566 N ND2 . ASN B 1 271 ? 41.324  -1.925  25.980  1.00 47.18  ? 496  ASN B ND2 1 
ATOM   4567 N N   . VAL B 1 272 ? 40.508  -6.959  27.670  1.00 33.62  ? 497  VAL B N   1 
ATOM   4568 C CA  . VAL B 1 272 ? 40.721  -8.383  27.883  1.00 26.91  ? 497  VAL B CA  1 
ATOM   4569 C C   . VAL B 1 272 ? 39.365  -9.059  27.754  1.00 21.96  ? 497  VAL B C   1 
ATOM   4570 O O   . VAL B 1 272 ? 38.322  -8.417  27.884  1.00 26.07  ? 497  VAL B O   1 
ATOM   4571 C CB  . VAL B 1 272 ? 41.348  -8.685  29.264  1.00 25.51  ? 497  VAL B CB  1 
ATOM   4572 C CG1 . VAL B 1 272 ? 42.678  -7.947  29.429  1.00 30.13  ? 497  VAL B CG1 1 
ATOM   4573 C CG2 . VAL B 1 272 ? 40.384  -8.300  30.379  1.00 29.80  ? 497  VAL B CG2 1 
ATOM   4574 N N   . ARG B 1 273 ? 39.385  -10.367 27.486  1.00 19.54  ? 498  ARG B N   1 
ATOM   4575 C CA  . ARG B 1 273 ? 38.139  -11.123 27.425  1.00 16.24  ? 498  ARG B CA  1 
ATOM   4576 C C   . ARG B 1 273 ? 37.364  -10.909 28.717  1.00 22.23  ? 498  ARG B C   1 
ATOM   4577 O O   . ARG B 1 273 ? 37.909  -11.041 29.818  1.00 20.77  ? 498  ARG B O   1 
ATOM   4578 C CB  . ARG B 1 273 ? 38.415  -12.610 27.202  1.00 17.02  ? 498  ARG B CB  1 
ATOM   4579 C CG  . ARG B 1 273 ? 37.140  -13.434 26.959  1.00 20.86  ? 498  ARG B CG  1 
ATOM   4580 C CD  . ARG B 1 273 ? 37.457  -14.931 26.953  1.00 21.30  ? 498  ARG B CD  1 
ATOM   4581 N NE  . ARG B 1 273 ? 36.397  -15.769 26.407  1.00 23.71  ? 498  ARG B NE  1 
ATOM   4582 C CZ  . ARG B 1 273 ? 35.369  -16.241 27.101  1.00 24.43  ? 498  ARG B CZ  1 
ATOM   4583 N NH1 . ARG B 1 273 ? 35.165  -15.897 28.365  1.00 28.19  ? 498  ARG B NH1 1 
ATOM   4584 N NH2 . ARG B 1 273 ? 34.531  -17.093 26.517  1.00 21.55  ? 498  ARG B NH2 1 
ATOM   4585 N N   . THR B 1 274 ? 36.109  -10.509 28.576  1.00 17.62  ? 499  THR B N   1 
ATOM   4586 C CA  . THR B 1 274 ? 35.312  -10.066 29.710  1.00 17.12  ? 499  THR B CA  1 
ATOM   4587 C C   . THR B 1 274 ? 33.949  -10.725 29.653  1.00 16.67  ? 499  THR B C   1 
ATOM   4588 O O   . THR B 1 274 ? 33.265  -10.651 28.630  1.00 18.35  ? 499  THR B O   1 
ATOM   4589 C CB  . THR B 1 274 ? 35.154  -8.551  29.710  1.00 20.59  ? 499  THR B CB  1 
ATOM   4590 O OG1 . THR B 1 274 ? 36.449  -7.945  29.745  1.00 22.41  ? 499  THR B OG1 1 
ATOM   4591 C CG2 . THR B 1 274 ? 34.344  -8.102  30.931  1.00 23.02  ? 499  THR B CG2 1 
ATOM   4592 N N   . GLU B 1 275 ? 33.560  -11.365 30.748  1.00 20.83  ? 500  GLU B N   1 
ATOM   4593 C CA  . GLU B 1 275 ? 32.258  -11.997 30.872  1.00 16.01  ? 500  GLU B CA  1 
ATOM   4594 C C   . GLU B 1 275 ? 31.314  -11.085 31.648  1.00 15.01  ? 500  GLU B C   1 
ATOM   4595 O O   . GLU B 1 275 ? 31.742  -10.237 32.436  1.00 16.46  ? 500  GLU B O   1 
ATOM   4596 C CB  . GLU B 1 275 ? 32.383  -13.346 31.578  1.00 21.22  ? 500  GLU B CB  1 
ATOM   4597 C CG  . GLU B 1 275 ? 31.824  -14.512 30.813  1.00 44.48  ? 500  GLU B CG  1 
ATOM   4598 C CD  . GLU B 1 275 ? 32.037  -15.805 31.556  1.00 54.04  ? 500  GLU B CD  1 
ATOM   4599 O OE1 . GLU B 1 275 ? 33.180  -16.037 32.006  1.00 46.71  ? 500  GLU B OE1 1 
ATOM   4600 O OE2 . GLU B 1 275 ? 31.061  -16.570 31.718  1.00 47.11  ? 500  GLU B OE2 1 
ATOM   4601 N N   . PHE B 1 276 ? 30.020  -11.275 31.410  1.00 13.34  ? 501  PHE B N   1 
ATOM   4602 C CA  . PHE B 1 276 ? 28.990  -10.460 32.027  1.00 16.54  ? 501  PHE B CA  1 
ATOM   4603 C C   . PHE B 1 276 ? 27.920  -11.334 32.661  1.00 16.10  ? 501  PHE B C   1 
ATOM   4604 O O   . PHE B 1 276 ? 27.697  -12.472 32.231  1.00 16.34  ? 501  PHE B O   1 
ATOM   4605 C CB  . PHE B 1 276 ? 28.349  -9.518  30.994  1.00 16.45  ? 501  PHE B CB  1 
ATOM   4606 C CG  . PHE B 1 276 ? 29.332  -8.601  30.335  1.00 12.91  ? 501  PHE B CG  1 
ATOM   4607 C CD1 . PHE B 1 276 ? 29.829  -7.491  31.009  1.00 17.72  ? 501  PHE B CD1 1 
ATOM   4608 C CD2 . PHE B 1 276 ? 29.785  -8.869  29.047  1.00 18.51  ? 501  PHE B CD2 1 
ATOM   4609 C CE1 . PHE B 1 276 ? 30.753  -6.649  30.406  1.00 19.15  ? 501  PHE B CE1 1 
ATOM   4610 C CE2 . PHE B 1 276 ? 30.715  -8.028  28.438  1.00 22.83  ? 501  PHE B CE2 1 
ATOM   4611 C CZ  . PHE B 1 276 ? 31.193  -6.920  29.116  1.00 25.88  ? 501  PHE B CZ  1 
ATOM   4612 N N   . PRO B 1 277 ? 27.234  -10.820 33.680  1.00 14.32  ? 502  PRO B N   1 
ATOM   4613 C CA  . PRO B 1 277 ? 26.141  -11.579 34.302  1.00 16.41  ? 502  PRO B CA  1 
ATOM   4614 C C   . PRO B 1 277 ? 25.045  -11.912 33.296  1.00 14.54  ? 502  PRO B C   1 
ATOM   4615 O O   . PRO B 1 277 ? 24.780  -11.155 32.361  1.00 15.58  ? 502  PRO B O   1 
ATOM   4616 C CB  . PRO B 1 277 ? 25.621  -10.628 35.390  1.00 21.39  ? 502  PRO B CB  1 
ATOM   4617 C CG  . PRO B 1 277 ? 26.726  -9.638  35.608  1.00 23.26  ? 502  PRO B CG  1 
ATOM   4618 C CD  . PRO B 1 277 ? 27.394  -9.487  34.284  1.00 14.68  ? 502  PRO B CD  1 
ATOM   4619 N N   . MET B 1 278 ? 24.387  -13.053 33.521  1.00 14.79  ? 503  MET B N   1 
ATOM   4620 C CA  . MET B 1 278 ? 23.382  -13.588 32.609  1.00 17.20  ? 503  MET B CA  1 
ATOM   4621 C C   . MET B 1 278 ? 21.955  -13.209 32.986  1.00 15.09  ? 503  MET B C   1 
ATOM   4622 O O   . MET B 1 278 ? 21.036  -13.475 32.205  1.00 16.22  ? 503  MET B O   1 
ATOM   4623 C CB  . MET B 1 278 ? 23.485  -15.117 32.550  1.00 14.42  ? 503  MET B CB  1 
ATOM   4624 C CG  . MET B 1 278 ? 24.729  -15.644 31.857  1.00 15.42  ? 503  MET B CG  1 
ATOM   4625 S SD  . MET B 1 278 ? 24.702  -15.296 30.095  1.00 15.55  ? 503  MET B SD  1 
ATOM   4626 C CE  . MET B 1 278 ? 23.379  -16.380 29.587  1.00 14.78  ? 503  MET B CE  1 
ATOM   4627 N N   . SER B 1 279 ? 21.744  -12.603 34.155  1.00 16.01  ? 504  SER B N   1 
ATOM   4628 C CA  . SER B 1 279 ? 20.398  -12.311 34.630  1.00 14.04  ? 504  SER B CA  1 
ATOM   4629 C C   . SER B 1 279 ? 19.909  -10.925 34.219  1.00 21.23  ? 504  SER B C   1 
ATOM   4630 O O   . SER B 1 279 ? 18.895  -10.454 34.746  1.00 25.76  ? 504  SER B O   1 
ATOM   4631 C CB  . SER B 1 279 ? 20.349  -12.457 36.155  1.00 20.65  ? 504  SER B CB  1 
ATOM   4632 O OG  . SER B 1 279 ? 21.399  -11.711 36.742  1.00 29.87  ? 504  SER B OG  1 
ATOM   4633 N N   . GLY B 1 280 ? 20.613  -10.253 33.311  1.00 17.03  ? 505  GLY B N   1 
ATOM   4634 C CA  . GLY B 1 280 ? 20.204  -8.934  32.888  1.00 17.84  ? 505  GLY B CA  1 
ATOM   4635 C C   . GLY B 1 280 ? 19.253  -8.972  31.703  1.00 14.08  ? 505  GLY B C   1 
ATOM   4636 O O   . GLY B 1 280 ? 19.097  -9.998  31.038  1.00 14.62  ? 505  GLY B O   1 
ATOM   4637 N N   . VAL B 1 281 ? 18.625  -7.822  31.449  1.00 14.89  ? 506  VAL B N   1 
ATOM   4638 C CA  . VAL B 1 281 ? 17.755  -7.621  30.293  1.00 15.25  ? 506  VAL B CA  1 
ATOM   4639 C C   . VAL B 1 281 ? 18.301  -6.457  29.476  1.00 12.22  ? 506  VAL B C   1 
ATOM   4640 O O   . VAL B 1 281 ? 18.683  -5.424  30.036  1.00 16.82  ? 506  VAL B O   1 
ATOM   4641 C CB  . VAL B 1 281 ? 16.292  -7.349  30.714  1.00 16.90  ? 506  VAL B CB  1 
ATOM   4642 C CG1 . VAL B 1 281 ? 15.410  -7.093  29.490  1.00 17.26  ? 506  VAL B CG1 1 
ATOM   4643 C CG2 . VAL B 1 281 ? 15.739  -8.531  31.480  1.00 17.69  ? 506  VAL B CG2 1 
ATOM   4644 N N   . PHE B 1 282 ? 18.348  -6.629  28.148  1.00 15.29  ? 507  PHE B N   1 
ATOM   4645 C CA  . PHE B 1 282 ? 18.703  -5.536  27.246  1.00 15.80  ? 507  PHE B CA  1 
ATOM   4646 C C   . PHE B 1 282 ? 17.475  -4.668  27.004  1.00 16.07  ? 507  PHE B C   1 
ATOM   4647 O O   . PHE B 1 282 ? 16.443  -5.171  26.545  1.00 19.23  ? 507  PHE B O   1 
ATOM   4648 C CB  . PHE B 1 282 ? 19.221  -6.084  25.915  1.00 14.88  ? 507  PHE B CB  1 
ATOM   4649 C CG  . PHE B 1 282 ? 20.540  -6.791  26.010  1.00 12.33  ? 507  PHE B CG  1 
ATOM   4650 C CD1 . PHE B 1 282 ? 20.599  -8.136  26.338  1.00 14.08  ? 507  PHE B CD1 1 
ATOM   4651 C CD2 . PHE B 1 282 ? 21.724  -6.115  25.728  1.00 12.92  ? 507  PHE B CD2 1 
ATOM   4652 C CE1 . PHE B 1 282 ? 21.826  -8.793  26.398  1.00 11.97  ? 507  PHE B CE1 1 
ATOM   4653 C CE2 . PHE B 1 282 ? 22.954  -6.759  25.791  1.00 15.52  ? 507  PHE B CE2 1 
ATOM   4654 C CZ  . PHE B 1 282 ? 23.008  -8.097  26.125  1.00 15.01  ? 507  PHE B CZ  1 
ATOM   4655 N N   . GLU B 1 283 ? 17.590  -3.370  27.284  1.00 17.00  ? 508  GLU B N   1 
ATOM   4656 C CA  . GLU B 1 283 ? 16.500  -2.411  27.139  1.00 19.03  ? 508  GLU B CA  1 
ATOM   4657 C C   . GLU B 1 283 ? 16.878  -1.371  26.096  1.00 21.21  ? 508  GLU B C   1 
ATOM   4658 O O   . GLU B 1 283 ? 17.972  -0.808  26.159  1.00 19.01  ? 508  GLU B O   1 
ATOM   4659 C CB  . GLU B 1 283 ? 16.203  -1.719  28.475  1.00 20.22  ? 508  GLU B CB  1 
ATOM   4660 C CG  . GLU B 1 283 ? 15.888  -2.705  29.592  1.00 28.62  ? 508  GLU B CG  1 
ATOM   4661 C CD  . GLU B 1 283 ? 15.800  -2.057  30.970  1.00 32.40  ? 508  GLU B CD  1 
ATOM   4662 O OE1 . GLU B 1 283 ? 16.177  -0.876  31.113  1.00 29.26  ? 508  GLU B OE1 1 
ATOM   4663 O OE2 . GLU B 1 283 ? 15.363  -2.744  31.917  1.00 50.31  ? 508  GLU B OE2 1 
ATOM   4664 N N   . PHE B 1 284 ? 15.967  -1.106  25.158  1.00 21.38  ? 509  PHE B N   1 
ATOM   4665 C CA  . PHE B 1 284 ? 16.197  -0.069  24.158  1.00 17.46  ? 509  PHE B CA  1 
ATOM   4666 C C   . PHE B 1 284 ? 16.180  1.318   24.788  1.00 19.72  ? 509  PHE B C   1 
ATOM   4667 O O   . PHE B 1 284 ? 15.312  1.647   25.603  1.00 20.98  ? 509  PHE B O   1 
ATOM   4668 C CB  . PHE B 1 284 ? 15.138  -0.153  23.057  1.00 20.29  ? 509  PHE B CB  1 
ATOM   4669 C CG  . PHE B 1 284 ? 15.201  0.975   22.053  1.00 15.95  ? 509  PHE B CG  1 
ATOM   4670 C CD1 . PHE B 1 284 ? 16.223  1.039   21.120  1.00 17.12  ? 509  PHE B CD1 1 
ATOM   4671 C CD2 . PHE B 1 284 ? 14.206  1.947   22.017  1.00 24.17  ? 509  PHE B CD2 1 
ATOM   4672 C CE1 . PHE B 1 284 ? 16.279  2.074   20.189  1.00 20.80  ? 509  PHE B CE1 1 
ATOM   4673 C CE2 . PHE B 1 284 ? 14.251  2.981   21.084  1.00 27.44  ? 509  PHE B CE2 1 
ATOM   4674 C CZ  . PHE B 1 284 ? 15.286  3.040   20.170  1.00 21.72  ? 509  PHE B CZ  1 
ATOM   4675 N N   . VAL B 1 285 ? 17.138  2.149   24.393  1.00 18.18  ? 510  VAL B N   1 
ATOM   4676 C CA  . VAL B 1 285 ? 17.228  3.521   24.863  1.00 19.70  ? 510  VAL B CA  1 
ATOM   4677 C C   . VAL B 1 285 ? 16.839  4.499   23.768  1.00 22.51  ? 510  VAL B C   1 
ATOM   4678 O O   . VAL B 1 285 ? 15.881  5.261   23.915  1.00 24.09  ? 510  VAL B O   1 
ATOM   4679 C CB  . VAL B 1 285 ? 18.637  3.827   25.416  1.00 21.46  ? 510  VAL B CB  1 
ATOM   4680 C CG1 . VAL B 1 285 ? 18.732  5.281   25.835  1.00 19.61  ? 510  VAL B CG1 1 
ATOM   4681 C CG2 . VAL B 1 285 ? 18.956  2.895   26.576  1.00 21.21  ? 510  VAL B CG2 1 
ATOM   4682 N N   . SER B 1 286 ? 17.565  4.487   22.654  1.00 20.02  ? 511  SER B N   1 
ATOM   4683 C CA  . SER B 1 286 ? 17.359  5.457   21.587  1.00 19.08  ? 511  SER B CA  1 
ATOM   4684 C C   . SER B 1 286 ? 18.140  4.998   20.365  1.00 19.53  ? 511  SER B C   1 
ATOM   4685 O O   . SER B 1 286 ? 18.946  4.068   20.435  1.00 22.26  ? 511  SER B O   1 
ATOM   4686 C CB  . SER B 1 286 ? 17.817  6.849   22.014  1.00 19.41  ? 511  SER B CB  1 
ATOM   4687 O OG  . SER B 1 286 ? 19.225  6.863   22.167  1.00 30.28  ? 511  SER B OG  1 
ATOM   4688 N N   . TRP B 1 287 ? 17.917  5.685   19.247  1.00 19.91  ? 512  TRP B N   1 
ATOM   4689 C CA  . TRP B 1 287 ? 18.687  5.439   18.034  1.00 21.86  ? 512  TRP B CA  1 
ATOM   4690 C C   . TRP B 1 287 ? 19.907  6.352   18.008  1.00 20.86  ? 512  TRP B C   1 
ATOM   4691 O O   . TRP B 1 287 ? 19.824  7.527   18.380  1.00 22.50  ? 512  TRP B O   1 
ATOM   4692 C CB  . TRP B 1 287 ? 17.828  5.672   16.786  1.00 21.80  ? 512  TRP B CB  1 
ATOM   4693 C CG  . TRP B 1 287 ? 16.758  4.642   16.613  1.00 21.85  ? 512  TRP B CG  1 
ATOM   4694 C CD1 . TRP B 1 287 ? 15.436  4.766   16.925  1.00 26.39  ? 512  TRP B CD1 1 
ATOM   4695 C CD2 . TRP B 1 287 ? 16.925  3.311   16.103  1.00 19.96  ? 512  TRP B CD2 1 
ATOM   4696 N NE1 . TRP B 1 287 ? 14.770  3.597   16.638  1.00 23.31  ? 512  TRP B NE1 1 
ATOM   4697 C CE2 . TRP B 1 287 ? 15.661  2.690   16.131  1.00 22.07  ? 512  TRP B CE2 1 
ATOM   4698 C CE3 . TRP B 1 287 ? 18.021  2.591   15.615  1.00 22.48  ? 512  TRP B CE3 1 
ATOM   4699 C CZ2 . TRP B 1 287 ? 15.461  1.384   15.687  1.00 20.45  ? 512  TRP B CZ2 1 
ATOM   4700 C CZ3 . TRP B 1 287 ? 17.825  1.296   15.184  1.00 19.17  ? 512  TRP B CZ3 1 
ATOM   4701 C CH2 . TRP B 1 287 ? 16.551  0.702   15.224  1.00 23.10  ? 512  TRP B CH2 1 
ATOM   4702 N N   . VAL B 1 288 ? 21.040  5.809   17.568  1.00 17.33  ? 513  VAL B N   1 
ATOM   4703 C CA  . VAL B 1 288 ? 22.274  6.591   17.494  1.00 16.98  ? 513  VAL B CA  1 
ATOM   4704 C C   . VAL B 1 288 ? 22.944  6.336   16.149  1.00 20.55  ? 513  VAL B C   1 
ATOM   4705 O O   . VAL B 1 288 ? 22.709  5.308   15.493  1.00 22.82  ? 513  VAL B O   1 
ATOM   4706 C CB  . VAL B 1 288 ? 23.235  6.269   18.666  1.00 18.54  ? 513  VAL B CB  1 
ATOM   4707 C CG1 . VAL B 1 288 ? 22.602  6.624   20.018  1.00 20.43  ? 513  VAL B CG1 1 
ATOM   4708 C CG2 . VAL B 1 288 ? 23.678  4.815   18.638  1.00 16.19  ? 513  VAL B CG2 1 
ATOM   4709 N N   . PRO B 1 289 ? 23.780  7.268   15.704  1.00 22.71  ? 514  PRO B N   1 
ATOM   4710 C CA  . PRO B 1 289 ? 24.567  7.044   14.482  1.00 17.41  ? 514  PRO B CA  1 
ATOM   4711 C C   . PRO B 1 289 ? 25.719  6.076   14.721  1.00 23.62  ? 514  PRO B C   1 
ATOM   4712 O O   . PRO B 1 289 ? 26.092  5.762   15.854  1.00 21.53  ? 514  PRO B O   1 
ATOM   4713 C CB  . PRO B 1 289 ? 25.085  8.438   14.134  1.00 21.60  ? 514  PRO B CB  1 
ATOM   4714 C CG  . PRO B 1 289 ? 25.098  9.167   15.436  1.00 26.23  ? 514  PRO B CG  1 
ATOM   4715 C CD  . PRO B 1 289 ? 23.925  8.641   16.216  1.00 22.53  ? 514  PRO B CD  1 
ATOM   4716 N N   . ASN B 1 290 ? 26.314  5.631   13.609  1.00 19.84  ? 515  ASN B N   1 
ATOM   4717 C CA  . ASN B 1 290 ? 27.435  4.692   13.669  1.00 18.97  ? 515  ASN B CA  1 
ATOM   4718 C C   . ASN B 1 290 ? 28.620  5.258   14.444  1.00 18.74  ? 515  ASN B C   1 
ATOM   4719 O O   . ASN B 1 290 ? 29.326  4.508   15.129  1.00 22.27  ? 515  ASN B O   1 
ATOM   4720 C CB  . ASN B 1 290 ? 27.886  4.311   12.257  1.00 21.30  ? 515  ASN B CB  1 
ATOM   4721 C CG  . ASN B 1 290 ? 26.936  3.351   11.578  1.00 39.09  ? 515  ASN B CG  1 
ATOM   4722 O OD1 . ASN B 1 290 ? 26.406  2.436   12.207  1.00 34.49  ? 515  ASN B OD1 1 
ATOM   4723 N ND2 . ASN B 1 290 ? 26.706  3.558   10.284  1.00 27.71  ? 515  ASN B ND2 1 
ATOM   4724 N N   . PHE B 1 291 ? 28.854  6.561   14.364  1.00 17.72  ? 516  PHE B N   1 
ATOM   4725 C CA  . PHE B 1 291 ? 30.019  7.132   15.033  1.00 18.32  ? 516  PHE B CA  1 
ATOM   4726 C C   . PHE B 1 291 ? 29.813  7.341   16.525  1.00 18.89  ? 516  PHE B C   1 
ATOM   4727 O O   . PHE B 1 291 ? 30.756  7.766   17.205  1.00 23.50  ? 516  PHE B O   1 
ATOM   4728 C CB  . PHE B 1 291 ? 30.425  8.463   14.381  1.00 23.62  ? 516  PHE B CB  1 
ATOM   4729 C CG  . PHE B 1 291 ? 29.404  9.565   14.511  1.00 29.14  ? 516  PHE B CG  1 
ATOM   4730 C CD1 . PHE B 1 291 ? 29.291  10.305  15.689  1.00 28.15  ? 516  PHE B CD1 1 
ATOM   4731 C CD2 . PHE B 1 291 ? 28.593  9.904   13.435  1.00 30.55  ? 516  PHE B CD2 1 
ATOM   4732 C CE1 . PHE B 1 291 ? 28.368  11.328  15.797  1.00 27.19  ? 516  PHE B CE1 1 
ATOM   4733 C CE2 . PHE B 1 291 ? 27.667  10.928  13.540  1.00 31.65  ? 516  PHE B CE2 1 
ATOM   4734 C CZ  . PHE B 1 291 ? 27.557  11.641  14.723  1.00 29.09  ? 516  PHE B CZ  1 
ATOM   4735 N N   . PHE B 1 292 ? 28.609  7.099   17.038  1.00 20.01  ? 517  PHE B N   1 
ATOM   4736 C CA  . PHE B 1 292 ? 28.352  7.304   18.457  1.00 25.50  ? 517  PHE B CA  1 
ATOM   4737 C C   . PHE B 1 292 ? 29.266  6.419   19.295  1.00 20.38  ? 517  PHE B C   1 
ATOM   4738 O O   . PHE B 1 292 ? 29.319  5.203   19.101  1.00 20.28  ? 517  PHE B O   1 
ATOM   4739 C CB  . PHE B 1 292 ? 26.890  6.997   18.779  1.00 24.11  ? 517  PHE B CB  1 
ATOM   4740 C CG  . PHE B 1 292 ? 26.537  7.221   20.217  1.00 27.39  ? 517  PHE B CG  1 
ATOM   4741 C CD1 . PHE B 1 292 ? 26.249  8.493   20.676  1.00 27.62  ? 517  PHE B CD1 1 
ATOM   4742 C CD2 . PHE B 1 292 ? 26.513  6.165   21.109  1.00 19.33  ? 517  PHE B CD2 1 
ATOM   4743 C CE1 . PHE B 1 292 ? 25.933  8.705   21.999  1.00 23.80  ? 517  PHE B CE1 1 
ATOM   4744 C CE2 . PHE B 1 292 ? 26.198  6.370   22.430  1.00 18.69  ? 517  PHE B CE2 1 
ATOM   4745 C CZ  . PHE B 1 292 ? 25.905  7.640   22.875  1.00 23.75  ? 517  PHE B CZ  1 
ATOM   4746 N N   . GLN B 1 293 ? 29.979  7.028   20.240  1.00 20.91  ? 518  GLN B N   1 
ATOM   4747 C CA  . GLN B 1 293 ? 30.928  6.303   21.072  1.00 18.47  ? 518  GLN B CA  1 
ATOM   4748 C C   . GLN B 1 293 ? 30.304  5.978   22.423  1.00 20.58  ? 518  GLN B C   1 
ATOM   4749 O O   . GLN B 1 293 ? 29.914  6.887   23.170  1.00 20.29  ? 518  GLN B O   1 
ATOM   4750 C CB  . GLN B 1 293 ? 32.216  7.102   21.237  1.00 19.32  ? 518  GLN B CB  1 
ATOM   4751 C CG  . GLN B 1 293 ? 32.986  7.174   19.943  1.00 21.79  ? 518  GLN B CG  1 
ATOM   4752 C CD  . GLN B 1 293 ? 34.320  7.842   20.109  1.00 27.19  ? 518  GLN B CD  1 
ATOM   4753 O OE1 . GLN B 1 293 ? 35.030  7.601   21.084  1.00 23.10  ? 518  GLN B OE1 1 
ATOM   4754 N NE2 . GLN B 1 293 ? 34.663  8.705   19.169  1.00 24.28  ? 518  GLN B NE2 1 
ATOM   4755 N N   . LEU B 1 294 ? 30.227  4.680   22.719  1.00 19.07  ? 519  LEU B N   1 
ATOM   4756 C CA  . LEU B 1 294 ? 29.655  4.159   23.952  1.00 17.66  ? 519  LEU B CA  1 
ATOM   4757 C C   . LEU B 1 294 ? 30.538  4.467   25.151  1.00 19.78  ? 519  LEU B C   1 
ATOM   4758 O O   . LEU B 1 294 ? 31.761  4.588   25.040  1.00 21.51  ? 519  LEU B O   1 
ATOM   4759 C CB  . LEU B 1 294 ? 29.487  2.647   23.842  1.00 16.45  ? 519  LEU B CB  1 
ATOM   4760 C CG  . LEU B 1 294 ? 28.534  2.139   22.773  1.00 15.81  ? 519  LEU B CG  1 
ATOM   4761 C CD1 . LEU B 1 294 ? 28.860  0.692   22.409  1.00 15.13  ? 519  LEU B CD1 1 
ATOM   4762 C CD2 . LEU B 1 294 ? 27.128  2.228   23.338  1.00 16.78  ? 519  LEU B CD2 1 
ATOM   4763 N N   . ALA B 1 295 ? 29.902  4.575   26.314  1.00 19.18  ? 520  ALA B N   1 
ATOM   4764 C CA  . ALA B 1 295 ? 30.652  4.564   27.556  1.00 24.43  ? 520  ALA B CA  1 
ATOM   4765 C C   . ALA B 1 295 ? 31.382  3.232   27.676  1.00 21.45  ? 520  ALA B C   1 
ATOM   4766 O O   . ALA B 1 295 ? 30.806  2.181   27.367  1.00 23.80  ? 520  ALA B O   1 
ATOM   4767 C CB  . ALA B 1 295 ? 29.719  4.764   28.754  1.00 24.01  ? 520  ALA B CB  1 
ATOM   4768 N N   . PRO B 1 296 ? 32.646  3.229   28.084  1.00 20.25  ? 521  PRO B N   1 
ATOM   4769 C CA  . PRO B 1 296 ? 33.357  1.954   28.229  1.00 21.88  ? 521  PRO B CA  1 
ATOM   4770 C C   . PRO B 1 296 ? 32.699  1.068   29.277  1.00 25.60  ? 521  PRO B C   1 
ATOM   4771 O O   . PRO B 1 296 ? 32.075  1.549   30.225  1.00 27.37  ? 521  PRO B O   1 
ATOM   4772 C CB  . PRO B 1 296 ? 34.770  2.381   28.651  1.00 25.94  ? 521  PRO B CB  1 
ATOM   4773 C CG  . PRO B 1 296 ? 34.616  3.787   29.151  1.00 35.01  ? 521  PRO B CG  1 
ATOM   4774 C CD  . PRO B 1 296 ? 33.521  4.385   28.339  1.00 26.79  ? 521  PRO B CD  1 
ATOM   4775 N N   . VAL B 1 297 ? 32.837  -0.241  29.096  1.00 20.39  ? 522  VAL B N   1 
ATOM   4776 C CA  . VAL B 1 297 ? 32.241  -1.169  30.053  1.00 20.32  ? 522  VAL B CA  1 
ATOM   4777 C C   . VAL B 1 297 ? 32.873  -0.959  31.425  1.00 43.17  ? 522  VAL B C   1 
ATOM   4778 O O   . VAL B 1 297 ? 34.072  -0.675  31.538  1.00 30.70  ? 522  VAL B O   1 
ATOM   4779 C CB  . VAL B 1 297 ? 32.377  -2.639  29.605  1.00 22.88  ? 522  VAL B CB  1 
ATOM   4780 C CG1 . VAL B 1 297 ? 31.504  -2.905  28.384  1.00 21.17  ? 522  VAL B CG1 1 
ATOM   4781 C CG2 . VAL B 1 297 ? 33.822  -2.987  29.320  1.00 29.21  ? 522  VAL B CG2 1 
ATOM   4782 O OXT . VAL B 1 297 ? 32.182  -1.049  32.443  1.00 31.51  ? 522  VAL B OXT 1 
HETATM 4783 S S   . SO4 C 2 .   ? 12.047  -48.751 14.189  1.00 81.80  ? 601  SO4 A S   1 
HETATM 4784 O O1  . SO4 C 2 .   ? 12.494  -47.831 13.143  1.00 42.92  ? 601  SO4 A O1  1 
HETATM 4785 O O2  . SO4 C 2 .   ? 11.182  -49.771 13.604  1.00 71.51  ? 601  SO4 A O2  1 
HETATM 4786 O O3  . SO4 C 2 .   ? 13.197  -49.391 14.824  1.00 65.90  ? 601  SO4 A O3  1 
HETATM 4787 O O4  . SO4 C 2 .   ? 11.299  -48.005 15.195  1.00 63.87  ? 601  SO4 A O4  1 
HETATM 4788 S S   . SO4 D 2 .   ? -0.060  -26.481 3.518   1.00 39.02  ? 602  SO4 A S   1 
HETATM 4789 O O1  . SO4 D 2 .   ? 1.371   -26.201 3.413   1.00 39.60  ? 602  SO4 A O1  1 
HETATM 4790 O O2  . SO4 D 2 .   ? -0.765  -25.214 3.727   1.00 36.38  ? 602  SO4 A O2  1 
HETATM 4791 O O3  . SO4 D 2 .   ? -0.535  -27.081 2.274   1.00 61.48  ? 602  SO4 A O3  1 
HETATM 4792 O O4  . SO4 D 2 .   ? -0.313  -27.415 4.623   1.00 33.11  ? 602  SO4 A O4  1 
HETATM 4793 S S   . SO4 E 2 .   ? 24.210  -14.474 36.784  1.00 106.02 ? 601  SO4 B S   1 
HETATM 4794 O O1  . SO4 E 2 .   ? 25.225  -14.589 35.732  1.00 27.95  ? 601  SO4 B O1  1 
HETATM 4795 O O2  . SO4 E 2 .   ? 23.444  -13.245 36.600  1.00 53.73  ? 601  SO4 B O2  1 
HETATM 4796 O O3  . SO4 E 2 .   ? 23.295  -15.617 36.735  1.00 47.84  ? 601  SO4 B O3  1 
HETATM 4797 O O4  . SO4 E 2 .   ? 24.868  -14.428 38.089  1.00 92.24  ? 601  SO4 B O4  1 
HETATM 4798 S S   . SO4 F 2 .   ? 35.322  -36.479 25.637  1.00 32.83  ? 602  SO4 B S   1 
HETATM 4799 O O1  . SO4 F 2 .   ? 35.630  -37.817 25.117  1.00 44.16  ? 602  SO4 B O1  1 
HETATM 4800 O O2  . SO4 F 2 .   ? 36.481  -35.947 26.365  1.00 30.11  ? 602  SO4 B O2  1 
HETATM 4801 O O3  . SO4 F 2 .   ? 34.979  -35.600 24.518  1.00 27.73  ? 602  SO4 B O3  1 
HETATM 4802 O O4  . SO4 F 2 .   ? 34.208  -36.570 26.579  1.00 24.90  ? 602  SO4 B O4  1 
HETATM 4803 O O   . HOH G 3 .   ? 14.882  -25.998 42.802  1.00 40.51  ? 701  HOH A O   1 
HETATM 4804 O O   . HOH G 3 .   ? 6.939   -12.796 31.729  1.00 31.63  ? 702  HOH A O   1 
HETATM 4805 O O   . HOH G 3 .   ? 0.346   -42.268 36.936  1.00 47.43  ? 703  HOH A O   1 
HETATM 4806 O O   . HOH G 3 .   ? 29.030  -26.127 38.512  1.00 48.18  ? 704  HOH A O   1 
HETATM 4807 O O   . HOH G 3 .   ? -2.891  -15.973 34.239  1.00 21.73  ? 705  HOH A O   1 
HETATM 4808 O O   . HOH G 3 .   ? 5.414   -32.075 48.411  1.00 29.53  ? 706  HOH A O   1 
HETATM 4809 O O   . HOH G 3 .   ? -18.978 -16.378 30.254  1.00 37.81  ? 707  HOH A O   1 
HETATM 4810 O O   . HOH G 3 .   ? 2.671   -20.125 37.078  1.00 34.96  ? 708  HOH A O   1 
HETATM 4811 O O   . HOH G 3 .   ? -4.982  -38.716 27.894  1.00 36.29  ? 709  HOH A O   1 
HETATM 4812 O O   . HOH G 3 .   ? 0.918   -46.526 17.736  1.00 26.64  ? 710  HOH A O   1 
HETATM 4813 O O   . HOH G 3 .   ? 25.164  -44.897 23.407  1.00 50.08  ? 711  HOH A O   1 
HETATM 4814 O O   . HOH G 3 .   ? -21.044 -27.402 21.580  1.00 42.53  ? 712  HOH A O   1 
HETATM 4815 O O   . HOH G 3 .   ? -6.192  -21.236 0.202   1.00 43.64  ? 713  HOH A O   1 
HETATM 4816 O O   . HOH G 3 .   ? -3.819  -39.812 22.334  1.00 24.11  ? 714  HOH A O   1 
HETATM 4817 O O   . HOH G 3 .   ? 24.038  -31.091 44.728  1.00 28.51  ? 715  HOH A O   1 
HETATM 4818 O O   . HOH G 3 .   ? 34.364  -45.913 33.752  1.00 40.42  ? 716  HOH A O   1 
HETATM 4819 O O   . HOH G 3 .   ? 0.090   -16.777 15.187  1.00 34.53  ? 717  HOH A O   1 
HETATM 4820 O O   . HOH G 3 .   ? 2.616   -53.751 11.791  1.00 40.76  ? 718  HOH A O   1 
HETATM 4821 O O   . HOH G 3 .   ? 6.201   -16.322 5.486   1.00 40.74  ? 719  HOH A O   1 
HETATM 4822 O O   . HOH G 3 .   ? 4.875   -47.075 38.018  1.00 37.26  ? 720  HOH A O   1 
HETATM 4823 O O   . HOH G 3 .   ? -1.704  -35.666 11.526  1.00 42.78  ? 721  HOH A O   1 
HETATM 4824 O O   . HOH G 3 .   ? 15.908  -49.655 38.297  1.00 42.70  ? 722  HOH A O   1 
HETATM 4825 O O   . HOH G 3 .   ? -6.724  -36.429 31.472  1.00 41.62  ? 723  HOH A O   1 
HETATM 4826 O O   . HOH G 3 .   ? 5.048   -49.918 17.287  1.00 33.58  ? 724  HOH A O   1 
HETATM 4827 O O   . HOH G 3 .   ? 7.454   -47.823 33.766  1.00 30.50  ? 725  HOH A O   1 
HETATM 4828 O O   . HOH G 3 .   ? 3.046   -53.056 25.969  1.00 56.62  ? 726  HOH A O   1 
HETATM 4829 O O   . HOH G 3 .   ? -15.827 -30.172 17.052  1.00 33.07  ? 727  HOH A O   1 
HETATM 4830 O O   . HOH G 3 .   ? -0.220  -18.388 13.440  1.00 29.75  ? 728  HOH A O   1 
HETATM 4831 O O   . HOH G 3 .   ? 23.662  -46.076 24.928  1.00 40.62  ? 729  HOH A O   1 
HETATM 4832 O O   . HOH G 3 .   ? -1.488  -12.872 14.114  1.00 20.95  ? 730  HOH A O   1 
HETATM 4833 O O   . HOH G 3 .   ? 30.816  -30.599 34.793  1.00 21.32  ? 731  HOH A O   1 
HETATM 4834 O O   . HOH G 3 .   ? 7.186   -33.719 43.970  1.00 21.57  ? 732  HOH A O   1 
HETATM 4835 O O   . HOH G 3 .   ? 10.405  -26.111 21.033  1.00 27.11  ? 733  HOH A O   1 
HETATM 4836 O O   . HOH G 3 .   ? 14.587  -47.975 22.399  1.00 29.35  ? 734  HOH A O   1 
HETATM 4837 O O   . HOH G 3 .   ? -2.432  -12.842 35.847  1.00 36.21  ? 735  HOH A O   1 
HETATM 4838 O O   . HOH G 3 .   ? -14.254 -32.353 9.370   1.00 45.65  ? 736  HOH A O   1 
HETATM 4839 O O   . HOH G 3 .   ? 8.212   -47.670 41.058  1.00 47.70  ? 737  HOH A O   1 
HETATM 4840 O O   . HOH G 3 .   ? 8.607   -18.863 35.830  1.00 39.52  ? 738  HOH A O   1 
HETATM 4841 O O   . HOH G 3 .   ? 17.314  -50.070 35.403  1.00 27.50  ? 739  HOH A O   1 
HETATM 4842 O O   . HOH G 3 .   ? 30.141  -46.424 30.462  1.00 20.71  ? 740  HOH A O   1 
HETATM 4843 O O   . HOH G 3 .   ? -18.070 -28.637 10.092  1.00 35.55  ? 741  HOH A O   1 
HETATM 4844 O O   . HOH G 3 .   ? 0.573   -46.396 36.460  1.00 43.93  ? 742  HOH A O   1 
HETATM 4845 O O   . HOH G 3 .   ? 14.908  -32.992 22.005  1.00 25.16  ? 743  HOH A O   1 
HETATM 4846 O O   . HOH G 3 .   ? 4.487   -46.251 24.013  1.00 18.36  ? 744  HOH A O   1 
HETATM 4847 O O   . HOH G 3 .   ? 3.706   -26.219 5.031   1.00 34.39  ? 745  HOH A O   1 
HETATM 4848 O O   . HOH G 3 .   ? -4.177  -7.213  18.024  1.00 34.89  ? 746  HOH A O   1 
HETATM 4849 O O   . HOH G 3 .   ? -0.538  -17.231 5.571   1.00 35.88  ? 747  HOH A O   1 
HETATM 4850 O O   . HOH G 3 .   ? -23.573 -21.675 23.382  1.00 34.12  ? 748  HOH A O   1 
HETATM 4851 O O   . HOH G 3 .   ? -8.189  -33.015 19.150  1.00 19.88  ? 749  HOH A O   1 
HETATM 4852 O O   . HOH G 3 .   ? 10.052  -28.197 38.486  1.00 22.13  ? 750  HOH A O   1 
HETATM 4853 O O   . HOH G 3 .   ? 1.980   -39.363 37.400  1.00 25.73  ? 751  HOH A O   1 
HETATM 4854 O O   . HOH G 3 .   ? -26.797 -23.901 20.107  1.00 27.78  ? 752  HOH A O   1 
HETATM 4855 O O   . HOH G 3 .   ? -5.850  -36.675 24.570  1.00 20.86  ? 753  HOH A O   1 
HETATM 4856 O O   . HOH G 3 .   ? 28.101  -46.264 22.354  1.00 43.68  ? 754  HOH A O   1 
HETATM 4857 O O   . HOH G 3 .   ? 8.824   -7.798  26.060  1.00 19.65  ? 755  HOH A O   1 
HETATM 4858 O O   . HOH G 3 .   ? 9.922   -19.870 14.867  1.00 15.54  ? 756  HOH A O   1 
HETATM 4859 O O   . HOH G 3 .   ? 15.212  -29.823 33.159  1.00 14.05  ? 757  HOH A O   1 
HETATM 4860 O O   . HOH G 3 .   ? -5.991  -6.302  20.060  1.00 36.55  ? 758  HOH A O   1 
HETATM 4861 O O   . HOH G 3 .   ? -3.838  -6.186  27.813  1.00 46.22  ? 759  HOH A O   1 
HETATM 4862 O O   . HOH G 3 .   ? 17.546  -46.205 33.061  1.00 14.54  ? 760  HOH A O   1 
HETATM 4863 O O   . HOH G 3 .   ? 26.029  -28.666 34.350  1.00 43.41  ? 761  HOH A O   1 
HETATM 4864 O O   . HOH G 3 .   ? 7.996   -19.755 5.480   1.00 31.87  ? 762  HOH A O   1 
HETATM 4865 O O   . HOH G 3 .   ? 26.936  -38.812 46.263  1.00 23.19  ? 763  HOH A O   1 
HETATM 4866 O O   . HOH G 3 .   ? 12.637  -38.943 46.909  1.00 38.20  ? 764  HOH A O   1 
HETATM 4867 O O   . HOH G 3 .   ? -19.290 -22.653 9.016   1.00 40.28  ? 765  HOH A O   1 
HETATM 4868 O O   . HOH G 3 .   ? -4.774  -22.860 2.542   1.00 36.81  ? 766  HOH A O   1 
HETATM 4869 O O   . HOH G 3 .   ? 7.941   -44.619 44.249  1.00 43.33  ? 767  HOH A O   1 
HETATM 4870 O O   . HOH G 3 .   ? 5.095   -48.507 40.370  1.00 49.26  ? 768  HOH A O   1 
HETATM 4871 O O   . HOH G 3 .   ? -11.155 -36.123 21.245  1.00 39.02  ? 769  HOH A O   1 
HETATM 4872 O O   . HOH G 3 .   ? -3.831  -37.649 33.462  1.00 30.98  ? 770  HOH A O   1 
HETATM 4873 O O   . HOH G 3 .   ? -2.395  -28.201 41.862  1.00 20.93  ? 771  HOH A O   1 
HETATM 4874 O O   . HOH G 3 .   ? -16.516 -10.295 20.696  1.00 35.19  ? 772  HOH A O   1 
HETATM 4875 O O   . HOH G 3 .   ? -0.047  -6.772  20.815  1.00 39.77  ? 773  HOH A O   1 
HETATM 4876 O O   . HOH G 3 .   ? 20.505  -29.494 20.660  1.00 27.00  ? 774  HOH A O   1 
HETATM 4877 O O   . HOH G 3 .   ? 6.853   -26.247 27.050  1.00 11.79  ? 775  HOH A O   1 
HETATM 4878 O O   . HOH G 3 .   ? 6.518   -23.941 34.633  1.00 21.96  ? 776  HOH A O   1 
HETATM 4879 O O   . HOH G 3 .   ? 14.548  -41.620 40.497  1.00 20.77  ? 777  HOH A O   1 
HETATM 4880 O O   . HOH G 3 .   ? -1.891  -45.581 25.707  1.00 21.97  ? 778  HOH A O   1 
HETATM 4881 O O   . HOH G 3 .   ? -4.398  -28.196 38.449  1.00 19.47  ? 779  HOH A O   1 
HETATM 4882 O O   A HOH G 3 .   ? 14.253  -51.279 28.099  0.51 30.42  ? 780  HOH A O   1 
HETATM 4883 O O   B HOH G 3 .   ? 15.842  -50.520 26.657  0.49 30.00  ? 780  HOH A O   1 
HETATM 4884 O O   . HOH G 3 .   ? -0.965  -39.498 21.672  1.00 23.56  ? 781  HOH A O   1 
HETATM 4885 O O   . HOH G 3 .   ? 3.088   -11.299 30.877  1.00 35.29  ? 782  HOH A O   1 
HETATM 4886 O O   . HOH G 3 .   ? -9.960  -32.520 25.344  1.00 26.05  ? 783  HOH A O   1 
HETATM 4887 O O   . HOH G 3 .   ? 12.545  -24.247 37.690  1.00 40.05  ? 784  HOH A O   1 
HETATM 4888 O O   . HOH G 3 .   ? -2.178  -36.056 19.248  1.00 23.09  ? 785  HOH A O   1 
HETATM 4889 O O   . HOH G 3 .   ? 5.909   -14.969 8.581   1.00 36.48  ? 786  HOH A O   1 
HETATM 4890 O O   . HOH G 3 .   ? 3.956   -30.756 7.203   1.00 34.81  ? 787  HOH A O   1 
HETATM 4891 O O   . HOH G 3 .   ? 6.472   -28.130 8.841   1.00 36.12  ? 788  HOH A O   1 
HETATM 4892 O O   . HOH G 3 .   ? 16.145  -26.021 45.855  1.00 52.14  ? 789  HOH A O   1 
HETATM 4893 O O   . HOH G 3 .   ? 9.686   -41.342 14.705  1.00 17.74  ? 790  HOH A O   1 
HETATM 4894 O O   . HOH G 3 .   ? 6.336   -12.730 10.315  1.00 34.94  ? 791  HOH A O   1 
HETATM 4895 O O   . HOH G 3 .   ? -2.131  -30.421 8.982   1.00 22.03  ? 792  HOH A O   1 
HETATM 4896 O O   . HOH G 3 .   ? 30.343  -46.306 41.286  1.00 26.75  ? 793  HOH A O   1 
HETATM 4897 O O   . HOH G 3 .   ? -16.288 -10.501 17.087  1.00 40.98  ? 794  HOH A O   1 
HETATM 4898 O O   . HOH G 3 .   ? 6.724   -32.474 26.798  1.00 16.64  ? 795  HOH A O   1 
HETATM 4899 O O   . HOH G 3 .   ? -2.444  -24.473 1.728   1.00 46.27  ? 796  HOH A O   1 
HETATM 4900 O O   . HOH G 3 .   ? 9.363   -11.935 30.520  1.00 39.61  ? 797  HOH A O   1 
HETATM 4901 O O   . HOH G 3 .   ? 15.504  -45.964 39.270  1.00 22.04  ? 798  HOH A O   1 
HETATM 4902 O O   . HOH G 3 .   ? -12.572 -14.881 32.054  1.00 37.98  ? 799  HOH A O   1 
HETATM 4903 O O   . HOH G 3 .   ? -0.183  -37.566 20.190  1.00 18.44  ? 800  HOH A O   1 
HETATM 4904 O O   . HOH G 3 .   ? -3.370  -39.901 43.872  1.00 29.86  ? 801  HOH A O   1 
HETATM 4905 O O   . HOH G 3 .   ? -8.367  -40.995 17.681  1.00 38.05  ? 802  HOH A O   1 
HETATM 4906 O O   . HOH G 3 .   ? 0.924   -9.586  15.820  1.00 22.83  ? 803  HOH A O   1 
HETATM 4907 O O   . HOH G 3 .   ? 8.244   -36.843 45.009  1.00 35.42  ? 804  HOH A O   1 
HETATM 4908 O O   . HOH G 3 .   ? 2.947   -33.808 12.888  1.00 32.04  ? 805  HOH A O   1 
HETATM 4909 O O   . HOH G 3 .   ? 4.476   -13.411 32.300  1.00 36.19  ? 806  HOH A O   1 
HETATM 4910 O O   . HOH G 3 .   ? 9.850   -18.787 21.440  1.00 16.70  ? 807  HOH A O   1 
HETATM 4911 O O   . HOH G 3 .   ? 30.913  -42.037 24.927  1.00 32.43  ? 808  HOH A O   1 
HETATM 4912 O O   . HOH G 3 .   ? 3.559   -30.810 19.131  1.00 14.35  ? 809  HOH A O   1 
HETATM 4913 O O   . HOH G 3 .   ? 15.686  -43.338 38.486  1.00 16.26  ? 810  HOH A O   1 
HETATM 4914 O O   A HOH G 3 .   ? -23.202 -23.969 21.860  0.52 30.45  ? 811  HOH A O   1 
HETATM 4915 O O   B HOH G 3 .   ? -23.157 -25.821 21.513  0.48 31.57  ? 811  HOH A O   1 
HETATM 4916 O O   . HOH G 3 .   ? 9.286   -47.549 38.604  1.00 24.60  ? 812  HOH A O   1 
HETATM 4917 O O   . HOH G 3 .   ? -16.491 -33.354 10.676  1.00 34.65  ? 813  HOH A O   1 
HETATM 4918 O O   . HOH G 3 .   ? 9.169   -34.169 25.898  1.00 17.30  ? 814  HOH A O   1 
HETATM 4919 O O   A HOH G 3 .   ? 2.087   -44.662 32.141  0.55 17.19  ? 815  HOH A O   1 
HETATM 4920 O O   B HOH G 3 .   ? 1.417   -43.594 33.958  0.45 29.52  ? 815  HOH A O   1 
HETATM 4921 O O   . HOH G 3 .   ? 10.338  -25.168 23.605  1.00 19.20  ? 816  HOH A O   1 
HETATM 4922 O O   . HOH G 3 .   ? 0.890   -36.675 28.434  1.00 15.02  ? 817  HOH A O   1 
HETATM 4923 O O   . HOH G 3 .   ? 10.237  -27.299 42.245  1.00 41.97  ? 818  HOH A O   1 
HETATM 4924 O O   . HOH G 3 .   ? 27.211  -42.021 22.216  1.00 29.59  ? 819  HOH A O   1 
HETATM 4925 O O   . HOH G 3 .   ? 0.224   -46.831 28.752  1.00 47.40  ? 820  HOH A O   1 
HETATM 4926 O O   . HOH G 3 .   ? -9.382  -27.547 30.689  1.00 31.14  ? 821  HOH A O   1 
HETATM 4927 O O   . HOH G 3 .   ? 27.665  -29.728 28.655  1.00 24.60  ? 822  HOH A O   1 
HETATM 4928 O O   . HOH G 3 .   ? 17.159  -30.847 34.990  1.00 16.30  ? 823  HOH A O   1 
HETATM 4929 O O   . HOH G 3 .   ? -12.274 -19.466 29.865  1.00 24.61  ? 824  HOH A O   1 
HETATM 4930 O O   . HOH G 3 .   ? 27.223  -40.370 18.399  1.00 33.95  ? 825  HOH A O   1 
HETATM 4931 O O   . HOH G 3 .   ? 11.443  -50.013 29.461  1.00 30.78  ? 826  HOH A O   1 
HETATM 4932 O O   . HOH G 3 .   ? 27.255  -45.458 38.831  1.00 21.66  ? 827  HOH A O   1 
HETATM 4933 O O   . HOH G 3 .   ? -22.392 -22.263 14.981  1.00 33.58  ? 828  HOH A O   1 
HETATM 4934 O O   . HOH G 3 .   ? 24.265  -30.552 21.848  1.00 12.67  ? 829  HOH A O   1 
HETATM 4935 O O   . HOH G 3 .   ? 12.752  -45.271 40.594  1.00 33.22  ? 830  HOH A O   1 
HETATM 4936 O O   . HOH G 3 .   ? -0.886  -41.440 33.976  1.00 31.52  ? 831  HOH A O   1 
HETATM 4937 O O   . HOH G 3 .   ? 16.979  -33.495 43.721  1.00 31.77  ? 832  HOH A O   1 
HETATM 4938 O O   . HOH G 3 .   ? 4.529   -38.975 11.905  1.00 37.08  ? 833  HOH A O   1 
HETATM 4939 O O   . HOH G 3 .   ? 26.416  -42.845 39.019  1.00 24.15  ? 834  HOH A O   1 
HETATM 4940 O O   . HOH G 3 .   ? -18.652 -25.640 30.382  1.00 33.16  ? 835  HOH A O   1 
HETATM 4941 O O   . HOH G 3 .   ? -4.810  -26.105 21.590  1.00 15.09  ? 836  HOH A O   1 
HETATM 4942 O O   . HOH G 3 .   ? -14.700 -22.835 8.333   1.00 34.31  ? 837  HOH A O   1 
HETATM 4943 O O   . HOH G 3 .   ? 8.107   -23.881 27.070  1.00 17.07  ? 838  HOH A O   1 
HETATM 4944 O O   . HOH G 3 .   ? 8.151   -44.274 35.552  1.00 18.91  ? 839  HOH A O   1 
HETATM 4945 O O   . HOH G 3 .   ? 6.911   -32.894 32.766  1.00 12.70  ? 840  HOH A O   1 
HETATM 4946 O O   . HOH G 3 .   ? 20.534  -44.103 23.843  1.00 38.30  ? 841  HOH A O   1 
HETATM 4947 O O   . HOH G 3 .   ? -5.075  -24.688 31.467  1.00 31.63  ? 842  HOH A O   1 
HETATM 4948 O O   . HOH G 3 .   ? -8.560  -34.039 7.128   1.00 39.03  ? 843  HOH A O   1 
HETATM 4949 O O   . HOH G 3 .   ? -2.334  -34.179 41.071  1.00 28.35  ? 844  HOH A O   1 
HETATM 4950 O O   . HOH G 3 .   ? 5.650   -6.112  24.793  1.00 39.72  ? 845  HOH A O   1 
HETATM 4951 O O   . HOH G 3 .   ? 0.219   -30.848 7.684   1.00 33.45  ? 846  HOH A O   1 
HETATM 4952 O O   . HOH G 3 .   ? 17.162  -48.804 23.610  1.00 33.77  ? 847  HOH A O   1 
HETATM 4953 O O   . HOH G 3 .   ? 33.473  -39.393 26.866  1.00 25.20  ? 848  HOH A O   1 
HETATM 4954 O O   . HOH G 3 .   ? 4.158   -25.457 38.080  1.00 27.39  ? 849  HOH A O   1 
HETATM 4955 O O   . HOH G 3 .   ? -18.161 -33.792 23.781  1.00 62.86  ? 850  HOH A O   1 
HETATM 4956 O O   . HOH G 3 .   ? -19.887 -17.829 15.265  1.00 33.81  ? 851  HOH A O   1 
HETATM 4957 O O   . HOH G 3 .   ? 8.595   -20.492 27.275  1.00 15.60  ? 852  HOH A O   1 
HETATM 4958 O O   . HOH G 3 .   ? -1.650  -36.346 29.346  1.00 17.74  ? 853  HOH A O   1 
HETATM 4959 O O   . HOH G 3 .   ? 7.371   -15.246 19.977  1.00 18.97  ? 854  HOH A O   1 
HETATM 4960 O O   . HOH G 3 .   ? 7.268   -43.772 31.219  1.00 15.74  ? 855  HOH A O   1 
HETATM 4961 O O   . HOH G 3 .   ? -15.238 -33.181 20.434  1.00 36.79  ? 856  HOH A O   1 
HETATM 4962 O O   . HOH G 3 .   ? 0.279   -35.758 22.122  1.00 13.91  ? 857  HOH A O   1 
HETATM 4963 O O   . HOH G 3 .   ? 1.945   -15.280 5.582   1.00 42.77  ? 858  HOH A O   1 
HETATM 4964 O O   . HOH G 3 .   ? -10.174 -29.861 33.328  1.00 27.88  ? 859  HOH A O   1 
HETATM 4965 O O   . HOH G 3 .   ? -7.831  -25.493 31.356  1.00 29.49  ? 860  HOH A O   1 
HETATM 4966 O O   . HOH G 3 .   ? 0.725   -28.210 25.496  1.00 13.88  ? 861  HOH A O   1 
HETATM 4967 O O   . HOH G 3 .   ? 3.526   -29.766 36.924  1.00 18.85  ? 862  HOH A O   1 
HETATM 4968 O O   . HOH G 3 .   ? 3.392   -40.356 39.713  1.00 24.75  ? 863  HOH A O   1 
HETATM 4969 O O   . HOH G 3 .   ? -17.790 -14.726 14.196  1.00 46.23  ? 864  HOH A O   1 
HETATM 4970 O O   . HOH G 3 .   ? 24.143  -52.347 34.072  1.00 49.42  ? 865  HOH A O   1 
HETATM 4971 O O   . HOH G 3 .   ? 1.599   -38.092 44.893  1.00 33.92  ? 866  HOH A O   1 
HETATM 4972 O O   . HOH G 3 .   ? 8.311   -26.270 8.793   1.00 26.84  ? 867  HOH A O   1 
HETATM 4973 O O   . HOH G 3 .   ? 12.676  -49.794 39.236  1.00 41.66  ? 868  HOH A O   1 
HETATM 4974 O O   . HOH G 3 .   ? 30.478  -29.903 27.930  1.00 21.75  ? 869  HOH A O   1 
HETATM 4975 O O   . HOH G 3 .   ? -14.750 -23.728 14.484  1.00 22.54  ? 870  HOH A O   1 
HETATM 4976 O O   . HOH G 3 .   ? 20.592  -51.413 29.105  1.00 36.50  ? 871  HOH A O   1 
HETATM 4977 O O   . HOH G 3 .   ? 10.444  -17.801 26.178  1.00 14.83  ? 872  HOH A O   1 
HETATM 4978 O O   . HOH G 3 .   ? -15.958 -31.511 23.815  1.00 44.43  ? 873  HOH A O   1 
HETATM 4979 O O   . HOH G 3 .   ? 0.018   -42.875 14.987  1.00 37.43  ? 874  HOH A O   1 
HETATM 4980 O O   . HOH G 3 .   ? 28.443  -42.631 45.774  1.00 28.79  ? 875  HOH A O   1 
HETATM 4981 O O   . HOH G 3 .   ? -19.582 -28.827 27.850  1.00 46.71  ? 876  HOH A O   1 
HETATM 4982 O O   . HOH G 3 .   ? 33.135  -31.744 41.071  1.00 24.25  ? 877  HOH A O   1 
HETATM 4983 O O   . HOH G 3 .   ? 0.501   -11.821 28.643  1.00 19.57  ? 878  HOH A O   1 
HETATM 4984 O O   . HOH G 3 .   ? -22.174 -17.341 18.181  1.00 45.20  ? 879  HOH A O   1 
HETATM 4985 O O   . HOH G 3 .   ? -2.511  -39.115 31.812  1.00 30.49  ? 880  HOH A O   1 
HETATM 4986 O O   . HOH G 3 .   ? -2.429  -24.267 28.813  1.00 19.17  ? 881  HOH A O   1 
HETATM 4987 O O   . HOH G 3 .   ? 24.461  -25.663 39.575  1.00 35.66  ? 882  HOH A O   1 
HETATM 4988 O O   . HOH G 3 .   ? 33.770  -43.548 36.328  1.00 33.10  ? 883  HOH A O   1 
HETATM 4989 O O   . HOH G 3 .   ? 36.772  -27.232 32.607  1.00 25.84  ? 884  HOH A O   1 
HETATM 4990 O O   . HOH G 3 .   ? -4.388  -44.330 41.005  1.00 47.38  ? 885  HOH A O   1 
HETATM 4991 O O   . HOH G 3 .   ? -18.094 -23.461 19.603  1.00 24.59  ? 886  HOH A O   1 
HETATM 4992 O O   . HOH G 3 .   ? 26.999  -28.679 41.247  1.00 35.49  ? 887  HOH A O   1 
HETATM 4993 O O   . HOH G 3 .   ? -7.065  -36.966 9.758   1.00 43.93  ? 888  HOH A O   1 
HETATM 4994 O O   . HOH G 3 .   ? -0.051  -10.242 31.841  1.00 30.15  ? 889  HOH A O   1 
HETATM 4995 O O   A HOH G 3 .   ? 12.968  -32.719 12.778  0.57 18.47  ? 890  HOH A O   1 
HETATM 4996 O O   B HOH G 3 .   ? 14.073  -33.086 11.340  0.43 16.34  ? 890  HOH A O   1 
HETATM 4997 O O   . HOH G 3 .   ? 8.027   -13.029 21.947  1.00 21.47  ? 891  HOH A O   1 
HETATM 4998 O O   . HOH G 3 .   ? 1.403   -29.651 5.207   1.00 38.17  ? 892  HOH A O   1 
HETATM 4999 O O   . HOH G 3 .   ? 6.681   -41.301 12.131  1.00 27.00  ? 893  HOH A O   1 
HETATM 5000 O O   . HOH G 3 .   ? 11.459  -36.274 13.165  1.00 27.33  ? 894  HOH A O   1 
HETATM 5001 O O   . HOH G 3 .   ? 39.109  -32.360 32.099  1.00 22.37  ? 895  HOH A O   1 
HETATM 5002 O O   . HOH G 3 .   ? -9.501  -28.898 6.466   1.00 36.64  ? 896  HOH A O   1 
HETATM 5003 O O   . HOH G 3 .   ? 4.672   -37.756 45.017  1.00 25.56  ? 897  HOH A O   1 
HETATM 5004 O O   . HOH G 3 .   ? -16.113 -13.464 28.562  1.00 28.14  ? 898  HOH A O   1 
HETATM 5005 O O   . HOH G 3 .   ? 6.078   -43.971 33.721  1.00 18.67  ? 899  HOH A O   1 
HETATM 5006 O O   . HOH G 3 .   ? 1.207   -25.091 37.446  1.00 25.98  ? 900  HOH A O   1 
HETATM 5007 O O   . HOH G 3 .   ? 5.059   -27.057 42.879  1.00 32.66  ? 901  HOH A O   1 
HETATM 5008 O O   . HOH G 3 .   ? 38.227  -36.285 33.448  1.00 44.86  ? 902  HOH A O   1 
HETATM 5009 O O   . HOH G 3 .   ? 27.943  -36.853 44.566  1.00 32.31  ? 903  HOH A O   1 
HETATM 5010 O O   . HOH G 3 .   ? 19.811  -25.172 45.455  1.00 46.39  ? 904  HOH A O   1 
HETATM 5011 O O   . HOH G 3 .   ? 30.614  -48.024 32.693  1.00 28.49  ? 905  HOH A O   1 
HETATM 5012 O O   . HOH G 3 .   ? -2.381  -41.784 18.579  1.00 27.99  ? 906  HOH A O   1 
HETATM 5013 O O   . HOH G 3 .   ? -17.508 -18.542 32.257  1.00 40.95  ? 907  HOH A O   1 
HETATM 5014 O O   . HOH G 3 .   ? 23.635  -35.987 45.576  1.00 25.58  ? 908  HOH A O   1 
HETATM 5015 O O   . HOH G 3 .   ? -15.116 -21.734 11.292  1.00 24.10  ? 909  HOH A O   1 
HETATM 5016 O O   . HOH G 3 .   ? -3.675  -48.584 22.918  1.00 37.23  ? 910  HOH A O   1 
HETATM 5017 O O   . HOH G 3 .   ? 21.591  -51.507 36.583  1.00 43.06  ? 911  HOH A O   1 
HETATM 5018 O O   . HOH G 3 .   ? -4.836  -36.440 40.685  1.00 54.40  ? 912  HOH A O   1 
HETATM 5019 O O   . HOH G 3 .   ? 33.622  -45.857 26.972  1.00 44.01  ? 913  HOH A O   1 
HETATM 5020 O O   . HOH G 3 .   ? 1.195   -45.617 11.862  1.00 35.66  ? 914  HOH A O   1 
HETATM 5021 O O   . HOH G 3 .   ? 35.447  -38.087 33.589  1.00 25.08  ? 915  HOH A O   1 
HETATM 5022 O O   . HOH G 3 .   ? 4.782   -17.812 35.048  1.00 25.19  ? 916  HOH A O   1 
HETATM 5023 O O   . HOH G 3 .   ? 8.062   -24.485 36.771  1.00 30.32  ? 917  HOH A O   1 
HETATM 5024 O O   . HOH G 3 .   ? -4.444  -36.074 38.447  1.00 52.60  ? 918  HOH A O   1 
HETATM 5025 O O   . HOH G 3 .   ? 12.500  -27.365 42.936  1.00 37.75  ? 919  HOH A O   1 
HETATM 5026 O O   . HOH G 3 .   ? -11.162 -32.369 22.507  1.00 27.41  ? 920  HOH A O   1 
HETATM 5027 O O   . HOH G 3 .   ? 11.308  -49.995 32.019  1.00 20.31  ? 921  HOH A O   1 
HETATM 5028 O O   . HOH G 3 .   ? -2.812  -30.691 40.602  1.00 23.22  ? 922  HOH A O   1 
HETATM 5029 O O   . HOH G 3 .   ? -20.248 -18.244 28.875  1.00 32.86  ? 923  HOH A O   1 
HETATM 5030 O O   . HOH G 3 .   ? -8.867  -13.020 36.179  1.00 43.70  ? 924  HOH A O   1 
HETATM 5031 O O   . HOH G 3 .   ? -2.013  -47.171 18.642  1.00 44.25  ? 925  HOH A O   1 
HETATM 5032 O O   . HOH G 3 .   ? 15.368  -22.772 43.867  1.00 58.75  ? 926  HOH A O   1 
HETATM 5033 O O   A HOH G 3 .   ? -9.356  -34.097 21.307  0.57 26.23  ? 927  HOH A O   1 
HETATM 5034 O O   B HOH G 3 .   ? -8.858  -34.086 22.997  0.43 19.47  ? 927  HOH A O   1 
HETATM 5035 O O   . HOH G 3 .   ? -22.650 -25.890 15.885  1.00 43.26  ? 928  HOH A O   1 
HETATM 5036 O O   . HOH G 3 .   ? -13.232 -7.705  22.157  1.00 35.90  ? 929  HOH A O   1 
HETATM 5037 O O   . HOH G 3 .   ? -7.185  -42.726 21.918  1.00 28.52  ? 930  HOH A O   1 
HETATM 5038 O O   . HOH G 3 .   ? 1.279   -49.030 25.558  1.00 51.07  ? 931  HOH A O   1 
HETATM 5039 O O   . HOH G 3 .   ? 23.064  -50.211 31.817  1.00 28.77  ? 932  HOH A O   1 
HETATM 5040 O O   . HOH G 3 .   ? -22.760 -17.562 20.609  1.00 33.14  ? 933  HOH A O   1 
HETATM 5041 O O   . HOH G 3 .   ? -3.326  -11.180 16.196  1.00 19.40  ? 934  HOH A O   1 
HETATM 5042 O O   . HOH G 3 .   ? -0.769  -49.547 16.744  1.00 37.99  ? 935  HOH A O   1 
HETATM 5043 O O   . HOH G 3 .   ? 2.836   -48.187 27.899  1.00 49.17  ? 936  HOH A O   1 
HETATM 5044 O O   . HOH G 3 .   ? 34.521  -41.765 27.621  1.00 23.00  ? 937  HOH A O   1 
HETATM 5045 O O   . HOH G 3 .   ? 4.293   -22.169 3.564   1.00 50.86  ? 938  HOH A O   1 
HETATM 5046 O O   . HOH G 3 .   ? -13.415 -7.640  31.181  1.00 42.36  ? 939  HOH A O   1 
HETATM 5047 O O   . HOH G 3 .   ? 31.634  -46.742 24.491  1.00 43.67  ? 940  HOH A O   1 
HETATM 5048 O O   . HOH G 3 .   ? -7.202  -6.817  24.218  1.00 26.78  ? 941  HOH A O   1 
HETATM 5049 O O   . HOH G 3 .   ? -13.839 -21.860 32.449  1.00 40.28  ? 942  HOH A O   1 
HETATM 5050 O O   . HOH G 3 .   ? -4.754  -7.818  26.446  1.00 37.65  ? 943  HOH A O   1 
HETATM 5051 O O   . HOH G 3 .   ? 14.857  -23.020 37.178  1.00 42.53  ? 944  HOH A O   1 
HETATM 5052 O O   . HOH G 3 .   ? 11.021  -22.532 19.387  1.00 32.37  ? 945  HOH A O   1 
HETATM 5053 O O   . HOH G 3 .   ? 2.322   -12.789 34.212  1.00 42.14  ? 946  HOH A O   1 
HETATM 5054 O O   . HOH G 3 .   ? 34.877  -36.754 36.147  1.00 24.67  ? 947  HOH A O   1 
HETATM 5055 O O   . HOH G 3 .   ? -3.815  -1.992  26.326  1.00 52.50  ? 948  HOH A O   1 
HETATM 5056 O O   . HOH G 3 .   ? 17.696  -43.804 42.662  1.00 43.76  ? 949  HOH A O   1 
HETATM 5057 O O   . HOH G 3 .   ? 3.341   -35.340 10.554  1.00 29.86  ? 950  HOH A O   1 
HETATM 5058 O O   . HOH G 3 .   ? 2.292   -22.056 1.084   1.00 48.54  ? 951  HOH A O   1 
HETATM 5059 O O   . HOH G 3 .   ? -5.225  -15.722 31.128  1.00 24.49  ? 952  HOH A O   1 
HETATM 5060 O O   . HOH G 3 .   ? 5.747   -28.167 38.060  1.00 24.86  ? 953  HOH A O   1 
HETATM 5061 O O   . HOH G 3 .   ? 26.321  -50.161 38.507  1.00 44.24  ? 954  HOH A O   1 
HETATM 5062 O O   . HOH G 3 .   ? -12.597 -34.386 7.661   1.00 51.27  ? 955  HOH A O   1 
HETATM 5063 O O   . HOH G 3 .   ? 4.893   -27.263 40.375  1.00 47.36  ? 956  HOH A O   1 
HETATM 5064 O O   . HOH G 3 .   ? 2.156   -23.447 41.432  1.00 26.31  ? 957  HOH A O   1 
HETATM 5065 O O   . HOH G 3 .   ? 33.676  -43.597 25.640  1.00 44.34  ? 958  HOH A O   1 
HETATM 5066 O O   . HOH G 3 .   ? 27.002  -37.948 23.052  1.00 26.19  ? 959  HOH A O   1 
HETATM 5067 O O   . HOH G 3 .   ? 23.075  -30.270 26.271  1.00 22.73  ? 960  HOH A O   1 
HETATM 5068 O O   . HOH G 3 .   ? -10.089 -21.053 30.106  1.00 19.80  ? 961  HOH A O   1 
HETATM 5069 O O   . HOH G 3 .   ? 10.360  -33.977 12.361  1.00 48.82  ? 962  HOH A O   1 
HETATM 5070 O O   . HOH G 3 .   ? 8.365   -52.627 21.202  1.00 38.60  ? 963  HOH A O   1 
HETATM 5071 O O   . HOH G 3 .   ? 23.891  -48.900 40.219  1.00 44.91  ? 964  HOH A O   1 
HETATM 5072 O O   . HOH G 3 .   ? 5.073   -22.568 36.803  1.00 51.80  ? 965  HOH A O   1 
HETATM 5073 O O   . HOH G 3 .   ? 3.870   -36.681 49.245  1.00 39.99  ? 966  HOH A O   1 
HETATM 5074 O O   . HOH G 3 .   ? 0.497   -13.210 36.859  1.00 41.66  ? 967  HOH A O   1 
HETATM 5075 O O   . HOH G 3 .   ? -4.108  -33.609 38.859  1.00 33.05  ? 968  HOH A O   1 
HETATM 5076 O O   . HOH G 3 .   ? 23.616  -25.812 43.284  1.00 44.21  ? 969  HOH A O   1 
HETATM 5077 O O   . HOH G 3 .   ? 8.042   -32.517 12.192  1.00 35.43  ? 970  HOH A O   1 
HETATM 5078 O O   . HOH G 3 .   ? -12.660 -18.119 2.317   1.00 49.80  ? 971  HOH A O   1 
HETATM 5079 O O   . HOH G 3 .   ? 6.357   -47.712 29.296  1.00 30.44  ? 972  HOH A O   1 
HETATM 5080 O O   . HOH G 3 .   ? 32.601  -50.231 34.923  1.00 40.20  ? 973  HOH A O   1 
HETATM 5081 O O   . HOH G 3 .   ? -2.053  -48.727 25.756  1.00 45.09  ? 974  HOH A O   1 
HETATM 5082 O O   . HOH G 3 .   ? 2.297   -16.207 38.462  1.00 45.67  ? 975  HOH A O   1 
HETATM 5083 O O   . HOH G 3 .   ? -19.255 -31.004 16.395  1.00 46.88  ? 976  HOH A O   1 
HETATM 5084 O O   . HOH G 3 .   ? 8.443   -35.502 47.639  1.00 44.41  ? 977  HOH A O   1 
HETATM 5085 O O   . HOH G 3 .   ? 27.828  -29.538 32.822  1.00 27.26  ? 978  HOH A O   1 
HETATM 5086 O O   . HOH G 3 .   ? 8.608   -49.870 39.006  1.00 49.84  ? 979  HOH A O   1 
HETATM 5087 O O   . HOH G 3 .   ? 4.162   -48.462 42.885  1.00 43.92  ? 980  HOH A O   1 
HETATM 5088 O O   A HOH G 3 .   ? -3.442  -30.326 5.311   0.53 30.96  ? 981  HOH A O   1 
HETATM 5089 O O   B HOH G 3 .   ? -5.246  -29.738 4.990   0.47 25.66  ? 981  HOH A O   1 
HETATM 5090 O O   . HOH G 3 .   ? 1.465   -7.489  17.275  1.00 33.81  ? 982  HOH A O   1 
HETATM 5091 O O   . HOH G 3 .   ? -10.331 -11.615 8.671   1.00 43.21  ? 983  HOH A O   1 
HETATM 5092 O O   . HOH G 3 .   ? -4.541  -40.095 30.367  1.00 41.34  ? 984  HOH A O   1 
HETATM 5093 O O   . HOH G 3 .   ? -16.195 -21.993 33.549  1.00 56.90  ? 985  HOH A O   1 
HETATM 5094 O O   . HOH G 3 .   ? 25.953  -25.859 41.894  1.00 37.93  ? 986  HOH A O   1 
HETATM 5095 O O   . HOH G 3 .   ? -2.252  -38.174 16.112  1.00 35.41  ? 987  HOH A O   1 
HETATM 5096 O O   . HOH G 3 .   ? 23.646  -51.628 29.959  1.00 42.74  ? 988  HOH A O   1 
HETATM 5097 O O   . HOH G 3 .   ? 22.657  -50.551 39.083  1.00 51.17  ? 989  HOH A O   1 
HETATM 5098 O O   . HOH G 3 .   ? -20.159 -25.406 20.100  1.00 35.57  ? 990  HOH A O   1 
HETATM 5099 O O   . HOH G 3 .   ? -18.314 -22.425 31.490  1.00 38.19  ? 991  HOH A O   1 
HETATM 5100 O O   . HOH G 3 .   ? 5.633   -47.206 44.631  1.00 46.64  ? 992  HOH A O   1 
HETATM 5101 O O   . HOH G 3 .   ? -12.178 -27.796 31.700  1.00 36.02  ? 993  HOH A O   1 
HETATM 5102 O O   . HOH G 3 .   ? 7.923   -27.120 37.354  1.00 31.51  ? 994  HOH A O   1 
HETATM 5103 O O   . HOH G 3 .   ? -1.700  -10.170 34.225  1.00 54.71  ? 995  HOH A O   1 
HETATM 5104 O O   . HOH G 3 .   ? 5.725   -51.282 27.983  1.00 48.14  ? 996  HOH A O   1 
HETATM 5105 O O   . HOH G 3 .   ? -1.043  -2.434  30.072  1.00 49.92  ? 997  HOH A O   1 
HETATM 5106 O O   . HOH G 3 .   ? -1.214  -11.211 12.022  1.00 34.22  ? 998  HOH A O   1 
HETATM 5107 O O   . HOH G 3 .   ? -13.660 -33.103 23.027  1.00 40.65  ? 999  HOH A O   1 
HETATM 5108 O O   . HOH G 3 .   ? 1.094   -47.767 43.243  1.00 44.80  ? 1000 HOH A O   1 
HETATM 5109 O O   . HOH G 3 .   ? -5.175  -46.664 24.026  1.00 42.07  ? 1001 HOH A O   1 
HETATM 5110 O O   . HOH G 3 .   ? -24.266 -24.008 13.990  1.00 37.04  ? 1002 HOH A O   1 
HETATM 5111 O O   . HOH G 3 .   ? -16.641 -11.666 26.623  1.00 37.51  ? 1003 HOH A O   1 
HETATM 5112 O O   . HOH G 3 .   ? -8.405  -10.461 12.032  1.00 52.60  ? 1004 HOH A O   1 
HETATM 5113 O O   . HOH G 3 .   ? 17.960  -45.427 20.002  1.00 34.74  ? 1005 HOH A O   1 
HETATM 5114 O O   . HOH G 3 .   ? 18.021  -49.386 40.984  1.00 50.27  ? 1006 HOH A O   1 
HETATM 5115 O O   . HOH G 3 .   ? 29.356  -39.178 20.011  1.00 30.53  ? 1007 HOH A O   1 
HETATM 5116 O O   . HOH G 3 .   ? 13.996  -25.366 47.238  1.00 53.93  ? 1008 HOH A O   1 
HETATM 5117 O O   . HOH G 3 .   ? 6.197   -20.107 3.212   1.00 46.17  ? 1009 HOH A O   1 
HETATM 5118 O O   . HOH G 3 .   ? 26.267  -26.312 30.342  1.00 43.56  ? 1010 HOH A O   1 
HETATM 5119 O O   . HOH G 3 .   ? 3.738   -14.486 7.266   1.00 61.39  ? 1011 HOH A O   1 
HETATM 5120 O O   . HOH G 3 .   ? -22.082 -19.945 14.054  1.00 42.05  ? 1012 HOH A O   1 
HETATM 5121 O O   . HOH G 3 .   ? 20.293  -43.293 44.251  1.00 40.05  ? 1013 HOH A O   1 
HETATM 5122 O O   . HOH G 3 .   ? 28.562  -28.067 30.490  1.00 36.74  ? 1014 HOH A O   1 
HETATM 5123 O O   . HOH G 3 .   ? -3.441  -15.777 -4.630  1.00 52.02  ? 1015 HOH A O   1 
HETATM 5124 O O   . HOH G 3 .   ? 32.652  -52.341 33.922  1.00 50.94  ? 1016 HOH A O   1 
HETATM 5125 O O   . HOH G 3 .   ? 17.637  -47.829 20.743  1.00 39.48  ? 1017 HOH A O   1 
HETATM 5126 O O   . HOH G 3 .   ? 1.251   -22.592 38.376  1.00 40.92  ? 1018 HOH A O   1 
HETATM 5127 O O   . HOH G 3 .   ? 36.986  -40.341 33.463  1.00 40.66  ? 1019 HOH A O   1 
HETATM 5128 O O   . HOH G 3 .   ? 23.073  -42.482 18.333  1.00 36.15  ? 1020 HOH A O   1 
HETATM 5129 O O   . HOH G 3 .   ? 3.922   -15.050 35.940  1.00 49.58  ? 1021 HOH A O   1 
HETATM 5130 O O   . HOH G 3 .   ? 8.765   -55.449 22.284  1.00 59.02  ? 1022 HOH A O   1 
HETATM 5131 O O   . HOH G 3 .   ? 2.473   -48.663 40.008  1.00 50.53  ? 1023 HOH A O   1 
HETATM 5132 O O   . HOH G 3 .   ? 1.887   -3.135  28.896  1.00 50.75  ? 1024 HOH A O   1 
HETATM 5133 O O   . HOH G 3 .   ? 4.237   -45.959 33.288  1.00 24.90  ? 1025 HOH A O   1 
HETATM 5134 O O   . HOH G 3 .   ? 22.743  -21.333 35.180  1.00 48.12  ? 1026 HOH A O   1 
HETATM 5135 O O   . HOH G 3 .   ? -23.365 -30.609 20.862  1.00 51.32  ? 1027 HOH A O   1 
HETATM 5136 O O   . HOH G 3 .   ? -18.222 -27.499 5.275   1.00 61.85  ? 1028 HOH A O   1 
HETATM 5137 O O   . HOH G 3 .   ? 13.028  -55.186 23.312  1.00 44.85  ? 1029 HOH A O   1 
HETATM 5138 O O   . HOH G 3 .   ? 31.074  -50.907 31.515  1.00 43.56  ? 1030 HOH A O   1 
HETATM 5139 O O   . HOH G 3 .   ? 7.430   -46.035 37.713  1.00 25.04  ? 1031 HOH A O   1 
HETATM 5140 O O   . HOH G 3 .   ? 21.451  -47.940 24.082  1.00 41.39  ? 1032 HOH A O   1 
HETATM 5141 O O   . HOH G 3 .   ? -12.295 -28.323 7.244   1.00 38.24  ? 1033 HOH A O   1 
HETATM 5142 O O   . HOH G 3 .   ? 18.372  -33.345 45.870  1.00 44.16  ? 1034 HOH A O   1 
HETATM 5143 O O   . HOH G 3 .   ? -5.253  -41.710 23.521  1.00 36.55  ? 1035 HOH A O   1 
HETATM 5144 O O   . HOH G 3 .   ? -9.515  -20.078 32.780  1.00 23.47  ? 1036 HOH A O   1 
HETATM 5145 O O   . HOH G 3 .   ? 8.242   -50.408 32.717  1.00 44.91  ? 1037 HOH A O   1 
HETATM 5146 O O   . HOH G 3 .   ? 15.615  -42.315 42.518  1.00 46.29  ? 1038 HOH A O   1 
HETATM 5147 O O   . HOH G 3 .   ? 24.490  -22.672 36.803  1.00 53.47  ? 1039 HOH A O   1 
HETATM 5148 O O   . HOH G 3 .   ? -24.260 -19.462 15.016  1.00 42.17  ? 1040 HOH A O   1 
HETATM 5149 O O   . HOH G 3 .   ? -10.461 -7.649  33.047  1.00 43.95  ? 1041 HOH A O   1 
HETATM 5150 O O   . HOH G 3 .   ? -3.836  -39.881 46.264  1.00 36.81  ? 1042 HOH A O   1 
HETATM 5151 O O   . HOH G 3 .   ? 32.487  -47.563 29.169  1.00 42.44  ? 1043 HOH A O   1 
HETATM 5152 O O   . HOH G 3 .   ? 33.060  -47.955 33.591  1.00 40.88  ? 1044 HOH A O   1 
HETATM 5153 O O   . HOH G 3 .   ? -4.528  -43.806 26.056  1.00 40.88  ? 1045 HOH A O   1 
HETATM 5154 O O   . HOH G 3 .   ? -16.952 -7.941  17.415  1.00 49.79  ? 1046 HOH A O   1 
HETATM 5155 O O   . HOH G 3 .   ? 11.838  -25.634 45.964  1.00 51.33  ? 1047 HOH A O   1 
HETATM 5156 O O   . HOH G 3 .   ? 28.902  -39.964 22.526  1.00 29.60  ? 1048 HOH A O   1 
HETATM 5157 O O   . HOH G 3 .   ? -21.730 -28.054 14.403  1.00 44.67  ? 1049 HOH A O   1 
HETATM 5158 O O   . HOH G 3 .   ? -19.861 -20.106 30.927  1.00 40.21  ? 1050 HOH A O   1 
HETATM 5159 O O   . HOH G 3 .   ? 6.450   -47.810 35.952  1.00 49.35  ? 1051 HOH A O   1 
HETATM 5160 O O   . HOH G 3 .   ? -14.199 -29.902 7.590   1.00 44.17  ? 1052 HOH A O   1 
HETATM 5161 O O   . HOH G 3 .   ? 21.928  -35.342 47.403  1.00 39.60  ? 1053 HOH A O   1 
HETATM 5162 O O   . HOH G 3 .   ? -4.011  -37.816 18.173  1.00 30.03  ? 1054 HOH A O   1 
HETATM 5163 O O   . HOH G 3 .   ? -16.462 -7.384  20.643  1.00 54.53  ? 1055 HOH A O   1 
HETATM 5164 O O   . HOH G 3 .   ? 4.167   -28.068 6.454   1.00 43.03  ? 1056 HOH A O   1 
HETATM 5165 O O   . HOH G 3 .   ? -8.673  -5.414  22.797  1.00 51.29  ? 1057 HOH A O   1 
HETATM 5166 O O   . HOH G 3 .   ? -11.915 -18.722 32.688  1.00 33.56  ? 1058 HOH A O   1 
HETATM 5167 O O   . HOH G 3 .   ? -3.742  -8.592  16.136  1.00 37.95  ? 1059 HOH A O   1 
HETATM 5168 O O   . HOH G 3 .   ? 12.339  -31.099 11.062  1.00 28.01  ? 1060 HOH A O   1 
HETATM 5169 O O   . HOH G 3 .   ? -8.352  -24.704 33.975  1.00 25.11  ? 1061 HOH A O   1 
HETATM 5170 O O   . HOH G 3 .   ? 11.880  -20.052 20.075  1.00 22.76  ? 1062 HOH A O   1 
HETATM 5171 O O   . HOH G 3 .   ? 10.034  -51.834 28.463  1.00 44.75  ? 1063 HOH A O   1 
HETATM 5172 O O   . HOH G 3 .   ? 7.700   -50.261 29.648  1.00 30.78  ? 1064 HOH A O   1 
HETATM 5173 O O   . HOH G 3 .   ? 8.477   -25.936 40.443  1.00 49.07  ? 1065 HOH A O   1 
HETATM 5174 O O   . HOH G 3 .   ? -2.835  -44.559 17.766  1.00 35.10  ? 1066 HOH A O   1 
HETATM 5175 O O   . HOH G 3 .   ? -0.634  -8.657  13.969  1.00 44.67  ? 1067 HOH A O   1 
HETATM 5176 O O   . HOH G 3 .   ? 8.038   -30.263 8.719   1.00 42.38  ? 1068 HOH A O   1 
HETATM 5177 O O   . HOH G 3 .   ? 20.683  -26.775 29.055  1.00 28.62  ? 1069 HOH A O   1 
HETATM 5178 O O   . HOH G 3 .   ? 22.614  -25.940 45.633  1.00 35.83  ? 1070 HOH A O   1 
HETATM 5179 O O   . HOH G 3 .   ? 27.413  -42.994 19.644  1.00 38.63  ? 1071 HOH A O   1 
HETATM 5180 O O   . HOH G 3 .   ? 9.852   -31.382 10.416  1.00 45.48  ? 1072 HOH A O   1 
HETATM 5181 O O   . HOH G 3 .   ? -5.524  -9.370  8.569   1.00 55.37  ? 1073 HOH A O   1 
HETATM 5182 O O   . HOH G 3 .   ? 18.812  -51.522 33.816  1.00 48.68  ? 1074 HOH A O   1 
HETATM 5183 O O   . HOH G 3 .   ? 31.028  -26.747 29.899  1.00 36.67  ? 1075 HOH A O   1 
HETATM 5184 O O   . HOH G 3 .   ? 21.899  -51.443 34.049  1.00 37.89  ? 1076 HOH A O   1 
HETATM 5185 O O   . HOH G 3 .   ? -6.329  -35.900 44.531  1.00 52.87  ? 1077 HOH A O   1 
HETATM 5186 O O   . HOH G 3 .   ? -22.456 -15.406 22.654  1.00 46.80  ? 1078 HOH A O   1 
HETATM 5187 O O   . HOH G 3 .   ? 15.321  -51.968 36.442  1.00 45.77  ? 1079 HOH A O   1 
HETATM 5188 O O   . HOH G 3 .   ? -18.888 -11.052 19.803  1.00 39.93  ? 1080 HOH A O   1 
HETATM 5189 O O   . HOH G 3 .   ? -13.396 -5.007  18.482  1.00 57.39  ? 1081 HOH A O   1 
HETATM 5190 O O   . HOH G 3 .   ? 32.766  -47.544 41.196  1.00 42.56  ? 1082 HOH A O   1 
HETATM 5191 O O   . HOH G 3 .   ? 0.836   -46.688 31.102  1.00 43.69  ? 1083 HOH A O   1 
HETATM 5192 O O   . HOH G 3 .   ? -21.726 -28.738 12.205  1.00 45.03  ? 1084 HOH A O   1 
HETATM 5193 O O   . HOH G 3 .   ? 27.585  -23.655 41.880  1.00 50.27  ? 1085 HOH A O   1 
HETATM 5194 O O   . HOH G 3 .   ? -11.013 -6.351  21.531  1.00 46.92  ? 1086 HOH A O   1 
HETATM 5195 O O   . HOH G 3 .   ? -22.454 -16.608 27.889  1.00 41.75  ? 1087 HOH A O   1 
HETATM 5196 O O   . HOH G 3 .   ? -9.259  -25.842 6.213   1.00 41.05  ? 1088 HOH A O   1 
HETATM 5197 O O   . HOH G 3 .   ? -4.262  -40.253 19.609  1.00 26.91  ? 1089 HOH A O   1 
HETATM 5198 O O   . HOH G 3 .   ? -24.720 -22.868 25.362  1.00 43.76  ? 1090 HOH A O   1 
HETATM 5199 O O   . HOH G 3 .   ? -17.210 -27.070 32.148  1.00 36.18  ? 1091 HOH A O   1 
HETATM 5200 O O   . HOH G 3 .   ? 22.266  -51.427 26.352  1.00 54.64  ? 1092 HOH A O   1 
HETATM 5201 O O   . HOH G 3 .   ? -12.437 -34.086 26.213  1.00 37.06  ? 1093 HOH A O   1 
HETATM 5202 O O   . HOH G 3 .   ? -6.356  -41.899 19.552  1.00 28.35  ? 1094 HOH A O   1 
HETATM 5203 O O   . HOH G 3 .   ? 22.601  -24.963 29.973  1.00 50.53  ? 1095 HOH A O   1 
HETATM 5204 O O   . HOH G 3 .   ? 9.624   -44.948 45.981  1.00 35.36  ? 1096 HOH A O   1 
HETATM 5205 O O   . HOH G 3 .   ? -7.268  -43.307 16.228  1.00 48.06  ? 1097 HOH A O   1 
HETATM 5206 O O   . HOH G 3 .   ? -5.620  -24.057 34.253  1.00 31.29  ? 1098 HOH A O   1 
HETATM 5207 O O   . HOH G 3 .   ? -16.947 -32.713 27.962  1.00 46.43  ? 1099 HOH A O   1 
HETATM 5208 O O   . HOH G 3 .   ? -13.253 -35.161 28.325  1.00 36.59  ? 1100 HOH A O   1 
HETATM 5209 O O   . HOH G 3 .   ? 13.854  -45.186 43.406  1.00 36.96  ? 1101 HOH A O   1 
HETATM 5210 O O   . HOH G 3 .   ? 6.747   -23.060 38.897  1.00 56.35  ? 1102 HOH A O   1 
HETATM 5211 O O   . HOH G 3 .   ? -20.469 -16.658 32.713  1.00 42.99  ? 1103 HOH A O   1 
HETATM 5212 O O   . HOH G 3 .   ? -12.629 -35.613 30.520  1.00 39.24  ? 1104 HOH A O   1 
HETATM 5213 O O   . HOH G 3 .   ? -21.048 -15.264 15.366  1.00 42.32  ? 1105 HOH A O   1 
HETATM 5214 O O   . HOH G 3 .   ? 16.472  -52.742 16.296  1.00 54.03  ? 1106 HOH A O   1 
HETATM 5215 O O   . HOH G 3 .   ? 12.841  -52.102 32.917  1.00 43.06  ? 1107 HOH A O   1 
HETATM 5216 O O   . HOH G 3 .   ? 18.937  -25.103 47.804  1.00 45.01  ? 1108 HOH A O   1 
HETATM 5217 O O   . HOH G 3 .   ? -8.467  -26.453 3.088   1.00 41.70  ? 1109 HOH A O   1 
HETATM 5218 O O   . HOH G 3 .   ? 39.359  -45.765 28.916  1.00 48.91  ? 1110 HOH A O   1 
HETATM 5219 O O   . HOH G 3 .   ? -24.574 -25.015 24.119  1.00 40.46  ? 1111 HOH A O   1 
HETATM 5220 O O   . HOH G 3 .   ? -7.283  -45.504 21.847  1.00 33.32  ? 1112 HOH A O   1 
HETATM 5221 O O   . HOH G 3 .   ? 34.400  -48.054 30.964  1.00 48.83  ? 1113 HOH A O   1 
HETATM 5222 O O   . HOH G 3 .   ? -9.117  -4.747  32.798  1.00 49.74  ? 1114 HOH A O   1 
HETATM 5223 O O   . HOH G 3 .   ? 5.646   -34.690 8.963   1.00 36.94  ? 1115 HOH A O   1 
HETATM 5224 O O   . HOH G 3 .   ? -21.477 -13.366 22.746  1.00 45.60  ? 1116 HOH A O   1 
HETATM 5225 O O   . HOH G 3 .   ? -12.465 -25.826 32.995  1.00 47.00  ? 1117 HOH A O   1 
HETATM 5226 O O   . HOH G 3 .   ? 2.642   -49.895 33.814  1.00 49.04  ? 1118 HOH A O   1 
HETATM 5227 O O   . HOH G 3 .   ? -5.171  -42.968 30.031  1.00 34.85  ? 1119 HOH A O   1 
HETATM 5228 O O   . HOH G 3 .   ? 28.019  -47.203 43.472  1.00 47.39  ? 1120 HOH A O   1 
HETATM 5229 O O   . HOH G 3 .   ? -6.344  -0.527  21.432  1.00 55.69  ? 1121 HOH A O   1 
HETATM 5230 O O   . HOH G 3 .   ? 10.807  -43.296 47.368  1.00 39.31  ? 1122 HOH A O   1 
HETATM 5231 O O   . HOH G 3 .   ? 15.366  -17.877 44.054  1.00 54.41  ? 1123 HOH A O   1 
HETATM 5232 O O   . HOH G 3 .   ? -5.532  -44.196 18.186  1.00 27.83  ? 1124 HOH A O   1 
HETATM 5233 O O   . HOH G 3 .   ? -6.920  -2.306  19.422  1.00 47.08  ? 1125 HOH A O   1 
HETATM 5234 O O   . HOH G 3 .   ? 15.105  -47.999 43.163  1.00 58.77  ? 1126 HOH A O   1 
HETATM 5235 O O   . HOH G 3 .   ? 6.504   -14.997 1.026   1.00 47.99  ? 1127 HOH A O   1 
HETATM 5236 O O   . HOH G 3 .   ? 12.299  -45.506 45.361  1.00 46.19  ? 1128 HOH A O   1 
HETATM 5237 O O   . HOH G 3 .   ? -0.040  -51.717 41.499  1.00 50.74  ? 1129 HOH A O   1 
HETATM 5238 O O   . HOH G 3 .   ? 23.459  -23.293 47.264  1.00 44.00  ? 1130 HOH A O   1 
HETATM 5239 O O   . HOH H 3 .   ? 20.039  -44.121 21.184  1.00 30.86  ? 701  HOH B O   1 
HETATM 5240 O O   . HOH H 3 .   ? 37.048  -16.071 23.649  1.00 28.30  ? 702  HOH B O   1 
HETATM 5241 O O   . HOH H 3 .   ? 23.024  -6.127  40.646  1.00 40.09  ? 703  HOH B O   1 
HETATM 5242 O O   . HOH H 3 .   ? 13.165  -5.182  1.845   1.00 28.65  ? 704  HOH B O   1 
HETATM 5243 O O   . HOH H 3 .   ? 42.323  -2.996  24.076  1.00 56.06  ? 705  HOH B O   1 
HETATM 5244 O O   . HOH H 3 .   ? 30.222  -23.928 -5.193  1.00 42.73  ? 706  HOH B O   1 
HETATM 5245 O O   . HOH H 3 .   ? 38.223  -28.850 1.845   1.00 57.02  ? 707  HOH B O   1 
HETATM 5246 O O   . HOH H 3 .   ? 34.962  -39.543 23.550  1.00 46.44  ? 708  HOH B O   1 
HETATM 5247 O O   . HOH H 3 .   ? 10.335  -7.746  33.649  1.00 52.79  ? 709  HOH B O   1 
HETATM 5248 O O   . HOH H 3 .   ? 20.590  -29.886 17.868  1.00 26.67  ? 710  HOH B O   1 
HETATM 5249 O O   . HOH H 3 .   ? 19.389  -22.652 1.529   1.00 22.09  ? 711  HOH B O   1 
HETATM 5250 O O   . HOH H 3 .   ? 13.558  -26.872 -5.618  1.00 48.73  ? 712  HOH B O   1 
HETATM 5251 O O   . HOH H 3 .   ? 8.794   0.975   13.514  1.00 48.49  ? 713  HOH B O   1 
HETATM 5252 O O   . HOH H 3 .   ? 20.401  9.921   17.933  1.00 50.00  ? 714  HOH B O   1 
HETATM 5253 O O   . HOH H 3 .   ? 12.279  -13.488 34.819  1.00 34.69  ? 715  HOH B O   1 
HETATM 5254 O O   . HOH H 3 .   ? 44.536  -13.406 19.234  1.00 50.97  ? 716  HOH B O   1 
HETATM 5255 O O   . HOH H 3 .   ? 21.880  -17.357 34.961  1.00 35.14  ? 717  HOH B O   1 
HETATM 5256 O O   . HOH H 3 .   ? 40.354  -36.344 19.304  1.00 35.63  ? 718  HOH B O   1 
HETATM 5257 O O   . HOH H 3 .   ? 41.086  -27.822 14.059  1.00 34.72  ? 719  HOH B O   1 
HETATM 5258 O O   . HOH H 3 .   ? 17.216  -24.270 -3.547  1.00 31.52  ? 720  HOH B O   1 
HETATM 5259 O O   . HOH H 3 .   ? 10.630  0.501   23.150  1.00 36.86  ? 721  HOH B O   1 
HETATM 5260 O O   . HOH H 3 .   ? 35.168  -16.522 6.669   1.00 31.91  ? 722  HOH B O   1 
HETATM 5261 O O   . HOH H 3 .   ? 25.521  -19.793 32.806  1.00 30.42  ? 723  HOH B O   1 
HETATM 5262 O O   . HOH H 3 .   ? 19.461  -31.514 -3.844  1.00 26.07  ? 724  HOH B O   1 
HETATM 5263 O O   . HOH H 3 .   ? 31.694  -16.709 -1.544  1.00 41.35  ? 725  HOH B O   1 
HETATM 5264 O O   . HOH H 3 .   ? 17.124  -29.694 19.898  1.00 31.12  ? 726  HOH B O   1 
HETATM 5265 O O   . HOH H 3 .   ? 38.581  -19.141 15.197  1.00 35.28  ? 727  HOH B O   1 
HETATM 5266 O O   A HOH H 3 .   ? 27.004  -27.260 -5.977  0.49 18.57  ? 728  HOH B O   1 
HETATM 5267 O O   B HOH H 3 .   ? 26.765  -28.059 -7.338  0.51 25.41  ? 728  HOH B O   1 
HETATM 5268 O O   . HOH H 3 .   ? 8.621   -11.248 8.721   1.00 28.62  ? 729  HOH B O   1 
HETATM 5269 O O   . HOH H 3 .   ? 21.858  -20.610 31.077  1.00 30.28  ? 730  HOH B O   1 
HETATM 5270 O O   . HOH H 3 .   ? 17.063  -21.463 16.407  1.00 20.53  ? 731  HOH B O   1 
HETATM 5271 O O   . HOH H 3 .   ? 17.683  -22.081 18.924  1.00 25.74  ? 732  HOH B O   1 
HETATM 5272 O O   . HOH H 3 .   ? 25.042  -24.520 -3.914  1.00 31.90  ? 733  HOH B O   1 
HETATM 5273 O O   . HOH H 3 .   ? 37.079  -5.641  30.797  1.00 40.68  ? 734  HOH B O   1 
HETATM 5274 O O   . HOH H 3 .   ? 18.690  -51.288 3.518   1.00 32.66  ? 735  HOH B O   1 
HETATM 5275 O O   . HOH H 3 .   ? 36.805  -16.473 11.684  1.00 28.09  ? 736  HOH B O   1 
HETATM 5276 O O   A HOH H 3 .   ? 17.514  -9.262  27.112  0.40 10.49  ? 737  HOH B O   1 
HETATM 5277 O O   B HOH H 3 .   ? 16.221  -8.942  25.766  0.60 25.11  ? 737  HOH B O   1 
HETATM 5278 O O   . HOH H 3 .   ? 37.976  -5.279  19.878  1.00 31.97  ? 738  HOH B O   1 
HETATM 5279 O O   . HOH H 3 .   ? 35.577  5.450   22.473  1.00 35.33  ? 739  HOH B O   1 
HETATM 5280 O O   . HOH H 3 .   ? 33.719  -39.971 1.395   1.00 36.61  ? 740  HOH B O   1 
HETATM 5281 O O   . HOH H 3 .   ? 22.037  -36.103 -4.549  1.00 40.24  ? 741  HOH B O   1 
HETATM 5282 O O   . HOH H 3 .   ? 25.183  8.311   10.405  1.00 43.90  ? 742  HOH B O   1 
HETATM 5283 O O   . HOH H 3 .   ? 13.824  -5.041  26.599  1.00 18.67  ? 743  HOH B O   1 
HETATM 5284 O O   . HOH H 3 .   ? 22.025  -53.189 1.747   1.00 42.60  ? 744  HOH B O   1 
HETATM 5285 O O   . HOH H 3 .   ? 44.988  -30.814 28.711  1.00 45.59  ? 745  HOH B O   1 
HETATM 5286 O O   . HOH H 3 .   ? 24.518  -47.999 17.130  1.00 41.81  ? 746  HOH B O   1 
HETATM 5287 O O   . HOH H 3 .   ? 32.708  -44.553 10.337  1.00 34.95  ? 747  HOH B O   1 
HETATM 5288 O O   . HOH H 3 .   ? 9.797   -41.854 4.748   1.00 23.33  ? 748  HOH B O   1 
HETATM 5289 O O   . HOH H 3 .   ? 27.684  -11.119 1.465   1.00 20.66  ? 749  HOH B O   1 
HETATM 5290 O O   . HOH H 3 .   ? 33.201  -24.243 0.190   1.00 26.12  ? 750  HOH B O   1 
HETATM 5291 O O   . HOH H 3 .   ? 40.931  -2.225  30.762  1.00 61.58  ? 751  HOH B O   1 
HETATM 5292 O O   . HOH H 3 .   ? 26.704  -13.036 -1.975  1.00 20.94  ? 752  HOH B O   1 
HETATM 5293 O O   . HOH H 3 .   ? 13.012  -18.554 25.468  1.00 13.64  ? 753  HOH B O   1 
HETATM 5294 O O   . HOH H 3 .   ? 3.448   -10.286 14.773  1.00 19.86  ? 754  HOH B O   1 
HETATM 5295 O O   . HOH H 3 .   ? 23.560  -43.281 -4.389  1.00 47.77  ? 755  HOH B O   1 
HETATM 5296 O O   . HOH H 3 .   ? 23.159  -49.836 9.160   1.00 22.88  ? 756  HOH B O   1 
HETATM 5297 O O   . HOH H 3 .   ? 30.460  -30.415 25.057  1.00 19.56  ? 757  HOH B O   1 
HETATM 5298 O O   . HOH H 3 .   ? 29.780  -5.127  10.174  1.00 24.09  ? 758  HOH B O   1 
HETATM 5299 O O   . HOH H 3 .   ? 32.374  -27.929 27.630  1.00 20.67  ? 759  HOH B O   1 
HETATM 5300 O O   . HOH H 3 .   ? 30.165  -39.171 6.601   1.00 16.55  ? 760  HOH B O   1 
HETATM 5301 O O   . HOH H 3 .   ? 37.064  -18.101 17.721  1.00 26.34  ? 761  HOH B O   1 
HETATM 5302 O O   . HOH H 3 .   ? 12.050  -17.540 18.886  1.00 17.13  ? 762  HOH B O   1 
HETATM 5303 O O   . HOH H 3 .   ? 37.216  -31.866 5.959   1.00 23.80  ? 763  HOH B O   1 
HETATM 5304 O O   . HOH H 3 .   ? 24.495  -18.161 2.878   1.00 17.10  ? 764  HOH B O   1 
HETATM 5305 O O   . HOH H 3 .   ? 37.448  -23.516 24.938  1.00 35.05  ? 765  HOH B O   1 
HETATM 5306 O O   . HOH H 3 .   ? 36.423  -0.792  30.275  1.00 36.70  ? 766  HOH B O   1 
HETATM 5307 O O   . HOH H 3 .   ? 10.313  -37.328 -1.398  1.00 31.73  ? 767  HOH B O   1 
HETATM 5308 O O   . HOH H 3 .   ? 26.764  -48.077 12.900  1.00 43.91  ? 768  HOH B O   1 
HETATM 5309 O O   . HOH H 3 .   ? 33.068  -17.370 20.650  1.00 21.13  ? 769  HOH B O   1 
HETATM 5310 O O   . HOH H 3 .   ? 19.050  -22.315 -2.964  1.00 45.31  ? 770  HOH B O   1 
HETATM 5311 O O   . HOH H 3 .   ? 39.741  -2.898  16.238  1.00 45.73  ? 771  HOH B O   1 
HETATM 5312 O O   . HOH H 3 .   ? 38.889  -4.526  29.552  1.00 42.97  ? 772  HOH B O   1 
HETATM 5313 O O   . HOH H 3 .   ? 20.730  3.959   9.433   1.00 41.85  ? 773  HOH B O   1 
HETATM 5314 O O   . HOH H 3 .   ? 22.599  4.432   27.965  1.00 40.33  ? 774  HOH B O   1 
HETATM 5315 O O   . HOH H 3 .   ? 38.152  -9.540  18.911  1.00 26.34  ? 775  HOH B O   1 
HETATM 5316 O O   . HOH H 3 .   ? 25.528  -19.160 20.816  1.00 11.72  ? 776  HOH B O   1 
HETATM 5317 O O   . HOH H 3 .   ? 14.650  -32.825 19.166  1.00 32.86  ? 777  HOH B O   1 
HETATM 5318 O O   . HOH H 3 .   ? 27.818  -34.116 -0.797  1.00 19.10  ? 778  HOH B O   1 
HETATM 5319 O O   . HOH H 3 .   ? 31.898  -8.219  34.215  1.00 29.83  ? 779  HOH B O   1 
HETATM 5320 O O   . HOH H 3 .   ? 11.592  -11.621 6.611   1.00 30.34  ? 780  HOH B O   1 
HETATM 5321 O O   . HOH H 3 .   ? 13.748  6.233   22.584  1.00 49.47  ? 781  HOH B O   1 
HETATM 5322 O O   . HOH H 3 .   ? 39.072  -2.633  22.709  1.00 41.17  ? 782  HOH B O   1 
HETATM 5323 O O   . HOH H 3 .   ? 28.554  -14.826 31.230  1.00 19.50  ? 783  HOH B O   1 
HETATM 5324 O O   . HOH H 3 .   ? 41.733  -30.447 21.773  1.00 41.43  ? 784  HOH B O   1 
HETATM 5325 O O   . HOH H 3 .   ? 14.226  -9.740  34.698  1.00 38.21  ? 785  HOH B O   1 
HETATM 5326 O O   . HOH H 3 .   ? 17.959  -17.240 5.503   1.00 23.21  ? 786  HOH B O   1 
HETATM 5327 O O   . HOH H 3 .   ? 9.660   -5.268  25.159  1.00 24.42  ? 787  HOH B O   1 
HETATM 5328 O O   . HOH H 3 .   ? 16.863  -8.717  35.120  1.00 29.66  ? 788  HOH B O   1 
HETATM 5329 O O   . HOH H 3 .   ? 33.332  -41.276 4.183   1.00 31.04  ? 789  HOH B O   1 
HETATM 5330 O O   . HOH H 3 .   ? 22.007  -44.688 0.781   1.00 22.76  ? 790  HOH B O   1 
HETATM 5331 O O   . HOH H 3 .   ? 35.451  -33.058 0.819   1.00 24.46  ? 791  HOH B O   1 
HETATM 5332 O O   . HOH H 3 .   ? 24.908  -25.675 14.108  1.00 14.63  ? 792  HOH B O   1 
HETATM 5333 O O   . HOH H 3 .   ? 28.619  -35.931 1.314   1.00 16.30  ? 793  HOH B O   1 
HETATM 5334 O O   . HOH H 3 .   ? 37.550  2.498   23.308  1.00 41.18  ? 794  HOH B O   1 
HETATM 5335 O O   . HOH H 3 .   ? 26.161  -23.528 -9.742  1.00 39.83  ? 795  HOH B O   1 
HETATM 5336 O O   . HOH H 3 .   ? 40.403  -25.066 10.844  1.00 24.56  ? 796  HOH B O   1 
HETATM 5337 O O   A HOH H 3 .   ? 23.264  -10.321 11.286  0.72 15.53  ? 797  HOH B O   1 
HETATM 5338 O O   B HOH H 3 .   ? 22.523  -10.983 12.827  0.28 16.36  ? 797  HOH B O   1 
HETATM 5339 O O   . HOH H 3 .   ? 36.659  -36.521 10.289  1.00 28.05  ? 798  HOH B O   1 
HETATM 5340 O O   . HOH H 3 .   ? 33.333  -37.889 17.210  1.00 28.58  ? 799  HOH B O   1 
HETATM 5341 O O   . HOH H 3 .   ? 19.758  -19.171 13.026  1.00 12.64  ? 800  HOH B O   1 
HETATM 5342 O O   . HOH H 3 .   ? 14.315  -17.178 34.724  1.00 31.16  ? 801  HOH B O   1 
HETATM 5343 O O   . HOH H 3 .   ? 37.542  -28.656 15.599  1.00 19.51  ? 802  HOH B O   1 
HETATM 5344 O O   . HOH H 3 .   ? 17.841  -28.021 6.723   1.00 13.82  ? 803  HOH B O   1 
HETATM 5345 O O   . HOH H 3 .   ? 11.643  -11.906 31.833  1.00 39.79  ? 804  HOH B O   1 
HETATM 5346 O O   . HOH H 3 .   ? 33.103  -19.915 19.704  1.00 20.29  ? 805  HOH B O   1 
HETATM 5347 O O   . HOH H 3 .   ? 35.920  -13.307 8.381   1.00 28.64  ? 806  HOH B O   1 
HETATM 5348 O O   . HOH H 3 .   ? 35.927  -2.874  23.146  1.00 26.97  ? 807  HOH B O   1 
HETATM 5349 O O   . HOH H 3 .   ? 20.568  -16.580 1.921   1.00 45.33  ? 808  HOH B O   1 
HETATM 5350 O O   . HOH H 3 .   ? 36.731  -3.221  16.335  1.00 23.35  ? 809  HOH B O   1 
HETATM 5351 O O   . HOH H 3 .   ? 40.657  -23.166 14.176  1.00 18.40  ? 810  HOH B O   1 
HETATM 5352 O O   A HOH H 3 .   ? 15.371  -27.176 18.989  0.54 22.07  ? 811  HOH B O   1 
HETATM 5353 O O   B HOH H 3 .   ? 15.726  -26.933 21.019  0.46 21.91  ? 811  HOH B O   1 
HETATM 5354 O O   . HOH H 3 .   ? 33.707  -30.364 4.170   1.00 18.32  ? 812  HOH B O   1 
HETATM 5355 O O   . HOH H 3 .   ? 26.278  -9.651  18.697  1.00 11.71  ? 813  HOH B O   1 
HETATM 5356 O O   . HOH H 3 .   ? 17.417  -30.158 4.933   1.00 15.08  ? 814  HOH B O   1 
HETATM 5357 O O   . HOH H 3 .   ? 9.474   -7.600  9.915   1.00 40.60  ? 815  HOH B O   1 
HETATM 5358 O O   . HOH H 3 .   ? 34.066  -10.801 20.875  1.00 16.67  ? 816  HOH B O   1 
HETATM 5359 O O   . HOH H 3 .   ? 31.704  -34.699 -0.850  1.00 28.81  ? 817  HOH B O   1 
HETATM 5360 O O   . HOH H 3 .   ? 10.817  -17.351 14.272  1.00 16.77  ? 818  HOH B O   1 
HETATM 5361 O O   . HOH H 3 .   ? 35.309  -20.219 18.144  1.00 21.13  ? 819  HOH B O   1 
HETATM 5362 O O   . HOH H 3 .   ? 24.738  -15.225 14.597  1.00 13.42  ? 820  HOH B O   1 
HETATM 5363 O O   . HOH H 3 .   ? 31.366  -19.293 17.772  1.00 14.05  ? 821  HOH B O   1 
HETATM 5364 O O   . HOH H 3 .   ? 20.065  9.227   20.536  1.00 48.57  ? 822  HOH B O   1 
HETATM 5365 O O   . HOH H 3 .   ? 24.909  -22.406 13.204  1.00 14.81  ? 823  HOH B O   1 
HETATM 5366 O O   . HOH H 3 .   ? 41.651  -12.272 25.246  1.00 32.52  ? 824  HOH B O   1 
HETATM 5367 O O   . HOH H 3 .   ? 31.609  2.746   20.857  1.00 18.89  ? 825  HOH B O   1 
HETATM 5368 O O   . HOH H 3 .   ? 16.593  -51.829 2.674   1.00 52.69  ? 826  HOH B O   1 
HETATM 5369 O O   . HOH H 3 .   ? 29.579  -0.163  32.183  1.00 29.81  ? 827  HOH B O   1 
HETATM 5370 O O   A HOH H 3 .   ? 22.184  1.336   37.861  0.48 19.26  ? 828  HOH B O   1 
HETATM 5371 O O   B HOH H 3 .   ? 24.157  0.926   38.402  0.52 24.92  ? 828  HOH B O   1 
HETATM 5372 O O   . HOH H 3 .   ? 9.591   -44.109 -1.339  1.00 22.40  ? 829  HOH B O   1 
HETATM 5373 O O   . HOH H 3 .   ? 12.460  -48.451 -1.973  1.00 27.03  ? 830  HOH B O   1 
HETATM 5374 O O   . HOH H 3 .   ? 40.109  -12.261 30.976  1.00 33.65  ? 831  HOH B O   1 
HETATM 5375 O O   . HOH H 3 .   ? 23.885  -46.735 0.902   1.00 24.30  ? 832  HOH B O   1 
HETATM 5376 O O   . HOH H 3 .   ? 31.760  3.801   31.810  1.00 39.13  ? 833  HOH B O   1 
HETATM 5377 O O   . HOH H 3 .   ? 32.556  -40.436 15.976  1.00 32.28  ? 834  HOH B O   1 
HETATM 5378 O O   . HOH H 3 .   ? 16.802  -5.275  6.093   1.00 24.67  ? 835  HOH B O   1 
HETATM 5379 O O   . HOH H 3 .   ? 39.910  -25.815 22.002  1.00 20.18  ? 836  HOH B O   1 
HETATM 5380 O O   . HOH H 3 .   ? 15.442  -48.644 13.049  1.00 23.25  ? 837  HOH B O   1 
HETATM 5381 O O   . HOH H 3 .   ? 31.728  -20.195 11.523  1.00 13.28  ? 838  HOH B O   1 
HETATM 5382 O O   . HOH H 3 .   ? 18.590  -38.134 -5.894  1.00 26.92  ? 839  HOH B O   1 
HETATM 5383 O O   . HOH H 3 .   ? 33.425  6.754   25.571  1.00 34.76  ? 840  HOH B O   1 
HETATM 5384 O O   . HOH H 3 .   ? 32.896  -21.720 3.048   1.00 34.22  ? 841  HOH B O   1 
HETATM 5385 O O   . HOH H 3 .   ? 27.169  -3.693  9.612   1.00 22.06  ? 842  HOH B O   1 
HETATM 5386 O O   . HOH H 3 .   ? 26.025  -30.753 -7.099  1.00 30.00  ? 843  HOH B O   1 
HETATM 5387 O O   . HOH H 3 .   ? 25.140  -22.920 7.183   1.00 10.49  ? 844  HOH B O   1 
HETATM 5388 O O   . HOH H 3 .   ? 24.379  7.185   26.623  1.00 48.48  ? 845  HOH B O   1 
HETATM 5389 O O   . HOH H 3 .   ? 21.065  -18.900 -8.190  1.00 29.00  ? 846  HOH B O   1 
HETATM 5390 O O   . HOH H 3 .   ? 36.496  -38.233 21.484  1.00 34.01  ? 847  HOH B O   1 
HETATM 5391 O O   . HOH H 3 .   ? 18.445  -15.389 36.520  1.00 42.83  ? 848  HOH B O   1 
HETATM 5392 O O   . HOH H 3 .   ? 31.725  -6.975  6.787   1.00 20.10  ? 849  HOH B O   1 
HETATM 5393 O O   . HOH H 3 .   ? 15.676  2.331   28.298  1.00 36.88  ? 850  HOH B O   1 
HETATM 5394 O O   . HOH H 3 .   ? 40.354  -31.560 23.321  1.00 28.31  ? 851  HOH B O   1 
HETATM 5395 O O   . HOH H 3 .   ? 38.232  -0.083  23.390  1.00 35.19  ? 852  HOH B O   1 
HETATM 5396 O O   . HOH H 3 .   ? 38.813  -10.183 10.315  1.00 30.42  ? 853  HOH B O   1 
HETATM 5397 O O   . HOH H 3 .   ? 11.000  3.013   14.606  1.00 37.40  ? 854  HOH B O   1 
HETATM 5398 O O   . HOH H 3 .   ? 11.492  -5.668  12.143  1.00 19.92  ? 855  HOH B O   1 
HETATM 5399 O O   . HOH H 3 .   ? 36.615  -21.117 6.184   1.00 22.49  ? 856  HOH B O   1 
HETATM 5400 O O   . HOH H 3 .   ? 33.871  -29.337 8.466   1.00 15.39  ? 857  HOH B O   1 
HETATM 5401 O O   . HOH H 3 .   ? 28.528  -20.835 26.840  1.00 31.16  ? 858  HOH B O   1 
HETATM 5402 O O   . HOH H 3 .   ? 22.394  -13.373 2.979   1.00 20.80  ? 859  HOH B O   1 
HETATM 5403 O O   . HOH H 3 .   ? 19.115  -47.947 14.701  1.00 33.04  ? 860  HOH B O   1 
HETATM 5404 O O   . HOH H 3 .   ? 10.236  -9.234  8.516   1.00 34.38  ? 861  HOH B O   1 
HETATM 5405 O O   . HOH H 3 .   ? 17.018  -18.753 13.093  1.00 18.92  ? 862  HOH B O   1 
HETATM 5406 O O   . HOH H 3 .   ? 21.155  -45.125 17.447  1.00 27.70  ? 863  HOH B O   1 
HETATM 5407 O O   . HOH H 3 .   ? 34.254  -8.914  14.854  1.00 24.62  ? 864  HOH B O   1 
HETATM 5408 O O   . HOH H 3 .   ? 13.534  -36.311 17.910  1.00 13.57  ? 865  HOH B O   1 
HETATM 5409 O O   . HOH H 3 .   ? 24.634  0.511   10.941  1.00 20.79  ? 866  HOH B O   1 
HETATM 5410 O O   . HOH H 3 .   ? 26.782  -19.175 -7.246  1.00 27.68  ? 867  HOH B O   1 
HETATM 5411 O O   . HOH H 3 .   ? 28.137  -48.548 1.215   1.00 39.98  ? 868  HOH B O   1 
HETATM 5412 O O   . HOH H 3 .   ? 30.874  -37.169 0.359   1.00 25.81  ? 869  HOH B O   1 
HETATM 5413 O O   . HOH H 3 .   ? 30.271  -0.252  26.017  1.00 17.01  ? 870  HOH B O   1 
HETATM 5414 O O   . HOH H 3 .   ? 36.355  -2.926  13.798  1.00 33.85  ? 871  HOH B O   1 
HETATM 5415 O O   . HOH H 3 .   ? 37.987  -10.454 32.594  1.00 38.86  ? 872  HOH B O   1 
HETATM 5416 O O   . HOH H 3 .   ? 26.761  -16.761 34.737  1.00 30.93  ? 873  HOH B O   1 
HETATM 5417 O O   . HOH H 3 .   ? 13.941  -17.402 13.077  1.00 17.21  ? 874  HOH B O   1 
HETATM 5418 O O   . HOH H 3 .   ? 16.766  -43.397 18.666  1.00 32.95  ? 875  HOH B O   1 
HETATM 5419 O O   . HOH H 3 .   ? 32.777  -17.860 10.640  1.00 15.04  ? 876  HOH B O   1 
HETATM 5420 O O   . HOH H 3 .   ? 19.373  -20.935 31.384  1.00 28.18  ? 877  HOH B O   1 
HETATM 5421 O O   . HOH H 3 .   ? 4.006   -6.836  16.321  1.00 29.25  ? 878  HOH B O   1 
HETATM 5422 O O   . HOH H 3 .   ? 28.333  -7.278  9.134   1.00 38.83  ? 879  HOH B O   1 
HETATM 5423 O O   . HOH H 3 .   ? 20.098  8.453   24.374  1.00 42.41  ? 880  HOH B O   1 
HETATM 5424 O O   . HOH H 3 .   ? 15.726  -49.553 -2.834  1.00 31.67  ? 881  HOH B O   1 
HETATM 5425 O O   . HOH H 3 .   ? 34.955  -7.888  17.721  1.00 22.67  ? 882  HOH B O   1 
HETATM 5426 O O   . HOH H 3 .   ? 19.518  -28.859 -10.045 1.00 26.28  ? 883  HOH B O   1 
HETATM 5427 O O   . HOH H 3 .   ? 21.836  7.155   12.549  1.00 37.84  ? 884  HOH B O   1 
HETATM 5428 O O   . HOH H 3 .   ? 25.662  -8.192  9.817   1.00 35.20  ? 885  HOH B O   1 
HETATM 5429 O O   . HOH H 3 .   ? 35.573  -14.730 15.220  1.00 18.15  ? 886  HOH B O   1 
HETATM 5430 O O   . HOH H 3 .   ? 39.476  -22.862 24.153  1.00 37.69  ? 887  HOH B O   1 
HETATM 5431 O O   . HOH H 3 .   ? 11.257  -38.529 11.566  1.00 33.67  ? 888  HOH B O   1 
HETATM 5432 O O   . HOH H 3 .   ? 28.345  -36.960 21.087  1.00 27.11  ? 889  HOH B O   1 
HETATM 5433 O O   . HOH H 3 .   ? 37.480  -25.589 7.416   1.00 24.36  ? 890  HOH B O   1 
HETATM 5434 O O   . HOH H 3 .   ? 10.134  -3.947  8.907   1.00 50.36  ? 891  HOH B O   1 
HETATM 5435 O O   . HOH H 3 .   ? 40.932  -15.127 21.951  1.00 35.17  ? 892  HOH B O   1 
HETATM 5436 O O   . HOH H 3 .   ? 15.653  -21.252 0.925   1.00 52.30  ? 893  HOH B O   1 
HETATM 5437 O O   . HOH H 3 .   ? 20.109  -14.934 -2.063  1.00 25.47  ? 894  HOH B O   1 
HETATM 5438 O O   A HOH H 3 .   ? 26.601  -40.630 15.973  0.47 19.02  ? 895  HOH B O   1 
HETATM 5439 O O   B HOH H 3 .   ? 28.350  -41.158 15.585  0.53 28.59  ? 895  HOH B O   1 
HETATM 5440 O O   . HOH H 3 .   ? 10.199  -36.615 5.514   1.00 48.26  ? 896  HOH B O   1 
HETATM 5441 O O   . HOH H 3 .   ? 28.190  7.491   25.439  1.00 39.24  ? 897  HOH B O   1 
HETATM 5442 O O   . HOH H 3 .   ? 39.376  -28.905 11.875  1.00 35.77  ? 898  HOH B O   1 
HETATM 5443 O O   . HOH H 3 .   ? 8.902   -33.214 -0.204  1.00 48.51  ? 899  HOH B O   1 
HETATM 5444 O O   . HOH H 3 .   ? 20.756  -52.398 12.200  1.00 47.87  ? 900  HOH B O   1 
HETATM 5445 O O   . HOH H 3 .   ? 24.269  -51.268 6.927   1.00 25.52  ? 901  HOH B O   1 
HETATM 5446 O O   . HOH H 3 .   ? 15.269  -52.681 6.497   1.00 41.59  ? 902  HOH B O   1 
HETATM 5447 O O   . HOH H 3 .   ? 37.690  -20.324 20.935  1.00 29.22  ? 903  HOH B O   1 
HETATM 5448 O O   . HOH H 3 .   ? 28.899  1.059   29.300  1.00 22.70  ? 904  HOH B O   1 
HETATM 5449 O O   . HOH H 3 .   ? 43.043  -6.051  22.956  1.00 51.15  ? 905  HOH B O   1 
HETATM 5450 O O   . HOH H 3 .   ? 34.387  -16.508 3.016   1.00 52.04  ? 906  HOH B O   1 
HETATM 5451 O O   . HOH H 3 .   ? 10.473  -13.603 20.770  1.00 17.98  ? 907  HOH B O   1 
HETATM 5452 O O   . HOH H 3 .   ? 12.333  -24.043 -3.326  1.00 52.29  ? 908  HOH B O   1 
HETATM 5453 O O   . HOH H 3 .   ? 28.549  5.685   9.389   1.00 27.82  ? 909  HOH B O   1 
HETATM 5454 O O   . HOH H 3 .   ? 14.766  5.930   26.567  1.00 45.06  ? 910  HOH B O   1 
HETATM 5455 O O   . HOH H 3 .   ? 34.736  -28.529 5.956   1.00 15.34  ? 911  HOH B O   1 
HETATM 5456 O O   . HOH H 3 .   ? 16.152  -24.544 17.670  1.00 36.79  ? 912  HOH B O   1 
HETATM 5457 O O   . HOH H 3 .   ? 24.771  1.922   8.748   1.00 42.69  ? 913  HOH B O   1 
HETATM 5458 O O   . HOH H 3 .   ? 29.363  -5.114  38.860  1.00 43.74  ? 914  HOH B O   1 
HETATM 5459 O O   . HOH H 3 .   ? 25.509  -28.828 26.864  1.00 29.87  ? 915  HOH B O   1 
HETATM 5460 O O   . HOH H 3 .   ? 13.855  -12.490 5.318   1.00 19.98  ? 916  HOH B O   1 
HETATM 5461 O O   . HOH H 3 .   ? 15.641  7.598   19.228  1.00 31.36  ? 917  HOH B O   1 
HETATM 5462 O O   . HOH H 3 .   ? 36.810  -14.232 30.200  1.00 29.56  ? 918  HOH B O   1 
HETATM 5463 O O   . HOH H 3 .   ? 35.780  -18.685 8.047   1.00 25.93  ? 919  HOH B O   1 
HETATM 5464 O O   . HOH H 3 .   ? 27.945  -16.995 32.498  1.00 21.84  ? 920  HOH B O   1 
HETATM 5465 O O   . HOH H 3 .   ? 13.481  -35.733 -4.968  1.00 25.47  ? 921  HOH B O   1 
HETATM 5466 O O   . HOH H 3 .   ? 21.078  -29.523 9.632   1.00 26.05  ? 922  HOH B O   1 
HETATM 5467 O O   . HOH H 3 .   ? 14.144  -51.515 4.085   1.00 51.62  ? 923  HOH B O   1 
HETATM 5468 O O   . HOH H 3 .   ? 31.704  -24.992 28.020  1.00 33.29  ? 924  HOH B O   1 
HETATM 5469 O O   . HOH H 3 .   ? 14.847  3.032   7.869   1.00 62.05  ? 925  HOH B O   1 
HETATM 5470 O O   . HOH H 3 .   ? 30.242  -46.133 7.747   1.00 31.12  ? 926  HOH B O   1 
HETATM 5471 O O   . HOH H 3 .   ? 40.512  -15.625 14.968  1.00 29.84  ? 927  HOH B O   1 
HETATM 5472 O O   . HOH H 3 .   ? 21.266  -32.708 -5.026  1.00 34.45  ? 928  HOH B O   1 
HETATM 5473 O O   . HOH H 3 .   ? 11.998  -35.383 3.440   1.00 25.29  ? 929  HOH B O   1 
HETATM 5474 O O   . HOH H 3 .   ? 45.698  -32.841 21.894  1.00 50.60  ? 930  HOH B O   1 
HETATM 5475 O O   . HOH H 3 .   ? 8.194   -12.849 18.716  1.00 28.78  ? 931  HOH B O   1 
HETATM 5476 O O   . HOH H 3 .   ? 29.636  -4.061  34.559  1.00 40.98  ? 932  HOH B O   1 
HETATM 5477 O O   . HOH H 3 .   ? 19.714  -10.444 40.390  1.00 40.12  ? 933  HOH B O   1 
HETATM 5478 O O   . HOH H 3 .   ? 29.717  10.022  20.253  1.00 23.86  ? 934  HOH B O   1 
HETATM 5479 O O   . HOH H 3 .   ? 9.505   -40.830 11.965  1.00 21.54  ? 935  HOH B O   1 
HETATM 5480 O O   . HOH H 3 .   ? 36.751  -36.228 7.599   1.00 22.54  ? 936  HOH B O   1 
HETATM 5481 O O   . HOH H 3 .   ? 37.236  -10.550 15.598  1.00 40.43  ? 937  HOH B O   1 
HETATM 5482 O O   . HOH H 3 .   ? 14.448  -20.518 20.831  1.00 27.95  ? 938  HOH B O   1 
HETATM 5483 O O   . HOH H 3 .   ? 17.568  -18.836 3.120   1.00 36.71  ? 939  HOH B O   1 
HETATM 5484 O O   . HOH H 3 .   ? 41.791  -15.540 17.580  1.00 39.93  ? 940  HOH B O   1 
HETATM 5485 O O   . HOH H 3 .   ? 11.770  3.388   16.977  1.00 25.74  ? 941  HOH B O   1 
HETATM 5486 O O   . HOH H 3 .   ? 13.423  -2.715  24.832  1.00 20.09  ? 942  HOH B O   1 
HETATM 5487 O O   . HOH H 3 .   ? 34.248  3.121   20.236  1.00 26.27  ? 943  HOH B O   1 
HETATM 5488 O O   . HOH H 3 .   ? 16.995  -50.794 12.146  1.00 22.14  ? 944  HOH B O   1 
HETATM 5489 O O   . HOH H 3 .   ? 12.648  -48.100 3.854   1.00 25.64  ? 945  HOH B O   1 
HETATM 5490 O O   . HOH H 3 .   ? 15.364  -24.691 -8.552  1.00 47.36  ? 946  HOH B O   1 
HETATM 5491 O O   . HOH H 3 .   ? 42.108  -11.744 27.346  1.00 33.92  ? 947  HOH B O   1 
HETATM 5492 O O   . HOH H 3 .   ? 41.221  -32.015 30.071  1.00 48.24  ? 948  HOH B O   1 
HETATM 5493 O O   . HOH H 3 .   ? 32.420  -14.207 1.402   1.00 31.40  ? 949  HOH B O   1 
HETATM 5494 O O   . HOH H 3 .   ? 29.119  -13.930 -0.827  1.00 21.89  ? 950  HOH B O   1 
HETATM 5495 O O   . HOH H 3 .   ? 35.168  -10.729 17.336  1.00 32.66  ? 951  HOH B O   1 
HETATM 5496 O O   . HOH H 3 .   ? 29.205  -21.936 29.675  1.00 38.28  ? 952  HOH B O   1 
HETATM 5497 O O   . HOH H 3 .   ? 24.229  -24.020 27.603  1.00 30.31  ? 953  HOH B O   1 
HETATM 5498 O O   . HOH H 3 .   ? 13.178  -49.673 6.047   1.00 27.69  ? 954  HOH B O   1 
HETATM 5499 O O   . HOH H 3 .   ? 12.309  -23.931 2.959   1.00 44.19  ? 955  HOH B O   1 
HETATM 5500 O O   . HOH H 3 .   ? 8.067   -36.390 -2.318  1.00 40.82  ? 956  HOH B O   1 
HETATM 5501 O O   . HOH H 3 .   ? 32.573  -19.036 32.831  1.00 51.95  ? 957  HOH B O   1 
HETATM 5502 O O   . HOH H 3 .   ? 25.087  -53.965 4.272   1.00 36.42  ? 958  HOH B O   1 
HETATM 5503 O O   . HOH H 3 .   ? 15.263  -55.060 9.845   1.00 46.85  ? 959  HOH B O   1 
HETATM 5504 O O   . HOH H 3 .   ? 42.066  -27.509 21.568  1.00 42.21  ? 960  HOH B O   1 
HETATM 5505 O O   . HOH H 3 .   ? 21.709  -28.173 27.371  1.00 39.29  ? 961  HOH B O   1 
HETATM 5506 O O   . HOH H 3 .   ? 24.739  -2.073  10.363  1.00 17.10  ? 962  HOH B O   1 
HETATM 5507 O O   . HOH H 3 .   ? 12.891  -14.928 5.155   1.00 37.44  ? 963  HOH B O   1 
HETATM 5508 O O   . HOH H 3 .   ? 41.887  -36.886 28.970  1.00 38.83  ? 964  HOH B O   1 
HETATM 5509 O O   . HOH H 3 .   ? 39.061  -3.324  19.943  1.00 41.13  ? 965  HOH B O   1 
HETATM 5510 O O   . HOH H 3 .   ? 18.817  -50.811 14.338  1.00 45.66  ? 966  HOH B O   1 
HETATM 5511 O O   . HOH H 3 .   ? 26.272  -7.755  38.510  1.00 32.08  ? 967  HOH B O   1 
HETATM 5512 O O   . HOH H 3 .   ? 9.134   -34.234 7.169   1.00 37.96  ? 968  HOH B O   1 
HETATM 5513 O O   . HOH H 3 .   ? 13.927  -35.027 13.546  1.00 24.94  ? 969  HOH B O   1 
HETATM 5514 O O   . HOH H 3 .   ? 37.717  -30.929 10.288  1.00 27.22  ? 970  HOH B O   1 
HETATM 5515 O O   . HOH H 3 .   ? 17.536  -2.991  9.482   1.00 26.99  ? 971  HOH B O   1 
HETATM 5516 O O   . HOH H 3 .   ? 37.806  -38.712 6.387   1.00 40.82  ? 972  HOH B O   1 
HETATM 5517 O O   . HOH H 3 .   ? 5.813   -26.470 3.233   1.00 46.45  ? 973  HOH B O   1 
HETATM 5518 O O   . HOH H 3 .   ? 28.001  7.427   11.369  1.00 28.23  ? 974  HOH B O   1 
HETATM 5519 O O   . HOH H 3 .   ? 21.881  -19.219 1.826   1.00 24.65  ? 975  HOH B O   1 
HETATM 5520 O O   . HOH H 3 .   ? 10.448  -38.513 6.960   1.00 36.39  ? 976  HOH B O   1 
HETATM 5521 O O   . HOH H 3 .   ? 15.834  -40.740 -4.792  1.00 38.44  ? 977  HOH B O   1 
HETATM 5522 O O   . HOH H 3 .   ? 34.657  -1.630  10.027  1.00 50.56  ? 978  HOH B O   1 
HETATM 5523 O O   . HOH H 3 .   ? 32.449  -45.768 2.882   1.00 50.83  ? 979  HOH B O   1 
HETATM 5524 O O   . HOH H 3 .   ? 35.969  -16.139 33.701  1.00 50.15  ? 980  HOH B O   1 
HETATM 5525 O O   . HOH H 3 .   ? 14.138  -10.772 3.112   1.00 32.40  ? 981  HOH B O   1 
HETATM 5526 O O   . HOH H 3 .   ? 17.384  -41.999 -5.984  1.00 37.18  ? 982  HOH B O   1 
HETATM 5527 O O   . HOH H 3 .   ? 35.584  -30.659 2.145   1.00 24.81  ? 983  HOH B O   1 
HETATM 5528 O O   . HOH H 3 .   ? 17.105  -12.541 38.176  1.00 46.44  ? 984  HOH B O   1 
HETATM 5529 O O   . HOH H 3 .   ? 38.234  -16.713 14.045  1.00 41.95  ? 985  HOH B O   1 
HETATM 5530 O O   . HOH H 3 .   ? 12.071  -9.234  2.886   1.00 44.76  ? 986  HOH B O   1 
HETATM 5531 O O   . HOH H 3 .   ? 24.222  -26.467 27.692  1.00 40.99  ? 987  HOH B O   1 
HETATM 5532 O O   . HOH H 3 .   ? 7.473   -4.482  23.761  1.00 34.72  ? 988  HOH B O   1 
HETATM 5533 O O   . HOH H 3 .   ? 35.000  -18.670 23.562  1.00 29.26  ? 989  HOH B O   1 
HETATM 5534 O O   . HOH H 3 .   ? 16.214  -15.943 37.136  1.00 44.85  ? 990  HOH B O   1 
HETATM 5535 O O   . HOH H 3 .   ? 18.053  4.720   6.534   1.00 56.52  ? 991  HOH B O   1 
HETATM 5536 O O   . HOH H 3 .   ? 9.902   -32.918 -3.359  1.00 41.83  ? 992  HOH B O   1 
HETATM 5537 O O   . HOH H 3 .   ? 35.960  -30.135 -5.838  1.00 45.83  ? 993  HOH B O   1 
HETATM 5538 O O   . HOH H 3 .   ? 37.679  -17.689 9.462   1.00 35.89  ? 994  HOH B O   1 
HETATM 5539 O O   . HOH H 3 .   ? 19.025  5.401   30.143  1.00 51.01  ? 995  HOH B O   1 
HETATM 5540 O O   . HOH H 3 .   ? 30.073  3.321   9.442   1.00 27.43  ? 996  HOH B O   1 
HETATM 5541 O O   . HOH H 3 .   ? 19.652  -20.433 2.646   1.00 30.90  ? 997  HOH B O   1 
HETATM 5542 O O   . HOH H 3 .   ? 20.560  8.488   15.061  1.00 42.53  ? 998  HOH B O   1 
HETATM 5543 O O   A HOH H 3 .   ? 36.828  -6.086  16.719  0.64 24.86  ? 999  HOH B O   1 
HETATM 5544 O O   B HOH H 3 .   ? 37.822  -7.065  18.024  0.36 25.68  ? 999  HOH B O   1 
HETATM 5545 O O   . HOH H 3 .   ? 12.389  -4.411  28.853  1.00 28.67  ? 1000 HOH B O   1 
HETATM 5546 O O   . HOH H 3 .   ? 30.703  -42.667 -1.867  1.00 53.60  ? 1001 HOH B O   1 
HETATM 5547 O O   . HOH H 3 .   ? 31.953  -43.800 14.372  1.00 43.92  ? 1002 HOH B O   1 
HETATM 5548 O O   . HOH H 3 .   ? 21.039  -19.477 35.140  1.00 44.22  ? 1003 HOH B O   1 
HETATM 5549 O O   . HOH H 3 .   ? 18.721  -20.845 -0.590  1.00 35.55  ? 1004 HOH B O   1 
HETATM 5550 O O   . HOH H 3 .   ? 8.948   -38.024 9.197   1.00 39.51  ? 1005 HOH B O   1 
HETATM 5551 O O   . HOH H 3 .   ? 21.335  -3.860  7.568   1.00 26.75  ? 1006 HOH B O   1 
HETATM 5552 O O   . HOH H 3 .   ? 6.208   -10.996 7.349   1.00 46.00  ? 1007 HOH B O   1 
HETATM 5553 O O   . HOH H 3 .   ? 19.015  -3.012  7.102   1.00 30.81  ? 1008 HOH B O   1 
HETATM 5554 O O   . HOH H 3 .   ? 8.666   -35.346 9.636   1.00 38.10  ? 1009 HOH B O   1 
HETATM 5555 O O   . HOH H 3 .   ? 24.734  -18.548 35.072  1.00 53.45  ? 1010 HOH B O   1 
HETATM 5556 O O   . HOH H 3 .   ? 43.200  -9.510  17.711  1.00 49.74  ? 1011 HOH B O   1 
HETATM 5557 O O   . HOH H 3 .   ? 18.531  -31.970 -6.405  1.00 31.30  ? 1012 HOH B O   1 
HETATM 5558 O O   . HOH H 3 .   ? 38.672  -29.549 8.123   1.00 38.87  ? 1013 HOH B O   1 
HETATM 5559 O O   . HOH H 3 .   ? 23.944  -51.906 10.685  1.00 44.95  ? 1014 HOH B O   1 
HETATM 5560 O O   A HOH H 3 .   ? 37.516  -0.436  12.330  0.55 29.84  ? 1015 HOH B O   1 
HETATM 5561 O O   B HOH H 3 .   ? 36.417  1.386   11.615  0.45 31.08  ? 1015 HOH B O   1 
HETATM 5562 O O   . HOH H 3 .   ? 35.183  -39.331 18.944  1.00 51.37  ? 1016 HOH B O   1 
HETATM 5563 O O   . HOH H 3 .   ? 36.375  -19.932 28.111  1.00 41.55  ? 1017 HOH B O   1 
HETATM 5564 O O   . HOH H 3 .   ? 38.627  -18.159 24.474  1.00 46.70  ? 1018 HOH B O   1 
HETATM 5565 O O   . HOH H 3 .   ? 38.744  -18.288 28.082  1.00 46.69  ? 1019 HOH B O   1 
HETATM 5566 O O   . HOH H 3 .   ? 33.069  -18.209 -8.654  1.00 45.96  ? 1020 HOH B O   1 
HETATM 5567 O O   . HOH H 3 .   ? 27.102  -21.497 -8.089  1.00 37.23  ? 1021 HOH B O   1 
HETATM 5568 O O   . HOH H 3 .   ? 27.430  -35.197 -2.933  1.00 42.89  ? 1022 HOH B O   1 
HETATM 5569 O O   . HOH H 3 .   ? 24.171  -41.913 21.381  1.00 33.44  ? 1023 HOH B O   1 
HETATM 5570 O O   . HOH H 3 .   ? 31.793  -40.537 18.894  1.00 46.13  ? 1024 HOH B O   1 
HETATM 5571 O O   . HOH H 3 .   ? 36.643  -40.753 5.187   1.00 40.91  ? 1025 HOH B O   1 
HETATM 5572 O O   A HOH H 3 .   ? 22.790  -52.904 5.734   0.47 25.62  ? 1026 HOH B O   1 
HETATM 5573 O O   B HOH H 3 .   ? 20.722  -52.936 5.900   0.53 25.00  ? 1026 HOH B O   1 
HETATM 5574 O O   A HOH H 3 .   ? 29.333  -44.714 -0.972  0.42 24.61  ? 1027 HOH B O   1 
HETATM 5575 O O   B HOH H 3 .   ? 28.582  -46.263 -0.266  0.58 33.35  ? 1027 HOH B O   1 
HETATM 5576 O O   . HOH H 3 .   ? 34.670  -33.368 -1.630  1.00 51.56  ? 1028 HOH B O   1 
HETATM 5577 O O   . HOH H 3 .   ? 2.644   -6.702  13.446  1.00 51.97  ? 1029 HOH B O   1 
HETATM 5578 O O   . HOH H 3 .   ? 31.249  -4.335  8.161   1.00 29.39  ? 1030 HOH B O   1 
HETATM 5579 O O   . HOH H 3 .   ? 17.661  -29.640 -7.851  1.00 27.32  ? 1031 HOH B O   1 
HETATM 5580 O O   . HOH H 3 .   ? 23.580  -2.126  7.773   1.00 24.92  ? 1032 HOH B O   1 
HETATM 5581 O O   . HOH H 3 .   ? 15.319  -16.673 4.313   1.00 53.35  ? 1033 HOH B O   1 
HETATM 5582 O O   . HOH H 3 .   ? 25.799  1.776   32.167  1.00 47.76  ? 1034 HOH B O   1 
HETATM 5583 O O   . HOH H 3 .   ? 26.373  -53.145 8.089   1.00 39.32  ? 1035 HOH B O   1 
HETATM 5584 O O   . HOH H 3 .   ? 11.477  5.166   18.279  1.00 48.24  ? 1036 HOH B O   1 
HETATM 5585 O O   . HOH H 3 .   ? 18.632  -45.340 17.172  1.00 30.56  ? 1037 HOH B O   1 
HETATM 5586 O O   . HOH H 3 .   ? 38.759  -34.044 7.140   1.00 44.25  ? 1038 HOH B O   1 
HETATM 5587 O O   . HOH H 3 .   ? 41.099  -20.689 13.490  1.00 35.83  ? 1039 HOH B O   1 
HETATM 5588 O O   . HOH H 3 .   ? 28.344  -21.289 33.023  1.00 47.05  ? 1040 HOH B O   1 
HETATM 5589 O O   . HOH H 3 .   ? 40.230  -16.883 20.545  1.00 39.38  ? 1041 HOH B O   1 
HETATM 5590 O O   . HOH H 3 .   ? 39.982  -29.697 -0.153  1.00 55.06  ? 1042 HOH B O   1 
HETATM 5591 O O   . HOH H 3 .   ? 22.974  -18.981 33.003  1.00 38.41  ? 1043 HOH B O   1 
HETATM 5592 O O   . HOH H 3 .   ? 29.497  -38.780 -1.537  1.00 44.35  ? 1044 HOH B O   1 
HETATM 5593 O O   . HOH H 3 .   ? 10.815  -3.607  6.127   1.00 48.88  ? 1045 HOH B O   1 
HETATM 5594 O O   . HOH H 3 .   ? 37.272  -27.916 6.144   1.00 24.43  ? 1046 HOH B O   1 
HETATM 5595 O O   . HOH H 3 .   ? 6.255   -32.361 7.393   1.00 40.82  ? 1047 HOH B O   1 
HETATM 5596 O O   . HOH H 3 .   ? 37.413  -30.678 3.522   1.00 45.21  ? 1048 HOH B O   1 
HETATM 5597 O O   . HOH H 3 .   ? 9.965   -16.300 20.205  1.00 14.01  ? 1049 HOH B O   1 
HETATM 5598 O O   . HOH H 3 .   ? 34.776  -41.114 15.439  1.00 53.74  ? 1050 HOH B O   1 
HETATM 5599 O O   . HOH H 3 .   ? 38.918  -33.289 9.842   1.00 35.74  ? 1051 HOH B O   1 
HETATM 5600 O O   . HOH H 3 .   ? 27.270  3.164   31.098  1.00 43.46  ? 1052 HOH B O   1 
HETATM 5601 O O   . HOH H 3 .   ? 22.031  -45.525 19.805  1.00 37.96  ? 1053 HOH B O   1 
HETATM 5602 O O   . HOH H 3 .   ? 26.697  0.237   7.630   1.00 40.78  ? 1054 HOH B O   1 
HETATM 5603 O O   . HOH H 3 .   ? 35.444  -17.235 21.874  1.00 30.09  ? 1055 HOH B O   1 
HETATM 5604 O O   . HOH H 3 .   ? 40.047  -21.422 21.938  1.00 30.63  ? 1056 HOH B O   1 
HETATM 5605 O O   . HOH H 3 .   ? 7.980   -34.053 -2.565  1.00 42.76  ? 1057 HOH B O   1 
HETATM 5606 O O   . HOH H 3 .   ? 24.836  8.105   7.522   1.00 47.78  ? 1058 HOH B O   1 
HETATM 5607 O O   . HOH H 3 .   ? 6.430   -32.229 0.176   1.00 56.18  ? 1059 HOH B O   1 
HETATM 5608 O O   . HOH H 3 .   ? 10.223  -10.265 4.954   1.00 42.94  ? 1060 HOH B O   1 
HETATM 5609 O O   . HOH H 3 .   ? 28.648  -7.258  37.403  1.00 33.63  ? 1061 HOH B O   1 
HETATM 5610 O O   . HOH H 3 .   ? 18.614  -18.774 -6.766  1.00 54.24  ? 1062 HOH B O   1 
HETATM 5611 O O   . HOH H 3 .   ? 36.067  -40.916 2.809   1.00 49.99  ? 1063 HOH B O   1 
HETATM 5612 O O   . HOH H 3 .   ? 20.994  4.110   29.586  1.00 41.24  ? 1064 HOH B O   1 
HETATM 5613 O O   . HOH H 3 .   ? 24.873  -45.451 -3.974  1.00 44.59  ? 1065 HOH B O   1 
HETATM 5614 O O   . HOH H 3 .   ? 11.602  -1.021  25.240  1.00 30.93  ? 1066 HOH B O   1 
HETATM 5615 O O   . HOH H 3 .   ? 35.347  -4.730  32.586  1.00 40.16  ? 1067 HOH B O   1 
HETATM 5616 O O   . HOH H 3 .   ? 37.055  -11.141 7.778   1.00 43.78  ? 1068 HOH B O   1 
HETATM 5617 O O   . HOH H 3 .   ? 29.463  -43.915 15.836  1.00 43.20  ? 1069 HOH B O   1 
HETATM 5618 O O   . HOH H 3 .   ? 39.243  -23.858 6.678   1.00 42.85  ? 1070 HOH B O   1 
HETATM 5619 O O   . HOH H 3 .   ? 41.972  -13.822 28.662  1.00 50.56  ? 1071 HOH B O   1 
HETATM 5620 O O   . HOH H 3 .   ? 9.930   -4.063  27.766  1.00 34.18  ? 1072 HOH B O   1 
HETATM 5621 O O   . HOH H 3 .   ? 33.546  -2.927  8.362   1.00 39.02  ? 1073 HOH B O   1 
HETATM 5622 O O   . HOH H 3 .   ? 39.178  -36.020 11.170  1.00 42.52  ? 1074 HOH B O   1 
HETATM 5623 O O   . HOH H 3 .   ? 42.284  -17.017 13.791  1.00 38.30  ? 1075 HOH B O   1 
HETATM 5624 O O   . HOH H 3 .   ? 36.376  -41.911 23.348  1.00 48.54  ? 1076 HOH B O   1 
HETATM 5625 O O   . HOH H 3 .   ? 43.157  -25.441 11.875  1.00 45.12  ? 1077 HOH B O   1 
HETATM 5626 O O   . HOH H 3 .   ? 33.602  -43.520 5.585   1.00 39.14  ? 1078 HOH B O   1 
HETATM 5627 O O   . HOH H 3 .   ? 37.978  -7.396  11.532  1.00 37.78  ? 1079 HOH B O   1 
HETATM 5628 O O   . HOH H 3 .   ? 13.501  6.720   19.818  1.00 41.26  ? 1080 HOH B O   1 
HETATM 5629 O O   . HOH H 3 .   ? 36.777  -7.848  14.111  1.00 32.78  ? 1081 HOH B O   1 
HETATM 5630 O O   . HOH H 3 .   ? 39.182  -13.515 33.481  1.00 42.73  ? 1082 HOH B O   1 
HETATM 5631 O O   . HOH H 3 .   ? 37.991  -3.559  12.028  1.00 45.56  ? 1083 HOH B O   1 
HETATM 5632 O O   . HOH H 3 .   ? 23.092  10.400  19.948  1.00 47.43  ? 1084 HOH B O   1 
HETATM 5633 O O   . HOH H 3 .   ? 39.112  -28.157 4.418   1.00 36.02  ? 1085 HOH B O   1 
HETATM 5634 O O   . HOH H 3 .   ? 19.184  -20.672 -9.360  1.00 45.25  ? 1086 HOH B O   1 
HETATM 5635 O O   . HOH H 3 .   ? 25.586  -22.734 32.781  1.00 60.31  ? 1087 HOH B O   1 
HETATM 5636 O O   . HOH H 3 .   ? 37.710  -17.900 20.314  1.00 26.07  ? 1088 HOH B O   1 
HETATM 5637 O O   . HOH H 3 .   ? 30.909  -35.648 -3.421  1.00 44.36  ? 1089 HOH B O   1 
HETATM 5638 O O   . HOH H 3 .   ? 39.223  -21.601 6.159   1.00 33.63  ? 1090 HOH B O   1 
HETATM 5639 O O   . HOH H 3 .   ? 41.424  -22.677 9.810   1.00 42.81  ? 1091 HOH B O   1 
HETATM 5640 O O   . HOH H 3 .   ? 29.324  -6.733  34.718  1.00 29.33  ? 1092 HOH B O   1 
HETATM 5641 O O   . HOH H 3 .   ? 32.946  -5.948  33.964  1.00 48.78  ? 1093 HOH B O   1 
HETATM 5642 O O   . HOH H 3 .   ? 32.059  -45.694 5.643   1.00 38.23  ? 1094 HOH B O   1 
HETATM 5643 O O   . HOH H 3 .   ? 6.496   -39.411 9.954   1.00 37.68  ? 1095 HOH B O   1 
HETATM 5644 O O   . HOH H 3 .   ? 39.885  -26.763 8.744   1.00 41.75  ? 1096 HOH B O   1 
HETATM 5645 O O   . HOH H 3 .   ? 27.219  -2.177  7.526   1.00 37.95  ? 1097 HOH B O   1 
HETATM 5646 O O   . HOH H 3 .   ? 25.320  11.022  18.358  1.00 31.02  ? 1098 HOH B O   1 
HETATM 5647 O O   . HOH H 3 .   ? 31.197  -23.210 29.930  1.00 36.69  ? 1099 HOH B O   1 
HETATM 5648 O O   . HOH H 3 .   ? 27.121  -5.905  6.076   1.00 36.03  ? 1100 HOH B O   1 
HETATM 5649 O O   . HOH H 3 .   ? 24.573  10.728  11.180  1.00 38.87  ? 1101 HOH B O   1 
HETATM 5650 O O   A HOH H 3 .   ? 36.505  -19.573 4.102   0.57 32.53  ? 1102 HOH B O   1 
HETATM 5651 O O   B HOH H 3 .   ? 34.571  -19.460 3.527   0.43 22.70  ? 1102 HOH B O   1 
HETATM 5652 O O   . HOH H 3 .   ? 30.158  -9.528  37.422  1.00 44.20  ? 1103 HOH B O   1 
HETATM 5653 O O   . HOH H 3 .   ? 20.854  -5.846  45.452  1.00 47.64  ? 1104 HOH B O   1 
HETATM 5654 O O   . HOH H 3 .   ? 20.966  -32.680 -7.539  1.00 28.78  ? 1105 HOH B O   1 
HETATM 5655 O O   . HOH H 3 .   ? 22.824  8.759   25.116  1.00 38.52  ? 1106 HOH B O   1 
HETATM 5656 O O   . HOH H 3 .   ? 27.258  -23.635 30.984  1.00 36.25  ? 1107 HOH B O   1 
HETATM 5657 O O   . HOH H 3 .   ? 46.588  -11.672 13.030  1.00 49.14  ? 1108 HOH B O   1 
HETATM 5658 O O   . HOH H 3 .   ? 23.863  5.442   32.025  1.00 48.95  ? 1109 HOH B O   1 
HETATM 5659 O O   . HOH H 3 .   ? 42.476  -11.442 32.085  1.00 33.38  ? 1110 HOH B O   1 
HETATM 5660 O O   . HOH H 3 .   ? 35.330  7.616   28.045  1.00 47.44  ? 1111 HOH B O   1 
HETATM 5661 O O   . HOH H 3 .   ? 21.204  7.947   26.872  1.00 46.76  ? 1112 HOH B O   1 
HETATM 5662 O O   . HOH H 3 .   ? 10.029  -32.249 -6.208  1.00 34.50  ? 1113 HOH B O   1 
HETATM 5663 O O   . HOH H 3 .   ? 13.483  -11.945 0.660   1.00 49.64  ? 1114 HOH B O   1 
HETATM 5664 O O   . HOH H 3 .   ? 37.574  -3.167  9.461   1.00 43.12  ? 1115 HOH B O   1 
HETATM 5665 O O   . HOH H 3 .   ? 27.515  11.951  19.587  1.00 29.82  ? 1116 HOH B O   1 
HETATM 5666 O O   . HOH H 3 .   ? 36.237  -8.761  7.198   1.00 38.71  ? 1117 HOH B O   1 
HETATM 5667 O O   . HOH H 3 .   ? 13.008  -21.879 -5.921  1.00 54.47  ? 1118 HOH B O   1 
HETATM 5668 O O   . HOH H 3 .   ? 24.384  12.783  16.483  1.00 44.83  ? 1119 HOH B O   1 
HETATM 5669 O O   . HOH H 3 .   ? 42.274  -20.476 21.723  1.00 38.75  ? 1120 HOH B O   1 
HETATM 5670 O O   . HOH H 3 .   ? 42.455  -18.513 20.438  1.00 39.15  ? 1121 HOH B O   1 
HETATM 5671 O O   . HOH H 3 .   ? 41.711  -9.434  33.979  1.00 42.39  ? 1122 HOH B O   1 
HETATM 5672 O O   . HOH H 3 .   ? 29.688  -2.519  6.751   1.00 37.01  ? 1123 HOH B O   1 
HETATM 5673 O O   . HOH H 3 .   ? 18.842  8.012   29.144  1.00 55.91  ? 1124 HOH B O   1 
HETATM 5674 O O   . HOH H 3 .   ? 31.004  -33.232 -6.753  1.00 45.26  ? 1125 HOH B O   1 
HETATM 5675 O O   . HOH H 3 .   ? 40.724  -21.190 8.247   1.00 44.16  ? 1126 HOH B O   1 
HETATM 5676 O O   A HOH H 3 .   ? 5.426   -33.104 -3.781  0.51 31.70  ? 1127 HOH B O   1 
HETATM 5677 O O   B HOH H 3 .   ? 4.198   -34.523 -4.037  0.49 26.61  ? 1127 HOH B O   1 
HETATM 5678 O O   . HOH H 3 .   ? 23.771  10.855  24.263  1.00 45.40  ? 1128 HOH B O   1 
HETATM 5679 O O   . HOH H 3 .   ? 4.911   7.151   13.306  1.00 54.26  ? 1129 HOH B O   1 
HETATM 5680 O O   . HOH H 3 .   ? 19.677  11.350  27.878  1.00 54.95  ? 1130 HOH B O   1 
HETATM 5681 O O   . HOH H 3 .   ? 0.623   3.569   21.672  1.00 48.48  ? 1131 HOH B O   1 
HETATM 5682 O O   . HOH H 3 .   ? 29.938  -36.416 -8.881  1.00 47.43  ? 1132 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   . GLU A 1   ? 0.5960 0.5980 0.6088 0.0650  0.0623  0.0195  226  GLU A N   
2    C CA  . GLU A 1   ? 0.6508 0.6579 0.6690 0.0655  0.0576  0.0241  226  GLU A CA  
3    C C   . GLU A 1   ? 0.5497 0.5750 0.5792 0.0672  0.0544  0.0292  226  GLU A C   
4    O O   . GLU A 1   ? 0.4543 0.4888 0.4867 0.0642  0.0534  0.0283  226  GLU A O   
5    C CB  . GLU A 1   ? 0.7080 0.7110 0.7210 0.0580  0.0524  0.0216  226  GLU A CB  
6    C CG  . GLU A 1   ? 0.5601 0.5662 0.5702 0.0510  0.0500  0.0174  226  GLU A CG  
7    C CD  . GLU A 1   ? 0.6851 0.6830 0.6881 0.0445  0.0469  0.0138  226  GLU A CD  
8    O OE1 . GLU A 1   ? 0.7096 0.7034 0.7120 0.0443  0.0450  0.0154  226  GLU A OE1 
9    O OE2 . GLU A 1   ? 0.5036 0.4992 0.5015 0.0397  0.0465  0.0094  226  GLU A OE2 
10   N N   . PRO A 2   ? 0.4401 0.4707 0.4759 0.0718  0.0528  0.0347  227  PRO A N   
11   C CA  . PRO A 2   ? 0.3776 0.4263 0.4246 0.0732  0.0494  0.0396  227  PRO A CA  
12   C C   . PRO A 2   ? 0.3391 0.3960 0.3872 0.0653  0.0425  0.0388  227  PRO A C   
13   O O   . PRO A 2   ? 0.2970 0.3468 0.3387 0.0603  0.0393  0.0363  227  PRO A O   
14   C CB  . PRO A 2   ? 0.4167 0.4666 0.4679 0.0793  0.0486  0.0453  227  PRO A CB  
15   C CG  . PRO A 2   ? 0.5573 0.5909 0.5988 0.0779  0.0489  0.0430  227  PRO A CG  
16   C CD  . PRO A 2   ? 0.5498 0.5702 0.5824 0.0754  0.0536  0.0367  227  PRO A CD  
17   N N   . PHE A 3   ? 0.2724 0.3440 0.3288 0.0642  0.0406  0.0408  228  PHE A N   
18   C CA  . PHE A 3   ? 0.2128 0.2915 0.2701 0.0567  0.0348  0.0397  228  PHE A CA  
19   C C   . PHE A 3   ? 0.1665 0.2474 0.2242 0.0547  0.0286  0.0419  228  PHE A C   
20   O O   . PHE A 3   ? 0.2202 0.3052 0.2823 0.0594  0.0277  0.0464  228  PHE A O   
21   C CB  . PHE A 3   ? 0.2014 0.2956 0.2682 0.0560  0.0342  0.0420  228  PHE A CB  
22   C CG  . PHE A 3   ? 0.2023 0.3020 0.2693 0.0482  0.0290  0.0404  228  PHE A CG  
23   C CD1 . PHE A 3   ? 0.1756 0.2691 0.2361 0.0434  0.0300  0.0359  228  PHE A CD1 
24   C CD2 . PHE A 3   ? 0.1701 0.2804 0.2431 0.0455  0.0229  0.0433  228  PHE A CD2 
25   C CE1 . PHE A 3   ? 0.2013 0.2988 0.2617 0.0366  0.0255  0.0346  228  PHE A CE1 
26   C CE2 . PHE A 3   ? 0.1442 0.2580 0.2166 0.0384  0.0184  0.0416  228  PHE A CE2 
27   C CZ  . PHE A 3   ? 0.1690 0.2762 0.2353 0.0341  0.0198  0.0374  228  PHE A CZ  
28   N N   . SER A 4   ? 0.1712 0.2494 0.2240 0.0478  0.0245  0.0388  229  SER A N   
29   C CA  . SER A 4   ? 0.2038 0.2838 0.2558 0.0451  0.0187  0.0402  229  SER A CA  
30   C C   . SER A 4   ? 0.1552 0.2370 0.2049 0.0376  0.0147  0.0370  229  SER A C   
31   O O   . SER A 4   ? 0.1701 0.2494 0.2175 0.0346  0.0165  0.0337  229  SER A O   
32   C CB  . SER A 4   ? 0.2095 0.2768 0.2540 0.0466  0.0197  0.0396  229  SER A CB  
33   O OG  . SER A 4   ? 0.2063 0.2626 0.2427 0.0423  0.0210  0.0345  229  SER A OG  
34   N N   . LEU A 5   ? 0.1687 0.2546 0.2187 0.0347  0.0093  0.0382  230  LEU A N   
35   C CA  . LEU A 5   ? 0.1883 0.2737 0.2348 0.0280  0.0053  0.0352  230  LEU A CA  
36   C C   . LEU A 5   ? 0.1516 0.2293 0.1914 0.0268  0.0032  0.0344  230  LEU A C   
37   O O   . LEU A 5   ? 0.1962 0.2727 0.2356 0.0306  0.0031  0.0373  230  LEU A O   
38   C CB  . LEU A 5   ? 0.1977 0.2959 0.2509 0.0251  0.0007  0.0372  230  LEU A CB  
39   C CG  . LEU A 5   ? 0.1764 0.2828 0.2365 0.0250  0.0027  0.0379  230  LEU A CG  
40   C CD1 . LEU A 5   ? 0.1563 0.2759 0.2239 0.0224  -0.0020 0.0405  230  LEU A CD1 
41   C CD2 . LEU A 5   ? 0.1781 0.2785 0.2337 0.0211  0.0047  0.0337  230  LEU A CD2 
42   N N   . PRO A 6   ? 0.1369 0.2093 0.1712 0.0218  0.0018  0.0308  231  PRO A N   
43   C CA  . PRO A 6   ? 0.1767 0.2420 0.2047 0.0207  0.0004  0.0300  231  PRO A CA  
44   C C   . PRO A 6   ? 0.2228 0.2943 0.2519 0.0204  -0.0043 0.0328  231  PRO A C   
45   O O   . PRO A 6   ? 0.2234 0.3038 0.2565 0.0181  -0.0079 0.0334  231  PRO A O   
46   C CB  . PRO A 6   ? 0.1940 0.2547 0.2176 0.0155  -0.0002 0.0256  231  PRO A CB  
47   C CG  . PRO A 6   ? 0.1607 0.2280 0.1885 0.0133  -0.0008 0.0248  231  PRO A CG  
48   C CD  . PRO A 6   ? 0.1402 0.2127 0.1738 0.0175  0.0019  0.0274  231  PRO A CD  
49   N N   . ASN A 7   ? 0.2070 0.2733 0.2318 0.0224  -0.0043 0.0343  232  ASN A N   
50   C CA  . ASN A 7   ? 0.1641 0.2354 0.1886 0.0227  -0.0085 0.0373  232  ASN A CA  
51   C C   . ASN A 7   ? 0.2297 0.2998 0.2492 0.0175  -0.0119 0.0344  232  ASN A C   
52   O O   . ASN A 7   ? 0.3817 0.4471 0.3955 0.0171  -0.0126 0.0346  232  ASN A O   
53   C CB  . ASN A 7   ? 0.1655 0.2309 0.1868 0.0273  -0.0065 0.0404  232  ASN A CB  
54   C CG  . ASN A 7   ? 0.5412 0.6115 0.5611 0.0281  -0.0108 0.0439  232  ASN A CG  
55   O OD1 . ASN A 7   ? 0.5444 0.6251 0.5684 0.0272  -0.0150 0.0453  232  ASN A OD1 
56   N ND2 . ASN A 7   ? 0.5660 0.6288 0.5798 0.0296  -0.0097 0.0454  232  ASN A ND2 
57   N N   . LEU A 8   ? 0.1788 0.2528 0.2005 0.0135  -0.0135 0.0318  233  LEU A N   
58   C CA  . LEU A 8   ? 0.1856 0.2586 0.2032 0.0087  -0.0165 0.0289  233  LEU A CA  
59   C C   . LEU A 8   ? 0.1977 0.2802 0.2189 0.0064  -0.0211 0.0298  233  LEU A C   
60   O O   . LEU A 8   ? 0.1891 0.2787 0.2170 0.0066  -0.0214 0.0311  233  LEU A O   
61   C CB  . LEU A 8   ? 0.1555 0.2234 0.1716 0.0056  -0.0144 0.0249  233  LEU A CB  
62   C CG  . LEU A 8   ? 0.1754 0.2341 0.1875 0.0064  -0.0105 0.0231  233  LEU A CG  
63   C CD1 . LEU A 8   ? 0.1599 0.2162 0.1719 0.0036  -0.0090 0.0196  233  LEU A CD1 
64   C CD2 . LEU A 8   ? 0.2534 0.3071 0.2596 0.0058  -0.0110 0.0228  233  LEU A CD2 
65   N N   . GLN A 9   ? 0.1525 0.2349 0.1690 0.0039  -0.0247 0.0291  234  GLN A N   
66   C CA  . GLN A 9   ? 0.1393 0.2292 0.1580 0.0004  -0.0294 0.0289  234  GLN A CA  
67   C C   . GLN A 9   ? 0.1345 0.2234 0.1547 -0.0037 -0.0290 0.0256  234  GLN A C   
68   O O   . GLN A 9   ? 0.1444 0.2261 0.1618 -0.0044 -0.0261 0.0229  234  GLN A O   
69   C CB  . GLN A 9   ? 0.2087 0.2972 0.2202 -0.0014 -0.0329 0.0282  234  GLN A CB  
70   C CG  . GLN A 9   ? 0.2420 0.3317 0.2512 0.0026  -0.0337 0.0321  234  GLN A CG  
71   C CD  . GLN A 9   ? 0.3601 0.4477 0.3610 0.0008  -0.0367 0.0312  234  GLN A CD  
72   O OE1 . GLN A 9   ? 0.3241 0.4088 0.3207 -0.0033 -0.0382 0.0275  234  GLN A OE1 
73   N NE2 . GLN A 9   ? 0.2945 0.3829 0.2924 0.0041  -0.0375 0.0348  234  GLN A NE2 
74   N N   . THR A 10  ? 0.1409 0.2375 0.1659 -0.0067 -0.0322 0.0259  235  THR A N   
75   C CA  . THR A 10  ? 0.1315 0.2270 0.1579 -0.0108 -0.0320 0.0232  235  THR A CA  
76   C C   . THR A 10  ? 0.1986 0.2850 0.2172 -0.0134 -0.0320 0.0193  235  THR A C   
77   O O   . THR A 10  ? 0.1489 0.2301 0.1666 -0.0144 -0.0295 0.0172  235  THR A O   
78   C CB  . THR A 10  ? 0.1255 0.2302 0.1575 -0.0144 -0.0358 0.0242  235  THR A CB  
79   O OG1 . THR A 10  ? 0.1579 0.2723 0.1974 -0.0114 -0.0360 0.0283  235  THR A OG1 
80   C CG2 . THR A 10  ? 0.1861 0.2896 0.2207 -0.0180 -0.0345 0.0223  235  THR A CG2 
81   N N   . ASP A 11  ? 0.1407 0.2252 0.1533 -0.0143 -0.0347 0.0186  236  ASP A N   
82   C CA  . ASP A 11  ? 0.1167 0.1928 0.1220 -0.0163 -0.0344 0.0149  236  ASP A CA  
83   C C   . ASP A 11  ? 0.1561 0.2251 0.1578 -0.0134 -0.0304 0.0143  236  ASP A C   
84   O O   . ASP A 11  ? 0.1645 0.2273 0.1609 -0.0145 -0.0296 0.0115  236  ASP A O   
85   C CB  . ASP A 11  ? 0.2098 0.2860 0.2091 -0.0183 -0.0384 0.0140  236  ASP A CB  
86   C CG  . ASP A 11  ? 0.2811 0.3595 0.2778 -0.0150 -0.0392 0.0168  236  ASP A CG  
87   O OD1 . ASP A 11  ? 0.2181 0.2964 0.2170 -0.0110 -0.0363 0.0193  236  ASP A OD1 
88   O OD2 . ASP A 11  ? 0.3577 0.4375 0.3495 -0.0165 -0.0428 0.0165  236  ASP A OD2 
89   N N   . GLU A 12  ? 0.1485 0.2183 0.1529 -0.0098 -0.0277 0.0166  237  GLU A N   
90   C CA  . GLU A 12  ? 0.1594 0.2226 0.1613 -0.0077 -0.0238 0.0158  237  GLU A CA  
91   C C   . GLU A 12  ? 0.1372 0.1991 0.1427 -0.0078 -0.0210 0.0148  237  GLU A C   
92   O O   . GLU A 12  ? 0.1561 0.2131 0.1601 -0.0066 -0.0179 0.0140  237  GLU A O   
93   C CB  . GLU A 12  ? 0.1482 0.2112 0.1496 -0.0039 -0.0224 0.0188  237  GLU A CB  
94   C CG  . GLU A 12  ? 0.1617 0.2251 0.1580 -0.0036 -0.0249 0.0200  237  GLU A CG  
95   C CD  . GLU A 12  ? 0.2763 0.3400 0.2724 0.0005  -0.0239 0.0239  237  GLU A CD  
96   O OE1 . GLU A 12  ? 0.2206 0.2869 0.2221 0.0032  -0.0224 0.0261  237  GLU A OE1 
97   O OE2 . GLU A 12  ? 0.3242 0.3855 0.3146 0.0012  -0.0243 0.0248  237  GLU A OE2 
98   N N   . MET A 13  ? 0.1409 0.2070 0.1509 -0.0097 -0.0220 0.0147  238  MET A N   
99   C CA  . MET A 13  ? 0.1355 0.2010 0.1485 -0.0097 -0.0194 0.0142  238  MET A CA  
100  C C   . MET A 13  ? 0.1319 0.1955 0.1440 -0.0131 -0.0202 0.0119  238  MET A C   
101  O O   . MET A 13  ? 0.1285 0.1910 0.1380 -0.0155 -0.0228 0.0106  238  MET A O   
102  C CB  . MET A 13  ? 0.1312 0.2034 0.1506 -0.0081 -0.0188 0.0168  238  MET A CB  
103  C CG  . MET A 13  ? 0.1168 0.1894 0.1371 -0.0038 -0.0168 0.0191  238  MET A CG  
104  S SD  . MET A 13  ? 0.1451 0.2249 0.1731 -0.0008 -0.0148 0.0221  238  MET A SD  
105  C CE  . MET A 13  ? 0.1449 0.2352 0.1780 -0.0023 -0.0195 0.0247  238  MET A CE  
106  N N   . SER A 14  ? 0.1256 0.1883 0.1395 -0.0132 -0.0179 0.0114  239  SER A N   
107  C CA  . SER A 14  ? 0.1038 0.1632 0.1162 -0.0155 -0.0179 0.0096  239  SER A CA  
108  C C   . SER A 14  ? 0.1134 0.1766 0.1301 -0.0171 -0.0176 0.0107  239  SER A C   
109  O O   . SER A 14  ? 0.1243 0.1916 0.1448 -0.0155 -0.0159 0.0125  239  SER A O   
110  C CB  . SER A 14  ? 0.1165 0.1710 0.1260 -0.0143 -0.0154 0.0081  239  SER A CB  
111  O OG  . SER A 14  ? 0.1826 0.2341 0.1888 -0.0129 -0.0150 0.0075  239  SER A OG  
112  N N   . SER A 15  ? 0.1115 0.1728 0.1274 -0.0200 -0.0189 0.0098  240  SER A N   
113  C CA  . SER A 15  ? 0.1128 0.1766 0.1322 -0.0217 -0.0180 0.0109  240  SER A CA  
114  C C   . SER A 15  ? 0.1353 0.1971 0.1537 -0.0199 -0.0148 0.0109  240  SER A C   
115  O O   . SER A 15  ? 0.1498 0.2069 0.1643 -0.0187 -0.0140 0.0093  240  SER A O   
116  C CB  . SER A 15  ? 0.1417 0.2022 0.1596 -0.0253 -0.0199 0.0100  240  SER A CB  
117  O OG  . SER A 15  ? 0.1284 0.1899 0.1489 -0.0269 -0.0185 0.0112  240  SER A OG  
118  N N   . SER A 16  ? 0.1267 0.1927 0.1489 -0.0199 -0.0130 0.0127  241  SER A N   
119  C CA  . SER A 16  ? 0.1107 0.1750 0.1313 -0.0186 -0.0101 0.0127  241  SER A CA  
120  C C   . SER A 16  ? 0.1107 0.1736 0.1308 -0.0211 -0.0099 0.0132  241  SER A C   
121  O O   . SER A 16  ? 0.1441 0.2060 0.1625 -0.0204 -0.0077 0.0135  241  SER A O   
122  C CB  . SER A 16  ? 0.1009 0.1701 0.1249 -0.0163 -0.0073 0.0142  241  SER A CB  
123  O OG  . SER A 16  ? 0.1005 0.1764 0.1304 -0.0178 -0.0078 0.0165  241  SER A OG  
124  N N   . ARG A 17  ? 0.1099 0.1720 0.1308 -0.0241 -0.0123 0.0134  242  ARG A N   
125  C CA  . ARG A 17  ? 0.1051 0.1639 0.1247 -0.0264 -0.0121 0.0140  242  ARG A CA  
126  C C   . ARG A 17  ? 0.1386 0.1905 0.1539 -0.0272 -0.0139 0.0122  242  ARG A C   
127  O O   . ARG A 17  ? 0.1454 0.1933 0.1587 -0.0281 -0.0135 0.0128  242  ARG A O   
128  C CB  . ARG A 17  ? 0.1462 0.2094 0.1708 -0.0298 -0.0124 0.0160  242  ARG A CB  
129  C CG  . ARG A 17  ? 0.1134 0.1833 0.1422 -0.0289 -0.0095 0.0184  242  ARG A CG  
130  C CD  . ARG A 17  ? 0.1093 0.1839 0.1435 -0.0327 -0.0095 0.0208  242  ARG A CD  
131  N NE  . ARG A 17  ? 0.1155 0.1849 0.1473 -0.0355 -0.0091 0.0216  242  ARG A NE  
132  C CZ  . ARG A 17  ? 0.1208 0.1882 0.1539 -0.0398 -0.0111 0.0218  242  ARG A CZ  
133  N NH1 . ARG A 17  ? 0.1326 0.2033 0.1691 -0.0423 -0.0140 0.0212  242  ARG A NH1 
134  N NH2 . ARG A 17  ? 0.1397 0.2016 0.1703 -0.0419 -0.0101 0.0230  242  ARG A NH2 
135  N N   . TRP A 18  ? 0.1135 0.1636 0.1270 -0.0264 -0.0156 0.0103  243  TRP A N   
136  C CA  . TRP A 18  ? 0.1439 0.1875 0.1532 -0.0263 -0.0167 0.0085  243  TRP A CA  
137  C C   . TRP A 18  ? 0.1208 0.1643 0.1282 -0.0240 -0.0171 0.0068  243  TRP A C   
138  O O   . TRP A 18  ? 0.1976 0.2443 0.2065 -0.0241 -0.0181 0.0067  243  TRP A O   
139  C CB  . TRP A 18  ? 0.1222 0.1625 0.1309 -0.0295 -0.0188 0.0078  243  TRP A CB  
140  C CG  . TRP A 18  ? 0.1288 0.1615 0.1330 -0.0288 -0.0189 0.0063  243  TRP A CG  
141  C CD1 . TRP A 18  ? 0.1593 0.1887 0.1602 -0.0275 -0.0197 0.0040  243  TRP A CD1 
142  C CD2 . TRP A 18  ? 0.1220 0.1497 0.1246 -0.0288 -0.0180 0.0071  243  TRP A CD2 
143  N NE1 . TRP A 18  ? 0.1750 0.1979 0.1727 -0.0266 -0.0192 0.0033  243  TRP A NE1 
144  C CE2 . TRP A 18  ? 0.1184 0.1400 0.1171 -0.0272 -0.0182 0.0053  243  TRP A CE2 
145  C CE3 . TRP A 18  ? 0.1437 0.1715 0.1475 -0.0298 -0.0167 0.0096  243  TRP A CE3 
146  C CZ2 . TRP A 18  ? 0.1241 0.1397 0.1206 -0.0262 -0.0174 0.0059  243  TRP A CZ2 
147  C CZ3 . TRP A 18  ? 0.1724 0.1940 0.1734 -0.0291 -0.0160 0.0103  243  TRP A CZ3 
148  C CH2 . TRP A 18  ? 0.1741 0.1898 0.1718 -0.0271 -0.0165 0.0085  243  TRP A CH2 
149  N N   . PRO A 19  ? 0.1312 0.1717 0.1358 -0.0219 -0.0162 0.0057  244  PRO A N   
150  C CA  . PRO A 19  ? 0.1710 0.2117 0.1742 -0.0200 -0.0161 0.0044  244  PRO A CA  
151  C C   . PRO A 19  ? 0.2514 0.2898 0.2526 -0.0207 -0.0178 0.0030  244  PRO A C   
152  O O   . PRO A 19  ? 0.2442 0.2781 0.2426 -0.0206 -0.0180 0.0018  244  PRO A O   
153  C CB  . PRO A 19  ? 0.1941 0.2326 0.1953 -0.0183 -0.0150 0.0037  244  PRO A CB  
154  C CG  . PRO A 19  ? 0.2235 0.2616 0.2251 -0.0189 -0.0144 0.0051  244  PRO A CG  
155  C CD  . PRO A 19  ? 0.1431 0.1803 0.1458 -0.0213 -0.0154 0.0060  244  PRO A CD  
156  N N   . ASN A 20  ? 0.1322 0.1737 0.1344 -0.0212 -0.0189 0.0034  245  ASN A N   
157  C CA  . ASN A 20  ? 0.1164 0.1563 0.1159 -0.0220 -0.0207 0.0021  245  ASN A CA  
158  C C   . ASN A 20  ? 0.1710 0.2161 0.1725 -0.0219 -0.0218 0.0034  245  ASN A C   
159  O O   . ASN A 20  ? 0.1472 0.1970 0.1529 -0.0217 -0.0213 0.0052  245  ASN A O   
160  C CB  . ASN A 20  ? 0.2003 0.2368 0.1984 -0.0249 -0.0224 0.0012  245  ASN A CB  
161  C CG  . ASN A 20  ? 0.2475 0.2772 0.2410 -0.0241 -0.0219 -0.0009 245  ASN A CG  
162  O OD1 . ASN A 20  ? 0.2283 0.2570 0.2197 -0.0218 -0.0207 -0.0018 245  ASN A OD1 
163  N ND2 . ASN A 20  ? 0.2482 0.2732 0.2404 -0.0261 -0.0225 -0.0017 245  ASN A ND2 
164  N N   . PRO A 21  ? 0.1522 0.1967 0.1506 -0.0216 -0.0232 0.0026  246  PRO A N   
165  C CA  . PRO A 21  ? 0.1151 0.1649 0.1152 -0.0212 -0.0246 0.0042  246  PRO A CA  
166  C C   . PRO A 21  ? 0.1521 0.2065 0.1557 -0.0241 -0.0271 0.0052  246  PRO A C   
167  O O   . PRO A 21  ? 0.1745 0.2265 0.1769 -0.0272 -0.0287 0.0038  246  PRO A O   
168  C CB  . PRO A 21  ? 0.1550 0.2022 0.1495 -0.0208 -0.0257 0.0030  246  PRO A CB  
169  C CG  . PRO A 21  ? 0.2465 0.2876 0.2372 -0.0201 -0.0238 0.0009  246  PRO A CG  
170  C CD  . PRO A 21  ? 0.1764 0.2156 0.1692 -0.0213 -0.0232 0.0004  246  PRO A CD  
171  N N   . LEU A 22  ? 0.1352 0.1964 0.1436 -0.0231 -0.0275 0.0077  247  LEU A N   
172  C CA  . LEU A 22  ? 0.1382 0.2056 0.1508 -0.0258 -0.0302 0.0090  247  LEU A CA  
173  C C   . LEU A 22  ? 0.1806 0.2475 0.1891 -0.0282 -0.0339 0.0077  247  LEU A C   
174  O O   . LEU A 22  ? 0.1884 0.2543 0.1927 -0.0263 -0.0345 0.0075  247  LEU A O   
175  C CB  . LEU A 22  ? 0.1382 0.2137 0.1569 -0.0235 -0.0297 0.0123  247  LEU A CB  
176  C CG  . LEU A 22  ? 0.1093 0.1854 0.1317 -0.0214 -0.0259 0.0134  247  LEU A CG  
177  C CD1 . LEU A 22  ? 0.1469 0.2304 0.1750 -0.0184 -0.0249 0.0165  247  LEU A CD1 
178  C CD2 . LEU A 22  ? 0.1371 0.2130 0.1619 -0.0246 -0.0255 0.0131  247  LEU A CD2 
179  N N   . ALA A 23  ? 0.1296 0.1970 0.1389 -0.0326 -0.0364 0.0067  248  ALA A N   
180  C CA  . ALA A 23  ? 0.1871 0.2536 0.1919 -0.0357 -0.0403 0.0049  248  ALA A CA  
181  C C   . ALA A 23  ? 0.2001 0.2755 0.2100 -0.0393 -0.0442 0.0064  248  ALA A C   
182  O O   . ALA A 23  ? 0.2095 0.2866 0.2160 -0.0411 -0.0479 0.0056  248  ALA A O   
183  C CB  . ALA A 23  ? 0.2270 0.2839 0.2260 -0.0386 -0.0402 0.0013  248  ALA A CB  
184  N N   A THR A 24  ? 0.1718 0.2532 0.1897 -0.0405 -0.0434 0.0087  249  THR A N   
185  N N   B THR A 24  ? 0.1718 0.2534 0.1898 -0.0403 -0.0434 0.0088  249  THR A N   
186  C CA  A THR A 24  ? 0.1523 0.2438 0.1768 -0.0439 -0.0469 0.0106  249  THR A CA  
187  C CA  B THR A 24  ? 0.1527 0.2441 0.1771 -0.0440 -0.0469 0.0106  249  THR A CA  
188  C C   A THR A 24  ? 0.1697 0.2707 0.2034 -0.0409 -0.0447 0.0146  249  THR A C   
189  C C   B THR A 24  ? 0.1693 0.2702 0.2032 -0.0412 -0.0448 0.0146  249  THR A C   
190  O O   A THR A 24  ? 0.1494 0.2478 0.1842 -0.0375 -0.0404 0.0154  249  THR A O   
191  O O   B THR A 24  ? 0.1553 0.2537 0.1906 -0.0382 -0.0404 0.0153  249  THR A O   
192  C CB  A THR A 24  ? 0.1793 0.2687 0.2046 -0.0505 -0.0487 0.0089  249  THR A CB  
193  C CB  B THR A 24  ? 0.1800 0.2683 0.2047 -0.0504 -0.0484 0.0086  249  THR A CB  
194  O OG1 A THR A 24  ? 0.1645 0.2496 0.1921 -0.0504 -0.0447 0.0092  249  THR A OG1 
195  O OG1 B THR A 24  ? 0.3073 0.3841 0.3224 -0.0519 -0.0490 0.0046  249  THR A OG1 
196  C CG2 A THR A 24  ? 0.2707 0.3508 0.2866 -0.0536 -0.0511 0.0047  249  THR A CG2 
197  C CG2 B THR A 24  ? 0.1231 0.2213 0.1531 -0.0552 -0.0531 0.0098  249  THR A CG2 
198  N N   . LEU A 25  ? 0.1579 0.2701 0.1979 -0.0422 -0.0479 0.0172  250  LEU A N   
199  C CA  . LEU A 25  ? 0.1273 0.2502 0.1772 -0.0394 -0.0461 0.0213  250  LEU A CA  
200  C C   . LEU A 25  ? 0.1555 0.2888 0.2129 -0.0449 -0.0498 0.0227  250  LEU A C   
201  O O   . LEU A 25  ? 0.1620 0.3004 0.2188 -0.0472 -0.0548 0.0227  250  LEU A O   
202  C CB  . LEU A 25  ? 0.1603 0.2876 0.2106 -0.0334 -0.0459 0.0238  250  LEU A CB  
203  C CG  . LEU A 25  ? 0.1509 0.2890 0.2110 -0.0295 -0.0439 0.0282  250  LEU A CG  
204  C CD1 . LEU A 25  ? 0.1589 0.2926 0.2204 -0.0269 -0.0379 0.0282  250  LEU A CD1 
205  C CD2 . LEU A 25  ? 0.1526 0.2936 0.2118 -0.0239 -0.0446 0.0307  250  LEU A CD2 
206  N N   . PHE A 26  ? 0.1335 0.2698 0.1974 -0.0474 -0.0476 0.0239  251  PHE A N   
207  C CA  . PHE A 26  ? 0.1340 0.2791 0.2046 -0.0539 -0.0512 0.0247  251  PHE A CA  
208  C C   . PHE A 26  ? 0.1447 0.2980 0.2257 -0.0542 -0.0477 0.0280  251  PHE A C   
209  O O   . PHE A 26  ? 0.1305 0.2798 0.2114 -0.0504 -0.0424 0.0287  251  PHE A O   
210  C CB  . PHE A 26  ? 0.1870 0.3222 0.2508 -0.0607 -0.0537 0.0206  251  PHE A CB  
211  C CG  . PHE A 26  ? 0.1681 0.2925 0.2288 -0.0615 -0.0493 0.0191  251  PHE A CG  
212  C CD1 . PHE A 26  ? 0.2294 0.3422 0.2819 -0.0571 -0.0461 0.0170  251  PHE A CD1 
213  C CD2 . PHE A 26  ? 0.1491 0.2752 0.2152 -0.0667 -0.0484 0.0200  251  PHE A CD2 
214  C CE1 . PHE A 26  ? 0.1778 0.2813 0.2276 -0.0576 -0.0424 0.0160  251  PHE A CE1 
215  C CE2 . PHE A 26  ? 0.2194 0.3355 0.2823 -0.0672 -0.0444 0.0191  251  PHE A CE2 
216  C CZ  . PHE A 26  ? 0.1634 0.2683 0.2180 -0.0624 -0.0416 0.0171  251  PHE A CZ  
217  N N   . ALA A 27  ? 0.1616 0.3237 0.2497 -0.0579 -0.0499 0.0295  252  ALA A N   
218  C CA  . ALA A 27  ? 0.1688 0.3384 0.2664 -0.0589 -0.0465 0.0324  252  ALA A CA  
219  C C   . ALA A 27  ? 0.1835 0.3502 0.2814 -0.0667 -0.0484 0.0306  252  ALA A C   
220  O O   . ALA A 27  ? 0.1950 0.3630 0.2917 -0.0700 -0.0530 0.0291  252  ALA A O   
221  C CB  . ALA A 27  ? 0.1735 0.3565 0.2802 -0.0544 -0.0461 0.0364  252  ALA A CB  
222  N N   . ASP A 28  ? 0.1872 0.3500 0.2863 -0.0698 -0.0450 0.0309  253  ASP A N   
223  C CA  . ASP A 28  ? 0.1677 0.3268 0.2672 -0.0774 -0.0461 0.0295  253  ASP A CA  
224  C C   . ASP A 28  ? 0.1560 0.3239 0.2656 -0.0784 -0.0423 0.0332  253  ASP A C   
225  O O   . ASP A 28  ? 0.2001 0.3656 0.3105 -0.0776 -0.0376 0.0348  253  ASP A O   
226  C CB  . ASP A 28  ? 0.2293 0.3736 0.3200 -0.0809 -0.0455 0.0264  253  ASP A CB  
227  C CG  . ASP A 28  ? 0.2193 0.3576 0.3088 -0.0888 -0.0472 0.0244  253  ASP A CG  
228  O OD1 . ASP A 28  ? 0.3632 0.5097 0.4604 -0.0920 -0.0477 0.0261  253  ASP A OD1 
229  O OD2 . ASP A 28  ? 0.4965 0.6216 0.5774 -0.0918 -0.0480 0.0212  253  ASP A OD2 
230  N N   . PRO A 29  ? 0.2108 0.3889 0.3280 -0.0803 -0.0442 0.0347  254  PRO A N   
231  C CA  . PRO A 29  ? 0.2028 0.3904 0.3302 -0.0809 -0.0403 0.0384  254  PRO A CA  
232  C C   . PRO A 29  ? 0.2711 0.4530 0.3988 -0.0881 -0.0388 0.0380  254  PRO A C   
233  O O   . PRO A 29  ? 0.3014 0.4904 0.4370 -0.0888 -0.0352 0.0411  254  PRO A O   
234  C CB  . PRO A 29  ? 0.2236 0.4240 0.3586 -0.0806 -0.0437 0.0400  254  PRO A CB  
235  C CG  . PRO A 29  ? 0.2165 0.4112 0.3444 -0.0844 -0.0500 0.0361  254  PRO A CG  
236  C CD  . PRO A 29  ? 0.2026 0.3843 0.3193 -0.0822 -0.0500 0.0331  254  PRO A CD  
237  N N   . ASN A 30  ? 0.1834 0.3525 0.3027 -0.0931 -0.0412 0.0343  255  ASN A N   
238  C CA  . ASN A 30  ? 0.2354 0.3978 0.3545 -0.1002 -0.0401 0.0338  255  ASN A CA  
239  C C   . ASN A 30  ? 0.2690 0.4179 0.3805 -0.1007 -0.0368 0.0331  255  ASN A C   
240  O O   . ASN A 30  ? 0.3781 0.5163 0.4852 -0.1065 -0.0373 0.0312  255  ASN A O   
241  C CB  . ASN A 30  ? 0.2630 0.4211 0.3791 -0.1068 -0.0455 0.0302  255  ASN A CB  
242  C CG  . ASN A 30  ? 0.3048 0.4765 0.4285 -0.1071 -0.0491 0.0311  255  ASN A CG  
243  O OD1 . ASN A 30  ? 0.4861 0.6572 0.6057 -0.1076 -0.0542 0.0283  255  ASN A OD1 
244  N ND2 . ASN A 30  ? 0.2692 0.4534 0.4038 -0.1067 -0.0465 0.0350  255  ASN A ND2 
245  N N   . VAL A 31  ? 0.2566 0.4055 0.3665 -0.0946 -0.0335 0.0346  256  VAL A N   
246  C CA  . VAL A 31  ? 0.2689 0.4063 0.3723 -0.0948 -0.0302 0.0345  256  VAL A CA  
247  C C   . VAL A 31  ? 0.2959 0.4352 0.4043 -0.0972 -0.0252 0.0381  256  VAL A C   
248  O O   . VAL A 31  ? 0.3409 0.4923 0.4579 -0.0954 -0.0227 0.0413  256  VAL A O   
249  C CB  . VAL A 31  ? 0.1701 0.3073 0.2699 -0.0878 -0.0286 0.0348  256  VAL A CB  
250  C CG1 . VAL A 31  ? 0.2996 0.4220 0.3902 -0.0859 -0.0249 0.0338  256  VAL A CG1 
251  C CG2 . VAL A 31  ? 0.2250 0.3607 0.3199 -0.0856 -0.0334 0.0314  256  VAL A CG2 
252  N N   . ALA A 32  ? 0.3120 0.4389 0.4147 -0.1012 -0.0236 0.0378  257  ALA A N   
253  C CA  . ALA A 32  ? 0.3352 0.4622 0.4418 -0.1047 -0.0193 0.0411  257  ALA A CA  
254  C C   . ALA A 32  ? 0.2904 0.4254 0.4010 -0.0995 -0.0135 0.0452  257  ALA A C   
255  O O   . ALA A 32  ? 0.4018 0.5452 0.5198 -0.1005 -0.0103 0.0483  257  ALA A O   
256  C CB  . ALA A 32  ? 0.4361 0.5466 0.5346 -0.1092 -0.0187 0.0401  257  ALA A CB  
257  N N   . VAL A 33  ? 0.3238 0.4566 0.4296 -0.0940 -0.0119 0.0453  258  VAL A N   
258  C CA  . VAL A 33  ? 0.2948 0.4321 0.4015 -0.0881 -0.0059 0.0483  258  VAL A CA  
259  C C   . VAL A 33  ? 0.1918 0.3303 0.2950 -0.0795 -0.0060 0.0463  258  VAL A C   
260  O O   . VAL A 33  ? 0.2884 0.4206 0.3858 -0.0778 -0.0100 0.0427  258  VAL A O   
261  C CB  . VAL A 33  ? 0.5153 0.6401 0.6142 -0.0884 -0.0018 0.0495  258  VAL A CB  
262  C CG1 . VAL A 33  ? 0.4956 0.6038 0.5830 -0.0876 -0.0045 0.0457  258  VAL A CG1 
263  C CG2 . VAL A 33  ? 0.4453 0.5732 0.5428 -0.0819 0.0042  0.0520  258  VAL A CG2 
264  N N   . ALA A 34  ? 0.1992 0.3465 0.3064 -0.0744 -0.0015 0.0489  259  ALA A N   
265  C CA  . ALA A 34  ? 0.1923 0.3405 0.2964 -0.0663 -0.0009 0.0473  259  ALA A CA  
266  C C   . ALA A 34  ? 0.1953 0.3287 0.2868 -0.0625 0.0000  0.0445  259  ALA A C   
267  O O   . ALA A 34  ? 0.1925 0.3184 0.2790 -0.0638 0.0028  0.0455  259  ALA A O   
268  C CB  . ALA A 34  ? 0.2146 0.3742 0.3252 -0.0618 0.0045  0.0505  259  ALA A CB  
269  N N   . PRO A 35  ? 0.1184 0.2479 0.2049 -0.0579 -0.0023 0.0414  260  PRO A N   
270  C CA  . PRO A 35  ? 0.1076 0.2244 0.1831 -0.0544 -0.0016 0.0389  260  PRO A CA  
271  C C   . PRO A 35  ? 0.1486 0.2660 0.2213 -0.0490 0.0036  0.0400  260  PRO A C   
272  O O   . PRO A 35  ? 0.1276 0.2542 0.2058 -0.0459 0.0063  0.0415  260  PRO A O   
273  C CB  . PRO A 35  ? 0.1759 0.2902 0.2484 -0.0518 -0.0058 0.0355  260  PRO A CB  
274  C CG  . PRO A 35  ? 0.1470 0.2744 0.2285 -0.0502 -0.0062 0.0371  260  PRO A CG  
275  C CD  . PRO A 35  ? 0.1691 0.3059 0.2599 -0.0556 -0.0055 0.0404  260  PRO A CD  
276  N N   . GLN A 36  ? 0.1219 0.2291 0.1858 -0.0478 0.0050  0.0391  261  GLN A N   
277  C CA  . GLN A 36  ? 0.1352 0.2411 0.1941 -0.0429 0.0094  0.0394  261  GLN A CA  
278  C C   . GLN A 36  ? 0.1121 0.2081 0.1616 -0.0395 0.0077  0.0360  261  GLN A C   
279  O O   . GLN A 36  ? 0.1582 0.2480 0.2005 -0.0380 0.0096  0.0360  261  GLN A O   
280  C CB  . GLN A 36  ? 0.1935 0.2986 0.2510 -0.0449 0.0134  0.0426  261  GLN A CB  
281  C CG  . GLN A 36  ? 0.1902 0.2972 0.2443 -0.0402 0.0185  0.0433  261  GLN A CG  
282  C CD  . GLN A 36  ? 0.1825 0.2896 0.2350 -0.0420 0.0229  0.0468  261  GLN A CD  
283  O OE1 . GLN A 36  ? 0.2161 0.3219 0.2707 -0.0471 0.0224  0.0492  261  GLN A OE1 
284  N NE2 . GLN A 36  ? 0.1864 0.2947 0.2347 -0.0380 0.0275  0.0472  261  GLN A NE2 
285  N N   . TRP A 37  ? 0.1231 0.2183 0.1728 -0.0382 0.0042  0.0334  262  TRP A N   
286  C CA  . TRP A 37  ? 0.1193 0.2065 0.1614 -0.0352 0.0024  0.0302  262  TRP A CA  
287  C C   . TRP A 37  ? 0.1097 0.1955 0.1468 -0.0307 0.0058  0.0296  262  TRP A C   
288  O O   . TRP A 37  ? 0.1436 0.2353 0.1834 -0.0283 0.0091  0.0306  262  TRP A O   
289  C CB  . TRP A 37  ? 0.1213 0.2103 0.1656 -0.0341 -0.0009 0.0280  262  TRP A CB  
290  C CG  . TRP A 37  ? 0.1355 0.2262 0.1841 -0.0387 -0.0047 0.0282  262  TRP A CG  
291  C CD1 . TRP A 37  ? 0.1335 0.2195 0.1812 -0.0433 -0.0062 0.0285  262  TRP A CD1 
292  C CD2 . TRP A 37  ? 0.1056 0.2028 0.1596 -0.0392 -0.0076 0.0279  262  TRP A CD2 
293  N NE1 . TRP A 37  ? 0.1472 0.2360 0.1990 -0.0471 -0.0098 0.0280  262  TRP A NE1 
294  C CE2 . TRP A 37  ? 0.1251 0.2213 0.1809 -0.0446 -0.0109 0.0277  262  TRP A CE2 
295  C CE3 . TRP A 37  ? 0.1163 0.2197 0.1736 -0.0355 -0.0076 0.0279  262  TRP A CE3 
296  C CZ2 . TRP A 37  ? 0.1739 0.2759 0.2343 -0.0468 -0.0146 0.0274  262  TRP A CZ2 
297  C CZ3 . TRP A 37  ? 0.1090 0.2184 0.1712 -0.0371 -0.0113 0.0281  262  TRP A CZ3 
298  C CH2 . TRP A 37  ? 0.1315 0.2404 0.1950 -0.0429 -0.0149 0.0278  262  TRP A CH2 
299  N N   . GLN A 38  ? 0.1032 0.1809 0.1325 -0.0297 0.0052  0.0280  263  GLN A N   
300  C CA  . GLN A 38  ? 0.1553 0.2311 0.1788 -0.0261 0.0077  0.0270  263  GLN A CA  
301  C C   . GLN A 38  ? 0.1009 0.1735 0.1213 -0.0232 0.0060  0.0236  263  GLN A C   
302  O O   . GLN A 38  ? 0.1085 0.1804 0.1251 -0.0203 0.0081  0.0223  263  GLN A O   
303  C CB  . GLN A 38  ? 0.1259 0.1961 0.1428 -0.0268 0.0083  0.0279  263  GLN A CB  
304  C CG  . GLN A 38  ? 0.1438 0.2165 0.1628 -0.0295 0.0110  0.0316  263  GLN A CG  
305  C CD  . GLN A 38  ? 0.1424 0.2224 0.1645 -0.0280 0.0154  0.0330  263  GLN A CD  
306  O OE1 . GLN A 38  ? 0.1272 0.2066 0.1442 -0.0248 0.0180  0.0319  263  GLN A OE1 
307  N NE2 . GLN A 38  ? 0.1238 0.2107 0.1541 -0.0303 0.0164  0.0353  263  GLN A NE2 
308  N N   . ASN A 39  ? 0.0986 0.1690 0.1201 -0.0242 0.0023  0.0222  264  ASN A N   
309  C CA  . ASN A 39  ? 0.1066 0.1750 0.1262 -0.0217 0.0009  0.0194  264  ASN A CA  
310  C C   . ASN A 39  ? 0.1215 0.1952 0.1471 -0.0211 0.0002  0.0197  264  ASN A C   
311  O O   . ASN A 39  ? 0.1354 0.2142 0.1667 -0.0233 -0.0004 0.0216  264  ASN A O   
312  C CB  . ASN A 39  ? 0.1352 0.1976 0.1514 -0.0227 -0.0024 0.0178  264  ASN A CB  
313  C CG  . ASN A 39  ? 0.1441 0.2017 0.1544 -0.0223 -0.0020 0.0176  264  ASN A CG  
314  O OD1 . ASN A 39  ? 0.1448 0.2026 0.1518 -0.0205 0.0001  0.0173  264  ASN A OD1 
315  N ND2 . ASN A 39  ? 0.1493 0.2027 0.1581 -0.0239 -0.0039 0.0180  264  ASN A ND2 
316  N N   . GLY A 40  ? 0.0988 0.1714 0.1230 -0.0183 0.0001  0.0178  265  GLY A N   
317  C CA  . GLY A 40  ? 0.1265 0.2039 0.1557 -0.0170 -0.0005 0.0184  265  GLY A CA  
318  C C   . GLY A 40  ? 0.1499 0.2340 0.1840 -0.0152 0.0028  0.0206  265  GLY A C   
319  O O   . GLY A 40  ? 0.1256 0.2163 0.1662 -0.0151 0.0019  0.0223  265  GLY A O   
320  N N   . ARG A 41  ? 0.1075 0.1905 0.1388 -0.0135 0.0066  0.0205  266  ARG A N   
321  C CA  . ARG A 41  ? 0.0941 0.1834 0.1297 -0.0115 0.0106  0.0226  266  ARG A CA  
322  C C   . ARG A 41  ? 0.1277 0.2135 0.1592 -0.0072 0.0140  0.0208  266  ARG A C   
323  O O   . ARG A 41  ? 0.1306 0.2100 0.1547 -0.0069 0.0150  0.0186  266  ARG A O   
324  C CB  . ARG A 41  ? 0.1253 0.2163 0.1606 -0.0137 0.0129  0.0244  266  ARG A CB  
325  C CG  . ARG A 41  ? 0.1565 0.2491 0.1950 -0.0186 0.0099  0.0260  266  ARG A CG  
326  C CD  . ARG A 41  ? 0.1385 0.2401 0.1865 -0.0200 0.0089  0.0285  266  ARG A CD  
327  N NE  . ARG A 41  ? 0.1291 0.2387 0.1825 -0.0182 0.0132  0.0310  266  ARG A NE  
328  C CZ  . ARG A 41  ? 0.1430 0.2569 0.1995 -0.0206 0.0157  0.0336  266  ARG A CZ  
329  N NH1 . ARG A 41  ? 0.1423 0.2525 0.1965 -0.0250 0.0143  0.0342  266  ARG A NH1 
330  N NH2 . ARG A 41  ? 0.1505 0.2725 0.2125 -0.0184 0.0200  0.0360  266  ARG A NH2 
331  N N   . CYS A 42  ? 0.1367 0.2268 0.1730 -0.0038 0.0158  0.0219  267  CYS A N   
332  C CA  . CYS A 42  ? 0.1256 0.2113 0.1580 0.0006  0.0192  0.0202  267  CYS A CA  
333  C C   . CYS A 42  ? 0.1659 0.2589 0.2056 0.0045  0.0222  0.0228  267  CYS A C   
334  O O   . CYS A 42  ? 0.1228 0.2227 0.1699 0.0041  0.0197  0.0252  267  CYS A O   
335  C CB  . CYS A 42  ? 0.1308 0.2096 0.1591 0.0011  0.0166  0.0178  267  CYS A CB  
336  S SG  . CYS A 42  ? 0.1560 0.2264 0.1777 0.0052  0.0205  0.0149  267  CYS A SG  
337  N N   . THR A 43  ? 0.1074 0.1989 0.1449 0.0082  0.0275  0.0223  268  THR A N   
338  C CA  . THR A 43  ? 0.1093 0.2072 0.1538 0.0129  0.0308  0.0248  268  THR A CA  
339  C C   . THR A 43  ? 0.1429 0.2362 0.1866 0.0165  0.0301  0.0240  268  THR A C   
340  O O   . THR A 43  ? 0.1525 0.2367 0.1892 0.0156  0.0283  0.0210  268  THR A O   
341  C CB  . THR A 43  ? 0.1461 0.2435 0.1881 0.0162  0.0374  0.0244  268  THR A CB  
342  O OG1 . THR A 43  ? 0.1561 0.2420 0.1883 0.0182  0.0395  0.0205  268  THR A OG1 
343  C CG2 . THR A 43  ? 0.1285 0.2287 0.1691 0.0125  0.0384  0.0251  268  THR A CG2 
344  N N   . LEU A 44  ? 0.1521 0.2522 0.2034 0.0209  0.0317  0.0270  269  LEU A N   
345  C CA  . LEU A 44  ? 0.1369 0.2327 0.1877 0.0248  0.0312  0.0270  269  LEU A CA  
346  C C   . LEU A 44  ? 0.1715 0.2552 0.2135 0.0278  0.0355  0.0236  269  LEU A C   
347  O O   . LEU A 44  ? 0.1801 0.2561 0.2182 0.0291  0.0345  0.0223  269  LEU A O   
348  C CB  . LEU A 44  ? 0.1499 0.2560 0.2109 0.0294  0.0323  0.0315  269  LEU A CB  
349  C CG  . LEU A 44  ? 0.2185 0.3377 0.2890 0.0260  0.0278  0.0349  269  LEU A CG  
350  C CD1 . LEU A 44  ? 0.1714 0.3011 0.2520 0.0307  0.0278  0.0394  269  LEU A CD1 
351  C CD2 . LEU A 44  ? 0.1938 0.3104 0.2613 0.0203  0.0214  0.0335  269  LEU A CD2 
352  N N   . GLU A 45  ? 0.1867 0.2683 0.2249 0.0287  0.0404  0.0220  270  GLU A N   
353  C CA  . GLU A 45  ? 0.1719 0.2415 0.2005 0.0308  0.0445  0.0181  270  GLU A CA  
354  C C   . GLU A 45  ? 0.2104 0.2713 0.2295 0.0257  0.0418  0.0139  270  GLU A C   
355  O O   . GLU A 45  ? 0.2770 0.3287 0.2875 0.0262  0.0448  0.0102  270  GLU A O   
356  C CB  . GLU A 45  ? 0.2131 0.2843 0.2412 0.0344  0.0511  0.0181  270  GLU A CB  
357  C CG  . GLU A 45  ? 0.1781 0.2584 0.2163 0.0403  0.0544  0.0224  270  GLU A CG  
358  C CD  . GLU A 45  ? 0.2244 0.3044 0.2611 0.0450  0.0621  0.0221  270  GLU A CD  
359  O OE1 . GLU A 45  ? 0.4029 0.4780 0.4315 0.0429  0.0646  0.0190  270  GLU A OE1 
360  O OE2 . GLU A 45  ? 0.2640 0.3490 0.3078 0.0511  0.0658  0.0250  270  GLU A OE2 
361  N N   . GLY A 46  ? 0.1746 0.2385 0.1950 0.0208  0.0362  0.0144  271  GLY A N   
362  C CA  . GLY A 46  ? 0.1320 0.1885 0.1447 0.0165  0.0332  0.0109  271  GLY A CA  
363  C C   . GLY A 46  ? 0.1884 0.2445 0.1959 0.0134  0.0338  0.0094  271  GLY A C   
364  O O   . GLY A 46  ? 0.1764 0.2255 0.1762 0.0109  0.0327  0.0060  271  GLY A O   
365  N N   . GLU A 47  ? 0.1340 0.1977 0.1455 0.0133  0.0354  0.0118  272  GLU A N   
366  C CA  . GLU A 47  ? 0.1394 0.2030 0.1459 0.0103  0.0358  0.0110  272  GLU A CA  
367  C C   . GLU A 47  ? 0.1197 0.1878 0.1297 0.0059  0.0309  0.0129  272  GLU A C   
368  O O   . GLU A 47  ? 0.1468 0.2229 0.1649 0.0053  0.0300  0.0163  272  GLU A O   
369  C CB  . GLU A 47  ? 0.1909 0.2592 0.1988 0.0128  0.0414  0.0127  272  GLU A CB  
370  C CG  . GLU A 47  ? 0.1982 0.2604 0.2011 0.0174  0.0468  0.0103  272  GLU A CG  
371  C CD  . GLU A 47  ? 0.4724 0.5383 0.4749 0.0199  0.0527  0.0114  272  GLU A CD  
372  O OE1 . GLU A 47  ? 0.5749 0.6416 0.5729 0.0171  0.0530  0.0113  272  GLU A OE1 
373  O OE2 . GLU A 47  ? 0.2567 0.3251 0.2636 0.0249  0.0572  0.0126  272  GLU A OE2 
374  N N   . LEU A 48  ? 0.1292 0.1922 0.1329 0.0027  0.0278  0.0108  273  LEU A N   
375  C CA  . LEU A 48  ? 0.1445 0.2102 0.1505 -0.0012 0.0235  0.0123  273  LEU A CA  
376  C C   . LEU A 48  ? 0.1570 0.2273 0.1637 -0.0027 0.0252  0.0147  273  LEU A C   
377  O O   . LEU A 48  ? 0.1728 0.2416 0.1742 -0.0018 0.0288  0.0141  273  LEU A O   
378  C CB  . LEU A 48  ? 0.1742 0.2337 0.1737 -0.0035 0.0201  0.0096  273  LEU A CB  
379  C CG  . LEU A 48  ? 0.1343 0.1892 0.1331 -0.0028 0.0183  0.0074  273  LEU A CG  
380  C CD1 . LEU A 48  ? 0.1838 0.2332 0.1759 -0.0050 0.0160  0.0046  273  LEU A CD1 
381  C CD2 . LEU A 48  ? 0.1540 0.2124 0.1596 -0.0033 0.0151  0.0093  273  LEU A CD2 
382  N N   . LEU A 49  ? 0.1582 0.2336 0.1711 -0.0052 0.0228  0.0175  274  LEU A N   
383  C CA  . LEU A 49  ? 0.1189 0.1984 0.1332 -0.0073 0.0242  0.0203  274  LEU A CA  
384  C C   . LEU A 49  ? 0.1511 0.2278 0.1632 -0.0111 0.0202  0.0206  274  LEU A C   
385  O O   . LEU A 49  ? 0.1500 0.2241 0.1627 -0.0123 0.0161  0.0195  274  LEU A O   
386  C CB  . LEU A 49  ? 0.1093 0.1979 0.1337 -0.0073 0.0255  0.0237  274  LEU A CB  
387  C CG  . LEU A 49  ? 0.1524 0.2452 0.1815 -0.0030 0.0288  0.0240  274  LEU A CG  
388  C CD1 . LEU A 49  ? 0.1705 0.2740 0.2107 -0.0037 0.0291  0.0278  274  LEU A CD1 
389  C CD2 . LEU A 49  ? 0.1779 0.2684 0.2014 0.0005  0.0345  0.0228  274  LEU A CD2 
390  N N   . GLY A 50  ? 0.1707 0.2478 0.1802 -0.0129 0.0217  0.0225  275  GLY A N   
391  C CA  . GLY A 50  ? 0.1199 0.1943 0.1280 -0.0161 0.0184  0.0236  275  GLY A CA  
392  C C   . GLY A 50  ? 0.1645 0.2321 0.1654 -0.0158 0.0155  0.0208  275  GLY A C   
393  O O   . GLY A 50  ? 0.1558 0.2206 0.1504 -0.0140 0.0168  0.0186  275  GLY A O   
394  N N   . THR A 51  ? 0.1468 0.2119 0.1488 -0.0178 0.0115  0.0208  276  THR A N   
395  C CA  . THR A 51  ? 0.1229 0.1829 0.1196 -0.0174 0.0086  0.0185  276  THR A CA  
396  C C   . THR A 51  ? 0.1450 0.2039 0.1436 -0.0164 0.0065  0.0158  276  THR A C   
397  O O   . THR A 51  ? 0.1295 0.1849 0.1252 -0.0164 0.0040  0.0140  276  THR A O   
398  C CB  . THR A 51  ? 0.1685 0.2257 0.1645 -0.0195 0.0059  0.0202  276  THR A CB  
399  O OG1 . THR A 51  ? 0.1597 0.2181 0.1620 -0.0214 0.0044  0.0212  276  THR A OG1 
400  C CG2 . THR A 51  ? 0.1633 0.2204 0.1557 -0.0204 0.0080  0.0231  276  THR A CG2 
401  N N   . THR A 52  ? 0.1396 0.2018 0.1432 -0.0153 0.0078  0.0157  277  THR A N   
402  C CA  . THR A 52  ? 0.1320 0.1932 0.1373 -0.0142 0.0061  0.0137  277  THR A CA  
403  C C   . THR A 52  ? 0.1176 0.1742 0.1171 -0.0129 0.0060  0.0107  277  THR A C   
404  O O   . THR A 52  ? 0.1389 0.1945 0.1348 -0.0115 0.0088  0.0096  277  THR A O   
405  C CB  . THR A 52  ? 0.1042 0.1698 0.1147 -0.0123 0.0083  0.0146  277  THR A CB  
406  O OG1 . THR A 52  ? 0.1075 0.1786 0.1239 -0.0139 0.0084  0.0175  277  THR A OG1 
407  C CG2 . THR A 52  ? 0.1310 0.1957 0.1434 -0.0111 0.0065  0.0132  277  THR A CG2 
408  N N   . PRO A 53  ? 0.1619 0.2157 0.1604 -0.0136 0.0030  0.0093  278  PRO A N   
409  C CA  . PRO A 53  ? 0.2182 0.2684 0.2118 -0.0131 0.0027  0.0066  278  PRO A CA  
410  C C   . PRO A 53  ? 0.2253 0.2741 0.2193 -0.0114 0.0042  0.0048  278  PRO A C   
411  O O   . PRO A 53  ? 0.1790 0.2291 0.1774 -0.0106 0.0040  0.0056  278  PRO A O   
412  C CB  . PRO A 53  ? 0.1582 0.2068 0.1519 -0.0143 -0.0008 0.0062  278  PRO A CB  
413  C CG  . PRO A 53  ? 0.1611 0.2115 0.1598 -0.0150 -0.0021 0.0079  278  PRO A CG  
414  C CD  . PRO A 53  ? 0.1435 0.1971 0.1446 -0.0152 -0.0001 0.0102  278  PRO A CD  
415  N N   A ARG A 54  ? 0.1552 0.2008 0.1442 -0.0110 0.0057  0.0025  279  ARG A N   
416  N N   B ARG A 54  ? 0.1551 0.2006 0.1440 -0.0110 0.0057  0.0025  279  ARG A N   
417  C CA  A ARG A 54  ? 0.1581 0.2005 0.1465 -0.0096 0.0073  0.0006  279  ARG A CA  
418  C CA  B ARG A 54  ? 0.1579 0.2003 0.1463 -0.0095 0.0073  0.0007  279  ARG A CA  
419  C C   A ARG A 54  ? 0.1555 0.1962 0.1453 -0.0104 0.0048  -0.0002 279  ARG A C   
420  C C   B ARG A 54  ? 0.1548 0.1953 0.1444 -0.0104 0.0048  -0.0003 279  ARG A C   
421  O O   A ARG A 54  ? 0.1922 0.2318 0.1844 -0.0090 0.0055  -0.0001 279  ARG A O   
422  O O   B ARG A 54  ? 0.1894 0.2284 0.1809 -0.0090 0.0057  -0.0004 279  ARG A O   
423  C CB  A ARG A 54  ? 0.1825 0.2209 0.1642 -0.0096 0.0094  -0.0021 279  ARG A CB  
424  C CB  B ARG A 54  ? 0.1825 0.2210 0.1644 -0.0094 0.0096  -0.0020 279  ARG A CB  
425  C CG  A ARG A 54  ? 0.2083 0.2416 0.1884 -0.0085 0.0113  -0.0044 279  ARG A CG  
426  C CG  B ARG A 54  ? 0.2082 0.2424 0.1892 -0.0075 0.0125  -0.0037 279  ARG A CG  
427  C CD  A ARG A 54  ? 0.2836 0.3126 0.2565 -0.0085 0.0139  -0.0073 279  ARG A CD  
428  C CD  B ARG A 54  ? 0.2814 0.3107 0.2548 -0.0078 0.0148  -0.0069 279  ARG A CD  
429  N NE  A ARG A 54  ? 0.2717 0.3029 0.2441 -0.0065 0.0172  -0.0060 279  ARG A NE  
430  N NE  B ARG A 54  ? 0.3296 0.3534 0.3020 -0.0057 0.0180  -0.0085 279  ARG A NE  
431  C CZ  A ARG A 54  ? 0.2666 0.2972 0.2410 -0.0033 0.0210  -0.0053 279  ARG A CZ  
432  C CZ  B ARG A 54  ? 0.2580 0.2818 0.2321 -0.0022 0.0219  -0.0074 279  ARG A CZ  
433  N NH1 A ARG A 54  ? 0.2759 0.3032 0.2525 -0.0016 0.0220  -0.0058 279  ARG A NH1 
434  N NH1 B ARG A 54  ? 0.3919 0.4215 0.3691 -0.0008 0.0231  -0.0048 279  ARG A NH1 
435  N NH2 A ARG A 54  ? 0.2466 0.2804 0.2212 -0.0016 0.0241  -0.0038 279  ARG A NH2 
436  N NH2 B ARG A 54  ? 0.4672 0.4851 0.4402 0.0000  0.0247  -0.0087 279  ARG A NH2 
437  N N   . ASN A 55  ? 0.1322 0.1729 0.1207 -0.0123 0.0020  -0.0008 280  ASN A N   
438  C CA  . ASN A 55  ? 0.1377 0.1776 0.1279 -0.0131 -0.0001 -0.0013 280  ASN A CA  
439  C C   . ASN A 55  ? 0.1321 0.1747 0.1265 -0.0130 -0.0019 0.0008  280  ASN A C   
440  O O   . ASN A 55  ? 0.1439 0.1883 0.1387 -0.0137 -0.0031 0.0021  280  ASN A O   
441  C CB  . ASN A 55  ? 0.1027 0.1421 0.0900 -0.0149 -0.0021 -0.0029 280  ASN A CB  
442  C CG  . ASN A 55  ? 0.1576 0.1963 0.1466 -0.0156 -0.0035 -0.0036 280  ASN A CG  
443  O OD1 . ASN A 55  ? 0.1756 0.2148 0.1677 -0.0149 -0.0040 -0.0025 280  ASN A OD1 
444  N ND2 . ASN A 55  ? 0.1277 0.1657 0.1146 -0.0172 -0.0043 -0.0056 280  ASN A ND2 
445  N N   . ALA A 56  ? 0.1503 0.1928 0.1474 -0.0122 -0.0020 0.0013  281  ALA A N   
446  C CA  . ALA A 56  ? 0.1540 0.1987 0.1543 -0.0124 -0.0039 0.0030  281  ALA A CA  
447  C C   . ALA A 56  ? 0.1744 0.2188 0.1739 -0.0138 -0.0062 0.0027  281  ALA A C   
448  O O   . ALA A 56  ? 0.1710 0.2166 0.1721 -0.0145 -0.0074 0.0039  281  ALA A O   
449  C CB  . ALA A 56  ? 0.1388 0.1829 0.1406 -0.0115 -0.0042 0.0032  281  ALA A CB  
450  N N   A SER A 57  ? 0.1589 0.2017 0.1564 -0.0142 -0.0066 0.0012  282  SER A N   
451  N N   B SER A 57  ? 0.1587 0.2015 0.1562 -0.0142 -0.0066 0.0012  282  SER A N   
452  C CA  A SER A 57  ? 0.1219 0.1648 0.1194 -0.0148 -0.0085 0.0011  282  SER A CA  
453  C CA  B SER A 57  ? 0.1213 0.1642 0.1187 -0.0148 -0.0085 0.0011  282  SER A CA  
454  C C   A SER A 57  ? 0.1493 0.1929 0.1454 -0.0152 -0.0092 0.0018  282  SER A C   
455  C C   B SER A 57  ? 0.1522 0.1959 0.1481 -0.0152 -0.0091 0.0017  282  SER A C   
456  O O   A SER A 57  ? 0.1678 0.2114 0.1641 -0.0151 -0.0106 0.0020  282  SER A O   
457  O O   B SER A 57  ? 0.1804 0.2242 0.1762 -0.0152 -0.0105 0.0018  282  SER A O   
458  C CB  A SER A 57  ? 0.1419 0.1840 0.1387 -0.0150 -0.0087 -0.0005 282  SER A CB  
459  C CB  B SER A 57  ? 0.1415 0.1836 0.1385 -0.0150 -0.0087 -0.0004 282  SER A CB  
460  O OG  A SER A 57  ? 0.2327 0.2738 0.2306 -0.0146 -0.0084 -0.0005 282  SER A OG  
461  O OG  B SER A 57  ? 0.1313 0.1729 0.1265 -0.0156 -0.0077 -0.0018 282  SER A OG  
462  N N   A TRP A 58  ? 0.1078 0.1521 0.1025 -0.0153 -0.0080 0.0023  283  TRP A N   
463  N N   B TRP A 58  ? 0.1099 0.1542 0.1045 -0.0152 -0.0078 0.0023  283  TRP A N   
464  C CA  A TRP A 58  ? 0.1206 0.1655 0.1136 -0.0155 -0.0086 0.0036  283  TRP A CA  
465  C CA  B TRP A 58  ? 0.1260 0.1710 0.1189 -0.0155 -0.0083 0.0036  283  TRP A CA  
466  C C   A TRP A 58  ? 0.1276 0.1725 0.1224 -0.0158 -0.0086 0.0058  283  TRP A C   
467  C C   B TRP A 58  ? 0.1274 0.1723 0.1222 -0.0158 -0.0087 0.0057  283  TRP A C   
468  O O   A TRP A 58  ? 0.1397 0.1845 0.1331 -0.0161 -0.0088 0.0074  283  TRP A O   
469  O O   B TRP A 58  ? 0.1355 0.1800 0.1290 -0.0160 -0.0092 0.0072  283  TRP A O   
470  C CB  A TRP A 58  ? 0.1369 0.1823 0.1264 -0.0157 -0.0072 0.0030  283  TRP A CB  
471  C CB  B TRP A 58  ? 0.1435 0.1889 0.1333 -0.0155 -0.0064 0.0034  283  TRP A CB  
472  C CG  A TRP A 58  ? 0.1640 0.2097 0.1507 -0.0162 -0.0084 0.0014  283  TRP A CG  
473  C CG  B TRP A 58  ? 0.2215 0.2663 0.2078 -0.0159 -0.0062 0.0010  283  TRP A CG  
474  C CD1 A TRP A 58  ? 0.1882 0.2330 0.1734 -0.0168 -0.0079 -0.0011 283  TRP A CD1 
475  C CD1 B TRP A 58  ? 0.1633 0.2084 0.1491 -0.0166 -0.0081 -0.0002 283  TRP A CD1 
476  C CD2 A TRP A 58  ? 0.1647 0.2119 0.1500 -0.0162 -0.0105 0.0023  283  TRP A CD2 
477  C CD2 B TRP A 58  ? 0.2962 0.3399 0.2790 -0.0159 -0.0041 -0.0004 283  TRP A CD2 
478  N NE1 A TRP A 58  ? 0.1371 0.1834 0.1204 -0.0178 -0.0098 -0.0020 283  TRP A NE1 
479  N NE1 B TRP A 58  ? 0.1881 0.2326 0.1705 -0.0175 -0.0075 -0.0025 283  TRP A NE1 
480  C CE2 A TRP A 58  ? 0.1382 0.1865 0.1217 -0.0172 -0.0115 0.0002  283  TRP A CE2 
481  C CE2 B TRP A 58  ? 0.2444 0.2872 0.2243 -0.0170 -0.0050 -0.0028 283  TRP A CE2 
482  C CE3 A TRP A 58  ? 0.2350 0.2826 0.2204 -0.0156 -0.0116 0.0048  283  TRP A CE3 
483  C CE3 B TRP A 58  ? 0.1042 0.1477 0.0863 -0.0150 -0.0012 0.0000  283  TRP A CE3 
484  C CZ2 A TRP A 58  ? 0.1784 0.2295 0.1609 -0.0173 -0.0138 0.0007  283  TRP A CZ2 
485  C CZ2 B TRP A 58  ? 0.1755 0.2161 0.1507 -0.0176 -0.0033 -0.0051 283  TRP A CZ2 
486  C CZ3 A TRP A 58  ? 0.1961 0.2456 0.1801 -0.0152 -0.0137 0.0055  283  TRP A CZ3 
487  C CZ3 B TRP A 58  ? 0.2170 0.2582 0.1944 -0.0149 0.0009  -0.0021 283  TRP A CZ3 
488  C CH2 A TRP A 58  ? 0.2351 0.2870 0.2179 -0.0160 -0.0149 0.0035  283  TRP A CH2 
489  C CH2 B TRP A 58  ? 0.1985 0.2378 0.1722 -0.0163 -0.0002 -0.0049 283  TRP A CH2 
490  N N   . LEU A 59  ? 0.1384 0.1835 0.1362 -0.0161 -0.0085 0.0060  284  LEU A N   
491  C CA  . LEU A 59  ? 0.1307 0.1758 0.1305 -0.0171 -0.0090 0.0078  284  LEU A CA  
492  C C   . LEU A 59  ? 0.1255 0.1676 0.1245 -0.0173 -0.0108 0.0079  284  LEU A C   
493  O O   . LEU A 59  ? 0.1266 0.1675 0.1255 -0.0167 -0.0118 0.0065  284  LEU A O   
494  C CB  . LEU A 59  ? 0.1448 0.1915 0.1480 -0.0175 -0.0091 0.0078  284  LEU A CB  
495  C CG  . LEU A 59  ? 0.1428 0.1899 0.1484 -0.0194 -0.0100 0.0093  284  LEU A CG  
496  C CD1 . LEU A 59  ? 0.1577 0.2071 0.1645 -0.0203 -0.0084 0.0114  284  LEU A CD1 
497  C CD2 . LEU A 59  ? 0.1624 0.2118 0.1709 -0.0197 -0.0109 0.0091  284  LEU A CD2 
498  N N   . ASN A 60  ? 0.1302 0.1710 0.1287 -0.0181 -0.0108 0.0098  285  ASN A N   
499  C CA  . ASN A 60  ? 0.1137 0.1508 0.1111 -0.0178 -0.0121 0.0103  285  ASN A CA  
500  C C   . ASN A 60  ? 0.1493 0.1863 0.1447 -0.0159 -0.0127 0.0098  285  ASN A C   
501  O O   . ASN A 60  ? 0.2460 0.2803 0.2410 -0.0148 -0.0136 0.0100  285  ASN A O   
502  C CB  . ASN A 60  ? 0.1227 0.1570 0.1212 -0.0185 -0.0132 0.0092  285  ASN A CB  
503  C CG  . ASN A 60  ? 0.1778 0.2107 0.1778 -0.0210 -0.0133 0.0104  285  ASN A CG  
504  O OD1 . ASN A 60  ? 0.2101 0.2446 0.2109 -0.0222 -0.0123 0.0123  285  ASN A OD1 
505  N ND2 . ASN A 60  ? 0.1864 0.2160 0.1865 -0.0221 -0.0145 0.0092  285  ASN A ND2 
506  N N   . ARG A 61  ? 0.1030 0.1431 0.0972 -0.0154 -0.0123 0.0092  286  ARG A N   
507  C CA  . ARG A 61  ? 0.1115 0.1528 0.1040 -0.0141 -0.0133 0.0090  286  ARG A CA  
508  C C   . ARG A 61  ? 0.1516 0.1937 0.1410 -0.0140 -0.0131 0.0110  286  ARG A C   
509  O O   . ARG A 61  ? 0.1608 0.2031 0.1492 -0.0150 -0.0117 0.0120  286  ARG A O   
510  C CB  . ARG A 61  ? 0.1282 0.1720 0.1209 -0.0141 -0.0132 0.0066  286  ARG A CB  
511  C CG  . ARG A 61  ? 0.1949 0.2383 0.1898 -0.0137 -0.0136 0.0050  286  ARG A CG  
512  C CD  . ARG A 61  ? 0.2370 0.2784 0.2334 -0.0142 -0.0130 0.0047  286  ARG A CD  
513  N NE  . ARG A 61  ? 0.2616 0.3028 0.2592 -0.0138 -0.0131 0.0031  286  ARG A NE  
514  C CZ  . ARG A 61  ? 0.2803 0.3208 0.2785 -0.0143 -0.0127 0.0024  286  ARG A CZ  
515  N NH1 . ARG A 61  ? 0.2065 0.2469 0.2053 -0.0151 -0.0123 0.0031  286  ARG A NH1 
516  N NH2 . ARG A 61  ? 0.2460 0.2864 0.2446 -0.0139 -0.0125 0.0012  286  ARG A NH2 
517  N N   . PHE A 62  ? 0.1356 0.1787 0.1237 -0.0126 -0.0146 0.0119  287  PHE A N   
518  C CA  . PHE A 62  ? 0.1553 0.1995 0.1397 -0.0123 -0.0149 0.0141  287  PHE A CA  
519  C C   . PHE A 62  ? 0.1931 0.2410 0.1765 -0.0112 -0.0169 0.0137  287  PHE A C   
520  O O   . PHE A 62  ? 0.1493 0.1985 0.1356 -0.0103 -0.0181 0.0127  287  PHE A O   
521  C CB  . PHE A 62  ? 0.1551 0.1956 0.1388 -0.0116 -0.0147 0.0175  287  PHE A CB  
522  C CG  . PHE A 62  ? 0.1568 0.1949 0.1426 -0.0096 -0.0159 0.0183  287  PHE A CG  
523  C CD1 . PHE A 62  ? 0.1878 0.2277 0.1726 -0.0073 -0.0176 0.0199  287  PHE A CD1 
524  C CD2 . PHE A 62  ? 0.1592 0.1933 0.1476 -0.0100 -0.0153 0.0173  287  PHE A CD2 
525  C CE1 . PHE A 62  ? 0.2161 0.2537 0.2031 -0.0048 -0.0182 0.0207  287  PHE A CE1 
526  C CE2 . PHE A 62  ? 0.1793 0.2103 0.1688 -0.0079 -0.0159 0.0177  287  PHE A CE2 
527  C CZ  . PHE A 62  ? 0.1913 0.2240 0.1804 -0.0050 -0.0171 0.0195  287  PHE A CZ  
528  N N   . ARG A 63  ? 0.1770 0.2272 0.1562 -0.0115 -0.0174 0.0146  288  ARG A N   
529  C CA  . ARG A 63  ? 0.1850 0.2397 0.1624 -0.0111 -0.0198 0.0142  288  ARG A CA  
530  C C   . ARG A 63  ? 0.1663 0.2216 0.1390 -0.0102 -0.0207 0.0176  288  ARG A C   
531  O O   . ARG A 63  ? 0.1883 0.2412 0.1576 -0.0109 -0.0187 0.0188  288  ARG A O   
532  C CB  . ARG A 63  ? 0.2393 0.2962 0.2149 -0.0133 -0.0196 0.0106  288  ARG A CB  
533  C CG  . ARG A 63  ? 0.5684 0.6303 0.5437 -0.0140 -0.0223 0.0091  288  ARG A CG  
534  C CD  . ARG A 63  ? 0.4283 0.4902 0.3995 -0.0167 -0.0215 0.0057  288  ARG A CD  
535  N NE  . ARG A 63  ? 0.5931 0.6588 0.5657 -0.0184 -0.0235 0.0031  288  ARG A NE  
536  C CZ  . ARG A 63  ? 0.5778 0.6420 0.5522 -0.0203 -0.0223 -0.0001 288  ARG A CZ  
537  N N   . GLY A 64  ? 0.1574 0.2162 0.1300 -0.0085 -0.0234 0.0194  289  GLY A N   
538  C CA  . GLY A 64  ? 0.1612 0.2210 0.1286 -0.0074 -0.0245 0.0228  289  GLY A CA  
539  C C   . GLY A 64  ? 0.2029 0.2686 0.1709 -0.0057 -0.0281 0.0242  289  GLY A C   
540  O O   . GLY A 64  ? 0.2504 0.3203 0.2228 -0.0058 -0.0297 0.0221  289  GLY A O   
541  N N   A VAL A 65  ? 0.1518 0.2185 0.1156 -0.0039 -0.0295 0.0283  290  VAL A N   
542  N N   B VAL A 65  ? 0.1521 0.2188 0.1156 -0.0040 -0.0295 0.0282  290  VAL A N   
543  C CA  A VAL A 65  ? 0.1418 0.2149 0.1061 -0.0016 -0.0333 0.0306  290  VAL A CA  
544  C CA  B VAL A 65  ? 0.1418 0.2148 0.1061 -0.0016 -0.0333 0.0307  290  VAL A CA  
545  C C   A VAL A 65  ? 0.1505 0.2205 0.1143 0.0023  -0.0334 0.0363  290  VAL A C   
546  C C   B VAL A 65  ? 0.1510 0.2204 0.1152 0.0023  -0.0331 0.0362  290  VAL A C   
547  O O   A VAL A 65  ? 0.1794 0.2442 0.1382 0.0022  -0.0315 0.0389  290  VAL A O   
548  O O   B VAL A 65  ? 0.1896 0.2531 0.1497 0.0022  -0.0309 0.0386  290  VAL A O   
549  C CB  A VAL A 65  ? 0.1717 0.2506 0.1296 -0.0037 -0.0360 0.0297  290  VAL A CB  
550  C CB  B VAL A 65  ? 0.1737 0.2526 0.1315 -0.0033 -0.0361 0.0303  290  VAL A CB  
551  C CG1 A VAL A 65  ? 0.1705 0.2568 0.1287 -0.0011 -0.0403 0.0331  290  VAL A CG1 
552  C CG1 B VAL A 65  ? 0.3061 0.3885 0.2647 -0.0070 -0.0367 0.0248  290  VAL A CG1 
553  C CG2 A VAL A 65  ? 0.3096 0.3911 0.2687 -0.0073 -0.0361 0.0241  290  VAL A CG2 
554  C CG2 B VAL A 65  ? 0.1537 0.2283 0.1031 -0.0042 -0.0341 0.0320  290  VAL A CG2 
555  N N   . SER A 66  ? 0.1572 0.2301 0.1263 0.0057  -0.0352 0.0383  291  SER A N   
556  C CA  . SER A 66  ? 0.1848 0.2537 0.1538 0.0100  -0.0350 0.0437  291  SER A CA  
557  C C   . SER A 66  ? 0.1922 0.2635 0.1542 0.0111  -0.0370 0.0480  291  SER A C   
558  O O   . SER A 66  ? 0.2218 0.3015 0.1815 0.0104  -0.0405 0.0478  291  SER A O   
559  C CB  . SER A 66  ? 0.1752 0.2477 0.1514 0.0141  -0.0364 0.0448  291  SER A CB  
560  O OG  . SER A 66  ? 0.1958 0.2795 0.1738 0.0141  -0.0402 0.0444  291  SER A OG  
561  N N   . THR A 67  ? 0.1811 0.2448 0.1391 0.0124  -0.0349 0.0522  292  THR A N   
562  C CA  . THR A 67  ? 0.1884 0.2534 0.1388 0.0137  -0.0365 0.0570  292  THR A CA  
563  C C   . THR A 67  ? 0.2412 0.3087 0.1930 0.0192  -0.0392 0.0626  292  THR A C   
564  O O   . THR A 67  ? 0.2569 0.3283 0.2029 0.0206  -0.0417 0.0667  292  THR A O   
565  C CB  . THR A 67  ? 0.2891 0.3448 0.2344 0.0123  -0.0326 0.0592  292  THR A CB  
566  O OG1 . THR A 67  ? 0.3604 0.4077 0.3092 0.0149  -0.0304 0.0622  292  THR A OG1 
567  C CG2 . THR A 67  ? 0.3214 0.3749 0.2670 0.0075  -0.0297 0.0539  292  THR A CG2 
568  N N   . ALA A 68  ? 0.2287 0.2942 0.1879 0.0226  -0.0386 0.0630  293  ALA A N   
569  C CA  . ALA A 68  ? 0.2004 0.2681 0.1622 0.0286  -0.0406 0.0684  293  ALA A CA  
570  C C   . ALA A 68  ? 0.2163 0.2848 0.1874 0.0308  -0.0399 0.0659  293  ALA A C   
571  O O   . ALA A 68  ? 0.2198 0.2845 0.1938 0.0278  -0.0374 0.0609  293  ALA A O   
572  C CB  . ALA A 68  ? 0.2484 0.3055 0.2058 0.0317  -0.0383 0.0744  293  ALA A CB  
573  N N   . ALA A 69  ? 0.2139 0.2877 0.1894 0.0364  -0.0421 0.0695  294  ALA A N   
574  C CA  . ALA A 69  ? 0.2225 0.2968 0.2066 0.0392  -0.0408 0.0675  294  ALA A CA  
575  C C   . ALA A 69  ? 0.1995 0.2592 0.1834 0.0406  -0.0361 0.0677  294  ALA A C   
576  O O   . ALA A 69  ? 0.2584 0.3088 0.2372 0.0420  -0.0346 0.0718  294  ALA A O   
577  C CB  . ALA A 69  ? 0.2866 0.3702 0.2760 0.0455  -0.0438 0.0720  294  ALA A CB  
578  N N   . VAL A 70  ? 0.2372 0.2948 0.2265 0.0400  -0.0339 0.0631  295  VAL A N   
579  C CA  . VAL A 70  ? 0.2362 0.2804 0.2257 0.0414  -0.0297 0.0626  295  VAL A CA  
580  C C   . VAL A 70  ? 0.2753 0.3142 0.2649 0.0484  -0.0291 0.0686  295  VAL A C   
581  O O   . VAL A 70  ? 0.2926 0.3400 0.2866 0.0536  -0.0312 0.0716  295  VAL A O   
582  C CB  . VAL A 70  ? 0.2494 0.2946 0.2448 0.0406  -0.0280 0.0571  295  VAL A CB  
583  C CG1 . VAL A 70  ? 0.2621 0.2941 0.2576 0.0433  -0.0241 0.0569  295  VAL A CG1 
584  C CG2 . VAL A 70  ? 0.2449 0.2920 0.2391 0.0337  -0.0279 0.0516  295  VAL A CG2 
585  N N   . ALA A 71  ? 0.2827 0.3076 0.2677 0.0485  -0.0262 0.0705  296  ALA A N   
586  C CA  . ALA A 71  ? 0.3062 0.3223 0.2906 0.0550  -0.0245 0.0757  296  ALA A CA  
587  C C   . ALA A 71  ? 0.3610 0.3601 0.3417 0.0527  -0.0204 0.0744  296  ALA A C   
588  O O   . ALA A 71  ? 0.3124 0.3074 0.2890 0.0465  -0.0196 0.0725  296  ALA A O   
589  C CB  . ALA A 71  ? 0.3330 0.3520 0.3133 0.0581  -0.0270 0.0829  296  ALA A CB  
590  N N   . ASN A 72  ? 0.3381 0.3275 0.3204 0.0576  -0.0176 0.0751  297  ASN A N   
591  C CA  . ASN A 72  ? 0.3379 0.3099 0.3164 0.0557  -0.0137 0.0738  297  ASN A CA  
592  C C   . ASN A 72  ? 0.2712 0.2414 0.2495 0.0482  -0.0126 0.0669  297  ASN A C   
593  O O   . ASN A 72  ? 0.2694 0.2294 0.2437 0.0433  -0.0108 0.0659  297  ASN A O   
594  C CB  . ASN A 72  ? 0.4034 0.3661 0.3754 0.0550  -0.0130 0.0795  297  ASN A CB  
595  C CG  . ASN A 72  ? 0.7296 0.6931 0.7012 0.0628  -0.0140 0.0870  297  ASN A CG  
596  O OD1 . ASN A 72  ? 0.7739 0.7405 0.7416 0.0627  -0.0158 0.0921  297  ASN A OD1 
597  N ND2 . ASN A 72  ? 0.5896 0.5505 0.5650 0.0698  -0.0127 0.0878  297  ASN A ND2 
598  N N   . GLN A 73  ? 0.2617 0.2424 0.2447 0.0472  -0.0138 0.0622  298  GLN A N   
599  C CA  . GLN A 73  ? 0.2916 0.2722 0.2752 0.0410  -0.0131 0.0557  298  GLN A CA  
600  C C   . GLN A 73  ? 0.2562 0.2393 0.2367 0.0342  -0.0142 0.0550  298  GLN A C   
601  O O   . GLN A 73  ? 0.2550 0.2339 0.2345 0.0288  -0.0130 0.0511  298  GLN A O   
602  C CB  . GLN A 73  ? 0.2651 0.2311 0.2469 0.0404  -0.0096 0.0527  298  GLN A CB  
603  C CG  . GLN A 73  ? 0.3194 0.2823 0.3039 0.0471  -0.0078 0.0524  298  GLN A CG  
604  C CD  . GLN A 73  ? 0.6050 0.5596 0.5887 0.0450  -0.0052 0.0465  298  GLN A CD  
605  O OE1 . GLN A 73  ? 0.4605 0.4053 0.4402 0.0397  -0.0041 0.0442  298  GLN A OE1 
606  N NE2 . GLN A 73  ? 0.6677 0.6270 0.6553 0.0487  -0.0043 0.0439  298  GLN A NE2 
607  N N   . VAL A 74  ? 0.2526 0.2431 0.2314 0.0345  -0.0165 0.0589  299  VAL A N   
608  C CA  . VAL A 74  ? 0.1935 0.1870 0.1690 0.0288  -0.0172 0.0587  299  VAL A CA  
609  C C   . VAL A 74  ? 0.2529 0.2610 0.2303 0.0279  -0.0203 0.0570  299  VAL A C   
610  O O   . VAL A 74  ? 0.2217 0.2377 0.2005 0.0320  -0.0227 0.0598  299  VAL A O   
611  C CB  . VAL A 74  ? 0.2685 0.2566 0.2386 0.0293  -0.0168 0.0647  299  VAL A CB  
612  C CG1 . VAL A 74  ? 0.2723 0.2651 0.2389 0.0238  -0.0173 0.0644  299  VAL A CG1 
613  C CG2 . VAL A 74  ? 0.2502 0.2227 0.2181 0.0294  -0.0136 0.0662  299  VAL A CG2 
614  N N   . LEU A 75  ? 0.2032 0.2147 0.1805 0.0224  -0.0202 0.0527  300  LEU A N   
615  C CA  . LEU A 75  ? 0.2151 0.2386 0.1931 0.0205  -0.0227 0.0507  300  LEU A CA  
616  C C   . LEU A 75  ? 0.1885 0.2115 0.1619 0.0156  -0.0220 0.0504  300  LEU A C   
617  O O   . LEU A 75  ? 0.2160 0.2342 0.1895 0.0118  -0.0199 0.0476  300  LEU A O   
618  C CB  . LEU A 75  ? 0.1936 0.2218 0.1766 0.0191  -0.0228 0.0452  300  LEU A CB  
619  C CG  . LEU A 75  ? 0.1763 0.2144 0.1597 0.0156  -0.0246 0.0419  300  LEU A CG  
620  C CD1 . LEU A 75  ? 0.1992 0.2472 0.1823 0.0178  -0.0280 0.0445  300  LEU A CD1 
621  C CD2 . LEU A 75  ? 0.2040 0.2446 0.1922 0.0142  -0.0240 0.0369  300  LEU A CD2 
622  N N   A HIS A 76  ? 0.2084 0.2365 0.1775 0.0159  -0.0238 0.0535  301  HIS A N   
623  N N   B HIS A 76  ? 0.2091 0.2372 0.1782 0.0158  -0.0238 0.0534  301  HIS A N   
624  C CA  A HIS A 76  ? 0.1886 0.2175 0.1528 0.0117  -0.0230 0.0533  301  HIS A CA  
625  C CA  B HIS A 76  ? 0.1867 0.2150 0.1512 0.0114  -0.0227 0.0530  301  HIS A CA  
626  C C   A HIS A 76  ? 0.2028 0.2410 0.1675 0.0091  -0.0246 0.0488  301  HIS A C   
627  C C   B HIS A 76  ? 0.2018 0.2397 0.1662 0.0091  -0.0245 0.0491  301  HIS A C   
628  O O   A HIS A 76  ? 0.1855 0.2316 0.1511 0.0109  -0.0276 0.0487  301  HIS A O   
629  O O   B HIS A 76  ? 0.1858 0.2314 0.1500 0.0109  -0.0276 0.0497  301  HIS A O   
630  C CB  A HIS A 76  ? 0.1948 0.2237 0.1528 0.0135  -0.0237 0.0591  301  HIS A CB  
631  C CB  B HIS A 76  ? 0.2048 0.2306 0.1629 0.0125  -0.0226 0.0588  301  HIS A CB  
632  C CG  A HIS A 76  ? 0.2254 0.2440 0.1816 0.0155  -0.0217 0.0641  301  HIS A CG  
633  C CG  B HIS A 76  ? 0.2916 0.3168 0.2451 0.0082  -0.0206 0.0585  301  HIS A CG  
634  N ND1 A HIS A 76  ? 0.2612 0.2722 0.2143 0.0123  -0.0186 0.0655  301  HIS A ND1 
635  N ND1 B HIS A 76  ? 0.3360 0.3688 0.2855 0.0065  -0.0218 0.0571  301  HIS A ND1 
636  C CD2 A HIS A 76  ? 0.3150 0.3295 0.2719 0.0206  -0.0222 0.0683  301  HIS A CD2 
637  C CD2 B HIS A 76  ? 0.2115 0.2298 0.1642 0.0051  -0.0172 0.0590  301  HIS A CD2 
638  C CE1 A HIS A 76  ? 0.2020 0.2041 0.1539 0.0147  -0.0173 0.0702  301  HIS A CE1 
639  C CE1 B HIS A 76  ? 0.1860 0.2165 0.1323 0.0031  -0.0190 0.0570  301  HIS A CE1 
640  N NE2 A HIS A 76  ? 0.2044 0.2079 0.1582 0.0200  -0.0194 0.0720  301  HIS A NE2 
641  N NE2 B HIS A 76  ? 0.2586 0.2809 0.2072 0.0021  -0.0162 0.0582  301  HIS A NE2 
642  N N   . LEU A 77  ? 0.1836 0.2208 0.1480 0.0049  -0.0227 0.0453  302  LEU A N   
643  C CA  . LEU A 77  ? 0.2081 0.2524 0.1720 0.0024  -0.0237 0.0412  302  LEU A CA  
644  C C   . LEU A 77  ? 0.2253 0.2698 0.1830 -0.0003 -0.0223 0.0417  302  LEU A C   
645  O O   . LEU A 77  ? 0.2689 0.3081 0.2257 -0.0020 -0.0193 0.0426  302  LEU A O   
646  C CB  . LEU A 77  ? 0.2071 0.2508 0.1760 0.0002  -0.0224 0.0362  302  LEU A CB  
647  C CG  . LEU A 77  ? 0.1922 0.2360 0.1670 0.0024  -0.0232 0.0348  302  LEU A CG  
648  C CD1 . LEU A 77  ? 0.2353 0.2786 0.2137 -0.0002 -0.0218 0.0301  302  LEU A CD1 
649  C CD2 . LEU A 77  ? 0.2258 0.2775 0.2019 0.0047  -0.0264 0.0352  302  LEU A CD2 
650  N N   . THR A 78  ? 0.1864 0.2372 0.1398 -0.0007 -0.0243 0.0409  303  THR A N   
651  C CA  . THR A 78  ? 0.1615 0.2131 0.1094 -0.0036 -0.0225 0.0393  303  THR A CA  
652  C C   . THR A 78  ? 0.1867 0.2393 0.1384 -0.0062 -0.0213 0.0337  303  THR A C   
653  O O   . THR A 78  ? 0.1833 0.2396 0.1383 -0.0062 -0.0234 0.0307  303  THR A O   
654  C CB  . THR A 78  ? 0.2407 0.2981 0.1818 -0.0034 -0.0252 0.0400  303  THR A CB  
655  O OG1 . THR A 78  ? 0.2944 0.3506 0.2315 -0.0008 -0.0262 0.0458  303  THR A OG1 
656  C CG2 . THR A 78  ? 0.2739 0.3314 0.2087 -0.0063 -0.0229 0.0376  303  THR A CG2 
657  N N   . LEU A 79  ? 0.1724 0.2218 0.1239 -0.0083 -0.0178 0.0326  304  LEU A N   
658  C CA  . LEU A 79  ? 0.1422 0.1916 0.0980 -0.0101 -0.0164 0.0281  304  LEU A CA  
659  C C   . LEU A 79  ? 0.1697 0.2225 0.1217 -0.0117 -0.0164 0.0242  304  LEU A C   
660  O O   . LEU A 79  ? 0.2229 0.2767 0.1680 -0.0121 -0.0158 0.0249  304  LEU A O   
661  C CB  . LEU A 79  ? 0.1828 0.2281 0.1411 -0.0114 -0.0129 0.0287  304  LEU A CB  
662  C CG  . LEU A 79  ? 0.2337 0.2746 0.1967 -0.0107 -0.0129 0.0309  304  LEU A CG  
663  C CD1 . LEU A 79  ? 0.2758 0.3135 0.2404 -0.0128 -0.0097 0.0321  304  LEU A CD1 
664  C CD2 . LEU A 79  ? 0.2207 0.2619 0.1894 -0.0101 -0.0145 0.0279  304  LEU A CD2 
665  N N   . TYR A 80  ? 0.1529 0.2069 0.1090 -0.0125 -0.0168 0.0202  305  TYR A N   
666  C CA  . TYR A 80  ? 0.1501 0.2053 0.1034 -0.0143 -0.0161 0.0160  305  TYR A CA  
667  C C   . TYR A 80  ? 0.1840 0.2366 0.1413 -0.0151 -0.0129 0.0139  305  TYR A C   
668  O O   . TYR A 80  ? 0.1952 0.2460 0.1580 -0.0147 -0.0122 0.0151  305  TYR A O   
669  C CB  . TYR A 80  ? 0.1835 0.2423 0.1385 -0.0149 -0.0193 0.0132  305  TYR A CB  
670  C CG  . TYR A 80  ? 0.2172 0.2805 0.1684 -0.0145 -0.0230 0.0146  305  TYR A CG  
671  C CD1 . TYR A 80  ? 0.2389 0.3025 0.1847 -0.0133 -0.0235 0.0183  305  TYR A CD1 
672  C CD2 . TYR A 80  ? 0.4435 0.5113 0.3967 -0.0155 -0.0261 0.0123  305  TYR A CD2 
673  C CE1 . TYR A 80  ? 0.2819 0.3504 0.2241 -0.0127 -0.0273 0.0199  305  TYR A CE1 
674  C CE2 . TYR A 80  ? 0.4441 0.5173 0.3944 -0.0153 -0.0299 0.0136  305  TYR A CE2 
675  C CZ  . TYR A 80  ? 0.4002 0.4739 0.3448 -0.0138 -0.0306 0.0174  305  TYR A CZ  
676  O OH  . TYR A 80  ? 0.5267 0.6065 0.4683 -0.0133 -0.0348 0.0191  305  TYR A OH  
677  N N   . GLU A 81  ? 0.2714 0.3237 0.2255 -0.0163 -0.0112 0.0107  306  GLU A N   
678  C CA  . GLU A 81  ? 0.2139 0.2643 0.1721 -0.0166 -0.0086 0.0084  306  GLU A CA  
679  C C   . GLU A 81  ? 0.2386 0.2894 0.2010 -0.0171 -0.0104 0.0057  306  GLU A C   
680  O O   . GLU A 81  ? 0.3232 0.3762 0.2849 -0.0175 -0.0134 0.0049  306  GLU A O   
681  C CB  . GLU A 81  ? 0.2933 0.3424 0.2463 -0.0171 -0.0054 0.0062  306  GLU A CB  
682  C CG  . GLU A 81  ? 0.3071 0.3560 0.2569 -0.0165 -0.0024 0.0090  306  GLU A CG  
683  C CD  . GLU A 81  ? 0.3974 0.4461 0.3536 -0.0160 0.0001  0.0111  306  GLU A CD  
684  O OE1 . GLU A 81  ? 0.2828 0.3313 0.2456 -0.0160 -0.0005 0.0103  306  GLU A OE1 
685  O OE2 . GLU A 81  ? 0.4457 0.4949 0.4004 -0.0159 0.0029  0.0136  306  GLU A OE2 
686  N N   . PRO A 82  ? 0.2713 0.3205 0.2384 -0.0170 -0.0087 0.0045  307  PRO A N   
687  C CA  . PRO A 82  ? 0.2493 0.2983 0.2195 -0.0176 -0.0099 0.0018  307  PRO A CA  
688  C C   . PRO A 82  ? 0.3279 0.3771 0.2939 -0.0192 -0.0106 -0.0014 307  PRO A C   
689  O O   . PRO A 82  ? 0.3170 0.3677 0.2852 -0.0201 -0.0127 -0.0027 307  PRO A O   
690  C CB  . PRO A 82  ? 0.2752 0.3220 0.2489 -0.0171 -0.0072 0.0013  307  PRO A CB  
691  C CG  . PRO A 82  ? 0.2715 0.3187 0.2472 -0.0163 -0.0062 0.0044  307  PRO A CG  
692  C CD  . PRO A 82  ? 0.2901 0.3381 0.2606 -0.0164 -0.0063 0.0061  307  PRO A CD  
693  N N   . ASP A 83  ? 0.3352 0.3829 0.2952 -0.0197 -0.0088 -0.0028 308  ASP A N   
694  C CA  . ASP A 83  ? 0.5443 0.5912 0.4994 -0.0218 -0.0097 -0.0064 308  ASP A CA  
695  C C   . ASP A 83  ? 0.6337 0.6848 0.5861 -0.0230 -0.0136 -0.0060 308  ASP A C   
696  O O   . ASP A 83  ? 0.6338 0.6852 0.5823 -0.0253 -0.0150 -0.0090 308  ASP A O   
697  C CB  . ASP A 83  ? 0.4638 0.5070 0.4123 -0.0218 -0.0063 -0.0085 308  ASP A CB  
698  C CG  . ASP A 83  ? 0.7970 0.8414 0.7404 -0.0209 -0.0054 -0.0062 308  ASP A CG  
699  O OD1 . ASP A 83  ? 0.5252 0.5731 0.4684 -0.0207 -0.0081 -0.0034 308  ASP A OD1 
700  O OD2 . ASP A 83  ? 0.7841 0.8258 0.7236 -0.0201 -0.0017 -0.0069 308  ASP A OD2 
701  N N   . GLY A 84  ? 0.4696 0.5239 0.4238 -0.0215 -0.0155 -0.0022 309  GLY A N   
702  C CA  . GLY A 84  ? 0.4008 0.4599 0.3531 -0.0219 -0.0193 -0.0010 309  GLY A CA  
703  C C   . GLY A 84  ? 0.3368 0.3964 0.2807 -0.0219 -0.0196 0.0001  309  GLY A C   
704  O O   . GLY A 84  ? 0.3947 0.4586 0.3367 -0.0217 -0.0230 0.0020  309  GLY A O   
705  N N   . SER A 85  ? 0.3908 0.4464 0.3297 -0.0218 -0.0159 -0.0008 310  SER A N   
706  C CA  . SER A 85  ? 0.3939 0.4498 0.3246 -0.0215 -0.0155 0.0007  310  SER A CA  
707  C C   . SER A 85  ? 0.4088 0.4655 0.3417 -0.0192 -0.0152 0.0060  310  SER A C   
708  O O   . SER A 85  ? 0.3424 0.3980 0.2825 -0.0180 -0.0140 0.0078  310  SER A O   
709  C CB  . SER A 85  ? 0.5045 0.5559 0.4294 -0.0218 -0.0110 -0.0019 310  SER A CB  
710  O OG  . SER A 85  ? 0.5881 0.6373 0.5181 -0.0201 -0.0071 -0.0002 310  SER A OG  
711  N N   A VAL A 86  ? 0.3627 0.4209 0.2887 -0.0188 -0.0161 0.0086  311  VAL A N   
712  N N   B VAL A 86  ? 0.3623 0.4206 0.2883 -0.0188 -0.0161 0.0086  311  VAL A N   
713  C CA  A VAL A 86  ? 0.3140 0.3723 0.2413 -0.0168 -0.0158 0.0140  311  VAL A CA  
714  C CA  B VAL A 86  ? 0.3135 0.3717 0.2406 -0.0168 -0.0157 0.0140  311  VAL A CA  
715  C C   A VAL A 86  ? 0.3527 0.4074 0.2811 -0.0163 -0.0107 0.0151  311  VAL A C   
716  C C   B VAL A 86  ? 0.3523 0.4069 0.2808 -0.0163 -0.0107 0.0150  311  VAL A C   
717  O O   A VAL A 86  ? 0.3820 0.4349 0.3061 -0.0170 -0.0075 0.0127  311  VAL A O   
718  O O   B VAL A 86  ? 0.3816 0.4345 0.3060 -0.0170 -0.0074 0.0126  311  VAL A O   
719  C CB  A VAL A 86  ? 0.5130 0.5738 0.4321 -0.0163 -0.0181 0.0169  311  VAL A CB  
720  C CB  B VAL A 86  ? 0.5143 0.5749 0.4328 -0.0164 -0.0178 0.0168  311  VAL A CB  
721  C CG1 A VAL A 86  ? 0.3835 0.4427 0.2924 -0.0173 -0.0154 0.0152  311  VAL A CG1 
722  C CG1 B VAL A 86  ? 0.5201 0.5800 0.4402 -0.0141 -0.0177 0.0228  311  VAL A CG1 
723  C CG2 A VAL A 86  ? 0.5151 0.5752 0.4361 -0.0140 -0.0181 0.0229  311  VAL A CG2 
724  C CG2 B VAL A 86  ? 0.4164 0.4818 0.3334 -0.0172 -0.0230 0.0152  311  VAL A CG2 
725  N N   . PHE A 87  ? 0.3029 0.3564 0.2374 -0.0153 -0.0100 0.0186  312  PHE A N   
726  C CA  . PHE A 87  ? 0.2789 0.3301 0.2155 -0.0153 -0.0057 0.0202  312  PHE A CA  
727  C C   . PHE A 87  ? 0.2484 0.2994 0.1776 -0.0150 -0.0037 0.0236  312  PHE A C   
728  O O   . PHE A 87  ? 0.3331 0.3844 0.2594 -0.0142 -0.0059 0.0273  312  PHE A O   
729  C CB  . PHE A 87  ? 0.2593 0.3090 0.2042 -0.0148 -0.0060 0.0226  312  PHE A CB  
730  C CG  . PHE A 87  ? 0.2107 0.2589 0.1582 -0.0154 -0.0022 0.0250  312  PHE A CG  
731  C CD1 . PHE A 87  ? 0.2696 0.3182 0.2209 -0.0160 0.0007  0.0227  312  PHE A CD1 
732  C CD2 . PHE A 87  ? 0.3118 0.3584 0.2580 -0.0153 -0.0015 0.0297  312  PHE A CD2 
733  C CE1 . PHE A 87  ? 0.2210 0.2696 0.1756 -0.0167 0.0041  0.0251  312  PHE A CE1 
734  C CE2 . PHE A 87  ? 0.3464 0.3922 0.2956 -0.0164 0.0021  0.0320  312  PHE A CE2 
735  C CZ  . PHE A 87  ? 0.2314 0.2788 0.1850 -0.0172 0.0047  0.0297  312  PHE A CZ  
736  N N   . ASN A 88  ? 0.2390 0.2895 0.1649 -0.0154 0.0006  0.0227  313  ASN A N   
737  C CA  . ASN A 88  ? 0.2773 0.3277 0.1953 -0.0152 0.0030  0.0257  313  ASN A CA  
738  C C   . ASN A 88  ? 0.2218 0.2715 0.1444 -0.0154 0.0070  0.0296  313  ASN A C   
739  O O   . ASN A 88  ? 0.3198 0.3699 0.2459 -0.0157 0.0108  0.0282  313  ASN A O   
740  C CB  . ASN A 88  ? 0.3905 0.4409 0.3001 -0.0154 0.0055  0.0220  313  ASN A CB  
741  C CG  . ASN A 88  ? 0.5997 0.6504 0.4988 -0.0151 0.0070  0.0250  313  ASN A CG  
742  O OD1 . ASN A 88  ? 0.3995 0.4501 0.2984 -0.0148 0.0071  0.0303  313  ASN A OD1 
743  N ND2 . ASN A 88  ? 0.8403 0.8904 0.7299 -0.0154 0.0084  0.0215  313  ASN A ND2 
744  N N   . PRO A 89  ? 0.2670 0.3155 0.1896 -0.0153 0.0063  0.0347  314  PRO A N   
745  C CA  . PRO A 89  ? 0.2239 0.2715 0.1509 -0.0162 0.0101  0.0386  314  PRO A CA  
746  C C   . PRO A 89  ? 0.2706 0.3198 0.1933 -0.0165 0.0155  0.0389  314  PRO A C   
747  O O   . PRO A 89  ? 0.3732 0.4236 0.3022 -0.0175 0.0192  0.0400  314  PRO A O   
748  C CB  . PRO A 89  ? 0.2911 0.3362 0.2155 -0.0159 0.0083  0.0440  314  PRO A CB  
749  C CG  . PRO A 89  ? 0.3639 0.4090 0.2872 -0.0144 0.0030  0.0427  314  PRO A CG  
750  C CD  . PRO A 89  ? 0.3912 0.4392 0.3103 -0.0143 0.0020  0.0374  314  PRO A CD  
751  N N   . LEU A 90  ? 0.2802 0.3300 0.1926 -0.0157 0.0161  0.0378  315  LEU A N   
752  C CA  . LEU A 90  ? 0.2756 0.3265 0.1826 -0.0156 0.0218  0.0383  315  LEU A CA  
753  C C   . LEU A 90  ? 0.2935 0.3460 0.2057 -0.0153 0.0252  0.0341  315  LEU A C   
754  O O   . LEU A 90  ? 0.3532 0.4074 0.2642 -0.0150 0.0308  0.0350  315  LEU A O   
755  C CB  . LEU A 90  ? 0.2842 0.3347 0.1776 -0.0148 0.0212  0.0374  315  LEU A CB  
756  C CG  . LEU A 90  ? 0.3846 0.4342 0.2713 -0.0146 0.0188  0.0426  315  LEU A CG  
757  C CD1 . LEU A 90  ? 0.4759 0.5259 0.3488 -0.0140 0.0175  0.0410  315  LEU A CD1 
758  C CD2 . LEU A 90  ? 0.3992 0.4483 0.2871 -0.0152 0.0232  0.0487  315  LEU A CD2 
759  N N   . SER A 91  ? 0.2988 0.3511 0.2167 -0.0152 0.0224  0.0300  316  SER A N   
760  C CA  . SER A 91  ? 0.3789 0.4322 0.3016 -0.0144 0.0255  0.0263  316  SER A CA  
761  C C   . SER A 91  ? 0.3459 0.4021 0.2785 -0.0149 0.0290  0.0292  316  SER A C   
762  O O   . SER A 91  ? 0.3517 0.4099 0.2879 -0.0137 0.0327  0.0273  316  SER A O   
763  C CB  . SER A 91  ? 0.3873 0.4393 0.3141 -0.0144 0.0214  0.0220  316  SER A CB  
764  O OG  . SER A 91  ? 0.3577 0.4102 0.2939 -0.0153 0.0184  0.0240  316  SER A OG  
765  N N   . GLY A 92  ? 0.2543 0.3109 0.1918 -0.0165 0.0278  0.0336  317  GLY A N   
766  C CA  . GLY A 92  ? 0.2489 0.3086 0.1967 -0.0178 0.0301  0.0361  317  GLY A CA  
767  C C   . GLY A 92  ? 0.2153 0.2751 0.1728 -0.0186 0.0266  0.0345  317  GLY A C   
768  O O   . GLY A 92  ? 0.2184 0.2809 0.1845 -0.0202 0.0276  0.0367  317  GLY A O   
769  N N   . ALA A 93  ? 0.1841 0.2413 0.1404 -0.0177 0.0224  0.0310  318  ALA A N   
770  C CA  . ALA A 93  ? 0.1797 0.2367 0.1441 -0.0184 0.0191  0.0297  318  ALA A CA  
771  C C   . ALA A 93  ? 0.1818 0.2365 0.1492 -0.0204 0.0165  0.0330  318  ALA A C   
772  O O   . ALA A 93  ? 0.2388 0.2907 0.2003 -0.0204 0.0153  0.0352  318  ALA A O   
773  C CB  . ALA A 93  ? 0.1970 0.2518 0.1590 -0.0171 0.0157  0.0253  318  ALA A CB  
774  N N   . PRO A 94  ? 0.2022 0.2578 0.1781 -0.0220 0.0156  0.0335  319  PRO A N   
775  C CA  . PRO A 94  ? 0.1715 0.2236 0.1497 -0.0240 0.0134  0.0362  319  PRO A CA  
776  C C   . PRO A 94  ? 0.1657 0.2134 0.1419 -0.0229 0.0089  0.0345  319  PRO A C   
777  O O   . PRO A 94  ? 0.1634 0.2070 0.1392 -0.0237 0.0073  0.0369  319  PRO A O   
778  C CB  . PRO A 94  ? 0.1892 0.2440 0.1767 -0.0263 0.0137  0.0364  319  PRO A CB  
779  C CG  . PRO A 94  ? 0.1886 0.2471 0.1789 -0.0245 0.0137  0.0326  319  PRO A CG  
780  C CD  . PRO A 94  ? 0.1866 0.2462 0.1702 -0.0220 0.0165  0.0316  319  PRO A CD  
781  N N   . ALA A 95  ? 0.1500 0.1985 0.1252 -0.0211 0.0072  0.0306  320  ALA A N   
782  C CA  . ALA A 95  ? 0.1599 0.2056 0.1348 -0.0201 0.0032  0.0288  320  ALA A CA  
783  C C   . ALA A 95  ? 0.1671 0.2146 0.1404 -0.0186 0.0025  0.0246  320  ALA A C   
784  O O   . ALA A 95  ? 0.1945 0.2446 0.1684 -0.0184 0.0050  0.0230  320  ALA A O   
785  C CB  . ALA A 95  ? 0.1503 0.1942 0.1318 -0.0215 0.0015  0.0285  320  ALA A CB  
786  N N   . PRO A 96  ? 0.1919 0.2381 0.1636 -0.0176 -0.0007 0.0229  321  PRO A N   
787  C CA  . PRO A 96  ? 0.1303 0.1777 0.1017 -0.0168 -0.0015 0.0189  321  PRO A CA  
788  C C   . PRO A 96  ? 0.1367 0.1847 0.1144 -0.0172 -0.0009 0.0172  321  PRO A C   
789  O O   . PRO A 96  ? 0.1569 0.2043 0.1394 -0.0181 -0.0012 0.0186  321  PRO A O   
790  C CB  . PRO A 96  ? 0.1812 0.2277 0.1518 -0.0161 -0.0052 0.0183  321  PRO A CB  
791  C CG  . PRO A 96  ? 0.1454 0.1906 0.1130 -0.0157 -0.0059 0.0221  321  PRO A CG  
792  C CD  . PRO A 96  ? 0.1985 0.2422 0.1686 -0.0169 -0.0035 0.0249  321  PRO A CD  
793  N N   . GLU A 97  ? 0.1537 0.2027 0.1310 -0.0166 0.0001  0.0141  322  GLU A N   
794  C CA  . GLU A 97  ? 0.1713 0.2209 0.1540 -0.0164 0.0005  0.0127  322  GLU A CA  
795  C C   . GLU A 97  ? 0.1770 0.2254 0.1636 -0.0169 -0.0024 0.0125  322  GLU A C   
796  O O   . GLU A 97  ? 0.2102 0.2573 0.1952 -0.0166 -0.0047 0.0117  322  GLU A O   
797  C CB  . GLU A 97  ? 0.2568 0.3060 0.2376 -0.0155 0.0014  0.0093  322  GLU A CB  
798  C CG  . GLU A 97  ? 0.4282 0.4777 0.4049 -0.0147 0.0049  0.0087  322  GLU A CG  
799  C CD  . GLU A 97  ? 0.3222 0.3697 0.2971 -0.0138 0.0059  0.0051  322  GLU A CD  
800  O OE1 . GLU A 97  ? 0.4122 0.4586 0.3900 -0.0138 0.0042  0.0037  322  GLU A OE1 
801  O OE2 . GLU A 97  ? 0.5311 0.5775 0.5012 -0.0130 0.0087  0.0038  322  GLU A OE2 
802  N N   . GLY A 98  ? 0.1383 0.1876 0.1301 -0.0175 -0.0022 0.0132  323  GLY A N   
803  C CA  . GLY A 98  ? 0.1386 0.1863 0.1333 -0.0179 -0.0047 0.0126  323  GLY A CA  
804  C C   . GLY A 98  ? 0.1224 0.1678 0.1178 -0.0191 -0.0060 0.0146  323  GLY A C   
805  O O   . GLY A 98  ? 0.1609 0.2044 0.1584 -0.0196 -0.0077 0.0140  323  GLY A O   
806  N N   . PHE A 99  ? 0.1376 0.1823 0.1306 -0.0196 -0.0051 0.0170  324  PHE A N   
807  C CA  . PHE A 99  ? 0.1267 0.1679 0.1199 -0.0207 -0.0061 0.0192  324  PHE A CA  
808  C C   . PHE A 99  ? 0.1254 0.1667 0.1232 -0.0232 -0.0058 0.0200  324  PHE A C   
809  O O   . PHE A 99  ? 0.1378 0.1832 0.1384 -0.0241 -0.0041 0.0205  324  PHE A O   
810  C CB  . PHE A 99  ? 0.1139 0.1542 0.1032 -0.0206 -0.0049 0.0221  324  PHE A CB  
811  C CG  . PHE A 99  ? 0.1306 0.1685 0.1159 -0.0188 -0.0066 0.0226  324  PHE A CG  
812  C CD1 . PHE A 99  ? 0.1655 0.2055 0.1485 -0.0171 -0.0077 0.0205  324  PHE A CD1 
813  C CD2 . PHE A 99  ? 0.1938 0.2274 0.1779 -0.0187 -0.0072 0.0254  324  PHE A CD2 
814  C CE1 . PHE A 99  ? 0.1587 0.1981 0.1389 -0.0154 -0.0096 0.0212  324  PHE A CE1 
815  C CE2 . PHE A 99  ? 0.1925 0.2246 0.1734 -0.0164 -0.0089 0.0263  324  PHE A CE2 
816  C CZ  . PHE A 99  ? 0.1809 0.2167 0.1602 -0.0147 -0.0103 0.0243  324  PHE A CZ  
817  N N   . PRO A 100 ? 0.1342 0.1712 0.1328 -0.0243 -0.0074 0.0202  325  PRO A N   
818  C CA  . PRO A 100 ? 0.1680 0.2047 0.1705 -0.0275 -0.0076 0.0208  325  PRO A CA  
819  C C   . PRO A 100 ? 0.1362 0.1757 0.1406 -0.0297 -0.0053 0.0238  325  PRO A C   
820  O O   . PRO A 100 ? 0.1680 0.2061 0.1693 -0.0293 -0.0037 0.0262  325  PRO A O   
821  C CB  . PRO A 100 ? 0.1936 0.2229 0.1943 -0.0281 -0.0091 0.0209  325  PRO A CB  
822  C CG  . PRO A 100 ? 0.2055 0.2333 0.2034 -0.0247 -0.0103 0.0189  325  PRO A CG  
823  C CD  . PRO A 100 ? 0.1732 0.2052 0.1691 -0.0227 -0.0091 0.0196  325  PRO A CD  
824  N N   . ASP A 101 ? 0.1274 0.1714 0.1369 -0.0319 -0.0051 0.0238  326  ASP A N   
825  C CA  . ASP A 101 ? 0.1307 0.1797 0.1437 -0.0340 -0.0026 0.0265  326  ASP A CA  
826  C C   . ASP A 101 ? 0.1569 0.2051 0.1741 -0.0386 -0.0035 0.0278  326  ASP A C   
827  O O   . ASP A 101 ? 0.1622 0.2170 0.1852 -0.0410 -0.0025 0.0291  326  ASP A O   
828  C CB  . ASP A 101 ? 0.1339 0.1907 0.1505 -0.0324 -0.0012 0.0258  326  ASP A CB  
829  C CG  . ASP A 101 ? 0.1577 0.2174 0.1789 -0.0332 -0.0036 0.0240  326  ASP A CG  
830  O OD1 . ASP A 101 ? 0.1420 0.1970 0.1620 -0.0343 -0.0064 0.0224  326  ASP A OD1 
831  O OD2 . ASP A 101 ? 0.1521 0.2187 0.1777 -0.0324 -0.0025 0.0242  326  ASP A OD2 
832  N N   . PHE A 102 ? 0.1211 0.1614 0.1356 -0.0401 -0.0053 0.0274  327  PHE A N   
833  C CA  . PHE A 102 ? 0.1258 0.1638 0.1434 -0.0450 -0.0063 0.0281  327  PHE A CA  
834  C C   . PHE A 102 ? 0.1808 0.2083 0.1936 -0.0458 -0.0064 0.0291  327  PHE A C   
835  O O   . PHE A 102 ? 0.1854 0.2082 0.1931 -0.0421 -0.0063 0.0290  327  PHE A O   
836  C CB  . PHE A 102 ? 0.1612 0.2004 0.1812 -0.0464 -0.0094 0.0250  327  PHE A CB  
837  C CG  . PHE A 102 ? 0.1551 0.1880 0.1702 -0.0435 -0.0114 0.0219  327  PHE A CG  
838  C CD1 . PHE A 102 ? 0.1711 0.2072 0.1850 -0.0393 -0.0116 0.0200  327  PHE A CD1 
839  C CD2 . PHE A 102 ? 0.1678 0.1914 0.1795 -0.0450 -0.0127 0.0208  327  PHE A CD2 
840  C CE1 . PHE A 102 ? 0.1828 0.2138 0.1928 -0.0369 -0.0131 0.0174  327  PHE A CE1 
841  C CE2 . PHE A 102 ? 0.1659 0.1842 0.1734 -0.0420 -0.0140 0.0181  327  PHE A CE2 
842  C CZ  . PHE A 102 ? 0.1843 0.2068 0.1912 -0.0380 -0.0142 0.0165  327  PHE A CZ  
843  N N   . THR A 103 ? 0.1797 0.2037 0.1945 -0.0507 -0.0067 0.0301  328  THR A N   
844  C CA  . THR A 103 ? 0.1724 0.1855 0.1831 -0.0521 -0.0063 0.0315  328  THR A CA  
845  C C   . THR A 103 ? 0.1924 0.1972 0.2001 -0.0519 -0.0089 0.0280  328  THR A C   
846  O O   . THR A 103 ? 0.1805 0.1872 0.1906 -0.0545 -0.0112 0.0251  328  THR A O   
847  C CB  . THR A 103 ? 0.1941 0.2068 0.2084 -0.0581 -0.0049 0.0345  328  THR A CB  
848  O OG1 . THR A 103 ? 0.2304 0.2505 0.2468 -0.0576 -0.0017 0.0380  328  THR A OG1 
849  C CG2 . THR A 103 ? 0.2343 0.2341 0.2441 -0.0599 -0.0044 0.0360  328  THR A CG2 
850  N N   . ALA A 104 ? 0.1950 0.1908 0.1971 -0.0487 -0.0086 0.0282  329  ALA A N   
851  C CA  . ALA A 104 ? 0.2053 0.1921 0.2039 -0.0478 -0.0103 0.0251  329  ALA A CA  
852  C C   . ALA A 104 ? 0.2375 0.2133 0.2313 -0.0461 -0.0088 0.0276  329  ALA A C   
853  O O   . ALA A 104 ? 0.2255 0.2022 0.2184 -0.0445 -0.0069 0.0315  329  ALA A O   
854  C CB  . ALA A 104 ? 0.1733 0.1634 0.1706 -0.0430 -0.0117 0.0220  329  ALA A CB  
855  N N   . GLN A 105 ? 0.2242 0.1893 0.2147 -0.0463 -0.0095 0.0254  330  GLN A N   
856  C CA  . GLN A 105 ? 0.1884 0.1422 0.1743 -0.0439 -0.0079 0.0279  330  GLN A CA  
857  C C   . GLN A 105 ? 0.2446 0.1994 0.2279 -0.0366 -0.0078 0.0283  330  GLN A C   
858  O O   . GLN A 105 ? 0.2256 0.1762 0.2063 -0.0335 -0.0064 0.0321  330  GLN A O   
859  C CB  . GLN A 105 ? 0.2242 0.1649 0.2070 -0.0464 -0.0083 0.0253  330  GLN A CB  
860  C CG  . GLN A 105 ? 0.2772 0.2147 0.2620 -0.0543 -0.0082 0.0258  330  GLN A CG  
861  C CD  . GLN A 105 ? 0.3065 0.2541 0.2960 -0.0588 -0.0105 0.0228  330  GLN A CD  
862  O OE1 . GLN A 105 ? 0.2515 0.2001 0.2401 -0.0579 -0.0126 0.0185  330  GLN A OE1 
863  N NE2 . GLN A 105 ? 0.2623 0.2182 0.2571 -0.0632 -0.0101 0.0253  330  GLN A NE2 
864  N N   A GLU A 106 ? 0.2145 0.1749 0.1986 -0.0340 -0.0093 0.0248  331  GLU A N   
865  N N   B GLU A 106 ? 0.2143 0.1749 0.1985 -0.0339 -0.0093 0.0249  331  GLU A N   
866  C CA  A GLU A 106 ? 0.2065 0.1697 0.1893 -0.0276 -0.0095 0.0247  331  GLU A CA  
867  C CA  B GLU A 106 ? 0.2015 0.1654 0.1844 -0.0276 -0.0094 0.0254  331  GLU A CA  
868  C C   A GLU A 106 ? 0.1831 0.1576 0.1688 -0.0271 -0.0108 0.0222  331  GLU A C   
869  C C   B GLU A 106 ? 0.1877 0.1613 0.1731 -0.0266 -0.0108 0.0221  331  GLU A C   
870  O O   A GLU A 106 ? 0.1958 0.1729 0.1835 -0.0303 -0.0119 0.0194  331  GLU A O   
871  O O   B GLU A 106 ? 0.1691 0.1435 0.1556 -0.0293 -0.0119 0.0188  331  GLU A O   
872  C CB  A GLU A 106 ? 0.2343 0.1885 0.2140 -0.0242 -0.0095 0.0226  331  GLU A CB  
873  C CB  B GLU A 106 ? 0.2607 0.2146 0.2400 -0.0235 -0.0089 0.0250  331  GLU A CB  
874  C CG  A GLU A 106 ? 0.2237 0.1653 0.1999 -0.0233 -0.0079 0.0252  331  GLU A CG  
875  C CG  B GLU A 106 ? 0.2531 0.1996 0.2309 -0.0252 -0.0093 0.0207  331  GLU A CG  
876  C CD  A GLU A 106 ? 0.2701 0.2018 0.2448 -0.0288 -0.0076 0.0235  331  GLU A CD  
877  C CD  B GLU A 106 ? 0.2806 0.2153 0.2561 -0.0296 -0.0084 0.0212  331  GLU A CD  
878  O OE1 A GLU A 106 ? 0.2903 0.2237 0.2658 -0.0323 -0.0090 0.0193  331  GLU A OE1 
879  O OE1 B GLU A 106 ? 0.3359 0.2653 0.3102 -0.0293 -0.0069 0.0254  331  GLU A OE1 
880  O OE2 A GLU A 106 ? 0.2965 0.2184 0.2689 -0.0300 -0.0060 0.0264  331  GLU A OE2 
881  O OE2 B GLU A 106 ? 0.3489 0.2795 0.3236 -0.0335 -0.0093 0.0174  331  GLU A OE2 
882  N N   . TYR A 107 ? 0.1812 0.1620 0.1670 -0.0229 -0.0108 0.0232  332  TYR A N   
883  C CA  . TYR A 107 ? 0.1724 0.1619 0.1602 -0.0217 -0.0119 0.0206  332  TYR A CA  
884  C C   . TYR A 107 ? 0.2091 0.1977 0.1956 -0.0168 -0.0122 0.0196  332  TYR A C   
885  O O   . TYR A 107 ? 0.2028 0.1924 0.1883 -0.0134 -0.0120 0.0221  332  TYR A O   
886  C CB  . TYR A 107 ? 0.1500 0.1482 0.1391 -0.0218 -0.0115 0.0225  332  TYR A CB  
887  C CG  . TYR A 107 ? 0.1516 0.1512 0.1424 -0.0260 -0.0104 0.0244  332  TYR A CG  
888  C CD1 . TYR A 107 ? 0.1984 0.1934 0.1875 -0.0271 -0.0091 0.0282  332  TYR A CD1 
889  C CD2 . TYR A 107 ? 0.1951 0.2011 0.1893 -0.0288 -0.0106 0.0229  332  TYR A CD2 
890  C CE1 . TYR A 107 ? 0.1732 0.1700 0.1642 -0.0312 -0.0077 0.0302  332  TYR A CE1 
891  C CE2 . TYR A 107 ? 0.1566 0.1650 0.1532 -0.0325 -0.0094 0.0249  332  TYR A CE2 
892  C CZ  . TYR A 107 ? 0.2004 0.2044 0.1955 -0.0339 -0.0079 0.0285  332  TYR A CZ  
893  O OH  . TYR A 107 ? 0.1757 0.1824 0.1735 -0.0378 -0.0064 0.0308  332  TYR A OH  
894  N N   . HIS A 108 ? 0.1558 0.1428 0.1423 -0.0164 -0.0128 0.0160  333  HIS A N   
895  C CA  . HIS A 108 ? 0.1950 0.1812 0.1807 -0.0118 -0.0126 0.0150  333  HIS A CA  
896  C C   . HIS A 108 ? 0.1641 0.1600 0.1520 -0.0099 -0.0133 0.0143  333  HIS A C   
897  O O   . HIS A 108 ? 0.1658 0.1673 0.1553 -0.0123 -0.0138 0.0128  333  HIS A O   
898  C CB  . HIS A 108 ? 0.1937 0.1739 0.1777 -0.0120 -0.0125 0.0114  333  HIS A CB  
899  C CG  . HIS A 108 ? 0.2156 0.1854 0.1970 -0.0148 -0.0120 0.0111  333  HIS A CG  
900  N ND1 . HIS A 108 ? 0.2442 0.2114 0.2246 -0.0191 -0.0129 0.0081  333  HIS A ND1 
901  C CD2 . HIS A 108 ? 0.2468 0.2078 0.2261 -0.0142 -0.0109 0.0134  333  HIS A CD2 
902  C CE1 . HIS A 108 ? 0.2481 0.2052 0.2259 -0.0214 -0.0123 0.0083  333  HIS A CE1 
903  N NE2 . HIS A 108 ? 0.2324 0.1851 0.2094 -0.0184 -0.0110 0.0116  333  HIS A NE2 
904  N N   . LEU A 109 ? 0.1435 0.1416 0.1318 -0.0057 -0.0133 0.0154  334  LEU A N   
905  C CA  . LEU A 109 ? 0.1593 0.1667 0.1496 -0.0047 -0.0140 0.0149  334  LEU A CA  
906  C C   . LEU A 109 ? 0.1795 0.1891 0.1712 -0.0006 -0.0140 0.0144  334  LEU A C   
907  O O   . LEU A 109 ? 0.1661 0.1703 0.1571 0.0023  -0.0132 0.0150  334  LEU A O   
908  C CB  . LEU A 109 ? 0.1407 0.1525 0.1306 -0.0051 -0.0146 0.0178  334  LEU A CB  
909  C CG  . LEU A 109 ? 0.1737 0.1831 0.1621 -0.0023 -0.0146 0.0216  334  LEU A CG  
910  C CD1 . LEU A 109 ? 0.1681 0.1825 0.1579 0.0019  -0.0156 0.0224  334  LEU A CD1 
911  C CD2 . LEU A 109 ? 0.1617 0.1730 0.1482 -0.0041 -0.0147 0.0243  334  LEU A CD2 
912  N N   . ARG A 110 ? 0.1500 0.1675 0.1439 -0.0006 -0.0146 0.0132  335  ARG A N   
913  C CA  . ARG A 110 ? 0.1297 0.1524 0.1260 0.0027  -0.0148 0.0133  335  ARG A CA  
914  C C   . ARG A 110 ? 0.1583 0.1891 0.1556 0.0019  -0.0163 0.0143  335  ARG A C   
915  O O   . ARG A 110 ? 0.1536 0.1862 0.1500 -0.0012 -0.0165 0.0134  335  ARG A O   
916  C CB  . ARG A 110 ? 0.1785 0.2027 0.1763 0.0029  -0.0139 0.0102  335  ARG A CB  
917  C CG  . ARG A 110 ? 0.2623 0.2791 0.2585 0.0045  -0.0123 0.0088  335  ARG A CG  
918  C CD  . ARG A 110 ? 0.2047 0.2244 0.2020 0.0047  -0.0113 0.0060  335  ARG A CD  
919  N NE  . ARG A 110 ? 0.2945 0.3067 0.2886 0.0046  -0.0100 0.0037  335  ARG A NE  
920  C CZ  . ARG A 110 ? 0.2972 0.3054 0.2905 0.0081  -0.0082 0.0031  335  ARG A CZ  
921  N NH1 . ARG A 110 ? 0.2516 0.2635 0.2481 0.0122  -0.0075 0.0049  335  ARG A NH1 
922  N NH2 . ARG A 110 ? 0.5222 0.5227 0.5113 0.0075  -0.0070 0.0006  335  ARG A NH2 
923  N N   . ALA A 111 ? 0.1418 0.1778 0.1411 0.0048  -0.0172 0.0159  336  ALA A N   
924  C CA  . ALA A 111 ? 0.1380 0.1817 0.1377 0.0037  -0.0190 0.0166  336  ALA A CA  
925  C C   . ALA A 111 ? 0.1732 0.2242 0.1768 0.0063  -0.0200 0.0171  336  ALA A C   
926  O O   . ALA A 111 ? 0.1566 0.2065 0.1625 0.0098  -0.0192 0.0179  336  ALA A O   
927  C CB  . ALA A 111 ? 0.1152 0.1578 0.1116 0.0036  -0.0199 0.0196  336  ALA A CB  
928  N N   . ALA A 112 ? 0.1384 0.1970 0.1429 0.0044  -0.0217 0.0165  337  ALA A N   
929  C CA  . ALA A 112 ? 0.1064 0.1738 0.1153 0.0060  -0.0232 0.0171  337  ALA A CA  
930  C C   . ALA A 112 ? 0.1735 0.2474 0.1809 0.0034  -0.0258 0.0172  337  ALA A C   
931  O O   . ALA A 112 ? 0.1685 0.2402 0.1721 0.0000  -0.0256 0.0155  337  ALA A O   
932  C CB  . ALA A 112 ? 0.1419 0.2118 0.1547 0.0053  -0.0217 0.0143  337  ALA A CB  
933  N N   . GLY A 113 ? 0.1592 0.2414 0.1697 0.0051  -0.0281 0.0190  338  GLY A N   
934  C CA  . GLY A 113 ? 0.1739 0.2635 0.1835 0.0023  -0.0310 0.0185  338  GLY A CA  
935  C C   . GLY A 113 ? 0.1871 0.2851 0.2025 0.0006  -0.0317 0.0166  338  GLY A C   
936  O O   . GLY A 113 ? 0.1710 0.2689 0.1909 0.0017  -0.0296 0.0156  338  GLY A O   
937  N N   . LYS A 114 ? 0.1961 0.3014 0.2110 -0.0023 -0.0347 0.0159  339  LYS A N   
938  C CA  . LYS A 114 ? 0.2154 0.3288 0.2357 -0.0050 -0.0356 0.0140  339  LYS A CA  
939  C C   . LYS A 114 ? 0.2704 0.3943 0.2979 -0.0018 -0.0376 0.0169  339  LYS A C   
940  O O   . LYS A 114 ? 0.2697 0.4023 0.3026 -0.0043 -0.0388 0.0158  339  LYS A O   
941  C CB  . LYS A 114 ? 0.3217 0.4376 0.3379 -0.0104 -0.0379 0.0113  339  LYS A CB  
942  C CG  . LYS A 114 ? 0.6611 0.7670 0.6702 -0.0128 -0.0357 0.0088  339  LYS A CG  
943  C CD  . LYS A 114 ? 0.5500 0.6571 0.5539 -0.0175 -0.0376 0.0061  339  LYS A CD  
944  C CE  . LYS A 114 ? 0.4845 0.5949 0.4835 -0.0167 -0.0408 0.0083  339  LYS A CE  
945  N NZ  . LYS A 114 ? 0.6318 0.7415 0.6240 -0.0214 -0.0422 0.0051  339  LYS A NZ  
946  N N   . VAL A 115 ? 0.2030 0.3265 0.2310 0.0035  -0.0380 0.0208  340  VAL A N   
947  C CA  . VAL A 115 ? 0.1819 0.3155 0.2171 0.0076  -0.0397 0.0242  340  VAL A CA  
948  C C   . VAL A 115 ? 0.1822 0.3103 0.2203 0.0134  -0.0361 0.0260  340  VAL A C   
949  O O   . VAL A 115 ? 0.1772 0.2937 0.2107 0.0140  -0.0331 0.0250  340  VAL A O   
950  C CB  . VAL A 115 ? 0.2017 0.3411 0.2348 0.0094  -0.0440 0.0280  340  VAL A CB  
951  C CG1 . VAL A 115 ? 0.2507 0.3961 0.2806 0.0035  -0.0477 0.0258  340  VAL A CG1 
952  C CG2 . VAL A 115 ? 0.2387 0.3676 0.2647 0.0124  -0.0429 0.0304  340  VAL A CG2 
953  N N   . ALA A 116 ? 0.2190 0.3559 0.2648 0.0176  -0.0364 0.0286  341  ALA A N   
954  C CA  . ALA A 116 ? 0.2736 0.4059 0.3226 0.0232  -0.0326 0.0298  341  ALA A CA  
955  C C   . ALA A 116 ? 0.2150 0.3375 0.2588 0.0278  -0.0320 0.0328  341  ALA A C   
956  O O   . ALA A 116 ? 0.2054 0.3284 0.2454 0.0281  -0.0350 0.0355  341  ALA A O   
957  C CB  . ALA A 116 ? 0.3102 0.4553 0.3692 0.0270  -0.0330 0.0323  341  ALA A CB  
958  N N   . ASN A 117 ? 0.1798 0.2929 0.2230 0.0312  -0.0279 0.0324  342  ASN A N   
959  C CA  . ASN A 117 ? 0.1915 0.2939 0.2305 0.0359  -0.0265 0.0350  342  ASN A CA  
960  C C   . ASN A 117 ? 0.1514 0.2443 0.1818 0.0323  -0.0272 0.0345  342  ASN A C   
961  O O   . ASN A 117 ? 0.2194 0.3066 0.2460 0.0351  -0.0277 0.0378  342  ASN A O   
962  C CB  . ASN A 117 ? 0.2373 0.3461 0.2802 0.0422  -0.0283 0.0404  342  ASN A CB  
963  C CG  . ASN A 117 ? 0.4691 0.5841 0.5203 0.0475  -0.0260 0.0414  342  ASN A CG  
964  O OD1 . ASN A 117 ? 0.4764 0.5822 0.5269 0.0511  -0.0218 0.0406  342  ASN A OD1 
965  N ND2 . ASN A 117 ? 0.3792 0.5098 0.4382 0.0478  -0.0286 0.0429  342  ASN A ND2 
966  N N   . THR A 118 ? 0.1529 0.2437 0.1802 0.0264  -0.0270 0.0305  343  THR A N   
967  C CA  . THR A 118 ? 0.1911 0.2734 0.2111 0.0230  -0.0271 0.0298  343  THR A CA  
968  C C   . THR A 118 ? 0.1774 0.2496 0.1944 0.0205  -0.0239 0.0262  343  THR A C   
969  O O   . THR A 118 ? 0.1723 0.2376 0.1840 0.0178  -0.0237 0.0257  343  THR A O   
970  C CB  . THR A 118 ? 0.1641 0.2527 0.1818 0.0181  -0.0301 0.0287  343  THR A CB  
971  O OG1 . THR A 118 ? 0.1496 0.2433 0.1704 0.0143  -0.0299 0.0249  343  THR A OG1 
972  C CG2 . THR A 118 ? 0.1625 0.2604 0.1814 0.0201  -0.0339 0.0324  343  THR A CG2 
973  N N   . THR A 119 ? 0.1167 0.1884 0.1371 0.0214  -0.0215 0.0239  344  THR A N   
974  C CA  . THR A 119 ? 0.1293 0.1917 0.1464 0.0193  -0.0188 0.0208  344  THR A CA  
975  C C   . THR A 119 ? 0.1688 0.2204 0.1828 0.0225  -0.0170 0.0222  344  THR A C   
976  O O   . THR A 119 ? 0.1557 0.2065 0.1720 0.0276  -0.0158 0.0240  344  THR A O   
977  C CB  . THR A 119 ? 0.1572 0.2223 0.1779 0.0192  -0.0168 0.0180  344  THR A CB  
978  O OG1 . THR A 119 ? 0.1766 0.2499 0.1995 0.0152  -0.0182 0.0163  344  THR A OG1 
979  C CG2 . THR A 119 ? 0.1570 0.2121 0.1737 0.0178  -0.0142 0.0151  344  THR A CG2 
980  N N   . GLY A 120 ? 0.1712 0.2143 0.1801 0.0196  -0.0167 0.0214  345  GLY A N   
981  C CA  . GLY A 120 ? 0.1684 0.2005 0.1741 0.0219  -0.0150 0.0225  345  GLY A CA  
982  C C   . GLY A 120 ? 0.1788 0.2026 0.1801 0.0175  -0.0141 0.0202  345  GLY A C   
983  O O   . GLY A 120 ? 0.1538 0.1806 0.1545 0.0132  -0.0149 0.0182  345  GLY A O   
984  N N   . GLY A 121 ? 0.1679 0.1812 0.1663 0.0188  -0.0125 0.0205  346  GLY A N   
985  C CA  . GLY A 121 ? 0.2096 0.2148 0.2039 0.0145  -0.0121 0.0191  346  GLY A CA  
986  C C   . GLY A 121 ? 0.1925 0.1913 0.1841 0.0148  -0.0122 0.0227  346  GLY A C   
987  O O   . GLY A 121 ? 0.1806 0.1779 0.1725 0.0193  -0.0120 0.0259  346  GLY A O   
988  N N   . GLY A 122 ? 0.2111 0.2066 0.2003 0.0102  -0.0124 0.0225  347  GLY A N   
989  C CA  . GLY A 122 ? 0.1753 0.1637 0.1616 0.0098  -0.0120 0.0258  347  GLY A CA  
990  C C   . GLY A 122 ? 0.1876 0.1727 0.1722 0.0040  -0.0119 0.0245  347  GLY A C   
991  O O   . GLY A 122 ? 0.1762 0.1621 0.1614 0.0011  -0.0119 0.0208  347  GLY A O   
992  N N   . GLU A 123 ? 0.1678 0.1496 0.1503 0.0024  -0.0116 0.0278  348  GLU A N   
993  C CA  . GLU A 123 ? 0.1721 0.1521 0.1540 -0.0032 -0.0113 0.0270  348  GLU A CA  
994  C C   . GLU A 123 ? 0.2010 0.1828 0.1815 -0.0044 -0.0112 0.0312  348  GLU A C   
995  O O   . GLU A 123 ? 0.2042 0.1856 0.1832 -0.0009 -0.0113 0.0349  348  GLU A O   
996  C CB  . GLU A 123 ? 0.2055 0.1742 0.1857 -0.0054 -0.0101 0.0257  348  GLU A CB  
997  C CG  . GLU A 123 ? 0.2189 0.1773 0.1962 -0.0034 -0.0088 0.0293  348  GLU A CG  
998  C CD  . GLU A 123 ? 0.3208 0.2666 0.2957 -0.0052 -0.0076 0.0272  348  GLU A CD  
999  O OE1 . GLU A 123 ? 0.3363 0.2818 0.3115 -0.0067 -0.0079 0.0227  348  GLU A OE1 
1000 O OE2 . GLU A 123 ? 0.3205 0.2565 0.2929 -0.0053 -0.0062 0.0301  348  GLU A OE2 
1001 N N   . ILE A 124 ? 0.1823 0.1665 0.1635 -0.0091 -0.0109 0.0307  349  ILE A N   
1002 C CA  . ILE A 124 ? 0.1840 0.1685 0.1635 -0.0109 -0.0100 0.0346  349  ILE A CA  
1003 C C   . ILE A 124 ? 0.1998 0.1760 0.1790 -0.0151 -0.0086 0.0352  349  ILE A C   
1004 O O   . ILE A 124 ? 0.2097 0.1869 0.1911 -0.0192 -0.0087 0.0324  349  ILE A O   
1005 C CB  . ILE A 124 ? 0.1839 0.1784 0.1645 -0.0129 -0.0103 0.0339  349  ILE A CB  
1006 C CG1 . ILE A 124 ? 0.1520 0.1541 0.1329 -0.0095 -0.0118 0.0325  349  ILE A CG1 
1007 C CG2 . ILE A 124 ? 0.1799 0.1747 0.1579 -0.0143 -0.0089 0.0382  349  ILE A CG2 
1008 C CD1 . ILE A 124 ? 0.2233 0.2337 0.2051 -0.0114 -0.0119 0.0306  349  ILE A CD1 
1009 N N   . LYS A 125 ? 0.1834 0.1511 0.1598 -0.0143 -0.0075 0.0390  350  LYS A N   
1010 C CA  . LYS A 125 ? 0.2166 0.1759 0.1925 -0.0190 -0.0060 0.0399  350  LYS A CA  
1011 C C   . LYS A 125 ? 0.2230 0.1885 0.2004 -0.0235 -0.0051 0.0416  350  LYS A C   
1012 O O   . LYS A 125 ? 0.2189 0.1920 0.1956 -0.0220 -0.0049 0.0436  350  LYS A O   
1013 C CB  . LYS A 125 ? 0.2519 0.2001 0.2241 -0.0167 -0.0047 0.0441  350  LYS A CB  
1014 C CG  . LYS A 125 ? 0.3218 0.2629 0.2928 -0.0120 -0.0050 0.0424  350  LYS A CG  
1015 C CD  . LYS A 125 ? 0.4321 0.3621 0.3994 -0.0084 -0.0035 0.0469  350  LYS A CD  
1016 C CE  . LYS A 125 ? 0.4628 0.3850 0.4293 -0.0038 -0.0033 0.0445  350  LYS A CE  
1017 N NZ  . LYS A 125 ? 0.3347 0.2669 0.3039 0.0004  -0.0049 0.0414  350  LYS A NZ  
1018 N N   . SER A 126 ? 0.2202 0.1827 0.1997 -0.0291 -0.0044 0.0406  351  SER A N   
1019 C CA  . SER A 126 ? 0.1825 0.1518 0.1647 -0.0336 -0.0032 0.0421  351  SER A CA  
1020 C C   . SER A 126 ? 0.2591 0.2293 0.2383 -0.0323 -0.0013 0.0475  351  SER A C   
1021 O O   . SER A 126 ? 0.2299 0.2093 0.2098 -0.0323 -0.0006 0.0483  351  SER A O   
1022 C CB  . SER A 126 ? 0.2284 0.1928 0.2131 -0.0400 -0.0027 0.0415  351  SER A CB  
1023 O OG  . SER A 126 ? 0.2223 0.1952 0.2109 -0.0440 -0.0015 0.0428  351  SER A OG  
1024 N N   . THR A 127 ? 0.2393 0.1997 0.2148 -0.0311 -0.0002 0.0513  352  THR A N   
1025 C CA  . THR A 127 ? 0.2412 0.2017 0.2130 -0.0301 0.0017  0.0569  352  THR A CA  
1026 C C   . THR A 127 ? 0.2253 0.1942 0.1945 -0.0249 0.0005  0.0575  352  THR A C   
1027 O O   . THR A 127 ? 0.2689 0.2419 0.2354 -0.0247 0.0019  0.0611  352  THR A O   
1028 C CB  . THR A 127 ? 0.2886 0.2358 0.2565 -0.0291 0.0029  0.0610  352  THR A CB  
1029 O OG1 . THR A 127 ? 0.4022 0.3494 0.3662 -0.0285 0.0049  0.0670  352  THR A OG1 
1030 C CG2 . THR A 127 ? 0.2782 0.2209 0.2439 -0.0229 0.0011  0.0600  352  THR A CG2 
1031 N N   . ASP A 128 ? 0.2007 0.1724 0.1707 -0.0211 -0.0019 0.0539  353  ASP A N   
1032 C CA  . ASP A 128 ? 0.1937 0.1738 0.1618 -0.0169 -0.0035 0.0537  353  ASP A CA  
1033 C C   . ASP A 128 ? 0.2263 0.2167 0.1974 -0.0184 -0.0040 0.0496  353  ASP A C   
1034 O O   . ASP A 128 ? 0.2043 0.2017 0.1737 -0.0158 -0.0052 0.0490  353  ASP A O   
1035 C CB  . ASP A 128 ? 0.1956 0.1734 0.1635 -0.0118 -0.0056 0.0525  353  ASP A CB  
1036 C CG  . ASP A 128 ? 0.2599 0.2280 0.2244 -0.0088 -0.0050 0.0571  353  ASP A CG  
1037 O OD1 . ASP A 128 ? 0.2643 0.2309 0.2251 -0.0087 -0.0038 0.0622  353  ASP A OD1 
1038 O OD2 . ASP A 128 ? 0.2766 0.2384 0.2420 -0.0061 -0.0056 0.0559  353  ASP A OD2 
1039 N N   . TYR A 129 ? 0.1861 0.1776 0.1614 -0.0226 -0.0033 0.0469  354  TYR A N   
1040 C CA  . TYR A 129 ? 0.2038 0.2045 0.1820 -0.0236 -0.0036 0.0434  354  TYR A CA  
1041 C C   . TYR A 129 ? 0.1814 0.1874 0.1584 -0.0253 -0.0012 0.0459  354  TYR A C   
1042 O O   . TYR A 129 ? 0.2141 0.2221 0.1944 -0.0291 0.0006  0.0462  354  TYR A O   
1043 C CB  . TYR A 129 ? 0.1891 0.1895 0.1724 -0.0269 -0.0041 0.0397  354  TYR A CB  
1044 C CG  . TYR A 129 ? 0.2094 0.2185 0.1956 -0.0268 -0.0047 0.0361  354  TYR A CG  
1045 C CD1 . TYR A 129 ? 0.2234 0.2349 0.2091 -0.0235 -0.0066 0.0331  354  TYR A CD1 
1046 C CD2 . TYR A 129 ? 0.1753 0.1902 0.1648 -0.0298 -0.0032 0.0360  354  TYR A CD2 
1047 C CE1 . TYR A 129 ? 0.2076 0.2259 0.1955 -0.0234 -0.0070 0.0300  354  TYR A CE1 
1048 C CE2 . TYR A 129 ? 0.1917 0.2138 0.1837 -0.0291 -0.0036 0.0329  354  TYR A CE2 
1049 C CZ  . TYR A 129 ? 0.2153 0.2385 0.2061 -0.0260 -0.0054 0.0300  354  TYR A CZ  
1050 O OH  . TYR A 129 ? 0.1986 0.2277 0.1914 -0.0254 -0.0056 0.0272  354  TYR A OH  
1051 N N   . THR A 130 ? 0.1872 0.1959 0.1593 -0.0224 -0.0012 0.0478  355  THR A N   
1052 C CA  . THR A 130 ? 0.1777 0.1910 0.1469 -0.0234 0.0013  0.0502  355  THR A CA  
1053 C C   . THR A 130 ? 0.1661 0.1863 0.1323 -0.0208 0.0003  0.0478  355  THR A C   
1054 O O   . THR A 130 ? 0.2053 0.2269 0.1655 -0.0190 0.0005  0.0501  355  THR A O   
1055 C CB  . THR A 130 ? 0.2113 0.2195 0.1756 -0.0231 0.0028  0.0559  355  THR A CB  
1056 O OG1 . THR A 130 ? 0.2335 0.2384 0.1937 -0.0190 0.0004  0.0573  355  THR A OG1 
1057 C CG2 . THR A 130 ? 0.2185 0.2195 0.1859 -0.0267 0.0044  0.0581  355  THR A CG2 
1058 N N   . PRO A 131 ? 0.1999 0.2244 0.1698 -0.0209 -0.0006 0.0431  356  PRO A N   
1059 C CA  . PRO A 131 ? 0.1871 0.2168 0.1541 -0.0186 -0.0018 0.0404  356  PRO A CA  
1060 C C   . PRO A 131 ? 0.2154 0.2492 0.1779 -0.0190 0.0007  0.0411  356  PRO A C   
1061 O O   . PRO A 131 ? 0.2105 0.2473 0.1683 -0.0172 -0.0003 0.0397  356  PRO A O   
1062 C CB  . PRO A 131 ? 0.1659 0.1979 0.1384 -0.0192 -0.0027 0.0357  356  PRO A CB  
1063 C CG  . PRO A 131 ? 0.1763 0.2072 0.1540 -0.0223 -0.0010 0.0363  356  PRO A CG  
1064 C CD  . PRO A 131 ? 0.1773 0.2019 0.1539 -0.0231 -0.0007 0.0403  356  PRO A CD  
1065 N N   . ALA A 132 ? 0.1812 0.2156 0.1451 -0.0213 0.0042  0.0432  357  ALA A N   
1066 C CA  . ALA A 132 ? 0.2146 0.2527 0.1736 -0.0212 0.0072  0.0441  357  ALA A CA  
1067 C C   . ALA A 132 ? 0.2849 0.3216 0.2353 -0.0194 0.0066  0.0473  357  ALA A C   
1068 O O   . ALA A 132 ? 0.2576 0.2971 0.2018 -0.0187 0.0082  0.0470  357  ALA A O   
1069 C CB  . ALA A 132 ? 0.2012 0.2407 0.1638 -0.0239 0.0113  0.0466  357  ALA A CB  
1070 N N   . LEU A 133 ? 0.1890 0.2210 0.1384 -0.0185 0.0044  0.0503  358  LEU A N   
1071 C CA  . LEU A 133 ? 0.2325 0.2634 0.1737 -0.0165 0.0035  0.0539  358  LEU A CA  
1072 C C   . LEU A 133 ? 0.2772 0.3113 0.2147 -0.0139 -0.0003 0.0511  358  LEU A C   
1073 O O   . LEU A 133 ? 0.3028 0.3378 0.2329 -0.0122 -0.0015 0.0536  358  LEU A O   
1074 C CB  . LEU A 133 ? 0.2767 0.3009 0.2182 -0.0160 0.0028  0.0587  358  LEU A CB  
1075 C CG  . LEU A 133 ? 0.3177 0.3379 0.2625 -0.0193 0.0064  0.0618  358  LEU A CG  
1076 C CD1 . LEU A 133 ? 0.2810 0.2931 0.2251 -0.0188 0.0059  0.0665  358  LEU A CD1 
1077 C CD2 . LEU A 133 ? 0.2609 0.2845 0.2015 -0.0208 0.0106  0.0641  358  LEU A CD2 
1078 N N   . GLY A 134 ? 0.2391 0.2754 0.1816 -0.0138 -0.0023 0.0462  359  GLY A N   
1079 C CA  . GLY A 134 ? 0.2511 0.2912 0.1909 -0.0122 -0.0056 0.0431  359  GLY A CA  
1080 C C   . GLY A 134 ? 0.2377 0.2772 0.1815 -0.0103 -0.0094 0.0426  359  GLY A C   
1081 O O   . GLY A 134 ? 0.2416 0.2850 0.1845 -0.0093 -0.0123 0.0399  359  GLY A O   
1082 N N   . GLY A 135 ? 0.2206 0.2551 0.1686 -0.0098 -0.0094 0.0450  360  GLY A N   
1083 C CA  . GLY A 135 ? 0.2668 0.3002 0.2185 -0.0075 -0.0124 0.0447  360  GLY A CA  
1084 C C   . GLY A 135 ? 0.2135 0.2407 0.1708 -0.0082 -0.0111 0.0452  360  GLY A C   
1085 O O   . GLY A 135 ? 0.2402 0.2641 0.1984 -0.0107 -0.0084 0.0462  360  GLY A O   
1086 N N   . VAL A 136 ? 0.2409 0.2666 0.2018 -0.0060 -0.0132 0.0442  361  VAL A N   
1087 C CA  . VAL A 136 ? 0.2113 0.2298 0.1762 -0.0063 -0.0122 0.0446  361  VAL A CA  
1088 C C   . VAL A 136 ? 0.1990 0.2144 0.1641 -0.0022 -0.0140 0.0469  361  VAL A C   
1089 O O   . VAL A 136 ? 0.2240 0.2446 0.1897 0.0005  -0.0165 0.0460  361  VAL A O   
1090 C CB  . VAL A 136 ? 0.2383 0.2573 0.2086 -0.0083 -0.0120 0.0397  361  VAL A CB  
1091 C CG1 . VAL A 136 ? 0.2605 0.2806 0.2318 -0.0122 -0.0096 0.0385  361  VAL A CG1 
1092 C CG2 . VAL A 136 ? 0.2499 0.2750 0.2219 -0.0068 -0.0141 0.0360  361  VAL A CG2 
1093 N N   . LYS A 137 ? 0.1889 0.1956 0.1537 -0.0019 -0.0126 0.0499  362  LYS A N   
1094 C CA  . LYS A 137 ? 0.1849 0.1866 0.1502 0.0023  -0.0136 0.0521  362  LYS A CA  
1095 C C   . LYS A 137 ? 0.2284 0.2261 0.1984 0.0020  -0.0132 0.0481  362  LYS A C   
1096 O O   . LYS A 137 ? 0.2111 0.2026 0.1821 -0.0013 -0.0114 0.0468  362  LYS A O   
1097 C CB  . LYS A 137 ? 0.1977 0.1907 0.1593 0.0029  -0.0119 0.0577  362  LYS A CB  
1098 C CG  . LYS A 137 ? 0.2197 0.2059 0.1816 0.0077  -0.0123 0.0604  362  LYS A CG  
1099 C CD  . LYS A 137 ? 0.3002 0.2760 0.2583 0.0075  -0.0101 0.0657  362  LYS A CD  
1100 C CE  . LYS A 137 ? 0.3859 0.3535 0.3440 0.0128  -0.0100 0.0686  362  LYS A CE  
1101 N NZ  . LYS A 137 ? 0.3652 0.3205 0.3196 0.0120  -0.0074 0.0734  362  LYS A NZ  
1102 N N   . ILE A 138 ? 0.1759 0.1778 0.1486 0.0052  -0.0150 0.0460  363  ILE A N   
1103 C CA  . ILE A 138 ? 0.1778 0.1764 0.1542 0.0056  -0.0146 0.0422  363  ILE A CA  
1104 C C   . ILE A 138 ? 0.2169 0.2073 0.1929 0.0100  -0.0139 0.0449  363  ILE A C   
1105 O O   . ILE A 138 ? 0.2429 0.2359 0.2183 0.0145  -0.0151 0.0484  363  ILE A O   
1106 C CB  . ILE A 138 ? 0.1542 0.1619 0.1340 0.0065  -0.0162 0.0385  363  ILE A CB  
1107 C CG1 . ILE A 138 ? 0.1933 0.2075 0.1730 0.0024  -0.0165 0.0358  363  ILE A CG1 
1108 C CG2 . ILE A 138 ? 0.1526 0.1565 0.1355 0.0075  -0.0155 0.0351  363  ILE A CG2 
1109 C CD1 . ILE A 138 ? 0.1822 0.2055 0.1646 0.0029  -0.0182 0.0325  363  ILE A CD1 
1110 N N   . THR A 139 ? 0.2019 0.1823 0.1779 0.0087  -0.0121 0.0436  364  THR A N   
1111 C CA  . THR A 139 ? 0.2169 0.1875 0.1919 0.0128  -0.0109 0.0456  364  THR A CA  
1112 C C   . THR A 139 ? 0.2142 0.1823 0.1916 0.0140  -0.0103 0.0410  364  THR A C   
1113 O O   . THR A 139 ? 0.2129 0.1863 0.1925 0.0112  -0.0108 0.0366  364  THR A O   
1114 C CB  . THR A 139 ? 0.2477 0.2062 0.2191 0.0101  -0.0088 0.0483  364  THR A CB  
1115 O OG1 . THR A 139 ? 0.2415 0.1976 0.2135 0.0039  -0.0081 0.0445  364  THR A OG1 
1116 C CG2 . THR A 139 ? 0.2945 0.2553 0.2630 0.0099  -0.0091 0.0537  364  THR A CG2 
1117 N N   . ALA A 140 ? 0.2303 0.1901 0.2070 0.0187  -0.0090 0.0423  365  ALA A N   
1118 C CA  . ALA A 140 ? 0.2190 0.1764 0.1975 0.0213  -0.0080 0.0385  365  ALA A CA  
1119 C C   . ALA A 140 ? 0.2217 0.1927 0.2046 0.0229  -0.0096 0.0363  365  ALA A C   
1120 O O   . ALA A 140 ? 0.2493 0.2215 0.2339 0.0226  -0.0090 0.0320  365  ALA A O   
1121 C CB  . ALA A 140 ? 0.2493 0.1984 0.2260 0.0163  -0.0067 0.0338  365  ALA A CB  
1122 N N   . TRP A 141 ? 0.1897 0.1709 0.1742 0.0245  -0.0117 0.0394  366  TRP A N   
1123 C CA  . TRP A 141 ? 0.2060 0.2002 0.1947 0.0255  -0.0135 0.0377  366  TRP A CA  
1124 C C   . TRP A 141 ? 0.2168 0.2125 0.2089 0.0319  -0.0128 0.0384  366  TRP A C   
1125 O O   . TRP A 141 ? 0.2571 0.2506 0.2490 0.0369  -0.0127 0.0429  366  TRP A O   
1126 C CB  . TRP A 141 ? 0.2045 0.2085 0.1931 0.0246  -0.0161 0.0405  366  TRP A CB  
1127 C CG  . TRP A 141 ? 0.1603 0.1773 0.1530 0.0254  -0.0181 0.0390  366  TRP A CG  
1128 C CD1 . TRP A 141 ? 0.1738 0.1991 0.1695 0.0298  -0.0200 0.0419  366  TRP A CD1 
1129 C CD2 . TRP A 141 ? 0.1634 0.1867 0.1581 0.0215  -0.0186 0.0345  366  TRP A CD2 
1130 N NE1 . TRP A 141 ? 0.1768 0.2132 0.1764 0.0283  -0.0216 0.0392  366  TRP A NE1 
1131 C CE2 . TRP A 141 ? 0.1978 0.2325 0.1965 0.0233  -0.0206 0.0347  366  TRP A CE2 
1132 C CE3 . TRP A 141 ? 0.1708 0.1913 0.1645 0.0166  -0.0176 0.0305  366  TRP A CE3 
1133 C CZ2 . TRP A 141 ? 0.2140 0.2563 0.2152 0.0202  -0.0213 0.0309  366  TRP A CZ2 
1134 C CZ3 . TRP A 141 ? 0.1944 0.2225 0.1905 0.0142  -0.0183 0.0271  366  TRP A CZ3 
1135 C CH2 . TRP A 141 ? 0.1766 0.2149 0.1763 0.0159  -0.0200 0.0272  366  TRP A CH2 
1136 N N   . ASP A 142 ? 0.2010 0.2008 0.1963 0.0321  -0.0121 0.0345  367  ASP A N   
1137 C CA  . ASP A 142 ? 0.2230 0.2221 0.2213 0.0381  -0.0103 0.0345  367  ASP A CA  
1138 C C   . ASP A 142 ? 0.2829 0.2965 0.2875 0.0410  -0.0118 0.0353  367  ASP A C   
1139 O O   . ASP A 142 ? 0.2773 0.2923 0.2854 0.0456  -0.0100 0.0348  367  ASP A O   
1140 C CB  . ASP A 142 ? 0.2008 0.1916 0.1974 0.0369  -0.0075 0.0296  367  ASP A CB  
1141 C CG  . ASP A 142 ? 0.2497 0.2476 0.2478 0.0323  -0.0081 0.0252  367  ASP A CG  
1142 O OD1 . ASP A 142 ? 0.1971 0.2069 0.1987 0.0309  -0.0103 0.0255  367  ASP A OD1 
1143 O OD2 . ASP A 142 ? 0.2640 0.2550 0.2594 0.0300  -0.0065 0.0213  367  ASP A OD2 
1144 N N   . ALA A 143 ? 0.1905 0.2149 0.1966 0.0384  -0.0150 0.0364  368  ALA A N   
1145 C CA  . ALA A 143 ? 0.1736 0.2121 0.1858 0.0408  -0.0169 0.0374  368  ALA A CA  
1146 C C   . ALA A 143 ? 0.2136 0.2567 0.2266 0.0450  -0.0192 0.0432  368  ALA A C   
1147 O O   . ALA A 143 ? 0.2179 0.2548 0.2260 0.0447  -0.0199 0.0461  368  ALA A O   
1148 C CB  . ALA A 143 ? 0.1882 0.2359 0.2014 0.0349  -0.0190 0.0345  368  ALA A CB  
1149 N N   . THR A 144 ? 0.2007 0.2554 0.2202 0.0490  -0.0205 0.0450  369  THR A N   
1150 C CA  . THR A 144 ? 0.1875 0.2482 0.2085 0.0536  -0.0232 0.0508  369  THR A CA  
1151 C C   . THR A 144 ? 0.2417 0.3107 0.2603 0.0492  -0.0274 0.0519  369  THR A C   
1152 O O   . THR A 144 ? 0.2678 0.3372 0.2836 0.0514  -0.0295 0.0566  369  THR A O   
1153 C CB  . THR A 144 ? 0.2638 0.3354 0.2933 0.0595  -0.0233 0.0527  369  THR A CB  
1154 O OG1 . THR A 144 ? 0.2952 0.3799 0.3298 0.0555  -0.0250 0.0496  369  THR A OG1 
1155 C CG2 . THR A 144 ? 0.2759 0.3384 0.3069 0.0642  -0.0185 0.0514  369  THR A CG2 
1156 N N   . GLY A 145 ? 0.1909 0.2662 0.2102 0.0433  -0.0285 0.0476  370  GLY A N   
1157 C CA  . GLY A 145 ? 0.1735 0.2548 0.1894 0.0385  -0.0319 0.0474  370  GLY A CA  
1158 C C   . GLY A 145 ? 0.2221 0.2943 0.2317 0.0328  -0.0304 0.0439  370  GLY A C   
1159 O O   . GLY A 145 ? 0.1781 0.2400 0.1864 0.0323  -0.0271 0.0419  370  GLY A O   
1160 N N   . PRO A 146 ? 0.1629 0.2392 0.1687 0.0282  -0.0327 0.0431  371  PRO A N   
1161 C CA  . PRO A 146 ? 0.1570 0.2456 0.1633 0.0274  -0.0369 0.0445  371  PRO A CA  
1162 C C   . PRO A 146 ? 0.1764 0.2667 0.1793 0.0308  -0.0395 0.0502  371  PRO A C   
1163 O O   . PRO A 146 ? 0.2035 0.2845 0.2022 0.0332  -0.0379 0.0535  371  PRO A O   
1164 C CB  . PRO A 146 ? 0.1936 0.2818 0.1952 0.0208  -0.0373 0.0405  371  PRO A CB  
1165 C CG  . PRO A 146 ? 0.1593 0.2348 0.1555 0.0198  -0.0341 0.0405  371  PRO A CG  
1166 C CD  . PRO A 146 ? 0.1533 0.2219 0.1534 0.0232  -0.0311 0.0405  371  PRO A CD  
1167 N N   . SER A 147 ? 0.1999 0.3027 0.2046 0.0308  -0.0437 0.0516  372  SER A N   
1168 C CA  . SER A 147 ? 0.1688 0.2746 0.1681 0.0323  -0.0469 0.0564  372  SER A CA  
1169 C C   . SER A 147 ? 0.1745 0.2758 0.1648 0.0268  -0.0468 0.0543  372  SER A C   
1170 O O   . SER A 147 ? 0.1949 0.2911 0.1840 0.0224  -0.0443 0.0495  372  SER A O   
1171 C CB  . SER A 147 ? 0.3244 0.4458 0.3282 0.0333  -0.0519 0.0580  372  SER A CB  
1172 O OG  . SER A 147 ? 0.3949 0.5214 0.4079 0.0387  -0.0515 0.0600  372  SER A OG  
1173 N N   . ALA A 148 ? 0.1930 0.2963 0.1768 0.0275  -0.0494 0.0582  373  ALA A N   
1174 C CA  . ALA A 148 ? 0.1862 0.2859 0.1611 0.0227  -0.0491 0.0565  373  ALA A CA  
1175 C C   . ALA A 148 ? 0.2133 0.3204 0.1877 0.0170  -0.0511 0.0509  373  ALA A C   
1176 O O   . ALA A 148 ? 0.1683 0.2862 0.1477 0.0167  -0.0545 0.0499  373  ALA A O   
1177 C CB  . ALA A 148 ? 0.1936 0.2945 0.1609 0.0249  -0.0516 0.0622  373  ALA A CB  
1178 N N   . GLY A 149 ? 0.1947 0.2959 0.1632 0.0125  -0.0488 0.0474  374  GLY A N   
1179 C CA  . GLY A 149 ? 0.1787 0.2849 0.1444 0.0072  -0.0504 0.0423  374  GLY A CA  
1180 C C   . GLY A 149 ? 0.1873 0.2947 0.1598 0.0043  -0.0491 0.0369  374  GLY A C   
1181 O O   . GLY A 149 ? 0.2003 0.3127 0.1717 0.0001  -0.0509 0.0329  374  GLY A O   
1182 N N   . VAL A 150 ? 0.1449 0.2473 0.1236 0.0064  -0.0461 0.0367  375  VAL A N   
1183 C CA  . VAL A 150 ? 0.1410 0.2446 0.1263 0.0044  -0.0447 0.0323  375  VAL A CA  
1184 C C   . VAL A 150 ? 0.1647 0.2589 0.1476 0.0015  -0.0406 0.0288  375  VAL A C   
1185 O O   . VAL A 150 ? 0.1558 0.2417 0.1366 0.0030  -0.0379 0.0305  375  VAL A O   
1186 C CB  . VAL A 150 ? 0.2110 0.3162 0.2048 0.0089  -0.0440 0.0344  375  VAL A CB  
1187 C CG1 . VAL A 150 ? 0.1615 0.2662 0.1611 0.0070  -0.0418 0.0301  375  VAL A CG1 
1188 C CG2 . VAL A 150 ? 0.2345 0.3509 0.2321 0.0119  -0.0482 0.0379  375  VAL A CG2 
1189 N N   . GLU A 151 ? 0.1598 0.2553 0.1433 -0.0026 -0.0402 0.0240  376  GLU A N   
1190 C CA  . GLU A 151 ? 0.1494 0.2370 0.1314 -0.0050 -0.0364 0.0208  376  GLU A CA  
1191 C C   . GLU A 151 ? 0.1694 0.2526 0.1573 -0.0029 -0.0338 0.0207  376  GLU A C   
1192 O O   . GLU A 151 ? 0.1953 0.2828 0.1894 -0.0018 -0.0344 0.0203  376  GLU A O   
1193 C CB  . GLU A 151 ? 0.2229 0.3126 0.2042 -0.0095 -0.0366 0.0159  376  GLU A CB  
1194 C CG  . GLU A 151 ? 0.4844 0.5741 0.4575 -0.0123 -0.0375 0.0145  376  GLU A CG  
1195 C CD  . GLU A 151 ? 0.4959 0.5819 0.4669 -0.0162 -0.0353 0.0096  376  GLU A CD  
1196 O OE1 . GLU A 151 ? 0.6523 0.7335 0.6267 -0.0162 -0.0323 0.0082  376  GLU A OE1 
1197 O OE2 . GLU A 151 ? 0.7395 0.8272 0.7051 -0.0192 -0.0367 0.0072  376  GLU A OE2 
1198 N N   . MET A 152 ? 0.1345 0.2095 0.1204 -0.0027 -0.0309 0.0210  377  MET A N   
1199 C CA  . MET A 152 ? 0.1558 0.2256 0.1459 -0.0013 -0.0285 0.0205  377  MET A CA  
1200 C C   . MET A 152 ? 0.1600 0.2248 0.1488 -0.0044 -0.0259 0.0173  377  MET A C   
1201 O O   . MET A 152 ? 0.1788 0.2414 0.1630 -0.0062 -0.0251 0.0172  377  MET A O   
1202 C CB  . MET A 152 ? 0.1446 0.2087 0.1340 0.0020  -0.0276 0.0243  377  MET A CB  
1203 C CG  . MET A 152 ? 0.1405 0.2090 0.1315 0.0060  -0.0299 0.0281  377  MET A CG  
1204 S SD  . MET A 152 ? 0.1638 0.2371 0.1628 0.0088  -0.0300 0.0272  377  MET A SD  
1205 C CE  . MET A 152 ? 0.1547 0.2170 0.1546 0.0104  -0.0263 0.0267  377  MET A CE  
1206 N N   A THR A 153 ? 0.1314 0.1948 0.1241 -0.0046 -0.0245 0.0151  378  THR A N   
1207 N N   B THR A 153 ? 0.1331 0.1968 0.1258 -0.0047 -0.0246 0.0150  378  THR A N   
1208 C CA  A THR A 153 ? 0.1245 0.1834 0.1167 -0.0068 -0.0222 0.0126  378  THR A CA  
1209 C CA  B THR A 153 ? 0.1266 0.1855 0.1188 -0.0068 -0.0222 0.0127  378  THR A CA  
1210 C C   A THR A 153 ? 0.1248 0.1788 0.1196 -0.0053 -0.0207 0.0128  378  THR A C   
1211 C C   B THR A 153 ? 0.1244 0.1782 0.1190 -0.0051 -0.0208 0.0131  378  THR A C   
1212 O O   A THR A 153 ? 0.1379 0.1933 0.1360 -0.0032 -0.0210 0.0130  378  THR A O   
1213 O O   B THR A 153 ? 0.1462 0.2009 0.1438 -0.0027 -0.0211 0.0138  378  THR A O   
1214 C CB  A THR A 153 ? 0.2029 0.2646 0.1962 -0.0093 -0.0221 0.0092  378  THR A CB  
1215 C CB  B THR A 153 ? 0.2023 0.2636 0.1959 -0.0093 -0.0219 0.0092  378  THR A CB  
1216 O OG1 A THR A 153 ? 0.2925 0.3588 0.2833 -0.0109 -0.0239 0.0087  378  THR A OG1 
1217 O OG1 B THR A 153 ? 0.1811 0.2468 0.1792 -0.0083 -0.0228 0.0087  378  THR A OG1 
1218 C CG2 A THR A 153 ? 0.1393 0.1965 0.1313 -0.0112 -0.0198 0.0074  378  THR A CG2 
1219 C CG2 B THR A 153 ? 0.2811 0.3450 0.2709 -0.0116 -0.0227 0.0079  378  THR A CG2 
1220 N N   . GLY A 154 ? 0.1310 0.1797 0.1244 -0.0065 -0.0191 0.0125  379  GLY A N   
1221 C CA  . GLY A 154 ? 0.1465 0.1901 0.1413 -0.0056 -0.0180 0.0125  379  GLY A CA  
1222 C C   . GLY A 154 ? 0.1877 0.2279 0.1822 -0.0079 -0.0167 0.0109  379  GLY A C   
1223 O O   . GLY A 154 ? 0.1328 0.1747 0.1263 -0.0098 -0.0162 0.0099  379  GLY A O   
1224 N N   A GLN A 155 ? 0.1479 0.1832 0.1429 -0.0075 -0.0160 0.0107  380  GLN A N   
1225 N N   B GLN A 155 ? 0.1471 0.1824 0.1421 -0.0075 -0.0160 0.0108  380  GLN A N   
1226 C CA  A GLN A 155 ? 0.1273 0.1600 0.1224 -0.0098 -0.0152 0.0094  380  GLN A CA  
1227 C CA  B GLN A 155 ? 0.1271 0.1599 0.1223 -0.0097 -0.0152 0.0093  380  GLN A CA  
1228 C C   A GLN A 155 ? 0.1458 0.1724 0.1400 -0.0101 -0.0149 0.0105  380  GLN A C   
1229 C C   B GLN A 155 ? 0.1463 0.1728 0.1405 -0.0101 -0.0149 0.0104  380  GLN A C   
1230 O O   A GLN A 155 ? 0.1401 0.1631 0.1339 -0.0080 -0.0150 0.0110  380  GLN A O   
1231 O O   B GLN A 155 ? 0.1409 0.1637 0.1347 -0.0080 -0.0149 0.0109  380  GLN A O   
1232 C CB  A GLN A 155 ? 0.1430 0.1767 0.1395 -0.0099 -0.0149 0.0068  380  GLN A CB  
1233 C CB  B GLN A 155 ? 0.1296 0.1632 0.1262 -0.0095 -0.0150 0.0068  380  GLN A CB  
1234 C CG  A GLN A 155 ? 0.0967 0.1289 0.0932 -0.0120 -0.0145 0.0057  380  GLN A CG  
1235 C CG  B GLN A 155 ? 0.1922 0.2257 0.1897 -0.0068 -0.0150 0.0066  380  GLN A CG  
1236 C CD  A GLN A 155 ? 0.1110 0.1444 0.1082 -0.0120 -0.0143 0.0036  380  GLN A CD  
1237 C CD  B GLN A 155 ? 0.2134 0.2491 0.2123 -0.0066 -0.0144 0.0044  380  GLN A CD  
1238 O OE1 A GLN A 155 ? 0.1260 0.1617 0.1239 -0.0108 -0.0140 0.0029  380  GLN A OE1 
1239 O OE1 B GLN A 155 ? 0.1791 0.2196 0.1792 -0.0074 -0.0144 0.0037  380  GLN A OE1 
1240 N NE2 A GLN A 155 ? 0.1184 0.1507 0.1155 -0.0135 -0.0143 0.0029  380  GLN A NE2 
1241 N NE2 B GLN A 155 ? 0.1549 0.1869 0.1532 -0.0058 -0.0136 0.0033  380  GLN A NE2 
1242 N N   . ILE A 156 ? 0.1377 0.1631 0.1318 -0.0126 -0.0146 0.0108  381  ILE A N   
1243 C CA  . ILE A 156 ? 0.1534 0.1729 0.1468 -0.0141 -0.0144 0.0115  381  ILE A CA  
1244 C C   . ILE A 156 ? 0.1118 0.1296 0.1057 -0.0152 -0.0147 0.0088  381  ILE A C   
1245 O O   . ILE A 156 ? 0.1662 0.1879 0.1614 -0.0165 -0.0149 0.0076  381  ILE A O   
1246 C CB  . ILE A 156 ? 0.1941 0.2141 0.1877 -0.0167 -0.0138 0.0136  381  ILE A CB  
1247 C CG1 . ILE A 156 ? 0.2355 0.2557 0.2273 -0.0152 -0.0134 0.0165  381  ILE A CG1 
1248 C CG2 . ILE A 156 ? 0.1618 0.1763 0.1555 -0.0194 -0.0138 0.0137  381  ILE A CG2 
1249 C CD1 . ILE A 156 ? 0.2723 0.2940 0.2637 -0.0173 -0.0123 0.0188  381  ILE A CD1 
1250 N N   A GLU A 157 ? 0.1476 0.1595 0.1400 -0.0144 -0.0148 0.0079  382  GLU A N   
1251 N N   B GLU A 157 ? 0.1478 0.1596 0.1401 -0.0143 -0.0147 0.0080  382  GLU A N   
1252 C CA  A GLU A 157 ? 0.1547 0.1649 0.1463 -0.0147 -0.0150 0.0051  382  GLU A CA  
1253 C CA  B GLU A 157 ? 0.1590 0.1688 0.1504 -0.0145 -0.0150 0.0051  382  GLU A CA  
1254 C C   A GLU A 157 ? 0.1590 0.1638 0.1491 -0.0178 -0.0156 0.0041  382  GLU A C   
1255 C C   B GLU A 157 ? 0.1593 0.1641 0.1494 -0.0177 -0.0156 0.0041  382  GLU A C   
1256 O O   A GLU A 157 ? 0.1647 0.1696 0.1540 -0.0190 -0.0163 0.0018  382  GLU A O   
1257 O O   B GLU A 157 ? 0.1638 0.1690 0.1532 -0.0189 -0.0163 0.0019  382  GLU A O   
1258 C CB  A GLU A 157 ? 0.1706 0.1784 0.1610 -0.0112 -0.0143 0.0041  382  GLU A CB  
1259 C CB  B GLU A 157 ? 0.1198 0.1261 0.1098 -0.0110 -0.0142 0.0044  382  GLU A CB  
1260 C CG  A GLU A 157 ? 0.1175 0.1315 0.1100 -0.0086 -0.0140 0.0049  382  GLU A CG  
1261 C CG  B GLU A 157 ? 0.1250 0.1367 0.1169 -0.0078 -0.0139 0.0056  382  GLU A CG  
1262 C CD  A GLU A 157 ? 0.1287 0.1413 0.1210 -0.0049 -0.0131 0.0044  382  GLU A CD  
1263 C CD  B GLU A 157 ? 0.1909 0.2089 0.1844 -0.0078 -0.0139 0.0040  382  GLU A CD  
1264 O OE1 A GLU A 157 ? 0.2085 0.2143 0.1989 -0.0035 -0.0125 0.0045  382  GLU A OE1 
1265 O OE1 B GLU A 157 ? 0.2068 0.2260 0.2002 -0.0101 -0.0142 0.0028  382  GLU A OE1 
1266 O OE2 A GLU A 157 ? 0.1512 0.1695 0.1455 -0.0035 -0.0129 0.0040  382  GLU A OE2 
1267 O OE2 B GLU A 157 ? 0.1825 0.2044 0.1776 -0.0055 -0.0136 0.0042  382  GLU A OE2 
1268 N N   . SER A 158 ? 0.1763 0.1764 0.1658 -0.0193 -0.0155 0.0058  383  SER A N   
1269 C CA  . SER A 158 ? 0.1588 0.1529 0.1469 -0.0229 -0.0161 0.0047  383  SER A CA  
1270 C C   . SER A 158 ? 0.1674 0.1582 0.1558 -0.0246 -0.0155 0.0077  383  SER A C   
1271 O O   . SER A 158 ? 0.1933 0.1861 0.1824 -0.0225 -0.0146 0.0103  383  SER A O   
1272 C CB  . SER A 158 ? 0.2068 0.1929 0.1909 -0.0216 -0.0158 0.0021  383  SER A CB  
1273 O OG  . SER A 158 ? 0.2265 0.2081 0.2092 -0.0176 -0.0144 0.0033  383  SER A OG  
1274 N N   . ILE A 159 ? 0.1873 0.1734 0.1752 -0.0289 -0.0161 0.0073  384  ILE A N   
1275 C CA  . ILE A 159 ? 0.1770 0.1595 0.1655 -0.0312 -0.0152 0.0103  384  ILE A CA  
1276 C C   . ILE A 159 ? 0.1763 0.1476 0.1615 -0.0339 -0.0153 0.0090  384  ILE A C   
1277 O O   . ILE A 159 ? 0.2133 0.1816 0.1966 -0.0355 -0.0165 0.0056  384  ILE A O   
1278 C CB  . ILE A 159 ? 0.2173 0.2074 0.2100 -0.0352 -0.0155 0.0121  384  ILE A CB  
1279 C CG1 . ILE A 159 ? 0.2094 0.2027 0.2039 -0.0390 -0.0175 0.0095  384  ILE A CG1 
1280 C CG2 . ILE A 159 ? 0.1647 0.1636 0.1596 -0.0324 -0.0147 0.0140  384  ILE A CG2 
1281 C CD1 . ILE A 159 ? 0.2595 0.2624 0.2565 -0.0374 -0.0183 0.0085  384  ILE A CD1 
1282 N N   . GLY A 160 ? 0.2153 0.1799 0.1993 -0.0343 -0.0139 0.0119  385  GLY A N   
1283 C CA  . GLY A 160 ? 0.2323 0.1864 0.2140 -0.0384 -0.0138 0.0112  385  GLY A CA  
1284 C C   . GLY A 160 ? 0.2154 0.1746 0.2010 -0.0448 -0.0147 0.0122  385  GLY A C   
1285 O O   . GLY A 160 ? 0.2081 0.1732 0.1970 -0.0452 -0.0137 0.0159  385  GLY A O   
1286 N N   . MET A 161 ? 0.2264 0.1844 0.2121 -0.0497 -0.0166 0.0091  386  MET A N   
1287 C CA  . MET A 161 ? 0.2008 0.1675 0.1919 -0.0552 -0.0179 0.0100  386  MET A CA  
1288 C C   . MET A 161 ? 0.2630 0.2226 0.2527 -0.0619 -0.0195 0.0077  386  MET A C   
1289 O O   . MET A 161 ? 0.2475 0.2079 0.2359 -0.0639 -0.0220 0.0039  386  MET A O   
1290 C CB  . MET A 161 ? 0.2271 0.2059 0.2214 -0.0537 -0.0196 0.0087  386  MET A CB  
1291 C CG  . MET A 161 ? 0.2041 0.1941 0.2051 -0.0576 -0.0203 0.0106  386  MET A CG  
1292 S SD  . MET A 161 ? 0.2054 0.2005 0.2099 -0.0560 -0.0171 0.0159  386  MET A SD  
1293 C CE  . MET A 161 ? 0.1940 0.2041 0.2064 -0.0588 -0.0180 0.0170  386  MET A CE  
1294 N N   . GLU A 162 ? 0.2372 0.1902 0.2272 -0.0658 -0.0182 0.0101  387  GLU A N   
1295 C CA  . GLU A 162 ? 0.2145 0.1592 0.2028 -0.0728 -0.0196 0.0078  387  GLU A CA  
1296 C C   . GLU A 162 ? 0.2797 0.2353 0.2742 -0.0794 -0.0223 0.0075  387  GLU A C   
1297 O O   . GLU A 162 ? 0.2774 0.2287 0.2704 -0.0852 -0.0247 0.0043  387  GLU A O   
1298 C CB  . GLU A 162 ? 0.2888 0.2217 0.2751 -0.0750 -0.0170 0.0107  387  GLU A CB  
1299 C CG  . GLU A 162 ? 0.4637 0.4043 0.4561 -0.0774 -0.0154 0.0160  387  GLU A CG  
1300 C CD  . GLU A 162 ? 0.7577 0.6861 0.7474 -0.0785 -0.0124 0.0195  387  GLU A CD  
1301 O OE1 . GLU A 162 ? 0.5726 0.4864 0.5558 -0.0768 -0.0116 0.0178  387  GLU A OE1 
1302 O OE2 . GLU A 162 ? 0.6051 0.5384 0.5989 -0.0808 -0.0105 0.0241  387  GLU A OE2 
1303 N N   . ASN A 163 ? 0.2958 0.2655 0.2971 -0.0785 -0.0219 0.0106  388  ASN A N   
1304 C CA  . ASN A 163 ? 0.2541 0.2353 0.2630 -0.0845 -0.0238 0.0116  388  ASN A CA  
1305 C C   . ASN A 163 ? 0.2229 0.2190 0.2366 -0.0805 -0.0245 0.0122  388  ASN A C   
1306 O O   . ASN A 163 ? 0.2290 0.2304 0.2446 -0.0759 -0.0220 0.0152  388  ASN A O   
1307 C CB  . ASN A 163 ? 0.2577 0.2395 0.2711 -0.0886 -0.0212 0.0162  388  ASN A CB  
1308 C CG  . ASN A 163 ? 0.3182 0.3109 0.3398 -0.0958 -0.0231 0.0172  388  ASN A CG  
1309 O OD1 . ASN A 163 ? 0.2950 0.2975 0.3199 -0.0967 -0.0263 0.0151  388  ASN A OD1 
1310 N ND2 . ASN A 163 ? 0.3230 0.3144 0.3481 -0.1009 -0.0210 0.0207  388  ASN A ND2 
1311 N N   . ASN A 164 ? 0.2272 0.2299 0.2424 -0.0824 -0.0281 0.0095  389  ASN A N   
1312 C CA  . ASN A 164 ? 0.2367 0.2524 0.2559 -0.0782 -0.0287 0.0101  389  ASN A CA  
1313 C C   . ASN A 164 ? 0.2018 0.2298 0.2296 -0.0786 -0.0268 0.0145  389  ASN A C   
1314 O O   . ASN A 164 ? 0.2130 0.2488 0.2430 -0.0734 -0.0255 0.0158  389  ASN A O   
1315 C CB  . ASN A 164 ? 0.2117 0.2324 0.2311 -0.0805 -0.0330 0.0069  389  ASN A CB  
1316 C CG  . ASN A 164 ? 0.2168 0.2464 0.2372 -0.0746 -0.0334 0.0069  389  ASN A CG  
1317 O OD1 . ASN A 164 ? 0.2023 0.2266 0.2170 -0.0693 -0.0325 0.0052  389  ASN A OD1 
1318 N ND2 . ASN A 164 ? 0.2346 0.2778 0.2626 -0.0753 -0.0346 0.0090  389  ASN A ND2 
1319 N N   . THR A 165 ? 0.2076 0.2372 0.2403 -0.0847 -0.0263 0.0168  390  THR A N   
1320 C CA  . THR A 165 ? 0.2179 0.2597 0.2590 -0.0850 -0.0241 0.0211  390  THR A CA  
1321 C C   . THR A 165 ? 0.2288 0.2691 0.2680 -0.0795 -0.0196 0.0240  390  THR A C   
1322 O O   . THR A 165 ? 0.1908 0.2413 0.2354 -0.0776 -0.0173 0.0269  390  THR A O   
1323 C CB  . THR A 165 ? 0.2132 0.2571 0.2601 -0.0933 -0.0242 0.0232  390  THR A CB  
1324 O OG1 . THR A 165 ? 0.2476 0.2776 0.2893 -0.0957 -0.0221 0.0238  390  THR A OG1 
1325 C CG2 . THR A 165 ? 0.3048 0.3523 0.3543 -0.0994 -0.0291 0.0204  390  THR A CG2 
1326 N N   . ASP A 166 ? 0.2309 0.2588 0.2623 -0.0766 -0.0183 0.0231  391  ASP A N   
1327 C CA  . ASP A 166 ? 0.2140 0.2406 0.2430 -0.0715 -0.0146 0.0258  391  ASP A CA  
1328 C C   . ASP A 166 ? 0.1741 0.2076 0.2028 -0.0650 -0.0143 0.0250  391  ASP A C   
1329 O O   . ASP A 166 ? 0.1751 0.2099 0.2025 -0.0611 -0.0114 0.0272  391  ASP A O   
1330 C CB  . ASP A 166 ? 0.2213 0.2333 0.2424 -0.0699 -0.0138 0.0253  391  ASP A CB  
1331 C CG  . ASP A 166 ? 0.3310 0.3355 0.3521 -0.0753 -0.0123 0.0278  391  ASP A CG  
1332 O OD1 . ASP A 166 ? 0.2620 0.2735 0.2888 -0.0790 -0.0107 0.0311  391  ASP A OD1 
1333 O OD2 . ASP A 166 ? 0.2785 0.2699 0.2938 -0.0757 -0.0125 0.0266  391  ASP A OD2 
1334 N N   . PHE A 167 ? 0.1756 0.2131 0.2050 -0.0638 -0.0171 0.0221  392  PHE A N   
1335 C CA  . PHE A 167 ? 0.1361 0.1803 0.1659 -0.0582 -0.0165 0.0217  392  PHE A CA  
1336 C C   . PHE A 167 ? 0.1338 0.1892 0.1701 -0.0577 -0.0140 0.0248  392  PHE A C   
1337 O O   . PHE A 167 ? 0.1580 0.2172 0.1937 -0.0528 -0.0122 0.0251  392  PHE A O   
1338 C CB  . PHE A 167 ? 0.1477 0.1943 0.1772 -0.0574 -0.0198 0.0185  392  PHE A CB  
1339 C CG  . PHE A 167 ? 0.1345 0.1711 0.1567 -0.0555 -0.0212 0.0152  392  PHE A CG  
1340 C CD1 . PHE A 167 ? 0.1596 0.1917 0.1772 -0.0503 -0.0194 0.0149  392  PHE A CD1 
1341 C CD2 . PHE A 167 ? 0.1628 0.1948 0.1826 -0.0587 -0.0243 0.0123  392  PHE A CD2 
1342 C CE1 . PHE A 167 ? 0.1382 0.1619 0.1498 -0.0482 -0.0203 0.0121  392  PHE A CE1 
1343 C CE2 . PHE A 167 ? 0.1731 0.1958 0.1860 -0.0565 -0.0249 0.0092  392  PHE A CE2 
1344 C CZ  . PHE A 167 ? 0.1794 0.1982 0.1885 -0.0511 -0.0228 0.0093  392  PHE A CZ  
1345 N N   . ASP A 168 ? 0.1699 0.2309 0.2125 -0.0627 -0.0138 0.0270  393  ASP A N   
1346 C CA  . ASP A 168 ? 0.1548 0.2269 0.2043 -0.0624 -0.0110 0.0303  393  ASP A CA  
1347 C C   . ASP A 168 ? 0.1541 0.2241 0.2033 -0.0640 -0.0071 0.0338  393  ASP A C   
1348 O O   . ASP A 168 ? 0.2198 0.2988 0.2755 -0.0654 -0.0046 0.0368  393  ASP A O   
1349 C CB  . ASP A 168 ? 0.1263 0.2086 0.1843 -0.0667 -0.0134 0.0309  393  ASP A CB  
1350 C CG  . ASP A 168 ? 0.1513 0.2384 0.2102 -0.0641 -0.0166 0.0284  393  ASP A CG  
1351 O OD1 . ASP A 168 ? 0.1761 0.2606 0.2303 -0.0584 -0.0161 0.0268  393  ASP A OD1 
1352 O OD2 . ASP A 168 ? 0.1767 0.2705 0.2410 -0.0680 -0.0199 0.0282  393  ASP A OD2 
1353 N N   . VAL A 169 ? 0.1498 0.2084 0.1918 -0.0635 -0.0064 0.0337  394  VAL A N   
1354 C CA  . VAL A 169 ? 0.1492 0.2047 0.1897 -0.0646 -0.0028 0.0373  394  VAL A CA  
1355 C C   . VAL A 169 ? 0.1988 0.2500 0.2322 -0.0586 -0.0008 0.0374  394  VAL A C   
1356 O O   . VAL A 169 ? 0.1621 0.2045 0.1893 -0.0563 -0.0026 0.0353  394  VAL A O   
1357 C CB  . VAL A 169 ? 0.1846 0.2300 0.2231 -0.0699 -0.0036 0.0379  394  VAL A CB  
1358 C CG1 . VAL A 169 ? 0.2127 0.2547 0.2491 -0.0706 0.0005  0.0423  394  VAL A CG1 
1359 C CG2 . VAL A 169 ? 0.1941 0.2439 0.2396 -0.0768 -0.0059 0.0376  394  VAL A CG2 
1360 N N   . LEU A 170 ? 0.1447 0.2022 0.1788 -0.0561 0.0027  0.0397  395  LEU A N   
1361 C CA  . LEU A 170 ? 0.1570 0.2110 0.1839 -0.0508 0.0042  0.0395  395  LEU A CA  
1362 C C   . LEU A 170 ? 0.1864 0.2296 0.2067 -0.0512 0.0043  0.0411  395  LEU A C   
1363 O O   . LEU A 170 ? 0.2130 0.2531 0.2344 -0.0553 0.0056  0.0440  395  LEU A O   
1364 C CB  . LEU A 170 ? 0.1910 0.2525 0.2187 -0.0487 0.0084  0.0418  395  LEU A CB  
1365 C CG  . LEU A 170 ? 0.1845 0.2555 0.2168 -0.0461 0.0090  0.0402  395  LEU A CG  
1366 C CD1 . LEU A 170 ? 0.2164 0.2932 0.2484 -0.0439 0.0138  0.0425  395  LEU A CD1 
1367 C CD2 . LEU A 170 ? 0.1934 0.2614 0.2217 -0.0420 0.0063  0.0363  395  LEU A CD2 
1368 N N   . PRO A 171 ? 0.1695 0.2072 0.1833 -0.0469 0.0032  0.0396  396  PRO A N   
1369 C CA  . PRO A 171 ? 0.1979 0.2262 0.2055 -0.0463 0.0034  0.0416  396  PRO A CA  
1370 C C   . PRO A 171 ? 0.2134 0.2433 0.2180 -0.0456 0.0071  0.0458  396  PRO A C   
1371 O O   . PRO A 171 ? 0.2195 0.2573 0.2256 -0.0447 0.0094  0.0463  396  PRO A O   
1372 C CB  . PRO A 171 ? 0.1814 0.2065 0.1844 -0.0415 0.0011  0.0387  396  PRO A CB  
1373 C CG  . PRO A 171 ? 0.1839 0.2177 0.1884 -0.0389 0.0015  0.0366  396  PRO A CG  
1374 C CD  . PRO A 171 ? 0.1914 0.2322 0.2033 -0.0423 0.0020  0.0364  396  PRO A CD  
1375 N N   . ASP A 172 ? 0.1599 0.1816 0.1597 -0.0458 0.0077  0.0488  397  ASP A N   
1376 C CA  . ASP A 172 ? 0.2440 0.2658 0.2392 -0.0449 0.0109  0.0531  397  ASP A CA  
1377 C C   . ASP A 172 ? 0.2266 0.2489 0.2151 -0.0393 0.0100  0.0521  397  ASP A C   
1378 O O   . ASP A 172 ? 0.2167 0.2328 0.1995 -0.0369 0.0091  0.0538  397  ASP A O   
1379 C CB  . ASP A 172 ? 0.1818 0.1943 0.1746 -0.0474 0.0119  0.0573  397  ASP A CB  
1380 C CG  . ASP A 172 ? 0.2639 0.2771 0.2631 -0.0539 0.0136  0.0590  397  ASP A CG  
1381 O OD1 . ASP A 172 ? 0.2826 0.3051 0.2884 -0.0561 0.0143  0.0577  397  ASP A OD1 
1382 O OD2 . ASP A 172 ? 0.3668 0.3712 0.3646 -0.0568 0.0142  0.0619  397  ASP A OD2 
1383 N N   . TYR A 173 ? 0.1862 0.2163 0.1759 -0.0374 0.0103  0.0493  398  TYR A N   
1384 C CA  . TYR A 173 ? 0.1726 0.2038 0.1569 -0.0328 0.0089  0.0473  398  TYR A CA  
1385 C C   . TYR A 173 ? 0.2065 0.2350 0.1828 -0.0308 0.0099  0.0507  398  TYR A C   
1386 O O   . TYR A 173 ? 0.1950 0.2218 0.1665 -0.0275 0.0076  0.0498  398  TYR A O   
1387 C CB  . TYR A 173 ? 0.1714 0.2107 0.1573 -0.0316 0.0104  0.0446  398  TYR A CB  
1388 C CG  . TYR A 173 ? 0.1840 0.2270 0.1763 -0.0320 0.0088  0.0407  398  TYR A CG  
1389 C CD1 . TYR A 173 ? 0.2102 0.2518 0.2017 -0.0297 0.0056  0.0370  398  TYR A CD1 
1390 C CD2 . TYR A 173 ? 0.1566 0.2054 0.1555 -0.0344 0.0108  0.0410  398  TYR A CD2 
1391 C CE1 . TYR A 173 ? 0.1966 0.2416 0.1933 -0.0298 0.0044  0.0338  398  TYR A CE1 
1392 C CE2 . TYR A 173 ? 0.1620 0.2148 0.1665 -0.0343 0.0093  0.0378  398  TYR A CE2 
1393 C CZ  . TYR A 173 ? 0.1930 0.2435 0.1959 -0.0320 0.0062  0.0343  398  TYR A CZ  
1394 O OH  . TYR A 173 ? 0.1650 0.2191 0.1727 -0.0317 0.0048  0.0316  398  TYR A OH  
1395 N N   . ASN A 174 ? 0.2009 0.2299 0.1756 -0.0326 0.0135  0.0549  399  ASN A N   
1396 C CA  . ASN A 174 ? 0.2070 0.2339 0.1734 -0.0306 0.0146  0.0586  399  ASN A CA  
1397 C C   . ASN A 174 ? 0.2466 0.2652 0.2112 -0.0320 0.0148  0.0634  399  ASN A C   
1398 O O   . ASN A 174 ? 0.2895 0.3060 0.2474 -0.0308 0.0163  0.0677  399  ASN A O   
1399 C CB  . ASN A 174 ? 0.2239 0.2567 0.1877 -0.0310 0.0190  0.0602  399  ASN A CB  
1400 C CG  . ASN A 174 ? 0.2557 0.2902 0.2251 -0.0353 0.0229  0.0633  399  ASN A CG  
1401 O OD1 . ASN A 174 ? 0.2948 0.3242 0.2677 -0.0383 0.0225  0.0656  399  ASN A OD1 
1402 N ND2 . ASN A 174 ? 0.2717 0.3133 0.2419 -0.0356 0.0268  0.0634  399  ASN A ND2 
1403 N N   . GLY A 175 ? 0.2172 0.2305 0.1870 -0.0342 0.0133  0.0628  400  GLY A N   
1404 C CA  . GLY A 175 ? 0.2322 0.2359 0.2000 -0.0354 0.0135  0.0669  400  GLY A CA  
1405 C C   . GLY A 175 ? 0.2663 0.2687 0.2359 -0.0401 0.0175  0.0713  400  GLY A C   
1406 O O   . GLY A 175 ? 0.3816 0.3753 0.3484 -0.0411 0.0183  0.0755  400  GLY A O   
1407 N N   . SER A 176 ? 0.2930 0.3037 0.2673 -0.0428 0.0201  0.0706  401  SER A N   
1408 C CA  . SER A 176 ? 0.2974 0.3087 0.2745 -0.0476 0.0242  0.0748  401  SER A CA  
1409 C C   . SER A 176 ? 0.2612 0.2798 0.2483 -0.0517 0.0246  0.0720  401  SER A C   
1410 O O   . SER A 176 ? 0.3131 0.3369 0.3037 -0.0501 0.0222  0.0671  401  SER A O   
1411 C CB  . SER A 176 ? 0.3086 0.3246 0.2801 -0.0463 0.0283  0.0786  401  SER A CB  
1412 O OG  . SER A 176 ? 0.2884 0.3151 0.2630 -0.0456 0.0299  0.0756  401  SER A OG  
1413 N N   . ALA A 177 ? 0.3434 0.3628 0.3351 -0.0570 0.0277  0.0754  402  ALA A N   
1414 C CA  . ALA A 177 ? 0.4329 0.4608 0.4348 -0.0613 0.0284  0.0737  402  ALA A CA  
1415 C C   . ALA A 177 ? 0.4257 0.4658 0.4298 -0.0597 0.0320  0.0739  402  ALA A C   
1416 O O   . ALA A 177 ? 0.4174 0.4662 0.4306 -0.0627 0.0330  0.0732  402  ALA A O   
1417 C CB  . ALA A 177 ? 0.4429 0.4671 0.4496 -0.0683 0.0302  0.0774  402  ALA A CB  
1418 N N   . PHE A 178 ? 0.2389 0.2800 0.2350 -0.0551 0.0340  0.0749  403  PHE A N   
1419 C CA  . PHE A 178 ? 0.2936 0.3446 0.2901 -0.0534 0.0383  0.0754  403  PHE A CA  
1420 C C   . PHE A 178 ? 0.3071 0.3615 0.3004 -0.0479 0.0363  0.0704  403  PHE A C   
1421 O O   . PHE A 178 ? 0.4238 0.4736 0.4080 -0.0441 0.0349  0.0696  403  PHE A O   
1422 C CB  . PHE A 178 ? 0.2571 0.3063 0.2461 -0.0532 0.0430  0.0808  403  PHE A CB  
1423 C CG  . PHE A 178 ? 0.2780 0.3245 0.2708 -0.0590 0.0457  0.0861  403  PHE A CG  
1424 C CD1 . PHE A 178 ? 0.3044 0.3395 0.2941 -0.0610 0.0435  0.0884  403  PHE A CD1 
1425 C CD2 . PHE A 178 ? 0.2168 0.2722 0.2170 -0.0626 0.0505  0.0886  403  PHE A CD2 
1426 C CE1 . PHE A 178 ? 0.2505 0.2820 0.2436 -0.0669 0.0461  0.0932  403  PHE A CE1 
1427 C CE2 . PHE A 178 ? 0.2847 0.3379 0.2891 -0.0687 0.0530  0.0935  403  PHE A CE2 
1428 C CZ  . PHE A 178 ? 0.3190 0.3597 0.3196 -0.0710 0.0508  0.0957  403  PHE A CZ  
1429 N N   . ASP A 179 ? 0.2595 0.3220 0.2604 -0.0477 0.0363  0.0671  404  ASP A N   
1430 C CA  . ASP A 179 ? 0.2490 0.3142 0.2480 -0.0430 0.0345  0.0622  404  ASP A CA  
1431 C C   . ASP A 179 ? 0.3490 0.4218 0.3468 -0.0403 0.0393  0.0620  404  ASP A C   
1432 O O   . ASP A 179 ? 0.3101 0.3860 0.3080 -0.0369 0.0387  0.0580  404  ASP A O   
1433 C CB  . ASP A 179 ? 0.3139 0.3814 0.3213 -0.0440 0.0306  0.0584  404  ASP A CB  
1434 C CG  . ASP A 179 ? 0.4253 0.5017 0.4438 -0.0475 0.0326  0.0597  404  ASP A CG  
1435 O OD1 . ASP A 179 ? 0.7232 0.8040 0.7437 -0.0495 0.0373  0.0637  404  ASP A OD1 
1436 O OD2 . ASP A 179 ? 0.5678 0.6474 0.5934 -0.0484 0.0296  0.0570  404  ASP A OD2 
1437 N N   . GLY A 180 ? 0.3709 0.4463 0.3672 -0.0416 0.0445  0.0664  405  GLY A N   
1438 C CA  . GLY A 180 ? 0.3886 0.4716 0.3845 -0.0391 0.0500  0.0664  405  GLY A CA  
1439 C C   . GLY A 180 ? 0.3423 0.4233 0.3281 -0.0339 0.0501  0.0628  405  GLY A C   
1440 O O   . GLY A 180 ? 0.4365 0.5229 0.4233 -0.0310 0.0531  0.0605  405  GLY A O   
1441 N N   . SER A 181 ? 0.2767 0.3498 0.2526 -0.0326 0.0468  0.0622  406  SER A N   
1442 C CA  . SER A 181 ? 0.2816 0.3528 0.2476 -0.0284 0.0463  0.0586  406  SER A CA  
1443 C C   . SER A 181 ? 0.3312 0.4015 0.2996 -0.0264 0.0418  0.0530  406  SER A C   
1444 O O   . SER A 181 ? 0.3145 0.3833 0.2756 -0.0233 0.0413  0.0494  406  SER A O   
1445 C CB  . SER A 181 ? 0.3968 0.4613 0.3512 -0.0278 0.0446  0.0606  406  SER A CB  
1446 O OG  . SER A 181 ? 0.5771 0.6424 0.5265 -0.0287 0.0496  0.0655  406  SER A OG  
1447 N N   . LEU A 182 ? 0.2437 0.3145 0.2215 -0.0283 0.0385  0.0522  407  LEU A N   
1448 C CA  . LEU A 182 ? 0.1685 0.2380 0.1484 -0.0266 0.0342  0.0473  407  LEU A CA  
1449 C C   . LEU A 182 ? 0.2516 0.3274 0.2376 -0.0249 0.0365  0.0447  407  LEU A C   
1450 O O   . LEU A 182 ? 0.2233 0.3055 0.2173 -0.0262 0.0397  0.0469  407  LEU A O   
1451 C CB  . LEU A 182 ? 0.2274 0.2938 0.2133 -0.0293 0.0295  0.0476  407  LEU A CB  
1452 C CG  . LEU A 182 ? 0.1950 0.2542 0.1752 -0.0304 0.0271  0.0501  407  LEU A CG  
1453 C CD1 . LEU A 182 ? 0.2243 0.2797 0.2103 -0.0328 0.0231  0.0499  407  LEU A CD1 
1454 C CD2 . LEU A 182 ? 0.2449 0.3005 0.2153 -0.0270 0.0249  0.0479  407  LEU A CD2 
1455 N N   . ASN A 183 ? 0.1637 0.2378 0.1463 -0.0219 0.0350  0.0403  408  ASN A N   
1456 C CA  . ASN A 183 ? 0.1846 0.2631 0.1719 -0.0194 0.0369  0.0375  408  ASN A CA  
1457 C C   . ASN A 183 ? 0.1746 0.2541 0.1707 -0.0205 0.0327  0.0362  408  ASN A C   
1458 O O   . ASN A 183 ? 0.1884 0.2638 0.1825 -0.0196 0.0288  0.0330  408  ASN A O   
1459 C CB  . ASN A 183 ? 0.1903 0.2651 0.1686 -0.0161 0.0375  0.0334  408  ASN A CB  
1460 C CG  . ASN A 183 ? 0.2636 0.3411 0.2459 -0.0131 0.0396  0.0304  408  ASN A CG  
1461 O OD1 . ASN A 183 ? 0.2085 0.2923 0.1995 -0.0128 0.0423  0.0322  408  ASN A OD1 
1462 N ND2 . ASN A 183 ? 0.2694 0.3422 0.2455 -0.0110 0.0384  0.0261  408  ASN A ND2 
1463 N N   . LEU A 184 ? 0.1598 0.2451 0.1656 -0.0228 0.0335  0.0389  409  LEU A N   
1464 C CA  . LEU A 184 ? 0.1286 0.2154 0.1425 -0.0246 0.0294  0.0383  409  LEU A CA  
1465 C C   . LEU A 184 ? 0.1551 0.2493 0.1770 -0.0225 0.0310  0.0376  409  LEU A C   
1466 O O   . LEU A 184 ? 0.2011 0.3021 0.2272 -0.0218 0.0356  0.0398  409  LEU A O   
1467 C CB  . LEU A 184 ? 0.1414 0.2293 0.1606 -0.0294 0.0284  0.0419  409  LEU A CB  
1468 C CG  . LEU A 184 ? 0.1880 0.2680 0.2005 -0.0315 0.0265  0.0433  409  LEU A CG  
1469 C CD1 . LEU A 184 ? 0.1913 0.2722 0.2096 -0.0365 0.0264  0.0469  409  LEU A CD1 
1470 C CD2 . LEU A 184 ? 0.2645 0.3376 0.2731 -0.0305 0.0215  0.0399  409  LEU A CD2 
1471 N N   . ALA A 185 ? 0.1304 0.2235 0.1547 -0.0214 0.0274  0.0348  410  ALA A N   
1472 C CA  . ALA A 185 ? 0.1347 0.2351 0.1676 -0.0198 0.0280  0.0349  410  ALA A CA  
1473 C C   . ALA A 185 ? 0.1142 0.2228 0.1570 -0.0235 0.0282  0.0386  410  ALA A C   
1474 O O   . ALA A 185 ? 0.1339 0.2403 0.1773 -0.0279 0.0258  0.0400  410  ALA A O   
1475 C CB  . ALA A 185 ? 0.1522 0.2496 0.1857 -0.0189 0.0234  0.0319  410  ALA A CB  
1476 N N   . PRO A 186 ? 0.1703 0.2884 0.2214 -0.0218 0.0311  0.0403  411  PRO A N   
1477 C CA  . PRO A 186 ? 0.2323 0.3597 0.2932 -0.0256 0.0320  0.0442  411  PRO A CA  
1478 C C   . PRO A 186 ? 0.1192 0.2492 0.1871 -0.0294 0.0263  0.0442  411  PRO A C   
1479 O O   . PRO A 186 ? 0.1336 0.2602 0.2000 -0.0279 0.0223  0.0415  411  PRO A O   
1480 C CB  . PRO A 186 ? 0.2180 0.3551 0.2852 -0.0214 0.0371  0.0458  411  PRO A CB  
1481 C CG  . PRO A 186 ? 0.1339 0.2673 0.1976 -0.0161 0.0365  0.0424  411  PRO A CG  
1482 C CD  . PRO A 186 ? 0.1775 0.2982 0.2292 -0.0161 0.0340  0.0389  411  PRO A CD  
1483 N N   . PRO A 187 ? 0.1102 0.2464 0.1856 -0.0345 0.0258  0.0473  412  PRO A N   
1484 C CA  . PRO A 187 ? 0.1562 0.2956 0.2382 -0.0386 0.0203  0.0471  412  PRO A CA  
1485 C C   . PRO A 187 ? 0.1470 0.2952 0.2362 -0.0351 0.0191  0.0469  412  PRO A C   
1486 O O   . PRO A 187 ? 0.1494 0.3047 0.2425 -0.0307 0.0234  0.0483  412  PRO A O   
1487 C CB  . PRO A 187 ? 0.1734 0.3191 0.2628 -0.0448 0.0214  0.0509  412  PRO A CB  
1488 C CG  . PRO A 187 ? 0.1957 0.3375 0.2793 -0.0444 0.0268  0.0527  412  PRO A CG  
1489 C CD  . PRO A 187 ? 0.1152 0.2554 0.1929 -0.0372 0.0304  0.0510  412  PRO A CD  
1490 N N   . ILE A 188 ? 0.1248 0.2722 0.2155 -0.0370 0.0134  0.0452  413  ILE A N   
1491 C CA  . ILE A 188 ? 0.1371 0.2917 0.2335 -0.0339 0.0112  0.0450  413  ILE A CA  
1492 C C   . ILE A 188 ? 0.1454 0.3131 0.2540 -0.0382 0.0092  0.0481  413  ILE A C   
1493 O O   . ILE A 188 ? 0.1782 0.3448 0.2879 -0.0444 0.0047  0.0476  413  ILE A O   
1494 C CB  . ILE A 188 ? 0.1148 0.2609 0.2048 -0.0333 0.0060  0.0414  413  ILE A CB  
1495 C CG1 . ILE A 188 ? 0.1643 0.2985 0.2431 -0.0294 0.0079  0.0384  413  ILE A CG1 
1496 C CG2 . ILE A 188 ? 0.1595 0.3134 0.2554 -0.0306 0.0034  0.0418  413  ILE A CG2 
1497 C CD1 . ILE A 188 ? 0.1767 0.3020 0.2488 -0.0294 0.0033  0.0350  413  ILE A CD1 
1498 N N   . VAL A 189 ? 0.1382 0.3183 0.2559 -0.0352 0.0127  0.0512  414  VAL A N   
1499 C CA  . VAL A 189 ? 0.1549 0.3495 0.2855 -0.0393 0.0113  0.0547  414  VAL A CA  
1500 C C   . VAL A 189 ? 0.2190 0.4253 0.3579 -0.0336 0.0113  0.0564  414  VAL A C   
1501 O O   . VAL A 189 ? 0.2281 0.4361 0.3671 -0.0269 0.0166  0.0572  414  VAL A O   
1502 C CB  . VAL A 189 ? 0.1622 0.3630 0.2981 -0.0421 0.0167  0.0581  414  VAL A CB  
1503 C CG1 . VAL A 189 ? 0.1608 0.3706 0.3063 -0.0463 0.0142  0.0598  414  VAL A CG1 
1504 C CG2 . VAL A 189 ? 0.2386 0.4266 0.3651 -0.0465 0.0174  0.0568  414  VAL A CG2 
1505 N N   . PRO A 190 ? 0.1521 0.3638 0.2958 -0.0355 0.0054  0.0564  415  PRO A N   
1506 C CA  . PRO A 190 ? 0.1677 0.3882 0.3176 -0.0294 0.0052  0.0580  415  PRO A CA  
1507 C C   . PRO A 190 ? 0.2003 0.4299 0.3580 -0.0263 0.0108  0.0611  415  PRO A C   
1508 O O   . PRO A 190 ? 0.1524 0.3847 0.3135 -0.0309 0.0124  0.0623  415  PRO A O   
1509 C CB  . PRO A 190 ? 0.1496 0.3732 0.3022 -0.0338 -0.0024 0.0573  415  PRO A CB  
1510 C CG  . PRO A 190 ? 0.2043 0.4173 0.3489 -0.0401 -0.0063 0.0541  415  PRO A CG  
1511 C CD  . PRO A 190 ? 0.2257 0.4332 0.3672 -0.0426 -0.0014 0.0543  415  PRO A CD  
1512 N N   . LEU A 191 ? 0.1757 0.4095 0.3360 -0.0182 0.0139  0.0624  416  LEU A N   
1513 C CA  . LEU A 191 ? 0.1837 0.4256 0.3508 -0.0142 0.0198  0.0652  416  LEU A CA  
1514 C C   . LEU A 191 ? 0.2673 0.5212 0.4450 -0.0163 0.0167  0.0676  416  LEU A C   
1515 O O   . LEU A 191 ? 0.2311 0.4919 0.4150 -0.0167 0.0206  0.0698  416  LEU A O   
1516 C CB  . LEU A 191 ? 0.2139 0.4548 0.3795 -0.0045 0.0247  0.0655  416  LEU A CB  
1517 C CG  . LEU A 191 ? 0.2953 0.5264 0.4517 -0.0013 0.0308  0.0636  416  LEU A CG  
1518 C CD1 . LEU A 191 ? 0.3540 0.5848 0.5096 -0.0042 0.0362  0.0643  416  LEU A CD1 
1519 C CD2 . LEU A 191 ? 0.2981 0.5187 0.4453 -0.0038 0.0273  0.0605  416  LEU A CD2 
1520 N N   . LEU A 192 ? 0.1834 0.4401 0.3630 -0.0176 0.0098  0.0674  417  LEU A N   
1521 C CA  . LEU A 192 ? 0.1926 0.4607 0.3816 -0.0205 0.0062  0.0695  417  LEU A CA  
1522 C C   . LEU A 192 ? 0.3144 0.5804 0.5024 -0.0304 0.0005  0.0677  417  LEU A C   
1523 O O   . LEU A 192 ? 0.2569 0.5128 0.4365 -0.0338 -0.0027 0.0647  417  LEU A O   
1524 C CB  . LEU A 192 ? 0.1876 0.4613 0.3796 -0.0154 0.0024  0.0707  417  LEU A CB  
1525 C CG  . LEU A 192 ? 0.2516 0.5314 0.4486 -0.0058 0.0074  0.0736  417  LEU A CG  
1526 C CD1 . LEU A 192 ? 0.1589 0.4426 0.3576 -0.0016 0.0026  0.0748  417  LEU A CD1 
1527 C CD2 . LEU A 192 ? 0.2576 0.5486 0.4647 -0.0058 0.0114  0.0766  417  LEU A CD2 
1528 N N   . PRO A 193 ? 0.3606 0.6356 0.5568 -0.0352 -0.0007 0.0693  418  PRO A N   
1529 C CA  . PRO A 193 ? 0.3342 0.6054 0.5287 -0.0450 -0.0048 0.0674  418  PRO A CA  
1530 C C   . PRO A 193 ? 0.3237 0.5921 0.5146 -0.0488 -0.0129 0.0649  418  PRO A C   
1531 O O   . PRO A 193 ? 0.3147 0.5742 0.4995 -0.0555 -0.0160 0.0621  418  PRO A O   
1532 C CB  . PRO A 193 ? 0.4547 0.7375 0.6600 -0.0482 -0.0031 0.0702  418  PRO A CB  
1533 C CG  . PRO A 193 ? 0.3297 0.6245 0.5431 -0.0407 -0.0018 0.0732  418  PRO A CG  
1534 C CD  . PRO A 193 ? 0.4191 0.7077 0.6264 -0.0321 0.0022  0.0729  418  PRO A CD  
1535 N N   . GLY A 194 ? 0.1937 0.4689 0.3876 -0.0446 -0.0165 0.0659  419  GLY A N   
1536 C CA  . GLY A 194 ? 0.1788 0.4508 0.3679 -0.0477 -0.0239 0.0635  419  GLY A CA  
1537 C C   . GLY A 194 ? 0.2756 0.5360 0.4539 -0.0448 -0.0252 0.0608  419  GLY A C   
1538 O O   . GLY A 194 ? 0.2173 0.4743 0.3906 -0.0467 -0.0312 0.0587  419  GLY A O   
1539 N N   . GLU A 195 ? 0.1735 0.4278 0.3479 -0.0402 -0.0198 0.0608  420  GLU A N   
1540 C CA  . GLU A 195 ? 0.1131 0.3568 0.2777 -0.0372 -0.0205 0.0585  420  GLU A CA  
1541 C C   . GLU A 195 ? 0.1913 0.4231 0.3476 -0.0438 -0.0221 0.0549  420  GLU A C   
1542 O O   . GLU A 195 ? 0.1706 0.4008 0.3281 -0.0489 -0.0200 0.0548  420  GLU A O   
1543 C CB  . GLU A 195 ? 0.1086 0.3512 0.2728 -0.0291 -0.0139 0.0599  420  GLU A CB  
1544 C CG  . GLU A 195 ? 0.1417 0.3930 0.3117 -0.0213 -0.0128 0.0630  420  GLU A CG  
1545 C CD  . GLU A 195 ? 0.1676 0.4172 0.3372 -0.0133 -0.0056 0.0643  420  GLU A CD  
1546 O OE1 . GLU A 195 ? 0.1240 0.3675 0.2899 -0.0143 -0.0011 0.0630  420  GLU A OE1 
1547 O OE2 . GLU A 195 ? 0.1405 0.3942 0.3129 -0.0060 -0.0044 0.0664  420  GLU A OE2 
1548 N N   . THR A 196 ? 0.1357 0.3590 0.2834 -0.0435 -0.0255 0.0522  421  THR A N   
1549 C CA  . THR A 196 ? 0.1087 0.3199 0.2477 -0.0490 -0.0273 0.0486  421  THR A CA  
1550 C C   . THR A 196 ? 0.1302 0.3334 0.2617 -0.0443 -0.0257 0.0472  421  THR A C   
1551 O O   . THR A 196 ? 0.1253 0.3302 0.2558 -0.0388 -0.0268 0.0477  421  THR A O   
1552 C CB  . THR A 196 ? 0.1625 0.3709 0.2979 -0.0547 -0.0342 0.0458  421  THR A CB  
1553 O OG1 . THR A 196 ? 0.1908 0.4075 0.3337 -0.0592 -0.0358 0.0471  421  THR A OG1 
1554 C CG2 . THR A 196 ? 0.2009 0.3958 0.3269 -0.0600 -0.0356 0.0420  421  THR A CG2 
1555 N N   . LEU A 197 ? 0.1276 0.3222 0.2540 -0.0465 -0.0230 0.0457  422  LEU A N   
1556 C CA  . LEU A 197 ? 0.1077 0.2899 0.2238 -0.0418 -0.0211 0.0431  422  LEU A CA  
1557 C C   . LEU A 197 ? 0.1474 0.3230 0.2561 -0.0421 -0.0264 0.0401  422  LEU A C   
1558 O O   . LEU A 197 ? 0.1230 0.2962 0.2295 -0.0483 -0.0310 0.0382  422  LEU A O   
1559 C CB  . LEU A 197 ? 0.1633 0.3338 0.2725 -0.0443 -0.0178 0.0412  422  LEU A CB  
1560 C CG  . LEU A 197 ? 0.1473 0.3031 0.2447 -0.0404 -0.0160 0.0379  422  LEU A CG  
1561 C CD1 . LEU A 197 ? 0.1457 0.3019 0.2424 -0.0327 -0.0114 0.0387  422  LEU A CD1 
1562 C CD2 . LEU A 197 ? 0.1607 0.3065 0.2523 -0.0440 -0.0140 0.0365  422  LEU A CD2 
1563 N N   . LEU A 198 ? 0.1048 0.2771 0.2093 -0.0356 -0.0256 0.0397  423  LEU A N   
1564 C CA  . LEU A 198 ? 0.0970 0.2621 0.1934 -0.0352 -0.0297 0.0370  423  LEU A CA  
1565 C C   . LEU A 198 ? 0.1164 0.2658 0.2018 -0.0352 -0.0278 0.0332  423  LEU A C   
1566 O O   . LEU A 198 ? 0.1433 0.2874 0.2257 -0.0309 -0.0231 0.0329  423  LEU A O   
1567 C CB  . LEU A 198 ? 0.1116 0.2805 0.2088 -0.0283 -0.0297 0.0388  423  LEU A CB  
1568 C CG  . LEU A 198 ? 0.1525 0.3158 0.2420 -0.0279 -0.0341 0.0367  423  LEU A CG  
1569 C CD1 . LEU A 198 ? 0.0996 0.2700 0.1916 -0.0338 -0.0407 0.0367  423  LEU A CD1 
1570 C CD2 . LEU A 198 ? 0.1351 0.2996 0.2243 -0.0204 -0.0327 0.0387  423  LEU A CD2 
1571 N N   . ARG A 199 ? 0.1147 0.2569 0.1941 -0.0401 -0.0314 0.0302  424  ARG A N   
1572 C CA  . ARG A 199 ? 0.0977 0.2261 0.1678 -0.0406 -0.0298 0.0269  424  ARG A CA  
1573 C C   . ARG A 199 ? 0.1648 0.2853 0.2264 -0.0379 -0.0316 0.0243  424  ARG A C   
1574 O O   . ARG A 199 ? 0.1483 0.2703 0.2083 -0.0396 -0.0359 0.0235  424  ARG A O   
1575 C CB  . ARG A 199 ? 0.1297 0.2539 0.1985 -0.0476 -0.0318 0.0254  424  ARG A CB  
1576 C CG  . ARG A 199 ? 0.1342 0.2645 0.2106 -0.0506 -0.0293 0.0280  424  ARG A CG  
1577 C CD  . ARG A 199 ? 0.1767 0.3028 0.2524 -0.0582 -0.0313 0.0269  424  ARG A CD  
1578 N NE  . ARG A 199 ? 0.1689 0.3013 0.2521 -0.0609 -0.0283 0.0299  424  ARG A NE  
1579 C CZ  . ARG A 199 ? 0.2269 0.3520 0.3075 -0.0626 -0.0250 0.0301  424  ARG A CZ  
1580 N NH1 . ARG A 199 ? 0.1543 0.2658 0.2254 -0.0621 -0.0247 0.0274  424  ARG A NH1 
1581 N NH2 . ARG A 199 ? 0.1884 0.3203 0.2760 -0.0646 -0.0219 0.0334  424  ARG A NH2 
1582 N N   . PHE A 200 ? 0.1118 0.2242 0.1679 -0.0338 -0.0281 0.0230  425  PHE A N   
1583 C CA  . PHE A 200 ? 0.1069 0.2109 0.1548 -0.0316 -0.0289 0.0205  425  PHE A CA  
1584 C C   . PHE A 200 ? 0.1509 0.2447 0.1922 -0.0348 -0.0293 0.0174  425  PHE A C   
1585 O O   . PHE A 200 ? 0.1417 0.2306 0.1815 -0.0344 -0.0262 0.0170  425  PHE A O   
1586 C CB  . PHE A 200 ? 0.1130 0.2143 0.1591 -0.0258 -0.0249 0.0209  425  PHE A CB  
1587 C CG  . PHE A 200 ? 0.1173 0.2271 0.1693 -0.0217 -0.0239 0.0239  425  PHE A CG  
1588 C CD1 . PHE A 200 ? 0.1109 0.2224 0.1618 -0.0191 -0.0259 0.0247  425  PHE A CD1 
1589 C CD2 . PHE A 200 ? 0.1372 0.2532 0.1957 -0.0204 -0.0207 0.0263  425  PHE A CD2 
1590 C CE1 . PHE A 200 ? 0.1245 0.2435 0.1809 -0.0148 -0.0249 0.0279  425  PHE A CE1 
1591 C CE2 . PHE A 200 ? 0.1399 0.2637 0.2042 -0.0161 -0.0194 0.0293  425  PHE A CE2 
1592 C CZ  . PHE A 200 ? 0.1435 0.2687 0.2069 -0.0131 -0.0216 0.0302  425  PHE A CZ  
1593 N N   . GLY A 201 ? 0.1438 0.2342 0.1808 -0.0377 -0.0329 0.0152  426  GLY A N   
1594 C CA  . GLY A 201 ? 0.1265 0.2076 0.1581 -0.0411 -0.0334 0.0125  426  GLY A CA  
1595 C C   . GLY A 201 ? 0.1627 0.2346 0.1860 -0.0387 -0.0331 0.0096  426  GLY A C   
1596 O O   . GLY A 201 ? 0.1396 0.2123 0.1603 -0.0362 -0.0341 0.0093  426  GLY A O   
1597 N N   . THR A 202 ? 0.1548 0.2181 0.1740 -0.0394 -0.0315 0.0079  427  THR A N   
1598 C CA  . THR A 202 ? 0.1158 0.1704 0.1275 -0.0378 -0.0312 0.0051  427  THR A CA  
1599 C C   . THR A 202 ? 0.2027 0.2492 0.2110 -0.0409 -0.0315 0.0032  427  THR A C   
1600 O O   . THR A 202 ? 0.1706 0.2174 0.1820 -0.0443 -0.0316 0.0042  427  THR A O   
1601 C CB  . THR A 202 ? 0.1614 0.2139 0.1718 -0.0331 -0.0279 0.0054  427  THR A CB  
1602 O OG1 . THR A 202 ? 0.1899 0.2362 0.1941 -0.0315 -0.0279 0.0030  427  THR A OG1 
1603 C CG2 . THR A 202 ? 0.1708 0.2204 0.1822 -0.0332 -0.0254 0.0061  427  THR A CG2 
1604 N N   . VAL A 203 ? 0.1707 0.2093 0.1723 -0.0398 -0.0314 0.0005  428  VAL A N   
1605 C CA  . VAL A 203 ? 0.1854 0.2149 0.1827 -0.0421 -0.0315 -0.0017 428  VAL A CA  
1606 C C   . VAL A 203 ? 0.1633 0.1869 0.1585 -0.0385 -0.0283 -0.0017 428  VAL A C   
1607 O O   . VAL A 203 ? 0.1989 0.2205 0.1907 -0.0350 -0.0272 -0.0029 428  VAL A O   
1608 C CB  . VAL A 203 ? 0.2148 0.2395 0.2056 -0.0435 -0.0338 -0.0049 428  VAL A CB  
1609 C CG1 . VAL A 203 ? 0.1771 0.1908 0.1629 -0.0455 -0.0333 -0.0074 428  VAL A CG1 
1610 C CG2 . VAL A 203 ? 0.2444 0.2759 0.2371 -0.0473 -0.0376 -0.0048 428  VAL A CG2 
1611 N N   . PRO A 204 ? 0.1558 0.1769 0.1528 -0.0394 -0.0268 -0.0002 429  PRO A N   
1612 C CA  . PRO A 204 ? 0.1421 0.1574 0.1367 -0.0361 -0.0243 -0.0002 429  PRO A CA  
1613 C C   . PRO A 204 ? 0.1544 0.1594 0.1435 -0.0368 -0.0244 -0.0026 429  PRO A C   
1614 O O   . PRO A 204 ? 0.1727 0.1739 0.1601 -0.0408 -0.0261 -0.0041 429  PRO A O   
1615 C CB  . PRO A 204 ? 0.1403 0.1573 0.1388 -0.0371 -0.0229 0.0028  429  PRO A CB  
1616 C CG  . PRO A 204 ? 0.1485 0.1672 0.1497 -0.0423 -0.0247 0.0033  429  PRO A CG  
1617 C CD  . PRO A 204 ? 0.1503 0.1738 0.1517 -0.0435 -0.0274 0.0016  429  PRO A CD  
1618 N N   . ILE A 205 ? 0.1512 0.1517 0.1374 -0.0328 -0.0225 -0.0032 430  ILE A N   
1619 C CA  . ILE A 205 ? 0.1826 0.1726 0.1639 -0.0325 -0.0218 -0.0051 430  ILE A CA  
1620 C C   . ILE A 205 ? 0.1644 0.1496 0.1468 -0.0341 -0.0209 -0.0030 430  ILE A C   
1621 O O   . ILE A 205 ? 0.1745 0.1627 0.1598 -0.0322 -0.0196 -0.0001 430  ILE A O   
1622 C CB  . ILE A 205 ? 0.1931 0.1811 0.1720 -0.0273 -0.0198 -0.0060 430  ILE A CB  
1623 C CG1 . ILE A 205 ? 0.1997 0.1911 0.1765 -0.0262 -0.0204 -0.0081 430  ILE A CG1 
1624 C CG2 . ILE A 205 ? 0.2016 0.1786 0.1759 -0.0262 -0.0185 -0.0074 430  ILE A CG2 
1625 C CD1 . ILE A 205 ? 0.1729 0.1642 0.1485 -0.0213 -0.0181 -0.0086 430  ILE A CD1 
1626 N N   . THR A 206 ? 0.1842 0.1615 0.1638 -0.0379 -0.0217 -0.0045 431  THR A N   
1627 C CA  . THR A 206 ? 0.1816 0.1526 0.1616 -0.0394 -0.0205 -0.0023 431  THR A CA  
1628 C C   . THR A 206 ? 0.2091 0.1666 0.1831 -0.0399 -0.0199 -0.0048 431  THR A C   
1629 O O   . THR A 206 ? 0.2355 0.1890 0.2051 -0.0412 -0.0210 -0.0086 431  THR A O   
1630 C CB  . THR A 206 ? 0.1862 0.1615 0.1707 -0.0450 -0.0217 -0.0002 431  THR A CB  
1631 O OG1 . THR A 206 ? 0.2306 0.1989 0.2126 -0.0504 -0.0232 -0.0024 431  THR A OG1 
1632 C CG2 . THR A 206 ? 0.1915 0.1797 0.1812 -0.0456 -0.0230 0.0007  431  THR A CG2 
1633 N N   . THR A 207 ? 0.2299 0.1803 0.2032 -0.0387 -0.0179 -0.0025 432  THR A N   
1634 C CA  . THR A 207 ? 0.2146 0.1508 0.1828 -0.0399 -0.0169 -0.0040 432  THR A CA  
1635 C C   . THR A 207 ? 0.2469 0.1802 0.2167 -0.0468 -0.0178 -0.0028 432  THR A C   
1636 O O   . THR A 207 ? 0.2566 0.1997 0.2317 -0.0501 -0.0191 -0.0008 432  THR A O   
1637 C CB  . THR A 207 ? 0.2633 0.1929 0.2299 -0.0340 -0.0141 -0.0018 432  THR A CB  
1638 O OG1 . THR A 207 ? 0.2439 0.1790 0.2148 -0.0333 -0.0134 0.0030  432  THR A OG1 
1639 C CG2 . THR A 207 ? 0.2605 0.1931 0.2260 -0.0276 -0.0131 -0.0032 432  THR A CG2 
1640 N N   . ARG A 208 ? 0.2527 0.1721 0.2178 -0.0489 -0.0168 -0.0039 433  ARG A N   
1641 C CA  . ARG A 208 ? 0.3087 0.2229 0.2747 -0.0559 -0.0174 -0.0029 433  ARG A CA  
1642 C C   . ARG A 208 ? 0.3027 0.2226 0.2702 -0.0629 -0.0208 -0.0058 433  ARG A C   
1643 O O   . ARG A 208 ? 0.2788 0.2046 0.2515 -0.0685 -0.0220 -0.0037 433  ARG A O   
1644 C CB  . ARG A 208 ? 0.2611 0.1810 0.2327 -0.0562 -0.0161 0.0027  433  ARG A CB  
1645 C CG  . ARG A 208 ? 0.2455 0.1600 0.2154 -0.0497 -0.0131 0.0061  433  ARG A CG  
1646 C CD  . ARG A 208 ? 0.2779 0.1962 0.2517 -0.0508 -0.0118 0.0116  433  ARG A CD  
1647 N NE  . ARG A 208 ? 0.3359 0.2501 0.3078 -0.0444 -0.0094 0.0152  433  ARG A NE  
1648 C CZ  . ARG A 208 ? 0.4747 0.3767 0.4435 -0.0442 -0.0073 0.0179  433  ARG A CZ  
1649 N NH1 . ARG A 208 ? 0.5016 0.3936 0.4687 -0.0504 -0.0070 0.0173  433  ARG A NH1 
1650 N NH2 . ARG A 208 ? 0.4908 0.3909 0.4582 -0.0376 -0.0056 0.0214  433  ARG A NH2 
1651 N N   . ARG A 209 ? 0.3042 0.2225 0.2670 -0.0627 -0.0225 -0.0106 434  ARG A N   
1652 C CA  . ARG A 209 ? 0.3392 0.2635 0.3027 -0.0687 -0.0263 -0.0134 434  ARG A CA  
1653 C C   . ARG A 209 ? 0.4905 0.4015 0.4472 -0.0746 -0.0275 -0.0178 434  ARG A C   
1654 O O   . ARG A 209 ? 0.3807 0.2935 0.3344 -0.0781 -0.0306 -0.0218 434  ARG A O   
1655 C CB  . ARG A 209 ? 0.2679 0.2010 0.2306 -0.0648 -0.0276 -0.0154 434  ARG A CB  
1656 C CG  . ARG A 209 ? 0.2647 0.2109 0.2341 -0.0601 -0.0267 -0.0114 434  ARG A CG  
1657 C CD  . ARG A 209 ? 0.2719 0.2279 0.2416 -0.0573 -0.0282 -0.0128 434  ARG A CD  
1658 N NE  . ARG A 209 ? 0.3054 0.2551 0.2685 -0.0524 -0.0268 -0.0158 434  ARG A NE  
1659 C CZ  . ARG A 209 ? 0.3463 0.2957 0.3044 -0.0529 -0.0285 -0.0195 434  ARG A CZ  
1660 N NH1 . ARG A 209 ? 0.2882 0.2428 0.2467 -0.0582 -0.0322 -0.0208 434  ARG A NH1 
1661 N NH2 . ARG A 209 ? 0.2934 0.2377 0.2460 -0.0479 -0.0265 -0.0216 434  ARG A NH2 
1662 N N   . GLN A 210 ? 0.3817 0.2791 0.3357 -0.0759 -0.0251 -0.0172 435  GLN A N   
1663 C CA  . GLN A 210 ? 0.4571 0.3401 0.4041 -0.0817 -0.0260 -0.0216 435  GLN A CA  
1664 C C   . GLN A 210 ? 0.4746 0.3628 0.4256 -0.0917 -0.0296 -0.0219 435  GLN A C   
1665 O O   . GLN A 210 ? 0.6395 0.5225 0.5854 -0.0975 -0.0325 -0.0268 435  GLN A O   
1666 C CB  . GLN A 210 ? 0.4432 0.3089 0.3858 -0.0798 -0.0220 -0.0206 435  GLN A CB  
1667 C CG  . GLN A 210 ? 0.6588 0.5188 0.5973 -0.0699 -0.0185 -0.0205 435  GLN A CG  
1668 C CD  . GLN A 210 ? 0.8736 0.7286 0.8042 -0.0674 -0.0189 -0.0264 435  GLN A CD  
1669 O OE1 . GLN A 210 ? 0.8887 0.7339 0.8126 -0.0727 -0.0203 -0.0313 435  GLN A OE1 
1670 N NE2 . GLN A 210 ? 0.7682 0.6301 0.6993 -0.0596 -0.0176 -0.0259 435  GLN A NE2 
1671 N N   A SER A 211 ? 0.6264 0.5251 0.5866 -0.0940 -0.0296 -0.0168 436  SER A N   
1672 N N   B SER A 211 ? 0.6262 0.5250 0.5864 -0.0940 -0.0296 -0.0168 436  SER A N   
1673 C CA  A SER A 211 ? 0.7303 0.6359 0.6960 -0.1034 -0.0329 -0.0165 436  SER A CA  
1674 C CA  B SER A 211 ? 0.7305 0.6360 0.6962 -0.1035 -0.0329 -0.0165 436  SER A CA  
1675 C C   A SER A 211 ? 0.8051 0.7244 0.7729 -0.1054 -0.0375 -0.0189 436  SER A C   
1676 C C   B SER A 211 ? 0.8054 0.7248 0.7732 -0.1055 -0.0375 -0.0189 436  SER A C   
1677 O O   A SER A 211 ? 0.7413 0.6588 0.7064 -0.1125 -0.0411 -0.0228 436  SER A O   
1678 O O   B SER A 211 ? 0.7413 0.6592 0.7067 -0.1126 -0.0412 -0.0227 436  SER A O   
1679 C CB  A SER A 211 ? 0.6180 0.5326 0.5931 -0.1044 -0.0311 -0.0101 436  SER A CB  
1680 C CB  B SER A 211 ? 0.6181 0.5324 0.5932 -0.1047 -0.0311 -0.0102 436  SER A CB  
1681 O OG  A SER A 211 ? 0.5174 0.4411 0.4993 -0.1132 -0.0341 -0.0094 436  SER A OG  
1682 O OG  B SER A 211 ? 0.4954 0.3958 0.4684 -0.1064 -0.0279 -0.0081 436  SER A OG  
1683 N N   . ASP A 212 ? 0.6372 0.5701 0.6093 -0.0993 -0.0374 -0.0167 437  ASP A N   
1684 C CA  . ASP A 212 ? 0.5794 0.5254 0.5534 -0.0998 -0.0414 -0.0183 437  ASP A CA  
1685 C C   . ASP A 212 ? 0.3987 0.3505 0.3724 -0.0905 -0.0395 -0.0172 437  ASP A C   
1686 O O   . ASP A 212 ? 0.5261 0.4816 0.5043 -0.0857 -0.0364 -0.0131 437  ASP A O   
1687 C CB  . ASP A 212 ? 0.7921 0.7539 0.7767 -0.1053 -0.0440 -0.0150 437  ASP A CB  
1688 C CG  . ASP A 212 ? 0.7511 0.7238 0.7442 -0.1005 -0.0411 -0.0093 437  ASP A CG  
1689 O OD1 . ASP A 212 ? 0.7403 0.7062 0.7335 -0.0983 -0.0372 -0.0066 437  ASP A OD1 
1690 O OD2 . ASP A 212 ? 0.7337 0.7215 0.7329 -0.0987 -0.0427 -0.0075 437  ASP A OD2 
1691 N N   . PRO A 213 ? 0.3394 0.2917 0.3074 -0.0880 -0.0413 -0.0207 438  PRO A N   
1692 C CA  . PRO A 213 ? 0.3554 0.3096 0.3216 -0.0793 -0.0388 -0.0202 438  PRO A CA  
1693 C C   . PRO A 213 ? 0.3013 0.2718 0.2743 -0.0761 -0.0398 -0.0171 438  PRO A C   
1694 O O   . PRO A 213 ? 0.3121 0.2843 0.2845 -0.0693 -0.0374 -0.0162 438  PRO A O   
1695 C CB  . PRO A 213 ? 0.3687 0.3140 0.3245 -0.0786 -0.0397 -0.0256 438  PRO A CB  
1696 C CG  . PRO A 213 ? 0.3406 0.2880 0.2951 -0.0866 -0.0445 -0.0283 438  PRO A CG  
1697 C CD  . PRO A 213 ? 0.3119 0.2599 0.2730 -0.0930 -0.0451 -0.0258 438  PRO A CD  
1698 N N   . ILE A 214 ? 0.2240 0.2065 0.2036 -0.0805 -0.0429 -0.0155 439  ILE A N   
1699 C CA  . ILE A 214 ? 0.2205 0.2175 0.2060 -0.0768 -0.0436 -0.0128 439  ILE A CA  
1700 C C   . ILE A 214 ? 0.2256 0.2281 0.2185 -0.0736 -0.0403 -0.0081 439  ILE A C   
1701 O O   . ILE A 214 ? 0.2162 0.2204 0.2144 -0.0774 -0.0397 -0.0056 439  ILE A O   
1702 C CB  . ILE A 214 ? 0.3075 0.3159 0.2974 -0.0819 -0.0483 -0.0125 439  ILE A CB  
1703 C CG1 . ILE A 214 ? 0.3067 0.3105 0.2880 -0.0843 -0.0518 -0.0173 439  ILE A CG1 
1704 C CG2 . ILE A 214 ? 0.3273 0.3501 0.3242 -0.0776 -0.0483 -0.0090 439  ILE A CG2 
1705 C CD1 . ILE A 214 ? 0.2508 0.2514 0.2250 -0.0775 -0.0504 -0.0190 439  ILE A CD1 
1706 N N   . ARG A 215 ? 0.2100 0.2155 0.2029 -0.0669 -0.0380 -0.0069 440  ARG A N   
1707 C CA  . ARG A 215 ? 0.1837 0.1945 0.1823 -0.0634 -0.0350 -0.0029 440  ARG A CA  
1708 C C   . ARG A 215 ? 0.2094 0.2325 0.2127 -0.0602 -0.0355 -0.0011 440  ARG A C   
1709 O O   . ARG A 215 ? 0.2052 0.2289 0.2050 -0.0567 -0.0359 -0.0026 440  ARG A O   
1710 C CB  . ARG A 215 ? 0.2195 0.2215 0.2138 -0.0583 -0.0315 -0.0030 440  ARG A CB  
1711 C CG  . ARG A 215 ? 0.2401 0.2296 0.2306 -0.0605 -0.0302 -0.0038 440  ARG A CG  
1712 C CD  . ARG A 215 ? 0.2335 0.2250 0.2295 -0.0642 -0.0293 -0.0003 440  ARG A CD  
1713 N NE  . ARG A 215 ? 0.2566 0.2354 0.2488 -0.0672 -0.0282 -0.0008 440  ARG A NE  
1714 C CZ  . ARG A 215 ? 0.3294 0.3029 0.3201 -0.0736 -0.0302 -0.0029 440  ARG A CZ  
1715 N NH1 . ARG A 215 ? 0.3248 0.3054 0.3176 -0.0780 -0.0338 -0.0046 440  ARG A NH1 
1716 N NH2 . ARG A 215 ? 0.3131 0.2735 0.2998 -0.0758 -0.0288 -0.0033 440  ARG A NH2 
1717 N N   . ILE A 216 ? 0.1859 0.2187 0.1971 -0.0613 -0.0350 0.0023  441  ILE A N   
1718 C CA  . ILE A 216 ? 0.1825 0.2267 0.1986 -0.0580 -0.0350 0.0044  441  ILE A CA  
1719 C C   . ILE A 216 ? 0.1370 0.1858 0.1586 -0.0561 -0.0316 0.0079  441  ILE A C   
1720 O O   . ILE A 216 ? 0.1822 0.2328 0.2081 -0.0599 -0.0310 0.0099  441  ILE A O   
1721 C CB  . ILE A 216 ? 0.1784 0.2323 0.1990 -0.0616 -0.0388 0.0048  441  ILE A CB  
1722 C CG1 . ILE A 216 ? 0.2464 0.2962 0.2604 -0.0631 -0.0424 0.0012  441  ILE A CG1 
1723 C CG2 . ILE A 216 ? 0.2151 0.2805 0.2417 -0.0576 -0.0381 0.0077  441  ILE A CG2 
1724 C CD1 . ILE A 216 ? 0.2927 0.3512 0.3104 -0.0680 -0.0470 0.0014  441  ILE A CD1 
1725 N N   . ILE A 217 ? 0.1320 0.1824 0.1531 -0.0506 -0.0293 0.0087  442  ILE A N   
1726 C CA  . ILE A 217 ? 0.1359 0.1912 0.1613 -0.0483 -0.0261 0.0117  442  ILE A CA  
1727 C C   . ILE A 217 ? 0.1428 0.2081 0.1728 -0.0455 -0.0261 0.0131  442  ILE A C   
1728 O O   . ILE A 217 ? 0.1454 0.2107 0.1727 -0.0427 -0.0272 0.0117  442  ILE A O   
1729 C CB  . ILE A 217 ? 0.1432 0.1915 0.1639 -0.0444 -0.0233 0.0114  442  ILE A CB  
1730 C CG1 . ILE A 217 ? 0.1527 0.2057 0.1767 -0.0426 -0.0200 0.0142  442  ILE A CG1 
1731 C CG2 . ILE A 217 ? 0.1577 0.2039 0.1741 -0.0402 -0.0235 0.0093  442  ILE A CG2 
1732 C CD1 . ILE A 217 ? 0.1543 0.2010 0.1737 -0.0396 -0.0178 0.0142  442  ILE A CD1 
1733 N N   . SER A 218 ? 0.1456 0.2192 0.1823 -0.0461 -0.0246 0.0160  443  SER A N   
1734 C CA  . SER A 218 ? 0.1159 0.1994 0.1579 -0.0433 -0.0244 0.0177  443  SER A CA  
1735 C C   . SER A 218 ? 0.1394 0.2241 0.1820 -0.0388 -0.0201 0.0192  443  SER A C   
1736 O O   . SER A 218 ? 0.1542 0.2348 0.1949 -0.0389 -0.0175 0.0196  443  SER A O   
1737 C CB  . SER A 218 ? 0.1946 0.2883 0.2449 -0.0471 -0.0260 0.0201  443  SER A CB  
1738 O OG  . SER A 218 ? 0.1758 0.2688 0.2251 -0.0517 -0.0304 0.0184  443  SER A OG  
1739 N N   . CYS A 219 ? 0.1187 0.2088 0.1635 -0.0349 -0.0194 0.0200  444  CYS A N   
1740 C CA  . CYS A 219 ? 0.1179 0.2094 0.1633 -0.0307 -0.0152 0.0211  444  CYS A CA  
1741 C C   . CYS A 219 ? 0.1454 0.2469 0.1977 -0.0283 -0.0145 0.0235  444  CYS A C   
1742 O O   . CYS A 219 ? 0.1202 0.2271 0.1759 -0.0290 -0.0176 0.0242  444  CYS A O   
1743 C CB  . CYS A 219 ? 0.1245 0.2083 0.1630 -0.0271 -0.0141 0.0188  444  CYS A CB  
1744 S SG  . CYS A 219 ? 0.1216 0.2051 0.1581 -0.0243 -0.0164 0.0176  444  CYS A SG  
1745 N N   . ALA A 220 ? 0.0950 0.1988 0.1490 -0.0251 -0.0102 0.0249  445  ALA A N   
1746 C CA  . ALA A 220 ? 0.0879 0.2012 0.1490 -0.0222 -0.0086 0.0275  445  ALA A CA  
1747 C C   . ALA A 220 ? 0.0956 0.2077 0.1548 -0.0172 -0.0083 0.0270  445  ALA A C   
1748 O O   . ALA A 220 ? 0.1051 0.2250 0.1701 -0.0148 -0.0087 0.0292  445  ALA A O   
1749 C CB  . ALA A 220 ? 0.1292 0.2453 0.1926 -0.0208 -0.0035 0.0292  445  ALA A CB  
1750 N N   . LEU A 221 ? 0.1259 0.2285 0.1773 -0.0154 -0.0076 0.0244  446  LEU A N   
1751 C CA  . LEU A 221 ? 0.0848 0.1844 0.1335 -0.0110 -0.0068 0.0237  446  LEU A CA  
1752 C C   . LEU A 221 ? 0.1100 0.2010 0.1515 -0.0120 -0.0090 0.0209  446  LEU A C   
1753 O O   . LEU A 221 ? 0.1087 0.1937 0.1456 -0.0139 -0.0087 0.0189  446  LEU A O   
1754 C CB  . LEU A 221 ? 0.0906 0.1874 0.1375 -0.0072 -0.0018 0.0234  446  LEU A CB  
1755 C CG  . LEU A 221 ? 0.1148 0.2190 0.1678 -0.0054 0.0018  0.0259  446  LEU A CG  
1756 C CD1 . LEU A 221 ? 0.1233 0.2216 0.1711 -0.0030 0.0065  0.0244  446  LEU A CD1 
1757 C CD2 . LEU A 221 ? 0.1180 0.2296 0.1774 -0.0017 0.0019  0.0287  446  LEU A CD2 
1758 N N   . PRO A 222 ? 0.1049 0.1953 0.1452 -0.0105 -0.0111 0.0208  447  PRO A N   
1759 C CA  . PRO A 222 ? 0.1315 0.2136 0.1647 -0.0107 -0.0120 0.0183  447  PRO A CA  
1760 C C   . PRO A 222 ? 0.1210 0.1968 0.1501 -0.0087 -0.0085 0.0166  447  PRO A C   
1761 O O   . PRO A 222 ? 0.1137 0.1905 0.1443 -0.0058 -0.0053 0.0175  447  PRO A O   
1762 C CB  . PRO A 222 ? 0.0969 0.1804 0.1301 -0.0083 -0.0137 0.0194  447  PRO A CB  
1763 C CG  . PRO A 222 ? 0.1038 0.1973 0.1442 -0.0085 -0.0155 0.0224  447  PRO A CG  
1764 C CD  . PRO A 222 ? 0.1027 0.2002 0.1479 -0.0082 -0.0123 0.0235  447  PRO A CD  
1765 N N   . GLN A 223 ? 0.1149 0.1843 0.1388 -0.0103 -0.0090 0.0142  448  GLN A N   
1766 C CA  . GLN A 223 ? 0.1479 0.2119 0.1678 -0.0090 -0.0063 0.0125  448  GLN A CA  
1767 C C   . GLN A 223 ? 0.1457 0.2077 0.1647 -0.0056 -0.0042 0.0126  448  GLN A C   
1768 O O   . GLN A 223 ? 0.1153 0.1749 0.1330 -0.0039 -0.0011 0.0120  448  GLN A O   
1769 C CB  . GLN A 223 ? 0.1096 0.1682 0.1248 -0.0109 -0.0077 0.0102  448  GLN A CB  
1770 C CG  . GLN A 223 ? 0.1227 0.1764 0.1339 -0.0099 -0.0055 0.0083  448  GLN A CG  
1771 C CD  . GLN A 223 ? 0.1602 0.2143 0.1710 -0.0099 -0.0033 0.0082  448  GLN A CD  
1772 O OE1 . GLN A 223 ? 0.1867 0.2420 0.1977 -0.0117 -0.0039 0.0086  448  GLN A OE1 
1773 N NE2 . GLN A 223 ? 0.1448 0.1973 0.1544 -0.0079 -0.0004 0.0077  448  GLN A NE2 
1774 N N   . GLU A 224 ? 0.1398 0.2021 0.1591 -0.0045 -0.0058 0.0135  449  GLU A N   
1775 C CA  . GLU A 224 ? 0.1026 0.1617 0.1206 -0.0013 -0.0037 0.0140  449  GLU A CA  
1776 C C   . GLU A 224 ? 0.1149 0.1774 0.1368 0.0020  -0.0009 0.0160  449  GLU A C   
1777 O O   . GLU A 224 ? 0.1196 0.1775 0.1396 0.0048  0.0021  0.0157  449  GLU A O   
1778 C CB  . GLU A 224 ? 0.1334 0.1924 0.1505 -0.0008 -0.0060 0.0151  449  GLU A CB  
1779 C CG  . GLU A 224 ? 0.1141 0.1685 0.1264 -0.0032 -0.0075 0.0129  449  GLU A CG  
1780 C CD  . GLU A 224 ? 0.1230 0.1796 0.1353 -0.0064 -0.0105 0.0120  449  GLU A CD  
1781 O OE1 . GLU A 224 ? 0.1134 0.1751 0.1295 -0.0075 -0.0118 0.0130  449  GLU A OE1 
1782 O OE2 . GLU A 224 ? 0.1664 0.2193 0.1750 -0.0080 -0.0115 0.0103  449  GLU A OE2 
1783 N N   . TRP A 225 ? 0.1276 0.1979 0.1551 0.0018  -0.0017 0.0181  450  TRP A N   
1784 C CA  . TRP A 225 ? 0.0934 0.1677 0.1252 0.0053  0.0015  0.0200  450  TRP A CA  
1785 C C   . TRP A 225 ? 0.1050 0.1756 0.1342 0.0053  0.0052  0.0181  450  TRP A C   
1786 O O   . TRP A 225 ? 0.1191 0.1873 0.1477 0.0088  0.0091  0.0181  450  TRP A O   
1787 C CB  . TRP A 225 ? 0.1023 0.1870 0.1416 0.0046  -0.0003 0.0229  450  TRP A CB  
1788 C CG  . TRP A 225 ? 0.1060 0.1963 0.1487 0.0052  -0.0038 0.0254  450  TRP A CG  
1789 C CD1 . TRP A 225 ? 0.1836 0.2701 0.2227 0.0059  -0.0058 0.0253  450  TRP A CD1 
1790 C CD2 . TRP A 225 ? 0.1240 0.2252 0.1745 0.0052  -0.0057 0.0285  450  TRP A CD2 
1791 N NE1 . TRP A 225 ? 0.1453 0.2396 0.1888 0.0064  -0.0092 0.0282  450  TRP A NE1 
1792 C CE2 . TRP A 225 ? 0.1251 0.2288 0.1759 0.0058  -0.0093 0.0301  450  TRP A CE2 
1793 C CE3 . TRP A 225 ? 0.1394 0.2491 0.1968 0.0043  -0.0047 0.0302  450  TRP A CE3 
1794 C CZ2 . TRP A 225 ? 0.1769 0.2916 0.2347 0.0056  -0.0125 0.0333  450  TRP A CZ2 
1795 C CZ3 . TRP A 225 ? 0.1118 0.2327 0.1770 0.0040  -0.0075 0.0335  450  TRP A CZ3 
1796 C CH2 . TRP A 225 ? 0.1380 0.2615 0.2033 0.0045  -0.0117 0.0349  450  TRP A CH2 
1797 N N   . ILE A 226 ? 0.1013 0.1711 0.1284 0.0016  0.0042  0.0164  451  ILE A N   
1798 C CA  . ILE A 226 ? 0.1099 0.1764 0.1334 0.0015  0.0073  0.0146  451  ILE A CA  
1799 C C   . ILE A 226 ? 0.1317 0.1897 0.1492 0.0029  0.0094  0.0121  451  ILE A C   
1800 O O   . ILE A 226 ? 0.1341 0.1894 0.1497 0.0053  0.0133  0.0113  451  ILE A O   
1801 C CB  . ILE A 226 ? 0.0958 0.1621 0.1174 -0.0026 0.0054  0.0136  451  ILE A CB  
1802 C CG1 . ILE A 226 ? 0.1023 0.1764 0.1300 -0.0045 0.0038  0.0162  451  ILE A CG1 
1803 C CG2 . ILE A 226 ? 0.1231 0.1855 0.1397 -0.0027 0.0082  0.0117  451  ILE A CG2 
1804 C CD1 . ILE A 226 ? 0.1418 0.2148 0.1676 -0.0084 0.0018  0.0156  451  ILE A CD1 
1805 N N   . THR A 227 ? 0.1199 0.1735 0.1343 0.0014  0.0071  0.0106  452  THR A N   
1806 C CA  . THR A 227 ? 0.1301 0.1759 0.1393 0.0021  0.0088  0.0083  452  THR A CA  
1807 C C   . THR A 227 ? 0.1461 0.1897 0.1563 0.0062  0.0119  0.0095  452  THR A C   
1808 O O   . THR A 227 ? 0.1629 0.2002 0.1691 0.0075  0.0151  0.0076  452  THR A O   
1809 C CB  . THR A 227 ? 0.1306 0.1734 0.1375 -0.0002 0.0060  0.0072  452  THR A CB  
1810 O OG1 . THR A 227 ? 0.1440 0.1884 0.1501 -0.0034 0.0036  0.0062  452  THR A OG1 
1811 C CG2 . THR A 227 ? 0.1642 0.1993 0.1664 -0.0002 0.0078  0.0049  452  THR A CG2 
1812 N N   . TRP A 228 ? 0.1252 0.1739 0.1405 0.0085  0.0108  0.0126  453  TRP A N   
1813 C CA  . TRP A 228 ? 0.1347 0.1821 0.1516 0.0132  0.0138  0.0145  453  TRP A CA  
1814 C C   . TRP A 228 ? 0.1560 0.2035 0.1734 0.0159  0.0182  0.0142  453  TRP A C   
1815 O O   . TRP A 228 ? 0.1580 0.1990 0.1727 0.0191  0.0220  0.0135  453  TRP A O   
1816 C CB  . TRP A 228 ? 0.1160 0.1713 0.1391 0.0150  0.0112  0.0184  453  TRP A CB  
1817 C CG  . TRP A 228 ? 0.1351 0.1887 0.1596 0.0199  0.0130  0.0211  453  TRP A CG  
1818 C CD1 . TRP A 228 ? 0.1238 0.1828 0.1538 0.0246  0.0151  0.0242  453  TRP A CD1 
1819 C CD2 . TRP A 228 ? 0.1568 0.2033 0.1774 0.0208  0.0129  0.0212  453  TRP A CD2 
1820 N NE1 . TRP A 228 ? 0.1597 0.2149 0.1893 0.0288  0.0161  0.0264  453  TRP A NE1 
1821 C CE2 . TRP A 228 ? 0.1745 0.2216 0.1979 0.0263  0.0148  0.0246  453  TRP A CE2 
1822 C CE3 . TRP A 228 ? 0.1485 0.1884 0.1636 0.0176  0.0115  0.0190  453  TRP A CE3 
1823 C CZ2 . TRP A 228 ? 0.1919 0.2323 0.2123 0.0286  0.0154  0.0260  453  TRP A CZ2 
1824 C CZ3 . TRP A 228 ? 0.1866 0.2203 0.1990 0.0195  0.0122  0.0203  453  TRP A CZ3 
1825 C CH2 . TRP A 228 ? 0.2125 0.2461 0.2272 0.0249  0.0142  0.0238  453  TRP A CH2 
1826 N N   . PHE A 229 ? 0.1550 0.2092 0.1755 0.0147  0.0182  0.0148  454  PHE A N   
1827 C CA  . PHE A 229 ? 0.1157 0.1704 0.1363 0.0173  0.0228  0.0146  454  PHE A CA  
1828 C C   . PHE A 229 ? 0.1594 0.2049 0.1716 0.0161  0.0254  0.0104  454  PHE A C   
1829 O O   . PHE A 229 ? 0.1740 0.2160 0.1838 0.0191  0.0300  0.0094  454  PHE A O   
1830 C CB  . PHE A 229 ? 0.1365 0.2008 0.1623 0.0157  0.0222  0.0164  454  PHE A CB  
1831 C CG  . PHE A 229 ? 0.1650 0.2392 0.1992 0.0160  0.0193  0.0203  454  PHE A CG  
1832 C CD1 . PHE A 229 ? 0.1726 0.2487 0.2106 0.0198  0.0191  0.0227  454  PHE A CD1 
1833 C CD2 . PHE A 229 ? 0.1744 0.2560 0.2126 0.0122  0.0166  0.0214  454  PHE A CD2 
1834 C CE1 . PHE A 229 ? 0.1489 0.2349 0.1945 0.0197  0.0158  0.0262  454  PHE A CE1 
1835 C CE2 . PHE A 229 ? 0.1104 0.2011 0.1560 0.0117  0.0135  0.0246  454  PHE A CE2 
1836 C CZ  . PHE A 229 ? 0.1516 0.2450 0.2010 0.0154  0.0129  0.0270  454  PHE A CZ  
1837 N N   . LEU A 230 ? 0.1507 0.1929 0.1584 0.0116  0.0224  0.0080  455  LEU A N   
1838 C CA  . LEU A 230 ? 0.1469 0.1813 0.1467 0.0098  0.0239  0.0040  455  LEU A CA  
1839 C C   . LEU A 230 ? 0.1770 0.2019 0.1725 0.0112  0.0258  0.0020  455  LEU A C   
1840 O O   . LEU A 230 ? 0.2442 0.2620 0.2333 0.0109  0.0285  -0.0013 455  LEU A O   
1841 C CB  . LEU A 230 ? 0.1387 0.1736 0.1361 0.0050  0.0198  0.0026  455  LEU A CB  
1842 C CG  . LEU A 230 ? 0.1432 0.1854 0.1435 0.0029  0.0178  0.0042  455  LEU A CG  
1843 C CD1 . LEU A 230 ? 0.1602 0.2012 0.1575 -0.0011 0.0141  0.0027  455  LEU A CD1 
1844 C CD2 . LEU A 230 ? 0.2364 0.2799 0.2349 0.0040  0.0214  0.0040  455  LEU A CD2 
1845 N N   . THR A 231 ? 0.1450 0.1692 0.1433 0.0124  0.0245  0.0038  456  THR A N   
1846 C CA  . THR A 231 ? 0.1822 0.1969 0.1765 0.0131  0.0261  0.0023  456  THR A CA  
1847 C C   . THR A 231 ? 0.2534 0.2650 0.2493 0.0188  0.0301  0.0043  456  THR A C   
1848 O O   . THR A 231 ? 0.2452 0.2482 0.2380 0.0199  0.0318  0.0037  456  THR A O   
1849 C CB  . THR A 231 ? 0.1573 0.1720 0.1525 0.0107  0.0222  0.0032  456  THR A CB  
1850 O OG1 . THR A 231 ? 0.1867 0.2091 0.1882 0.0125  0.0200  0.0071  456  THR A OG1 
1851 C CG2 . THR A 231 ? 0.2099 0.2261 0.2028 0.0056  0.0189  0.0009  456  THR A CG2 
1852 N N   . HIS A 232 ? 0.2187 0.2373 0.2196 0.0224  0.0319  0.0068  457  HIS A N   
1853 C CA  . HIS A 232 ? 0.2094 0.2262 0.2125 0.0285  0.0362  0.0089  457  HIS A CA  
1854 C C   . HIS A 232 ? 0.2581 0.2764 0.2606 0.0307  0.0405  0.0078  457  HIS A C   
1855 O O   . HIS A 232 ? 0.2789 0.3029 0.2816 0.0278  0.0394  0.0070  457  HIS A O   
1856 C CB  . HIS A 232 ? 0.2179 0.2437 0.2294 0.0317  0.0342  0.0141  457  HIS A CB  
1857 C CG  . HIS A 232 ? 0.2176 0.2413 0.2289 0.0305  0.0306  0.0154  457  HIS A CG  
1858 N ND1 . HIS A 232 ? 0.1688 0.1961 0.1801 0.0255  0.0257  0.0150  457  HIS A ND1 
1859 C CD2 . HIS A 232 ? 0.2916 0.3097 0.3024 0.0338  0.0317  0.0174  457  HIS A CD2 
1860 C CE1 . HIS A 232 ? 0.2095 0.2337 0.2200 0.0257  0.0239  0.0165  457  HIS A CE1 
1861 N NE2 . HIS A 232 ? 0.2109 0.2296 0.2211 0.0306  0.0274  0.0181  457  HIS A NE2 
1862 N N   . ASN A 233 ? 0.2614 0.2741 0.2628 0.0360  0.0458  0.0079  458  ASN A N   
1863 C CA  . ASN A 233 ? 0.3981 0.4113 0.3982 0.0389  0.0509  0.0068  458  ASN A CA  
1864 C C   . ASN A 233 ? 0.3341 0.3575 0.3439 0.0448  0.0530  0.0118  458  ASN A C   
1865 O O   . ASN A 233 ? 0.3939 0.4136 0.4043 0.0509  0.0580  0.0128  458  ASN A O   
1866 C CB  . ASN A 233 ? 0.3770 0.3756 0.3678 0.0406  0.0560  0.0025  458  ASN A CB  
1867 N N   . PHE A 234 ? 0.2473 0.2838 0.2648 0.0429  0.0489  0.0151  459  PHE A N   
1868 C CA  . PHE A 234 ? 0.2240 0.2723 0.2521 0.0476  0.0498  0.0202  459  PHE A CA  
1869 C C   . PHE A 234 ? 0.2330 0.2866 0.2632 0.0501  0.0548  0.0205  459  PHE A C   
1870 O O   . PHE A 234 ? 0.2398 0.2934 0.2658 0.0462  0.0552  0.0178  459  PHE A O   
1871 C CB  . PHE A 234 ? 0.1694 0.2296 0.2049 0.0439  0.0434  0.0234  459  PHE A CB  
1872 C CG  . PHE A 234 ? 0.1416 0.1986 0.1761 0.0422  0.0385  0.0240  459  PHE A CG  
1873 C CD1 . PHE A 234 ? 0.2871 0.3364 0.3197 0.0465  0.0402  0.0249  459  PHE A CD1 
1874 C CD2 . PHE A 234 ? 0.1719 0.2335 0.2073 0.0364  0.0326  0.0240  459  PHE A CD2 
1875 C CE1 . PHE A 234 ? 0.1800 0.2268 0.2115 0.0448  0.0360  0.0259  459  PHE A CE1 
1876 C CE2 . PHE A 234 ? 0.2264 0.2853 0.2605 0.0350  0.0286  0.0246  459  PHE A CE2 
1877 C CZ  . PHE A 234 ? 0.2658 0.3176 0.2979 0.0391  0.0302  0.0256  459  PHE A CZ  
1878 N N   . THR A 235 ? 0.2249 0.2838 0.2620 0.0568  0.0587  0.0240  460  THR A N   
1879 C CA  . THR A 235 ? 0.2451 0.3124 0.2871 0.0599  0.0635  0.0255  460  THR A CA  
1880 C C   . THR A 235 ? 0.2857 0.3704 0.3411 0.0604  0.0604  0.0313  460  THR A C   
1881 O O   . THR A 235 ? 0.3241 0.4129 0.3859 0.0640  0.0586  0.0350  460  THR A O   
1882 C CB  . THR A 235 ? 0.3798 0.4401 0.4197 0.0678  0.0713  0.0252  460  THR A CB  
1883 O OG1 . THR A 235 ? 0.3579 0.4014 0.3846 0.0666  0.0739  0.0193  460  THR A OG1 
1884 C CG2 . THR A 235 ? 0.3095 0.3796 0.3550 0.0713  0.0768  0.0270  460  THR A CG2 
1885 N N   . ALA A 236 ? 0.2382 0.3328 0.2975 0.0565  0.0596  0.0321  461  ALA A N   
1886 C CA  . ALA A 236 ? 0.3160 0.4277 0.3884 0.0562  0.0568  0.0373  461  ALA A CA  
1887 C C   . ALA A 236 ? 0.2825 0.4017 0.3631 0.0641  0.0629  0.0410  461  ALA A C   
1888 O O   . ALA A 236 ? 0.3393 0.4612 0.4203 0.0658  0.0686  0.0407  461  ALA A O   
1889 C CB  . ALA A 236 ? 0.2582 0.3769 0.3320 0.0495  0.0548  0.0371  461  ALA A CB  
1890 N N   . LEU A 237 ? 0.2095 0.3323 0.2965 0.0693  0.0618  0.0446  462  LEU A N   
1891 C CA  . LEU A 237 ? 0.2216 0.3518 0.3171 0.0778  0.0675  0.0485  462  LEU A CA  
1892 C C   . LEU A 237 ? 0.2158 0.3667 0.3260 0.0774  0.0661  0.0538  462  LEU A C   
1893 O O   . LEU A 237 ? 0.3057 0.4654 0.4246 0.0844  0.0710  0.0576  462  LEU A O   
1894 C CB  . LEU A 237 ? 0.3160 0.4409 0.4120 0.0842  0.0672  0.0507  462  LEU A CB  
1895 C CG  . LEU A 237 ? 0.3462 0.4502 0.4285 0.0857  0.0700  0.0458  462  LEU A CG  
1896 C CD1 . LEU A 237 ? 0.4020 0.5011 0.4852 0.0914  0.0691  0.0486  462  LEU A CD1 
1897 C CD2 . LEU A 237 ? 0.3837 0.4793 0.4599 0.0898  0.0787  0.0426  462  LEU A CD2 
1898 N N   . GLY A 238 ? 0.2432 0.4020 0.3565 0.0694  0.0597  0.0542  463  GLY A N   
1899 C CA  . GLY A 238 ? 0.1593 0.3373 0.2861 0.0674  0.0580  0.0588  463  GLY A CA  
1900 C C   . GLY A 238 ? 0.1727 0.3523 0.2973 0.0577  0.0539  0.0568  463  GLY A C   
1901 O O   . GLY A 238 ? 0.1718 0.3384 0.2848 0.0532  0.0521  0.0522  463  GLY A O   
1902 N N   . ASP A 239 ? 0.1649 0.3609 0.3011 0.0546  0.0524  0.0605  464  ASP A N   
1903 C CA  . ASP A 239 ? 0.1371 0.3355 0.2724 0.0455  0.0488  0.0593  464  ASP A CA  
1904 C C   . ASP A 239 ? 0.1802 0.3731 0.3107 0.0394  0.0404  0.0573  464  ASP A C   
1905 O O   . ASP A 239 ? 0.1322 0.3188 0.2560 0.0327  0.0380  0.0543  464  ASP A O   
1906 C CB  . ASP A 239 ? 0.1121 0.3279 0.2607 0.0429  0.0483  0.0636  464  ASP A CB  
1907 C CG  . ASP A 239 ? 0.2073 0.4247 0.3573 0.0469  0.0560  0.0642  464  ASP A CG  
1908 O OD1 . ASP A 239 ? 0.2121 0.4197 0.3533 0.0496  0.0623  0.0614  464  ASP A OD1 
1909 O OD2 . ASP A 239 ? 0.2141 0.4423 0.3734 0.0470  0.0557  0.0674  464  ASP A OD2 
1910 N N   . ALA A 240 ? 0.1483 0.3439 0.2821 0.0418  0.0360  0.0592  465  ALA A N   
1911 C CA  . ALA A 240 ? 0.1171 0.3088 0.2469 0.0363  0.0283  0.0577  465  ALA A CA  
1912 C C   . ALA A 240 ? 0.1424 0.3293 0.2698 0.0416  0.0264  0.0584  465  ALA A C   
1913 O O   . ALA A 240 ? 0.1334 0.3256 0.2668 0.0489  0.0294  0.0617  465  ALA A O   
1914 C CB  . ALA A 240 ? 0.1169 0.3234 0.2567 0.0301  0.0224  0.0605  465  ALA A CB  
1915 N N   . ALA A 241 ? 0.1153 0.2918 0.2337 0.0380  0.0217  0.0553  466  ALA A N   
1916 C CA  . ALA A 241 ? 0.1229 0.2954 0.2389 0.0415  0.0187  0.0563  466  ALA A CA  
1917 C C   . ALA A 241 ? 0.1251 0.3097 0.2480 0.0380  0.0113  0.0593  466  ALA A C   
1918 O O   . ALA A 241 ? 0.1429 0.3275 0.2636 0.0306  0.0065  0.0573  466  ALA A O   
1919 C CB  . ALA A 241 ? 0.1062 0.2613 0.2087 0.0395  0.0180  0.0515  466  ALA A CB  
1920 N N   . LEU A 242 ? 0.1655 0.3606 0.2969 0.0434  0.0104  0.0641  467  LEU A N   
1921 C CA  . LEU A 242 ? 0.1013 0.3073 0.2381 0.0407  0.0028  0.0670  467  LEU A CA  
1922 C C   . LEU A 242 ? 0.1174 0.3117 0.2436 0.0399  -0.0011 0.0650  467  LEU A C   
1923 O O   . LEU A 242 ? 0.1513 0.3358 0.2720 0.0458  0.0018  0.0651  467  LEU A O   
1924 C CB  . LEU A 242 ? 0.1487 0.3685 0.2967 0.0471  0.0031  0.0729  467  LEU A CB  
1925 C CG  . LEU A 242 ? 0.1470 0.3743 0.2972 0.0440  -0.0047 0.0750  467  LEU A CG  
1926 C CD1 . LEU A 242 ? 0.1592 0.3940 0.3128 0.0347  -0.0091 0.0734  467  LEU A CD1 
1927 C CD2 . LEU A 242 ? 0.1142 0.3484 0.2708 0.0508  -0.0034 0.0795  467  LEU A CD2 
1928 N N   . LEU A 243 ? 0.1349 0.3293 0.2577 0.0325  -0.0074 0.0630  468  LEU A N   
1929 C CA  . LEU A 243 ? 0.1338 0.3179 0.2465 0.0310  -0.0112 0.0609  468  LEU A CA  
1930 C C   . LEU A 243 ? 0.1473 0.3422 0.2637 0.0286  -0.0187 0.0636  468  LEU A C   
1931 O O   . LEU A 243 ? 0.1366 0.3452 0.2617 0.0249  -0.0220 0.0654  468  LEU A O   
1932 C CB  . LEU A 243 ? 0.1789 0.3513 0.2821 0.0243  -0.0118 0.0552  468  LEU A CB  
1933 C CG  . LEU A 243 ? 0.1062 0.2699 0.2058 0.0238  -0.0059 0.0518  468  LEU A CG  
1934 C CD1 . LEU A 243 ? 0.1131 0.2677 0.2043 0.0169  -0.0082 0.0471  468  LEU A CD1 
1935 C CD2 . LEU A 243 ? 0.1795 0.3327 0.2741 0.0305  -0.0003 0.0514  468  LEU A CD2 
1936 N N   . ARG A 244 ? 0.1541 0.3424 0.2630 0.0302  -0.0215 0.0638  469  ARG A N   
1937 C CA  . ARG A 244 ? 0.1493 0.3445 0.2578 0.0268  -0.0291 0.0651  469  ARG A CA  
1938 C C   . ARG A 244 ? 0.1699 0.3523 0.2662 0.0214  -0.0314 0.0601  469  ARG A C   
1939 O O   . ARG A 244 ? 0.1909 0.3593 0.2786 0.0234  -0.0278 0.0577  469  ARG A O   
1940 C CB  . ARG A 244 ? 0.1538 0.3538 0.2641 0.0337  -0.0307 0.0703  469  ARG A CB  
1941 C CG  . ARG A 244 ? 0.3204 0.5335 0.4417 0.0369  -0.0303 0.0745  469  ARG A CG  
1942 C CD  . ARG A 244 ? 0.4225 0.6355 0.5441 0.0451  -0.0294 0.0791  469  ARG A CD  
1943 N NE  . ARG A 244 ? 0.3814 0.6042 0.5131 0.0491  -0.0270 0.0825  469  ARG A NE  
1944 C CZ  . ARG A 244 ? 0.4708 0.6928 0.6049 0.0578  -0.0230 0.0865  469  ARG A CZ  
1945 N NH1 . ARG A 244 ? 0.3823 0.5936 0.5094 0.0633  -0.0210 0.0877  469  ARG A NH1 
1946 N NH2 . ARG A 244 ? 0.4876 0.7191 0.6311 0.0609  -0.0208 0.0893  469  ARG A NH2 
1947 N N   . TYR A 245 ? 0.1664 0.3536 0.2621 0.0144  -0.0373 0.0585  470  TYR A N   
1948 C CA  . TYR A 245 ? 0.1396 0.3160 0.2241 0.0094  -0.0400 0.0541  470  TYR A CA  
1949 C C   . TYR A 245 ? 0.1636 0.3433 0.2443 0.0103  -0.0455 0.0563  470  TYR A C   
1950 O O   . TYR A 245 ? 0.2178 0.4096 0.3035 0.0077  -0.0510 0.0583  470  TYR A O   
1951 C CB  . TYR A 245 ? 0.1819 0.3595 0.2668 0.0012  -0.0424 0.0504  470  TYR A CB  
1952 C CG  . TYR A 245 ? 0.1826 0.3476 0.2559 -0.0033 -0.0439 0.0454  470  TYR A CG  
1953 C CD1 . TYR A 245 ? 0.1041 0.2552 0.1696 -0.0014 -0.0394 0.0427  470  TYR A CD1 
1954 C CD2 . TYR A 245 ? 0.2192 0.3864 0.2895 -0.0096 -0.0498 0.0435  470  TYR A CD2 
1955 C CE1 . TYR A 245 ? 0.1695 0.3101 0.2252 -0.0051 -0.0405 0.0384  470  TYR A CE1 
1956 C CE2 . TYR A 245 ? 0.1735 0.3291 0.2332 -0.0132 -0.0507 0.0390  470  TYR A CE2 
1957 C CZ  . TYR A 245 ? 0.1468 0.2895 0.1997 -0.0107 -0.0459 0.0366  470  TYR A CZ  
1958 O OH  . TYR A 245 ? 0.1471 0.2793 0.1904 -0.0139 -0.0465 0.0324  470  TYR A OH  
1959 N N   . ARG A 246 ? 0.1697 0.3386 0.2414 0.0137  -0.0440 0.0560  471  ARG A N   
1960 C CA  . ARG A 246 ? 0.2342 0.4054 0.3017 0.0160  -0.0482 0.0590  471  ARG A CA  
1961 C C   . ARG A 246 ? 0.2589 0.4184 0.3136 0.0125  -0.0497 0.0551  471  ARG A C   
1962 O O   . ARG A 246 ? 0.2270 0.3738 0.2756 0.0124  -0.0453 0.0517  471  ARG A O   
1963 C CB  . ARG A 246 ? 0.2193 0.3891 0.2885 0.0248  -0.0444 0.0638  471  ARG A CB  
1964 C CG  . ARG A 246 ? 0.3981 0.5715 0.4640 0.0284  -0.0484 0.0682  471  ARG A CG  
1965 C CD  . ARG A 246 ? 0.5692 0.7369 0.6349 0.0370  -0.0434 0.0724  471  ARG A CD  
1966 N NE  . ARG A 246 ? 0.4932 0.6678 0.5700 0.0420  -0.0396 0.0753  471  ARG A NE  
1967 N N   . ASN A 247 ? 0.2404 0.4045 0.2910 0.0096  -0.0558 0.0554  472  ASN A N   
1968 C CA  . ASN A 247 ? 0.2713 0.4248 0.3092 0.0075  -0.0570 0.0525  472  ASN A CA  
1969 C C   . ASN A 247 ? 0.3249 0.4738 0.3582 0.0142  -0.0549 0.0565  472  ASN A C   
1970 O O   . ASN A 247 ? 0.3290 0.4861 0.3636 0.0172  -0.0586 0.0612  472  ASN A O   
1971 C CB  . ASN A 247 ? 0.4368 0.5963 0.4708 0.0019  -0.0641 0.0511  472  ASN A CB  
1972 C CG  . ASN A 247 ? 0.6088 0.7571 0.6292 -0.0004 -0.0648 0.0476  472  ASN A CG  
1973 O OD1 . ASN A 247 ? 0.5059 0.6478 0.5198 0.0039  -0.0627 0.0495  472  ASN A OD1 
1974 N ND2 . ASN A 247 ? 0.4803 0.6257 0.4962 -0.0071 -0.0673 0.0426  472  ASN A ND2 
1975 N N   . GLN A 248 ? 0.4091 0.5450 0.4373 0.0164  -0.0492 0.0548  473  GLN A N   
1976 C CA  . GLN A 248 ? 0.5314 0.6619 0.5563 0.0228  -0.0463 0.0588  473  GLN A CA  
1977 C C   . GLN A 248 ? 0.5830 0.7114 0.5980 0.0226  -0.0498 0.0601  473  GLN A C   
1978 O O   . GLN A 248 ? 0.5745 0.7035 0.5880 0.0280  -0.0497 0.0652  473  GLN A O   
1979 C CB  . GLN A 248 ? 0.4580 0.5752 0.4800 0.0243  -0.0393 0.0563  473  GLN A CB  
1980 C CG  . GLN A 248 ? 0.5844 0.7031 0.6154 0.0261  -0.0352 0.0560  473  GLN A CG  
1981 C CD  . GLN A 248 ? 0.7256 0.8312 0.7531 0.0279  -0.0287 0.0538  473  GLN A CD  
1982 O OE1 . GLN A 248 ? 0.7021 0.7979 0.7214 0.0260  -0.0274 0.0514  473  GLN A OE1 
1983 N NE2 . GLN A 248 ? 0.5699 0.6756 0.6038 0.0314  -0.0244 0.0547  473  GLN A NE2 
1984 N N   . ALA A 249 ? 0.3385 0.4640 0.3461 0.0168  -0.0525 0.0557  474  ALA A N   
1985 C CA  . ALA A 249 ? 0.3866 0.5107 0.3841 0.0164  -0.0560 0.0568  474  ALA A CA  
1986 C C   . ALA A 249 ? 0.5206 0.6583 0.5210 0.0175  -0.0625 0.0613  474  ALA A C   
1987 O O   . ALA A 249 ? 0.5478 0.6867 0.5444 0.0219  -0.0637 0.0662  474  ALA A O   
1988 C CB  . ALA A 249 ? 0.4721 0.5903 0.4612 0.0100  -0.0572 0.0507  474  ALA A CB  
1989 N N   . THR A 250 ? 0.5112 0.6592 0.5186 0.0134  -0.0667 0.0599  475  THR A N   
1990 C CA  . THR A 250 ? 0.5815 0.7381 0.5917 0.0127  -0.0715 0.0612  475  THR A CA  
1991 C C   . THR A 250 ? 0.4645 0.6305 0.4868 0.0177  -0.0707 0.0662  475  THR A C   
1992 O O   . THR A 250 ? 0.6641 0.8381 0.6893 0.0179  -0.0746 0.0681  475  THR A O   
1993 C CB  . THR A 250 ? 0.6563 0.8158 0.6668 0.0048  -0.0755 0.0557  475  THR A CB  
1994 O OG1 . THR A 250 ? 0.5468 0.7116 0.5686 0.0031  -0.0739 0.0548  475  THR A OG1 
1995 C CG2 . THR A 250 ? 0.6051 0.7544 0.6042 0.0000  -0.0755 0.0503  475  THR A CG2 
1996 N N   . GLY A 251 ? 0.6846 0.8500 0.7140 0.0218  -0.0656 0.0681  476  GLY A N   
1997 C CA  . GLY A 251 ? 0.7316 0.9050 0.7724 0.0272  -0.0638 0.0726  476  GLY A CA  
1998 C C   . GLY A 251 ? 0.7036 0.8876 0.7553 0.0235  -0.0654 0.0711  476  GLY A C   
1999 O O   . GLY A 251 ? 0.6691 0.8592 0.7310 0.0277  -0.0626 0.0743  476  GLY A O   
2000 N N   . GLN A 252 ? 0.4635 0.6492 0.5131 0.0157  -0.0695 0.0665  477  GLN A N   
2001 C CA  . GLN A 252 ? 0.4161 0.6116 0.4753 0.0116  -0.0715 0.0653  477  GLN A CA  
2002 C C   . GLN A 252 ? 0.5526 0.7494 0.6207 0.0122  -0.0665 0.0649  477  GLN A C   
2003 O O   . GLN A 252 ? 0.3304 0.5196 0.3950 0.0099  -0.0640 0.0616  477  GLN A O   
2004 C CB  . GLN A 252 ? 0.5266 0.7203 0.5797 0.0030  -0.0762 0.0598  477  GLN A CB  
2005 C CG  . GLN A 252 ? 0.5918 0.7960 0.6529 -0.0017 -0.0799 0.0591  477  GLN A CG  
2006 C CD  . GLN A 252 ? 0.7378 0.9379 0.7931 -0.0104 -0.0833 0.0530  477  GLN A CD  
2007 O OE1 . GLN A 252 ? 0.6338 0.8232 0.6799 -0.0128 -0.0823 0.0492  477  GLN A OE1 
2008 N NE2 . GLN A 252 ? 0.6519 0.8602 0.7123 -0.0150 -0.0872 0.0522  477  GLN A NE2 
2009 N N   . LEU A 253 ? 0.4816 0.6880 0.5609 0.0155  -0.0650 0.0684  478  LEU A N   
2010 C CA  . LEU A 253 ? 0.2385 0.4478 0.3268 0.0150  -0.0607 0.0677  478  LEU A CA  
2011 C C   . LEU A 253 ? 0.3359 0.5480 0.4258 0.0062  -0.0637 0.0634  478  LEU A C   
2012 O O   . LEU A 253 ? 0.3505 0.5705 0.4435 0.0028  -0.0680 0.0636  478  LEU A O   
2013 C CB  . LEU A 253 ? 0.3587 0.5775 0.4581 0.0212  -0.0580 0.0727  478  LEU A CB  
2014 C CG  . LEU A 253 ? 0.3653 0.5876 0.4741 0.0219  -0.0527 0.0727  478  LEU A CG  
2015 N N   . LEU A 254 ? 0.2128 0.4182 0.3003 0.0023  -0.0614 0.0595  479  LEU A N   
2016 C CA  . LEU A 254 ? 0.2395 0.4451 0.3271 -0.0062 -0.0639 0.0552  479  LEU A CA  
2017 C C   . LEU A 254 ? 0.2462 0.4602 0.3454 -0.0075 -0.0614 0.0563  479  LEU A C   
2018 O O   . LEU A 254 ? 0.2852 0.5061 0.3888 -0.0123 -0.0646 0.0558  479  LEU A O   
2019 C CB  . LEU A 254 ? 0.2513 0.4451 0.3302 -0.0099 -0.0629 0.0506  479  LEU A CB  
2020 C CG  . LEU A 254 ? 0.3345 0.5198 0.4010 -0.0096 -0.0654 0.0490  479  LEU A CG  
2021 C CD1 . LEU A 254 ? 0.2291 0.4031 0.2876 -0.0127 -0.0638 0.0447  479  LEU A CD1 
2022 C CD2 . LEU A 254 ? 0.3923 0.5799 0.4546 -0.0139 -0.0714 0.0475  479  LEU A CD2 
2023 N N   . PHE A 255 ? 0.2066 0.4202 0.3108 -0.0034 -0.0556 0.0578  480  PHE A N   
2024 C CA  . PHE A 255 ? 0.1569 0.3788 0.2720 -0.0038 -0.0526 0.0593  480  PHE A CA  
2025 C C   . PHE A 255 ? 0.1536 0.3747 0.2727 0.0036  -0.0459 0.0618  480  PHE A C   
2026 O O   . PHE A 255 ? 0.1922 0.4053 0.3053 0.0077  -0.0437 0.0617  480  PHE A O   
2027 C CB  . PHE A 255 ? 0.1609 0.3804 0.2760 -0.0119 -0.0529 0.0553  480  PHE A CB  
2028 C CG  . PHE A 255 ? 0.1482 0.3561 0.2558 -0.0136 -0.0507 0.0518  480  PHE A CG  
2029 C CD1 . PHE A 255 ? 0.1575 0.3633 0.2678 -0.0103 -0.0447 0.0524  480  PHE A CD1 
2030 C CD2 . PHE A 255 ? 0.2351 0.4343 0.3328 -0.0187 -0.0544 0.0478  480  PHE A CD2 
2031 C CE1 . PHE A 255 ? 0.1539 0.3488 0.2570 -0.0119 -0.0428 0.0490  480  PHE A CE1 
2032 C CE2 . PHE A 255 ? 0.2595 0.4484 0.3505 -0.0202 -0.0524 0.0446  480  PHE A CE2 
2033 C CZ  . PHE A 255 ? 0.2569 0.4428 0.3502 -0.0168 -0.0465 0.0451  480  PHE A CZ  
2034 N N   . GLU A 256 ? 0.1498 0.3791 0.2789 0.0052  -0.0424 0.0641  481  GLU A N   
2035 C CA  . GLU A 256 ? 0.1812 0.4090 0.3138 0.0110  -0.0353 0.0655  481  GLU A CA  
2036 C C   . GLU A 256 ? 0.1631 0.3900 0.2980 0.0058  -0.0324 0.0630  481  GLU A C   
2037 O O   . GLU A 256 ? 0.1245 0.3546 0.2611 -0.0014 -0.0355 0.0613  481  GLU A O   
2038 C CB  . GLU A 256 ? 0.1613 0.3979 0.3027 0.0182  -0.0322 0.0703  481  GLU A CB  
2039 C CG  . GLU A 256 ? 0.3722 0.6212 0.5232 0.0150  -0.0336 0.0719  481  GLU A CG  
2040 C CD  . GLU A 256 ? 0.4112 0.6685 0.5709 0.0227  -0.0298 0.0766  481  GLU A CD  
2041 O OE1 . GLU A 256 ? 0.2600 0.5138 0.4175 0.0304  -0.0279 0.0790  481  GLU A OE1 
2042 O OE2 . GLU A 256 ? 0.1644 0.4311 0.3330 0.0213  -0.0283 0.0780  481  GLU A OE2 
2043 N N   . CYS A 257 ? 0.1177 0.3396 0.2520 0.0094  -0.0265 0.0625  482  CYS A N   
2044 C CA  . CYS A 257 ? 0.1042 0.3239 0.2391 0.0046  -0.0235 0.0601  482  CYS A CA  
2045 C C   . CYS A 257 ? 0.1336 0.3506 0.2701 0.0109  -0.0155 0.0609  482  CYS A C   
2046 O O   . CYS A 257 ? 0.1216 0.3361 0.2573 0.0186  -0.0125 0.0626  482  CYS A O   
2047 C CB  . CYS A 257 ? 0.0925 0.2990 0.2161 -0.0010 -0.0258 0.0551  482  CYS A CB  
2048 S SG  . CYS A 257 ? 0.1316 0.3204 0.2418 0.0041  -0.0236 0.0523  482  CYS A SG  
2049 N N   . LYS A 258 ? 0.0932 0.3088 0.2306 0.0077  -0.0118 0.0593  483  LYS A N   
2050 C CA  . LYS A 258 ? 0.1072 0.3181 0.2438 0.0128  -0.0039 0.0591  483  LYS A CA  
2051 C C   . LYS A 258 ? 0.0882 0.2830 0.2130 0.0098  -0.0018 0.0541  483  LYS A C   
2052 O O   . LYS A 258 ? 0.1171 0.3101 0.2399 0.0028  -0.0040 0.0521  483  LYS A O   
2053 C CB  . LYS A 258 ? 0.0883 0.3131 0.2368 0.0125  -0.0005 0.0624  483  LYS A CB  
2054 C CG  . LYS A 258 ? 0.0932 0.3271 0.2495 0.0185  0.0004  0.0664  483  LYS A CG  
2055 C CD  . LYS A 258 ? 0.1266 0.3710 0.2916 0.0149  0.0006  0.0682  483  LYS A CD  
2056 C CE  . LYS A 258 ? 0.1575 0.4009 0.3235 0.0151  0.0077  0.0677  483  LYS A CE  
2057 N NZ  . LYS A 258 ? 0.1596 0.4134 0.3343 0.0115  0.0082  0.0697  483  LYS A NZ  
2058 N N   . LEU A 259 ? 0.0903 0.2735 0.2074 0.0150  0.0024  0.0522  484  LEU A N   
2059 C CA  . LEU A 259 ? 0.0904 0.2595 0.1970 0.0132  0.0052  0.0478  484  LEU A CA  
2060 C C   . LEU A 259 ? 0.1362 0.3061 0.2447 0.0164  0.0124  0.0483  484  LEU A C   
2061 O O   . LEU A 259 ? 0.1091 0.2766 0.2171 0.0230  0.0170  0.0489  484  LEU A O   
2062 C CB  . LEU A 259 ? 0.1127 0.2687 0.2094 0.0161  0.0049  0.0452  484  LEU A CB  
2063 C CG  . LEU A 259 ? 0.1054 0.2472 0.1917 0.0160  0.0086  0.0410  484  LEU A CG  
2064 C CD1 . LEU A 259 ? 0.1287 0.2668 0.2108 0.0091  0.0065  0.0383  484  LEU A CD1 
2065 C CD2 . LEU A 259 ? 0.1066 0.2374 0.1849 0.0187  0.0079  0.0391  484  LEU A CD2 
2066 N N   . TYR A 260 ? 0.1032 0.2766 0.2138 0.0116  0.0135  0.0482  485  TYR A N   
2067 C CA  . TYR A 260 ? 0.1061 0.2811 0.2183 0.0143  0.0203  0.0489  485  TYR A CA  
2068 C C   . TYR A 260 ? 0.0983 0.2583 0.1985 0.0167  0.0244  0.0448  485  TYR A C   
2069 O O   . TYR A 260 ? 0.1284 0.2776 0.2196 0.0139  0.0215  0.0414  485  TYR A O   
2070 C CB  . TYR A 260 ? 0.0926 0.2741 0.2091 0.0081  0.0204  0.0499  485  TYR A CB  
2071 C CG  . TYR A 260 ? 0.1090 0.3076 0.2393 0.0062  0.0184  0.0543  485  TYR A CG  
2072 C CD1 . TYR A 260 ? 0.1249 0.3352 0.2650 0.0113  0.0230  0.0581  485  TYR A CD1 
2073 C CD2 . TYR A 260 ? 0.1046 0.3079 0.2383 -0.0008 0.0119  0.0547  485  TYR A CD2 
2074 C CE1 . TYR A 260 ? 0.1466 0.3734 0.2999 0.0094  0.0209  0.0623  485  TYR A CE1 
2075 C CE2 . TYR A 260 ? 0.0909 0.3106 0.2375 -0.0033 0.0096  0.0586  485  TYR A CE2 
2076 C CZ  . TYR A 260 ? 0.1149 0.3443 0.2699 0.0018  0.0139  0.0619  485  TYR A CZ  
2077 O OH  . TYR A 260 ? 0.1357 0.3752 0.2992 -0.0007 0.0112  0.0643  485  TYR A OH  
2078 N N   . ARG A 261 ? 0.1123 0.2718 0.2124 0.0220  0.0311  0.0452  486  ARG A N   
2079 C CA  . ARG A 261 ? 0.1568 0.3020 0.2452 0.0244  0.0347  0.0412  486  ARG A CA  
2080 C C   . ARG A 261 ? 0.1171 0.2546 0.1970 0.0189  0.0341  0.0380  486  ARG A C   
2081 O O   . ARG A 261 ? 0.1547 0.2800 0.2242 0.0193  0.0348  0.0343  486  ARG A O   
2082 C CB  . ARG A 261 ? 0.2033 0.3489 0.2925 0.0312  0.0422  0.0419  486  ARG A CB  
2083 C CG  . ARG A 261 ? 0.1787 0.3325 0.2725 0.0303  0.0468  0.0437  486  ARG A CG  
2084 C CD  . ARG A 261 ? 0.4774 0.6301 0.5705 0.0376  0.0548  0.0438  486  ARG A CD  
2085 N NE  . ARG A 261 ? 0.3824 0.5193 0.4618 0.0391  0.0578  0.0389  486  ARG A NE  
2086 C CZ  . ARG A 261 ? 0.5864 0.7180 0.6617 0.0452  0.0646  0.0376  486  ARG A CZ  
2087 N NH1 . ARG A 261 ? 0.3843 0.5249 0.4683 0.0513  0.0696  0.0410  486  ARG A NH1 
2088 N NH2 . ARG A 261 ? 0.2723 0.3893 0.3345 0.0453  0.0666  0.0327  486  ARG A NH2 
2089 N N   . SER A 262 ? 0.1030 0.2472 0.1869 0.0137  0.0328  0.0396  487  SER A N   
2090 C CA  . SER A 262 ? 0.1369 0.2736 0.2128 0.0087  0.0320  0.0371  487  SER A CA  
2091 C C   . SER A 262 ? 0.1443 0.2747 0.2158 0.0044  0.0255  0.0350  487  SER A C   
2092 O O   . SER A 262 ? 0.1516 0.2753 0.2163 0.0006  0.0245  0.0330  487  SER A O   
2093 C CB  . SER A 262 ? 0.1698 0.3148 0.2511 0.0050  0.0337  0.0399  487  SER A CB  
2094 O OG  . SER A 262 ? 0.1775 0.3315 0.2677 0.0006  0.0290  0.0424  487  SER A OG  
2095 N N   . GLY A 263 ? 0.1447 0.2772 0.2197 0.0051  0.0214  0.0356  488  GLY A N   
2096 C CA  . GLY A 263 ? 0.1222 0.2476 0.1918 0.0021  0.0161  0.0332  488  GLY A CA  
2097 C C   . GLY A 263 ? 0.1363 0.2667 0.2103 -0.0034 0.0106  0.0342  488  GLY A C   
2098 O O   . GLY A 263 ? 0.1302 0.2542 0.1988 -0.0076 0.0080  0.0322  488  GLY A O   
2099 N N   . PHE A 264 ? 0.1064 0.2481 0.1899 -0.0035 0.0088  0.0374  489  PHE A N   
2100 C CA  . PHE A 264 ? 0.1314 0.2768 0.2179 -0.0088 0.0029  0.0378  489  PHE A CA  
2101 C C   . PHE A 264 ? 0.0996 0.2564 0.1951 -0.0069 0.0005  0.0409  489  PHE A C   
2102 O O   . PHE A 264 ? 0.1127 0.2761 0.2138 -0.0018 0.0039  0.0434  489  PHE A O   
2103 C CB  . PHE A 264 ? 0.0903 0.2385 0.1793 -0.0149 0.0026  0.0385  489  PHE A CB  
2104 C CG  . PHE A 264 ? 0.0874 0.2477 0.1863 -0.0148 0.0059  0.0422  489  PHE A CG  
2105 C CD1 . PHE A 264 ? 0.1232 0.2831 0.2213 -0.0119 0.0122  0.0429  489  PHE A CD1 
2106 C CD2 . PHE A 264 ? 0.1206 0.2930 0.2296 -0.0181 0.0027  0.0450  489  PHE A CD2 
2107 C CE1 . PHE A 264 ? 0.1696 0.3412 0.2770 -0.0118 0.0157  0.0465  489  PHE A CE1 
2108 C CE2 . PHE A 264 ? 0.1171 0.3020 0.2363 -0.0183 0.0058  0.0487  489  PHE A CE2 
2109 C CZ  . PHE A 264 ? 0.1768 0.3612 0.2953 -0.0150 0.0126  0.0496  489  PHE A CZ  
2110 N N   . VAL A 265 ? 0.1190 0.2778 0.2152 -0.0109 -0.0055 0.0407  490  VAL A N   
2111 C CA  . VAL A 265 ? 0.0847 0.2536 0.1878 -0.0095 -0.0091 0.0433  490  VAL A CA  
2112 C C   . VAL A 265 ? 0.1089 0.2890 0.2204 -0.0157 -0.0128 0.0453  490  VAL A C   
2113 O O   . VAL A 265 ? 0.1201 0.2961 0.2288 -0.0220 -0.0148 0.0433  490  VAL A O   
2114 C CB  . VAL A 265 ? 0.0987 0.2603 0.1945 -0.0090 -0.0134 0.0413  490  VAL A CB  
2115 C CG1 . VAL A 265 ? 0.1441 0.3162 0.2462 -0.0067 -0.0170 0.0445  490  VAL A CG1 
2116 C CG2 . VAL A 265 ? 0.1315 0.2809 0.2186 -0.0042 -0.0098 0.0390  490  VAL A CG2 
2117 N N   . VAL A 266 ? 0.0993 0.2936 0.2213 -0.0139 -0.0139 0.0492  491  VAL A N   
2118 C CA  . VAL A 266 ? 0.0850 0.2917 0.2161 -0.0200 -0.0179 0.0512  491  VAL A CA  
2119 C C   . VAL A 266 ? 0.1055 0.3200 0.2402 -0.0185 -0.0230 0.0530  491  VAL A C   
2120 O O   . VAL A 266 ? 0.1195 0.3361 0.2550 -0.0115 -0.0220 0.0549  491  VAL A O   
2121 C CB  . VAL A 266 ? 0.0999 0.3164 0.2406 -0.0202 -0.0133 0.0542  491  VAL A CB  
2122 C CG1 . VAL A 266 ? 0.1053 0.3131 0.2409 -0.0220 -0.0083 0.0525  491  VAL A CG1 
2123 C CG2 . VAL A 266 ? 0.1118 0.3357 0.2586 -0.0119 -0.0093 0.0575  491  VAL A CG2 
2124 N N   . VAL A 267 ? 0.1125 0.3291 0.2479 -0.0248 -0.0281 0.0521  492  VAL A N   
2125 C CA  . VAL A 267 ? 0.1159 0.3397 0.2543 -0.0242 -0.0329 0.0536  492  VAL A CA  
2126 C C   . VAL A 267 ? 0.1406 0.3739 0.2877 -0.0284 -0.0334 0.0551  492  VAL A C   
2127 O O   . VAL A 267 ? 0.1333 0.3655 0.2822 -0.0331 -0.0312 0.0544  492  VAL A O   
2128 C CB  . VAL A 267 ? 0.1164 0.3335 0.2461 -0.0280 -0.0393 0.0505  492  VAL A CB  
2129 C CG1 . VAL A 267 ? 0.1096 0.3190 0.2316 -0.0231 -0.0389 0.0496  492  VAL A CG1 
2130 C CG2 . VAL A 267 ? 0.1555 0.3656 0.2809 -0.0365 -0.0411 0.0468  492  VAL A CG2 
2131 N N   . ASN A 268 ? 0.1180 0.3606 0.2704 -0.0270 -0.0365 0.0574  493  ASN A N   
2132 C CA  . ASN A 268 ? 0.1390 0.3925 0.3008 -0.0304 -0.0374 0.0593  493  ASN A CA  
2133 C C   . ASN A 268 ? 0.1246 0.3798 0.2847 -0.0365 -0.0447 0.0576  493  ASN A C   
2134 O O   . ASN A 268 ? 0.2061 0.4570 0.3593 -0.0356 -0.0489 0.0562  493  ASN A O   
2135 C CB  . ASN A 268 ? 0.1100 0.3749 0.2810 -0.0231 -0.0344 0.0639  493  ASN A CB  
2136 C CG  . ASN A 268 ? 0.1862 0.4633 0.3680 -0.0262 -0.0343 0.0662  493  ASN A CG  
2137 O OD1 . ASN A 268 ? 0.2653 0.5418 0.4486 -0.0331 -0.0340 0.0648  493  ASN A OD1 
2138 N ND2 . ASN A 268 ? 0.2035 0.4917 0.3930 -0.0212 -0.0344 0.0699  493  ASN A ND2 
2139 N N   . GLY A 269 ? 0.1975 0.4588 0.3636 -0.0428 -0.0460 0.0576  494  GLY A N   
2140 C CA  . GLY A 269 ? 0.2241 0.4888 0.3901 -0.0484 -0.0528 0.0562  494  GLY A CA  
2141 C C   . GLY A 269 ? 0.3159 0.5685 0.4716 -0.0553 -0.0566 0.0513  494  GLY A C   
2142 O O   . GLY A 269 ? 0.2374 0.4901 0.3895 -0.0584 -0.0624 0.0495  494  GLY A O   
2143 N N   . VAL A 270 ? 0.2057 0.4476 0.3562 -0.0575 -0.0533 0.0490  495  VAL A N   
2144 C CA  . VAL A 270 ? 0.1732 0.4025 0.3138 -0.0638 -0.0562 0.0442  495  VAL A CA  
2145 C C   . VAL A 270 ? 0.2282 0.4574 0.3725 -0.0717 -0.0560 0.0432  495  VAL A C   
2146 O O   . VAL A 270 ? 0.2587 0.4883 0.4074 -0.0720 -0.0509 0.0448  495  VAL A O   
2147 C CB  . VAL A 270 ? 0.1986 0.4158 0.3307 -0.0609 -0.0530 0.0424  495  VAL A CB  
2148 C CG1 . VAL A 270 ? 0.2568 0.4610 0.3797 -0.0675 -0.0550 0.0378  495  VAL A CG1 
2149 C CG2 . VAL A 270 ? 0.2595 0.4758 0.3869 -0.0540 -0.0540 0.0430  495  VAL A CG2 
2150 N N   . ASN A 271 ? 0.2771 0.5055 0.4194 -0.0782 -0.0613 0.0406  496  ASN A N   
2151 C CA  . ASN A 271 ? 0.3201 0.5478 0.4656 -0.0863 -0.0615 0.0394  496  ASN A CA  
2152 C C   . ASN A 271 ? 0.4092 0.6211 0.5440 -0.0922 -0.0630 0.0346  496  ASN A C   
2153 O O   . ASN A 271 ? 0.3414 0.5493 0.4776 -0.0981 -0.0615 0.0337  496  ASN A O   
2154 C CB  . ASN A 271 ? 0.3681 0.6074 0.5206 -0.0902 -0.0663 0.0402  496  ASN A CB  
2155 C CG  . ASN A 271 ? 0.5332 0.7887 0.6971 -0.0845 -0.0650 0.0452  496  ASN A CG  
2156 O OD1 . ASN A 271 ? 0.5765 0.8397 0.7418 -0.0819 -0.0690 0.0463  496  ASN A OD1 
2157 N ND2 . ASN A 271 ? 0.4481 0.7086 0.6197 -0.0824 -0.0591 0.0484  496  ASN A ND2 
2158 N N   . VAL A 272 ? 0.2897 0.4925 0.4139 -0.0904 -0.0656 0.0315  497  VAL A N   
2159 C CA  . VAL A 272 ? 0.3193 0.5063 0.4325 -0.0948 -0.0665 0.0268  497  VAL A CA  
2160 C C   . VAL A 272 ? 0.2297 0.4085 0.3348 -0.0889 -0.0646 0.0259  497  VAL A C   
2161 O O   . VAL A 272 ? 0.2656 0.4506 0.3725 -0.0821 -0.0639 0.0284  497  VAL A O   
2162 C CB  . VAL A 272 ? 0.2800 0.4637 0.3874 -0.1001 -0.0726 0.0228  497  VAL A CB  
2163 C CG1 . VAL A 272 ? 0.3503 0.5424 0.4662 -0.1066 -0.0746 0.0235  497  VAL A CG1 
2164 C CG2 . VAL A 272 ? 0.2787 0.4670 0.3828 -0.0952 -0.0763 0.0229  497  VAL A CG2 
2165 N N   . ARG A 273 ? 0.2240 0.3884 0.3200 -0.0915 -0.0638 0.0224  498  ARG A N   
2166 C CA  . ARG A 273 ? 0.2066 0.3628 0.2946 -0.0865 -0.0622 0.0213  498  ARG A CA  
2167 C C   . ARG A 273 ? 0.3293 0.4873 0.4123 -0.0826 -0.0659 0.0204  498  ARG A C   
2168 O O   . ARG A 273 ? 0.2760 0.4317 0.3541 -0.0860 -0.0703 0.0175  498  ARG A O   
2169 C CB  . ARG A 273 ? 0.2419 0.3822 0.3205 -0.0904 -0.0615 0.0174  498  ARG A CB  
2170 C CG  . ARG A 273 ? 0.2592 0.3915 0.3308 -0.0855 -0.0591 0.0166  498  ARG A CG  
2171 C CD  . ARG A 273 ? 0.2562 0.3728 0.3186 -0.0895 -0.0587 0.0127  498  ARG A CD  
2172 N NE  . ARG A 273 ? 0.2625 0.3719 0.3194 -0.0853 -0.0560 0.0123  498  ARG A NE  
2173 C CZ  . ARG A 273 ? 0.2930 0.3986 0.3425 -0.0815 -0.0574 0.0103  498  ARG A CZ  
2174 N NH1 . ARG A 273 ? 0.3881 0.4964 0.4345 -0.0808 -0.0611 0.0089  498  ARG A NH1 
2175 N NH2 . ARG A 273 ? 0.3061 0.4024 0.3499 -0.0763 -0.0534 0.0095  498  ARG A NH2 
2176 N N   . THR A 274 ? 0.2213 0.3833 0.3054 -0.0755 -0.0639 0.0230  499  THR A N   
2177 C CA  . THR A 274 ? 0.2000 0.3660 0.2813 -0.0709 -0.0668 0.0235  499  THR A CA  
2178 C C   . THR A 274 ? 0.2365 0.3951 0.3106 -0.0656 -0.0648 0.0229  499  THR A C   
2179 O O   . THR A 274 ? 0.1837 0.3433 0.2612 -0.0618 -0.0605 0.0251  499  THR A O   
2180 C CB  . THR A 274 ? 0.2202 0.4013 0.3122 -0.0668 -0.0666 0.0284  499  THR A CB  
2181 O OG1 . THR A 274 ? 0.2453 0.4341 0.3445 -0.0720 -0.0687 0.0289  499  THR A OG1 
2182 C CG2 . THR A 274 ? 0.2528 0.4375 0.3417 -0.0617 -0.0694 0.0294  499  THR A CG2 
2183 N N   . GLU A 275 ? 0.2556 0.4071 0.3196 -0.0655 -0.0677 0.0198  500  GLU A N   
2184 C CA  . GLU A 275 ? 0.3369 0.4816 0.3935 -0.0607 -0.0661 0.0192  500  GLU A CA  
2185 C C   . GLU A 275 ? 0.2121 0.3639 0.2693 -0.0547 -0.0674 0.0221  500  GLU A C   
2186 O O   . GLU A 275 ? 0.2190 0.3776 0.2780 -0.0553 -0.0710 0.0231  500  GLU A O   
2187 C CB  . GLU A 275 ? 0.2634 0.3948 0.3077 -0.0639 -0.0678 0.0141  500  GLU A CB  
2188 C CG  . GLU A 275 ? 0.4454 0.5675 0.4878 -0.0689 -0.0660 0.0113  500  GLU A CG  
2189 C CD  . GLU A 275 ? 0.8255 0.9339 0.8555 -0.0707 -0.0668 0.0064  500  GLU A CD  
2190 O OE1 . GLU A 275 ? 0.8450 0.9514 0.8677 -0.0686 -0.0690 0.0050  500  GLU A OE1 
2191 O OE2 . GLU A 275 ? 0.9186 1.0178 0.9460 -0.0739 -0.0650 0.0042  500  GLU A OE2 
2192 N N   . PHE A 276 ? 0.2108 0.3609 0.2664 -0.0491 -0.0645 0.0236  501  PHE A N   
2193 C CA  . PHE A 276 ? 0.2098 0.3657 0.2662 -0.0427 -0.0649 0.0270  501  PHE A CA  
2194 C C   . PHE A 276 ? 0.2173 0.3644 0.2629 -0.0401 -0.0650 0.0253  501  PHE A C   
2195 O O   . PHE A 276 ? 0.1931 0.3288 0.2320 -0.0413 -0.0626 0.0218  501  PHE A O   
2196 C CB  . PHE A 276 ? 0.2150 0.3785 0.2811 -0.0375 -0.0607 0.0314  501  PHE A CB  
2197 C CG  . PHE A 276 ? 0.2043 0.3775 0.2814 -0.0394 -0.0600 0.0336  501  PHE A CG  
2198 C CD1 . PHE A 276 ? 0.1826 0.3660 0.2655 -0.0386 -0.0626 0.0362  501  PHE A CD1 
2199 C CD2 . PHE A 276 ? 0.1549 0.3271 0.2364 -0.0421 -0.0566 0.0331  501  PHE A CD2 
2200 C CE1 . PHE A 276 ? 0.1984 0.3910 0.2915 -0.0404 -0.0619 0.0383  501  PHE A CE1 
2201 C CE2 . PHE A 276 ? 0.1484 0.3295 0.2398 -0.0440 -0.0556 0.0353  501  PHE A CE2 
2202 C CZ  . PHE A 276 ? 0.1558 0.3473 0.2532 -0.0431 -0.0582 0.0378  501  PHE A CZ  
2203 N N   . PRO A 277 ? 0.1932 0.3432 0.2361 -0.0358 -0.0667 0.0275  502  PRO A N   
2204 C CA  . PRO A 277 ? 0.1725 0.3135 0.2048 -0.0330 -0.0660 0.0261  502  PRO A CA  
2205 C C   . PRO A 277 ? 0.2051 0.3373 0.2366 -0.0283 -0.0593 0.0258  502  PRO A C   
2206 O O   . PRO A 277 ? 0.1898 0.3263 0.2293 -0.0250 -0.0559 0.0286  502  PRO A O   
2207 C CB  . PRO A 277 ? 0.1975 0.3453 0.2295 -0.0286 -0.0686 0.0299  502  PRO A CB  
2208 C CG  . PRO A 277 ? 0.2322 0.3892 0.2711 -0.0312 -0.0718 0.0310  502  PRO A CG  
2209 C CD  . PRO A 277 ? 0.2025 0.3630 0.2509 -0.0338 -0.0694 0.0309  502  PRO A CD  
2210 N N   . MET A 278 ? 0.1951 0.3152 0.2169 -0.0279 -0.0573 0.0225  503  MET A N   
2211 C CA  . MET A 278 ? 0.2011 0.3125 0.2214 -0.0244 -0.0514 0.0217  503  MET A CA  
2212 C C   . MET A 278 ? 0.1718 0.2811 0.1893 -0.0184 -0.0491 0.0241  503  MET A C   
2213 O O   . MET A 278 ? 0.1853 0.2884 0.2025 -0.0153 -0.0443 0.0238  503  MET A O   
2214 C CB  . MET A 278 ? 0.2058 0.3057 0.2182 -0.0273 -0.0502 0.0169  503  MET A CB  
2215 C CG  . MET A 278 ? 0.2253 0.3244 0.2403 -0.0327 -0.0510 0.0145  503  MET A CG  
2216 S SD  . MET A 278 ? 0.1990 0.2991 0.2224 -0.0312 -0.0461 0.0160  503  MET A SD  
2217 C CE  . MET A 278 ? 0.1827 0.2708 0.1992 -0.0275 -0.0412 0.0139  503  MET A CE  
2218 N N   A SER A 279 ? 0.2022 0.3160 0.2173 -0.0167 -0.0523 0.0265  504  SER A N   
2219 N N   B SER A 279 ? 0.2028 0.3167 0.2180 -0.0168 -0.0524 0.0265  504  SER A N   
2220 C CA  A SER A 279 ? 0.2490 0.3593 0.2602 -0.0113 -0.0500 0.0289  504  SER A CA  
2221 C CA  B SER A 279 ? 0.2496 0.3604 0.2609 -0.0114 -0.0503 0.0290  504  SER A CA  
2222 C C   A SER A 279 ? 0.2498 0.3673 0.2691 -0.0061 -0.0486 0.0339  504  SER A C   
2223 C C   B SER A 279 ? 0.2539 0.3725 0.2734 -0.0063 -0.0492 0.0341  504  SER A C   
2224 O O   A SER A 279 ? 0.3359 0.4522 0.3525 -0.0015 -0.0477 0.0369  504  SER A O   
2225 O O   B SER A 279 ? 0.3072 0.4264 0.3243 -0.0020 -0.0494 0.0375  504  SER A O   
2226 C CB  A SER A 279 ? 0.2784 0.3881 0.2810 -0.0118 -0.0539 0.0290  504  SER A CB  
2227 C CB  B SER A 279 ? 0.2772 0.3873 0.2797 -0.0121 -0.0542 0.0289  504  SER A CB  
2228 O OG  A SER A 279 ? 0.2625 0.3832 0.2684 -0.0138 -0.0596 0.0310  504  SER A OG  
2229 O OG  B SER A 279 ? 0.2439 0.3461 0.2384 -0.0164 -0.0547 0.0240  504  SER A OG  
2230 N N   . GLY A 280 ? 0.1912 0.3157 0.2200 -0.0064 -0.0479 0.0351  505  GLY A N   
2231 C CA  . GLY A 280 ? 0.1775 0.3089 0.2143 -0.0011 -0.0460 0.0397  505  GLY A CA  
2232 C C   . GLY A 280 ? 0.1632 0.2871 0.2011 0.0022  -0.0395 0.0390  505  GLY A C   
2233 O O   . GLY A 280 ? 0.1922 0.3077 0.2264 -0.0002 -0.0370 0.0352  505  GLY A O   
2234 N N   . VAL A 281 ? 0.1400 0.2672 0.1831 0.0080  -0.0368 0.0429  506  VAL A N   
2235 C CA  . VAL A 281 ? 0.1620 0.2829 0.2065 0.0115  -0.0306 0.0425  506  VAL A CA  
2236 C C   . VAL A 281 ? 0.1422 0.2729 0.1973 0.0140  -0.0291 0.0454  506  VAL A C   
2237 O O   . VAL A 281 ? 0.2121 0.3534 0.2732 0.0164  -0.0317 0.0496  506  VAL A O   
2238 C CB  . VAL A 281 ? 0.2082 0.3209 0.2476 0.0167  -0.0276 0.0442  506  VAL A CB  
2239 C CG1 . VAL A 281 ? 0.1895 0.2954 0.2301 0.0199  -0.0213 0.0435  506  VAL A CG1 
2240 C CG2 . VAL A 281 ? 0.1733 0.2771 0.2027 0.0141  -0.0287 0.0416  506  VAL A CG2 
2241 N N   . PHE A 282 ? 0.1566 0.2843 0.2139 0.0135  -0.0248 0.0433  507  PHE A N   
2242 C CA  . PHE A 282 ? 0.1539 0.2893 0.2203 0.0166  -0.0219 0.0459  507  PHE A CA  
2243 C C   . PHE A 282 ? 0.1860 0.3166 0.2523 0.0238  -0.0168 0.0480  507  PHE A C   
2244 O O   . PHE A 282 ? 0.2174 0.3358 0.2768 0.0247  -0.0133 0.0455  507  PHE A O   
2245 C CB  . PHE A 282 ? 0.1322 0.2657 0.1998 0.0129  -0.0192 0.0427  507  PHE A CB  
2246 C CG  . PHE A 282 ? 0.1219 0.2604 0.1910 0.0060  -0.0234 0.0410  507  PHE A CG  
2247 C CD1 . PHE A 282 ? 0.1521 0.2825 0.2134 0.0013  -0.0255 0.0371  507  PHE A CD1 
2248 C CD2 . PHE A 282 ? 0.1495 0.3007 0.2282 0.0043  -0.0249 0.0434  507  PHE A CD2 
2249 C CE1 . PHE A 282 ? 0.1602 0.2938 0.2225 -0.0050 -0.0290 0.0355  507  PHE A CE1 
2250 C CE2 . PHE A 282 ? 0.1203 0.2752 0.2003 -0.0025 -0.0286 0.0418  507  PHE A CE2 
2251 C CZ  . PHE A 282 ? 0.1149 0.2603 0.1863 -0.0071 -0.0306 0.0377  507  PHE A CZ  
2252 N N   A GLU A 283 ? 0.1660 0.3061 0.2401 0.0288  -0.0165 0.0527  508  GLU A N   
2253 N N   B GLU A 283 ? 0.1660 0.3061 0.2401 0.0288  -0.0165 0.0527  508  GLU A N   
2254 C CA  A GLU A 283 ? 0.1630 0.2989 0.2376 0.0364  -0.0117 0.0553  508  GLU A CA  
2255 C CA  B GLU A 283 ? 0.1631 0.2989 0.2377 0.0364  -0.0117 0.0553  508  GLU A CA  
2256 C C   A GLU A 283 ? 0.2469 0.3907 0.3309 0.0401  -0.0077 0.0575  508  GLU A C   
2257 C C   B GLU A 283 ? 0.2468 0.3906 0.3308 0.0401  -0.0077 0.0575  508  GLU A C   
2258 O O   A GLU A 283 ? 0.1825 0.3406 0.2757 0.0390  -0.0104 0.0601  508  GLU A O   
2259 O O   B GLU A 283 ? 0.1825 0.3406 0.2756 0.0390  -0.0104 0.0601  508  GLU A O   
2260 C CB  A GLU A 283 ? 0.2213 0.3603 0.2958 0.0407  -0.0147 0.0600  508  GLU A CB  
2261 C CB  B GLU A 283 ? 0.2212 0.3602 0.2957 0.0407  -0.0147 0.0600  508  GLU A CB  
2262 N N   . PHE A 284 ? 0.1882 0.3231 0.2700 0.0442  -0.0012 0.0563  509  PHE A N   
2263 C CA  . PHE A 284 ? 0.1485 0.2897 0.2382 0.0486  0.0036  0.0582  509  PHE A CA  
2264 C C   . PHE A 284 ? 0.1781 0.3293 0.2760 0.0557  0.0033  0.0644  509  PHE A C   
2265 O O   . PHE A 284 ? 0.2268 0.3732 0.3213 0.0598  0.0026  0.0667  509  PHE A O   
2266 C CB  . PHE A 284 ? 0.2248 0.3522 0.3082 0.0514  0.0106  0.0549  509  PHE A CB  
2267 C CG  . PHE A 284 ? 0.2250 0.3567 0.3149 0.0568  0.0165  0.0566  509  PHE A CG  
2268 C CD1 . PHE A 284 ? 0.1657 0.3074 0.2622 0.0542  0.0174  0.0564  509  PHE A CD1 
2269 C CD2 . PHE A 284 ? 0.2795 0.4045 0.3684 0.0646  0.0217  0.0583  509  PHE A CD2 
2270 C CE1 . PHE A 284 ? 0.2096 0.3554 0.3118 0.0594  0.0234  0.0579  509  PHE A CE1 
2271 C CE2 . PHE A 284 ? 0.2552 0.3836 0.3496 0.0701  0.0278  0.0596  509  PHE A CE2 
2272 C CZ  . PHE A 284 ? 0.2346 0.3737 0.3356 0.0675  0.0287  0.0594  509  PHE A CZ  
2273 N N   . VAL A 285 ? 0.1332 0.2988 0.2423 0.0571  0.0039  0.0673  510  VAL A N   
2274 C CA  . VAL A 285 ? 0.1670 0.3440 0.2857 0.0646  0.0044  0.0735  510  VAL A CA  
2275 C C   . VAL A 285 ? 0.2477 0.4235 0.3705 0.0713  0.0126  0.0743  510  VAL A C   
2276 O O   . VAL A 285 ? 0.2554 0.4239 0.3763 0.0790  0.0168  0.0762  510  VAL A O   
2277 C CB  . VAL A 285 ? 0.2112 0.4082 0.3410 0.0613  -0.0017 0.0770  510  VAL A CB  
2278 C CG1 . VAL A 285 ? 0.1971 0.4036 0.3350 0.0681  -0.0013 0.0827  510  VAL A CG1 
2279 C CG2 . VAL A 285 ? 0.1591 0.3560 0.2834 0.0544  -0.0096 0.0756  510  VAL A CG2 
2280 N N   . SER A 286 ? 0.1842 0.3664 0.3121 0.0687  0.0152  0.0729  511  SER A N   
2281 C CA  . SER A 286 ? 0.2102 0.3928 0.3424 0.0750  0.0231  0.0736  511  SER A CA  
2282 C C   . SER A 286 ? 0.1915 0.3775 0.3252 0.0694  0.0253  0.0705  511  SER A C   
2283 O O   . SER A 286 ? 0.1747 0.3644 0.3081 0.0612  0.0204  0.0686  511  SER A O   
2284 C CB  . SER A 286 ? 0.2198 0.4157 0.3631 0.0815  0.0236  0.0797  511  SER A CB  
2285 O OG  . SER A 286 ? 0.2426 0.4529 0.3932 0.0752  0.0178  0.0811  511  SER A OG  
2286 N N   . TRP A 287 ? 0.1461 0.3304 0.2813 0.0741  0.0330  0.0701  512  TRP A N   
2287 C CA  . TRP A 287 ? 0.1960 0.3843 0.3332 0.0702  0.0363  0.0681  512  TRP A CA  
2288 C C   . TRP A 287 ? 0.1318 0.3385 0.2824 0.0703  0.0357  0.0725  512  TRP A C   
2289 O O   . TRP A 287 ? 0.1947 0.4052 0.3500 0.0761  0.0370  0.0758  512  TRP A O   
2290 C CB  . TRP A 287 ? 0.1536 0.3292 0.2836 0.0748  0.0450  0.0648  512  TRP A CB  
2291 C CG  . TRP A 287 ? 0.2081 0.3635 0.3229 0.0724  0.0452  0.0591  512  TRP A CG  
2292 C CD1 . TRP A 287 ? 0.2412 0.3827 0.3484 0.0773  0.0473  0.0581  512  TRP A CD1 
2293 C CD2 . TRP A 287 ? 0.1885 0.3359 0.2944 0.0644  0.0433  0.0541  512  TRP A CD2 
2294 N NE1 . TRP A 287 ? 0.2193 0.3454 0.3139 0.0724  0.0467  0.0525  512  TRP A NE1 
2295 C CE2 . TRP A 287 ? 0.1751 0.3048 0.2688 0.0648  0.0441  0.0500  512  TRP A CE2 
2296 C CE3 . TRP A 287 ? 0.1517 0.3050 0.2589 0.0570  0.0409  0.0528  512  TRP A CE3 
2297 C CZ2 . TRP A 287 ? 0.1821 0.3014 0.2657 0.0583  0.0425  0.0449  512  TRP A CZ2 
2298 C CZ3 . TRP A 287 ? 0.1647 0.3066 0.2612 0.0510  0.0395  0.0478  512  TRP A CZ3 
2299 C CH2 . TRP A 287 ? 0.2418 0.3675 0.3269 0.0517  0.0402  0.0439  512  TRP A CH2 
2300 N N   . VAL A 288 ? 0.1501 0.3643 0.3039 0.0625  0.0332  0.0716  513  VAL A N   
2301 C CA  . VAL A 288 ? 0.1468 0.3746 0.3103 0.0600  0.0317  0.0744  513  VAL A CA  
2302 C C   . VAL A 288 ? 0.2096 0.4393 0.3739 0.0557  0.0358  0.0726  513  VAL A C   
2303 O O   . VAL A 288 ? 0.1673 0.3894 0.3247 0.0524  0.0374  0.0691  513  VAL A O   
2304 C CB  . VAL A 288 ? 0.1841 0.4209 0.3518 0.0535  0.0225  0.0759  513  VAL A CB  
2305 C CG1 . VAL A 288 ? 0.1538 0.3901 0.3211 0.0581  0.0186  0.0784  513  VAL A CG1 
2306 C CG2 . VAL A 288 ? 0.1486 0.3812 0.3108 0.0451  0.0182  0.0724  513  VAL A CG2 
2307 N N   . PRO A 289 ? 0.1700 0.4099 0.3425 0.0559  0.0377  0.0750  514  PRO A N   
2308 C CA  . PRO A 289 ? 0.1732 0.4153 0.3465 0.0517  0.0416  0.0738  514  PRO A CA  
2309 C C   . PRO A 289 ? 0.1404 0.3868 0.3149 0.0414  0.0356  0.0729  514  PRO A C   
2310 O O   . PRO A 289 ? 0.1888 0.4382 0.3647 0.0373  0.0282  0.0733  514  PRO A O   
2311 C CB  . PRO A 289 ? 0.1812 0.4338 0.3640 0.0556  0.0450  0.0773  514  PRO A CB  
2312 C CG  . PRO A 289 ? 0.1851 0.4451 0.3740 0.0578  0.0395  0.0806  514  PRO A CG  
2313 C CD  . PRO A 289 ? 0.1381 0.3874 0.3191 0.0610  0.0374  0.0792  514  PRO A CD  
2314 N N   . ASN A 290 ? 0.1441 0.3897 0.3172 0.0372  0.0392  0.0714  515  ASN A N   
2315 C CA  . ASN A 290 ? 0.1570 0.4045 0.3301 0.0274  0.0346  0.0704  515  ASN A CA  
2316 C C   . ASN A 290 ? 0.1550 0.4143 0.3374 0.0227  0.0283  0.0729  515  ASN A C   
2317 O O   . ASN A 290 ? 0.2095 0.4687 0.3909 0.0153  0.0220  0.0718  515  ASN A O   
2318 C CB  . ASN A 290 ? 0.1770 0.4229 0.3481 0.0246  0.0403  0.0695  515  ASN A CB  
2319 C CG  . ASN A 290 ? 0.2138 0.4474 0.3737 0.0237  0.0430  0.0660  515  ASN A CG  
2320 O OD1 . ASN A 290 ? 0.2616 0.4885 0.4158 0.0228  0.0393  0.0640  515  ASN A OD1 
2321 N ND2 . ASN A 290 ? 0.3770 0.6076 0.5333 0.0239  0.0495  0.0652  515  ASN A ND2 
2322 N N   . PHE A 291 ? 0.1284 0.3977 0.3196 0.0267  0.0301  0.0762  516  PHE A N   
2323 C CA  . PHE A 291 ? 0.1802 0.4618 0.3807 0.0223  0.0247  0.0787  516  PHE A CA  
2324 C C   . PHE A 291 ? 0.1806 0.4662 0.3837 0.0254  0.0191  0.0804  516  PHE A C   
2325 O O   . PHE A 291 ? 0.1760 0.4730 0.3876 0.0235  0.0153  0.0830  516  PHE A O   
2326 C CB  . PHE A 291 ? 0.2423 0.5342 0.4520 0.0239  0.0298  0.0814  516  PHE A CB  
2327 C CG  . PHE A 291 ? 0.3039 0.5937 0.5119 0.0189  0.0341  0.0802  516  PHE A CG  
2328 C CD1 . PHE A 291 ? 0.3719 0.6531 0.5724 0.0120  0.0318  0.0772  516  PHE A CD1 
2329 C CD2 . PHE A 291 ? 0.4898 0.7861 0.7036 0.0211  0.0405  0.0822  516  PHE A CD2 
2330 C CE1 . PHE A 291 ? 0.5251 0.8038 0.7235 0.0075  0.0358  0.0764  516  PHE A CE1 
2331 C CE2 . PHE A 291 ? 0.4826 0.7766 0.6942 0.0165  0.0446  0.0812  516  PHE A CE2 
2332 C CZ  . PHE A 291 ? 0.4980 0.7831 0.7018 0.0097  0.0422  0.0784  516  PHE A CZ  
2333 N N   . PHE A 292 ? 0.1443 0.4207 0.3400 0.0299  0.0185  0.0792  517  PHE A N   
2334 C CA  . PHE A 292 ? 0.1533 0.4319 0.3495 0.0318  0.0124  0.0806  517  PHE A CA  
2335 C C   . PHE A 292 ? 0.1901 0.4712 0.3858 0.0226  0.0041  0.0793  517  PHE A C   
2336 O O   . PHE A 292 ? 0.1484 0.4216 0.3373 0.0168  0.0023  0.0759  517  PHE A O   
2337 C CB  . PHE A 292 ? 0.2103 0.4769 0.3976 0.0376  0.0136  0.0792  517  PHE A CB  
2338 C CG  . PHE A 292 ? 0.1453 0.4131 0.3321 0.0402  0.0080  0.0810  517  PHE A CG  
2339 C CD1 . PHE A 292 ? 0.1994 0.4710 0.3903 0.0484  0.0100  0.0846  517  PHE A CD1 
2340 C CD2 . PHE A 292 ? 0.1565 0.4213 0.3382 0.0344  0.0008  0.0791  517  PHE A CD2 
2341 C CE1 . PHE A 292 ? 0.2201 0.4927 0.4101 0.0508  0.0048  0.0866  517  PHE A CE1 
2342 C CE2 . PHE A 292 ? 0.1820 0.4476 0.3623 0.0367  -0.0043 0.0808  517  PHE A CE2 
2343 C CZ  . PHE A 292 ? 0.2133 0.4829 0.3977 0.0449  -0.0024 0.0847  517  PHE A CZ  
2344 N N   . GLN A 293 ? 0.1799 0.4718 0.3826 0.0212  -0.0009 0.0818  518  GLN A N   
2345 C CA  . GLN A 293 ? 0.1414 0.4361 0.3440 0.0122  -0.0085 0.0803  518  GLN A CA  
2346 C C   . GLN A 293 ? 0.1606 0.4503 0.3564 0.0128  -0.0146 0.0795  518  GLN A C   
2347 O O   . GLN A 293 ? 0.1649 0.4584 0.3627 0.0190  -0.0156 0.0823  518  GLN A O   
2348 C CB  . GLN A 293 ? 0.1228 0.4323 0.3365 0.0095  -0.0108 0.0831  518  GLN A CB  
2349 C CG  . GLN A 293 ? 0.1766 0.4882 0.3899 -0.0005 -0.0180 0.0811  518  GLN A CG  
2350 C CD  . GLN A 293 ? 0.2201 0.5468 0.4449 -0.0033 -0.0202 0.0839  518  GLN A CD  
2351 O OE1 . GLN A 293 ? 0.2408 0.5734 0.4726 -0.0049 -0.0160 0.0850  518  GLN A OE1 
2352 N NE2 . GLN A 293 ? 0.1828 0.5163 0.4098 -0.0036 -0.0266 0.0852  518  GLN A NE2 
2353 N N   . LEU A 294 ? 0.1469 0.4279 0.3345 0.0066  -0.0183 0.0757  519  LEU A N   
2354 C CA  . LEU A 294 ? 0.1245 0.3993 0.3042 0.0066  -0.0238 0.0743  519  LEU A CA  
2355 C C   . LEU A 294 ? 0.1780 0.4608 0.3604 0.0022  -0.0312 0.0750  519  LEU A C   
2356 O O   . LEU A 294 ? 0.1371 0.4273 0.3253 -0.0039 -0.0332 0.0750  519  LEU A O   
2357 C CB  . LEU A 294 ? 0.1056 0.3683 0.2755 0.0013  -0.0249 0.0698  519  LEU A CB  
2358 C CG  . LEU A 294 ? 0.1066 0.3597 0.2715 0.0052  -0.0188 0.0685  519  LEU A CG  
2359 C CD1 . LEU A 294 ? 0.1315 0.3758 0.2895 -0.0020 -0.0200 0.0644  519  LEU A CD1 
2360 C CD2 . LEU A 294 ? 0.1099 0.3574 0.2695 0.0122  -0.0188 0.0692  519  LEU A CD2 
2361 N N   . ALA A 295 ? 0.1565 0.4372 0.3341 0.0052  -0.0352 0.0757  520  ALA A N   
2362 C CA  . ALA A 295 ? 0.1657 0.4513 0.3427 0.0003  -0.0428 0.0753  520  ALA A CA  
2363 C C   . ALA A 295 ? 0.1620 0.4400 0.3319 -0.0090 -0.0465 0.0703  520  ALA A C   
2364 O O   . ALA A 295 ? 0.1552 0.4215 0.3166 -0.0097 -0.0452 0.0674  520  ALA A O   
2365 C CB  . ALA A 295 ? 0.1879 0.4712 0.3595 0.0056  -0.0459 0.0769  520  ALA A CB  
2366 N N   . PRO A 296 ? 0.1437 0.4279 0.3169 -0.0163 -0.0511 0.0693  521  PRO A N   
2367 C CA  . PRO A 296 ? 0.1260 0.4019 0.2921 -0.0251 -0.0545 0.0645  521  PRO A CA  
2368 C C   . PRO A 296 ? 0.1776 0.4435 0.3318 -0.0250 -0.0585 0.0618  521  PRO A C   
2369 O O   . PRO A 296 ? 0.2113 0.4798 0.3638 -0.0205 -0.0611 0.0638  521  PRO A O   
2370 C CB  . PRO A 296 ? 0.2331 0.5191 0.4057 -0.0316 -0.0591 0.0646  521  PRO A CB  
2371 C CG  . PRO A 296 ? 0.2472 0.5472 0.4321 -0.0267 -0.0566 0.0696  521  PRO A CG  
2372 C CD  . PRO A 296 ? 0.2169 0.5157 0.4004 -0.0168 -0.0537 0.0725  521  PRO A CD  
2373 N N   . VAL A 297 ? 0.1944 0.4486 0.3400 -0.0300 -0.0587 0.0574  522  VAL A N   
2374 C CA  . VAL A 297 ? 0.1452 0.3891 0.2789 -0.0305 -0.0622 0.0544  522  VAL A CA  
2375 C C   . VAL A 297 ? 0.2961 0.5439 0.4276 -0.0340 -0.0691 0.0537  522  VAL A C   
2376 O O   . VAL A 297 ? 0.3012 0.5448 0.4248 -0.0319 -0.0720 0.0531  522  VAL A O   
2377 C CB  . VAL A 297 ? 0.1995 0.4305 0.3251 -0.0357 -0.0611 0.0497  522  VAL A CB  
2378 C CG1 . VAL A 297 ? 0.1820 0.4095 0.3095 -0.0322 -0.0545 0.0505  522  VAL A CG1 
2379 C CG2 . VAL A 297 ? 0.3005 0.5318 0.4274 -0.0445 -0.0637 0.0470  522  VAL A CG2 
2380 O OXT . VAL A 297 ? 0.2713 0.5268 0.4087 -0.0391 -0.0717 0.0537  522  VAL A OXT 
2381 N N   . GLU B 1   ? 0.6326 0.5858 0.6217 0.0533  0.0394  0.0427  226  GLU B N   
2382 C CA  . GLU B 1   ? 0.5734 0.5242 0.5619 0.0505  0.0415  0.0367  226  GLU B CA  
2383 C C   . GLU B 1   ? 0.4809 0.4190 0.4625 0.0441  0.0435  0.0317  226  GLU B C   
2384 O O   . GLU B 1   ? 0.5308 0.4688 0.5102 0.0392  0.0412  0.0315  226  GLU B O   
2385 C CB  . GLU B 1   ? 0.6895 0.6550 0.6828 0.0474  0.0371  0.0346  226  GLU B CB  
2386 C CG  . GLU B 1   ? 0.6615 0.6250 0.6530 0.0431  0.0384  0.0283  226  GLU B CG  
2387 C CD  . GLU B 1   ? 0.7438 0.7203 0.7411 0.0439  0.0365  0.0278  226  GLU B CD  
2388 O OE1 . GLU B 1   ? 0.9115 0.8968 0.9147 0.0490  0.0356  0.0323  226  GLU B OE1 
2389 O OE2 . GLU B 1   ? 0.5882 0.5662 0.5842 0.0393  0.0359  0.0232  226  GLU B OE2 
2390 N N   . PRO B 2   ? 0.5470 0.4747 0.5253 0.0442  0.0481  0.0277  227  PRO B N   
2391 C CA  . PRO B 2   ? 0.4639 0.3802 0.4360 0.0375  0.0497  0.0226  227  PRO B CA  
2392 C C   . PRO B 2   ? 0.4816 0.4064 0.4542 0.0301  0.0455  0.0185  227  PRO B C   
2393 O O   . PRO B 2   ? 0.3165 0.2528 0.2931 0.0302  0.0428  0.0175  227  PRO B O   
2394 C CB  . PRO B 2   ? 0.4857 0.3910 0.4542 0.0397  0.0550  0.0190  227  PRO B CB  
2395 C CG  . PRO B 2   ? 0.5487 0.4637 0.5227 0.0462  0.0553  0.0210  227  PRO B CG  
2396 C CD  . PRO B 2   ? 0.5601 0.4855 0.5399 0.0505  0.0522  0.0278  227  PRO B CD  
2397 N N   . PHE B 3   ? 0.3548 0.2741 0.3238 0.0238  0.0450  0.0163  228  PHE B N   
2398 C CA  . PHE B 3   ? 0.3133 0.2409 0.2833 0.0173  0.0409  0.0131  228  PHE B CA  
2399 C C   . PHE B 3   ? 0.3188 0.2482 0.2881 0.0150  0.0409  0.0078  228  PHE B C   
2400 O O   . PHE B 3   ? 0.3211 0.2409 0.2866 0.0156  0.0447  0.0048  228  PHE B O   
2401 C CB  . PHE B 3   ? 0.2925 0.2136 0.2592 0.0111  0.0410  0.0118  228  PHE B CB  
2402 C CG  . PHE B 3   ? 0.2325 0.1631 0.2010 0.0051  0.0369  0.0093  228  PHE B CG  
2403 C CD1 . PHE B 3   ? 0.2380 0.1789 0.2097 0.0055  0.0333  0.0124  228  PHE B CD1 
2404 C CD2 . PHE B 3   ? 0.2622 0.1916 0.2290 -0.0005 0.0365  0.0040  228  PHE B CD2 
2405 C CE1 . PHE B 3   ? 0.2491 0.1983 0.2225 0.0006  0.0299  0.0102  228  PHE B CE1 
2406 C CE2 . PHE B 3   ? 0.2764 0.2147 0.2452 -0.0053 0.0328  0.0021  228  PHE B CE2 
2407 C CZ  . PHE B 3   ? 0.2537 0.2018 0.2260 -0.0045 0.0297  0.0052  228  PHE B CZ  
2408 N N   . SER B 4   ? 0.2677 0.2091 0.2402 0.0124  0.0368  0.0066  229  SER B N   
2409 C CA  . SER B 4   ? 0.2464 0.1906 0.2179 0.0097  0.0362  0.0020  229  SER B CA  
2410 C C   . SER B 4   ? 0.2499 0.2049 0.2241 0.0053  0.0314  0.0012  229  SER B C   
2411 O O   . SER B 4   ? 0.2335 0.1946 0.2107 0.0053  0.0287  0.0042  229  SER B O   
2412 C CB  . SER B 4   ? 0.3070 0.2552 0.2807 0.0150  0.0377  0.0027  229  SER B CB  
2413 O OG  . SER B 4   ? 0.3023 0.2632 0.2819 0.0171  0.0342  0.0062  229  SER B OG  
2414 N N   . LEU B 5   ? 0.2353 0.1924 0.2080 0.0017  0.0304  -0.0030 230  LEU B N   
2415 C CA  . LEU B 5   ? 0.1861 0.1536 0.1615 -0.0015 0.0261  -0.0038 230  LEU B CA  
2416 C C   . LEU B 5   ? 0.2284 0.2017 0.2048 0.0004  0.0258  -0.0046 230  LEU B C   
2417 O O   . LEU B 5   ? 0.2649 0.2328 0.2384 0.0024  0.0291  -0.0064 230  LEU B O   
2418 C CB  . LEU B 5   ? 0.2763 0.2419 0.2490 -0.0079 0.0248  -0.0076 230  LEU B CB  
2419 C CG  . LEU B 5   ? 0.2316 0.1930 0.2040 -0.0106 0.0250  -0.0066 230  LEU B CG  
2420 C CD1 . LEU B 5   ? 0.2604 0.2204 0.2308 -0.0170 0.0240  -0.0105 230  LEU B CD1 
2421 C CD2 . LEU B 5   ? 0.2149 0.1846 0.1915 -0.0095 0.0223  -0.0029 230  LEU B CD2 
2422 N N   . PRO B 6   ? 0.1867 0.1704 0.1670 0.0000  0.0224  -0.0034 231  PRO B N   
2423 C CA  . PRO B 6   ? 0.1748 0.1640 0.1561 0.0015  0.0224  -0.0039 231  PRO B CA  
2424 C C   . PRO B 6   ? 0.2763 0.2620 0.2526 -0.0016 0.0232  -0.0084 231  PRO B C   
2425 O O   . PRO B 6   ? 0.2724 0.2554 0.2460 -0.0061 0.0219  -0.0110 231  PRO B O   
2426 C CB  . PRO B 6   ? 0.2265 0.2259 0.2123 0.0004  0.0182  -0.0020 231  PRO B CB  
2427 C CG  . PRO B 6   ? 0.2371 0.2359 0.2225 -0.0030 0.0160  -0.0023 231  PRO B CG  
2428 C CD  . PRO B 6   ? 0.1743 0.1644 0.1575 -0.0021 0.0187  -0.0018 231  PRO B CD  
2429 N N   A ASN B 7   ? 0.2379 0.2244 0.2130 0.0006  0.0252  -0.0091 232  ASN B N   
2430 N N   B ASN B 7   ? 0.2364 0.2225 0.2116 0.0008  0.0254  -0.0090 232  ASN B N   
2431 C CA  A ASN B 7   ? 0.2118 0.1939 0.1808 -0.0018 0.0265  -0.0134 232  ASN B CA  
2432 C CA  B ASN B 7   ? 0.2152 0.1983 0.1847 -0.0015 0.0264  -0.0131 232  ASN B CA  
2433 C C   A ASN B 7   ? 0.2344 0.2236 0.2030 -0.0054 0.0229  -0.0146 232  ASN B C   
2434 C C   B ASN B 7   ? 0.2182 0.2103 0.1890 -0.0040 0.0228  -0.0131 232  ASN B C   
2435 O O   A ASN B 7   ? 0.2728 0.2611 0.2368 -0.0063 0.0239  -0.0171 232  ASN B O   
2436 O O   B ASN B 7   ? 0.2136 0.2094 0.1839 -0.0027 0.0236  -0.0131 232  ASN B O   
2437 C CB  A ASN B 7   ? 0.2628 0.2419 0.2298 0.0026  0.0310  -0.0137 232  ASN B CB  
2438 C CB  B ASN B 7   ? 0.2625 0.2415 0.2296 0.0028  0.0311  -0.0136 232  ASN B CB  
2439 C CG  A ASN B 7   ? 0.2983 0.2874 0.2703 0.0053  0.0305  -0.0108 232  ASN B CG  
2440 C CG  B ASN B 7   ? 0.3441 0.3192 0.3039 0.0005  0.0325  -0.0181 232  ASN B CG  
2441 O OD1 A ASN B 7   ? 0.2882 0.2856 0.2654 0.0045  0.0269  -0.0082 232  ASN B OD1 
2442 O OD1 B ASN B 7   ? 0.3590 0.3286 0.3136 -0.0039 0.0315  -0.0217 232  ASN B OD1 
2443 N ND2 A ASN B 7   ? 0.3523 0.3403 0.3224 0.0086  0.0344  -0.0113 232  ASN B ND2 
2444 N ND2 B ASN B 7   ? 0.3977 0.3760 0.3571 0.0034  0.0348  -0.0177 232  ASN B ND2 
2445 N N   . LEU B 8   ? 0.2019 0.1974 0.1746 -0.0074 0.0191  -0.0129 233  LEU B N   
2446 C CA  . LEU B 8   ? 0.1721 0.1745 0.1452 -0.0101 0.0157  -0.0132 233  LEU B CA  
2447 C C   . LEU B 8   ? 0.2176 0.2176 0.1869 -0.0148 0.0139  -0.0165 233  LEU B C   
2448 O O   . LEU B 8   ? 0.1876 0.1837 0.1569 -0.0167 0.0138  -0.0173 233  LEU B O   
2449 C CB  . LEU B 8   ? 0.1622 0.1718 0.1413 -0.0097 0.0126  -0.0099 233  LEU B CB  
2450 C CG  . LEU B 8   ? 0.1944 0.2077 0.1781 -0.0058 0.0135  -0.0065 233  LEU B CG  
2451 C CD1 . LEU B 8   ? 0.2242 0.2428 0.2125 -0.0061 0.0103  -0.0040 233  LEU B CD1 
2452 C CD2 . LEU B 8   ? 0.2389 0.2561 0.2224 -0.0047 0.0144  -0.0062 233  LEU B CD2 
2453 N N   . GLN B 9   ? 0.1921 0.1949 0.1582 -0.0167 0.0125  -0.0182 234  GLN B N   
2454 C CA  . GLN B 9   ? 0.1819 0.1851 0.1456 -0.0212 0.0098  -0.0207 234  GLN B CA  
2455 C C   . GLN B 9   ? 0.1828 0.1923 0.1521 -0.0225 0.0064  -0.0186 234  GLN B C   
2456 O O   . GLN B 9   ? 0.1766 0.1906 0.1504 -0.0202 0.0055  -0.0155 234  GLN B O   
2457 C CB  . GLN B 9   ? 0.2127 0.2187 0.1718 -0.0225 0.0085  -0.0223 234  GLN B CB  
2458 C CG  . GLN B 9   ? 0.2277 0.2275 0.1801 -0.0213 0.0122  -0.0247 234  GLN B CG  
2459 C CD  . GLN B 9   ? 0.3054 0.3085 0.2529 -0.0220 0.0113  -0.0256 234  GLN B CD  
2460 O OE1 . GLN B 9   ? 0.3486 0.3584 0.2975 -0.0235 0.0076  -0.0243 234  GLN B OE1 
2461 N NE2 . GLN B 9   ? 0.3153 0.3132 0.2564 -0.0207 0.0148  -0.0278 234  GLN B NE2 
2462 N N   . THR B 10  ? 0.1558 0.1654 0.1247 -0.0264 0.0045  -0.0204 235  THR B N   
2463 C CA  . THR B 10  ? 0.1448 0.1603 0.1190 -0.0274 0.0018  -0.0185 235  THR B CA  
2464 C C   . THR B 10  ? 0.1527 0.1755 0.1292 -0.0259 -0.0007 -0.0164 235  THR B C   
2465 O O   . THR B 10  ? 0.1618 0.1882 0.1428 -0.0244 -0.0016 -0.0139 235  THR B O   
2466 C CB  . THR B 10  ? 0.1323 0.1483 0.1062 -0.0319 0.0002  -0.0207 235  THR B CB  
2467 O OG1 . THR B 10  ? 0.1932 0.2009 0.1639 -0.0337 0.0028  -0.0231 235  THR B OG1 
2468 C CG2 . THR B 10  ? 0.1554 0.1765 0.1353 -0.0323 -0.0013 -0.0186 235  THR B CG2 
2469 N N   . ASP B 11  ? 0.1468 0.1714 0.1197 -0.0264 -0.0017 -0.0174 236  ASP B N   
2470 C CA  . ASP B 11  ? 0.1903 0.2209 0.1648 -0.0251 -0.0038 -0.0151 236  ASP B CA  
2471 C C   . ASP B 11  ? 0.2019 0.2325 0.1779 -0.0217 -0.0021 -0.0127 236  ASP B C   
2472 O O   . ASP B 11  ? 0.1753 0.2101 0.1528 -0.0207 -0.0036 -0.0105 236  ASP B O   
2473 C CB  . ASP B 11  ? 0.1939 0.2266 0.1636 -0.0268 -0.0055 -0.0165 236  ASP B CB  
2474 C CG  . ASP B 11  ? 0.2480 0.2757 0.2112 -0.0266 -0.0029 -0.0186 236  ASP B CG  
2475 O OD1 . ASP B 11  ? 0.2153 0.2384 0.1783 -0.0244 0.0005  -0.0186 236  ASP B OD1 
2476 O OD2 . ASP B 11  ? 0.3351 0.3635 0.2930 -0.0285 -0.0042 -0.0204 236  ASP B OD2 
2477 N N   . GLU B 12  ? 0.1335 0.1598 0.1095 -0.0200 0.0009  -0.0127 237  GLU B N   
2478 C CA  . GLU B 12  ? 0.1310 0.1586 0.1098 -0.0169 0.0022  -0.0101 237  GLU B CA  
2479 C C   . GLU B 12  ? 0.1680 0.1964 0.1516 -0.0159 0.0017  -0.0082 237  GLU B C   
2480 O O   . GLU B 12  ? 0.1398 0.1697 0.1262 -0.0137 0.0023  -0.0061 237  GLU B O   
2481 C CB  . GLU B 12  ? 0.1738 0.1971 0.1499 -0.0150 0.0059  -0.0109 237  GLU B CB  
2482 C CG  . GLU B 12  ? 0.1598 0.1825 0.1302 -0.0155 0.0069  -0.0126 237  GLU B CG  
2483 C CD  . GLU B 12  ? 0.3018 0.3190 0.2685 -0.0136 0.0111  -0.0142 237  GLU B CD  
2484 O OE1 . GLU B 12  ? 0.2653 0.2783 0.2334 -0.0122 0.0132  -0.0143 237  GLU B OE1 
2485 O OE2 . GLU B 12  ? 0.3123 0.3293 0.2745 -0.0133 0.0127  -0.0151 237  GLU B OE2 
2486 N N   . MET B 13  ? 0.1434 0.1713 0.1280 -0.0175 0.0004  -0.0089 238  MET B N   
2487 C CA  . MET B 13  ? 0.1443 0.1726 0.1324 -0.0166 0.0001  -0.0073 238  MET B CA  
2488 C C   . MET B 13  ? 0.1287 0.1611 0.1191 -0.0176 -0.0026 -0.0066 238  MET B C   
2489 O O   . MET B 13  ? 0.1334 0.1686 0.1232 -0.0188 -0.0042 -0.0071 238  MET B O   
2490 C CB  . MET B 13  ? 0.1409 0.1641 0.1280 -0.0173 0.0019  -0.0083 238  MET B CB  
2491 C CG  . MET B 13  ? 0.1922 0.2104 0.1774 -0.0153 0.0049  -0.0085 238  MET B CG  
2492 S SD  . MET B 13  ? 0.1706 0.1814 0.1546 -0.0154 0.0075  -0.0089 238  MET B SD  
2493 C CE  . MET B 13  ? 0.1469 0.1545 0.1272 -0.0201 0.0072  -0.0127 238  MET B CE  
2494 N N   . SER B 14  ? 0.1264 0.1592 0.1192 -0.0167 -0.0028 -0.0052 239  SER B N   
2495 C CA  . SER B 14  ? 0.1206 0.1566 0.1155 -0.0168 -0.0047 -0.0043 239  SER B CA  
2496 C C   . SER B 14  ? 0.1373 0.1728 0.1330 -0.0176 -0.0044 -0.0046 239  SER B C   
2497 O O   . SER B 14  ? 0.1549 0.1872 0.1500 -0.0177 -0.0028 -0.0046 239  SER B O   
2498 C CB  . SER B 14  ? 0.1385 0.1754 0.1347 -0.0150 -0.0053 -0.0025 239  SER B CB  
2499 O OG  . SER B 14  ? 0.1641 0.2017 0.1602 -0.0143 -0.0050 -0.0018 239  SER B OG  
2500 N N   . SER B 15  ? 0.1155 0.1541 0.1127 -0.0181 -0.0058 -0.0046 240  SER B N   
2501 C CA  . SER B 15  ? 0.1144 0.1534 0.1128 -0.0186 -0.0052 -0.0045 240  SER B CA  
2502 C C   . SER B 15  ? 0.1362 0.1736 0.1341 -0.0169 -0.0047 -0.0032 240  SER B C   
2503 O O   . SER B 15  ? 0.1446 0.1823 0.1424 -0.0155 -0.0058 -0.0024 240  SER B O   
2504 C CB  . SER B 15  ? 0.1649 0.2082 0.1655 -0.0188 -0.0064 -0.0047 240  SER B CB  
2505 O OG  . SER B 15  ? 0.1369 0.1811 0.1389 -0.0188 -0.0055 -0.0043 240  SER B OG  
2506 N N   . SER B 16  ? 0.1276 0.1632 0.1251 -0.0172 -0.0032 -0.0028 241  SER B N   
2507 C CA  . SER B 16  ? 0.1106 0.1451 0.1070 -0.0158 -0.0029 -0.0015 241  SER B CA  
2508 C C   . SER B 16  ? 0.1128 0.1492 0.1095 -0.0156 -0.0027 -0.0015 241  SER B C   
2509 O O   . SER B 16  ? 0.1375 0.1729 0.1324 -0.0146 -0.0023 -0.0007 241  SER B O   
2510 C CB  . SER B 16  ? 0.1375 0.1681 0.1323 -0.0158 -0.0009 -0.0006 241  SER B CB  
2511 O OG  . SER B 16  ? 0.1276 0.1574 0.1230 -0.0179 0.0007  -0.0013 241  SER B OG  
2512 N N   . ARG B 17  ? 0.1154 0.1551 0.1144 -0.0164 -0.0031 -0.0024 242  ARG B N   
2513 C CA  . ARG B 17  ? 0.1127 0.1548 0.1127 -0.0156 -0.0027 -0.0024 242  ARG B CA  
2514 C C   . ARG B 17  ? 0.1513 0.1953 0.1523 -0.0142 -0.0043 -0.0028 242  ARG B C   
2515 O O   . ARG B 17  ? 0.1542 0.1989 0.1550 -0.0128 -0.0038 -0.0028 242  ARG B O   
2516 C CB  . ARG B 17  ? 0.1150 0.1598 0.1176 -0.0173 -0.0010 -0.0026 242  ARG B CB  
2517 C CG  . ARG B 17  ? 0.1061 0.1480 0.1071 -0.0183 0.0013  -0.0018 242  ARG B CG  
2518 C CD  . ARG B 17  ? 0.1145 0.1598 0.1187 -0.0204 0.0032  -0.0018 242  ARG B CD  
2519 N NE  . ARG B 17  ? 0.1176 0.1668 0.1233 -0.0187 0.0040  -0.0016 242  ARG B NE  
2520 C CZ  . ARG B 17  ? 0.1451 0.2003 0.1555 -0.0191 0.0040  -0.0019 242  ARG B CZ  
2521 N NH1 . ARG B 17  ? 0.1330 0.1915 0.1469 -0.0216 0.0028  -0.0025 242  ARG B NH1 
2522 N NH2 . ARG B 17  ? 0.1389 0.1970 0.1503 -0.0169 0.0053  -0.0015 242  ARG B NH2 
2523 N N   . TRP B 18  ? 0.1298 0.1743 0.1313 -0.0145 -0.0059 -0.0030 243  TRP B N   
2524 C CA  . TRP B 18  ? 0.1278 0.1728 0.1295 -0.0131 -0.0074 -0.0028 243  TRP B CA  
2525 C C   . TRP B 18  ? 0.1434 0.1869 0.1440 -0.0135 -0.0086 -0.0025 243  TRP B C   
2526 O O   . TRP B 18  ? 0.1625 0.2067 0.1633 -0.0148 -0.0086 -0.0028 243  TRP B O   
2527 C CB  . TRP B 18  ? 0.1395 0.1888 0.1442 -0.0128 -0.0079 -0.0028 243  TRP B CB  
2528 C CG  . TRP B 18  ? 0.1236 0.1725 0.1283 -0.0107 -0.0090 -0.0022 243  TRP B CG  
2529 C CD1 . TRP B 18  ? 0.1637 0.2120 0.1678 -0.0105 -0.0105 -0.0015 243  TRP B CD1 
2530 C CD2 . TRP B 18  ? 0.1420 0.1900 0.1466 -0.0085 -0.0081 -0.0021 243  TRP B CD2 
2531 N NE1 . TRP B 18  ? 0.1400 0.1868 0.1440 -0.0084 -0.0108 -0.0009 243  TRP B NE1 
2532 C CE2 . TRP B 18  ? 0.1178 0.1641 0.1220 -0.0070 -0.0093 -0.0015 243  TRP B CE2 
2533 C CE3 . TRP B 18  ? 0.1329 0.1809 0.1375 -0.0075 -0.0062 -0.0026 243  TRP B CE3 
2534 C CZ2 . TRP B 18  ? 0.1555 0.1994 0.1591 -0.0044 -0.0087 -0.0014 243  TRP B CZ2 
2535 C CZ3 . TRP B 18  ? 0.1399 0.1860 0.1437 -0.0048 -0.0054 -0.0028 243  TRP B CZ3 
2536 C CH2 . TRP B 18  ? 0.1280 0.1718 0.1313 -0.0033 -0.0067 -0.0023 243  TRP B CH2 
2537 N N   . PRO B 19  ? 0.1475 0.1889 0.1467 -0.0128 -0.0095 -0.0021 244  PRO B N   
2538 C CA  . PRO B 19  ? 0.1746 0.2154 0.1735 -0.0133 -0.0103 -0.0015 244  PRO B CA  
2539 C C   . PRO B 19  ? 0.1947 0.2371 0.1942 -0.0135 -0.0110 -0.0012 244  PRO B C   
2540 O O   . PRO B 19  ? 0.2235 0.2659 0.2232 -0.0127 -0.0118 -0.0007 244  PRO B O   
2541 C CB  . PRO B 19  ? 0.2036 0.2423 0.2014 -0.0130 -0.0112 -0.0011 244  PRO B CB  
2542 C CG  . PRO B 19  ? 0.2104 0.2477 0.2069 -0.0122 -0.0107 -0.0018 244  PRO B CG  
2543 C CD  . PRO B 19  ? 0.1676 0.2070 0.1655 -0.0116 -0.0097 -0.0022 244  PRO B CD  
2544 N N   . ASN B 20  ? 0.1242 0.1678 0.1236 -0.0145 -0.0105 -0.0017 245  ASN B N   
2545 C CA  . ASN B 20  ? 0.1237 0.1690 0.1226 -0.0150 -0.0113 -0.0015 245  ASN B CA  
2546 C C   . ASN B 20  ? 0.1349 0.1800 0.1325 -0.0164 -0.0104 -0.0027 245  ASN B C   
2547 O O   . ASN B 20  ? 0.1629 0.2067 0.1607 -0.0169 -0.0092 -0.0035 245  ASN B O   
2548 C CB  . ASN B 20  ? 0.1426 0.1910 0.1430 -0.0145 -0.0123 -0.0014 245  ASN B CB  
2549 C CG  . ASN B 20  ? 0.2201 0.2682 0.2205 -0.0130 -0.0134 0.0001  245  ASN B CG  
2550 O OD1 . ASN B 20  ? 0.2288 0.2748 0.2278 -0.0129 -0.0135 0.0010  245  ASN B OD1 
2551 N ND2 . ASN B 20  ? 0.2210 0.2712 0.2232 -0.0116 -0.0140 0.0006  245  ASN B ND2 
2552 N N   . PRO B 21  ? 0.1429 0.1886 0.1388 -0.0168 -0.0107 -0.0027 246  PRO B N   
2553 C CA  . PRO B 21  ? 0.1460 0.1905 0.1396 -0.0182 -0.0096 -0.0043 246  PRO B CA  
2554 C C   . PRO B 21  ? 0.1383 0.1842 0.1323 -0.0200 -0.0101 -0.0059 246  PRO B C   
2555 O O   . PRO B 21  ? 0.1629 0.2126 0.1587 -0.0202 -0.0117 -0.0056 246  PRO B O   
2556 C CB  . PRO B 21  ? 0.1977 0.2431 0.1886 -0.0182 -0.0101 -0.0039 246  PRO B CB  
2557 C CG  . PRO B 21  ? 0.2384 0.2847 0.2306 -0.0168 -0.0110 -0.0017 246  PRO B CG  
2558 C CD  . PRO B 21  ? 0.1908 0.2378 0.1859 -0.0162 -0.0119 -0.0013 246  PRO B CD  
2559 N N   . LEU B 22  ? 0.1433 0.1862 0.1360 -0.0213 -0.0085 -0.0075 247  LEU B N   
2560 C CA  . LEU B 22  ? 0.1234 0.1673 0.1162 -0.0240 -0.0089 -0.0092 247  LEU B CA  
2561 C C   . LEU B 22  ? 0.1970 0.2439 0.1877 -0.0255 -0.0108 -0.0102 247  LEU B C   
2562 O O   . LEU B 22  ? 0.1699 0.2152 0.1569 -0.0251 -0.0106 -0.0105 247  LEU B O   
2563 C CB  . LEU B 22  ? 0.1239 0.1623 0.1148 -0.0253 -0.0065 -0.0108 247  LEU B CB  
2564 C CG  . LEU B 22  ? 0.1379 0.1736 0.1305 -0.0238 -0.0048 -0.0096 247  LEU B CG  
2565 C CD1 . LEU B 22  ? 0.1844 0.2139 0.1749 -0.0248 -0.0023 -0.0107 247  LEU B CD1 
2566 C CD2 . LEU B 22  ? 0.1458 0.1849 0.1420 -0.0243 -0.0054 -0.0087 247  LEU B CD2 
2567 N N   . ALA B 23  ? 0.1267 0.1785 0.1198 -0.0271 -0.0127 -0.0105 248  ALA B N   
2568 C CA  . ALA B 23  ? 0.1849 0.2410 0.1764 -0.0286 -0.0153 -0.0110 248  ALA B CA  
2569 C C   . ALA B 23  ? 0.1739 0.2319 0.1655 -0.0327 -0.0163 -0.0134 248  ALA B C   
2570 O O   . ALA B 23  ? 0.1746 0.2347 0.1629 -0.0346 -0.0183 -0.0146 248  ALA B O   
2571 C CB  . ALA B 23  ? 0.2109 0.2732 0.2061 -0.0264 -0.0175 -0.0084 248  ALA B CB  
2572 N N   A THR B 24  ? 0.1317 0.1892 0.1266 -0.0343 -0.0150 -0.0140 249  THR B N   
2573 N N   B THR B 24  ? 0.1322 0.1892 0.1268 -0.0343 -0.0149 -0.0141 249  THR B N   
2574 C CA  A THR B 24  ? 0.1349 0.1938 0.1302 -0.0389 -0.0158 -0.0163 249  THR B CA  
2575 C CA  B THR B 24  ? 0.1367 0.1957 0.1321 -0.0389 -0.0158 -0.0162 249  THR B CA  
2576 C C   A THR B 24  ? 0.1586 0.2105 0.1535 -0.0405 -0.0126 -0.0175 249  THR B C   
2577 C C   B THR B 24  ? 0.1573 0.2096 0.1526 -0.0405 -0.0126 -0.0174 249  THR B C   
2578 O O   A THR B 24  ? 0.1539 0.2023 0.1498 -0.0377 -0.0103 -0.0159 249  THR B O   
2579 O O   B THR B 24  ? 0.1560 0.2052 0.1527 -0.0379 -0.0104 -0.0158 249  THR B O   
2580 C CB  A THR B 24  ? 0.1744 0.2428 0.1761 -0.0400 -0.0180 -0.0151 249  THR B CB  
2581 C CB  B THR B 24  ? 0.1757 0.2443 0.1776 -0.0394 -0.0180 -0.0147 249  THR B CB  
2582 O OG1 A THR B 24  ? 0.1503 0.2199 0.1568 -0.0372 -0.0164 -0.0128 249  THR B OG1 
2583 O OG1 B THR B 24  ? 0.3059 0.3799 0.3079 -0.0369 -0.0207 -0.0130 249  THR B OG1 
2584 C CG2 A THR B 24  ? 0.2785 0.3540 0.2803 -0.0388 -0.0216 -0.0139 249  THR B CG2 
2585 C CG2 B THR B 24  ? 0.1117 0.1837 0.1150 -0.0447 -0.0194 -0.0169 249  THR B CG2 
2586 N N   . LEU B 25  ? 0.1642 0.2138 0.1572 -0.0450 -0.0125 -0.0202 250  LEU B N   
2587 C CA  . LEU B 25  ? 0.1674 0.2096 0.1596 -0.0472 -0.0095 -0.0214 250  LEU B CA  
2588 C C   . LEU B 25  ? 0.1735 0.2192 0.1681 -0.0529 -0.0108 -0.0233 250  LEU B C   
2589 O O   . LEU B 25  ? 0.1845 0.2317 0.1762 -0.0563 -0.0131 -0.0258 250  LEU B O   
2590 C CB  . LEU B 25  ? 0.1702 0.2024 0.1553 -0.0467 -0.0072 -0.0235 250  LEU B CB  
2591 C CG  . LEU B 25  ? 0.1738 0.1966 0.1570 -0.0488 -0.0039 -0.0249 250  LEU B CG  
2592 C CD1 . LEU B 25  ? 0.1700 0.1911 0.1566 -0.0458 -0.0014 -0.0219 250  LEU B CD1 
2593 C CD2 . LEU B 25  ? 0.1732 0.1866 0.1490 -0.0481 -0.0018 -0.0274 250  LEU B CD2 
2594 N N   . PHE B 26  ? 0.1505 0.1981 0.1504 -0.0542 -0.0094 -0.0220 251  PHE B N   
2595 C CA  . PHE B 26  ? 0.1674 0.2213 0.1714 -0.0597 -0.0111 -0.0231 251  PHE B CA  
2596 C C   . PHE B 26  ? 0.1622 0.2140 0.1701 -0.0617 -0.0080 -0.0220 251  PHE B C   
2597 O O   . PHE B 26  ? 0.1639 0.2121 0.1722 -0.0580 -0.0052 -0.0197 251  PHE B O   
2598 C CB  . PHE B 26  ? 0.1679 0.2349 0.1777 -0.0587 -0.0147 -0.0213 251  PHE B CB  
2599 C CG  . PHE B 26  ? 0.1389 0.2108 0.1543 -0.0542 -0.0135 -0.0178 251  PHE B CG  
2600 C CD1 . PHE B 26  ? 0.1813 0.2510 0.1949 -0.0484 -0.0129 -0.0160 251  PHE B CD1 
2601 C CD2 . PHE B 26  ? 0.1743 0.2529 0.1969 -0.0560 -0.0127 -0.0164 251  PHE B CD2 
2602 C CE1 . PHE B 26  ? 0.1692 0.2424 0.1870 -0.0446 -0.0118 -0.0132 251  PHE B CE1 
2603 C CE2 . PHE B 26  ? 0.1907 0.2732 0.2177 -0.0517 -0.0112 -0.0135 251  PHE B CE2 
2604 C CZ  . PHE B 26  ? 0.1672 0.2466 0.1914 -0.0460 -0.0108 -0.0121 251  PHE B CZ  
2605 N N   . ALA B 27  ? 0.1678 0.2220 0.1782 -0.0679 -0.0086 -0.0237 252  ALA B N   
2606 C CA  . ALA B 27  ? 0.1763 0.2298 0.1910 -0.0708 -0.0057 -0.0225 252  ALA B CA  
2607 C C   . ALA B 27  ? 0.2082 0.2753 0.2314 -0.0741 -0.0081 -0.0217 252  ALA B C   
2608 O O   . ALA B 27  ? 0.2007 0.2733 0.2246 -0.0785 -0.0116 -0.0239 252  ALA B O   
2609 C CB  . ALA B 27  ? 0.2283 0.2703 0.2383 -0.0759 -0.0034 -0.0252 252  ALA B CB  
2610 N N   . ASP B 28  ? 0.1905 0.2634 0.2199 -0.0719 -0.0062 -0.0185 253  ASP B N   
2611 C CA  . ASP B 28  ? 0.1862 0.2730 0.2248 -0.0743 -0.0077 -0.0172 253  ASP B CA  
2612 C C   . ASP B 28  ? 0.1838 0.2698 0.2265 -0.0784 -0.0039 -0.0161 253  ASP B C   
2613 O O   . ASP B 28  ? 0.2510 0.3349 0.2945 -0.0748 -0.0003 -0.0134 253  ASP B O   
2614 C CB  . ASP B 28  ? 0.2278 0.3235 0.2707 -0.0678 -0.0084 -0.0142 253  ASP B CB  
2615 C CG  . ASP B 28  ? 0.2742 0.3854 0.3269 -0.0695 -0.0105 -0.0128 253  ASP B CG  
2616 O OD1 . ASP B 28  ? 0.3283 0.4438 0.3852 -0.0761 -0.0109 -0.0138 253  ASP B OD1 
2617 O OD2 . ASP B 28  ? 0.3145 0.4335 0.3708 -0.0642 -0.0116 -0.0106 253  ASP B OD2 
2618 N N   . PRO B 29  ? 0.1863 0.2740 0.2315 -0.0861 -0.0047 -0.0180 254  PRO B N   
2619 C CA  . PRO B 29  ? 0.2181 0.3042 0.2671 -0.0907 -0.0008 -0.0169 254  PRO B CA  
2620 C C   . PRO B 29  ? 0.3981 0.4988 0.4577 -0.0908 0.0000  -0.0138 254  PRO B C   
2621 O O   . PRO B 29  ? 0.3432 0.4437 0.4066 -0.0945 0.0036  -0.0124 254  PRO B O   
2622 C CB  . PRO B 29  ? 0.2132 0.2954 0.2604 -0.0995 -0.0024 -0.0206 254  PRO B CB  
2623 C CG  . PRO B 29  ? 0.2855 0.3776 0.3339 -0.1002 -0.0083 -0.0226 254  PRO B CG  
2624 C CD  . PRO B 29  ? 0.1978 0.2890 0.2421 -0.0915 -0.0093 -0.0214 254  PRO B CD  
2625 N N   . ASN B 30  ? 0.2248 0.3378 0.2895 -0.0867 -0.0030 -0.0125 255  ASN B N   
2626 C CA  . ASN B 30  ? 0.3138 0.4419 0.3893 -0.0863 -0.0023 -0.0097 255  ASN B CA  
2627 C C   . ASN B 30  ? 0.3983 0.5283 0.4746 -0.0778 0.0002  -0.0066 255  ASN B C   
2628 O O   . ASN B 30  ? 0.3256 0.4685 0.4098 -0.0748 -0.0003 -0.0044 255  ASN B O   
2629 C CB  . ASN B 30  ? 0.2958 0.4383 0.3779 -0.0888 -0.0078 -0.0104 255  ASN B CB  
2630 C CG  . ASN B 30  ? 0.3783 0.5198 0.4603 -0.0978 -0.0102 -0.0134 255  ASN B CG  
2631 O OD1 . ASN B 30  ? 0.4597 0.5960 0.5425 -0.1029 -0.0070 -0.0136 255  ASN B OD1 
2632 N ND2 . ASN B 30  ? 0.4044 0.5476 0.4836 -0.0982 -0.0155 -0.0156 255  ASN B ND2 
2633 N N   . VAL B 31  ? 0.3089 0.4260 0.3770 -0.0736 0.0030  -0.0063 256  VAL B N   
2634 C CA  . VAL B 31  ? 0.2970 0.4141 0.3648 -0.0666 0.0061  -0.0037 256  VAL B CA  
2635 C C   . VAL B 31  ? 0.2771 0.3942 0.3478 -0.0686 0.0113  -0.0016 256  VAL B C   
2636 O O   . VAL B 31  ? 0.3701 0.4769 0.4360 -0.0720 0.0138  -0.0019 256  VAL B O   
2637 C CB  . VAL B 31  ? 0.3337 0.4381 0.3915 -0.0615 0.0062  -0.0043 256  VAL B CB  
2638 C CG1 . VAL B 31  ? 0.3988 0.5034 0.4558 -0.0548 0.0088  -0.0020 256  VAL B CG1 
2639 C CG2 . VAL B 31  ? 0.2898 0.3940 0.3445 -0.0602 0.0014  -0.0064 256  VAL B CG2 
2640 N N   . ALA B 32  ? 0.2754 0.4040 0.3538 -0.0664 0.0132  0.0009  257  ALA B N   
2641 C CA  . ALA B 32  ? 0.3696 0.5008 0.4523 -0.0693 0.0182  0.0030  257  ALA B CA  
2642 C C   . ALA B 32  ? 0.3850 0.5046 0.4598 -0.0659 0.0228  0.0045  257  ALA B C   
2643 O O   . ALA B 32  ? 0.3352 0.4507 0.4094 -0.0697 0.0267  0.0057  257  ALA B O   
2644 C CB  . ALA B 32  ? 0.3135 0.4608 0.4068 -0.0671 0.0193  0.0053  257  ALA B CB  
2645 N N   . VAL B 33  ? 0.2456 0.3599 0.3140 -0.0589 0.0223  0.0044  258  VAL B N   
2646 C CA  . VAL B 33  ? 0.1708 0.2757 0.2318 -0.0552 0.0261  0.0059  258  VAL B CA  
2647 C C   . VAL B 33  ? 0.1839 0.2762 0.2352 -0.0530 0.0239  0.0043  258  VAL B C   
2648 O O   . VAL B 33  ? 0.2245 0.3173 0.2747 -0.0506 0.0199  0.0026  258  VAL B O   
2649 C CB  . VAL B 33  ? 0.1698 0.2806 0.2321 -0.0488 0.0283  0.0074  258  VAL B CB  
2650 C CG1 . VAL B 33  ? 0.2460 0.3470 0.2995 -0.0454 0.0319  0.0087  258  VAL B CG1 
2651 C CG2 . VAL B 33  ? 0.2257 0.3500 0.2984 -0.0506 0.0311  0.0093  258  VAL B CG2 
2652 N N   . ALA B 34  ? 0.2142 0.2959 0.2590 -0.0538 0.0265  0.0052  259  ALA B N   
2653 C CA  . ALA B 34  ? 0.1968 0.2671 0.2333 -0.0518 0.0247  0.0042  259  ALA B CA  
2654 C C   . ALA B 34  ? 0.1585 0.2279 0.1907 -0.0450 0.0234  0.0042  259  ALA B C   
2655 O O   . ALA B 34  ? 0.1989 0.2722 0.2316 -0.0417 0.0256  0.0056  259  ALA B O   
2656 C CB  . ALA B 34  ? 0.2112 0.2708 0.2419 -0.0534 0.0281  0.0058  259  ALA B CB  
2657 N N   . PRO B 35  ? 0.1388 0.2031 0.1668 -0.0430 0.0202  0.0026  260  PRO B N   
2658 C CA  . PRO B 35  ? 0.1329 0.1957 0.1568 -0.0373 0.0189  0.0026  260  PRO B CA  
2659 C C   . PRO B 35  ? 0.1609 0.2159 0.1778 -0.0349 0.0212  0.0043  260  PRO B C   
2660 O O   . PRO B 35  ? 0.1521 0.2003 0.1659 -0.0370 0.0229  0.0053  260  PRO B O   
2661 C CB  . PRO B 35  ? 0.1864 0.2463 0.2084 -0.0369 0.0149  0.0005  260  PRO B CB  
2662 C CG  . PRO B 35  ? 0.1690 0.2235 0.1901 -0.0416 0.0152  -0.0002 260  PRO B CG  
2663 C CD  . PRO B 35  ? 0.1536 0.2133 0.1803 -0.0461 0.0176  0.0005  260  PRO B CD  
2664 N N   . GLN B 36  ? 0.1300 0.1857 0.1441 -0.0304 0.0213  0.0047  261  GLN B N   
2665 C CA  . GLN B 36  ? 0.1325 0.1818 0.1394 -0.0279 0.0229  0.0063  261  GLN B CA  
2666 C C   . GLN B 36  ? 0.1929 0.2396 0.1955 -0.0239 0.0198  0.0052  261  GLN B C   
2667 O O   . GLN B 36  ? 0.1658 0.2116 0.1642 -0.0209 0.0204  0.0056  261  GLN B O   
2668 C CB  . GLN B 36  ? 0.1213 0.1735 0.1278 -0.0269 0.0269  0.0079  261  GLN B CB  
2669 C CG  . GLN B 36  ? 0.1673 0.2124 0.1659 -0.0256 0.0289  0.0101  261  GLN B CG  
2670 C CD  . GLN B 36  ? 0.2219 0.2693 0.2188 -0.0248 0.0332  0.0119  261  GLN B CD  
2671 O OE1 . GLN B 36  ? 0.1908 0.2455 0.1932 -0.0253 0.0354  0.0117  261  GLN B OE1 
2672 N NE2 . GLN B 36  ? 0.1842 0.2257 0.1731 -0.0232 0.0347  0.0138  261  GLN B NE2 
2673 N N   . TRP B 37  ? 0.1415 0.1872 0.1453 -0.0244 0.0166  0.0037  262  TRP B N   
2674 C CA  . TRP B 37  ? 0.1305 0.1743 0.1313 -0.0214 0.0135  0.0027  262  TRP B CA  
2675 C C   . TRP B 37  ? 0.1629 0.2011 0.1571 -0.0193 0.0138  0.0041  262  TRP B C   
2676 O O   . TRP B 37  ? 0.1501 0.1838 0.1417 -0.0202 0.0152  0.0057  262  TRP B O   
2677 C CB  . TRP B 37  ? 0.1389 0.1815 0.1412 -0.0228 0.0109  0.0015  262  TRP B CB  
2678 C CG  . TRP B 37  ? 0.1296 0.1779 0.1378 -0.0252 0.0101  0.0002  262  TRP B CG  
2679 C CD1 . TRP B 37  ? 0.1726 0.2280 0.1852 -0.0247 0.0102  -0.0001 262  TRP B CD1 
2680 C CD2 . TRP B 37  ? 0.1180 0.1657 0.1279 -0.0284 0.0089  -0.0010 262  TRP B CD2 
2681 N NE1 . TRP B 37  ? 0.1505 0.2106 0.1680 -0.0274 0.0087  -0.0011 262  TRP B NE1 
2682 C CE2 . TRP B 37  ? 0.1008 0.1560 0.1162 -0.0300 0.0078  -0.0019 262  TRP B CE2 
2683 C CE3 . TRP B 37  ? 0.1412 0.1825 0.1483 -0.0298 0.0087  -0.0015 262  TRP B CE3 
2684 C CZ2 . TRP B 37  ? 0.1321 0.1889 0.1498 -0.0335 0.0062  -0.0034 262  TRP B CZ2 
2685 C CZ3 . TRP B 37  ? 0.1269 0.1689 0.1360 -0.0332 0.0075  -0.0033 262  TRP B CZ3 
2686 C CH2 . TRP B 37  ? 0.1266 0.1763 0.1406 -0.0352 0.0061  -0.0043 262  TRP B CH2 
2687 N N   . GLN B 38  ? 0.1313 0.1695 0.1226 -0.0164 0.0122  0.0034  263  GLN B N   
2688 C CA  . GLN B 38  ? 0.1137 0.1476 0.0987 -0.0146 0.0116  0.0045  263  GLN B CA  
2689 C C   . GLN B 38  ? 0.1111 0.1429 0.0952 -0.0138 0.0083  0.0041  263  GLN B C   
2690 O O   . GLN B 38  ? 0.1518 0.1805 0.1318 -0.0128 0.0075  0.0055  263  GLN B O   
2691 C CB  . GLN B 38  ? 0.1506 0.1852 0.1318 -0.0124 0.0123  0.0040  263  GLN B CB  
2692 C CG  . GLN B 38  ? 0.1558 0.1926 0.1372 -0.0128 0.0164  0.0048  263  GLN B CG  
2693 C CD  . GLN B 38  ? 0.1813 0.2151 0.1599 -0.0141 0.0187  0.0075  263  GLN B CD  
2694 O OE1 . GLN B 38  ? 0.1672 0.1970 0.1395 -0.0128 0.0182  0.0088  263  GLN B OE1 
2695 N NE2 . GLN B 38  ? 0.1436 0.1791 0.1268 -0.0167 0.0213  0.0084  263  GLN B NE2 
2696 N N   . ASN B 39  ? 0.1143 0.1482 0.1021 -0.0142 0.0063  0.0025  264  ASN B N   
2697 C CA  . ASN B 39  ? 0.1356 0.1681 0.1235 -0.0138 0.0037  0.0022  264  ASN B CA  
2698 C C   . ASN B 39  ? 0.1147 0.1460 0.1052 -0.0155 0.0041  0.0023  264  ASN B C   
2699 O O   . ASN B 39  ? 0.1543 0.1864 0.1471 -0.0175 0.0059  0.0020  264  ASN B O   
2700 C CB  . ASN B 39  ? 0.1319 0.1666 0.1213 -0.0130 0.0014  0.0006  264  ASN B CB  
2701 C CG  . ASN B 39  ? 0.1289 0.1630 0.1146 -0.0114 0.0008  0.0002  264  ASN B CG  
2702 O OD1 . ASN B 39  ? 0.1404 0.1724 0.1219 -0.0107 0.0004  0.0011  264  ASN B OD1 
2703 N ND2 . ASN B 39  ? 0.1326 0.1683 0.1196 -0.0107 0.0007  -0.0012 264  ASN B ND2 
2704 N N   . GLY B 40  ? 0.1025 0.1319 0.0924 -0.0148 0.0027  0.0026  265  GLY B N   
2705 C CA  . GLY B 40  ? 0.1427 0.1699 0.1341 -0.0161 0.0035  0.0023  265  GLY B CA  
2706 C C   . GLY B 40  ? 0.1826 0.2054 0.1724 -0.0169 0.0061  0.0038  265  GLY B C   
2707 O O   . GLY B 40  ? 0.1508 0.1715 0.1419 -0.0191 0.0074  0.0030  265  GLY B O   
2708 N N   . ARG B 41  ? 0.1287 0.1497 0.1154 -0.0153 0.0069  0.0060  266  ARG B N   
2709 C CA  . ARG B 41  ? 0.1358 0.1522 0.1204 -0.0159 0.0097  0.0080  266  ARG B CA  
2710 C C   . ARG B 41  ? 0.1490 0.1617 0.1307 -0.0131 0.0093  0.0104  266  ARG B C   
2711 O O   . ARG B 41  ? 0.1667 0.1813 0.1462 -0.0108 0.0075  0.0117  266  ARG B O   
2712 C CB  . ARG B 41  ? 0.1517 0.1694 0.1345 -0.0163 0.0113  0.0091  266  ARG B CB  
2713 C CG  . ARG B 41  ? 0.1901 0.2127 0.1764 -0.0184 0.0119  0.0071  266  ARG B CG  
2714 C CD  . ARG B 41  ? 0.1458 0.1677 0.1357 -0.0219 0.0137  0.0063  266  ARG B CD  
2715 N NE  . ARG B 41  ? 0.1620 0.1791 0.1500 -0.0233 0.0169  0.0084  266  ARG B NE  
2716 C CZ  . ARG B 41  ? 0.1674 0.1858 0.1555 -0.0248 0.0196  0.0097  266  ARG B CZ  
2717 N NH1 . ARG B 41  ? 0.1693 0.1940 0.1595 -0.0246 0.0197  0.0089  266  ARG B NH1 
2718 N NH2 . ARG B 41  ? 0.1889 0.2019 0.1750 -0.0263 0.0226  0.0119  266  ARG B NH2 
2719 N N   . CYS B 42  ? 0.1333 0.1407 0.1150 -0.0132 0.0111  0.0111  267  CYS B N   
2720 C CA  . CYS B 42  ? 0.1720 0.1761 0.1519 -0.0100 0.0110  0.0137  267  CYS B CA  
2721 C C   . CYS B 42  ? 0.1915 0.1878 0.1703 -0.0105 0.0143  0.0147  267  CYS B C   
2722 O O   . CYS B 42  ? 0.1943 0.1882 0.1747 -0.0132 0.0155  0.0122  267  CYS B O   
2723 C CB  . CYS B 42  ? 0.1697 0.1768 0.1519 -0.0083 0.0086  0.0125  267  CYS B CB  
2724 S SG  . CYS B 42  ? 0.1939 0.1996 0.1753 -0.0036 0.0082  0.0161  267  CYS B SG  
2725 N N   . THR B 43  ? 0.1649 0.1570 0.1407 -0.0081 0.0157  0.0184  268  THR B N   
2726 C CA  . THR B 43  ? 0.1613 0.1444 0.1356 -0.0081 0.0190  0.0197  268  THR B CA  
2727 C C   . THR B 43  ? 0.1525 0.1330 0.1281 -0.0054 0.0190  0.0193  268  THR B C   
2728 O O   . THR B 43  ? 0.1734 0.1595 0.1508 -0.0029 0.0164  0.0192  268  THR B O   
2729 C CB  . THR B 43  ? 0.1595 0.1384 0.1299 -0.0060 0.0208  0.0244  268  THR B CB  
2730 O OG1 . THR B 43  ? 0.2201 0.2011 0.1895 -0.0010 0.0188  0.0274  268  THR B OG1 
2731 C CG2 . THR B 43  ? 0.2311 0.2137 0.1996 -0.0079 0.0208  0.0251  268  THR B CG2 
2732 N N   . LEU B 44  ? 0.2120 0.1836 0.1864 -0.0060 0.0222  0.0190  269  LEU B N   
2733 C CA  . LEU B 44  ? 0.2095 0.1777 0.1846 -0.0030 0.0229  0.0184  269  LEU B CA  
2734 C C   . LEU B 44  ? 0.2052 0.1744 0.1800 0.0029  0.0223  0.0228  269  LEU B C   
2735 O O   . LEU B 44  ? 0.2304 0.2015 0.2074 0.0061  0.0218  0.0226  269  LEU B O   
2736 C CB  . LEU B 44  ? 0.2230 0.1799 0.1959 -0.0049 0.0269  0.0171  269  LEU B CB  
2737 C CG  . LEU B 44  ? 0.3364 0.2924 0.3097 -0.0113 0.0272  0.0127  269  LEU B CG  
2738 C CD1 . LEU B 44  ? 0.2572 0.2017 0.2280 -0.0131 0.0307  0.0106  269  LEU B CD1 
2739 C CD2 . LEU B 44  ? 0.2559 0.2212 0.2322 -0.0128 0.0239  0.0092  269  LEU B CD2 
2740 N N   . GLU B 45  ? 0.2043 0.1734 0.1769 0.0045  0.0223  0.0269  270  GLU B N   
2741 C CA  . GLU B 45  ? 0.2425 0.2145 0.2150 0.0100  0.0208  0.0313  270  GLU B CA  
2742 C C   . GLU B 45  ? 0.2437 0.2273 0.2185 0.0106  0.0162  0.0311  270  GLU B C   
2743 O O   . GLU B 45  ? 0.2747 0.2625 0.2496 0.0145  0.0142  0.0348  270  GLU B O   
2744 C CB  . GLU B 45  ? 0.3284 0.2949 0.2967 0.0115  0.0226  0.0361  270  GLU B CB  
2745 C CG  . GLU B 45  ? 0.4144 0.3681 0.3804 0.0112  0.0275  0.0365  270  GLU B CG  
2746 C CD  . GLU B 45  ? 0.7311 0.6781 0.6928 0.0135  0.0297  0.0420  270  GLU B CD  
2747 O OE1 . GLU B 45  ? 0.8019 0.7542 0.7614 0.0142  0.0276  0.0450  270  GLU B OE1 
2748 O OE2 . GLU B 45  ? 0.6066 0.5424 0.5664 0.0147  0.0336  0.0434  270  GLU B OE2 
2749 N N   . GLY B 46  ? 0.1925 0.1812 0.1691 0.0068  0.0144  0.0271  271  GLY B N   
2750 C CA  . GLY B 46  ? 0.1976 0.1959 0.1763 0.0070  0.0103  0.0263  271  GLY B CA  
2751 C C   . GLY B 46  ? 0.2712 0.2737 0.2471 0.0063  0.0080  0.0276  271  GLY B C   
2752 O O   . GLY B 46  ? 0.2495 0.2587 0.2260 0.0077  0.0046  0.0286  271  GLY B O   
2753 N N   . GLU B 47  ? 0.1936 0.1923 0.1661 0.0039  0.0099  0.0276  272  GLU B N   
2754 C CA  . GLU B 47  ? 0.2194 0.2216 0.1884 0.0031  0.0083  0.0284  272  GLU B CA  
2755 C C   . GLU B 47  ? 0.2148 0.2197 0.1849 -0.0008 0.0082  0.0243  272  GLU B C   
2756 O O   . GLU B 47  ? 0.1718 0.1733 0.1429 -0.0035 0.0109  0.0226  272  GLU B O   
2757 C CB  . GLU B 47  ? 0.2437 0.2405 0.2078 0.0039  0.0109  0.0322  272  GLU B CB  
2758 C CG  . GLU B 47  ? 0.3100 0.3037 0.2732 0.0084  0.0112  0.0367  272  GLU B CG  
2759 C CD  . GLU B 47  ? 0.3787 0.3710 0.3360 0.0103  0.0114  0.0413  272  GLU B CD  
2760 O OE1 . GLU B 47  ? 0.4650 0.4585 0.4186 0.0080  0.0116  0.0406  272  GLU B OE1 
2761 O OE2 . GLU B 47  ? 0.3899 0.3801 0.3462 0.0144  0.0114  0.0456  272  GLU B OE2 
2762 N N   . LEU B 48  ? 0.1835 0.1945 0.1534 -0.0011 0.0050  0.0229  273  LEU B N   
2763 C CA  . LEU B 48  ? 0.1948 0.2085 0.1659 -0.0039 0.0047  0.0192  273  LEU B CA  
2764 C C   . LEU B 48  ? 0.1838 0.1962 0.1512 -0.0053 0.0068  0.0196  273  LEU B C   
2765 O O   . LEU B 48  ? 0.1910 0.2023 0.1536 -0.0040 0.0071  0.0223  273  LEU B O   
2766 C CB  . LEU B 48  ? 0.1633 0.1826 0.1350 -0.0037 0.0009  0.0177  273  LEU B CB  
2767 C CG  . LEU B 48  ? 0.2029 0.2246 0.1787 -0.0026 -0.0011 0.0174  273  LEU B CG  
2768 C CD1 . LEU B 48  ? 0.2474 0.2744 0.2233 -0.0029 -0.0049 0.0162  273  LEU B CD1 
2769 C CD2 . LEU B 48  ? 0.1842 0.2047 0.1641 -0.0042 0.0004  0.0149  273  LEU B CD2 
2770 N N   . LEU B 49  ? 0.1630 0.1761 0.1329 -0.0080 0.0084  0.0169  274  LEU B N   
2771 C CA  . LEU B 49  ? 0.1597 0.1730 0.1273 -0.0094 0.0108  0.0169  274  LEU B CA  
2772 C C   . LEU B 49  ? 0.1582 0.1762 0.1269 -0.0100 0.0094  0.0139  274  LEU B C   
2773 O O   . LEU B 49  ? 0.1601 0.1806 0.1323 -0.0103 0.0073  0.0116  274  LEU B O   
2774 C CB  . LEU B 49  ? 0.1714 0.1819 0.1416 -0.0121 0.0143  0.0169  274  LEU B CB  
2775 C CG  . LEU B 49  ? 0.2024 0.2069 0.1730 -0.0121 0.0160  0.0188  274  LEU B CG  
2776 C CD1 . LEU B 49  ? 0.2607 0.2627 0.2341 -0.0158 0.0192  0.0179  274  LEU B CD1 
2777 C CD2 . LEU B 49  ? 0.1891 0.1897 0.1544 -0.0095 0.0167  0.0230  274  LEU B CD2 
2778 N N   . GLY B 50  ? 0.1556 0.1745 0.1209 -0.0101 0.0110  0.0141  275  GLY B N   
2779 C CA  . GLY B 50  ? 0.1461 0.1686 0.1124 -0.0104 0.0107  0.0112  275  GLY B CA  
2780 C C   . GLY B 50  ? 0.1721 0.1960 0.1366 -0.0090 0.0069  0.0096  275  GLY B C   
2781 O O   . GLY B 50  ? 0.1911 0.2140 0.1511 -0.0078 0.0049  0.0110  275  GLY B O   
2782 N N   . THR B 51  ? 0.1381 0.1643 0.1060 -0.0095 0.0059  0.0069  276  THR B N   
2783 C CA  . THR B 51  ? 0.1481 0.1749 0.1148 -0.0088 0.0025  0.0052  276  THR B CA  
2784 C C   . THR B 51  ? 0.1516 0.1793 0.1226 -0.0091 -0.0001 0.0051  276  THR B C   
2785 O O   . THR B 51  ? 0.1611 0.1897 0.1326 -0.0091 -0.0027 0.0037  276  THR B O   
2786 C CB  . THR B 51  ? 0.1508 0.1789 0.1182 -0.0086 0.0030  0.0025  276  THR B CB  
2787 O OG1 . THR B 51  ? 0.1488 0.1792 0.1224 -0.0094 0.0046  0.0019  276  THR B OG1 
2788 C CG2 . THR B 51  ? 0.1460 0.1730 0.1077 -0.0076 0.0055  0.0024  276  THR B CG2 
2789 N N   . THR B 52  ? 0.1403 0.1672 0.1142 -0.0095 0.0009  0.0066  277  THR B N   
2790 C CA  . THR B 52  ? 0.1484 0.1760 0.1263 -0.0097 -0.0008 0.0064  277  THR B CA  
2791 C C   . THR B 52  ? 0.1215 0.1501 0.0979 -0.0086 -0.0039 0.0071  277  THR B C   
2792 O O   . THR B 52  ? 0.1838 0.2117 0.1572 -0.0074 -0.0043 0.0093  277  THR B O   
2793 C CB  . THR B 52  ? 0.1436 0.1686 0.1230 -0.0099 0.0012  0.0079  277  THR B CB  
2794 O OG1 . THR B 52  ? 0.1315 0.1560 0.1123 -0.0116 0.0039  0.0072  277  THR B OG1 
2795 C CG2 . THR B 52  ? 0.1503 0.1757 0.1332 -0.0098 0.0001  0.0074  277  THR B CG2 
2796 N N   . PRO B 53  ? 0.1641 0.1947 0.1429 -0.0090 -0.0061 0.0056  278  PRO B N   
2797 C CA  . PRO B 53  ? 0.1907 0.2231 0.1690 -0.0086 -0.0091 0.0063  278  PRO B CA  
2798 C C   . PRO B 53  ? 0.1667 0.2003 0.1481 -0.0076 -0.0094 0.0084  278  PRO B C   
2799 O O   . PRO B 53  ? 0.1965 0.2293 0.1811 -0.0076 -0.0078 0.0082  278  PRO B O   
2800 C CB  . PRO B 53  ? 0.1873 0.2209 0.1674 -0.0099 -0.0107 0.0040  278  PRO B CB  
2801 C CG  . PRO B 53  ? 0.1933 0.2263 0.1764 -0.0103 -0.0087 0.0029  278  PRO B CG  
2802 C CD  . PRO B 53  ? 0.1732 0.2045 0.1547 -0.0101 -0.0059 0.0033  278  PRO B CD  
2803 N N   . ARG B 54  ? 0.1760 0.2115 0.1561 -0.0065 -0.0115 0.0103  279  ARG B N   
2804 C CA  . ARG B 54  ? 0.1905 0.2281 0.1741 -0.0049 -0.0118 0.0127  279  ARG B CA  
2805 C C   . ARG B 54  ? 0.2147 0.2553 0.2031 -0.0057 -0.0129 0.0116  279  ARG B C   
2806 O O   . ARG B 54  ? 0.1873 0.2281 0.1792 -0.0045 -0.0114 0.0124  279  ARG B O   
2807 C CB  . ARG B 54  ? 0.2167 0.2571 0.1981 -0.0035 -0.0144 0.0153  279  ARG B CB  
2808 C CG  . ARG B 54  ? 0.3346 0.3771 0.3193 -0.0009 -0.0143 0.0184  279  ARG B CG  
2809 C CD  . ARG B 54  ? 0.3078 0.3523 0.2893 0.0010  -0.0163 0.0217  279  ARG B CD  
2810 N NE  . ARG B 54  ? 0.3589 0.4051 0.3441 0.0043  -0.0156 0.0251  279  ARG B NE  
2811 C CZ  . ARG B 54  ? 0.3146 0.3559 0.2989 0.0068  -0.0123 0.0272  279  ARG B CZ  
2812 N NH1 . ARG B 54  ? 0.4389 0.4740 0.4185 0.0060  -0.0098 0.0267  279  ARG B NH1 
2813 N NH2 . ARG B 54  ? 0.4205 0.4628 0.4086 0.0101  -0.0114 0.0300  279  ARG B NH2 
2814 N N   . ASN B 55  ? 0.1393 0.1816 0.1276 -0.0076 -0.0151 0.0098  280  ASN B N   
2815 C CA  . ASN B 55  ? 0.1487 0.1934 0.1411 -0.0089 -0.0159 0.0089  280  ASN B CA  
2816 C C   . ASN B 55  ? 0.1429 0.1845 0.1355 -0.0098 -0.0139 0.0067  280  ASN B C   
2817 O O   . ASN B 55  ? 0.1579 0.1972 0.1477 -0.0107 -0.0138 0.0050  280  ASN B O   
2818 C CB  . ASN B 55  ? 0.1551 0.2022 0.1469 -0.0109 -0.0192 0.0081  280  ASN B CB  
2819 C CG  . ASN B 55  ? 0.1630 0.2129 0.1593 -0.0124 -0.0200 0.0078  280  ASN B CG  
2820 O OD1 . ASN B 55  ? 0.1748 0.2234 0.1731 -0.0124 -0.0181 0.0071  280  ASN B OD1 
2821 N ND2 . ASN B 55  ? 0.1223 0.1760 0.1200 -0.0140 -0.0230 0.0084  280  ASN B ND2 
2822 N N   . ALA B 56  ? 0.1342 0.1760 0.1299 -0.0094 -0.0123 0.0068  281  ALA B N   
2823 C CA  . ALA B 56  ? 0.1729 0.2127 0.1688 -0.0103 -0.0108 0.0049  281  ALA B CA  
2824 C C   . ALA B 56  ? 0.1961 0.2359 0.1915 -0.0118 -0.0122 0.0033  281  ALA B C   
2825 O O   . ALA B 56  ? 0.1817 0.2198 0.1761 -0.0122 -0.0114 0.0020  281  ALA B O   
2826 C CB  . ALA B 56  ? 0.1559 0.1964 0.1545 -0.0099 -0.0094 0.0051  281  ALA B CB  
2827 N N   A SER B 57  ? 0.1460 0.1878 0.1424 -0.0127 -0.0143 0.0037  282  SER B N   
2828 N N   B SER B 57  ? 0.1456 0.1873 0.1418 -0.0127 -0.0143 0.0037  282  SER B N   
2829 C CA  A SER B 57  ? 0.1414 0.1820 0.1373 -0.0142 -0.0153 0.0024  282  SER B CA  
2830 C CA  B SER B 57  ? 0.1375 0.1780 0.1331 -0.0142 -0.0155 0.0023  282  SER B CA  
2831 C C   A SER B 57  ? 0.1650 0.2031 0.1571 -0.0147 -0.0164 0.0010  282  SER B C   
2832 C C   B SER B 57  ? 0.1516 0.1897 0.1431 -0.0147 -0.0166 0.0011  282  SER B C   
2833 O O   A SER B 57  ? 0.1837 0.2198 0.1749 -0.0158 -0.0172 -0.0002 282  SER B O   
2834 O O   B SER B 57  ? 0.1371 0.1733 0.1276 -0.0159 -0.0176 -0.0002 282  SER B O   
2835 C CB  A SER B 57  ? 0.1576 0.2010 0.1565 -0.0156 -0.0168 0.0033  282  SER B CB  
2836 C CB  B SER B 57  ? 0.1689 0.2120 0.1673 -0.0156 -0.0170 0.0032  282  SER B CB  
2837 O OG  A SER B 57  ? 0.1388 0.1851 0.1383 -0.0160 -0.0187 0.0044  282  SER B OG  
2838 O OG  B SER B 57  ? 0.1839 0.2287 0.1853 -0.0151 -0.0154 0.0040  282  SER B OG  
2839 N N   A TRP B 58  ? 0.1476 0.1851 0.1369 -0.0139 -0.0162 0.0012  283  TRP B N   
2840 N N   B TRP B 58  ? 0.1378 0.1754 0.1267 -0.0137 -0.0161 0.0013  283  TRP B N   
2841 C CA  A TRP B 58  ? 0.1208 0.1554 0.1055 -0.0140 -0.0164 -0.0004 283  TRP B CA  
2842 C CA  B TRP B 58  ? 0.1300 0.1647 0.1142 -0.0137 -0.0162 -0.0002 283  TRP B CA  
2843 C C   A TRP B 58  ? 0.1155 0.1481 0.0995 -0.0129 -0.0139 -0.0014 283  TRP B C   
2844 C C   B TRP B 58  ? 0.1174 0.1500 0.1012 -0.0128 -0.0138 -0.0013 283  TRP B C   
2845 O O   A TRP B 58  ? 0.1396 0.1697 0.1200 -0.0126 -0.0134 -0.0028 283  TRP B O   
2846 O O   B TRP B 58  ? 0.1398 0.1699 0.1203 -0.0126 -0.0134 -0.0028 283  TRP B O   
2847 C CB  A TRP B 58  ? 0.1807 0.2158 0.1618 -0.0136 -0.0173 0.0004  283  TRP B CB  
2848 C CB  B TRP B 58  ? 0.1496 0.1846 0.1303 -0.0130 -0.0165 0.0009  283  TRP B CB  
2849 C CG  A TRP B 58  ? 0.1332 0.1694 0.1129 -0.0153 -0.0206 0.0002  283  TRP B CG  
2850 C CG  B TRP B 58  ? 0.1923 0.2300 0.1726 -0.0138 -0.0196 0.0019  283  TRP B CG  
2851 C CD1 A TRP B 58  ? 0.1599 0.2006 0.1423 -0.0159 -0.0228 0.0021  283  TRP B CD1 
2852 C CD1 B TRP B 58  ? 0.1931 0.2319 0.1744 -0.0159 -0.0221 0.0012  283  TRP B CD1 
2853 C CD2 A TRP B 58  ? 0.1768 0.2099 0.1525 -0.0170 -0.0220 -0.0021 283  TRP B CD2 
2854 C CD2 B TRP B 58  ? 0.2843 0.3243 0.2633 -0.0128 -0.0205 0.0041  283  TRP B CD2 
2855 N NE1 A TRP B 58  ? 0.1774 0.2185 0.1579 -0.0182 -0.0258 0.0011  283  TRP B NE1 
2856 N NE1 B TRP B 58  ? 0.2319 0.2745 0.2131 -0.0165 -0.0248 0.0027  283  TRP B NE1 
2857 C CE2 A TRP B 58  ? 0.1579 0.1937 0.1337 -0.0191 -0.0254 -0.0017 283  TRP B CE2 
2858 C CE2 B TRP B 58  ? 0.2193 0.2628 0.1990 -0.0142 -0.0240 0.0046  283  TRP B CE2 
2859 C CE3 A TRP B 58  ? 0.2495 0.2776 0.2213 -0.0168 -0.0207 -0.0046 283  TRP B CE3 
2860 C CE3 B TRP B 58  ? 0.1553 0.1947 0.1326 -0.0108 -0.0187 0.0059  283  TRP B CE3 
2861 C CZ2 A TRP B 58  ? 0.2599 0.2928 0.2316 -0.0215 -0.0277 -0.0040 283  TRP B CZ2 
2862 C CZ2 B TRP B 58  ? 0.2193 0.2667 0.1984 -0.0134 -0.0260 0.0070  283  TRP B CZ2 
2863 C CZ3 A TRP B 58  ? 0.2128 0.2374 0.1802 -0.0186 -0.0225 -0.0068 283  TRP B CZ3 
2864 C CZ3 B TRP B 58  ? 0.3238 0.3659 0.2999 -0.0097 -0.0204 0.0085  283  TRP B CZ3 
2865 C CH2 A TRP B 58  ? 0.2705 0.2971 0.2376 -0.0213 -0.0260 -0.0067 283  TRP B CH2 
2866 C CH2 B TRP B 58  ? 0.2611 0.3076 0.2382 -0.0109 -0.0242 0.0090  283  TRP B CH2 
2867 N N   . LEU B 59  ? 0.1367 0.1705 0.1238 -0.0124 -0.0122 -0.0008 284  LEU B N   
2868 C CA  . LEU B 59  ? 0.1328 0.1661 0.1205 -0.0118 -0.0103 -0.0016 284  LEU B CA  
2869 C C   . LEU B 59  ? 0.1407 0.1727 0.1284 -0.0117 -0.0107 -0.0029 284  LEU B C   
2870 O O   . LEU B 59  ? 0.1500 0.1821 0.1394 -0.0124 -0.0120 -0.0027 284  LEU B O   
2871 C CB  . LEU B 59  ? 0.1138 0.1489 0.1049 -0.0120 -0.0091 -0.0011 284  LEU B CB  
2872 C CG  . LEU B 59  ? 0.1186 0.1546 0.1111 -0.0119 -0.0075 -0.0017 284  LEU B CG  
2873 C CD1 . LEU B 59  ? 0.1341 0.1696 0.1248 -0.0116 -0.0057 -0.0017 284  LEU B CD1 
2874 C CD2 . LEU B 59  ? 0.1398 0.1773 0.1350 -0.0128 -0.0070 -0.0016 284  LEU B CD2 
2875 N N   . ASN B 60  ? 0.1534 0.1840 0.1392 -0.0107 -0.0094 -0.0039 285  ASN B N   
2876 C CA  . ASN B 60  ? 0.1277 0.1562 0.1132 -0.0098 -0.0093 -0.0050 285  ASN B CA  
2877 C C   . ASN B 60  ? 0.1718 0.1965 0.1543 -0.0107 -0.0112 -0.0060 285  ASN B C   
2878 O O   . ASN B 60  ? 0.2290 0.2509 0.2113 -0.0102 -0.0113 -0.0066 285  ASN B O   
2879 C CB  . ASN B 60  ? 0.1252 0.1559 0.1149 -0.0095 -0.0094 -0.0043 285  ASN B CB  
2880 C CG  . ASN B 60  ? 0.1796 0.2135 0.1719 -0.0084 -0.0076 -0.0042 285  ASN B CG  
2881 O OD1 . ASN B 60  ? 0.2024 0.2372 0.1940 -0.0082 -0.0060 -0.0043 285  ASN B OD1 
2882 N ND2 . ASN B 60  ? 0.1753 0.2114 0.1708 -0.0078 -0.0079 -0.0036 285  ASN B ND2 
2883 N N   . ARG B 61  ? 0.1310 0.1555 0.1111 -0.0120 -0.0127 -0.0059 286  ARG B N   
2884 C CA  . ARG B 61  ? 0.1340 0.1550 0.1107 -0.0135 -0.0147 -0.0071 286  ARG B CA  
2885 C C   . ARG B 61  ? 0.1938 0.2120 0.1644 -0.0131 -0.0143 -0.0087 286  ARG B C   
2886 O O   . ARG B 61  ? 0.1985 0.2184 0.1677 -0.0121 -0.0129 -0.0082 286  ARG B O   
2887 C CB  . ARG B 61  ? 0.1427 0.1665 0.1212 -0.0157 -0.0172 -0.0059 286  ARG B CB  
2888 C CG  . ARG B 61  ? 0.3075 0.3346 0.2915 -0.0162 -0.0174 -0.0041 286  ARG B CG  
2889 C CD  . ARG B 61  ? 0.3926 0.4187 0.3789 -0.0153 -0.0161 -0.0040 286  ARG B CD  
2890 N NE  . ARG B 61  ? 0.3231 0.3515 0.3130 -0.0164 -0.0167 -0.0025 286  ARG B NE  
2891 C CZ  . ARG B 61  ? 0.4912 0.5231 0.4841 -0.0158 -0.0159 -0.0013 286  ARG B CZ  
2892 N NH1 . ARG B 61  ? 0.3131 0.3465 0.3062 -0.0145 -0.0145 -0.0013 286  ARG B NH1 
2893 N NH2 . ARG B 61  ? 0.4368 0.4705 0.4323 -0.0168 -0.0162 0.0000  286  ARG B NH2 
2894 N N   . PHE B 62  ? 0.1675 0.1808 0.1337 -0.0142 -0.0154 -0.0108 287  PHE B N   
2895 C CA  . PHE B 62  ? 0.1661 0.1761 0.1252 -0.0140 -0.0151 -0.0127 287  PHE B CA  
2896 C C   . PHE B 62  ? 0.1954 0.2017 0.1504 -0.0169 -0.0181 -0.0146 287  PHE B C   
2897 O O   . PHE B 62  ? 0.1812 0.1860 0.1388 -0.0188 -0.0196 -0.0146 287  PHE B O   
2898 C CB  . PHE B 62  ? 0.1785 0.1846 0.1352 -0.0111 -0.0117 -0.0143 287  PHE B CB  
2899 C CG  . PHE B 62  ? 0.1684 0.1698 0.1260 -0.0106 -0.0111 -0.0155 287  PHE B CG  
2900 C CD1 . PHE B 62  ? 0.1973 0.1913 0.1491 -0.0117 -0.0119 -0.0182 287  PHE B CD1 
2901 C CD2 . PHE B 62  ? 0.1736 0.1774 0.1375 -0.0089 -0.0099 -0.0139 287  PHE B CD2 
2902 C CE1 . PHE B 62  ? 0.1897 0.1781 0.1421 -0.0110 -0.0111 -0.0190 287  PHE B CE1 
2903 C CE2 . PHE B 62  ? 0.2161 0.2154 0.1807 -0.0080 -0.0094 -0.0144 287  PHE B CE2 
2904 C CZ  . PHE B 62  ? 0.1987 0.1900 0.1577 -0.0089 -0.0098 -0.0168 287  PHE B CZ  
2905 N N   . ARG B 63  ? 0.1922 0.1968 0.1403 -0.0176 -0.0191 -0.0160 288  ARG B N   
2906 C CA  . ARG B 63  ? 0.1653 0.1658 0.1084 -0.0209 -0.0220 -0.0184 288  ARG B CA  
2907 C C   . ARG B 63  ? 0.1885 0.1843 0.1219 -0.0203 -0.0213 -0.0212 288  ARG B C   
2908 O O   . ARG B 63  ? 0.2141 0.2119 0.1451 -0.0179 -0.0192 -0.0203 288  ARG B O   
2909 C CB  . ARG B 63  ? 0.2438 0.2502 0.1899 -0.0240 -0.0262 -0.0166 288  ARG B CB  
2910 C CG  . ARG B 63  ? 0.2823 0.2942 0.2268 -0.0233 -0.0272 -0.0147 288  ARG B CG  
2911 C CD  . ARG B 63  ? 0.2857 0.3039 0.2339 -0.0261 -0.0315 -0.0129 288  ARG B CD  
2912 N NE  . ARG B 63  ? 0.3878 0.4034 0.3317 -0.0302 -0.0350 -0.0154 288  ARG B NE  
2913 C CZ  . ARG B 63  ? 0.5345 0.5557 0.4808 -0.0334 -0.0393 -0.0143 288  ARG B CZ  
2914 N NH1 . ARG B 63  ? 0.4695 0.4993 0.4229 -0.0325 -0.0402 -0.0105 288  ARG B NH1 
2915 N NH2 . ARG B 63  ? 0.6270 0.6453 0.5688 -0.0377 -0.0426 -0.0171 288  ARG B NH2 
2916 N N   . GLY B 64  ? 0.2063 0.1952 0.1336 -0.0226 -0.0226 -0.0246 289  GLY B N   
2917 C CA  . GLY B 64  ? 0.1855 0.1686 0.1023 -0.0221 -0.0216 -0.0278 289  GLY B CA  
2918 C C   . GLY B 64  ? 0.1979 0.1730 0.1084 -0.0257 -0.0239 -0.0317 289  GLY B C   
2919 O O   . GLY B 64  ? 0.2288 0.2046 0.1433 -0.0294 -0.0271 -0.0314 289  GLY B O   
2920 N N   . VAL B 65  ? 0.2152 0.1825 0.1157 -0.0248 -0.0220 -0.0355 290  VAL B N   
2921 C CA  . VAL B 65  ? 0.2479 0.2057 0.1405 -0.0283 -0.0238 -0.0401 290  VAL B CA  
2922 C C   . VAL B 65  ? 0.2698 0.2171 0.1565 -0.0247 -0.0187 -0.0433 290  VAL B C   
2923 O O   . VAL B 65  ? 0.2347 0.1825 0.1185 -0.0204 -0.0147 -0.0432 290  VAL B O   
2924 C CB  . VAL B 65  ? 0.2315 0.1901 0.1150 -0.0321 -0.0279 -0.0421 290  VAL B CB  
2925 C CG1 . VAL B 65  ? 0.2427 0.2015 0.1182 -0.0286 -0.0251 -0.0426 290  VAL B CG1 
2926 C CG2 . VAL B 65  ? 0.2542 0.2027 0.1296 -0.0367 -0.0302 -0.0471 290  VAL B CG2 
2927 N N   . SER B 66  ? 0.2455 0.1834 0.1309 -0.0262 -0.0184 -0.0460 291  SER B N   
2928 C CA  . SER B 66  ? 0.2490 0.1760 0.1287 -0.0223 -0.0134 -0.0491 291  SER B CA  
2929 C C   . SER B 66  ? 0.2988 0.2194 0.1650 -0.0222 -0.0124 -0.0536 291  SER B C   
2930 O O   . SER B 66  ? 0.2937 0.2120 0.1524 -0.0273 -0.0165 -0.0564 291  SER B O   
2931 C CB  . SER B 66  ? 0.2557 0.1727 0.1359 -0.0243 -0.0136 -0.0509 291  SER B CB  
2932 O OG  . SER B 66  ? 0.2661 0.1779 0.1398 -0.0308 -0.0181 -0.0542 291  SER B OG  
2933 N N   . THR B 67  ? 0.3164 0.2345 0.1792 -0.0165 -0.0068 -0.0543 292  THR B N   
2934 C CA  . THR B 67  ? 0.3934 0.3048 0.2426 -0.0156 -0.0047 -0.0586 292  THR B CA  
2935 C C   . THR B 67  ? 0.4059 0.3016 0.2462 -0.0153 -0.0022 -0.0641 292  THR B C   
2936 O O   . THR B 67  ? 0.4409 0.3287 0.2679 -0.0165 -0.0018 -0.0689 292  THR B O   
2937 C CB  . THR B 67  ? 0.3750 0.2918 0.2251 -0.0096 0.0008  -0.0566 292  THR B CB  
2938 O OG1 . THR B 67  ? 0.5384 0.4499 0.3917 -0.0041 0.0064  -0.0569 292  THR B OG1 
2939 C CG2 . THR B 67  ? 0.4309 0.3617 0.2924 -0.0092 -0.0007 -0.0507 292  THR B CG2 
2940 N N   . ALA B 68  ? 0.4016 0.2922 0.2484 -0.0138 -0.0005 -0.0634 293  ALA B N   
2941 C CA  . ALA B 68  ? 0.3366 0.2112 0.1759 -0.0133 0.0020  -0.0681 293  ALA B CA  
2942 C C   . ALA B 68  ? 0.3955 0.2677 0.2437 -0.0152 0.0002  -0.0660 293  ALA B C   
2943 O O   . ALA B 68  ? 0.4040 0.2870 0.2644 -0.0148 -0.0013 -0.0608 293  ALA B O   
2944 C CB  . ALA B 68  ? 0.3550 0.2242 0.1912 -0.0055 0.0095  -0.0693 293  ALA B CB  
2945 N N   . ALA B 69  ? 0.3984 0.2557 0.2399 -0.0173 0.0006  -0.0701 294  ALA B N   
2946 C CA  . ALA B 69  ? 0.4162 0.2692 0.2653 -0.0182 0.0001  -0.0679 294  ALA B CA  
2947 C C   . ALA B 69  ? 0.3948 0.2503 0.2524 -0.0101 0.0053  -0.0640 294  ALA B C   
2948 O O   . ALA B 69  ? 0.3932 0.2475 0.2479 -0.0037 0.0104  -0.0648 294  ALA B O   
2949 C CB  . ALA B 69  ? 0.4932 0.3279 0.3324 -0.0216 0.0003  -0.0733 294  ALA B CB  
2950 N N   . VAL B 70  ? 0.3586 0.2184 0.2270 -0.0104 0.0039  -0.0594 295  VAL B N   
2951 C CA  . VAL B 70  ? 0.3179 0.1808 0.1949 -0.0033 0.0080  -0.0553 295  VAL B CA  
2952 C C   . VAL B 70  ? 0.3953 0.2428 0.2658 0.0019  0.0134  -0.0582 295  VAL B C   
2953 O O   . VAL B 70  ? 0.4255 0.2581 0.2883 -0.0012 0.0131  -0.0619 295  VAL B O   
2954 C CB  . VAL B 70  ? 0.3175 0.1861 0.2053 -0.0053 0.0052  -0.0503 295  VAL B CB  
2955 C CG1 . VAL B 70  ? 0.3712 0.2395 0.2658 0.0017  0.0091  -0.0466 295  VAL B CG1 
2956 C CG2 . VAL B 70  ? 0.3597 0.2449 0.2551 -0.0082 0.0012  -0.0468 295  VAL B CG2 
2957 N N   . ALA B 71  ? 0.3542 0.2052 0.2279 0.0099  0.0184  -0.0565 296  ALA B N   
2958 C CA  . ALA B 71  ? 0.4223 0.2602 0.2914 0.0163  0.0242  -0.0585 296  ALA B CA  
2959 C C   . ALA B 71  ? 0.4165 0.2643 0.2959 0.0246  0.0281  -0.0535 296  ALA B C   
2960 O O   . ALA B 71  ? 0.3564 0.2185 0.2412 0.0261  0.0282  -0.0513 296  ALA B O   
2961 C CB  . ALA B 71  ? 0.4558 0.2837 0.3112 0.0171  0.0274  -0.0648 296  ALA B CB  
2962 N N   . ASN B 72  ? 0.3824 0.2225 0.2647 0.0298  0.0312  -0.0517 297  ASN B N   
2963 C CA  . ASN B 72  ? 0.3584 0.2073 0.2505 0.0381  0.0348  -0.0470 297  ASN B CA  
2964 C C   . ASN B 72  ? 0.3007 0.1687 0.2050 0.0365  0.0311  -0.0415 297  ASN B C   
2965 O O   . ASN B 72  ? 0.3528 0.2333 0.2637 0.0408  0.0331  -0.0390 297  ASN B O   
2966 C CB  . ASN B 72  ? 0.4026 0.2518 0.2910 0.0446  0.0408  -0.0493 297  ASN B CB  
2967 C CG  . ASN B 72  ? 0.7316 0.5615 0.6061 0.0457  0.0446  -0.0556 297  ASN B CG  
2968 O OD1 . ASN B 72  ? 0.8200 0.6353 0.6912 0.0470  0.0459  -0.0564 297  ASN B OD1 
2969 N ND2 . ASN B 72  ? 0.6820 0.5110 0.5475 0.0448  0.0463  -0.0601 297  ASN B ND2 
2970 N N   . GLN B 73  ? 0.3032 0.1733 0.2102 0.0299  0.0257  -0.0399 298  GLN B N   
2971 C CA  . GLN B 73  ? 0.3079 0.1941 0.2254 0.0278  0.0220  -0.0351 298  GLN B CA  
2972 C C   . GLN B 73  ? 0.3208 0.2198 0.2396 0.0264  0.0213  -0.0355 298  GLN B C   
2973 O O   . GLN B 73  ? 0.2689 0.1819 0.1968 0.0273  0.0203  -0.0316 298  GLN B O   
2974 C CB  . GLN B 73  ? 0.3279 0.2206 0.2554 0.0339  0.0235  -0.0297 298  GLN B CB  
2975 C CG  . GLN B 73  ? 0.3067 0.1868 0.2331 0.0356  0.0242  -0.0284 298  GLN B CG  
2976 C CD  . GLN B 73  ? 0.5681 0.4566 0.5047 0.0392  0.0234  -0.0222 298  GLN B CD  
2977 O OE1 . GLN B 73  ? 0.5008 0.4039 0.4453 0.0420  0.0234  -0.0192 298  GLN B OE1 
2978 N NE2 . GLN B 73  ? 0.9413 0.8206 0.8775 0.0388  0.0227  -0.0202 298  GLN B NE2 
2979 N N   . VAL B 74  ? 0.2971 0.1912 0.2065 0.0239  0.0217  -0.0401 299  VAL B N   
2980 C CA  . VAL B 74  ? 0.2785 0.1833 0.1877 0.0222  0.0210  -0.0404 299  VAL B CA  
2981 C C   . VAL B 74  ? 0.2833 0.1867 0.1869 0.0143  0.0160  -0.0427 299  VAL B C   
2982 O O   . VAL B 74  ? 0.3068 0.1979 0.2011 0.0112  0.0152  -0.0469 299  VAL B O   
2983 C CB  . VAL B 74  ? 0.3176 0.2195 0.2203 0.0269  0.0263  -0.0434 299  VAL B CB  
2984 C CG1 . VAL B 74  ? 0.3024 0.2135 0.2030 0.0242  0.0253  -0.0439 299  VAL B CG1 
2985 C CG2 . VAL B 74  ? 0.3110 0.2173 0.2212 0.0349  0.0312  -0.0405 299  VAL B CG2 
2986 N N   . LEU B 75  ? 0.2749 0.1909 0.1842 0.0112  0.0127  -0.0400 300  LEU B N   
2987 C CA  . LEU B 75  ? 0.2642 0.1821 0.1697 0.0045  0.0080  -0.0413 300  LEU B CA  
2988 C C   . LEU B 75  ? 0.2671 0.1949 0.1723 0.0049  0.0084  -0.0407 300  LEU B C   
2989 O O   . LEU B 75  ? 0.2538 0.1927 0.1677 0.0067  0.0088  -0.0368 300  LEU B O   
2990 C CB  . LEU B 75  ? 0.2408 0.1643 0.1541 0.0003  0.0034  -0.0380 300  LEU B CB  
2991 C CG  . LEU B 75  ? 0.2573 0.1868 0.1702 -0.0059 -0.0016 -0.0379 300  LEU B CG  
2992 C CD1 . LEU B 75  ? 0.2923 0.2125 0.1946 -0.0105 -0.0037 -0.0426 300  LEU B CD1 
2993 C CD2 . LEU B 75  ? 0.2117 0.1469 0.1332 -0.0089 -0.0049 -0.0343 300  LEU B CD2 
2994 N N   A HIS B 76  ? 0.2662 0.1898 0.1612 0.0033  0.0084  -0.0443 301  HIS B N   
2995 N N   B HIS B 76  ? 0.2649 0.1882 0.1597 0.0032  0.0084  -0.0444 301  HIS B N   
2996 C CA  A HIS B 76  ? 0.2580 0.1905 0.1520 0.0032  0.0087  -0.0433 301  HIS B CA  
2997 C CA  B HIS B 76  ? 0.2641 0.1955 0.1569 0.0029  0.0085  -0.0438 301  HIS B CA  
2998 C C   A HIS B 76  ? 0.2411 0.1777 0.1336 -0.0029 0.0029  -0.0430 301  HIS B C   
2999 C C   B HIS B 76  ? 0.2411 0.1776 0.1339 -0.0031 0.0026  -0.0429 301  HIS B C   
3000 O O   A HIS B 76  ? 0.2487 0.1782 0.1337 -0.0070 -0.0001 -0.0462 301  HIS B O   
3001 O O   B HIS B 76  ? 0.2580 0.1882 0.1448 -0.0076 -0.0008 -0.0457 301  HIS B O   
3002 C CB  A HIS B 76  ? 0.3324 0.2594 0.2159 0.0061  0.0129  -0.0468 301  HIS B CB  
3003 C CB  B HIS B 76  ? 0.2993 0.2231 0.1797 0.0046  0.0119  -0.0481 301  HIS B CB  
3004 C CG  A HIS B 76  ? 0.3346 0.2713 0.2185 0.0072  0.0143  -0.0447 301  HIS B CG  
3005 C CG  B HIS B 76  ? 0.3183 0.2376 0.1982 0.0113  0.0183  -0.0491 301  HIS B CG  
3006 N ND1 A HIS B 76  ? 0.4080 0.3484 0.2871 0.0031  0.0108  -0.0447 301  HIS B ND1 
3007 N ND1 B HIS B 76  ? 0.3158 0.2427 0.1989 0.0158  0.0228  -0.0470 301  HIS B ND1 
3008 C CD2 A HIS B 76  ? 0.3744 0.3183 0.2637 0.0117  0.0188  -0.0422 301  HIS B CD2 
3009 C CD2 B HIS B 76  ? 0.3325 0.2403 0.2089 0.0142  0.0213  -0.0518 301  HIS B CD2 
3010 C CE1 A HIS B 76  ? 0.2601 0.2084 0.1409 0.0052  0.0133  -0.0422 301  HIS B CE1 
3011 C CE1 B HIS B 76  ? 0.2636 0.1851 0.1460 0.0215  0.0282  -0.0483 301  HIS B CE1 
3012 N NE2 A HIS B 76  ? 0.4030 0.3537 0.2901 0.0101  0.0182  -0.0407 301  HIS B NE2 
3013 N NE2 B HIS B 76  ? 0.3191 0.2285 0.1972 0.0209  0.0275  -0.0511 301  HIS B NE2 
3014 N N   . LEU B 77  ? 0.2194 0.1676 0.1193 -0.0033 0.0015  -0.0390 302  LEU B N   
3015 C CA  . LEU B 77  ? 0.2454 0.1994 0.1459 -0.0081 -0.0036 -0.0376 302  LEU B CA  
3016 C C   . LEU B 77  ? 0.3152 0.2746 0.2116 -0.0075 -0.0029 -0.0368 302  LEU B C   
3017 O O   . LEU B 77  ? 0.3001 0.2651 0.2006 -0.0041 0.0006  -0.0345 302  LEU B O   
3018 C CB  . LEU B 77  ? 0.2495 0.2119 0.1618 -0.0091 -0.0058 -0.0334 302  LEU B CB  
3019 C CG  . LEU B 77  ? 0.3184 0.2777 0.2355 -0.0111 -0.0079 -0.0330 302  LEU B CG  
3020 C CD1 . LEU B 77  ? 0.3224 0.2914 0.2500 -0.0117 -0.0096 -0.0287 302  LEU B CD1 
3021 C CD2 . LEU B 77  ? 0.3442 0.2974 0.2552 -0.0162 -0.0118 -0.0359 302  LEU B CD2 
3022 N N   . THR B 78  ? 0.2399 0.1980 0.1284 -0.0111 -0.0064 -0.0386 303  THR B N   
3023 C CA  . THR B 78  ? 0.2187 0.1835 0.1045 -0.0113 -0.0071 -0.0365 303  THR B CA  
3024 C C   . THR B 78  ? 0.2158 0.1899 0.1111 -0.0133 -0.0108 -0.0323 303  THR B C   
3025 O O   . THR B 78  ? 0.2296 0.2041 0.1279 -0.0168 -0.0150 -0.0323 303  THR B O   
3026 C CB  . THR B 78  ? 0.2475 0.2077 0.1207 -0.0142 -0.0098 -0.0399 303  THR B CB  
3027 O OG1 . THR B 78  ? 0.3115 0.2626 0.1749 -0.0117 -0.0056 -0.0440 303  THR B OG1 
3028 C CG2 . THR B 78  ? 0.2646 0.2322 0.1352 -0.0146 -0.0115 -0.0370 303  THR B CG2 
3029 N N   . LEU B 79  ? 0.2128 0.1941 0.1131 -0.0112 -0.0089 -0.0286 304  LEU B N   
3030 C CA  . LEU B 79  ? 0.2038 0.1928 0.1139 -0.0122 -0.0113 -0.0247 304  LEU B CA  
3031 C C   . LEU B 79  ? 0.1856 0.1793 0.0937 -0.0148 -0.0155 -0.0229 304  LEU B C   
3032 O O   . LEU B 79  ? 0.2036 0.1970 0.1036 -0.0146 -0.0157 -0.0231 304  LEU B O   
3033 C CB  . LEU B 79  ? 0.1981 0.1923 0.1151 -0.0091 -0.0073 -0.0216 304  LEU B CB  
3034 C CG  . LEU B 79  ? 0.2527 0.2451 0.1750 -0.0066 -0.0040 -0.0222 304  LEU B CG  
3035 C CD1 . LEU B 79  ? 0.2257 0.2234 0.1531 -0.0038 0.0001  -0.0197 304  LEU B CD1 
3036 C CD2 . LEU B 79  ? 0.2030 0.1964 0.1330 -0.0082 -0.0066 -0.0215 304  LEU B CD2 
3037 N N   . TYR B 80  ? 0.1842 0.1825 0.0997 -0.0168 -0.0189 -0.0208 305  TYR B N   
3038 C CA  . TYR B 80  ? 0.1742 0.1789 0.0912 -0.0183 -0.0226 -0.0179 305  TYR B CA  
3039 C C   . TYR B 80  ? 0.2030 0.2138 0.1291 -0.0164 -0.0210 -0.0138 305  TYR B C   
3040 O O   . TYR B 80  ? 0.2056 0.2161 0.1374 -0.0148 -0.0180 -0.0135 305  TYR B O   
3041 C CB  . TYR B 80  ? 0.2197 0.2258 0.1391 -0.0223 -0.0276 -0.0185 305  TYR B CB  
3042 C CG  . TYR B 80  ? 0.2492 0.2495 0.1598 -0.0254 -0.0302 -0.0227 305  TYR B CG  
3043 C CD1 . TYR B 80  ? 0.1985 0.1932 0.0982 -0.0245 -0.0286 -0.0255 305  TYR B CD1 
3044 C CD2 . TYR B 80  ? 0.3148 0.3150 0.2278 -0.0295 -0.0341 -0.0238 305  TYR B CD2 
3045 C CE1 . TYR B 80  ? 0.3036 0.2921 0.1943 -0.0277 -0.0310 -0.0298 305  TYR B CE1 
3046 C CE2 . TYR B 80  ? 0.3005 0.2950 0.2054 -0.0331 -0.0367 -0.0279 305  TYR B CE2 
3047 C CZ  . TYR B 80  ? 0.3039 0.2921 0.1973 -0.0322 -0.0353 -0.0311 305  TYR B CZ  
3048 O OH  . TYR B 80  ? 0.3092 0.2908 0.1936 -0.0361 -0.0379 -0.0356 305  TYR B OH  
3049 N N   A GLU B 81  ? 0.2113 0.2273 0.1382 -0.0164 -0.0230 -0.0107 306  GLU B N   
3050 N N   B GLU B 81  ? 0.2125 0.2285 0.1393 -0.0164 -0.0231 -0.0107 306  GLU B N   
3051 C CA  A GLU B 81  ? 0.2430 0.2640 0.1785 -0.0151 -0.0221 -0.0071 306  GLU B CA  
3052 C CA  B GLU B 81  ? 0.2449 0.2660 0.1801 -0.0151 -0.0223 -0.0070 306  GLU B CA  
3053 C C   A GLU B 81  ? 0.3175 0.3417 0.2602 -0.0170 -0.0250 -0.0066 306  GLU B C   
3054 C C   B GLU B 81  ? 0.3169 0.3411 0.2595 -0.0170 -0.0251 -0.0065 306  GLU B C   
3055 O O   A GLU B 81  ? 0.3103 0.3337 0.2513 -0.0197 -0.0282 -0.0085 306  GLU B O   
3056 O O   B GLU B 81  ? 0.3094 0.3329 0.2504 -0.0197 -0.0283 -0.0084 306  GLU B O   
3057 C CB  A GLU B 81  ? 0.2337 0.2582 0.1672 -0.0137 -0.0225 -0.0036 306  GLU B CB  
3058 C CB  B GLU B 81  ? 0.2406 0.2653 0.1734 -0.0140 -0.0231 -0.0036 306  GLU B CB  
3059 C CG  A GLU B 81  ? 0.3190 0.3411 0.2472 -0.0116 -0.0186 -0.0030 306  GLU B CG  
3060 C CG  B GLU B 81  ? 0.2628 0.2845 0.1870 -0.0124 -0.0205 -0.0037 306  GLU B CG  
3061 C CD  A GLU B 81  ? 0.2593 0.2821 0.1938 -0.0098 -0.0144 -0.0011 306  GLU B CD  
3062 C CD  B GLU B 81  ? 0.3616 0.3865 0.2838 -0.0109 -0.0209 0.0004  306  GLU B CD  
3063 O OE1 A GLU B 81  ? 0.1917 0.2161 0.1341 -0.0100 -0.0143 -0.0008 306  GLU B OE1 
3064 O OE1 B GLU B 81  ? 0.3533 0.3827 0.2802 -0.0110 -0.0238 0.0031  306  GLU B OE1 
3065 O OE2 A GLU B 81  ? 0.3754 0.3970 0.3064 -0.0084 -0.0112 0.0002  306  GLU B OE2 
3066 O OE2 B GLU B 81  ? 0.2734 0.2961 0.1894 -0.0095 -0.0180 0.0012  306  GLU B OE2 
3067 N N   . PRO B 82  ? 0.3216 0.3490 0.2722 -0.0159 -0.0237 -0.0042 307  PRO B N   
3068 C CA  . PRO B 82  ? 0.3653 0.3963 0.3228 -0.0175 -0.0260 -0.0033 307  PRO B CA  
3069 C C   . PRO B 82  ? 0.3408 0.3761 0.2980 -0.0196 -0.0306 -0.0024 307  PRO B C   
3070 O O   . PRO B 82  ? 0.4030 0.4396 0.3635 -0.0222 -0.0328 -0.0032 307  PRO B O   
3071 C CB  . PRO B 82  ? 0.2909 0.3249 0.2546 -0.0154 -0.0238 -0.0005 307  PRO B CB  
3072 C CG  . PRO B 82  ? 0.2618 0.2923 0.2237 -0.0136 -0.0199 -0.0013 307  PRO B CG  
3073 C CD  . PRO B 82  ? 0.3187 0.3459 0.2722 -0.0135 -0.0197 -0.0029 307  PRO B CD  
3074 N N   . ASP B 83  ? 0.3815 0.4195 0.3350 -0.0187 -0.0321 -0.0006 308  ASP B N   
3075 C CA  . ASP B 83  ? 0.5183 0.5619 0.4723 -0.0206 -0.0368 0.0007  308  ASP B CA  
3076 C C   . ASP B 83  ? 0.6374 0.6784 0.5844 -0.0240 -0.0400 -0.0027 308  ASP B C   
3077 O O   . ASP B 83  ? 0.5573 0.6032 0.5032 -0.0260 -0.0445 -0.0018 308  ASP B O   
3078 C CB  . ASP B 83  ? 0.4592 0.5070 0.4119 -0.0179 -0.0375 0.0046  308  ASP B CB  
3079 C CG  . ASP B 83  ? 0.7148 0.7584 0.6575 -0.0168 -0.0364 0.0039  308  ASP B CG  
3080 O OD1 . ASP B 83  ? 0.5705 0.6079 0.5077 -0.0176 -0.0346 0.0004  308  ASP B OD1 
3081 O OD2 . ASP B 83  ? 0.8037 0.8502 0.7440 -0.0148 -0.0372 0.0072  308  ASP B OD2 
3082 N N   . GLY B 84  ? 0.5155 0.5490 0.4578 -0.0249 -0.0380 -0.0064 309  GLY B N   
3083 C CA  . GLY B 84  ? 0.3392 0.3683 0.2738 -0.0281 -0.0405 -0.0102 309  GLY B CA  
3084 C C   . GLY B 84  ? 0.4068 0.4339 0.3308 -0.0274 -0.0411 -0.0111 309  GLY B C   
3085 O O   . GLY B 84  ? 0.4070 0.4290 0.3229 -0.0300 -0.0427 -0.0149 309  GLY B O   
3086 N N   . SER B 85  ? 0.4289 0.4591 0.3520 -0.0242 -0.0398 -0.0078 310  SER B N   
3087 C CA  . SER B 85  ? 0.3891 0.4165 0.3014 -0.0231 -0.0393 -0.0084 310  SER B CA  
3088 C C   . SER B 85  ? 0.4150 0.4344 0.3222 -0.0215 -0.0342 -0.0115 310  SER B C   
3089 O O   . SER B 85  ? 0.3245 0.3418 0.2377 -0.0202 -0.0306 -0.0119 310  SER B O   
3090 C CB  . SER B 85  ? 0.4435 0.4758 0.3565 -0.0199 -0.0387 -0.0035 310  SER B CB  
3091 O OG  . SER B 85  ? 0.6019 0.6340 0.5219 -0.0170 -0.0341 -0.0013 310  SER B OG  
3092 N N   . VAL B 86  ? 0.3957 0.4108 0.2915 -0.0216 -0.0340 -0.0138 311  VAL B N   
3093 C CA  . VAL B 86  ? 0.3504 0.3580 0.2406 -0.0199 -0.0290 -0.0169 311  VAL B CA  
3094 C C   . VAL B 86  ? 0.3428 0.3519 0.2358 -0.0160 -0.0239 -0.0137 311  VAL B C   
3095 O O   . VAL B 86  ? 0.4228 0.4359 0.3150 -0.0147 -0.0242 -0.0099 311  VAL B O   
3096 C CB  . VAL B 86  ? 0.4909 0.4933 0.3673 -0.0212 -0.0300 -0.0206 311  VAL B CB  
3097 C CG2 . VAL B 86  ? 0.3640 0.3621 0.2379 -0.0253 -0.0336 -0.0251 311  VAL B CG2 
3098 N N   . PHE B 87  ? 0.3221 0.3280 0.2188 -0.0143 -0.0193 -0.0150 312  PHE B N   
3099 C CA  . PHE B 87  ? 0.2636 0.2707 0.1632 -0.0112 -0.0143 -0.0125 312  PHE B CA  
3100 C C   . PHE B 87  ? 0.2888 0.2921 0.1776 -0.0097 -0.0110 -0.0138 312  PHE B C   
3101 O O   . PHE B 87  ? 0.3083 0.3061 0.1917 -0.0095 -0.0092 -0.0178 312  PHE B O   
3102 C CB  . PHE B 87  ? 0.2296 0.2359 0.1377 -0.0102 -0.0111 -0.0134 312  PHE B CB  
3103 C CG  . PHE B 87  ? 0.1918 0.1996 0.1033 -0.0076 -0.0060 -0.0114 312  PHE B CG  
3104 C CD1 . PHE B 87  ? 0.2462 0.2587 0.1644 -0.0073 -0.0056 -0.0075 312  PHE B CD1 
3105 C CD2 . PHE B 87  ? 0.2646 0.2693 0.1729 -0.0057 -0.0014 -0.0134 312  PHE B CD2 
3106 C CE1 . PHE B 87  ? 0.2011 0.2149 0.1223 -0.0057 -0.0010 -0.0057 312  PHE B CE1 
3107 C CE2 . PHE B 87  ? 0.2678 0.2750 0.1800 -0.0038 0.0032  -0.0114 312  PHE B CE2 
3108 C CZ  . PHE B 87  ? 0.2165 0.2283 0.1353 -0.0041 0.0033  -0.0076 312  PHE B CZ  
3109 N N   . ASN B 88  ? 0.2991 0.3050 0.1846 -0.0085 -0.0100 -0.0104 313  ASN B N   
3110 C CA  . ASN B 88  ? 0.2366 0.2392 0.1109 -0.0072 -0.0068 -0.0112 313  ASN B CA  
3111 C C   . ASN B 88  ? 0.2444 0.2466 0.1223 -0.0047 -0.0001 -0.0105 313  ASN B C   
3112 O O   . ASN B 88  ? 0.2792 0.2850 0.1632 -0.0038 0.0019  -0.0066 313  ASN B O   
3113 C CB  . ASN B 88  ? 0.3101 0.3154 0.1783 -0.0071 -0.0089 -0.0074 313  ASN B CB  
3114 C CG  . ASN B 88  ? 0.3144 0.3162 0.1693 -0.0060 -0.0061 -0.0083 313  ASN B CG  
3115 O OD1 . ASN B 88  ? 0.3352 0.3328 0.1864 -0.0048 -0.0015 -0.0114 313  ASN B OD1 
3116 N ND2 . ASN B 88  ? 0.5016 0.5051 0.3489 -0.0061 -0.0088 -0.0055 313  ASN B ND2 
3117 N N   . PRO B 89  ? 0.2748 0.2727 0.1493 -0.0034 0.0035  -0.0142 314  PRO B N   
3118 C CA  . PRO B 89  ? 0.2494 0.2484 0.1291 -0.0010 0.0098  -0.0134 314  PRO B CA  
3119 C C   . PRO B 89  ? 0.3241 0.3240 0.1980 0.0005  0.0142  -0.0109 314  PRO B C   
3120 O O   . PRO B 89  ? 0.3594 0.3616 0.2385 0.0021  0.0195  -0.0096 314  PRO B O   
3121 C CB  . PRO B 89  ? 0.2872 0.2810 0.1641 0.0003  0.0120  -0.0183 314  PRO B CB  
3122 C CG  . PRO B 89  ? 0.3659 0.3543 0.2303 -0.0012 0.0087  -0.0215 314  PRO B CG  
3123 C CD  . PRO B 89  ? 0.3219 0.3136 0.1879 -0.0042 0.0022  -0.0193 314  PRO B CD  
3124 N N   . LEU B 90  ? 0.2900 0.2887 0.1534 -0.0001 0.0123  -0.0100 315  LEU B N   
3125 C CA  . LEU B 90  ? 0.2956 0.2949 0.1527 0.0011  0.0163  -0.0068 315  LEU B CA  
3126 C C   . LEU B 90  ? 0.4327 0.4363 0.2957 0.0006  0.0155  -0.0012 315  LEU B C   
3127 O O   . LEU B 90  ? 0.4542 0.4582 0.3131 0.0014  0.0190  0.0022  315  LEU B O   
3128 C CB  . LEU B 90  ? 0.3025 0.2979 0.1438 0.0010  0.0147  -0.0085 315  LEU B CB  
3129 C CG  . LEU B 90  ? 0.4326 0.4220 0.2662 0.0016  0.0162  -0.0146 315  LEU B CG  
3130 C CD1 . LEU B 90  ? 0.3848 0.3701 0.2018 0.0010  0.0144  -0.0165 315  LEU B CD1 
3131 C CD2 . LEU B 90  ? 0.3957 0.3847 0.2323 0.0045  0.0239  -0.0155 315  LEU B CD2 
3132 N N   . SER B 91  ? 0.3355 0.3417 0.2079 -0.0007 0.0114  0.0000  316  SER B N   
3133 C CA  . SER B 91  ? 0.3188 0.3278 0.1957 -0.0010 0.0102  0.0051  316  SER B CA  
3134 C C   . SER B 91  ? 0.2979 0.3090 0.1844 -0.0008 0.0150  0.0076  316  SER B C   
3135 O O   . SER B 91  ? 0.4069 0.4189 0.2956 -0.0009 0.0153  0.0119  316  SER B O   
3136 C CB  . SER B 91  ? 0.3102 0.3213 0.1930 -0.0023 0.0041  0.0052  316  SER B CB  
3137 O OG  . SER B 91  ? 0.5033 0.5155 0.3967 -0.0030 0.0042  0.0031  316  SER B OG  
3138 N N   . GLY B 92  ? 0.2885 0.3003 0.1808 -0.0005 0.0184  0.0051  317  GLY B N   
3139 C CA  . GLY B 92  ? 0.2517 0.2663 0.1536 -0.0009 0.0224  0.0073  317  GLY B CA  
3140 C C   . GLY B 92  ? 0.2104 0.2273 0.1238 -0.0021 0.0199  0.0068  317  GLY B C   
3141 O O   . GLY B 92  ? 0.2499 0.2693 0.1714 -0.0028 0.0227  0.0081  317  GLY B O   
3142 N N   . ALA B 93  ? 0.2255 0.2419 0.1397 -0.0025 0.0148  0.0050  318  ALA B N   
3143 C CA  . ALA B 93  ? 0.1980 0.2165 0.1224 -0.0035 0.0127  0.0044  318  ALA B CA  
3144 C C   . ALA B 93  ? 0.2027 0.2224 0.1320 -0.0030 0.0148  0.0014  318  ALA B C   
3145 O O   . ALA B 93  ? 0.2166 0.2342 0.1405 -0.0018 0.0158  -0.0014 318  ALA B O   
3146 C CB  . ALA B 93  ? 0.2339 0.2519 0.1579 -0.0042 0.0070  0.0036  318  ALA B CB  
3147 N N   . PRO B 94  ? 0.2032 0.2259 0.1421 -0.0037 0.0157  0.0018  319  PRO B N   
3148 C CA  . PRO B 94  ? 0.2113 0.2359 0.1553 -0.0028 0.0175  -0.0006 319  PRO B CA  
3149 C C   . PRO B 94  ? 0.2017 0.2244 0.1458 -0.0024 0.0140  -0.0035 319  PRO B C   
3150 O O   . PRO B 94  ? 0.1857 0.2081 0.1305 -0.0008 0.0157  -0.0057 319  PRO B O   
3151 C CB  . PRO B 94  ? 0.2220 0.2509 0.1759 -0.0043 0.0184  0.0011  319  PRO B CB  
3152 C CG  . PRO B 94  ? 0.1900 0.2176 0.1443 -0.0059 0.0157  0.0032  319  PRO B CG  
3153 C CD  . PRO B 94  ? 0.1669 0.1912 0.1119 -0.0053 0.0155  0.0046  319  PRO B CD  
3154 N N   . ALA B 95  ? 0.1797 0.2011 0.1233 -0.0036 0.0096  -0.0035 320  ALA B N   
3155 C CA  . ALA B 95  ? 0.1720 0.1919 0.1168 -0.0039 0.0063  -0.0058 320  ALA B CA  
3156 C C   . ALA B 95  ? 0.1912 0.2107 0.1349 -0.0055 0.0018  -0.0049 320  ALA B C   
3157 O O   . ALA B 95  ? 0.1750 0.1960 0.1190 -0.0060 0.0015  -0.0021 320  ALA B O   
3158 C CB  . ALA B 95  ? 0.1376 0.1602 0.0914 -0.0038 0.0066  -0.0060 320  ALA B CB  
3159 N N   . PRO B 96  ? 0.1671 0.1847 0.1098 -0.0063 -0.0015 -0.0068 321  PRO B N   
3160 C CA  . PRO B 96  ? 0.1564 0.1754 0.1007 -0.0079 -0.0057 -0.0056 321  PRO B CA  
3161 C C   . PRO B 96  ? 0.1574 0.1799 0.1102 -0.0082 -0.0056 -0.0035 321  PRO B C   
3162 O O   . PRO B 96  ? 0.1862 0.2097 0.1440 -0.0078 -0.0035 -0.0039 321  PRO B O   
3163 C CB  . PRO B 96  ? 0.1996 0.2161 0.1427 -0.0091 -0.0085 -0.0083 321  PRO B CB  
3164 C CG  . PRO B 96  ? 0.2117 0.2237 0.1486 -0.0080 -0.0061 -0.0112 321  PRO B CG  
3165 C CD  . PRO B 96  ? 0.2014 0.2151 0.1413 -0.0059 -0.0015 -0.0102 321  PRO B CD  
3166 N N   . GLU B 97  ? 0.1662 0.1906 0.1204 -0.0088 -0.0079 -0.0014 322  GLU B N   
3167 C CA  . GLU B 97  ? 0.1595 0.1863 0.1208 -0.0090 -0.0076 0.0003  322  GLU B CA  
3168 C C   . GLU B 97  ? 0.1610 0.1883 0.1274 -0.0096 -0.0081 -0.0014 322  GLU B C   
3169 O O   . GLU B 97  ? 0.1971 0.2234 0.1626 -0.0103 -0.0102 -0.0030 322  GLU B O   
3170 C CB  . GLU B 97  ? 0.1976 0.2262 0.1596 -0.0091 -0.0102 0.0026  322  GLU B CB  
3171 C CG  . GLU B 97  ? 0.3366 0.3649 0.2940 -0.0081 -0.0098 0.0051  322  GLU B CG  
3172 C CD  . GLU B 97  ? 0.4925 0.5233 0.4513 -0.0076 -0.0126 0.0076  322  GLU B CD  
3173 O OE1 . GLU B 97  ? 0.5107 0.5437 0.4752 -0.0080 -0.0138 0.0076  322  GLU B OE1 
3174 O OE2 . GLU B 97  ? 0.5714 0.6025 0.5256 -0.0067 -0.0134 0.0098  322  GLU B OE2 
3175 N N   . GLY B 98  ? 0.1317 0.1604 0.1032 -0.0095 -0.0063 -0.0009 323  GLY B N   
3176 C CA  . GLY B 98  ? 0.1438 0.1734 0.1200 -0.0100 -0.0068 -0.0019 323  GLY B CA  
3177 C C   . GLY B 98  ? 0.1468 0.1759 0.1235 -0.0092 -0.0053 -0.0036 323  GLY B C   
3178 O O   . GLY B 98  ? 0.1585 0.1887 0.1392 -0.0092 -0.0056 -0.0040 323  GLY B O   
3179 N N   . PHE B 99  ? 0.1503 0.1778 0.1229 -0.0082 -0.0035 -0.0044 324  PHE B N   
3180 C CA  . PHE B 99  ? 0.1557 0.1831 0.1294 -0.0068 -0.0016 -0.0057 324  PHE B CA  
3181 C C   . PHE B 99  ? 0.1478 0.1794 0.1274 -0.0067 0.0005  -0.0048 324  PHE B C   
3182 O O   . PHE B 99  ? 0.1468 0.1802 0.1276 -0.0076 0.0016  -0.0034 324  PHE B O   
3183 C CB  . PHE B 99  ? 0.1237 0.1487 0.0914 -0.0055 0.0005  -0.0068 324  PHE B CB  
3184 C CG  . PHE B 99  ? 0.1770 0.1971 0.1396 -0.0051 -0.0008 -0.0091 324  PHE B CG  
3185 C CD1 . PHE B 99  ? 0.1524 0.1704 0.1116 -0.0068 -0.0041 -0.0095 324  PHE B CD1 
3186 C CD2 . PHE B 99  ? 0.1807 0.1985 0.1422 -0.0030 0.0014  -0.0109 324  PHE B CD2 
3187 C CE1 . PHE B 99  ? 0.1849 0.1979 0.1392 -0.0072 -0.0055 -0.0120 324  PHE B CE1 
3188 C CE2 . PHE B 99  ? 0.1949 0.2068 0.1511 -0.0028 0.0004  -0.0133 324  PHE B CE2 
3189 C CZ  . PHE B 99  ? 0.2081 0.2175 0.1606 -0.0052 -0.0032 -0.0140 324  PHE B CZ  
3190 N N   . PRO B 100 ? 0.1326 0.1657 0.1158 -0.0056 0.0008  -0.0054 325  PRO B N   
3191 C CA  . PRO B 100 ? 0.1277 0.1659 0.1169 -0.0057 0.0024  -0.0045 325  PRO B CA  
3192 C C   . PRO B 100 ? 0.1496 0.1900 0.1387 -0.0057 0.0056  -0.0039 325  PRO B C   
3193 O O   . PRO B 100 ? 0.1454 0.1838 0.1302 -0.0042 0.0076  -0.0044 325  PRO B O   
3194 C CB  . PRO B 100 ? 0.1385 0.1777 0.1302 -0.0035 0.0024  -0.0052 325  PRO B CB  
3195 C CG  . PRO B 100 ? 0.2015 0.2357 0.1900 -0.0035 -0.0001 -0.0060 325  PRO B CG  
3196 C CD  . PRO B 100 ? 0.1773 0.2075 0.1596 -0.0044 -0.0004 -0.0067 325  PRO B CD  
3197 N N   . ASP B 101 ? 0.1187 0.1627 0.1121 -0.0076 0.0062  -0.0028 326  ASP B N   
3198 C CA  . ASP B 101 ? 0.1054 0.1516 0.0995 -0.0085 0.0093  -0.0017 326  ASP B CA  
3199 C C   . ASP B 101 ? 0.1152 0.1680 0.1163 -0.0089 0.0108  -0.0014 326  ASP B C   
3200 O O   . ASP B 101 ? 0.1380 0.1937 0.1423 -0.0113 0.0122  -0.0004 326  ASP B O   
3201 C CB  . ASP B 101 ? 0.1351 0.1791 0.1281 -0.0110 0.0090  -0.0005 326  ASP B CB  
3202 C CG  . ASP B 101 ? 0.1491 0.1947 0.1465 -0.0130 0.0071  -0.0006 326  ASP B CG  
3203 O OD1 . ASP B 101 ? 0.1436 0.1920 0.1443 -0.0125 0.0054  -0.0015 326  ASP B OD1 
3204 O OD2 . ASP B 101 ? 0.1228 0.1666 0.1200 -0.0150 0.0074  0.0002  326  ASP B OD2 
3205 N N   . PHE B 102 ? 0.1342 0.1896 0.1379 -0.0065 0.0106  -0.0020 327  PHE B N   
3206 C CA  . PHE B 102 ? 0.1148 0.1780 0.1259 -0.0065 0.0117  -0.0013 327  PHE B CA  
3207 C C   . PHE B 102 ? 0.1125 0.1772 0.1246 -0.0024 0.0131  -0.0017 327  PHE B C   
3208 O O   . PHE B 102 ? 0.1729 0.2318 0.1797 0.0000  0.0128  -0.0028 327  PHE B O   
3209 C CB  . PHE B 102 ? 0.1111 0.1775 0.1268 -0.0086 0.0085  -0.0012 327  PHE B CB  
3210 C CG  . PHE B 102 ? 0.1322 0.1957 0.1463 -0.0069 0.0055  -0.0019 327  PHE B CG  
3211 C CD1 . PHE B 102 ? 0.1306 0.1882 0.1401 -0.0079 0.0034  -0.0024 327  PHE B CD1 
3212 C CD2 . PHE B 102 ? 0.1217 0.1886 0.1391 -0.0041 0.0050  -0.0016 327  PHE B CD2 
3213 C CE1 . PHE B 102 ? 0.1206 0.1757 0.1288 -0.0067 0.0010  -0.0028 327  PHE B CE1 
3214 C CE2 . PHE B 102 ? 0.1275 0.1912 0.1433 -0.0026 0.0024  -0.0018 327  PHE B CE2 
3215 C CZ  . PHE B 102 ? 0.1357 0.1934 0.1467 -0.0042 0.0005  -0.0024 327  PHE B CZ  
3216 N N   . THR B 103 ? 0.1076 0.1803 0.1267 -0.0017 0.0147  -0.0007 328  THR B N   
3217 C CA  . THR B 103 ? 0.1239 0.1994 0.1453 0.0028  0.0168  -0.0006 328  THR B CA  
3218 C C   . THR B 103 ? 0.1585 0.2357 0.1833 0.0047  0.0137  -0.0004 328  THR B C   
3219 O O   . THR B 103 ? 0.1409 0.2229 0.1703 0.0024  0.0109  0.0004  328  THR B O   
3220 C CB  . THR B 103 ? 0.1313 0.2159 0.1595 0.0026  0.0203  0.0008  328  THR B CB  
3221 O OG1 . THR B 103 ? 0.1219 0.2039 0.1460 0.0009  0.0234  0.0008  328  THR B OG1 
3222 C CG2 . THR B 103 ? 0.1171 0.2057 0.1488 0.0079  0.0230  0.0012  328  THR B CG2 
3223 N N   . ALA B 104 ? 0.1398 0.2123 0.1615 0.0090  0.0143  -0.0011 329  ALA B N   
3224 C CA  . ALA B 104 ? 0.1200 0.1931 0.1444 0.0116  0.0120  -0.0004 329  ALA B CA  
3225 C C   . ALA B 104 ? 0.1447 0.2150 0.1679 0.0171  0.0151  -0.0007 329  ALA B C   
3226 O O   . ALA B 104 ? 0.1771 0.2425 0.1950 0.0183  0.0182  -0.0022 329  ALA B O   
3227 C CB  . ALA B 104 ? 0.1642 0.2300 0.1836 0.0098  0.0083  -0.0011 329  ALA B CB  
3228 N N   . GLN B 105 ? 0.1211 0.1941 0.1486 0.0206  0.0142  0.0007  330  GLN B N   
3229 C CA  . GLN B 105 ? 0.1878 0.2570 0.2141 0.0265  0.0173  0.0004  330  GLN B CA  
3230 C C   . GLN B 105 ? 0.1782 0.2339 0.1951 0.0272  0.0168  -0.0018 330  GLN B C   
3231 O O   . GLN B 105 ? 0.1798 0.2290 0.1918 0.0304  0.0202  -0.0034 330  GLN B O   
3232 C CB  . GLN B 105 ? 0.1662 0.2426 0.2003 0.0306  0.0167  0.0031  330  GLN B CB  
3233 C CG  . GLN B 105 ? 0.1802 0.2707 0.2242 0.0308  0.0179  0.0052  330  GLN B CG  
3234 C CD  . GLN B 105 ? 0.2624 0.3601 0.3101 0.0248  0.0142  0.0059  330  GLN B CD  
3235 O OE1 . GLN B 105 ? 0.2220 0.3184 0.2689 0.0229  0.0100  0.0064  330  GLN B OE1 
3236 N NE2 . GLN B 105 ? 0.1871 0.2917 0.2385 0.0216  0.0159  0.0059  330  GLN B NE2 
3237 N N   . GLU B 106 ? 0.1761 0.2277 0.1905 0.0241  0.0128  -0.0018 331  GLU B N   
3238 C CA  . GLU B 106 ? 0.1756 0.2154 0.1819 0.0235  0.0116  -0.0037 331  GLU B CA  
3239 C C   . GLU B 106 ? 0.1531 0.1918 0.1572 0.0181  0.0080  -0.0040 331  GLU B C   
3240 O O   . GLU B 106 ? 0.1507 0.1960 0.1595 0.0158  0.0057  -0.0024 331  GLU B O   
3241 C CB  . GLU B 106 ? 0.1962 0.2314 0.2029 0.0270  0.0108  -0.0025 331  GLU B CB  
3242 C CG  . GLU B 106 ? 0.2751 0.3100 0.2838 0.0333  0.0145  -0.0020 331  GLU B CG  
3243 C CD  . GLU B 106 ? 0.2189 0.2663 0.2375 0.0360  0.0145  0.0012  331  GLU B CD  
3244 O OE1 . GLU B 106 ? 0.2216 0.2755 0.2445 0.0334  0.0108  0.0032  331  GLU B OE1 
3245 O OE2 . GLU B 106 ? 0.2684 0.3192 0.2903 0.0408  0.0182  0.0018  331  GLU B OE2 
3246 N N   . TYR B 107 ? 0.1415 0.1716 0.1382 0.0161  0.0075  -0.0062 332  TYR B N   
3247 C CA  . TYR B 107 ? 0.1468 0.1750 0.1412 0.0116  0.0042  -0.0064 332  TYR B CA  
3248 C C   . TYR B 107 ? 0.1749 0.1945 0.1653 0.0117  0.0026  -0.0070 332  TYR B C   
3249 O O   . TYR B 107 ? 0.1909 0.2025 0.1752 0.0121  0.0036  -0.0092 332  TYR B O   
3250 C CB  . TYR B 107 ? 0.1738 0.2007 0.1637 0.0088  0.0046  -0.0079 332  TYR B CB  
3251 C CG  . TYR B 107 ? 0.1790 0.2128 0.1719 0.0088  0.0069  -0.0073 332  TYR B CG  
3252 C CD1 . TYR B 107 ? 0.1284 0.1630 0.1210 0.0119  0.0108  -0.0078 332  TYR B CD1 
3253 C CD2 . TYR B 107 ? 0.1915 0.2307 0.1876 0.0056  0.0057  -0.0061 332  TYR B CD2 
3254 C CE1 . TYR B 107 ? 0.1524 0.1936 0.1481 0.0116  0.0132  -0.0070 332  TYR B CE1 
3255 C CE2 . TYR B 107 ? 0.1160 0.1608 0.1147 0.0051  0.0080  -0.0055 332  TYR B CE2 
3256 C CZ  . TYR B 107 ? 0.1552 0.2014 0.1540 0.0079  0.0118  -0.0058 332  TYR B CZ  
3257 O OH  . TYR B 107 ? 0.1501 0.2022 0.1519 0.0072  0.0144  -0.0048 332  TYR B OH  
3258 N N   . HIS B 108 ? 0.1383 0.1592 0.1318 0.0111  0.0002  -0.0051 333  HIS B N   
3259 C CA  . HIS B 108 ? 0.1552 0.1681 0.1455 0.0111  -0.0010 -0.0051 333  HIS B CA  
3260 C C   . HIS B 108 ? 0.1743 0.1835 0.1607 0.0065  -0.0032 -0.0063 333  HIS B C   
3261 O O   . HIS B 108 ? 0.1511 0.1654 0.1392 0.0037  -0.0047 -0.0058 333  HIS B O   
3262 C CB  . HIS B 108 ? 0.1454 0.1615 0.1401 0.0122  -0.0025 -0.0022 333  HIS B CB  
3263 C CG  . HIS B 108 ? 0.1860 0.2082 0.1859 0.0165  -0.0011 -0.0004 333  HIS B CG  
3264 N ND1 . HIS B 108 ? 0.1943 0.2261 0.1999 0.0164  -0.0026 0.0019  333  HIS B ND1 
3265 C CD2 . HIS B 108 ? 0.2501 0.2706 0.2505 0.0213  0.0017  -0.0005 333  HIS B CD2 
3266 C CE1 . HIS B 108 ? 0.2033 0.2399 0.2133 0.0206  -0.0011 0.0033  333  HIS B CE1 
3267 N NE2 . HIS B 108 ? 0.2469 0.2770 0.2542 0.0239  0.0017  0.0020  333  HIS B NE2 
3268 N N   . LEU B 109 ? 0.1345 0.1347 0.1159 0.0058  -0.0035 -0.0078 334  LEU B N   
3269 C CA  . LEU B 109 ? 0.1341 0.1318 0.1123 0.0013  -0.0057 -0.0089 334  LEU B CA  
3270 C C   . LEU B 109 ? 0.1590 0.1486 0.1345 -0.0003 -0.0068 -0.0091 334  LEU B C   
3271 O O   . LEU B 109 ? 0.1727 0.1565 0.1474 0.0023  -0.0056 -0.0088 334  LEU B O   
3272 C CB  . LEU B 109 ? 0.1581 0.1541 0.1314 0.0004  -0.0049 -0.0116 334  LEU B CB  
3273 C CG  . LEU B 109 ? 0.2083 0.1963 0.1759 0.0027  -0.0026 -0.0142 334  LEU B CG  
3274 C CD1 . LEU B 109 ? 0.1972 0.1753 0.1592 0.0002  -0.0040 -0.0162 334  LEU B CD1 
3275 C CD2 . LEU B 109 ? 0.1767 0.1667 0.1409 0.0030  -0.0011 -0.0159 334  LEU B CD2 
3276 N N   A ARG B 110 ? 0.1567 0.1462 0.1312 -0.0046 -0.0092 -0.0095 335  ARG B N   
3277 N N   B ARG B 110 ? 0.1576 0.1471 0.1321 -0.0046 -0.0092 -0.0095 335  ARG B N   
3278 C CA  A ARG B 110 ? 0.1575 0.1396 0.1290 -0.0076 -0.0105 -0.0102 335  ARG B CA  
3279 C CA  B ARG B 110 ? 0.1591 0.1413 0.1307 -0.0077 -0.0105 -0.0101 335  ARG B CA  
3280 C C   A ARG B 110 ? 0.2012 0.1827 0.1690 -0.0113 -0.0122 -0.0125 335  ARG B C   
3281 C C   B ARG B 110 ? 0.2003 0.1818 0.1681 -0.0114 -0.0122 -0.0125 335  ARG B C   
3282 O O   A ARG B 110 ? 0.1844 0.1728 0.1536 -0.0120 -0.0130 -0.0123 335  ARG B O   
3283 O O   B ARG B 110 ? 0.1840 0.1724 0.1533 -0.0121 -0.0130 -0.0122 335  ARG B O   
3284 C CB  A ARG B 110 ? 0.2145 0.1992 0.1900 -0.0097 -0.0121 -0.0073 335  ARG B CB  
3285 C CB  B ARG B 110 ? 0.2132 0.1982 0.1888 -0.0097 -0.0121 -0.0072 335  ARG B CB  
3286 C CG  A ARG B 110 ? 0.2707 0.2550 0.2488 -0.0066 -0.0110 -0.0046 335  ARG B CG  
3287 C CG  B ARG B 110 ? 0.3215 0.3022 0.2981 -0.0074 -0.0111 -0.0051 335  ARG B CG  
3288 C CD  A ARG B 110 ? 0.2049 0.1908 0.1855 -0.0093 -0.0124 -0.0020 335  ARG B CD  
3289 C CD  B ARG B 110 ? 0.2418 0.2256 0.2216 -0.0099 -0.0125 -0.0022 335  ARG B CD  
3290 N NE  A ARG B 110 ? 0.2178 0.2058 0.2010 -0.0063 -0.0118 0.0011  335  ARG B NE  
3291 N NE  B ARG B 110 ? 0.3137 0.2926 0.2936 -0.0081 -0.0117 0.0002  335  ARG B NE  
3292 C CZ  A ARG B 110 ? 0.3500 0.3316 0.3321 -0.0052 -0.0112 0.0029  335  ARG B CZ  
3293 C CZ  B ARG B 110 ? 0.3413 0.3241 0.3239 -0.0046 -0.0111 0.0029  335  ARG B CZ  
3294 N NH1 A ARG B 110 ? 0.2628 0.2346 0.2413 -0.0069 -0.0108 0.0017  335  ARG B NH1 
3295 N NH1 B ARG B 110 ? 0.1483 0.1399 0.1338 -0.0028 -0.0112 0.0031  335  ARG B NH1 
3296 N NH2 A ARG B 110 ? 0.4802 0.4649 0.4646 -0.0023 -0.0110 0.0060  335  ARG B NH2 
3297 N NH2 B ARG B 110 ? 0.4099 0.3876 0.3919 -0.0030 -0.0105 0.0054  335  ARG B NH2 
3298 N N   . ALA B 111 ? 0.2045 0.1776 0.1673 -0.0137 -0.0129 -0.0148 336  ALA B N   
3299 C CA  . ALA B 111 ? 0.1920 0.1650 0.1511 -0.0177 -0.0152 -0.0170 336  ALA B CA  
3300 C C   . ALA B 111 ? 0.2291 0.1946 0.1854 -0.0220 -0.0169 -0.0183 336  ALA B C   
3301 O O   . ALA B 111 ? 0.2172 0.1754 0.1730 -0.0214 -0.0157 -0.0180 336  ALA B O   
3302 C CB  . ALA B 111 ? 0.2047 0.1752 0.1577 -0.0158 -0.0138 -0.0200 336  ALA B CB  
3303 N N   . ALA B 112 ? 0.1958 0.1633 0.1505 -0.0265 -0.0199 -0.0195 337  ALA B N   
3304 C CA  . ALA B 112 ? 0.1867 0.1482 0.1391 -0.0317 -0.0221 -0.0210 337  ALA B CA  
3305 C C   . ALA B 112 ? 0.2683 0.2321 0.2168 -0.0355 -0.0252 -0.0234 337  ALA B C   
3306 O O   . ALA B 112 ? 0.2136 0.1860 0.1636 -0.0347 -0.0262 -0.0225 337  ALA B O   
3307 C CB  . ALA B 112 ? 0.1892 0.1545 0.1483 -0.0346 -0.0232 -0.0178 337  ALA B CB  
3308 N N   . GLY B 113 ? 0.2124 0.1683 0.1557 -0.0400 -0.0269 -0.0263 338  GLY B N   
3309 C CA  . GLY B 113 ? 0.2491 0.2073 0.1887 -0.0446 -0.0307 -0.0286 338  GLY B CA  
3310 C C   . GLY B 113 ? 0.2309 0.1916 0.1748 -0.0510 -0.0340 -0.0276 338  GLY B C   
3311 O O   . GLY B 113 ? 0.2687 0.2299 0.2187 -0.0516 -0.0330 -0.0248 338  GLY B O   
3312 N N   . LYS B 114 ? 0.2405 0.2031 0.1811 -0.0560 -0.0380 -0.0298 339  LYS B N   
3313 C CA  . LYS B 114 ? 0.3018 0.2688 0.2473 -0.0626 -0.0416 -0.0288 339  LYS B CA  
3314 C C   . LYS B 114 ? 0.3351 0.2899 0.2775 -0.0672 -0.0413 -0.0311 339  LYS B C   
3315 O O   . LYS B 114 ? 0.4622 0.4201 0.4095 -0.0731 -0.0438 -0.0299 339  LYS B O   
3316 C CB  . LYS B 114 ? 0.3109 0.2849 0.2541 -0.0665 -0.0464 -0.0302 339  LYS B CB  
3317 C CG  . LYS B 114 ? 0.4080 0.3937 0.3538 -0.0626 -0.0471 -0.0277 339  LYS B CG  
3318 C CD  . LYS B 114 ? 0.4794 0.4694 0.4201 -0.0660 -0.0519 -0.0297 339  LYS B CD  
3319 C CE  . LYS B 114 ? 0.7889 0.7886 0.7307 -0.0615 -0.0522 -0.0272 339  LYS B CE  
3320 N NZ  . LYS B 114 ? 0.7490 0.7522 0.6844 -0.0643 -0.0568 -0.0290 339  LYS B NZ  
3321 N N   . VAL B 115 ? 0.2549 0.1960 0.1896 -0.0648 -0.0383 -0.0342 340  VAL B N   
3322 C CA  . VAL B 115 ? 0.2547 0.1822 0.1848 -0.0692 -0.0380 -0.0370 340  VAL B CA  
3323 C C   . VAL B 115 ? 0.3395 0.2588 0.2711 -0.0644 -0.0332 -0.0349 340  VAL B C   
3324 O O   . VAL B 115 ? 0.2863 0.2093 0.2204 -0.0575 -0.0303 -0.0326 340  VAL B O   
3325 C CB  . VAL B 115 ? 0.3885 0.3047 0.3064 -0.0712 -0.0389 -0.0432 340  VAL B CB  
3326 C CG1 . VAL B 115 ? 0.4096 0.3347 0.3259 -0.0764 -0.0443 -0.0448 340  VAL B CG1 
3327 C CG2 . VAL B 115 ? 0.4563 0.3672 0.3677 -0.0636 -0.0349 -0.0449 340  VAL B CG2 
3328 N N   . ALA B 116 ? 0.4009 0.3093 0.3312 -0.0682 -0.0325 -0.0356 341  ALA B N   
3329 C CA  . ALA B 116 ? 0.3926 0.2932 0.3244 -0.0639 -0.0283 -0.0330 341  ALA B CA  
3330 C C   . ALA B 116 ? 0.4696 0.3600 0.3941 -0.0570 -0.0245 -0.0356 341  ALA B C   
3331 O O   . ALA B 116 ? 0.3816 0.2671 0.2980 -0.0568 -0.0248 -0.0402 341  ALA B O   
3332 C CB  . ALA B 116 ? 0.4616 0.3516 0.3931 -0.0699 -0.0283 -0.0330 341  ALA B CB  
3333 N N   . ASN B 117 ? 0.2995 0.1874 0.2271 -0.0512 -0.0208 -0.0322 342  ASN B N   
3334 C CA  . ASN B 117 ? 0.3510 0.2308 0.2739 -0.0437 -0.0166 -0.0333 342  ASN B CA  
3335 C C   . ASN B 117 ? 0.3241 0.2128 0.2465 -0.0388 -0.0162 -0.0342 342  ASN B C   
3336 O O   . ASN B 117 ? 0.3130 0.1950 0.2296 -0.0339 -0.0132 -0.0368 342  ASN B O   
3337 C CB  . ASN B 117 ? 0.4102 0.2716 0.3231 -0.0451 -0.0150 -0.0381 342  ASN B CB  
3338 C CG  . ASN B 117 ? 0.5687 0.4185 0.4823 -0.0466 -0.0133 -0.0361 342  ASN B CG  
3339 O OD1 . ASN B 117 ? 0.6216 0.4661 0.5342 -0.0541 -0.0155 -0.0372 342  ASN B OD1 
3340 N ND2 . ASN B 117 ? 0.5987 0.4453 0.5145 -0.0395 -0.0095 -0.0327 342  ASN B ND2 
3341 N N   . THR B 118 ? 0.2710 0.1747 0.1993 -0.0399 -0.0187 -0.0320 343  THR B N   
3342 C CA  . THR B 118 ? 0.2309 0.1435 0.1596 -0.0352 -0.0180 -0.0320 343  THR B CA  
3343 C C   . THR B 118 ? 0.2353 0.1591 0.1728 -0.0309 -0.0169 -0.0271 343  THR B C   
3344 O O   . THR B 118 ? 0.2390 0.1704 0.1777 -0.0272 -0.0161 -0.0267 343  THR B O   
3345 C CB  . THR B 118 ? 0.2270 0.1470 0.1537 -0.0394 -0.0217 -0.0340 343  THR B CB  
3346 O OG1 . THR B 118 ? 0.2635 0.1933 0.1976 -0.0439 -0.0250 -0.0310 343  THR B OG1 
3347 C CG2 . THR B 118 ? 0.2682 0.1775 0.1849 -0.0436 -0.0231 -0.0394 343  THR B CG2 
3348 N N   . THR B 119 ? 0.2759 0.2009 0.2192 -0.0316 -0.0168 -0.0234 344  THR B N   
3349 C CA  . THR B 119 ? 0.2403 0.1749 0.1908 -0.0275 -0.0157 -0.0191 344  THR B CA  
3350 C C   . THR B 119 ? 0.2844 0.2138 0.2339 -0.0209 -0.0121 -0.0185 344  THR B C   
3351 O O   . THR B 119 ? 0.2689 0.1877 0.2159 -0.0199 -0.0104 -0.0184 344  THR B O   
3352 C CB  . THR B 119 ? 0.2299 0.1679 0.1863 -0.0305 -0.0168 -0.0153 344  THR B CB  
3353 O OG1 . THR B 119 ? 0.2512 0.1964 0.2100 -0.0361 -0.0200 -0.0155 344  THR B OG1 
3354 C CG2 . THR B 119 ? 0.2300 0.1765 0.1924 -0.0261 -0.0156 -0.0112 344  THR B CG2 
3355 N N   . GLY B 120 ? 0.2350 0.1721 0.1865 -0.0163 -0.0109 -0.0179 345  GLY B N   
3356 C CA  . GLY B 120 ? 0.2219 0.1564 0.1737 -0.0098 -0.0076 -0.0170 345  GLY B CA  
3357 C C   . GLY B 120 ? 0.2351 0.1819 0.1930 -0.0062 -0.0071 -0.0144 345  GLY B C   
3358 O O   . GLY B 120 ? 0.2206 0.1767 0.1812 -0.0085 -0.0090 -0.0139 345  GLY B O   
3359 N N   . GLY B 121 ? 0.2095 0.1560 0.1693 -0.0006 -0.0046 -0.0127 346  GLY B N   
3360 C CA  . GLY B 121 ? 0.1855 0.1428 0.1503 0.0030  -0.0038 -0.0110 346  GLY B CA  
3361 C C   . GLY B 121 ? 0.1971 0.1520 0.1592 0.0074  -0.0007 -0.0132 346  GLY B C   
3362 O O   . GLY B 121 ? 0.2085 0.1526 0.1652 0.0090  0.0013  -0.0155 346  GLY B O   
3363 N N   . GLY B 122 ? 0.1792 0.1438 0.1447 0.0093  0.0000  -0.0128 347  GLY B N   
3364 C CA  . GLY B 122 ? 0.1912 0.1554 0.1552 0.0137  0.0034  -0.0144 347  GLY B CA  
3365 C C   . GLY B 122 ? 0.1634 0.1403 0.1333 0.0147  0.0036  -0.0127 347  GLY B C   
3366 O O   . GLY B 122 ? 0.1876 0.1722 0.1627 0.0130  0.0014  -0.0101 347  GLY B O   
3367 N N   . GLU B 123 ? 0.1754 0.1540 0.1440 0.0175  0.0066  -0.0141 348  GLU B N   
3368 C CA  . GLU B 123 ? 0.1871 0.1774 0.1614 0.0181  0.0072  -0.0125 348  GLU B CA  
3369 C C   . GLU B 123 ? 0.2116 0.2017 0.1816 0.0188  0.0100  -0.0150 348  GLU B C   
3370 O O   . GLU B 123 ? 0.2111 0.1926 0.1745 0.0206  0.0123  -0.0177 348  GLU B O   
3371 C CB  . GLU B 123 ? 0.1977 0.1946 0.1796 0.0227  0.0086  -0.0095 348  GLU B CB  
3372 C CG  . GLU B 123 ? 0.2468 0.2390 0.2274 0.0286  0.0127  -0.0103 348  GLU B CG  
3373 C CD  . GLU B 123 ? 0.3445 0.3436 0.3331 0.0334  0.0135  -0.0067 348  GLU B CD  
3374 O OE1 . GLU B 123 ? 0.3015 0.3063 0.2949 0.0319  0.0104  -0.0039 348  GLU B OE1 
3375 O OE2 . GLU B 123 ? 0.2938 0.2931 0.2838 0.0388  0.0173  -0.0066 348  GLU B OE2 
3376 N N   . ILE B 124 ? 0.1941 0.1933 0.1675 0.0175  0.0100  -0.0140 349  ILE B N   
3377 C CA  . ILE B 124 ? 0.1761 0.1771 0.1468 0.0187  0.0133  -0.0154 349  ILE B CA  
3378 C C   . ILE B 124 ? 0.1610 0.1712 0.1396 0.0224  0.0160  -0.0130 349  ILE B C   
3379 O O   . ILE B 124 ? 0.1842 0.2035 0.1699 0.0208  0.0144  -0.0106 349  ILE B O   
3380 C CB  . ILE B 124 ? 0.1683 0.1722 0.1365 0.0143  0.0115  -0.0157 349  ILE B CB  
3381 C CG1 . ILE B 124 ? 0.1772 0.1741 0.1393 0.0105  0.0081  -0.0174 349  ILE B CG1 
3382 C CG2 . ILE B 124 ? 0.1693 0.1741 0.1336 0.0156  0.0152  -0.0169 349  ILE B CG2 
3383 C CD1 . ILE B 124 ? 0.2093 0.2103 0.1709 0.0064  0.0056  -0.0167 349  ILE B CD1 
3384 N N   . LYS B 125 ? 0.1874 0.1956 0.1652 0.0272  0.0202  -0.0138 350  LYS B N   
3385 C CA  . LYS B 125 ? 0.1776 0.1958 0.1635 0.0308  0.0232  -0.0116 350  LYS B CA  
3386 C C   . LYS B 125 ? 0.1728 0.1981 0.1595 0.0284  0.0247  -0.0114 350  LYS B C   
3387 O O   . LYS B 125 ? 0.1892 0.2098 0.1684 0.0259  0.0249  -0.0134 350  LYS B O   
3388 C CB  . LYS B 125 ? 0.2317 0.2456 0.2162 0.0371  0.0278  -0.0125 350  LYS B CB  
3389 C CG  . LYS B 125 ? 0.2822 0.2897 0.2673 0.0400  0.0267  -0.0118 350  LYS B CG  
3390 C CD  . LYS B 125 ? 0.4405 0.4392 0.4210 0.0459  0.0314  -0.0137 350  LYS B CD  
3391 C CE  . LYS B 125 ? 0.4784 0.4712 0.4606 0.0495  0.0306  -0.0122 350  LYS B CE  
3392 N NZ  . LYS B 125 ? 0.3257 0.3108 0.3039 0.0448  0.0259  -0.0127 350  LYS B NZ  
3393 N N   . SER B 126 ? 0.1695 0.2063 0.1654 0.0290  0.0256  -0.0087 351  SER B N   
3394 C CA  . SER B 126 ? 0.1704 0.2140 0.1679 0.0261  0.0270  -0.0080 351  SER B CA  
3395 C C   . SER B 126 ? 0.1985 0.2377 0.1885 0.0276  0.0315  -0.0100 351  SER B C   
3396 O O   . SER B 126 ? 0.1950 0.2329 0.1800 0.0242  0.0314  -0.0106 351  SER B O   
3397 C CB  . SER B 126 ? 0.1714 0.2279 0.1801 0.0269  0.0280  -0.0051 351  SER B CB  
3398 O OG  . SER B 126 ? 0.1621 0.2244 0.1724 0.0231  0.0291  -0.0044 351  SER B OG  
3399 N N   A THR B 127 ? 0.1839 0.2206 0.1728 0.0329  0.0356  -0.0110 352  THR B N   
3400 N N   B THR B 127 ? 0.1856 0.2223 0.1744 0.0329  0.0356  -0.0110 352  THR B N   
3401 C CA  A THR B 127 ? 0.2185 0.2508 0.1995 0.0348  0.0404  -0.0131 352  THR B CA  
3402 C CA  B THR B 127 ? 0.2184 0.2506 0.1993 0.0347  0.0404  -0.0131 352  THR B CA  
3403 C C   A THR B 127 ? 0.2265 0.2471 0.1949 0.0320  0.0384  -0.0163 352  THR B C   
3404 C C   B THR B 127 ? 0.2251 0.2460 0.1936 0.0317  0.0382  -0.0163 352  THR B C   
3405 O O   A THR B 127 ? 0.2412 0.2591 0.2020 0.0315  0.0410  -0.0178 352  THR B O   
3406 O O   B THR B 127 ? 0.2390 0.2575 0.2001 0.0309  0.0406  -0.0176 352  THR B O   
3407 C CB  A THR B 127 ? 0.2099 0.2405 0.1916 0.0416  0.0454  -0.0138 352  THR B CB  
3408 C CB  B THR B 127 ? 0.2111 0.2410 0.1922 0.0415  0.0452  -0.0140 352  THR B CB  
3409 O OG1 A THR B 127 ? 0.2484 0.2775 0.2239 0.0435  0.0509  -0.0154 352  THR B OG1 
3410 O OG1 B THR B 127 ? 0.2701 0.2917 0.2493 0.0434  0.0429  -0.0151 352  THR B OG1 
3411 C CG2 A THR B 127 ? 0.3000 0.3183 0.2754 0.0437  0.0439  -0.0163 352  THR B CG2 
3412 C CG2 B THR B 127 ? 0.1940 0.2374 0.1877 0.0445  0.0480  -0.0106 352  THR B CG2 
3413 N N   . ASP B 128 ? 0.1796 0.1938 0.1457 0.0299  0.0337  -0.0173 353  ASP B N   
3414 C CA  . ASP B 128 ? 0.1994 0.2038 0.1549 0.0266  0.0310  -0.0201 353  ASP B CA  
3415 C C   . ASP B 128 ? 0.2083 0.2162 0.1645 0.0211  0.0266  -0.0187 353  ASP B C   
3416 O O   . ASP B 128 ? 0.2189 0.2207 0.1673 0.0181  0.0239  -0.0205 353  ASP B O   
3417 C CB  . ASP B 128 ? 0.1930 0.1880 0.1455 0.0274  0.0288  -0.0220 353  ASP B CB  
3418 C CG  . ASP B 128 ? 0.2213 0.2101 0.1710 0.0332  0.0335  -0.0238 353  ASP B CG  
3419 O OD1 . ASP B 128 ? 0.2652 0.2519 0.2090 0.0355  0.0380  -0.0257 353  ASP B OD1 
3420 O OD2 . ASP B 128 ? 0.2556 0.2411 0.2086 0.0356  0.0329  -0.0233 353  ASP B OD2 
3421 N N   . TYR B 129 ? 0.1843 0.2019 0.1497 0.0198  0.0257  -0.0156 354  TYR B N   
3422 C CA  . TYR B 129 ? 0.1760 0.1963 0.1423 0.0150  0.0220  -0.0142 354  TYR B CA  
3423 C C   . TYR B 129 ? 0.1929 0.2149 0.1549 0.0137  0.0243  -0.0139 354  TYR B C   
3424 O O   . TYR B 129 ? 0.1889 0.2181 0.1562 0.0127  0.0257  -0.0116 354  TYR B O   
3425 C CB  . TYR B 129 ? 0.1503 0.1789 0.1270 0.0138  0.0201  -0.0115 354  TYR B CB  
3426 C CG  . TYR B 129 ? 0.1344 0.1636 0.1111 0.0093  0.0162  -0.0106 354  TYR B CG  
3427 C CD1 . TYR B 129 ? 0.1725 0.1965 0.1463 0.0075  0.0122  -0.0114 354  TYR B CD1 
3428 C CD2 . TYR B 129 ? 0.1338 0.1687 0.1135 0.0070  0.0167  -0.0087 354  TYR B CD2 
3429 C CE1 . TYR B 129 ? 0.1777 0.2028 0.1520 0.0040  0.0090  -0.0105 354  TYR B CE1 
3430 C CE2 . TYR B 129 ? 0.1351 0.1698 0.1146 0.0035  0.0134  -0.0079 354  TYR B CE2 
3431 C CZ  . TYR B 129 ? 0.1711 0.2013 0.1481 0.0023  0.0097  -0.0087 354  TYR B CZ  
3432 O OH  . TYR B 129 ? 0.1672 0.1976 0.1444 -0.0006 0.0069  -0.0077 354  TYR B OH  
3433 N N   . THR B 130 ? 0.1747 0.1893 0.1261 0.0135  0.0245  -0.0162 355  THR B N   
3434 C CA  . THR B 130 ? 0.2006 0.2156 0.1459 0.0125  0.0265  -0.0159 355  THR B CA  
3435 C C   . THR B 130 ? 0.1939 0.2038 0.1313 0.0093  0.0223  -0.0168 355  THR B C   
3436 O O   . THR B 130 ? 0.1988 0.2032 0.1259 0.0095  0.0230  -0.0188 355  THR B O   
3437 C CB  . THR B 130 ? 0.2515 0.2638 0.1909 0.0162  0.0319  -0.0177 355  THR B CB  
3438 O OG1 . THR B 130 ? 0.2353 0.2384 0.1673 0.0178  0.0313  -0.0213 355  THR B OG1 
3439 C CG2 . THR B 130 ? 0.2309 0.2506 0.1798 0.0196  0.0364  -0.0160 355  THR B CG2 
3440 N N   . PRO B 131 ? 0.1673 0.1795 0.1092 0.0063  0.0180  -0.0151 356  PRO B N   
3441 C CA  . PRO B 131 ? 0.1627 0.1711 0.0984 0.0035  0.0136  -0.0157 356  PRO B CA  
3442 C C   . PRO B 131 ? 0.2223 0.2309 0.1511 0.0025  0.0142  -0.0147 356  PRO B C   
3443 O O   . PRO B 131 ? 0.2135 0.2185 0.1350 0.0008  0.0110  -0.0157 356  PRO B O   
3444 C CB  . PRO B 131 ? 0.1521 0.1644 0.0959 0.0012  0.0100  -0.0137 356  PRO B CB  
3445 C CG  . PRO B 131 ? 0.1734 0.1925 0.1258 0.0020  0.0128  -0.0113 356  PRO B CG  
3446 C CD  . PRO B 131 ? 0.1847 0.2034 0.1372 0.0054  0.0170  -0.0126 356  PRO B CD  
3447 N N   . ALA B 132 ? 0.1875 0.2002 0.1181 0.0034  0.0181  -0.0125 357  ALA B N   
3448 C CA  . ALA B 132 ? 0.2006 0.2128 0.1238 0.0027  0.0191  -0.0111 357  ALA B CA  
3449 C C   . ALA B 132 ? 0.2424 0.2487 0.1537 0.0039  0.0201  -0.0140 357  ALA B C   
3450 O O   . ALA B 132 ? 0.2472 0.2519 0.1501 0.0029  0.0190  -0.0133 357  ALA B O   
3451 C CB  . ALA B 132 ? 0.2023 0.2196 0.1298 0.0033  0.0238  -0.0082 357  ALA B CB  
3452 N N   . LEU B 133 ? 0.1899 0.1925 0.0996 0.0060  0.0219  -0.0173 358  LEU B N   
3453 C CA  . LEU B 133 ? 0.2569 0.2525 0.1544 0.0071  0.0231  -0.0208 358  LEU B CA  
3454 C C   . LEU B 133 ? 0.2412 0.2313 0.1323 0.0045  0.0174  -0.0233 358  LEU B C   
3455 O O   . LEU B 133 ? 0.2867 0.2705 0.1664 0.0044  0.0174  -0.0266 358  LEU B O   
3456 C CB  . LEU B 133 ? 0.3064 0.2993 0.2049 0.0108  0.0277  -0.0234 358  LEU B CB  
3457 C CG  . LEU B 133 ? 0.2334 0.2325 0.1381 0.0137  0.0338  -0.0212 358  LEU B CG  
3458 C CD1 . LEU B 133 ? 0.2696 0.2661 0.1750 0.0181  0.0383  -0.0237 358  LEU B CD1 
3459 C CD2 . LEU B 133 ? 0.2848 0.2852 0.1822 0.0136  0.0371  -0.0196 358  LEU B CD2 
3460 N N   . GLY B 134 ? 0.2384 0.2309 0.1364 0.0020  0.0126  -0.0220 359  GLY B N   
3461 C CA  . GLY B 134 ? 0.2754 0.2647 0.1688 -0.0011 0.0069  -0.0236 359  GLY B CA  
3462 C C   . GLY B 134 ? 0.2974 0.2818 0.1928 -0.0018 0.0050  -0.0265 359  GLY B C   
3463 O O   . GLY B 134 ? 0.2424 0.2244 0.1351 -0.0049 0.0003  -0.0279 359  GLY B O   
3464 N N   . GLY B 135 ? 0.2524 0.2356 0.1528 0.0010  0.0086  -0.0273 360  GLY B N   
3465 C CA  . GLY B 135 ? 0.2349 0.2128 0.1374 0.0009  0.0073  -0.0296 360  GLY B CA  
3466 C C   . GLY B 135 ? 0.2696 0.2505 0.1820 0.0040  0.0105  -0.0280 360  GLY B C   
3467 O O   . GLY B 135 ? 0.2386 0.2255 0.1556 0.0063  0.0140  -0.0258 360  GLY B O   
3468 N N   . VAL B 136 ? 0.2395 0.2167 0.1553 0.0040  0.0091  -0.0290 361  VAL B N   
3469 C CA  . VAL B 136 ? 0.1875 0.1670 0.1119 0.0074  0.0118  -0.0276 361  VAL B CA  
3470 C C   . VAL B 136 ? 0.2349 0.2048 0.1560 0.0090  0.0127  -0.0305 361  VAL B C   
3471 O O   . VAL B 136 ? 0.2594 0.2228 0.1761 0.0060  0.0093  -0.0325 361  VAL B O   
3472 C CB  . VAL B 136 ? 0.2412 0.2281 0.1762 0.0058  0.0090  -0.0241 361  VAL B CB  
3473 C CG1 . VAL B 136 ? 0.3021 0.2980 0.2417 0.0054  0.0097  -0.0210 361  VAL B CG1 
3474 C CG2 . VAL B 136 ? 0.2893 0.2739 0.2237 0.0016  0.0039  -0.0243 361  VAL B CG2 
3475 N N   . LYS B 137 ? 0.2238 0.1931 0.1473 0.0139  0.0172  -0.0305 362  LYS B N   
3476 C CA  . LYS B 137 ? 0.2183 0.1787 0.1401 0.0166  0.0188  -0.0325 362  LYS B CA  
3477 C C   . LYS B 137 ? 0.2530 0.2173 0.1851 0.0172  0.0171  -0.0293 362  LYS B C   
3478 O O   . LYS B 137 ? 0.2462 0.2194 0.1870 0.0198  0.0186  -0.0262 362  LYS B O   
3479 C CB  . LYS B 137 ? 0.2565 0.2145 0.1755 0.0223  0.0250  -0.0339 362  LYS B CB  
3480 C CG  . LYS B 137 ? 0.2258 0.1748 0.1442 0.0264  0.0275  -0.0354 362  LYS B CG  
3481 C CD  . LYS B 137 ? 0.3042 0.2533 0.2219 0.0329  0.0341  -0.0360 362  LYS B CD  
3482 C CE  . LYS B 137 ? 0.4376 0.3771 0.3544 0.0378  0.0371  -0.0374 362  LYS B CE  
3483 N NZ  . LYS B 137 ? 0.4378 0.3775 0.3538 0.0445  0.0440  -0.0380 362  LYS B NZ  
3484 N N   . ILE B 138 ? 0.2041 0.1621 0.1351 0.0144  0.0136  -0.0300 363  ILE B N   
3485 C CA  . ILE B 138 ? 0.1933 0.1537 0.1325 0.0147  0.0119  -0.0271 363  ILE B CA  
3486 C C   . ILE B 138 ? 0.2213 0.1731 0.1594 0.0193  0.0150  -0.0279 363  ILE B C   
3487 O O   . ILE B 138 ? 0.2617 0.2018 0.1913 0.0191  0.0159  -0.0315 363  ILE B O   
3488 C CB  . ILE B 138 ? 0.2023 0.1611 0.1414 0.0091  0.0069  -0.0268 363  ILE B CB  
3489 C CG1 . ILE B 138 ? 0.1931 0.1604 0.1334 0.0053  0.0041  -0.0257 363  ILE B CG1 
3490 C CG2 . ILE B 138 ? 0.1994 0.1598 0.1460 0.0096  0.0055  -0.0237 363  ILE B CG2 
3491 C CD1 . ILE B 138 ? 0.2619 0.2281 0.2014 -0.0002 -0.0006 -0.0258 363  ILE B CD1 
3492 N N   . THR B 139 ? 0.2011 0.1586 0.1475 0.0236  0.0166  -0.0247 364  THR B N   
3493 C CA  . THR B 139 ? 0.2099 0.1603 0.1565 0.0288  0.0197  -0.0246 364  THR B CA  
3494 C C   . THR B 139 ? 0.2020 0.1531 0.1547 0.0286  0.0170  -0.0212 364  THR B C   
3495 O O   . THR B 139 ? 0.2258 0.1839 0.1830 0.0246  0.0132  -0.0190 364  THR B O   
3496 C CB  . THR B 139 ? 0.2373 0.1940 0.1882 0.0352  0.0245  -0.0235 364  THR B CB  
3497 O OG1 . THR B 139 ? 0.2355 0.2069 0.1960 0.0348  0.0233  -0.0198 364  THR B OG1 
3498 C CG2 . THR B 139 ? 0.2505 0.2035 0.1933 0.0360  0.0281  -0.0272 364  THR B CG2 
3499 N N   . ALA B 140 ? 0.2754 0.2184 0.2276 0.0330  0.0192  -0.0208 365  ALA B N   
3500 C CA  . ALA B 140 ? 0.2607 0.2014 0.2167 0.0329  0.0170  -0.0177 365  ALA B CA  
3501 C C   . ALA B 140 ? 0.2094 0.1451 0.1618 0.0258  0.0129  -0.0187 365  ALA B C   
3502 O O   . ALA B 140 ? 0.2338 0.1727 0.1907 0.0238  0.0100  -0.0155 365  ALA B O   
3503 C CB  . ALA B 140 ? 0.2169 0.1714 0.1833 0.0350  0.0158  -0.0128 365  ALA B CB  
3504 N N   . TRP B 141 ? 0.2373 0.1656 0.1814 0.0220  0.0125  -0.0230 366  TRP B N   
3505 C CA  . TRP B 141 ? 0.2603 0.1845 0.2012 0.0150  0.0085  -0.0241 366  TRP B CA  
3506 C C   . TRP B 141 ? 0.2633 0.1744 0.2011 0.0146  0.0087  -0.0242 366  TRP B C   
3507 O O   . TRP B 141 ? 0.2746 0.1738 0.2064 0.0176  0.0119  -0.0268 366  TRP B O   
3508 C CB  . TRP B 141 ? 0.2433 0.1643 0.1761 0.0111  0.0078  -0.0287 366  TRP B CB  
3509 C CG  . TRP B 141 ? 0.2314 0.1490 0.1612 0.0039  0.0036  -0.0300 366  TRP B CG  
3510 C CD1 . TRP B 141 ? 0.2626 0.1674 0.1844 0.0004  0.0030  -0.0337 366  TRP B CD1 
3511 C CD2 . TRP B 141 ? 0.2107 0.1380 0.1458 -0.0008 -0.0005 -0.0276 366  TRP B CD2 
3512 N NE1 . TRP B 141 ? 0.2728 0.1799 0.1952 -0.0064 -0.0015 -0.0335 366  TRP B NE1 
3513 C CE2 . TRP B 141 ? 0.2436 0.1644 0.1742 -0.0070 -0.0035 -0.0298 366  TRP B CE2 
3514 C CE3 . TRP B 141 ? 0.2375 0.1780 0.1805 -0.0005 -0.0017 -0.0240 366  TRP B CE3 
3515 C CZ2 . TRP B 141 ? 0.2460 0.1741 0.1806 -0.0123 -0.0075 -0.0280 366  TRP B CZ2 
3516 C CZ3 . TRP B 141 ? 0.2361 0.1826 0.1822 -0.0056 -0.0055 -0.0226 366  TRP B CZ3 
3517 C CH2 . TRP B 141 ? 0.2132 0.1541 0.1555 -0.0112 -0.0082 -0.0245 366  TRP B CH2 
3518 N N   . ASP B 142 ? 0.2228 0.1355 0.1645 0.0110  0.0057  -0.0213 367  ASP B N   
3519 C CA  . ASP B 142 ? 0.2620 0.1635 0.2024 0.0115  0.0063  -0.0200 367  ASP B CA  
3520 C C   . ASP B 142 ? 0.3165 0.2086 0.2518 0.0043  0.0038  -0.0222 367  ASP B C   
3521 O O   . ASP B 142 ? 0.2795 0.1626 0.2142 0.0036  0.0041  -0.0206 367  ASP B O   
3522 C CB  . ASP B 142 ? 0.2800 0.1893 0.2286 0.0140  0.0055  -0.0143 367  ASP B CB  
3523 C CG  . ASP B 142 ? 0.3000 0.2203 0.2536 0.0088  0.0017  -0.0121 367  ASP B CG  
3524 O OD1 . ASP B 142 ? 0.2391 0.1595 0.1902 0.0028  -0.0007 -0.0144 367  ASP B OD1 
3525 O OD2 . ASP B 142 ? 0.3276 0.2566 0.2875 0.0109  0.0010  -0.0079 367  ASP B OD2 
3526 N N   . ALA B 143 ? 0.2788 0.1729 0.2106 -0.0011 0.0015  -0.0256 368  ALA B N   
3527 C CA  . ALA B 143 ? 0.2535 0.1392 0.1804 -0.0082 -0.0010 -0.0281 368  ALA B CA  
3528 C C   . ALA B 143 ? 0.2639 0.1360 0.1803 -0.0085 0.0008  -0.0338 368  ALA B C   
3529 O O   . ALA B 143 ? 0.3478 0.2202 0.2608 -0.0043 0.0033  -0.0361 368  ALA B O   
3530 C CB  . ALA B 143 ? 0.2837 0.1805 0.2134 -0.0143 -0.0053 -0.0280 368  ALA B CB  
3531 N N   . THR B 144 ? 0.2907 0.1505 0.2019 -0.0139 -0.0004 -0.0362 369  THR B N   
3532 C CA  . THR B 144 ? 0.3098 0.1548 0.2099 -0.0146 0.0014  -0.0421 369  THR B CA  
3533 C C   . THR B 144 ? 0.3411 0.1905 0.2358 -0.0192 -0.0014 -0.0463 369  THR B C   
3534 O O   . THR B 144 ? 0.3813 0.2225 0.2668 -0.0177 0.0006  -0.0512 369  THR B O   
3535 C CB  . THR B 144 ? 0.4357 0.2652 0.3315 -0.0194 0.0010  -0.0434 369  THR B CB  
3536 O OG1 . THR B 144 ? 0.3759 0.2112 0.2749 -0.0279 -0.0038 -0.0427 369  THR B OG1 
3537 C CG2 . THR B 144 ? 0.4271 0.2510 0.3274 -0.0144 0.0041  -0.0388 369  THR B CG2 
3538 N N   . GLY B 145 ? 0.3365 0.1981 0.2363 -0.0245 -0.0060 -0.0446 370  GLY B N   
3539 C CA  . GLY B 145 ? 0.3336 0.2019 0.2295 -0.0280 -0.0089 -0.0475 370  GLY B CA  
3540 C C   . GLY B 145 ? 0.2961 0.1806 0.1987 -0.0243 -0.0090 -0.0442 370  GLY B C   
3541 O O   . GLY B 145 ? 0.2902 0.1808 0.2003 -0.0193 -0.0069 -0.0401 370  GLY B O   
3542 N N   . PRO B 146 ? 0.2600 0.1519 0.1600 -0.0271 -0.0118 -0.0458 371  PRO B N   
3543 C CA  . PRO B 146 ? 0.2703 0.1580 0.1623 -0.0337 -0.0154 -0.0501 371  PRO B CA  
3544 C C   . PRO B 146 ? 0.3367 0.2125 0.2160 -0.0326 -0.0132 -0.0559 371  PRO B C   
3545 O O   . PRO B 146 ? 0.3181 0.1906 0.1947 -0.0260 -0.0084 -0.0565 371  PRO B O   
3546 C CB  . PRO B 146 ? 0.2574 0.1605 0.1533 -0.0353 -0.0188 -0.0480 371  PRO B CB  
3547 C CG  . PRO B 146 ? 0.2474 0.1574 0.1471 -0.0281 -0.0151 -0.0454 371  PRO B CG  
3548 C CD  . PRO B 146 ? 0.2454 0.1519 0.1513 -0.0242 -0.0119 -0.0427 371  PRO B CD  
3549 N N   A SER B 147 ? 0.2993 0.1689 0.1705 -0.0392 -0.0166 -0.0602 372  SER B N   
3550 N N   B SER B 147 ? 0.2995 0.1689 0.1706 -0.0392 -0.0166 -0.0603 372  SER B N   
3551 C CA  A SER B 147 ? 0.3148 0.1755 0.1727 -0.0390 -0.0154 -0.0660 372  SER B CA  
3552 C CA  B SER B 147 ? 0.3147 0.1755 0.1726 -0.0390 -0.0155 -0.0660 372  SER B CA  
3553 C C   A SER B 147 ? 0.3090 0.1822 0.1659 -0.0374 -0.0167 -0.0652 372  SER B C   
3554 C C   B SER B 147 ? 0.3087 0.1821 0.1657 -0.0375 -0.0167 -0.0651 372  SER B C   
3555 O O   A SER B 147 ? 0.2982 0.1855 0.1648 -0.0360 -0.0178 -0.0602 372  SER B O   
3556 O O   B SER B 147 ? 0.2959 0.1834 0.1626 -0.0362 -0.0180 -0.0602 372  SER B O   
3557 C CB  A SER B 147 ? 0.4179 0.2680 0.2672 -0.0471 -0.0192 -0.0711 372  SER B CB  
3558 C CB  B SER B 147 ? 0.4197 0.2700 0.2689 -0.0472 -0.0192 -0.0711 372  SER B CB  
3559 O OG  A SER B 147 ? 0.3980 0.2358 0.2484 -0.0485 -0.0176 -0.0715 372  SER B OG  
3560 O OG  B SER B 147 ? 0.4164 0.2777 0.2711 -0.0542 -0.0255 -0.0692 372  SER B OG  
3561 N N   . ALA B 148 ? 0.3648 0.2323 0.2093 -0.0377 -0.0162 -0.0700 373  ALA B N   
3562 C CA  . ALA B 148 ? 0.3313 0.2091 0.1734 -0.0357 -0.0167 -0.0691 373  ALA B CA  
3563 C C   . ALA B 148 ? 0.3078 0.1968 0.1521 -0.0421 -0.0235 -0.0676 373  ALA B C   
3564 O O   . ALA B 148 ? 0.3151 0.2008 0.1571 -0.0491 -0.0282 -0.0698 373  ALA B O   
3565 C CB  . ALA B 148 ? 0.4204 0.2881 0.2475 -0.0337 -0.0136 -0.0747 373  ALA B CB  
3566 N N   . GLY B 149 ? 0.3111 0.2134 0.1598 -0.0396 -0.0241 -0.0637 374  GLY B N   
3567 C CA  . GLY B 149 ? 0.2895 0.2032 0.1401 -0.0442 -0.0301 -0.0618 374  GLY B CA  
3568 C C   . GLY B 149 ? 0.2820 0.2053 0.1459 -0.0472 -0.0336 -0.0572 374  GLY B C   
3569 O O   . GLY B 149 ? 0.3020 0.2333 0.1677 -0.0520 -0.0391 -0.0561 374  GLY B O   
3570 N N   . VAL B 150 ? 0.2661 0.1893 0.1395 -0.0441 -0.0305 -0.0543 375  VAL B N   
3571 C CA  . VAL B 150 ? 0.2546 0.1850 0.1399 -0.0468 -0.0329 -0.0503 375  VAL B CA  
3572 C C   . VAL B 150 ? 0.2371 0.1802 0.1322 -0.0425 -0.0318 -0.0448 375  VAL B C   
3573 O O   . VAL B 150 ? 0.2326 0.1754 0.1288 -0.0366 -0.0273 -0.0437 375  VAL B O   
3574 C CB  . VAL B 150 ? 0.2866 0.2071 0.1747 -0.0467 -0.0303 -0.0508 375  VAL B CB  
3575 C CG1 . VAL B 150 ? 0.2777 0.2061 0.1783 -0.0484 -0.0319 -0.0460 375  VAL B CG1 
3576 C CG2 . VAL B 150 ? 0.3076 0.2143 0.1857 -0.0519 -0.0317 -0.0564 375  VAL B CG2 
3577 N N   . GLU B 151 ? 0.2278 0.1820 0.1302 -0.0454 -0.0358 -0.0415 376  GLU B N   
3578 C CA  . GLU B 151 ? 0.2121 0.1774 0.1238 -0.0416 -0.0347 -0.0365 376  GLU B CA  
3579 C C   . GLU B 151 ? 0.2044 0.1688 0.1244 -0.0391 -0.0315 -0.0340 376  GLU B C   
3580 O O   . GLU B 151 ? 0.2545 0.2147 0.1772 -0.0421 -0.0322 -0.0343 376  GLU B O   
3581 C CB  . GLU B 151 ? 0.2518 0.2288 0.1696 -0.0450 -0.0394 -0.0334 376  GLU B CB  
3582 C CG  . GLU B 151 ? 0.4271 0.4079 0.3381 -0.0470 -0.0430 -0.0345 376  GLU B CG  
3583 C CD  . GLU B 151 ? 0.4763 0.4705 0.3950 -0.0475 -0.0463 -0.0301 376  GLU B CD  
3584 O OE1 . GLU B 151 ? 0.7052 0.7053 0.6338 -0.0456 -0.0449 -0.0263 376  GLU B OE1 
3585 O OE2 . GLU B 151 ? 0.6500 0.6488 0.5644 -0.0497 -0.0503 -0.0303 376  GLU B OE2 
3586 N N   . MET B 152 ? 0.1950 0.1634 0.1189 -0.0338 -0.0281 -0.0315 377  MET B N   
3587 C CA  . MET B 152 ? 0.1901 0.1594 0.1218 -0.0310 -0.0254 -0.0288 377  MET B CA  
3588 C C   . MET B 152 ? 0.2198 0.2001 0.1591 -0.0288 -0.0251 -0.0247 377  MET B C   
3589 O O   . MET B 152 ? 0.2275 0.2123 0.1648 -0.0270 -0.0249 -0.0243 377  MET B O   
3590 C CB  . MET B 152 ? 0.2191 0.1807 0.1476 -0.0263 -0.0208 -0.0304 377  MET B CB  
3591 C CG  . MET B 152 ? 0.2557 0.2044 0.1761 -0.0278 -0.0202 -0.0346 377  MET B CG  
3592 S SD  . MET B 152 ? 0.2284 0.1713 0.1531 -0.0311 -0.0212 -0.0338 377  MET B SD  
3593 C CE  . MET B 152 ? 0.2263 0.1712 0.1586 -0.0250 -0.0171 -0.0301 377  MET B CE  
3594 N N   A THR B 153 ? 0.1661 0.1501 0.1134 -0.0287 -0.0250 -0.0218 378  THR B N   
3595 N N   B THR B 153 ? 0.1670 0.1512 0.1144 -0.0288 -0.0251 -0.0218 378  THR B N   
3596 C CA  A THR B 153 ? 0.1635 0.1566 0.1178 -0.0264 -0.0242 -0.0183 378  THR B CA  
3597 C CA  B THR B 153 ? 0.1636 0.1565 0.1177 -0.0263 -0.0241 -0.0184 378  THR B CA  
3598 C C   A THR B 153 ? 0.1844 0.1764 0.1435 -0.0237 -0.0215 -0.0167 378  THR B C   
3599 C C   B THR B 153 ? 0.1845 0.1760 0.1430 -0.0234 -0.0212 -0.0170 378  THR B C   
3600 O O   A THR B 153 ? 0.1982 0.1855 0.1582 -0.0249 -0.0214 -0.0168 378  THR B O   
3601 O O   B THR B 153 ? 0.1887 0.1743 0.1472 -0.0243 -0.0209 -0.0174 378  THR B O   
3602 C CB  A THR B 153 ? 0.2202 0.2209 0.1798 -0.0295 -0.0273 -0.0160 378  THR B CB  
3603 C CB  B THR B 153 ? 0.2255 0.2265 0.1854 -0.0290 -0.0270 -0.0158 378  THR B CB  
3604 O OG1 A THR B 153 ? 0.3127 0.3141 0.2679 -0.0327 -0.0306 -0.0175 378  THR B OG1 
3605 O OG1 B THR B 153 ? 0.2125 0.2118 0.1756 -0.0322 -0.0282 -0.0154 378  THR B OG1 
3606 C CG2 A THR B 153 ? 0.1570 0.1658 0.1218 -0.0269 -0.0264 -0.0129 378  THR B CG2 
3607 C CG2 B THR B 153 ? 0.2476 0.2517 0.2038 -0.0313 -0.0301 -0.0166 378  THR B CG2 
3608 N N   . GLY B 154 ? 0.1439 0.1405 0.1059 -0.0201 -0.0193 -0.0151 379  GLY B N   
3609 C CA  . GLY B 154 ? 0.1996 0.1960 0.1657 -0.0175 -0.0170 -0.0137 379  GLY B CA  
3610 C C   . GLY B 154 ? 0.1648 0.1686 0.1360 -0.0155 -0.0160 -0.0113 379  GLY B C   
3611 O O   . GLY B 154 ? 0.1589 0.1678 0.1310 -0.0160 -0.0167 -0.0104 379  GLY B O   
3612 N N   A GLN B 155 ? 0.1555 0.1597 0.1299 -0.0131 -0.0142 -0.0101 380  GLN B N   
3613 N N   B GLN B 155 ? 0.1554 0.1595 0.1298 -0.0131 -0.0143 -0.0101 380  GLN B N   
3614 C CA  A GLN B 155 ? 0.1529 0.1637 0.1323 -0.0118 -0.0135 -0.0080 380  GLN B CA  
3615 C CA  B GLN B 155 ? 0.1524 0.1630 0.1316 -0.0116 -0.0134 -0.0081 380  GLN B CA  
3616 C C   A GLN B 155 ? 0.1775 0.1885 0.1581 -0.0084 -0.0112 -0.0079 380  GLN B C   
3617 C C   B GLN B 155 ? 0.1704 0.1808 0.1509 -0.0083 -0.0111 -0.0079 380  GLN B C   
3618 O O   A GLN B 155 ? 0.1538 0.1602 0.1335 -0.0068 -0.0104 -0.0082 380  GLN B O   
3619 O O   B GLN B 155 ? 0.1566 0.1624 0.1364 -0.0070 -0.0106 -0.0080 380  GLN B O   
3620 C CB  A GLN B 155 ? 0.1384 0.1516 0.1217 -0.0134 -0.0148 -0.0060 380  GLN B CB  
3621 C CB  B GLN B 155 ? 0.1467 0.1605 0.1300 -0.0133 -0.0147 -0.0060 380  GLN B CB  
3622 C CG  A GLN B 155 ? 0.1469 0.1550 0.1299 -0.0137 -0.0149 -0.0056 380  GLN B CG  
3623 C CG  B GLN B 155 ? 0.1189 0.1386 0.1063 -0.0121 -0.0139 -0.0044 380  GLN B CG  
3624 C CD  A GLN B 155 ? 0.2667 0.2766 0.2524 -0.0163 -0.0163 -0.0038 380  GLN B CD  
3625 C CD  B GLN B 155 ? 0.1747 0.1974 0.1650 -0.0138 -0.0149 -0.0027 380  GLN B CD  
3626 O OE1 A GLN B 155 ? 0.1991 0.2107 0.1851 -0.0191 -0.0178 -0.0039 380  GLN B OE1 
3627 O OE1 B GLN B 155 ? 0.1275 0.1487 0.1176 -0.0159 -0.0161 -0.0024 380  GLN B OE1 
3628 N NE2 A GLN B 155 ? 0.1759 0.1857 0.1636 -0.0153 -0.0157 -0.0019 380  GLN B NE2 
3629 N NE2 B GLN B 155 ? 0.2022 0.2292 0.1950 -0.0130 -0.0142 -0.0017 380  GLN B NE2 
3630 N N   A ILE B 156 ? 0.1553 0.1716 0.1381 -0.0072 -0.0100 -0.0073 381  ILE B N   
3631 N N   B ILE B 156 ? 0.1617 0.1770 0.1441 -0.0068 -0.0098 -0.0075 381  ILE B N   
3632 C CA  A ILE B 156 ? 0.1978 0.2168 0.1836 -0.0044 -0.0081 -0.0066 381  ILE B CA  
3633 C CA  B ILE B 156 ? 0.1588 0.1765 0.1441 -0.0039 -0.0079 -0.0068 381  ILE B CA  
3634 C C   A ILE B 156 ? 0.1411 0.1640 0.1313 -0.0048 -0.0092 -0.0046 381  ILE B C   
3635 C C   B ILE B 156 ? 0.1530 0.1752 0.1430 -0.0042 -0.0089 -0.0048 381  ILE B C   
3636 O O   A ILE B 156 ? 0.1284 0.1548 0.1202 -0.0067 -0.0101 -0.0039 381  ILE B O   
3637 O O   B ILE B 156 ? 0.1602 0.1864 0.1519 -0.0060 -0.0097 -0.0041 381  ILE B O   
3638 C CB  A ILE B 156 ? 0.1705 0.1936 0.1568 -0.0038 -0.0064 -0.0068 381  ILE B CB  
3639 C CB  B ILE B 156 ? 0.1251 0.1464 0.1106 -0.0028 -0.0059 -0.0072 381  ILE B CB  
3640 C CG1 A ILE B 156 ? 0.1930 0.2122 0.1739 -0.0036 -0.0053 -0.0086 381  ILE B CG1 
3641 C CG1 B ILE B 156 ? 0.1371 0.1536 0.1168 -0.0023 -0.0046 -0.0093 381  ILE B CG1 
3642 C CG2 A ILE B 156 ? 0.1083 0.1355 0.0987 -0.0012 -0.0045 -0.0061 381  ILE B CG2 
3643 C CG2 B ILE B 156 ? 0.1405 0.1663 0.1305 -0.0003 -0.0042 -0.0062 381  ILE B CG2 
3644 C CD1 A ILE B 156 ? 0.1922 0.2065 0.1703 -0.0010 -0.0035 -0.0101 381  ILE B CD1 
3645 C CD1 B ILE B 156 ? 0.1181 0.1377 0.0970 -0.0017 -0.0025 -0.0095 381  ILE B CD1 
3646 N N   A GLU B 157 ? 0.1469 0.1689 0.1386 -0.0027 -0.0089 -0.0037 382  GLU B N   
3647 N N   B GLU B 157 ? 0.1397 0.1607 0.1311 -0.0023 -0.0088 -0.0038 382  GLU B N   
3648 C CA  A GLU B 157 ? 0.1258 0.1504 0.1203 -0.0030 -0.0101 -0.0017 382  GLU B CA  
3649 C CA  B GLU B 157 ? 0.1300 0.1539 0.1242 -0.0027 -0.0101 -0.0017 382  GLU B CA  
3650 C C   A GLU B 157 ? 0.1201 0.1507 0.1185 -0.0010 -0.0098 -0.0005 382  GLU B C   
3651 C C   B GLU B 157 ? 0.1206 0.1511 0.1190 -0.0010 -0.0097 -0.0005 382  GLU B C   
3652 O O   A GLU B 157 ? 0.1394 0.1738 0.1397 -0.0019 -0.0110 0.0009  382  GLU B O   
3653 O O   B GLU B 157 ? 0.1442 0.1787 0.1445 -0.0021 -0.0110 0.0007  382  GLU B O   
3654 C CB  A GLU B 157 ? 0.1607 0.1793 0.1535 -0.0025 -0.0107 -0.0010 382  GLU B CB  
3655 C CB  B GLU B 157 ? 0.1470 0.1652 0.1398 -0.0020 -0.0105 -0.0008 382  GLU B CB  
3656 C CG  A GLU B 157 ? 0.1149 0.1283 0.1044 -0.0054 -0.0116 -0.0020 382  GLU B CG  
3657 C CG  B GLU B 157 ? 0.1405 0.1514 0.1293 -0.0038 -0.0108 -0.0023 382  GLU B CG  
3658 C CD  A GLU B 157 ? 0.1847 0.1914 0.1725 -0.0055 -0.0118 -0.0013 382  GLU B CD  
3659 C CD  B GLU B 157 ? 0.2402 0.2521 0.2290 -0.0076 -0.0125 -0.0020 382  GLU B CD  
3660 O OE1 A GLU B 157 ? 0.2278 0.2318 0.2157 -0.0024 -0.0108 -0.0005 382  GLU B OE1 
3661 O OE1 B GLU B 157 ? 0.2163 0.2341 0.2076 -0.0084 -0.0130 -0.0010 382  GLU B OE1 
3662 O OE2 A GLU B 157 ? 0.2175 0.2217 0.2042 -0.0086 -0.0130 -0.0013 382  GLU B OE2 
3663 O OE2 B GLU B 157 ? 0.2179 0.2246 0.2043 -0.0097 -0.0133 -0.0026 382  GLU B OE2 
3664 N N   . SER B 158 ? 0.1513 0.1832 0.1510 0.0017  -0.0081 -0.0008 383  SER B N   
3665 C CA  . SER B 158 ? 0.1237 0.1626 0.1281 0.0036  -0.0079 0.0006  383  SER B CA  
3666 C C   . SER B 158 ? 0.1231 0.1634 0.1285 0.0060  -0.0053 -0.0003 383  SER B C   
3667 O O   . SER B 158 ? 0.1666 0.2016 0.1683 0.0063  -0.0038 -0.0020 383  SER B O   
3668 C CB  . SER B 158 ? 0.1825 0.2211 0.1881 0.0059  -0.0089 0.0028  383  SER B CB  
3669 O OG  . SER B 158 ? 0.1959 0.2269 0.1987 0.0083  -0.0078 0.0026  383  SER B OG  
3670 N N   A ILE B 159 ? 0.1153 0.1632 0.1259 0.0075  -0.0049 0.0009  384  ILE B N   
3671 N N   B ILE B 159 ? 0.1137 0.1618 0.1244 0.0074  -0.0049 0.0008  384  ILE B N   
3672 C CA  A ILE B 159 ? 0.1225 0.1734 0.1354 0.0099  -0.0021 0.0005  384  ILE B CA  
3673 C CA  B ILE B 159 ? 0.1214 0.1724 0.1343 0.0098  -0.0020 0.0004  384  ILE B CA  
3674 C C   A ILE B 159 ? 0.1551 0.2119 0.1735 0.0138  -0.0018 0.0026  384  ILE B C   
3675 C C   B ILE B 159 ? 0.1557 0.2127 0.1741 0.0136  -0.0018 0.0025  384  ILE B C   
3676 O O   A ILE B 159 ? 0.1638 0.2245 0.1848 0.0138  -0.0043 0.0044  384  ILE B O   
3677 O O   B ILE B 159 ? 0.1622 0.2235 0.1835 0.0134  -0.0043 0.0044  384  ILE B O   
3678 C CB  A ILE B 159 ? 0.1411 0.1977 0.1561 0.0070  -0.0013 -0.0002 384  ILE B CB  
3679 C CB  B ILE B 159 ? 0.1414 0.1976 0.1561 0.0070  -0.0011 -0.0003 384  ILE B CB  
3680 C CG1 A ILE B 159 ? 0.1593 0.2221 0.1777 0.0041  -0.0039 0.0008  384  ILE B CG1 
3681 C CG1 B ILE B 159 ? 0.1543 0.2179 0.1733 0.0042  -0.0033 0.0007  384  ILE B CG1 
3682 C CG2 A ILE B 159 ? 0.1442 0.1947 0.1535 0.0046  -0.0006 -0.0020 384  ILE B CG2 
3683 C CG2 B ILE B 159 ? 0.1444 0.1944 0.1533 0.0045  -0.0006 -0.0021 384  ILE B CG2 
3684 C CD1 A ILE B 159 ? 0.1213 0.1889 0.1420 0.0010  -0.0031 0.0003  384  ILE B CD1 
3685 C CD1 B ILE B 159 ? 0.1717 0.2322 0.1874 0.0003  -0.0053 0.0000  384  ILE B CD1 
3686 N N   . GLY B 160 ? 0.1357 0.1932 0.1555 0.0174  0.0013  0.0024  385  GLY B N   
3687 C CA  . GLY B 160 ? 0.1703 0.2361 0.1970 0.0211  0.0021  0.0045  385  GLY B CA  
3688 C C   . GLY B 160 ? 0.2131 0.2887 0.2449 0.0184  0.0027  0.0045  385  GLY B C   
3689 O O   . GLY B 160 ? 0.1670 0.2412 0.1970 0.0174  0.0054  0.0029  385  GLY B O   
3690 N N   . MET B 161 ? 0.1710 0.2561 0.2088 0.0169  0.0002  0.0062  386  MET B N   
3691 C CA  . MET B 161 ? 0.1555 0.2483 0.1971 0.0127  0.0002  0.0058  386  MET B CA  
3692 C C   . MET B 161 ? 0.1727 0.2784 0.2233 0.0136  -0.0009 0.0081  386  MET B C   
3693 O O   . MET B 161 ? 0.2055 0.3159 0.2580 0.0116  -0.0047 0.0091  386  MET B O   
3694 C CB  . MET B 161 ? 0.1290 0.2185 0.1666 0.0073  -0.0025 0.0046  386  MET B CB  
3695 C CG  . MET B 161 ? 0.1580 0.2518 0.1977 0.0028  -0.0018 0.0036  386  MET B CG  
3696 S SD  . MET B 161 ? 0.1457 0.2344 0.1820 0.0032  0.0028  0.0022  386  MET B SD  
3697 C CE  . MET B 161 ? 0.1023 0.1932 0.1392 -0.0031 0.0026  0.0015  386  MET B CE  
3698 N N   . GLU B 162 ? 0.1305 0.2423 0.1865 0.0165  0.0023  0.0089  387  GLU B N   
3699 C CA  . GLU B 162 ? 0.1481 0.2736 0.2139 0.0179  0.0014  0.0114  387  GLU B CA  
3700 C C   . GLU B 162 ? 0.2248 0.3590 0.2949 0.0115  -0.0008 0.0112  387  GLU B C   
3701 O O   . GLU B 162 ? 0.2126 0.3570 0.2888 0.0107  -0.0041 0.0129  387  GLU B O   
3702 C CB  . GLU B 162 ? 0.1753 0.3053 0.2460 0.0227  0.0062  0.0123  387  GLU B CB  
3703 C CG  . GLU B 162 ? 0.3748 0.5188 0.4561 0.0261  0.0054  0.0156  387  GLU B CG  
3704 C CD  . GLU B 162 ? 0.6400 0.7817 0.7208 0.0318  0.0035  0.0178  387  GLU B CD  
3705 O OE1 . GLU B 162 ? 0.5131 0.6437 0.5880 0.0363  0.0061  0.0171  387  GLU B OE1 
3706 O OE2 . GLU B 162 ? 0.5478 0.6985 0.6338 0.0317  -0.0006 0.0202  387  GLU B OE2 
3707 N N   . ASN B 163 ? 0.1625 0.2928 0.2294 0.0069  0.0009  0.0091  388  ASN B N   
3708 C CA  . ASN B 163 ? 0.1813 0.3189 0.2525 0.0008  -0.0002 0.0087  388  ASN B CA  
3709 C C   . ASN B 163 ? 0.1567 0.2850 0.2204 -0.0043 -0.0014 0.0063  388  ASN B C   
3710 O O   . ASN B 163 ? 0.1269 0.2460 0.1845 -0.0041 0.0012  0.0050  388  ASN B O   
3711 C CB  . ASN B 163 ? 0.1924 0.3367 0.2694 0.0004  0.0041  0.0092  388  ASN B CB  
3712 C CG  . ASN B 163 ? 0.2330 0.3891 0.3193 0.0052  0.0051  0.0118  388  ASN B CG  
3713 O OD1 . ASN B 163 ? 0.4150 0.5821 0.5085 0.0042  0.0018  0.0135  388  ASN B OD1 
3714 N ND2 . ASN B 163 ? 0.3106 0.4646 0.3967 0.0105  0.0098  0.0122  388  ASN B ND2 
3715 N N   . ASN B 164 ? 0.1602 0.2911 0.2241 -0.0086 -0.0052 0.0058  389  ASN B N   
3716 C CA  . ASN B 164 ? 0.1469 0.2690 0.2039 -0.0130 -0.0060 0.0036  389  ASN B CA  
3717 C C   . ASN B 164 ? 0.1213 0.2411 0.1780 -0.0164 -0.0027 0.0026  389  ASN B C   
3718 O O   . ASN B 164 ? 0.1377 0.2479 0.1877 -0.0179 -0.0018 0.0012  389  ASN B O   
3719 C CB  . ASN B 164 ? 0.1439 0.2694 0.2011 -0.0171 -0.0103 0.0030  389  ASN B CB  
3720 C CG  . ASN B 164 ? 0.1441 0.2590 0.1929 -0.0195 -0.0113 0.0009  389  ASN B CG  
3721 O OD1 . ASN B 164 ? 0.1506 0.2591 0.1945 -0.0167 -0.0120 0.0011  389  ASN B OD1 
3722 N ND2 . ASN B 164 ? 0.1804 0.2932 0.2279 -0.0248 -0.0110 -0.0008 389  ASN B ND2 
3723 N N   . THR B 165 ? 0.1438 0.2725 0.2077 -0.0177 -0.0007 0.0036  390  THR B N   
3724 C CA  . THR B 165 ? 0.0949 0.2213 0.1583 -0.0212 0.0027  0.0031  390  THR B CA  
3725 C C   . THR B 165 ? 0.1279 0.2455 0.1853 -0.0179 0.0065  0.0030  390  THR B C   
3726 O O   . THR B 165 ? 0.1330 0.2453 0.1870 -0.0206 0.0088  0.0025  390  THR B O   
3727 C CB  . THR B 165 ? 0.1648 0.3035 0.2379 -0.0231 0.0044  0.0045  390  THR B CB  
3728 O OG1 . THR B 165 ? 0.1555 0.3009 0.2335 -0.0173 0.0060  0.0064  390  THR B OG1 
3729 C CG2 . THR B 165 ? 0.1295 0.2764 0.2078 -0.0282 0.0004  0.0042  390  THR B CG2 
3730 N N   . ASP B 166 ? 0.1155 0.2308 0.1708 -0.0122 0.0069  0.0034  391  ASP B N   
3731 C CA  . ASP B 166 ? 0.1474 0.2542 0.1963 -0.0094 0.0101  0.0029  391  ASP B CA  
3732 C C   . ASP B 166 ? 0.1233 0.2191 0.1636 -0.0109 0.0088  0.0014  391  ASP B C   
3733 O O   . ASP B 166 ? 0.1102 0.1992 0.1447 -0.0097 0.0110  0.0010  391  ASP B O   
3734 C CB  . ASP B 166 ? 0.1190 0.2256 0.1677 -0.0032 0.0110  0.0033  391  ASP B CB  
3735 C CG  . ASP B 166 ? 0.1712 0.2865 0.2266 -0.0005 0.0148  0.0048  391  ASP B CG  
3736 O OD1 . ASP B 166 ? 0.1467 0.2658 0.2047 -0.0031 0.0177  0.0053  391  ASP B OD1 
3737 O OD2 . ASP B 166 ? 0.1938 0.3120 0.2520 0.0045  0.0150  0.0056  391  ASP B OD2 
3738 N N   . PHE B 167 ? 0.1142 0.2084 0.1534 -0.0135 0.0052  0.0007  392  PHE B N   
3739 C CA  . PHE B 167 ? 0.1220 0.2067 0.1541 -0.0150 0.0044  -0.0004 392  PHE B CA  
3740 C C   . PHE B 167 ? 0.1270 0.2087 0.1572 -0.0181 0.0070  -0.0003 392  PHE B C   
3741 O O   . PHE B 167 ? 0.1395 0.2134 0.1635 -0.0180 0.0074  -0.0007 392  PHE B O   
3742 C CB  . PHE B 167 ? 0.1376 0.2214 0.1689 -0.0171 0.0007  -0.0011 392  PHE B CB  
3743 C CG  . PHE B 167 ? 0.0951 0.1785 0.1254 -0.0139 -0.0018 -0.0009 392  PHE B CG  
3744 C CD1 . PHE B 167 ? 0.1267 0.2030 0.1519 -0.0111 -0.0016 -0.0011 392  PHE B CD1 
3745 C CD2 . PHE B 167 ? 0.1472 0.2372 0.1817 -0.0141 -0.0045 -0.0004 392  PHE B CD2 
3746 C CE1 . PHE B 167 ? 0.1301 0.2054 0.1544 -0.0085 -0.0037 -0.0007 392  PHE B CE1 
3747 C CE2 . PHE B 167 ? 0.1390 0.2281 0.1722 -0.0111 -0.0066 0.0003  392  PHE B CE2 
3748 C CZ  . PHE B 167 ? 0.1515 0.2329 0.1797 -0.0083 -0.0060 0.0002  392  PHE B CZ  
3749 N N   . ASP B 168 ? 0.1277 0.2156 0.1632 -0.0209 0.0087  0.0003  393  ASP B N   
3750 C CA  . ASP B 168 ? 0.1076 0.1924 0.1416 -0.0240 0.0116  0.0007  393  ASP B CA  
3751 C C   . ASP B 168 ? 0.1152 0.2021 0.1499 -0.0222 0.0159  0.0021  393  ASP B C   
3752 O O   . ASP B 168 ? 0.1294 0.2161 0.1646 -0.0251 0.0187  0.0030  393  ASP B O   
3753 C CB  . ASP B 168 ? 0.1349 0.2240 0.1738 -0.0295 0.0109  0.0005  393  ASP B CB  
3754 C CG  . ASP B 168 ? 0.1628 0.2474 0.1988 -0.0318 0.0074  -0.0011 393  ASP B CG  
3755 O OD1 . ASP B 168 ? 0.1543 0.2316 0.1843 -0.0296 0.0063  -0.0017 393  ASP B OD1 
3756 O OD2 . ASP B 168 ? 0.1755 0.2640 0.2152 -0.0361 0.0059  -0.0019 393  ASP B OD2 
3757 N N   . VAL B 169 ? 0.1153 0.2038 0.1497 -0.0174 0.0167  0.0022  394  VAL B N   
3758 C CA  . VAL B 169 ? 0.1019 0.1918 0.1359 -0.0150 0.0211  0.0031  394  VAL B CA  
3759 C C   . VAL B 169 ? 0.1334 0.2142 0.1581 -0.0117 0.0215  0.0023  394  VAL B C   
3760 O O   . VAL B 169 ? 0.1292 0.2075 0.1518 -0.0084 0.0195  0.0013  394  VAL B O   
3761 C CB  . VAL B 169 ? 0.1084 0.2079 0.1497 -0.0120 0.0223  0.0038  394  VAL B CB  
3762 C CG1 . VAL B 169 ? 0.1396 0.2399 0.1796 -0.0091 0.0274  0.0046  394  VAL B CG1 
3763 C CG2 . VAL B 169 ? 0.1184 0.2282 0.1693 -0.0158 0.0213  0.0047  394  VAL B CG2 
3764 N N   . LEU B 170 ? 0.1251 0.2008 0.1442 -0.0126 0.0239  0.0029  395  LEU B N   
3765 C CA  . LEU B 170 ? 0.1282 0.1959 0.1383 -0.0099 0.0239  0.0022  395  LEU B CA  
3766 C C   . LEU B 170 ? 0.1247 0.1934 0.1337 -0.0054 0.0258  0.0014  395  LEU B C   
3767 O O   . LEU B 170 ? 0.1396 0.2148 0.1534 -0.0042 0.0292  0.0021  395  LEU B O   
3768 C CB  . LEU B 170 ? 0.1247 0.1880 0.1291 -0.0113 0.0265  0.0035  395  LEU B CB  
3769 C CG  . LEU B 170 ? 0.1372 0.1960 0.1398 -0.0148 0.0249  0.0043  395  LEU B CG  
3770 C CD1 . LEU B 170 ? 0.1599 0.2145 0.1566 -0.0153 0.0281  0.0062  395  LEU B CD1 
3771 C CD2 . LEU B 170 ? 0.1302 0.1839 0.1293 -0.0139 0.0205  0.0030  395  LEU B CD2 
3772 N N   . PRO B 171 ? 0.1566 0.2192 0.1596 -0.0028 0.0239  -0.0002 396  PRO B N   
3773 C CA  . PRO B 171 ? 0.1424 0.2039 0.1429 0.0015  0.0260  -0.0014 396  PRO B CA  
3774 C C   . PRO B 171 ? 0.1607 0.2193 0.1544 0.0026  0.0301  -0.0014 396  PRO B C   
3775 O O   . PRO B 171 ? 0.1949 0.2510 0.1845 0.0002  0.0306  -0.0003 396  PRO B O   
3776 C CB  . PRO B 171 ? 0.1575 0.2120 0.1530 0.0026  0.0222  -0.0032 396  PRO B CB  
3777 C CG  . PRO B 171 ? 0.1191 0.1695 0.1104 -0.0007 0.0198  -0.0028 396  PRO B CG  
3778 C CD  . PRO B 171 ? 0.1148 0.1706 0.1124 -0.0039 0.0201  -0.0010 396  PRO B CD  
3779 N N   . ASP B 172 ? 0.1690 0.2277 0.1612 0.0065  0.0333  -0.0024 397  ASP B N   
3780 C CA  . ASP B 172 ? 0.1861 0.2416 0.1706 0.0081  0.0376  -0.0028 397  ASP B CA  
3781 C C   . ASP B 172 ? 0.1870 0.2326 0.1603 0.0087  0.0351  -0.0051 397  ASP B C   
3782 O O   . ASP B 172 ? 0.1938 0.2346 0.1620 0.0119  0.0359  -0.0074 397  ASP B O   
3783 C CB  . ASP B 172 ? 0.1531 0.2127 0.1405 0.0124  0.0423  -0.0031 397  ASP B CB  
3784 C CG  . ASP B 172 ? 0.4091 0.4662 0.3887 0.0141  0.0475  -0.0034 397  ASP B CG  
3785 O OD1 . ASP B 172 ? 0.3074 0.3616 0.2810 0.0113  0.0477  -0.0024 397  ASP B OD1 
3786 O OD2 . ASP B 172 ? 0.4687 0.5264 0.4477 0.0184  0.0516  -0.0045 397  ASP B OD2 
3787 N N   . TYR B 173 ? 0.1861 0.2285 0.1559 0.0055  0.0319  -0.0043 398  TYR B N   
3788 C CA  . TYR B 173 ? 0.1537 0.1884 0.1148 0.0052  0.0283  -0.0061 398  TYR B CA  
3789 C C   . TYR B 173 ? 0.2018 0.2308 0.1522 0.0074  0.0306  -0.0082 398  TYR B C   
3790 O O   . TYR B 173 ? 0.2030 0.2258 0.1472 0.0078  0.0278  -0.0106 398  TYR B O   
3791 C CB  . TYR B 173 ? 0.1527 0.1861 0.1115 0.0019  0.0258  -0.0042 398  TYR B CB  
3792 C CG  . TYR B 173 ? 0.1452 0.1813 0.1113 -0.0006 0.0224  -0.0029 398  TYR B CG  
3793 C CD1 . TYR B 173 ? 0.1333 0.1670 0.1000 -0.0012 0.0179  -0.0041 398  TYR B CD1 
3794 C CD2 . TYR B 173 ? 0.1512 0.1914 0.1226 -0.0028 0.0239  -0.0005 398  TYR B CD2 
3795 C CE1 . TYR B 173 ? 0.1411 0.1768 0.1134 -0.0034 0.0152  -0.0029 398  TYR B CE1 
3796 C CE2 . TYR B 173 ? 0.1494 0.1908 0.1261 -0.0052 0.0211  0.0003  398  TYR B CE2 
3797 C CZ  . TYR B 173 ? 0.1444 0.1836 0.1213 -0.0053 0.0169  -0.0009 398  TYR B CZ  
3798 O OH  . TYR B 173 ? 0.1486 0.1888 0.1300 -0.0075 0.0146  -0.0001 398  TYR B OH  
3799 N N   . ASN B 174 ? 0.2391 0.2698 0.1868 0.0086  0.0356  -0.0073 399  ASN B N   
3800 C CA  . ASN B 174 ? 0.2281 0.2530 0.1643 0.0107  0.0381  -0.0094 399  ASN B CA  
3801 C C   . ASN B 174 ? 0.2276 0.2537 0.1649 0.0148  0.0433  -0.0110 399  ASN B C   
3802 O O   . ASN B 174 ? 0.2496 0.2714 0.1773 0.0169  0.0467  -0.0127 399  ASN B O   
3803 C CB  . ASN B 174 ? 0.2381 0.2626 0.1674 0.0093  0.0400  -0.0073 399  ASN B CB  
3804 C CG  . ASN B 174 ? 0.2531 0.2846 0.1885 0.0092  0.0453  -0.0043 399  ASN B CG  
3805 O OD1 . ASN B 174 ? 0.3409 0.3783 0.2858 0.0104  0.0478  -0.0039 399  ASN B OD1 
3806 N ND2 . ASN B 174 ? 0.4135 0.4443 0.3432 0.0078  0.0472  -0.0018 399  ASN B ND2 
3807 N N   . GLY B 175 ? 0.2267 0.2584 0.1749 0.0163  0.0441  -0.0103 400  GLY B N   
3808 C CA  . GLY B 175 ? 0.2474 0.2810 0.1980 0.0208  0.0489  -0.0114 400  GLY B CA  
3809 C C   . GLY B 175 ? 0.4531 0.4913 0.4032 0.0224  0.0556  -0.0099 400  GLY B C   
3810 O O   . GLY B 175 ? 0.4451 0.4836 0.3947 0.0268  0.0604  -0.0112 400  GLY B O   
3811 N N   . SER B 176 ? 0.3429 0.3848 0.2933 0.0191  0.0564  -0.0071 401  SER B N   
3812 C CA  . SER B 176 ? 0.4075 0.4529 0.3558 0.0200  0.0629  -0.0055 401  SER B CA  
3813 C C   . SER B 176 ? 0.5218 0.5788 0.4836 0.0188  0.0658  -0.0020 401  SER B C   
3814 O O   . SER B 176 ? 0.6093 0.6702 0.5709 0.0180  0.0706  0.0003  401  SER B O   
3815 C CB  . SER B 176 ? 0.4245 0.4652 0.3623 0.0171  0.0624  -0.0043 401  SER B CB  
3816 O OG  . SER B 176 ? 0.5290 0.5731 0.4729 0.0127  0.0594  -0.0012 401  SER B OG  
3817 N N   . ALA B 177 ? 0.4606 0.5233 0.4340 0.0185  0.0628  -0.0016 402  ALA B N   
3818 C CA  . ALA B 177 ? 0.4828 0.5569 0.4695 0.0162  0.0642  0.0015  402  ALA B CA  
3819 C C   . ALA B 177 ? 0.5242 0.5988 0.5105 0.0107  0.0635  0.0042  402  ALA B C   
3820 O O   . ALA B 177 ? 0.5271 0.6081 0.5178 0.0090  0.0680  0.0068  402  ALA B O   
3821 C CB  . ALA B 177 ? 0.5156 0.5978 0.5078 0.0199  0.0712  0.0026  402  ALA B CB  
3822 N N   . PHE B 178 ? 0.6015 0.6691 0.5827 0.0080  0.0581  0.0036  403  PHE B N   
3823 C CA  . PHE B 178 ? 0.6612 0.7280 0.6423 0.0031  0.0566  0.0060  403  PHE B CA  
3824 C C   . PHE B 178 ? 0.6904 0.7563 0.6654 0.0023  0.0618  0.0083  403  PHE B C   
3825 O O   . PHE B 178 ? 0.7706 0.8434 0.7525 0.0003  0.0659  0.0109  403  PHE B O   
3826 C CB  . PHE B 178 ? 0.5886 0.6636 0.5827 -0.0004 0.0553  0.0077  403  PHE B CB  
3827 C CG  . PHE B 178 ? 0.6815 0.7593 0.6825 0.0007  0.0510  0.0059  403  PHE B CG  
3828 C CD1 . PHE B 178 ? 0.3980 0.4707 0.3973 -0.0009 0.0451  0.0048  403  PHE B CD1 
3829 C CD2 . PHE B 178 ? 0.5055 0.5912 0.5146 0.0036  0.0529  0.0057  403  PHE B CD2 
3830 C CE1 . PHE B 178 ? 0.3531 0.4282 0.3582 0.0001  0.0414  0.0035  403  PHE B CE1 
3831 C CE2 . PHE B 178 ? 0.4824 0.5705 0.4974 0.0049  0.0489  0.0046  403  PHE B CE2 
3832 C CZ  . PHE B 178 ? 0.4714 0.5540 0.4840 0.0030  0.0431  0.0035  403  PHE B CZ  
3833 N N   . ASP B 179 ? 0.5148 0.5725 0.4769 0.0035  0.0617  0.0076  404  ASP B N   
3834 C CA  . ASP B 179 ? 0.5975 0.6539 0.5523 0.0033  0.0669  0.0099  404  ASP B CA  
3835 C C   . ASP B 179 ? 0.7850 0.8375 0.7361 -0.0005 0.0653  0.0130  404  ASP B C   
3836 O O   . ASP B 179 ? 0.6635 0.7151 0.6091 -0.0012 0.0697  0.0158  404  ASP B O   
3837 C CB  . ASP B 179 ? 0.5857 0.6358 0.5273 0.0073  0.0686  0.0075  404  ASP B CB  
3838 C CG  . ASP B 179 ? 0.7664 0.8077 0.6981 0.0072  0.0624  0.0054  404  ASP B CG  
3839 O OD1 . ASP B 179 ? 0.6000 0.6402 0.5352 0.0045  0.0572  0.0061  404  ASP B OD1 
3840 O OD2 . ASP B 179 ? 0.5298 0.5656 0.4502 0.0098  0.0630  0.0030  404  ASP B OD2 
3841 N N   . GLY B 180 ? 0.5262 0.5761 0.4800 -0.0029 0.0596  0.0130  405  GLY B N   
3842 C CA  . GLY B 180 ? 0.4253 0.4715 0.3770 -0.0061 0.0584  0.0161  405  GLY B CA  
3843 C C   . GLY B 180 ? 0.5127 0.5511 0.4516 -0.0050 0.0562  0.0167  405  GLY B C   
3844 O O   . GLY B 180 ? 0.5604 0.5953 0.4965 -0.0070 0.0560  0.0200  405  GLY B O   
3845 N N   . SER B 181 ? 0.3616 0.3967 0.2925 -0.0019 0.0543  0.0137  406  SER B N   
3846 C CA  . SER B 181 ? 0.2971 0.3257 0.2162 -0.0012 0.0510  0.0140  406  SER B CA  
3847 C C   . SER B 181 ? 0.2959 0.3220 0.2170 -0.0021 0.0442  0.0131  406  SER B C   
3848 O O   . SER B 181 ? 0.3458 0.3676 0.2589 -0.0019 0.0409  0.0141  406  SER B O   
3849 C CB  . SER B 181 ? 0.3612 0.3870 0.2700 0.0019  0.0517  0.0108  406  SER B CB  
3850 O OG  . SER B 181 ? 0.5375 0.5640 0.4507 0.0033  0.0493  0.0066  406  SER B OG  
3851 N N   . LEU B 182 ? 0.2545 0.2836 0.1860 -0.0031 0.0420  0.0116  407  LEU B N   
3852 C CA  . LEU B 182 ? 0.2437 0.2708 0.1770 -0.0037 0.0359  0.0104  407  LEU B CA  
3853 C C   . LEU B 182 ? 0.2100 0.2359 0.1464 -0.0060 0.0344  0.0136  407  LEU B C   
3854 O O   . LEU B 182 ? 0.2266 0.2541 0.1680 -0.0079 0.0377  0.0160  407  LEU B O   
3855 C CB  . LEU B 182 ? 0.2162 0.2465 0.1580 -0.0035 0.0341  0.0073  407  LEU B CB  
3856 C CG  . LEU B 182 ? 0.2342 0.2641 0.1725 -0.0007 0.0351  0.0039  407  LEU B CG  
3857 C CD1 . LEU B 182 ? 0.3016 0.3343 0.2483 -0.0002 0.0332  0.0015  407  LEU B CD1 
3858 C CD2 . LEU B 182 ? 0.3091 0.3333 0.2361 0.0004  0.0321  0.0023  407  LEU B CD2 
3859 N N   . ASN B 183 ? 0.2035 0.2263 0.1369 -0.0057 0.0296  0.0137  408  ASN B N   
3860 C CA  . ASN B 183 ? 0.1908 0.2116 0.1266 -0.0071 0.0279  0.0165  408  ASN B CA  
3861 C C   . ASN B 183 ? 0.1880 0.2110 0.1339 -0.0086 0.0259  0.0148  408  ASN B C   
3862 O O   . ASN B 183 ? 0.2023 0.2255 0.1496 -0.0080 0.0218  0.0127  408  ASN B O   
3863 C CB  . ASN B 183 ? 0.2300 0.2478 0.1586 -0.0056 0.0236  0.0174  408  ASN B CB  
3864 C CG  . ASN B 183 ? 0.3728 0.3883 0.3035 -0.0061 0.0220  0.0206  408  ASN B CG  
3865 O OD1 . ASN B 183 ? 0.3036 0.3181 0.2388 -0.0076 0.0248  0.0226  408  ASN B OD1 
3866 N ND2 . ASN B 183 ? 0.3166 0.3312 0.2441 -0.0048 0.0175  0.0211  408  ASN B ND2 
3867 N N   . LEU B 184 ? 0.1757 0.2007 0.1285 -0.0108 0.0289  0.0157  409  LEU B N   
3868 C CA  . LEU B 184 ? 0.1847 0.2122 0.1465 -0.0126 0.0273  0.0140  409  LEU B CA  
3869 C C   . LEU B 184 ? 0.1869 0.2113 0.1514 -0.0148 0.0273  0.0161  409  LEU B C   
3870 O O   . LEU B 184 ? 0.2138 0.2358 0.1768 -0.0161 0.0307  0.0189  409  LEU B O   
3871 C CB  . LEU B 184 ? 0.1924 0.2256 0.1608 -0.0137 0.0302  0.0128  409  LEU B CB  
3872 C CG  . LEU B 184 ? 0.1883 0.2245 0.1551 -0.0112 0.0310  0.0105  409  LEU B CG  
3873 C CD1 . LEU B 184 ? 0.1987 0.2413 0.1726 -0.0120 0.0347  0.0103  409  LEU B CD1 
3874 C CD2 . LEU B 184 ? 0.2066 0.2427 0.1745 -0.0098 0.0266  0.0077  409  LEU B CD2 
3875 N N   . ALA B 185 ? 0.1748 0.1986 0.1430 -0.0152 0.0239  0.0147  410  ALA B N   
3876 C CA  . ALA B 185 ? 0.1454 0.1659 0.1167 -0.0173 0.0243  0.0159  410  ALA B CA  
3877 C C   . ALA B 185 ? 0.1646 0.1875 0.1417 -0.0209 0.0274  0.0157  410  ALA B C   
3878 O O   . ALA B 185 ? 0.1849 0.2139 0.1664 -0.0215 0.0279  0.0139  410  ALA B O   
3879 C CB  . ALA B 185 ? 0.1598 0.1800 0.1340 -0.0169 0.0204  0.0139  410  ALA B CB  
3880 N N   . PRO B 186 ? 0.1700 0.1885 0.1478 -0.0234 0.0296  0.0176  411  PRO B N   
3881 C CA  . PRO B 186 ? 0.2064 0.2272 0.1892 -0.0275 0.0330  0.0178  411  PRO B CA  
3882 C C   . PRO B 186 ? 0.1410 0.1659 0.1312 -0.0303 0.0311  0.0148  411  PRO B C   
3883 O O   . PRO B 186 ? 0.1693 0.1934 0.1601 -0.0293 0.0275  0.0128  411  PRO B O   
3884 C CB  . PRO B 186 ? 0.2538 0.2666 0.2335 -0.0292 0.0356  0.0210  411  PRO B CB  
3885 C CG  . PRO B 186 ? 0.2702 0.2771 0.2461 -0.0265 0.0327  0.0212  411  PRO B CG  
3886 C CD  . PRO B 186 ? 0.2183 0.2291 0.1915 -0.0224 0.0294  0.0200  411  PRO B CD  
3887 N N   . PRO B 187 ? 0.1483 0.1783 0.1444 -0.0340 0.0333  0.0145  412  PRO B N   
3888 C CA  . PRO B 187 ? 0.1811 0.2155 0.1842 -0.0372 0.0313  0.0118  412  PRO B CA  
3889 C C   . PRO B 187 ? 0.1681 0.1952 0.1703 -0.0397 0.0300  0.0110  412  PRO B C   
3890 O O   . PRO B 187 ? 0.2006 0.2194 0.1986 -0.0403 0.0321  0.0130  412  PRO B O   
3891 C CB  . PRO B 187 ? 0.1837 0.2245 0.1928 -0.0411 0.0345  0.0126  412  PRO B CB  
3892 C CG  . PRO B 187 ? 0.1939 0.2360 0.1996 -0.0384 0.0380  0.0150  412  PRO B CG  
3893 C CD  . PRO B 187 ? 0.1599 0.1926 0.1567 -0.0354 0.0378  0.0168  412  PRO B CD  
3894 N N   . ILE B 188 ? 0.1543 0.1841 0.1600 -0.0408 0.0268  0.0080  413  ILE B N   
3895 C CA  . ILE B 188 ? 0.1482 0.1715 0.1528 -0.0431 0.0255  0.0064  413  ILE B CA  
3896 C C   . ILE B 188 ? 0.1817 0.2066 0.1912 -0.0494 0.0267  0.0053  413  ILE B C   
3897 O O   . ILE B 188 ? 0.1879 0.2215 0.2031 -0.0516 0.0249  0.0035  413  ILE B O   
3898 C CB  . ILE B 188 ? 0.1593 0.1846 0.1640 -0.0408 0.0214  0.0038  413  ILE B CB  
3899 C CG1 . ILE B 188 ? 0.1687 0.1926 0.1690 -0.0352 0.0202  0.0049  413  ILE B CG1 
3900 C CG2 . ILE B 188 ? 0.1788 0.1974 0.1821 -0.0432 0.0206  0.0019  413  ILE B CG2 
3901 C CD1 . ILE B 188 ? 0.2388 0.2662 0.2400 -0.0330 0.0164  0.0028  413  ILE B CD1 
3902 N N   . VAL B 189 ? 0.1518 0.1684 0.1590 -0.0525 0.0297  0.0066  414  VAL B N   
3903 C CA  . VAL B 189 ? 0.1893 0.2066 0.2008 -0.0594 0.0312  0.0057  414  VAL B CA  
3904 C C   . VAL B 189 ? 0.2277 0.2331 0.2352 -0.0622 0.0317  0.0044  414  VAL B C   
3905 O O   . VAL B 189 ? 0.2507 0.2459 0.2526 -0.0601 0.0341  0.0066  414  VAL B O   
3906 C CB  . VAL B 189 ? 0.2480 0.2669 0.2613 -0.0615 0.0356  0.0090  414  VAL B CB  
3907 C CG1 . VAL B 189 ? 0.2612 0.2827 0.2804 -0.0693 0.0369  0.0081  414  VAL B CG1 
3908 C CG2 . VAL B 189 ? 0.1989 0.2278 0.2144 -0.0575 0.0359  0.0105  414  VAL B CG2 
3909 N N   . PRO B 190 ? 0.2214 0.2274 0.2314 -0.0669 0.0296  0.0008  415  PRO B N   
3910 C CA  . PRO B 190 ? 0.2217 0.2151 0.2272 -0.0700 0.0307  -0.0008 415  PRO B CA  
3911 C C   . PRO B 190 ? 0.2176 0.2027 0.2218 -0.0736 0.0354  0.0019  415  PRO B C   
3912 O O   . PRO B 190 ? 0.2124 0.2037 0.2215 -0.0773 0.0373  0.0035  415  PRO B O   
3913 C CB  . PRO B 190 ? 0.2085 0.2065 0.2176 -0.0757 0.0277  -0.0052 415  PRO B CB  
3914 C CG  . PRO B 190 ? 0.2185 0.2301 0.2321 -0.0729 0.0240  -0.0058 415  PRO B CG  
3915 C CD  . PRO B 190 ? 0.2024 0.2201 0.2185 -0.0694 0.0261  -0.0019 415  PRO B CD  
3916 N N   . LEU B 191 ? 0.2290 0.2001 0.2268 -0.0723 0.0376  0.0025  416  LEU B N   
3917 C CA  . LEU B 191 ? 0.2194 0.1812 0.2151 -0.0750 0.0424  0.0057  416  LEU B CA  
3918 C C   . LEU B 191 ? 0.2166 0.1744 0.2147 -0.0840 0.0437  0.0034  416  LEU B C   
3919 O O   . LEU B 191 ? 0.2661 0.2189 0.2644 -0.0878 0.0478  0.0061  416  LEU B O   
3920 C CB  . LEU B 191 ? 0.2657 0.2138 0.2537 -0.0697 0.0444  0.0080  416  LEU B CB  
3921 C CG  . LEU B 191 ? 0.3068 0.2591 0.2926 -0.0613 0.0432  0.0110  416  LEU B CG  
3922 C CD1 . LEU B 191 ? 0.3018 0.2412 0.2808 -0.0564 0.0453  0.0139  416  LEU B CD1 
3923 C CD2 . LEU B 191 ? 0.4206 0.3817 0.4089 -0.0607 0.0444  0.0144  416  LEU B CD2 
3924 N N   . LEU B 192 ? 0.2529 0.2128 0.2526 -0.0880 0.0404  -0.0017 417  LEU B N   
3925 C CA  . LEU B 192 ? 0.2467 0.2051 0.2494 -0.0974 0.0409  -0.0044 417  LEU B CA  
3926 C C   . LEU B 192 ? 0.2327 0.2083 0.2439 -0.1014 0.0372  -0.0064 417  LEU B C   
3927 O O   . LEU B 192 ? 0.2339 0.2187 0.2465 -0.0974 0.0332  -0.0080 417  LEU B O   
3928 C CB  . LEU B 192 ? 0.2378 0.1831 0.2345 -0.1000 0.0403  -0.0089 417  LEU B CB  
3929 C CG  . LEU B 192 ? 0.2872 0.2145 0.2754 -0.0958 0.0440  -0.0073 417  LEU B CG  
3930 C CD1 . LEU B 192 ? 0.2663 0.1810 0.2490 -0.0993 0.0438  -0.0124 417  LEU B CD1 
3931 C CD2 . LEU B 192 ? 0.2939 0.2136 0.2817 -0.0978 0.0492  -0.0026 417  LEU B CD2 
3932 N N   . PRO B 193 ? 0.2779 0.2583 0.2952 -0.1093 0.0384  -0.0062 418  PRO B N   
3933 C CA  . PRO B 193 ? 0.2567 0.2555 0.2835 -0.1125 0.0351  -0.0073 418  PRO B CA  
3934 C C   . PRO B 193 ? 0.3398 0.3437 0.3672 -0.1149 0.0295  -0.0125 418  PRO B C   
3935 O O   . PRO B 193 ? 0.3428 0.3622 0.3767 -0.1140 0.0259  -0.0128 418  PRO B O   
3936 C CB  . PRO B 193 ? 0.3361 0.3368 0.3687 -0.1211 0.0382  -0.0058 418  PRO B CB  
3937 C CG  . PRO B 193 ? 0.2954 0.2764 0.3204 -0.1245 0.0418  -0.0062 418  PRO B CG  
3938 C CD  . PRO B 193 ? 0.2525 0.2229 0.2690 -0.1151 0.0433  -0.0042 418  PRO B CD  
3939 N N   . GLY B 194 ? 0.2775 0.2688 0.2983 -0.1179 0.0288  -0.0164 419  GLY B N   
3940 C CA  . GLY B 194 ? 0.2793 0.2753 0.2995 -0.1200 0.0236  -0.0213 419  GLY B CA  
3941 C C   . GLY B 194 ? 0.2923 0.2888 0.3079 -0.1115 0.0209  -0.0221 419  GLY B C   
3942 O O   . GLY B 194 ? 0.2985 0.2988 0.3127 -0.1124 0.0166  -0.0258 419  GLY B O   
3943 N N   . GLU B 195 ? 0.2036 0.1967 0.2165 -0.1035 0.0233  -0.0185 420  GLU B N   
3944 C CA  . GLU B 195 ? 0.1934 0.1863 0.2021 -0.0957 0.0213  -0.0188 420  GLU B CA  
3945 C C   . GLU B 195 ? 0.2118 0.2209 0.2266 -0.0916 0.0182  -0.0172 420  GLU B C   
3946 O O   . GLU B 195 ? 0.2015 0.2200 0.2230 -0.0924 0.0192  -0.0144 420  GLU B O   
3947 C CB  . GLU B 195 ? 0.1970 0.1779 0.1996 -0.0892 0.0250  -0.0159 420  GLU B CB  
3948 C CG  . GLU B 195 ? 0.2134 0.1768 0.2087 -0.0915 0.0278  -0.0179 420  GLU B CG  
3949 C CD  . GLU B 195 ? 0.2530 0.2051 0.2432 -0.0854 0.0318  -0.0141 420  GLU B CD  
3950 O OE1 . GLU B 195 ? 0.2367 0.1942 0.2294 -0.0812 0.0329  -0.0098 420  GLU B OE1 
3951 O OE2 . GLU B 195 ? 0.2604 0.1983 0.2441 -0.0847 0.0339  -0.0155 420  GLU B OE2 
3952 N N   . THR B 196 ? 0.1734 0.1852 0.1857 -0.0872 0.0149  -0.0188 421  THR B N   
3953 C CA  . THR B 196 ? 0.1825 0.2078 0.1996 -0.0828 0.0119  -0.0175 421  THR B CA  
3954 C C   . THR B 196 ? 0.1753 0.1965 0.1874 -0.0749 0.0118  -0.0165 421  THR B C   
3955 O O   . THR B 196 ? 0.1852 0.1972 0.1908 -0.0735 0.0117  -0.0184 421  THR B O   
3956 C CB  . THR B 196 ? 0.1757 0.2107 0.1956 -0.0864 0.0070  -0.0206 421  THR B CB  
3957 O OG1 . THR B 196 ? 0.2042 0.2443 0.2296 -0.0943 0.0067  -0.0215 421  THR B OG1 
3958 C CG2 . THR B 196 ? 0.1711 0.2194 0.1958 -0.0812 0.0041  -0.0188 421  THR B CG2 
3959 N N   . LEU B 197 ? 0.1477 0.1757 0.1627 -0.0697 0.0119  -0.0134 422  LEU B N   
3960 C CA  . LEU B 197 ? 0.1574 0.1829 0.1685 -0.0627 0.0115  -0.0123 422  LEU B CA  
3961 C C   . LEU B 197 ? 0.2013 0.2291 0.2105 -0.0615 0.0077  -0.0149 422  LEU B C   
3962 O O   . LEU B 197 ? 0.1733 0.2107 0.1864 -0.0633 0.0046  -0.0160 422  LEU B O   
3963 C CB  . LEU B 197 ? 0.1612 0.1946 0.1760 -0.0584 0.0119  -0.0092 422  LEU B CB  
3964 C CG  . LEU B 197 ? 0.1491 0.1818 0.1608 -0.0517 0.0108  -0.0081 422  LEU B CG  
3965 C CD1 . LEU B 197 ? 0.1743 0.1961 0.1801 -0.0489 0.0132  -0.0068 422  LEU B CD1 
3966 C CD2 . LEU B 197 ? 0.1618 0.2029 0.1773 -0.0485 0.0108  -0.0059 422  LEU B CD2 
3967 N N   . LEU B 198 ? 0.1616 0.1811 0.1648 -0.0582 0.0082  -0.0156 423  LEU B N   
3968 C CA  . LEU B 198 ? 0.1378 0.1590 0.1384 -0.0563 0.0052  -0.0176 423  LEU B CA  
3969 C C   . LEU B 198 ? 0.1388 0.1656 0.1408 -0.0504 0.0040  -0.0152 423  LEU B C   
3970 O O   . LEU B 198 ? 0.1812 0.2040 0.1817 -0.0464 0.0058  -0.0130 423  LEU B O   
3971 C CB  . LEU B 198 ? 0.1505 0.1603 0.1443 -0.0558 0.0067  -0.0196 423  LEU B CB  
3972 C CG  . LEU B 198 ? 0.1847 0.1957 0.1752 -0.0545 0.0041  -0.0219 423  LEU B CG  
3973 C CD1 . LEU B 198 ? 0.1820 0.1985 0.1732 -0.0600 0.0010  -0.0249 423  LEU B CD1 
3974 C CD2 . LEU B 198 ? 0.1874 0.1870 0.1713 -0.0524 0.0066  -0.0232 423  LEU B CD2 
3975 N N   . ARG B 199 ? 0.1242 0.1603 0.1293 -0.0501 0.0008  -0.0155 424  ARG B N   
3976 C CA  . ARG B 199 ? 0.1391 0.1808 0.1461 -0.0452 -0.0004 -0.0134 424  ARG B CA  
3977 C C   . ARG B 199 ? 0.1316 0.1722 0.1350 -0.0423 -0.0023 -0.0141 424  ARG B C   
3978 O O   . ARG B 199 ? 0.1562 0.1983 0.1581 -0.0444 -0.0044 -0.0162 424  ARG B O   
3979 C CB  . ARG B 199 ? 0.1316 0.1842 0.1449 -0.0460 -0.0022 -0.0126 424  ARG B CB  
3980 C CG  . ARG B 199 ? 0.1202 0.1750 0.1377 -0.0479 0.0003  -0.0111 424  ARG B CG  
3981 C CD  . ARG B 199 ? 0.1510 0.2175 0.1755 -0.0487 -0.0011 -0.0103 424  ARG B CD  
3982 N NE  . ARG B 199 ? 0.1597 0.2285 0.1884 -0.0505 0.0019  -0.0087 424  ARG B NE  
3983 C CZ  . ARG B 199 ? 0.1599 0.2333 0.1916 -0.0472 0.0035  -0.0065 424  ARG B CZ  
3984 N NH1 . ARG B 199 ? 0.1856 0.2618 0.2172 -0.0422 0.0022  -0.0057 424  ARG B NH1 
3985 N NH2 . ARG B 199 ? 0.2062 0.2808 0.2408 -0.0490 0.0068  -0.0051 424  ARG B NH2 
3986 N N   . PHE B 200 ? 0.1098 0.1479 0.1116 -0.0378 -0.0015 -0.0124 425  PHE B N   
3987 C CA  . PHE B 200 ? 0.1436 0.1817 0.1430 -0.0348 -0.0030 -0.0124 425  PHE B CA  
3988 C C   . PHE B 200 ? 0.1677 0.2131 0.1704 -0.0325 -0.0050 -0.0109 425  PHE B C   
3989 O O   . PHE B 200 ? 0.1556 0.2018 0.1600 -0.0301 -0.0042 -0.0091 425  PHE B O   
3990 C CB  . PHE B 200 ? 0.1164 0.1481 0.1129 -0.0316 -0.0011 -0.0113 425  PHE B CB  
3991 C CG  . PHE B 200 ? 0.1169 0.1403 0.1099 -0.0329 0.0014  -0.0125 425  PHE B CG  
3992 C CD1 . PHE B 200 ? 0.1525 0.1717 0.1459 -0.0338 0.0038  -0.0116 425  PHE B CD1 
3993 C CD2 . PHE B 200 ? 0.1648 0.1842 0.1540 -0.0330 0.0016  -0.0143 425  PHE B CD2 
3994 C CE1 . PHE B 200 ? 0.1677 0.1781 0.1576 -0.0347 0.0064  -0.0124 425  PHE B CE1 
3995 C CE2 . PHE B 200 ? 0.1713 0.1820 0.1569 -0.0337 0.0043  -0.0156 425  PHE B CE2 
3996 C CZ  . PHE B 200 ? 0.1618 0.1677 0.1479 -0.0346 0.0067  -0.0146 425  PHE B CZ  
3997 N N   . GLY B 201 ? 0.1458 0.1962 0.1490 -0.0331 -0.0076 -0.0115 426  GLY B N   
3998 C CA  . GLY B 201 ? 0.1189 0.1764 0.1258 -0.0311 -0.0095 -0.0099 426  GLY B CA  
3999 C C   . GLY B 201 ? 0.1630 0.2202 0.1678 -0.0280 -0.0108 -0.0090 426  GLY B C   
4000 O O   . GLY B 201 ? 0.1411 0.1951 0.1420 -0.0282 -0.0111 -0.0099 426  GLY B O   
4001 N N   . THR B 202 ? 0.1274 0.1876 0.1346 -0.0250 -0.0113 -0.0072 427  THR B N   
4002 C CA  . THR B 202 ? 0.1324 0.1926 0.1382 -0.0224 -0.0126 -0.0060 427  THR B CA  
4003 C C   . THR B 202 ? 0.1483 0.2140 0.1577 -0.0204 -0.0139 -0.0044 427  THR B C   
4004 O O   . THR B 202 ? 0.1438 0.2134 0.1571 -0.0207 -0.0134 -0.0043 427  THR B O   
4005 C CB  . THR B 202 ? 0.1666 0.2214 0.1703 -0.0203 -0.0113 -0.0052 427  THR B CB  
4006 O OG1 . THR B 202 ? 0.1828 0.2373 0.1849 -0.0186 -0.0125 -0.0042 427  THR B OG1 
4007 C CG2 . THR B 202 ? 0.1587 0.2134 0.1644 -0.0186 -0.0102 -0.0044 427  THR B CG2 
4008 N N   . VAL B 203 ? 0.1469 0.2130 0.1552 -0.0183 -0.0154 -0.0031 428  VAL B N   
4009 C CA  . VAL B 203 ? 0.1470 0.2176 0.1584 -0.0158 -0.0166 -0.0013 428  VAL B CA  
4010 C C   . VAL B 203 ? 0.1670 0.2332 0.1777 -0.0127 -0.0154 -0.0002 428  VAL B C   
4011 O O   . VAL B 203 ? 0.1621 0.2243 0.1698 -0.0121 -0.0157 0.0004  428  VAL B O   
4012 C CB  . VAL B 203 ? 0.1740 0.2481 0.1842 -0.0157 -0.0192 -0.0003 428  VAL B CB  
4013 C CG1 . VAL B 203 ? 0.1753 0.2538 0.1890 -0.0123 -0.0203 0.0021  428  VAL B CG1 
4014 C CG2 . VAL B 203 ? 0.1559 0.2344 0.1661 -0.0193 -0.0208 -0.0019 428  VAL B CG2 
4015 N N   . PRO B 204 ? 0.1330 0.1997 0.1463 -0.0111 -0.0140 0.0000  429  PRO B N   
4016 C CA  . PRO B 204 ? 0.1319 0.1941 0.1439 -0.0082 -0.0132 0.0007  429  PRO B CA  
4017 C C   . PRO B 204 ? 0.1253 0.1899 0.1390 -0.0052 -0.0143 0.0026  429  PRO B C   
4018 O O   . PRO B 204 ? 0.1482 0.2195 0.1654 -0.0049 -0.0154 0.0035  429  PRO B O   
4019 C CB  . PRO B 204 ? 0.1337 0.1956 0.1470 -0.0076 -0.0109 -0.0001 429  PRO B CB  
4020 C CG  . PRO B 204 ? 0.1400 0.2093 0.1578 -0.0088 -0.0109 -0.0001 429  PRO B CG  
4021 C CD  . PRO B 204 ? 0.1419 0.2133 0.1591 -0.0118 -0.0130 -0.0005 429  PRO B CD  
4022 N N   . ILE B 205 ? 0.1313 0.1904 0.1427 -0.0032 -0.0141 0.0034  430  ILE B N   
4023 C CA  . ILE B 205 ? 0.1252 0.1850 0.1380 0.0003  -0.0146 0.0055  430  ILE B CA  
4024 C C   . ILE B 205 ? 0.1462 0.2075 0.1620 0.0030  -0.0127 0.0053  430  ILE B C   
4025 O O   . ILE B 205 ? 0.1355 0.1923 0.1495 0.0031  -0.0107 0.0037  430  ILE B O   
4026 C CB  . ILE B 205 ? 0.1355 0.1877 0.1444 0.0013  -0.0147 0.0064  430  ILE B CB  
4027 C CG1 . ILE B 205 ? 0.1354 0.1871 0.1417 -0.0012 -0.0162 0.0070  430  ILE B CG1 
4028 C CG2 . ILE B 205 ? 0.1564 0.2075 0.1664 0.0054  -0.0146 0.0086  430  ILE B CG2 
4029 C CD1 . ILE B 205 ? 0.1240 0.1686 0.1270 -0.0011 -0.0160 0.0080  430  ILE B CD1 
4030 N N   . THR B 206 ? 0.1427 0.2111 0.1631 0.0053  -0.0132 0.0069  431  THR B N   
4031 C CA  . THR B 206 ? 0.1333 0.2037 0.1571 0.0086  -0.0109 0.0070  431  THR B CA  
4032 C C   . THR B 206 ? 0.1521 0.2257 0.1791 0.0133  -0.0115 0.0098  431  THR B C   
4033 O O   . THR B 206 ? 0.1779 0.2558 0.2061 0.0133  -0.0142 0.0118  431  THR B O   
4034 C CB  . THR B 206 ? 0.1872 0.2654 0.2156 0.0068  -0.0099 0.0061  431  THR B CB  
4035 O OG1 . THR B 206 ? 0.2184 0.3067 0.2530 0.0081  -0.0112 0.0080  431  THR B OG1 
4036 C CG2 . THR B 206 ? 0.1471 0.2250 0.1734 0.0016  -0.0107 0.0043  431  THR B CG2 
4037 N N   . THR B 207 ? 0.1590 0.2302 0.1871 0.0174  -0.0088 0.0099  432  THR B N   
4038 C CA  . THR B 207 ? 0.1572 0.2326 0.1897 0.0228  -0.0085 0.0127  432  THR B CA  
4039 C C   . THR B 207 ? 0.1483 0.2351 0.1882 0.0235  -0.0074 0.0130  432  THR B C   
4040 O O   . THR B 207 ? 0.1705 0.2610 0.2115 0.0195  -0.0069 0.0111  432  THR B O   
4041 C CB  . THR B 207 ? 0.2321 0.2976 0.2612 0.0272  -0.0056 0.0125  432  THR B CB  
4042 O OG1 . THR B 207 ? 0.2175 0.2794 0.2447 0.0267  -0.0024 0.0096  432  THR B OG1 
4043 C CG2 . THR B 207 ? 0.2646 0.3194 0.2872 0.0261  -0.0068 0.0125  432  THR B CG2 
4044 N N   . ARG B 208 ? 0.1821 0.2745 0.2273 0.0288  -0.0068 0.0156  433  ARG B N   
4045 C CA  . ARG B 208 ? 0.2207 0.3256 0.2745 0.0300  -0.0058 0.0166  433  ARG B CA  
4046 C C   . ARG B 208 ? 0.2671 0.3833 0.3253 0.0252  -0.0095 0.0172  433  ARG B C   
4047 O O   . ARG B 208 ? 0.1936 0.3185 0.2572 0.0228  -0.0088 0.0166  433  ARG B O   
4048 C CB  . ARG B 208 ? 0.2131 0.3165 0.2669 0.0296  -0.0014 0.0141  433  ARG B CB  
4049 C CG  . ARG B 208 ? 0.1886 0.2803 0.2370 0.0340  0.0024  0.0129  433  ARG B CG  
4050 C CD  . ARG B 208 ? 0.2176 0.3091 0.2658 0.0340  0.0068  0.0107  433  ARG B CD  
4051 N NE  . ARG B 208 ? 0.2530 0.3334 0.2955 0.0383  0.0104  0.0093  433  ARG B NE  
4052 C CZ  . ARG B 208 ? 0.4506 0.5322 0.4961 0.0447  0.0139  0.0104  433  ARG B CZ  
4053 N NH1 . ARG B 208 ? 0.4273 0.5216 0.4824 0.0479  0.0141  0.0134  433  ARG B NH1 
4054 N NH2 . ARG B 208 ? 0.4107 0.4804 0.4494 0.0480  0.0173  0.0084  433  ARG B NH2 
4055 N N   . ARG B 209 ? 0.2161 0.3316 0.2714 0.0237  -0.0134 0.0183  434  ARG B N   
4056 C CA  . ARG B 209 ? 0.2752 0.3997 0.3327 0.0189  -0.0174 0.0185  434  ARG B CA  
4057 C C   . ARG B 209 ? 0.2802 0.4161 0.3438 0.0219  -0.0206 0.0223  434  ARG B C   
4058 O O   . ARG B 209 ? 0.3042 0.4466 0.3681 0.0183  -0.0246 0.0226  434  ARG B O   
4059 C CB  . ARG B 209 ? 0.2072 0.3237 0.2567 0.0149  -0.0196 0.0171  434  ARG B CB  
4060 C CG  . ARG B 209 ? 0.2004 0.3075 0.2446 0.0115  -0.0172 0.0137  434  ARG B CG  
4061 C CD  . ARG B 209 ? 0.1862 0.2882 0.2241 0.0073  -0.0194 0.0124  434  ARG B CD  
4062 N NE  . ARG B 209 ? 0.2062 0.3021 0.2396 0.0096  -0.0205 0.0142  434  ARG B NE  
4063 C CZ  . ARG B 209 ? 0.2207 0.3200 0.2529 0.0095  -0.0237 0.0162  434  ARG B CZ  
4064 N NH1 . ARG B 209 ? 0.2111 0.3198 0.2458 0.0067  -0.0265 0.0161  434  ARG B NH1 
4065 N NH2 . ARG B 209 ? 0.1761 0.2691 0.2040 0.0118  -0.0242 0.0182  434  ARG B NH2 
4066 N N   . GLN B 210 ? 0.2212 0.3595 0.2893 0.0286  -0.0189 0.0251  435  GLN B N   
4067 C CA  . GLN B 210 ? 0.3588 0.5072 0.4322 0.0325  -0.0221 0.0294  435  GLN B CA  
4068 C C   . GLN B 210 ? 0.4818 0.6466 0.5632 0.0289  -0.0252 0.0299  435  GLN B C   
4069 O O   . GLN B 210 ? 0.3924 0.5660 0.4761 0.0291  -0.0297 0.0326  435  GLN B O   
4070 C CB  . GLN B 210 ? 0.3396 0.4877 0.4172 0.0409  -0.0189 0.0322  435  GLN B CB  
4071 C CG  . GLN B 210 ? 0.6060 0.7373 0.6758 0.0444  -0.0156 0.0315  435  GLN B CG  
4072 C CD  . GLN B 210 ? 0.7034 0.8271 0.7711 0.0439  -0.0106 0.0278  435  GLN B CD  
4073 O OE1 . GLN B 210 ? 0.6298 0.7597 0.7009 0.0401  -0.0095 0.0256  435  GLN B OE1 
4074 N NE2 . GLN B 210 ? 0.5572 0.6672 0.6189 0.0474  -0.0075 0.0271  435  GLN B NE2 
4075 N N   . SER B 211 ? 0.2289 0.3979 0.3143 0.0252  -0.0229 0.0273  436  SER B N   
4076 C CA  . SER B 211 ? 0.4189 0.6038 0.5133 0.0217  -0.0251 0.0278  436  SER B CA  
4077 C C   . SER B 211 ? 0.3266 0.5119 0.4176 0.0129  -0.0279 0.0245  436  SER B C   
4078 O O   . SER B 211 ? 0.2436 0.4408 0.3391 0.0093  -0.0320 0.0252  436  SER B O   
4079 C CB  . SER B 211 ? 0.5321 0.7220 0.6339 0.0234  -0.0202 0.0275  436  SER B CB  
4080 O OG  . SER B 211 ? 0.4140 0.6049 0.5199 0.0320  -0.0175 0.0306  436  SER B OG  
4081 N N   . ASP B 212 ? 0.2416 0.4142 0.3247 0.0094  -0.0257 0.0210  437  ASP B N   
4082 C CA  . ASP B 212 ? 0.2073 0.3777 0.2860 0.0017  -0.0276 0.0177  437  ASP B CA  
4083 C C   . ASP B 212 ? 0.1996 0.3546 0.2676 0.0016  -0.0267 0.0159  437  ASP B C   
4084 O O   . ASP B 212 ? 0.2798 0.4252 0.3444 0.0021  -0.0228 0.0142  437  ASP B O   
4085 C CB  . ASP B 212 ? 0.3144 0.4871 0.3969 -0.0029 -0.0247 0.0153  437  ASP B CB  
4086 C CG  . ASP B 212 ? 0.3616 0.5282 0.4380 -0.0102 -0.0257 0.0117  437  ASP B CG  
4087 O OD1 . ASP B 212 ? 0.5361 0.7008 0.6072 -0.0126 -0.0294 0.0110  437  ASP B OD1 
4088 O OD2 . ASP B 212 ? 0.6401 0.8031 0.7165 -0.0133 -0.0224 0.0097  437  ASP B OD2 
4089 N N   . PRO B 213 ? 0.2121 0.3647 0.2745 0.0008  -0.0303 0.0164  438  PRO B N   
4090 C CA  . PRO B 213 ? 0.1827 0.3217 0.2360 0.0018  -0.0293 0.0156  438  PRO B CA  
4091 C C   . PRO B 213 ? 0.1719 0.3027 0.2191 -0.0036 -0.0283 0.0118  438  PRO B C   
4092 O O   . PRO B 213 ? 0.2202 0.3405 0.2607 -0.0029 -0.0271 0.0112  438  PRO B O   
4093 C CB  . PRO B 213 ? 0.1943 0.3356 0.2447 0.0032  -0.0333 0.0181  438  PRO B CB  
4094 C CG  . PRO B 213 ? 0.1794 0.3340 0.2348 0.0000  -0.0372 0.0184  438  PRO B CG  
4095 C CD  . PRO B 213 ? 0.2341 0.3973 0.2990 0.0005  -0.0352 0.0186  438  PRO B CD  
4096 N N   . ILE B 214 ? 0.1878 0.3228 0.2369 -0.0090 -0.0286 0.0095  439  ILE B N   
4097 C CA  . ILE B 214 ? 0.1490 0.2758 0.1921 -0.0137 -0.0276 0.0061  439  ILE B CA  
4098 C C   . ILE B 214 ? 0.1862 0.3069 0.2297 -0.0133 -0.0232 0.0049  439  ILE B C   
4099 O O   . ILE B 214 ? 0.1465 0.2727 0.1959 -0.0136 -0.0215 0.0051  439  ILE B O   
4100 C CB  . ILE B 214 ? 0.2193 0.3517 0.2632 -0.0199 -0.0300 0.0041  439  ILE B CB  
4101 C CG1 . ILE B 214 ? 0.2001 0.3375 0.2415 -0.0205 -0.0346 0.0050  439  ILE B CG1 
4102 C CG2 . ILE B 214 ? 0.2327 0.3559 0.2710 -0.0241 -0.0280 0.0007  439  ILE B CG2 
4103 C CD1 . ILE B 214 ? 0.2420 0.3702 0.2750 -0.0185 -0.0348 0.0053  439  ILE B CD1 
4104 N N   . ARG B 215 ? 0.1294 0.2392 0.1665 -0.0127 -0.0215 0.0038  440  ARG B N   
4105 C CA  . ARG B 215 ? 0.1356 0.2390 0.1715 -0.0127 -0.0178 0.0026  440  ARG B CA  
4106 C C   . ARG B 215 ? 0.1761 0.2721 0.2064 -0.0164 -0.0173 0.0002  440  ARG B C   
4107 O O   . ARG B 215 ? 0.1498 0.2407 0.1749 -0.0164 -0.0184 -0.0001 440  ARG B O   
4108 C CB  . ARG B 215 ? 0.1685 0.2660 0.2025 -0.0078 -0.0160 0.0037  440  ARG B CB  
4109 C CG  . ARG B 215 ? 0.1898 0.2930 0.2292 -0.0033 -0.0153 0.0058  440  ARG B CG  
4110 C CD  . ARG B 215 ? 0.1645 0.2721 0.2089 -0.0036 -0.0124 0.0055  440  ARG B CD  
4111 N NE  . ARG B 215 ? 0.1538 0.2677 0.2040 0.0012  -0.0115 0.0076  440  ARG B NE  
4112 C CZ  . ARG B 215 ? 0.1963 0.3213 0.2531 0.0017  -0.0135 0.0095  440  ARG B CZ  
4113 N NH1 . ARG B 215 ? 0.2310 0.3621 0.2893 -0.0029 -0.0167 0.0091  440  ARG B NH1 
4114 N NH2 . ARG B 215 ? 0.1950 0.3254 0.2572 0.0069  -0.0124 0.0118  440  ARG B NH2 
4115 N N   . ILE B 216 ? 0.1256 0.2210 0.1570 -0.0194 -0.0154 -0.0012 441  ILE B N   
4116 C CA  . ILE B 216 ? 0.1214 0.2096 0.1479 -0.0227 -0.0145 -0.0033 441  ILE B CA  
4117 C C   . ILE B 216 ? 0.1070 0.1912 0.1335 -0.0226 -0.0110 -0.0035 441  ILE B C   
4118 O O   . ILE B 216 ? 0.1470 0.2358 0.1780 -0.0234 -0.0096 -0.0031 441  ILE B O   
4119 C CB  . ILE B 216 ? 0.1363 0.2276 0.1632 -0.0277 -0.0160 -0.0049 441  ILE B CB  
4120 C CG1 . ILE B 216 ? 0.1733 0.2685 0.1989 -0.0280 -0.0196 -0.0048 441  ILE B CG1 
4121 C CG2 . ILE B 216 ? 0.1570 0.2398 0.1790 -0.0304 -0.0142 -0.0069 441  ILE B CG2 
4122 C CD1 . ILE B 216 ? 0.2873 0.3878 0.3141 -0.0331 -0.0219 -0.0065 441  ILE B CD1 
4123 N N   . ILE B 217 ? 0.1024 0.1785 0.1240 -0.0215 -0.0098 -0.0039 442  ILE B N   
4124 C CA  . ILE B 217 ? 0.1087 0.1802 0.1289 -0.0215 -0.0069 -0.0040 442  ILE B CA  
4125 C C   . ILE B 217 ? 0.1666 0.2324 0.1831 -0.0245 -0.0064 -0.0053 442  ILE B C   
4126 O O   . ILE B 217 ? 0.1526 0.2152 0.1659 -0.0246 -0.0077 -0.0059 442  ILE B O   
4127 C CB  . ILE B 217 ? 0.1156 0.1827 0.1330 -0.0178 -0.0061 -0.0032 442  ILE B CB  
4128 C CG1 . ILE B 217 ? 0.1459 0.2092 0.1615 -0.0177 -0.0033 -0.0032 442  ILE B CG1 
4129 C CG2 . ILE B 217 ? 0.1298 0.1919 0.1430 -0.0169 -0.0076 -0.0034 442  ILE B CG2 
4130 C CD1 . ILE B 217 ? 0.1414 0.2005 0.1537 -0.0145 -0.0027 -0.0028 442  ILE B CD1 
4131 N N   . SER B 218 ? 0.1521 0.2166 0.1693 -0.0267 -0.0042 -0.0055 443  SER B N   
4132 C CA  . SER B 218 ? 0.1283 0.1868 0.1423 -0.0294 -0.0032 -0.0065 443  SER B CA  
4133 C C   . SER B 218 ? 0.1766 0.2286 0.1872 -0.0277 -0.0009 -0.0056 443  SER B C   
4134 O O   . SER B 218 ? 0.1625 0.2151 0.1733 -0.0255 0.0002  -0.0044 443  SER B O   
4135 C CB  . SER B 218 ? 0.1274 0.1884 0.1444 -0.0338 -0.0024 -0.0073 443  SER B CB  
4136 O OG  . SER B 218 ? 0.1859 0.2530 0.2055 -0.0360 -0.0050 -0.0084 443  SER B OG  
4137 N N   . CYS B 219 ? 0.1178 0.1634 0.1249 -0.0287 -0.0002 -0.0062 444  CYS B N   
4138 C CA  . CYS B 219 ? 0.1019 0.1418 0.1060 -0.0270 0.0017  -0.0049 444  CYS B CA  
4139 C C   . CYS B 219 ? 0.1673 0.2011 0.1694 -0.0294 0.0035  -0.0055 444  CYS B C   
4140 O O   . CYS B 219 ? 0.1558 0.1891 0.1579 -0.0322 0.0029  -0.0074 444  CYS B O   
4141 C CB  . CYS B 219 ? 0.0967 0.1347 0.0983 -0.0237 0.0005  -0.0043 444  CYS B CB  
4142 S SG  . CYS B 219 ? 0.1413 0.1768 0.1409 -0.0237 -0.0007 -0.0056 444  CYS B SG  
4143 N N   . ALA B 220 ? 0.1351 0.1639 0.1349 -0.0284 0.0057  -0.0039 445  ALA B N   
4144 C CA  . ALA B 220 ? 0.1414 0.1634 0.1392 -0.0305 0.0080  -0.0040 445  ALA B CA  
4145 C C   . ALA B 220 ? 0.1385 0.1546 0.1330 -0.0288 0.0080  -0.0044 445  ALA B C   
4146 O O   . ALA B 220 ? 0.1485 0.1588 0.1412 -0.0308 0.0095  -0.0056 445  ALA B O   
4147 C CB  . ALA B 220 ? 0.1808 0.1998 0.1774 -0.0299 0.0106  -0.0015 445  ALA B CB  
4148 N N   . LEU B 221 ? 0.1610 0.1785 0.1547 -0.0252 0.0067  -0.0035 446  LEU B N   
4149 C CA  . LEU B 221 ? 0.1253 0.1387 0.1168 -0.0229 0.0069  -0.0034 446  LEU B CA  
4150 C C   . LEU B 221 ? 0.1554 0.1737 0.1478 -0.0211 0.0044  -0.0038 446  LEU B C   
4151 O O   . LEU B 221 ? 0.1364 0.1593 0.1303 -0.0200 0.0028  -0.0029 446  LEU B O   
4152 C CB  . LEU B 221 ? 0.1456 0.1553 0.1354 -0.0198 0.0083  -0.0006 446  LEU B CB  
4153 C CG  . LEU B 221 ? 0.1416 0.1457 0.1299 -0.0209 0.0110  0.0008  446  LEU B CG  
4154 C CD1 . LEU B 221 ? 0.1907 0.1936 0.1773 -0.0174 0.0115  0.0042  446  LEU B CD1 
4155 C CD2 . LEU B 221 ? 0.1521 0.1486 0.1385 -0.0222 0.0132  -0.0005 446  LEU B CD2 
4156 N N   . PRO B 222 ? 0.1095 0.1265 0.1009 -0.0208 0.0043  -0.0052 447  PRO B N   
4157 C CA  . PRO B 222 ? 0.1332 0.1542 0.1253 -0.0188 0.0024  -0.0049 447  PRO B CA  
4158 C C   . PRO B 222 ? 0.1080 0.1294 0.1006 -0.0157 0.0023  -0.0023 447  PRO B C   
4159 O O   . PRO B 222 ? 0.1414 0.1590 0.1329 -0.0143 0.0039  -0.0009 447  PRO B O   
4160 C CB  . PRO B 222 ? 0.1098 0.1279 0.0998 -0.0188 0.0034  -0.0064 447  PRO B CB  
4161 C CG  . PRO B 222 ? 0.1491 0.1626 0.1371 -0.0219 0.0048  -0.0086 447  PRO B CG  
4162 C CD  . PRO B 222 ? 0.1324 0.1437 0.1213 -0.0224 0.0060  -0.0071 447  PRO B CD  
4163 N N   . GLN B 223 ? 0.1181 0.1441 0.1121 -0.0148 0.0002  -0.0017 448  GLN B N   
4164 C CA  . GLN B 223 ? 0.1126 0.1398 0.1071 -0.0124 -0.0005 0.0004  448  GLN B CA  
4165 C C   . GLN B 223 ? 0.1381 0.1632 0.1324 -0.0103 0.0008  0.0015  448  GLN B C   
4166 O O   . GLN B 223 ? 0.1392 0.1638 0.1336 -0.0083 0.0011  0.0036  448  GLN B O   
4167 C CB  . GLN B 223 ? 0.1248 0.1563 0.1206 -0.0123 -0.0029 0.0005  448  GLN B CB  
4168 C CG  . GLN B 223 ? 0.1158 0.1492 0.1124 -0.0106 -0.0041 0.0024  448  GLN B CG  
4169 C CD  . GLN B 223 ? 0.1532 0.1857 0.1483 -0.0100 -0.0043 0.0036  448  GLN B CD  
4170 O OE1 . GLN B 223 ? 0.2123 0.2441 0.2071 -0.0083 -0.0039 0.0055  448  GLN B OE1 
4171 N NE2 . GLN B 223 ? 0.1320 0.1649 0.1261 -0.0110 -0.0049 0.0028  448  GLN B NE2 
4172 N N   . GLU B 224 ? 0.1325 0.1566 0.1266 -0.0104 0.0018  0.0002  449  GLU B N   
4173 C CA  . GLU B 224 ? 0.1266 0.1492 0.1210 -0.0078 0.0036  0.0013  449  GLU B CA  
4174 C C   . GLU B 224 ? 0.1408 0.1574 0.1335 -0.0066 0.0061  0.0021  449  GLU B C   
4175 O O   . GLU B 224 ? 0.1472 0.1629 0.1407 -0.0035 0.0073  0.0041  449  GLU B O   
4176 C CB  . GLU B 224 ? 0.1403 0.1625 0.1337 -0.0082 0.0047  -0.0005 449  GLU B CB  
4177 C CG  . GLU B 224 ? 0.1217 0.1496 0.1168 -0.0086 0.0027  -0.0002 449  GLU B CG  
4178 C CD  . GLU B 224 ? 0.1579 0.1877 0.1525 -0.0113 0.0005  -0.0016 449  GLU B CD  
4179 O OE1 . GLU B 224 ? 0.1524 0.1804 0.1459 -0.0130 0.0004  -0.0028 449  GLU B OE1 
4180 O OE2 . GLU B 224 ? 0.1755 0.2088 0.1710 -0.0117 -0.0009 -0.0013 449  GLU B OE2 
4181 N N   . TRP B 225 ? 0.1433 0.1558 0.1340 -0.0090 0.0069  0.0007  450  TRP B N   
4182 C CA  . TRP B 225 ? 0.1193 0.1253 0.1082 -0.0081 0.0095  0.0018  450  TRP B CA  
4183 C C   . TRP B 225 ? 0.1516 0.1591 0.1411 -0.0063 0.0086  0.0049  450  TRP B C   
4184 O O   . TRP B 225 ? 0.1617 0.1657 0.1505 -0.0036 0.0102  0.0073  450  TRP B O   
4185 C CB  . TRP B 225 ? 0.1395 0.1408 0.1263 -0.0118 0.0107  -0.0006 450  TRP B CB  
4186 C CG  . TRP B 225 ? 0.1323 0.1301 0.1170 -0.0138 0.0118  -0.0038 450  TRP B CG  
4187 C CD1 . TRP B 225 ? 0.1697 0.1686 0.1538 -0.0127 0.0119  -0.0051 450  TRP B CD1 
4188 C CD2 . TRP B 225 ? 0.1636 0.1562 0.1461 -0.0176 0.0131  -0.0063 450  TRP B CD2 
4189 N NE1 . TRP B 225 ? 0.1803 0.1748 0.1612 -0.0155 0.0130  -0.0085 450  TRP B NE1 
4190 C CE2 . TRP B 225 ? 0.1405 0.1311 0.1206 -0.0187 0.0135  -0.0094 450  TRP B CE2 
4191 C CE3 . TRP B 225 ? 0.1796 0.1693 0.1619 -0.0205 0.0139  -0.0062 450  TRP B CE3 
4192 C CZ2 . TRP B 225 ? 0.1851 0.1708 0.1623 -0.0229 0.0144  -0.0126 450  TRP B CZ2 
4193 C CZ3 . TRP B 225 ? 0.2056 0.1907 0.1859 -0.0248 0.0149  -0.0092 450  TRP B CZ3 
4194 C CH2 . TRP B 225 ? 0.1819 0.1650 0.1595 -0.0260 0.0149  -0.0125 450  TRP B CH2 
4195 N N   . ILE B 226 ? 0.1415 0.1539 0.1318 -0.0077 0.0062  0.0050  451  ILE B N   
4196 C CA  . ILE B 226 ? 0.1371 0.1512 0.1271 -0.0062 0.0052  0.0077  451  ILE B CA  
4197 C C   . ILE B 226 ? 0.1425 0.1596 0.1340 -0.0027 0.0042  0.0102  451  ILE B C   
4198 O O   . ILE B 226 ? 0.1594 0.1749 0.1501 -0.0002 0.0047  0.0130  451  ILE B O   
4199 C CB  . ILE B 226 ? 0.1430 0.1616 0.1331 -0.0081 0.0030  0.0069  451  ILE B CB  
4200 C CG1 . ILE B 226 ? 0.1315 0.1480 0.1209 -0.0110 0.0044  0.0052  451  ILE B CG1 
4201 C CG2 . ILE B 226 ? 0.1311 0.1515 0.1198 -0.0065 0.0016  0.0093  451  ILE B CG2 
4202 C CD1 . ILE B 226 ? 0.1300 0.1509 0.1200 -0.0125 0.0028  0.0042  451  ILE B CD1 
4203 N N   . THR B 227 ? 0.1416 0.1632 0.1355 -0.0026 0.0027  0.0093  452  THR B N   
4204 C CA  . THR B 227 ? 0.1530 0.1787 0.1496 0.0002  0.0017  0.0116  452  THR B CA  
4205 C C   . THR B 227 ? 0.1581 0.1799 0.1549 0.0035  0.0046  0.0132  452  THR B C   
4206 O O   . THR B 227 ? 0.1550 0.1789 0.1533 0.0067  0.0042  0.0164  452  THR B O   
4207 C CB  . THR B 227 ? 0.1289 0.1599 0.1282 -0.0008 0.0001  0.0104  452  THR B CB  
4208 O OG1 . THR B 227 ? 0.1693 0.2027 0.1680 -0.0034 -0.0024 0.0091  452  THR B OG1 
4209 C CG2 . THR B 227 ? 0.1483 0.1849 0.1514 0.0017  -0.0010 0.0131  452  THR B CG2 
4210 N N   . TRP B 228 ? 0.1520 0.1681 0.1472 0.0028  0.0075  0.0110  453  TRP B N   
4211 C CA  . TRP B 228 ? 0.1247 0.1350 0.1192 0.0060  0.0108  0.0121  453  TRP B CA  
4212 C C   . TRP B 228 ? 0.1671 0.1732 0.1598 0.0078  0.0117  0.0151  453  TRP B C   
4213 O O   . TRP B 228 ? 0.1643 0.1698 0.1582 0.0121  0.0129  0.0182  453  TRP B O   
4214 C CB  . TRP B 228 ? 0.1826 0.1861 0.1742 0.0039  0.0135  0.0086  453  TRP B CB  
4215 C CG  . TRP B 228 ? 0.1683 0.1656 0.1588 0.0070  0.0173  0.0086  453  TRP B CG  
4216 C CD1 . TRP B 228 ? 0.1916 0.1791 0.1787 0.0076  0.0206  0.0083  453  TRP B CD1 
4217 C CD2 . TRP B 228 ? 0.1609 0.1609 0.1534 0.0098  0.0187  0.0085  453  TRP B CD2 
4218 N NE1 . TRP B 228 ? 0.2294 0.2126 0.2159 0.0109  0.0240  0.0079  453  TRP B NE1 
4219 C CE2 . TRP B 228 ? 0.2386 0.2298 0.2285 0.0125  0.0230  0.0081  453  TRP B CE2 
4220 C CE3 . TRP B 228 ? 0.2185 0.2271 0.2146 0.0103  0.0170  0.0089  453  TRP B CE3 
4221 C CZ2 . TRP B 228 ? 0.2025 0.1938 0.1934 0.0161  0.0257  0.0080  453  TRP B CZ2 
4222 C CZ3 . TRP B 228 ? 0.2148 0.2241 0.2123 0.0135  0.0197  0.0091  453  TRP B CZ3 
4223 C CH2 . TRP B 228 ? 0.2198 0.2207 0.2147 0.0166  0.0241  0.0086  453  TRP B CH2 
4224 N N   . PHE B 229 ? 0.1482 0.1520 0.1383 0.0050  0.0112  0.0146  454  PHE B N   
4225 C CA  . PHE B 229 ? 0.1464 0.1456 0.1342 0.0066  0.0123  0.0177  454  PHE B CA  
4226 C C   . PHE B 229 ? 0.1539 0.1596 0.1430 0.0094  0.0096  0.0214  454  PHE B C   
4227 O O   . PHE B 229 ? 0.1839 0.1869 0.1718 0.0127  0.0105  0.0251  454  PHE B O   
4228 C CB  . PHE B 229 ? 0.1666 0.1623 0.1515 0.0027  0.0129  0.0165  454  PHE B CB  
4229 C CG  . PHE B 229 ? 0.1705 0.1607 0.1543 -0.0009 0.0150  0.0127  454  PHE B CG  
4230 C CD1 . PHE B 229 ? 0.2116 0.1961 0.1949 0.0002  0.0176  0.0113  454  PHE B CD1 
4231 C CD2 . PHE B 229 ? 0.2060 0.1973 0.1894 -0.0053 0.0144  0.0106  454  PHE B CD2 
4232 C CE1 . PHE B 229 ? 0.2060 0.1855 0.1876 -0.0037 0.0192  0.0076  454  PHE B CE1 
4233 C CE2 . PHE B 229 ? 0.1909 0.1783 0.1737 -0.0090 0.0159  0.0072  454  PHE B CE2 
4234 C CZ  . PHE B 229 ? 0.2022 0.1836 0.1837 -0.0084 0.0180  0.0056  454  PHE B CZ  
4235 N N   . LEU B 230 ? 0.1696 0.1834 0.1608 0.0081  0.0060  0.0206  455  LEU B N   
4236 C CA  . LEU B 230 ? 0.1517 0.1721 0.1438 0.0101  0.0029  0.0237  455  LEU B CA  
4237 C C   . LEU B 230 ? 0.2381 0.2626 0.2343 0.0142  0.0026  0.0264  455  LEU B C   
4238 O O   . LEU B 230 ? 0.2330 0.2623 0.2301 0.0166  0.0004  0.0299  455  LEU B O   
4239 C CB  . LEU B 230 ? 0.1370 0.1638 0.1298 0.0070  -0.0007 0.0217  455  LEU B CB  
4240 C CG  . LEU B 230 ? 0.1705 0.1950 0.1597 0.0035  -0.0008 0.0194  455  LEU B CG  
4241 C CD1 . LEU B 230 ? 0.2136 0.2438 0.2040 0.0012  -0.0039 0.0172  455  LEU B CD1 
4242 C CD2 . LEU B 230 ? 0.2022 0.2243 0.1871 0.0043  -0.0007 0.0219  455  LEU B CD2 
4243 N N   . THR B 231 ? 0.1600 0.1837 0.1589 0.0150  0.0048  0.0249  456  THR B N   
4244 C CA  . THR B 231 ? 0.1718 0.2007 0.1757 0.0189  0.0050  0.0272  456  THR B CA  
4245 C C   . THR B 231 ? 0.2445 0.2665 0.2480 0.0233  0.0093  0.0289  456  THR B C   
4246 O O   . THR B 231 ? 0.2522 0.2775 0.2599 0.0271  0.0106  0.0306  456  THR B O   
4247 C CB  . THR B 231 ? 0.2017 0.2352 0.2089 0.0170  0.0048  0.0244  456  THR B CB  
4248 O OG1 . THR B 231 ? 0.1825 0.2087 0.1867 0.0149  0.0077  0.0207  456  THR B OG1 
4249 C CG2 . THR B 231 ? 0.1565 0.1965 0.1644 0.0131  0.0006  0.0232  456  THR B CG2 
4250 N N   . HIS B 232 ? 0.1945 0.2066 0.1931 0.0229  0.0118  0.0286  457  HIS B N   
4251 C CA  . HIS B 232 ? 0.1867 0.1904 0.1840 0.0271  0.0160  0.0305  457  HIS B CA  
4252 C C   . HIS B 232 ? 0.2278 0.2270 0.2215 0.0282  0.0160  0.0340  457  HIS B C   
4253 O O   . HIS B 232 ? 0.2637 0.2639 0.2547 0.0247  0.0137  0.0336  457  HIS B O   
4254 C CB  . HIS B 232 ? 0.2174 0.2113 0.2115 0.0249  0.0200  0.0262  457  HIS B CB  
4255 C CG  . HIS B 232 ? 0.2194 0.2166 0.2161 0.0247  0.0208  0.0233  457  HIS B CG  
4256 N ND1 . HIS B 232 ? 0.2098 0.2133 0.2076 0.0205  0.0181  0.0203  457  HIS B ND1 
4257 C CD2 . HIS B 232 ? 0.2532 0.2484 0.2514 0.0285  0.0242  0.0232  457  HIS B CD2 
4258 C CE1 . HIS B 232 ? 0.2066 0.2119 0.2063 0.0215  0.0197  0.0186  457  HIS B CE1 
4259 N NE2 . HIS B 232 ? 0.1974 0.1978 0.1972 0.0263  0.0235  0.0202  457  HIS B NE2 
4260 N N   . ASN B 233 ? 0.3492 0.3435 0.3427 0.0335  0.0186  0.0378  458  ASN B N   
4261 C CA  . ASN B 233 ? 0.5775 0.5661 0.5670 0.0352  0.0192  0.0417  458  ASN B CA  
4262 C C   . ASN B 233 ? 0.6553 0.6294 0.6403 0.0343  0.0243  0.0401  458  ASN B C   
4263 O O   . ASN B 233 ? 0.6017 0.5682 0.5862 0.0389  0.0280  0.0423  458  ASN B O   
4264 C CB  . ASN B 233 ? 0.4414 0.4346 0.4337 0.0419  0.0183  0.0478  458  ASN B CB  
4265 N N   . PHE B 234 ? 0.4627 0.4331 0.4448 0.0281  0.0246  0.0359  459  PHE B N   
4266 C CA  . PHE B 234 ? 0.5019 0.4592 0.4799 0.0258  0.0289  0.0336  459  PHE B CA  
4267 C C   . PHE B 234 ? 0.4695 0.4195 0.4432 0.0256  0.0304  0.0371  459  PHE B C   
4268 O O   . PHE B 234 ? 0.4421 0.3977 0.4150 0.0245  0.0276  0.0393  459  PHE B O   
4269 C CB  . PHE B 234 ? 0.3770 0.3345 0.3544 0.0191  0.0284  0.0277  459  PHE B CB  
4270 C CG  . PHE B 234 ? 0.2548 0.2160 0.2348 0.0189  0.0282  0.0239  459  PHE B CG  
4271 C CD1 . PHE B 234 ? 0.2959 0.2540 0.2770 0.0238  0.0309  0.0245  459  PHE B CD1 
4272 C CD2 . PHE B 234 ? 0.2262 0.1940 0.2075 0.0142  0.0255  0.0200  459  PHE B CD2 
4273 C CE1 . PHE B 234 ? 0.3226 0.2842 0.3057 0.0236  0.0311  0.0211  459  PHE B CE1 
4274 C CE2 . PHE B 234 ? 0.2399 0.2110 0.2230 0.0141  0.0254  0.0169  459  PHE B CE2 
4275 C CZ  . PHE B 234 ? 0.3056 0.2736 0.2894 0.0186  0.0283  0.0173  459  PHE B CZ  
4276 N N   . THR B 235 ? 0.5025 0.4393 0.4730 0.0266  0.0350  0.0375  460  THR B N   
4277 C CA  . THR B 235 ? 0.4943 0.4217 0.4602 0.0251  0.0374  0.0402  460  THR B CA  
4278 C C   . THR B 235 ? 0.5517 0.4690 0.5149 0.0191  0.0406  0.0354  460  THR B C   
4279 O O   . THR B 235 ? 0.4863 0.3948 0.4485 0.0198  0.0438  0.0328  460  THR B O   
4280 C CB  . THR B 235 ? 0.5728 0.4926 0.5370 0.0320  0.0403  0.0460  460  THR B CB  
4281 O OG1 . THR B 235 ? 0.7515 0.6825 0.7188 0.0374  0.0367  0.0506  460  THR B OG1 
4282 C CG2 . THR B 235 ? 0.5335 0.4430 0.4925 0.0303  0.0430  0.0492  460  THR B CG2 
4283 N N   . ALA B 236 ? 0.4220 0.3408 0.3840 0.0130  0.0397  0.0339  461  ALA B N   
4284 C CA  . ALA B 236 ? 0.5267 0.4372 0.4868 0.0065  0.0422  0.0296  461  ALA B CA  
4285 C C   . ALA B 236 ? 0.4580 0.3529 0.4138 0.0073  0.0472  0.0322  461  ALA B C   
4286 O O   . ALA B 236 ? 0.5312 0.4230 0.4847 0.0076  0.0483  0.0367  461  ALA B O   
4287 C CB  . ALA B 236 ? 0.4695 0.3868 0.4304 0.0005  0.0402  0.0283  461  ALA B CB  
4288 N N   . LEU B 237 ? 0.5680 0.4525 0.5222 0.0079  0.0504  0.0294  462  LEU B N   
4289 C CA  . LEU B 237 ? 0.7210 0.5887 0.6706 0.0085  0.0555  0.0313  462  LEU B CA  
4290 C C   . LEU B 237 ? 0.7037 0.5636 0.6509 -0.0002 0.0574  0.0279  462  LEU B C   
4291 O O   . LEU B 237 ? 0.6657 0.5102 0.6089 -0.0013 0.0619  0.0282  462  LEU B O   
4292 C CB  . LEU B 237 ? 0.5507 0.4094 0.4989 0.0133  0.0586  0.0297  462  LEU B CB  
4293 C CG  . LEU B 237 ? 0.6224 0.4903 0.5743 0.0216  0.0567  0.0324  462  LEU B CG  
4294 C CD1 . LEU B 237 ? 0.5308 0.3886 0.4811 0.0267  0.0608  0.0311  462  LEU B CD1 
4295 C CD2 . LEU B 237 ? 0.6573 0.5303 0.6102 0.0272  0.0553  0.0400  462  LEU B CD2 
4296 N N   . GLY B 238 ? 0.5626 0.4329 0.5126 -0.0063 0.0542  0.0248  463  GLY B N   
4297 C CA  . GLY B 238 ? 0.4264 0.2922 0.3756 -0.0149 0.0555  0.0218  463  GLY B CA  
4298 C C   . GLY B 238 ? 0.3494 0.2300 0.3026 -0.0190 0.0517  0.0210  463  GLY B C   
4299 O O   . GLY B 238 ? 0.3945 0.2875 0.3505 -0.0157 0.0481  0.0219  463  GLY B O   
4300 N N   . ASP B 239 ? 0.3990 0.2777 0.3525 -0.0265 0.0528  0.0194  464  ASP B N   
4301 C CA  . ASP B 239 ? 0.3178 0.2100 0.2755 -0.0306 0.0499  0.0185  464  ASP B CA  
4302 C C   . ASP B 239 ? 0.3581 0.2613 0.3194 -0.0316 0.0457  0.0135  464  ASP B C   
4303 O O   . ASP B 239 ? 0.2895 0.2055 0.2543 -0.0319 0.0425  0.0136  464  ASP B O   
4304 C CB  . ASP B 239 ? 0.4054 0.2934 0.3636 -0.0388 0.0522  0.0176  464  ASP B CB  
4305 C CG  . ASP B 239 ? 0.5160 0.3937 0.4707 -0.0384 0.0566  0.0230  464  ASP B CG  
4306 O OD1 . ASP B 239 ? 0.4562 0.3358 0.4092 -0.0326 0.0566  0.0283  464  ASP B OD1 
4307 O OD2 . ASP B 239 ? 0.3623 0.2300 0.3157 -0.0444 0.0599  0.0221  464  ASP B OD2 
4308 N N   . ALA B 240 ? 0.2878 0.1857 0.2478 -0.0322 0.0458  0.0093  465  ALA B N   
4309 C CA  . ALA B 240 ? 0.2390 0.1465 0.2018 -0.0341 0.0421  0.0045  465  ALA B CA  
4310 C C   . ALA B 240 ? 0.2967 0.1978 0.2566 -0.0311 0.0428  0.0015  465  ALA B C   
4311 O O   . ALA B 240 ? 0.2908 0.1782 0.2465 -0.0307 0.0465  0.0012  465  ALA B O   
4312 C CB  . ALA B 240 ? 0.2688 0.1792 0.2337 -0.0426 0.0413  0.0006  465  ALA B CB  
4313 N N   . ALA B 241 ? 0.2596 0.1703 0.2216 -0.0291 0.0395  -0.0006 466  ALA B N   
4314 C CA  . ALA B 241 ? 0.2394 0.1461 0.1989 -0.0266 0.0400  -0.0037 466  ALA B CA  
4315 C C   . ALA B 241 ? 0.2506 0.1570 0.2089 -0.0333 0.0388  -0.0097 466  ALA B C   
4316 O O   . ALA B 241 ? 0.2527 0.1704 0.2144 -0.0366 0.0352  -0.0113 466  ALA B O   
4317 C CB  . ALA B 241 ? 0.2352 0.1526 0.1975 -0.0208 0.0372  -0.0023 466  ALA B CB  
4318 N N   . LEU B 242 ? 0.2537 0.1469 0.2068 -0.0352 0.0419  -0.0129 467  LEU B N   
4319 C CA  . LEU B 242 ? 0.2712 0.1635 0.2219 -0.0412 0.0406  -0.0191 467  LEU B CA  
4320 C C   . LEU B 242 ? 0.2504 0.1490 0.2005 -0.0374 0.0387  -0.0212 467  LEU B C   
4321 O O   . LEU B 242 ? 0.2892 0.1830 0.2371 -0.0312 0.0411  -0.0202 467  LEU B O   
4322 C CB  . LEU B 242 ? 0.2563 0.1312 0.2006 -0.0443 0.0448  -0.0221 467  LEU B CB  
4323 C CG  . LEU B 242 ? 0.2703 0.1421 0.2106 -0.0510 0.0436  -0.0289 467  LEU B CG  
4324 C CD1 . LEU B 242 ? 0.3154 0.1963 0.2600 -0.0592 0.0401  -0.0302 467  LEU B CD1 
4325 C CD2 . LEU B 242 ? 0.3150 0.1674 0.2478 -0.0528 0.0484  -0.0319 467  LEU B CD2 
4326 N N   . LEU B 243 ? 0.2712 0.1809 0.2235 -0.0410 0.0346  -0.0237 468  LEU B N   
4327 C CA  . LEU B 243 ? 0.2254 0.1415 0.1770 -0.0382 0.0326  -0.0256 468  LEU B CA  
4328 C C   . LEU B 243 ? 0.2752 0.1896 0.2225 -0.0442 0.0313  -0.0315 468  LEU B C   
4329 O O   . LEU B 243 ? 0.2753 0.1896 0.2229 -0.0511 0.0299  -0.0337 468  LEU B O   
4330 C CB  . LEU B 243 ? 0.2285 0.1602 0.1861 -0.0364 0.0285  -0.0230 468  LEU B CB  
4331 C CG  . LEU B 243 ? 0.2273 0.1636 0.1897 -0.0327 0.0285  -0.0175 468  LEU B CG  
4332 C CD1 . LEU B 243 ? 0.1987 0.1495 0.1662 -0.0320 0.0243  -0.0161 468  LEU B CD1 
4333 C CD2 . LEU B 243 ? 0.2609 0.1915 0.2221 -0.0256 0.0315  -0.0144 468  LEU B CD2 
4334 N N   . ARG B 244 ? 0.2504 0.1641 0.1936 -0.0416 0.0315  -0.0341 469  ARG B N   
4335 C CA  . ARG B 244 ? 0.2937 0.2090 0.2327 -0.0466 0.0291  -0.0393 469  ARG B CA  
4336 C C   . ARG B 244 ? 0.2448 0.1738 0.1867 -0.0441 0.0255  -0.0383 469  ARG B C   
4337 O O   . ARG B 244 ? 0.2832 0.2155 0.2270 -0.0378 0.0264  -0.0353 469  ARG B O   
4338 C CB  . ARG B 244 ? 0.3254 0.2268 0.2553 -0.0464 0.0329  -0.0439 469  ARG B CB  
4339 C CG  . ARG B 244 ? 0.4993 0.3974 0.4273 -0.0382 0.0364  -0.0423 469  ARG B CG  
4340 C CD  . ARG B 244 ? 0.6074 0.4922 0.5257 -0.0385 0.0400  -0.0476 469  ARG B CD  
4341 N NE  . ARG B 244 ? 0.7923 0.6706 0.7090 -0.0304 0.0450  -0.0458 469  ARG B NE  
4342 C CZ  . ARG B 244 ? 0.8292 0.6949 0.7377 -0.0287 0.0494  -0.0497 469  ARG B CZ  
4343 N NH1 . ARG B 244 ? 0.8954 0.7530 0.7956 -0.0349 0.0493  -0.0560 469  ARG B NH1 
4344 N NH2 . ARG B 244 ? 0.9933 0.8547 0.9019 -0.0206 0.0540  -0.0472 469  ARG B NH2 
4345 N N   . TYR B 245 ? 0.2691 0.2063 0.2117 -0.0493 0.0213  -0.0405 470  TYR B N   
4346 C CA  . TYR B 245 ? 0.2602 0.2097 0.2050 -0.0477 0.0177  -0.0396 470  TYR B CA  
4347 C C   . TYR B 245 ? 0.2759 0.2221 0.2127 -0.0494 0.0174  -0.0443 470  TYR B C   
4348 O O   . TYR B 245 ? 0.2774 0.2212 0.2104 -0.0557 0.0158  -0.0484 470  TYR B O   
4349 C CB  . TYR B 245 ? 0.1998 0.1612 0.1508 -0.0515 0.0131  -0.0383 470  TYR B CB  
4350 C CG  . TYR B 245 ? 0.2144 0.1879 0.1682 -0.0490 0.0097  -0.0366 470  TYR B CG  
4351 C CD1 . TYR B 245 ? 0.1951 0.1721 0.1518 -0.0428 0.0105  -0.0328 470  TYR B CD1 
4352 C CD2 . TYR B 245 ? 0.2072 0.1886 0.1607 -0.0530 0.0055  -0.0385 470  TYR B CD2 
4353 C CE1 . TYR B 245 ? 0.1983 0.1852 0.1575 -0.0409 0.0076  -0.0312 470  TYR B CE1 
4354 C CE2 . TYR B 245 ? 0.1740 0.1657 0.1299 -0.0504 0.0026  -0.0364 470  TYR B CE2 
4355 C CZ  . TYR B 245 ? 0.1642 0.1580 0.1228 -0.0445 0.0038  -0.0328 470  TYR B CZ  
4356 O OH  . TYR B 245 ? 0.1852 0.1880 0.1459 -0.0422 0.0011  -0.0307 470  TYR B OH  
4357 N N   . ARG B 246 ? 0.2296 0.1758 0.1638 -0.0441 0.0191  -0.0438 471  ARG B N   
4358 C CA  . ARG B 246 ? 0.2749 0.2156 0.2001 -0.0447 0.0203  -0.0482 471  ARG B CA  
4359 C C   . ARG B 246 ? 0.3085 0.2595 0.2339 -0.0421 0.0180  -0.0469 471  ARG B C   
4360 O O   . ARG B 246 ? 0.2668 0.2243 0.1978 -0.0371 0.0182  -0.0426 471  ARG B O   
4361 C CB  . ARG B 246 ? 0.3569 0.2847 0.2772 -0.0402 0.0264  -0.0491 471  ARG B CB  
4362 C CG  . ARG B 246 ? 0.4485 0.3701 0.3588 -0.0399 0.0285  -0.0538 471  ARG B CG  
4363 C CD  . ARG B 246 ? 0.6306 0.5434 0.5383 -0.0329 0.0346  -0.0531 471  ARG B CD  
4364 N NE  . ARG B 246 ? 0.6148 0.5152 0.5222 -0.0323 0.0384  -0.0531 471  ARG B NE  
4365 N N   . ASN B 247 ? 0.2987 0.2510 0.2176 -0.0458 0.0158  -0.0507 472  ASN B N   
4366 C CA  . ASN B 247 ? 0.3873 0.3461 0.3037 -0.0429 0.0149  -0.0499 472  ASN B CA  
4367 C C   . ASN B 247 ? 0.5000 0.4498 0.4102 -0.0382 0.0205  -0.0512 472  ASN B C   
4368 O O   . ASN B 247 ? 0.4936 0.4332 0.3949 -0.0402 0.0229  -0.0561 472  ASN B O   
4369 C CB  . ASN B 247 ? 0.5235 0.4870 0.4344 -0.0482 0.0105  -0.0531 472  ASN B CB  
4370 C CG  . ASN B 247 ? 0.7666 0.7384 0.6760 -0.0454 0.0090  -0.0512 472  ASN B CG  
4371 O OD1 . ASN B 247 ? 0.6286 0.5977 0.5351 -0.0406 0.0128  -0.0504 472  ASN B OD1 
4372 N ND2 . ASN B 247 ? 0.6367 0.6187 0.5481 -0.0482 0.0037  -0.0501 472  ASN B ND2 
4373 N N   . GLN B 248 ? 0.5571 0.5106 0.4722 -0.0320 0.0228  -0.0470 473  GLN B N   
4374 C CA  . GLN B 248 ? 0.6786 0.6244 0.5895 -0.0268 0.0287  -0.0476 473  GLN B CA  
4375 C C   . GLN B 248 ? 0.6665 0.6119 0.5685 -0.0267 0.0297  -0.0505 473  GLN B C   
4376 O O   . GLN B 248 ? 0.6020 0.5382 0.4971 -0.0241 0.0348  -0.0533 473  GLN B O   
4377 C CB  . GLN B 248 ? 0.6707 0.6220 0.5903 -0.0205 0.0305  -0.0420 473  GLN B CB  
4378 C CG  . GLN B 248 ? 0.6074 0.5566 0.5340 -0.0194 0.0308  -0.0392 473  GLN B CG  
4379 C CD  . GLN B 248 ? 0.8867 0.8416 0.8212 -0.0133 0.0323  -0.0339 473  GLN B CD  
4380 O OE1 . GLN B 248 ? 0.8033 0.7667 0.7402 -0.0112 0.0315  -0.0316 473  GLN B OE1 
4381 N NE2 . GLN B 248 ? 0.5608 0.5112 0.4991 -0.0107 0.0343  -0.0317 473  GLN B NE2 
4382 N N   . ALA B 249 ? 0.5214 0.4765 0.4230 -0.0291 0.0253  -0.0498 474  ALA B N   
4383 C CA  . ALA B 249 ? 0.7359 0.6912 0.6283 -0.0291 0.0261  -0.0523 474  ALA B CA  
4384 C C   . ALA B 249 ? 0.7277 0.6730 0.6085 -0.0339 0.0264  -0.0589 474  ALA B C   
4385 O O   . ALA B 249 ? 0.5489 0.4860 0.4206 -0.0321 0.0309  -0.0623 474  ALA B O   
4386 C CB  . ALA B 249 ? 0.6915 0.6592 0.5863 -0.0306 0.0209  -0.0494 474  ALA B CB  
4387 N N   . THR B 250 ? 0.6840 0.6300 0.5652 -0.0401 0.0217  -0.0610 475  THR B N   
4388 C CA  . THR B 250 ? 0.5036 0.4409 0.3744 -0.0459 0.0211  -0.0675 475  THR B CA  
4389 C C   . THR B 250 ? 0.6301 0.5535 0.4994 -0.0468 0.0250  -0.0706 475  THR B C   
4390 O O   . THR B 250 ? 0.4967 0.4098 0.3559 -0.0510 0.0260  -0.0766 475  THR B O   
4391 C CB  . THR B 250 ? 0.4565 0.4023 0.3290 -0.0527 0.0139  -0.0682 475  THR B CB  
4392 O OG1 . THR B 250 ? 0.5777 0.5263 0.4608 -0.0543 0.0121  -0.0656 475  THR B OG1 
4393 C CG2 . THR B 250 ? 0.5474 0.5067 0.4219 -0.0514 0.0099  -0.0645 475  THR B CG2 
4394 N N   . GLY B 251 ? 0.5480 0.4705 0.4265 -0.0431 0.0273  -0.0666 476  GLY B N   
4395 C CA  . GLY B 251 ? 0.6022 0.5119 0.4802 -0.0438 0.0308  -0.0685 476  GLY B CA  
4396 C C   . GLY B 251 ? 0.4859 0.3954 0.3665 -0.0512 0.0267  -0.0700 476  GLY B C   
4397 O O   . GLY B 251 ? 0.7234 0.6216 0.6033 -0.0527 0.0295  -0.0716 476  GLY B O   
4398 N N   . GLN B 252 ? 0.4048 0.3264 0.2887 -0.0558 0.0205  -0.0693 477  GLN B N   
4399 C CA  . GLN B 252 ? 0.4017 0.3242 0.2879 -0.0634 0.0166  -0.0711 477  GLN B CA  
4400 C C   . GLN B 252 ? 0.4182 0.3425 0.3154 -0.0621 0.0172  -0.0666 477  GLN B C   
4401 O O   . GLN B 252 ? 0.3530 0.2882 0.2589 -0.0584 0.0155  -0.0613 477  GLN B O   
4402 C CB  . GLN B 252 ? 0.4880 0.4243 0.3755 -0.0678 0.0098  -0.0711 477  GLN B CB  
4403 C CG  . GLN B 252 ? 0.5372 0.4771 0.4286 -0.0757 0.0054  -0.0725 477  GLN B CG  
4404 C CD  . GLN B 252 ? 0.7719 0.7275 0.6667 -0.0788 -0.0014 -0.0712 477  GLN B CD  
4405 O OE1 . GLN B 252 ? 0.5521 0.5160 0.4468 -0.0748 -0.0030 -0.0687 477  GLN B OE1 
4406 N NE2 . GLN B 252 ? 0.6058 0.5659 0.5040 -0.0860 -0.0055 -0.0727 477  GLN B NE2 
4407 N N   . LEU B 253 ? 0.3443 0.2574 0.2404 -0.0654 0.0195  -0.0686 478  LEU B N   
4408 C CA  . LEU B 253 ? 0.3338 0.2490 0.2395 -0.0657 0.0195  -0.0645 478  LEU B CA  
4409 C C   . LEU B 253 ? 0.3786 0.3058 0.2902 -0.0722 0.0136  -0.0642 478  LEU B C   
4410 O O   . LEU B 253 ? 0.4566 0.3823 0.3637 -0.0795 0.0111  -0.0687 478  LEU B O   
4411 C CB  . LEU B 253 ? 0.3691 0.2680 0.2716 -0.0671 0.0242  -0.0664 478  LEU B CB  
4412 C CG  . LEU B 253 ? 0.5659 0.4652 0.4772 -0.0654 0.0256  -0.0613 478  LEU B CG  
4413 N N   . LEU B 254 ? 0.2841 0.2232 0.2056 -0.0697 0.0115  -0.0588 479  LEU B N   
4414 C CA  . LEU B 254 ? 0.2561 0.2082 0.1842 -0.0746 0.0062  -0.0578 479  LEU B CA  
4415 C C   . LEU B 254 ? 0.3059 0.2566 0.2401 -0.0787 0.0067  -0.0565 479  LEU B C   
4416 O O   . LEU B 254 ? 0.3735 0.3286 0.3095 -0.0858 0.0035  -0.0585 479  LEU B O   
4417 C CB  . LEU B 254 ? 0.2783 0.2444 0.2131 -0.0696 0.0035  -0.0530 479  LEU B CB  
4418 C CG  . LEU B 254 ? 0.3375 0.3071 0.2668 -0.0665 0.0022  -0.0538 479  LEU B CG  
4419 C CD1 . LEU B 254 ? 0.3872 0.3684 0.3232 -0.0612 0.0004  -0.0486 479  LEU B CD1 
4420 C CD2 . LEU B 254 ? 0.4677 0.4408 0.3915 -0.0726 -0.0020 -0.0580 479  LEU B CD2 
4421 N N   . PHE B 255 ? 0.2553 0.2005 0.1929 -0.0745 0.0107  -0.0530 480  PHE B N   
4422 C CA  . PHE B 255 ? 0.2766 0.2188 0.2190 -0.0782 0.0120  -0.0516 480  PHE B CA  
4423 C C   . PHE B 255 ? 0.2878 0.2204 0.2304 -0.0723 0.0172  -0.0483 480  PHE B C   
4424 O O   . PHE B 255 ? 0.2807 0.2124 0.2219 -0.0652 0.0189  -0.0465 480  PHE B O   
4425 C CB  . PHE B 255 ? 0.2595 0.2169 0.2117 -0.0801 0.0083  -0.0483 480  PHE B CB  
4426 C CG  . PHE B 255 ? 0.2385 0.2059 0.1962 -0.0730 0.0074  -0.0434 480  PHE B CG  
4427 C CD1 . PHE B 255 ? 0.2060 0.1711 0.1672 -0.0681 0.0104  -0.0391 480  PHE B CD1 
4428 C CD2 . PHE B 255 ? 0.2489 0.2278 0.2080 -0.0716 0.0034  -0.0431 480  PHE B CD2 
4429 C CE1 . PHE B 255 ? 0.1842 0.1579 0.1499 -0.0622 0.0094  -0.0351 480  PHE B CE1 
4430 C CE2 . PHE B 255 ? 0.2625 0.2494 0.2262 -0.0655 0.0027  -0.0389 480  PHE B CE2 
4431 C CZ  . PHE B 255 ? 0.2682 0.2525 0.2352 -0.0610 0.0056  -0.0351 480  PHE B CZ  
4432 N N   . GLU B 256 ? 0.2569 0.1828 0.2014 -0.0753 0.0196  -0.0472 481  GLU B N   
4433 C CA  . GLU B 256 ? 0.2492 0.1691 0.1957 -0.0697 0.0237  -0.0427 481  GLU B CA  
4434 C C   . GLU B 256 ? 0.2563 0.1866 0.2115 -0.0702 0.0222  -0.0381 481  GLU B C   
4435 O O   . GLU B 256 ? 0.2733 0.2118 0.2328 -0.0761 0.0193  -0.0389 481  GLU B O   
4436 C CB  . GLU B 256 ? 0.3055 0.2074 0.2462 -0.0715 0.0286  -0.0444 481  GLU B CB  
4437 C CG  . GLU B 256 ? 0.3632 0.2607 0.3041 -0.0808 0.0284  -0.0469 481  GLU B CG  
4438 C CD  . GLU B 256 ? 0.4890 0.3672 0.4242 -0.0817 0.0339  -0.0477 481  GLU B CD  
4439 O OE1 . GLU B 256 ? 0.4184 0.2855 0.3475 -0.0760 0.0374  -0.0484 481  GLU B OE1 
4440 O OE2 . GLU B 256 ? 0.3734 0.2473 0.3103 -0.0880 0.0349  -0.0476 481  GLU B OE2 
4441 N N   . CYS B 257 ? 0.2463 0.1769 0.2041 -0.0637 0.0242  -0.0333 482  CYS B N   
4442 C CA  . CYS B 257 ? 0.2234 0.1636 0.1884 -0.0631 0.0231  -0.0289 482  CYS B CA  
4443 C C   . CYS B 257 ? 0.2492 0.1821 0.2139 -0.0582 0.0270  -0.0245 482  CYS B C   
4444 O O   . CYS B 257 ? 0.2434 0.1659 0.2034 -0.0541 0.0300  -0.0244 482  CYS B O   
4445 C CB  . CYS B 257 ? 0.2046 0.1594 0.1740 -0.0598 0.0192  -0.0274 482  CYS B CB  
4446 S SG  . CYS B 257 ? 0.2254 0.1798 0.1920 -0.0511 0.0197  -0.0261 482  CYS B SG  
4447 N N   . LYS B 258 ? 0.2335 0.1721 0.2032 -0.0584 0.0270  -0.0206 483  LYS B N   
4448 C CA  . LYS B 258 ? 0.2160 0.1494 0.1855 -0.0537 0.0301  -0.0158 483  LYS B CA  
4449 C C   . LYS B 258 ? 0.2129 0.1576 0.1863 -0.0484 0.0280  -0.0122 483  LYS B C   
4450 O O   . LYS B 258 ? 0.2033 0.1591 0.1814 -0.0503 0.0255  -0.0118 483  LYS B O   
4451 C CB  . LYS B 258 ? 0.2114 0.1402 0.1821 -0.0584 0.0327  -0.0140 483  LYS B CB  
4452 C CG  . LYS B 258 ? 0.2277 0.1407 0.1931 -0.0619 0.0363  -0.0160 483  LYS B CG  
4453 C CD  . LYS B 258 ? 0.2548 0.1666 0.2227 -0.0698 0.0375  -0.0161 483  LYS B CD  
4454 C CE  . LYS B 258 ? 0.2350 0.1447 0.2043 -0.0681 0.0406  -0.0104 483  LYS B CE  
4455 N NZ  . LYS B 258 ? 0.2443 0.1549 0.2170 -0.0761 0.0418  -0.0102 483  LYS B NZ  
4456 N N   . LEU B 259 ? 0.1900 0.1319 0.1615 -0.0416 0.0290  -0.0096 484  LEU B N   
4457 C CA  . LEU B 259 ? 0.1793 0.1302 0.1538 -0.0366 0.0273  -0.0059 484  LEU B CA  
4458 C C   . LEU B 259 ? 0.1995 0.1460 0.1734 -0.0348 0.0299  -0.0014 484  LEU B C   
4459 O O   . LEU B 259 ? 0.2142 0.1518 0.1849 -0.0311 0.0325  0.0008  484  LEU B O   
4460 C CB  . LEU B 259 ? 0.1759 0.1277 0.1491 -0.0309 0.0264  -0.0059 484  LEU B CB  
4461 C CG  . LEU B 259 ? 0.1732 0.1319 0.1485 -0.0253 0.0249  -0.0020 484  LEU B CG  
4462 C CD1 . LEU B 259 ? 0.1897 0.1599 0.1690 -0.0269 0.0218  -0.0017 484  LEU B CD1 
4463 C CD2 . LEU B 259 ? 0.2070 0.1665 0.1818 -0.0206 0.0244  -0.0024 484  LEU B CD2 
4464 N N   . TYR B 260 ? 0.1932 0.1457 0.1699 -0.0374 0.0294  0.0002  485  TYR B N   
4465 C CA  . TYR B 260 ? 0.1843 0.1330 0.1599 -0.0362 0.0320  0.0047  485  TYR B CA  
4466 C C   . TYR B 260 ? 0.2119 0.1635 0.1865 -0.0294 0.0311  0.0084  485  TYR B C   
4467 O O   . TYR B 260 ? 0.2430 0.2029 0.2194 -0.0268 0.0280  0.0077  485  TYR B O   
4468 C CB  . TYR B 260 ? 0.2104 0.1658 0.1893 -0.0407 0.0320  0.0053  485  TYR B CB  
4469 C CG  . TYR B 260 ? 0.2093 0.1601 0.1891 -0.0479 0.0340  0.0031  485  TYR B CG  
4470 C CD1 . TYR B 260 ? 0.2162 0.1549 0.1928 -0.0498 0.0380  0.0048  485  TYR B CD1 
4471 C CD2 . TYR B 260 ? 0.2022 0.1610 0.1863 -0.0531 0.0317  -0.0005 485  TYR B CD2 
4472 C CE1 . TYR B 260 ? 0.2499 0.1840 0.2274 -0.0572 0.0397  0.0026  485  TYR B CE1 
4473 C CE2 . TYR B 260 ? 0.2101 0.1657 0.1955 -0.0604 0.0331  -0.0026 485  TYR B CE2 
4474 C CZ  . TYR B 260 ? 0.2185 0.1616 0.2006 -0.0627 0.0371  -0.0012 485  TYR B CZ  
4475 O OH  . TYR B 260 ? 0.2205 0.1597 0.2038 -0.0705 0.0385  -0.0033 485  TYR B OH  
4476 N N   A ARG B 261 ? 0.2278 0.1720 0.1992 -0.0267 0.0338  0.0126  486  ARG B N   
4477 N N   B ARG B 261 ? 0.2275 0.1716 0.1989 -0.0267 0.0338  0.0126  486  ARG B N   
4478 C CA  A ARG B 261 ? 0.2301 0.1765 0.2002 -0.0202 0.0328  0.0165  486  ARG B CA  
4479 C CA  B ARG B 261 ? 0.2316 0.1781 0.2017 -0.0203 0.0328  0.0165  486  ARG B CA  
4480 C C   A ARG B 261 ? 0.2327 0.1907 0.2047 -0.0193 0.0298  0.0174  486  ARG B C   
4481 C C   B ARG B 261 ? 0.2321 0.1906 0.2044 -0.0195 0.0296  0.0170  486  ARG B C   
4482 O O   A ARG B 261 ? 0.2130 0.1759 0.1850 -0.0148 0.0274  0.0187  486  ARG B O   
4483 O O   B ARG B 261 ? 0.2284 0.1921 0.2010 -0.0152 0.0270  0.0180  486  ARG B O   
4484 C CB  A ARG B 261 ? 0.3104 0.2470 0.2765 -0.0181 0.0363  0.0212  486  ARG B CB  
4485 C CB  B ARG B 261 ? 0.3219 0.2599 0.2883 -0.0183 0.0361  0.0214  486  ARG B CB  
4486 C CG  A ARG B 261 ? 0.3729 0.3141 0.3375 -0.0138 0.0353  0.0260  486  ARG B CG  
4487 C CG  B ARG B 261 ? 0.4123 0.3372 0.3756 -0.0169 0.0395  0.0221  486  ARG B CG  
4488 C CD  A ARG B 261 ? 0.5169 0.4497 0.4776 -0.0138 0.0389  0.0306  486  ARG B CD  
4489 C CD  B ARG B 261 ? 0.4407 0.3580 0.4004 -0.0152 0.0426  0.0276  486  ARG B CD  
4490 N NE  A ARG B 261 ? 0.5569 0.4769 0.5151 -0.0120 0.0422  0.0319  486  ARG B NE  
4491 N NE  B ARG B 261 ? 0.4817 0.4051 0.4404 -0.0095 0.0406  0.0321  486  ARG B NE  
4492 C CZ  A ARG B 261 ? 0.7254 0.6415 0.6814 -0.0056 0.0425  0.0357  486  ARG B CZ  
4493 C CZ  B ARG B 261 ? 0.7049 0.6229 0.6609 -0.0037 0.0417  0.0368  486  ARG B CZ  
4494 N NH1 A ARG B 261 ? 0.6903 0.6149 0.6465 -0.0008 0.0394  0.0386  486  ARG B NH1 
4495 N NH1 B ARG B 261 ? 0.7357 0.6410 0.6894 -0.0024 0.0454  0.0377  486  ARG B NH1 
4496 N NH2 A ARG B 261 ? 0.7398 0.6433 0.6935 -0.0041 0.0460  0.0366  486  ARG B NH2 
4497 N NH2 B ARG B 261 ? 0.6390 0.5643 0.5943 0.0008  0.0391  0.0405  486  ARG B NH2 
4498 N N   . SER B 262 ? 0.1730 0.1356 0.1467 -0.0235 0.0299  0.0165  487  SER B N   
4499 C CA  . SER B 262 ? 0.1829 0.1556 0.1580 -0.0225 0.0275  0.0171  487  SER B CA  
4500 C C   . SER B 262 ? 0.2228 0.2037 0.2014 -0.0227 0.0240  0.0134  487  SER B C   
4501 O O   . SER B 262 ? 0.2148 0.2033 0.1943 -0.0216 0.0219  0.0134  487  SER B O   
4502 C CB  . SER B 262 ? 0.2723 0.2470 0.2481 -0.0263 0.0296  0.0179  487  SER B CB  
4503 O OG  . SER B 262 ? 0.2780 0.2550 0.2579 -0.0315 0.0298  0.0144  487  SER B OG  
4504 N N   . GLY B 263 ? 0.1837 0.1627 0.1636 -0.0238 0.0233  0.0103  488  GLY B N   
4505 C CA  . GLY B 263 ? 0.1703 0.1562 0.1526 -0.0230 0.0200  0.0076  488  GLY B CA  
4506 C C   . GLY B 263 ? 0.1707 0.1621 0.1564 -0.0273 0.0187  0.0041  488  GLY B C   
4507 O O   . GLY B 263 ? 0.1619 0.1612 0.1499 -0.0267 0.0162  0.0033  488  GLY B O   
4508 N N   . PHE B 264 ? 0.1639 0.1511 0.1499 -0.0315 0.0202  0.0021  489  PHE B N   
4509 C CA  . PHE B 264 ? 0.1539 0.1469 0.1432 -0.0355 0.0183  -0.0013 489  PHE B CA  
4510 C C   . PHE B 264 ? 0.1625 0.1482 0.1501 -0.0393 0.0196  -0.0040 489  PHE B C   
4511 O O   . PHE B 264 ? 0.1755 0.1516 0.1601 -0.0395 0.0225  -0.0030 489  PHE B O   
4512 C CB  . PHE B 264 ? 0.1685 0.1686 0.1615 -0.0382 0.0183  -0.0007 489  PHE B CB  
4513 C CG  . PHE B 264 ? 0.1756 0.1711 0.1686 -0.0418 0.0217  0.0007  489  PHE B CG  
4514 C CD1 . PHE B 264 ? 0.2022 0.1935 0.1926 -0.0397 0.0243  0.0043  489  PHE B CD1 
4515 C CD2 . PHE B 264 ? 0.1642 0.1600 0.1598 -0.0478 0.0222  -0.0015 489  PHE B CD2 
4516 C CE1 . PHE B 264 ? 0.1960 0.1827 0.1862 -0.0432 0.0277  0.0060  489  PHE B CE1 
4517 C CE2 . PHE B 264 ? 0.2031 0.1946 0.1990 -0.0518 0.0255  -0.0001 489  PHE B CE2 
4518 C CZ  . PHE B 264 ? 0.2225 0.2092 0.2157 -0.0494 0.0285  0.0037  489  PHE B CZ  
4519 N N   . VAL B 265 ? 0.1706 0.1607 0.1599 -0.0423 0.0173  -0.0074 490  VAL B N   
4520 C CA  . VAL B 265 ? 0.1555 0.1393 0.1424 -0.0461 0.0178  -0.0108 490  VAL B CA  
4521 C C   . VAL B 265 ? 0.1612 0.1494 0.1515 -0.0527 0.0170  -0.0127 490  VAL B C   
4522 O O   . VAL B 265 ? 0.1588 0.1577 0.1538 -0.0534 0.0148  -0.0123 490  VAL B O   
4523 C CB  . VAL B 265 ? 0.1799 0.1652 0.1648 -0.0442 0.0155  -0.0133 490  VAL B CB  
4524 C CG1 . VAL B 265 ? 0.1844 0.1620 0.1653 -0.0479 0.0162  -0.0172 490  VAL B CG1 
4525 C CG2 . VAL B 265 ? 0.1779 0.1616 0.1611 -0.0377 0.0159  -0.0111 490  VAL B CG2 
4526 N N   . VAL B 266 ? 0.1721 0.1520 0.1601 -0.0575 0.0189  -0.0147 491  VAL B N   
4527 C CA  . VAL B 266 ? 0.1751 0.1591 0.1665 -0.0647 0.0180  -0.0168 491  VAL B CA  
4528 C C   . VAL B 266 ? 0.1884 0.1659 0.1757 -0.0690 0.0173  -0.0214 491  VAL B C   
4529 O O   . VAL B 266 ? 0.2034 0.1696 0.1847 -0.0672 0.0193  -0.0226 491  VAL B O   
4530 C CB  . VAL B 266 ? 0.2249 0.2058 0.2184 -0.0682 0.0213  -0.0144 491  VAL B CB  
4531 C CG1 . VAL B 266 ? 0.1909 0.1778 0.1874 -0.0639 0.0223  -0.0099 491  VAL B CG1 
4532 C CG2 . VAL B 266 ? 0.1889 0.1540 0.1766 -0.0690 0.0252  -0.0145 491  VAL B CG2 
4533 N N   . VAL B 267 ? 0.2048 0.1898 0.1953 -0.0748 0.0145  -0.0240 492  VAL B N   
4534 C CA  . VAL B 267 ? 0.1897 0.1692 0.1763 -0.0808 0.0135  -0.0287 492  VAL B CA  
4535 C C   . VAL B 267 ? 0.1957 0.1768 0.1865 -0.0888 0.0139  -0.0294 492  VAL B C   
4536 O O   . VAL B 267 ? 0.2276 0.2170 0.2251 -0.0895 0.0144  -0.0262 492  VAL B O   
4537 C CB  . VAL B 267 ? 0.2044 0.1922 0.1904 -0.0808 0.0089  -0.0316 492  VAL B CB  
4538 C CG1 . VAL B 267 ? 0.1896 0.1732 0.1702 -0.0739 0.0092  -0.0316 492  VAL B CG1 
4539 C CG2 . VAL B 267 ? 0.2062 0.2103 0.2002 -0.0806 0.0056  -0.0295 492  VAL B CG2 
4540 N N   . ASN B 268 ? 0.2326 0.2060 0.2193 -0.0952 0.0139  -0.0337 493  ASN B N   
4541 C CA  . ASN B 268 ? 0.2723 0.2449 0.2621 -0.1039 0.0146  -0.0348 493  ASN B CA  
4542 C C   . ASN B 268 ? 0.2519 0.2328 0.2431 -0.1108 0.0097  -0.0391 493  ASN B C   
4543 O O   . ASN B 268 ? 0.2542 0.2346 0.2401 -0.1096 0.0070  -0.0424 493  ASN B O   
4544 C CB  . ASN B 268 ? 0.2536 0.2073 0.2367 -0.1064 0.0192  -0.0360 493  ASN B CB  
4545 C CG  . ASN B 268 ? 0.2695 0.2211 0.2561 -0.1155 0.0207  -0.0365 493  ASN B CG  
4546 O OD1 . ASN B 268 ? 0.3031 0.2667 0.2981 -0.1180 0.0201  -0.0337 493  ASN B OD1 
4547 N ND2 . ASN B 268 ? 0.3691 0.3052 0.3490 -0.1205 0.0230  -0.0400 493  ASN B ND2 
4548 N N   . GLY B 269 ? 0.2513 0.2405 0.2497 -0.1180 0.0087  -0.0389 494  GLY B N   
4549 C CA  . GLY B 269 ? 0.3047 0.3016 0.3046 -0.1256 0.0039  -0.0430 494  GLY B CA  
4550 C C   . GLY B 269 ? 0.3989 0.4132 0.4035 -0.1229 -0.0015 -0.0425 494  GLY B C   
4551 O O   . GLY B 269 ? 0.3761 0.3945 0.3786 -0.1258 -0.0059 -0.0458 494  GLY B O   
4552 N N   . VAL B 270 ? 0.2539 0.2778 0.2643 -0.1159 -0.0013 -0.0378 495  VAL B N   
4553 C CA  . VAL B 270 ? 0.2848 0.3246 0.3000 -0.1126 -0.0059 -0.0367 495  VAL B CA  
4554 C C   . VAL B 270 ? 0.3247 0.3803 0.3514 -0.1167 -0.0075 -0.0345 495  VAL B C   
4555 O O   . VAL B 270 ? 0.2787 0.3368 0.3113 -0.1152 -0.0040 -0.0307 495  VAL B O   
4556 C CB  . VAL B 270 ? 0.3002 0.3406 0.3146 -0.1025 -0.0046 -0.0332 495  VAL B CB  
4557 C CG1 . VAL B 270 ? 0.3148 0.3700 0.3335 -0.0991 -0.0092 -0.0320 495  VAL B CG1 
4558 C CG2 . VAL B 270 ? 0.3292 0.3547 0.3333 -0.0984 -0.0026 -0.0349 495  VAL B CG2 
4559 N N   . ASN B 271 ? 0.2988 0.3645 0.3285 -0.1196 -0.0124 -0.0359 496  ASN B N   
4560 C CA  . ASN B 271 ? 0.4244 0.5046 0.4650 -0.1213 -0.0140 -0.0332 496  ASN B CA  
4561 C C   . ASN B 271 ? 0.5082 0.6048 0.5552 -0.1161 -0.0178 -0.0306 496  ASN B C   
4562 O O   . ASN B 271 ? 0.3524 0.4615 0.4095 -0.1157 -0.0179 -0.0274 496  ASN B O   
4563 C CB  . ASN B 271 ? 0.3889 0.4683 0.4293 -0.1280 -0.0165 -0.0361 496  ASN B CB  
4564 C CG  . ASN B 271 ? 0.6357 0.6978 0.6694 -0.1332 -0.0127 -0.0388 496  ASN B CG  
4565 O OD1 . ASN B 271 ? 0.6544 0.7069 0.6798 -0.1362 -0.0141 -0.0431 496  ASN B OD1 
4566 N ND2 . ASN B 271 ? 0.5660 0.6236 0.6029 -0.1339 -0.0076 -0.0362 496  ASN B ND2 
4567 N N   . VAL B 272 ? 0.3799 0.4764 0.4213 -0.1118 -0.0206 -0.0316 497  VAL B N   
4568 C CA  . VAL B 272 ? 0.2889 0.3987 0.3350 -0.1059 -0.0237 -0.0288 497  VAL B CA  
4569 C C   . VAL B 272 ? 0.2301 0.3340 0.2702 -0.1004 -0.0224 -0.0286 497  VAL B C   
4570 O O   . VAL B 272 ? 0.2902 0.3792 0.3210 -0.1000 -0.0202 -0.0309 497  VAL B O   
4571 C CB  . VAL B 272 ? 0.2688 0.3861 0.3143 -0.1065 -0.0295 -0.0300 497  VAL B CB  
4572 C CG1 . VAL B 272 ? 0.3234 0.4464 0.3749 -0.1125 -0.0310 -0.0304 497  VAL B CG1 
4573 C CG2 . VAL B 272 ? 0.3309 0.4370 0.3642 -0.1073 -0.0310 -0.0341 497  VAL B CG2 
4574 N N   . ARG B 273 ? 0.1950 0.3078 0.2395 -0.0934 -0.0232 -0.0251 498  ARG B N   
4575 C CA  . ARG B 273 ? 0.1578 0.2631 0.1960 -0.0855 -0.0220 -0.0240 498  ARG B CA  
4576 C C   . ARG B 273 ? 0.2394 0.3376 0.2678 -0.0864 -0.0245 -0.0274 498  ARG B C   
4577 O O   . ARG B 273 ? 0.2185 0.3240 0.2466 -0.0894 -0.0292 -0.0290 498  ARG B O   
4578 C CB  . ARG B 273 ? 0.1620 0.2785 0.2061 -0.0788 -0.0233 -0.0202 498  ARG B CB  
4579 C CG  . ARG B 273 ? 0.2152 0.3239 0.2535 -0.0711 -0.0216 -0.0188 498  ARG B CG  
4580 C CD  . ARG B 273 ? 0.2157 0.3346 0.2589 -0.0651 -0.0235 -0.0155 498  ARG B CD  
4581 N NE  . ARG B 273 ? 0.2497 0.3620 0.2893 -0.0581 -0.0212 -0.0137 498  ARG B NE  
4582 C CZ  . ARG B 273 ? 0.2630 0.3695 0.2957 -0.0550 -0.0223 -0.0142 498  ARG B CZ  
4583 N NH1 . ARG B 273 ? 0.3129 0.4180 0.3403 -0.0578 -0.0253 -0.0166 498  ARG B NH1 
4584 N NH2 . ARG B 273 ? 0.2286 0.3307 0.2596 -0.0491 -0.0204 -0.0124 498  ARG B NH2 
4585 N N   . THR B 274 ? 0.1884 0.2724 0.2086 -0.0838 -0.0213 -0.0286 499  THR B N   
4586 C CA  . THR B 274 ? 0.1883 0.2636 0.1985 -0.0850 -0.0225 -0.0322 499  THR B CA  
4587 C C   . THR B 274 ? 0.1868 0.2552 0.1916 -0.0776 -0.0206 -0.0308 499  THR B C   
4588 O O   . THR B 274 ? 0.2102 0.2720 0.2152 -0.0740 -0.0166 -0.0291 499  THR B O   
4589 C CB  . THR B 274 ? 0.2381 0.3011 0.2432 -0.0908 -0.0199 -0.0359 499  THR B CB  
4590 O OG1 . THR B 274 ? 0.2571 0.3268 0.2677 -0.0985 -0.0217 -0.0372 499  THR B OG1 
4591 C CG2 . THR B 274 ? 0.2758 0.3292 0.2698 -0.0917 -0.0207 -0.0400 499  THR B CG2 
4592 N N   . GLU B 275 ? 0.2403 0.3106 0.2404 -0.0755 -0.0235 -0.0315 500  GLU B N   
4593 C CA  . GLU B 275 ? 0.1829 0.2474 0.1778 -0.0692 -0.0219 -0.0304 500  GLU B CA  
4594 C C   . GLU B 275 ? 0.1777 0.2301 0.1626 -0.0706 -0.0203 -0.0341 500  GLU B C   
4595 O O   . GLU B 275 ? 0.1982 0.2482 0.1789 -0.0762 -0.0217 -0.0379 500  GLU B O   
4596 C CB  . GLU B 275 ? 0.2455 0.3195 0.2414 -0.0656 -0.0256 -0.0282 500  GLU B CB  
4597 C CG  . GLU B 275 ? 0.5384 0.6140 0.5377 -0.0588 -0.0242 -0.0242 500  GLU B CG  
4598 C CD  . GLU B 275 ? 0.6564 0.7405 0.6565 -0.0556 -0.0277 -0.0219 500  GLU B CD  
4599 O OE1 . GLU B 275 ? 0.5588 0.6531 0.5629 -0.0579 -0.0314 -0.0215 500  GLU B OE1 
4600 O OE2 . GLU B 275 ? 0.5708 0.6516 0.5676 -0.0509 -0.0269 -0.0204 500  GLU B OE2 
4601 N N   . PHE B 276 ? 0.1603 0.2051 0.1415 -0.0653 -0.0172 -0.0331 501  PHE B N   
4602 C CA  . PHE B 276 ? 0.2077 0.2408 0.1800 -0.0653 -0.0147 -0.0361 501  PHE B CA  
4603 C C   . PHE B 276 ? 0.2035 0.2365 0.1717 -0.0600 -0.0147 -0.0349 501  PHE B C   
4604 O O   . PHE B 276 ? 0.2032 0.2420 0.1757 -0.0555 -0.0153 -0.0312 501  PHE B O   
4605 C CB  . PHE B 276 ? 0.2101 0.2326 0.1822 -0.0643 -0.0099 -0.0360 501  PHE B CB  
4606 C CG  . PHE B 276 ? 0.1644 0.1858 0.1402 -0.0697 -0.0092 -0.0369 501  PHE B CG  
4607 C CD1 . PHE B 276 ? 0.2287 0.2445 0.2000 -0.0761 -0.0095 -0.0412 501  PHE B CD1 
4608 C CD2 . PHE B 276 ? 0.2314 0.2572 0.2148 -0.0686 -0.0082 -0.0335 501  PHE B CD2 
4609 C CE1 . PHE B 276 ? 0.2460 0.2607 0.2209 -0.0817 -0.0088 -0.0419 501  PHE B CE1 
4610 C CE2 . PHE B 276 ? 0.2850 0.3102 0.2721 -0.0738 -0.0072 -0.0340 501  PHE B CE2 
4611 C CZ  . PHE B 276 ? 0.3268 0.3465 0.3099 -0.0804 -0.0075 -0.0381 501  PHE B CZ  
4612 N N   . PRO B 277 ? 0.1862 0.2121 0.1456 -0.0604 -0.0137 -0.0379 502  PRO B N   
4613 C CA  . PRO B 277 ? 0.2143 0.2396 0.1696 -0.0555 -0.0130 -0.0366 502  PRO B CA  
4614 C C   . PRO B 277 ? 0.1904 0.2127 0.1492 -0.0499 -0.0095 -0.0334 502  PRO B C   
4615 O O   . PRO B 277 ? 0.2050 0.2212 0.1656 -0.0496 -0.0065 -0.0333 502  PRO B O   
4616 C CB  . PRO B 277 ? 0.2838 0.3000 0.2289 -0.0574 -0.0113 -0.0411 502  PRO B CB  
4617 C CG  . PRO B 277 ? 0.3085 0.3231 0.2521 -0.0644 -0.0130 -0.0450 502  PRO B CG  
4618 C CD  . PRO B 277 ? 0.1960 0.2131 0.1486 -0.0655 -0.0127 -0.0429 502  PRO B CD  
4619 N N   . MET B 278 ? 0.1921 0.2186 0.1514 -0.0456 -0.0101 -0.0306 503  MET B N   
4620 C CA  . MET B 278 ? 0.2217 0.2472 0.1848 -0.0407 -0.0077 -0.0272 503  MET B CA  
4621 C C   . MET B 278 ? 0.1989 0.2173 0.1570 -0.0376 -0.0040 -0.0278 503  MET B C   
4622 O O   . MET B 278 ? 0.2125 0.2299 0.1739 -0.0338 -0.0019 -0.0252 503  MET B O   
4623 C CB  . MET B 278 ? 0.1822 0.2162 0.1494 -0.0380 -0.0102 -0.0237 503  MET B CB  
4624 C CG  . MET B 278 ? 0.1903 0.2317 0.1641 -0.0393 -0.0130 -0.0221 503  MET B CG  
4625 S SD  . MET B 278 ? 0.1906 0.2296 0.1705 -0.0382 -0.0105 -0.0206 503  MET B SD  
4626 C CE  . MET B 278 ? 0.1806 0.2193 0.1618 -0.0328 -0.0092 -0.0173 503  MET B CE  
4627 N N   . SER B 279 ? 0.2147 0.2286 0.1651 -0.0391 -0.0031 -0.0310 504  SER B N   
4628 C CA  . SER B 279 ? 0.1932 0.2012 0.1390 -0.0357 0.0007  -0.0314 504  SER B CA  
4629 C C   . SER B 279 ? 0.2885 0.2862 0.2321 -0.0355 0.0049  -0.0336 504  SER B C   
4630 O O   . SER B 279 ? 0.3493 0.3412 0.2882 -0.0329 0.0085  -0.0347 504  SER B O   
4631 C CB  . SER B 279 ? 0.2796 0.2878 0.2172 -0.0369 0.0000  -0.0337 504  SER B CB  
4632 O OG  . SER B 279 ? 0.3987 0.4048 0.3316 -0.0420 -0.0020 -0.0377 504  SER B OG  
4633 N N   . GLY B 280 ? 0.2349 0.2302 0.1818 -0.0378 0.0047  -0.0340 505  GLY B N   
4634 C CA  . GLY B 280 ? 0.2495 0.2343 0.1942 -0.0375 0.0087  -0.0356 505  GLY B CA  
4635 C C   . GLY B 280 ? 0.2003 0.1842 0.1504 -0.0326 0.0113  -0.0318 505  GLY B C   
4636 O O   . GLY B 280 ? 0.2027 0.1941 0.1587 -0.0304 0.0096  -0.0282 505  GLY B O   
4637 N N   . VAL B 281 ? 0.2147 0.1887 0.1623 -0.0309 0.0155  -0.0327 506  VAL B N   
4638 C CA  . VAL B 281 ? 0.2183 0.1905 0.1704 -0.0263 0.0180  -0.0291 506  VAL B CA  
4639 C C   . VAL B 281 ? 0.1827 0.1468 0.1348 -0.0283 0.0197  -0.0297 506  VAL B C   
4640 O O   . VAL B 281 ? 0.2459 0.2010 0.1922 -0.0313 0.0214  -0.0334 506  VAL B O   
4641 C CB  . VAL B 281 ? 0.2413 0.2097 0.1912 -0.0209 0.0219  -0.0285 506  VAL B CB  
4642 C CG1 . VAL B 281 ? 0.2445 0.2119 0.1995 -0.0162 0.0241  -0.0245 506  VAL B CG1 
4643 C CG2 . VAL B 281 ? 0.2484 0.2251 0.1988 -0.0192 0.0206  -0.0275 506  VAL B CG2 
4644 N N   . PHE B 282 ? 0.2188 0.1856 0.1766 -0.0269 0.0192  -0.0260 507  PHE B N   
4645 C CA  . PHE B 282 ? 0.2279 0.1867 0.1858 -0.0281 0.0214  -0.0255 507  PHE B CA  
4646 C C   . PHE B 282 ? 0.2347 0.1850 0.1908 -0.0228 0.0258  -0.0241 507  PHE B C   
4647 O O   . PHE B 282 ? 0.2721 0.2269 0.2316 -0.0176 0.0262  -0.0206 507  PHE B O   
4648 C CB  . PHE B 282 ? 0.2120 0.1773 0.1761 -0.0283 0.0194  -0.0219 507  PHE B CB  
4649 C CG  . PHE B 282 ? 0.1762 0.1494 0.1428 -0.0332 0.0156  -0.0229 507  PHE B CG  
4650 C CD1 . PHE B 282 ? 0.1941 0.1775 0.1634 -0.0325 0.0123  -0.0222 507  PHE B CD1 
4651 C CD2 . PHE B 282 ? 0.1846 0.1550 0.1514 -0.0384 0.0155  -0.0243 507  PHE B CD2 
4652 C CE1 . PHE B 282 ? 0.1639 0.1549 0.1361 -0.0363 0.0090  -0.0227 507  PHE B CE1 
4653 C CE2 . PHE B 282 ? 0.2135 0.1924 0.1836 -0.0426 0.0122  -0.0249 507  PHE B CE2 
4654 C CZ  . PHE B 282 ? 0.2027 0.1920 0.1756 -0.0413 0.0089  -0.0241 507  PHE B CZ  
4655 N N   . GLU B 283 ? 0.2524 0.1904 0.2032 -0.0242 0.0292  -0.0268 508  GLU B N   
4656 C CA  . GLU B 283 ? 0.2821 0.2104 0.2306 -0.0189 0.0340  -0.0257 508  GLU B CA  
4657 C C   . GLU B 283 ? 0.3127 0.2321 0.2612 -0.0197 0.0361  -0.0240 508  GLU B C   
4658 O O   . GLU B 283 ? 0.2873 0.2015 0.2335 -0.0257 0.0359  -0.0267 508  GLU B O   
4659 C CB  . GLU B 283 ? 0.3027 0.2219 0.2435 -0.0192 0.0370  -0.0305 508  GLU B CB  
4660 C CG  . GLU B 283 ? 0.4068 0.3343 0.3464 -0.0188 0.0351  -0.0322 508  GLU B CG  
4661 C CD  . GLU B 283 ? 0.4606 0.3793 0.3912 -0.0201 0.0377  -0.0376 508  GLU B CD  
4662 O OE1 . GLU B 283 ? 0.4269 0.3330 0.3520 -0.0225 0.0404  -0.0408 508  GLU B OE1 
4663 O OE2 . GLU B 283 ? 0.6862 0.6104 0.6149 -0.0189 0.0372  -0.0387 508  GLU B OE2 
4664 N N   . PHE B 284 ? 0.3144 0.2324 0.2657 -0.0138 0.0382  -0.0195 509  PHE B N   
4665 C CA  . PHE B 284 ? 0.2680 0.1766 0.2188 -0.0137 0.0408  -0.0172 509  PHE B CA  
4666 C C   . PHE B 284 ? 0.3044 0.1967 0.2482 -0.0144 0.0454  -0.0206 509  PHE B C   
4667 O O   . PHE B 284 ? 0.3232 0.2104 0.2634 -0.0105 0.0483  -0.0223 509  PHE B O   
4668 C CB  . PHE B 284 ? 0.3015 0.2131 0.2564 -0.0067 0.0416  -0.0112 509  PHE B CB  
4669 C CG  . PHE B 284 ? 0.2504 0.1516 0.2041 -0.0054 0.0447  -0.0081 509  PHE B CG  
4670 C CD1 . PHE B 284 ? 0.2648 0.1662 0.2196 -0.0097 0.0434  -0.0066 509  PHE B CD1 
4671 C CD2 . PHE B 284 ? 0.3586 0.2498 0.3100 0.0007  0.0492  -0.0063 509  PHE B CD2 
4672 C CE1 . PHE B 284 ? 0.3152 0.2066 0.2684 -0.0085 0.0465  -0.0034 509  PHE B CE1 
4673 C CE2 . PHE B 284 ? 0.4039 0.2849 0.3538 0.0022  0.0521  -0.0030 509  PHE B CE2 
4674 C CZ  . PHE B 284 ? 0.3312 0.2122 0.2818 -0.0025 0.0507  -0.0014 509  PHE B CZ  
4675 N N   . VAL B 285 ? 0.2885 0.1721 0.2301 -0.0194 0.0465  -0.0215 510  VAL B N   
4676 C CA  . VAL B 285 ? 0.3158 0.1822 0.2504 -0.0209 0.0510  -0.0248 510  VAL B CA  
4677 C C   . VAL B 285 ? 0.3549 0.2111 0.2895 -0.0170 0.0549  -0.0202 510  VAL B C   
4678 O O   . VAL B 285 ? 0.3792 0.2254 0.3107 -0.0111 0.0593  -0.0194 510  VAL B O   
4679 C CB  . VAL B 285 ? 0.3405 0.2032 0.2718 -0.0306 0.0495  -0.0300 510  VAL B CB  
4680 C CG1 . VAL B 285 ? 0.3260 0.1694 0.2496 -0.0327 0.0542  -0.0335 510  VAL B CG1 
4681 C CG2 . VAL B 285 ? 0.3343 0.2068 0.2649 -0.0338 0.0456  -0.0342 510  VAL B CG2 
4682 N N   . SER B 286 ? 0.3214 0.1799 0.2593 -0.0198 0.0536  -0.0168 511  SER B N   
4683 C CA  . SER B 286 ? 0.3133 0.1614 0.2504 -0.0169 0.0572  -0.0122 511  SER B CA  
4684 C C   . SER B 286 ? 0.3146 0.1711 0.2565 -0.0198 0.0545  -0.0082 511  SER B C   
4685 O O   . SER B 286 ? 0.3441 0.2124 0.2894 -0.0246 0.0504  -0.0097 511  SER B O   
4686 C CB  . SER B 286 ? 0.3260 0.1552 0.2562 -0.0208 0.0616  -0.0157 511  SER B CB  
4687 O OG  . SER B 286 ? 0.4636 0.2934 0.3935 -0.0306 0.0596  -0.0191 511  SER B OG  
4688 N N   . TRP B 287 ? 0.3217 0.1714 0.2633 -0.0167 0.0572  -0.0030 512  TRP B N   
4689 C CA  . TRP B 287 ? 0.3436 0.1988 0.2883 -0.0195 0.0557  0.0010  512  TRP B CA  
4690 C C   . TRP B 287 ? 0.3354 0.1798 0.2772 -0.0275 0.0580  -0.0011 512  TRP B C   
4691 O O   . TRP B 287 ? 0.3633 0.1916 0.2999 -0.0282 0.0622  -0.0027 512  TRP B O   
4692 C CB  . TRP B 287 ? 0.3428 0.1970 0.2883 -0.0122 0.0572  0.0082  512  TRP B CB  
4693 C CG  . TRP B 287 ? 0.3378 0.2052 0.2872 -0.0055 0.0541  0.0107  512  TRP B CG  
4694 C CD1 . TRP B 287 ? 0.3956 0.2620 0.3452 0.0021  0.0553  0.0121  512  TRP B CD1 
4695 C CD2 . TRP B 287 ? 0.3068 0.1906 0.2610 -0.0060 0.0493  0.0120  512  TRP B CD2 
4696 N NE1 . TRP B 287 ? 0.3499 0.2316 0.3043 0.0057  0.0513  0.0143  512  TRP B NE1 
4697 C CE2 . TRP B 287 ? 0.3300 0.2217 0.2869 0.0008  0.0476  0.0141  512  TRP B CE2 
4698 C CE3 . TRP B 287 ? 0.3350 0.2273 0.2916 -0.0116 0.0465  0.0116  512  TRP B CE3 
4699 C CZ2 . TRP B 287 ? 0.3029 0.2098 0.2642 0.0018  0.0431  0.0155  512  TRP B CZ2 
4700 C CZ3 . TRP B 287 ? 0.2870 0.1939 0.2476 -0.0100 0.0423  0.0130  512  TRP B CZ3 
4701 C CH2 . TRP B 287 ? 0.3338 0.2474 0.2964 -0.0035 0.0406  0.0148  512  TRP B CH2 
4702 N N   . VAL B 288 ? 0.2866 0.1400 0.2320 -0.0337 0.0554  -0.0011 513  VAL B N   
4703 C CA  . VAL B 288 ? 0.2852 0.1307 0.2293 -0.0421 0.0573  -0.0028 513  VAL B CA  
4704 C C   . VAL B 288 ? 0.3271 0.1791 0.2747 -0.0436 0.0570  0.0023  513  VAL B C   
4705 O O   . VAL B 288 ? 0.3501 0.2153 0.3016 -0.0399 0.0541  0.0054  513  VAL B O   
4706 C CB  . VAL B 288 ? 0.3031 0.1532 0.2480 -0.0501 0.0545  -0.0096 513  VAL B CB  
4707 C CG1 . VAL B 288 ? 0.3314 0.1735 0.2711 -0.0489 0.0553  -0.0149 513  VAL B CG1 
4708 C CG2 . VAL B 288 ? 0.2648 0.1344 0.2159 -0.0510 0.0493  -0.0098 513  VAL B CG2 
4709 N N   . PRO B 289 ? 0.3581 0.2005 0.3042 -0.0492 0.0601  0.0032  514  PRO B N   
4710 C CA  . PRO B 289 ? 0.2878 0.1366 0.2372 -0.0516 0.0603  0.0077  514  PRO B CA  
4711 C C   . PRO B 289 ? 0.3594 0.2235 0.3147 -0.0580 0.0565  0.0048  514  PRO B C   
4712 O O   . PRO B 289 ? 0.3311 0.1992 0.2877 -0.0620 0.0539  -0.0008 514  PRO B O   
4713 C CB  . PRO B 289 ? 0.3475 0.1799 0.2932 -0.0562 0.0654  0.0092  514  PRO B CB  
4714 C CG  . PRO B 289 ? 0.4114 0.2321 0.3533 -0.0600 0.0665  0.0029  514  PRO B CG  
4715 C CD  . PRO B 289 ? 0.3638 0.1876 0.3045 -0.0528 0.0644  0.0008  514  PRO B CD  
4716 N N   . ASN B 290 ? 0.3074 0.1801 0.2661 -0.0587 0.0564  0.0089  515  ASN B N   
4717 C CA  . ASN B 290 ? 0.2894 0.1772 0.2543 -0.0639 0.0533  0.0070  515  ASN B CA  
4718 C C   . ASN B 290 ? 0.2867 0.1719 0.2534 -0.0737 0.0537  0.0025  515  ASN B C   
4719 O O   . ASN B 290 ? 0.3259 0.2229 0.2973 -0.0777 0.0500  -0.0012 515  ASN B O   
4720 C CB  . ASN B 290 ? 0.3157 0.2106 0.2830 -0.0630 0.0544  0.0124  515  ASN B CB  
4721 C CG  . ASN B 290 ? 0.5385 0.4413 0.5053 -0.0546 0.0523  0.0157  515  ASN B CG  
4722 O OD1 . ASN B 290 ? 0.4772 0.3877 0.4455 -0.0514 0.0485  0.0131  515  ASN B OD1 
4723 N ND2 . ASN B 290 ? 0.3959 0.2964 0.3603 -0.0512 0.0546  0.0214  515  ASN B ND2 
4724 N N   . PHE B 291 ? 0.2800 0.1502 0.2432 -0.0778 0.0578  0.0029  516  PHE B N   
4725 C CA  . PHE B 291 ? 0.2877 0.1556 0.2528 -0.0881 0.0581  -0.0013 516  PHE B CA  
4726 C C   . PHE B 291 ? 0.2976 0.1606 0.2597 -0.0906 0.0560  -0.0081 516  PHE B C   
4727 O O   . PHE B 291 ? 0.3559 0.2177 0.3192 -0.0995 0.0554  -0.0124 516  PHE B O   
4728 C CB  . PHE B 291 ? 0.3608 0.2137 0.3230 -0.0927 0.0635  0.0015  516  PHE B CB  
4729 C CG  . PHE B 291 ? 0.4401 0.2728 0.3941 -0.0887 0.0673  0.0020  516  PHE B CG  
4730 C CD1 . PHE B 291 ? 0.4333 0.2537 0.3828 -0.0923 0.0678  -0.0038 516  PHE B CD1 
4731 C CD2 . PHE B 291 ? 0.4616 0.2870 0.4120 -0.0813 0.0706  0.0085  516  PHE B CD2 
4732 C CE1 . PHE B 291 ? 0.4299 0.2311 0.3719 -0.0882 0.0718  -0.0033 516  PHE B CE1 
4733 C CE2 . PHE B 291 ? 0.4841 0.2911 0.4275 -0.0770 0.0743  0.0095  516  PHE B CE2 
4734 C CZ  . PHE B 291 ? 0.4572 0.2518 0.3965 -0.0803 0.0751  0.0035  516  PHE B CZ  
4735 N N   . PHE B 292 ? 0.3141 0.1740 0.2721 -0.0832 0.0551  -0.0092 517  PHE B N   
4736 C CA  . PHE B 292 ? 0.3867 0.2414 0.3408 -0.0850 0.0535  -0.0157 517  PHE B CA  
4737 C C   . PHE B 292 ? 0.3151 0.1851 0.2742 -0.0907 0.0483  -0.0201 517  PHE B C   
4738 O O   . PHE B 292 ? 0.3068 0.1926 0.2710 -0.0876 0.0449  -0.0186 517  PHE B O   
4739 C CB  . PHE B 292 ? 0.3713 0.2234 0.3214 -0.0754 0.0534  -0.0153 517  PHE B CB  
4740 C CG  . PHE B 292 ? 0.4164 0.2626 0.3616 -0.0764 0.0525  -0.0217 517  PHE B CG  
4741 C CD1 . PHE B 292 ? 0.4282 0.2551 0.3661 -0.0779 0.0566  -0.0244 517  PHE B CD1 
4742 C CD2 . PHE B 292 ? 0.3094 0.1684 0.2565 -0.0760 0.0478  -0.0251 517  PHE B CD2 
4743 C CE1 . PHE B 292 ? 0.3836 0.2045 0.3160 -0.0789 0.0560  -0.0306 517  PHE B CE1 
4744 C CE2 . PHE B 292 ? 0.3050 0.1585 0.2467 -0.0770 0.0472  -0.0309 517  PHE B CE2 
4745 C CZ  . PHE B 292 ? 0.3779 0.2124 0.3120 -0.0785 0.0513  -0.0338 517  PHE B CZ  
4746 N N   . GLN B 293 ? 0.3241 0.1890 0.2814 -0.0991 0.0477  -0.0255 518  GLN B N   
4747 C CA  . GLN B 293 ? 0.2869 0.1660 0.2488 -0.1052 0.0426  -0.0296 518  GLN B CA  
4748 C C   . GLN B 293 ? 0.3154 0.1941 0.2723 -0.1031 0.0397  -0.0348 518  GLN B C   
4749 O O   . GLN B 293 ? 0.3193 0.1831 0.2686 -0.1048 0.0417  -0.0389 518  GLN B O   
4750 C CB  . GLN B 293 ? 0.2979 0.1743 0.2618 -0.1166 0.0430  -0.0322 518  GLN B CB  
4751 C CG  . GLN B 293 ? 0.3255 0.2068 0.2959 -0.1190 0.0453  -0.0267 518  GLN B CG  
4752 C CD  . GLN B 293 ? 0.3924 0.2742 0.3665 -0.1304 0.0452  -0.0289 518  GLN B CD  
4753 O OE1 . GLN B 293 ? 0.3366 0.2279 0.3133 -0.1348 0.0404  -0.0333 518  GLN B OE1 
4754 N NE2 . GLN B 293 ? 0.3577 0.2322 0.3326 -0.1319 0.0493  -0.0250 518  GLN B NE2 
4755 N N   . LEU B 294 ? 0.2896 0.1844 0.2506 -0.0995 0.0354  -0.0346 519  LEU B N   
4756 C CA  . LEU B 294 ? 0.2723 0.1694 0.2292 -0.0971 0.0324  -0.0388 519  LEU B CA  
4757 C C   . LEU B 294 ? 0.2997 0.1972 0.2546 -0.1060 0.0294  -0.0450 519  LEU B C   
4758 O O   . LEU B 294 ? 0.3178 0.2217 0.2778 -0.1140 0.0277  -0.0456 519  LEU B O   
4759 C CB  . LEU B 294 ? 0.2493 0.1638 0.2118 -0.0916 0.0285  -0.0362 519  LEU B CB  
4760 C CG  . LEU B 294 ? 0.2402 0.1563 0.2044 -0.0826 0.0304  -0.0306 519  LEU B CG  
4761 C CD1 . LEU B 294 ? 0.2230 0.1572 0.1945 -0.0800 0.0266  -0.0280 519  LEU B CD1 
4762 C CD2 . LEU B 294 ? 0.2573 0.1653 0.2151 -0.0758 0.0318  -0.0316 519  LEU B CD2 
4763 N N   . ALA B 295 ? 0.2966 0.1881 0.2440 -0.1048 0.0286  -0.0496 520  ALA B N   
4764 C CA  . ALA B 295 ? 0.3626 0.2579 0.3076 -0.1122 0.0245  -0.0556 520  ALA B CA  
4765 C C   . ALA B 295 ? 0.3150 0.2317 0.2682 -0.1127 0.0188  -0.0541 520  ALA B C   
4766 O O   . ALA B 295 ? 0.3406 0.2666 0.2971 -0.1052 0.0178  -0.0504 520  ALA B O   
4767 C CB  . ALA B 295 ? 0.3639 0.2497 0.2986 -0.1093 0.0250  -0.0603 520  ALA B CB  
4768 N N   . PRO B 296 ? 0.2956 0.2210 0.2527 -0.1214 0.0150  -0.0565 521  PRO B N   
4769 C CA  . PRO B 296 ? 0.3067 0.2528 0.2719 -0.1214 0.0097  -0.0548 521  PRO B CA  
4770 C C   . PRO B 296 ? 0.3535 0.3048 0.3143 -0.1164 0.0064  -0.0566 521  PRO B C   
4771 O O   . PRO B 296 ? 0.3827 0.3234 0.3338 -0.1164 0.0070  -0.0610 521  PRO B O   
4772 C CB  . PRO B 296 ? 0.3546 0.3073 0.3238 -0.1305 0.0064  -0.0570 521  PRO B CB  
4773 C CG  . PRO B 296 ? 0.4781 0.4134 0.4388 -0.1339 0.0089  -0.0610 521  PRO B CG  
4774 C CD  . PRO B 296 ? 0.3813 0.2996 0.3370 -0.1301 0.0154  -0.0596 521  PRO B CD  
4775 N N   . VAL B 297 ? 0.2801 0.2472 0.2476 -0.1119 0.0033  -0.0530 522  VAL B N   
4776 C CA  . VAL B 297 ? 0.2786 0.2512 0.2423 -0.1072 0.0002  -0.0541 522  VAL B CA  
4777 C C   . VAL B 297 ? 0.5688 0.5437 0.5278 -0.1141 -0.0041 -0.0595 522  VAL B C   
4778 O O   . VAL B 297 ? 0.4072 0.3885 0.3706 -0.1213 -0.0069 -0.0606 522  VAL B O   
4779 C CB  . VAL B 297 ? 0.3028 0.2918 0.2748 -0.1017 -0.0024 -0.0492 522  VAL B CB  
4780 C CG1 . VAL B 297 ? 0.2815 0.2670 0.2559 -0.0941 0.0017  -0.0445 522  VAL B CG1 
4781 C CG2 . VAL B 297 ? 0.3750 0.3784 0.3566 -0.1070 -0.0057 -0.0479 522  VAL B CG2 
4782 O OXT . VAL B 297 ? 0.4255 0.3959 0.3760 -0.1120 -0.0048 -0.0626 522  VAL B OXT 
4783 S S   . SO4 C .   ? 1.0855 0.9898 1.0325 -0.0471 -0.0185 -0.0188 601  SO4 A S   
4784 O O1  . SO4 C .   ? 0.5919 0.5023 0.5367 -0.0445 -0.0194 -0.0217 601  SO4 A O1  
4785 O O2  . SO4 C .   ? 0.9602 0.8543 0.9026 -0.0540 -0.0200 -0.0220 601  SO4 A O2  
4786 O O3  . SO4 C .   ? 0.8873 0.7834 0.8329 -0.0409 -0.0148 -0.0170 601  SO4 A O3  
4787 O O4  . SO4 C .   ? 0.8515 0.7685 0.8069 -0.0490 -0.0198 -0.0144 601  SO4 A O4  
4788 S S   . SO4 D .   ? 0.4587 0.5685 0.4553 -0.0315 -0.0649 0.0174  602  SO4 A S   
4789 O O1  . SO4 D .   ? 0.4727 0.5709 0.4611 -0.0287 -0.0606 0.0153  602  SO4 A O1  
4790 O O2  . SO4 D .   ? 0.4199 0.5386 0.4239 -0.0264 -0.0644 0.0228  602  SO4 A O2  
4791 O O3  . SO4 D .   ? 0.7442 0.8569 0.7348 -0.0355 -0.0709 0.0160  602  SO4 A O3  
4792 O O4  . SO4 D .   ? 0.3820 0.4914 0.3848 -0.0352 -0.0638 0.0155  602  SO4 A O4  
4793 S S   . SO4 E .   ? 1.3496 1.3838 1.2948 -0.0455 -0.0152 -0.0317 601  SO4 B S   
4794 O O1  . SO4 E .   ? 0.3563 0.3956 0.3099 -0.0470 -0.0171 -0.0303 601  SO4 B O1  
4795 O O2  . SO4 E .   ? 0.6921 0.7158 0.6334 -0.0457 -0.0108 -0.0346 601  SO4 B O2  
4796 O O3  . SO4 E .   ? 0.6115 0.6479 0.5582 -0.0406 -0.0142 -0.0277 601  SO4 B O3  
4797 O O4  . SO4 E .   ? 1.1764 1.2135 1.1148 -0.0489 -0.0185 -0.0340 601  SO4 B O4  
4798 S S   . SO4 F .   ? 0.3697 0.4659 0.4117 0.0299  -0.0177 0.0239  602  SO4 B S   
4799 O O1  . SO4 F .   ? 0.5151 0.6054 0.5575 0.0364  -0.0150 0.0258  602  SO4 B O1  
4800 O O2  . SO4 F .   ? 0.3281 0.4389 0.3770 0.0299  -0.0206 0.0260  602  SO4 B O2  
4801 O O3  . SO4 F .   ? 0.3062 0.4001 0.3474 0.0262  -0.0153 0.0200  602  SO4 B O3  
4802 O O4  . SO4 F .   ? 0.2736 0.3635 0.3090 0.0272  -0.0199 0.0243  602  SO4 B O4  
4803 O O   . HOH G .   ? 0.5206 0.5697 0.4489 -0.0172 -0.0012 0.0079  701  HOH A O   
4804 O O   . HOH G .   ? 0.4011 0.4197 0.3810 0.0074  0.0304  -0.0054 702  HOH A O   
4805 O O   . HOH G .   ? 0.5817 0.6235 0.5968 -0.0574 0.0186  0.0584  703  HOH A O   
4806 O O   . HOH G .   ? 0.5857 0.6857 0.5591 -0.0225 -0.0417 0.0047  704  HOH A O   
4807 O O   . HOH G .   ? 0.2385 0.3221 0.2649 0.0251  0.0518  0.0192  705  HOH A O   
4808 O O   . HOH G .   ? 0.3815 0.4385 0.3018 -0.0173 0.0360  0.0442  706  HOH A O   
4809 O O   . HOH G .   ? 0.3382 0.5847 0.5137 0.0518  0.0600  0.0731  707  HOH A O   
4810 O O   . HOH G .   ? 0.4260 0.4879 0.4143 0.0019  0.0363  0.0102  708  HOH A O   
4811 O O   . HOH G .   ? 0.4019 0.5021 0.4750 -0.0716 -0.0037 0.0410  709  HOH A O   
4812 O O   . HOH G .   ? 0.3384 0.3273 0.3466 -0.0944 -0.0343 0.0020  710  HOH A O   
4813 O O   . HOH G .   ? 0.6475 0.6211 0.6344 0.0217  -0.0060 0.0182  711  HOH A O   
4814 O O   . HOH G .   ? 0.3726 0.6652 0.5782 -0.0309 -0.0132 0.0716  712  HOH A O   
4815 O O   . HOH G .   ? 0.4886 0.6574 0.5121 -0.0096 -0.0799 0.0468  713  HOH A O   
4816 O O   . HOH G .   ? 0.2565 0.3402 0.3194 -0.0803 -0.0243 0.0263  714  HOH A O   
4817 O O   . HOH G .   ? 0.3587 0.4383 0.2864 -0.0111 -0.0357 0.0260  715  HOH A O   
4818 O O   . HOH G .   ? 0.4880 0.5449 0.5029 0.0638  -0.0270 0.0657  716  HOH A O   
4819 O O   . HOH G .   ? 0.3904 0.4876 0.4337 0.0130  -0.0123 0.0338  717  HOH A O   
4820 O O   . HOH G .   ? 0.5725 0.4567 0.5196 -0.1194 -0.0410 -0.0320 718  HOH A O   
4821 O O   . HOH G .   ? 0.4993 0.5628 0.4856 0.0070  -0.0258 0.0321  719  HOH A O   
4822 O O   . HOH G .   ? 0.4815 0.4686 0.4656 -0.0511 0.0144  0.0673  720  HOH A O   
4823 O O   . HOH G .   ? 0.5028 0.5907 0.5320 -0.0686 -0.0550 0.0056  721  HOH A O   
4824 O O   . HOH G .   ? 0.5729 0.5236 0.5260 -0.0048 -0.0016 0.0729  722  HOH A O   
4825 O O   . HOH G .   ? 0.4577 0.5831 0.5404 -0.0608 0.0131  0.0504  723  HOH A O   
4826 O O   . HOH G .   ? 0.4576 0.3846 0.4338 -0.0842 -0.0267 -0.0060 724  HOH A O   
4827 O O   . HOH G .   ? 0.4024 0.3689 0.3874 -0.0466 0.0034  0.0525  725  HOH A O   
4828 O O   . HOH G .   ? 0.7463 0.6646 0.7405 -0.0912 -0.0068 0.0300  726  HOH A O   
4829 O O   . HOH G .   ? 0.2878 0.5259 0.4427 -0.0522 -0.0399 0.0518  727  HOH A O   
4830 O O   . HOH G .   ? 0.3273 0.4330 0.3701 0.0067  -0.0214 0.0340  728  HOH A O   
4831 O O   . HOH G .   ? 0.5326 0.4957 0.5150 0.0177  -0.0069 0.0230  729  HOH A O   
4832 O O   . HOH G .   ? 0.2166 0.3144 0.2650 0.0316  -0.0066 0.0451  730  HOH A O   
4833 O O   . HOH G .   ? 0.2346 0.3389 0.2366 -0.0045 -0.0388 0.0178  731  HOH A O   
4834 O O   . HOH G .   ? 0.2735 0.3246 0.2216 -0.0205 0.0201  0.0422  732  HOH A O   
4835 O O   . HOH G .   ? 0.3243 0.3736 0.3320 -0.0164 -0.0124 0.0063  733  HOH A O   
4836 O O   . HOH G .   ? 0.4054 0.3336 0.3762 -0.0252 -0.0095 0.0113  734  HOH A O   
4837 O O   . HOH G .   ? 0.4365 0.4959 0.4433 0.0352  0.0644  0.0108  735  HOH A O   
4838 O O   . HOH G .   ? 0.4698 0.6826 0.5822 -0.0703 -0.0744 0.0340  736  HOH A O   
4839 O O   . HOH G .   ? 0.6254 0.6022 0.5848 -0.0348 0.0138  0.0775  737  HOH A O   
4840 O O   . HOH G .   ? 0.4983 0.5365 0.4670 -0.0062 0.0204  -0.0027 738  HOH A O   
4841 O O   . HOH G .   ? 0.3812 0.3226 0.3412 -0.0004 -0.0036 0.0635  739  HOH A O   
4842 O O   . HOH G .   ? 0.2594 0.2686 0.2591 0.0482  -0.0151 0.0494  740  HOH A O   
4843 O O   . HOH G .   ? 0.3116 0.5762 0.4629 -0.0500 -0.0701 0.0530  741  HOH A O   
4844 O O   . HOH G .   ? 0.5490 0.5601 0.5600 -0.0689 0.0173  0.0645  742  HOH A O   
4845 O O   . HOH G .   ? 0.3105 0.3379 0.3076 -0.0178 -0.0154 0.0046  743  HOH A O   
4846 O O   . HOH G .   ? 0.2385 0.2164 0.2428 -0.0685 -0.0155 0.0195  744  HOH A O   
4847 O O   . HOH G .   ? 0.4135 0.4937 0.3995 -0.0255 -0.0500 0.0113  745  HOH A O   
4848 O O   . HOH G .   ? 0.3951 0.4758 0.4549 0.0644  0.0233  0.0525  746  HOH A O   
4849 O O   . HOH G .   ? 0.4096 0.5249 0.4289 0.0102  -0.0425 0.0449  747  HOH A O   
4850 O O   . HOH G .   ? 0.2501 0.5686 0.4779 0.0115  0.0097  0.0857  748  HOH A O   
4851 O O   . HOH G .   ? 0.1636 0.3258 0.2661 -0.0620 -0.0333 0.0351  749  HOH A O   
4852 O O   . HOH G .   ? 0.2745 0.3258 0.2405 -0.0161 0.0076  0.0172  750  HOH A O   
4853 O O   . HOH G .   ? 0.3073 0.3567 0.3136 -0.0446 0.0173  0.0515  751  HOH A O   
4854 O O   . HOH G .   ? 0.1474 0.5064 0.4018 -0.0078 -0.0136 0.0906  752  HOH A O   
4855 O O   . HOH G .   ? 0.1965 0.3161 0.2800 -0.0688 -0.0145 0.0359  753  HOH A O   
4856 O O   . HOH G .   ? 0.5661 0.5367 0.5567 0.0372  -0.0008 0.0194  754  HOH A O   
4857 O O   . HOH G .   ? 0.2591 0.2467 0.2408 0.0119  0.0307  -0.0029 755  HOH A O   
4858 O O   . HOH G .   ? 0.1797 0.2280 0.1826 -0.0061 -0.0118 0.0110  756  HOH A O   
4859 O O   . HOH G .   ? 0.1689 0.2144 0.1504 -0.0156 -0.0092 0.0127  757  HOH A O   
4860 O O   . HOH G .   ? 0.4112 0.4968 0.4809 0.0753  0.0348  0.0542  758  HOH A O   
4861 O O   . HOH G .   ? 0.5597 0.6023 0.5943 0.0663  0.0612  0.0260  759  HOH A O   
4862 O O   . HOH G .   ? 0.2034 0.1738 0.1751 -0.0037 -0.0085 0.0463  760  HOH A O   
4863 O O   . HOH G .   ? 0.5289 0.6054 0.5150 -0.0125 -0.0288 0.0093  761  HOH A O   
4864 O O   . HOH G .   ? 0.3914 0.4497 0.3699 -0.0039 -0.0283 0.0204  762  HOH A O   
4865 O O   . HOH G .   ? 0.2895 0.3706 0.2208 0.0142  -0.0450 0.0636  763  HOH A O   
4866 O O   . HOH G .   ? 0.5002 0.5328 0.4182 -0.0132 0.0044  0.0624  764  HOH A O   
4867 O O   . HOH G .   ? 0.3589 0.6486 0.5230 -0.0120 -0.0653 0.0718  765  HOH A O   
4868 O O   . HOH G .   ? 0.4051 0.5623 0.4313 -0.0173 -0.0734 0.0387  766  HOH A O   
4869 O O   . HOH G .   ? 0.5653 0.5690 0.5119 -0.0295 0.0177  0.0785  767  HOH A O   
4870 O O   . HOH G .   ? 0.6406 0.6178 0.6132 -0.0497 0.0197  0.0790  768  HOH A O   
4871 O O   . HOH G .   ? 0.3961 0.5685 0.5177 -0.0794 -0.0281 0.0406  769  HOH A O   
4872 O O   . HOH G .   ? 0.3423 0.4369 0.3977 -0.0572 0.0159  0.0496  770  HOH A O   
4873 O O   . HOH G .   ? 0.2313 0.3295 0.2344 -0.0140 0.0512  0.0397  771  HOH A O   
4874 O O   . HOH G .   ? 0.3171 0.5393 0.4807 0.0814  0.0276  0.0839  772  HOH A O   
4875 O O   . HOH G .   ? 0.4818 0.5180 0.5113 0.0506  0.0319  0.0328  773  HOH A O   
4876 O O   . HOH G .   ? 0.3301 0.3673 0.3286 -0.0104 -0.0127 0.0001  774  HOH A O   
4877 O O   . HOH G .   ? 0.1243 0.1855 0.1382 -0.0163 -0.0022 0.0129  775  HOH A O   
4878 O O   . HOH G .   ? 0.2621 0.3201 0.2523 -0.0106 0.0151  0.0114  776  HOH A O   
4879 O O   . HOH G .   ? 0.2743 0.2875 0.2275 -0.0116 -0.0048 0.0560  777  HOH A O   
4880 O O   . HOH G .   ? 0.2558 0.2820 0.2969 -0.0920 -0.0134 0.0318  778  HOH A O   
4881 O O   . HOH G .   ? 0.1955 0.3120 0.2321 -0.0165 0.0452  0.0422  779  HOH A O   
4882 O O   A HOH G .   ? 0.4266 0.3354 0.3939 -0.0227 -0.0027 0.0356  780  HOH A O   
4883 O O   B HOH G .   ? 0.4198 0.3325 0.3874 -0.0155 -0.0040 0.0295  780  HOH A O   
4884 O O   . HOH G .   ? 0.2629 0.3251 0.3070 -0.0708 -0.0248 0.0201  781  HOH A O   
4885 O O   . HOH G .   ? 0.4394 0.4664 0.4352 0.0228  0.0408  0.0029  782  HOH A O   
4886 O O   . HOH G .   ? 0.2304 0.4080 0.3514 -0.0546 -0.0061 0.0478  783  HOH A O   
4887 O O   . HOH G .   ? 0.5053 0.5514 0.4649 -0.0153 0.0043  0.0040  784  HOH A O   
4888 O O   . HOH G .   ? 0.2442 0.3351 0.2981 -0.0633 -0.0313 0.0194  785  HOH A O   
4889 O O   . HOH G .   ? 0.4423 0.5019 0.4416 0.0109  -0.0174 0.0318  786  HOH A O   
4890 O O   . HOH G .   ? 0.4228 0.4883 0.4114 -0.0397 -0.0496 0.0009  787  HOH A O   
4891 O O   . HOH G .   ? 0.4410 0.4999 0.4313 -0.0268 -0.0377 0.0041  788  HOH A O   
4892 O O   . HOH G .   ? 0.6749 0.7262 0.5800 -0.0185 -0.0046 0.0079  789  HOH A O   
4893 O O   . HOH G .   ? 0.2383 0.2202 0.2154 -0.0457 -0.0274 -0.0094 790  HOH A O   
4894 O O   . HOH G .   ? 0.4261 0.4737 0.4278 0.0161  -0.0083 0.0325  791  HOH A O   
4895 O O   . HOH G .   ? 0.2301 0.3457 0.2611 -0.0484 -0.0589 0.0144  792  HOH A O   
4896 O O   . HOH G .   ? 0.3326 0.3810 0.3028 0.0499  -0.0373 0.0854  793  HOH A O   
4897 O O   . HOH G .   ? 0.3886 0.6184 0.5500 0.0766  0.0083  0.0889  794  HOH A O   
4898 O O   . HOH G .   ? 0.1885 0.2405 0.2032 -0.0285 -0.0085 0.0174  795  HOH A O   
4899 O O   . HOH G .   ? 0.5398 0.6749 0.5433 -0.0251 -0.0736 0.0284  796  HOH A O   
4900 O O   . HOH G .   ? 0.5072 0.5153 0.4823 0.0019  0.0255  -0.0092 797  HOH A O   
4901 O O   . HOH G .   ? 0.2998 0.2831 0.2545 -0.0075 -0.0045 0.0656  798  HOH A O   
4902 O O   . HOH G .   ? 0.3845 0.5600 0.4987 0.0532  0.0682  0.0521  799  HOH A O   
4903 O O   . HOH G .   ? 0.1975 0.2648 0.2382 -0.0629 -0.0278 0.0167  800  HOH A O   
4904 O O   . HOH G .   ? 0.3502 0.4279 0.3566 -0.0513 0.0497  0.0759  801  HOH A O   
4905 O O   . HOH G .   ? 0.4157 0.5308 0.4993 -0.1034 -0.0448 0.0218  802  HOH A O   
4906 O O   . HOH G .   ? 0.2591 0.3177 0.2907 0.0383  0.0089  0.0396  803  HOH A O   
4907 O O   . HOH G .   ? 0.4547 0.4961 0.3950 -0.0215 0.0171  0.0535  804  HOH A O   
4908 O O   . HOH G .   ? 0.3812 0.4429 0.3934 -0.0483 -0.0410 0.0034  805  HOH A O   
4909 O O   . HOH G .   ? 0.4519 0.4827 0.4405 0.0132  0.0355  -0.0001 806  HOH A O   
4910 O O   . HOH G .   ? 0.1947 0.2390 0.2009 -0.0054 -0.0015 0.0068  807  HOH A O   
4911 O O   . HOH G .   ? 0.3968 0.4261 0.4094 0.0372  -0.0100 0.0255  808  HOH A O   
4912 O O   . HOH G .   ? 0.1488 0.2195 0.1770 -0.0333 -0.0230 0.0132  809  HOH A O   
4913 O O   . HOH G .   ? 0.2191 0.2196 0.1790 -0.0087 -0.0072 0.0555  810  HOH A O   
4914 O O   A HOH G .   ? 0.2049 0.5225 0.4296 -0.0068 -0.0043 0.0817  811  HOH A O   
4915 O O   B HOH G .   ? 0.2198 0.5361 0.4435 -0.0202 -0.0102 0.0788  811  HOH A O   
4916 O O   . HOH G .   ? 0.3321 0.3042 0.2983 -0.0330 0.0080  0.0682  812  HOH A O   
4917 O O   . HOH G .   ? 0.3174 0.5482 0.4508 -0.0775 -0.0724 0.0379  813  HOH A O   
4918 O O   . HOH G .   ? 0.2042 0.2420 0.2110 -0.0278 -0.0119 0.0147  814  HOH A O   
4919 O O   A HOH G .   ? 0.2082 0.2210 0.2239 -0.0640 0.0035  0.0464  815  HOH A O   
4920 O O   B HOH G .   ? 0.3597 0.3853 0.3765 -0.0613 0.0088  0.0510  815  HOH A O   
4921 O O   . HOH G .   ? 0.2240 0.2744 0.2312 -0.0149 -0.0082 0.0068  816  HOH A O   
4922 O O   . HOH G .   ? 0.1558 0.2222 0.1926 -0.0487 -0.0040 0.0309  817  HOH A O   
4923 O O   . HOH G .   ? 0.5340 0.5844 0.4763 -0.0150 0.0126  0.0164  818  HOH A O   
4924 O O   . HOH G .   ? 0.3754 0.3764 0.3726 0.0237  -0.0066 0.0139  819  HOH A O   
4925 O O   . HOH G .   ? 0.5907 0.5937 0.6164 -0.0827 -0.0040 0.0397  820  HOH A O   
4926 O O   . HOH G .   ? 0.3012 0.4740 0.4081 -0.0213 0.0252  0.0501  821  HOH A O   
4927 O O   . HOH G .   ? 0.2843 0.3582 0.2920 -0.0061 -0.0231 0.0081  822  HOH A O   
4928 O O   . HOH G .   ? 0.1993 0.2465 0.1736 -0.0138 -0.0127 0.0158  823  HOH A O   
4929 O O   . HOH G .   ? 0.2035 0.4000 0.3316 0.0244  0.0437  0.0556  824  HOH A O   
4930 O O   . HOH G .   ? 0.4316 0.4328 0.4254 0.0201  -0.0024 0.0031  825  HOH A O   
4931 O O   . HOH G .   ? 0.4221 0.3505 0.3969 -0.0352 -0.0029 0.0390  826  HOH A O   
4932 O O   . HOH G .   ? 0.2754 0.3018 0.2458 0.0352  -0.0277 0.0702  827  HOH A O   
4933 O O   . HOH G .   ? 0.2498 0.5679 0.4581 -0.0028 -0.0369 0.0817  828  HOH A O   
4934 O O   . HOH G .   ? 0.1441 0.1894 0.1481 -0.0051 -0.0129 0.0019  829  HOH A O   
4935 O O   . HOH G .   ? 0.4398 0.4295 0.3928 -0.0167 0.0015  0.0677  830  HOH A O   
4936 O O   . HOH G .   ? 0.3706 0.4241 0.4027 -0.0623 0.0119  0.0509  831  HOH A O   
4937 O O   . HOH G .   ? 0.4084 0.4590 0.3397 -0.0113 -0.0118 0.0343  832  HOH A O   
4938 O O   . HOH G .   ? 0.4660 0.4868 0.4559 -0.0612 -0.0425 -0.0087 833  HOH A O   
4939 O O   . HOH G .   ? 0.3028 0.3427 0.2721 0.0249  -0.0295 0.0610  834  HOH A O   
4940 O O   . HOH G .   ? 0.2726 0.5325 0.4549 -0.0091 0.0366  0.0717  835  HOH A O   
4941 O O   . HOH G .   ? 0.1167 0.2578 0.1987 -0.0210 -0.0121 0.0344  836  HOH A O   
4942 O O   . HOH G .   ? 0.3112 0.5558 0.4369 -0.0140 -0.0648 0.0606  837  HOH A O   
4943 O O   . HOH G .   ? 0.1947 0.2508 0.2031 -0.0123 -0.0003 0.0092  838  HOH A O   
4944 O O   . HOH G .   ? 0.2466 0.2419 0.2300 -0.0371 0.0034  0.0511  839  HOH A O   
4945 O O   . HOH G .   ? 0.1429 0.1949 0.1448 -0.0258 0.0017  0.0252  840  HOH A O   
4946 O O   . HOH G .   ? 0.5016 0.4706 0.4831 0.0016  -0.0095 0.0155  841  HOH A O   
4947 O O   . HOH G .   ? 0.3347 0.4650 0.4022 -0.0075 0.0271  0.0366  842  HOH A O   
4948 O O   . HOH G .   ? 0.4250 0.5760 0.4819 -0.0745 -0.0772 0.0148  843  HOH A O   
4949 O O   . HOH G .   ? 0.3239 0.4160 0.3373 -0.0339 0.0413  0.0536  844  HOH A O   
4950 O O   . HOH G .   ? 0.5096 0.4983 0.5014 0.0284  0.0379  0.0068  845  HOH A O   
4951 O O   . HOH G .   ? 0.3892 0.4827 0.3990 -0.0469 -0.0578 0.0075  846  HOH A O   
4952 O O   . HOH G .   ? 0.4640 0.3863 0.4328 -0.0115 -0.0062 0.0168  847  HOH A O   
4953 O O   . HOH G .   ? 0.2862 0.3566 0.3145 0.0360  -0.0177 0.0293  848  HOH A O   
4954 O O   . HOH G .   ? 0.3298 0.3958 0.3150 -0.0110 0.0256  0.0187  849  HOH A O   
4955 O O   . HOH G .   ? 0.6548 0.8998 0.8339 -0.0687 -0.0127 0.0600  850  HOH A O   
4956 O O   . HOH G .   ? 0.2682 0.5584 0.4581 0.0276  -0.0238 0.0853  851  HOH A O   
4957 O O   . HOH G .   ? 0.1801 0.2294 0.1834 -0.0073 0.0047  0.0056  852  HOH A O   
4958 O O   . HOH G .   ? 0.1795 0.2645 0.2302 -0.0522 0.0007  0.0365  853  HOH A O   
4959 O O   . HOH G .   ? 0.2223 0.2654 0.2331 0.0053  0.0038  0.0131  854  HOH A O   
4960 O O   . HOH G .   ? 0.2018 0.1979 0.1983 -0.0439 -0.0029 0.0379  855  HOH A O   
4961 O O   . HOH G .   ? 0.3410 0.5624 0.4946 -0.0667 -0.0284 0.0502  856  HOH A O   
4962 O O   . HOH G .   ? 0.1374 0.2111 0.1802 -0.0532 -0.0209 0.0203  857  HOH A O   
4963 O O   . HOH G .   ? 0.5096 0.6000 0.5156 0.0156  -0.0325 0.0441  858  HOH A O   
4964 O O   . HOH G .   ? 0.2591 0.4340 0.3660 -0.0309 0.0342  0.0558  859  HOH A O   
4965 O O   . HOH G .   ? 0.2914 0.4475 0.3817 -0.0104 0.0296  0.0446  860  HOH A O   
4966 O O   . HOH G .   ? 0.1302 0.2224 0.1746 -0.0242 -0.0041 0.0236  861  HOH A O   
4967 O O   . HOH G .   ? 0.2160 0.2858 0.2146 -0.0204 0.0192  0.0286  862  HOH A O   
4968 O O   . HOH G .   ? 0.3041 0.3429 0.2934 -0.0410 0.0198  0.0575  863  HOH A O   
4969 O O   . HOH G .   ? 0.4400 0.7052 0.6113 0.0465  -0.0199 0.0876  864  HOH A O   
4970 O O   . HOH G .   ? 0.6601 0.5933 0.6246 0.0365  -0.0062 0.0696  865  HOH A O   
4971 O O   . HOH G .   ? 0.4207 0.4780 0.3901 -0.0349 0.0381  0.0649  866  HOH A O   
4972 O O   . HOH G .   ? 0.3267 0.3801 0.3130 -0.0199 -0.0318 0.0052  867  HOH A O   
4973 O O   . HOH G .   ? 0.5597 0.5100 0.5131 -0.0187 0.0047  0.0762  868  HOH A O   
4974 O O   . HOH G .   ? 0.2396 0.3279 0.2588 -0.0029 -0.0243 0.0095  869  HOH A O   
4975 O O   . HOH G .   ? 0.1550 0.3988 0.3026 -0.0144 -0.0400 0.0605  870  HOH A O   
4976 O O   . HOH G .   ? 0.5016 0.4172 0.4679 0.0124  -0.0025 0.0434  871  HOH A O   
4977 O O   . HOH G .   ? 0.1763 0.2137 0.1736 -0.0061 0.0058  0.0013  872  HOH A O   
4978 O O   . HOH G .   ? 0.4299 0.6633 0.5950 -0.0536 -0.0099 0.0582  873  HOH A O   
4979 O O   . HOH G .   ? 0.4607 0.4862 0.4753 -0.0885 -0.0441 -0.0012 874  HOH A O   
4980 O O   . HOH G .   ? 0.3606 0.4326 0.3009 0.0307  -0.0455 0.0811  875  HOH A O   
4981 O O   . HOH G .   ? 0.4375 0.7065 0.6310 -0.0327 0.0170  0.0713  876  HOH A O   
4982 O O   . HOH G .   ? 0.2678 0.4025 0.2511 -0.0024 -0.0583 0.0306  877  HOH A O   
4983 O O   . HOH G .   ? 0.2249 0.2744 0.2441 0.0298  0.0385  0.0143  878  HOH A O   
4984 O O   . HOH G .   ? 0.3991 0.7069 0.6113 0.0357  -0.0075 0.0906  879  HOH A O   
4985 O O   . HOH G .   ? 0.3437 0.4214 0.3933 -0.0616 0.0078  0.0454  880  HOH A O   
4986 O O   . HOH G .   ? 0.1867 0.2990 0.2428 -0.0086 0.0149  0.0296  881  HOH A O   
4987 O O   . HOH G .   ? 0.4422 0.5169 0.3958 -0.0223 -0.0302 0.0023  882  HOH A O   
4988 O O   . HOH G .   ? 0.3904 0.4691 0.3982 0.0513  -0.0367 0.0652  883  HOH A O   
4989 O O   . HOH G .   ? 0.2641 0.4152 0.3023 -0.0143 -0.0445 0.0122  884  HOH A O   
4990 O O   . HOH G .   ? 0.5709 0.6312 0.5983 -0.0737 0.0410  0.0814  885  HOH A O   
4991 O O   . HOH G .   ? 0.1601 0.4312 0.3428 -0.0070 -0.0155 0.0700  886  HOH A O   
4992 O O   . HOH G .   ? 0.4339 0.5261 0.3885 -0.0158 -0.0409 0.0144  887  HOH A O   
4993 O O   . HOH G .   ? 0.4974 0.6212 0.5504 -0.0858 -0.0688 0.0092  888  HOH A O   
4994 O O   . HOH G .   ? 0.3681 0.4039 0.3735 0.0362  0.0533  0.0080  889  HOH A O   
4995 O O   A HOH G .   ? 0.2333 0.2536 0.2148 -0.0237 -0.0231 -0.0061 890  HOH A O   
4996 O O   B HOH G .   ? 0.2108 0.2251 0.1849 -0.0221 -0.0221 -0.0091 890  HOH A O   
4997 O O   . HOH G .   ? 0.2610 0.2897 0.2650 0.0076  0.0118  0.0091  891  HOH A O   
4998 O O   . HOH G .   ? 0.4566 0.5446 0.4491 -0.0416 -0.0602 0.0062  892  HOH A O   
4999 O O   . HOH G .   ? 0.3527 0.3443 0.3289 -0.0596 -0.0374 -0.0138 893  HOH A O   
5000 O O   . HOH G .   ? 0.3506 0.3581 0.3297 -0.0322 -0.0263 -0.0085 894  HOH A O   
5001 O O   . HOH G .   ? 0.2088 0.3752 0.2661 0.0130  -0.0443 0.0299  895  HOH A O   
5002 O O   . HOH G .   ? 0.3800 0.5618 0.4503 -0.0489 -0.0758 0.0305  896  HOH A O   
5003 O O   . HOH G .   ? 0.3235 0.3704 0.2774 -0.0286 0.0286  0.0602  897  HOH A O   
5004 O O   . HOH G .   ? 0.2339 0.4476 0.3877 0.0661  0.0585  0.0679  898  HOH A O   
5005 O O   . HOH G .   ? 0.2373 0.2389 0.2330 -0.0459 0.0028  0.0465  899  HOH A O   
5006 O O   . HOH G .   ? 0.3016 0.3815 0.3041 -0.0087 0.0324  0.0234  900  HOH A O   
5007 O O   . HOH G .   ? 0.4085 0.4693 0.3633 -0.0127 0.0311  0.0229  901  HOH A O   
5008 O O   . HOH G .   ? 0.5027 0.6519 0.5499 0.0306  -0.0442 0.0424  902  HOH A O   
5009 O O   . HOH G .   ? 0.3973 0.4883 0.3419 0.0098  -0.0470 0.0523  903  HOH A O   
5010 O O   . HOH G .   ? 0.5989 0.6582 0.5054 -0.0226 -0.0182 0.0024  904  HOH A O   
5011 O O   . HOH G .   ? 0.3601 0.3665 0.3558 0.0559  -0.0173 0.0618  905  HOH A O   
5012 O O   . HOH G .   ? 0.3214 0.3778 0.3643 -0.0888 -0.0365 0.0133  906  HOH A O   
5013 O O   . HOH G .   ? 0.3865 0.6218 0.5476 0.0379  0.0636  0.0677  907  HOH A O   
5014 O O   . HOH G .   ? 0.3251 0.3955 0.2514 0.0007  -0.0344 0.0477  908  HOH A O   
5015 O O   . HOH G .   ? 0.1749 0.4244 0.3165 -0.0045 -0.0502 0.0653  909  HOH A O   
5016 O O   . HOH G .   ? 0.4537 0.4643 0.4965 -0.1170 -0.0229 0.0245  910  HOH A O   
5017 O O   . HOH G .   ? 0.5797 0.5202 0.5364 0.0233  -0.0070 0.0750  911  HOH A O   
5018 O O   . HOH G .   ? 0.6432 0.7466 0.6770 -0.0459 0.0447  0.0632  912  HOH A O   
5019 O O   . HOH G .   ? 0.5428 0.5682 0.5612 0.0609  -0.0090 0.0422  913  HOH A O   
5020 O O   . HOH G .   ? 0.4601 0.4483 0.4465 -0.0979 -0.0499 -0.0163 914  HOH A O   
5021 O O   . HOH G .   ? 0.2695 0.3850 0.2985 0.0332  -0.0387 0.0437  915  HOH A O   
5022 O O   . HOH G .   ? 0.3085 0.3555 0.2929 0.0030  0.0307  0.0029  916  HOH A O   
5023 O O   . HOH G .   ? 0.3744 0.4275 0.3501 -0.0121 0.0144  0.0102  917  HOH A O   
5024 O O   . HOH G .   ? 0.6179 0.7211 0.6597 -0.0465 0.0359  0.0577  918  HOH A O   
5025 O O   . HOH G .   ? 0.4840 0.5333 0.4170 -0.0157 0.0058  0.0146  919  HOH A O   
5026 O O   . HOH G .   ? 0.2402 0.4312 0.3699 -0.0580 -0.0184 0.0467  920  HOH A O   
5027 O O   . HOH G .   ? 0.2881 0.2225 0.2612 -0.0330 -0.0002 0.0489  921  HOH A O   
5028 O O   . HOH G .   ? 0.2548 0.3562 0.2712 -0.0232 0.0449  0.0457  922  HOH A O   
5029 O O   . HOH G .   ? 0.2627 0.5309 0.4548 0.0393  0.0479  0.0774  923  HOH A O   
5030 O O   . HOH G .   ? 0.4976 0.6108 0.5520 0.0546  0.0836  0.0307  924  HOH A O   
5031 O O   . HOH G .   ? 0.5495 0.5559 0.5759 -0.1098 -0.0357 0.0080  925  HOH A O   
5032 O O   . HOH G .   ? 0.7585 0.8017 0.6721 -0.0198 0.0009  -0.0040 926  HOH A O   
5033 O O   A HOH G .   ? 0.2381 0.4069 0.3516 -0.0674 -0.0260 0.0399  927  HOH A O   
5034 O O   B HOH G .   ? 0.1556 0.3180 0.2661 -0.0643 -0.0185 0.0412  927  HOH A O   
5035 O O   . HOH G .   ? 0.3723 0.6888 0.5827 -0.0273 -0.0401 0.0747  928  HOH A O   
5036 O O   . HOH G .   ? 0.3527 0.5243 0.4871 0.0946  0.0442  0.0747  929  HOH A O   
5037 O O   . HOH G .   ? 0.3021 0.3973 0.3842 -0.1066 -0.0291 0.0300  930  HOH A O   
5038 O O   . HOH G .   ? 0.6514 0.6233 0.6656 -0.0895 -0.0117 0.0284  931  HOH A O   
5039 O O   . HOH G .   ? 0.3930 0.3367 0.3635 0.0253  -0.0070 0.0542  932  HOH A O   
5040 O O   . HOH G .   ? 0.2435 0.5532 0.4623 0.0372  0.0050  0.0904  933  HOH A O   
5041 O O   . HOH G .   ? 0.1917 0.2934 0.2521 0.0436  0.0042  0.0491  934  HOH A O   
5042 O O   . HOH G .   ? 0.4898 0.4590 0.4947 -0.1160 -0.0387 -0.0028 935  HOH A O   
5043 O O   . HOH G .   ? 0.6283 0.6024 0.6375 -0.0761 -0.0060 0.0351  936  HOH A O   
5044 O O   . HOH G .   ? 0.2591 0.3254 0.2893 0.0483  -0.0170 0.0374  937  HOH A O   
5045 O O   . HOH G .   ? 0.6235 0.7049 0.6041 -0.0113 -0.0455 0.0215  938  HOH A O   
5046 O O   . HOH G .   ? 0.4549 0.5939 0.5607 0.0972  0.0892  0.0525  939  HOH A O   
5047 O O   . HOH G .   ? 0.5531 0.5472 0.5589 0.0551  -0.0020 0.0322  940  HOH A O   
5048 O O   . HOH G .   ? 0.2851 0.3744 0.3581 0.0773  0.0505  0.0471  941  HOH A O   
5049 O O   . HOH G .   ? 0.3928 0.6069 0.5307 0.0143  0.0531  0.0606  942  HOH A O   
5050 O O   . HOH G .   ? 0.4376 0.5050 0.4881 0.0631  0.0523  0.0330  943  HOH A O   
5051 O O   . HOH G .   ? 0.5384 0.5823 0.4955 -0.0173 -0.0008 -0.0015 944  HOH A O   
5052 O O   . HOH G .   ? 0.3923 0.4397 0.3979 -0.0114 -0.0098 0.0059  945  HOH A O   
5053 O O   . HOH G .   ? 0.5265 0.5603 0.5143 0.0207  0.0468  0.0008  946  HOH A O   
5054 O O   . HOH G .   ? 0.2652 0.3892 0.2831 0.0247  -0.0463 0.0437  947  HOH A O   
5055 O O   . HOH G .   ? 0.6533 0.6617 0.6798 0.0841  0.0713  0.0293  948  HOH A O   
5056 O O   . HOH G .   ? 0.5715 0.5798 0.5113 0.0006  -0.0107 0.0695  949  HOH A O   
5057 O O   . HOH G .   ? 0.3623 0.4122 0.3602 -0.0543 -0.0467 -0.0034 950  HOH A O   
5058 O O   . HOH G .   ? 0.5905 0.6878 0.5661 -0.0121 -0.0571 0.0266  951  HOH A O   
5059 O O   . HOH G .   ? 0.2555 0.3633 0.3117 0.0308  0.0466  0.0296  952  HOH A O   
5060 O O   . HOH G .   ? 0.3003 0.3619 0.2825 -0.0163 0.0180  0.0224  953  HOH A O   
5061 O O   . HOH G .   ? 0.5792 0.5599 0.5420 0.0446  -0.0182 0.0838  954  HOH A O   
5062 O O   . HOH G .   ? 0.5580 0.7443 0.6458 -0.0811 -0.0810 0.0226  955  HOH A O   
5063 O O   . HOH G .   ? 0.5883 0.6514 0.5600 -0.0139 0.0261  0.0227  956  HOH A O   
5064 O O   . HOH G .   ? 0.3201 0.3880 0.2914 -0.0040 0.0427  0.0176  957  HOH A O   
5065 O O   . HOH G .   ? 0.5409 0.5801 0.5638 0.0527  -0.0091 0.0340  958  HOH A O   
5066 O O   . HOH G .   ? 0.3208 0.3495 0.3249 0.0141  -0.0115 0.0117  959  HOH A O   
5067 O O   . HOH G .   ? 0.2711 0.3210 0.2713 -0.0082 -0.0168 0.0055  960  HOH A O   
5068 O O   . HOH G .   ? 0.1560 0.3314 0.2649 0.0128  0.0374  0.0488  961  HOH A O   
5069 O O   . HOH G .   ? 0.6166 0.6387 0.5997 -0.0316 -0.0286 -0.0063 962  HOH A O   
5070 O O   . HOH G .   ? 0.5371 0.4261 0.5037 -0.0659 -0.0120 0.0074  963  HOH A O   
5071 O O   . HOH G .   ? 0.5895 0.5747 0.5421 0.0312  -0.0179 0.0832  964  HOH A O   
5072 O O   . HOH G .   ? 0.6420 0.7008 0.6254 -0.0065 0.0249  0.0108  965  HOH A O   
5073 O O   . HOH G .   ? 0.5135 0.5664 0.4394 -0.0246 0.0412  0.0655  966  HOH A O   
5074 O O   . HOH G .   ? 0.5193 0.5602 0.5033 0.0249  0.0579  0.0017  967  HOH A O   
5075 O O   . HOH G .   ? 0.3706 0.4780 0.4073 -0.0363 0.0389  0.0527  968  HOH A O   
5076 O O   . HOH G .   ? 0.5590 0.6333 0.4875 -0.0234 -0.0313 0.0037  969  HOH A O   
5077 O O   . HOH G .   ? 0.4389 0.4769 0.4304 -0.0338 -0.0324 -0.0023 970  HOH A O   
5078 O O   . HOH G .   ? 0.5262 0.7541 0.6120 0.0107  -0.0769 0.0711  971  HOH A O   
5079 O O   . HOH G .   ? 0.3992 0.3634 0.3940 -0.0567 -0.0039 0.0371  972  HOH A O   
5080 O O   . HOH G .   ? 0.5075 0.5163 0.5037 0.0737  -0.0200 0.0798  973  HOH A O   
5081 O O   . HOH G .   ? 0.5600 0.5585 0.5948 -0.1048 -0.0125 0.0327  974  HOH A O   
5082 O O   . HOH G .   ? 0.5724 0.6176 0.5452 0.0120  0.0492  0.0013  975  HOH A O   
5083 O O   . HOH G .   ? 0.4449 0.7132 0.6234 -0.0598 -0.0452 0.0567  976  HOH A O   
5084 O O   . HOH G .   ? 0.5739 0.6196 0.4938 -0.0186 0.0209  0.0530  977  HOH A O   
5085 O O   . HOH G .   ? 0.3185 0.4013 0.3159 -0.0086 -0.0299 0.0112  978  HOH A O   
5086 O O   . HOH G .   ? 0.6589 0.6126 0.6223 -0.0377 0.0118  0.0759  979  HOH A O   
5087 O O   . HOH G .   ? 0.5732 0.5570 0.5386 -0.0503 0.0272  0.0886  980  HOH A O   
5088 O O   A HOH G .   ? 0.3433 0.4689 0.3641 -0.0518 -0.0723 0.0135  981  HOH A O   
5089 O O   B HOH G .   ? 0.2671 0.4089 0.2990 -0.0507 -0.0754 0.0183  981  HOH A O   
5090 O O   . HOH G .   ? 0.4069 0.4453 0.4322 0.0437  0.0192  0.0370  982  HOH A O   
5091 O O   . HOH G .   ? 0.4486 0.6428 0.5503 0.0554  -0.0325 0.0844  983  HOH A O   
5092 O O   . HOH G .   ? 0.4724 0.5607 0.5377 -0.0729 0.0042  0.0466  984  HOH A O   
5093 O O   . HOH G .   ? 0.5939 0.8232 0.7448 0.0162  0.0603  0.0653  985  HOH A O   
5094 O O   . HOH G .   ? 0.4710 0.5562 0.4142 -0.0240 -0.0377 0.0037  986  HOH A O   
5095 O O   . HOH G .   ? 0.4076 0.4867 0.4511 -0.0760 -0.0429 0.0112  987  HOH A O   
5096 O O   . HOH G .   ? 0.5764 0.5014 0.5461 0.0297  -0.0032 0.0502  988  HOH A O   
5097 O O   . HOH G .   ? 0.6768 0.6382 0.6291 0.0285  -0.0120 0.0832  989  HOH A O   
5098 O O   . HOH G .   ? 0.2884 0.5767 0.4865 -0.0192 -0.0170 0.0718  990  HOH A O   
5099 O O   . HOH G .   ? 0.3411 0.5940 0.5159 0.0128  0.0499  0.0709  991  HOH A O   
5100 O O   . HOH G .   ? 0.6100 0.6011 0.5612 -0.0402 0.0262  0.0898  992  HOH A O   
5101 O O   . HOH G .   ? 0.3457 0.5472 0.4757 -0.0222 0.0335  0.0589  993  HOH A O   
5102 O O   . HOH G .   ? 0.3884 0.4439 0.3651 -0.0152 0.0125  0.0165  994  HOH A O   
5103 O O   . HOH G .   ? 0.6785 0.7187 0.6816 0.0420  0.0649  0.0076  995  HOH A O   
5104 O O   . HOH G .   ? 0.6372 0.5661 0.6260 -0.0688 -0.0034 0.0359  996  HOH A O   
5105 O O   . HOH G .   ? 0.6409 0.6208 0.6351 0.0668  0.0762  0.0079  997  HOH A O   
5106 O O   . HOH G .   ? 0.3889 0.4805 0.4307 0.0381  -0.0082 0.0510  998  HOH A O   
5107 O O   . HOH G .   ? 0.3968 0.6049 0.5430 -0.0628 -0.0164 0.0513  999  HOH A O   
5108 O O   . HOH G .   ? 0.5734 0.5760 0.5527 -0.0608 0.0353  0.0905  1000 HOH A O   
5109 O O   . HOH G .   ? 0.4985 0.5417 0.5585 -0.1138 -0.0203 0.0312  1001 HOH A O   
5110 O O   . HOH G .   ? 0.2828 0.6209 0.5036 -0.0162 -0.0467 0.0821  1002 HOH A O   
5111 O O   . HOH G .   ? 0.3507 0.5650 0.5096 0.0770  0.0542  0.0728  1003 HOH A O   
5112 O O   . HOH G .   ? 0.5814 0.7418 0.6753 0.0600  -0.0124 0.0754  1004 HOH A O   
5113 O O   . HOH G .   ? 0.4679 0.4129 0.4391 -0.0108 -0.0094 0.0033  1005 HOH A O   
5114 O O   . HOH G .   ? 0.6681 0.6311 0.6109 0.0068  -0.0055 0.0832  1006 HOH A O   
5115 O O   . HOH G .   ? 0.3765 0.4004 0.3831 0.0243  -0.0041 0.0084  1007 HOH A O   
5116 O O   . HOH G .   ? 0.7025 0.7496 0.5970 -0.0174 0.0053  0.0072  1008 HOH A O   
5117 O O   . HOH G .   ? 0.5708 0.6399 0.5437 -0.0044 -0.0375 0.0241  1009 HOH A O   
5118 O O   . HOH G .   ? 0.5282 0.6006 0.5264 -0.0160 -0.0232 0.0017  1010 HOH A O   
5119 O O   . HOH G .   ? 0.7519 0.8251 0.7557 0.0159  -0.0229 0.0395  1011 HOH A O   
5120 O O   . HOH G .   ? 0.3592 0.6749 0.5635 0.0125  -0.0361 0.0863  1012 HOH A O   
5121 O O   . HOH G .   ? 0.5225 0.5445 0.4547 0.0086  -0.0185 0.0731  1013 HOH A O   
5122 O O   . HOH G .   ? 0.4353 0.5194 0.4413 -0.0112 -0.0270 0.0064  1014 HOH A O   
5123 O O   . HOH G .   ? 0.6181 0.7620 0.5963 0.0166  -0.0764 0.0653  1015 HOH A O   
5124 O O   . HOH G .   ? 0.6527 0.6362 0.6466 0.0819  -0.0132 0.0821  1016 HOH A O   
5125 O O   . HOH G .   ? 0.5365 0.4608 0.5028 -0.0115 -0.0072 0.0062  1017 HOH A O   
5126 O O   . HOH G .   ? 0.4959 0.5700 0.4890 -0.0019 0.0390  0.0179  1018 HOH A O   
5127 O O   . HOH G .   ? 0.4634 0.5810 0.5004 0.0476  -0.0377 0.0528  1019 HOH A O   
5128 O O   . HOH G .   ? 0.4742 0.4462 0.4533 0.0081  -0.0054 0.0003  1020 HOH A O   
5129 O O   . HOH G .   ? 0.6235 0.6597 0.6004 0.0106  0.0411  -0.0016 1021 HOH A O   
5130 O O   . HOH G .   ? 0.8098 0.6648 0.7678 -0.0668 -0.0062 0.0123  1022 HOH A O   
5131 O O   . HOH G .   ? 0.6494 0.6353 0.6351 -0.0618 0.0243  0.0800  1023 HOH A O   
5132 O O   . HOH G .   ? 0.6571 0.6288 0.6425 0.0506  0.0637  0.0032  1024 HOH A O   
5133 O O   . HOH G .   ? 0.3171 0.3104 0.3185 -0.0574 0.0046  0.0498  1025 HOH A O   
5134 O O   . HOH G .   ? 0.6020 0.6579 0.5684 -0.0272 -0.0184 -0.0102 1026 HOH A O   
5135 O O   . HOH G .   ? 0.4728 0.7826 0.6947 -0.0543 -0.0226 0.0715  1027 HOH A O   
5136 O O   . HOH G .   ? 0.6492 0.9188 0.7820 -0.0468 -0.0898 0.0524  1028 HOH A O   
5137 O O   . HOH G .   ? 0.6339 0.4847 0.5856 -0.0375 -0.0008 0.0177  1029 HOH A O   
5138 O O   . HOH G .   ? 0.5615 0.5388 0.5548 0.0677  -0.0097 0.0655  1030 HOH A O   
5139 O O   . HOH G .   ? 0.3291 0.3161 0.3060 -0.0398 0.0089  0.0622  1031 HOH A O   
5140 O O   . HOH G .   ? 0.5538 0.4912 0.5275 0.0096  -0.0048 0.0203  1032 HOH A O   
5141 O O   . HOH G .   ? 0.3829 0.5920 0.4781 -0.0470 -0.0756 0.0386  1033 HOH A O   
5142 O O   . HOH G .   ? 0.5685 0.6246 0.4848 -0.0101 -0.0165 0.0365  1034 HOH A O   
5143 O O   . HOH G .   ? 0.4113 0.4953 0.4822 -0.0920 -0.0214 0.0312  1035 HOH A O   
5144 O O   . HOH G .   ? 0.2127 0.3735 0.3054 0.0191  0.0507  0.0449  1036 HOH A O   
5145 O O   . HOH G .   ? 0.5964 0.5345 0.5756 -0.0479 0.0032  0.0527  1037 HOH A O   
5146 O O   . HOH G .   ? 0.6012 0.6146 0.5431 -0.0071 -0.0062 0.0636  1038 HOH A O   
5147 O O   . HOH G .   ? 0.6667 0.7342 0.6307 -0.0276 -0.0254 -0.0073 1039 HOH A O   
5148 O O   . HOH G .   ? 0.3467 0.6842 0.5714 0.0180  -0.0305 0.0928  1040 HOH A O   
5149 O O   . HOH G .   ? 0.4999 0.6006 0.5695 0.0868  0.0921  0.0368  1041 HOH A O   
5150 O O   . HOH G .   ? 0.4414 0.5213 0.4357 -0.0492 0.0594  0.0823  1042 HOH A O   
5151 O O   . HOH G .   ? 0.5311 0.5416 0.5399 0.0622  -0.0113 0.0512  1043 HOH A O   
5152 O O   . HOH G .   ? 0.5065 0.5349 0.5118 0.0667  -0.0216 0.0688  1044 HOH A O   
5153 O O   . HOH G .   ? 0.4760 0.5385 0.5388 -0.0950 -0.0125 0.0367  1045 HOH A O   
5154 O O   . HOH G .   ? 0.5034 0.7234 0.6650 0.0947  0.0188  0.0940  1046 HOH A O   
5155 O O   . HOH G .   ? 0.6648 0.7117 0.5737 -0.0153 0.0127  0.0101  1047 HOH A O   
5156 O O   . HOH G .   ? 0.3645 0.3887 0.3713 0.0246  -0.0082 0.0144  1048 HOH A O   
5157 O O   . HOH G .   ? 0.3990 0.7023 0.5959 -0.0436 -0.0513 0.0667  1049 HOH A O   
5158 O O   . HOH G .   ? 0.3594 0.6232 0.5454 0.0285  0.0539  0.0747  1050 HOH A O   
5159 O O   . HOH G .   ? 0.6396 0.6125 0.6229 -0.0484 0.0084  0.0607  1051 HOH A O   
5160 O O   . HOH G .   ? 0.4495 0.6710 0.5578 -0.0572 -0.0785 0.0384  1052 HOH A O   
5161 O O   . HOH G .   ? 0.5093 0.5761 0.4192 -0.0030 -0.0299 0.0475  1053 HOH A O   
5162 O O   . HOH G .   ? 0.3274 0.4247 0.3887 -0.0773 -0.0379 0.0191  1054 HOH A O   
5163 O O   . HOH G .   ? 0.5709 0.7735 0.7275 0.1001  0.0375  0.0870  1055 HOH A O   
5164 O O   . HOH G .   ? 0.5245 0.5972 0.5130 -0.0307 -0.0479 0.0064  1056 HOH A O   
5165 O O   . HOH G .   ? 0.5886 0.6865 0.6735 0.0905  0.0514  0.0570  1057 HOH A O   
5166 O O   . HOH G .   ? 0.3265 0.5091 0.4395 0.0302  0.0588  0.0518  1058 HOH A O   
5167 O O   . HOH G .   ? 0.4306 0.5212 0.4900 0.0567  0.0120  0.0540  1059 HOH A O   
5168 O O   . HOH G .   ? 0.3530 0.3794 0.3320 -0.0232 -0.0249 -0.0056 1060 HOH A O   
5169 O O   . HOH G .   ? 0.2379 0.3938 0.3222 -0.0042 0.0431  0.0457  1061 HOH A O   
5170 O O   . HOH G .   ? 0.2733 0.3154 0.2762 -0.0090 -0.0054 0.0048  1062 HOH A O   
5171 O O   . HOH G .   ? 0.6057 0.5155 0.5793 -0.0456 -0.0018 0.0373  1063 HOH A O   
5172 O O   . HOH G .   ? 0.4167 0.3521 0.4008 -0.0543 -0.0015 0.0407  1064 HOH A O   
5173 O O   . HOH G .   ? 0.6186 0.6710 0.5749 -0.0135 0.0171  0.0138  1065 HOH A O   
5174 O O   . HOH G .   ? 0.4199 0.4569 0.4567 -0.1038 -0.0401 0.0089  1066 HOH A O   
5175 O O   . HOH G .   ? 0.5302 0.5989 0.5680 0.0470  0.0058  0.0495  1067 HOH A O   
5176 O O   . HOH G .   ? 0.5284 0.5725 0.5095 -0.0300 -0.0364 -0.0022 1068 HOH A O   
5177 O O   . HOH G .   ? 0.3481 0.3993 0.3398 -0.0149 -0.0152 0.0023  1069 HOH A O   
5178 O O   . HOH G .   ? 0.4599 0.5317 0.3697 -0.0235 -0.0296 0.0049  1070 HOH A O   
5179 O O   . HOH G .   ? 0.4967 0.4829 0.4880 0.0264  -0.0014 0.0078  1071 HOH A O   
5180 O O   . HOH G .   ? 0.5711 0.6044 0.5525 -0.0285 -0.0308 -0.0045 1072 HOH A O   
5181 O O   . HOH G .   ? 0.6371 0.7680 0.6988 0.0580  -0.0195 0.0755  1073 HOH A O   
5182 O O   . HOH G .   ? 0.6548 0.5797 0.6152 0.0069  -0.0029 0.0615  1074 HOH A O   
5183 O O   . HOH G .   ? 0.4260 0.5249 0.4423 -0.0143 -0.0289 0.0045  1075 HOH A O   
5184 O O   . HOH G .   ? 0.5142 0.4486 0.4770 0.0230  -0.0058 0.0648  1076 HOH A O   
5185 O O   . HOH G .   ? 0.6244 0.7379 0.6467 -0.0414 0.0641  0.0719  1077 HOH A O   
5186 O O   . HOH G .   ? 0.4225 0.7189 0.6369 0.0546  0.0225  0.0909  1078 HOH A O   
5187 O O   . HOH G .   ? 0.6204 0.5435 0.5752 -0.0084 0.0017  0.0715  1079 HOH A O   
5188 O O   . HOH G .   ? 0.3617 0.6121 0.5435 0.0784  0.0204  0.0906  1080 HOH A O   
5189 O O   . HOH G .   ? 0.6295 0.7911 0.7598 0.1088  0.0355  0.0865  1081 HOH A O   
5190 O O   . HOH G .   ? 0.5263 0.5841 0.5066 0.0643  -0.0405 0.0938  1082 HOH A O   
5191 O O   . HOH G .   ? 0.5456 0.5483 0.5661 -0.0763 0.0023  0.0468  1083 HOH A O   
5192 O O   . HOH G .   ? 0.4065 0.7089 0.5957 -0.0505 -0.0633 0.0631  1084 HOH A O   
5193 O O   . HOH G .   ? 0.6251 0.7162 0.5688 -0.0320 -0.0419 -0.0045 1085 HOH A O   
5194 O O   . HOH G .   ? 0.5120 0.6481 0.6227 0.0945  0.0444  0.0687  1086 HOH A O   
5195 O O   . HOH G .   ? 0.3634 0.6501 0.5728 0.0516  0.0482  0.0848  1087 HOH A O   
5196 O O   . HOH G .   ? 0.4326 0.6220 0.5052 -0.0324 -0.0724 0.0391  1088 HOH A O   
5197 O O   . HOH G .   ? 0.2923 0.3766 0.3536 -0.0874 -0.0345 0.0204  1089 HOH A O   
5198 O O   . HOH G .   ? 0.3661 0.6933 0.6033 0.0058  0.0183  0.0871  1090 HOH A O   
5199 O O   . HOH G .   ? 0.3214 0.5648 0.4886 -0.0165 0.0419  0.0693  1091 HOH A O   
5200 O O   . HOH G .   ? 0.7327 0.6433 0.7002 0.0194  -0.0006 0.0337  1092 HOH A O   
5201 O O   . HOH G .   ? 0.3589 0.5524 0.4969 -0.0644 -0.0032 0.0535  1093 HOH A O   
5202 O O   . HOH G .   ? 0.3037 0.3965 0.3770 -0.1029 -0.0375 0.0227  1094 HOH A O   
5203 O O   . HOH G .   ? 0.6242 0.6812 0.6147 -0.0179 -0.0171 -0.0011 1095 HOH A O   
5204 O O   . HOH G .   ? 0.4704 0.4715 0.4017 -0.0226 0.0154  0.0842  1096 HOH A O   
5205 O O   . HOH G .   ? 0.5582 0.6441 0.6236 -0.1132 -0.0498 0.0127  1097 HOH A O   
5206 O O   . HOH G .   ? 0.3328 0.4627 0.3932 -0.0026 0.0398  0.0374  1098 HOH A O   
5207 O O   . HOH G .   ? 0.4526 0.6878 0.6236 -0.0564 0.0096  0.0644  1099 HOH A O   
5208 O O   . HOH G .   ? 0.3515 0.5458 0.4929 -0.0684 0.0060  0.0580  1100 HOH A O   
5209 O O   . HOH G .   ? 0.4905 0.4856 0.4282 -0.0106 0.0008  0.0762  1101 HOH A O   
5210 O O   . HOH G .   ? 0.7073 0.7600 0.6736 -0.0089 0.0236  0.0086  1102 HOH A O   
5211 O O   . HOH G .   ? 0.4004 0.6535 0.5796 0.0536  0.0736  0.0742  1103 HOH A O   
5212 O O   . HOH G .   ? 0.3904 0.5764 0.5242 -0.0678 0.0156  0.0610  1104 HOH A O   
5213 O O   . HOH G .   ? 0.3711 0.6675 0.5694 0.0466  -0.0163 0.0936  1105 HOH A O   
5214 O O   . HOH G .   ? 0.7534 0.6097 0.6896 -0.0225 -0.0029 -0.0121 1106 HOH A O   
5215 O O   . HOH G .   ? 0.5863 0.4993 0.5506 -0.0253 0.0022  0.0564  1107 HOH A O   
5216 O O   . HOH G .   ? 0.5888 0.6458 0.4756 -0.0227 -0.0151 0.0029  1108 HOH A O   
5217 O O   . HOH G .   ? 0.4523 0.6309 0.5013 -0.0368 -0.0825 0.0334  1109 HOH A O   
5218 O O   . HOH G .   ? 0.5735 0.6587 0.6261 0.0844  -0.0159 0.0595  1110 HOH A O   
5219 O O   . HOH G .   ? 0.3241 0.6521 0.5610 -0.0112 0.0063  0.0842  1111 HOH A O   
5220 O O   . HOH G .   ? 0.3728 0.4449 0.4482 -0.1193 -0.0296 0.0277  1112 HOH A O   
5221 O O   . HOH G .   ? 0.6038 0.6318 0.6198 0.0730  -0.0157 0.0621  1113 HOH A O   
5222 O O   . HOH G .   ? 0.5930 0.6550 0.6419 0.0959  0.0982  0.0298  1114 HOH A O   
5223 O O   . HOH G .   ? 0.4613 0.4990 0.4434 -0.0472 -0.0445 -0.0077 1115 HOH A O   
5224 O O   . HOH G .   ? 0.4166 0.6954 0.6205 0.0681  0.0291  0.0906  1116 HOH A O   
5225 O O   . HOH G .   ? 0.4856 0.6878 0.6125 -0.0095 0.0443  0.0590  1117 HOH A O   
5226 O O   . HOH G .   ? 0.6321 0.5985 0.6328 -0.0729 0.0096  0.0591  1118 HOH A O   
5227 O O   . HOH G .   ? 0.3941 0.4693 0.4609 -0.0877 0.0024  0.0488  1119 HOH A O   
5228 O O   . HOH G .   ? 0.6061 0.6383 0.5564 0.0446  -0.0342 0.0932  1120 HOH A O   
5229 O O   . HOH G .   ? 0.6761 0.7092 0.7306 0.1052  0.0624  0.0556  1121 HOH A O   
5230 O O   . HOH G .   ? 0.5206 0.5327 0.4402 -0.0172 0.0124  0.0816  1122 HOH A O   
5231 O O   . HOH G .   ? 0.7144 0.7391 0.6138 -0.0231 0.0078  -0.0220 1123 HOH A O   
5232 O O   . HOH G .   ? 0.3114 0.3767 0.3693 -0.1128 -0.0422 0.0149  1124 HOH A O   
5233 O O   . HOH G .   ? 0.5526 0.6158 0.6204 0.0996  0.0478  0.0632  1125 HOH A O   
5234 O O   . HOH G .   ? 0.7742 0.7491 0.7098 -0.0049 0.0000  0.0854  1126 HOH A O   
5235 O O   . HOH G .   ? 0.5997 0.6610 0.5626 0.0115  -0.0305 0.0410  1127 HOH A O   
5236 O O   . HOH G .   ? 0.6102 0.6057 0.5391 -0.0143 0.0069  0.0836  1128 HOH A O   
5237 O O   . HOH G .   ? 0.6558 0.6276 0.6445 -0.0787 0.0354  0.0958  1129 HOH A O   
5238 O O   . HOH G .   ? 0.5697 0.6407 0.4615 -0.0317 -0.0326 -0.0066 1130 HOH A O   
5239 O O   . HOH H .   ? 0.4113 0.3724 0.3889 -0.0016 -0.0088 0.0073  701  HOH B O   
5240 O O   . HOH H .   ? 0.3037 0.4184 0.3531 -0.0540 -0.0137 -0.0094 702  HOH B O   
5241 O O   . HOH H .   ? 0.5570 0.5213 0.4447 -0.0638 0.0014  -0.0658 703  HOH B O   
5242 O O   . HOH H .   ? 0.3853 0.3704 0.3328 0.0198  0.0125  0.0552  704  HOH B O   
5243 O O   . HOH H .   ? 0.6666 0.7433 0.7201 -0.1300 -0.0040 -0.0282 705  HOH B O   
5244 O O   . HOH H .   ? 0.5638 0.5852 0.4747 0.0061  0.0428  -0.0013 706  HOH B O   
5245 O O   . HOH H .   ? 0.6998 0.7705 0.6961 0.0239  0.0545  -0.0033 707  HOH B O   
5246 O O   . HOH H .   ? 0.5529 0.6226 0.5888 0.0421  -0.0087 0.0241  708  HOH B O   
5247 O O   . HOH H .   ? 0.6963 0.6675 0.6418 0.0008  0.0380  -0.0247 709  HOH B O   
5248 O O   . HOH H .   ? 0.3287 0.3609 0.3239 -0.0096 -0.0116 -0.0022 710  HOH B O   
5249 O O   . HOH H .   ? 0.2930 0.3149 0.2315 -0.0067 -0.0038 0.0022  711  HOH B O   
5250 O O   . HOH H .   ? 0.6516 0.6693 0.5306 -0.0163 -0.0314 -0.0076 712  HOH B O   
5251 O O   . HOH H .   ? 0.6448 0.5777 0.6200 0.0384  0.0398  0.0384  713  HOH B O   
5252 O O   . HOH H .   ? 0.7251 0.5215 0.6532 -0.0326 0.0708  -0.0016 714  HOH B O   
5253 O O   . HOH H .   ? 0.4527 0.4605 0.4050 -0.0105 0.0201  -0.0189 715  HOH B O   
5254 O O   . HOH H .   ? 0.5537 0.7245 0.6585 -0.0756 0.0013  0.0001  716  HOH B O   
5255 O O   . HOH H .   ? 0.4458 0.4850 0.4042 -0.0325 -0.0115 -0.0201 717  HOH B O   
5256 O O   . HOH H .   ? 0.3879 0.5076 0.4584 0.0457  0.0042  0.0204  718  HOH B O   
5257 O O   . HOH H .   ? 0.3686 0.5072 0.4433 0.0107  0.0178  0.0093  719  HOH B O   
5258 O O   . HOH H .   ? 0.4274 0.4436 0.3267 -0.0078 -0.0127 -0.0007 720  HOH B O   
5259 O O   . HOH H .   ? 0.5096 0.4212 0.4695 0.0178  0.0500  -0.0022 721  HOH B O   
5260 O O   . HOH H .   ? 0.3748 0.4458 0.3918 -0.0251 0.0346  0.0093  722  HOH B O   
5261 O O   . HOH H .   ? 0.3715 0.4330 0.3514 -0.0325 -0.0207 -0.0135 723  HOH B O   
5262 O O   . HOH H .   ? 0.3750 0.3611 0.2544 -0.0097 -0.0074 -0.0260 724  HOH B O   
5263 O O   . HOH H .   ? 0.5262 0.5633 0.4816 -0.0109 0.0456  0.0168  725  HOH B O   
5264 O O   . HOH H .   ? 0.3840 0.4175 0.3808 -0.0140 -0.0140 0.0005  726  HOH B O   
5265 O O   . HOH H .   ? 0.3862 0.5062 0.4480 -0.0305 0.0115  0.0030  727  HOH B O   
5266 O O   A HOH H .   ? 0.2728 0.2749 0.1580 0.0064  0.0289  -0.0131 728  HOH B O   
5267 O O   B HOH H .   ? 0.3668 0.3620 0.2364 0.0074  0.0296  -0.0167 728  HOH B O   
5268 O O   . HOH H .   ? 0.3559 0.3870 0.3445 0.0155  -0.0042 0.0335  729  HOH B O   
5269 O O   . HOH H .   ? 0.3736 0.4224 0.3546 -0.0246 -0.0129 -0.0096 730  HOH B O   
5270 O O   . HOH H .   ? 0.2496 0.2858 0.2448 -0.0123 -0.0076 0.0009  731  HOH B O   
5271 O O   . HOH H .   ? 0.3141 0.3522 0.3117 -0.0136 -0.0078 -0.0006 732  HOH B O   
5272 O O   . HOH H .   ? 0.4322 0.4437 0.3363 0.0005  0.0189  -0.0042 733  HOH B O   
5273 O O   . HOH H .   ? 0.4957 0.5518 0.4981 -0.1122 -0.0221 -0.0450 734  HOH B O   
5274 O O   . HOH H .   ? 0.5155 0.3452 0.3803 -0.0201 0.0012  -0.0621 735  HOH B O   
5275 O O   . HOH H .   ? 0.3109 0.4030 0.3535 -0.0343 0.0226  0.0046  736  HOH B O   
5276 O O   A HOH H .   ? 0.1476 0.1345 0.1163 -0.0214 0.0144  -0.0189 737  HOH B O   
5277 O O   B HOH H .   ? 0.3321 0.3174 0.3046 -0.0157 0.0168  -0.0144 737  HOH B O   
5278 O O   . HOH H .   ? 0.3740 0.4276 0.4132 -0.0974 0.0113  -0.0157 738  HOH B O   
5279 O O   . HOH H .   ? 0.4785 0.4008 0.4629 -0.1349 0.0300  -0.0376 739  HOH B O   
5280 O O   . HOH H .   ? 0.4934 0.4685 0.4290 0.0461  0.0483  -0.0298 740  HOH B O   
5281 O O   . HOH H .   ? 0.5713 0.5259 0.4319 -0.0034 0.0049  -0.0421 741  HOH B O   
5282 O O   . HOH H .   ? 0.6277 0.4666 0.5738 -0.0490 0.0692  0.0271  742  HOH B O   
5283 O O   . HOH H .   ? 0.2645 0.2189 0.2259 -0.0062 0.0310  -0.0165 743  HOH B O   
5284 O O   . HOH H .   ? 0.6596 0.4563 0.5027 0.0004  0.0192  -0.0711 744  HOH B O   
5285 O O   . HOH H .   ? 0.4652 0.6910 0.5761 0.0141  -0.0391 0.0324  745  HOH B O   
5286 O O   . HOH H .   ? 0.5679 0.4896 0.5309 0.0213  0.0046  -0.0017 746  HOH B O   
5287 O O   . HOH H .   ? 0.4632 0.4282 0.4366 0.0529  0.0290  -0.0127 747  HOH B O   
5288 O O   . HOH H .   ? 0.3346 0.2940 0.2579 -0.0546 -0.0399 -0.0363 748  HOH B O   
5289 O O   . HOH H .   ? 0.2708 0.2831 0.2310 -0.0190 0.0352  0.0253  749  HOH B O   
5290 O O   . HOH H .   ? 0.3269 0.3737 0.2917 0.0048  0.0420  -0.0004 750  HOH B O   
5291 O O   . HOH H .   ? 0.7557 0.8131 0.7711 -0.1355 -0.0233 -0.0486 751  HOH B O   
5292 O O   . HOH H .   ? 0.2820 0.2949 0.2186 -0.0108 0.0344  0.0272  752  HOH B O   
5293 O O   . HOH H .   ? 0.1628 0.1981 0.1573 -0.0105 0.0012  -0.0011 753  HOH B O   
5294 O O   . HOH H .   ? 0.2295 0.2767 0.2485 0.0290  0.0050  0.0344  754  HOH B O   
5295 O O   . HOH H .   ? 0.6953 0.5885 0.5311 0.0039  0.0171  -0.0643 755  HOH B O   
5296 O O   . HOH H .   ? 0.3613 0.2310 0.2770 0.0114  0.0119  -0.0337 756  HOH B O   
5297 O O   . HOH H .   ? 0.2133 0.2941 0.2358 0.0003  -0.0183 0.0078  757  HOH B O   
5298 O O   . HOH H .   ? 0.3100 0.3018 0.3034 -0.0486 0.0350  0.0123  758  HOH B O   
5299 O O   . HOH H .   ? 0.2182 0.3211 0.2459 -0.0081 -0.0254 0.0069  759  HOH B O   
5300 O O   . HOH H .   ? 0.2290 0.2127 0.1870 0.0291  0.0233  -0.0210 760  HOH B O   
5301 O O   . HOH H .   ? 0.2788 0.3891 0.3330 -0.0368 0.0031  -0.0009 761  HOH B O   
5302 O O   . HOH H .   ? 0.2047 0.2408 0.2054 -0.0059 -0.0024 0.0059  762  HOH B O   
5303 O O   . HOH H .   ? 0.2766 0.3422 0.2854 0.0293  0.0397  -0.0048 763  HOH B O   
5304 O O   . HOH H .   ? 0.2225 0.2475 0.1799 -0.0088 0.0150  0.0095  764  HOH B O   
5305 O O   . HOH H .   ? 0.3787 0.5167 0.4364 -0.0231 -0.0216 0.0027  765  HOH B O   
5306 O O   . HOH H .   ? 0.4693 0.4720 0.4530 -0.1277 -0.0094 -0.0549 766  HOH B O   
5307 O O   . HOH H .   ? 0.4442 0.4264 0.3349 -0.0464 -0.0462 -0.0376 767  HOH B O   
5308 O O   . HOH H .   ? 0.6016 0.5141 0.5528 0.0314  0.0146  -0.0144 768  HOH B O   
5309 O O   . HOH H .   ? 0.2291 0.3126 0.2609 -0.0380 -0.0046 -0.0066 769  HOH B O   
5310 O O   . HOH H .   ? 0.5989 0.6159 0.5066 -0.0049 -0.0037 0.0045  770  HOH B O   
5311 O O   . HOH H .   ? 0.5479 0.5940 0.5958 -0.1080 0.0272  -0.0062 771  HOH B O   
5312 O O   . HOH H .   ? 0.5186 0.5798 0.5341 -0.1201 -0.0198 -0.0428 772  HOH B O   
5313 O O   . HOH H .   ? 0.5843 0.4702 0.5355 -0.0170 0.0529  0.0335  773  HOH B O   
5314 O O   . HOH H .   ? 0.5841 0.4430 0.5054 -0.0606 0.0420  -0.0480 774  HOH B O   
5315 O O   . HOH H .   ? 0.2886 0.3732 0.3391 -0.0775 0.0078  -0.0090 775  HOH B O   
5316 O O   . HOH H .   ? 0.1301 0.1795 0.1357 -0.0236 -0.0053 -0.0061 776  HOH B O   
5317 O O   . HOH H .   ? 0.4097 0.4345 0.4045 -0.0188 -0.0169 0.0010  777  HOH B O   
5318 O O   . HOH H .   ? 0.2758 0.2614 0.1886 0.0140  0.0250  -0.0275 778  HOH B O   
5319 O O   . HOH H .   ? 0.3770 0.4136 0.3429 -0.0871 -0.0228 -0.0475 779  HOH B O   
5320 O O   . HOH H .   ? 0.3855 0.4074 0.3599 0.0093  -0.0029 0.0312  780  HOH B O   
5321 O O   . HOH H .   ? 0.7026 0.5405 0.6366 0.0053  0.0656  -0.0092 781  HOH B O   
5322 O O   . HOH H .   ? 0.4958 0.5386 0.5300 -0.1203 0.0058  -0.0273 782  HOH B O   
5323 O O   . HOH H .   ? 0.2331 0.2894 0.2185 -0.0500 -0.0189 -0.0241 783  HOH B O   
5324 O O   . HOH H .   ? 0.4399 0.6049 0.5293 0.0162  -0.0096 0.0187  784  HOH B O   
5325 O O   . HOH H .   ? 0.5102 0.4922 0.4492 -0.0161 0.0231  -0.0299 785  HOH B O   
5326 O O   . HOH H .   ? 0.2980 0.3221 0.2619 -0.0061 -0.0013 0.0129  786  HOH B O   
5327 O O   . HOH H .   ? 0.3289 0.2952 0.3039 0.0129  0.0355  -0.0039 787  HOH B O   
5328 O O   . HOH H .   ? 0.4068 0.3820 0.3380 -0.0270 0.0181  -0.0371 788  HOH B O   
5329 O O   . HOH H .   ? 0.4189 0.3920 0.3686 0.0473  0.0414  -0.0257 789  HOH B O   
5330 O O   . HOH H .   ? 0.3647 0.2606 0.2393 -0.0018 0.0073  -0.0540 790  HOH B O   
5331 O O   . HOH H .   ? 0.3125 0.3425 0.2746 0.0326  0.0501  -0.0154 791  HOH B O   
5332 O O   . HOH H .   ? 0.1720 0.2143 0.1695 -0.0085 -0.0027 -0.0035 792  HOH B O   
5333 O O   . HOH H .   ? 0.2367 0.2197 0.1630 0.0186  0.0254  -0.0276 793  HOH B O   
5334 O O   . HOH H .   ? 0.5282 0.5032 0.5333 -0.1359 0.0169  -0.0371 794  HOH B O   
5335 O O   . HOH H .   ? 0.5514 0.5542 0.4077 0.0047  0.0318  -0.0006 795  HOH B O   
5336 O O   . HOH H .   ? 0.2482 0.3746 0.3105 0.0011  0.0279  0.0070  796  HOH B O   
5337 O O   A HOH H .   ? 0.2003 0.2047 0.1849 -0.0217 0.0167  0.0093  797  HOH B O   
5338 O O   B HOH H .   ? 0.2092 0.2161 0.1961 -0.0209 0.0136  0.0063  797  HOH B O   
5339 O O   . HOH H .   ? 0.3319 0.3848 0.3491 0.0419  0.0287  -0.0025 798  HOH B O   
5340 O O   . HOH H .   ? 0.3398 0.3858 0.3602 0.0335  0.0050  0.0063  799  HOH B O   
5341 O O   . HOH H .   ? 0.1532 0.1845 0.1425 -0.0124 -0.0022 0.0021  800  HOH B O   
5342 O O   . HOH H .   ? 0.3997 0.4256 0.3585 -0.0163 0.0077  -0.0136 801  HOH B O   
5343 O O   . HOH H .   ? 0.1926 0.3028 0.2459 0.0091  0.0085  0.0056  802  HOH B O   
5344 O O   . HOH H .   ? 0.1817 0.2020 0.1413 -0.0118 -0.0129 -0.0077 803  HOH B O   
5345 O O   . HOH H .   ? 0.5153 0.5173 0.4792 -0.0059 0.0222  -0.0158 804  HOH B O   
5346 O O   . HOH H .   ? 0.2161 0.3045 0.2502 -0.0283 -0.0043 -0.0036 805  HOH B O   
5347 O O   . HOH H .   ? 0.3305 0.4002 0.3573 -0.0394 0.0342  0.0102  806  HOH B O   
5348 O O   . HOH H .   ? 0.3310 0.3485 0.3451 -0.1053 0.0077  -0.0288 807  HOH B O   
5349 O O   . HOH H .   ? 0.5853 0.6045 0.5326 -0.0058 0.0070  0.0161  808  HOH B O   
5350 O O   . HOH H .   ? 0.2784 0.3015 0.3074 -0.0937 0.0267  -0.0070 809  HOH B O   
5351 O O   . HOH H .   ? 0.1616 0.3012 0.2362 -0.0118 0.0160  0.0072  810  HOH B O   
5352 O O   A HOH H .   ? 0.2675 0.3054 0.2656 -0.0149 -0.0135 0.0009  811  HOH B O   
5353 O O   B HOH H .   ? 0.2646 0.3042 0.2639 -0.0148 -0.0124 0.0015  811  HOH B O   
5354 O O   . HOH H .   ? 0.2237 0.2672 0.2053 0.0185  0.0339  -0.0090 812  HOH B O   
5355 O O   . HOH H .   ? 0.1459 0.1568 0.1420 -0.0402 0.0110  -0.0081 813  HOH B O   
5356 O O   . HOH H .   ? 0.2052 0.2163 0.1513 -0.0135 -0.0152 -0.0130 814  HOH B O   
5357 O O   . HOH H .   ? 0.5170 0.5232 0.5026 0.0207  0.0081  0.0357  815  HOH B O   
5358 O O   . HOH H .   ? 0.1815 0.2433 0.2088 -0.0635 0.0019  -0.0132 816  HOH B O   
5359 O O   . HOH H .   ? 0.3913 0.3866 0.3168 0.0268  0.0409  -0.0256 817  HOH B O   
5360 O O   . HOH H .   ? 0.1993 0.2398 0.1983 -0.0026 -0.0074 0.0125  818  HOH B O   
5361 O O   . HOH H .   ? 0.2187 0.3203 0.2640 -0.0273 0.0001  -0.0011 819  HOH B O   
5362 O O   . HOH H .   ? 0.1607 0.1911 0.1582 -0.0229 0.0065  -0.0001 820  HOH B O   
5363 O O   . HOH H .   ? 0.1453 0.2184 0.1703 -0.0265 0.0003  -0.0034 821  HOH B O   
5364 O O   . HOH H .   ? 0.7065 0.5075 0.6314 -0.0348 0.0676  -0.0140 822  HOH B O   
5365 O O   . HOH H .   ? 0.1745 0.2169 0.1713 -0.0123 0.0004  -0.0021 823  HOH B O   
5366 O O   . HOH H .   ? 0.3399 0.4845 0.4114 -0.0861 -0.0203 -0.0150 824  HOH B O   
5367 O O   . HOH H .   ? 0.2705 0.1979 0.2494 -0.0982 0.0320  -0.0259 825  HOH B O   
5368 O O   . HOH H .   ? 0.7748 0.5973 0.6301 -0.0350 -0.0066 -0.0680 826  HOH B O   
5369 O O   . HOH H .   ? 0.4175 0.3602 0.3550 -0.1001 0.0052  -0.0626 827  HOH B O   
5370 O O   A HOH H .   ? 0.3250 0.2071 0.1994 -0.0699 0.0266  -0.0802 828  HOH B O   
5371 O O   B HOH H .   ? 0.3922 0.2868 0.2678 -0.0822 0.0174  -0.0835 828  HOH B O   
5372 O O   . HOH H .   ? 0.3527 0.2788 0.2194 -0.0665 -0.0478 -0.0598 829  HOH B O   
5373 O O   . HOH H .   ? 0.4433 0.3059 0.2778 -0.0610 -0.0319 -0.0772 830  HOH B O   
5374 O O   . HOH H .   ? 0.3689 0.5008 0.4089 -0.0888 -0.0375 -0.0254 831  HOH B O   
5375 O O   . HOH H .   ? 0.3926 0.2682 0.2624 0.0091  0.0177  -0.0572 832  HOH B O   
5376 O O   . HOH H .   ? 0.5478 0.4590 0.4800 -0.1237 0.0103  -0.0713 833  HOH B O   
5377 O O   . HOH H .   ? 0.3996 0.4196 0.4075 0.0394  0.0096  0.0033  834  HOH B O   
5378 O O   . HOH H .   ? 0.3343 0.3081 0.2951 0.0032  0.0214  0.0367  835  HOH B O   
5379 O O   . HOH H .   ? 0.1786 0.3325 0.2556 -0.0090 -0.0125 0.0091  836  HOH B O   
5380 O O   . HOH H .   ? 0.3500 0.2455 0.2878 -0.0295 -0.0116 -0.0225 837  HOH B O   
5381 O O   . HOH H .   ? 0.1411 0.2068 0.1569 -0.0174 0.0137  0.0008  838  HOH B O   
5382 O O   . HOH H .   ? 0.4156 0.3543 0.2528 -0.0178 -0.0105 -0.0523 839  HOH B O   
5383 O O   . HOH H .   ? 0.4919 0.3801 0.4488 -0.1317 0.0291  -0.0518 840  HOH B O   
5384 O O   . HOH H .   ? 0.4203 0.4751 0.4049 -0.0046 0.0350  0.0037  841  HOH B O   
5385 O O   . HOH H .   ? 0.2955 0.2662 0.2765 -0.0405 0.0366  0.0168  842  HOH B O   
5386 O O   . HOH H .   ? 0.4318 0.4144 0.2938 0.0076  0.0255  -0.0262 843  HOH B O   
5387 O O   . HOH H .   ? 0.1294 0.1632 0.1058 -0.0076 0.0073  -0.0013 844  HOH B O   
5388 O O   . HOH H .   ? 0.6980 0.5278 0.6162 -0.0746 0.0484  -0.0488 845  HOH B O   
5389 O O   . HOH H .   ? 0.4067 0.4171 0.2779 0.0004  0.0104  0.0181  846  HOH B O   
5390 O O   . HOH H .   ? 0.3882 0.4707 0.4332 0.0423  -0.0036 0.0202  847  HOH B O   
5391 O O   . HOH H .   ? 0.5546 0.5753 0.4974 -0.0282 0.0002  -0.0246 848  HOH B O   
5392 O O   . HOH H .   ? 0.2523 0.2637 0.2476 -0.0452 0.0409  0.0191  849  HOH B O   
5393 O O   . HOH H .   ? 0.5336 0.4077 0.4598 -0.0163 0.0510  -0.0344 850  HOH B O   
5394 O O   . HOH H .   ? 0.2813 0.4343 0.3600 0.0185  -0.0147 0.0197  851  HOH B O   
5395 O O   . HOH H .   ? 0.4362 0.4460 0.4548 -0.1296 0.0098  -0.0338 852  HOH B O   
5396 O O   . HOH H .   ? 0.3422 0.4233 0.3902 -0.0609 0.0358  0.0098  853  HOH B O   
5397 O O   . HOH H .   ? 0.5189 0.4196 0.4826 0.0292  0.0486  0.0308  854  HOH B O   
5398 O O   . HOH H .   ? 0.2640 0.2472 0.2458 0.0157  0.0180  0.0286  855  HOH B O   
5399 O O   . HOH H .   ? 0.2494 0.3343 0.2708 -0.0098 0.0363  0.0059  856  HOH B O   
5400 O O   . HOH H .   ? 0.1722 0.2332 0.1793 0.0126  0.0230  -0.0040 857  HOH B O   
5401 O O   . HOH H .   ? 0.3673 0.4406 0.3761 -0.0285 -0.0175 -0.0079 858  HOH B O   
5402 O O   . HOH H .   ? 0.2741 0.2865 0.2299 -0.0093 0.0162  0.0206  859  HOH B O   
5403 O O   . HOH H .   ? 0.4675 0.3733 0.4145 -0.0083 -0.0041 -0.0146 860  HOH B O   
5404 O O   . HOH H .   ? 0.4367 0.4508 0.4186 0.0160  0.0029  0.0345  861  HOH B O   
5405 O O   . HOH H .   ? 0.2328 0.2639 0.2219 -0.0101 -0.0046 0.0046  862  HOH B O   
5406 O O   . HOH H .   ? 0.3807 0.3241 0.3478 0.0021  -0.0048 -0.0034 863  HOH B O   
5407 O O   . HOH H .   ? 0.2879 0.3336 0.3139 -0.0608 0.0205  -0.0015 864  HOH B O   
5408 O O   . HOH H .   ? 0.1725 0.1816 0.1616 -0.0243 -0.0192 -0.0011 865  HOH B O   
5409 O O   . HOH H .   ? 0.2986 0.2247 0.2664 -0.0374 0.0438  0.0185  866  HOH B O   
5410 O O   . HOH H .   ? 0.3826 0.3964 0.2728 0.0001  0.0346  0.0144  867  HOH B O   
5411 O O   . HOH H .   ? 0.5930 0.4576 0.4686 0.0357  0.0382  -0.0555 868  HOH B O   
5412 O O   . HOH H .   ? 0.3591 0.3386 0.2829 0.0288  0.0368  -0.0299 869  HOH B O   
5413 O O   . HOH H .   ? 0.2421 0.1929 0.2111 -0.0919 0.0153  -0.0408 870  HOH B O   
5414 O O   . HOH H .   ? 0.4149 0.4308 0.4405 -0.0880 0.0348  0.0009  871  HOH B O   
5415 O O   . HOH H .   ? 0.4533 0.5557 0.4676 -0.0947 -0.0365 -0.0350 872  HOH B O   
5416 O O   . HOH H .   ? 0.3831 0.4407 0.3514 -0.0443 -0.0227 -0.0233 873  HOH B O   
5417 O O   . HOH H .   ? 0.2101 0.2426 0.2012 -0.0060 -0.0057 0.0093  874  HOH B O   
5418 O O   . HOH H .   ? 0.4398 0.3990 0.4132 -0.0167 -0.0126 -0.0012 875  HOH B O   
5419 O O   . HOH H .   ? 0.1623 0.2288 0.1805 -0.0237 0.0190  0.0031  876  HOH B O   
5420 O O   . HOH H .   ? 0.3496 0.3933 0.3278 -0.0213 -0.0090 -0.0078 877  HOH B O   
5421 O O   . HOH H .   ? 0.3602 0.3794 0.3718 0.0372  0.0188  0.0332  878  HOH B O   
5422 O O   . HOH H .   ? 0.4954 0.4955 0.4845 -0.0376 0.0310  0.0139  879  HOH B O   
5423 O O   . HOH H .   ? 0.6303 0.4349 0.5462 -0.0416 0.0633  -0.0325 880  HOH B O   
5424 O O   . HOH H .   ? 0.5172 0.3525 0.3338 -0.0434 -0.0152 -0.0836 881  HOH B O   
5425 O O   . HOH H .   ? 0.2620 0.3088 0.2906 -0.0716 0.0145  -0.0085 882  HOH B O   
5426 O O   . HOH H .   ? 0.3949 0.3810 0.2227 -0.0072 -0.0047 -0.0216 883  HOH B O   
5427 O O   . HOH H .   ? 0.5495 0.3941 0.4943 -0.0305 0.0626  0.0211  884  HOH B O   
5428 O O   . HOH H .   ? 0.4520 0.4493 0.4360 -0.0289 0.0250  0.0129  885  HOH B O   
5429 O O   . HOH H .   ? 0.1883 0.2722 0.2289 -0.0441 0.0126  -0.0006 886  HOH B O   
5430 O O   . HOH H .   ? 0.4019 0.5565 0.4736 -0.0261 -0.0201 0.0039  887  HOH B O   
5431 O O   . HOH H .   ? 0.4399 0.4316 0.4079 -0.0373 -0.0284 -0.0144 888  HOH B O   
5432 O O   . HOH H .   ? 0.3291 0.3639 0.3372 0.0157  -0.0084 0.0080  889  HOH B O   
5433 O O   . HOH H .   ? 0.2687 0.3600 0.2969 0.0052  0.0337  0.0024  890  HOH B O   
5434 O O   . HOH H .   ? 0.6526 0.6320 0.6289 0.0266  0.0181  0.0435  891  HOH B O   
5435 O O   . HOH H .   ? 0.3717 0.5165 0.4483 -0.0634 -0.0096 -0.0055 892  HOH B O   
5436 O O   . HOH H .   ? 0.6741 0.7020 0.6110 -0.0066 -0.0140 0.0089  893  HOH B O   
5437 O O   . HOH H .   ? 0.3437 0.3570 0.2671 -0.0019 0.0097  0.0259  894  HOH B O   
5438 O O   A HOH H .   ? 0.2495 0.2390 0.2343 0.0183  0.0006  -0.0033 895  HOH B O   
5439 O O   B HOH H .   ? 0.3691 0.3604 0.3569 0.0258  0.0045  -0.0027 895  HOH B O   
5440 O O   . HOH H .   ? 0.6304 0.6293 0.5741 -0.0409 -0.0381 -0.0223 896  HOH B O   
5441 O O   . HOH H .   ? 0.5717 0.4154 0.5037 -0.0995 0.0428  -0.0486 897  HOH B O   
5442 O O   . HOH H .   ? 0.3971 0.5104 0.4518 0.0160  0.0236  0.0055  898  HOH B O   
5443 O O   . HOH H .   ? 0.6362 0.6539 0.5532 -0.0398 -0.0492 -0.0209 899  HOH B O   
5444 O O   . HOH H .   ? 0.6842 0.5311 0.6036 0.0005  0.0072  -0.0263 900  HOH B O   
5445 O O   . HOH H .   ? 0.4090 0.2545 0.3061 0.0180  0.0201  -0.0432 901  HOH B O   
5446 O O   . HOH H .   ? 0.6239 0.4506 0.5057 -0.0406 -0.0094 -0.0544 902  HOH B O   
5447 O O   . HOH H .   ? 0.3077 0.4347 0.3679 -0.0324 -0.0081 -0.0006 903  HOH B O   
5448 O O   . HOH H .   ? 0.3304 0.2568 0.2754 -0.0944 0.0154  -0.0543 904  HOH B O   
5449 O O   . HOH H .   ? 0.5873 0.6978 0.6585 -0.1167 -0.0052 -0.0197 905  HOH B O   
5450 O O   . HOH H .   ? 0.6409 0.6998 0.6367 -0.0194 0.0427  0.0131  906  HOH B O   
5451 O O   . HOH H .   ? 0.2199 0.2444 0.2190 0.0013  0.0077  0.0065  907  HOH B O   
5452 O O   . HOH H .   ? 0.6826 0.7149 0.5891 -0.0123 -0.0318 0.0045  908  HOH B O   
5453 O O   . HOH H .   ? 0.4037 0.2869 0.3666 -0.0637 0.0636  0.0252  909  HOH B O   
5454 O O   . HOH H .   ? 0.6536 0.4856 0.5729 -0.0076 0.0650  -0.0294 910  HOH B O   
5455 O O   . HOH H .   ? 0.1736 0.2350 0.1743 0.0135  0.0316  -0.0041 911  HOH B O   
5456 O O   . HOH H .   ? 0.4541 0.4926 0.4511 -0.0134 -0.0113 0.0004  912  HOH B O   
5457 O O   . HOH H .   ? 0.5823 0.4959 0.5438 -0.0359 0.0503  0.0281  913  HOH B O   
5458 O O   . HOH H .   ? 0.5857 0.5764 0.4997 -0.0946 -0.0181 -0.0689 914  HOH B O   
5459 O O   . HOH H .   ? 0.3562 0.4181 0.3607 -0.0089 -0.0187 0.0044  915  HOH B O   
5460 O O   . HOH H .   ? 0.2582 0.2769 0.2241 0.0042  -0.0015 0.0280  916  HOH B O   
5461 O O   . HOH H .   ? 0.4770 0.3023 0.4121 -0.0015 0.0666  0.0018  917  HOH B O   
5462 O O   . HOH H .   ? 0.3272 0.4414 0.3545 -0.0718 -0.0318 -0.0221 918  HOH B O   
5463 O O   . HOH H .   ? 0.2927 0.3743 0.3181 -0.0203 0.0302  0.0064  919  HOH B O   
5464 O O   . HOH H .   ? 0.2611 0.3248 0.2439 -0.0438 -0.0223 -0.0204 920  HOH B O   
5465 O O   . HOH H .   ? 0.3787 0.3520 0.2369 -0.0334 -0.0354 -0.0404 921  HOH B O   
5466 O O   . HOH H .   ? 0.3325 0.3526 0.3048 -0.0076 -0.0069 -0.0088 922  HOH B O   
5467 O O   . HOH H .   ? 0.7514 0.5882 0.6216 -0.0492 -0.0165 -0.0624 923  HOH B O   
5468 O O   . HOH H .   ? 0.3809 0.4806 0.4034 -0.0188 -0.0253 0.0007  924  HOH B O   
5469 O O   . HOH H .   ? 0.8345 0.7371 0.7859 0.0170  0.0448  0.0495  925  HOH B O   
5470 O O   . HOH H .   ? 0.4381 0.3644 0.3800 0.0446  0.0300  -0.0260 926  HOH B O   
5471 O O   . HOH H .   ? 0.3108 0.4388 0.3839 -0.0485 0.0157  0.0036  927  HOH B O   
5472 O O   . HOH H .   ? 0.4890 0.4644 0.3556 -0.0053 0.0011  -0.0315 928  HOH B O   
5473 O O   . HOH H .   ? 0.3449 0.3411 0.2747 -0.0339 -0.0344 -0.0242 929  HOH B O   
5474 O O   . HOH H .   ? 0.5326 0.7363 0.6535 0.0356  -0.0072 0.0304  930  HOH B O   
5475 O O   . HOH H .   ? 0.3525 0.3832 0.3579 0.0088  0.0071  0.0143  931  HOH B O   
5476 O O   . HOH H .   ? 0.5446 0.5281 0.4842 -0.0921 -0.0087 -0.0599 932  HOH B O   
5477 O O   . HOH H .   ? 0.5439 0.5337 0.4466 -0.0416 0.0046  -0.0472 933  HOH B O   
5478 O O   . HOH H .   ? 0.3805 0.2020 0.3240 -0.1053 0.0579  -0.0276 934  HOH B O   
5479 O O   . HOH H .   ? 0.2894 0.2715 0.2574 -0.0476 -0.0315 -0.0156 935  HOH B O   
5480 O O   . HOH H .   ? 0.2688 0.3140 0.2738 0.0427  0.0368  -0.0072 936  HOH B O   
5481 O O   . HOH H .   ? 0.4707 0.5489 0.5168 -0.0646 0.0170  -0.0018 937  HOH B O   
5482 O O   . HOH H .   ? 0.3414 0.3799 0.3406 -0.0118 -0.0056 0.0013  938  HOH B O   
5483 O O   . HOH H .   ? 0.4728 0.4981 0.4241 -0.0054 -0.0047 0.0120  939  HOH B O   
5484 O O   . HOH H .   ? 0.4288 0.5747 0.5136 -0.0555 0.0065  0.0016  940  HOH B O   
5485 O O   . HOH H .   ? 0.3765 0.2658 0.3359 0.0224  0.0523  0.0195  941  HOH B O   
5486 O O   . HOH H .   ? 0.2889 0.2251 0.2493 -0.0013 0.0372  -0.0123 942  HOH B O   
5487 O O   . HOH H .   ? 0.3553 0.2961 0.3468 -0.1134 0.0317  -0.0251 943  HOH B O   
5488 O O   . HOH H .   ? 0.3501 0.2165 0.2744 -0.0227 -0.0052 -0.0275 944  HOH B O   
5489 O O   . HOH H .   ? 0.4018 0.2844 0.2880 -0.0533 -0.0265 -0.0552 945  HOH B O   
5490 O O   . HOH H .   ? 0.6435 0.6574 0.4986 -0.0096 -0.0226 -0.0011 946  HOH B O   
5491 O O   . HOH H .   ? 0.3590 0.5046 0.4253 -0.0914 -0.0277 -0.0189 947  HOH B O   
5492 O O   . HOH H .   ? 0.5240 0.7073 0.6015 0.0155  -0.0399 0.0300  948  HOH B O   
5493 O O   . HOH H .   ? 0.3915 0.4319 0.3696 -0.0210 0.0438  0.0187  949  HOH B O   
5494 O O   . HOH H .   ? 0.2858 0.3089 0.2371 -0.0143 0.0390  0.0225  950  HOH B O   
5495 O O   . HOH H .   ? 0.3803 0.4457 0.4150 -0.0612 0.0113  -0.0060 951  HOH B O   
5496 O O   . HOH H .   ? 0.4554 0.5383 0.4607 -0.0286 -0.0241 -0.0068 952  HOH B O   
5497 O O   . HOH H .   ? 0.3647 0.4240 0.3630 -0.0188 -0.0163 -0.0031 953  HOH B O   
5498 O O   . HOH H .   ? 0.4296 0.2981 0.3242 -0.0505 -0.0211 -0.0507 954  HOH B O   
5499 O O   . HOH H .   ? 0.5639 0.6012 0.5140 -0.0124 -0.0261 0.0047  955  HOH B O   
5500 O O   . HOH H .   ? 0.5530 0.5526 0.4454 -0.0526 -0.0570 -0.0342 956  HOH B O   
5501 O O   . HOH H .   ? 0.6225 0.7250 0.6262 -0.0462 -0.0347 -0.0145 957  HOH B O   
5502 O O   . HOH H .   ? 0.5725 0.3726 0.4387 0.0242  0.0313  -0.0581 958  HOH B O   
5503 O O   . HOH H .   ? 0.6936 0.4994 0.5870 -0.0391 -0.0042 -0.0436 959  HOH B O   
5504 O O   . HOH H .   ? 0.4459 0.6192 0.5389 0.0011  -0.0104 0.0147  960  HOH B O   
5505 O O   . HOH H .   ? 0.4817 0.5326 0.4784 -0.0124 -0.0160 0.0034  961  HOH B O   
5506 O O   . HOH H .   ? 0.2421 0.1925 0.2151 -0.0340 0.0375  0.0180  962  HOH B O   
5507 O O   . HOH H .   ? 0.4753 0.5049 0.4422 0.0022  -0.0087 0.0243  963  HOH B O   
5508 O O   . HOH H .   ? 0.4076 0.5775 0.4903 0.0449  -0.0313 0.0425  964  HOH B O   
5509 O O   . HOH H .   ? 0.4915 0.5384 0.5328 -0.1110 0.0139  -0.0177 965  HOH B O   
5510 O O   . HOH H .   ? 0.6424 0.5151 0.5774 -0.0099 -0.0008 -0.0178 966  HOH B O   
5511 O O   . HOH H .   ? 0.4352 0.4314 0.3522 -0.0717 -0.0119 -0.0573 967  HOH B O   
5512 O O   . HOH H .   ? 0.4867 0.5067 0.4488 -0.0378 -0.0383 -0.0133 968  HOH B O   
5513 O O   . HOH H .   ? 0.3201 0.3286 0.2989 -0.0237 -0.0214 -0.0080 969  HOH B O   
5514 O O   . HOH H .   ? 0.3038 0.3917 0.3385 0.0232  0.0267  0.0013  970  HOH B O   
5515 O O   . HOH H .   ? 0.3688 0.3221 0.3347 -0.0022 0.0291  0.0292  971  HOH B O   
5516 O O   . HOH H .   ? 0.5073 0.5387 0.5052 0.0560  0.0464  -0.0101 972  HOH B O   
5517 O O   . HOH H .   ? 0.5778 0.6429 0.5442 -0.0246 -0.0481 0.0066  973  HOH B O   
5518 O O   . HOH H .   ? 0.4190 0.2772 0.3764 -0.0678 0.0657  0.0181  974  HOH B O   
5519 O O   . HOH H .   ? 0.3227 0.3449 0.2690 -0.0064 0.0073  0.0091  975  HOH B O   
5520 O O   . HOH H .   ? 0.4830 0.4702 0.4293 -0.0431 -0.0357 -0.0237 976  HOH B O   
5521 O O   . HOH H .   ? 0.5657 0.4911 0.4038 -0.0322 -0.0229 -0.0592 977  HOH B O   
5522 O O   . HOH H .   ? 0.6406 0.6309 0.6497 -0.0775 0.0473  0.0136  978  HOH B O   
5523 O O   . HOH H .   ? 0.6975 0.6176 0.6163 0.0548  0.0478  -0.0380 979  HOH B O   
5524 O O   . HOH H .   ? 0.5910 0.7116 0.6028 -0.0663 -0.0423 -0.0219 980  HOH B O   
5525 O O   . HOH H .   ? 0.4213 0.4330 0.3766 0.0075  0.0014  0.0358  981  HOH B O   
5526 O O   . HOH H .   ? 0.5621 0.4683 0.3821 -0.0271 -0.0146 -0.0668 982  HOH B O   
5527 O O   . HOH H .   ? 0.3059 0.3528 0.2841 0.0246  0.0455  -0.0094 983  HOH B O   
5528 O O   . HOH H .   ? 0.6131 0.6138 0.5378 -0.0280 0.0096  -0.0336 984  HOH B O   
5529 O O   . HOH H .   ? 0.4760 0.5850 0.5327 -0.0387 0.0164  0.0031  985  HOH B O   
5530 O O   . HOH H .   ? 0.5774 0.5889 0.5344 0.0149  0.0001  0.0437  986  HOH B O   
5531 O O   . HOH H .   ? 0.4992 0.5593 0.4989 -0.0144 -0.0178 0.0009  987  HOH B O   
5532 O O   . HOH H .   ? 0.4555 0.4248 0.4387 0.0248  0.0387  0.0048  988  HOH B O   
5533 O O   . HOH H .   ? 0.3216 0.4276 0.3624 -0.0398 -0.0140 -0.0067 989  HOH B O   
5534 O O   . HOH H .   ? 0.5810 0.6010 0.5222 -0.0224 0.0057  -0.0216 990  HOH B O   
5535 O O   . HOH H .   ? 0.7744 0.6559 0.7172 0.0027  0.0537  0.0517  991  HOH B O   
5536 O O   . HOH H .   ? 0.5634 0.5734 0.4527 -0.0377 -0.0492 -0.0250 992  HOH B O   
5537 O O   . HOH H .   ? 0.5997 0.6239 0.5177 0.0301  0.0699  -0.0153 993  HOH B O   
5538 O O   . HOH H .   ? 0.4082 0.5052 0.4503 -0.0274 0.0299  0.0072  994  HOH B O   
5539 O O   . HOH H .   ? 0.7338 0.5679 0.6365 -0.0419 0.0534  -0.0532 995  HOH B O   
5540 O O   . HOH H .   ? 0.3835 0.2999 0.3587 -0.0675 0.0575  0.0215  996  HOH B O   
5541 O O   . HOH H .   ? 0.4009 0.4246 0.3487 -0.0065 -0.0009 0.0070  997  HOH B O   
5542 O O   . HOH H .   ? 0.6188 0.4406 0.5566 -0.0275 0.0664  0.0121  998  HOH B O   
5543 O O   A HOH H .   ? 0.2871 0.3345 0.3231 -0.0834 0.0202  -0.0066 999  HOH B O   
5544 O O   B HOH H .   ? 0.2892 0.3533 0.3331 -0.0855 0.0144  -0.0091 999  HOH B O   
5545 O O   . HOH H .   ? 0.3964 0.3433 0.3495 -0.0016 0.0373  -0.0210 1000 HOH B O   
5546 O O   . HOH H .   ? 0.7428 0.6669 0.6267 0.0391  0.0465  -0.0483 1001 HOH B O   
5547 O O   . HOH H .   ? 0.5648 0.5483 0.5555 0.0472  0.0167  -0.0015 1002 HOH B O   
5548 O O   . HOH H .   ? 0.5582 0.6029 0.5192 -0.0277 -0.0122 -0.0143 1003 HOH B O   
5549 O O   . HOH H .   ? 0.4676 0.4888 0.3945 -0.0051 -0.0036 0.0082  1004 HOH B O   
5550 O O   . HOH H .   ? 0.5123 0.5128 0.4762 -0.0457 -0.0368 -0.0170 1005 HOH B O   
5551 O O   . HOH H .   ? 0.3635 0.3244 0.3282 -0.0147 0.0315  0.0285  1006 HOH B O   
5552 O O   . HOH H .   ? 0.5704 0.6144 0.5628 0.0223  -0.0097 0.0418  1007 HOH B O   
5553 O O   . HOH H .   ? 0.4186 0.3729 0.3791 -0.0051 0.0308  0.0344  1008 HOH B O   
5554 O O   . HOH H .   ? 0.4851 0.5040 0.4585 -0.0402 -0.0364 -0.0111 1009 HOH B O   
5555 O O   . HOH H .   ? 0.6701 0.7252 0.6355 -0.0360 -0.0202 -0.0182 1010 HOH B O   
5556 O O   . HOH H .   ? 0.5567 0.6887 0.6445 -0.0908 0.0114  -0.0028 1011 HOH B O   
5557 O O   . HOH H .   ? 0.4517 0.4314 0.3059 -0.0126 -0.0113 -0.0303 1012 HOH B O   
5558 O O   . HOH H .   ? 0.4500 0.5430 0.4837 0.0214  0.0352  0.0014  1013 HOH B O   
5559 O O   . HOH H .   ? 0.6461 0.4978 0.5638 0.0190  0.0164  -0.0290 1014 HOH B O   
5560 O O   A HOH H .   ? 0.3688 0.3701 0.3947 -0.0998 0.0449  0.0059  1015 HOH B O   
5561 O O   B HOH H .   ? 0.3974 0.3721 0.4114 -0.0998 0.0508  0.0089  1015 HOH B O   
5562 O O   . HOH H .   ? 0.6215 0.6776 0.6529 0.0437  0.0040  0.0136  1016 HOH B O   
5563 O O   . HOH H .   ? 0.4694 0.5984 0.5109 -0.0422 -0.0291 -0.0066 1017 HOH B O   
5564 O O   . HOH H .   ? 0.5252 0.6630 0.5863 -0.0484 -0.0190 -0.0055 1018 HOH B O   
5565 O O   . HOH H .   ? 0.5245 0.6708 0.5788 -0.0533 -0.0313 -0.0083 1019 HOH B O   
5566 O O   . HOH H .   ? 0.6045 0.6337 0.5081 0.0003  0.0663  0.0200  1020 HOH B O   
5567 O O   . HOH H .   ? 0.5081 0.5192 0.3874 0.0029  0.0353  0.0067  1021 HOH B O   
5568 O O   . HOH H .   ? 0.5894 0.5607 0.4797 0.0146  0.0272  -0.0340 1022 HOH B O   
5569 O O   . HOH H .   ? 0.4314 0.4193 0.4199 0.0122  -0.0077 0.0090  1023 HOH B O   
5570 O O   . HOH H .   ? 0.5721 0.5969 0.5839 0.0364  0.0020  0.0095  1024 HOH B O   
5571 O O   . HOH H .   ? 0.5252 0.5274 0.5019 0.0594  0.0492  -0.0171 1025 HOH B O   
5572 O O   A HOH H .   ? 0.4260 0.2433 0.3042 0.0087  0.0188  -0.0525 1026 HOH B O   
5573 O O   B HOH H .   ? 0.4190 0.2352 0.2956 -0.0050 0.0111  -0.0539 1026 HOH B O   
5574 O O   A HOH H .   ? 0.3850 0.2872 0.2629 0.0359  0.0413  -0.0525 1027 HOH B O   
5575 O O   B HOH H .   ? 0.5022 0.3882 0.3768 0.0344  0.0390  -0.0549 1027 HOH B O   
5576 O O   . HOH H .   ? 0.6686 0.6837 0.6065 0.0328  0.0541  -0.0204 1028 HOH B O   
5577 O O   . HOH H .   ? 0.6419 0.6744 0.6582 0.0437  0.0121  0.0445  1029 HOH B O   
5578 O O   . HOH H .   ? 0.3771 0.3690 0.3707 -0.0524 0.0424  0.0183  1030 HOH B O   
5579 O O   . HOH H .   ? 0.4001 0.3906 0.2475 -0.0124 -0.0147 -0.0225 1031 HOH B O   
5580 O O   . HOH H .   ? 0.3439 0.2933 0.3095 -0.0250 0.0388  0.0277  1032 HOH B O   
5581 O O   . HOH H .   ? 0.6802 0.7071 0.6398 -0.0026 -0.0068 0.0182  1033 HOH B O   
5582 O O   . HOH H .   ? 0.6660 0.5652 0.5835 -0.0832 0.0213  -0.0640 1034 HOH B O   
5583 O O   . HOH H .   ? 0.5871 0.4180 0.4888 0.0345  0.0295  -0.0383 1035 HOH B O   
5584 O O   . HOH H .   ? 0.6715 0.5375 0.6237 0.0248  0.0605  0.0155  1036 HOH B O   
5585 O O   . HOH H .   ? 0.4196 0.3581 0.3836 -0.0095 -0.0083 -0.0055 1037 HOH B O   
5586 O O   . HOH H .   ? 0.5298 0.6010 0.5504 0.0404  0.0418  -0.0030 1038 HOH B O   
5587 O O   . HOH H .   ? 0.3814 0.5221 0.4581 -0.0227 0.0193  0.0073  1039 HOH B O   
5588 O O   . HOH H .   ? 0.5725 0.6531 0.5622 -0.0326 -0.0281 -0.0098 1040 HOH B O   
5589 O O   . HOH H .   ? 0.4268 0.5681 0.5015 -0.0510 -0.0054 -0.0021 1041 HOH B O   
5590 O O   . HOH H .   ? 0.6752 0.7490 0.6677 0.0324  0.0679  -0.0038 1042 HOH B O   
5591 O O   . HOH H .   ? 0.4794 0.5280 0.4518 -0.0303 -0.0147 -0.0149 1043 HOH B O   
5592 O O   . HOH H .   ? 0.6109 0.5664 0.5080 0.0269  0.0363  -0.0391 1044 HOH B O   
5593 O O   . HOH H .   ? 0.6375 0.6154 0.6042 0.0272  0.0167  0.0511  1045 HOH B O   
5594 O O   . HOH H .   ? 0.2766 0.3574 0.2940 0.0149  0.0376  -0.0005 1046 HOH B O   
5595 O O   . HOH H .   ? 0.5099 0.5542 0.4868 -0.0399 -0.0446 -0.0058 1047 HOH B O   
5596 O O   . HOH H .   ? 0.5521 0.6157 0.5502 0.0274  0.0473  -0.0057 1048 HOH B O   
5597 O O   . HOH H .   ? 0.1636 0.2009 0.1677 -0.0014 0.0015  0.0079  1049 HOH B O   
5598 O O   . HOH H .   ? 0.6662 0.6938 0.6820 0.0500  0.0154  0.0054  1050 HOH B O   
5599 O O   . HOH H .   ? 0.4117 0.4979 0.4483 0.0356  0.0324  0.0016  1051 HOH B O   
5600 O O   . HOH H .   ? 0.6132 0.5035 0.5345 -0.0937 0.0227  -0.0645 1052 HOH B O   
5601 O O   . HOH H .   ? 0.5068 0.4551 0.4802 0.0075  -0.0046 0.0047  1053 HOH B O   
5602 O O   . HOH H .   ? 0.5487 0.4842 0.5165 -0.0413 0.0489  0.0282  1054 HOH B O   
5603 O O   . HOH H .   ? 0.3325 0.4350 0.3759 -0.0438 -0.0085 -0.0068 1055 HOH B O   
5604 O O   . HOH H .   ? 0.3115 0.4645 0.3880 -0.0306 -0.0122 0.0029  1056 HOH B O   
5605 O O   . HOH H .   ? 0.5704 0.5856 0.4686 -0.0461 -0.0569 -0.0261 1057 HOH B O   
5606 O O   . HOH H .   ? 0.6763 0.5203 0.6189 -0.0406 0.0715  0.0413  1058 HOH B O   
5607 O O   . HOH H .   ? 0.7219 0.7598 0.6527 -0.0432 -0.0574 -0.0144 1059 HOH B O   
5608 O O   . HOH H .   ? 0.5462 0.5686 0.5167 0.0160  -0.0042 0.0400  1060 HOH B O   
5609 O O   . HOH H .   ? 0.4473 0.4535 0.3773 -0.0818 -0.0174 -0.0574 1061 HOH B O   
5610 O O   . HOH H .   ? 0.7211 0.7364 0.6035 -0.0005 -0.0007 0.0192  1062 HOH B O   
5611 O O   . HOH H .   ? 0.6522 0.6391 0.6082 0.0583  0.0545  -0.0243 1063 HOH B O   
5612 O O   . HOH H .   ? 0.5993 0.4555 0.5121 -0.0527 0.0439  -0.0519 1064 HOH B O   
5613 O O   . HOH H .   ? 0.6630 0.5357 0.4957 0.0119  0.0257  -0.0688 1065 HOH B O   
5614 O O   . HOH H .   ? 0.4324 0.3538 0.3890 0.0087  0.0457  -0.0111 1066 HOH B O   
5615 O O   . HOH H .   ? 0.5042 0.5375 0.4844 -0.1122 -0.0215 -0.0528 1067 HOH B O   
5616 O O   . HOH H .   ? 0.5217 0.5895 0.5522 -0.0484 0.0403  0.0135  1068 HOH B O   
5617 O O   . HOH H .   ? 0.5603 0.5352 0.5457 0.0367  0.0092  -0.0006 1069 HOH B O   
5618 O O   . HOH H .   ? 0.4949 0.6000 0.5332 0.0005  0.0402  0.0059  1070 HOH B O   
5619 O O   . HOH H .   ? 0.5662 0.7232 0.6318 -0.0818 -0.0341 -0.0162 1071 HOH B O   
5620 O O   . HOH H .   ? 0.4622 0.4124 0.4240 0.0111  0.0421  -0.0131 1072 HOH B O   
5621 O O   . HOH H .   ? 0.4956 0.4890 0.4981 -0.0656 0.0477  0.0183  1073 HOH B O   
5622 O O   . HOH H .   ? 0.4993 0.5785 0.5379 0.0468  0.0309  0.0034  1074 HOH B O   
5623 O O   . HOH H .   ? 0.4076 0.5543 0.4932 -0.0423 0.0207  0.0074  1075 HOH B O   
5624 O O   . HOH H .   ? 0.5800 0.6446 0.6198 0.0566  -0.0045 0.0295  1076 HOH B O   
5625 O O   . HOH H .   ? 0.4906 0.6465 0.5772 0.0032  0.0285  0.0113  1077 HOH B O   
5626 O O   . HOH H .   ? 0.5247 0.4849 0.4775 0.0545  0.0419  -0.0245 1078 HOH B O   
5627 O O   . HOH H .   ? 0.4447 0.5046 0.4862 -0.0722 0.0348  0.0074  1079 HOH B O   
5628 O O   . HOH H .   ? 0.5965 0.4348 0.5362 0.0113  0.0659  0.0039  1080 HOH B O   
5629 O O   . HOH H .   ? 0.3837 0.4402 0.4217 -0.0713 0.0253  0.0006  1081 HOH B O   
5630 O O   . HOH H .   ? 0.4887 0.6203 0.5143 -0.0831 -0.0447 -0.0263 1082 HOH B O   
5631 O O   . HOH H .   ? 0.5543 0.5868 0.5899 -0.0887 0.0398  0.0066  1083 HOH B O   
5632 O O   . HOH H .   ? 0.6956 0.4862 0.6204 -0.0567 0.0684  -0.0169 1084 HOH B O   
5633 O O   . HOH H .   ? 0.4202 0.5086 0.4398 0.0202  0.0484  0.0006  1085 HOH B O   
5634 O O   . HOH H .   ? 0.6177 0.6281 0.4734 -0.0007 -0.0001 0.0130  1086 HOH B O   
5635 O O   . HOH H .   ? 0.7460 0.8149 0.7307 -0.0257 -0.0233 -0.0063 1087 HOH B O   
5636 O O   . HOH H .   ? 0.2705 0.3910 0.3291 -0.0422 -0.0048 -0.0029 1088 HOH B O   
5637 O O   . HOH H .   ? 0.6037 0.5808 0.5009 0.0271  0.0438  -0.0331 1089 HOH B O   
5638 O O   . HOH H .   ? 0.3784 0.4830 0.4162 -0.0081 0.0422  0.0080  1090 HOH B O   
5639 O O   . HOH H .   ? 0.4748 0.6090 0.5427 -0.0082 0.0334  0.0090  1091 HOH B O   
5640 O O   . HOH H .   ? 0.3869 0.3931 0.3343 -0.0823 -0.0137 -0.0525 1092 HOH B O   
5641 O O   . HOH H .   ? 0.6213 0.6465 0.5856 -0.0999 -0.0210 -0.0537 1093 HOH B O   
5642 O O   . HOH H .   ? 0.5281 0.4588 0.4656 0.0527  0.0398  -0.0296 1094 HOH B O   
5643 O O   . HOH H .   ? 0.4852 0.4892 0.4571 -0.0572 -0.0418 -0.0158 1095 HOH B O   
5644 O O   . HOH H .   ? 0.4750 0.5876 0.5238 0.0107  0.0348  0.0051  1096 HOH B O   
5645 O O   . HOH H .   ? 0.5033 0.4618 0.4770 -0.0397 0.0434  0.0250  1097 HOH B O   
5646 O O   . HOH H .   ? 0.4860 0.2764 0.4162 -0.0707 0.0697  -0.0124 1098 HOH B O   
5647 O O   . HOH H .   ? 0.4273 0.5254 0.4413 -0.0264 -0.0282 -0.0033 1099 HOH B O   
5648 O O   . HOH H .   ? 0.4695 0.4553 0.4442 -0.0314 0.0369  0.0243  1100 HOH B O   
5649 O O   . HOH H .   ? 0.5789 0.3824 0.5155 -0.0494 0.0769  0.0262  1101 HOH B O   
5650 O O   A HOH H .   ? 0.3820 0.4604 0.3937 -0.0125 0.0430  0.0088  1102 HOH B O   
5651 O O   B HOH H .   ? 0.2667 0.3315 0.2644 -0.0115 0.0396  0.0080  1102 HOH B O   
5652 O O   . HOH H .   ? 0.5669 0.6020 0.5105 -0.0805 -0.0265 -0.0504 1103 HOH B O   
5653 O O   . HOH H .   ? 0.6733 0.6213 0.5156 -0.0601 0.0083  -0.0776 1104 HOH B O   
5654 O O   . HOH H .   ? 0.4272 0.3970 0.2694 -0.0061 0.0010  -0.0346 1105 HOH B O   
5655 O O   . HOH H .   ? 0.5815 0.3863 0.4960 -0.0631 0.0586  -0.0412 1106 HOH B O   
5656 O O   . HOH H .   ? 0.4347 0.5111 0.4314 -0.0235 -0.0244 -0.0038 1107 HOH B O   
5657 O O   . HOH H .   ? 0.5259 0.6983 0.6429 -0.0781 0.0309  0.0119  1108 HOH B O   
5658 O O   . HOH H .   ? 0.7064 0.5500 0.6034 -0.0783 0.0386  -0.0694 1109 HOH B O   
5659 O O   . HOH H .   ? 0.3581 0.5040 0.4061 -0.0969 -0.0436 -0.0263 1110 HOH B O   
5660 O O   . HOH H .   ? 0.6506 0.5466 0.6052 -0.1451 0.0199  -0.0621 1111 HOH B O   
5661 O O   . HOH H .   ? 0.6863 0.4955 0.5950 -0.0537 0.0581  -0.0460 1112 HOH B O   
5662 O O   . HOH H .   ? 0.4788 0.4880 0.3439 -0.0368 -0.0520 -0.0261 1113 HOH B O   
5663 O O   . HOH H .   ? 0.6411 0.6601 0.5849 0.0086  -0.0045 0.0383  1114 HOH B O   
5664 O O   . HOH H .   ? 0.5289 0.5524 0.5570 -0.0832 0.0484  0.0146  1115 HOH B O   
5665 O O   . HOH H .   ? 0.4737 0.2565 0.4027 -0.0919 0.0689  -0.0226 1116 HOH B O   
5666 O O   . HOH H .   ? 0.4666 0.5158 0.4884 -0.0539 0.0440  0.0164  1117 HOH B O   
5667 O O   . HOH H .   ? 0.7169 0.7477 0.6050 -0.0070 -0.0286 0.0123  1118 HOH B O   
5668 O O   . HOH H .   ? 0.6718 0.4359 0.5957 -0.0621 0.0793  -0.0010 1119 HOH B O   
5669 O O   . HOH H .   ? 0.4018 0.5758 0.4945 -0.0369 -0.0118 0.0044  1120 HOH B O   
5670 O O   . HOH H .   ? 0.4087 0.5772 0.5017 -0.0457 -0.0062 0.0027  1121 HOH B O   
5671 O O   . HOH H .   ? 0.4857 0.6109 0.5138 -0.1068 -0.0458 -0.0358 1122 HOH B O   
5672 O O   . HOH H .   ? 0.4852 0.4553 0.4658 -0.0480 0.0472  0.0254  1123 HOH B O   
5673 O O   . HOH H .   ? 0.8099 0.6091 0.7053 -0.0409 0.0635  -0.0526 1124 HOH B O   
5674 O O   . HOH H .   ? 0.6211 0.6028 0.4956 0.0243  0.0499  -0.0310 1125 HOH B O   
5675 O O   . HOH H .   ? 0.4990 0.6222 0.5567 -0.0128 0.0381  0.0092  1126 HOH B O   
5676 O O   A HOH H .   ? 0.4229 0.4590 0.3226 -0.0514 -0.0697 -0.0212 1127 HOH B O   
5677 O O   B HOH H .   ? 0.3581 0.3933 0.2596 -0.0580 -0.0744 -0.0252 1127 HOH B O   
5678 O O   . HOH H .   ? 0.6792 0.4571 0.5888 -0.0715 0.0652  -0.0408 1128 HOH B O   
5679 O O   . HOH H .   ? 0.7366 0.6184 0.7069 0.0765  0.0634  0.0582  1129 HOH B O   
5680 O O   . HOH H .   ? 0.8166 0.5692 0.7021 -0.0476 0.0745  -0.0529 1130 HOH B O   
5681 O O   . HOH H .   ? 0.6403 0.5683 0.6333 0.0836  0.0719  0.0320  1131 HOH B O   
5682 O O   . HOH H .   ? 0.6722 0.6212 0.5087 0.0264  0.0506  -0.0462 1132 HOH B O   
# 
