data_6G6T
# 
_entry.id   6G6T 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.383 
_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   6G6T         pdb_00006g6t 10.2210/pdb6g6t/pdb 
WWPDB D_1200009485 ?            ?                   
# 
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 
1 'Structure model' 1 0 2019-03-13 
2 'Structure model' 1 1 2024-01-17 
# 
_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' 'Data collection'        
2 2 'Structure model' 'Database references'    
3 2 'Structure model' 'Refinement description' 
# 
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' chem_comp_atom                
2 2 'Structure model' chem_comp_bond                
3 2 'Structure model' database_2                    
4 2 'Structure model' pdbx_initial_refinement_model 
# 
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' '_database_2.pdbx_DOI'                
2 2 'Structure model' '_database_2.pdbx_database_accession' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        6G6T 
_pdbx_database_status.recvd_initial_deposition_date   2018-04-03 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_nmr_data            ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Smirnov, A.'  1 ? 
'Manakova, E.' 2 ? 
'Grazulis, S.' 3 ? 
# 
_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                   FR 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Eur J Med Chem' 
_citation.journal_id_ASTM           EJMCA5 
_citation.journal_id_CSD            0493 
_citation.journal_id_ISSN           1768-3254 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            156 
_citation.language                  ? 
_citation.page_first                61 
_citation.page_last                 78 
_citation.title                     
'Design of two-tail compounds with rotationally fixed benzenesulfonamide ring as inhibitors of carbonic anhydrases.' 
_citation.year                      2018 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.ejmech.2018.06.059 
_citation.pdbx_database_id_PubMed   30006175 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Zaksauskas, A.'   1 ? 
primary 'Capkauskaite, E.' 2 ? 
primary 'Jezepcikas, L.'   3 ? 
primary 'Linkuviene, V.'   4 ? 
primary 'Kisonaite, M.'    5 ? 
primary 'Smirnov, A.'      6 ? 
primary 'Manakova, E.'     7 ? 
primary 'Grazulis, S.'     8 ? 
primary 'Matulis, D.'      9 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Carbonic anhydrase 2'                                29289.062 1   4.2.1.1 ? 'human carbonic anhydrase II' ? 
2 non-polymer syn 'ZINC ION'                                            65.409    1   ?       
N-butyl-2,4-dichloro-5-sulfamoyl-benzamide ?                             ? 
3 non-polymer syn 'DIMETHYL SULFOXIDE'                                  78.133    1   ?       ? Zn                            ? 
4 non-polymer syn BICINE                                                163.172   1   ?       ? Bicine                        ? 
5 non-polymer syn '~{N}-butyl-2,4-bis(chloranyl)-5-sulfamoyl-benzamide' 325.211   1   ?       ? 'Dimethyl sulfoxide'          ? 
6 water       nat water                                                 18.015    328 ?       ? ?                             ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Carbonate dehydratase II,Carbonic anhydrase C,CAC,Carbonic anhydrase II,CA-II' 
# 
_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       
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLK
GGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLK
GGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'ZINC ION'                                            ZN  
3 'DIMETHYL SULFOXIDE'                                  DMS 
4 BICINE                                                BCN 
5 '~{N}-butyl-2,4-bis(chloranyl)-5-sulfamoyl-benzamide' ENN 
6 water                                                 HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   SER n 
1 3   HIS n 
1 4   HIS n 
1 5   TRP n 
1 6   GLY n 
1 7   TYR n 
1 8   GLY n 
1 9   LYS n 
1 10  HIS n 
1 11  ASN n 
1 12  GLY n 
1 13  PRO n 
1 14  GLU n 
1 15  HIS n 
1 16  TRP n 
1 17  HIS n 
1 18  LYS n 
1 19  ASP n 
1 20  PHE n 
1 21  PRO n 
1 22  ILE n 
1 23  ALA n 
1 24  LYS n 
1 25  GLY n 
1 26  GLU n 
1 27  ARG n 
1 28  GLN n 
1 29  SER n 
1 30  PRO n 
1 31  VAL n 
1 32  ASP n 
1 33  ILE n 
1 34  ASP n 
1 35  THR n 
1 36  HIS n 
1 37  THR n 
1 38  ALA n 
1 39  LYS n 
1 40  TYR n 
1 41  ASP n 
1 42  PRO n 
1 43  SER n 
1 44  LEU n 
1 45  LYS n 
1 46  PRO n 
1 47  LEU n 
1 48  SER n 
1 49  VAL n 
1 50  SER n 
1 51  TYR n 
1 52  ASP n 
1 53  GLN n 
1 54  ALA n 
1 55  THR n 
1 56  SER n 
1 57  LEU n 
1 58  ARG n 
1 59  ILE n 
1 60  LEU n 
1 61  ASN n 
1 62  ASN n 
1 63  GLY n 
1 64  HIS n 
1 65  ALA n 
1 66  PHE n 
1 67  ASN n 
1 68  VAL n 
1 69  GLU n 
1 70  PHE n 
1 71  ASP n 
1 72  ASP n 
1 73  SER n 
1 74  GLN n 
1 75  ASP n 
1 76  LYS n 
1 77  ALA n 
1 78  VAL n 
1 79  LEU n 
1 80  LYS n 
1 81  GLY n 
1 82  GLY n 
1 83  PRO n 
1 84  LEU n 
1 85  ASP n 
1 86  GLY n 
1 87  THR n 
1 88  TYR n 
1 89  ARG n 
1 90  LEU n 
1 91  ILE n 
1 92  GLN n 
1 93  PHE n 
1 94  HIS n 
1 95  PHE n 
1 96  HIS n 
1 97  TRP n 
1 98  GLY n 
1 99  SER n 
1 100 LEU n 
1 101 ASP n 
1 102 GLY n 
1 103 GLN n 
1 104 GLY n 
1 105 SER n 
1 106 GLU n 
1 107 HIS n 
1 108 THR n 
1 109 VAL n 
1 110 ASP n 
1 111 LYS n 
1 112 LYS n 
1 113 LYS n 
1 114 TYR n 
1 115 ALA n 
1 116 ALA n 
1 117 GLU n 
1 118 LEU n 
1 119 HIS n 
1 120 LEU n 
1 121 VAL n 
1 122 HIS n 
1 123 TRP n 
1 124 ASN n 
1 125 THR n 
1 126 LYS n 
1 127 TYR n 
1 128 GLY n 
1 129 ASP n 
1 130 PHE n 
1 131 GLY n 
1 132 LYS n 
1 133 ALA n 
1 134 VAL n 
1 135 GLN n 
1 136 GLN n 
1 137 PRO n 
1 138 ASP n 
1 139 GLY n 
1 140 LEU n 
1 141 ALA n 
1 142 VAL n 
1 143 LEU n 
1 144 GLY n 
1 145 ILE n 
1 146 PHE n 
1 147 LEU n 
1 148 LYS n 
1 149 VAL n 
1 150 GLY n 
1 151 SER n 
1 152 ALA n 
1 153 LYS n 
1 154 PRO n 
1 155 GLY n 
1 156 LEU n 
1 157 GLN n 
1 158 LYS n 
1 159 VAL n 
1 160 VAL n 
1 161 ASP n 
1 162 VAL n 
1 163 LEU n 
1 164 ASP n 
1 165 SER n 
1 166 ILE n 
1 167 LYS n 
1 168 THR n 
1 169 LYS n 
1 170 GLY n 
1 171 LYS n 
1 172 SER n 
1 173 ALA n 
1 174 ASP n 
1 175 PHE n 
1 176 THR n 
1 177 ASN n 
1 178 PHE n 
1 179 ASP n 
1 180 PRO n 
1 181 ARG n 
1 182 GLY n 
1 183 LEU n 
1 184 LEU n 
1 185 PRO n 
1 186 GLU n 
1 187 SER n 
1 188 LEU n 
1 189 ASP n 
1 190 TYR n 
1 191 TRP n 
1 192 THR n 
1 193 TYR n 
1 194 PRO n 
1 195 GLY n 
1 196 SER n 
1 197 LEU n 
1 198 THR n 
1 199 THR n 
1 200 PRO n 
1 201 PRO n 
1 202 LEU n 
1 203 LEU n 
1 204 GLU n 
1 205 CYS n 
1 206 VAL n 
1 207 THR n 
1 208 TRP n 
1 209 ILE n 
1 210 VAL n 
1 211 LEU n 
1 212 LYS n 
1 213 GLU n 
1 214 PRO n 
1 215 ILE n 
1 216 SER n 
1 217 VAL n 
1 218 SER n 
1 219 SER n 
1 220 GLU n 
1 221 GLN n 
1 222 VAL n 
1 223 LEU n 
1 224 LYS n 
1 225 PHE n 
1 226 ARG n 
1 227 LYS n 
1 228 LEU n 
1 229 ASN n 
1 230 PHE n 
1 231 ASN n 
1 232 GLY n 
1 233 GLU n 
1 234 GLY n 
1 235 GLU n 
1 236 PRO n 
1 237 GLU n 
1 238 GLU n 
1 239 LEU n 
1 240 MET n 
1 241 VAL n 
1 242 ASP n 
1 243 ASN n 
1 244 TRP n 
1 245 ARG n 
1 246 PRO n 
1 247 ALA n 
1 248 GLN n 
1 249 PRO n 
1 250 LEU n 
1 251 LYS n 
1 252 ASN n 
1 253 ARG n 
1 254 GLN n 
1 255 ILE n 
1 256 LYS n 
1 257 ALA n 
1 258 SER n 
1 259 PHE n 
1 260 LYS 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                   260 
_entity_src_gen.gene_src_common_name               Human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 CA2 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_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     469008 
_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               'BL21(DE3)' 
_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          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pET15b 
_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 
BCN non-polymer         . BICINE                                                ? 'C6 H13 N O4'         163.172 
CYS 'L-peptide linking' y CYSTEINE                                              ? 'C3 H7 N O2 S'        121.158 
DMS non-polymer         . 'DIMETHYL SULFOXIDE'                                  ? 'C2 H6 O S'           78.133  
ENN non-polymer         . '~{N}-butyl-2,4-bis(chloranyl)-5-sulfamoyl-benzamide' ? 'C11 H14 Cl2 N2 O3 S' 325.211 
GLN 'L-peptide linking' y GLUTAMINE                                             ? 'C5 H10 N2 O3'        146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                                       ? 'C5 H9 N O4'          147.129 
GLY 'peptide linking'   y GLYCINE                                               ? 'C2 H5 N O2'          75.067  
HIS 'L-peptide linking' y HISTIDINE                                             ? 'C6 H10 N3 O2 1'      156.162 
HOH non-polymer         . WATER                                                 ? 'H2 O'                18.015  
ILE 'L-peptide linking' y ISOLEUCINE                                            ? 'C6 H13 N O2'         131.173 
LEU 'L-peptide linking' y LEUCINE                                               ? 'C6 H13 N O2'         131.173 
LYS 'L-peptide linking' y LYSINE                                                ? 'C6 H15 N2 O2 1'      147.195 
MET 'L-peptide linking' y METHIONINE                                            ? 'C5 H11 N O2 S'       149.211 
PHE 'L-peptide linking' y PHENYLALANINE                                         ? 'C9 H11 N O2'         165.189 
PRO 'L-peptide linking' y PROLINE                                               ? 'C5 H9 N O2'          115.130 
SER 'L-peptide linking' y SERINE                                                ? 'C3 H7 N O3'          105.093 
THR 'L-peptide linking' y THREONINE                                             ? 'C4 H9 N O3'          119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                            ? 'C11 H12 N2 O2'       204.225 
TYR 'L-peptide linking' y TYROSINE                                              ? 'C9 H11 N O3'         181.189 
VAL 'L-peptide linking' y VALINE                                                ? 'C5 H11 N O2'         117.146 
ZN  non-polymer         . 'ZINC ION'                                            ? 'Zn 2'                65.409  
# 
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   MET 1   1   ?   ?   ?   A . n 
A 1 2   SER 2   2   ?   ?   ?   A . n 
A 1 3   HIS 3   3   ?   ?   ?   A . n 
A 1 4   HIS 4   4   4   HIS HIS A . n 
A 1 5   TRP 5   5   5   TRP TRP A . n 
A 1 6   GLY 6   6   6   GLY GLY A . n 
A 1 7   TYR 7   7   7   TYR TYR A . n 
A 1 8   GLY 8   8   8   GLY GLY A . n 
A 1 9   LYS 9   9   9   LYS LYS A . n 
A 1 10  HIS 10  10  10  HIS HIS A . n 
A 1 11  ASN 11  11  11  ASN ASN A . n 
A 1 12  GLY 12  12  12  GLY GLY A . n 
A 1 13  PRO 13  13  13  PRO PRO A . n 
A 1 14  GLU 14  14  14  GLU GLU A . n 
A 1 15  HIS 15  15  15  HIS HIS A . n 
A 1 16  TRP 16  16  16  TRP TRP A . n 
A 1 17  HIS 17  17  17  HIS HIS A . n 
A 1 18  LYS 18  18  18  LYS LYS A . n 
A 1 19  ASP 19  19  19  ASP ASP A . n 
A 1 20  PHE 20  20  20  PHE PHE A . n 
A 1 21  PRO 21  21  21  PRO PRO A . n 
A 1 22  ILE 22  22  22  ILE ILE A . n 
A 1 23  ALA 23  23  23  ALA ALA A . n 
A 1 24  LYS 24  24  24  LYS LYS A . n 
A 1 25  GLY 25  25  25  GLY GLY A . n 
A 1 26  GLU 26  26  26  GLU GLU A . n 
A 1 27  ARG 27  27  27  ARG ARG A . n 
A 1 28  GLN 28  28  28  GLN GLN A . n 
A 1 29  SER 29  29  29  SER SER A . n 
A 1 30  PRO 30  30  30  PRO PRO A . n 
A 1 31  VAL 31  31  31  VAL VAL A . n 
A 1 32  ASP 32  32  32  ASP ASP A . n 
A 1 33  ILE 33  33  33  ILE ILE A . n 
A 1 34  ASP 34  34  34  ASP ASP A . n 
A 1 35  THR 35  35  35  THR THR A . n 
A 1 36  HIS 36  36  36  HIS HIS A . n 
A 1 37  THR 37  37  37  THR THR A . n 
A 1 38  ALA 38  38  38  ALA ALA A . n 
A 1 39  LYS 39  39  39  LYS LYS A . n 
A 1 40  TYR 40  40  40  TYR TYR A . n 
A 1 41  ASP 41  41  41  ASP ASP A . n 
A 1 42  PRO 42  42  42  PRO PRO A . n 
A 1 43  SER 43  43  43  SER SER A . n 
A 1 44  LEU 44  44  44  LEU LEU A . n 
A 1 45  LYS 45  45  45  LYS LYS A . n 
A 1 46  PRO 46  46  46  PRO PRO A . n 
A 1 47  LEU 47  47  47  LEU LEU A . n 
A 1 48  SER 48  48  48  SER SER A . n 
A 1 49  VAL 49  49  49  VAL VAL A . n 
A 1 50  SER 50  50  50  SER SER A . n 
A 1 51  TYR 51  51  51  TYR TYR A . n 
A 1 52  ASP 52  52  52  ASP ASP A . n 
A 1 53  GLN 53  53  53  GLN GLN A . n 
A 1 54  ALA 54  54  54  ALA ALA A . n 
A 1 55  THR 55  55  55  THR THR A . n 
A 1 56  SER 56  56  56  SER SER A . n 
A 1 57  LEU 57  57  57  LEU LEU A . n 
A 1 58  ARG 58  58  58  ARG ARG A . n 
A 1 59  ILE 59  59  59  ILE ILE A . n 
A 1 60  LEU 60  60  60  LEU LEU A . n 
A 1 61  ASN 61  61  61  ASN ASN A . n 
A 1 62  ASN 62  62  62  ASN ASN A . n 
A 1 63  GLY 63  63  63  GLY GLY A . n 
A 1 64  HIS 64  64  64  HIS HIS A . n 
A 1 65  ALA 65  65  65  ALA ALA A . n 
A 1 66  PHE 66  66  66  PHE PHE A . n 
A 1 67  ASN 67  67  67  ASN ASN A . n 
A 1 68  VAL 68  68  68  VAL VAL A . n 
A 1 69  GLU 69  69  69  GLU GLU A . n 
A 1 70  PHE 70  70  70  PHE PHE A . n 
A 1 71  ASP 71  71  71  ASP ASP A . n 
A 1 72  ASP 72  72  72  ASP ASP A . n 
A 1 73  SER 73  73  73  SER SER A . n 
A 1 74  GLN 74  74  74  GLN GLN A . n 
A 1 75  ASP 75  75  75  ASP ASP A . n 
A 1 76  LYS 76  76  76  LYS LYS A . n 
A 1 77  ALA 77  77  77  ALA ALA A . n 
A 1 78  VAL 78  78  78  VAL VAL A . n 
A 1 79  LEU 79  79  79  LEU LEU A . n 
A 1 80  LYS 80  80  80  LYS LYS A . n 
A 1 81  GLY 81  81  81  GLY GLY A . n 
A 1 82  GLY 82  82  82  GLY GLY A . n 
A 1 83  PRO 83  83  83  PRO PRO A . n 
A 1 84  LEU 84  84  84  LEU LEU A . n 
A 1 85  ASP 85  85  85  ASP ASP A . n 
A 1 86  GLY 86  86  86  GLY GLY A . n 
A 1 87  THR 87  87  87  THR THR A . n 
A 1 88  TYR 88  88  88  TYR TYR A . n 
A 1 89  ARG 89  89  89  ARG ARG A . n 
A 1 90  LEU 90  90  90  LEU LEU A . n 
A 1 91  ILE 91  91  91  ILE ILE A . n 
A 1 92  GLN 92  92  92  GLN GLN A . n 
A 1 93  PHE 93  93  93  PHE PHE A . n 
A 1 94  HIS 94  94  94  HIS HIS A . n 
A 1 95  PHE 95  95  95  PHE PHE A . n 
A 1 96  HIS 96  96  96  HIS HIS A . n 
A 1 97  TRP 97  97  97  TRP TRP A . n 
A 1 98  GLY 98  98  98  GLY GLY A . n 
A 1 99  SER 99  99  99  SER SER A . n 
A 1 100 LEU 100 100 100 LEU LEU A . n 
A 1 101 ASP 101 101 101 ASP ASP A . n 
A 1 102 GLY 102 102 102 GLY GLY A . n 
A 1 103 GLN 103 103 103 GLN GLN A . n 
A 1 104 GLY 104 104 104 GLY GLY A . n 
A 1 105 SER 105 105 105 SER SER A . n 
A 1 106 GLU 106 106 106 GLU GLU A . n 
A 1 107 HIS 107 107 107 HIS HIS A . n 
A 1 108 THR 108 108 108 THR THR A . n 
A 1 109 VAL 109 109 109 VAL VAL A . n 
A 1 110 ASP 110 110 110 ASP ASP A . n 
A 1 111 LYS 111 111 111 LYS LYS A . n 
A 1 112 LYS 112 112 112 LYS LYS A . n 
A 1 113 LYS 113 113 113 LYS LYS A . n 
A 1 114 TYR 114 114 114 TYR TYR A . n 
A 1 115 ALA 115 115 115 ALA ALA A . n 
A 1 116 ALA 116 116 116 ALA ALA A . n 
A 1 117 GLU 117 117 117 GLU GLU A . n 
A 1 118 LEU 118 118 118 LEU LEU A . n 
A 1 119 HIS 119 119 119 HIS HIS A . n 
A 1 120 LEU 120 120 120 LEU LEU A . n 
A 1 121 VAL 121 121 121 VAL VAL A . n 
A 1 122 HIS 122 122 122 HIS HIS A . n 
A 1 123 TRP 123 123 123 TRP TRP A . n 
A 1 124 ASN 124 124 124 ASN ASN A . n 
A 1 125 THR 125 125 125 THR THR A . n 
A 1 126 LYS 126 127 127 LYS LYS A . n 
A 1 127 TYR 127 128 128 TYR TYR A . n 
A 1 128 GLY 128 129 129 GLY GLY A . n 
A 1 129 ASP 129 130 130 ASP ASP A . n 
A 1 130 PHE 130 131 131 PHE PHE A . n 
A 1 131 GLY 131 132 132 GLY GLY A . n 
A 1 132 LYS 132 133 133 LYS LYS A . n 
A 1 133 ALA 133 134 134 ALA ALA A . n 
A 1 134 VAL 134 135 135 VAL VAL A . n 
A 1 135 GLN 135 136 136 GLN GLN A . n 
A 1 136 GLN 136 137 137 GLN GLN A . n 
A 1 137 PRO 137 138 138 PRO PRO A . n 
A 1 138 ASP 138 139 139 ASP ASP A . n 
A 1 139 GLY 139 140 140 GLY GLY A . n 
A 1 140 LEU 140 141 141 LEU LEU A . n 
A 1 141 ALA 141 142 142 ALA ALA A . n 
A 1 142 VAL 142 143 143 VAL VAL A . n 
A 1 143 LEU 143 144 144 LEU LEU A . n 
A 1 144 GLY 144 145 145 GLY GLY A . n 
A 1 145 ILE 145 146 146 ILE ILE A . n 
A 1 146 PHE 146 147 147 PHE PHE A . n 
A 1 147 LEU 147 148 148 LEU LEU A . n 
A 1 148 LYS 148 149 149 LYS LYS A . n 
A 1 149 VAL 149 150 150 VAL VAL A . n 
A 1 150 GLY 150 151 151 GLY GLY A . n 
A 1 151 SER 151 152 152 SER SER A . n 
A 1 152 ALA 152 153 153 ALA ALA A . n 
A 1 153 LYS 153 154 154 LYS LYS A . n 
A 1 154 PRO 154 155 155 PRO PRO A . n 
A 1 155 GLY 155 156 156 GLY GLY A . n 
A 1 156 LEU 156 157 157 LEU LEU A . n 
A 1 157 GLN 157 158 158 GLN GLN A . n 
A 1 158 LYS 158 159 159 LYS LYS A . n 
A 1 159 VAL 159 160 160 VAL VAL A . n 
A 1 160 VAL 160 161 161 VAL VAL A . n 
A 1 161 ASP 161 162 162 ASP ASP A . n 
A 1 162 VAL 162 163 163 VAL VAL A . n 
A 1 163 LEU 163 164 164 LEU LEU A . n 
A 1 164 ASP 164 165 165 ASP ASP A . n 
A 1 165 SER 165 166 166 SER SER A . n 
A 1 166 ILE 166 167 167 ILE ILE A . n 
A 1 167 LYS 167 168 168 LYS LYS A . n 
A 1 168 THR 168 169 169 THR THR A . n 
A 1 169 LYS 169 170 170 LYS LYS A . n 
A 1 170 GLY 170 171 171 GLY GLY A . n 
A 1 171 LYS 171 172 172 LYS LYS A . n 
A 1 172 SER 172 173 173 SER SER A . n 
A 1 173 ALA 173 174 174 ALA ALA A . n 
A 1 174 ASP 174 175 175 ASP ASP A . n 
A 1 175 PHE 175 176 176 PHE PHE A . n 
A 1 176 THR 176 177 177 THR THR A . n 
A 1 177 ASN 177 178 178 ASN ASN A . n 
A 1 178 PHE 178 179 179 PHE PHE A . n 
A 1 179 ASP 179 180 180 ASP ASP A . n 
A 1 180 PRO 180 181 181 PRO PRO A . n 
A 1 181 ARG 181 182 182 ARG ARG A . n 
A 1 182 GLY 182 183 183 GLY GLY A . n 
A 1 183 LEU 183 184 184 LEU LEU A . n 
A 1 184 LEU 184 185 185 LEU LEU A . n 
A 1 185 PRO 185 186 186 PRO PRO A . n 
A 1 186 GLU 186 187 187 GLU GLU A . n 
A 1 187 SER 187 188 188 SER SER A . n 
A 1 188 LEU 188 189 189 LEU LEU A . n 
A 1 189 ASP 189 190 190 ASP ASP A . n 
A 1 190 TYR 190 191 191 TYR TYR A . n 
A 1 191 TRP 191 192 192 TRP TRP A . n 
A 1 192 THR 192 193 193 THR THR A . n 
A 1 193 TYR 193 194 194 TYR TYR A . n 
A 1 194 PRO 194 195 195 PRO PRO A . n 
A 1 195 GLY 195 196 196 GLY GLY A . n 
A 1 196 SER 196 197 197 SER SER A . n 
A 1 197 LEU 197 198 198 LEU LEU A . n 
A 1 198 THR 198 199 199 THR THR A . n 
A 1 199 THR 199 200 200 THR THR A . n 
A 1 200 PRO 200 201 201 PRO PRO A . n 
A 1 201 PRO 201 202 202 PRO PRO A . n 
A 1 202 LEU 202 203 203 LEU LEU A . n 
A 1 203 LEU 203 204 204 LEU LEU A . n 
A 1 204 GLU 204 205 205 GLU GLU A . n 
A 1 205 CYS 205 206 206 CYS CYS A . n 
A 1 206 VAL 206 207 207 VAL VAL A . n 
A 1 207 THR 207 208 208 THR THR A . n 
A 1 208 TRP 208 209 209 TRP TRP A . n 
A 1 209 ILE 209 210 210 ILE ILE A . n 
A 1 210 VAL 210 211 211 VAL VAL A . n 
A 1 211 LEU 211 212 212 LEU LEU A . n 
A 1 212 LYS 212 213 213 LYS LYS A . n 
A 1 213 GLU 213 214 214 GLU GLU A . n 
A 1 214 PRO 214 215 215 PRO PRO A . n 
A 1 215 ILE 215 216 216 ILE ILE A . n 
A 1 216 SER 216 217 217 SER SER A . n 
A 1 217 VAL 217 218 218 VAL VAL A . n 
A 1 218 SER 218 219 219 SER SER A . n 
A 1 219 SER 219 220 220 SER SER A . n 
A 1 220 GLU 220 221 221 GLU GLU A . n 
A 1 221 GLN 221 222 222 GLN GLN A . n 
A 1 222 VAL 222 223 223 VAL VAL A . n 
A 1 223 LEU 223 224 224 LEU LEU A . n 
A 1 224 LYS 224 225 225 LYS LYS A . n 
A 1 225 PHE 225 226 226 PHE PHE A . n 
A 1 226 ARG 226 227 227 ARG ARG A . n 
A 1 227 LYS 227 228 228 LYS LYS A . n 
A 1 228 LEU 228 229 229 LEU LEU A . n 
A 1 229 ASN 229 230 230 ASN ASN A . n 
A 1 230 PHE 230 231 231 PHE PHE A . n 
A 1 231 ASN 231 232 232 ASN ASN A . n 
A 1 232 GLY 232 233 233 GLY GLY A . n 
A 1 233 GLU 233 234 234 GLU GLU A . n 
A 1 234 GLY 234 235 235 GLY GLY A . n 
A 1 235 GLU 235 236 236 GLU GLU A . n 
A 1 236 PRO 236 237 237 PRO PRO A . n 
A 1 237 GLU 237 238 238 GLU GLU A . n 
A 1 238 GLU 238 239 239 GLU GLU A . n 
A 1 239 LEU 239 240 240 LEU LEU A . n 
A 1 240 MET 240 241 241 MET MET A . n 
A 1 241 VAL 241 242 242 VAL VAL A . n 
A 1 242 ASP 242 243 243 ASP ASP A . n 
A 1 243 ASN 243 244 244 ASN ASN A . n 
A 1 244 TRP 244 245 245 TRP TRP A . n 
A 1 245 ARG 245 246 246 ARG ARG A . n 
A 1 246 PRO 246 247 247 PRO PRO A . n 
A 1 247 ALA 247 248 248 ALA ALA A . n 
A 1 248 GLN 248 249 249 GLN GLN A . n 
A 1 249 PRO 249 250 250 PRO PRO A . n 
A 1 250 LEU 250 251 251 LEU LEU A . n 
A 1 251 LYS 251 252 252 LYS LYS A . n 
A 1 252 ASN 252 253 253 ASN ASN A . n 
A 1 253 ARG 253 254 254 ARG ARG A . n 
A 1 254 GLN 254 255 255 GLN GLN A . n 
A 1 255 ILE 255 256 256 ILE ILE A . n 
A 1 256 LYS 256 257 257 LYS LYS A . n 
A 1 257 ALA 257 258 258 ALA ALA A . n 
A 1 258 SER 258 259 259 SER SER A . n 
A 1 259 PHE 259 260 260 PHE PHE A . n 
A 1 260 LYS 260 261 261 LYS LYS A . 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 
B 2 ZN  1   301 1   ZN  ZN  A . 
C 3 DMS 1   302 1   DMS DMS A . 
D 4 BCN 1   303 2   BCN BCN A . 
E 5 ENN 1   304 1   ENN EA1 A . 
F 6 HOH 1   401 180 HOH HOH A . 
F 6 HOH 2   402 170 HOH HOH A . 
F 6 HOH 3   403 236 HOH HOH A . 
F 6 HOH 4   404 249 HOH HOH A . 
F 6 HOH 5   405 54  HOH HOH A . 
F 6 HOH 6   406 293 HOH HOH A . 
F 6 HOH 7   407 270 HOH HOH A . 
F 6 HOH 8   408 149 HOH HOH A . 
F 6 HOH 9   409 130 HOH HOH A . 
F 6 HOH 10  410 123 HOH HOH A . 
F 6 HOH 11  411 281 HOH HOH A . 
F 6 HOH 12  412 286 HOH HOH A . 
F 6 HOH 13  413 206 HOH HOH A . 
F 6 HOH 14  414 117 HOH HOH A . 
F 6 HOH 15  415 237 HOH HOH A . 
F 6 HOH 16  416 300 HOH HOH A . 
F 6 HOH 17  417 108 HOH HOH A . 
F 6 HOH 18  418 181 HOH HOH A . 
F 6 HOH 19  419 207 HOH HOH A . 
F 6 HOH 20  420 324 HOH HOH A . 
F 6 HOH 21  421 200 HOH HOH A . 
F 6 HOH 22  422 291 HOH HOH A . 
F 6 HOH 23  423 159 HOH HOH A . 
F 6 HOH 24  424 158 HOH HOH A . 
F 6 HOH 25  425 102 HOH HOH A . 
F 6 HOH 26  426 154 HOH HOH A . 
F 6 HOH 27  427 203 HOH HOH A . 
F 6 HOH 28  428 260 HOH HOH A . 
F 6 HOH 29  429 133 HOH HOH A . 
F 6 HOH 30  430 183 HOH HOH A . 
F 6 HOH 31  431 138 HOH HOH A . 
F 6 HOH 32  432 6   HOH HOH A . 
F 6 HOH 33  433 299 HOH HOH A . 
F 6 HOH 34  434 94  HOH HOH A . 
F 6 HOH 35  435 93  HOH HOH A . 
F 6 HOH 36  436 14  HOH HOH A . 
F 6 HOH 37  437 226 HOH HOH A . 
F 6 HOH 38  438 82  HOH HOH A . 
F 6 HOH 39  439 32  HOH HOH A . 
F 6 HOH 40  440 220 HOH HOH A . 
F 6 HOH 41  441 265 HOH HOH A . 
F 6 HOH 42  442 326 HOH HOH A . 
F 6 HOH 43  443 78  HOH HOH A . 
F 6 HOH 44  444 34  HOH HOH A . 
F 6 HOH 45  445 109 HOH HOH A . 
F 6 HOH 46  446 99  HOH HOH A . 
F 6 HOH 47  447 120 HOH HOH A . 
F 6 HOH 48  448 143 HOH HOH A . 
F 6 HOH 49  449 273 HOH HOH A . 
F 6 HOH 50  450 131 HOH HOH A . 
F 6 HOH 51  451 65  HOH HOH A . 
F 6 HOH 52  452 127 HOH HOH A . 
F 6 HOH 53  453 176 HOH HOH A . 
F 6 HOH 54  454 56  HOH HOH A . 
F 6 HOH 55  455 3   HOH HOH A . 
F 6 HOH 56  456 304 HOH HOH A . 
F 6 HOH 57  457 192 HOH HOH A . 
F 6 HOH 58  458 191 HOH HOH A . 
F 6 HOH 59  459 168 HOH HOH A . 
F 6 HOH 60  460 202 HOH HOH A . 
F 6 HOH 61  461 114 HOH HOH A . 
F 6 HOH 62  462 66  HOH HOH A . 
F 6 HOH 63  463 322 HOH HOH A . 
F 6 HOH 64  464 42  HOH HOH A . 
F 6 HOH 65  465 74  HOH HOH A . 
F 6 HOH 66  466 163 HOH HOH A . 
F 6 HOH 67  467 51  HOH HOH A . 
F 6 HOH 68  468 186 HOH HOH A . 
F 6 HOH 69  469 11  HOH HOH A . 
F 6 HOH 70  470 90  HOH HOH A . 
F 6 HOH 71  471 89  HOH HOH A . 
F 6 HOH 72  472 151 HOH HOH A . 
F 6 HOH 73  473 52  HOH HOH A . 
F 6 HOH 74  474 251 HOH HOH A . 
F 6 HOH 75  475 287 HOH HOH A . 
F 6 HOH 76  476 126 HOH HOH A . 
F 6 HOH 77  477 184 HOH HOH A . 
F 6 HOH 78  478 195 HOH HOH A . 
F 6 HOH 79  479 61  HOH HOH A . 
F 6 HOH 80  480 136 HOH HOH A . 
F 6 HOH 81  481 150 HOH HOH A . 
F 6 HOH 82  482 269 HOH HOH A . 
F 6 HOH 83  483 58  HOH HOH A . 
F 6 HOH 84  484 13  HOH HOH A . 
F 6 HOH 85  485 1   HOH HOH A . 
F 6 HOH 86  486 164 HOH HOH A . 
F 6 HOH 87  487 190 HOH HOH A . 
F 6 HOH 88  488 15  HOH HOH A . 
F 6 HOH 89  489 30  HOH HOH A . 
F 6 HOH 90  490 67  HOH HOH A . 
F 6 HOH 91  491 169 HOH HOH A . 
F 6 HOH 92  492 31  HOH HOH A . 
F 6 HOH 93  493 5   HOH HOH A . 
F 6 HOH 94  494 302 HOH HOH A . 
F 6 HOH 95  495 118 HOH HOH A . 
F 6 HOH 96  496 83  HOH HOH A . 
F 6 HOH 97  497 297 HOH HOH A . 
F 6 HOH 98  498 137 HOH HOH A . 
F 6 HOH 99  499 2   HOH HOH A . 
F 6 HOH 100 500 165 HOH HOH A . 
F 6 HOH 101 501 148 HOH HOH A . 
F 6 HOH 102 502 272 HOH HOH A . 
F 6 HOH 103 503 212 HOH HOH A . 
F 6 HOH 104 504 101 HOH HOH A . 
F 6 HOH 105 505 178 HOH HOH A . 
F 6 HOH 106 506 17  HOH HOH A . 
F 6 HOH 107 507 100 HOH HOH A . 
F 6 HOH 108 508 37  HOH HOH A . 
F 6 HOH 109 509 9   HOH HOH A . 
F 6 HOH 110 510 199 HOH HOH A . 
F 6 HOH 111 511 139 HOH HOH A . 
F 6 HOH 112 512 72  HOH HOH A . 
F 6 HOH 113 513 81  HOH HOH A . 
F 6 HOH 114 514 24  HOH HOH A . 
F 6 HOH 115 515 316 HOH HOH A . 
F 6 HOH 116 516 36  HOH HOH A . 
F 6 HOH 117 517 64  HOH HOH A . 
F 6 HOH 118 518 213 HOH HOH A . 
F 6 HOH 119 519 23  HOH HOH A . 
F 6 HOH 120 520 187 HOH HOH A . 
F 6 HOH 121 521 63  HOH HOH A . 
F 6 HOH 122 522 62  HOH HOH A . 
F 6 HOH 123 523 153 HOH HOH A . 
F 6 HOH 124 524 198 HOH HOH A . 
F 6 HOH 125 525 105 HOH HOH A . 
F 6 HOH 126 526 79  HOH HOH A . 
F 6 HOH 127 527 328 HOH HOH A . 
F 6 HOH 128 528 255 HOH HOH A . 
F 6 HOH 129 529 39  HOH HOH A . 
F 6 HOH 130 530 69  HOH HOH A . 
F 6 HOH 131 531 16  HOH HOH A . 
F 6 HOH 132 532 185 HOH HOH A . 
F 6 HOH 133 533 106 HOH HOH A . 
F 6 HOH 134 534 76  HOH HOH A . 
F 6 HOH 135 535 172 HOH HOH A . 
F 6 HOH 136 536 21  HOH HOH A . 
F 6 HOH 137 537 196 HOH HOH A . 
F 6 HOH 138 538 75  HOH HOH A . 
F 6 HOH 139 539 28  HOH HOH A . 
F 6 HOH 140 540 110 HOH HOH A . 
F 6 HOH 141 541 278 HOH HOH A . 
F 6 HOH 142 542 46  HOH HOH A . 
F 6 HOH 143 543 29  HOH HOH A . 
F 6 HOH 144 544 116 HOH HOH A . 
F 6 HOH 145 545 115 HOH HOH A . 
F 6 HOH 146 546 134 HOH HOH A . 
F 6 HOH 147 547 20  HOH HOH A . 
F 6 HOH 148 548 41  HOH HOH A . 
F 6 HOH 149 549 68  HOH HOH A . 
F 6 HOH 150 550 53  HOH HOH A . 
F 6 HOH 151 551 77  HOH HOH A . 
F 6 HOH 152 552 22  HOH HOH A . 
F 6 HOH 153 553 8   HOH HOH A . 
F 6 HOH 154 554 12  HOH HOH A . 
F 6 HOH 155 555 298 HOH HOH A . 
F 6 HOH 156 556 26  HOH HOH A . 
F 6 HOH 157 557 132 HOH HOH A . 
F 6 HOH 158 558 50  HOH HOH A . 
F 6 HOH 159 559 156 HOH HOH A . 
F 6 HOH 160 560 129 HOH HOH A . 
F 6 HOH 161 561 27  HOH HOH A . 
F 6 HOH 162 562 179 HOH HOH A . 
F 6 HOH 163 563 35  HOH HOH A . 
F 6 HOH 164 564 157 HOH HOH A . 
F 6 HOH 165 565 197 HOH HOH A . 
F 6 HOH 166 566 121 HOH HOH A . 
F 6 HOH 167 567 70  HOH HOH A . 
F 6 HOH 168 568 188 HOH HOH A . 
F 6 HOH 169 569 97  HOH HOH A . 
F 6 HOH 170 570 45  HOH HOH A . 
F 6 HOH 171 571 167 HOH HOH A . 
F 6 HOH 172 572 177 HOH HOH A . 
F 6 HOH 173 573 283 HOH HOH A . 
F 6 HOH 174 574 57  HOH HOH A . 
F 6 HOH 175 575 276 HOH HOH A . 
F 6 HOH 176 576 146 HOH HOH A . 
F 6 HOH 177 577 47  HOH HOH A . 
F 6 HOH 178 578 85  HOH HOH A . 
F 6 HOH 179 579 111 HOH HOH A . 
F 6 HOH 180 580 140 HOH HOH A . 
F 6 HOH 181 581 10  HOH HOH A . 
F 6 HOH 182 582 18  HOH HOH A . 
F 6 HOH 183 583 96  HOH HOH A . 
F 6 HOH 184 584 44  HOH HOH A . 
F 6 HOH 185 585 25  HOH HOH A . 
F 6 HOH 186 586 40  HOH HOH A . 
F 6 HOH 187 587 268 HOH HOH A . 
F 6 HOH 188 588 98  HOH HOH A . 
F 6 HOH 189 589 55  HOH HOH A . 
F 6 HOH 190 590 277 HOH HOH A . 
F 6 HOH 191 591 104 HOH HOH A . 
F 6 HOH 192 592 86  HOH HOH A . 
F 6 HOH 193 593 43  HOH HOH A . 
F 6 HOH 194 594 290 HOH HOH A . 
F 6 HOH 195 595 267 HOH HOH A . 
F 6 HOH 196 596 38  HOH HOH A . 
F 6 HOH 197 597 210 HOH HOH A . 
F 6 HOH 198 598 91  HOH HOH A . 
F 6 HOH 199 599 7   HOH HOH A . 
F 6 HOH 200 600 142 HOH HOH A . 
F 6 HOH 201 601 311 HOH HOH A . 
F 6 HOH 202 602 92  HOH HOH A . 
F 6 HOH 203 603 80  HOH HOH A . 
F 6 HOH 204 604 87  HOH HOH A . 
F 6 HOH 205 605 119 HOH HOH A . 
F 6 HOH 206 606 208 HOH HOH A . 
F 6 HOH 207 607 160 HOH HOH A . 
F 6 HOH 208 608 88  HOH HOH A . 
F 6 HOH 209 609 216 HOH HOH A . 
F 6 HOH 210 610 182 HOH HOH A . 
F 6 HOH 211 611 262 HOH HOH A . 
F 6 HOH 212 612 224 HOH HOH A . 
F 6 HOH 213 613 141 HOH HOH A . 
F 6 HOH 214 614 325 HOH HOH A . 
F 6 HOH 215 615 60  HOH HOH A . 
F 6 HOH 216 616 214 HOH HOH A . 
F 6 HOH 217 617 288 HOH HOH A . 
F 6 HOH 218 618 250 HOH HOH A . 
F 6 HOH 219 619 257 HOH HOH A . 
F 6 HOH 220 620 201 HOH HOH A . 
F 6 HOH 221 621 254 HOH HOH A . 
F 6 HOH 222 622 217 HOH HOH A . 
F 6 HOH 223 623 205 HOH HOH A . 
F 6 HOH 224 624 71  HOH HOH A . 
F 6 HOH 225 625 107 HOH HOH A . 
F 6 HOH 226 626 124 HOH HOH A . 
F 6 HOH 227 627 263 HOH HOH A . 
F 6 HOH 228 628 161 HOH HOH A . 
F 6 HOH 229 629 194 HOH HOH A . 
F 6 HOH 230 630 128 HOH HOH A . 
F 6 HOH 231 631 223 HOH HOH A . 
F 6 HOH 232 632 113 HOH HOH A . 
F 6 HOH 233 633 189 HOH HOH A . 
F 6 HOH 234 634 235 HOH HOH A . 
F 6 HOH 235 635 4   HOH HOH A . 
F 6 HOH 236 636 84  HOH HOH A . 
F 6 HOH 237 637 227 HOH HOH A . 
F 6 HOH 238 638 166 HOH HOH A . 
F 6 HOH 239 639 144 HOH HOH A . 
F 6 HOH 240 640 245 HOH HOH A . 
F 6 HOH 241 641 215 HOH HOH A . 
F 6 HOH 242 642 222 HOH HOH A . 
F 6 HOH 243 643 266 HOH HOH A . 
F 6 HOH 244 644 219 HOH HOH A . 
F 6 HOH 245 645 280 HOH HOH A . 
F 6 HOH 246 646 59  HOH HOH A . 
F 6 HOH 247 647 19  HOH HOH A . 
F 6 HOH 248 648 152 HOH HOH A . 
F 6 HOH 249 649 231 HOH HOH A . 
F 6 HOH 250 650 296 HOH HOH A . 
F 6 HOH 251 651 95  HOH HOH A . 
F 6 HOH 252 652 258 HOH HOH A . 
F 6 HOH 253 653 306 HOH HOH A . 
F 6 HOH 254 654 147 HOH HOH A . 
F 6 HOH 255 655 247 HOH HOH A . 
F 6 HOH 256 656 241 HOH HOH A . 
F 6 HOH 257 657 234 HOH HOH A . 
F 6 HOH 258 658 289 HOH HOH A . 
F 6 HOH 259 659 253 HOH HOH A . 
F 6 HOH 260 660 259 HOH HOH A . 
F 6 HOH 261 661 264 HOH HOH A . 
F 6 HOH 262 662 301 HOH HOH A . 
F 6 HOH 263 663 228 HOH HOH A . 
F 6 HOH 264 664 112 HOH HOH A . 
F 6 HOH 265 665 221 HOH HOH A . 
F 6 HOH 266 666 308 HOH HOH A . 
F 6 HOH 267 667 292 HOH HOH A . 
F 6 HOH 268 668 248 HOH HOH A . 
F 6 HOH 269 669 327 HOH HOH A . 
F 6 HOH 270 670 315 HOH HOH A . 
F 6 HOH 271 671 211 HOH HOH A . 
F 6 HOH 272 672 204 HOH HOH A . 
F 6 HOH 273 673 238 HOH HOH A . 
F 6 HOH 274 674 313 HOH HOH A . 
F 6 HOH 275 675 73  HOH HOH A . 
F 6 HOH 276 676 230 HOH HOH A . 
F 6 HOH 277 677 218 HOH HOH A . 
F 6 HOH 278 678 317 HOH HOH A . 
F 6 HOH 279 679 125 HOH HOH A . 
F 6 HOH 280 680 155 HOH HOH A . 
F 6 HOH 281 681 295 HOH HOH A . 
F 6 HOH 282 682 135 HOH HOH A . 
F 6 HOH 283 683 282 HOH HOH A . 
F 6 HOH 284 684 243 HOH HOH A . 
F 6 HOH 285 685 209 HOH HOH A . 
F 6 HOH 286 686 232 HOH HOH A . 
F 6 HOH 287 687 310 HOH HOH A . 
F 6 HOH 288 688 229 HOH HOH A . 
F 6 HOH 289 689 162 HOH HOH A . 
F 6 HOH 290 690 175 HOH HOH A . 
F 6 HOH 291 691 284 HOH HOH A . 
F 6 HOH 292 692 242 HOH HOH A . 
F 6 HOH 293 693 319 HOH HOH A . 
F 6 HOH 294 694 49  HOH HOH A . 
F 6 HOH 295 695 145 HOH HOH A . 
F 6 HOH 296 696 233 HOH HOH A . 
F 6 HOH 297 697 312 HOH HOH A . 
F 6 HOH 298 698 256 HOH HOH A . 
F 6 HOH 299 699 305 HOH HOH A . 
F 6 HOH 300 700 318 HOH HOH A . 
F 6 HOH 301 701 307 HOH HOH A . 
F 6 HOH 302 702 173 HOH HOH A . 
F 6 HOH 303 703 285 HOH HOH A . 
F 6 HOH 304 704 252 HOH HOH A . 
F 6 HOH 305 705 103 HOH HOH A . 
F 6 HOH 306 706 171 HOH HOH A . 
F 6 HOH 307 707 261 HOH HOH A . 
F 6 HOH 308 708 33  HOH HOH A . 
F 6 HOH 309 709 323 HOH HOH A . 
F 6 HOH 310 710 246 HOH HOH A . 
F 6 HOH 311 711 174 HOH HOH A . 
F 6 HOH 312 712 122 HOH HOH A . 
F 6 HOH 313 713 193 HOH HOH A . 
F 6 HOH 314 714 271 HOH HOH A . 
F 6 HOH 315 715 309 HOH HOH A . 
F 6 HOH 316 716 274 HOH HOH A . 
F 6 HOH 317 717 279 HOH HOH A . 
F 6 HOH 318 718 321 HOH HOH A . 
F 6 HOH 319 719 225 HOH HOH A . 
F 6 HOH 320 720 303 HOH HOH A . 
F 6 HOH 321 721 48  HOH HOH A . 
F 6 HOH 322 722 294 HOH HOH A . 
F 6 HOH 323 723 240 HOH HOH A . 
F 6 HOH 324 724 244 HOH HOH A . 
F 6 HOH 325 725 239 HOH HOH A . 
F 6 HOH 326 726 275 HOH HOH A . 
F 6 HOH 327 727 320 HOH HOH A . 
F 6 HOH 328 728 314 HOH HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A LYS 9   ? CG ? A LYS 9   CG 
2  1 Y 1 A LYS 9   ? CD ? A LYS 9   CD 
3  1 Y 1 A LYS 9   ? CE ? A LYS 9   CE 
4  1 Y 1 A LYS 9   ? NZ ? A LYS 9   NZ 
5  1 Y 1 A LYS 45  ? CE ? A LYS 45  CE 
6  1 Y 1 A LYS 45  ? NZ ? A LYS 45  NZ 
7  1 Y 1 A LYS 228 ? CE ? A LYS 227 CE 
8  1 Y 1 A LYS 228 ? NZ ? A LYS 227 NZ 
9  1 Y 1 A LYS 261 ? C  ? A LYS 260 C  
10 1 Y 1 A LYS 261 ? O  ? A LYS 260 O  
11 1 Y 1 A LYS 261 ? CG ? A LYS 260 CG 
12 1 Y 1 A LYS 261 ? CD ? A LYS 260 CD 
13 1 Y 1 A LYS 261 ? CE ? A LYS 260 CE 
14 1 Y 1 A LYS 261 ? NZ ? A LYS 260 NZ 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement        ? ? ? ? ? ? ? ? ? ? ? REFMAC      ? ? ? .      1 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? SCALA       ? ? ? 3.3.20 2 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? 3.10   3 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? XDS         ? ? ? .      4 
? phasing           ? ? ? ? ? ? ? ? ? ? ? MOLREP      ? ? ? .      5 
? 'model building'  ? ? ? ? ? ? ? ? ? ? ? Coot        ? ? ? .      6 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   104.190 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     6G6T 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     42.057 
_cell.length_a_esd                 ? 
_cell.length_b                     41.196 
_cell.length_b_esd                 ? 
_cell.length_c                     72.094 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        2 
_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             ? 
# 
_symmetry.entry_id                         6G6T 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1 21 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                   6G6T 
_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         40.2 
_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_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              7.0 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp            291 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
'Crystallization buffer: 0.1M sodium bicine (pH 9), 0.2M ammonium sulfate and 2M sodium malonate (pH 7)' 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_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_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2013-05-21 
# 
_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   0.975522 
_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                        'PETRA III, EMBL c/o DESY BEAMLINE P14 (MX2)' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.975522 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   'P14 (MX2)' 
_diffrn_source.pdbx_synchrotron_site       'PETRA III, EMBL c/o DESY' 
# 
_reflns.B_iso_Wilson_estimate            ? 
_reflns.entry_id                         6G6T 
_reflns.data_reduction_details           ? 
_reflns.data_reduction_method            ? 
_reflns.d_resolution_high                1.120 
_reflns.d_resolution_low                 41.196 
_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                       86201 
_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             94.300 
_reflns.R_free_details                   ? 
_reflns.Rmerge_F_all                     ? 
_reflns.Rmerge_F_obs                     ? 
_reflns.Friedel_coverage                 ? 
_reflns.number_gt                        ? 
_reflns.threshold_expression             ? 
_reflns.pdbx_redundancy                  6.400 
_reflns.pdbx_Rmerge_I_obs                ? 
_reflns.pdbx_Rmerge_I_all                ? 
_reflns.pdbx_Rsym_value                  0.052 
_reflns.pdbx_netI_over_av_sigmaI         3.664 
_reflns.pdbx_netI_over_sigmaI            28.400 
_reflns.pdbx_res_netI_over_av_sigmaI_2   ? 
_reflns.pdbx_res_netI_over_sigmaI_2      ? 
_reflns.pdbx_chi_squared                 ? 
_reflns.pdbx_scaling_rejects             ? 
_reflns.pdbx_d_res_high_opt              ? 
_reflns.pdbx_d_res_low_opt               ? 
_reflns.pdbx_d_res_opt_method            ? 
_reflns.phase_calculation_details        ? 
_reflns.pdbx_Rrim_I_all                  0.066 
_reflns.pdbx_Rpim_I_all                  0.025 
_reflns.pdbx_d_opt                       ? 
_reflns.pdbx_number_measured_all         ? 
_reflns.pdbx_diffrn_id                   1 
_reflns.pdbx_ordinal                     1 
_reflns.pdbx_CC_half                     ? 
_reflns.pdbx_R_split                     ? 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_measured_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.number_unique_obs 
_reflns_shell.percent_possible_all 
_reflns_shell.percent_possible_obs 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.Rmerge_I_all 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_gt 
_reflns_shell.meanI_over_uI_all 
_reflns_shell.meanI_over_uI_gt 
_reflns_shell.number_measured_gt 
_reflns_shell.number_unique_gt 
_reflns_shell.percent_possible_gt 
_reflns_shell.Rmerge_F_gt 
_reflns_shell.Rmerge_I_gt 
_reflns_shell.pdbx_redundancy 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_netI_over_sigmaI_all 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_rejects 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_CC_half 
_reflns_shell.pdbx_R_split 
1.123 1.180  ? 11.0 ? ? ? ? ? 73.400 ? ? ? ? 0.064 ? ? ? ? ? ? ? ? 5.000 0.064 ? ? ? 0.089 0.038 ? 1  1 ? ? 
1.180 1.260  ? 12.3 ? ? ? ? ? 94.200 ? ? ? ? 0.058 ? ? ? ? ? ? ? ? 5.800 0.058 ? ? ? 0.081 0.032 ? 2  1 ? ? 
1.260 1.340  ? 13.9 ? ? ? ? ? 98.400 ? ? ? ? 0.052 ? ? ? ? ? ? ? ? 6.700 0.052 ? ? ? 0.072 0.028 ? 3  1 ? ? 
1.340 1.450  ? 16.2 ? ? ? ? ? 98.600 ? ? ? ? 0.044 ? ? ? ? ? ? ? ? 6.600 0.044 ? ? ? 0.063 0.024 ? 4  1 ? ? 
1.450 1.590  ? 18.5 ? ? ? ? ? 98.100 ? ? ? ? 0.037 ? ? ? ? ? ? ? ? 6.700 0.037 ? ? ? 0.055 0.021 ? 5  1 ? ? 
1.590 1.780  ? 20.5 ? ? ? ? ? 98.700 ? ? ? ? 0.033 ? ? ? ? ? ? ? ? 6.700 0.033 ? ? ? 0.048 0.018 ? 6  1 ? ? 
1.780 2.050  ? 21.8 ? ? ? ? ? 99.200 ? ? ? ? 0.030 ? ? ? ? ? ? ? ? 6.900 0.030 ? ? ? 0.041 0.015 ? 7  1 ? ? 
2.050 2.510  ? 18.4 ? ? ? ? ? 99.000 ? ? ? ? 0.030 ? ? ? ? ? ? ? ? 6.900 0.030 ? ? ? 0.039 0.015 ? 8  1 ? ? 
2.510 3.550  ? 8.1  ? ? ? ? ? 99.200 ? ? ? ? 0.049 ? ? ? ? ? ? ? ? 6.900 0.049 ? ? ? 0.059 0.022 ? 9  1 ? ? 
3.550 41.196 ? 6.6  ? ? ? ? ? 98.600 ? ? ? ? 0.083 ? ? ? ? ? ? ? ? 6.600 0.083 ? ? ? 0.102 0.039 ? 10 1 ? ? 
# 
_refine.aniso_B[1][1]                            0.5000 
_refine.aniso_B[1][2]                            0.0000 
_refine.aniso_B[1][3]                            0.0700 
_refine.aniso_B[2][2]                            -0.5300 
_refine.aniso_B[2][3]                            0.0000 
_refine.aniso_B[3][3]                            0.0000 
_refine.B_iso_max                                143.740 
_refine.B_iso_mean                               16.1384 
_refine.B_iso_min                                5.310 
_refine.correlation_coeff_Fo_to_Fc               0.9660 
_refine.correlation_coeff_Fo_to_Fc_free          0.9570 
_refine.details                                  
'HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT U VALUES      : REFINED INDIVIDUALLY' 
_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                                 6G6T 
_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                            1.1200 
_refine.ls_d_res_low                             39.7100 
_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                     86179 
_refine.ls_number_reflns_R_free                  8706 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    94.3000 
_refine.ls_percent_reflns_R_free                 10.1000 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1467 
_refine.ls_R_factor_R_free                       0.1774 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1433 
_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                    ? 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_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                          0.000 
_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               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      4HT0 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.0360 
_refine.pdbx_overall_ESU_R_Free                  0.0380 
_refine.pdbx_solvent_vdw_probe_radii             1.4000 
_refine.pdbx_solvent_ion_probe_radii             0.8000 
_refine.pdbx_solvent_shrinkage_radii             0.8000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_R_Cruickshank_DPI             0.0365 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        2034 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         35 
_refine_hist.number_atoms_solvent             328 
_refine_hist.number_atoms_total               2397 
_refine_hist.d_res_high                       1.1200 
_refine_hist.d_res_low                        39.7100 
# 
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' ? 0.030  0.019  2265 ? r_bond_refined_d       ? ? 
'X-RAY DIFFRACTION' ? 2.837  1.961  3092 ? r_angle_refined_deg    ? ? 
'X-RAY DIFFRACTION' ? 6.107  5.000  283  ? r_dihedral_angle_1_deg ? ? 
'X-RAY DIFFRACTION' ? 35.000 24.660 103  ? r_dihedral_angle_2_deg ? ? 
'X-RAY DIFFRACTION' ? 13.910 15.000 371  ? r_dihedral_angle_3_deg ? ? 
'X-RAY DIFFRACTION' ? 19.480 15.000 8    ? r_dihedral_angle_4_deg ? ? 
'X-RAY DIFFRACTION' ? 0.185  0.200  319  ? r_chiral_restr         ? ? 
'X-RAY DIFFRACTION' ? 0.018  0.021  1781 ? r_gen_planes_refined   ? ? 
'X-RAY DIFFRACTION' ? 2.343  1.206  1097 ? r_mcbond_it            ? ? 
'X-RAY DIFFRACTION' ? 2.502  1.823  1391 ? r_mcangle_it           ? ? 
'X-RAY DIFFRACTION' ? 3.742  1.504  1168 ? r_scbond_it            ? ? 
'X-RAY DIFFRACTION' ? 10.839 3.000  2265 ? r_rigid_bond_restr     ? ? 
'X-RAY DIFFRACTION' ? 22.362 5.000  170  ? r_sphericity_free      ? ? 
'X-RAY DIFFRACTION' ? 14.823 5.000  2351 ? r_sphericity_bonded    ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.1230 
_refine_ls_shell.d_res_low                        1.1520 
_refine_ls_shell.number_reflns_all                4208 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             415 
_refine_ls_shell.number_reflns_R_work             3793 
_refine_ls_shell.percent_reflns_obs               62.4100 
_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                  0.1830 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.1380 
_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_total_number_of_bins_used   20 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
# 
_struct.entry_id                     6G6T 
_struct.title                        
'Crystal structure of human carbonic anhydrase isozyme II with N-butyl-2,4-dichloro-5-sulfamoyl-benzamide' 
_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        6G6T 
_struct_keywords.text            
'drug design, carbonic anhydrase, benzenesulfonamide, metal-binding, lyase-lyase inhibitor comple, lyase' 
_struct_keywords.pdbx_keywords   LYASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 5 ? 
F N N 6 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    CAH2_HUMAN 
_struct_ref.pdbx_db_accession          P00918 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLK
GGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              6G6T 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 260 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P00918 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  260 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       261 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
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)' 490   ? 
1 MORE         4     ? 
1 'SSA (A^2)'  11270 ? 
# 
_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 
# 
_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 GLY A 12  ? ASP A 19  ? GLY A 12  ASP A 19  5 ? 8 
HELX_P HELX_P2 AA2 PHE A 20  ? GLY A 25  ? PHE A 20  GLY A 25  5 ? 6 
HELX_P HELX_P3 AA3 LYS A 126 ? GLY A 128 ? LYS A 127 GLY A 129 5 ? 3 
HELX_P HELX_P4 AA4 ASP A 129 ? VAL A 134 ? ASP A 130 VAL A 135 1 ? 6 
HELX_P HELX_P5 AA5 LYS A 153 ? GLY A 155 ? LYS A 154 GLY A 156 5 ? 3 
HELX_P HELX_P6 AA6 LEU A 156 ? LEU A 163 ? LEU A 157 LEU A 164 1 ? 8 
HELX_P HELX_P7 AA7 ASP A 164 ? LYS A 167 ? ASP A 165 LYS A 168 5 ? 4 
HELX_P HELX_P8 AA8 ASP A 179 ? LEU A 184 ? ASP A 180 LEU A 185 5 ? 6 
HELX_P HELX_P9 AA9 SER A 218 ? ARG A 226 ? SER A 219 ARG A 227 1 ? 9 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A HIS 94  NE2 ? ? ? 1_555 B ZN  . ZN ? ? A HIS 94  A ZN  301 1_555 ? ? ? ? ? ? ? 2.007 ? ? 
metalc2 metalc ? ? A HIS 96  NE2 ? ? ? 1_555 B ZN  . ZN ? ? A HIS 96  A ZN  301 1_555 ? ? ? ? ? ? ? 2.016 ? ? 
metalc3 metalc ? ? A HIS 119 ND1 ? ? ? 1_555 B ZN  . ZN ? ? A HIS 119 A ZN  301 1_555 ? ? ? ? ? ? ? 2.016 ? ? 
metalc4 metalc ? ? B ZN  .   ZN  ? ? ? 1_555 E ENN . N8 ? ? A ZN  301 A ENN 304 1_555 ? ? ? ? ? ? ? 1.948 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1 NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 103.9 ? 
2 NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 112.7 ? 
3 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 98.9  ? 
4 NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N8  ? E ENN .   ? A ENN 304 ? 1_555 109.8 ? 
5 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N8  ? E ENN .   ? A ENN 304 ? 1_555 115.3 ? 
6 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N8  ? E ENN .   ? A ENN 304 ? 1_555 115.4 ? 
# 
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 SER 29  A . ? SER 29  A PRO 30  A ? PRO 30  A 1 -2.70 
2 PRO 200 A . ? PRO 201 A PRO 201 A ? PRO 202 A 1 11.18 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2  ? 
AA2 ? 10 ? 
AA3 ? 6  ? 
# 
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  ? parallel      
AA2 1 2  ? parallel      
AA2 2 3  ? anti-parallel 
AA2 3 4  ? anti-parallel 
AA2 4 5  ? parallel      
AA2 5 6  ? anti-parallel 
AA2 6 7  ? anti-parallel 
AA2 7 8  ? anti-parallel 
AA2 8 9  ? anti-parallel 
AA2 9 10 ? 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  ? 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  ASP A 32  ? ILE A 33  ? ASP A 32  ILE A 33  
AA1 2  THR A 108 ? VAL A 109 ? THR A 108 VAL A 109 
AA2 1  LYS A 39  ? TYR A 40  ? LYS A 39  TYR A 40  
AA2 2  LYS A 256 ? ALA A 257 ? LYS A 257 ALA A 258 
AA2 3  TYR A 190 ? GLY A 195 ? TYR A 191 GLY A 196 
AA2 4  VAL A 206 ? LEU A 211 ? VAL A 207 LEU A 212 
AA2 5  LEU A 140 ? VAL A 149 ? LEU A 141 VAL A 150 
AA2 6  ALA A 116 ? ASN A 124 ? ALA A 116 ASN A 124 
AA2 7  TYR A 88  ? TRP A 97  ? TYR A 88  TRP A 97  
AA2 8  PHE A 66  ? PHE A 70  ? PHE A 66  PHE A 70  
AA2 9  SER A 56  ? ASN A 61  ? SER A 56  ASN A 61  
AA2 10 SER A 172 ? ASP A 174 ? SER A 173 ASP A 175 
AA3 1  LEU A 47  ? SER A 50  ? LEU A 47  SER A 50  
AA3 2  VAL A 78  ? GLY A 81  ? VAL A 78  GLY A 81  
AA3 3  TYR A 88  ? TRP A 97  ? TYR A 88  TRP A 97  
AA3 4  ALA A 116 ? ASN A 124 ? ALA A 116 ASN A 124 
AA3 5  LEU A 140 ? VAL A 149 ? LEU A 141 VAL A 150 
AA3 6  ILE A 215 ? VAL A 217 ? ILE A 216 VAL A 218 
# 
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  N ILE A 33  ? N ILE A 33  O THR A 108 ? O THR A 108 
AA2 1 2  N LYS A 39  ? N LYS A 39  O ALA A 257 ? O ALA A 258 
AA2 2 3  O LYS A 256 ? O LYS A 257 N THR A 192 ? N THR A 193 
AA2 3 4  N GLY A 195 ? N GLY A 196 O VAL A 206 ? O VAL A 207 
AA2 4 5  O ILE A 209 ? O ILE A 210 N GLY A 144 ? N GLY A 145 
AA2 5 6  O ILE A 145 ? O ILE A 146 N LEU A 118 ? N LEU A 118 
AA2 6 7  O HIS A 119 ? O HIS A 119 N HIS A 94  ? N HIS A 94  
AA2 7 8  O PHE A 93  ? O PHE A 93  N VAL A 68  ? N VAL A 68  
AA2 8 9  O GLU A 69  ? O GLU A 69  N ARG A 58  ? N ARG A 58  
AA2 9 10 N ILE A 59  ? N ILE A 59  O ALA A 173 ? O ALA A 174 
AA3 1 2  N SER A 48  ? N SER A 48  O LYS A 80  ? O LYS A 80  
AA3 2 3  N LEU A 79  ? N LEU A 79  O TYR A 88  ? O TYR A 88  
AA3 3 4  N HIS A 94  ? N HIS A 94  O HIS A 119 ? O HIS A 119 
AA3 4 5  N LEU A 118 ? N LEU A 118 O ILE A 145 ? O ILE A 146 
AA3 5 6  N PHE A 146 ? N PHE A 147 O ILE A 215 ? O ILE A 216 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software A ZN  301 ? 4  'binding site for residue ZN A 301'  
AC2 Software A DMS 302 ? 5  'binding site for residue DMS A 302' 
AC3 Software A BCN 303 ? 9  'binding site for residue BCN A 303' 
AC4 Software A ENN 304 ? 13 'binding site for residue ENN A 304' 
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1  AC1 4  HIS A 94  ? HIS A 94  . ? 1_555 ? 
2  AC1 4  HIS A 96  ? HIS A 96  . ? 1_555 ? 
3  AC1 4  HIS A 119 ? HIS A 119 . ? 1_555 ? 
4  AC1 4  ENN E .   ? ENN A 304 . ? 1_555 ? 
5  AC2 5  TYR A 7   ? TYR A 7   . ? 1_555 ? 
6  AC2 5  ASP A 242 ? ASP A 243 . ? 1_555 ? 
7  AC2 5  TRP A 244 ? TRP A 245 . ? 1_555 ? 
8  AC2 5  PRO A 246 ? PRO A 247 . ? 1_555 ? 
9  AC2 5  HOH F .   ? HOH A 683 . ? 1_555 ? 
10 AC3 9  LYS A 148 ? LYS A 149 . ? 1_555 ? 
11 AC3 9  LYS A 212 ? LYS A 213 . ? 1_555 ? 
12 AC3 9  GLU A 213 ? GLU A 214 . ? 1_555 ? 
13 AC3 9  PRO A 214 ? PRO A 215 . ? 1_555 ? 
14 AC3 9  HOH F .   ? HOH A 464 . ? 1_555 ? 
15 AC3 9  HOH F .   ? HOH A 479 . ? 1_555 ? 
16 AC3 9  HOH F .   ? HOH A 497 . ? 1_555 ? 
17 AC3 9  HOH F .   ? HOH A 515 . ? 1_555 ? 
18 AC3 9  HOH F .   ? HOH A 570 . ? 1_555 ? 
19 AC4 13 GLN A 92  ? GLN A 92  . ? 1_555 ? 
20 AC4 13 HIS A 94  ? HIS A 94  . ? 1_555 ? 
21 AC4 13 HIS A 96  ? HIS A 96  . ? 1_555 ? 
22 AC4 13 HIS A 119 ? HIS A 119 . ? 1_555 ? 
23 AC4 13 LEU A 140 ? LEU A 141 . ? 1_555 ? 
24 AC4 13 VAL A 142 ? VAL A 143 . ? 1_555 ? 
25 AC4 13 LEU A 197 ? LEU A 198 . ? 1_555 ? 
26 AC4 13 THR A 198 ? THR A 199 . ? 1_555 ? 
27 AC4 13 THR A 199 ? THR A 200 . ? 1_555 ? 
28 AC4 13 TRP A 208 ? TRP A 209 . ? 1_555 ? 
29 AC4 13 ZN  B .   ? ZN  A 301 . ? 1_555 ? 
30 AC4 13 HOH F .   ? HOH A 428 . ? 1_555 ? 
31 AC4 13 HOH F .   ? HOH A 540 . ? 1_555 ? 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 OE1 A GLU 214 ? B O A HOH 401 ? ? 1.92 
2 1 CG  A ARG 89  ? A O A HOH 633 ? ? 2.01 
3 1 NH2 A ARG 89  ? B O A HOH 402 ? ? 2.18 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 CD A LYS 39  ? B CE A LYS 39  ? B NZ A LYS 39  ? B 97.75  111.70 -13.95 2.30 N 
2 1 CA A LEU 57  ? ? CB A LEU 57  ? ? CG A LEU 57  ? ? 130.09 115.30 14.79  2.30 N 
3 1 CD A LYS 154 ? ? CE A LYS 154 ? ? NZ A LYS 154 ? ? 96.78  111.70 -14.92 2.30 N 
4 1 CD A LYS 168 ? ? CE A LYS 168 ? ? NZ A LYS 168 ? ? 90.71  111.70 -20.99 2.30 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 11  ? ? -140.63 17.74   
2 1 ARG A 27  ? ? -144.08 58.61   
3 1 LYS A 76  ? ? -121.39 -55.61  
4 1 GLU A 106 ? ? -90.79  -60.72  
5 1 LYS A 111 ? ? 73.72   -1.40   
6 1 ASN A 244 ? ? -95.40  46.42   
7 1 LYS A 252 ? ? 56.15   -136.25 
# 
loop_
_pdbx_validate_main_chain_plane.id 
_pdbx_validate_main_chain_plane.PDB_model_num 
_pdbx_validate_main_chain_plane.auth_comp_id 
_pdbx_validate_main_chain_plane.auth_asym_id 
_pdbx_validate_main_chain_plane.auth_seq_id 
_pdbx_validate_main_chain_plane.PDB_ins_code 
_pdbx_validate_main_chain_plane.label_alt_id 
_pdbx_validate_main_chain_plane.improper_torsion_angle 
1 1 LYS A 76 ? ? 10.66  
2 1 GLY A 86 ? ? -15.52 
3 1 GLY A 86 ? ? -17.32 
# 
_phasing.method   MR 
# 
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 727 ? 5.82 . 
2 1 O ? A HOH 728 ? 6.21 . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A MET 1 ? A MET 1 
2 1 Y 1 A SER 2 ? A SER 2 
3 1 Y 1 A HIS 3 ? A HIS 3 
# 
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  
BCN N1   N  N N 74  
BCN C1   C  N N 75  
BCN C2   C  N N 76  
BCN O21  O  N N 77  
BCN O22  O  N N 78  
BCN C3   C  N N 79  
BCN C4   C  N N 80  
BCN O4   O  N N 81  
BCN C5   C  N N 82  
BCN C6   C  N N 83  
BCN O6   O  N N 84  
BCN H11  H  N N 85  
BCN H12  H  N N 86  
BCN HO2  H  N N 87  
BCN H31  H  N N 88  
BCN H32  H  N N 89  
BCN H41  H  N N 90  
BCN H42  H  N N 91  
BCN HO4  H  N N 92  
BCN H51  H  N N 93  
BCN H52  H  N N 94  
BCN H61  H  N N 95  
BCN H62  H  N N 96  
BCN HO6  H  N N 97  
CYS N    N  N N 98  
CYS CA   C  N R 99  
CYS C    C  N N 100 
CYS O    O  N N 101 
CYS CB   C  N N 102 
CYS SG   S  N N 103 
CYS OXT  O  N N 104 
CYS H    H  N N 105 
CYS H2   H  N N 106 
CYS HA   H  N N 107 
CYS HB2  H  N N 108 
CYS HB3  H  N N 109 
CYS HG   H  N N 110 
CYS HXT  H  N N 111 
DMS S    S  N N 112 
DMS O    O  N N 113 
DMS C1   C  N N 114 
DMS C2   C  N N 115 
DMS H11  H  N N 116 
DMS H12  H  N N 117 
DMS H13  H  N N 118 
DMS H21  H  N N 119 
DMS H22  H  N N 120 
DMS H23  H  N N 121 
ENN C5   C  Y N 122 
ENN C4   C  Y N 123 
ENN C6   C  Y N 124 
ENN C2   C  Y N 125 
ENN O14  O  N N 126 
ENN C13  C  N N 127 
ENN N15  N  N N 128 
ENN C16  C  N N 129 
ENN C17  C  N N 130 
ENN C18  C  N N 131 
ENN C19  C  N N 132 
ENN C3   C  Y N 133 
ENN CL1  CL N N 134 
ENN C1   C  Y N 135 
ENN CL2  CL N N 136 
ENN S7   S  N N 137 
ENN O9   O  N N 138 
ENN O10  O  N N 139 
ENN N8   N  N N 140 
ENN H1   H  N N 141 
ENN H2   H  N N 142 
ENN H3   H  N N 143 
ENN H4   H  N N 144 
ENN H5   H  N N 145 
ENN H6   H  N N 146 
ENN H7   H  N N 147 
ENN H8   H  N N 148 
ENN H9   H  N N 149 
ENN H10  H  N N 150 
ENN H11  H  N N 151 
ENN H12  H  N N 152 
ENN H13  H  N N 153 
ENN H14  H  N N 154 
GLN N    N  N N 155 
GLN CA   C  N S 156 
GLN C    C  N N 157 
GLN O    O  N N 158 
GLN CB   C  N N 159 
GLN CG   C  N N 160 
GLN CD   C  N N 161 
GLN OE1  O  N N 162 
GLN NE2  N  N N 163 
GLN OXT  O  N N 164 
GLN H    H  N N 165 
GLN H2   H  N N 166 
GLN HA   H  N N 167 
GLN HB2  H  N N 168 
GLN HB3  H  N N 169 
GLN HG2  H  N N 170 
GLN HG3  H  N N 171 
GLN HE21 H  N N 172 
GLN HE22 H  N N 173 
GLN HXT  H  N N 174 
GLU N    N  N N 175 
GLU CA   C  N S 176 
GLU C    C  N N 177 
GLU O    O  N N 178 
GLU CB   C  N N 179 
GLU CG   C  N N 180 
GLU CD   C  N N 181 
GLU OE1  O  N N 182 
GLU OE2  O  N N 183 
GLU OXT  O  N N 184 
GLU H    H  N N 185 
GLU H2   H  N N 186 
GLU HA   H  N N 187 
GLU HB2  H  N N 188 
GLU HB3  H  N N 189 
GLU HG2  H  N N 190 
GLU HG3  H  N N 191 
GLU HE2  H  N N 192 
GLU HXT  H  N N 193 
GLY N    N  N N 194 
GLY CA   C  N N 195 
GLY C    C  N N 196 
GLY O    O  N N 197 
GLY OXT  O  N N 198 
GLY H    H  N N 199 
GLY H2   H  N N 200 
GLY HA2  H  N N 201 
GLY HA3  H  N N 202 
GLY HXT  H  N N 203 
HIS N    N  N N 204 
HIS CA   C  N S 205 
HIS C    C  N N 206 
HIS O    O  N N 207 
HIS CB   C  N N 208 
HIS CG   C  Y N 209 
HIS ND1  N  Y N 210 
HIS CD2  C  Y N 211 
HIS CE1  C  Y N 212 
HIS NE2  N  Y N 213 
HIS OXT  O  N N 214 
HIS H    H  N N 215 
HIS H2   H  N N 216 
HIS HA   H  N N 217 
HIS HB2  H  N N 218 
HIS HB3  H  N N 219 
HIS HD1  H  N N 220 
HIS HD2  H  N N 221 
HIS HE1  H  N N 222 
HIS HE2  H  N N 223 
HIS HXT  H  N N 224 
HOH O    O  N N 225 
HOH H1   H  N N 226 
HOH H2   H  N N 227 
ILE N    N  N N 228 
ILE CA   C  N S 229 
ILE C    C  N N 230 
ILE O    O  N N 231 
ILE CB   C  N S 232 
ILE CG1  C  N N 233 
ILE CG2  C  N N 234 
ILE CD1  C  N N 235 
ILE OXT  O  N N 236 
ILE H    H  N N 237 
ILE H2   H  N N 238 
ILE HA   H  N N 239 
ILE HB   H  N N 240 
ILE HG12 H  N N 241 
ILE HG13 H  N N 242 
ILE HG21 H  N N 243 
ILE HG22 H  N N 244 
ILE HG23 H  N N 245 
ILE HD11 H  N N 246 
ILE HD12 H  N N 247 
ILE HD13 H  N N 248 
ILE HXT  H  N N 249 
LEU N    N  N N 250 
LEU CA   C  N S 251 
LEU C    C  N N 252 
LEU O    O  N N 253 
LEU CB   C  N N 254 
LEU CG   C  N N 255 
LEU CD1  C  N N 256 
LEU CD2  C  N N 257 
LEU OXT  O  N N 258 
LEU H    H  N N 259 
LEU H2   H  N N 260 
LEU HA   H  N N 261 
LEU HB2  H  N N 262 
LEU HB3  H  N N 263 
LEU HG   H  N N 264 
LEU HD11 H  N N 265 
LEU HD12 H  N N 266 
LEU HD13 H  N N 267 
LEU HD21 H  N N 268 
LEU HD22 H  N N 269 
LEU HD23 H  N N 270 
LEU HXT  H  N N 271 
LYS N    N  N N 272 
LYS CA   C  N S 273 
LYS C    C  N N 274 
LYS O    O  N N 275 
LYS CB   C  N N 276 
LYS CG   C  N N 277 
LYS CD   C  N N 278 
LYS CE   C  N N 279 
LYS NZ   N  N N 280 
LYS OXT  O  N N 281 
LYS H    H  N N 282 
LYS H2   H  N N 283 
LYS HA   H  N N 284 
LYS HB2  H  N N 285 
LYS HB3  H  N N 286 
LYS HG2  H  N N 287 
LYS HG3  H  N N 288 
LYS HD2  H  N N 289 
LYS HD3  H  N N 290 
LYS HE2  H  N N 291 
LYS HE3  H  N N 292 
LYS HZ1  H  N N 293 
LYS HZ2  H  N N 294 
LYS HZ3  H  N N 295 
LYS HXT  H  N N 296 
MET N    N  N N 297 
MET CA   C  N S 298 
MET C    C  N N 299 
MET O    O  N N 300 
MET CB   C  N N 301 
MET CG   C  N N 302 
MET SD   S  N N 303 
MET CE   C  N N 304 
MET OXT  O  N N 305 
MET H    H  N N 306 
MET H2   H  N N 307 
MET HA   H  N N 308 
MET HB2  H  N N 309 
MET HB3  H  N N 310 
MET HG2  H  N N 311 
MET HG3  H  N N 312 
MET HE1  H  N N 313 
MET HE2  H  N N 314 
MET HE3  H  N N 315 
MET HXT  H  N N 316 
PHE N    N  N N 317 
PHE CA   C  N S 318 
PHE C    C  N N 319 
PHE O    O  N N 320 
PHE CB   C  N N 321 
PHE CG   C  Y N 322 
PHE CD1  C  Y N 323 
PHE CD2  C  Y N 324 
PHE CE1  C  Y N 325 
PHE CE2  C  Y N 326 
PHE CZ   C  Y N 327 
PHE OXT  O  N N 328 
PHE H    H  N N 329 
PHE H2   H  N N 330 
PHE HA   H  N N 331 
PHE HB2  H  N N 332 
PHE HB3  H  N N 333 
PHE HD1  H  N N 334 
PHE HD2  H  N N 335 
PHE HE1  H  N N 336 
PHE HE2  H  N N 337 
PHE HZ   H  N N 338 
PHE HXT  H  N N 339 
PRO N    N  N N 340 
PRO CA   C  N S 341 
PRO C    C  N N 342 
PRO O    O  N N 343 
PRO CB   C  N N 344 
PRO CG   C  N N 345 
PRO CD   C  N N 346 
PRO OXT  O  N N 347 
PRO H    H  N N 348 
PRO HA   H  N N 349 
PRO HB2  H  N N 350 
PRO HB3  H  N N 351 
PRO HG2  H  N N 352 
PRO HG3  H  N N 353 
PRO HD2  H  N N 354 
PRO HD3  H  N N 355 
PRO HXT  H  N N 356 
SER N    N  N N 357 
SER CA   C  N S 358 
SER C    C  N N 359 
SER O    O  N N 360 
SER CB   C  N N 361 
SER OG   O  N N 362 
SER OXT  O  N N 363 
SER H    H  N N 364 
SER H2   H  N N 365 
SER HA   H  N N 366 
SER HB2  H  N N 367 
SER HB3  H  N N 368 
SER HG   H  N N 369 
SER HXT  H  N N 370 
THR N    N  N N 371 
THR CA   C  N S 372 
THR C    C  N N 373 
THR O    O  N N 374 
THR CB   C  N R 375 
THR OG1  O  N N 376 
THR CG2  C  N N 377 
THR OXT  O  N N 378 
THR H    H  N N 379 
THR H2   H  N N 380 
THR HA   H  N N 381 
THR HB   H  N N 382 
THR HG1  H  N N 383 
THR HG21 H  N N 384 
THR HG22 H  N N 385 
THR HG23 H  N N 386 
THR HXT  H  N N 387 
TRP N    N  N N 388 
TRP CA   C  N S 389 
TRP C    C  N N 390 
TRP O    O  N N 391 
TRP CB   C  N N 392 
TRP CG   C  Y N 393 
TRP CD1  C  Y N 394 
TRP CD2  C  Y N 395 
TRP NE1  N  Y N 396 
TRP CE2  C  Y N 397 
TRP CE3  C  Y N 398 
TRP CZ2  C  Y N 399 
TRP CZ3  C  Y N 400 
TRP CH2  C  Y N 401 
TRP OXT  O  N N 402 
TRP H    H  N N 403 
TRP H2   H  N N 404 
TRP HA   H  N N 405 
TRP HB2  H  N N 406 
TRP HB3  H  N N 407 
TRP HD1  H  N N 408 
TRP HE1  H  N N 409 
TRP HE3  H  N N 410 
TRP HZ2  H  N N 411 
TRP HZ3  H  N N 412 
TRP HH2  H  N N 413 
TRP HXT  H  N N 414 
TYR N    N  N N 415 
TYR CA   C  N S 416 
TYR C    C  N N 417 
TYR O    O  N N 418 
TYR CB   C  N N 419 
TYR CG   C  Y N 420 
TYR CD1  C  Y N 421 
TYR CD2  C  Y N 422 
TYR CE1  C  Y N 423 
TYR CE2  C  Y N 424 
TYR CZ   C  Y N 425 
TYR OH   O  N N 426 
TYR OXT  O  N N 427 
TYR H    H  N N 428 
TYR H2   H  N N 429 
TYR HA   H  N N 430 
TYR HB2  H  N N 431 
TYR HB3  H  N N 432 
TYR HD1  H  N N 433 
TYR HD2  H  N N 434 
TYR HE1  H  N N 435 
TYR HE2  H  N N 436 
TYR HH   H  N N 437 
TYR HXT  H  N N 438 
VAL N    N  N N 439 
VAL CA   C  N S 440 
VAL C    C  N N 441 
VAL O    O  N N 442 
VAL CB   C  N N 443 
VAL CG1  C  N N 444 
VAL CG2  C  N N 445 
VAL OXT  O  N N 446 
VAL H    H  N N 447 
VAL H2   H  N N 448 
VAL HA   H  N N 449 
VAL HB   H  N N 450 
VAL HG11 H  N N 451 
VAL HG12 H  N N 452 
VAL HG13 H  N N 453 
VAL HG21 H  N N 454 
VAL HG22 H  N N 455 
VAL HG23 H  N N 456 
VAL HXT  H  N N 457 
ZN  ZN   ZN N N 458 
# 
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  
BCN N1  C1   sing N N 70  
BCN N1  C3   sing N N 71  
BCN N1  C5   sing N N 72  
BCN C1  C2   sing N N 73  
BCN C1  H11  sing N N 74  
BCN C1  H12  sing N N 75  
BCN C2  O21  doub N N 76  
BCN C2  O22  sing N N 77  
BCN O22 HO2  sing N N 78  
BCN C3  C4   sing N N 79  
BCN C3  H31  sing N N 80  
BCN C3  H32  sing N N 81  
BCN C4  O4   sing N N 82  
BCN C4  H41  sing N N 83  
BCN C4  H42  sing N N 84  
BCN O4  HO4  sing N N 85  
BCN C5  C6   sing N N 86  
BCN C5  H51  sing N N 87  
BCN C5  H52  sing N N 88  
BCN C6  O6   sing N N 89  
BCN C6  H61  sing N N 90  
BCN C6  H62  sing N N 91  
BCN O6  HO6  sing N N 92  
CYS N   CA   sing N N 93  
CYS N   H    sing N N 94  
CYS N   H2   sing N N 95  
CYS CA  C    sing N N 96  
CYS CA  CB   sing N N 97  
CYS CA  HA   sing N N 98  
CYS C   O    doub N N 99  
CYS C   OXT  sing N N 100 
CYS CB  SG   sing N N 101 
CYS CB  HB2  sing N N 102 
CYS CB  HB3  sing N N 103 
CYS SG  HG   sing N N 104 
CYS OXT HXT  sing N N 105 
DMS S   O    doub N N 106 
DMS S   C1   sing N N 107 
DMS S   C2   sing N N 108 
DMS C1  H11  sing N N 109 
DMS C1  H12  sing N N 110 
DMS C1  H13  sing N N 111 
DMS C2  H21  sing N N 112 
DMS C2  H22  sing N N 113 
DMS C2  H23  sing N N 114 
ENN CL2 C1   sing N N 115 
ENN CL1 C3   sing N N 116 
ENN C2  C1   doub Y N 117 
ENN C2  C3   sing Y N 118 
ENN C1  C6   sing Y N 119 
ENN C3  C4   doub Y N 120 
ENN C6  C5   doub Y N 121 
ENN C6  S7   sing N N 122 
ENN C4  C5   sing Y N 123 
ENN C4  C13  sing N N 124 
ENN C18 C17  sing N N 125 
ENN C18 C19  sing N N 126 
ENN O9  S7   doub N N 127 
ENN N15 C13  sing N N 128 
ENN N15 C16  sing N N 129 
ENN C17 C16  sing N N 130 
ENN C13 O14  doub N N 131 
ENN S7  O10  doub N N 132 
ENN S7  N8   sing N N 133 
ENN C5  H1   sing N N 134 
ENN C2  H2   sing N N 135 
ENN N15 H3   sing N N 136 
ENN C16 H4   sing N N 137 
ENN C16 H5   sing N N 138 
ENN C17 H6   sing N N 139 
ENN C17 H7   sing N N 140 
ENN C18 H8   sing N N 141 
ENN C18 H9   sing N N 142 
ENN C19 H10  sing N N 143 
ENN C19 H11  sing N N 144 
ENN C19 H12  sing N N 145 
ENN N8  H13  sing N N 146 
ENN N8  H14  sing N N 147 
GLN N   CA   sing N N 148 
GLN N   H    sing N N 149 
GLN N   H2   sing N N 150 
GLN CA  C    sing N N 151 
GLN CA  CB   sing N N 152 
GLN CA  HA   sing N N 153 
GLN C   O    doub N N 154 
GLN C   OXT  sing N N 155 
GLN CB  CG   sing N N 156 
GLN CB  HB2  sing N N 157 
GLN CB  HB3  sing N N 158 
GLN CG  CD   sing N N 159 
GLN CG  HG2  sing N N 160 
GLN CG  HG3  sing N N 161 
GLN CD  OE1  doub N N 162 
GLN CD  NE2  sing N N 163 
GLN NE2 HE21 sing N N 164 
GLN NE2 HE22 sing N N 165 
GLN OXT HXT  sing N N 166 
GLU N   CA   sing N N 167 
GLU N   H    sing N N 168 
GLU N   H2   sing N N 169 
GLU CA  C    sing N N 170 
GLU CA  CB   sing N N 171 
GLU CA  HA   sing N N 172 
GLU C   O    doub N N 173 
GLU C   OXT  sing N N 174 
GLU CB  CG   sing N N 175 
GLU CB  HB2  sing N N 176 
GLU CB  HB3  sing N N 177 
GLU CG  CD   sing N N 178 
GLU CG  HG2  sing N N 179 
GLU CG  HG3  sing N N 180 
GLU CD  OE1  doub N N 181 
GLU CD  OE2  sing N N 182 
GLU OE2 HE2  sing N N 183 
GLU OXT HXT  sing N N 184 
GLY N   CA   sing N N 185 
GLY N   H    sing N N 186 
GLY N   H2   sing N N 187 
GLY CA  C    sing N N 188 
GLY CA  HA2  sing N N 189 
GLY CA  HA3  sing N N 190 
GLY C   O    doub N N 191 
GLY C   OXT  sing N N 192 
GLY OXT HXT  sing N N 193 
HIS N   CA   sing N N 194 
HIS N   H    sing N N 195 
HIS N   H2   sing N N 196 
HIS CA  C    sing N N 197 
HIS CA  CB   sing N N 198 
HIS CA  HA   sing N N 199 
HIS C   O    doub N N 200 
HIS C   OXT  sing N N 201 
HIS CB  CG   sing N N 202 
HIS CB  HB2  sing N N 203 
HIS CB  HB3  sing N N 204 
HIS CG  ND1  sing Y N 205 
HIS CG  CD2  doub Y N 206 
HIS ND1 CE1  doub Y N 207 
HIS ND1 HD1  sing N N 208 
HIS CD2 NE2  sing Y N 209 
HIS CD2 HD2  sing N N 210 
HIS CE1 NE2  sing Y N 211 
HIS CE1 HE1  sing N N 212 
HIS NE2 HE2  sing N N 213 
HIS OXT HXT  sing N N 214 
HOH O   H1   sing N N 215 
HOH O   H2   sing N N 216 
ILE N   CA   sing N N 217 
ILE N   H    sing N N 218 
ILE N   H2   sing N N 219 
ILE CA  C    sing N N 220 
ILE CA  CB   sing N N 221 
ILE CA  HA   sing N N 222 
ILE C   O    doub N N 223 
ILE C   OXT  sing N N 224 
ILE CB  CG1  sing N N 225 
ILE CB  CG2  sing N N 226 
ILE CB  HB   sing N N 227 
ILE CG1 CD1  sing N N 228 
ILE CG1 HG12 sing N N 229 
ILE CG1 HG13 sing N N 230 
ILE CG2 HG21 sing N N 231 
ILE CG2 HG22 sing N N 232 
ILE CG2 HG23 sing N N 233 
ILE CD1 HD11 sing N N 234 
ILE CD1 HD12 sing N N 235 
ILE CD1 HD13 sing N N 236 
ILE OXT HXT  sing N N 237 
LEU N   CA   sing N N 238 
LEU N   H    sing N N 239 
LEU N   H2   sing N N 240 
LEU CA  C    sing N N 241 
LEU CA  CB   sing N N 242 
LEU CA  HA   sing N N 243 
LEU C   O    doub N N 244 
LEU C   OXT  sing N N 245 
LEU CB  CG   sing N N 246 
LEU CB  HB2  sing N N 247 
LEU CB  HB3  sing N N 248 
LEU CG  CD1  sing N N 249 
LEU CG  CD2  sing N N 250 
LEU CG  HG   sing N N 251 
LEU CD1 HD11 sing N N 252 
LEU CD1 HD12 sing N N 253 
LEU CD1 HD13 sing N N 254 
LEU CD2 HD21 sing N N 255 
LEU CD2 HD22 sing N N 256 
LEU CD2 HD23 sing N N 257 
LEU OXT HXT  sing N N 258 
LYS N   CA   sing N N 259 
LYS N   H    sing N N 260 
LYS N   H2   sing N N 261 
LYS CA  C    sing N N 262 
LYS CA  CB   sing N N 263 
LYS CA  HA   sing N N 264 
LYS C   O    doub N N 265 
LYS C   OXT  sing N N 266 
LYS CB  CG   sing N N 267 
LYS CB  HB2  sing N N 268 
LYS CB  HB3  sing N N 269 
LYS CG  CD   sing N N 270 
LYS CG  HG2  sing N N 271 
LYS CG  HG3  sing N N 272 
LYS CD  CE   sing N N 273 
LYS CD  HD2  sing N N 274 
LYS CD  HD3  sing N N 275 
LYS CE  NZ   sing N N 276 
LYS CE  HE2  sing N N 277 
LYS CE  HE3  sing N N 278 
LYS NZ  HZ1  sing N N 279 
LYS NZ  HZ2  sing N N 280 
LYS NZ  HZ3  sing N N 281 
LYS OXT HXT  sing N N 282 
MET N   CA   sing N N 283 
MET N   H    sing N N 284 
MET N   H2   sing N N 285 
MET CA  C    sing N N 286 
MET CA  CB   sing N N 287 
MET CA  HA   sing N N 288 
MET C   O    doub N N 289 
MET C   OXT  sing N N 290 
MET CB  CG   sing N N 291 
MET CB  HB2  sing N N 292 
MET CB  HB3  sing N N 293 
MET CG  SD   sing N N 294 
MET CG  HG2  sing N N 295 
MET CG  HG3  sing N N 296 
MET SD  CE   sing N N 297 
MET CE  HE1  sing N N 298 
MET CE  HE2  sing N N 299 
MET CE  HE3  sing N N 300 
MET OXT HXT  sing N N 301 
PHE N   CA   sing N N 302 
PHE N   H    sing N N 303 
PHE N   H2   sing N N 304 
PHE CA  C    sing N N 305 
PHE CA  CB   sing N N 306 
PHE CA  HA   sing N N 307 
PHE C   O    doub N N 308 
PHE C   OXT  sing N N 309 
PHE CB  CG   sing N N 310 
PHE CB  HB2  sing N N 311 
PHE CB  HB3  sing N N 312 
PHE CG  CD1  doub Y N 313 
PHE CG  CD2  sing Y N 314 
PHE CD1 CE1  sing Y N 315 
PHE CD1 HD1  sing N N 316 
PHE CD2 CE2  doub Y N 317 
PHE CD2 HD2  sing N N 318 
PHE CE1 CZ   doub Y N 319 
PHE CE1 HE1  sing N N 320 
PHE CE2 CZ   sing Y N 321 
PHE CE2 HE2  sing N N 322 
PHE CZ  HZ   sing N N 323 
PHE OXT HXT  sing N N 324 
PRO N   CA   sing N N 325 
PRO N   CD   sing N N 326 
PRO N   H    sing N N 327 
PRO CA  C    sing N N 328 
PRO CA  CB   sing N N 329 
PRO CA  HA   sing N N 330 
PRO C   O    doub N N 331 
PRO C   OXT  sing N N 332 
PRO CB  CG   sing N N 333 
PRO CB  HB2  sing N N 334 
PRO CB  HB3  sing N N 335 
PRO CG  CD   sing N N 336 
PRO CG  HG2  sing N N 337 
PRO CG  HG3  sing N N 338 
PRO CD  HD2  sing N N 339 
PRO CD  HD3  sing N N 340 
PRO OXT HXT  sing N N 341 
SER N   CA   sing N N 342 
SER N   H    sing N N 343 
SER N   H2   sing N N 344 
SER CA  C    sing N N 345 
SER CA  CB   sing N N 346 
SER CA  HA   sing N N 347 
SER C   O    doub N N 348 
SER C   OXT  sing N N 349 
SER CB  OG   sing N N 350 
SER CB  HB2  sing N N 351 
SER CB  HB3  sing N N 352 
SER OG  HG   sing N N 353 
SER OXT HXT  sing N N 354 
THR N   CA   sing N N 355 
THR N   H    sing N N 356 
THR N   H2   sing N N 357 
THR CA  C    sing N N 358 
THR CA  CB   sing N N 359 
THR CA  HA   sing N N 360 
THR C   O    doub N N 361 
THR C   OXT  sing N N 362 
THR CB  OG1  sing N N 363 
THR CB  CG2  sing N N 364 
THR CB  HB   sing N N 365 
THR OG1 HG1  sing N N 366 
THR CG2 HG21 sing N N 367 
THR CG2 HG22 sing N N 368 
THR CG2 HG23 sing N N 369 
THR OXT HXT  sing N N 370 
TRP N   CA   sing N N 371 
TRP N   H    sing N N 372 
TRP N   H2   sing N N 373 
TRP CA  C    sing N N 374 
TRP CA  CB   sing N N 375 
TRP CA  HA   sing N N 376 
TRP C   O    doub N N 377 
TRP C   OXT  sing N N 378 
TRP CB  CG   sing N N 379 
TRP CB  HB2  sing N N 380 
TRP CB  HB3  sing N N 381 
TRP CG  CD1  doub Y N 382 
TRP CG  CD2  sing Y N 383 
TRP CD1 NE1  sing Y N 384 
TRP CD1 HD1  sing N N 385 
TRP CD2 CE2  doub Y N 386 
TRP CD2 CE3  sing Y N 387 
TRP NE1 CE2  sing Y N 388 
TRP NE1 HE1  sing N N 389 
TRP CE2 CZ2  sing Y N 390 
TRP CE3 CZ3  doub Y N 391 
TRP CE3 HE3  sing N N 392 
TRP CZ2 CH2  doub Y N 393 
TRP CZ2 HZ2  sing N N 394 
TRP CZ3 CH2  sing Y N 395 
TRP CZ3 HZ3  sing N N 396 
TRP CH2 HH2  sing N N 397 
TRP OXT HXT  sing N N 398 
TYR N   CA   sing N N 399 
TYR N   H    sing N N 400 
TYR N   H2   sing N N 401 
TYR CA  C    sing N N 402 
TYR CA  CB   sing N N 403 
TYR CA  HA   sing N N 404 
TYR C   O    doub N N 405 
TYR C   OXT  sing N N 406 
TYR CB  CG   sing N N 407 
TYR CB  HB2  sing N N 408 
TYR CB  HB3  sing N N 409 
TYR CG  CD1  doub Y N 410 
TYR CG  CD2  sing Y N 411 
TYR CD1 CE1  sing Y N 412 
TYR CD1 HD1  sing N N 413 
TYR CD2 CE2  doub Y N 414 
TYR CD2 HD2  sing N N 415 
TYR CE1 CZ   doub Y N 416 
TYR CE1 HE1  sing N N 417 
TYR CE2 CZ   sing Y N 418 
TYR CE2 HE2  sing N N 419 
TYR CZ  OH   sing N N 420 
TYR OH  HH   sing N N 421 
TYR OXT HXT  sing N N 422 
VAL N   CA   sing N N 423 
VAL N   H    sing N N 424 
VAL N   H2   sing N N 425 
VAL CA  C    sing N N 426 
VAL CA  CB   sing N N 427 
VAL CA  HA   sing N N 428 
VAL C   O    doub N N 429 
VAL C   OXT  sing N N 430 
VAL CB  CG1  sing N N 431 
VAL CB  CG2  sing N N 432 
VAL CB  HB   sing N N 433 
VAL CG1 HG11 sing N N 434 
VAL CG1 HG12 sing N N 435 
VAL CG1 HG13 sing N N 436 
VAL CG2 HG21 sing N N 437 
VAL CG2 HG22 sing N N 438 
VAL CG2 HG23 sing N N 439 
VAL OXT HXT  sing N N 440 
# 
_pdbx_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   4HT0 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    6G6T 
_atom_sites.fract_transf_matrix[1][1]   0.023777 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.006013 
_atom_sites.fract_transf_matrix[2][1]   -0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.024274 
_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]   0.014307 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
# 
loop_
_atom_type.symbol 
C  
CL 
N  
O  
S  
ZN 
# 
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   A HIS A 1 4   ? 11.165  -0.668  7.945   0.50 33.20  ? 4   HIS A N   1 
ATOM   2    N  N   B HIS A 1 4   ? 11.111  -0.059  8.072   0.50 28.77  ? 4   HIS A N   1 
ATOM   3    C  CA  A HIS A 1 4   ? 10.068  -0.001  8.690   0.50 24.77  ? 4   HIS A CA  1 
ATOM   4    C  CA  B HIS A 1 4   ? 10.188  0.414   9.148   0.50 24.91  ? 4   HIS A CA  1 
ATOM   5    C  C   A HIS A 1 4   ? 9.185   -1.029  9.460   0.50 17.95  ? 4   HIS A C   1 
ATOM   6    C  C   B HIS A 1 4   ? 9.408   -0.859  9.648   0.50 20.68  ? 4   HIS A C   1 
ATOM   7    O  O   A HIS A 1 4   ? 9.239   -2.286  9.143   0.50 16.81  ? 4   HIS A O   1 
ATOM   8    O  O   B HIS A 1 4   ? 9.732   -2.081  9.322   0.50 22.82  ? 4   HIS A O   1 
ATOM   9    C  CB  A HIS A 1 4   ? 9.216   0.798   7.773   0.50 26.39  ? 4   HIS A CB  1 
ATOM   10   C  CB  B HIS A 1 4   ? 9.254   1.473   8.540   0.50 29.30  ? 4   HIS A CB  1 
ATOM   11   C  CG  A HIS A 1 4   ? 8.655   1.977   8.485   0.50 24.80  ? 4   HIS A CG  1 
ATOM   12   C  CG  B HIS A 1 4   ? 8.523   0.915   7.339   0.50 29.73  ? 4   HIS A CG  1 
ATOM   13   N  ND1 A HIS A 1 4   ? 9.373   2.625   9.481   0.50 32.98  ? 4   HIS A ND1 1 
ATOM   14   N  ND1 B HIS A 1 4   ? 8.910   -0.256  6.729   0.50 27.02  ? 4   HIS A ND1 1 
ATOM   15   C  CD2 A HIS A 1 4   ? 7.411   2.555   8.429   0.50 12.96  ? 4   HIS A CD2 1 
ATOM   16   C  CD2 B HIS A 1 4   ? 7.493   1.396   6.589   0.50 42.42  ? 4   HIS A CD2 1 
ATOM   17   C  CE1 A HIS A 1 4   ? 8.576   3.557   9.989   0.50 50.07  ? 4   HIS A CE1 1 
ATOM   18   C  CE1 B HIS A 1 4   ? 8.115   -0.509  5.696   0.50 34.05  ? 4   HIS A CE1 1 
ATOM   19   N  NE2 A HIS A 1 4   ? 7.418   3.573   9.339   0.50 36.99  ? 4   HIS A NE2 1 
ATOM   20   N  NE2 B HIS A 1 4   ? 7.262   0.483   5.574   0.50 39.91  ? 4   HIS A NE2 1 
ATOM   21   N  N   . TRP A 1 5   ? 8.392   -0.583  10.420  1.00 18.84  ? 5   TRP A N   1 
ATOM   22   C  CA  . TRP A 1 5   ? 7.680   -1.565  11.257  1.00 14.06  ? 5   TRP A CA  1 
ATOM   23   C  C   . TRP A 1 5   ? 6.681   -2.360  10.437  1.00 14.47  ? 5   TRP A C   1 
ATOM   24   O  O   . TRP A 1 5   ? 6.166   -1.876  9.429   1.00 16.29  ? 5   TRP A O   1 
ATOM   25   C  CB  . TRP A 1 5   ? 7.074   -0.856  12.426  1.00 15.88  ? 5   TRP A CB  1 
ATOM   26   C  CG  . TRP A 1 5   ? 5.882   -0.048  12.087  1.00 12.68  ? 5   TRP A CG  1 
ATOM   27   C  CD1 . TRP A 1 5   ? 5.826   1.296   11.722  1.00 15.16  ? 5   TRP A CD1 1 
ATOM   28   C  CD2 . TRP A 1 5   ? 4.486   -0.528  12.067  1.00 12.06  ? 5   TRP A CD2 1 
ATOM   29   N  NE1 . TRP A 1 5   ? 4.566   1.682   11.545  1.00 14.41  ? 5   TRP A NE1 1 
ATOM   30   C  CE2 . TRP A 1 5   ? 3.709   0.600   11.750  1.00 13.23  ? 5   TRP A CE2 1 
ATOM   31   C  CE3 . TRP A 1 5   ? 3.888   -1.760  12.357  1.00 12.31  ? 5   TRP A CE3 1 
ATOM   32   C  CZ2 . TRP A 1 5   ? 2.348   0.571   11.636  1.00 13.14  ? 5   TRP A CZ2 1 
ATOM   33   C  CZ3 . TRP A 1 5   ? 2.468   -1.824  12.226  1.00 12.03  ? 5   TRP A CZ3 1 
ATOM   34   C  CH2 . TRP A 1 5   ? 1.742   -0.623  11.885  1.00 12.76  ? 5   TRP A CH2 1 
ATOM   35   N  N   . GLY A 1 6   ? 6.419   -3.558  10.936  1.00 13.29  ? 6   GLY A N   1 
ATOM   36   C  CA  . GLY A 1 6   ? 5.370   -4.363  10.346  1.00 13.98  ? 6   GLY A CA  1 
ATOM   37   C  C   . GLY A 1 6   ? 5.048   -5.483  11.266  1.00 14.05  ? 6   GLY A C   1 
ATOM   38   O  O   . GLY A 1 6   ? 5.088   -5.341  12.489  1.00 12.67  ? 6   GLY A O   1 
ATOM   39   N  N   . TYR A 1 7   ? 4.721   -6.615  10.663  1.00 16.54  ? 7   TYR A N   1 
ATOM   40   C  CA  . TYR A 1 7   ? 4.299   -7.796  11.511  1.00 16.79  ? 7   TYR A CA  1 
ATOM   41   C  C   . TYR A 1 7   ? 5.270   -9.052  11.473  1.00 19.22  ? 7   TYR A C   1 
ATOM   42   O  O   . TYR A 1 7   ? 4.979   -10.141 12.053  1.00 25.12  ? 7   TYR A O   1 
ATOM   43   C  CB  . TYR A 1 7   ? 2.802   -8.106  11.211  1.00 15.87  ? 7   TYR A CB  1 
ATOM   44   C  CG  . TYR A 1 7   ? 1.931   -6.984  11.756  1.00 11.13  ? 7   TYR A CG  1 
ATOM   45   C  CD1 . TYR A 1 7   ? 1.564   -7.019  13.115  1.00 10.35  ? 7   TYR A CD1 1 
ATOM   46   C  CD2 . TYR A 1 7   ? 1.481   -5.954  10.941  1.00 12.32  ? 7   TYR A CD2 1 
ATOM   47   C  CE1 . TYR A 1 7   ? 0.717   -6.001  13.597  1.00 9.21   ? 7   TYR A CE1 1 
ATOM   48   C  CE2 . TYR A 1 7   ? 0.661   -4.957  11.430  1.00 10.67  ? 7   TYR A CE2 1 
ATOM   49   C  CZ  . TYR A 1 7   ? 0.264   -5.008  12.781  1.00 9.00   ? 7   TYR A CZ  1 
ATOM   50   O  OH  . TYR A 1 7   ? -0.550  -4.032  13.249  1.00 9.37   ? 7   TYR A OH  1 
ATOM   51   N  N   . GLY A 1 8   ? 6.480   -8.879  10.930  1.00 21.58  ? 8   GLY A N   1 
ATOM   52   C  CA  . GLY A 1 8   ? 7.445   -9.984  10.829  1.00 16.23  ? 8   GLY A CA  1 
ATOM   53   C  C   . GLY A 1 8   ? 8.463   -10.305 11.940  1.00 18.11  ? 8   GLY A C   1 
ATOM   54   O  O   . GLY A 1 8   ? 8.529   -9.680  12.965  1.00 23.86  ? 8   GLY A O   1 
ATOM   55   N  N   . LYS A 1 9   ? 9.293   -11.311 11.725  1.00 20.96  ? 9   LYS A N   1 
ATOM   56   C  CA  . LYS A 1 9   ? 10.330  -11.728 12.715  1.00 23.29  ? 9   LYS A CA  1 
ATOM   57   C  C   . LYS A 1 9   ? 11.274  -10.552 13.013  1.00 17.79  ? 9   LYS A C   1 
ATOM   58   O  O   . LYS A 1 9   ? 11.771  -10.522 14.163  1.00 22.66  ? 9   LYS A O   1 
ATOM   59   C  CB  . LYS A 1 9   ? 11.172  -12.727 12.046  1.00 27.84  ? 9   LYS A CB  1 
ATOM   60   N  N   . HIS A 1 10  ? 11.680  -9.833  11.910  1.00 23.04  ? 10  HIS A N   1 
ATOM   61   C  CA  . HIS A 1 10  ? 12.726  -8.790  11.994  1.00 22.61  ? 10  HIS A CA  1 
ATOM   62   C  C   . HIS A 1 10  ? 12.041  -7.482  12.109  1.00 19.91  ? 10  HIS A C   1 
ATOM   63   O  O   . HIS A 1 10  ? 12.778  -6.631  12.421  1.00 23.16  ? 10  HIS A O   1 
ATOM   64   C  CB  . HIS A 1 10  ? 13.579  -8.810  10.784  1.00 20.86  ? 10  HIS A CB  1 
ATOM   65   C  CG  . HIS A 1 10  ? 14.302  -10.102 10.689  1.00 17.89  ? 10  HIS A CG  1 
ATOM   66   N  ND1 . HIS A 1 10  ? 15.372  -10.588 11.453  1.00 20.21  ? 10  HIS A ND1 1 
ATOM   67   C  CD2 . HIS A 1 10  ? 13.921  -11.052 9.924   1.00 21.68  ? 10  HIS A CD2 1 
ATOM   68   C  CE1 . HIS A 1 10  ? 15.718  -11.798 10.987  1.00 23.30  ? 10  HIS A CE1 1 
ATOM   69   N  NE2 . HIS A 1 10  ? 14.837  -12.083 10.015  1.00 18.87  ? 10  HIS A NE2 1 
ATOM   70   N  N   . ASN A 1 11  ? 10.629  -7.233  11.925  1.00 23.76  ? 11  ASN A N   1 
ATOM   71   C  CA  . ASN A 1 11  ? 10.085  -5.882  12.075  1.00 18.46  ? 11  ASN A CA  1 
ATOM   72   C  C   . ASN A 1 11  ? 8.710   -5.912  12.792  1.00 15.20  ? 11  ASN A C   1 
ATOM   73   O  O   . ASN A 1 11  ? 8.136   -4.860  12.936  1.00 15.82  ? 11  ASN A O   1 
ATOM   74   C  CB  . ASN A 1 11  ? 9.835   -5.142  10.728  1.00 17.42  ? 11  ASN A CB  1 
ATOM   75   C  CG  . ASN A 1 11  ? 8.756   -5.761  9.800   1.00 17.75  ? 11  ASN A CG  1 
ATOM   76   O  OD1 . ASN A 1 11  ? 8.163   -6.793  10.113  1.00 20.77  ? 11  ASN A OD1 1 
ATOM   77   N  ND2 . ASN A 1 11  ? 8.492   -5.126  8.633   1.00 19.46  ? 11  ASN A ND2 1 
ATOM   78   N  N   . GLY A 1 12  ? 8.418   -7.020  13.462  1.00 15.79  ? 12  GLY A N   1 
ATOM   79   C  CA  . GLY A 1 12  ? 7.148   -7.170  14.125  1.00 14.95  ? 12  GLY A CA  1 
ATOM   80   C  C   . GLY A 1 12  ? 7.177   -6.628  15.503  1.00 13.27  ? 12  GLY A C   1 
ATOM   81   O  O   . GLY A 1 12  ? 8.086   -5.929  15.974  1.00 14.35  ? 12  GLY A O   1 
ATOM   82   N  N   . PRO A 1 13  ? 6.065   -6.939  16.249  1.00 12.39  ? 13  PRO A N   1 
ATOM   83   C  CA  . PRO A 1 13  ? 5.820   -6.362  17.538  1.00 13.34  ? 13  PRO A CA  1 
ATOM   84   C  C   . PRO A 1 13  ? 6.980   -6.386  18.527  1.00 13.44  ? 13  PRO A C   1 
ATOM   85   O  O   . PRO A 1 13  ? 7.105   -5.441  19.355  1.00 13.47  ? 13  PRO A O   1 
ATOM   86   C  CB  . PRO A 1 13  ? 4.632   -7.171  18.083  1.00 13.60  ? 13  PRO A CB  1 
ATOM   87   C  CG  . PRO A 1 13  ? 3.813   -7.434  16.837  1.00 13.63  ? 13  PRO A CG  1 
ATOM   88   C  CD  . PRO A 1 13  ? 4.881   -7.678  15.758  1.00 13.38  ? 13  PRO A CD  1 
ATOM   89   N  N   . GLU A 1 14  ? 7.856   -7.431  18.631  1.00 15.11  ? 14  GLU A N   1 
ATOM   90   C  CA  . GLU A 1 14  ? 8.971   -7.440  19.626  1.00 17.19  ? 14  GLU A CA  1 
ATOM   91   C  C   . GLU A 1 14  ? 10.074  -6.461  19.239  1.00 14.41  ? 14  GLU A C   1 
ATOM   92   O  O   . GLU A 1 14  ? 10.952  -6.241  20.078  1.00 17.49  ? 14  GLU A O   1 
ATOM   93   C  CB  . GLU A 1 14  ? 9.614   -8.819  19.867  1.00 23.28  ? 14  GLU A CB  1 
ATOM   94   C  CG  . GLU A 1 14  ? 8.774   -10.017 20.120  1.00 28.10  ? 14  GLU A CG  1 
ATOM   95   C  CD  . GLU A 1 14  ? 8.153   -10.067 21.472  1.00 43.51  ? 14  GLU A CD  1 
ATOM   96   O  OE1 . GLU A 1 14  ? 7.715   -11.193 21.786  1.00 32.64  ? 14  GLU A OE1 1 
ATOM   97   O  OE2 . GLU A 1 14  ? 7.997   -9.035  22.168  1.00 33.50  ? 14  GLU A OE2 1 
ATOM   98   N  N   . HIS A 1 15  ? 9.976   -5.910  18.010  1.00 14.38  ? 15  HIS A N   1 
ATOM   99   C  CA  . HIS A 1 15  ? 11.009  -4.909  17.590  1.00 13.87  ? 15  HIS A CA  1 
ATOM   100  C  C   . HIS A 1 15  ? 10.503  -3.461  17.739  1.00 13.43  ? 15  HIS A C   1 
ATOM   101  O  O   . HIS A 1 15  ? 11.370  -2.527  17.726  1.00 14.00  ? 15  HIS A O   1 
ATOM   102  C  CB  . HIS A 1 15  ? 11.320  -5.097  16.106  1.00 14.20  ? 15  HIS A CB  1 
ATOM   103  C  CG  . HIS A 1 15  ? 12.065  -6.334  15.860  1.00 16.32  ? 15  HIS A CG  1 
ATOM   104  N  ND1 . HIS A 1 15  ? 13.447  -6.398  15.982  1.00 18.70  ? 15  HIS A ND1 1 
ATOM   105  C  CD2 . HIS A 1 15  ? 11.602  -7.566  15.538  1.00 17.96  ? 15  HIS A CD2 1 
ATOM   106  C  CE1 . HIS A 1 15  ? 13.792  -7.646  15.708  1.00 22.23  ? 15  HIS A CE1 1 
ATOM   107  N  NE2 . HIS A 1 15  ? 12.727  -8.372  15.384  1.00 21.67  ? 15  HIS A NE2 1 
ATOM   108  N  N   . TRP A 1 16  ? 9.211   -3.218  17.924  1.00 11.64  ? 16  TRP A N   1 
ATOM   109  C  CA  . TRP A 1 16  ? 8.697   -1.885  17.839  1.00 10.54  ? 16  TRP A CA  1 
ATOM   110  C  C   . TRP A 1 16  ? 9.269   -0.912  18.850  1.00 10.92  ? 16  TRP A C   1 
ATOM   111  O  O   . TRP A 1 16  ? 9.355   0.278   18.558  1.00 12.04  ? 16  TRP A O   1 
ATOM   112  C  CB  . TRP A 1 16  ? 7.145   -1.931  17.956  1.00 10.94  ? 16  TRP A CB  1 
ATOM   113  C  CG  . TRP A 1 16  ? 6.463   -2.622  16.815  1.00 9.97   ? 16  TRP A CG  1 
ATOM   114  C  CD1 . TRP A 1 16  ? 6.972   -3.054  15.607  1.00 11.11  ? 16  TRP A CD1 1 
ATOM   115  C  CD2 . TRP A 1 16  ? 5.068   -2.931  16.753  1.00 10.08  ? 16  TRP A CD2 1 
ATOM   116  N  NE1 . TRP A 1 16  ? 5.991   -3.649  14.843  1.00 11.06  ? 16  TRP A NE1 1 
ATOM   117  C  CE2 . TRP A 1 16  ? 4.823   -3.574  15.529  1.00 10.02  ? 16  TRP A CE2 1 
ATOM   118  C  CE3 . TRP A 1 16  ? 4.010   -2.763  17.677  1.00 9.84   ? 16  TRP A CE3 1 
ATOM   119  C  CZ2 . TRP A 1 16  ? 3.533   -4.009  15.118  1.00 9.81   ? 16  TRP A CZ2 1 
ATOM   120  C  CZ3 . TRP A 1 16  ? 2.729   -3.170  17.267  1.00 10.31  ? 16  TRP A CZ3 1 
ATOM   121  C  CH2 . TRP A 1 16  ? 2.502   -3.781  16.033  1.00 10.47  ? 16  TRP A CH2 1 
ATOM   122  N  N   . HIS A 1 17  ? 9.627   -1.462  19.977  1.00 11.39  ? 17  HIS A N   1 
ATOM   123  C  CA  . HIS A 1 17  ? 10.098  -0.599  21.039  1.00 11.85  ? 17  HIS A CA  1 
ATOM   124  C  C   . HIS A 1 17  ? 11.380  0.185   20.667  1.00 13.50  ? 17  HIS A C   1 
ATOM   125  O  O   . HIS A 1 17  ? 11.670  1.250   21.320  1.00 14.36  ? 17  HIS A O   1 
ATOM   126  C  CB  . HIS A 1 17  ? 10.430  -1.360  22.370  1.00 12.85  ? 17  HIS A CB  1 
ATOM   127  C  CG  . HIS A 1 17  ? 11.633  -2.210  22.244  1.00 13.79  ? 17  HIS A CG  1 
ATOM   128  N  ND1 . HIS A 1 17  ? 12.848  -1.785  22.745  1.00 17.35  ? 17  HIS A ND1 1 
ATOM   129  C  CD2 . HIS A 1 17  ? 11.835  -3.396  21.725  1.00 15.52  ? 17  HIS A CD2 1 
ATOM   130  C  CE1 . HIS A 1 17  ? 13.744  -2.682  22.576  1.00 19.07  ? 17  HIS A CE1 1 
ATOM   131  N  NE2 . HIS A 1 17  ? 13.207  -3.682  21.933  1.00 16.31  ? 17  HIS A NE2 1 
ATOM   132  N  N   . LYS A 1 18  ? 12.137  -0.308  19.686  1.00 14.04  ? 18  LYS A N   1 
ATOM   133  C  CA  . LYS A 1 18  ? 13.385  0.434   19.305  1.00 14.95  ? 18  LYS A CA  1 
ATOM   134  C  C   . LYS A 1 18  ? 13.064  1.780   18.668  1.00 16.27  ? 18  LYS A C   1 
ATOM   135  O  O   . LYS A 1 18  ? 13.748  2.774   18.953  1.00 22.56  ? 18  LYS A O   1 
ATOM   136  C  CB  . LYS A 1 18  ? 14.198  -0.451  18.417  1.00 15.96  ? 18  LYS A CB  1 
ATOM   137  C  CG  . LYS A 1 18  ? 14.839  -1.613  19.124  1.00 17.37  ? 18  LYS A CG  1 
ATOM   138  C  CD  . LYS A 1 18  ? 15.563  -2.591  18.157  1.00 16.26  ? 18  LYS A CD  1 
ATOM   139  C  CE  . LYS A 1 18  ? 14.573  -3.549  17.582  1.00 15.87  ? 18  LYS A CE  1 
ATOM   140  N  NZ  . LYS A 1 18  ? 15.235  -4.385  16.508  1.00 17.20  ? 18  LYS A NZ  1 
ATOM   141  N  N   . ASP A 1 19  ? 12.032  1.809   17.825  1.00 14.76  ? 19  ASP A N   1 
ATOM   142  C  CA  . ASP A 1 19  ? 11.604  3.092   17.201  1.00 15.76  ? 19  ASP A CA  1 
ATOM   143  C  C   . ASP A 1 19  ? 10.576  3.831   18.073  1.00 14.73  ? 19  ASP A C   1 
ATOM   144  O  O   . ASP A 1 19  ? 10.473  5.024   17.953  1.00 16.08  ? 19  ASP A O   1 
ATOM   145  C  CB  . ASP A 1 19  ? 11.075  2.884   15.753  1.00 18.62  ? 19  ASP A CB  1 
ATOM   146  C  CG  . ASP A 1 19  ? 12.189  2.965   14.686  1.00 21.56  ? 19  ASP A CG  1 
ATOM   147  O  OD1 . ASP A 1 19  ? 13.258  3.505   14.947  1.00 31.10  ? 19  ASP A OD1 1 
ATOM   148  O  OD2 . ASP A 1 19  ? 11.993  2.361   13.620  1.00 39.57  ? 19  ASP A OD2 1 
ATOM   149  N  N   . PHE A 1 20  ? 9.844   3.071   18.911  1.00 13.01  ? 20  PHE A N   1 
ATOM   150  C  CA  . PHE A 1 20  ? 8.723   3.624   19.610  1.00 12.71  ? 20  PHE A CA  1 
ATOM   151  C  C   . PHE A 1 20  ? 8.830   3.121   21.079  1.00 12.50  ? 20  PHE A C   1 
ATOM   152  O  O   . PHE A 1 20  ? 8.171   2.161   21.460  1.00 11.93  ? 20  PHE A O   1 
ATOM   153  C  CB  . PHE A 1 20  ? 7.360   3.157   18.973  1.00 13.60  ? 20  PHE A CB  1 
ATOM   154  C  CG  . PHE A 1 20  ? 7.296   3.509   17.540  1.00 13.83  ? 20  PHE A CG  1 
ATOM   155  C  CD1 . PHE A 1 20  ? 6.920   4.780   17.195  1.00 16.37  ? 20  PHE A CD1 1 
ATOM   156  C  CD2 . PHE A 1 20  ? 7.612   2.581   16.539  1.00 15.92  ? 20  PHE A CD2 1 
ATOM   157  C  CE1 . PHE A 1 20  ? 6.918   5.120   15.792  1.00 16.34  ? 20  PHE A CE1 1 
ATOM   158  C  CE2 . PHE A 1 20  ? 7.646   2.890   15.233  1.00 16.78  ? 20  PHE A CE2 1 
ATOM   159  C  CZ  . PHE A 1 20  ? 7.240   4.152   14.828  1.00 17.17  ? 20  PHE A CZ  1 
ATOM   160  N  N   . PRO A 1 21  ? 9.691   3.753   21.870  1.00 13.54  ? 21  PRO A N   1 
ATOM   161  C  CA  . PRO A 1 21  ? 9.920   3.210   23.185  1.00 13.23  ? 21  PRO A CA  1 
ATOM   162  C  C   . PRO A 1 21  ? 8.703   3.144   24.148  1.00 12.69  ? 21  PRO A C   1 
ATOM   163  O  O   . PRO A 1 21  ? 8.733   2.372   25.108  1.00 13.46  ? 21  PRO A O   1 
ATOM   164  C  CB  . PRO A 1 21  ? 11.014  4.183   23.844  1.00 18.62  ? 21  PRO A CB  1 
ATOM   165  C  CG  . PRO A 1 21  ? 11.129  5.270   22.903  1.00 24.53  ? 21  PRO A CG  1 
ATOM   166  C  CD  . PRO A 1 21  ? 10.649  4.832   21.540  1.00 15.33  ? 21  PRO A CD  1 
ATOM   167  N  N   A ILE A 1 22  ? 7.690   3.851   23.637  0.50 10.26  ? 22  ILE A N   1 
ATOM   168  N  N   B ILE A 1 22  ? 7.672   3.977   24.117  0.50 10.39  ? 22  ILE A N   1 
ATOM   169  C  CA  A ILE A 1 22  ? 6.422   3.887   24.374  0.50 10.30  ? 22  ILE A CA  1 
ATOM   170  C  CA  B ILE A 1 22  ? 6.439   3.748   24.856  0.50 10.22  ? 22  ILE A CA  1 
ATOM   171  C  C   A ILE A 1 22  ? 5.830   2.444   24.435  0.50 10.98  ? 22  ILE A C   1 
ATOM   172  C  C   B ILE A 1 22  ? 5.870   2.330   24.579  0.50 11.21  ? 22  ILE A C   1 
ATOM   173  O  O   A ILE A 1 22  ? 4.959   2.127   25.291  0.50 11.72  ? 22  ILE A O   1 
ATOM   174  O  O   B ILE A 1 22  ? 4.894   1.977   25.224  0.50 10.89  ? 22  ILE A O   1 
ATOM   175  C  CB  A ILE A 1 22  ? 5.447   4.966   23.874  0.50 9.16   ? 22  ILE A CB  1 
ATOM   176  C  CB  B ILE A 1 22  ? 5.396   4.795   24.414  0.50 8.74   ? 22  ILE A CB  1 
ATOM   177  C  CG1 A ILE A 1 22  ? 4.426   5.261   24.966  0.50 9.77   ? 22  ILE A CG1 1 
ATOM   178  C  CG1 B ILE A 1 22  ? 4.321   5.075   25.434  0.50 12.16  ? 22  ILE A CG1 1 
ATOM   179  C  CG2 A ILE A 1 22  ? 4.868   4.568   22.554  0.50 9.55   ? 22  ILE A CG2 1 
ATOM   180  C  CG2 B ILE A 1 22  ? 4.771   4.399   23.079  0.50 10.79  ? 22  ILE A CG2 1 
ATOM   181  C  CD1 A ILE A 1 22  ? 3.486   6.356   24.738  0.50 12.38  ? 22  ILE A CD1 1 
ATOM   182  C  CD1 B ILE A 1 22  ? 4.931   5.806   26.546  0.50 17.17  ? 22  ILE A CD1 1 
ATOM   183  N  N   . ALA A 1 23  ? 6.322   1.547   23.586  1.00 10.66  ? 23  ALA A N   1 
ATOM   184  C  CA  . ALA A 1 23  ? 5.873   0.154   23.473  1.00 11.11  ? 23  ALA A CA  1 
ATOM   185  C  C   . ALA A 1 23  ? 5.955   -0.536  24.790  1.00 11.32  ? 23  ALA A C   1 
ATOM   186  O  O   . ALA A 1 23  ? 5.275   -1.560  24.969  1.00 11.72  ? 23  ALA A O   1 
ATOM   187  C  CB  . ALA A 1 23  ? 6.697   -0.619  22.491  1.00 11.69  ? 23  ALA A CB  1 
ATOM   188  N  N   . LYS A 1 24  ? 6.937   -0.112  25.646  1.00 11.79  ? 24  LYS A N   1 
ATOM   189  C  CA  . LYS A 1 24  ? 7.081   -0.738  26.965  1.00 12.62  ? 24  LYS A CA  1 
ATOM   190  C  C   . LYS A 1 24  ? 6.470   0.138   28.058  1.00 14.15  ? 24  LYS A C   1 
ATOM   191  O  O   . LYS A 1 24  ? 6.832   0.031   29.222  1.00 15.78  ? 24  LYS A O   1 
ATOM   192  C  CB  . LYS A 1 24  ? 8.588   -1.023  27.342  1.00 15.19  ? 24  LYS A CB  1 
ATOM   193  C  CG  . LYS A 1 24  ? 9.187   -1.938  26.328  1.00 16.10  ? 24  LYS A CG  1 
ATOM   194  C  CD  . LYS A 1 24  ? 10.707  -2.175  26.739  1.00 21.53  ? 24  LYS A CD  1 
ATOM   195  C  CE  . LYS A 1 24  ? 11.352  -3.042  25.723  1.00 21.74  ? 24  LYS A CE  1 
ATOM   196  N  NZ  . LYS A 1 24  ? 11.023  -4.457  25.951  1.00 29.51  ? 24  LYS A NZ  1 
ATOM   197  N  N   . GLY A 1 25  ? 5.467   0.953   27.724  1.00 13.49  ? 25  GLY A N   1 
ATOM   198  C  CA  . GLY A 1 25  ? 4.874   1.956   28.657  1.00 14.45  ? 25  GLY A CA  1 
ATOM   199  C  C   . GLY A 1 25  ? 3.877   1.297   29.611  1.00 11.76  ? 25  GLY A C   1 
ATOM   200  O  O   . GLY A 1 25  ? 3.690   0.057   29.710  1.00 13.55  ? 25  GLY A O   1 
ATOM   201  N  N   . GLU A 1 26  ? 3.243   2.192   30.346  1.00 13.26  ? 26  GLU A N   1 
ATOM   202  C  CA  . GLU A 1 26  ? 2.366   1.802   31.446  1.00 14.31  ? 26  GLU A CA  1 
ATOM   203  C  C   . GLU A 1 26  ? 0.919   1.558   31.057  1.00 11.42  ? 26  GLU A C   1 
ATOM   204  O  O   . GLU A 1 26  ? 0.143   1.098   31.886  1.00 13.35  ? 26  GLU A O   1 
ATOM   205  C  CB  . GLU A 1 26  ? 2.393   2.913   32.526  1.00 15.58  ? 26  GLU A CB  1 
ATOM   206  C  CG  . GLU A 1 26  ? 3.865   3.141   33.115  1.00 18.59  ? 26  GLU A CG  1 
ATOM   207  C  CD  . GLU A 1 26  ? 4.374   1.840   33.783  1.00 23.55  ? 26  GLU A CD  1 
ATOM   208  O  OE1 . GLU A 1 26  ? 3.709   1.258   34.690  1.00 30.95  ? 26  GLU A OE1 1 
ATOM   209  O  OE2 . GLU A 1 26  ? 5.464   1.393   33.402  1.00 32.96  ? 26  GLU A OE2 1 
ATOM   210  N  N   . ARG A 1 27  ? 0.547   1.893   29.827  1.00 9.71   ? 27  ARG A N   1 
ATOM   211  C  CA  . ARG A 1 27  ? -0.861  1.666   29.448  1.00 8.76   ? 27  ARG A CA  1 
ATOM   212  C  C   . ARG A 1 27  ? -0.923  1.239   27.979  1.00 8.11   ? 27  ARG A C   1 
ATOM   213  O  O   . ARG A 1 27  ? -1.617  1.878   27.143  1.00 8.47   ? 27  ARG A O   1 
ATOM   214  C  CB  . ARG A 1 27  ? -1.769  2.907   29.789  1.00 11.04  ? 27  ARG A CB  1 
ATOM   215  C  CG  . ARG A 1 27  ? -1.435  4.212   29.200  1.00 13.92  ? 27  ARG A CG  1 
ATOM   216  C  CD  . ARG A 1 27  ? -2.433  5.337   29.425  1.00 15.38  ? 27  ARG A CD  1 
ATOM   217  N  NE  . ARG A 1 27  ? -3.561  5.284   28.494  1.00 13.10  ? 27  ARG A NE  1 
ATOM   218  C  CZ  . ARG A 1 27  ? -4.527  6.197   28.431  1.00 10.98  ? 27  ARG A CZ  1 
ATOM   219  N  NH1 . ARG A 1 27  ? -4.512  7.244   29.244  1.00 13.19  ? 27  ARG A NH1 1 
ATOM   220  N  NH2 . ARG A 1 27  ? -5.510  6.063   27.552  1.00 12.60  ? 27  ARG A NH2 1 
ATOM   221  N  N   . GLN A 1 28  ? -0.238  0.145   27.703  1.00 7.71   ? 28  GLN A N   1 
ATOM   222  C  CA  . GLN A 1 28  ? -0.200  -0.394  26.340  1.00 7.42   ? 28  GLN A CA  1 
ATOM   223  C  C   . GLN A 1 28  ? -1.379  -1.347  26.080  1.00 6.70   ? 28  GLN A C   1 
ATOM   224  O  O   . GLN A 1 28  ? -1.845  -2.045  26.970  1.00 8.19   ? 28  GLN A O   1 
ATOM   225  C  CB  . GLN A 1 28  ? 1.156   -1.082  26.096  1.00 8.63   ? 28  GLN A CB  1 
ATOM   226  C  CG  . GLN A 1 28  ? 2.254   0.005   25.968  1.00 9.08   ? 28  GLN A CG  1 
ATOM   227  C  CD  . GLN A 1 28  ? 2.152   0.782   24.691  1.00 8.08   ? 28  GLN A CD  1 
ATOM   228  O  OE1 . GLN A 1 28  ? 2.334   0.230   23.598  1.00 8.44   ? 28  GLN A OE1 1 
ATOM   229  N  NE2 . GLN A 1 28  ? 1.825   2.058   24.799  1.00 8.59   ? 28  GLN A NE2 1 
ATOM   230  N  N   . SER A 1 29  ? -1.733  -1.429  24.800  1.00 6.64   ? 29  SER A N   1 
ATOM   231  C  CA  . SER A 1 29  ? -2.796  -2.310  24.309  1.00 6.41   ? 29  SER A CA  1 
ATOM   232  C  C   . SER A 1 29  ? -2.276  -3.200  23.224  1.00 6.10   ? 29  SER A C   1 
ATOM   233  O  O   . SER A 1 29  ? -1.296  -2.815  22.513  1.00 7.25   ? 29  SER A O   1 
ATOM   234  C  CB  . SER A 1 29  ? -3.929  -1.435  23.775  1.00 6.17   ? 29  SER A CB  1 
ATOM   235  O  OG  . SER A 1 29  ? -4.544  -0.712  24.841  1.00 6.55   ? 29  SER A OG  1 
ATOM   236  N  N   . PRO A 1 30  ? -2.899  -4.331  22.952  1.00 5.97   ? 30  PRO A N   1 
ATOM   237  C  CA  . PRO A 1 30  ? -4.076  -4.867  23.668  1.00 6.10   ? 30  PRO A CA  1 
ATOM   238  C  C   . PRO A 1 30  ? -3.674  -5.516  24.961  1.00 6.14   ? 30  PRO A C   1 
ATOM   239  O  O   . PRO A 1 30  ? -2.460  -5.574  25.309  1.00 7.40   ? 30  PRO A O   1 
ATOM   240  C  CB  . PRO A 1 30  ? -4.611  -5.903  22.687  1.00 6.46   ? 30  PRO A CB  1 
ATOM   241  C  CG  . PRO A 1 30  ? -3.299  -6.458  22.068  1.00 7.06   ? 30  PRO A CG  1 
ATOM   242  C  CD  . PRO A 1 30  ? -2.427  -5.235  21.911  1.00 6.91   ? 30  PRO A CD  1 
ATOM   243  N  N   . VAL A 1 31  ? -4.661  -6.075  25.657  1.00 6.84   ? 31  VAL A N   1 
ATOM   244  C  CA  . VAL A 1 31  ? -4.497  -6.850  26.918  1.00 6.60   ? 31  VAL A CA  1 
ATOM   245  C  C   . VAL A 1 31  ? -5.314  -8.058  26.837  1.00 6.54   ? 31  VAL A C   1 
ATOM   246  O  O   . VAL A 1 31  ? -6.314  -8.127  26.099  1.00 7.56   ? 31  VAL A O   1 
ATOM   247  C  CB  . VAL A 1 31  ? -4.768  -5.995  28.138  1.00 7.73   ? 31  VAL A CB  1 
ATOM   248  C  CG1 . VAL A 1 31  ? -3.870  -4.819  28.267  1.00 8.50   ? 31  VAL A CG1 1 
ATOM   249  C  CG2 . VAL A 1 31  ? -6.277  -5.578  28.222  1.00 8.46   ? 31  VAL A CG2 1 
ATOM   250  N  N   . ASP A 1 32  ? -5.020  -9.035  27.716  1.00 7.16   ? 32  ASP A N   1 
ATOM   251  C  CA  . ASP A 1 32  ? -5.921  -10.131 28.019  1.00 7.36   ? 32  ASP A CA  1 
ATOM   252  C  C   . ASP A 1 32  ? -6.974  -9.620  28.998  1.00 7.67   ? 32  ASP A C   1 
ATOM   253  O  O   . ASP A 1 32  ? -6.643  -8.956  29.981  1.00 9.72   ? 32  ASP A O   1 
ATOM   254  C  CB  . ASP A 1 32  ? -5.179  -11.300 28.616  1.00 8.76   ? 32  ASP A CB  1 
ATOM   255  C  CG  . ASP A 1 32  ? -6.114  -12.465 28.902  1.00 9.43   ? 32  ASP A CG  1 
ATOM   256  O  OD1 . ASP A 1 32  ? -6.812  -12.911 27.993  1.00 8.84   ? 32  ASP A OD1 1 
ATOM   257  O  OD2 . ASP A 1 32  ? -6.173  -12.902 30.092  1.00 12.00  ? 32  ASP A OD2 1 
ATOM   258  N  N   . ILE A 1 33  ? -8.232  -9.909  28.716  1.00 7.30   ? 33  ILE A N   1 
ATOM   259  C  CA  . ILE A 1 33  ? -9.370  -9.540  29.583  1.00 7.58   ? 33  ILE A CA  1 
ATOM   260  C  C   . ILE A 1 33  ? -9.650  -10.809 30.408  1.00 8.64   ? 33  ILE A C   1 
ATOM   261  O  O   . ILE A 1 33  ? -10.176 -11.789 29.940  1.00 9.84   ? 33  ILE A O   1 
ATOM   262  C  CB  . ILE A 1 33  ? -10.545 -9.117  28.753  1.00 8.16   ? 33  ILE A CB  1 
ATOM   263  C  CG1 . ILE A 1 33  ? -10.164 -7.907  27.917  1.00 8.94   ? 33  ILE A CG1 1 
ATOM   264  C  CG2 . ILE A 1 33  ? -11.719 -8.875  29.728  1.00 10.49  ? 33  ILE A CG2 1 
ATOM   265  C  CD1 . ILE A 1 33  ? -11.215 -7.592  26.779  1.00 10.73  ? 33  ILE A CD1 1 
ATOM   266  N  N   A ASP A 1 34  ? -9.151  -10.770 31.648  0.50 9.92   ? 34  ASP A N   1 
ATOM   267  N  N   B ASP A 1 34  ? -9.360  -10.668 31.716  0.50 9.81   ? 34  ASP A N   1 
ATOM   268  C  CA  A ASP A 1 34  ? -9.470  -11.865 32.580  0.50 11.27  ? 34  ASP A CA  1 
ATOM   269  C  CA  B ASP A 1 34  ? -9.643  -11.730 32.703  0.50 10.32  ? 34  ASP A CA  1 
ATOM   270  C  C   A ASP A 1 34  ? -10.854 -11.529 33.123  0.50 11.25  ? 34  ASP A C   1 
ATOM   271  C  C   B ASP A 1 34  ? -11.075 -11.530 33.166  0.50 12.03  ? 34  ASP A C   1 
ATOM   272  O  O   A ASP A 1 34  ? -10.926 -10.489 33.922  0.50 11.01  ? 34  ASP A O   1 
ATOM   273  O  O   B ASP A 1 34  ? -11.479 -10.646 33.924  0.50 11.14  ? 34  ASP A O   1 
ATOM   274  C  CB  A ASP A 1 34  ? -8.408  -11.915 33.676  0.50 13.89  ? 34  ASP A CB  1 
ATOM   275  C  CB  B ASP A 1 34  ? -8.612  -11.646 33.834  0.50 13.24  ? 34  ASP A CB  1 
ATOM   276  C  CG  A ASP A 1 34  ? -8.605  -13.110 34.583  0.50 15.34  ? 34  ASP A CG  1 
ATOM   277  C  CG  B ASP A 1 34  ? -8.847  -12.696 34.916  0.50 15.36  ? 34  ASP A CG  1 
ATOM   278  O  OD1 A ASP A 1 34  ? -8.204  -14.167 34.122  0.50 19.94  ? 34  ASP A OD1 1 
ATOM   279  O  OD1 B ASP A 1 34  ? -9.997  -13.156 35.094  0.50 13.91  ? 34  ASP A OD1 1 
ATOM   280  O  OD2 A ASP A 1 34  ? -9.170  -12.987 35.718  0.50 18.13  ? 34  ASP A OD2 1 
ATOM   281  O  OD2 B ASP A 1 34  ? -7.923  -13.073 35.632  0.50 20.69  ? 34  ASP A OD2 1 
ATOM   282  N  N   . THR A 1 35  ? -11.910 -12.302 32.686  1.00 12.15  ? 35  THR A N   1 
ATOM   283  C  CA  . THR A 1 35  ? -13.332 -11.991 32.942  1.00 13.06  ? 35  THR A CA  1 
ATOM   284  C  C   . THR A 1 35  ? -13.747 -12.176 34.345  1.00 12.58  ? 35  THR A C   1 
ATOM   285  O  O   . THR A 1 35  ? -14.632 -11.402 34.802  1.00 16.65  ? 35  THR A O   1 
ATOM   286  C  CB  . THR A 1 35  ? -14.175 -12.873 32.117  1.00 14.35  ? 35  THR A CB  1 
ATOM   287  O  OG1 . THR A 1 35  ? -14.072 -14.225 32.578  1.00 16.04  ? 35  THR A OG1 1 
ATOM   288  C  CG2 . THR A 1 35  ? -13.954 -12.726 30.661  1.00 16.72  ? 35  THR A CG2 1 
ATOM   289  N  N   . HIS A 1 36  ? -13.068 -12.981 35.119  1.00 15.60  ? 36  HIS A N   1 
ATOM   290  C  CA  . HIS A 1 36  ? -13.308 -13.105 36.540  1.00 16.17  ? 36  HIS A CA  1 
ATOM   291  C  C   . HIS A 1 36  ? -12.855 -11.974 37.347  1.00 18.61  ? 36  HIS A C   1 
ATOM   292  O  O   . HIS A 1 36  ? -13.522 -11.698 38.370  1.00 17.92  ? 36  HIS A O   1 
ATOM   293  C  CB  . HIS A 1 36  ? -12.796 -14.493 37.007  1.00 20.55  ? 36  HIS A CB  1 
ATOM   294  C  CG  . HIS A 1 36  ? -13.699 -15.591 36.522  1.00 18.32  ? 36  HIS A CG  1 
ATOM   295  N  ND1 . HIS A 1 36  ? -13.355 -16.398 35.421  1.00 39.62  ? 36  HIS A ND1 1 
ATOM   296  C  CD2 . HIS A 1 36  ? -15.042 -15.777 36.799  1.00 18.11  ? 36  HIS A CD2 1 
ATOM   297  C  CE1 . HIS A 1 36  ? -14.391 -17.191 35.204  1.00 50.42  ? 36  HIS A CE1 1 
ATOM   298  N  NE2 . HIS A 1 36  ? -15.411 -16.862 35.998  1.00 34.63  ? 36  HIS A NE2 1 
ATOM   299  N  N   . THR A 1 37  ? -11.731 -11.307 36.925  1.00 17.75  ? 37  THR A N   1 
ATOM   300  C  CA  . THR A 1 37  ? -11.105 -10.177 37.662  1.00 17.62  ? 37  THR A CA  1 
ATOM   301  C  C   . THR A 1 37  ? -11.695 -8.804  37.228  1.00 15.16  ? 37  THR A C   1 
ATOM   302  O  O   . THR A 1 37  ? -11.614 -7.856  37.994  1.00 19.95  ? 37  THR A O   1 
ATOM   303  C  CB  . THR A 1 37  ? -9.594  -10.211 37.440  1.00 25.51  ? 37  THR A CB  1 
ATOM   304  O  OG1 . THR A 1 37  ? -9.180  -11.374 38.161  1.00 30.60  ? 37  THR A OG1 1 
ATOM   305  C  CG2 . THR A 1 37  ? -8.804  -8.977  38.121  1.00 20.82  ? 37  THR A CG2 1 
ATOM   306  N  N   . ALA A 1 38  ? -12.338 -8.733  36.065  1.00 14.36  ? 38  ALA A N   1 
ATOM   307  C  CA  . ALA A 1 38  ? -12.906 -7.480  35.655  1.00 13.79  ? 38  ALA A CA  1 
ATOM   308  C  C   . ALA A 1 38  ? -14.033 -7.156  36.619  1.00 15.19  ? 38  ALA A C   1 
ATOM   309  O  O   . ALA A 1 38  ? -14.733 -8.000  37.077  1.00 22.14  ? 38  ALA A O   1 
ATOM   310  C  CB  . ALA A 1 38  ? -13.444 -7.622  34.240  1.00 14.84  ? 38  ALA A CB  1 
ATOM   311  N  N   A LYS A 1 39  ? -14.031 -5.882  36.937  0.50 14.80  ? 39  LYS A N   1 
ATOM   312  N  N   B LYS A 1 39  ? -14.241 -5.984  37.102  0.50 15.09  ? 39  LYS A N   1 
ATOM   313  C  CA  A LYS A 1 39  ? -14.937 -5.271  37.977  0.50 13.35  ? 39  LYS A CA  1 
ATOM   314  C  CA  B LYS A 1 39  ? -15.378 -5.980  38.041  0.50 13.62  ? 39  LYS A CA  1 
ATOM   315  C  C   A LYS A 1 39  ? -16.387 -4.869  37.366  0.50 13.50  ? 39  LYS A C   1 
ATOM   316  C  C   B LYS A 1 39  ? -16.408 -5.157  37.334  0.50 14.23  ? 39  LYS A C   1 
ATOM   317  O  O   A LYS A 1 39  ? -16.381 -3.924  36.550  0.50 12.31  ? 39  LYS A O   1 
ATOM   318  O  O   B LYS A 1 39  ? -16.153 -4.099  36.695  0.50 13.30  ? 39  LYS A O   1 
ATOM   319  C  CB  A LYS A 1 39  ? -14.204 -4.120  38.679  0.50 12.96  ? 39  LYS A CB  1 
ATOM   320  C  CB  B LYS A 1 39  ? -14.971 -5.255  39.281  0.50 14.43  ? 39  LYS A CB  1 
ATOM   321  C  CG  A LYS A 1 39  ? -14.869 -3.339  39.774  0.50 16.33  ? 39  LYS A CG  1 
ATOM   322  C  CG  B LYS A 1 39  ? -15.943 -5.206  40.426  0.50 16.23  ? 39  LYS A CG  1 
ATOM   323  C  CD  A LYS A 1 39  ? -15.191 -4.179  40.898  0.50 17.07  ? 39  LYS A CD  1 
ATOM   324  C  CD  B LYS A 1 39  ? -15.361 -4.259  41.426  0.50 20.14  ? 39  LYS A CD  1 
ATOM   325  C  CE  A LYS A 1 39  ? -15.664 -3.262  42.003  0.50 14.55  ? 39  LYS A CE  1 
ATOM   326  C  CE  B LYS A 1 39  ? -16.530 -3.588  42.019  0.50 21.97  ? 39  LYS A CE  1 
ATOM   327  N  NZ  A LYS A 1 39  ? -16.168 -4.034  43.240  0.50 19.55  ? 39  LYS A NZ  1 
ATOM   328  N  NZ  B LYS A 1 39  ? -17.015 -4.717  42.834  0.50 29.72  ? 39  LYS A NZ  1 
ATOM   329  N  N   . TYR A 1 40  ? -17.579 -5.467  37.752  1.00 16.74  ? 40  TYR A N   1 
ATOM   330  C  CA  . TYR A 1 40  ? -18.810 -4.921  37.215  1.00 15.13  ? 40  TYR A CA  1 
ATOM   331  C  C   . TYR A 1 40  ? -18.864 -3.480  37.939  1.00 12.95  ? 40  TYR A C   1 
ATOM   332  O  O   . TYR A 1 40  ? -18.692 -3.307  39.154  1.00 15.59  ? 40  TYR A O   1 
ATOM   333  C  CB  . TYR A 1 40  ? -19.976 -5.672  37.683  1.00 21.84  ? 40  TYR A CB  1 
ATOM   334  C  CG  . TYR A 1 40  ? -21.279 -4.939  37.543  1.00 20.84  ? 40  TYR A CG  1 
ATOM   335  C  CD1 . TYR A 1 40  ? -21.697 -4.457  36.292  1.00 19.75  ? 40  TYR A CD1 1 
ATOM   336  C  CD2 . TYR A 1 40  ? -22.120 -4.754  38.625  1.00 23.14  ? 40  TYR A CD2 1 
ATOM   337  C  CE1 . TYR A 1 40  ? -22.889 -3.748  36.142  1.00 21.85  ? 40  TYR A CE1 1 
ATOM   338  C  CE2 . TYR A 1 40  ? -23.319 -4.076  38.470  1.00 26.26  ? 40  TYR A CE2 1 
ATOM   339  C  CZ  . TYR A 1 40  ? -23.701 -3.552  37.239  1.00 25.12  ? 40  TYR A CZ  1 
ATOM   340  O  OH  . TYR A 1 40  ? -24.917 -2.871  37.117  1.00 30.86  ? 40  TYR A OH  1 
ATOM   341  N  N   . ASP A 1 41  ? -19.076 -2.481  37.096  1.00 12.04  ? 41  ASP A N   1 
ATOM   342  C  CA  . ASP A 1 41  ? -19.189 -1.075  37.582  1.00 13.32  ? 41  ASP A CA  1 
ATOM   343  C  C   . ASP A 1 41  ? -20.540 -0.601  37.329  1.00 14.48  ? 41  ASP A C   1 
ATOM   344  O  O   . ASP A 1 41  ? -20.907 -0.231  36.179  1.00 15.35  ? 41  ASP A O   1 
ATOM   345  C  CB  . ASP A 1 41  ? -18.112 -0.205  36.902  1.00 14.71  ? 41  ASP A CB  1 
ATOM   346  C  CG  . ASP A 1 41  ? -18.037 1.206   37.366  1.00 17.39  ? 41  ASP A CG  1 
ATOM   347  O  OD1 . ASP A 1 41  ? -18.998 1.581   38.143  1.00 19.19  ? 41  ASP A OD1 1 
ATOM   348  O  OD2 . ASP A 1 41  ? -17.065 1.882   37.026  1.00 20.28  ? 41  ASP A OD2 1 
ATOM   349  N  N   . PRO A 1 42  ? -21.375 -0.497  38.351  1.00 18.00  ? 42  PRO A N   1 
ATOM   350  C  CA  . PRO A 1 42  ? -22.785 -0.102  38.124  1.00 19.65  ? 42  PRO A CA  1 
ATOM   351  C  C   . PRO A 1 42  ? -22.884 1.404   37.700  1.00 21.81  ? 42  PRO A C   1 
ATOM   352  O  O   . PRO A 1 42  ? -23.946 1.902   37.241  1.00 30.21  ? 42  PRO A O   1 
ATOM   353  C  CB  . PRO A 1 42  ? -23.424 -0.398  39.496  1.00 30.08  ? 42  PRO A CB  1 
ATOM   354  C  CG  . PRO A 1 42  ? -22.351 -0.240  40.500  1.00 25.12  ? 42  PRO A CG  1 
ATOM   355  C  CD  . PRO A 1 42  ? -21.137 -0.870  39.793  1.00 22.04  ? 42  PRO A CD  1 
ATOM   356  N  N   . SER A 1 43  ? -21.814 2.173   37.885  1.00 20.11  ? 43  SER A N   1 
ATOM   357  C  CA  . SER A 1 43  ? -21.709 3.600   37.439  1.00 22.99  ? 43  SER A CA  1 
ATOM   358  C  C   . SER A 1 43  ? -21.483 3.778   35.915  1.00 20.49  ? 43  SER A C   1 
ATOM   359  O  O   . SER A 1 43  ? -21.675 4.922   35.342  1.00 26.23  ? 43  SER A O   1 
ATOM   360  C  CB  . SER A 1 43  ? -20.612 4.396   38.156  1.00 24.30  ? 43  SER A CB  1 
ATOM   361  O  OG  . SER A 1 43  ? -19.288 4.140   37.731  1.00 24.73  ? 43  SER A OG  1 
ATOM   362  N  N   . LEU A 1 44  ? -21.098 2.718   35.236  1.00 19.23  ? 44  LEU A N   1 
ATOM   363  C  CA  . LEU A 1 44  ? -20.906 2.764   33.766  1.00 17.50  ? 44  LEU A CA  1 
ATOM   364  C  C   . LEU A 1 44  ? -22.291 2.876   33.082  1.00 19.08  ? 44  LEU A C   1 
ATOM   365  O  O   . LEU A 1 44  ? -23.304 2.397   33.526  1.00 26.32  ? 44  LEU A O   1 
ATOM   366  C  CB  . LEU A 1 44  ? -20.232 1.488   33.246  1.00 16.22  ? 44  LEU A CB  1 
ATOM   367  C  CG  . LEU A 1 44  ? -18.765 1.433   33.489  1.00 14.90  ? 44  LEU A CG  1 
ATOM   368  C  CD1 . LEU A 1 44  ? -18.291 0.073   33.114  1.00 16.90  ? 44  LEU A CD1 1 
ATOM   369  C  CD2 . LEU A 1 44  ? -18.011 2.561   32.736  1.00 17.26  ? 44  LEU A CD2 1 
ATOM   370  N  N   . LYS A 1 45  ? -22.337 3.631   32.004  1.00 18.04  ? 45  LYS A N   1 
ATOM   371  C  CA  . LYS A 1 45  ? -23.614 3.869   31.284  1.00 16.80  ? 45  LYS A CA  1 
ATOM   372  C  C   . LYS A 1 45  ? -23.668 2.974   30.097  1.00 16.14  ? 45  LYS A C   1 
ATOM   373  O  O   . LYS A 1 45  ? -22.661 2.470   29.656  1.00 18.50  ? 45  LYS A O   1 
ATOM   374  C  CB  . LYS A 1 45  ? -23.657 5.231   30.855  1.00 18.39  ? 45  LYS A CB  1 
ATOM   375  C  CG  . LYS A 1 45  ? -23.581 6.185   31.977  1.00 26.56  ? 45  LYS A CG  1 
ATOM   376  C  CD  . LYS A 1 45  ? -23.589 7.618   31.507  1.00 36.81  ? 45  LYS A CD  1 
ATOM   377  N  N   . PRO A 1 46  ? -24.944 2.789   29.566  1.00 16.90  ? 46  PRO A N   1 
ATOM   378  C  CA  . PRO A 1 46  ? -24.993 2.127   28.245  1.00 16.63  ? 46  PRO A CA  1 
ATOM   379  C  C   . PRO A 1 46  ? -24.151 2.883   27.274  1.00 12.91  ? 46  PRO A C   1 
ATOM   380  O  O   . PRO A 1 46  ? -24.109 4.078   27.355  1.00 14.64  ? 46  PRO A O   1 
ATOM   381  C  CB  . PRO A 1 46  ? -26.499 2.157   27.932  1.00 19.03  ? 46  PRO A CB  1 
ATOM   382  C  CG  . PRO A 1 46  ? -27.252 2.329   29.312  1.00 21.77  ? 46  PRO A CG  1 
ATOM   383  C  CD  . PRO A 1 46  ? -26.281 3.050   30.182  1.00 20.38  ? 46  PRO A CD  1 
ATOM   384  N  N   . LEU A 1 47  ? -23.598 2.127   26.331  1.00 16.46  ? 47  LEU A N   1 
ATOM   385  C  CA  . LEU A 1 47  ? -22.842 2.774   25.363  1.00 15.78  ? 47  LEU A CA  1 
ATOM   386  C  C   . LEU A 1 47  ? -23.855 3.413   24.349  1.00 19.01  ? 47  LEU A C   1 
ATOM   387  O  O   . LEU A 1 47  ? -24.887 2.729   24.065  1.00 30.56  ? 47  LEU A O   1 
ATOM   388  C  CB  . LEU A 1 47  ? -22.081 1.721   24.561  1.00 23.93  ? 47  LEU A CB  1 
ATOM   389  C  CG  . LEU A 1 47  ? -20.950 2.087   23.617  1.00 23.60  ? 47  LEU A CG  1 
ATOM   390  C  CD1 . LEU A 1 47  ? -20.015 2.857   24.543  1.00 34.84  ? 47  LEU A CD1 1 
ATOM   391  C  CD2 . LEU A 1 47  ? -20.388 0.761   23.076  1.00 24.24  ? 47  LEU A CD2 1 
ATOM   392  N  N   . SER A 1 48  ? -23.636 4.570   23.818  1.00 13.36  ? 48  SER A N   1 
ATOM   393  C  CA  . SER A 1 48  ? -24.496 5.168   22.791  1.00 13.89  ? 48  SER A CA  1 
ATOM   394  C  C   . SER A 1 48  ? -23.726 5.227   21.475  1.00 13.63  ? 48  SER A C   1 
ATOM   395  O  O   . SER A 1 48  ? -22.666 5.935   21.335  1.00 13.02  ? 48  SER A O   1 
ATOM   396  C  CB  . SER A 1 48  ? -24.799 6.656   23.246  1.00 15.39  ? 48  SER A CB  1 
ATOM   397  O  OG  . SER A 1 48  ? -25.436 7.358   22.219  1.00 19.25  ? 48  SER A OG  1 
ATOM   398  N  N   . VAL A 1 49  ? -24.156 4.445   20.558  1.00 13.74  ? 49  VAL A N   1 
ATOM   399  C  CA  . VAL A 1 49  ? -23.523 4.333   19.295  1.00 15.46  ? 49  VAL A CA  1 
ATOM   400  C  C   . VAL A 1 49  ? -24.512 4.936   18.265  1.00 16.44  ? 49  VAL A C   1 
ATOM   401  O  O   . VAL A 1 49  ? -25.576 4.359   18.036  1.00 22.07  ? 49  VAL A O   1 
ATOM   402  C  CB  . VAL A 1 49  ? -23.235 2.861   18.871  1.00 17.10  ? 49  VAL A CB  1 
ATOM   403  C  CG1 . VAL A 1 49  ? -22.637 2.849   17.427  1.00 23.48  ? 49  VAL A CG1 1 
ATOM   404  C  CG2 . VAL A 1 49  ? -22.410 2.160   19.978  1.00 19.33  ? 49  VAL A CG2 1 
ATOM   405  N  N   . SER A 1 50  ? -24.214 6.085   17.639  1.00 15.91  ? 50  SER A N   1 
ATOM   406  C  CA  . SER A 1 50  ? -25.182 6.817   16.772  1.00 18.61  ? 50  SER A CA  1 
ATOM   407  C  C   . SER A 1 50  ? -24.538 6.891   15.485  1.00 16.28  ? 50  SER A C   1 
ATOM   408  O  O   . SER A 1 50  ? -23.851 7.882   15.143  1.00 18.46  ? 50  SER A O   1 
ATOM   409  C  CB  . SER A 1 50  ? -25.640 8.207   17.360  1.00 22.48  ? 50  SER A CB  1 
ATOM   410  O  OG  . SER A 1 50  ? -26.197 7.947   18.686  1.00 25.30  ? 50  SER A OG  1 
ATOM   411  N  N   . TYR A 1 51  ? -24.816 5.912   14.643  1.00 16.55  ? 51  TYR A N   1 
ATOM   412  C  CA  . TYR A 1 51  ? -24.189 5.807   13.341  1.00 15.49  ? 51  TYR A CA  1 
ATOM   413  C  C   . TYR A 1 51  ? -25.151 6.090   12.131  1.00 18.52  ? 51  TYR A C   1 
ATOM   414  O  O   . TYR A 1 51  ? -24.727 5.891   11.001  1.00 18.10  ? 51  TYR A O   1 
ATOM   415  C  CB  . TYR A 1 51  ? -23.487 4.455   13.138  1.00 15.01  ? 51  TYR A CB  1 
ATOM   416  C  CG  . TYR A 1 51  ? -22.212 4.150   13.905  1.00 12.99  ? 51  TYR A CG  1 
ATOM   417  C  CD1 . TYR A 1 51  ? -21.519 5.166   14.561  1.00 14.70  ? 51  TYR A CD1 1 
ATOM   418  C  CD2 . TYR A 1 51  ? -21.750 2.831   13.956  1.00 12.71  ? 51  TYR A CD2 1 
ATOM   419  C  CE1 . TYR A 1 51  ? -20.303 4.818   15.220  1.00 11.96  ? 51  TYR A CE1 1 
ATOM   420  C  CE2 . TYR A 1 51  ? -20.592 2.478   14.649  1.00 12.47  ? 51  TYR A CE2 1 
ATOM   421  C  CZ  . TYR A 1 51  ? -19.875 3.549   15.274  1.00 11.90  ? 51  TYR A CZ  1 
ATOM   422  O  OH  . TYR A 1 51  ? -18.685 3.162   15.916  1.00 11.84  ? 51  TYR A OH  1 
ATOM   423  N  N   . ASP A 1 52  ? -26.383 6.510   12.424  1.00 21.36  ? 52  ASP A N   1 
ATOM   424  C  CA  . ASP A 1 52  ? -27.381 6.803   11.421  1.00 22.73  ? 52  ASP A CA  1 
ATOM   425  C  C   . ASP A 1 52  ? -26.970 7.748   10.306  1.00 21.40  ? 52  ASP A C   1 
ATOM   426  O  O   . ASP A 1 52  ? -27.505 7.577   9.179   1.00 22.27  ? 52  ASP A O   1 
ATOM   427  C  CB  . ASP A 1 52  ? -28.731 7.209   12.102  1.00 28.98  ? 52  ASP A CB  1 
ATOM   428  C  CG  . ASP A 1 52  ? -28.554 8.159   13.321  1.00 30.06  ? 52  ASP A CG  1 
ATOM   429  O  OD1 . ASP A 1 52  ? -27.735 7.912   14.235  1.00 37.05  ? 52  ASP A OD1 1 
ATOM   430  O  OD2 . ASP A 1 52  ? -29.327 9.128   13.385  1.00 57.24  ? 52  ASP A OD2 1 
ATOM   431  N  N   . GLN A 1 53  ? -26.039 8.637   10.549  1.00 23.71  ? 53  GLN A N   1 
ATOM   432  C  CA  . GLN A 1 53  ? -25.636 9.566   9.480   1.00 24.27  ? 53  GLN A CA  1 
ATOM   433  C  C   . GLN A 1 53  ? -24.190 9.351   9.019   1.00 18.70  ? 53  GLN A C   1 
ATOM   434  O  O   . GLN A 1 53  ? -23.605 10.232  8.405   1.00 19.00  ? 53  GLN A O   1 
ATOM   435  C  CB  . GLN A 1 53  ? -25.863 11.041  9.971   1.00 29.47  ? 53  GLN A CB  1 
ATOM   436  C  CG  . GLN A 1 53  ? -27.305 11.278  10.551  1.00 36.53  ? 53  GLN A CG  1 
ATOM   437  C  CD  . GLN A 1 53  ? -28.290 11.356  9.409   1.00 53.00  ? 53  GLN A CD  1 
ATOM   438  O  OE1 . GLN A 1 53  ? -27.879 11.546  8.262   1.00 59.82  ? 53  GLN A OE1 1 
ATOM   439  N  NE2 . GLN A 1 53  ? -29.594 11.172  9.696   1.00 44.67  ? 53  GLN A NE2 1 
ATOM   440  N  N   . ALA A 1 54  ? -23.667 8.203   9.288   1.00 18.58  ? 54  ALA A N   1 
ATOM   441  C  CA  . ALA A 1 54  ? -22.295 7.984   8.902   1.00 16.79  ? 54  ALA A CA  1 
ATOM   442  C  C   . ALA A 1 54  ? -22.055 8.078   7.436   1.00 19.69  ? 54  ALA A C   1 
ATOM   443  O  O   . ALA A 1 54  ? -22.865 7.628   6.617   1.00 23.61  ? 54  ALA A O   1 
ATOM   444  C  CB  . ALA A 1 54  ? -21.713 6.593   9.392   1.00 20.66  ? 54  ALA A CB  1 
ATOM   445  N  N   . THR A 1 55  ? -20.980 8.733   7.008   1.00 15.66  ? 55  THR A N   1 
ATOM   446  C  CA  . THR A 1 55  ? -20.672 8.951   5.611   1.00 16.70  ? 55  THR A CA  1 
ATOM   447  C  C   . THR A 1 55  ? -19.311 8.364   5.346   1.00 13.40  ? 55  THR A C   1 
ATOM   448  O  O   . THR A 1 55  ? -18.317 8.983   5.595   1.00 13.83  ? 55  THR A O   1 
ATOM   449  C  CB  . THR A 1 55  ? -20.625 10.447  5.238   1.00 22.03  ? 55  THR A CB  1 
ATOM   450  O  OG1 . THR A 1 55  ? -21.872 11.097  5.375   1.00 28.47  ? 55  THR A OG1 1 
ATOM   451  C  CG2 . THR A 1 55  ? -20.170 10.514  3.717   1.00 26.26  ? 55  THR A CG2 1 
ATOM   452  N  N   . SER A 1 56  ? -19.368 7.165   4.827   1.00 14.11  ? 56  SER A N   1 
ATOM   453  C  CA  . SER A 1 56  ? -18.181 6.500   4.491   1.00 13.53  ? 56  SER A CA  1 
ATOM   454  C  C   . SER A 1 56  ? -17.870 7.127   3.176   1.00 13.68  ? 56  SER A C   1 
ATOM   455  O  O   . SER A 1 56  ? -18.692 7.580   2.348   1.00 15.41  ? 56  SER A O   1 
ATOM   456  C  CB  . SER A 1 56  ? -18.394 5.002   4.384   1.00 14.29  ? 56  SER A CB  1 
ATOM   457  O  OG  . SER A 1 56  ? -18.904 4.658   3.117   1.00 15.99  ? 56  SER A OG  1 
ATOM   458  N  N   . LEU A 1 57  ? -16.605 7.218   2.999   1.00 10.10  ? 57  LEU A N   1 
ATOM   459  C  CA  . LEU A 1 57  ? -15.972 7.842   1.804   1.00 13.79  ? 57  LEU A CA  1 
ATOM   460  C  C   . LEU A 1 57  ? -15.075 6.974   0.919   1.00 12.61  ? 57  LEU A C   1 
ATOM   461  O  O   . LEU A 1 57  ? -15.273 6.914   -0.276  1.00 14.07  ? 57  LEU A O   1 
ATOM   462  C  CB  . LEU A 1 57  ? -14.992 8.926   2.259   1.00 17.98  ? 57  LEU A CB  1 
ATOM   463  C  CG  . LEU A 1 57  ? -15.245 10.370  2.651   1.00 24.39  ? 57  LEU A CG  1 
ATOM   464  C  CD1 . LEU A 1 57  ? -14.042 10.890  3.433   1.00 26.51  ? 57  LEU A CD1 1 
ATOM   465  C  CD2 . LEU A 1 57  ? -15.422 11.203  1.396   1.00 27.27  ? 57  LEU A CD2 1 
ATOM   466  N  N   . ARG A 1 58  ? -14.031 6.392   1.528   1.00 17.01  ? 58  ARG A N   1 
ATOM   467  C  CA  . ARG A 1 58  ? -12.989 5.596   0.848   1.00 16.10  ? 58  ARG A CA  1 
ATOM   468  C  C   . ARG A 1 58  ? -12.580 4.321   1.614   1.00 11.87  ? 58  ARG A C   1 
ATOM   469  O  O   . ARG A 1 58  ? -12.755 4.257   2.831   1.00 12.75  ? 58  ARG A O   1 
ATOM   470  C  CB  . ARG A 1 58  ? -11.698 6.447   0.801   1.00 18.01  ? 58  ARG A CB  1 
ATOM   471  C  CG  . ARG A 1 58  ? -11.358 7.226   -0.469  1.00 27.05  ? 58  ARG A CG  1 
ATOM   472  C  CD  . ARG A 1 58  ? -9.866  7.191   -0.755  1.00 18.42  ? 58  ARG A CD  1 
ATOM   473  N  NE  . ARG A 1 58  ? -9.075  7.131   0.470   1.00 16.84  ? 58  ARG A NE  1 
ATOM   474  C  CZ  . ARG A 1 58  ? -7.758  7.307   0.519   1.00 16.77  ? 58  ARG A CZ  1 
ATOM   475  N  NH1 . ARG A 1 58  ? -7.079  7.555   -0.592  1.00 20.30  ? 58  ARG A NH1 1 
ATOM   476  N  NH2 . ARG A 1 58  ? -7.120  7.235   1.679   1.00 18.94  ? 58  ARG A NH2 1 
ATOM   477  N  N   . ILE A 1 59  ? -12.037 3.313   0.918   1.00 14.94  ? 59  ILE A N   1 
ATOM   478  C  CA  . ILE A 1 59  ? -11.497 2.134   1.609   1.00 13.18  ? 59  ILE A CA  1 
ATOM   479  C  C   . ILE A 1 59  ? -10.032 2.217   1.165   1.00 11.59  ? 59  ILE A C   1 
ATOM   480  O  O   . ILE A 1 59  ? -9.765  2.370   -0.036  1.00 17.12  ? 59  ILE A O   1 
ATOM   481  C  CB  . ILE A 1 59  ? -12.074 0.803   1.294   1.00 14.82  ? 59  ILE A CB  1 
ATOM   482  C  CG1 . ILE A 1 59  ? -11.384 -0.223  2.177   1.00 14.30  ? 59  ILE A CG1 1 
ATOM   483  C  CG2 . ILE A 1 59  ? -11.874 0.511   -0.168  1.00 16.30  ? 59  ILE A CG2 1 
ATOM   484  C  CD1 . ILE A 1 59  ? -12.176 -1.495  2.141   1.00 14.96  ? 59  ILE A CD1 1 
ATOM   485  N  N   . LEU A 1 60  ? -9.087  1.984   1.999   1.00 13.81  ? 60  LEU A N   1 
ATOM   486  C  CA  . LEU A 1 60  ? -7.728  2.052   1.779   1.00 10.57  ? 60  LEU A CA  1 
ATOM   487  C  C   . LEU A 1 60  ? -6.719  0.903   2.279   1.00 12.62  ? 60  LEU A C   1 
ATOM   488  O  O   . LEU A 1 60  ? -6.857  0.560   3.418   1.00 12.21  ? 60  LEU A O   1 
ATOM   489  C  CB  . LEU A 1 60  ? -7.114  3.375   2.339   1.00 13.34  ? 60  LEU A CB  1 
ATOM   490  C  CG  . LEU A 1 60  ? -5.617  3.475   2.302   1.00 12.29  ? 60  LEU A CG  1 
ATOM   491  C  CD1 . LEU A 1 60  ? -5.030  3.846   0.856   1.00 15.45  ? 60  LEU A CD1 1 
ATOM   492  C  CD2 . LEU A 1 60  ? -5.041  4.617   3.266   1.00 14.24  ? 60  LEU A CD2 1 
ATOM   493  N  N   . ASN A 1 61  ? -5.924  0.311   1.474   1.00 12.42  ? 61  ASN A N   1 
ATOM   494  C  CA  . ASN A 1 61  ? -4.885  -0.596  1.825   1.00 13.64  ? 61  ASN A CA  1 
ATOM   495  C  C   . ASN A 1 61  ? -3.584  0.108   2.254   1.00 13.25  ? 61  ASN A C   1 
ATOM   496  O  O   . ASN A 1 61  ? -2.966  0.635   1.350   1.00 14.95  ? 61  ASN A O   1 
ATOM   497  C  CB  . ASN A 1 61  ? -4.683  -1.715  0.771   1.00 14.43  ? 61  ASN A CB  1 
ATOM   498  C  CG  . ASN A 1 61  ? -3.556  -2.704  1.151   1.00 12.64  ? 61  ASN A CG  1 
ATOM   499  O  OD1 . ASN A 1 61  ? -2.672  -2.531  2.040   1.00 14.57  ? 61  ASN A OD1 1 
ATOM   500  N  ND2 . ASN A 1 61  ? -3.596  -3.964  0.602   1.00 15.05  ? 61  ASN A ND2 1 
ATOM   501  N  N   . ASN A 1 62  ? -3.500  0.319   3.519   1.00 13.68  ? 62  ASN A N   1 
ATOM   502  C  CA  . ASN A 1 62  ? -2.362  1.125   3.944   1.00 12.89  ? 62  ASN A CA  1 
ATOM   503  C  C   . ASN A 1 62  ? -1.126  0.335   4.106   1.00 11.40  ? 62  ASN A C   1 
ATOM   504  O  O   . ASN A 1 62  ? -0.113  0.862   4.578   1.00 17.90  ? 62  ASN A O   1 
ATOM   505  C  CB  . ASN A 1 62  ? -2.653  1.886   5.229   1.00 16.90  ? 62  ASN A CB  1 
ATOM   506  C  CG  . ASN A 1 62  ? -2.859  0.973   6.420   1.00 14.35  ? 62  ASN A CG  1 
ATOM   507  O  OD1 . ASN A 1 62  ? -2.377  -0.163  6.444   1.00 13.26  ? 62  ASN A OD1 1 
ATOM   508  N  ND2 . ASN A 1 62  ? -3.589  1.464   7.404   1.00 19.54  ? 62  ASN A ND2 1 
ATOM   509  N  N   . GLY A 1 63  ? -1.206  -0.990  3.834   1.00 14.17  ? 63  GLY A N   1 
ATOM   510  C  CA  . GLY A 1 63  ? -0.043  -1.921  3.972   1.00 11.31  ? 63  GLY A CA  1 
ATOM   511  C  C   . GLY A 1 63  ? 0.155   -2.734  5.281   1.00 14.58  ? 63  GLY A C   1 
ATOM   512  O  O   . GLY A 1 63  ? 0.992   -3.623  5.521   1.00 14.51  ? 63  GLY A O   1 
ATOM   513  N  N   . HIS A 1 64  ? -0.653  -2.362  6.215   1.00 12.43  ? 64  HIS A N   1 
ATOM   514  C  CA  . HIS A 1 64  ? -0.755  -3.003  7.618   1.00 12.07  ? 64  HIS A CA  1 
ATOM   515  C  C   . HIS A 1 64  ? -2.141  -3.584  7.748   1.00 12.02  ? 64  HIS A C   1 
ATOM   516  O  O   . HIS A 1 64  ? -2.187  -4.698  8.338   1.00 17.06  ? 64  HIS A O   1 
ATOM   517  C  CB  . HIS A 1 64  ? -0.527  -1.895  8.669   1.00 12.18  ? 64  HIS A CB  1 
ATOM   518  C  CG  . HIS A 1 64  ? 0.798   -1.203  8.542   1.00 12.79  ? 64  HIS A CG  1 
ATOM   519  N  ND1 . HIS A 1 64  ? 2.005   -1.858  8.695   1.00 14.16  ? 64  HIS A ND1 1 
ATOM   520  C  CD2 . HIS A 1 64  ? 1.050   0.090   8.270   1.00 14.88  ? 64  HIS A CD2 1 
ATOM   521  C  CE1 . HIS A 1 64  ? 2.963   -0.951  8.546   1.00 16.47  ? 64  HIS A CE1 1 
ATOM   522  N  NE2 . HIS A 1 64  ? 2.426   0.223   8.213   1.00 16.74  ? 64  HIS A NE2 1 
ATOM   523  N  N   . ALA A 1 65  ? -3.139  -2.955  7.274   1.00 10.75  ? 65  ALA A N   1 
ATOM   524  C  CA  . ALA A 1 65  ? -4.494  -3.467  7.246   1.00 10.63  ? 65  ALA A CA  1 
ATOM   525  C  C   . ALA A 1 65  ? -5.186  -2.738  6.126   1.00 10.72  ? 65  ALA A C   1 
ATOM   526  O  O   . ALA A 1 65  ? -4.522  -2.071  5.316   1.00 12.87  ? 65  ALA A O   1 
ATOM   527  C  CB  . ALA A 1 65  ? -5.181  -3.329  8.639   1.00 11.45  ? 65  ALA A CB  1 
ATOM   528  N  N   . PHE A 1 66  ? -6.514  -2.721  6.116   1.00 10.82  ? 66  PHE A N   1 
ATOM   529  C  CA  . PHE A 1 66  ? -7.328  -1.781  5.288   1.00 11.41  ? 66  PHE A CA  1 
ATOM   530  C  C   . PHE A 1 66  ? -8.121  -0.914  6.173   1.00 11.24  ? 66  PHE A C   1 
ATOM   531  O  O   . PHE A 1 66  ? -8.774  -1.399  7.137   1.00 11.65  ? 66  PHE A O   1 
ATOM   532  C  CB  . PHE A 1 66  ? -8.071  -2.476  4.193   1.00 12.43  ? 66  PHE A CB  1 
ATOM   533  C  CG  . PHE A 1 66  ? -9.109  -3.397  4.658   1.00 11.75  ? 66  PHE A CG  1 
ATOM   534  C  CD1 . PHE A 1 66  ? -10.367 -2.924  5.009   1.00 12.76  ? 66  PHE A CD1 1 
ATOM   535  C  CD2 . PHE A 1 66  ? -8.874  -4.784  4.817   1.00 12.12  ? 66  PHE A CD2 1 
ATOM   536  C  CE1 . PHE A 1 66  ? -11.370 -3.775  5.524   1.00 12.13  ? 66  PHE A CE1 1 
ATOM   537  C  CE2 . PHE A 1 66  ? -9.888  -5.664  5.321   1.00 12.69  ? 66  PHE A CE2 1 
ATOM   538  C  CZ  . PHE A 1 66  ? -11.145 -5.149  5.667   1.00 12.55  ? 66  PHE A CZ  1 
ATOM   539  N  N   . ASN A 1 67  ? -8.297  0.354   5.751   1.00 11.31  ? 67  ASN A N   1 
ATOM   540  C  CA  . ASN A 1 67  ? -9.159  1.303   6.525   1.00 12.04  ? 67  ASN A CA  1 
ATOM   541  C  C   . ASN A 1 67  ? -10.443 1.772   5.769   1.00 10.16  ? 67  ASN A C   1 
ATOM   542  O  O   . ASN A 1 67  ? -10.320 2.211   4.617   1.00 14.11  ? 67  ASN A O   1 
ATOM   543  C  CB  . ASN A 1 67  ? -8.393  2.596   6.905   1.00 15.84  ? 67  ASN A CB  1 
ATOM   544  C  CG  . ASN A 1 67  ? -7.291  2.404   7.934   1.00 16.92  ? 67  ASN A CG  1 
ATOM   545  O  OD1 . ASN A 1 67  ? -7.231  1.396   8.625   1.00 18.84  ? 67  ASN A OD1 1 
ATOM   546  N  ND2 . ASN A 1 67  ? -6.439  3.418   8.057   1.00 20.37  ? 67  ASN A ND2 1 
ATOM   547  N  N   . VAL A 1 68  ? -11.651 1.679   6.374   1.00 13.48  ? 68  VAL A N   1 
ATOM   548  C  CA  . VAL A 1 68  ? -12.819 2.217   5.793   1.00 11.72  ? 68  VAL A CA  1 
ATOM   549  C  C   . VAL A 1 68  ? -12.838 3.642   6.476   1.00 13.20  ? 68  VAL A C   1 
ATOM   550  O  O   . VAL A 1 68  ? -12.872 3.745   7.715   1.00 12.33  ? 68  VAL A O   1 
ATOM   551  C  CB  . VAL A 1 68  ? -14.054 1.407   6.024   1.00 12.52  ? 68  VAL A CB  1 
ATOM   552  C  CG1 . VAL A 1 68  ? -15.274 2.224   5.573   1.00 14.39  ? 68  VAL A CG1 1 
ATOM   553  C  CG2 . VAL A 1 68  ? -13.861 0.116   5.210   1.00 14.72  ? 68  VAL A CG2 1 
ATOM   554  N  N   . GLU A 1 69  ? -12.798 4.705   5.660   1.00 13.98  ? 69  GLU A N   1 
ATOM   555  C  CA  . GLU A 1 69  ? -12.752 6.109   6.153   1.00 14.20  ? 69  GLU A CA  1 
ATOM   556  C  C   . GLU A 1 69  ? -14.003 6.805   6.152   1.00 14.59  ? 69  GLU A C   1 
ATOM   557  O  O   . GLU A 1 69  ? -14.846 6.576   5.257   1.00 14.71  ? 69  GLU A O   1 
ATOM   558  C  CB  . GLU A 1 69  ? -11.808 6.804   5.198   1.00 14.93  ? 69  GLU A CB  1 
ATOM   559  C  CG  . GLU A 1 69  ? -10.474 6.282   5.306   1.00 14.84  ? 69  GLU A CG  1 
ATOM   560  C  CD  . GLU A 1 69  ? -9.628  6.631   4.109   1.00 14.21  ? 69  GLU A CD  1 
ATOM   561  O  OE1 . GLU A 1 69  ? -10.137 7.391   3.188   1.00 17.47  ? 69  GLU A OE1 1 
ATOM   562  O  OE2 . GLU A 1 69  ? -8.430  6.318   4.007   1.00 16.05  ? 69  GLU A OE2 1 
ATOM   563  N  N   . PHE A 1 70  ? -14.186 7.699   7.079   1.00 13.09  ? 70  PHE A N   1 
ATOM   564  C  CA  . PHE A 1 70  ? -15.382 8.412   7.150   1.00 12.26  ? 70  PHE A CA  1 
ATOM   565  C  C   . PHE A 1 70  ? -15.162 9.898   7.061   1.00 14.10  ? 70  PHE A C   1 
ATOM   566  O  O   . PHE A 1 70  ? -14.110 10.405  7.452   1.00 14.58  ? 70  PHE A O   1 
ATOM   567  C  CB  . PHE A 1 70  ? -16.086 8.067   8.418   1.00 12.31  ? 70  PHE A CB  1 
ATOM   568  C  CG  . PHE A 1 70  ? -16.668 6.652   8.380   1.00 12.48  ? 70  PHE A CG  1 
ATOM   569  C  CD1 . PHE A 1 70  ? -15.814 5.540   8.611   1.00 12.64  ? 70  PHE A CD1 1 
ATOM   570  C  CD2 . PHE A 1 70  ? -17.975 6.450   8.066   1.00 12.91  ? 70  PHE A CD2 1 
ATOM   571  C  CE1 . PHE A 1 70  ? -16.303 4.279   8.481   1.00 13.26  ? 70  PHE A CE1 1 
ATOM   572  C  CE2 . PHE A 1 70  ? -18.496 5.159   7.947   1.00 12.80  ? 70  PHE A CE2 1 
ATOM   573  C  CZ  . PHE A 1 70  ? -17.611 4.054   8.137   1.00 13.62  ? 70  PHE A CZ  1 
ATOM   574  N  N   . ASP A 1 71  ? -16.165 10.626  6.607   1.00 15.99  ? 71  ASP A N   1 
ATOM   575  C  CA  . ASP A 1 71  ? -16.076 12.063  6.682   1.00 15.41  ? 71  ASP A CA  1 
ATOM   576  C  C   . ASP A 1 71  ? -16.461 12.408  8.140   1.00 15.33  ? 71  ASP A C   1 
ATOM   577  O  O   . ASP A 1 71  ? -17.564 12.254  8.580   1.00 19.26  ? 71  ASP A O   1 
ATOM   578  C  CB  . ASP A 1 71  ? -17.097 12.610  5.699   1.00 21.02  ? 71  ASP A CB  1 
ATOM   579  C  CG  . ASP A 1 71  ? -17.311 14.102  5.897   1.00 25.10  ? 71  ASP A CG  1 
ATOM   580  O  OD1 . ASP A 1 71  ? -16.576 14.786  6.606   1.00 21.44  ? 71  ASP A OD1 1 
ATOM   581  O  OD2 . ASP A 1 71  ? -18.253 14.705  5.393   1.00 40.09  ? 71  ASP A OD2 1 
ATOM   582  N  N   . ASP A 1 72  ? -15.431 12.913  8.765   1.00 13.13  ? 72  ASP A N   1 
ATOM   583  C  CA  . ASP A 1 72  ? -15.503 13.305  10.182  1.00 14.22  ? 72  ASP A CA  1 
ATOM   584  C  C   . ASP A 1 72  ? -15.487 14.829  10.317  1.00 15.97  ? 72  ASP A C   1 
ATOM   585  O  O   . ASP A 1 72  ? -15.162 15.352  11.363  1.00 17.49  ? 72  ASP A O   1 
ATOM   586  C  CB  . ASP A 1 72  ? -14.428 12.657  11.063  1.00 13.69  ? 72  ASP A CB  1 
ATOM   587  C  CG  . ASP A 1 72  ? -13.078 13.174  10.695  1.00 14.05  ? 72  ASP A CG  1 
ATOM   588  O  OD1 . ASP A 1 72  ? -12.931 13.892  9.624   1.00 16.08  ? 72  ASP A OD1 1 
ATOM   589  O  OD2 . ASP A 1 72  ? -12.074 12.872  11.455  1.00 15.72  ? 72  ASP A OD2 1 
ATOM   590  N  N   . SER A 1 73  ? -15.934 15.566  9.293   1.00 16.95  ? 73  SER A N   1 
ATOM   591  C  CA  . SER A 1 73  ? -15.900 17.122  9.331   1.00 19.10  ? 73  SER A CA  1 
ATOM   592  C  C   . SER A 1 73  ? -17.270 17.635  9.935   1.00 18.64  ? 73  SER A C   1 
ATOM   593  O  O   . SER A 1 73  ? -17.364 18.849  10.058  1.00 18.28  ? 73  SER A O   1 
ATOM   594  C  CB  . SER A 1 73  ? -15.637 17.626  7.950   1.00 23.67  ? 73  SER A CB  1 
ATOM   595  O  OG  . SER A 1 73  ? -16.762 17.406  7.158   1.00 20.01  ? 73  SER A OG  1 
ATOM   596  N  N   . GLN A 1 74  ? -18.260 16.796  10.200  1.00 22.89  ? 74  GLN A N   1 
ATOM   597  C  CA  . GLN A 1 74  ? -19.508 17.237  10.824  1.00 22.97  ? 74  GLN A CA  1 
ATOM   598  C  C   . GLN A 1 74  ? -19.757 16.258  11.941  1.00 20.77  ? 74  GLN A C   1 
ATOM   599  O  O   . GLN A 1 74  ? -19.219 15.120  11.937  1.00 16.82  ? 74  GLN A O   1 
ATOM   600  C  CB  . GLN A 1 74  ? -20.719 17.255  9.808   1.00 24.48  ? 74  GLN A CB  1 
ATOM   601  C  CG  . GLN A 1 74  ? -20.484 18.338  8.824   1.00 28.91  ? 74  GLN A CG  1 
ATOM   602  C  CD  . GLN A 1 74  ? -20.754 17.879  7.340   1.00 37.96  ? 74  GLN A CD  1 
ATOM   603  O  OE1 . GLN A 1 74  ? -21.909 17.889  6.984   1.00 41.84  ? 74  GLN A OE1 1 
ATOM   604  N  NE2 . GLN A 1 74  ? -19.678 17.552  6.472   1.00 30.65  ? 74  GLN A NE2 1 
ATOM   605  N  N   . ASP A 1 75  ? -20.708 16.637  12.756  1.00 26.80  ? 75  ASP A N   1 
ATOM   606  C  CA  . ASP A 1 75  ? -21.114 15.779  13.879  1.00 20.08  ? 75  ASP A CA  1 
ATOM   607  C  C   . ASP A 1 75  ? -22.133 14.705  13.174  1.00 22.29  ? 75  ASP A C   1 
ATOM   608  O  O   . ASP A 1 75  ? -23.369 14.934  13.105  1.00 27.09  ? 75  ASP A O   1 
ATOM   609  C  CB  . ASP A 1 75  ? -21.578 16.501  15.079  1.00 34.94  ? 75  ASP A CB  1 
ATOM   610  C  CG  . ASP A 1 75  ? -21.290 15.714  16.280  1.00 45.77  ? 75  ASP A CG  1 
ATOM   611  O  OD1 . ASP A 1 75  ? -20.097 15.448  16.565  1.00 35.09  ? 75  ASP A OD1 1 
ATOM   612  O  OD2 . ASP A 1 75  ? -22.276 15.268  16.872  1.00 42.73  ? 75  ASP A OD2 1 
ATOM   613  N  N   . LYS A 1 76  ? -21.599 13.530  12.837  1.00 17.35  ? 76  LYS A N   1 
ATOM   614  C  CA  . LYS A 1 76  ? -22.411 12.463  12.168  1.00 21.73  ? 76  LYS A CA  1 
ATOM   615  C  C   . LYS A 1 76  ? -22.597 11.085  12.754  1.00 37.41  ? 76  LYS A C   1 
ATOM   616  O  O   . LYS A 1 76  ? -23.709 10.418  12.638  1.00 40.03  ? 76  LYS A O   1 
ATOM   617  C  CB  . LYS A 1 76  ? -21.869 12.341  10.711  1.00 22.55  ? 76  LYS A CB  1 
ATOM   618  C  CG  . LYS A 1 76  ? -22.208 13.525  9.816   1.00 33.29  ? 76  LYS A CG  1 
ATOM   619  C  CD  . LYS A 1 76  ? -21.753 13.288  8.366   1.00 40.08  ? 76  LYS A CD  1 
ATOM   620  C  CE  . LYS A 1 76  ? -21.693 14.390  7.274   1.00 39.72  ? 76  LYS A CE  1 
ATOM   621  N  NZ  . LYS A 1 76  ? -21.681 13.926  5.857   1.00 30.66  ? 76  LYS A NZ  1 
ATOM   622  N  N   . ALA A 1 77  ? -21.523 10.490  12.999  1.00 24.31  ? 77  ALA A N   1 
ATOM   623  C  CA  . ALA A 1 77  ? -21.307 9.062   13.520  1.00 15.74  ? 77  ALA A CA  1 
ATOM   624  C  C   . ALA A 1 77  ? -20.577 9.217   14.812  1.00 13.89  ? 77  ALA A C   1 
ATOM   625  O  O   . ALA A 1 77  ? -19.354 9.350   14.846  1.00 19.71  ? 77  ALA A O   1 
ATOM   626  C  CB  . ALA A 1 77  ? -20.436 8.394   12.476  1.00 17.42  ? 77  ALA A CB  1 
ATOM   627  N  N   . VAL A 1 78  ? -21.255 9.276   15.887  1.00 13.60  ? 78  VAL A N   1 
ATOM   628  C  CA  . VAL A 1 78  ? -20.624 9.460   17.168  1.00 14.77  ? 78  VAL A CA  1 
ATOM   629  C  C   . VAL A 1 78  ? -20.895 8.410   18.237  1.00 11.58  ? 78  VAL A C   1 
ATOM   630  O  O   . VAL A 1 78  ? -21.911 7.739   18.283  1.00 15.42  ? 78  VAL A O   1 
ATOM   631  C  CB  . VAL A 1 78  ? -21.033 10.809  17.745  1.00 22.32  ? 78  VAL A CB  1 
ATOM   632  C  CG1 . VAL A 1 78  ? -20.736 11.907  16.736  1.00 26.52  ? 78  VAL A CG1 1 
ATOM   633  C  CG2 . VAL A 1 78  ? -22.513 10.773  18.086  1.00 22.97  ? 78  VAL A CG2 1 
ATOM   634  N  N   . LEU A 1 79  ? -19.845 8.251   19.050  1.00 10.85  ? 79  LEU A N   1 
ATOM   635  C  CA  . LEU A 1 79  ? -19.842 7.331   20.222  1.00 11.54  ? 79  LEU A CA  1 
ATOM   636  C  C   . LEU A 1 79  ? -19.862 8.203   21.431  1.00 10.76  ? 79  LEU A C   1 
ATOM   637  O  O   . LEU A 1 79  ? -19.013 9.143   21.553  1.00 12.85  ? 79  LEU A O   1 
ATOM   638  C  CB  . LEU A 1 79  ? -18.566 6.437   20.125  1.00 12.82  ? 79  LEU A CB  1 
ATOM   639  C  CG  . LEU A 1 79  ? -18.439 5.403   21.155  1.00 12.14  ? 79  LEU A CG  1 
ATOM   640  C  CD1 . LEU A 1 79  ? -19.466 4.328   20.893  1.00 17.94  ? 79  LEU A CD1 1 
ATOM   641  C  CD2 . LEU A 1 79  ? -17.082 4.766   21.089  1.00 12.12  ? 79  LEU A CD2 1 
ATOM   642  N  N   . LYS A 1 80  ? -20.702 7.859   22.381  1.00 11.64  ? 80  LYS A N   1 
ATOM   643  C  CA  . LYS A 1 80  ? -20.781 8.565   23.669  1.00 12.44  ? 80  LYS A CA  1 
ATOM   644  C  C   . LYS A 1 80  ? -21.287 7.633   24.707  1.00 11.72  ? 80  LYS A C   1 
ATOM   645  O  O   . LYS A 1 80  ? -21.588 6.491   24.428  1.00 12.25  ? 80  LYS A O   1 
ATOM   646  C  CB  . LYS A 1 80  ? -21.521 9.846   23.574  1.00 17.09  ? 80  LYS A CB  1 
ATOM   647  C  CG  . LYS A 1 80  ? -22.922 9.651   23.379  1.00 16.20  ? 80  LYS A CG  1 
ATOM   648  C  CD  . LYS A 1 80  ? -23.635 11.002  23.125  1.00 25.54  ? 80  LYS A CD  1 
ATOM   649  C  CE  . LYS A 1 80  ? -22.922 11.562  21.927  1.00 39.67  ? 80  LYS A CE  1 
ATOM   650  N  NZ  . LYS A 1 80  ? -23.506 12.665  21.050  1.00 58.62  ? 80  LYS A NZ  1 
ATOM   651  N  N   . GLY A 1 81  ? -21.404 8.155   25.933  1.00 13.91  ? 81  GLY A N   1 
ATOM   652  C  CA  . GLY A 1 81  ? -21.906 7.280   27.039  1.00 15.39  ? 81  GLY A CA  1 
ATOM   653  C  C   . GLY A 1 81  ? -20.914 6.232   27.334  1.00 14.32  ? 81  GLY A C   1 
ATOM   654  O  O   . GLY A 1 81  ? -19.691 6.448   27.161  1.00 13.31  ? 81  GLY A O   1 
ATOM   655  N  N   . GLY A 1 82  ? -21.349 5.108   27.890  1.00 17.38  ? 82  GLY A N   1 
ATOM   656  C  CA  . GLY A 1 82  ? -20.390 4.089   28.282  1.00 18.45  ? 82  GLY A CA  1 
ATOM   657  C  C   . GLY A 1 82  ? -19.524 4.725   29.363  1.00 16.45  ? 82  GLY A C   1 
ATOM   658  O  O   . GLY A 1 82  ? -20.052 5.358   30.278  1.00 21.39  ? 82  GLY A O   1 
ATOM   659  N  N   . PRO A 1 83  ? -18.192 4.566   29.272  1.00 14.19  ? 83  PRO A N   1 
ATOM   660  C  CA  . PRO A 1 83  ? -17.322 5.147   30.199  1.00 13.61  ? 83  PRO A CA  1 
ATOM   661  C  C   . PRO A 1 83  ? -16.877 6.586   29.785  1.00 14.51  ? 83  PRO A C   1 
ATOM   662  O  O   . PRO A 1 83  ? -16.089 7.186   30.478  1.00 16.59  ? 83  PRO A O   1 
ATOM   663  C  CB  . PRO A 1 83  ? -16.038 4.255   30.043  1.00 15.22  ? 83  PRO A CB  1 
ATOM   664  C  CG  . PRO A 1 83  ? -16.011 3.918   28.597  1.00 12.44  ? 83  PRO A CG  1 
ATOM   665  C  CD  . PRO A 1 83  ? -17.509 3.703   28.295  1.00 12.86  ? 83  PRO A CD  1 
ATOM   666  N  N   . LEU A 1 84  ? -17.372 7.104   28.701  1.00 12.43  ? 84  LEU A N   1 
ATOM   667  C  CA  . LEU A 1 84  ? -16.867 8.273   28.110  1.00 12.36  ? 84  LEU A CA  1 
ATOM   668  C  C   . LEU A 1 84  ? -17.463 9.517   28.681  1.00 13.61  ? 84  LEU A C   1 
ATOM   669  O  O   . LEU A 1 84  ? -18.654 9.570   28.937  1.00 15.51  ? 84  LEU A O   1 
ATOM   670  C  CB  . LEU A 1 84  ? -17.108 8.291   26.593  1.00 10.30  ? 84  LEU A CB  1 
ATOM   671  C  CG  . LEU A 1 84  ? -16.504 7.032   25.900  1.00 9.79   ? 84  LEU A CG  1 
ATOM   672  C  CD1 . LEU A 1 84  ? -16.954 7.011   24.410  1.00 11.24  ? 84  LEU A CD1 1 
ATOM   673  C  CD2 . LEU A 1 84  ? -14.930 7.040   25.994  1.00 10.74  ? 84  LEU A CD2 1 
ATOM   674  N  N   . ASP A 1 85  ? -16.711 10.602  28.753  1.00 14.91  ? 85  ASP A N   1 
ATOM   675  C  CA  . ASP A 1 85  ? -17.236 11.962  29.000  1.00 18.45  ? 85  ASP A CA  1 
ATOM   676  C  C   . ASP A 1 85  ? -17.236 12.578  27.525  1.00 18.77  ? 85  ASP A C   1 
ATOM   677  O  O   . ASP A 1 85  ? -16.210 12.587  26.804  1.00 22.72  ? 85  ASP A O   1 
ATOM   678  C  CB  . ASP A 1 85  ? -16.253 12.714  29.963  1.00 22.57  ? 85  ASP A CB  1 
ATOM   679  C  CG  . ASP A 1 85  ? -16.287 12.212  31.413  1.00 34.81  ? 85  ASP A CG  1 
ATOM   680  O  OD1 . ASP A 1 85  ? -17.336 11.616  31.848  1.00 42.32  ? 85  ASP A OD1 1 
ATOM   681  O  OD2 . ASP A 1 85  ? -15.216 12.511  32.101  1.00 45.83  ? 85  ASP A OD2 1 
ATOM   682  N  N   . GLY A 1 86  ? -18.310 13.210  27.144  1.00 23.66  ? 86  GLY A N   1 
ATOM   683  C  CA  . GLY A 1 86  ? -18.176 13.832  25.868  1.00 22.41  ? 86  GLY A CA  1 
ATOM   684  C  C   . GLY A 1 86  ? -18.644 13.074  24.676  1.00 21.03  ? 86  GLY A C   1 
ATOM   685  O  O   . GLY A 1 86  ? -18.976 11.858  24.834  1.00 25.82  ? 86  GLY A O   1 
ATOM   686  N  N   A THR A 1 87  ? -18.134 13.508  23.543  0.50 14.70  ? 87  THR A N   1 
ATOM   687  N  N   B THR A 1 87  ? -18.049 13.487  23.555  0.50 14.60  ? 87  THR A N   1 
ATOM   688  C  CA  A THR A 1 87  ? -18.585 12.851  22.314  0.50 13.79  ? 87  THR A CA  1 
ATOM   689  C  CA  B THR A 1 87  ? -18.506 12.877  22.307  0.50 14.33  ? 87  THR A CA  1 
ATOM   690  C  C   A THR A 1 87  ? -17.349 12.615  21.467  0.50 10.74  ? 87  THR A C   1 
ATOM   691  C  C   B THR A 1 87  ? -17.299 12.625  21.452  0.50 10.86  ? 87  THR A C   1 
ATOM   692  O  O   A THR A 1 87  ? -16.445 13.446  21.366  0.50 11.55  ? 87  THR A O   1 
ATOM   693  O  O   B THR A 1 87  ? -16.360 13.434  21.356  0.50 11.68  ? 87  THR A O   1 
ATOM   694  C  CB  A THR A 1 87  ? -19.525 13.776  21.573  0.50 15.01  ? 87  THR A CB  1 
ATOM   695  C  CB  B THR A 1 87  ? -19.430 13.884  21.584  0.50 17.30  ? 87  THR A CB  1 
ATOM   696  O  OG1 A THR A 1 87  ? -18.936 15.042  21.485  0.50 13.63  ? 87  THR A OG1 1 
ATOM   697  O  OG1 B THR A 1 87  ? -20.652 14.133  22.302  0.50 21.92  ? 87  THR A OG1 1 
ATOM   698  C  CG2 A THR A 1 87  ? -20.694 14.105  22.360  0.50 19.73  ? 87  THR A CG2 1 
ATOM   699  C  CG2 B THR A 1 87  ? -19.790 13.487  20.140  0.50 19.03  ? 87  THR A CG2 1 
ATOM   700  N  N   . TYR A 1 88  ? -17.361 11.478  20.803  1.00 10.08  ? 88  TYR A N   1 
ATOM   701  C  CA  . TYR A 1 88  ? -16.234 10.997  20.009  1.00 9.19   ? 88  TYR A CA  1 
ATOM   702  C  C   . TYR A 1 88  ? -16.764 10.674  18.614  1.00 9.74   ? 88  TYR A C   1 
ATOM   703  O  O   . TYR A 1 88  ? -17.713 9.978   18.440  1.00 13.18  ? 88  TYR A O   1 
ATOM   704  C  CB  . TYR A 1 88  ? -15.606 9.747   20.604  1.00 9.37   ? 88  TYR A CB  1 
ATOM   705  C  CG  . TYR A 1 88  ? -14.870 9.982   21.941  1.00 8.12   ? 88  TYR A CG  1 
ATOM   706  C  CD1 . TYR A 1 88  ? -15.526 10.305  23.128  1.00 9.27   ? 88  TYR A CD1 1 
ATOM   707  C  CD2 . TYR A 1 88  ? -13.454 9.837   21.965  1.00 7.98   ? 88  TYR A CD2 1 
ATOM   708  C  CE1 . TYR A 1 88  ? -14.853 10.528  24.291  1.00 9.04   ? 88  TYR A CE1 1 
ATOM   709  C  CE2 . TYR A 1 88  ? -12.758 9.979   23.180  1.00 7.72   ? 88  TYR A CE2 1 
ATOM   710  C  CZ  . TYR A 1 88  ? -13.464 10.280  24.335  1.00 8.45   ? 88  TYR A CZ  1 
ATOM   711  O  OH  . TYR A 1 88  ? -12.756 10.374  25.504  1.00 8.69   ? 88  TYR A OH  1 
ATOM   712  N  N   A ARG A 1 89  ? -16.092 11.124  17.639  0.50 7.70   ? 89  ARG A N   1 
ATOM   713  N  N   B ARG A 1 89  ? -16.037 11.215  17.620  0.50 9.31   ? 89  ARG A N   1 
ATOM   714  C  CA  A ARG A 1 89  ? -16.653 11.035  16.308  0.50 7.75   ? 89  ARG A CA  1 
ATOM   715  C  CA  B ARG A 1 89  ? -16.303 11.110  16.074  0.50 9.24   ? 89  ARG A CA  1 
ATOM   716  C  C   A ARG A 1 89  ? -15.823 9.992   15.583  0.50 7.04   ? 89  ARG A C   1 
ATOM   717  C  C   B ARG A 1 89  ? -15.634 9.973   15.413  0.50 7.26   ? 89  ARG A C   1 
ATOM   718  O  O   A ARG A 1 89  ? -14.576 9.920   15.702  0.50 6.38   ? 89  ARG A O   1 
ATOM   719  O  O   B ARG A 1 89  ? -14.392 9.799   15.383  0.50 7.28   ? 89  ARG A O   1 
ATOM   720  C  CB  A ARG A 1 89  ? -16.442 12.396  15.666  0.50 8.37   ? 89  ARG A CB  1 
ATOM   721  C  CB  B ARG A 1 89  ? -15.913 12.383  15.250  0.50 10.09  ? 89  ARG A CB  1 
ATOM   722  C  CG  A ARG A 1 89  ? -17.041 12.503  14.324  0.50 9.81   ? 89  ARG A CG  1 
ATOM   723  C  CG  B ARG A 1 89  ? -16.823 13.546  15.594  0.50 16.28  ? 89  ARG A CG  1 
ATOM   724  C  CD  A ARG A 1 89  ? -16.871 13.916  13.720  0.50 8.61   ? 89  ARG A CD  1 
ATOM   725  C  CD  B ARG A 1 89  ? -16.604 14.607  14.493  0.50 18.86  ? 89  ARG A CD  1 
ATOM   726  N  NE  A ARG A 1 89  ? -17.616 14.902  14.513  0.50 8.14   ? 89  ARG A NE  1 
ATOM   727  N  NE  B ARG A 1 89  ? -17.314 15.809  14.939  0.50 22.08  ? 89  ARG A NE  1 
ATOM   728  C  CZ  A ARG A 1 89  ? -17.471 16.237  14.318  0.50 9.00   ? 89  ARG A CZ  1 
ATOM   729  C  CZ  B ARG A 1 89  ? -16.934 17.029  14.600  0.50 24.81  ? 89  ARG A CZ  1 
ATOM   730  N  NH1 A ARG A 1 89  ? -16.666 16.741  13.371  0.50 9.75   ? 89  ARG A NH1 1 
ATOM   731  N  NH1 B ARG A 1 89  ? -15.907 17.202  13.719  0.50 24.47  ? 89  ARG A NH1 1 
ATOM   732  N  NH2 A ARG A 1 89  ? -18.041 17.084  15.141  0.50 9.12   ? 89  ARG A NH2 1 
ATOM   733  N  NH2 B ARG A 1 89  ? -17.604 18.051  15.113  0.50 30.17  ? 89  ARG A NH2 1 
ATOM   734  N  N   . LEU A 1 90  ? -16.470 9.151   14.759  1.00 8.37   ? 90  LEU A N   1 
ATOM   735  C  CA  . LEU A 1 90  ? -15.873 8.055   13.963  1.00 7.71   ? 90  LEU A CA  1 
ATOM   736  C  C   . LEU A 1 90  ? -15.021 8.626   12.830  1.00 8.57   ? 90  LEU A C   1 
ATOM   737  O  O   . LEU A 1 90  ? -15.517 9.425   12.023  1.00 10.37  ? 90  LEU A O   1 
ATOM   738  C  CB  . LEU A 1 90  ? -16.987 7.205   13.389  1.00 9.07   ? 90  LEU A CB  1 
ATOM   739  C  CG  . LEU A 1 90  ? -16.541 6.022   12.517  1.00 9.56   ? 90  LEU A CG  1 
ATOM   740  C  CD1 . LEU A 1 90  ? -15.787 4.960   13.318  1.00 10.34  ? 90  LEU A CD1 1 
ATOM   741  C  CD2 . LEU A 1 90  ? -17.814 5.355   11.883  1.00 12.82  ? 90  LEU A CD2 1 
ATOM   742  N  N   . ILE A 1 91  ? -13.793 8.172   12.748  1.00 8.42   ? 91  ILE A N   1 
ATOM   743  C  CA  . ILE A 1 91  ? -12.894 8.541   11.657  1.00 8.19   ? 91  ILE A CA  1 
ATOM   744  C  C   . ILE A 1 91  ? -12.624 7.362   10.712  1.00 8.17   ? 91  ILE A C   1 
ATOM   745  O  O   . ILE A 1 91  ? -12.526 7.552   9.514   1.00 8.75   ? 91  ILE A O   1 
ATOM   746  C  CB  . ILE A 1 91  ? -11.599 9.197   12.152  1.00 8.67   ? 91  ILE A CB  1 
ATOM   747  C  CG1 . ILE A 1 91  ? -10.704 9.586   10.974  1.00 12.33  ? 91  ILE A CG1 1 
ATOM   748  C  CG2 . ILE A 1 91  ? -10.834 8.379   13.197  1.00 9.74   ? 91  ILE A CG2 1 
ATOM   749  C  CD1 . ILE A 1 91  ? -9.604  10.543  11.389  1.00 15.45  ? 91  ILE A CD1 1 
ATOM   750  N  N   . GLN A 1 92  ? -12.482 6.132   11.238  1.00 8.25   ? 92  GLN A N   1 
ATOM   751  C  CA  . GLN A 1 92  ? -12.144 4.985   10.388  1.00 8.70   ? 92  GLN A CA  1 
ATOM   752  C  C   . GLN A 1 92  ? -12.433 3.718   11.169  1.00 7.70   ? 92  GLN A C   1 
ATOM   753  O  O   . GLN A 1 92  ? -12.504 3.736   12.388  1.00 8.16   ? 92  GLN A O   1 
ATOM   754  C  CB  . GLN A 1 92  ? -10.689 4.999   9.940   1.00 10.48  ? 92  GLN A CB  1 
ATOM   755  C  CG  . GLN A 1 92  ? -9.655  5.089   11.075  1.00 10.58  ? 92  GLN A CG  1 
ATOM   756  C  CD  . GLN A 1 92  ? -8.882  3.838   11.220  1.00 10.26  ? 92  GLN A CD  1 
ATOM   757  O  OE1 . GLN A 1 92  ? -9.405  2.709   11.216  1.00 11.03  ? 92  GLN A OE1 1 
ATOM   758  N  NE2 . GLN A 1 92  ? -7.594  3.990   11.358  1.00 13.08  ? 92  GLN A NE2 1 
ATOM   759  N  N   . PHE A 1 93  ? -12.578 2.625   10.422  1.00 8.22   ? 93  PHE A N   1 
ATOM   760  C  CA  . PHE A 1 93  ? -12.440 1.304   11.036  1.00 8.14   ? 93  PHE A CA  1 
ATOM   761  C  C   . PHE A 1 93  ? -11.519 0.474   10.211  1.00 7.63   ? 93  PHE A C   1 
ATOM   762  O  O   . PHE A 1 93  ? -11.271 0.687   9.018   1.00 9.34   ? 93  PHE A O   1 
ATOM   763  C  CB  . PHE A 1 93  ? -13.807 0.620   11.247  1.00 8.86   ? 93  PHE A CB  1 
ATOM   764  C  CG  . PHE A 1 93  ? -14.554 0.147   10.004  1.00 8.76   ? 93  PHE A CG  1 
ATOM   765  C  CD1 . PHE A 1 93  ? -14.199 -1.016  9.334   1.00 10.33  ? 93  PHE A CD1 1 
ATOM   766  C  CD2 . PHE A 1 93  ? -15.654 0.866   9.564   1.00 10.90  ? 93  PHE A CD2 1 
ATOM   767  C  CE1 . PHE A 1 93  ? -14.887 -1.412  8.212   1.00 10.95  ? 93  PHE A CE1 1 
ATOM   768  C  CE2 . PHE A 1 93  ? -16.375 0.408   8.436   1.00 13.63  ? 93  PHE A CE2 1 
ATOM   769  C  CZ  . PHE A 1 93  ? -15.994 -0.713  7.771   1.00 13.84  ? 93  PHE A CZ  1 
ATOM   770  N  N   . HIS A 1 94  ? -10.989 -0.568  10.877  1.00 7.40   ? 94  HIS A N   1 
ATOM   771  C  CA  . HIS A 1 94  ? -10.133 -1.555  10.283  1.00 7.46   ? 94  HIS A CA  1 
ATOM   772  C  C   . HIS A 1 94  ? -10.223 -2.826  11.103  1.00 6.52   ? 94  HIS A C   1 
ATOM   773  O  O   . HIS A 1 94  ? -10.838 -2.829  12.164  1.00 7.07   ? 94  HIS A O   1 
ATOM   774  C  CB  . HIS A 1 94  ? -8.661  -1.089  10.204  1.00 7.97   ? 94  HIS A CB  1 
ATOM   775  C  CG  . HIS A 1 94  ? -8.124  -0.794  11.574  1.00 7.54   ? 94  HIS A CG  1 
ATOM   776  N  ND1 . HIS A 1 94  ? -8.277  0.420   12.203  1.00 7.49   ? 94  HIS A ND1 1 
ATOM   777  C  CD2 . HIS A 1 94  ? -7.538  -1.647  12.484  1.00 6.97   ? 94  HIS A CD2 1 
ATOM   778  C  CE1 . HIS A 1 94  ? -7.811  0.287   13.452  1.00 6.86   ? 94  HIS A CE1 1 
ATOM   779  N  NE2 . HIS A 1 94  ? -7.358  -0.953  13.667  1.00 6.73   ? 94  HIS A NE2 1 
ATOM   780  N  N   . PHE A 1 95  ? -9.553  -3.870  10.638  1.00 7.03   ? 95  PHE A N   1 
ATOM   781  C  CA  . PHE A 1 95  ? -9.516  -5.155  11.311  1.00 7.06   ? 95  PHE A CA  1 
ATOM   782  C  C   . PHE A 1 95  ? -8.090  -5.605  11.522  1.00 7.04   ? 95  PHE A C   1 
ATOM   783  O  O   . PHE A 1 95  ? -7.152  -5.150  10.832  1.00 7.71   ? 95  PHE A O   1 
ATOM   784  C  CB  . PHE A 1 95  ? -10.262 -6.243  10.484  1.00 7.73   ? 95  PHE A CB  1 
ATOM   785  C  CG  . PHE A 1 95  ? -11.678 -5.967  10.161  1.00 7.50   ? 95  PHE A CG  1 
ATOM   786  C  CD1 . PHE A 1 95  ? -12.006 -5.087  9.098   1.00 8.44   ? 95  PHE A CD1 1 
ATOM   787  C  CD2 . PHE A 1 95  ? -12.725 -6.600  10.847  1.00 8.30   ? 95  PHE A CD2 1 
ATOM   788  C  CE1 . PHE A 1 95  ? -13.367 -4.887  8.751   1.00 9.53   ? 95  PHE A CE1 1 
ATOM   789  C  CE2 . PHE A 1 95  ? -14.052 -6.383  10.503  1.00 8.83   ? 95  PHE A CE2 1 
ATOM   790  C  CZ  . PHE A 1 95  ? -14.359 -5.509  9.427   1.00 9.38   ? 95  PHE A CZ  1 
ATOM   791  N  N   . HIS A 1 96  ? -7.927  -6.590  12.422  1.00 6.78   ? 96  HIS A N   1 
ATOM   792  C  CA  . HIS A 1 96  ? -6.750  -7.392  12.574  1.00 6.58   ? 96  HIS A CA  1 
ATOM   793  C  C   . HIS A 1 96  ? -7.188  -8.845  12.464  1.00 6.45   ? 96  HIS A C   1 
ATOM   794  O  O   . HIS A 1 96  ? -8.261  -9.189  12.985  1.00 6.75   ? 96  HIS A O   1 
ATOM   795  C  CB  . HIS A 1 96  ? -6.053  -7.161  13.936  1.00 7.02   ? 96  HIS A CB  1 
ATOM   796  C  CG  . HIS A 1 96  ? -5.762  -5.723  14.213  1.00 6.50   ? 96  HIS A CG  1 
ATOM   797  N  ND1 . HIS A 1 96  ? -4.539  -5.150  14.038  1.00 7.80   ? 96  HIS A ND1 1 
ATOM   798  C  CD2 . HIS A 1 96  ? -6.582  -4.711  14.624  1.00 6.34   ? 96  HIS A CD2 1 
ATOM   799  C  CE1 . HIS A 1 96  ? -4.610  -3.875  14.344  1.00 7.77   ? 96  HIS A CE1 1 
ATOM   800  N  NE2 . HIS A 1 96  ? -5.865  -3.548  14.701  1.00 6.76   ? 96  HIS A NE2 1 
ATOM   801  N  N   . TRP A 1 97  ? -6.409  -9.702  11.811  1.00 6.54   ? 97  TRP A N   1 
ATOM   802  C  CA  . TRP A 1 97  ? -6.815  -11.066 11.624  1.00 7.04   ? 97  TRP A CA  1 
ATOM   803  C  C   . TRP A 1 97  ? -5.635  -11.978 11.474  1.00 6.87   ? 97  TRP A C   1 
ATOM   804  O  O   . TRP A 1 97  ? -4.455  -11.557 11.391  1.00 8.01   ? 97  TRP A O   1 
ATOM   805  C  CB  . TRP A 1 97  ? -7.761  -11.185 10.359  1.00 7.92   ? 97  TRP A CB  1 
ATOM   806  C  CG  . TRP A 1 97  ? -7.095  -10.779 9.075   1.00 8.01   ? 97  TRP A CG  1 
ATOM   807  C  CD1 . TRP A 1 97  ? -6.421  -11.609 8.225   1.00 9.12   ? 97  TRP A CD1 1 
ATOM   808  C  CD2 . TRP A 1 97  ? -7.015  -9.511  8.501   1.00 7.96   ? 97  TRP A CD2 1 
ATOM   809  N  NE1 . TRP A 1 97  ? -6.001  -10.906 7.122   1.00 9.97   ? 97  TRP A NE1 1 
ATOM   810  C  CE2 . TRP A 1 97  ? -6.337  -9.602  7.305   1.00 8.82   ? 97  TRP A CE2 1 
ATOM   811  C  CE3 . TRP A 1 97  ? -7.509  -8.220  8.907   1.00 8.41   ? 97  TRP A CE3 1 
ATOM   812  C  CZ2 . TRP A 1 97  ? -6.139  -8.481  6.423   1.00 10.08  ? 97  TRP A CZ2 1 
ATOM   813  C  CZ3 . TRP A 1 97  ? -7.259  -7.127  8.091   1.00 9.07   ? 97  TRP A CZ3 1 
ATOM   814  C  CH2 . TRP A 1 97  ? -6.622  -7.255  6.854   1.00 10.18  ? 97  TRP A CH2 1 
ATOM   815  N  N   . GLY A 1 98  ? -5.936  -13.281 11.498  1.00 7.85   ? 98  GLY A N   1 
ATOM   816  C  CA  . GLY A 1 98  ? -4.913  -14.291 11.530  1.00 7.92   ? 98  GLY A CA  1 
ATOM   817  C  C   . GLY A 1 98  ? -4.730  -14.988 10.198  1.00 8.71   ? 98  GLY A C   1 
ATOM   818  O  O   . GLY A 1 98  ? -5.455  -14.861 9.225   1.00 9.50   ? 98  GLY A O   1 
ATOM   819  N  N   . SER A 1 99  ? -3.696  -15.855 10.205  1.00 9.37   ? 99  SER A N   1 
ATOM   820  C  CA  . SER A 1 99  ? -3.451  -16.802 9.108   1.00 10.84  ? 99  SER A CA  1 
ATOM   821  C  C   . SER A 1 99  ? -4.365  -18.035 9.238   1.00 10.88  ? 99  SER A C   1 
ATOM   822  O  O   . SER A 1 99  ? -4.528  -18.753 8.231   1.00 12.34  ? 99  SER A O   1 
ATOM   823  C  CB  . SER A 1 99  ? -2.021  -17.171 9.057   1.00 12.56  ? 99  SER A CB  1 
ATOM   824  O  OG  . SER A 1 99  ? -1.549  -17.692 10.309  1.00 12.46  ? 99  SER A OG  1 
ATOM   825  N  N   . LEU A 1 100 ? -4.900  -18.314 10.415  1.00 10.06  ? 100 LEU A N   1 
ATOM   826  C  CA  . LEU A 1 100 ? -5.780  -19.440 10.760  1.00 11.74  ? 100 LEU A CA  1 
ATOM   827  C  C   . LEU A 1 100 ? -6.878  -18.913 11.537  1.00 10.31  ? 100 LEU A C   1 
ATOM   828  O  O   . LEU A 1 100 ? -6.755  -17.844 12.160  1.00 10.92  ? 100 LEU A O   1 
ATOM   829  C  CB  . LEU A 1 100 ? -4.973  -20.441 11.600  1.00 19.22  ? 100 LEU A CB  1 
ATOM   830  C  CG  . LEU A 1 100 ? -3.600  -20.830 11.027  1.00 22.14  ? 100 LEU A CG  1 
ATOM   831  C  CD1 . LEU A 1 100 ? -2.617  -21.359 12.067  1.00 32.31  ? 100 LEU A CD1 1 
ATOM   832  C  CD2 . LEU A 1 100 ? -3.874  -21.881 9.971   1.00 29.32  ? 100 LEU A CD2 1 
ATOM   833  N  N   . ASP A 1 101 ? -7.932  -19.691 11.711  1.00 11.18  ? 101 ASP A N   1 
ATOM   834  C  CA  . ASP A 1 101 ? -9.097  -19.189 12.489  1.00 10.24  ? 101 ASP A CA  1 
ATOM   835  C  C   . ASP A 1 101 ? -8.846  -19.077 13.988  1.00 10.70  ? 101 ASP A C   1 
ATOM   836  O  O   . ASP A 1 101 ? -9.462  -18.363 14.691  1.00 12.51  ? 101 ASP A O   1 
ATOM   837  C  CB  . ASP A 1 101 ? -10.322 -20.074 12.227  1.00 12.08  ? 101 ASP A CB  1 
ATOM   838  C  CG  . ASP A 1 101 ? -10.774 -20.131 10.829  1.00 13.66  ? 101 ASP A CG  1 
ATOM   839  O  OD1 . ASP A 1 101 ? -10.418 -19.286 10.016  1.00 13.49  ? 101 ASP A OD1 1 
ATOM   840  O  OD2 . ASP A 1 101 ? -11.705 -20.988 10.604  1.00 17.15  ? 101 ASP A OD2 1 
ATOM   841  N  N   . GLY A 1 102 ? -7.833  -19.870 14.448  1.00 11.54  ? 102 GLY A N   1 
ATOM   842  C  CA  . GLY A 1 102 ? -7.486  -19.853 15.893  1.00 11.23  ? 102 GLY A CA  1 
ATOM   843  C  C   . GLY A 1 102 ? -6.673  -18.693 16.394  1.00 10.51  ? 102 GLY A C   1 
ATOM   844  O  O   . GLY A 1 102 ? -6.323  -18.688 17.585  1.00 11.38  ? 102 GLY A O   1 
ATOM   845  N  N   A GLN A 1 103 ? -6.410  -17.712 15.550  0.50 9.16   ? 103 GLN A N   1 
ATOM   846  N  N   B GLN A 1 103 ? -6.369  -17.698 15.593  0.50 9.32   ? 103 GLN A N   1 
ATOM   847  C  CA  A GLN A 1 103 ? -5.687  -16.523 15.979  0.50 8.40   ? 103 GLN A CA  1 
ATOM   848  C  CA  B GLN A 1 103 ? -5.694  -16.505 16.124  0.50 8.57   ? 103 GLN A CA  1 
ATOM   849  C  C   A GLN A 1 103 ? -6.119  -15.360 15.158  0.50 7.55   ? 103 GLN A C   1 
ATOM   850  C  C   B GLN A 1 103 ? -6.063  -15.383 15.213  0.50 7.55   ? 103 GLN A C   1 
ATOM   851  O  O   A GLN A 1 103 ? -6.671  -15.530 14.039  0.50 8.16   ? 103 GLN A O   1 
ATOM   852  O  O   B GLN A 1 103 ? -6.548  -15.603 14.098  0.50 8.09   ? 103 GLN A O   1 
ATOM   853  C  CB  A GLN A 1 103 ? -4.168  -16.750 15.875  0.50 8.49   ? 103 GLN A CB  1 
ATOM   854  C  CB  B GLN A 1 103 ? -4.156  -16.742 16.255  0.50 10.54  ? 103 GLN A CB  1 
ATOM   855  C  CG  A GLN A 1 103 ? -3.619  -16.894 14.461  0.50 10.21  ? 103 GLN A CG  1 
ATOM   856  C  CG  B GLN A 1 103 ? -3.594  -17.040 14.865  0.50 10.61  ? 103 GLN A CG  1 
ATOM   857  C  CD  A GLN A 1 103 ? -2.295  -17.627 14.533  0.50 12.54  ? 103 GLN A CD  1 
ATOM   858  C  CD  B GLN A 1 103 ? -2.124  -17.389 14.904  0.50 11.47  ? 103 GLN A CD  1 
ATOM   859  O  OE1 A GLN A 1 103 ? -2.240  -18.743 15.172  0.50 14.15  ? 103 GLN A OE1 1 
ATOM   860  O  OE1 B GLN A 1 103 ? -1.614  -17.967 15.977  0.50 15.34  ? 103 GLN A OE1 1 
ATOM   861  N  NE2 A GLN A 1 103 ? -1.200  -16.940 14.116  0.50 12.98  ? 103 GLN A NE2 1 
ATOM   862  N  NE2 B GLN A 1 103 ? -1.454  -17.176 13.717  0.50 11.70  ? 103 GLN A NE2 1 
ATOM   863  N  N   . GLY A 1 104 ? -5.769  -14.146 15.625  1.00 7.21   ? 104 GLY A N   1 
ATOM   864  C  CA  . GLY A 1 104 ? -6.035  -12.959 14.825  1.00 7.27   ? 104 GLY A CA  1 
ATOM   865  C  C   . GLY A 1 104 ? -6.469  -11.780 15.670  1.00 6.83   ? 104 GLY A C   1 
ATOM   866  O  O   . GLY A 1 104 ? -6.204  -10.647 15.306  1.00 7.49   ? 104 GLY A O   1 
ATOM   867  N  N   . SER A 1 105 ? -7.209  -12.032 16.781  1.00 6.72   ? 105 SER A N   1 
ATOM   868  C  CA  . SER A 1 105 ? -7.600  -10.902 17.621  1.00 6.80   ? 105 SER A CA  1 
ATOM   869  C  C   . SER A 1 105 ? -6.393  -10.351 18.386  1.00 6.13   ? 105 SER A C   1 
ATOM   870  O  O   . SER A 1 105 ? -5.373  -11.043 18.606  1.00 7.35   ? 105 SER A O   1 
ATOM   871  C  CB  . SER A 1 105 ? -8.737  -11.251 18.561  1.00 6.50   ? 105 SER A CB  1 
ATOM   872  O  OG  . SER A 1 105 ? -8.376  -12.206 19.556  1.00 6.71   ? 105 SER A OG  1 
ATOM   873  N  N   . GLU A 1 106 ? -6.525  -9.110  18.776  1.00 6.15   ? 106 GLU A N   1 
ATOM   874  C  CA  . GLU A 1 106 ? -5.506  -8.382  19.604  1.00 6.17   ? 106 GLU A CA  1 
ATOM   875  C  C   . GLU A 1 106 ? -5.833  -8.570  21.067  1.00 6.16   ? 106 GLU A C   1 
ATOM   876  O  O   . GLU A 1 106 ? -5.063  -9.151  21.859  1.00 6.85   ? 106 GLU A O   1 
ATOM   877  C  CB  . GLU A 1 106 ? -5.443  -6.954  19.146  1.00 6.66   ? 106 GLU A CB  1 
ATOM   878  C  CG  . GLU A 1 106 ? -4.915  -6.826  17.736  1.00 8.66   ? 106 GLU A CG  1 
ATOM   879  C  CD  . GLU A 1 106 ? -4.289  -5.536  17.407  1.00 6.85   ? 106 GLU A CD  1 
ATOM   880  O  OE1 . GLU A 1 106 ? -4.898  -4.483  17.673  1.00 6.77   ? 106 GLU A OE1 1 
ATOM   881  O  OE2 . GLU A 1 106 ? -3.132  -5.552  16.905  1.00 8.20   ? 106 GLU A OE2 1 
ATOM   882  N  N   . HIS A 1 107 ? -7.028  -8.114  21.500  1.00 5.78   ? 107 HIS A N   1 
ATOM   883  C  CA  . HIS A 1 107 ? -7.505  -8.492  22.795  1.00 5.76   ? 107 HIS A CA  1 
ATOM   884  C  C   . HIS A 1 107 ? -7.826  -10.001 22.805  1.00 5.98   ? 107 HIS A C   1 
ATOM   885  O  O   . HIS A 1 107 ? -8.149  -10.609 21.804  1.00 6.31   ? 107 HIS A O   1 
ATOM   886  C  CB  . HIS A 1 107 ? -8.757  -7.683  23.184  1.00 6.24   ? 107 HIS A CB  1 
ATOM   887  C  CG  . HIS A 1 107 ? -8.443  -6.242  23.335  1.00 5.68   ? 107 HIS A CG  1 
ATOM   888  N  ND1 . HIS A 1 107 ? -8.482  -5.349  22.279  1.00 6.27   ? 107 HIS A ND1 1 
ATOM   889  C  CD2 . HIS A 1 107 ? -7.952  -5.531  24.384  1.00 5.85   ? 107 HIS A CD2 1 
ATOM   890  C  CE1 . HIS A 1 107 ? -8.047  -4.171  22.720  1.00 6.20   ? 107 HIS A CE1 1 
ATOM   891  N  NE2 . HIS A 1 107 ? -7.716  -4.232  24.002  1.00 6.12   ? 107 HIS A NE2 1 
ATOM   892  N  N   . THR A 1 108 ? -7.664  -10.578 24.019  1.00 6.77   ? 108 THR A N   1 
ATOM   893  C  CA  . THR A 1 108 ? -8.025  -11.946 24.294  1.00 6.73   ? 108 THR A CA  1 
ATOM   894  C  C   . THR A 1 108 ? -8.986  -11.941 25.489  1.00 6.55   ? 108 THR A C   1 
ATOM   895  O  O   . THR A 1 108 ? -9.007  -10.969 26.262  1.00 7.05   ? 108 THR A O   1 
ATOM   896  C  CB  . THR A 1 108 ? -6.831  -12.833 24.489  1.00 7.84   ? 108 THR A CB  1 
ATOM   897  O  OG1 . THR A 1 108 ? -5.981  -12.358 25.523  1.00 8.14   ? 108 THR A OG1 1 
ATOM   898  C  CG2 . THR A 1 108 ? -6.025  -12.892 23.216  1.00 8.39   ? 108 THR A CG2 1 
ATOM   899  N  N   . VAL A 1 109 ? -9.739  -13.017 25.638  1.00 7.23   ? 109 VAL A N   1 
ATOM   900  C  CA  . VAL A 1 109 ? -10.757 -13.112 26.718  1.00 8.01   ? 109 VAL A CA  1 
ATOM   901  C  C   . VAL A 1 109 ? -10.430 -14.402 27.463  1.00 7.95   ? 109 VAL A C   1 
ATOM   902  O  O   . VAL A 1 109 ? -10.572 -15.514 26.905  1.00 8.21   ? 109 VAL A O   1 
ATOM   903  C  CB  . VAL A 1 109 ? -12.212 -13.117 26.155  1.00 8.08   ? 109 VAL A CB  1 
ATOM   904  C  CG1 . VAL A 1 109 ? -13.183 -13.258 27.318  1.00 9.28   ? 109 VAL A CG1 1 
ATOM   905  C  CG2 . VAL A 1 109 ? -12.481 -11.847 25.354  1.00 9.85   ? 109 VAL A CG2 1 
ATOM   906  N  N   . ASP A 1 110 ? -9.871  -14.291 28.682  1.00 8.75   ? 110 ASP A N   1 
ATOM   907  C  CA  . ASP A 1 110 ? -9.429  -15.512 29.393  1.00 9.17   ? 110 ASP A CA  1 
ATOM   908  C  C   . ASP A 1 110 ? -8.508  -16.326 28.518  1.00 9.43   ? 110 ASP A C   1 
ATOM   909  O  O   . ASP A 1 110 ? -8.579  -17.560 28.447  1.00 10.01  ? 110 ASP A O   1 
ATOM   910  C  CB  . ASP A 1 110 ? -10.604 -16.342 29.885  1.00 11.20  ? 110 ASP A CB  1 
ATOM   911  C  CG  . ASP A 1 110 ? -11.462 -15.577 30.916  1.00 11.61  ? 110 ASP A CG  1 
ATOM   912  O  OD1 . ASP A 1 110 ? -10.879 -14.694 31.598  1.00 13.12  ? 110 ASP A OD1 1 
ATOM   913  O  OD2 . ASP A 1 110 ? -12.613 -15.899 31.064  1.00 14.19  ? 110 ASP A OD2 1 
ATOM   914  N  N   . LYS A 1 111 ? -7.635  -15.594 27.814  1.00 8.63   ? 111 LYS A N   1 
ATOM   915  C  CA  . LYS A 1 111 ? -6.585  -16.131 26.899  1.00 9.55   ? 111 LYS A CA  1 
ATOM   916  C  C   . LYS A 1 111 ? -7.187  -16.669 25.565  1.00 8.69   ? 111 LYS A C   1 
ATOM   917  O  O   . LYS A 1 111 ? -6.378  -17.046 24.704  1.00 10.47  ? 111 LYS A O   1 
ATOM   918  C  CB  . LYS A 1 111 ? -5.660  -17.166 27.532  1.00 11.32  ? 111 LYS A CB  1 
ATOM   919  C  CG  . LYS A 1 111 ? -5.006  -16.651 28.814  1.00 15.87  ? 111 LYS A CG  1 
ATOM   920  C  CD  . LYS A 1 111 ? -3.995  -15.463 28.484  1.00 18.04  ? 111 LYS A CD  1 
ATOM   921  C  CE  . LYS A 1 111 ? -3.223  -14.793 29.647  1.00 21.39  ? 111 LYS A CE  1 
ATOM   922  N  NZ  . LYS A 1 111 ? -2.118  -15.624 29.907  1.00 25.09  ? 111 LYS A NZ  1 
ATOM   923  N  N   . LYS A 1 112 ? -8.480  -16.639 25.372  1.00 8.08   ? 112 LYS A N   1 
ATOM   924  C  CA  . LYS A 1 112 ? -9.040  -17.026 24.076  1.00 8.71   ? 112 LYS A CA  1 
ATOM   925  C  C   . LYS A 1 112 ? -8.722  -15.964 23.024  1.00 7.24   ? 112 LYS A C   1 
ATOM   926  O  O   . LYS A 1 112 ? -8.965  -14.774 23.231  1.00 7.64   ? 112 LYS A O   1 
ATOM   927  C  CB  . LYS A 1 112 ? -10.606 -17.086 24.191  1.00 9.74   ? 112 LYS A CB  1 
ATOM   928  C  CG  . LYS A 1 112 ? -11.287 -17.514 22.884  1.00 10.41  ? 112 LYS A CG  1 
ATOM   929  C  CD  . LYS A 1 112 ? -12.801 -17.383 22.913  1.00 11.98  ? 112 LYS A CD  1 
ATOM   930  C  CE  . LYS A 1 112 ? -13.403 -17.650 21.661  1.00 13.33  ? 112 LYS A CE  1 
ATOM   931  N  NZ  . LYS A 1 112 ? -13.274 -18.936 21.168  1.00 13.78  ? 112 LYS A NZ  1 
ATOM   932  N  N   A LYS A 1 113 ? -8.242  -16.500 21.906  0.50 7.76   ? 113 LYS A N   1 
ATOM   933  N  N   B LYS A 1 113 ? -8.166  -16.411 21.903  0.50 7.61   ? 113 LYS A N   1 
ATOM   934  C  CA  A LYS A 1 113 ? -8.042  -15.718 20.705  0.50 7.54   ? 113 LYS A CA  1 
ATOM   935  C  CA  B LYS A 1 113 ? -7.982  -15.577 20.708  0.50 7.64   ? 113 LYS A CA  1 
ATOM   936  C  C   A LYS A 1 113 ? -9.214  -15.896 19.793  0.50 7.62   ? 113 LYS A C   1 
ATOM   937  C  C   B LYS A 1 113 ? -9.042  -15.862 19.688  0.50 7.34   ? 113 LYS A C   1 
ATOM   938  O  O   A LYS A 1 113 ? -9.709  -17.018 19.609  0.50 8.45   ? 113 LYS A O   1 
ATOM   939  O  O   B LYS A 1 113 ? -9.308  -17.029 19.303  0.50 7.63   ? 113 LYS A O   1 
ATOM   940  C  CB  A LYS A 1 113 ? -6.759  -16.194 19.999  0.50 7.94   ? 113 LYS A CB  1 
ATOM   941  C  CB  B LYS A 1 113 ? -6.640  -15.937 20.034  0.50 8.40   ? 113 LYS A CB  1 
ATOM   942  C  CG  A LYS A 1 113 ? -5.492  -15.923 20.785  0.50 7.82   ? 113 LYS A CG  1 
ATOM   943  C  CG  B LYS A 1 113 ? -5.414  -15.500 20.801  0.50 9.36   ? 113 LYS A CG  1 
ATOM   944  C  CD  A LYS A 1 113 ? -4.258  -16.571 20.107  0.50 10.20  ? 113 LYS A CD  1 
ATOM   945  C  CD  B LYS A 1 113 ? -4.186  -16.161 20.227  0.50 9.77   ? 113 LYS A CD  1 
ATOM   946  C  CE  A LYS A 1 113 ? -2.905  -15.984 20.644  0.50 11.44  ? 113 LYS A CE  1 
ATOM   947  C  CE  B LYS A 1 113 ? -2.938  -15.630 20.988  0.50 12.86  ? 113 LYS A CE  1 
ATOM   948  N  NZ  A LYS A 1 113 ? -2.534  -16.475 21.965  0.50 12.21  ? 113 LYS A NZ  1 
ATOM   949  N  NZ  B LYS A 1 113 ? -1.747  -16.407 20.631  0.50 16.53  ? 113 LYS A NZ  1 
ATOM   950  N  N   . TYR A 1 114 ? -9.709  -14.794 19.221  1.00 7.51   ? 114 TYR A N   1 
ATOM   951  C  CA  . TYR A 1 114 ? -10.707 -14.836 18.197  1.00 7.51   ? 114 TYR A CA  1 
ATOM   952  C  C   . TYR A 1 114 ? -10.017 -14.801 16.815  1.00 6.77   ? 114 TYR A C   1 
ATOM   953  O  O   . TYR A 1 114 ? -8.823  -14.512 16.688  1.00 7.70   ? 114 TYR A O   1 
ATOM   954  C  CB  . TYR A 1 114 ? -11.738 -13.727 18.324  1.00 7.00   ? 114 TYR A CB  1 
ATOM   955  C  CG  . TYR A 1 114 ? -12.684 -13.941 19.484  1.00 7.63   ? 114 TYR A CG  1 
ATOM   956  C  CD1 . TYR A 1 114 ? -12.403 -13.545 20.785  1.00 8.76   ? 114 TYR A CD1 1 
ATOM   957  C  CD2 . TYR A 1 114 ? -13.910 -14.578 19.229  1.00 8.51   ? 114 TYR A CD2 1 
ATOM   958  C  CE1 . TYR A 1 114 ? -13.328 -13.734 21.834  1.00 10.60  ? 114 TYR A CE1 1 
ATOM   959  C  CE2 . TYR A 1 114 ? -14.886 -14.726 20.208  1.00 10.29  ? 114 TYR A CE2 1 
ATOM   960  C  CZ  . TYR A 1 114 ? -14.564 -14.318 21.475  1.00 10.98  ? 114 TYR A CZ  1 
ATOM   961  O  OH  . TYR A 1 114 ? -15.464 -14.447 22.561  1.00 16.23  ? 114 TYR A OH  1 
ATOM   962  N  N   . ALA A 1 115 ? -10.795 -15.123 15.766  1.00 7.20   ? 115 ALA A N   1 
ATOM   963  C  CA  . ALA A 1 115 ? -10.253 -15.140 14.405  1.00 7.45   ? 115 ALA A CA  1 
ATOM   964  C  C   . ALA A 1 115 ? -9.876  -13.738 13.934  1.00 7.29   ? 115 ALA A C   1 
ATOM   965  O  O   . ALA A 1 115 ? -9.015  -13.613 13.038  1.00 7.77   ? 115 ALA A O   1 
ATOM   966  C  CB  . ALA A 1 115 ? -11.288 -15.760 13.463  1.00 8.47   ? 115 ALA A CB  1 
ATOM   967  N  N   . ALA A 1 116 ? -10.520 -12.704 14.438  1.00 6.53   ? 116 ALA A N   1 
ATOM   968  C  CA  . ALA A 1 116 ? -10.215 -11.347 13.997  1.00 7.07   ? 116 ALA A CA  1 
ATOM   969  C  C   . ALA A 1 116 ? -10.808 -10.412 15.008  1.00 6.22   ? 116 ALA A C   1 
ATOM   970  O  O   . ALA A 1 116 ? -11.560 -10.793 15.909  1.00 6.61   ? 116 ALA A O   1 
ATOM   971  C  CB  . ALA A 1 116 ? -10.746 -11.071 12.560  1.00 8.00   ? 116 ALA A CB  1 
ATOM   972  N  N   . GLU A 1 117 ? -10.489 -9.112  14.819  1.00 6.44   ? 117 GLU A N   1 
ATOM   973  C  CA  . GLU A 1 117 ? -11.021 -8.059  15.701  1.00 5.86   ? 117 GLU A CA  1 
ATOM   974  C  C   . GLU A 1 117 ? -11.198 -6.813  14.861  1.00 6.19   ? 117 GLU A C   1 
ATOM   975  O  O   . GLU A 1 117 ? -10.270 -6.399  14.132  1.00 7.66   ? 117 GLU A O   1 
ATOM   976  C  CB  . GLU A 1 117 ? -10.036 -7.840  16.879  1.00 6.48   ? 117 GLU A CB  1 
ATOM   977  C  CG  . GLU A 1 117 ? -10.549 -6.875  17.938  1.00 6.92   ? 117 GLU A CG  1 
ATOM   978  C  CD  . GLU A 1 117 ? -9.639  -6.825  19.163  1.00 5.81   ? 117 GLU A CD  1 
ATOM   979  O  OE1 . GLU A 1 117 ? -8.975  -7.844  19.451  1.00 7.19   ? 117 GLU A OE1 1 
ATOM   980  O  OE2 . GLU A 1 117 ? -9.594  -5.743  19.814  1.00 7.03   ? 117 GLU A OE2 1 
ATOM   981  N  N   . LEU A 1 118 ? -12.352 -6.210  14.984  1.00 5.92   ? 118 LEU A N   1 
ATOM   982  C  CA  . LEU A 1 118 ? -12.744 -4.949  14.311  1.00 6.31   ? 118 LEU A CA  1 
ATOM   983  C  C   . LEU A 1 118 ? -12.500 -3.817  15.293  1.00 6.40   ? 118 LEU A C   1 
ATOM   984  O  O   . LEU A 1 118 ? -12.930 -3.889  16.475  1.00 6.17   ? 118 LEU A O   1 
ATOM   985  C  CB  . LEU A 1 118 ? -14.217 -5.039  13.978  1.00 6.95   ? 118 LEU A CB  1 
ATOM   986  C  CG  . LEU A 1 118 ? -14.934 -3.764  13.580  1.00 7.65   ? 118 LEU A CG  1 
ATOM   987  C  CD1 . LEU A 1 118 ? -14.333 -3.086  12.351  1.00 8.32   ? 118 LEU A CD1 1 
ATOM   988  C  CD2 . LEU A 1 118 ? -16.437 -4.064  13.345  1.00 9.10   ? 118 LEU A CD2 1 
ATOM   989  N  N   . HIS A 1 119 ? -11.870 -2.744  14.820  1.00 5.86   ? 119 HIS A N   1 
ATOM   990  C  CA  . HIS A 1 119 ? -11.616 -1.536  15.589  1.00 6.08   ? 119 HIS A CA  1 
ATOM   991  C  C   . HIS A 1 119 ? -12.292 -0.359  14.903  1.00 5.53   ? 119 HIS A C   1 
ATOM   992  O  O   . HIS A 1 119 ? -11.916 0.002   13.788  1.00 6.94   ? 119 HIS A O   1 
ATOM   993  C  CB  . HIS A 1 119 ? -10.114 -1.252  15.713  1.00 6.16   ? 119 HIS A CB  1 
ATOM   994  C  CG  . HIS A 1 119 ? -9.431  -2.251  16.571  1.00 5.31   ? 119 HIS A CG  1 
ATOM   995  N  ND1 . HIS A 1 119 ? -8.073  -2.502  16.550  1.00 5.55   ? 119 HIS A ND1 1 
ATOM   996  C  CD2 . HIS A 1 119 ? -9.991  -3.064  17.523  1.00 6.18   ? 119 HIS A CD2 1 
ATOM   997  C  CE1 . HIS A 1 119 ? -7.836  -3.433  17.445  1.00 6.05   ? 119 HIS A CE1 1 
ATOM   998  N  NE2 . HIS A 1 119 ? -8.943  -3.781  18.074  1.00 6.06   ? 119 HIS A NE2 1 
ATOM   999  N  N   . LEU A 1 120 ? -13.295 0.241   15.584  1.00 5.98   ? 120 LEU A N   1 
ATOM   1000 C  CA  . LEU A 1 120 ? -13.945 1.488   15.120  1.00 6.71   ? 120 LEU A CA  1 
ATOM   1001 C  C   . LEU A 1 120 ? -13.310 2.592   15.933  1.00 5.65   ? 120 LEU A C   1 
ATOM   1002 O  O   . LEU A 1 120 ? -13.454 2.650   17.135  1.00 5.96   ? 120 LEU A O   1 
ATOM   1003 C  CB  . LEU A 1 120 ? -15.434 1.383   15.333  1.00 7.04   ? 120 LEU A CB  1 
ATOM   1004 C  CG  . LEU A 1 120 ? -16.107 0.305   14.429  1.00 8.92   ? 120 LEU A CG  1 
ATOM   1005 C  CD1 . LEU A 1 120 ? -17.013 -0.567  15.291  1.00 11.69  ? 120 LEU A CD1 1 
ATOM   1006 C  CD2 . LEU A 1 120 ? -16.954 0.988   13.336  1.00 10.15  ? 120 LEU A CD2 1 
ATOM   1007 N  N   . VAL A 1 121 ? -12.568 3.462   15.229  1.00 6.33   ? 121 VAL A N   1 
ATOM   1008 C  CA  . VAL A 1 121 ? -11.716 4.497   15.869  1.00 6.48   ? 121 VAL A CA  1 
ATOM   1009 C  C   . VAL A 1 121 ? -12.453 5.836   15.878  1.00 6.50   ? 121 VAL A C   1 
ATOM   1010 O  O   . VAL A 1 121 ? -12.895 6.296   14.823  1.00 7.37   ? 121 VAL A O   1 
ATOM   1011 C  CB  . VAL A 1 121 ? -10.398 4.601   15.095  1.00 6.97   ? 121 VAL A CB  1 
ATOM   1012 C  CG1 . VAL A 1 121 ? -9.494  5.672   15.720  1.00 8.31   ? 121 VAL A CG1 1 
ATOM   1013 C  CG2 . VAL A 1 121 ? -9.674  3.259   15.009  1.00 7.81   ? 121 VAL A CG2 1 
ATOM   1014 N  N   . HIS A 1 122 ? -12.526 6.437   17.050  1.00 6.28   ? 122 HIS A N   1 
ATOM   1015 C  CA  . HIS A 1 122 ? -13.218 7.698   17.228  1.00 6.58   ? 122 HIS A CA  1 
ATOM   1016 C  C   . HIS A 1 122 ? -12.345 8.682   17.984  1.00 7.08   ? 122 HIS A C   1 
ATOM   1017 O  O   . HIS A 1 122 ? -11.617 8.282   18.899  1.00 7.65   ? 122 HIS A O   1 
ATOM   1018 C  CB  . HIS A 1 122 ? -14.506 7.518   18.067  1.00 7.30   ? 122 HIS A CB  1 
ATOM   1019 C  CG  . HIS A 1 122 ? -15.397 6.385   17.653  1.00 6.64   ? 122 HIS A CG  1 
ATOM   1020 N  ND1 . HIS A 1 122 ? -15.078 5.074   17.908  1.00 6.94   ? 122 HIS A ND1 1 
ATOM   1021 C  CD2 . HIS A 1 122 ? -16.614 6.344   17.030  1.00 7.95   ? 122 HIS A CD2 1 
ATOM   1022 C  CE1 . HIS A 1 122 ? -16.085 4.305   17.466  1.00 7.85   ? 122 HIS A CE1 1 
ATOM   1023 N  NE2 . HIS A 1 122 ? -17.035 5.037   16.905  1.00 8.11   ? 122 HIS A NE2 1 
ATOM   1024 N  N   . TRP A 1 123 ? -12.462 9.987   17.658  1.00 6.67   ? 123 TRP A N   1 
ATOM   1025 C  CA  . TRP A 1 123 ? -11.653 10.991  18.373  1.00 7.01   ? 123 TRP A CA  1 
ATOM   1026 C  C   . TRP A 1 123 ? -12.557 11.969  19.118  1.00 6.87   ? 123 TRP A C   1 
ATOM   1027 O  O   . TRP A 1 123 ? -13.676 12.298  18.702  1.00 7.90   ? 123 TRP A O   1 
ATOM   1028 C  CB  . TRP A 1 123 ? -10.694 11.737  17.414  1.00 8.81   ? 123 TRP A CB  1 
ATOM   1029 C  CG  . TRP A 1 123 ? -11.385 12.367  16.221  1.00 8.93   ? 123 TRP A CG  1 
ATOM   1030 C  CD1 . TRP A 1 123 ? -11.607 11.785  15.021  1.00 9.94   ? 123 TRP A CD1 1 
ATOM   1031 C  CD2 . TRP A 1 123 ? -11.883 13.714  16.101  1.00 9.63   ? 123 TRP A CD2 1 
ATOM   1032 N  NE1 . TRP A 1 123 ? -12.205 12.628  14.156  1.00 10.41  ? 123 TRP A NE1 1 
ATOM   1033 C  CE2 . TRP A 1 123 ? -12.420 13.833  14.794  1.00 11.11  ? 123 TRP A CE2 1 
ATOM   1034 C  CE3 . TRP A 1 123 ? -11.978 14.824  16.975  1.00 11.20  ? 123 TRP A CE3 1 
ATOM   1035 C  CZ2 . TRP A 1 123 ? -13.009 14.980  14.325  1.00 12.67  ? 123 TRP A CZ2 1 
ATOM   1036 C  CZ3 . TRP A 1 123 ? -12.549 15.972  16.491  1.00 13.57  ? 123 TRP A CZ3 1 
ATOM   1037 C  CH2 . TRP A 1 123 ? -13.048 16.055  15.175  1.00 14.29  ? 123 TRP A CH2 1 
ATOM   1038 N  N   . ASN A 1 124 ? -12.028 12.419  20.247  1.00 7.59   ? 124 ASN A N   1 
ATOM   1039 C  CA  . ASN A 1 124 ? -12.793 13.307  21.170  1.00 7.97   ? 124 ASN A CA  1 
ATOM   1040 C  C   . ASN A 1 124 ? -12.934 14.677  20.569  1.00 8.11   ? 124 ASN A C   1 
ATOM   1041 O  O   . ASN A 1 124 ? -11.910 15.370  20.299  1.00 8.74   ? 124 ASN A O   1 
ATOM   1042 C  CB  . ASN A 1 124 ? -11.995 13.365  22.467  1.00 8.44   ? 124 ASN A CB  1 
ATOM   1043 C  CG  . ASN A 1 124 ? -12.797 13.960  23.586  1.00 8.51   ? 124 ASN A CG  1 
ATOM   1044 O  OD1 . ASN A 1 124 ? -13.609 14.842  23.372  1.00 10.00  ? 124 ASN A OD1 1 
ATOM   1045 N  ND2 . ASN A 1 124 ? -12.495 13.504  24.806  1.00 10.34  ? 124 ASN A ND2 1 
ATOM   1046 N  N   . THR A 1 125 ? -14.179 15.106  20.367  1.00 9.18   ? 125 THR A N   1 
ATOM   1047 C  CA  . THR A 1 125 ? -14.415 16.402  19.667  1.00 10.19  ? 125 THR A CA  1 
ATOM   1048 C  C   . THR A 1 125 ? -13.871 17.570  20.429  1.00 10.75  ? 125 THR A C   1 
ATOM   1049 O  O   . THR A 1 125 ? -13.724 18.635  19.822  1.00 11.96  ? 125 THR A O   1 
ATOM   1050 C  CB  . THR A 1 125 ? -15.923 16.533  19.350  1.00 13.26  ? 125 THR A CB  1 
ATOM   1051 O  OG1 . THR A 1 125 ? -16.690 16.521  20.554  1.00 17.51  ? 125 THR A OG1 1 
ATOM   1052 C  CG2 . THR A 1 125 ? -16.363 15.455  18.329  1.00 15.98  ? 125 THR A CG2 1 
ATOM   1053 N  N   . LYS A 1 126 ? -13.569 17.415  21.752  1.00 10.39  ? 127 LYS A N   1 
ATOM   1054 C  CA  . LYS A 1 126 ? -13.087 18.550  22.488  1.00 11.00  ? 127 LYS A CA  1 
ATOM   1055 C  C   . LYS A 1 126 ? -11.650 18.928  21.998  1.00 10.82  ? 127 LYS A C   1 
ATOM   1056 O  O   . LYS A 1 126 ? -11.157 20.015  22.389  1.00 12.47  ? 127 LYS A O   1 
ATOM   1057 C  CB  . LYS A 1 126 ? -13.181 18.310  23.937  1.00 13.90  ? 127 LYS A CB  1 
ATOM   1058 C  CG  . LYS A 1 126 ? -12.055 17.469  24.498  1.00 13.55  ? 127 LYS A CG  1 
ATOM   1059 C  CD  . LYS A 1 126 ? -12.443 17.020  25.986  1.00 18.50  ? 127 LYS A CD  1 
ATOM   1060 C  CE  . LYS A 1 126 ? -11.531 16.384  26.946  1.00 26.98  ? 127 LYS A CE  1 
ATOM   1061 N  NZ  . LYS A 1 126 ? -11.232 17.332  28.072  1.00 48.74  ? 127 LYS A NZ  1 
ATOM   1062 N  N   . TYR A 1 127 ? -10.970 18.095  21.200  1.00 9.52   ? 128 TYR A N   1 
ATOM   1063 C  CA  . TYR A 1 127 ? -9.609  18.384  20.716  1.00 10.01  ? 128 TYR A CA  1 
ATOM   1064 C  C   . TYR A 1 127 ? -9.599  18.757  19.271  1.00 10.64  ? 128 TYR A C   1 
ATOM   1065 O  O   . TYR A 1 127 ? -8.525  19.016  18.714  1.00 10.69  ? 128 TYR A O   1 
ATOM   1066 C  CB  . TYR A 1 127 ? -8.684  17.201  21.032  1.00 11.23  ? 128 TYR A CB  1 
ATOM   1067 C  CG  . TYR A 1 127 ? -8.582  16.902  22.473  1.00 9.31   ? 128 TYR A CG  1 
ATOM   1068 C  CD1 . TYR A 1 127 ? -8.223  17.913  23.388  1.00 11.24  ? 128 TYR A CD1 1 
ATOM   1069 C  CD2 . TYR A 1 127 ? -8.912  15.644  22.961  1.00 9.15   ? 128 TYR A CD2 1 
ATOM   1070 C  CE1 . TYR A 1 127 ? -8.161  17.607  24.732  1.00 11.89  ? 128 TYR A CE1 1 
ATOM   1071 C  CE2 . TYR A 1 127 ? -8.815  15.343  24.286  1.00 9.02   ? 128 TYR A CE2 1 
ATOM   1072 C  CZ  . TYR A 1 127 ? -8.457  16.344  25.186  1.00 11.70  ? 128 TYR A CZ  1 
ATOM   1073 O  OH  . TYR A 1 127 ? -8.390  16.132  26.532  1.00 12.88  ? 128 TYR A OH  1 
ATOM   1074 N  N   . GLY A 1 128 ? -10.775 18.859  18.645  1.00 9.79   ? 129 GLY A N   1 
ATOM   1075 C  CA  . GLY A 1 128 ? -10.881 19.522  17.336  1.00 11.57  ? 129 GLY A CA  1 
ATOM   1076 C  C   . GLY A 1 128 ? -10.527 18.672  16.136  1.00 10.97  ? 129 GLY A C   1 
ATOM   1077 O  O   . GLY A 1 128 ? -11.149 18.806  15.084  1.00 13.22  ? 129 GLY A O   1 
ATOM   1078 N  N   . ASP A 1 129 ? -9.535  17.801  16.219  1.00 11.78  ? 130 ASP A N   1 
ATOM   1079 C  CA  . ASP A 1 129 ? -9.188  16.916  15.104  1.00 13.52  ? 130 ASP A CA  1 
ATOM   1080 C  C   . ASP A 1 129 ? -8.483  15.692  15.658  1.00 12.40  ? 130 ASP A C   1 
ATOM   1081 O  O   . ASP A 1 129 ? -8.043  15.683  16.826  1.00 13.13  ? 130 ASP A O   1 
ATOM   1082 C  CB  . ASP A 1 129 ? -8.577  17.524  13.923  1.00 16.90  ? 130 ASP A CB  1 
ATOM   1083 C  CG  . ASP A 1 129 ? -7.191  17.971  14.138  1.00 14.51  ? 130 ASP A CG  1 
ATOM   1084 O  OD1 . ASP A 1 129 ? -6.553  17.636  15.129  1.00 25.11  ? 130 ASP A OD1 1 
ATOM   1085 O  OD2 . ASP A 1 129 ? -6.724  18.677  13.241  1.00 21.94  ? 130 ASP A OD2 1 
ATOM   1086 N  N   . PHE A 1 130 ? -8.315  14.666  14.828  1.00 11.74  ? 131 PHE A N   1 
ATOM   1087 C  CA  . PHE A 1 130 ? -7.647  13.433  15.236  1.00 10.23  ? 131 PHE A CA  1 
ATOM   1088 C  C   . PHE A 1 130 ? -6.186  13.650  15.649  1.00 10.35  ? 131 PHE A C   1 
ATOM   1089 O  O   . PHE A 1 130 ? -5.716  13.090  16.621  1.00 9.79   ? 131 PHE A O   1 
ATOM   1090 C  CB  . PHE A 1 130 ? -7.734  12.449  14.068  1.00 11.45  ? 131 PHE A CB  1 
ATOM   1091 C  CG  . PHE A 1 130 ? -7.075  11.159  14.334  1.00 9.58   ? 131 PHE A CG  1 
ATOM   1092 C  CD1 . PHE A 1 130 ? -7.715  10.109  14.977  1.00 10.30  ? 131 PHE A CD1 1 
ATOM   1093 C  CD2 . PHE A 1 130 ? -5.742  10.924  13.962  1.00 12.50  ? 131 PHE A CD2 1 
ATOM   1094 C  CE1 . PHE A 1 130 ? -7.090  8.903   15.207  1.00 11.70  ? 131 PHE A CE1 1 
ATOM   1095 C  CE2 . PHE A 1 130 ? -5.112  9.752   14.153  1.00 15.52  ? 131 PHE A CE2 1 
ATOM   1096 C  CZ  . PHE A 1 130 ? -5.784  8.698   14.795  1.00 13.43  ? 131 PHE A CZ  1 
ATOM   1097 N  N   . GLY A 1 131 ? -5.409  14.434  14.859  1.00 12.30  ? 132 GLY A N   1 
ATOM   1098 C  CA  . GLY A 1 131 ? -4.029  14.617  15.149  1.00 13.62  ? 132 GLY A CA  1 
ATOM   1099 C  C   . GLY A 1 131 ? -3.735  15.277  16.495  1.00 13.35  ? 132 GLY A C   1 
ATOM   1100 O  O   . GLY A 1 131 ? -2.762  14.935  17.197  1.00 14.45  ? 132 GLY A O   1 
ATOM   1101 N  N   . LYS A 1 132 ? -4.624  16.197  16.918  1.00 12.19  ? 133 LYS A N   1 
ATOM   1102 C  CA  . LYS A 1 132 ? -4.470  16.784  18.268  1.00 11.36  ? 133 LYS A CA  1 
ATOM   1103 C  C   . LYS A 1 132 ? -4.982  15.766  19.301  1.00 10.14  ? 133 LYS A C   1 
ATOM   1104 O  O   . LYS A 1 132 ? -4.430  15.694  20.406  1.00 10.52  ? 133 LYS A O   1 
ATOM   1105 C  CB  . LYS A 1 132 ? -5.229  18.079  18.359  1.00 11.64  ? 133 LYS A CB  1 
ATOM   1106 C  CG  . LYS A 1 132 ? -4.493  19.203  17.606  1.00 16.01  ? 133 LYS A CG  1 
ATOM   1107 C  CD  . LYS A 1 132 ? -3.244  19.641  18.405  1.00 20.08  ? 133 LYS A CD  1 
ATOM   1108 C  CE  . LYS A 1 132 ? -2.740  20.963  17.953  1.00 28.50  ? 133 LYS A CE  1 
ATOM   1109 N  NZ  . LYS A 1 132 ? -1.814  21.475  18.994  1.00 35.45  ? 133 LYS A NZ  1 
ATOM   1110 N  N   . ALA A 1 133 ? -6.068  15.049  18.990  1.00 9.81   ? 134 ALA A N   1 
ATOM   1111 C  CA  . ALA A 1 133 ? -6.594  14.098  19.963  1.00 9.34   ? 134 ALA A CA  1 
ATOM   1112 C  C   . ALA A 1 133 ? -5.586  13.053  20.384  1.00 8.44   ? 134 ALA A C   1 
ATOM   1113 O  O   . ALA A 1 133 ? -5.592  12.657  21.532  1.00 8.84   ? 134 ALA A O   1 
ATOM   1114 C  CB  . ALA A 1 133 ? -7.869  13.479  19.387  1.00 8.75   ? 134 ALA A CB  1 
ATOM   1115 N  N   . VAL A 1 134 ? -4.782  12.545  19.468  1.00 9.16   ? 135 VAL A N   1 
ATOM   1116 C  CA  . VAL A 1 134 ? -3.875  11.460  19.839  1.00 9.80   ? 135 VAL A CA  1 
ATOM   1117 C  C   . VAL A 1 134 ? -2.779  11.879  20.790  1.00 9.71   ? 135 VAL A C   1 
ATOM   1118 O  O   . VAL A 1 134 ? -2.105  11.020  21.309  1.00 10.35  ? 135 VAL A O   1 
ATOM   1119 C  CB  . VAL A 1 134 ? -3.292  10.772  18.601  1.00 10.57  ? 135 VAL A CB  1 
ATOM   1120 C  CG1 . VAL A 1 134 ? -4.351  10.084  17.798  1.00 12.28  ? 135 VAL A CG1 1 
ATOM   1121 C  CG2 . VAL A 1 134 ? -2.389  11.656  17.778  1.00 11.71  ? 135 VAL A CG2 1 
ATOM   1122 N  N   . GLN A 1 135 ? -2.655  13.196  20.982  1.00 10.06  ? 136 GLN A N   1 
ATOM   1123 C  CA  . GLN A 1 135 ? -1.675  13.692  21.970  1.00 10.60  ? 136 GLN A CA  1 
ATOM   1124 C  C   . GLN A 1 135 ? -2.249  13.812  23.342  1.00 10.03  ? 136 GLN A C   1 
ATOM   1125 O  O   . GLN A 1 135 ? -1.574  14.380  24.258  1.00 12.56  ? 136 GLN A O   1 
ATOM   1126 C  CB  . GLN A 1 135 ? -1.178  15.100  21.431  1.00 12.07  ? 136 GLN A CB  1 
ATOM   1127 C  CG  . GLN A 1 135 ? -0.500  14.975  20.119  1.00 15.92  ? 136 GLN A CG  1 
ATOM   1128 C  CD  . GLN A 1 135 ? -0.057  16.312  19.669  1.00 17.84  ? 136 GLN A CD  1 
ATOM   1129 O  OE1 . GLN A 1 135 ? 0.891   16.878  20.279  1.00 23.92  ? 136 GLN A OE1 1 
ATOM   1130 N  NE2 . GLN A 1 135 ? -0.587  16.736  18.476  1.00 19.59  ? 136 GLN A NE2 1 
ATOM   1131 N  N   . GLN A 1 136 ? -3.457  13.339  23.561  1.00 9.27   ? 137 GLN A N   1 
ATOM   1132 C  CA  . GLN A 1 136 ? -4.164  13.515  24.828  1.00 9.25   ? 137 GLN A CA  1 
ATOM   1133 C  C   . GLN A 1 136 ? -4.506  12.167  25.426  1.00 8.47   ? 137 GLN A C   1 
ATOM   1134 O  O   . GLN A 1 136 ? -4.876  11.260  24.717  1.00 8.75   ? 137 GLN A O   1 
ATOM   1135 C  CB  . GLN A 1 136 ? -5.429  14.323  24.670  1.00 9.67   ? 137 GLN A CB  1 
ATOM   1136 C  CG  . GLN A 1 136 ? -5.271  15.584  23.931  1.00 13.85  ? 137 GLN A CG  1 
ATOM   1137 C  CD  . GLN A 1 136 ? -4.372  16.508  24.455  1.00 17.52  ? 137 GLN A CD  1 
ATOM   1138 O  OE1 . GLN A 1 136 ? -4.176  16.610  25.616  1.00 19.87  ? 137 GLN A OE1 1 
ATOM   1139 N  NE2 . GLN A 1 136 ? -3.663  17.239  23.554  1.00 29.10  ? 137 GLN A NE2 1 
ATOM   1140 N  N   . PRO A 1 137 ? -4.555  12.065  26.780  1.00 8.59   ? 138 PRO A N   1 
ATOM   1141 C  CA  . PRO A 1 137 ? -4.801  10.732  27.406  1.00 9.86   ? 138 PRO A CA  1 
ATOM   1142 C  C   . PRO A 1 137 ? -6.231  10.242  27.221  1.00 9.08   ? 138 PRO A C   1 
ATOM   1143 O  O   . PRO A 1 137 ? -6.463  9.044   27.305  1.00 12.61  ? 138 PRO A O   1 
ATOM   1144 C  CB  . PRO A 1 137 ? -4.526  10.918  28.892  1.00 12.50  ? 138 PRO A CB  1 
ATOM   1145 C  CG  . PRO A 1 137 ? -4.446  12.379  29.035  1.00 18.54  ? 138 PRO A CG  1 
ATOM   1146 C  CD  . PRO A 1 137 ? -4.044  13.043  27.766  1.00 12.87  ? 138 PRO A CD  1 
ATOM   1147 N  N   . ASP A 1 138 ? -7.157  11.166  26.903  1.00 8.57   ? 139 ASP A N   1 
ATOM   1148 C  CA  . ASP A 1 138 ? -8.581  10.874  26.643  1.00 8.71   ? 139 ASP A CA  1 
ATOM   1149 C  C   . ASP A 1 138 ? -8.893  11.276  25.209  1.00 7.60   ? 139 ASP A C   1 
ATOM   1150 O  O   . ASP A 1 138 ? -10.039 11.670  24.914  1.00 8.57   ? 139 ASP A O   1 
ATOM   1151 C  CB  . ASP A 1 138 ? -9.527  11.460  27.653  1.00 10.73  ? 139 ASP A CB  1 
ATOM   1152 C  CG  . ASP A 1 138 ? -9.450  12.972  27.681  1.00 10.96  ? 139 ASP A CG  1 
ATOM   1153 O  OD1 . ASP A 1 138 ? -8.485  13.575  27.094  1.00 11.06  ? 139 ASP A OD1 1 
ATOM   1154 O  OD2 . ASP A 1 138 ? -10.307 13.569  28.362  1.00 14.29  ? 139 ASP A OD2 1 
ATOM   1155 N  N   . GLY A 1 139 ? -7.949  11.172  24.279  1.00 7.41   ? 140 GLY A N   1 
ATOM   1156 C  CA  . GLY A 1 139 ? -8.190  11.645  22.954  1.00 7.70   ? 140 GLY A CA  1 
ATOM   1157 C  C   . GLY A 1 139 ? -9.013  10.744  22.057  1.00 6.38   ? 140 GLY A C   1 
ATOM   1158 O  O   . GLY A 1 139 ? -9.698  11.233  21.185  1.00 7.51   ? 140 GLY A O   1 
ATOM   1159 N  N   . LEU A 1 140 ? -8.885  9.400   22.215  1.00 6.50   ? 141 LEU A N   1 
ATOM   1160 C  CA  . LEU A 1 140 ? -9.559  8.462   21.322  1.00 6.24   ? 141 LEU A CA  1 
ATOM   1161 C  C   . LEU A 1 140 ? -10.406 7.504   22.120  1.00 6.07   ? 141 LEU A C   1 
ATOM   1162 O  O   . LEU A 1 140 ? -10.138 7.226   23.300  1.00 6.75   ? 141 LEU A O   1 
ATOM   1163 C  CB  . LEU A 1 140 ? -8.559  7.613   20.516  1.00 6.66   ? 141 LEU A CB  1 
ATOM   1164 C  CG  . LEU A 1 140 ? -7.635  8.330   19.548  1.00 8.12   ? 141 LEU A CG  1 
ATOM   1165 C  CD1 . LEU A 1 140 ? -6.891  7.272   18.716  1.00 8.09   ? 141 LEU A CD1 1 
ATOM   1166 C  CD2 . LEU A 1 140 ? -8.306  9.316   18.640  1.00 9.40   ? 141 LEU A CD2 1 
ATOM   1167 N  N   . ALA A 1 141 ? -11.435 6.989   21.465  1.00 6.40   ? 142 ALA A N   1 
ATOM   1168 C  CA  . ALA A 1 141 ? -12.221 5.850   21.974  1.00 6.72   ? 142 ALA A CA  1 
ATOM   1169 C  C   . ALA A 1 141 ? -12.285 4.870   20.845  1.00 6.41   ? 142 ALA A C   1 
ATOM   1170 O  O   . ALA A 1 141 ? -12.681 5.223   19.719  1.00 7.04   ? 142 ALA A O   1 
ATOM   1171 C  CB  . ALA A 1 141 ? -13.622 6.302   22.414  1.00 8.66   ? 142 ALA A CB  1 
ATOM   1172 N  N   . VAL A 1 142 ? -11.871 3.614   21.108  1.00 5.85   ? 143 VAL A N   1 
ATOM   1173 C  CA  . VAL A 1 142 ? -11.924 2.551   20.121  1.00 5.96   ? 143 VAL A CA  1 
ATOM   1174 C  C   . VAL A 1 142 ? -12.936 1.542   20.596  1.00 6.08   ? 143 VAL A C   1 
ATOM   1175 O  O   . VAL A 1 142 ? -12.833 1.030   21.705  1.00 6.29   ? 143 VAL A O   1 
ATOM   1176 C  CB  . VAL A 1 142 ? -10.568 1.933   19.784  1.00 6.85   ? 143 VAL A CB  1 
ATOM   1177 C  CG1 . VAL A 1 142 ? -10.755 0.905   18.671  1.00 8.22   ? 143 VAL A CG1 1 
ATOM   1178 C  CG2 . VAL A 1 142 ? -9.574  3.002   19.373  1.00 9.21   ? 143 VAL A CG2 1 
ATOM   1179 N  N   . LEU A 1 143 ? -13.916 1.252   19.713  1.00 6.22   ? 144 LEU A N   1 
ATOM   1180 C  CA  . LEU A 1 143 ? -14.859 0.207   19.944  1.00 6.23   ? 144 LEU A CA  1 
ATOM   1181 C  C   . LEU A 1 143 ? -14.293 -1.026  19.255  1.00 6.21   ? 144 LEU A C   1 
ATOM   1182 O  O   . LEU A 1 143 ? -14.143 -1.066  18.032  1.00 7.36   ? 144 LEU A O   1 
ATOM   1183 C  CB  . LEU A 1 143 ? -16.228 0.641   19.362  1.00 8.30   ? 144 LEU A CB  1 
ATOM   1184 C  CG  . LEU A 1 143 ? -17.363 -0.345  19.527  1.00 9.08   ? 144 LEU A CG  1 
ATOM   1185 C  CD1 . LEU A 1 143 ? -17.602 -0.676  20.968  1.00 11.33  ? 144 LEU A CD1 1 
ATOM   1186 C  CD2 . LEU A 1 143 ? -18.641 0.223   18.840  1.00 10.77  ? 144 LEU A CD2 1 
ATOM   1187 N  N   . GLY A 1 144 ? -14.005 -2.053  20.070  1.00 5.84   ? 145 GLY A N   1 
ATOM   1188 C  CA  . GLY A 1 144 ? -13.443 -3.312  19.592  1.00 5.94   ? 145 GLY A CA  1 
ATOM   1189 C  C   . GLY A 1 144 ? -14.502 -4.393  19.609  1.00 5.61   ? 145 GLY A C   1 
ATOM   1190 O  O   . GLY A 1 144 ? -15.223 -4.555  20.583  1.00 6.75   ? 145 GLY A O   1 
ATOM   1191 N  N   . ILE A 1 145 ? -14.548 -5.157  18.498  1.00 5.76   ? 146 ILE A N   1 
ATOM   1192 C  CA  . ILE A 1 145 ? -15.549 -6.175  18.312  1.00 5.54   ? 146 ILE A CA  1 
ATOM   1193 C  C   . ILE A 1 145 ? -14.849 -7.411  17.810  1.00 5.88   ? 146 ILE A C   1 
ATOM   1194 O  O   . ILE A 1 145 ? -14.133 -7.383  16.793  1.00 6.59   ? 146 ILE A O   1 
ATOM   1195 C  CB  . ILE A 1 145 ? -16.652 -5.699  17.311  1.00 7.17   ? 146 ILE A CB  1 
ATOM   1196 C  CG1 . ILE A 1 145 ? -17.258 -4.393  17.832  1.00 9.33   ? 146 ILE A CG1 1 
ATOM   1197 C  CG2 . ILE A 1 145 ? -17.677 -6.806  17.126  1.00 9.04   ? 146 ILE A CG2 1 
ATOM   1198 C  CD1 . ILE A 1 145 ? -18.330 -3.803  16.922  1.00 8.51   ? 146 ILE A CD1 1 
ATOM   1199 N  N   . PHE A 1 146 ? -15.027 -8.532  18.493  1.00 6.01   ? 147 PHE A N   1 
ATOM   1200 C  CA  . PHE A 1 146 ? -14.416 -9.808  18.067  1.00 6.15   ? 147 PHE A CA  1 
ATOM   1201 C  C   . PHE A 1 146 ? -15.195 -10.417 16.914  1.00 6.22   ? 147 PHE A C   1 
ATOM   1202 O  O   . PHE A 1 146 ? -16.403 -10.272 16.833  1.00 7.16   ? 147 PHE A O   1 
ATOM   1203 C  CB  . PHE A 1 146 ? -14.436 -10.761 19.245  1.00 6.51   ? 147 PHE A CB  1 
ATOM   1204 C  CG  . PHE A 1 146 ? -13.567 -10.305 20.395  1.00 5.83   ? 147 PHE A CG  1 
ATOM   1205 C  CD1 . PHE A 1 146 ? -12.203 -10.124 20.215  1.00 6.73   ? 147 PHE A CD1 1 
ATOM   1206 C  CD2 . PHE A 1 146 ? -14.102 -10.071 21.647  1.00 7.07   ? 147 PHE A CD2 1 
ATOM   1207 C  CE1 . PHE A 1 146 ? -11.381 -9.758  21.317  1.00 6.97   ? 147 PHE A CE1 1 
ATOM   1208 C  CE2 . PHE A 1 146 ? -13.297 -9.688  22.713  1.00 6.76   ? 147 PHE A CE2 1 
ATOM   1209 C  CZ  . PHE A 1 146 ? -11.957 -9.562  22.557  1.00 6.91   ? 147 PHE A CZ  1 
ATOM   1210 N  N   . LEU A 1 147 ? -14.476 -11.137 16.071  1.00 6.43   ? 148 LEU A N   1 
ATOM   1211 C  CA  . LEU A 1 147 ? -15.063 -11.931 14.978  1.00 7.16   ? 148 LEU A CA  1 
ATOM   1212 C  C   . LEU A 1 147 ? -14.719 -13.403 15.210  1.00 6.48   ? 148 LEU A C   1 
ATOM   1213 O  O   . LEU A 1 147 ? -13.533 -13.746 15.447  1.00 7.21   ? 148 LEU A O   1 
ATOM   1214 C  CB  . LEU A 1 147 ? -14.450 -11.532 13.625  1.00 7.56   ? 148 LEU A CB  1 
ATOM   1215 C  CG  . LEU A 1 147 ? -14.989 -10.261 12.948  1.00 8.18   ? 148 LEU A CG  1 
ATOM   1216 C  CD1 . LEU A 1 147 ? -14.786 -9.030  13.785  1.00 9.05   ? 148 LEU A CD1 1 
ATOM   1217 C  CD2 . LEU A 1 147 ? -14.376 -10.067 11.564  1.00 9.59   ? 148 LEU A CD2 1 
ATOM   1218 N  N   . LYS A 1 148 ? -15.731 -14.222 15.096  1.00 7.48   ? 149 LYS A N   1 
ATOM   1219 C  CA  . LYS A 1 148 ? -15.569 -15.679 15.076  1.00 8.22   ? 149 LYS A CA  1 
ATOM   1220 C  C   . LYS A 1 148 ? -16.056 -16.155 13.696  1.00 8.31   ? 149 LYS A C   1 
ATOM   1221 O  O   . LYS A 1 148 ? -16.882 -15.513 13.051  1.00 9.42   ? 149 LYS A O   1 
ATOM   1222 C  CB  . LYS A 1 148 ? -16.284 -16.364 16.197  1.00 9.12   ? 149 LYS A CB  1 
ATOM   1223 C  CG  . LYS A 1 148 ? -17.823 -16.202 16.140  1.00 10.92  ? 149 LYS A CG  1 
ATOM   1224 C  CD  . LYS A 1 148 ? -18.512 -16.935 17.320  1.00 16.70  ? 149 LYS A CD  1 
ATOM   1225 C  CE  . LYS A 1 148 ? -20.009 -17.048 17.114  1.00 26.70  ? 149 LYS A CE  1 
ATOM   1226 N  NZ  . LYS A 1 148 ? -20.499 -17.939 18.198  1.00 54.46  ? 149 LYS A NZ  1 
ATOM   1227 N  N   . VAL A 1 149 ? -15.576 -17.323 13.296  1.00 8.77   ? 150 VAL A N   1 
ATOM   1228 C  CA  . VAL A 1 149 ? -15.956 -17.926 11.999  1.00 9.32   ? 150 VAL A CA  1 
ATOM   1229 C  C   . VAL A 1 149 ? -17.170 -18.831 12.196  1.00 9.87   ? 150 VAL A C   1 
ATOM   1230 O  O   . VAL A 1 149 ? -17.134 -19.788 12.979  1.00 11.47  ? 150 VAL A O   1 
ATOM   1231 C  CB  . VAL A 1 149 ? -14.732 -18.637 11.432  1.00 9.92   ? 150 VAL A CB  1 
ATOM   1232 C  CG1 . VAL A 1 149 ? -15.110 -19.438 10.138  1.00 13.09  ? 150 VAL A CG1 1 
ATOM   1233 C  CG2 . VAL A 1 149 ? -13.657 -17.636 11.096  1.00 12.10  ? 150 VAL A CG2 1 
ATOM   1234 N  N   . GLY A 1 150 ? -18.217 -18.566 11.429  1.00 9.83   ? 151 GLY A N   1 
ATOM   1235 C  CA  . GLY A 1 150 ? -19.432 -19.390 11.475  1.00 11.61  ? 151 GLY A CA  1 
ATOM   1236 C  C   . GLY A 1 150 ? -20.300 -18.926 10.348  1.00 10.81  ? 151 GLY A C   1 
ATOM   1237 O  O   . GLY A 1 150 ? -19.947 -18.989 9.173   1.00 11.98  ? 151 GLY A O   1 
ATOM   1238 N  N   A SER A 1 151 ? -21.501 -18.398 10.659  0.50 11.75  ? 152 SER A N   1 
ATOM   1239 N  N   B SER A 1 151 ? -21.472 -18.372 10.692  0.50 11.32  ? 152 SER A N   1 
ATOM   1240 C  CA  A SER A 1 151 ? -22.433 -17.866 9.649   0.50 13.15  ? 152 SER A CA  1 
ATOM   1241 C  CA  B SER A 1 151 ? -22.371 -17.746 9.750   0.50 11.90  ? 152 SER A CA  1 
ATOM   1242 C  C   A SER A 1 151 ? -21.874 -16.530 9.158   0.50 10.82  ? 152 SER A C   1 
ATOM   1243 C  C   B SER A 1 151 ? -21.668 -16.543 9.086   0.50 12.19  ? 152 SER A C   1 
ATOM   1244 O  O   A SER A 1 151 ? -21.307 -15.777 9.949   0.50 10.90  ? 152 SER A O   1 
ATOM   1245 O  O   B SER A 1 151 ? -20.817 -15.879 9.687   0.50 8.91   ? 152 SER A O   1 
ATOM   1246 C  CB  A SER A 1 151 ? -23.818 -17.553 10.206  0.50 20.68  ? 152 SER A CB  1 
ATOM   1247 C  CB  B SER A 1 151 ? -23.660 -17.342 10.417  0.50 12.29  ? 152 SER A CB  1 
ATOM   1248 O  OG  A SER A 1 151 ? -23.694 -16.590 11.251  0.50 21.97  ? 152 SER A OG  1 
ATOM   1249 O  OG  B SER A 1 151 ? -24.301 -18.514 10.934  0.50 17.90  ? 152 SER A OG  1 
ATOM   1250 N  N   . ALA A 1 152 ? -22.077 -16.220 7.852   1.00 11.54  ? 153 ALA A N   1 
ATOM   1251 C  CA  . ALA A 1 152 ? -21.704 -14.959 7.291   1.00 12.07  ? 153 ALA A CA  1 
ATOM   1252 C  C   . ALA A 1 152 ? -22.350 -13.790 7.959   1.00 11.01  ? 153 ALA A C   1 
ATOM   1253 O  O   . ALA A 1 152 ? -23.457 -13.820 8.437   1.00 13.53  ? 153 ALA A O   1 
ATOM   1254 C  CB  . ALA A 1 152 ? -22.029 -14.941 5.761   1.00 15.29  ? 153 ALA A CB  1 
ATOM   1255 N  N   . LYS A 1 153 ? -21.598 -12.626 7.856   1.00 12.18  ? 154 LYS A N   1 
ATOM   1256 C  CA  . LYS A 1 153 ? -22.159 -11.338 8.376   1.00 13.21  ? 154 LYS A CA  1 
ATOM   1257 C  C   . LYS A 1 153 ? -22.535 -10.583 7.066   1.00 11.35  ? 154 LYS A C   1 
ATOM   1258 O  O   . LYS A 1 153 ? -21.722 -10.119 6.300   1.00 12.27  ? 154 LYS A O   1 
ATOM   1259 C  CB  . LYS A 1 153 ? -21.142 -10.583 9.152   1.00 12.50  ? 154 LYS A CB  1 
ATOM   1260 C  CG  . LYS A 1 153 ? -21.627 -9.377  9.882   1.00 16.21  ? 154 LYS A CG  1 
ATOM   1261 C  CD  . LYS A 1 153 ? -22.439 -9.716  11.065  1.00 16.77  ? 154 LYS A CD  1 
ATOM   1262 C  CE  . LYS A 1 153 ? -22.329 -8.449  11.862  1.00 18.24  ? 154 LYS A CE  1 
ATOM   1263 N  NZ  . LYS A 1 153 ? -23.308 -8.810  12.898  1.00 16.86  ? 154 LYS A NZ  1 
ATOM   1264 N  N   . PRO A 1 154 ? -23.838 -10.456 6.808   1.00 13.71  ? 155 PRO A N   1 
ATOM   1265 C  CA  . PRO A 1 154 ? -24.253 -9.864  5.523   1.00 15.23  ? 155 PRO A CA  1 
ATOM   1266 C  C   . PRO A 1 154 ? -23.784 -8.412  5.356   1.00 14.29  ? 155 PRO A C   1 
ATOM   1267 O  O   . PRO A 1 154 ? -23.309 -8.054  4.259   1.00 17.08  ? 155 PRO A O   1 
ATOM   1268 C  CB  . PRO A 1 154 ? -25.822 -9.922  5.614   1.00 16.99  ? 155 PRO A CB  1 
ATOM   1269 C  CG  . PRO A 1 154 ? -26.041 -11.145 6.504   1.00 19.55  ? 155 PRO A CG  1 
ATOM   1270 C  CD  . PRO A 1 154 ? -25.023 -10.984 7.580   1.00 16.29  ? 155 PRO A CD  1 
ATOM   1271 N  N   . GLY A 1 155 ? -23.691 -7.702  6.490   1.00 14.39  ? 156 GLY A N   1 
ATOM   1272 C  CA  . GLY A 1 155 ? -23.299 -6.329  6.427   1.00 17.97  ? 156 GLY A CA  1 
ATOM   1273 C  C   . GLY A 1 155 ? -21.841 -6.131  6.224   1.00 15.15  ? 156 GLY A C   1 
ATOM   1274 O  O   . GLY A 1 155 ? -21.353 -5.013  6.011   1.00 18.07  ? 156 GLY A O   1 
ATOM   1275 N  N   . LEU A 1 156 ? -21.085 -7.208  6.273   1.00 14.19  ? 157 LEU A N   1 
ATOM   1276 C  CA  . LEU A 1 156 ? -19.675 -7.214  5.935   1.00 13.04  ? 157 LEU A CA  1 
ATOM   1277 C  C   . LEU A 1 156 ? -19.383 -7.392  4.468   1.00 14.64  ? 157 LEU A C   1 
ATOM   1278 O  O   . LEU A 1 156 ? -18.210 -7.106  3.947   1.00 13.76  ? 157 LEU A O   1 
ATOM   1279 C  CB  . LEU A 1 156 ? -18.852 -8.235  6.771   1.00 13.56  ? 157 LEU A CB  1 
ATOM   1280 C  CG  . LEU A 1 156 ? -17.322 -8.356  6.591   1.00 13.48  ? 157 LEU A CG  1 
ATOM   1281 C  CD1 . LEU A 1 156 ? -16.579 -7.036  6.935   1.00 14.65  ? 157 LEU A CD1 1 
ATOM   1282 C  CD2 . LEU A 1 156 ? -16.723 -9.479  7.405   1.00 14.15  ? 157 LEU A CD2 1 
ATOM   1283 N  N   . GLN A 1 157 ? -20.357 -7.932  3.719   1.00 13.50  ? 158 GLN A N   1 
ATOM   1284 C  CA  . GLN A 1 157 ? -20.009 -8.467  2.354   1.00 14.75  ? 158 GLN A CA  1 
ATOM   1285 C  C   . GLN A 1 157 ? -19.554 -7.256  1.444   1.00 14.88  ? 158 GLN A C   1 
ATOM   1286 O  O   . GLN A 1 157 ? -18.733 -7.494  0.600   1.00 14.96  ? 158 GLN A O   1 
ATOM   1287 C  CB  . GLN A 1 157 ? -21.172 -9.249  1.785   1.00 17.21  ? 158 GLN A CB  1 
ATOM   1288 C  CG  . GLN A 1 157 ? -20.750 -9.992  0.500   1.00 19.13  ? 158 GLN A CG  1 
ATOM   1289 C  CD  . GLN A 1 157 ? -19.678 -10.994 0.706   1.00 16.32  ? 158 GLN A CD  1 
ATOM   1290 O  OE1 . GLN A 1 157 ? -19.512 -11.572 1.839   1.00 16.53  ? 158 GLN A OE1 1 
ATOM   1291 N  NE2 . GLN A 1 157 ? -18.884 -11.277 -0.357  1.00 18.88  ? 158 GLN A NE2 1 
ATOM   1292 N  N   A LYS A 1 158 ? -20.102 -6.055  1.578   0.50 15.82  ? 159 LYS A N   1 
ATOM   1293 N  N   B LYS A 1 158 ? -20.132 -6.071  1.555   0.50 15.65  ? 159 LYS A N   1 
ATOM   1294 C  CA  A LYS A 1 158 ? -19.685 -4.967  0.712   0.50 15.79  ? 159 LYS A CA  1 
ATOM   1295 C  CA  B LYS A 1 158 ? -19.700 -4.978  0.696   0.50 15.69  ? 159 LYS A CA  1 
ATOM   1296 C  C   A LYS A 1 158 ? -18.176 -4.689  0.881   0.50 14.72  ? 159 LYS A C   1 
ATOM   1297 C  C   B LYS A 1 158 ? -18.194 -4.643  0.886   0.50 14.81  ? 159 LYS A C   1 
ATOM   1298 O  O   A LYS A 1 158 ? -17.505 -4.354  -0.124  0.50 16.32  ? 159 LYS A O   1 
ATOM   1299 O  O   B LYS A 1 158 ? -17.520 -4.298  -0.074  0.50 16.37  ? 159 LYS A O   1 
ATOM   1300 C  CB  A LYS A 1 158 ? -20.537 -3.753  1.013   0.50 18.53  ? 159 LYS A CB  1 
ATOM   1301 C  CB  B LYS A 1 158 ? -20.612 -3.771  0.937   0.50 18.78  ? 159 LYS A CB  1 
ATOM   1302 C  CG  A LYS A 1 158 ? -21.846 -3.654  0.258   0.50 27.15  ? 159 LYS A CG  1 
ATOM   1303 C  CG  B LYS A 1 158 ? -21.986 -3.975  0.242   0.50 25.00  ? 159 LYS A CG  1 
ATOM   1304 C  CD  A LYS A 1 158 ? -22.404 -2.191  0.441   0.50 37.40  ? 159 LYS A CD  1 
ATOM   1305 C  CD  B LYS A 1 158 ? -22.892 -2.725  0.307   0.50 38.06  ? 159 LYS A CD  1 
ATOM   1306 C  CE  A LYS A 1 158 ? -21.355 -1.052  0.645   0.50 29.78  ? 159 LYS A CE  1 
ATOM   1307 C  CE  B LYS A 1 158 ? -24.385 -2.933  -0.120  0.50 31.54  ? 159 LYS A CE  1 
ATOM   1308 N  NZ  A LYS A 1 158 ? -21.784 0.418   0.503   0.50 36.22  ? 159 LYS A NZ  1 
ATOM   1309 N  NZ  B LYS A 1 158 ? -25.228 -1.672  -0.021  0.50 31.33  ? 159 LYS A NZ  1 
ATOM   1310 N  N   . VAL A 1 159 ? -17.691 -4.818  2.086   1.00 14.43  ? 160 VAL A N   1 
ATOM   1311 C  CA  . VAL A 1 159 ? -16.241 -4.634  2.361   1.00 13.43  ? 160 VAL A CA  1 
ATOM   1312 C  C   . VAL A 1 159 ? -15.453 -5.757  1.634   1.00 13.16  ? 160 VAL A C   1 
ATOM   1313 O  O   . VAL A 1 159 ? -14.488 -5.542  0.897   1.00 14.94  ? 160 VAL A O   1 
ATOM   1314 C  CB  . VAL A 1 159 ? -15.930 -4.640  3.881   1.00 13.79  ? 160 VAL A CB  1 
ATOM   1315 C  CG1 . VAL A 1 159 ? -14.370 -4.725  4.086   1.00 15.39  ? 160 VAL A CG1 1 
ATOM   1316 C  CG2 . VAL A 1 159 ? -16.620 -3.449  4.507   1.00 16.30  ? 160 VAL A CG2 1 
ATOM   1317 N  N   . VAL A 1 160 ? -15.894 -7.011  1.895   1.00 12.65  ? 161 VAL A N   1 
ATOM   1318 C  CA  . VAL A 1 160 ? -15.162 -8.086  1.286   1.00 15.09  ? 161 VAL A CA  1 
ATOM   1319 C  C   . VAL A 1 160 ? -15.123 -8.033  -0.195  1.00 15.21  ? 161 VAL A C   1 
ATOM   1320 O  O   . VAL A 1 160 ? -14.080 -8.337  -0.757  1.00 16.59  ? 161 VAL A O   1 
ATOM   1321 C  CB  . VAL A 1 160 ? -15.883 -9.440  1.705   1.00 19.03  ? 161 VAL A CB  1 
ATOM   1322 C  CG1 . VAL A 1 160 ? -15.491 -10.659 0.850   1.00 20.78  ? 161 VAL A CG1 1 
ATOM   1323 C  CG2 . VAL A 1 160 ? -15.691 -9.733  3.198   1.00 19.08  ? 161 VAL A CG2 1 
ATOM   1324 N  N   . ASP A 1 161 ? -16.210 -7.597  -0.818  1.00 15.99  ? 162 ASP A N   1 
ATOM   1325 C  CA  . ASP A 1 161 ? -16.213 -7.616  -2.285  1.00 20.38  ? 162 ASP A CA  1 
ATOM   1326 C  C   . ASP A 1 161 ? -15.362 -6.508  -2.917  1.00 19.44  ? 162 ASP A C   1 
ATOM   1327 O  O   . ASP A 1 161 ? -14.974 -6.660  -4.104  1.00 26.41  ? 162 ASP A O   1 
ATOM   1328 C  CB  . ASP A 1 161 ? -17.642 -7.482  -2.687  1.00 23.94  ? 162 ASP A CB  1 
ATOM   1329 C  CG  . ASP A 1 161 ? -18.424 -8.888  -2.643  1.00 18.42  ? 162 ASP A CG  1 
ATOM   1330 O  OD1 . ASP A 1 161 ? -17.694 -9.981  -2.647  1.00 24.47  ? 162 ASP A OD1 1 
ATOM   1331 O  OD2 . ASP A 1 161 ? -19.615 -8.865  -2.452  1.00 26.54  ? 162 ASP A OD2 1 
ATOM   1332 N  N   . VAL A 1 162 ? -14.922 -5.481  -2.173  1.00 19.03  ? 163 VAL A N   1 
ATOM   1333 C  CA  . VAL A 1 162 ? -14.100 -4.448  -2.724  1.00 18.94  ? 163 VAL A CA  1 
ATOM   1334 C  C   . VAL A 1 162 ? -12.584 -4.780  -2.567  1.00 16.48  ? 163 VAL A C   1 
ATOM   1335 O  O   . VAL A 1 162 ? -11.676 -4.143  -3.113  1.00 19.19  ? 163 VAL A O   1 
ATOM   1336 C  CB  . VAL A 1 162 ? -14.495 -3.069  -2.150  1.00 24.05  ? 163 VAL A CB  1 
ATOM   1337 C  CG1 . VAL A 1 162 ? -13.797 -2.820  -0.825  1.00 21.88  ? 163 VAL A CG1 1 
ATOM   1338 C  CG2 . VAL A 1 162 ? -14.426 -1.857  -3.074  1.00 19.74  ? 163 VAL A CG2 1 
ATOM   1339 N  N   . LEU A 1 163 ? -12.314 -5.791  -1.726  1.00 17.18  ? 164 LEU A N   1 
ATOM   1340 C  CA  . LEU A 1 163 ? -10.944 -6.054  -1.439  1.00 15.53  ? 164 LEU A CA  1 
ATOM   1341 C  C   . LEU A 1 163 ? -10.045 -6.416  -2.608  1.00 17.20  ? 164 LEU A C   1 
ATOM   1342 O  O   . LEU A 1 163 ? -8.824  -6.105  -2.625  1.00 17.38  ? 164 LEU A O   1 
ATOM   1343 C  CB  . LEU A 1 163 ? -10.745 -7.086  -0.293  1.00 14.40  ? 164 LEU A CB  1 
ATOM   1344 C  CG  . LEU A 1 163 ? -11.387 -6.732  1.005   1.00 13.86  ? 164 LEU A CG  1 
ATOM   1345 C  CD1 . LEU A 1 163 ? -11.181 -7.904  2.023   1.00 16.04  ? 164 LEU A CD1 1 
ATOM   1346 C  CD2 . LEU A 1 163 ? -10.786 -5.427  1.592   1.00 14.45  ? 164 LEU A CD2 1 
ATOM   1347 N  N   . ASP A 1 164 ? -10.591 -7.075  -3.594  1.00 19.12  ? 165 ASP A N   1 
ATOM   1348 C  CA  . ASP A 1 164 ? -9.790  -7.379  -4.756  1.00 22.05  ? 165 ASP A CA  1 
ATOM   1349 C  C   . ASP A 1 164 ? -9.312  -6.102  -5.466  1.00 23.71  ? 165 ASP A C   1 
ATOM   1350 O  O   . ASP A 1 164 ? -8.335  -6.212  -6.236  1.00 27.11  ? 165 ASP A O   1 
ATOM   1351 C  CB  . ASP A 1 164 ? -10.580 -8.241  -5.772  1.00 27.56  ? 165 ASP A CB  1 
ATOM   1352 C  CG  . ASP A 1 164 ? -11.560 -7.327  -6.578  1.00 50.98  ? 165 ASP A CG  1 
ATOM   1353 O  OD1 . ASP A 1 164 ? -12.405 -6.694  -5.901  1.00 43.78  ? 165 ASP A OD1 1 
ATOM   1354 O  OD2 . ASP A 1 164 ? -11.507 -7.221  -7.901  1.00 65.61  ? 165 ASP A OD2 1 
ATOM   1355 N  N   . SER A 1 165 ? -9.975  -4.947  -5.295  1.00 19.97  ? 166 SER A N   1 
ATOM   1356 C  CA  . SER A 1 165 ? -9.588  -3.636  -5.933  1.00 20.49  ? 166 SER A CA  1 
ATOM   1357 C  C   . SER A 1 165 ? -8.606  -2.922  -5.115  1.00 16.30  ? 166 SER A C   1 
ATOM   1358 O  O   . SER A 1 165 ? -7.977  -1.974  -5.617  1.00 21.63  ? 166 SER A O   1 
ATOM   1359 C  CB  . SER A 1 165 ? -10.779 -2.790  -6.207  1.00 27.07  ? 166 SER A CB  1 
ATOM   1360 O  OG  . SER A 1 165 ? -11.179 -2.242  -5.023  1.00 24.82  ? 166 SER A OG  1 
ATOM   1361 N  N   . ILE A 1 166 ? -8.225  -3.438  -3.879  1.00 18.01  ? 167 ILE A N   1 
ATOM   1362 C  CA  . ILE A 1 166 ? -7.276  -2.798  -3.102  1.00 15.14  ? 167 ILE A CA  1 
ATOM   1363 C  C   . ILE A 1 166 ? -6.237  -3.793  -2.598  1.00 13.58  ? 167 ILE A C   1 
ATOM   1364 O  O   . ILE A 1 166 ? -5.813  -3.869  -1.409  1.00 15.47  ? 167 ILE A O   1 
ATOM   1365 C  CB  . ILE A 1 166 ? -7.799  -1.946  -1.922  1.00 16.10  ? 167 ILE A CB  1 
ATOM   1366 C  CG1 . ILE A 1 166 ? -8.676  -2.778  -1.016  1.00 14.78  ? 167 ILE A CG1 1 
ATOM   1367 C  CG2 . ILE A 1 166 ? -8.480  -0.733  -2.490  1.00 18.81  ? 167 ILE A CG2 1 
ATOM   1368 C  CD1 . ILE A 1 166 ? -8.620  -2.208  0.391   1.00 15.16  ? 167 ILE A CD1 1 
ATOM   1369 N  N   . LYS A 1 167 ? -5.945  -4.735  -3.464  1.00 15.50  ? 168 LYS A N   1 
ATOM   1370 C  CA  . LYS A 1 167 ? -5.058  -5.815  -3.049  1.00 15.31  ? 168 LYS A CA  1 
ATOM   1371 C  C   . LYS A 1 167 ? -3.805  -5.533  -2.402  1.00 14.54  ? 168 LYS A C   1 
ATOM   1372 O  O   . LYS A 1 167 ? -3.311  -6.137  -1.412  1.00 14.46  ? 168 LYS A O   1 
ATOM   1373 C  CB  . LYS A 1 167 ? -4.712  -6.808  -4.229  1.00 17.28  ? 168 LYS A CB  1 
ATOM   1374 C  CG  . LYS A 1 167 ? -3.988  -8.048  -3.783  1.00 17.25  ? 168 LYS A CG  1 
ATOM   1375 C  CD  . LYS A 1 167 ? -3.972  -8.889  -5.050  1.00 25.41  ? 168 LYS A CD  1 
ATOM   1376 C  CE  . LYS A 1 167 ? -2.539  -9.206  -5.425  1.00 31.11  ? 168 LYS A CE  1 
ATOM   1377 N  NZ  . LYS A 1 167 ? -2.608  -10.493 -4.675  1.00 36.18  ? 168 LYS A NZ  1 
ATOM   1378 N  N   . THR A 1 168 ? -3.151  -4.575  -3.044  1.00 13.79  ? 169 THR A N   1 
ATOM   1379 C  CA  . THR A 1 168 ? -1.831  -4.162  -2.621  1.00 13.64  ? 169 THR A CA  1 
ATOM   1380 C  C   . THR A 1 168 ? -1.794  -2.849  -1.880  1.00 11.83  ? 169 THR A C   1 
ATOM   1381 O  O   . THR A 1 168 ? -2.718  -2.038  -1.939  1.00 14.81  ? 169 THR A O   1 
ATOM   1382 C  CB  . THR A 1 168 ? -0.865  -4.075  -3.820  1.00 16.57  ? 169 THR A CB  1 
ATOM   1383 O  OG1 . THR A 1 168 ? -1.482  -3.336  -4.882  1.00 18.26  ? 169 THR A OG1 1 
ATOM   1384 C  CG2 . THR A 1 168 ? -0.507  -5.466  -4.317  1.00 18.13  ? 169 THR A CG2 1 
ATOM   1385 N  N   . LYS A 1 169 ? -0.679  -2.651  -1.183  1.00 15.75  ? 170 LYS A N   1 
ATOM   1386 C  CA  . LYS A 1 169 ? -0.414  -1.456  -0.385  1.00 15.43  ? 170 LYS A CA  1 
ATOM   1387 C  C   . LYS A 1 169 ? -0.546  -0.183  -1.213  1.00 16.75  ? 170 LYS A C   1 
ATOM   1388 O  O   . LYS A 1 169 ? 0.008   -0.069  -2.306  1.00 18.60  ? 170 LYS A O   1 
ATOM   1389 C  CB  . LYS A 1 169 ? 0.988   -1.548  0.227   1.00 13.51  ? 170 LYS A CB  1 
ATOM   1390 C  CG  . LYS A 1 169 ? 1.373   -0.367  1.101   1.00 17.39  ? 170 LYS A CG  1 
ATOM   1391 C  CD  . LYS A 1 169 ? 2.882   -0.189  1.150   1.00 18.39  ? 170 LYS A CD  1 
ATOM   1392 C  CE  . LYS A 1 169 ? 3.510   -1.090  2.200   1.00 28.15  ? 170 LYS A CE  1 
ATOM   1393 N  NZ  . LYS A 1 169 ? 4.412   -0.319  3.099   1.00 46.13  ? 170 LYS A NZ  1 
ATOM   1394 N  N   . GLY A 1 170 ? -1.225  0.817   -0.687  1.00 17.87  ? 171 GLY A N   1 
ATOM   1395 C  CA  . GLY A 1 170 ? -1.369  2.016   -1.471  1.00 17.56  ? 171 GLY A CA  1 
ATOM   1396 C  C   . GLY A 1 170 ? -2.696  2.186   -2.165  1.00 15.63  ? 171 GLY A C   1 
ATOM   1397 O  O   . GLY A 1 170 ? -3.097  3.365   -2.274  1.00 20.26  ? 171 GLY A O   1 
ATOM   1398 N  N   . LYS A 1 171 ? -3.328  1.083   -2.644  1.00 14.68  ? 172 LYS A N   1 
ATOM   1399 C  CA  . LYS A 1 171 ? -4.631  1.165   -3.311  1.00 17.56  ? 172 LYS A CA  1 
ATOM   1400 C  C   . LYS A 1 171 ? -5.754  1.662   -2.567  1.00 15.03  ? 172 LYS A C   1 
ATOM   1401 O  O   . LYS A 1 171 ? -5.907  1.205   -1.337  1.00 15.54  ? 172 LYS A O   1 
ATOM   1402 C  CB  . LYS A 1 171 ? -4.743  -0.179  -4.036  1.00 17.83  ? 172 LYS A CB  1 
ATOM   1403 C  CG  . LYS A 1 171 ? -3.619  -0.574  -4.991  1.00 21.84  ? 172 LYS A CG  1 
ATOM   1404 C  CD  . LYS A 1 171 ? -4.059  -1.603  -6.037  1.00 26.91  ? 172 LYS A CD  1 
ATOM   1405 C  CE  . LYS A 1 171 ? -5.371  -1.270  -6.873  1.00 32.35  ? 172 LYS A CE  1 
ATOM   1406 N  NZ  . LYS A 1 171 ? -5.698  -2.335  -7.961  1.00 32.81  ? 172 LYS A NZ  1 
ATOM   1407 N  N   . SER A 1 172 ? -6.637  2.437   -3.201  1.00 16.01  ? 173 SER A N   1 
ATOM   1408 C  CA  . SER A 1 172 ? -7.848  2.964   -2.560  1.00 16.65  ? 173 SER A CA  1 
ATOM   1409 C  C   . SER A 1 172 ? -9.044  2.973   -3.532  1.00 12.00  ? 173 SER A C   1 
ATOM   1410 O  O   . SER A 1 172 ? -8.861  3.156   -4.736  1.00 16.99  ? 173 SER A O   1 
ATOM   1411 C  CB  . SER A 1 172 ? -7.598  4.372   -2.017  1.00 16.47  ? 173 SER A CB  1 
ATOM   1412 O  OG  . SER A 1 172 ? -7.218  5.259   -3.055  1.00 25.15  ? 173 SER A OG  1 
ATOM   1413 N  N   . ALA A 1 173 ? -10.259 2.778   -3.013  1.00 17.03  ? 174 ALA A N   1 
ATOM   1414 C  CA  . ALA A 1 173 ? -11.389 2.768   -3.791  1.00 16.93  ? 174 ALA A CA  1 
ATOM   1415 C  C   . ALA A 1 173 ? -12.540 3.529   -3.116  1.00 14.16  ? 174 ALA A C   1 
ATOM   1416 O  O   . ALA A 1 173 ? -12.601 3.598   -1.882  1.00 14.81  ? 174 ALA A O   1 
ATOM   1417 C  CB  . ALA A 1 173 ? -11.754 1.308   -4.037  1.00 22.28  ? 174 ALA A CB  1 
ATOM   1418 N  N   . ASP A 1 174 ? -13.316 4.226   -3.966  1.00 17.89  ? 175 ASP A N   1 
ATOM   1419 C  CA  . ASP A 1 174 ? -14.532 4.892   -3.420  1.00 18.19  ? 175 ASP A CA  1 
ATOM   1420 C  C   . ASP A 1 174 ? -15.304 3.870   -2.685  1.00 17.13  ? 175 ASP A C   1 
ATOM   1421 O  O   . ASP A 1 174 ? -15.438 2.687   -3.144  1.00 26.97  ? 175 ASP A O   1 
ATOM   1422 C  CB  . ASP A 1 174 ? -15.303 5.375   -4.665  1.00 26.12  ? 175 ASP A CB  1 
ATOM   1423 C  CG  . ASP A 1 174 ? -14.639 6.601   -5.321  1.00 37.22  ? 175 ASP A CG  1 
ATOM   1424 O  OD1 . ASP A 1 174 ? -14.141 7.499   -4.603  1.00 48.16  ? 175 ASP A OD1 1 
ATOM   1425 O  OD2 . ASP A 1 174 ? -14.612 6.641   -6.608  1.00 32.52  ? 175 ASP A OD2 1 
ATOM   1426 N  N   . PHE A 1 175 ? -15.719 4.323   -1.541  1.00 17.73  ? 176 PHE A N   1 
ATOM   1427 C  CA  . PHE A 1 175 ? -16.491 3.425   -0.699  1.00 18.99  ? 176 PHE A CA  1 
ATOM   1428 C  C   . PHE A 1 175 ? -17.488 4.206   0.037   1.00 17.65  ? 176 PHE A C   1 
ATOM   1429 O  O   . PHE A 1 175 ? -17.335 4.451   1.214   1.00 21.48  ? 176 PHE A O   1 
ATOM   1430 C  CB  . PHE A 1 175 ? -15.481 2.607   0.161   1.00 19.09  ? 176 PHE A CB  1 
ATOM   1431 C  CG  . PHE A 1 175 ? -16.052 1.382   0.667   1.00 18.37  ? 176 PHE A CG  1 
ATOM   1432 C  CD1 . PHE A 1 175 ? -16.328 0.353   -0.150  1.00 20.74  ? 176 PHE A CD1 1 
ATOM   1433 C  CD2 . PHE A 1 175 ? -16.247 1.241   1.955   1.00 18.51  ? 176 PHE A CD2 1 
ATOM   1434 C  CE1 . PHE A 1 175 ? -16.858 -0.789  0.304   1.00 20.35  ? 176 PHE A CE1 1 
ATOM   1435 C  CE2 . PHE A 1 175 ? -16.786 0.077   2.504   1.00 19.59  ? 176 PHE A CE2 1 
ATOM   1436 C  CZ  . PHE A 1 175 ? -17.102 -0.933  1.663   1.00 20.60  ? 176 PHE A CZ  1 
ATOM   1437 N  N   . THR A 1 176 ? -18.470 4.679   -0.688  1.00 18.63  ? 177 THR A N   1 
ATOM   1438 C  CA  . THR A 1 176 ? -19.486 5.459   -0.080  1.00 17.00  ? 177 THR A CA  1 
ATOM   1439 C  C   . THR A 1 176 ? -20.685 4.704   0.343   1.00 14.59  ? 177 THR A C   1 
ATOM   1440 O  O   . THR A 1 176 ? -20.788 3.554   -0.132  1.00 17.99  ? 177 THR A O   1 
ATOM   1441 C  CB  . THR A 1 176 ? -19.830 6.565   -1.201  1.00 19.13  ? 177 THR A CB  1 
ATOM   1442 O  OG1 . THR A 1 176 ? -20.092 5.914   -2.457  1.00 23.17  ? 177 THR A OG1 1 
ATOM   1443 C  CG2 . THR A 1 176 ? -18.604 7.604   -1.375  1.00 24.88  ? 177 THR A CG2 1 
ATOM   1444 N  N   . ASN A 1 177 ? -21.579 5.163   1.248   1.00 14.61  ? 178 ASN A N   1 
ATOM   1445 C  CA  . ASN A 1 177 ? -22.818 4.603   1.622   1.00 17.00  ? 178 ASN A CA  1 
ATOM   1446 C  C   . ASN A 1 177 ? -22.585 3.311   2.362   1.00 17.50  ? 178 ASN A C   1 
ATOM   1447 O  O   . ASN A 1 177 ? -23.407 2.527   2.277   1.00 24.13  ? 178 ASN A O   1 
ATOM   1448 C  CB  . ASN A 1 177 ? -23.610 4.500   0.393   1.00 18.27  ? 178 ASN A CB  1 
ATOM   1449 C  CG  . ASN A 1 177 ? -23.839 5.923   -0.203  1.00 17.72  ? 178 ASN A CG  1 
ATOM   1450 O  OD1 . ASN A 1 177 ? -24.446 6.773   0.444   1.00 20.77  ? 178 ASN A OD1 1 
ATOM   1451 N  ND2 . ASN A 1 177 ? -23.245 6.202   -1.350  1.00 17.56  ? 178 ASN A ND2 1 
ATOM   1452 N  N   . PHE A 1 178 ? -21.389 3.107   2.974   1.00 16.35  ? 179 PHE A N   1 
ATOM   1453 C  CA  . PHE A 1 178 ? -21.283 1.887   3.770   1.00 15.92  ? 179 PHE A CA  1 
ATOM   1454 C  C   . PHE A 1 178 ? -21.769 2.149   5.146   1.00 13.78  ? 179 PHE A C   1 
ATOM   1455 O  O   . PHE A 1 178 ? -21.350 3.146   5.777   1.00 15.11  ? 179 PHE A O   1 
ATOM   1456 C  CB  . PHE A 1 178 ? -19.880 1.424   3.833   1.00 15.75  ? 179 PHE A CB  1 
ATOM   1457 C  CG  . PHE A 1 178 ? -19.689 0.182   4.680   1.00 15.86  ? 179 PHE A CG  1 
ATOM   1458 C  CD1 . PHE A 1 178 ? -20.047 -1.090  4.152   1.00 17.04  ? 179 PHE A CD1 1 
ATOM   1459 C  CD2 . PHE A 1 178 ? -19.314 0.274   6.030   1.00 13.60  ? 179 PHE A CD2 1 
ATOM   1460 C  CE1 . PHE A 1 178 ? -20.081 -2.175  4.948   1.00 18.36  ? 179 PHE A CE1 1 
ATOM   1461 C  CE2 . PHE A 1 178 ? -19.289 -0.936  6.810   1.00 13.63  ? 179 PHE A CE2 1 
ATOM   1462 C  CZ  . PHE A 1 178 ? -19.660 -2.107  6.283   1.00 15.91  ? 179 PHE A CZ  1 
ATOM   1463 N  N   . ASP A 1 179 ? -22.628 1.301   5.647   1.00 14.81  ? 180 ASP A N   1 
ATOM   1464 C  CA  . ASP A 1 179 ? -23.255 1.558   6.964   1.00 14.98  ? 180 ASP A CA  1 
ATOM   1465 C  C   . ASP A 1 179 ? -22.601 0.664   7.998   1.00 12.86  ? 180 ASP A C   1 
ATOM   1466 O  O   . ASP A 1 179 ? -22.846 -0.553  8.036   1.00 13.01  ? 180 ASP A O   1 
ATOM   1467 C  CB  . ASP A 1 179 ? -24.730 1.143   6.804   1.00 17.32  ? 180 ASP A CB  1 
ATOM   1468 C  CG  . ASP A 1 179 ? -25.541 1.552   8.041   1.00 17.49  ? 180 ASP A CG  1 
ATOM   1469 O  OD1 . ASP A 1 179 ? -24.988 1.798   9.141   1.00 16.52  ? 180 ASP A OD1 1 
ATOM   1470 O  OD2 . ASP A 1 179 ? -26.721 1.655   7.933   1.00 25.38  ? 180 ASP A OD2 1 
ATOM   1471 N  N   . PRO A 1 180 ? -21.834 1.244   8.949   1.00 11.53  ? 181 PRO A N   1 
ATOM   1472 C  CA  . PRO A 1 180 ? -21.121 0.391   9.931   1.00 11.48  ? 181 PRO A CA  1 
ATOM   1473 C  C   . PRO A 1 180 ? -22.062 -0.197  10.972  1.00 11.15  ? 181 PRO A C   1 
ATOM   1474 O  O   . PRO A 1 180 ? -21.608 -1.093  11.714  1.00 10.95  ? 181 PRO A O   1 
ATOM   1475 C  CB  . PRO A 1 180 ? -20.149 1.406   10.533  1.00 12.69  ? 181 PRO A CB  1 
ATOM   1476 C  CG  . PRO A 1 180 ? -20.765 2.715   10.380  1.00 13.12  ? 181 PRO A CG  1 
ATOM   1477 C  CD  . PRO A 1 180 ? -21.477 2.669   8.990   1.00 13.06  ? 181 PRO A CD  1 
ATOM   1478 N  N   . ARG A 1 181 ? -23.340 0.185   10.965  1.00 11.16  ? 182 ARG A N   1 
ATOM   1479 C  CA  . ARG A 1 181 ? -24.279 -0.438  11.936  1.00 12.11  ? 182 ARG A CA  1 
ATOM   1480 C  C   . ARG A 1 181 ? -24.373 -1.935  11.550  1.00 13.10  ? 182 ARG A C   1 
ATOM   1481 O  O   . ARG A 1 181 ? -24.742 -2.763  12.469  1.00 13.74  ? 182 ARG A O   1 
ATOM   1482 C  CB  . ARG A 1 181 ? -25.664 0.127   11.845  1.00 13.10  ? 182 ARG A CB  1 
ATOM   1483 C  CG  . ARG A 1 181 ? -25.632 1.597   12.381  1.00 14.21  ? 182 ARG A CG  1 
ATOM   1484 C  CD  . ARG A 1 181 ? -26.974 2.286   12.327  1.00 18.19  ? 182 ARG A CD  1 
ATOM   1485 N  NE  . ARG A 1 181 ? -27.344 2.581   10.956  1.00 18.22  ? 182 ARG A NE  1 
ATOM   1486 C  CZ  . ARG A 1 181 ? -28.436 3.240   10.607  1.00 20.87  ? 182 ARG A CZ  1 
ATOM   1487 N  NH1 . ARG A 1 181 ? -29.283 3.674   11.530  1.00 24.66  ? 182 ARG A NH1 1 
ATOM   1488 N  NH2 . ARG A 1 181 ? -28.680 3.446   9.323   1.00 25.09  ? 182 ARG A NH2 1 
ATOM   1489 N  N   . GLY A 1 182 ? -24.129 -2.329  10.295  1.00 13.01  ? 183 GLY A N   1 
ATOM   1490 C  CA  . GLY A 1 182 ? -24.258 -3.732  9.905   1.00 14.82  ? 183 GLY A CA  1 
ATOM   1491 C  C   . GLY A 1 182 ? -23.082 -4.592  10.434  1.00 15.18  ? 183 GLY A C   1 
ATOM   1492 O  O   . GLY A 1 182 ? -23.101 -5.779  10.150  1.00 16.59  ? 183 GLY A O   1 
ATOM   1493 N  N   . LEU A 1 183 ? -22.099 -4.009  11.177  1.00 12.40  ? 184 LEU A N   1 
ATOM   1494 C  CA  . LEU A 1 183 ? -21.012 -4.763  11.756  1.00 13.08  ? 184 LEU A CA  1 
ATOM   1495 C  C   . LEU A 1 183 ? -21.182 -4.962  13.223  1.00 11.99  ? 184 LEU A C   1 
ATOM   1496 O  O   . LEU A 1 183 ? -20.269 -5.562  13.859  1.00 12.99  ? 184 LEU A O   1 
ATOM   1497 C  CB  . LEU A 1 183 ? -19.720 -4.034  11.463  1.00 12.58  ? 184 LEU A CB  1 
ATOM   1498 C  CG  . LEU A 1 183 ? -19.396 -3.942  9.988   1.00 14.44  ? 184 LEU A CG  1 
ATOM   1499 C  CD1 . LEU A 1 183 ? -18.202 -3.057  9.865   1.00 17.61  ? 184 LEU A CD1 1 
ATOM   1500 C  CD2 . LEU A 1 183 ? -19.229 -5.210  9.231   1.00 18.21  ? 184 LEU A CD2 1 
ATOM   1501 N  N   . LEU A 1 184 ? -22.267 -4.492  13.849  1.00 12.16  ? 185 LEU A N   1 
ATOM   1502 C  CA  . LEU A 1 184 ? -22.381 -4.590  15.260  1.00 10.99  ? 185 LEU A CA  1 
ATOM   1503 C  C   . LEU A 1 184 ? -23.146 -5.832  15.716  1.00 13.49  ? 185 LEU A C   1 
ATOM   1504 O  O   . LEU A 1 184 ? -24.040 -6.290  15.027  1.00 23.50  ? 185 LEU A O   1 
ATOM   1505 C  CB  . LEU A 1 184 ? -23.207 -3.349  15.811  1.00 11.20  ? 185 LEU A CB  1 
ATOM   1506 C  CG  . LEU A 1 184 ? -22.616 -1.953  15.398  1.00 9.70   ? 185 LEU A CG  1 
ATOM   1507 C  CD1 . LEU A 1 184 ? -23.500 -0.850  15.899  1.00 12.05  ? 185 LEU A CD1 1 
ATOM   1508 C  CD2 . LEU A 1 184 ? -21.234 -1.801  15.956  1.00 12.20  ? 185 LEU A CD2 1 
ATOM   1509 N  N   . PRO A 1 185 ? -22.815 -6.398  16.882  1.00 10.90  ? 186 PRO A N   1 
ATOM   1510 C  CA  . PRO A 1 185 ? -23.546 -7.492  17.455  1.00 12.07  ? 186 PRO A CA  1 
ATOM   1511 C  C   . PRO A 1 185 ? -24.827 -6.959  18.079  1.00 12.73  ? 186 PRO A C   1 
ATOM   1512 O  O   . PRO A 1 185 ? -25.042 -5.777  18.157  1.00 15.46  ? 186 PRO A O   1 
ATOM   1513 C  CB  . PRO A 1 185 ? -22.592 -8.120  18.475  1.00 10.90  ? 186 PRO A CB  1 
ATOM   1514 C  CG  . PRO A 1 185 ? -21.904 -6.883  18.953  1.00 9.79   ? 186 PRO A CG  1 
ATOM   1515 C  CD  . PRO A 1 185 ? -21.669 -5.978  17.724  1.00 8.86   ? 186 PRO A CD  1 
ATOM   1516 N  N   . GLU A 1 186 ? -25.658 -7.902  18.584  1.00 12.96  ? 187 GLU A N   1 
ATOM   1517 C  CA  . GLU A 1 186 ? -26.926 -7.482  19.180  1.00 14.33  ? 187 GLU A CA  1 
ATOM   1518 C  C   . GLU A 1 186 ? -26.701 -6.743  20.483  1.00 12.86  ? 187 GLU A C   1 
ATOM   1519 O  O   . GLU A 1 186 ? -27.314 -5.647  20.740  1.00 15.79  ? 187 GLU A O   1 
ATOM   1520 C  CB  . GLU A 1 186 ? -27.633 -8.732  19.498  1.00 18.97  ? 187 GLU A CB  1 
ATOM   1521 C  CG  . GLU A 1 186 ? -28.803 -8.616  20.346  1.00 34.29  ? 187 GLU A CG  1 
ATOM   1522 C  CD  . GLU A 1 186 ? -29.462 -9.955  20.576  1.00 30.71  ? 187 GLU A CD  1 
ATOM   1523 O  OE1 . GLU A 1 186 ? -29.279 -10.826 19.714  1.00 23.70  ? 187 GLU A OE1 1 
ATOM   1524 O  OE2 . GLU A 1 186 ? -30.136 -10.051 21.611  1.00 39.02  ? 187 GLU A OE2 1 
ATOM   1525 N  N   . SER A 1 187 ? -25.868 -7.263  21.342  1.00 11.79  ? 188 SER A N   1 
ATOM   1526 C  CA  . SER A 1 187 ? -25.618 -6.655  22.628  1.00 12.51  ? 188 SER A CA  1 
ATOM   1527 C  C   . SER A 1 187 ? -24.481 -5.618  22.608  1.00 11.12  ? 188 SER A C   1 
ATOM   1528 O  O   . SER A 1 187 ? -23.445 -5.885  21.970  1.00 12.75  ? 188 SER A O   1 
ATOM   1529 C  CB  . SER A 1 187 ? -25.202 -7.709  23.623  1.00 14.48  ? 188 SER A CB  1 
ATOM   1530 O  OG  . SER A 1 187 ? -24.953 -7.123  24.938  1.00 14.67  ? 188 SER A OG  1 
ATOM   1531 N  N   . LEU A 1 188 ? -24.646 -4.560  23.357  1.00 11.52  ? 189 LEU A N   1 
ATOM   1532 C  CA  . LEU A 1 188 ? -23.587 -3.564  23.595  1.00 11.10  ? 189 LEU A CA  1 
ATOM   1533 C  C   . LEU A 1 188 ? -22.962 -3.713  24.953  1.00 10.61  ? 189 LEU A C   1 
ATOM   1534 O  O   . LEU A 1 188 ? -22.279 -2.788  25.413  1.00 12.72  ? 189 LEU A O   1 
ATOM   1535 C  CB  . LEU A 1 188 ? -24.082 -2.130  23.291  1.00 13.19  ? 189 LEU A CB  1 
ATOM   1536 C  CG  . LEU A 1 188 ? -24.489 -1.786  21.914  1.00 15.45  ? 189 LEU A CG  1 
ATOM   1537 C  CD1 . LEU A 1 188 ? -25.033 -0.364  21.921  1.00 17.62  ? 189 LEU A CD1 1 
ATOM   1538 C  CD2 . LEU A 1 188 ? -23.366 -1.971  20.951  1.00 16.59  ? 189 LEU A CD2 1 
ATOM   1539 N  N   . ASP A 1 189 ? -23.096 -4.874  25.625  1.00 10.33  ? 190 ASP A N   1 
ATOM   1540 C  CA  . ASP A 1 189 ? -22.377 -5.068  26.846  1.00 10.96  ? 190 ASP A CA  1 
ATOM   1541 C  C   . ASP A 1 189 ? -20.834 -5.049  26.563  1.00 8.84   ? 190 ASP A C   1 
ATOM   1542 O  O   . ASP A 1 189 ? -20.402 -5.589  25.520  1.00 8.74   ? 190 ASP A O   1 
ATOM   1543 C  CB  . ASP A 1 189 ? -22.702 -6.417  27.439  1.00 14.21  ? 190 ASP A CB  1 
ATOM   1544 C  CG  . ASP A 1 189 ? -24.096 -6.515  28.110  1.00 16.73  ? 190 ASP A CG  1 
ATOM   1545 O  OD1 . ASP A 1 189 ? -24.740 -5.426  28.275  1.00 24.44  ? 190 ASP A OD1 1 
ATOM   1546 O  OD2 . ASP A 1 189 ? -24.501 -7.694  28.359  1.00 26.49  ? 190 ASP A OD2 1 
ATOM   1547 N  N   . TYR A 1 190 ? -20.062 -4.467  27.470  1.00 8.75   ? 191 TYR A N   1 
ATOM   1548 C  CA  . TYR A 1 190 ? -18.639 -4.233  27.121  1.00 8.48   ? 191 TYR A CA  1 
ATOM   1549 C  C   . TYR A 1 190 ? -17.779 -4.301  28.383  1.00 7.69   ? 191 TYR A C   1 
ATOM   1550 O  O   . TYR A 1 190 ? -18.190 -4.163  29.563  1.00 8.84   ? 191 TYR A O   1 
ATOM   1551 C  CB  . TYR A 1 190 ? -18.485 -2.840  26.493  1.00 8.89   ? 191 TYR A CB  1 
ATOM   1552 C  CG  . TYR A 1 190 ? -18.903 -1.676  27.357  1.00 8.68   ? 191 TYR A CG  1 
ATOM   1553 C  CD1 . TYR A 1 190 ? -17.974 -1.071  28.220  1.00 8.85   ? 191 TYR A CD1 1 
ATOM   1554 C  CD2 . TYR A 1 190 ? -20.191 -1.167  27.291  1.00 9.71   ? 191 TYR A CD2 1 
ATOM   1555 C  CE1 . TYR A 1 190 ? -18.348 -0.027  29.051  1.00 10.05  ? 191 TYR A CE1 1 
ATOM   1556 C  CE2 . TYR A 1 190 ? -20.551 -0.102  28.105  1.00 10.18  ? 191 TYR A CE2 1 
ATOM   1557 C  CZ  . TYR A 1 190 ? -19.678 0.470   28.971  1.00 10.22  ? 191 TYR A CZ  1 
ATOM   1558 O  OH  . TYR A 1 190 ? -20.030 1.503   29.830  1.00 11.77  ? 191 TYR A OH  1 
ATOM   1559 N  N   . TRP A 1 191 ? -16.469 -4.432  28.076  1.00 7.15   ? 192 TRP A N   1 
ATOM   1560 C  CA  . TRP A 1 191 ? -15.381 -4.159  29.019  1.00 7.21   ? 192 TRP A CA  1 
ATOM   1561 C  C   . TRP A 1 191 ? -14.691 -2.882  28.609  1.00 6.76   ? 192 TRP A C   1 
ATOM   1562 O  O   . TRP A 1 191 ? -14.621 -2.537  27.426  1.00 7.91   ? 192 TRP A O   1 
ATOM   1563 C  CB  . TRP A 1 191 ? -14.356 -5.308  29.027  1.00 7.70   ? 192 TRP A CB  1 
ATOM   1564 C  CG  . TRP A 1 191 ? -14.862 -6.632  29.434  1.00 7.93   ? 192 TRP A CG  1 
ATOM   1565 C  CD1 . TRP A 1 191 ? -15.076 -7.048  30.725  1.00 9.66   ? 192 TRP A CD1 1 
ATOM   1566 C  CD2 . TRP A 1 191 ? -15.142 -7.762  28.605  1.00 7.77   ? 192 TRP A CD2 1 
ATOM   1567 N  NE1 . TRP A 1 191 ? -15.507 -8.389  30.685  1.00 10.40  ? 192 TRP A NE1 1 
ATOM   1568 C  CE2 . TRP A 1 191 ? -15.557 -8.805  29.408  1.00 9.45   ? 192 TRP A CE2 1 
ATOM   1569 C  CE3 . TRP A 1 191 ? -15.073 -7.979  27.199  1.00 8.09   ? 192 TRP A CE3 1 
ATOM   1570 C  CZ2 . TRP A 1 191 ? -15.866 -10.082 28.878  1.00 10.60  ? 192 TRP A CZ2 1 
ATOM   1571 C  CZ3 . TRP A 1 191 ? -15.340 -9.217  26.715  1.00 9.57   ? 192 TRP A CZ3 1 
ATOM   1572 C  CH2 . TRP A 1 191 ? -15.714 -10.244 27.539  1.00 11.01  ? 192 TRP A CH2 1 
ATOM   1573 N  N   . THR A 1 192 ? -14.097 -2.168  29.587  1.00 6.58   ? 193 THR A N   1 
ATOM   1574 C  CA  . THR A 1 192 ? -13.380 -0.959  29.245  1.00 6.92   ? 193 THR A CA  1 
ATOM   1575 C  C   . THR A 1 192 ? -12.159 -0.798  30.128  1.00 6.66   ? 193 THR A C   1 
ATOM   1576 O  O   . THR A 1 192 ? -12.109 -1.195  31.296  1.00 7.50   ? 193 THR A O   1 
ATOM   1577 C  CB  . THR A 1 192 ? -14.316 0.262   29.363  1.00 7.49   ? 193 THR A CB  1 
ATOM   1578 O  OG1 . THR A 1 192 ? -13.626 1.449   28.971  1.00 7.55   ? 193 THR A OG1 1 
ATOM   1579 C  CG2 . THR A 1 192 ? -14.878 0.480   30.767  1.00 8.63   ? 193 THR A CG2 1 
ATOM   1580 N  N   . TYR A 1 193 ? -11.107 -0.183  29.544  1.00 6.55   ? 194 TYR A N   1 
ATOM   1581 C  CA  . TYR A 1 193 ? -9.863  0.092   30.259  1.00 6.96   ? 194 TYR A CA  1 
ATOM   1582 C  C   . TYR A 1 193 ? -9.102  1.150   29.493  1.00 6.31   ? 194 TYR A C   1 
ATOM   1583 O  O   . TYR A 1 193 ? -9.325  1.338   28.299  1.00 6.77   ? 194 TYR A O   1 
ATOM   1584 C  CB  . TYR A 1 193 ? -9.018  -1.185  30.453  1.00 7.43   ? 194 TYR A CB  1 
ATOM   1585 C  CG  . TYR A 1 193 ? -8.345  -1.642  29.181  1.00 6.68   ? 194 TYR A CG  1 
ATOM   1586 C  CD1 . TYR A 1 193 ? -9.006  -2.370  28.194  1.00 6.86   ? 194 TYR A CD1 1 
ATOM   1587 C  CD2 . TYR A 1 193 ? -7.027  -1.311  28.945  1.00 7.13   ? 194 TYR A CD2 1 
ATOM   1588 C  CE1 . TYR A 1 193 ? -8.380  -2.719  27.007  1.00 6.45   ? 194 TYR A CE1 1 
ATOM   1589 C  CE2 . TYR A 1 193 ? -6.371  -1.644  27.774  1.00 7.26   ? 194 TYR A CE2 1 
ATOM   1590 C  CZ  . TYR A 1 193 ? -7.063  -2.337  26.787  1.00 5.92   ? 194 TYR A CZ  1 
ATOM   1591 O  OH  . TYR A 1 193 ? -6.417  -2.663  25.623  1.00 6.74   ? 194 TYR A OH  1 
ATOM   1592 N  N   . PRO A 1 194 ? -8.151  1.846   30.158  1.00 6.60   ? 195 PRO A N   1 
ATOM   1593 C  CA  . PRO A 1 194 ? -7.325  2.867   29.468  1.00 7.11   ? 195 PRO A CA  1 
ATOM   1594 C  C   . PRO A 1 194 ? -6.128  2.198   28.782  1.00 6.34   ? 195 PRO A C   1 
ATOM   1595 O  O   . PRO A 1 194 ? -5.380  1.425   29.442  1.00 7.56   ? 195 PRO A O   1 
ATOM   1596 C  CB  . PRO A 1 194 ? -6.855  3.761   30.620  1.00 8.70   ? 195 PRO A CB  1 
ATOM   1597 C  CG  . PRO A 1 194 ? -6.843  2.821   31.830  1.00 9.37   ? 195 PRO A CG  1 
ATOM   1598 C  CD  . PRO A 1 194 ? -7.983  1.882   31.627  1.00 8.14   ? 195 PRO A CD  1 
ATOM   1599 N  N   . GLY A 1 195 ? -5.898  2.511   27.528  1.00 6.28   ? 196 GLY A N   1 
ATOM   1600 C  CA  . GLY A 1 195 ? -4.792  1.893   26.808  1.00 6.62   ? 196 GLY A CA  1 
ATOM   1601 C  C   . GLY A 1 195 ? -4.255  2.787   25.714  1.00 6.58   ? 196 GLY A C   1 
ATOM   1602 O  O   . GLY A 1 195 ? -4.139  4.014   25.869  1.00 6.84   ? 196 GLY A O   1 
ATOM   1603 N  N   . SER A 1 196 ? -3.840  2.129   24.634  1.00 6.27   ? 197 SER A N   1 
ATOM   1604 C  CA  . SER A 1 196 ? -3.032  2.794   23.590  1.00 6.61   ? 197 SER A CA  1 
ATOM   1605 C  C   . SER A 1 196 ? -3.475  2.367   22.244  1.00 5.74   ? 197 SER A C   1 
ATOM   1606 O  O   . SER A 1 196 ? -4.218  1.401   22.054  1.00 6.30   ? 197 SER A O   1 
ATOM   1607 C  CB  . SER A 1 196 ? -1.542  2.389   23.785  1.00 7.36   ? 197 SER A CB  1 
ATOM   1608 O  OG  . SER A 1 196 ? -1.296  1.035   23.386  1.00 6.92   ? 197 SER A OG  1 
ATOM   1609 N  N   . LEU A 1 197 ? -2.860  3.011   21.237  1.00 6.05   ? 198 LEU A N   1 
ATOM   1610 C  CA  . LEU A 1 197 ? -2.990  2.498   19.886  1.00 6.50   ? 198 LEU A CA  1 
ATOM   1611 C  C   . LEU A 1 197 ? -2.218  1.122   19.926  1.00 6.42   ? 198 LEU A C   1 
ATOM   1612 O  O   . LEU A 1 197 ? -1.194  0.968   20.652  1.00 7.17   ? 198 LEU A O   1 
ATOM   1613 C  CB  . LEU A 1 197 ? -2.127  3.326   18.942  1.00 7.99   ? 198 LEU A CB  1 
ATOM   1614 C  CG  . LEU A 1 197 ? -2.809  4.446   18.183  1.00 13.08  ? 198 LEU A CG  1 
ATOM   1615 C  CD1 . LEU A 1 197 ? -3.627  5.416   19.015  1.00 12.00  ? 198 LEU A CD1 1 
ATOM   1616 C  CD2 . LEU A 1 197 ? -1.872  5.153   17.249  1.00 15.67  ? 198 LEU A CD2 1 
ATOM   1617 N  N   . THR A 1 198 ? -2.692  0.147   19.150  1.00 6.10   ? 199 THR A N   1 
ATOM   1618 C  CA  . THR A 1 198 ? -1.989  -1.137  19.080  1.00 7.37   ? 199 THR A CA  1 
ATOM   1619 C  C   . THR A 1 198 ? -0.998  -1.202  17.944  1.00 7.02   ? 199 THR A C   1 
ATOM   1620 O  O   . THR A 1 198 ? -0.354  -2.265  17.771  1.00 7.82   ? 199 THR A O   1 
ATOM   1621 C  CB  . THR A 1 198 ? -2.998  -2.280  18.944  1.00 6.97   ? 199 THR A CB  1 
ATOM   1622 O  OG1 . THR A 1 198 ? -3.549  -2.223  17.639  1.00 6.69   ? 199 THR A OG1 1 
ATOM   1623 C  CG2 . THR A 1 198 ? -4.045  -2.318  20.037  1.00 7.16   ? 199 THR A CG2 1 
ATOM   1624 N  N   . THR A 1 199 ? -0.901  -0.151  17.159  1.00 7.87   ? 200 THR A N   1 
ATOM   1625 C  CA  . THR A 1 199 ? 0.102   -0.033  16.095  1.00 8.55   ? 200 THR A CA  1 
ATOM   1626 C  C   . THR A 1 199 ? 0.965   1.175   16.447  1.00 8.35   ? 200 THR A C   1 
ATOM   1627 O  O   . THR A 1 199 ? 0.539   2.128   17.068  1.00 8.86   ? 200 THR A O   1 
ATOM   1628 C  CB  . THR A 1 199 ? -0.566  0.265   14.733  1.00 9.26   ? 200 THR A CB  1 
ATOM   1629 O  OG1 . THR A 1 199 ? -1.344  1.435   14.782  1.00 12.10  ? 200 THR A OG1 1 
ATOM   1630 C  CG2 . THR A 1 199 ? -1.390  -0.881  14.297  1.00 9.50   ? 200 THR A CG2 1 
ATOM   1631 N  N   . PRO A 1 200 ? 2.234   1.169   15.972  1.00 9.18   ? 201 PRO A N   1 
ATOM   1632 C  CA  . PRO A 1 200 ? 3.036   2.381   16.046  1.00 9.56   ? 201 PRO A CA  1 
ATOM   1633 C  C   . PRO A 1 200 ? 2.189   3.575   15.500  1.00 10.79  ? 201 PRO A C   1 
ATOM   1634 O  O   . PRO A 1 200 ? 1.490   3.426   14.486  1.00 12.56  ? 201 PRO A O   1 
ATOM   1635 C  CB  . PRO A 1 200 ? 4.215   2.032   15.153  1.00 11.73  ? 201 PRO A CB  1 
ATOM   1636 C  CG  . PRO A 1 200 ? 4.429   0.585   15.426  1.00 11.94  ? 201 PRO A CG  1 
ATOM   1637 C  CD  . PRO A 1 200 ? 3.008   0.039   15.363  1.00 10.62  ? 201 PRO A CD  1 
ATOM   1638 N  N   . PRO A 1 201 ? 2.264   4.735   16.154  1.00 10.07  ? 202 PRO A N   1 
ATOM   1639 C  CA  . PRO A 1 201 ? 3.218   5.123   17.210  1.00 9.92   ? 202 PRO A CA  1 
ATOM   1640 C  C   . PRO A 1 201 ? 2.817   4.708   18.607  1.00 9.07   ? 202 PRO A C   1 
ATOM   1641 O  O   . PRO A 1 201 ? 3.508   5.131   19.571  1.00 9.80   ? 202 PRO A O   1 
ATOM   1642 C  CB  . PRO A 1 201 ? 3.285   6.657   17.056  1.00 13.26  ? 202 PRO A CB  1 
ATOM   1643 C  CG  . PRO A 1 201 ? 1.902   7.033   16.538  1.00 13.64  ? 202 PRO A CG  1 
ATOM   1644 C  CD  . PRO A 1 201 ? 1.514   5.918   15.628  1.00 12.21  ? 202 PRO A CD  1 
ATOM   1645 N  N   . LEU A 1 202 ? 1.801   3.877   18.823  1.00 8.37   ? 203 LEU A N   1 
ATOM   1646 C  CA  . LEU A 1 202 ? 1.590   3.258   20.142  1.00 8.00   ? 203 LEU A CA  1 
ATOM   1647 C  C   . LEU A 1 202 ? 1.207   4.274   21.221  1.00 7.67   ? 203 LEU A C   1 
ATOM   1648 O  O   . LEU A 1 202 ? 1.346   4.026   22.417  1.00 7.82   ? 203 LEU A O   1 
ATOM   1649 C  CB  . LEU A 1 202 ? 2.744   2.350   20.610  1.00 8.40   ? 203 LEU A CB  1 
ATOM   1650 C  CG  . LEU A 1 202 ? 3.067   1.194   19.652  1.00 8.44   ? 203 LEU A CG  1 
ATOM   1651 C  CD1 . LEU A 1 202 ? 4.364   0.541   20.075  1.00 11.09  ? 203 LEU A CD1 1 
ATOM   1652 C  CD2 . LEU A 1 202 ? 1.946   0.188   19.599  1.00 9.37   ? 203 LEU A CD2 1 
ATOM   1653 N  N   . LEU A 1 203 ? 0.629   5.412   20.804  1.00 8.02   ? 204 LEU A N   1 
ATOM   1654 C  CA  . LEU A 1 203 ? 0.338   6.511   21.732  1.00 8.30   ? 204 LEU A CA  1 
ATOM   1655 C  C   . LEU A 1 203 ? -0.699  6.089   22.738  1.00 7.83   ? 204 LEU A C   1 
ATOM   1656 O  O   . LEU A 1 203 ? -1.676  5.369   22.447  1.00 8.00   ? 204 LEU A O   1 
ATOM   1657 C  CB  . LEU A 1 203 ? -0.152  7.724   20.952  1.00 9.27   ? 204 LEU A CB  1 
ATOM   1658 C  CG  . LEU A 1 203 ? 0.900   8.309   20.014  1.00 11.40  ? 204 LEU A CG  1 
ATOM   1659 C  CD1 . LEU A 1 203 ? 0.284   9.373   19.094  1.00 13.08  ? 204 LEU A CD1 1 
ATOM   1660 C  CD2 . LEU A 1 203 ? 2.143   8.879   20.858  1.00 15.56  ? 204 LEU A CD2 1 
ATOM   1661 N  N   . GLU A 1 204 ? -0.503  6.558   23.965  1.00 8.65   ? 205 GLU A N   1 
ATOM   1662 C  CA  . GLU A 1 204 ? -1.332  6.182   25.118  1.00 8.25   ? 205 GLU A CA  1 
ATOM   1663 C  C   . GLU A 1 204 ? -2.494  7.160   25.296  1.00 7.64   ? 205 GLU A C   1 
ATOM   1664 O  O   . GLU A 1 204 ? -2.616  7.921   26.249  1.00 10.17  ? 205 GLU A O   1 
ATOM   1665 C  CB  . GLU A 1 204 ? -0.439  6.034   26.372  1.00 9.37   ? 205 GLU A CB  1 
ATOM   1666 C  CG  . GLU A 1 204 ? 0.451   4.824   26.219  1.00 9.94   ? 205 GLU A CG  1 
ATOM   1667 C  CD  . GLU A 1 204 ? 1.358   4.537   27.410  1.00 9.94   ? 205 GLU A CD  1 
ATOM   1668 O  OE1 . GLU A 1 204 ? 1.713   5.464   28.185  1.00 12.36  ? 205 GLU A OE1 1 
ATOM   1669 O  OE2 . GLU A 1 204 ? 1.743   3.352   27.565  1.00 10.40  ? 205 GLU A OE2 1 
ATOM   1670 N  N   . CYS A 1 205 ? -3.417  7.070   24.354  1.00 7.38   ? 206 CYS A N   1 
ATOM   1671 C  CA  . CYS A 1 205 ? -4.497  8.050   24.164  1.00 7.34   ? 206 CYS A CA  1 
ATOM   1672 C  C   . CYS A 1 205 ? -5.833  7.419   24.042  1.00 6.71   ? 206 CYS A C   1 
ATOM   1673 O  O   . CYS A 1 205 ? -6.779  8.134   23.692  1.00 8.42   ? 206 CYS A O   1 
ATOM   1674 C  CB  . CYS A 1 205 ? -4.200  8.933   22.927  1.00 8.26   ? 206 CYS A CB  1 
ATOM   1675 S  SG  . CYS A 1 205 ? -4.155  7.979   21.387  1.00 9.09   ? 206 CYS A SG  1 
ATOM   1676 N  N   . VAL A 1 206 ? -5.976  6.116   24.290  1.00 6.87   ? 207 VAL A N   1 
ATOM   1677 C  CA  . VAL A 1 206 ? -7.216  5.430   23.934  1.00 6.48   ? 207 VAL A CA  1 
ATOM   1678 C  C   . VAL A 1 206 ? -7.970  4.953   25.159  1.00 6.32   ? 207 VAL A C   1 
ATOM   1679 O  O   . VAL A 1 206 ? -7.438  4.304   26.046  1.00 7.83   ? 207 VAL A O   1 
ATOM   1680 C  CB  . VAL A 1 206 ? -6.908  4.161   23.083  1.00 6.95   ? 207 VAL A CB  1 
ATOM   1681 C  CG1 . VAL A 1 206 ? -8.247  3.442   22.731  1.00 6.95   ? 207 VAL A CG1 1 
ATOM   1682 C  CG2 . VAL A 1 206 ? -6.190  4.553   21.761  1.00 8.14   ? 207 VAL A CG2 1 
ATOM   1683 N  N   . THR A 1 207 ? -9.308  5.261   25.207  1.00 6.05   ? 208 THR A N   1 
ATOM   1684 C  CA  . THR A 1 207 ? -10.211 4.504   26.055  1.00 6.45   ? 208 THR A CA  1 
ATOM   1685 C  C   . THR A 1 207 ? -10.748 3.348   25.223  1.00 5.82   ? 208 THR A C   1 
ATOM   1686 O  O   . THR A 1 207 ? -11.436 3.554   24.200  1.00 6.55   ? 208 THR A O   1 
ATOM   1687 C  CB  . THR A 1 207 ? -11.413 5.392   26.519  1.00 7.33   ? 208 THR A CB  1 
ATOM   1688 O  OG1 . THR A 1 207 ? -10.912 6.528   27.238  1.00 7.94   ? 208 THR A OG1 1 
ATOM   1689 C  CG2 . THR A 1 207 ? -12.352 4.593   27.390  1.00 8.63   ? 208 THR A CG2 1 
ATOM   1690 N  N   . TRP A 1 208 ? -10.396 2.141   25.626  1.00 5.75   ? 209 TRP A N   1 
ATOM   1691 C  CA  . TRP A 1 208 ? -10.849 0.945   24.917  1.00 5.76   ? 209 TRP A CA  1 
ATOM   1692 C  C   . TRP A 1 208 ? -12.218 0.531   25.441  1.00 5.50   ? 209 TRP A C   1 
ATOM   1693 O  O   . TRP A 1 208 ? -12.434 0.467   26.660  1.00 6.21   ? 209 TRP A O   1 
ATOM   1694 C  CB  . TRP A 1 208 ? -9.831  -0.212  25.135  1.00 5.76   ? 209 TRP A CB  1 
ATOM   1695 C  CG  . TRP A 1 208 ? -8.709  -0.106  24.172  1.00 5.73   ? 209 TRP A CG  1 
ATOM   1696 C  CD1 . TRP A 1 208 ? -7.481  0.495   24.325  1.00 6.16   ? 209 TRP A CD1 1 
ATOM   1697 C  CD2 . TRP A 1 208 ? -8.781  -0.513  22.809  1.00 5.62   ? 209 TRP A CD2 1 
ATOM   1698 N  NE1 . TRP A 1 208 ? -6.809  0.493   23.161  1.00 6.33   ? 209 TRP A NE1 1 
ATOM   1699 C  CE2 . TRP A 1 208 ? -7.544  -0.124  22.202  1.00 5.86   ? 209 TRP A CE2 1 
ATOM   1700 C  CE3 . TRP A 1 208 ? -9.744  -1.168  22.015  1.00 5.50   ? 209 TRP A CE3 1 
ATOM   1701 C  CZ2 . TRP A 1 208 ? -7.276  -0.360  20.840  1.00 6.49   ? 209 TRP A CZ2 1 
ATOM   1702 C  CZ3 . TRP A 1 208 ? -9.468  -1.439  20.716  1.00 6.69   ? 209 TRP A CZ3 1 
ATOM   1703 C  CH2 . TRP A 1 208 ? -8.252  -1.010  20.119  1.00 6.77   ? 209 TRP A CH2 1 
ATOM   1704 N  N   . ILE A 1 209 ? -13.098 0.161   24.512  1.00 5.56   ? 210 ILE A N   1 
ATOM   1705 C  CA  . ILE A 1 209 ? -14.440 -0.352  24.799  1.00 5.93   ? 210 ILE A CA  1 
ATOM   1706 C  C   . ILE A 1 209 ? -14.549 -1.616  23.978  1.00 5.53   ? 210 ILE A C   1 
ATOM   1707 O  O   . ILE A 1 209 ? -14.671 -1.535  22.741  1.00 6.71   ? 210 ILE A O   1 
ATOM   1708 C  CB  . ILE A 1 209 ? -15.497 0.682   24.467  1.00 6.78   ? 210 ILE A CB  1 
ATOM   1709 C  CG1 . ILE A 1 209 ? -15.282 1.963   25.295  1.00 8.15   ? 210 ILE A CG1 1 
ATOM   1710 C  CG2 . ILE A 1 209 ? -16.881 0.108   24.687  1.00 8.37   ? 210 ILE A CG2 1 
ATOM   1711 C  CD1 . ILE A 1 209 ? -16.098 3.150   24.831  1.00 9.85   ? 210 ILE A CD1 1 
ATOM   1712 N  N   . VAL A 1 210 ? -14.473 -2.790  24.621  1.00 5.80   ? 211 VAL A N   1 
ATOM   1713 C  CA  . VAL A 1 210 ? -14.433 -4.069  23.903  1.00 5.53   ? 211 VAL A CA  1 
ATOM   1714 C  C   . VAL A 1 210 ? -15.748 -4.750  24.163  1.00 5.98   ? 211 VAL A C   1 
ATOM   1715 O  O   . VAL A 1 210 ? -16.093 -5.051  25.306  1.00 6.82   ? 211 VAL A O   1 
ATOM   1716 C  CB  . VAL A 1 210 ? -13.211 -4.912  24.379  1.00 6.57   ? 211 VAL A CB  1 
ATOM   1717 C  CG1 . VAL A 1 210 ? -13.241 -6.271  23.653  1.00 7.60   ? 211 VAL A CG1 1 
ATOM   1718 C  CG2 . VAL A 1 210 ? -11.906 -4.172  24.075  1.00 7.48   ? 211 VAL A CG2 1 
ATOM   1719 N  N   . LEU A 1 211 ? -16.514 -5.030  23.108  1.00 6.49   ? 212 LEU A N   1 
ATOM   1720 C  CA  . LEU A 1 211 ? -17.807 -5.709  23.272  1.00 6.62   ? 212 LEU A CA  1 
ATOM   1721 C  C   . LEU A 1 211 ? -17.610 -7.171  23.625  1.00 6.52   ? 212 LEU A C   1 
ATOM   1722 O  O   . LEU A 1 211 ? -16.753 -7.876  23.104  1.00 7.49   ? 212 LEU A O   1 
ATOM   1723 C  CB  . LEU A 1 211 ? -18.632 -5.558  22.011  1.00 7.70   ? 212 LEU A CB  1 
ATOM   1724 C  CG  . LEU A 1 211 ? -19.017 -4.141  21.589  1.00 8.33   ? 212 LEU A CG  1 
ATOM   1725 C  CD1 . LEU A 1 211 ? -20.017 -4.191  20.419  1.00 11.35  ? 212 LEU A CD1 1 
ATOM   1726 C  CD2 . LEU A 1 211 ? -19.526 -3.311  22.734  1.00 9.68   ? 212 LEU A CD2 1 
ATOM   1727 N  N   A LYS A 1 212 ? -18.517 -7.525  24.549  0.50 8.06   ? 213 LYS A N   1 
ATOM   1728 N  N   B LYS A 1 212 ? -18.474 -7.712  24.510  0.50 7.42   ? 213 LYS A N   1 
ATOM   1729 C  CA  A LYS A 1 212 ? -18.519 -8.910  25.004  0.50 8.41   ? 213 LYS A CA  1 
ATOM   1730 C  CA  B LYS A 1 212 ? -18.372 -9.185  24.844  0.50 7.34   ? 213 LYS A CA  1 
ATOM   1731 C  C   A LYS A 1 212 ? -18.972 -9.867  23.923  0.50 7.33   ? 213 LYS A C   1 
ATOM   1732 C  C   B LYS A 1 212 ? -18.857 -10.021 23.730  0.50 7.17   ? 213 LYS A C   1 
ATOM   1733 O  O   A LYS A 1 212 ? -18.456 -10.973 23.957  0.50 9.01   ? 213 LYS A O   1 
ATOM   1734 O  O   B LYS A 1 212 ? -18.318 -11.138 23.492  0.50 7.26   ? 213 LYS A O   1 
ATOM   1735 C  CB  A LYS A 1 212 ? -19.348 -9.064  26.238  0.50 9.61   ? 213 LYS A CB  1 
ATOM   1736 C  CB  B LYS A 1 212 ? -19.127 -9.462  26.118  0.50 7.71   ? 213 LYS A CB  1 
ATOM   1737 C  CG  A LYS A 1 212 ? -19.375 -10.513 26.745  0.50 11.56  ? 213 LYS A CG  1 
ATOM   1738 C  CG  B LYS A 1 212 ? -19.395 -10.971 26.420  0.50 12.14  ? 213 LYS A CG  1 
ATOM   1739 C  CD  A LYS A 1 212 ? -20.479 -10.841 27.822  0.50 16.06  ? 213 LYS A CD  1 
ATOM   1740 C  CD  B LYS A 1 212 ? -19.632 -11.036 27.940  0.50 14.05  ? 213 LYS A CD  1 
ATOM   1741 C  CE  A LYS A 1 212 ? -21.520 -9.746  27.744  0.50 21.21  ? 213 LYS A CE  1 
ATOM   1742 C  CE  B LYS A 1 212 ? -20.244 -12.360 28.319  0.50 19.92  ? 213 LYS A CE  1 
ATOM   1743 N  NZ  A LYS A 1 212 ? -22.717 -9.741  28.670  0.50 34.46  ? 213 LYS A NZ  1 
ATOM   1744 N  NZ  B LYS A 1 212 ? -20.429 -12.766 29.723  0.50 31.47  ? 213 LYS A NZ  1 
ATOM   1745 N  N   A GLU A 1 213 ? -19.978 -9.578  23.079  0.50 7.72   ? 214 GLU A N   1 
ATOM   1746 N  N   B GLU A 1 213 ? -19.902 -9.600  23.059  0.50 7.87   ? 214 GLU A N   1 
ATOM   1747 C  CA  A GLU A 1 213 ? -20.599 -10.469 22.060  0.50 7.97   ? 214 GLU A CA  1 
ATOM   1748 C  CA  B GLU A 1 213 ? -20.524 -10.461 22.049  0.50 8.21   ? 214 GLU A CA  1 
ATOM   1749 C  C   A GLU A 1 213 ? -19.817 -10.350 20.774  0.50 7.25   ? 214 GLU A C   1 
ATOM   1750 C  C   B GLU A 1 213 ? -19.747 -10.345 20.776  0.50 7.45   ? 214 GLU A C   1 
ATOM   1751 O  O   A GLU A 1 213 ? -19.763 -9.257  20.220  0.50 7.57   ? 214 GLU A O   1 
ATOM   1752 O  O   B GLU A 1 213 ? -19.677 -9.259  20.218  0.50 7.95   ? 214 GLU A O   1 
ATOM   1753 C  CB  A GLU A 1 213 ? -22.044 -10.103 21.849  0.50 8.93   ? 214 GLU A CB  1 
ATOM   1754 C  CB  B GLU A 1 213 ? -21.962 -10.110 21.842  0.50 9.07   ? 214 GLU A CB  1 
ATOM   1755 C  CG  A GLU A 1 213 ? -22.716 -11.046 20.883  0.50 11.95  ? 214 GLU A CG  1 
ATOM   1756 C  CG  B GLU A 1 213 ? -22.727 -11.020 20.871  0.50 12.64  ? 214 GLU A CG  1 
ATOM   1757 C  CD  A GLU A 1 213 ? -24.191 -10.859 20.765  0.50 12.34  ? 214 GLU A CD  1 
ATOM   1758 C  CD  B GLU A 1 213 ? -24.210 -10.560 20.714  0.50 15.67  ? 214 GLU A CD  1 
ATOM   1759 O  OE1 A GLU A 1 213 ? -24.773 -9.918  21.333  0.50 10.73  ? 214 GLU A OE1 1 
ATOM   1760 O  OE1 B GLU A 1 213 ? -24.783 -10.482 19.553  0.50 16.74  ? 214 GLU A OE1 1 
ATOM   1761 O  OE2 A GLU A 1 213 ? -24.729 -11.839 20.158  0.50 21.22  ? 214 GLU A OE2 1 
ATOM   1762 O  OE2 B GLU A 1 213 ? -24.854 -10.212 21.733  0.50 30.39  ? 214 GLU A OE2 1 
ATOM   1763 N  N   . PRO A 1 214 ? -19.234 -11.467 20.264  1.00 7.90   ? 215 PRO A N   1 
ATOM   1764 C  CA  . PRO A 1 214 ? -18.599 -11.420 18.951  1.00 7.80   ? 215 PRO A CA  1 
ATOM   1765 C  C   . PRO A 1 214 ? -19.584 -11.344 17.838  1.00 8.15   ? 215 PRO A C   1 
ATOM   1766 O  O   . PRO A 1 214 ? -20.773 -11.748 18.035  1.00 10.53  ? 215 PRO A O   1 
ATOM   1767 C  CB  . PRO A 1 214 ? -17.837 -12.731 18.848  1.00 8.64   ? 215 PRO A CB  1 
ATOM   1768 C  CG  . PRO A 1 214 ? -18.719 -13.701 19.679  1.00 13.26  ? 215 PRO A CG  1 
ATOM   1769 C  CD  . PRO A 1 214 ? -19.223 -12.810 20.859  1.00 9.48   ? 215 PRO A CD  1 
ATOM   1770 N  N   . ILE A 1 215 ? -19.176 -10.908 16.670  1.00 8.07   ? 216 ILE A N   1 
ATOM   1771 C  CA  . ILE A 1 215 ? -19.959 -11.152 15.460  1.00 8.36   ? 216 ILE A CA  1 
ATOM   1772 C  C   . ILE A 1 215 ? -19.458 -12.388 14.768  1.00 8.45   ? 216 ILE A C   1 
ATOM   1773 O  O   . ILE A 1 215 ? -18.276 -12.757 14.924  1.00 9.39   ? 216 ILE A O   1 
ATOM   1774 C  CB  . ILE A 1 215 ? -19.954 -9.936  14.539  1.00 9.44   ? 216 ILE A CB  1 
ATOM   1775 C  CG1 . ILE A 1 215 ? -18.577 -9.562  14.010  1.00 10.24  ? 216 ILE A CG1 1 
ATOM   1776 C  CG2 . ILE A 1 215 ? -20.653 -8.758  15.186  1.00 11.40  ? 216 ILE A CG2 1 
ATOM   1777 C  CD1 . ILE A 1 215 ? -18.541 -8.569  12.828  1.00 11.93  ? 216 ILE A CD1 1 
ATOM   1778 N  N   . SER A 1 216 ? -20.300 -13.049 14.008  1.00 9.15   ? 217 SER A N   1 
ATOM   1779 C  CA  . SER A 1 216 ? -19.912 -14.173 13.187  1.00 9.31   ? 217 SER A CA  1 
ATOM   1780 C  C   . SER A 1 216 ? -19.696 -13.747 11.775  1.00 8.71   ? 217 SER A C   1 
ATOM   1781 O  O   . SER A 1 216 ? -20.543 -12.998 11.235  1.00 10.56  ? 217 SER A O   1 
ATOM   1782 C  CB  . SER A 1 216 ? -21.018 -15.240 13.240  1.00 13.39  ? 217 SER A CB  1 
ATOM   1783 O  OG  . SER A 1 216 ? -21.105 -15.899 14.436  1.00 16.94  ? 217 SER A OG  1 
ATOM   1784 N  N   . VAL A 1 217 ? -18.619 -14.211 11.174  1.00 8.94   ? 218 VAL A N   1 
ATOM   1785 C  CA  . VAL A 1 217 ? -18.342 -14.011 9.734   1.00 9.09   ? 218 VAL A CA  1 
ATOM   1786 C  C   . VAL A 1 217 ? -18.083 -15.372 9.148   1.00 8.87   ? 218 VAL A C   1 
ATOM   1787 O  O   . VAL A 1 217 ? -17.742 -16.335 9.858   1.00 9.33   ? 218 VAL A O   1 
ATOM   1788 C  CB  . VAL A 1 217 ? -17.110 -13.082 9.503   1.00 9.84   ? 218 VAL A CB  1 
ATOM   1789 C  CG1 . VAL A 1 217 ? -17.371 -11.756 10.206  1.00 10.90  ? 218 VAL A CG1 1 
ATOM   1790 C  CG2 . VAL A 1 217 ? -15.876 -13.720 10.012  1.00 11.99  ? 218 VAL A CG2 1 
ATOM   1791 N  N   . SER A 1 218 ? -18.280 -15.519 7.841   1.00 9.39   ? 219 SER A N   1 
ATOM   1792 C  CA  . SER A 1 218 ? -18.055 -16.854 7.263   1.00 9.80   ? 219 SER A CA  1 
ATOM   1793 C  C   . SER A 1 218 ? -16.600 -17.135 6.997   1.00 9.54   ? 219 SER A C   1 
ATOM   1794 O  O   . SER A 1 218 ? -15.760 -16.209 6.832   1.00 10.06  ? 219 SER A O   1 
ATOM   1795 C  CB  . SER A 1 218 ? -18.887 -17.018 5.996   1.00 10.46  ? 219 SER A CB  1 
ATOM   1796 O  OG  . SER A 1 218 ? -18.416 -16.154 5.028   1.00 12.00  ? 219 SER A OG  1 
ATOM   1797 N  N   A SER A 1 219 ? -16.284 -18.406 6.811   0.50 9.94   ? 220 SER A N   1 
ATOM   1798 N  N   B SER A 1 219 ? -16.297 -18.387 6.789   0.50 10.34  ? 220 SER A N   1 
ATOM   1799 C  CA  A SER A 1 219 ? -14.957 -18.790 6.379   0.50 11.26  ? 220 SER A CA  1 
ATOM   1800 C  CA  B SER A 1 219 ? -14.973 -18.756 6.436   0.50 12.16  ? 220 SER A CA  1 
ATOM   1801 C  C   A SER A 1 219 ? -14.593 -18.071 5.100   0.50 11.75  ? 220 SER A C   1 
ATOM   1802 C  C   B SER A 1 219 ? -14.582 -18.127 5.067   0.50 11.64  ? 220 SER A C   1 
ATOM   1803 O  O   A SER A 1 219 ? -13.496 -17.584 4.986   0.50 12.59  ? 220 SER A O   1 
ATOM   1804 O  O   B SER A 1 219 ? -13.478 -17.689 4.875   0.50 13.28  ? 220 SER A O   1 
ATOM   1805 C  CB  A SER A 1 219 ? -14.836 -20.307 6.268   0.50 11.96  ? 220 SER A CB  1 
ATOM   1806 C  CB  B SER A 1 219 ? -14.876 -20.261 6.578   0.50 13.46  ? 220 SER A CB  1 
ATOM   1807 O  OG  A SER A 1 219 ? -15.796 -20.842 5.380   0.50 11.98  ? 220 SER A OG  1 
ATOM   1808 O  OG  B SER A 1 219 ? -13.596 -20.648 6.205   0.50 15.67  ? 220 SER A OG  1 
ATOM   1809 N  N   . GLU A 1 220 ? -15.535 -17.990 4.161   1.00 11.05  ? 221 GLU A N   1 
ATOM   1810 C  CA  . GLU A 1 220 ? -15.275 -17.353 2.882   1.00 12.99  ? 221 GLU A CA  1 
ATOM   1811 C  C   . GLU A 1 220 ? -14.943 -15.899 3.054   1.00 12.21  ? 221 GLU A C   1 
ATOM   1812 O  O   . GLU A 1 220 ? -14.090 -15.331 2.345   1.00 13.14  ? 221 GLU A O   1 
ATOM   1813 C  CB  . GLU A 1 220 ? -16.429 -17.494 1.986   1.00 16.42  ? 221 GLU A CB  1 
ATOM   1814 C  CG  . GLU A 1 220 ? -16.645 -19.009 1.520   1.00 21.27  ? 221 GLU A CG  1 
ATOM   1815 C  CD  . GLU A 1 220 ? -17.577 -19.753 2.414   1.00 19.69  ? 221 GLU A CD  1 
ATOM   1816 O  OE1 . GLU A 1 220 ? -18.005 -19.284 3.465   1.00 19.71  ? 221 GLU A OE1 1 
ATOM   1817 O  OE2 . GLU A 1 220 ? -17.939 -20.833 2.043   1.00 33.17  ? 221 GLU A OE2 1 
ATOM   1818 N  N   . GLN A 1 221 ? -15.638 -15.201 3.955   1.00 11.24  ? 222 GLN A N   1 
ATOM   1819 C  CA  . GLN A 1 221 ? -15.365 -13.777 4.197   1.00 11.25  ? 222 GLN A CA  1 
ATOM   1820 C  C   . GLN A 1 221 ? -13.912 -13.580 4.772   1.00 10.54  ? 222 GLN A C   1 
ATOM   1821 O  O   . GLN A 1 221 ? -13.150 -12.741 4.251   1.00 11.98  ? 222 GLN A O   1 
ATOM   1822 C  CB  . GLN A 1 221 ? -16.389 -13.197 5.141   1.00 10.92  ? 222 GLN A CB  1 
ATOM   1823 C  CG  . GLN A 1 221 ? -17.737 -13.051 4.459   1.00 11.05  ? 222 GLN A CG  1 
ATOM   1824 C  CD  . GLN A 1 221 ? -18.854 -12.499 5.319   1.00 10.53  ? 222 GLN A CD  1 
ATOM   1825 O  OE1 . GLN A 1 221 ? -18.984 -12.874 6.519   1.00 10.58  ? 222 GLN A OE1 1 
ATOM   1826 N  NE2 . GLN A 1 221 ? -19.677 -11.646 4.753   1.00 11.45  ? 222 GLN A NE2 1 
ATOM   1827 N  N   A VAL A 1 222 ? -13.494 -14.342 5.750   0.50 10.51  ? 223 VAL A N   1 
ATOM   1828 N  N   B VAL A 1 222 ? -13.557 -14.331 5.802   0.50 11.42  ? 223 VAL A N   1 
ATOM   1829 C  CA  A VAL A 1 222 ? -12.167 -14.132 6.333   0.50 10.94  ? 223 VAL A CA  1 
ATOM   1830 C  CA  B VAL A 1 222 ? -12.193 -14.220 6.337   0.50 11.70  ? 223 VAL A CA  1 
ATOM   1831 C  C   A VAL A 1 222 ? -11.037 -14.673 5.359   0.50 11.05  ? 223 VAL A C   1 
ATOM   1832 C  C   B VAL A 1 222 ? -11.134 -14.611 5.304   0.50 11.46  ? 223 VAL A C   1 
ATOM   1833 O  O   A VAL A 1 222 ? -9.885  -14.130 5.337   0.50 11.94  ? 223 VAL A O   1 
ATOM   1834 O  O   B VAL A 1 222 ? -10.125 -13.908 5.224   0.50 12.21  ? 223 VAL A O   1 
ATOM   1835 C  CB  A VAL A 1 222 ? -12.134 -14.694 7.766   0.50 11.03  ? 223 VAL A CB  1 
ATOM   1836 C  CB  B VAL A 1 222 ? -11.939 -14.966 7.653   0.50 14.89  ? 223 VAL A CB  1 
ATOM   1837 C  CG1 A VAL A 1 222 ? -12.082 -16.232 7.693   0.50 10.64  ? 223 VAL A CG1 1 
ATOM   1838 C  CG1 B VAL A 1 222 ? -10.597 -14.515 8.228   0.50 15.48  ? 223 VAL A CG1 1 
ATOM   1839 C  CG2 A VAL A 1 222 ? -11.027 -14.052 8.612   0.50 12.55  ? 223 VAL A CG2 1 
ATOM   1840 C  CG2 B VAL A 1 222 ? -12.935 -14.537 8.647   0.50 16.58  ? 223 VAL A CG2 1 
ATOM   1841 N  N   . LEU A 1 223 ? -11.376 -15.635 4.509   1.00 12.19  ? 224 LEU A N   1 
ATOM   1842 C  CA  . LEU A 1 223 ? -10.453 -16.035 3.505   1.00 13.61  ? 224 LEU A CA  1 
ATOM   1843 C  C   . LEU A 1 223 ? -10.185 -14.871 2.523   1.00 13.04  ? 224 LEU A C   1 
ATOM   1844 O  O   . LEU A 1 223 ? -9.009  -14.782 2.096   1.00 15.04  ? 224 LEU A O   1 
ATOM   1845 C  CB  . LEU A 1 223 ? -10.947 -17.260 2.789   1.00 15.59  ? 224 LEU A CB  1 
ATOM   1846 C  CG  . LEU A 1 223 ? -10.763 -18.562 3.657   1.00 23.49  ? 224 LEU A CG  1 
ATOM   1847 C  CD1 . LEU A 1 223 ? -11.650 -19.689 3.125   1.00 24.06  ? 224 LEU A CD1 1 
ATOM   1848 C  CD2 . LEU A 1 223 ? -9.275  -19.065 3.755   1.00 31.02  ? 224 LEU A CD2 1 
ATOM   1849 N  N   . LYS A 1 224 ? -11.146 -14.014 2.246   1.00 13.84  ? 225 LYS A N   1 
ATOM   1850 C  CA  . LYS A 1 224 ? -10.880 -12.882 1.352   1.00 13.77  ? 225 LYS A CA  1 
ATOM   1851 C  C   . LYS A 1 224 ? -10.016 -11.846 2.058   1.00 12.72  ? 225 LYS A C   1 
ATOM   1852 O  O   . LYS A 1 224 ? -9.180  -11.244 1.391   1.00 12.77  ? 225 LYS A O   1 
ATOM   1853 C  CB  . LYS A 1 224 ? -12.212 -12.389 0.786   1.00 16.98  ? 225 LYS A CB  1 
ATOM   1854 C  CG  . LYS A 1 224 ? -12.728 -13.469 -0.267  1.00 20.92  ? 225 LYS A CG  1 
ATOM   1855 C  CD  . LYS A 1 224 ? -14.136 -13.227 -0.833  1.00 22.94  ? 225 LYS A CD  1 
ATOM   1856 C  CE  . LYS A 1 224 ? -14.566 -14.234 -1.936  1.00 27.50  ? 225 LYS A CE  1 
ATOM   1857 N  NZ  . LYS A 1 224 ? -15.883 -13.995 -2.568  1.00 33.00  ? 225 LYS A NZ  1 
ATOM   1858 N  N   . PHE A 1 225 ? -10.044 -11.683 3.385   1.00 11.99  ? 226 PHE A N   1 
ATOM   1859 C  CA  . PHE A 1 225 ? -9.158  -10.780 4.060   1.00 10.87  ? 226 PHE A CA  1 
ATOM   1860 C  C   . PHE A 1 225 ? -7.723  -11.317 3.908   1.00 10.78  ? 226 PHE A C   1 
ATOM   1861 O  O   . PHE A 1 225 ? -6.783  -10.559 3.675   1.00 11.41  ? 226 PHE A O   1 
ATOM   1862 C  CB  . PHE A 1 225 ? -9.365  -10.802 5.611   1.00 11.28  ? 226 PHE A CB  1 
ATOM   1863 C  CG  . PHE A 1 225 ? -10.564 -10.044 6.151   1.00 11.29  ? 226 PHE A CG  1 
ATOM   1864 C  CD1 . PHE A 1 225 ? -11.603 -9.585  5.351   1.00 17.18  ? 226 PHE A CD1 1 
ATOM   1865 C  CD2 . PHE A 1 225 ? -10.640 -9.819  7.521   1.00 15.82  ? 226 PHE A CD2 1 
ATOM   1866 C  CE1 . PHE A 1 225 ? -12.667 -8.881  5.916   1.00 18.83  ? 226 PHE A CE1 1 
ATOM   1867 C  CE2 . PHE A 1 225 ? -11.686 -9.122  8.086   1.00 16.86  ? 226 PHE A CE2 1 
ATOM   1868 C  CZ  . PHE A 1 225 ? -12.695 -8.641  7.289   1.00 14.96  ? 226 PHE A CZ  1 
ATOM   1869 N  N   . ARG A 1 226 ? -7.572  -12.662 3.934   1.00 10.32  ? 227 ARG A N   1 
ATOM   1870 C  CA  . ARG A 1 226 ? -6.284  -13.239 3.880   1.00 11.34  ? 227 ARG A CA  1 
ATOM   1871 C  C   . ARG A 1 226 ? -5.678  -13.291 2.456   1.00 12.19  ? 227 ARG A C   1 
ATOM   1872 O  O   . ARG A 1 226 ? -4.500  -13.691 2.338   1.00 13.32  ? 227 ARG A O   1 
ATOM   1873 C  CB  . ARG A 1 226 ? -6.319  -14.733 4.420   1.00 11.98  ? 227 ARG A CB  1 
ATOM   1874 C  CG  . ARG A 1 226 ? -6.748  -14.831 5.871   1.00 11.42  ? 227 ARG A CG  1 
ATOM   1875 C  CD  . ARG A 1 226 ? -6.730  -16.279 6.337   1.00 14.00  ? 227 ARG A CD  1 
ATOM   1876 N  NE  . ARG A 1 226 ? -7.246  -16.426 7.667   1.00 10.99  ? 227 ARG A NE  1 
ATOM   1877 C  CZ  . ARG A 1 226 ? -8.149  -17.295 8.079   1.00 11.80  ? 227 ARG A CZ  1 
ATOM   1878 N  NH1 . ARG A 1 226 ? -8.593  -18.238 7.261   1.00 15.49  ? 227 ARG A NH1 1 
ATOM   1879 N  NH2 . ARG A 1 226 ? -8.673  -17.219 9.280   1.00 13.38  ? 227 ARG A NH2 1 
ATOM   1880 N  N   . LYS A 1 227 ? -6.376  -12.815 1.439   1.00 10.80  ? 228 LYS A N   1 
ATOM   1881 C  CA  . LYS A 1 227 ? -5.820  -12.687 0.088   1.00 12.56  ? 228 LYS A CA  1 
ATOM   1882 C  C   . LYS A 1 227 ? -5.162  -11.319 -0.099  1.00 12.35  ? 228 LYS A C   1 
ATOM   1883 O  O   . LYS A 1 227 ? -4.521  -11.121 -1.126  1.00 15.16  ? 228 LYS A O   1 
ATOM   1884 C  CB  . LYS A 1 227 ? -6.951  -12.897 -0.934  1.00 15.60  ? 228 LYS A CB  1 
ATOM   1885 C  CG  . LYS A 1 227 ? -7.440  -14.285 -1.027  1.00 18.01  ? 228 LYS A CG  1 
ATOM   1886 C  CD  . LYS A 1 227 ? -8.544  -14.471 -2.063  1.00 26.82  ? 228 LYS A CD  1 
ATOM   1887 N  N   . LEU A 1 228 ? -5.388  -10.365 0.794   1.00 12.60  ? 229 LEU A N   1 
ATOM   1888 C  CA  . LEU A 1 228 ? -4.819  -9.083  0.692   1.00 12.25  ? 229 LEU A CA  1 
ATOM   1889 C  C   . LEU A 1 228 ? -3.353  -9.223  0.831   1.00 12.41  ? 229 LEU A C   1 
ATOM   1890 O  O   . LEU A 1 228 ? -2.749  -10.294 1.256   1.00 12.36  ? 229 LEU A O   1 
ATOM   1891 C  CB  . LEU A 1 228 ? -5.374  -8.141  1.794   1.00 12.90  ? 229 LEU A CB  1 
ATOM   1892 C  CG  . LEU A 1 228 ? -6.847  -7.689  1.562   1.00 13.17  ? 229 LEU A CG  1 
ATOM   1893 C  CD1 . LEU A 1 228 ? -7.241  -7.067  2.891   1.00 13.90  ? 229 LEU A CD1 1 
ATOM   1894 C  CD2 . LEU A 1 228 ? -6.867  -6.619  0.442   1.00 15.14  ? 229 LEU A CD2 1 
ATOM   1895 N  N   . ASN A 1 229 ? -2.639  -8.189  0.426   1.00 12.81  ? 230 ASN A N   1 
ATOM   1896 C  CA  . ASN A 1 229 ? -1.221  -8.212  0.454   1.00 12.68  ? 230 ASN A CA  1 
ATOM   1897 C  C   . ASN A 1 229 ? -0.675  -6.959  1.231   1.00 13.94  ? 230 ASN A C   1 
ATOM   1898 O  O   . ASN A 1 229 ? -1.152  -5.892  1.226   1.00 15.49  ? 230 ASN A O   1 
ATOM   1899 C  CB  . ASN A 1 229 ? -0.603  -7.987  -1.002  1.00 15.09  ? 230 ASN A CB  1 
ATOM   1900 C  CG  . ASN A 1 229 ? -0.580  -9.226  -1.896  1.00 17.29  ? 230 ASN A CG  1 
ATOM   1901 O  OD1 . ASN A 1 229 ? 0.033   -9.109  -2.969  1.00 20.20  ? 230 ASN A OD1 1 
ATOM   1902 N  ND2 . ASN A 1 229 ? -1.217  -10.322 -1.534  1.00 16.18  ? 230 ASN A ND2 1 
ATOM   1903 N  N   . PHE A 1 230 ? 0.368   -7.333  1.951   1.00 12.61  ? 231 PHE A N   1 
ATOM   1904 C  CA  . PHE A 1 230 ? 1.161   -6.264  2.645   1.00 13.36  ? 231 PHE A CA  1 
ATOM   1905 C  C   . PHE A 1 230 ? 2.084   -5.531  1.722   1.00 17.30  ? 231 PHE A C   1 
ATOM   1906 O  O   . PHE A 1 230 ? 2.367   -4.351  1.999   1.00 17.37  ? 231 PHE A O   1 
ATOM   1907 C  CB  . PHE A 1 230 ? 2.143   -6.864  3.659   1.00 13.95  ? 231 PHE A CB  1 
ATOM   1908 C  CG  . PHE A 1 230 ? 1.586   -7.443  4.953   1.00 13.73  ? 231 PHE A CG  1 
ATOM   1909 C  CD1 . PHE A 1 230 ? 0.838   -6.651  5.847   1.00 14.62  ? 231 PHE A CD1 1 
ATOM   1910 C  CD2 . PHE A 1 230 ? 1.980   -8.678  5.406   1.00 14.13  ? 231 PHE A CD2 1 
ATOM   1911 C  CE1 . PHE A 1 230 ? 0.366   -7.127  7.043   1.00 15.49  ? 231 PHE A CE1 1 
ATOM   1912 C  CE2 . PHE A 1 230 ? 1.508   -9.223  6.614   1.00 15.30  ? 231 PHE A CE2 1 
ATOM   1913 C  CZ  . PHE A 1 230 ? 0.752   -8.391  7.472   1.00 14.19  ? 231 PHE A CZ  1 
ATOM   1914 N  N   . ASN A 1 231 ? 2.501   -6.167  0.644   1.00 17.44  ? 232 ASN A N   1 
ATOM   1915 C  CA  . ASN A 1 231 ? 3.334   -5.500  -0.330  1.00 14.55  ? 232 ASN A CA  1 
ATOM   1916 C  C   . ASN A 1 231 ? 2.504   -4.677  -1.334  1.00 13.83  ? 232 ASN A C   1 
ATOM   1917 O  O   . ASN A 1 231 ? 1.269   -4.765  -1.405  1.00 17.31  ? 232 ASN A O   1 
ATOM   1918 C  CB  . ASN A 1 231 ? 4.149   -6.550  -1.077  1.00 18.12  ? 232 ASN A CB  1 
ATOM   1919 C  CG  . ASN A 1 231 ? 3.289   -7.652  -1.638  1.00 19.56  ? 232 ASN A CG  1 
ATOM   1920 O  OD1 . ASN A 1 231 ? 2.818   -8.532  -0.907  1.00 23.18  ? 232 ASN A OD1 1 
ATOM   1921 N  ND2 . ASN A 1 231 ? 3.030   -7.611  -2.943  1.00 22.70  ? 232 ASN A ND2 1 
ATOM   1922 N  N   . GLY A 1 232 ? 3.331   -3.724  -2.086  1.00 16.66  ? 233 GLY A N   1 
ATOM   1923 C  CA  . GLY A 1 232 ? 2.716   -2.928  -3.143  1.00 15.91  ? 233 GLY A CA  1 
ATOM   1924 C  C   . GLY A 1 232 ? 2.796   -3.695  -4.454  1.00 14.88  ? 233 GLY A C   1 
ATOM   1925 O  O   . GLY A 1 232 ? 3.429   -4.776  -4.439  1.00 20.91  ? 233 GLY A O   1 
ATOM   1926 N  N   . GLU A 1 233 ? 2.059   -3.156  -5.393  1.00 15.80  ? 234 GLU A N   1 
ATOM   1927 C  CA  . GLU A 1 233 ? 1.973   -3.754  -6.727  1.00 14.88  ? 234 GLU A CA  1 
ATOM   1928 C  C   . GLU A 1 233 ? 3.316   -3.881  -7.358  1.00 18.17  ? 234 GLU A C   1 
ATOM   1929 O  O   . GLU A 1 233 ? 4.171   -3.016  -7.175  1.00 20.29  ? 234 GLU A O   1 
ATOM   1930 C  CB  . GLU A 1 233 ? 1.068   -2.914  -7.613  1.00 17.31  ? 234 GLU A CB  1 
ATOM   1931 C  CG  . GLU A 1 233 ? 0.871   -3.411  -9.019  1.00 19.72  ? 234 GLU A CG  1 
ATOM   1932 C  CD  . GLU A 1 233 ? 0.084   -2.437  -9.844  1.00 27.86  ? 234 GLU A CD  1 
ATOM   1933 O  OE1 . GLU A 1 233 ? -0.281  -1.346  -9.342  1.00 29.25  ? 234 GLU A OE1 1 
ATOM   1934 O  OE2 . GLU A 1 233 ? -0.176  -2.768  -11.018 1.00 31.28  ? 234 GLU A OE2 1 
ATOM   1935 N  N   . GLY A 1 234 ? 3.593   -5.066  -7.950  1.00 23.92  ? 235 GLY A N   1 
ATOM   1936 C  CA  . GLY A 1 234 ? 4.862   -5.235  -8.606  1.00 23.92  ? 235 GLY A CA  1 
ATOM   1937 C  C   . GLY A 1 234 ? 5.978   -5.656  -7.685  1.00 22.11  ? 235 GLY A C   1 
ATOM   1938 O  O   . GLY A 1 234 ? 7.165   -5.783  -8.048  1.00 34.81  ? 235 GLY A O   1 
ATOM   1939 N  N   . GLU A 1 235 ? 5.563   -5.941  -6.449  1.00 21.16  ? 236 GLU A N   1 
ATOM   1940 C  CA  . GLU A 1 235 ? 6.561   -6.510  -5.526  1.00 17.09  ? 236 GLU A CA  1 
ATOM   1941 C  C   . GLU A 1 235 ? 6.085   -7.946  -5.076  1.00 20.71  ? 236 GLU A C   1 
ATOM   1942 O  O   . GLU A 1 235 ? 4.929   -8.346  -5.367  1.00 22.66  ? 236 GLU A O   1 
ATOM   1943 C  CB  . GLU A 1 235 ? 6.516   -5.768  -4.183  1.00 24.13  ? 236 GLU A CB  1 
ATOM   1944 C  CG  . GLU A 1 235 ? 7.017   -4.338  -4.268  1.00 23.93  ? 236 GLU A CG  1 
ATOM   1945 C  CD  . GLU A 1 235 ? 6.795   -3.485  -3.046  1.00 31.73  ? 236 GLU A CD  1 
ATOM   1946 O  OE1 . GLU A 1 235 ? 6.076   -3.849  -2.104  1.00 25.22  ? 236 GLU A OE1 1 
ATOM   1947 O  OE2 . GLU A 1 235 ? 7.393   -2.407  -3.024  1.00 36.60  ? 236 GLU A OE2 1 
ATOM   1948 N  N   . PRO A 1 236 ? 7.023   -8.772  -4.569  1.00 18.75  ? 237 PRO A N   1 
ATOM   1949 C  CA  . PRO A 1 236 ? 6.809   -10.190 -4.207  1.00 24.45  ? 237 PRO A CA  1 
ATOM   1950 C  C   . PRO A 1 236 ? 5.705   -10.356 -3.227  1.00 25.95  ? 237 PRO A C   1 
ATOM   1951 O  O   . PRO A 1 236 ? 5.785   -9.667  -2.207  1.00 28.46  ? 237 PRO A O   1 
ATOM   1952 C  CB  . PRO A 1 236 ? 8.110   -10.611 -3.534  1.00 30.39  ? 237 PRO A CB  1 
ATOM   1953 C  CG  . PRO A 1 236 ? 9.064   -9.508  -3.748  1.00 38.38  ? 237 PRO A CG  1 
ATOM   1954 C  CD  . PRO A 1 236 ? 8.319   -8.266  -4.099  1.00 28.66  ? 237 PRO A CD  1 
ATOM   1955 N  N   . GLU A 1 237 ? 4.882   -11.393 -3.354  1.00 22.43  ? 238 GLU A N   1 
ATOM   1956 C  CA  . GLU A 1 237 ? 3.781   -11.478 -2.517  1.00 21.06  ? 238 GLU A CA  1 
ATOM   1957 C  C   . GLU A 1 237 ? 3.968   -11.834 -1.113  1.00 19.96  ? 238 GLU A C   1 
ATOM   1958 O  O   . GLU A 1 237 ? 4.532   -12.818 -0.833  1.00 17.46  ? 238 GLU A O   1 
ATOM   1959 C  CB  . GLU A 1 237 ? 2.766   -12.442 -3.144  1.00 18.56  ? 238 GLU A CB  1 
ATOM   1960 C  CG  . GLU A 1 237 ? 1.426   -12.364 -2.437  1.00 19.91  ? 238 GLU A CG  1 
ATOM   1961 C  CD  . GLU A 1 237 ? 0.302   -13.129 -3.162  1.00 15.29  ? 238 GLU A CD  1 
ATOM   1962 O  OE1 . GLU A 1 237 ? 0.609   -14.255 -3.632  1.00 23.82  ? 238 GLU A OE1 1 
ATOM   1963 O  OE2 . GLU A 1 237 ? -0.846  -12.600 -3.275  1.00 17.33  ? 238 GLU A OE2 1 
ATOM   1964 N  N   . GLU A 1 238 ? 3.416   -11.030 -0.183  1.00 17.25  ? 239 GLU A N   1 
ATOM   1965 C  CA  . GLU A 1 238 ? 3.519   -11.380 1.315   1.00 19.48  ? 239 GLU A CA  1 
ATOM   1966 C  C   . GLU A 1 238 ? 2.017   -11.163 1.688   1.00 13.45  ? 239 GLU A C   1 
ATOM   1967 O  O   . GLU A 1 238 ? 1.522   -10.064 1.766   1.00 18.59  ? 239 GLU A O   1 
ATOM   1968 C  CB  . GLU A 1 238 ? 4.473   -10.573 2.101   1.00 28.15  ? 239 GLU A CB  1 
ATOM   1969 C  CG  . GLU A 1 238 ? 5.957   -11.021 1.884   1.00 37.51  ? 239 GLU A CG  1 
ATOM   1970 C  CD  . GLU A 1 238 ? 7.083   -10.627 2.863   1.00 26.44  ? 239 GLU A CD  1 
ATOM   1971 O  OE1 . GLU A 1 238 ? 7.148   -10.994 4.071   1.00 27.85  ? 239 GLU A OE1 1 
ATOM   1972 O  OE2 . GLU A 1 238 ? 8.028   -9.918  2.419   1.00 36.88  ? 239 GLU A OE2 1 
ATOM   1973 N  N   . LEU A 1 239 ? 1.375   -12.339 1.994   1.00 13.09  ? 240 LEU A N   1 
ATOM   1974 C  CA  . LEU A 1 239 ? -0.042  -12.208 2.300   1.00 11.81  ? 240 LEU A CA  1 
ATOM   1975 C  C   . LEU A 1 239 ? -0.258  -11.366 3.576   1.00 11.55  ? 240 LEU A C   1 
ATOM   1976 O  O   . LEU A 1 239 ? 0.517   -11.610 4.571   1.00 12.77  ? 240 LEU A O   1 
ATOM   1977 C  CB  . LEU A 1 239 ? -0.657  -13.636 2.522   1.00 11.95  ? 240 LEU A CB  1 
ATOM   1978 C  CG  . LEU A 1 239 ? -0.691  -14.513 1.253   1.00 12.10  ? 240 LEU A CG  1 
ATOM   1979 C  CD1 . LEU A 1 239 ? -1.294  -15.829 1.756   1.00 16.82  ? 240 LEU A CD1 1 
ATOM   1980 C  CD2 . LEU A 1 239 ? -1.457  -13.815 0.184   1.00 14.34  ? 240 LEU A CD2 1 
ATOM   1981 N  N   . MET A 1 240 ? -1.280  -10.571 3.583   1.00 12.31  ? 241 MET A N   1 
ATOM   1982 C  CA  . MET A 1 240 ? -1.623  -9.725  4.784   1.00 12.67  ? 241 MET A CA  1 
ATOM   1983 C  C   . MET A 1 240 ? -2.472  -10.666 5.692   1.00 11.51  ? 241 MET A C   1 
ATOM   1984 O  O   . MET A 1 240 ? -3.646  -10.826 5.607   1.00 11.13  ? 241 MET A O   1 
ATOM   1985 C  CB  . MET A 1 240 ? -2.523  -8.568  4.250   1.00 12.56  ? 241 MET A CB  1 
ATOM   1986 C  CG  . MET A 1 240 ? -2.834  -7.539  5.482   1.00 14.25  ? 241 MET A CG  1 
ATOM   1987 S  SD  . MET A 1 240 ? -3.786  -6.185  4.937   1.00 13.76  ? 241 MET A SD  1 
ATOM   1988 C  CE  . MET A 1 240 ? -2.446  -5.107  4.336   1.00 15.08  ? 241 MET A CE  1 
ATOM   1989 N  N   . VAL A 1 241 ? -1.669  -11.292 6.597   1.00 10.88  ? 242 VAL A N   1 
ATOM   1990 C  CA  . VAL A 1 241 ? -2.214  -12.190 7.681   1.00 9.95   ? 242 VAL A CA  1 
ATOM   1991 C  C   . VAL A 1 241 ? -1.377  -11.956 8.956   1.00 9.83   ? 242 VAL A C   1 
ATOM   1992 O  O   . VAL A 1 241 ? -0.227  -11.540 8.860   1.00 10.87  ? 242 VAL A O   1 
ATOM   1993 C  CB  . VAL A 1 241 ? -2.119  -13.669 7.287   1.00 10.54  ? 242 VAL A CB  1 
ATOM   1994 C  CG1 . VAL A 1 241 ? -3.064  -13.982 6.074   1.00 12.11  ? 242 VAL A CG1 1 
ATOM   1995 C  CG2 . VAL A 1 241 ? -0.741  -14.149 7.043   1.00 12.51  ? 242 VAL A CG2 1 
ATOM   1996 N  N   . ASP A 1 242 ? -1.988  -12.260 10.103  1.00 8.92   ? 243 ASP A N   1 
ATOM   1997 C  CA  . ASP A 1 242 ? -1.329  -12.115 11.355  1.00 9.12   ? 243 ASP A CA  1 
ATOM   1998 C  C   . ASP A 1 242 ? -0.850  -10.680 11.589  1.00 8.90   ? 243 ASP A C   1 
ATOM   1999 O  O   . ASP A 1 242 ? 0.288   -10.460 12.083  1.00 10.75  ? 243 ASP A O   1 
ATOM   2000 C  CB  . ASP A 1 242 ? -0.191  -13.200 11.599  1.00 9.59   ? 243 ASP A CB  1 
ATOM   2001 C  CG  . ASP A 1 242 ? -0.809  -14.584 11.714  1.00 10.31  ? 243 ASP A CG  1 
ATOM   2002 O  OD1 . ASP A 1 242 ? -1.877  -14.740 12.353  1.00 9.31   ? 243 ASP A OD1 1 
ATOM   2003 O  OD2 . ASP A 1 242 ? -0.235  -15.506 11.071  1.00 11.43  ? 243 ASP A OD2 1 
ATOM   2004 N  N   . ASN A 1 243 ? -1.733  -9.747  11.322  1.00 8.54   ? 244 ASN A N   1 
ATOM   2005 C  CA  . ASN A 1 243 ? -1.459  -8.308  11.514  1.00 8.79   ? 244 ASN A CA  1 
ATOM   2006 C  C   . ASN A 1 243 ? -1.988  -7.844  12.898  1.00 7.18   ? 244 ASN A C   1 
ATOM   2007 O  O   . ASN A 1 243 ? -2.621  -6.819  13.002  1.00 8.62   ? 244 ASN A O   1 
ATOM   2008 C  CB  . ASN A 1 243 ? -1.996  -7.447  10.389  1.00 9.05   ? 244 ASN A CB  1 
ATOM   2009 C  CG  . ASN A 1 243 ? -3.456  -7.612  10.163  1.00 9.05   ? 244 ASN A CG  1 
ATOM   2010 O  OD1 . ASN A 1 243 ? -4.112  -8.465  10.732  1.00 9.47   ? 244 ASN A OD1 1 
ATOM   2011 N  ND2 . ASN A 1 243 ? -3.987  -6.777  9.304   1.00 13.66  ? 244 ASN A ND2 1 
ATOM   2012 N  N   . TRP A 1 244 ? -1.689  -8.627  13.937  1.00 7.64   ? 245 TRP A N   1 
ATOM   2013 C  CA  . TRP A 1 244 ? -2.107  -8.365  15.295  1.00 7.26   ? 245 TRP A CA  1 
ATOM   2014 C  C   . TRP A 1 244 ? -0.893  -8.269  16.237  1.00 7.43   ? 245 TRP A C   1 
ATOM   2015 O  O   . TRP A 1 244 ? 0.083   -9.008  16.108  1.00 9.19   ? 245 TRP A O   1 
ATOM   2016 C  CB  . TRP A 1 244 ? -3.088  -9.473  15.807  1.00 7.51   ? 245 TRP A CB  1 
ATOM   2017 C  CG  . TRP A 1 244 ? -2.620  -10.873 15.657  1.00 7.44   ? 245 TRP A CG  1 
ATOM   2018 C  CD1 . TRP A 1 244 ? -2.758  -11.629 14.521  1.00 8.31   ? 245 TRP A CD1 1 
ATOM   2019 C  CD2 . TRP A 1 244 ? -2.048  -11.739 16.609  1.00 7.48   ? 245 TRP A CD2 1 
ATOM   2020 N  NE1 . TRP A 1 244 ? -2.222  -12.898 14.694  1.00 8.34   ? 245 TRP A NE1 1 
ATOM   2021 C  CE2 . TRP A 1 244 ? -1.812  -12.991 15.983  1.00 7.74   ? 245 TRP A CE2 1 
ATOM   2022 C  CE3 . TRP A 1 244 ? -1.733  -11.587 17.979  1.00 8.65   ? 245 TRP A CE3 1 
ATOM   2023 C  CZ2 . TRP A 1 244 ? -1.259  -14.049 16.680  1.00 9.55   ? 245 TRP A CZ2 1 
ATOM   2024 C  CZ3 . TRP A 1 244 ? -1.198  -12.637 18.665  1.00 10.20  ? 245 TRP A CZ3 1 
ATOM   2025 C  CH2 . TRP A 1 244 ? -0.912  -13.871 18.002  1.00 10.38  ? 245 TRP A CH2 1 
ATOM   2026 N  N   . ARG A 1 245 ? -1.083  -7.405  17.229  1.00 7.58   ? 246 ARG A N   1 
ATOM   2027 C  CA  . ARG A 1 245 ? -0.099  -7.237  18.254  1.00 7.89   ? 246 ARG A CA  1 
ATOM   2028 C  C   . ARG A 1 245 ? -0.565  -8.133  19.464  1.00 7.20   ? 246 ARG A C   1 
ATOM   2029 O  O   . ARG A 1 245 ? -1.785  -8.148  19.754  1.00 8.25   ? 246 ARG A O   1 
ATOM   2030 C  CB  . ARG A 1 245 ? -0.050  -5.811  18.808  1.00 7.47   ? 246 ARG A CB  1 
ATOM   2031 C  CG  . ARG A 1 245 ? 1.062   -5.566  19.840  1.00 7.88   ? 246 ARG A CG  1 
ATOM   2032 C  CD  . ARG A 1 245 ? 0.989   -4.196  20.461  1.00 7.81   ? 246 ARG A CD  1 
ATOM   2033 N  NE  . ARG A 1 245 ? 2.251   -3.854  21.110  1.00 8.67   ? 246 ARG A NE  1 
ATOM   2034 C  CZ  . ARG A 1 245 ? 2.427   -2.861  21.977  1.00 8.16   ? 246 ARG A CZ  1 
ATOM   2035 N  NH1 . ARG A 1 245 ? 1.414   -2.091  22.364  1.00 8.79   ? 246 ARG A NH1 1 
ATOM   2036 N  NH2 . ARG A 1 245 ? 3.638   -2.647  22.466  1.00 9.93   ? 246 ARG A NH2 1 
ATOM   2037 N  N   A PRO A 1 246 ? 0.297   -8.960  20.039  0.50 8.21   ? 247 PRO A N   1 
ATOM   2038 N  N   B PRO A 1 246 ? 0.304   -8.945  20.089  0.50 8.23   ? 247 PRO A N   1 
ATOM   2039 C  CA  A PRO A 1 246 ? -0.066  -9.777  21.207  0.50 8.49   ? 247 PRO A CA  1 
ATOM   2040 C  CA  B PRO A 1 246 ? -0.168  -9.813  21.157  0.50 8.65   ? 247 PRO A CA  1 
ATOM   2041 C  C   A PRO A 1 246 ? -0.486  -8.962  22.437  0.50 8.03   ? 247 PRO A C   1 
ATOM   2042 C  C   B PRO A 1 246 ? -0.490  -8.993  22.412  0.50 8.01   ? 247 PRO A C   1 
ATOM   2043 O  O   A PRO A 1 246 ? -0.124  -7.755  22.591  0.50 8.35   ? 247 PRO A O   1 
ATOM   2044 O  O   B PRO A 1 246 ? -0.093  -7.797  22.532  0.50 8.61   ? 247 PRO A O   1 
ATOM   2045 C  CB  A PRO A 1 246 ? 1.199   -10.503 21.544  0.50 10.69  ? 247 PRO A CB  1 
ATOM   2046 C  CB  B PRO A 1 246 ? 0.986   -10.757 21.407  0.50 10.91  ? 247 PRO A CB  1 
ATOM   2047 C  CG  A PRO A 1 246 ? 1.911   -10.632 20.179  0.50 9.89   ? 247 PRO A CG  1 
ATOM   2048 C  CG  B PRO A 1 246 ? 2.255   -9.885  21.108  0.50 13.81  ? 247 PRO A CG  1 
ATOM   2049 C  CD  A PRO A 1 246 ? 1.671   -9.267  19.551  0.50 8.52   ? 247 PRO A CD  1 
ATOM   2050 C  CD  B PRO A 1 246 ? 1.788   -9.010  19.942  0.50 10.09  ? 247 PRO A CD  1 
ATOM   2051 N  N   . ALA A 1 247 ? -1.132  -9.624  23.381  1.00 8.59   ? 248 ALA A N   1 
ATOM   2052 C  CA  . ALA A 1 247 ? -1.476  -8.983  24.647  1.00 8.96   ? 248 ALA A CA  1 
ATOM   2053 C  C   . ALA A 1 247 ? -0.216  -8.489  25.388  1.00 8.31   ? 248 ALA A C   1 
ATOM   2054 O  O   . ALA A 1 247 ? 0.827   -9.142  25.410  1.00 9.79   ? 248 ALA A O   1 
ATOM   2055 C  CB  . ALA A 1 247 ? -2.238  -9.979  25.542  1.00 10.95  ? 248 ALA A CB  1 
ATOM   2056 N  N   . GLN A 1 248 ? -0.345  -7.281  25.970  1.00 8.35   ? 249 GLN A N   1 
ATOM   2057 C  CA  . GLN A 1 248 ? 0.724   -6.588  26.700  1.00 8.67   ? 249 GLN A CA  1 
ATOM   2058 C  C   . GLN A 1 248 ? 0.415   -6.597  28.153  1.00 9.22   ? 249 GLN A C   1 
ATOM   2059 O  O   . GLN A 1 248 ? -0.725  -6.801  28.618  1.00 9.94   ? 249 GLN A O   1 
ATOM   2060 C  CB  . GLN A 1 248 ? 0.736   -5.141  26.181  1.00 9.95   ? 249 GLN A CB  1 
ATOM   2061 C  CG  . GLN A 1 248 ? 1.065   -5.034  24.672  1.00 9.72   ? 249 GLN A CG  1 
ATOM   2062 C  CD  . GLN A 1 248 ? 2.373   -5.735  24.331  1.00 10.30  ? 249 GLN A CD  1 
ATOM   2063 O  OE1 . GLN A 1 248 ? 3.406   -5.383  24.921  1.00 12.54  ? 249 GLN A OE1 1 
ATOM   2064 N  NE2 . GLN A 1 248 ? 2.374   -6.667  23.389  1.00 11.91  ? 249 GLN A NE2 1 
ATOM   2065 N  N   . PRO A 1 249 ? 1.394   -6.296  28.998  1.00 11.41  ? 250 PRO A N   1 
ATOM   2066 C  CA  . PRO A 1 249 ? 1.201   -6.337  30.439  1.00 12.84  ? 250 PRO A CA  1 
ATOM   2067 C  C   . PRO A 1 249 ? 0.127   -5.318  30.901  1.00 10.49  ? 250 PRO A C   1 
ATOM   2068 O  O   . PRO A 1 249 ? 0.161   -4.141  30.552  1.00 10.89  ? 250 PRO A O   1 
ATOM   2069 C  CB  . PRO A 1 249 ? 2.604   -5.946  31.026  1.00 15.07  ? 250 PRO A CB  1 
ATOM   2070 C  CG  . PRO A 1 249 ? 3.536   -6.377  29.978  1.00 17.29  ? 250 PRO A CG  1 
ATOM   2071 C  CD  . PRO A 1 249 ? 2.824   -6.091  28.626  1.00 14.86  ? 250 PRO A CD  1 
ATOM   2072 N  N   . LEU A 1 250 ? -0.730  -5.804  31.822  1.00 11.71  ? 251 LEU A N   1 
ATOM   2073 C  CA  . LEU A 1 250 ? -1.808  -4.928  32.297  1.00 10.57  ? 251 LEU A CA  1 
ATOM   2074 C  C   . LEU A 1 250 ? -1.298  -3.860  33.215  1.00 10.61  ? 251 LEU A C   1 
ATOM   2075 O  O   . LEU A 1 250 ? -1.856  -2.764  33.293  1.00 11.00  ? 251 LEU A O   1 
ATOM   2076 C  CB  . LEU A 1 250 ? -2.854  -5.782  33.031  1.00 13.08  ? 251 LEU A CB  1 
ATOM   2077 C  CG  . LEU A 1 250 ? -4.087  -5.062  33.499  1.00 12.96  ? 251 LEU A CG  1 
ATOM   2078 C  CD1 . LEU A 1 250 ? -4.916  -4.508  32.242  1.00 12.72  ? 251 LEU A CD1 1 
ATOM   2079 C  CD2 . LEU A 1 250 ? -5.038  -6.036  34.261  1.00 17.10  ? 251 LEU A CD2 1 
ATOM   2080 N  N   . LYS A 1 251 ? -0.223  -4.138  33.974  1.00 12.34  ? 252 LYS A N   1 
ATOM   2081 C  CA  . LYS A 1 251 ? 0.448   -3.116  34.864  1.00 12.89  ? 252 LYS A CA  1 
ATOM   2082 C  C   . LYS A 1 251 ? -0.601  -2.541  35.834  1.00 14.52  ? 252 LYS A C   1 
ATOM   2083 O  O   . LYS A 1 251 ? -1.451  -3.349  36.272  1.00 15.79  ? 252 LYS A O   1 
ATOM   2084 C  CB  . LYS A 1 251 ? 1.230   -2.078  34.056  1.00 15.98  ? 252 LYS A CB  1 
ATOM   2085 C  CG  . LYS A 1 251 ? 2.262   -2.770  33.239  1.00 19.18  ? 252 LYS A CG  1 
ATOM   2086 C  CD  . LYS A 1 251 ? 3.304   -1.841  32.684  1.00 19.44  ? 252 LYS A CD  1 
ATOM   2087 C  CE  . LYS A 1 251 ? 4.361   -2.577  31.977  1.00 28.85  ? 252 LYS A CE  1 
ATOM   2088 N  NZ  . LYS A 1 251 ? 5.296   -1.571  31.373  1.00 27.81  ? 252 LYS A NZ  1 
ATOM   2089 N  N   . ASN A 1 252 ? -0.634  -1.282  36.049  1.00 13.29  ? 253 ASN A N   1 
ATOM   2090 C  CA  . ASN A 1 252 ? -1.481  -0.793  37.025  1.00 19.29  ? 253 ASN A CA  1 
ATOM   2091 C  C   . ASN A 1 252 ? -2.803  -0.346  36.502  1.00 18.80  ? 253 ASN A C   1 
ATOM   2092 O  O   . ASN A 1 252 ? -2.958  0.916   36.463  1.00 19.26  ? 253 ASN A O   1 
ATOM   2093 C  CB  . ASN A 1 252 ? -0.704  0.343   37.790  1.00 26.35  ? 253 ASN A CB  1 
ATOM   2094 C  CG  . ASN A 1 252 ? -1.508  0.874   39.030  1.00 25.23  ? 253 ASN A CG  1 
ATOM   2095 O  OD1 . ASN A 1 252 ? -2.258  0.132   39.668  1.00 33.15  ? 253 ASN A OD1 1 
ATOM   2096 N  ND2 . ASN A 1 252 ? -1.380  2.152   39.329  1.00 42.53  ? 253 ASN A ND2 1 
ATOM   2097 N  N   . ARG A 1 253 ? -3.618  -1.360  35.881  1.00 13.59  ? 254 ARG A N   1 
ATOM   2098 C  CA  . ARG A 1 253 ? -4.842  -1.015  35.360  1.00 10.42  ? 254 ARG A CA  1 
ATOM   2099 C  C   . ARG A 1 253 ? -5.933  -1.925  35.817  1.00 11.88  ? 254 ARG A C   1 
ATOM   2100 O  O   . ARG A 1 253 ? -5.722  -3.075  36.054  1.00 18.47  ? 254 ARG A O   1 
ATOM   2101 C  CB  . ARG A 1 253 ? -4.795  -0.972  33.847  1.00 10.15  ? 254 ARG A CB  1 
ATOM   2102 C  CG  . ARG A 1 253 ? -3.885  0.136   33.343  1.00 10.40  ? 254 ARG A CG  1 
ATOM   2103 C  CD  . ARG A 1 253 ? -3.774  0.140   31.821  1.00 9.48   ? 254 ARG A CD  1 
ATOM   2104 N  NE  . ARG A 1 253 ? -2.943  -0.991  31.364  1.00 9.00   ? 254 ARG A NE  1 
ATOM   2105 C  CZ  . ARG A 1 253 ? -2.730  -1.264  30.096  1.00 7.47   ? 254 ARG A CZ  1 
ATOM   2106 N  NH1 . ARG A 1 253 ? -3.315  -0.569  29.116  1.00 7.35   ? 254 ARG A NH1 1 
ATOM   2107 N  NH2 . ARG A 1 253 ? -1.900  -2.241  29.772  1.00 8.16   ? 254 ARG A NH2 1 
ATOM   2108 N  N   . GLN A 1 254 ? -7.170  -1.398  35.839  1.00 11.58  ? 255 GLN A N   1 
ATOM   2109 C  CA  . GLN A 1 254 ? -8.378  -2.192  36.143  1.00 12.56  ? 255 GLN A CA  1 
ATOM   2110 C  C   . GLN A 1 254 ? -9.249  -2.209  34.907  1.00 11.57  ? 255 GLN A C   1 
ATOM   2111 O  O   . GLN A 1 254 ? -9.474  -1.154  34.239  1.00 14.79  ? 255 GLN A O   1 
ATOM   2112 C  CB  . GLN A 1 254 ? -9.194  -1.657  37.297  1.00 15.08  ? 255 GLN A CB  1 
ATOM   2113 C  CG  . GLN A 1 254 ? -9.880  -2.714  38.251  1.00 24.68  ? 255 GLN A CG  1 
ATOM   2114 C  CD  . GLN A 1 254 ? -9.399  -2.361  39.643  1.00 32.30  ? 255 GLN A CD  1 
ATOM   2115 O  OE1 . GLN A 1 254 ? -8.826  -1.214  39.945  1.00 31.33  ? 255 GLN A OE1 1 
ATOM   2116 N  NE2 . GLN A 1 254 ? -9.414  -3.357  40.631  1.00 37.49  ? 255 GLN A NE2 1 
ATOM   2117 N  N   . ILE A 1 255 ? -9.688  -3.398  34.525  1.00 9.83   ? 256 ILE A N   1 
ATOM   2118 C  CA  . ILE A 1 255 ? -10.713 -3.573  33.453  1.00 9.13   ? 256 ILE A CA  1 
ATOM   2119 C  C   . ILE A 1 255 ? -12.066 -3.553  34.132  1.00 9.48   ? 256 ILE A C   1 
ATOM   2120 O  O   . ILE A 1 255 ? -12.251 -4.293  35.125  1.00 11.21  ? 256 ILE A O   1 
ATOM   2121 C  CB  . ILE A 1 255 ? -10.447 -4.797  32.643  1.00 9.64   ? 256 ILE A CB  1 
ATOM   2122 C  CG1 . ILE A 1 255 ? -8.955  -4.804  32.092  1.00 10.73  ? 256 ILE A CG1 1 
ATOM   2123 C  CG2 . ILE A 1 255 ? -11.522 -4.971  31.545  1.00 10.34  ? 256 ILE A CG2 1 
ATOM   2124 C  CD1 . ILE A 1 255 ? -8.661  -5.983  31.245  1.00 12.05  ? 256 ILE A CD1 1 
ATOM   2125 N  N   . LYS A 1 256 ? -12.997 -2.765  33.649  1.00 8.42   ? 257 LYS A N   1 
ATOM   2126 C  CA  . LYS A 1 256 ? -14.336 -2.680  34.191  1.00 8.94   ? 257 LYS A CA  1 
ATOM   2127 C  C   . LYS A 1 256 ? -15.323 -3.295  33.232  1.00 8.80   ? 257 LYS A C   1 
ATOM   2128 O  O   . LYS A 1 256 ? -15.119 -3.178  32.026  1.00 10.93  ? 257 LYS A O   1 
ATOM   2129 C  CB  . LYS A 1 256 ? -14.694 -1.201  34.476  1.00 10.66  ? 257 LYS A CB  1 
ATOM   2130 C  CG  . LYS A 1 256 ? -13.745 -0.600  35.524  1.00 15.63  ? 257 LYS A CG  1 
ATOM   2131 C  CD  . LYS A 1 256 ? -13.896 0.801   35.867  1.00 20.89  ? 257 LYS A CD  1 
ATOM   2132 C  CE  . LYS A 1 256 ? -12.740 1.166   36.819  1.00 28.96  ? 257 LYS A CE  1 
ATOM   2133 N  NZ  . LYS A 1 256 ? -12.788 2.609   37.292  1.00 27.30  ? 257 LYS A NZ  1 
ATOM   2134 N  N   . ALA A 1 257 ? -16.332 -3.916  33.762  1.00 9.60   ? 258 ALA A N   1 
ATOM   2135 C  CA  . ALA A 1 257 ? -17.407 -4.526  32.996  1.00 9.71   ? 258 ALA A CA  1 
ATOM   2136 C  C   . ALA A 1 257 ? -18.677 -3.717  33.145  1.00 9.70   ? 258 ALA A C   1 
ATOM   2137 O  O   . ALA A 1 257 ? -19.032 -3.274  34.264  1.00 11.23  ? 258 ALA A O   1 
ATOM   2138 C  CB  . ALA A 1 257 ? -17.661 -6.006  33.408  1.00 12.69  ? 258 ALA A CB  1 
ATOM   2139 N  N   . SER A 1 258 ? -19.445 -3.568  32.025  1.00 9.70   ? 259 SER A N   1 
ATOM   2140 C  CA  . SER A 1 258 ? -20.692 -2.879  32.061  1.00 11.38  ? 259 SER A CA  1 
ATOM   2141 C  C   . SER A 1 258 ? -21.847 -3.755  32.481  1.00 11.71  ? 259 SER A C   1 
ATOM   2142 O  O   . SER A 1 258 ? -22.988 -3.219  32.622  1.00 15.69  ? 259 SER A O   1 
ATOM   2143 C  CB  . SER A 1 258 ? -21.040 -2.281  30.700  1.00 12.21  ? 259 SER A CB  1 
ATOM   2144 O  OG  . SER A 1 258 ? -21.423 -3.331  29.780  1.00 10.70  ? 259 SER A OG  1 
ATOM   2145 N  N   . PHE A 1 259 ? -21.603 -4.996  32.697  1.00 12.90  ? 260 PHE A N   1 
ATOM   2146 C  CA  . PHE A 1 259 ? -22.615 -6.052  32.881  1.00 15.12  ? 260 PHE A CA  1 
ATOM   2147 C  C   . PHE A 1 259 ? -22.179 -6.954  33.972  1.00 17.20  ? 260 PHE A C   1 
ATOM   2148 O  O   . PHE A 1 259 ? -21.019 -7.159  34.301  1.00 18.35  ? 260 PHE A O   1 
ATOM   2149 C  CB  . PHE A 1 259 ? -22.846 -6.804  31.582  1.00 16.01  ? 260 PHE A CB  1 
ATOM   2150 C  CG  . PHE A 1 259 ? -21.551 -7.544  31.163  1.00 14.35  ? 260 PHE A CG  1 
ATOM   2151 C  CD1 . PHE A 1 259 ? -20.551 -6.852  30.435  1.00 12.30  ? 260 PHE A CD1 1 
ATOM   2152 C  CD2 . PHE A 1 259 ? -21.277 -8.847  31.580  1.00 18.35  ? 260 PHE A CD2 1 
ATOM   2153 C  CE1 . PHE A 1 259 ? -19.288 -7.498  30.154  1.00 14.86  ? 260 PHE A CE1 1 
ATOM   2154 C  CE2 . PHE A 1 259 ? -20.040 -9.432  31.363  1.00 18.27  ? 260 PHE A CE2 1 
ATOM   2155 C  CZ  . PHE A 1 259 ? -19.044 -8.827  30.602  1.00 18.73  ? 260 PHE A CZ  1 
ATOM   2156 N  N   . LYS A 1 260 ? -23.208 -7.575  34.516  1.00 28.22  ? 261 LYS A N   1 
ATOM   2157 C  CA  . LYS A 1 260 ? -23.078 -8.542  35.643  1.00 37.50  ? 261 LYS A CA  1 
ATOM   2158 C  CB  . LYS A 1 260 ? -22.988 -10.001 35.063  1.00 53.48  ? 261 LYS A CB  1 
HETATM 2159 ZN ZN  . ZN  B 2 .   ? -6.627  -1.793  15.337  1.00 6.08   ? 301 ZN  A ZN  1 
HETATM 2160 S  S   . DMS C 3 .   ? 1.354   -11.801 15.002  1.00 17.59  ? 302 DMS A S   1 
HETATM 2161 O  O   . DMS C 3 .   ? 2.466   -10.713 14.641  1.00 27.62  ? 302 DMS A O   1 
HETATM 2162 C  C1  . DMS C 3 .   ? 1.955   -13.193 14.610  1.00 17.71  ? 302 DMS A C1  1 
HETATM 2163 C  C2  . DMS C 3 .   ? 1.591   -11.678 16.657  1.00 16.77  ? 302 DMS A C2  1 
HETATM 2164 N  N1  . BCN D 4 .   ? -20.583 -14.871 23.401  1.00 28.59  ? 303 BCN A N1  1 
HETATM 2165 C  C1  . BCN D 4 .   ? -19.612 -14.255 24.352  1.00 26.12  ? 303 BCN A C1  1 
HETATM 2166 C  C2  . BCN D 4 .   ? -19.946 -15.188 25.540  1.00 28.41  ? 303 BCN A C2  1 
HETATM 2167 O  O21 . BCN D 4 .   ? -20.873 -16.071 25.502  1.00 32.03  ? 303 BCN A O21 1 
HETATM 2168 O  O22 . BCN D 4 .   ? -19.301 -15.091 26.565  1.00 29.40  ? 303 BCN A O22 1 
HETATM 2169 C  C3  . BCN D 4 .   ? -21.636 -13.974 23.083  1.00 19.59  ? 303 BCN A C3  1 
HETATM 2170 C  C4  . BCN D 4 .   ? -21.441 -12.832 24.036  1.00 39.58  ? 303 BCN A C4  1 
HETATM 2171 O  O4  . BCN D 4 .   ? -22.425 -12.428 25.038  1.00 27.71  ? 303 BCN A O4  1 
HETATM 2172 C  C5  . BCN D 4 .   ? -20.038 -15.634 22.323  1.00 16.54  ? 303 BCN A C5  1 
HETATM 2173 C  C6  . BCN D 4 .   ? -20.613 -16.815 21.509  1.00 37.47  ? 303 BCN A C6  1 
HETATM 2174 O  O6  . BCN D 4 .   ? -21.105 -16.270 20.231  1.00 38.89  ? 303 BCN A O6  1 
HETATM 2175 C  C5  . ENN E 5 .   ? -4.843  1.861   14.596  1.00 7.89   ? 304 ENN A C5  1 
HETATM 2176 C  C4  . ENN E 5 .   ? -4.621  2.900   13.690  1.00 9.51   ? 304 ENN A C4  1 
HETATM 2177 C  C6  . ENN E 5 .   ? -5.515  2.082   15.811  1.00 7.40   ? 304 ENN A C6  1 
HETATM 2178 C  C2  . ENN E 5 .   ? -5.631  4.462   15.252  1.00 9.65   ? 304 ENN A C2  1 
HETATM 2179 O  O14 . ENN E 5 .   ? -4.590  3.022   11.318  1.00 14.04  ? 304 ENN A O14 1 
HETATM 2180 C  C13 . ENN E 5 .   ? -3.996  2.661   12.420  1.00 12.09  ? 304 ENN A C13 1 
HETATM 2181 N  N15 . ENN E 5 .   ? -2.915  1.976   12.383  1.00 14.29  ? 304 ENN A N15 1 
HETATM 2182 C  C16 . ENN E 5 .   ? -2.108  1.697   11.150  1.00 21.05  ? 304 ENN A C16 1 
HETATM 2183 C  C17 . ENN E 5 .   ? -0.837  2.546   11.118  1.00 24.20  ? 304 ENN A C17 1 
HETATM 2184 C  C18 . ENN E 5 .   ? -1.267  4.024   11.104  1.00 47.94  ? 304 ENN A C18 1 
HETATM 2185 C  C19 . ENN E 5 .   ? 0.068   4.908   11.288  1.00 48.06  ? 304 ENN A C19 1 
HETATM 2186 C  C3  . ENN E 5 .   ? -5.007  4.188   14.041  1.00 10.34  ? 304 ENN A C3  1 
HETATM 2187 CL CL1 . ENN E 5 .   ? -4.529  5.515   13.111  1.00 30.39  ? 304 ENN A CL1 1 
HETATM 2188 C  C1  . ENN E 5 .   ? -5.866  3.412   16.127  1.00 8.47   ? 304 ENN A C1  1 
HETATM 2189 CL CL2 . ENN E 5 .   ? -6.685  3.778   17.601  1.00 8.72   ? 304 ENN A CL2 1 
HETATM 2190 S  S7  . ENN E 5 .   ? -5.930  0.719   16.858  1.00 6.26   ? 304 ENN A S7  1 
HETATM 2191 O  O9  . ENN E 5 .   ? -5.286  0.970   18.126  1.00 6.54   ? 304 ENN A O9  1 
HETATM 2192 O  O10 . ENN E 5 .   ? -7.372  0.711   16.837  1.00 6.32   ? 304 ENN A O10 1 
HETATM 2193 N  N8  . ENN E 5 .   ? -5.349  -0.587  16.177  1.00 6.23   ? 304 ENN A N8  1 
HETATM 2194 O  O   . HOH F 6 .   ? -25.492 -10.651 17.780  1.00 23.96  ? 401 HOH A O   1 
HETATM 2195 O  O   . HOH F 6 .   ? -18.654 19.906  14.674  1.00 21.10  ? 402 HOH A O   1 
HETATM 2196 O  O   . HOH F 6 .   ? -8.933  6.394   -3.823  1.00 27.38  ? 403 HOH A O   1 
HETATM 2197 O  O   . HOH F 6 .   ? -15.425 19.310  13.162  1.00 14.56  ? 404 HOH A O   1 
HETATM 2198 O  O   . HOH F 6 .   ? -20.879 7.847   1.889   1.00 21.49  ? 405 HOH A O   1 
HETATM 2199 O  O   . HOH F 6 .   ? -3.403  18.063  21.475  1.00 21.47  ? 406 HOH A O   1 
HETATM 2200 O  O   . HOH F 6 .   ? -13.967 -5.078  -6.391  1.00 36.50  ? 407 HOH A O   1 
HETATM 2201 O  O   . HOH F 6 .   ? -10.462 -5.898  38.402  1.00 28.90  ? 408 HOH A O   1 
HETATM 2202 O  O   . HOH F 6 .   ? -20.954 -6.916  -1.945  1.00 36.17  ? 409 HOH A O   1 
HETATM 2203 O  O   . HOH F 6 .   ? -11.047 -15.163 34.226  1.00 23.56  ? 410 HOH A O   1 
HETATM 2204 O  O   . HOH F 6 .   ? 12.768  -0.612  9.767   1.00 38.80  ? 411 HOH A O   1 
HETATM 2205 O  O   . HOH F 6 .   ? 5.750   -9.828  21.284  1.00 38.98  ? 412 HOH A O   1 
HETATM 2206 O  O   . HOH F 6 .   ? -19.143 13.976  9.317   1.00 32.51  ? 413 HOH A O   1 
HETATM 2207 O  O   . HOH F 6 .   ? -17.805 -22.125 6.053   1.00 15.54  ? 414 HOH A O   1 
HETATM 2208 O  O   . HOH F 6 .   ? -16.968 18.070  22.480  1.00 39.80  ? 415 HOH A O   1 
HETATM 2209 O  O   . HOH F 6 .   ? -13.042 -0.847  -5.917  1.00 35.81  ? 416 HOH A O   1 
HETATM 2210 O  O   . HOH F 6 .   ? -12.819 13.196  31.924  1.00 29.50  ? 417 HOH A O   1 
HETATM 2211 O  O   . HOH F 6 .   ? -19.898 15.741  19.046  1.00 29.16  ? 418 HOH A O   1 
HETATM 2212 O  O   . HOH F 6 .   ? -12.146 10.739  5.921   1.00 35.29  ? 419 HOH A O   1 
HETATM 2213 O  O   . HOH F 6 .   ? 2.816   -9.156  -6.467  1.00 31.92  ? 420 HOH A O   1 
HETATM 2214 O  O   . HOH F 6 .   ? -6.172  -11.626 36.716  1.00 45.44  ? 421 HOH A O   1 
HETATM 2215 O  O   . HOH F 6 .   ? -12.970 -22.436 12.237  1.00 30.61  ? 422 HOH A O   1 
HETATM 2216 O  O   . HOH F 6 .   ? -0.940  23.675  18.077  1.00 31.74  ? 423 HOH A O   1 
HETATM 2217 O  O   . HOH F 6 .   ? -24.046 -3.239  29.383  1.00 39.31  ? 424 HOH A O   1 
HETATM 2218 O  O   . HOH F 6 .   ? -18.547 4.230   -3.598  1.00 103.40 ? 425 HOH A O   1 
HETATM 2219 O  O   . HOH F 6 .   ? -2.398  21.944  21.477  1.00 25.52  ? 426 HOH A O   1 
HETATM 2220 O  O   . HOH F 6 .   ? -27.175 -10.920 22.667  1.00 37.02  ? 427 HOH A O   1 
HETATM 2221 O  O   . HOH F 6 .   ? -1.040  3.968   14.194  1.00 28.25  ? 428 HOH A O   1 
HETATM 2222 O  O   . HOH F 6 .   ? -9.993  15.789  29.775  1.00 29.76  ? 429 HOH A O   1 
HETATM 2223 O  O   . HOH F 6 .   ? 1.164   2.890   5.616   1.00 36.12  ? 430 HOH A O   1 
HETATM 2224 O  O   . HOH F 6 .   ? -25.890 -6.191  13.182  1.00 30.97  ? 431 HOH A O   1 
HETATM 2225 O  O   . HOH F 6 .   ? -1.214  -4.090  15.780  1.00 8.99   ? 432 HOH A O   1 
HETATM 2226 O  O   . HOH F 6 .   ? -13.705 -8.896  -5.334  1.00 31.03  ? 433 HOH A O   1 
HETATM 2227 O  O   . HOH F 6 .   ? -6.196  -4.694  -6.388  1.00 27.42  ? 434 HOH A O   1 
HETATM 2228 O  O   . HOH F 6 .   ? 4.401   -2.545  29.099  1.00 23.96  ? 435 HOH A O   1 
HETATM 2229 O  O   . HOH F 6 .   ? -8.687  -3.906  7.932   1.00 9.31   ? 436 HOH A O   1 
HETATM 2230 O  O   . HOH F 6 .   ? -16.508 14.428  33.366  1.00 27.68  ? 437 HOH A O   1 
HETATM 2231 O  O   . HOH F 6 .   ? 4.219   -3.487  26.574  1.00 18.54  ? 438 HOH A O   1 
HETATM 2232 O  O   . HOH F 6 .   ? 3.666   4.991   29.908  1.00 18.51  ? 439 HOH A O   1 
HETATM 2233 O  O   . HOH F 6 .   ? 7.188   -0.716  -0.997  1.00 48.45  ? 440 HOH A O   1 
HETATM 2234 O  O   . HOH F 6 .   ? 2.277   8.053   28.219  1.00 45.25  ? 441 HOH A O   1 
HETATM 2235 O  O   . HOH F 6 .   ? 7.538   -8.072  -1.021  1.00 32.70  ? 442 HOH A O   1 
HETATM 2236 O  O   . HOH F 6 .   ? -14.295 -16.688 29.174  1.00 20.02  ? 443 HOH A O   1 
HETATM 2237 O  O   . HOH F 6 .   ? 0.089   -1.206  -4.732  1.00 18.59  ? 444 HOH A O   1 
HETATM 2238 O  O   . HOH F 6 .   ? -9.125  5.833   29.073  1.00 15.35  ? 445 HOH A O   1 
HETATM 2239 O  O   . HOH F 6 .   ? -4.765  0.239   9.444   1.00 23.29  ? 446 HOH A O   1 
HETATM 2240 O  O   . HOH F 6 .   ? -12.980 -22.262 8.653   1.00 29.07  ? 447 HOH A O   1 
HETATM 2241 O  O   . HOH F 6 .   ? 11.675  -0.398  16.162  1.00 22.55  ? 448 HOH A O   1 
HETATM 2242 O  O   . HOH F 6 .   ? -25.645 -1.162  35.212  1.00 32.10  ? 449 HOH A O   1 
HETATM 2243 O  O   . HOH F 6 .   ? -12.491 12.411  29.347  1.00 25.29  ? 450 HOH A O   1 
HETATM 2244 O  O   . HOH F 6 .   ? -24.106 8.541   20.240  1.00 18.75  ? 451 HOH A O   1 
HETATM 2245 O  O   . HOH F 6 .   ? 0.741   -10.039 -5.364  1.00 34.66  ? 452 HOH A O   1 
HETATM 2246 O  O   . HOH F 6 .   ? -1.883  -4.857  -7.040  1.00 31.20  ? 453 HOH A O   1 
HETATM 2247 O  O   . HOH F 6 .   ? 2.430   -13.349 5.242   1.00 20.21  ? 454 HOH A O   1 
HETATM 2248 O  O   . HOH F 6 .   ? -10.618 8.658   25.650  1.00 8.68   ? 455 HOH A O   1 
HETATM 2249 O  O   . HOH F 6 .   ? -20.985 -0.145  -1.985  1.00 32.23  ? 456 HOH A O   1 
HETATM 2250 O  O   . HOH F 6 .   ? 1.076   14.668  24.472  1.00 29.66  ? 457 HOH A O   1 
HETATM 2251 O  O   . HOH F 6 .   ? -19.746 -4.215  41.438  1.00 40.28  ? 458 HOH A O   1 
HETATM 2252 O  O   . HOH F 6 .   ? -25.617 -15.271 7.796   1.00 33.06  ? 459 HOH A O   1 
HETATM 2253 O  O   . HOH F 6 .   ? -15.904 3.680   35.412  1.00 32.86  ? 460 HOH A O   1 
HETATM 2254 O  O   . HOH F 6 .   ? -7.040  5.927   6.269   1.00 17.34  ? 461 HOH A O   1 
HETATM 2255 O  O   . HOH F 6 .   ? -1.142  9.244   28.062  1.00 22.67  ? 462 HOH A O   1 
HETATM 2256 O  O   . HOH F 6 .   ? 4.633   -1.016  -5.443  1.00 29.77  ? 463 HOH A O   1 
HETATM 2257 O  O   . HOH F 6 .   ? -16.846 -14.007 26.455  1.00 16.33  ? 464 HOH A O   1 
HETATM 2258 O  O   . HOH F 6 .   ? -6.939  -14.922 31.690  1.00 21.76  ? 465 HOH A O   1 
HETATM 2259 O  O   . HOH F 6 .   ? -19.370 -20.837 5.185   1.00 24.32  ? 466 HOH A O   1 
HETATM 2260 O  O   . HOH F 6 .   ? -20.353 10.681  26.823  1.00 17.11  ? 467 HOH A O   1 
HETATM 2261 O  O   . HOH F 6 .   ? -27.998 6.583   21.928  1.00 80.71  ? 468 HOH A O   1 
HETATM 2262 O  O   . HOH F 6 .   ? -7.995  -15.558 11.459  1.00 9.57   ? 469 HOH A O   1 
HETATM 2263 O  O   . HOH F 6 .   ? -0.017  1.059   34.576  1.00 26.77  ? 470 HOH A O   1 
HETATM 2264 O  O   . HOH F 6 .   ? -4.734  -12.020 32.195  1.00 18.95  ? 471 HOH A O   1 
HETATM 2265 O  O   . HOH F 6 .   ? -15.031 2.429   38.778  1.00 25.11  ? 472 HOH A O   1 
HETATM 2266 O  O   . HOH F 6 .   ? -22.841 -5.835  2.796   1.00 24.06  ? 473 HOH A O   1 
HETATM 2267 O  O   . HOH F 6 .   ? -10.387 13.463  8.827   1.00 27.38  ? 474 HOH A O   1 
HETATM 2268 O  O   . HOH F 6 .   ? 0.489   6.976   30.058  1.00 32.11  ? 475 HOH A O   1 
HETATM 2269 O  O   . HOH F 6 .   ? -18.741 -12.304 -3.549  1.00 26.25  ? 476 HOH A O   1 
HETATM 2270 O  O   . HOH F 6 .   ? 10.835  -9.743  9.342   1.00 143.74 ? 477 HOH A O   1 
HETATM 2271 O  O   . HOH F 6 .   ? -18.899 2.051   40.808  1.00 50.80  ? 478 HOH A O   1 
HETATM 2272 O  O   . HOH F 6 .   ? -17.423 -16.264 22.118  1.00 19.46  ? 479 HOH A O   1 
HETATM 2273 O  O   . HOH F 6 .   ? 2.070   -7.291  -8.229  1.00 34.37  ? 480 HOH A O   1 
HETATM 2274 O  O   . HOH F 6 .   ? -25.902 6.111   27.131  1.00 23.09  ? 481 HOH A O   1 
HETATM 2275 O  O   . HOH F 6 .   ? 2.350   -14.635 -5.688  1.00 45.04  ? 482 HOH A O   1 
HETATM 2276 O  O   . HOH F 6 .   ? 1.814   -15.759 9.292   1.00 21.36  ? 483 HOH A O   1 
HETATM 2277 O  O   . HOH F 6 .   ? -16.099 -12.383 24.490  1.00 12.18  ? 484 HOH A O   1 
HETATM 2278 O  O   . HOH F 6 .   ? -4.551  -13.610 18.141  1.00 8.56   ? 485 HOH A O   1 
HETATM 2279 O  O   . HOH F 6 .   ? 8.271   2.991   27.733  1.00 30.86  ? 486 HOH A O   1 
HETATM 2280 O  O   . HOH F 6 .   ? -26.313 -7.942  30.396  1.00 67.56  ? 487 HOH A O   1 
HETATM 2281 O  O   . HOH F 6 .   ? -2.519  -8.791  29.180  1.00 10.35  ? 488 HOH A O   1 
HETATM 2282 O  O   . HOH F 6 .   ? -6.773  20.892  19.670  1.00 11.44  ? 489 HOH A O   1 
HETATM 2283 O  O   . HOH F 6 .   ? 15.307  -2.564  14.460  1.00 18.91  ? 490 HOH A O   1 
HETATM 2284 O  O   . HOH F 6 .   ? -18.485 -3.817  -2.628  1.00 28.50  ? 491 HOH A O   1 
HETATM 2285 O  O   . HOH F 6 .   ? -13.903 10.295  27.994  1.00 16.89  ? 492 HOH A O   1 
HETATM 2286 O  O   . HOH F 6 .   ? -3.510  -11.222 20.950  1.00 8.86   ? 493 HOH A O   1 
HETATM 2287 O  O   . HOH F 6 .   ? -25.726 -6.914  33.641  1.00 42.35  ? 494 HOH A O   1 
HETATM 2288 O  O   . HOH F 6 .   ? -0.382  13.949  16.240  1.00 26.53  ? 495 HOH A O   1 
HETATM 2289 O  O   . HOH F 6 .   ? -8.690  -15.470 36.795  1.00 22.09  ? 496 HOH A O   1 
HETATM 2290 O  O   . HOH F 6 .   ? -22.066 -14.082 18.697  1.00 29.04  ? 497 HOH A O   1 
HETATM 2291 O  O   . HOH F 6 .   ? -10.627 8.502   7.767   1.00 20.62  ? 498 HOH A O   1 
HETATM 2292 O  O   . HOH F 6 .   ? -17.023 -8.452  20.428  1.00 7.57   ? 499 HOH A O   1 
HETATM 2293 O  O   . HOH F 6 .   ? -14.987 6.098   32.756  1.00 28.96  ? 500 HOH A O   1 
HETATM 2294 O  O   . HOH F 6 .   ? -17.390 -7.527  39.572  1.00 45.37  ? 501 HOH A O   1 
HETATM 2295 O  O   . HOH F 6 .   ? -27.277 -7.724  26.291  1.00 37.16  ? 502 HOH A O   1 
HETATM 2296 O  O   . HOH F 6 .   ? 5.794   0.713   8.560   1.00 28.67  ? 503 HOH A O   1 
HETATM 2297 O  O   . HOH F 6 .   ? -15.374 8.910   -2.174  1.00 29.79  ? 504 HOH A O   1 
HETATM 2298 O  O   . HOH F 6 .   ? -20.655 8.111   30.148  1.00 28.97  ? 505 HOH A O   1 
HETATM 2299 O  O   . HOH F 6 .   ? -17.921 10.603  11.360  1.00 15.70  ? 506 HOH A O   1 
HETATM 2300 O  O   . HOH F 6 .   ? -4.235  -8.570  31.270  1.00 18.52  ? 507 HOH A O   1 
HETATM 2301 O  O   . HOH F 6 .   ? -16.166 15.787  23.810  1.00 15.66  ? 508 HOH A O   1 
HETATM 2302 O  O   . HOH F 6 .   ? -21.597 -7.244  23.658  1.00 11.49  ? 509 HOH A O   1 
HETATM 2303 O  O   . HOH F 6 .   ? 3.094   2.892   8.480   1.00 46.05  ? 510 HOH A O   1 
HETATM 2304 O  O   . HOH F 6 .   ? -5.585  3.273   -5.618  1.00 63.97  ? 511 HOH A O   1 
HETATM 2305 O  O   . HOH F 6 .   ? -13.974 14.130  27.324  1.00 21.06  ? 512 HOH A O   1 
HETATM 2306 O  O   . HOH F 6 .   ? 1.184   -11.878 25.208  1.00 23.16  ? 513 HOH A O   1 
HETATM 2307 O  O   . HOH F 6 .   ? -17.932 -20.489 8.013   1.00 12.80  ? 514 HOH A O   1 
HETATM 2308 O  O   . HOH F 6 .   ? -23.257 -17.828 21.016  1.00 34.72  ? 515 HOH A O   1 
HETATM 2309 O  O   . HOH F 6 .   ? 2.641   -4.424  7.863   1.00 18.91  ? 516 HOH A O   1 
HETATM 2310 O  O   . HOH F 6 .   ? -3.552  -13.089 -2.820  1.00 22.22  ? 517 HOH A O   1 
HETATM 2311 O  O   . HOH F 6 .   ? -25.305 11.047  19.697  1.00 27.50  ? 518 HOH A O   1 
HETATM 2312 O  O   . HOH F 6 .   ? 8.562   -3.872  21.120  1.00 14.62  ? 519 HOH A O   1 
HETATM 2313 O  O   . HOH F 6 .   ? 1.557   2.269   36.123  1.00 41.24  ? 520 HOH A O   1 
HETATM 2314 O  O   . HOH F 6 .   ? -14.959 20.009  17.748  1.00 16.22  ? 521 HOH A O   1 
HETATM 2315 O  O   . HOH F 6 .   ? -11.029 -19.693 7.337   1.00 27.59  ? 522 HOH A O   1 
HETATM 2316 O  O   . HOH F 6 .   ? -26.190 3.294   15.545  1.00 31.79  ? 523 HOH A O   1 
HETATM 2317 O  O   . HOH F 6 .   ? -7.456  8.069   29.712  1.00 24.17  ? 524 HOH A O   1 
HETATM 2318 O  O   . HOH F 6 .   ? -8.542  0.587   -6.543  1.00 32.36  ? 525 HOH A O   1 
HETATM 2319 O  O   . HOH F 6 .   ? -22.096 -18.353 13.578  1.00 19.55  ? 526 HOH A O   1 
HETATM 2320 O  O   . HOH F 6 .   ? 5.017   -7.447  25.873  1.00 34.44  ? 527 HOH A O   1 
HETATM 2321 O  O   . HOH F 6 .   ? -0.200  -20.633 15.341  1.00 44.08  ? 528 HOH A O   1 
HETATM 2322 O  O   . HOH F 6 .   ? -22.014 3.976   -3.016  1.00 25.21  ? 529 HOH A O   1 
HETATM 2323 O  O   . HOH F 6 .   ? 13.402  0.224   24.597  1.00 20.72  ? 530 HOH A O   1 
HETATM 2324 O  O   . HOH F 6 .   ? -3.386  -13.344 25.239  1.00 10.21  ? 531 HOH A O   1 
HETATM 2325 O  O   . HOH F 6 .   ? -30.689 -12.783 21.765  1.00 39.10  ? 532 HOH A O   1 
HETATM 2326 O  O   . HOH F 6 .   ? -7.282  -16.865 1.387   1.00 21.32  ? 533 HOH A O   1 
HETATM 2327 O  O   . HOH F 6 .   ? -13.713 19.915  15.227  1.00 15.30  ? 534 HOH A O   1 
HETATM 2328 O  O   . HOH F 6 .   ? -23.033 -14.840 16.164  1.00 29.43  ? 535 HOH A O   1 
HETATM 2329 O  O   . HOH F 6 .   ? -21.774 5.736   4.775   1.00 19.78  ? 536 HOH A O   1 
HETATM 2330 O  O   . HOH F 6 .   ? -20.042 17.033  23.112  1.00 40.11  ? 537 HOH A O   1 
HETATM 2331 O  O   . HOH F 6 .   ? -23.174 -2.988  6.658   1.00 21.01  ? 538 HOH A O   1 
HETATM 2332 O  O   . HOH F 6 .   ? -0.445  10.813  23.554  1.00 15.17  ? 539 HOH A O   1 
HETATM 2333 O  O   . HOH F 6 .   ? -4.101  5.207   9.636   1.00 23.54  ? 540 HOH A O   1 
HETATM 2334 O  O   . HOH F 6 .   ? 4.888   -3.658  3.003   1.00 31.24  ? 541 HOH A O   1 
HETATM 2335 O  O   . HOH F 6 .   ? -10.678 21.650  20.166  1.00 14.87  ? 542 HOH A O   1 
HETATM 2336 O  O   . HOH F 6 .   ? 5.396   7.066   20.307  1.00 16.10  ? 543 HOH A O   1 
HETATM 2337 O  O   . HOH F 6 .   ? -9.320  -10.153 -1.187  1.00 23.67  ? 544 HOH A O   1 
HETATM 2338 O  O   . HOH F 6 .   ? -16.468 -15.667 32.806  1.00 36.10  ? 545 HOH A O   1 
HETATM 2339 O  O   . HOH F 6 .   ? 9.247   7.489   18.497  1.00 40.66  ? 546 HOH A O   1 
HETATM 2340 O  O   . HOH F 6 .   ? -19.224 10.018  8.930   1.00 14.39  ? 547 HOH A O   1 
HETATM 2341 O  O   . HOH F 6 .   ? -24.830 -7.726  9.056   1.00 18.68  ? 548 HOH A O   1 
HETATM 2342 O  O   . HOH F 6 .   ? 4.225   -6.674  7.900   1.00 24.73  ? 549 HOH A O   1 
HETATM 2343 O  O   . HOH F 6 .   ? -2.537  -3.176  11.457  1.00 17.04  ? 550 HOH A O   1 
HETATM 2344 O  O   . HOH F 6 .   ? -6.609  -5.314  37.502  1.00 17.03  ? 551 HOH A O   1 
HETATM 2345 O  O   . HOH F 6 .   ? -14.705 -18.614 18.770  1.00 12.80  ? 552 HOH A O   1 
HETATM 2346 O  O   . HOH F 6 .   ? -3.796  -15.963 24.440  1.00 12.02  ? 553 HOH A O   1 
HETATM 2347 O  O   . HOH F 6 .   ? 4.896   -4.957  21.028  1.00 13.50  ? 554 HOH A O   1 
HETATM 2348 O  O   . HOH F 6 .   ? -25.505 -8.760  11.130  1.00 23.72  ? 555 HOH A O   1 
HETATM 2349 O  O   . HOH F 6 .   ? -16.326 -9.999  33.033  1.00 16.41  ? 556 HOH A O   1 
HETATM 2350 O  O   . HOH F 6 .   ? 2.504   -11.423 9.571   1.00 23.85  ? 557 HOH A O   1 
HETATM 2351 O  O   . HOH F 6 .   ? -13.456 -18.606 14.652  1.00 12.23  ? 558 HOH A O   1 
HETATM 2352 O  O   . HOH F 6 .   ? -23.267 -0.335  34.623  1.00 30.95  ? 559 HOH A O   1 
HETATM 2353 O  O   . HOH F 6 .   ? 15.642  2.920   21.050  1.00 34.04  ? 560 HOH A O   1 
HETATM 2354 O  O   . HOH F 6 .   ? -13.040 -16.892 26.764  1.00 12.91  ? 561 HOH A O   1 
HETATM 2355 O  O   . HOH F 6 .   ? -4.796  -15.970 0.685   1.00 24.97  ? 562 HOH A O   1 
HETATM 2356 O  O   . HOH F 6 .   ? -7.332  -8.722  32.718  1.00 16.57  ? 563 HOH A O   1 
HETATM 2357 O  O   . HOH F 6 .   ? -24.806 4.751   8.407   1.00 38.61  ? 564 HOH A O   1 
HETATM 2358 O  O   . HOH F 6 .   ? -28.332 -0.338  6.721   1.00 41.87  ? 565 HOH A O   1 
HETATM 2359 O  O   . HOH F 6 .   ? -12.781 7.795   28.971  1.00 24.42  ? 566 HOH A O   1 
HETATM 2360 O  O   . HOH F 6 .   ? -0.010  -14.333 31.320  1.00 27.94  ? 567 HOH A O   1 
HETATM 2361 O  O   . HOH F 6 .   ? -12.548 -18.367 32.487  1.00 25.70  ? 568 HOH A O   1 
HETATM 2362 O  O   . HOH F 6 .   ? 2.753   -14.676 1.114   1.00 27.74  ? 569 HOH A O   1 
HETATM 2363 O  O   . HOH F 6 .   ? -22.695 -9.610  25.391  1.00 20.46  ? 570 HOH A O   1 
HETATM 2364 O  O   . HOH F 6 .   ? -23.440 -11.227 17.148  1.00 25.78  ? 571 HOH A O   1 
HETATM 2365 O  O   . HOH F 6 .   ? -12.849 -8.905  -3.277  1.00 31.00  ? 572 HOH A O   1 
HETATM 2366 O  O   . HOH F 6 .   ? 1.520   -17.777 13.809  1.00 35.95  ? 573 HOH A O   1 
HETATM 2367 O  O   . HOH F 6 .   ? 11.201  1.307   26.104  1.00 22.42  ? 574 HOH A O   1 
HETATM 2368 O  O   . HOH F 6 .   ? 6.580   -5.957  6.664   1.00 29.96  ? 575 HOH A O   1 
HETATM 2369 O  O   . HOH F 6 .   ? 13.905  5.630   19.178  1.00 31.07  ? 576 HOH A O   1 
HETATM 2370 O  O   . HOH F 6 .   ? -9.549  -7.988  34.209  1.00 20.22  ? 577 HOH A O   1 
HETATM 2371 O  O   . HOH F 6 .   ? -8.568  -19.917 26.802  1.00 19.54  ? 578 HOH A O   1 
HETATM 2372 O  O   . HOH F 6 .   ? 1.577   -6.327  34.462  1.00 24.61  ? 579 HOH A O   1 
HETATM 2373 O  O   . HOH F 6 .   ? -23.409 -13.241 11.299  1.00 19.17  ? 580 HOH A O   1 
HETATM 2374 O  O   . HOH F 6 .   ? 1.204   -1.552  29.532  1.00 12.90  ? 581 HOH A O   1 
HETATM 2375 O  O   . HOH F 6 .   ? -23.987 -0.782  26.581  1.00 16.23  ? 582 HOH A O   1 
HETATM 2376 O  O   . HOH F 6 .   ? -11.118 1.102   33.515  1.00 19.32  ? 583 HOH A O   1 
HETATM 2377 O  O   . HOH F 6 .   ? 1.313   8.756   24.408  1.00 17.31  ? 584 HOH A O   1 
HETATM 2378 O  O   . HOH F 6 .   ? 7.623   6.045   21.764  1.00 15.59  ? 585 HOH A O   1 
HETATM 2379 O  O   . HOH F 6 .   ? -12.010 2.656   31.035  1.00 16.31  ? 586 HOH A O   1 
HETATM 2380 O  O   . HOH F 6 .   ? -17.971 -3.145  45.321  1.00 36.37  ? 587 HOH A O   1 
HETATM 2381 O  O   . HOH F 6 .   ? 4.930   -7.510  22.321  1.00 26.92  ? 588 HOH A O   1 
HETATM 2382 O  O   . HOH F 6 .   ? -23.686 -0.782  3.928   1.00 26.71  ? 589 HOH A O   1 
HETATM 2383 O  O   . HOH F 6 .   ? 5.645   -2.986  6.800   1.00 34.17  ? 590 HOH A O   1 
HETATM 2384 O  O   . HOH F 6 .   ? -6.244  -19.829 23.889  1.00 19.59  ? 591 HOH A O   1 
HETATM 2385 O  O   . HOH F 6 .   ? 13.006  -5.860  24.357  1.00 26.70  ? 592 HOH A O   1 
HETATM 2386 O  O   . HOH F 6 .   ? -9.103  -5.851  35.990  1.00 17.85  ? 593 HOH A O   1 
HETATM 2387 O  O   . HOH F 6 .   ? -6.387  -19.452 5.782   1.00 32.37  ? 594 HOH A O   1 
HETATM 2388 O  O   . HOH F 6 .   ? -13.534 -16.646 -0.203  1.00 41.39  ? 595 HOH A O   1 
HETATM 2389 O  O   . HOH F 6 .   ? -9.982  14.734  12.297  1.00 18.07  ? 596 HOH A O   1 
HETATM 2390 O  O   . HOH F 6 .   ? 3.955   4.382   10.593  1.00 36.64  ? 597 HOH A O   1 
HETATM 2391 O  O   . HOH F 6 .   ? -0.593  -8.614  32.648  1.00 24.24  ? 598 HOH A O   1 
HETATM 2392 O  O   . HOH F 6 .   ? -2.085  -12.366 22.932  1.00 9.73   ? 599 HOH A O   1 
HETATM 2393 O  O   . HOH F 6 .   ? -6.023  17.632  27.662  1.00 26.34  ? 600 HOH A O   1 
HETATM 2394 O  O   . HOH F 6 .   ? -10.925 -5.879  40.619  1.00 30.85  ? 601 HOH A O   1 
HETATM 2395 O  O   . HOH F 6 .   ? -15.091 -20.089 23.180  1.00 28.42  ? 602 HOH A O   1 
HETATM 2396 O  O   . HOH F 6 .   ? -0.312  -14.410 22.255  1.00 20.82  ? 603 HOH A O   1 
HETATM 2397 O  O   . HOH F 6 .   ? -22.933 -11.695 13.956  1.00 20.36  ? 604 HOH A O   1 
HETATM 2398 O  O   . HOH F 6 .   ? -6.983  1.495   35.195  1.00 21.18  ? 605 HOH A O   1 
HETATM 2399 O  O   . HOH F 6 .   ? -23.901 -17.606 5.956   1.00 50.62  ? 606 HOH A O   1 
HETATM 2400 O  O   . HOH F 6 .   ? -7.444  -8.738  -2.493  1.00 28.01  ? 607 HOH A O   1 
HETATM 2401 O  O   . HOH F 6 .   ? -5.822  15.360  12.058  1.00 27.93  ? 608 HOH A O   1 
HETATM 2402 O  O   . HOH F 6 .   ? -24.622 11.948  6.183   1.00 27.03  ? 609 HOH A O   1 
HETATM 2403 O  O   . HOH F 6 .   ? -12.792 3.615   -6.847  1.00 31.31  ? 610 HOH A O   1 
HETATM 2404 O  O   . HOH F 6 .   ? -9.744  1.525   39.151  1.00 29.23  ? 611 HOH A O   1 
HETATM 2405 O  O   . HOH F 6 .   ? 6.978   -3.739  30.158  1.00 37.95  ? 612 HOH A O   1 
HETATM 2406 O  O   . HOH F 6 .   ? -25.579 3.613   35.070  1.00 48.04  ? 613 HOH A O   1 
HETATM 2407 O  O   . HOH F 6 .   ? 8.007   -8.673  -8.046  1.00 36.55  ? 614 HOH A O   1 
HETATM 2408 O  O   . HOH F 6 .   ? -6.467  6.650   10.502  1.00 23.29  ? 615 HOH A O   1 
HETATM 2409 O  O   . HOH F 6 .   ? -17.056 -1.050  40.298  1.00 32.29  ? 616 HOH A O   1 
HETATM 2410 O  O   . HOH F 6 .   ? -17.069 -11.576 36.586  1.00 34.38  ? 617 HOH A O   1 
HETATM 2411 O  O   . HOH F 6 .   ? -11.055 17.508  12.353  1.00 21.62  ? 618 HOH A O   1 
HETATM 2412 O  O   . HOH F 6 .   ? 0.411   19.500  17.657  1.00 37.13  ? 619 HOH A O   1 
HETATM 2413 O  O   . HOH F 6 .   ? -6.650  -8.689  -6.912  1.00 36.57  ? 620 HOH A O   1 
HETATM 2414 O  O   . HOH F 6 .   ? -17.779 19.887  17.571  1.00 22.91  ? 621 HOH A O   1 
HETATM 2415 O  O   . HOH F 6 .   ? -31.287 4.227   7.880   1.00 49.37  ? 622 HOH A O   1 
HETATM 2416 O  O   . HOH F 6 .   ? 12.880  -3.737  13.484  1.00 28.25  ? 623 HOH A O   1 
HETATM 2417 O  O   . HOH F 6 .   ? -8.223  18.940  10.544  1.00 22.83  ? 624 HOH A O   1 
HETATM 2418 O  O   . HOH F 6 .   ? -30.573 -7.114  22.531  1.00 29.92  ? 625 HOH A O   1 
HETATM 2419 O  O   . HOH F 6 .   ? -24.699 -9.538  1.903   1.00 25.84  ? 626 HOH A O   1 
HETATM 2420 O  O   . HOH F 6 .   ? -2.509  4.378   7.586   1.00 29.81  ? 627 HOH A O   1 
HETATM 2421 O  O   . HOH F 6 .   ? -16.712 -16.670 -3.939  1.00 43.83  ? 628 HOH A O   1 
HETATM 2422 O  O   . HOH F 6 .   ? -2.724  -14.892 32.885  1.00 28.82  ? 629 HOH A O   1 
HETATM 2423 O  O   . HOH F 6 .   ? 10.106  -2.607  13.906  1.00 25.27  ? 630 HOH A O   1 
HETATM 2424 O  O   . HOH F 6 .   ? -23.774 -0.272  31.847  1.00 37.45  ? 631 HOH A O   1 
HETATM 2425 O  O   . HOH F 6 .   ? -1.558  11.452  26.018  1.00 23.72  ? 632 HOH A O   1 
HETATM 2426 O  O   . HOH F 6 .   ? -18.620 12.243  13.100  1.00 30.99  ? 633 HOH A O   1 
HETATM 2427 O  O   . HOH F 6 .   ? -0.209  -15.491 27.381  1.00 36.47  ? 634 HOH A O   1 
HETATM 2428 O  O   . HOH F 6 .   ? -12.933 -17.265 16.962  1.00 10.53  ? 635 HOH A O   1 
HETATM 2429 O  O   . HOH F 6 .   ? 0.666   0.460   -6.745  1.00 35.37  ? 636 HOH A O   1 
HETATM 2430 O  O   . HOH F 6 .   ? -18.338 -9.057  34.706  1.00 41.09  ? 637 HOH A O   1 
HETATM 2431 O  O   . HOH F 6 .   ? -17.867 -20.771 -1.285  1.00 31.70  ? 638 HOH A O   1 
HETATM 2432 O  O   . HOH F 6 .   ? -7.219  16.574  10.675  1.00 30.47  ? 639 HOH A O   1 
HETATM 2433 O  O   . HOH F 6 .   ? 8.515   -4.692  23.699  1.00 26.32  ? 640 HOH A O   1 
HETATM 2434 O  O   . HOH F 6 .   ? 15.623  -10.114 14.791  1.00 53.97  ? 641 HOH A O   1 
HETATM 2435 O  O   . HOH F 6 .   ? -17.826 -12.112 31.788  1.00 33.94  ? 642 HOH A O   1 
HETATM 2436 O  O   . HOH F 6 .   ? -0.355  13.600  27.345  1.00 36.20  ? 643 HOH A O   1 
HETATM 2437 O  O   . HOH F 6 .   ? -1.267  4.441   -4.945  1.00 58.23  ? 644 HOH A O   1 
HETATM 2438 O  O   . HOH F 6 .   ? 9.686   -0.040  14.468  1.00 32.39  ? 645 HOH A O   1 
HETATM 2439 O  O   . HOH F 6 .   ? -4.229  -1.163  11.849  1.00 15.23  ? 646 HOH A O   1 
HETATM 2440 O  O   . HOH F 6 .   ? -8.242  21.763  21.814  1.00 12.11  ? 647 HOH A O   1 
HETATM 2441 O  O   . HOH F 6 .   ? 10.160  5.255   13.026  1.00 45.14  ? 648 HOH A O   1 
HETATM 2442 O  O   . HOH F 6 .   ? -15.342 -16.225 25.567  1.00 32.01  ? 649 HOH A O   1 
HETATM 2443 O  O   . HOH F 6 .   ? -3.036  17.577  14.122  1.00 31.14  ? 650 HOH A O   1 
HETATM 2444 O  O   . HOH F 6 .   ? -8.354  -17.599 35.011  1.00 23.20  ? 651 HOH A O   1 
HETATM 2445 O  O   . HOH F 6 .   ? -23.857 -3.377  4.073   1.00 42.45  ? 652 HOH A O   1 
HETATM 2446 O  O   . HOH F 6 .   ? 6.126   -11.069 15.316  1.00 32.12  ? 653 HOH A O   1 
HETATM 2447 O  O   . HOH F 6 .   ? -12.727 10.755  -5.320  1.00 32.99  ? 654 HOH A O   1 
HETATM 2448 O  O   . HOH F 6 .   ? -16.601 -14.672 28.956  1.00 30.86  ? 655 HOH A O   1 
HETATM 2449 O  O   . HOH F 6 .   ? 14.560  0.104   15.131  1.00 29.13  ? 656 HOH A O   1 
HETATM 2450 O  O   . HOH F 6 .   ? -21.768 -21.710 12.170  1.00 27.57  ? 657 HOH A O   1 
HETATM 2451 O  O   . HOH F 6 .   ? -12.544 6.768   31.277  1.00 29.34  ? 658 HOH A O   1 
HETATM 2452 O  O   . HOH F 6 .   ? -21.231 21.485  6.659   1.00 22.12  ? 659 HOH A O   1 
HETATM 2453 O  O   . HOH F 6 .   ? 2.778   -13.522 8.065   1.00 25.57  ? 660 HOH A O   1 
HETATM 2454 O  O   . HOH F 6 .   ? 1.071   2.991   1.792   1.00 32.99  ? 661 HOH A O   1 
HETATM 2455 O  O   . HOH F 6 .   ? -5.602  -12.723 -4.936  1.00 32.10  ? 662 HOH A O   1 
HETATM 2456 O  O   . HOH F 6 .   ? -1.399  -13.186 27.137  1.00 25.00  ? 663 HOH A O   1 
HETATM 2457 O  O   . HOH F 6 .   ? 15.221  -4.000  25.103  1.00 20.29  ? 664 HOH A O   1 
HETATM 2458 O  O   . HOH F 6 .   ? -25.147 8.632   26.086  1.00 36.41  ? 665 HOH A O   1 
HETATM 2459 O  O   . HOH F 6 .   ? 5.178   -10.977 18.971  1.00 34.17  ? 666 HOH A O   1 
HETATM 2460 O  O   . HOH F 6 .   ? -7.173  -17.424 32.374  1.00 30.59  ? 667 HOH A O   1 
HETATM 2461 O  O   . HOH F 6 .   ? -17.151 -13.953 37.806  1.00 27.18  ? 668 HOH A O   1 
HETATM 2462 O  O   . HOH F 6 .   ? 1.297   -10.139 29.257  1.00 34.94  ? 669 HOH A O   1 
HETATM 2463 O  O   . HOH F 6 .   ? -21.677 -21.513 17.270  1.00 32.96  ? 670 HOH A O   1 
HETATM 2464 O  O   . HOH F 6 .   ? -16.705 -17.754 24.211  1.00 24.31  ? 671 HOH A O   1 
HETATM 2465 O  O   . HOH F 6 .   ? 6.445   -5.570  27.385  1.00 40.42  ? 672 HOH A O   1 
HETATM 2466 O  O   . HOH F 6 .   ? -1.997  -17.570 25.698  1.00 24.12  ? 673 HOH A O   1 
HETATM 2467 O  O   . HOH F 6 .   ? 0.669   -15.869 24.161  1.00 31.57  ? 674 HOH A O   1 
HETATM 2468 O  O   . HOH F 6 .   ? -16.973 -18.015 20.187  1.00 21.08  ? 675 HOH A O   1 
HETATM 2469 O  O   . HOH F 6 .   ? -4.916  20.470  21.640  1.00 18.80  ? 676 HOH A O   1 
HETATM 2470 O  O   . HOH F 6 .   ? -19.947 -2.055  43.132  1.00 34.24  ? 677 HOH A O   1 
HETATM 2471 O  O   . HOH F 6 .   ? -27.330 -6.789  7.889   1.00 32.46  ? 678 HOH A O   1 
HETATM 2472 O  O   . HOH F 6 .   ? -10.628 4.876   31.015  1.00 20.43  ? 679 HOH A O   1 
HETATM 2473 O  O   . HOH F 6 .   ? -4.897  -9.641  33.530  1.00 28.62  ? 680 HOH A O   1 
HETATM 2474 O  O   . HOH F 6 .   ? -3.257  15.145  11.543  1.00 32.64  ? 681 HOH A O   1 
HETATM 2475 O  O   . HOH F 6 .   ? -2.152  -11.993 31.638  1.00 32.17  ? 682 HOH A O   1 
HETATM 2476 O  O   . HOH F 6 .   ? 3.299   -13.899 12.218  1.00 33.60  ? 683 HOH A O   1 
HETATM 2477 O  O   . HOH F 6 .   ? 15.270  -1.330  26.031  1.00 21.61  ? 684 HOH A O   1 
HETATM 2478 O  O   . HOH F 6 .   ? -10.932 -11.113 -2.898  1.00 39.76  ? 685 HOH A O   1 
HETATM 2479 O  O   . HOH F 6 .   ? 1.824   12.415  23.020  1.00 27.08  ? 686 HOH A O   1 
HETATM 2480 O  O   . HOH F 6 .   ? 4.216   6.977   13.258  1.00 37.69  ? 687 HOH A O   1 
HETATM 2481 O  O   . HOH F 6 .   ? -4.809  7.410   5.721   1.00 21.00  ? 688 HOH A O   1 
HETATM 2482 O  O   . HOH F 6 .   ? -6.046  20.255  26.378  1.00 27.03  ? 689 HOH A O   1 
HETATM 2483 O  O   . HOH F 6 .   ? -1.133  -13.308 33.232  1.00 24.57  ? 690 HOH A O   1 
HETATM 2484 O  O   . HOH F 6 .   ? 1.640   -16.335 18.166  1.00 44.33  ? 691 HOH A O   1 
HETATM 2485 O  O   . HOH F 6 .   ? 14.622  2.832   23.915  1.00 28.49  ? 692 HOH A O   1 
HETATM 2486 O  O   . HOH F 6 .   ? -31.721 -10.909 16.240  1.00 24.42  ? 693 HOH A O   1 
HETATM 2487 O  O   . HOH F 6 .   ? -10.452 22.849  17.214  1.00 10.64  ? 694 HOH A O   1 
HETATM 2488 O  O   . HOH F 6 .   ? 2.976   1.029   -6.296  1.00 26.89  ? 695 HOH A O   1 
HETATM 2489 O  O   . HOH F 6 .   ? -13.969 3.608   33.270  1.00 26.93  ? 696 HOH A O   1 
HETATM 2490 O  O   . HOH F 6 .   ? -28.037 5.177   25.718  1.00 31.72  ? 697 HOH A O   1 
HETATM 2491 O  O   . HOH F 6 .   ? -16.173 16.893  26.404  1.00 34.14  ? 698 HOH A O   1 
HETATM 2492 O  O   . HOH F 6 .   ? -11.548 1.176   -7.648  1.00 33.38  ? 699 HOH A O   1 
HETATM 2493 O  O   . HOH F 6 .   ? -18.946 -0.837  -2.522  1.00 35.64  ? 700 HOH A O   1 
HETATM 2494 O  O   . HOH F 6 .   ? 1.523   -17.593 7.247   1.00 31.72  ? 701 HOH A O   1 
HETATM 2495 O  O   . HOH F 6 .   ? -8.201  7.449   8.201   1.00 26.60  ? 702 HOH A O   1 
HETATM 2496 O  O   . HOH F 6 .   ? 2.023   -14.235 20.743  1.00 34.85  ? 703 HOH A O   1 
HETATM 2497 O  O   . HOH F 6 .   ? -8.055  14.504  10.482  1.00 29.25  ? 704 HOH A O   1 
HETATM 2498 O  O   . HOH F 6 .   ? -10.643 -20.415 25.117  1.00 16.53  ? 705 HOH A O   1 
HETATM 2499 O  O   . HOH F 6 .   ? 1.350   9.648   26.958  1.00 32.20  ? 706 HOH A O   1 
HETATM 2500 O  O   . HOH F 6 .   ? 3.308   2.598   0.028   1.00 34.29  ? 707 HOH A O   1 
HETATM 2501 O  O   . HOH F 6 .   ? -1.146  -11.200 29.024  1.00 16.43  ? 708 HOH A O   1 
HETATM 2502 O  O   . HOH F 6 .   ? -0.366  -7.054  -7.605  1.00 37.25  ? 709 HOH A O   1 
HETATM 2503 O  O   . HOH F 6 .   ? 3.388   6.537   32.210  1.00 48.24  ? 710 HOH A O   1 
HETATM 2504 O  O   . HOH F 6 .   ? -21.235 -20.668 14.709  1.00 28.62  ? 711 HOH A O   1 
HETATM 2505 O  O   . HOH F 6 .   ? -3.988  -15.702 -2.418  1.00 32.89  ? 712 HOH A O   1 
HETATM 2506 O  O   . HOH F 6 .   ? -14.995 8.054   34.756  1.00 40.94  ? 713 HOH A O   1 
HETATM 2507 O  O   . HOH F 6 .   ? -7.197  -10.274 -4.652  1.00 29.30  ? 714 HOH A O   1 
HETATM 2508 O  O   . HOH F 6 .   ? 1.529   5.049   5.127   1.00 40.42  ? 715 HOH A O   1 
HETATM 2509 O  O   . HOH F 6 .   ? 1.506   12.804  17.522  1.00 32.55  ? 716 HOH A O   1 
HETATM 2510 O  O   . HOH F 6 .   ? 6.388   -5.530  3.876   1.00 30.95  ? 717 HOH A O   1 
HETATM 2511 O  O   . HOH F 6 .   ? -5.970  -18.244 3.451   1.00 30.58  ? 718 HOH A O   1 
HETATM 2512 O  O   . HOH F 6 .   ? 1.826   14.007  27.405  1.00 35.59  ? 719 HOH A O   1 
HETATM 2513 O  O   . HOH F 6 .   ? 6.670   8.274   18.097  1.00 27.22  ? 720 HOH A O   1 
HETATM 2514 O  O   . HOH F 6 .   ? -12.933 -19.601 26.252  1.00 19.86  ? 721 HOH A O   1 
HETATM 2515 O  O   . HOH F 6 .   ? -1.664  16.344  12.484  1.00 32.71  ? 722 HOH A O   1 
HETATM 2516 O  O   . HOH F 6 .   ? 5.488   9.032   21.861  1.00 29.65  ? 723 HOH A O   1 
HETATM 2517 O  O   . HOH F 6 .   ? 14.011  -1.362  28.514  1.00 30.94  ? 724 HOH A O   1 
HETATM 2518 O  O   . HOH F 6 .   ? 3.753   9.843   23.860  1.00 26.44  ? 725 HOH A O   1 
HETATM 2519 O  O   . HOH F 6 .   ? -6.739  9.991   8.085   1.00 31.01  ? 726 HOH A O   1 
HETATM 2520 O  O   . HOH F 6 .   ? -34.149 -9.574  16.779  1.00 22.53  ? 727 HOH A O   1 
HETATM 2521 O  O   . HOH F 6 .   ? -4.193  9.183   7.533   1.00 34.25  ? 728 HOH A O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N  N   A HIS A 4   ? 0.5527 0.2565 0.4521 0.0579  0.1605  -0.0284 4   HIS A N   
2    N  N   B HIS A 4   ? 0.0701 0.6243 0.3987 0.0685  0.0220  -0.1071 4   HIS A N   
3    C  CA  A HIS A 4   ? 0.2302 0.2746 0.4362 -0.0396 0.1189  0.1374  4   HIS A CA  
4    C  CA  B HIS A 4   ? 0.1834 0.3828 0.3802 0.0004  0.1393  0.0401  4   HIS A CA  
5    C  C   A HIS A 4   ? 0.1950 0.2135 0.2733 -0.0730 0.0982  0.0183  4   HIS A C   
6    C  C   B HIS A 4   ? 0.1318 0.3123 0.3418 0.0034  0.0653  -0.0262 4   HIS A C   
7    O  O   A HIS A 4   ? 0.1313 0.2124 0.2949 -0.0357 0.1075  -0.0077 4   HIS A O   
8    O  O   B HIS A 4   ? 0.1421 0.2520 0.4728 -0.0675 -0.0118 0.0554  4   HIS A O   
9    C  CB  A HIS A 4   ? 0.1433 0.2723 0.5871 0.0464  0.1133  0.1103  4   HIS A CB  
10   C  CB  B HIS A 4   ? 0.2329 0.5317 0.3486 0.0543  0.1265  0.0451  4   HIS A CB  
11   C  CG  A HIS A 4   ? 0.2133 0.3273 0.4014 0.1058  -0.1590 0.0659  4   HIS A CG  
12   C  CG  B HIS A 4   ? 0.3057 0.2689 0.5549 -0.1187 0.0127  0.0869  4   HIS A CG  
13   N  ND1 A HIS A 4   ? 0.1889 0.3503 0.7137 -0.0958 -0.0617 -0.0741 4   HIS A ND1 
14   N  ND1 B HIS A 4   ? 0.2522 0.3556 0.4189 0.0376  -0.0361 0.1110  4   HIS A ND1 
15   C  CD2 A HIS A 4   ? 0.0807 0.2058 0.2060 -0.0469 -0.0847 0.0817  4   HIS A CD2 
16   C  CD2 B HIS A 4   ? 0.3739 0.5272 0.7106 -0.0189 -0.0561 0.0508  4   HIS A CD2 
17   C  CE1 A HIS A 4   ? 0.2209 0.6994 0.9820 0.1130  0.0998  0.0531  4   HIS A CE1 
18   C  CE1 B HIS A 4   ? 0.3628 0.3502 0.5807 0.1747  -0.0758 -0.1644 4   HIS A CE1 
19   N  NE2 A HIS A 4   ? 0.5948 0.3831 0.4275 -0.0179 -0.0469 -0.0761 4   HIS A NE2 
20   N  NE2 B HIS A 4   ? 0.3316 0.3574 0.8274 0.1366  -0.1225 -0.0033 4   HIS A NE2 
21   N  N   . TRP A 5   ? 0.1661 0.2037 0.3459 -0.0114 0.1083  0.0186  5   TRP A N   
22   C  CA  . TRP A 5   ? 0.1011 0.1794 0.2536 -0.0177 0.0681  0.0126  5   TRP A CA  
23   C  C   . TRP A 5   ? 0.1345 0.1672 0.2478 -0.0061 0.0829  -0.0193 5   TRP A C   
24   O  O   . TRP A 5   ? 0.1782 0.1816 0.2591 -0.0295 0.0872  0.0034  5   TRP A O   
25   C  CB  . TRP A 5   ? 0.1119 0.1658 0.3258 -0.0094 0.0694  -0.0351 5   TRP A CB  
26   C  CG  . TRP A 5   ? 0.1257 0.1652 0.1909 -0.0307 0.0622  -0.0067 5   TRP A CG  
27   C  CD1 . TRP A 5   ? 0.1548 0.1746 0.2464 -0.0265 0.0696  0.0142  5   TRP A CD1 
28   C  CD2 . TRP A 5   ? 0.1002 0.1769 0.1807 0.0044  0.0541  -0.0186 5   TRP A CD2 
29   N  NE1 . TRP A 5   ? 0.1843 0.1620 0.2010 0.0051  0.0479  0.0117  5   TRP A NE1 
30   C  CE2 . TRP A 5   ? 0.1340 0.1857 0.1830 0.0109  0.0219  -0.0237 5   TRP A CE2 
31   C  CE3 . TRP A 5   ? 0.1070 0.1791 0.1816 -0.0310 0.0509  -0.0398 5   TRP A CE3 
32   C  CZ2 . TRP A 5   ? 0.1404 0.1972 0.1613 0.0122  0.0155  -0.0229 5   TRP A CZ2 
33   C  CZ3 . TRP A 5   ? 0.1178 0.1886 0.1505 -0.0183 0.0254  -0.0609 5   TRP A CZ3 
34   C  CH2 . TRP A 5   ? 0.1097 0.2168 0.1584 0.0080  0.0135  -0.0603 5   TRP A CH2 
35   N  N   . GLY A 6   ? 0.1356 0.1399 0.2293 -0.0146 0.0945  -0.0259 6   GLY A N   
36   C  CA  . GLY A 6   ? 0.1729 0.1331 0.2250 -0.0408 0.1026  -0.0401 6   GLY A CA  
37   C  C   . GLY A 6   ? 0.1227 0.1706 0.2403 -0.0177 0.1171  -0.0347 6   GLY A C   
38   O  O   . GLY A 6   ? 0.1187 0.1482 0.2144 0.0113  0.0811  0.0064  6   GLY A O   
39   N  N   . TYR A 7   ? 0.1643 0.1559 0.3082 -0.0346 0.1486  -0.0525 7   TYR A N   
40   C  CA  . TYR A 7   ? 0.1609 0.1196 0.3573 -0.0093 0.1437  -0.0372 7   TYR A CA  
41   C  C   . TYR A 7   ? 0.1717 0.1661 0.3924 -0.0176 0.1163  -0.0515 7   TYR A C   
42   O  O   . TYR A 7   ? 0.2028 0.1670 0.5845 -0.0115 0.1822  -0.0545 7   TYR A O   
43   C  CB  . TYR A 7   ? 0.1654 0.1435 0.2938 -0.0259 0.1251  -0.0571 7   TYR A CB  
44   C  CG  . TYR A 7   ? 0.1059 0.1311 0.1857 -0.0325 0.0697  -0.0486 7   TYR A CG  
45   C  CD1 . TYR A 7   ? 0.0803 0.1236 0.1893 -0.0269 0.0423  -0.0353 7   TYR A CD1 
46   C  CD2 . TYR A 7   ? 0.1622 0.1142 0.1916 -0.0417 0.0604  -0.0307 7   TYR A CD2 
47   C  CE1 . TYR A 7   ? 0.0776 0.1070 0.1650 -0.0185 0.0258  -0.0230 7   TYR A CE1 
48   C  CE2 . TYR A 7   ? 0.1081 0.1473 0.1498 -0.0233 0.0387  -0.0408 7   TYR A CE2 
49   C  CZ  . TYR A 7   ? 0.0981 0.1142 0.1297 -0.0122 0.0240  -0.0253 7   TYR A CZ  
50   O  OH  . TYR A 7   ? 0.1063 0.1186 0.1311 -0.0027 0.0210  -0.0176 7   TYR A OH  
51   N  N   . GLY A 8   ? 0.2028 0.1859 0.4313 0.0043  0.1726  -0.0695 8   GLY A N   
52   C  CA  . GLY A 8   ? 0.1230 0.2046 0.2891 0.0017  0.0252  -0.0792 8   GLY A CA  
53   C  C   . GLY A 8   ? 0.1561 0.2735 0.2584 -0.0278 0.0741  -0.0780 8   GLY A C   
54   O  O   . GLY A 8   ? 0.2315 0.2426 0.4322 -0.0614 0.1766  -0.1609 8   GLY A O   
55   N  N   . LYS A 9   ? 0.1713 0.2654 0.3596 -0.0146 0.1156  -0.0846 9   LYS A N   
56   C  CA  . LYS A 9   ? 0.2649 0.2636 0.3565 0.0092  -0.0759 -0.0455 9   LYS A CA  
57   C  C   . LYS A 9   ? 0.1311 0.2239 0.3209 0.0141  0.0301  -0.0286 9   LYS A C   
58   O  O   . LYS A 9   ? 0.1717 0.3661 0.3231 -0.0567 0.0333  -0.0295 9   LYS A O   
59   C  CB  . LYS A 9   ? 0.2347 0.4774 0.3456 0.0619  -0.1259 -0.0551 9   LYS A CB  
60   N  N   . HIS A 10  ? 0.2243 0.1977 0.4535 0.0761  0.1085  -0.0769 10  HIS A N   
61   C  CA  . HIS A 10  ? 0.2365 0.1888 0.4337 0.0092  0.2002  0.0055  10  HIS A CA  
62   C  C   . HIS A 10  ? 0.2074 0.1771 0.3718 0.0511  0.1559  -0.0172 10  HIS A C   
63   O  O   . HIS A 10  ? 0.1778 0.2597 0.4423 0.0831  0.1592  0.0509  10  HIS A O   
64   C  CB  . HIS A 10  ? 0.1584 0.1961 0.4381 0.0376  0.1599  0.0521  10  HIS A CB  
65   C  CG  . HIS A 10  ? 0.1643 0.2937 0.2216 0.0148  -0.0182 -0.0025 10  HIS A CG  
66   N  ND1 . HIS A 10  ? 0.1559 0.2979 0.3138 0.0277  -0.0033 -0.0149 10  HIS A ND1 
67   C  CD2 . HIS A 10  ? 0.2317 0.2881 0.3040 0.0161  0.1482  -0.1080 10  HIS A CD2 
68   C  CE1 . HIS A 10  ? 0.3203 0.2549 0.3102 0.1442  -0.0416 0.0145  10  HIS A CE1 
69   N  NE2 . HIS A 10  ? 0.1435 0.2983 0.2751 0.0086  0.0715  -0.0273 10  HIS A NE2 
70   N  N   . ASN A 11  ? 0.1945 0.1909 0.5170 0.0378  0.2014  0.0247  11  ASN A N   
71   C  CA  . ASN A 11  ? 0.1482 0.2069 0.3462 0.0443  0.1512  -0.0023 11  ASN A CA  
72   C  C   . ASN A 11  ? 0.1282 0.1749 0.2743 0.0417  0.1166  0.0211  11  ASN A C   
73   O  O   . ASN A 11  ? 0.1140 0.1862 0.3007 0.0496  0.1158  0.0223  11  ASN A O   
74   C  CB  . ASN A 11  ? 0.1252 0.2019 0.3349 0.0002  0.1524  -0.0160 11  ASN A CB  
75   C  CG  . ASN A 11  ? 0.1764 0.1918 0.3061 0.0051  0.1420  -0.0442 11  ASN A CG  
76   O  OD1 . ASN A 11  ? 0.1771 0.1993 0.4125 -0.0269 0.1312  0.0043  11  ASN A OD1 
77   N  ND2 . ASN A 11  ? 0.2042 0.2094 0.3258 -0.0114 0.1155  0.0122  11  ASN A ND2 
78   N  N   . GLY A 12  ? 0.1342 0.1792 0.2866 0.0072  0.1223  0.0138  12  GLY A N   
79   C  CA  . GLY A 12  ? 0.0943 0.2117 0.2620 0.0245  0.0983  -0.0194 12  GLY A CA  
80   C  C   . GLY A 12  ? 0.1113 0.1527 0.2399 0.0237  0.0814  0.0386  12  GLY A C   
81   O  O   . GLY A 12  ? 0.0920 0.1386 0.3146 0.0119  0.0658  0.0184  12  GLY A O   
82   N  N   . PRO A 13  ? 0.0952 0.1338 0.2414 -0.0038 0.0806  -0.0100 13  PRO A N   
83   C  CA  . PRO A 13  ? 0.1038 0.1577 0.2451 -0.0173 0.0724  -0.0127 13  PRO A CA  
84   C  C   . PRO A 13  ? 0.1419 0.1392 0.2293 0.0120  0.0704  -0.0164 13  PRO A C   
85   O  O   . PRO A 13  ? 0.0670 0.1844 0.2603 -0.0078 0.0476  -0.0336 13  PRO A O   
86   C  CB  . PRO A 13  ? 0.1137 0.1620 0.2410 -0.0326 0.0762  -0.0372 13  PRO A CB  
87   C  CG  . PRO A 13  ? 0.1150 0.1747 0.2279 -0.0372 0.0762  -0.0438 13  PRO A CG  
88   C  CD  . PRO A 13  ? 0.1034 0.1735 0.2315 -0.0027 0.0910  -0.0025 13  PRO A CD  
89   N  N   . GLU A 14  ? 0.1282 0.1252 0.3204 -0.0102 0.0828  0.0034  14  GLU A N   
90   C  CA  . GLU A 14  ? 0.1316 0.1828 0.3387 0.0214  0.0696  0.0264  14  GLU A CA  
91   C  C   . GLU A 14  ? 0.1020 0.1704 0.2748 0.0158  0.0542  -0.0092 14  GLU A C   
92   O  O   . GLU A 14  ? 0.1482 0.1830 0.3335 0.0119  0.0334  0.0429  14  GLU A O   
93   C  CB  . GLU A 14  ? 0.2524 0.1855 0.4466 0.0039  -0.0127 0.0863  14  GLU A CB  
94   C  CG  . GLU A 14  ? 0.3018 0.2709 0.4950 -0.0198 0.0890  0.0531  14  GLU A CG  
95   C  CD  . GLU A 14  ? 0.6876 0.4242 0.5413 0.0022  0.0871  -0.0093 14  GLU A CD  
96   O  OE1 . GLU A 14  ? 0.3287 0.4258 0.4856 0.0359  -0.0303 0.0306  14  GLU A OE1 
97   O  OE2 . GLU A 14  ? 0.3250 0.4196 0.5283 0.0170  0.0018  0.0168  14  GLU A OE2 
98   N  N   . HIS A 15  ? 0.0818 0.1755 0.2892 0.0182  0.0646  -0.0061 15  HIS A N   
99   C  CA  . HIS A 15  ? 0.0696 0.1561 0.3012 0.0183  0.0346  -0.0198 15  HIS A CA  
100  C  C   . HIS A 15  ? 0.0523 0.1460 0.3120 0.0120  0.0518  -0.0171 15  HIS A C   
101  O  O   . HIS A 15  ? 0.0427 0.1685 0.3207 0.0114  0.0387  0.0218  15  HIS A O   
102  C  CB  . HIS A 15  ? 0.0679 0.1738 0.2977 0.0367  0.0440  0.0271  15  HIS A CB  
103  C  CG  . HIS A 15  ? 0.1286 0.1726 0.3186 0.0212  0.0961  0.0282  15  HIS A CG  
104  N  ND1 . HIS A 15  ? 0.1347 0.2577 0.3181 0.0853  0.0524  -0.0177 15  HIS A ND1 
105  C  CD2 . HIS A 15  ? 0.1586 0.1778 0.3459 0.0581  0.0735  -0.0106 15  HIS A CD2 
106  C  CE1 . HIS A 15  ? 0.3107 0.2951 0.2389 0.1209  0.0005  -0.0249 15  HIS A CE1 
107  N  NE2 . HIS A 15  ? 0.2398 0.2026 0.3808 0.0972  0.1068  -0.0035 15  HIS A NE2 
108  N  N   . TRP A 16  ? 0.0507 0.1410 0.2507 0.0076  0.0340  0.0035  16  TRP A N   
109  C  CA  . TRP A 16  ? 0.0303 0.1164 0.2537 0.0061  0.0256  -0.0041 16  TRP A CA  
110  C  C   . TRP A 16  ? 0.0441 0.1394 0.2311 0.0095  0.0245  0.0126  16  TRP A C   
111  O  O   . TRP A 16  ? 0.0528 0.1458 0.2586 0.0037  -0.0104 0.0039  16  TRP A O   
112  C  CB  . TRP A 16  ? 0.0297 0.1620 0.2238 0.0038  0.0212  -0.0383 16  TRP A CB  
113  C  CG  . TRP A 16  ? 0.0538 0.1230 0.2019 0.0002  0.0220  -0.0172 16  TRP A CG  
114  C  CD1 . TRP A 16  ? 0.0860 0.1530 0.1830 0.0062  0.0326  0.0159  16  TRP A CD1 
115  C  CD2 . TRP A 16  ? 0.0481 0.1202 0.2146 0.0133  0.0408  -0.0063 16  TRP A CD2 
116  N  NE1 . TRP A 16  ? 0.0708 0.1372 0.2121 0.0004  0.0480  -0.0201 16  TRP A NE1 
117  C  CE2 . TRP A 16  ? 0.0643 0.1217 0.1947 0.0066  0.0485  -0.0086 16  TRP A CE2 
118  C  CE3 . TRP A 16  ? 0.0442 0.1241 0.2053 0.0093  0.0312  -0.0050 16  TRP A CE3 
119  C  CZ2 . TRP A 16  ? 0.0756 0.1114 0.1857 -0.0018 0.0446  0.0023  16  TRP A CZ2 
120  C  CZ3 . TRP A 16  ? 0.0499 0.1480 0.1936 0.0020  0.0419  -0.0273 16  TRP A CZ3 
121  C  CH2 . TRP A 16  ? 0.0731 0.1261 0.1985 0.0000  0.0483  -0.0207 16  TRP A CH2 
122  N  N   . HIS A 17  ? 0.0385 0.1555 0.2388 -0.0005 -0.0040 -0.0199 17  HIS A N   
123  C  CA  . HIS A 17  ? 0.0273 0.1703 0.2527 -0.0024 -0.0078 0.0155  17  HIS A CA  
124  C  C   . HIS A 17  ? 0.0430 0.1859 0.2842 -0.0086 0.0054  0.0166  17  HIS A C   
125  O  O   . HIS A 17  ? 0.0550 0.1882 0.3025 -0.0093 -0.0098 0.0093  17  HIS A O   
126  C  CB  . HIS A 17  ? 0.0379 0.1974 0.2529 0.0086  -0.0002 0.0133  17  HIS A CB  
127  C  CG  . HIS A 17  ? 0.0613 0.1970 0.2656 0.0041  0.0022  0.0194  17  HIS A CG  
128  N  ND1 . HIS A 17  ? 0.0622 0.2394 0.3578 0.0022  -0.0270 0.0445  17  HIS A ND1 
129  C  CD2 . HIS A 17  ? 0.0775 0.2011 0.3109 0.0344  0.0370  0.0418  17  HIS A CD2 
130  C  CE1 . HIS A 17  ? 0.1061 0.2356 0.3827 0.0385  0.0269  0.0392  17  HIS A CE1 
131  N  NE2 . HIS A 17  ? 0.0965 0.2268 0.2963 0.0517  0.0232  0.0572  17  HIS A NE2 
132  N  N   . LYS A 18  ? 0.0243 0.1823 0.3269 0.0029  0.0171  0.0233  18  LYS A N   
133  C  CA  . LYS A 18  ? 0.0343 0.2092 0.3244 -0.0031 0.0199  0.0548  18  LYS A CA  
134  C  C   . LYS A 18  ? 0.0421 0.2365 0.3394 -0.0299 0.0043  0.0609  18  LYS A C   
135  O  O   . LYS A 18  ? 0.0941 0.2399 0.5228 -0.0565 -0.0779 0.1153  18  LYS A O   
136  C  CB  . LYS A 18  ? 0.0725 0.2114 0.3224 0.0041  0.0306  0.0734  18  LYS A CB  
137  C  CG  . LYS A 18  ? 0.0674 0.1979 0.3948 0.0355  0.0302  0.0428  18  LYS A CG  
138  C  CD  . LYS A 18  ? 0.0590 0.2518 0.3068 0.0269  0.0125  0.0623  18  LYS A CD  
139  C  CE  . LYS A 18  ? 0.0746 0.2153 0.3132 0.0385  0.0229  0.0590  18  LYS A CE  
140  N  NZ  . LYS A 18  ? 0.0560 0.2779 0.3198 0.0706  0.0474  0.1035  18  LYS A NZ  
141  N  N   . ASP A 19  ? 0.0674 0.1976 0.2957 0.0034  0.0062  0.0528  19  ASP A N   
142  C  CA  . ASP A 19  ? 0.0804 0.1902 0.3283 -0.0046 0.0266  0.0539  19  ASP A CA  
143  C  C   . ASP A 19  ? 0.0712 0.1516 0.3369 -0.0157 0.0409  0.0143  19  ASP A C   
144  O  O   . ASP A 19  ? 0.0930 0.1550 0.3629 -0.0128 0.0369  0.0497  19  ASP A O   
145  C  CB  . ASP A 19  ? 0.1147 0.2856 0.3072 0.0320  -0.0009 0.0463  19  ASP A CB  
146  C  CG  . ASP A 19  ? 0.1372 0.3602 0.3216 0.0167  0.0104  -0.0350 19  ASP A CG  
147  O  OD1 . ASP A 19  ? 0.1485 0.5153 0.5179 -0.0706 0.0666  0.0373  19  ASP A OD1 
148  O  OD2 . ASP A 19  ? 0.4050 0.6133 0.4850 -0.1077 0.0589  -0.2109 19  ASP A OD2 
149  N  N   . PHE A 20  ? 0.0484 0.1690 0.2769 -0.0179 0.0040  0.0111  20  PHE A N   
150  C  CA  . PHE A 20  ? 0.0481 0.1627 0.2721 -0.0063 0.0114  0.0018  20  PHE A CA  
151  C  C   . PHE A 20  ? 0.0416 0.1647 0.2683 -0.0155 0.0206  -0.0145 20  PHE A C   
152  O  O   . PHE A 20  ? 0.0657 0.1496 0.2381 -0.0089 0.0036  0.0012  20  PHE A O   
153  C  CB  . PHE A 20  ? 0.0610 0.1870 0.2689 -0.0307 0.0093  0.0008  20  PHE A CB  
154  C  CG  . PHE A 20  ? 0.0546 0.2049 0.2658 -0.0386 0.0026  0.0289  20  PHE A CG  
155  C  CD1 . PHE A 20  ? 0.0792 0.2419 0.3010 -0.0392 0.0100  0.0715  20  PHE A CD1 
156  C  CD2 . PHE A 20  ? 0.0961 0.2394 0.2693 -0.0441 0.0245  0.0179  20  PHE A CD2 
157  C  CE1 . PHE A 20  ? 0.0975 0.2390 0.2843 -0.0211 0.0134  0.0575  20  PHE A CE1 
158  C  CE2 . PHE A 20  ? 0.0670 0.2581 0.3123 -0.0104 0.0317  0.0312  20  PHE A CE2 
159  C  CZ  . PHE A 20  ? 0.0788 0.2594 0.3143 -0.0359 0.0258  0.0387  20  PHE A CZ  
160  N  N   . PRO A 21  ? 0.0770 0.1649 0.2724 -0.0238 -0.0162 0.0072  21  PRO A N   
161  C  CA  . PRO A 21  ? 0.0564 0.1914 0.2545 -0.0341 -0.0222 -0.0184 21  PRO A CA  
162  C  C   . PRO A 21  ? 0.0757 0.1706 0.2356 -0.0163 -0.0374 -0.0230 21  PRO A C   
163  O  O   . PRO A 21  ? 0.0533 0.1979 0.2603 -0.0134 -0.0457 -0.0079 21  PRO A O   
164  C  CB  . PRO A 21  ? 0.0905 0.2901 0.3268 -0.0927 -0.0475 0.0281  21  PRO A CB  
165  C  CG  . PRO A 21  ? 0.2654 0.2806 0.3860 -0.1372 -0.1259 0.0182  21  PRO A CG  
166  C  CD  . PRO A 21  ? 0.0803 0.1859 0.3161 -0.0452 -0.0061 0.0132  21  PRO A CD  
167  N  N   A ILE A 22  ? 0.0464 0.1681 0.1751 -0.0227 -0.0425 -0.0541 22  ILE A N   
168  N  N   B ILE A 22  ? 0.0398 0.1489 0.2058 -0.0201 -0.0103 -0.0324 22  ILE A N   
169  C  CA  A ILE A 22  ? 0.0664 0.1570 0.1679 -0.0062 -0.0179 -0.0182 22  ILE A CA  
170  C  CA  B ILE A 22  ? 0.0330 0.1525 0.2028 -0.0086 -0.0134 0.0008  22  ILE A CA  
171  C  C   A ILE A 22  ? 0.0692 0.1455 0.2022 -0.0080 -0.0425 -0.0339 22  ILE A C   
172  C  C   B ILE A 22  ? 0.0436 0.1539 0.2284 -0.0197 -0.0239 -0.0291 22  ILE A C   
173  O  O   A ILE A 22  ? 0.0589 0.1615 0.2249 -0.0120 -0.0254 -0.0399 22  ILE A O   
174  O  O   B ILE A 22  ? 0.0445 0.1521 0.2169 -0.0110 -0.0185 -0.0229 22  ILE A O   
175  C  CB  A ILE A 22  ? 0.0693 0.1476 0.1309 -0.0043 -0.0097 -0.0145 22  ILE A CB  
176  C  CB  B ILE A 22  ? 0.0225 0.1534 0.1559 -0.0218 -0.0260 -0.0048 22  ILE A CB  
177  C  CG1 A ILE A 22  ? 0.0851 0.1318 0.1543 -0.0050 0.0083  -0.0172 22  ILE A CG1 
178  C  CG1 B ILE A 22  ? 0.1054 0.1798 0.1765 0.0212  0.0275  0.0085  22  ILE A CG1 
179  C  CG2 A ILE A 22  ? 0.1129 0.1430 0.1069 -0.0499 -0.0297 0.0199  22  ILE A CG2 
180  C  CG2 B ILE A 22  ? 0.0867 0.1794 0.1437 -0.0348 -0.0217 0.0098  22  ILE A CG2 
181  C  CD1 A ILE A 22  ? 0.1061 0.1306 0.2335 -0.0062 -0.0303 -0.0185 22  ILE A CD1 
182  C  CD1 B ILE A 22  ? 0.1742 0.2110 0.2669 0.0254  -0.0844 0.0080  22  ILE A CD1 
183  N  N   . ALA A 23  ? 0.0597 0.1444 0.2008 -0.0160 -0.0257 -0.0054 23  ALA A N   
184  C  CA  . ALA A 23  ? 0.0807 0.1259 0.2155 -0.0027 0.0008  -0.0138 23  ALA A CA  
185  C  C   . ALA A 23  ? 0.0525 0.1465 0.2311 0.0042  -0.0116 -0.0231 23  ALA A C   
186  O  O   . ALA A 23  ? 0.0700 0.1620 0.2130 -0.0182 -0.0122 -0.0111 23  ALA A O   
187  C  CB  . ALA A 23  ? 0.0292 0.1724 0.2425 0.0082  -0.0310 -0.0262 23  ALA A CB  
188  N  N   . LYS A 24  ? 0.0781 0.1672 0.2026 0.0102  -0.0363 -0.0032 24  LYS A N   
189  C  CA  . LYS A 24  ? 0.0615 0.1904 0.2275 -0.0043 -0.0316 -0.0221 24  LYS A CA  
190  C  C   . LYS A 24  ? 0.1045 0.2200 0.2130 -0.0159 -0.0656 -0.0324 24  LYS A C   
191  O  O   . LYS A 24  ? 0.1040 0.2595 0.2362 -0.0144 -0.0581 -0.0139 24  LYS A O   
192  C  CB  . LYS A 24  ? 0.0783 0.2272 0.2715 0.0190  -0.0229 0.0257  24  LYS A CB  
193  C  CG  . LYS A 24  ? 0.1029 0.2555 0.2531 0.0535  -0.0127 0.0201  24  LYS A CG  
194  C  CD  . LYS A 24  ? 0.0943 0.3608 0.3630 0.0774  0.0027  0.0062  24  LYS A CD  
195  C  CE  . LYS A 24  ? 0.1361 0.3160 0.3740 0.0375  0.0129  0.0194  24  LYS A CE  
196  N  NZ  . LYS A 24  ? 0.2013 0.3536 0.5662 -0.0604 0.0895  -0.1108 24  LYS A NZ  
197  N  N   . GLY A 25  ? 0.0869 0.1861 0.2394 0.0089  -0.0419 -0.0342 25  GLY A N   
198  C  CA  . GLY A 25  ? 0.1002 0.2037 0.2451 -0.0159 -0.0102 -0.0523 25  GLY A CA  
199  C  C   . GLY A 25  ? 0.0887 0.1986 0.1593 0.0072  -0.0409 -0.0425 25  GLY A C   
200  O  O   . GLY A 25  ? 0.1092 0.2139 0.1918 0.0015  -0.0567 -0.0310 25  GLY A O   
201  N  N   . GLU A 26  ? 0.0910 0.2397 0.1729 0.0023  -0.0652 -0.0414 26  GLU A N   
202  C  CA  . GLU A 26  ? 0.1279 0.2579 0.1579 -0.0087 -0.0511 -0.0442 26  GLU A CA  
203  C  C   . GLU A 26  ? 0.0941 0.2139 0.1257 0.0148  -0.0451 -0.0347 26  GLU A C   
204  O  O   . GLU A 26  ? 0.1543 0.2340 0.1190 -0.0114 -0.0606 -0.0130 26  GLU A O   
205  C  CB  . GLU A 26  ? 0.1543 0.2615 0.1758 -0.0226 -0.0662 -0.0935 26  GLU A CB  
206  C  CG  . GLU A 26  ? 0.1938 0.3204 0.1918 0.0096  -0.0893 -0.0449 26  GLU A CG  
207  C  CD  . GLU A 26  ? 0.2931 0.3323 0.2694 0.0154  -0.1791 -0.0551 26  GLU A CD  
208  O  OE1 . GLU A 26  ? 0.3131 0.4684 0.3944 -0.0247 -0.1321 -0.0098 26  GLU A OE1 
209  O  OE2 . GLU A 26  ? 0.2666 0.4935 0.4921 0.0702  -0.0957 -0.0417 26  GLU A OE2 
210  N  N   . ARG A 27  ? 0.0984 0.1449 0.1254 -0.0008 -0.0517 -0.0272 27  ARG A N   
211  C  CA  . ARG A 27  ? 0.0773 0.1379 0.1176 0.0108  -0.0395 -0.0283 27  ARG A CA  
212  C  C   . ARG A 27  ? 0.0754 0.1273 0.1054 0.0003  -0.0294 -0.0320 27  ARG A C   
213  O  O   . ARG A 27  ? 0.0699 0.1367 0.1154 0.0132  -0.0336 -0.0178 27  ARG A O   
214  C  CB  . ARG A 27  ? 0.1376 0.1631 0.1186 0.0154  -0.0395 -0.0438 27  ARG A CB  
215  C  CG  . ARG A 27  ? 0.1753 0.1934 0.1600 -0.0139 -0.0161 -0.0218 27  ARG A CG  
216  C  CD  . ARG A 27  ? 0.2261 0.2067 0.1514 0.0326  -0.0488 -0.0201 27  ARG A CD  
217  N  NE  . ARG A 27  ? 0.1791 0.1552 0.1631 -0.0023 0.0013  -0.0306 27  ARG A NE  
218  C  CZ  . ARG A 27  ? 0.1324 0.1737 0.1111 0.0184  -0.0103 -0.0025 27  ARG A CZ  
219  N  NH1 . ARG A 27  ? 0.1510 0.2044 0.1458 0.0260  0.0040  -0.0613 27  ARG A NH1 
220  N  NH2 . ARG A 27  ? 0.1367 0.1954 0.1464 -0.0120 -0.0048 -0.0126 27  ARG A NH2 
221  N  N   . GLN A 28  ? 0.0730 0.1112 0.1088 0.0005  -0.0261 -0.0196 28  GLN A N   
222  C  CA  . GLN A 28  ? 0.0476 0.1194 0.1150 -0.0001 -0.0194 -0.0251 28  GLN A CA  
223  C  C   . GLN A 28  ? 0.0501 0.1101 0.0943 0.0029  -0.0065 -0.0122 28  GLN A C   
224  O  O   . GLN A 28  ? 0.0889 0.1286 0.0936 -0.0105 -0.0240 -0.0126 28  GLN A O   
225  C  CB  . GLN A 28  ? 0.0383 0.1456 0.1437 -0.0049 -0.0194 -0.0212 28  GLN A CB  
226  C  CG  . GLN A 28  ? 0.0545 0.1437 0.1465 -0.0077 -0.0174 -0.0211 28  GLN A CG  
227  C  CD  . GLN A 28  ? 0.0403 0.1361 0.1306 -0.0053 -0.0223 -0.0240 28  GLN A CD  
228  O  OE1 . GLN A 28  ? 0.0610 0.1264 0.1329 -0.0176 -0.0025 -0.0323 28  GLN A OE1 
229  N  NE2 . GLN A 28  ? 0.0531 0.1280 0.1449 -0.0052 -0.0205 -0.0309 28  GLN A NE2 
230  N  N   . SER A 29  ? 0.0440 0.1108 0.0973 -0.0012 -0.0164 -0.0199 29  SER A N   
231  C  CA  . SER A 29  ? 0.0445 0.0955 0.1034 0.0026  -0.0170 -0.0236 29  SER A CA  
232  C  C   . SER A 29  ? 0.0430 0.0970 0.0916 0.0111  -0.0100 -0.0122 29  SER A C   
233  O  O   . SER A 29  ? 0.0494 0.1142 0.1117 0.0034  -0.0027 -0.0128 29  SER A O   
234  C  CB  . SER A 29  ? 0.0422 0.0973 0.0950 0.0104  -0.0119 -0.0211 29  SER A CB  
235  O  OG  . SER A 29  ? 0.0575 0.0991 0.0923 0.0058  -0.0043 -0.0166 29  SER A OG  
236  N  N   . PRO A 30  ? 0.0429 0.0959 0.0880 0.0005  -0.0058 -0.0158 30  PRO A N   
237  C  CA  . PRO A 30  ? 0.0462 0.0977 0.0878 -0.0050 -0.0115 -0.0037 30  PRO A CA  
238  C  C   . PRO A 30  ? 0.0476 0.0955 0.0903 0.0098  -0.0044 -0.0099 30  PRO A C   
239  O  O   . PRO A 30  ? 0.0629 0.1111 0.1070 0.0089  -0.0125 -0.0075 30  PRO A O   
240  C  CB  . PRO A 30  ? 0.0423 0.1088 0.0941 0.0108  -0.0152 -0.0130 30  PRO A CB  
241  C  CG  . PRO A 30  ? 0.0675 0.1029 0.0977 0.0005  0.0033  -0.0144 30  PRO A CG  
242  C  CD  . PRO A 30  ? 0.0693 0.0950 0.0983 -0.0054 0.0025  -0.0226 30  PRO A CD  
243  N  N   . VAL A 31  ? 0.0709 0.1013 0.0876 -0.0006 -0.0065 -0.0011 31  VAL A N   
244  C  CA  . VAL A 31  ? 0.0642 0.1020 0.0845 0.0019  -0.0201 0.0034  31  VAL A CA  
245  C  C   . VAL A 31  ? 0.0620 0.1008 0.0858 0.0184  -0.0137 -0.0010 31  VAL A C   
246  O  O   . VAL A 31  ? 0.0727 0.1121 0.1026 0.0011  -0.0210 0.0128  31  VAL A O   
247  C  CB  . VAL A 31  ? 0.0842 0.1124 0.0968 0.0013  -0.0147 -0.0057 31  VAL A CB  
248  C  CG1 . VAL A 31  ? 0.0937 0.1230 0.1063 -0.0044 -0.0085 -0.0186 31  VAL A CG1 
249  C  CG2 . VAL A 31  ? 0.0908 0.1105 0.1201 0.0179  0.0006  -0.0021 31  VAL A CG2 
250  N  N   . ASP A 32  ? 0.0754 0.0975 0.0991 0.0053  -0.0208 0.0060  32  ASP A N   
251  C  CA  . ASP A 32  ? 0.0932 0.0973 0.0892 0.0149  0.0046  0.0040  32  ASP A CA  
252  C  C   . ASP A 32  ? 0.1011 0.1018 0.0886 0.0128  -0.0275 0.0010  32  ASP A C   
253  O  O   . ASP A 32  ? 0.1166 0.1449 0.1076 0.0076  -0.0230 -0.0200 32  ASP A O   
254  C  CB  . ASP A 32  ? 0.1220 0.1027 0.1081 0.0176  -0.0230 0.0089  32  ASP A CB  
255  C  CG  . ASP A 32  ? 0.1185 0.1164 0.1234 0.0206  -0.0280 0.0080  32  ASP A CG  
256  O  OD1 . ASP A 32  ? 0.1084 0.1174 0.1101 0.0146  -0.0254 0.0061  32  ASP A OD1 
257  O  OD2 . ASP A 32  ? 0.1880 0.1546 0.1130 -0.0175 -0.0355 0.0291  32  ASP A OD2 
258  N  N   . ILE A 33  ? 0.0783 0.1137 0.0855 0.0072  -0.0098 0.0006  33  ILE A N   
259  C  CA  . ILE A 33  ? 0.0971 0.1056 0.0851 0.0093  -0.0004 0.0027  33  ILE A CA  
260  C  C   . ILE A 33  ? 0.1241 0.1180 0.0862 0.0297  0.0016  -0.0033 33  ILE A C   
261  O  O   . ILE A 33  ? 0.1446 0.1270 0.1022 0.0132  0.0082  0.0044  33  ILE A O   
262  C  CB  . ILE A 33  ? 0.0916 0.1142 0.1041 0.0265  0.0019  0.0110  33  ILE A CB  
263  C  CG1 . ILE A 33  ? 0.0957 0.1248 0.1191 0.0209  -0.0142 0.0186  33  ILE A CG1 
264  C  CG2 . ILE A 33  ? 0.0908 0.1694 0.1383 0.0149  0.0234  0.0170  33  ILE A CG2 
265  C  CD1 . ILE A 33  ? 0.1138 0.1638 0.1300 0.0030  -0.0223 0.0287  33  ILE A CD1 
266  N  N   A ASP A 34  ? 0.1300 0.1476 0.0992 0.0342  -0.0116 0.0126  34  ASP A N   
267  N  N   B ASP A 34  ? 0.1713 0.1306 0.0708 0.0251  0.0258  0.0102  34  ASP A N   
268  C  CA  A ASP A 34  ? 0.1916 0.1449 0.0916 0.0681  0.0178  0.0190  34  ASP A CA  
269  C  CA  B ASP A 34  ? 0.1853 0.1333 0.0734 0.0330  0.0130  0.0205  34  ASP A CA  
270  C  C   A ASP A 34  ? 0.2218 0.1291 0.0763 0.0544  0.0464  0.0203  34  ASP A C   
271  C  C   B ASP A 34  ? 0.1977 0.1394 0.1200 0.0221  0.0498  0.0211  34  ASP A C   
272  O  O   A ASP A 34  ? 0.1485 0.1654 0.1043 0.0438  0.0300  0.0108  34  ASP A O   
273  O  O   B ASP A 34  ? 0.1279 0.1886 0.1068 0.0118  0.0195  0.0042  34  ASP A O   
274  C  CB  A ASP A 34  ? 0.2737 0.1412 0.1126 0.0838  -0.0229 0.0402  34  ASP A CB  
275  C  CB  B ASP A 34  ? 0.1990 0.1852 0.1187 0.0113  0.0019  0.0116  34  ASP A CB  
276  C  CG  A ASP A 34  ? 0.2843 0.1503 0.1480 0.0588  0.0029  0.0325  34  ASP A CG  
277  C  CG  B ASP A 34  ? 0.2146 0.2435 0.1255 0.0030  -0.0398 0.0418  34  ASP A CG  
278  O  OD1 A ASP A 34  ? 0.3899 0.1995 0.1681 0.1289  0.0138  0.0122  34  ASP A OD1 
279  O  OD1 B ASP A 34  ? 0.1954 0.2004 0.1329 0.0252  -0.0140 0.0787  34  ASP A OD1 
280  O  OD2 A ASP A 34  ? 0.2856 0.2141 0.1893 0.0925  0.0087  0.0175  34  ASP A OD2 
281  O  OD2 B ASP A 34  ? 0.2839 0.3365 0.1658 0.0484  -0.0421 0.1408  34  ASP A OD2 
282  N  N   . THR A 35  ? 0.2022 0.1539 0.1056 0.0483  0.0275  0.0408  35  THR A N   
283  C  CA  . THR A 35  ? 0.2042 0.1808 0.1111 0.0741  0.0339  0.0402  35  THR A CA  
284  C  C   . THR A 35  ? 0.1999 0.1638 0.1141 0.0502  0.0457  0.0223  35  THR A C   
285  O  O   . THR A 35  ? 0.2776 0.1990 0.1561 0.0917  0.0662  0.0432  35  THR A O   
286  C  CB  . THR A 35  ? 0.1893 0.2044 0.1514 0.0467  0.0373  0.0368  35  THR A CB  
287  O  OG1 . THR A 35  ? 0.2362 0.2133 0.1600 0.0450  0.0569  0.0431  35  THR A OG1 
288  C  CG2 . THR A 35  ? 0.2328 0.2512 0.1514 0.0632  0.0505  0.0536  35  THR A CG2 
289  N  N   . HIS A 36  ? 0.3167 0.1740 0.1020 0.0695  0.0463  0.0644  36  HIS A N   
290  C  CA  . HIS A 36  ? 0.2947 0.1909 0.1286 0.0513  0.0586  0.0653  36  HIS A CA  
291  C  C   . HIS A 36  ? 0.3515 0.2567 0.0988 0.0580  0.0330  0.0427  36  HIS A C   
292  O  O   . HIS A 36  ? 0.2543 0.2869 0.1394 0.0567  0.0147  0.0250  36  HIS A O   
293  C  CB  . HIS A 36  ? 0.4175 0.2415 0.1218 0.0573  0.0094  0.0886  36  HIS A CB  
294  C  CG  . HIS A 36  ? 0.3257 0.2205 0.1496 0.0706  0.0043  0.0546  36  HIS A CG  
295  N  ND1 . HIS A 36  ? 0.7325 0.4300 0.3426 0.0741  0.1059  -0.1432 36  HIS A ND1 
296  C  CD2 . HIS A 36  ? 0.3356 0.1805 0.1720 0.0152  -0.0697 0.0310  36  HIS A CD2 
297  C  CE1 . HIS A 36  ? 1.0005 0.3908 0.5245 -0.0019 -0.0146 -0.1081 36  HIS A CE1 
298  N  NE2 . HIS A 36  ? 0.7310 0.2994 0.2855 0.0143  -0.2258 -0.0208 36  HIS A NE2 
299  N  N   . THR A 37  ? 0.3599 0.1631 0.1512 0.0849  0.0607  0.0067  37  THR A N   
300  C  CA  . THR A 37  ? 0.3416 0.1938 0.1338 0.1012  0.0537  0.0537  37  THR A CA  
301  C  C   . THR A 37  ? 0.2394 0.2089 0.1277 0.0897  0.0146  0.0103  37  THR A C   
302  O  O   . THR A 37  ? 0.3344 0.2496 0.1737 0.1254  -0.0517 -0.0275 37  THR A O   
303  C  CB  . THR A 37  ? 0.3797 0.1738 0.4155 0.0973  -0.1355 0.0334  37  THR A CB  
304  O  OG1 . THR A 37  ? 0.4583 0.2360 0.4684 0.1294  -0.0685 0.0630  37  THR A OG1 
305  C  CG2 . THR A 37  ? 0.3027 0.3101 0.1782 0.0768  -0.0501 0.0390  37  THR A CG2 
306  N  N   . ALA A 38  ? 0.2672 0.1801 0.0984 0.0756  0.0318  0.0363  38  ALA A N   
307  C  CA  . ALA A 38  ? 0.2428 0.1870 0.0941 0.0774  0.0291  0.0311  38  ALA A CA  
308  C  C   . ALA A 38  ? 0.2291 0.1744 0.1737 0.0521  0.0616  0.0365  38  ALA A C   
309  O  O   . ALA A 38  ? 0.3642 0.2203 0.2569 0.0760  0.1494  0.0591  38  ALA A O   
310  C  CB  . ALA A 38  ? 0.2455 0.1834 0.1345 0.0514  -0.0096 0.0089  38  ALA A CB  
311  N  N   A LYS A 39  ? 0.2535 0.1925 0.1162 0.1004  0.0039  -0.0261 39  LYS A N   
312  N  N   B LYS A 39  ? 0.2040 0.2134 0.1559 0.1046  0.0337  0.0408  39  LYS A N   
313  C  CA  A LYS A 39  ? 0.2514 0.1527 0.1029 0.0477  0.0234  -0.0150 39  LYS A CA  
314  C  CA  B LYS A 39  ? 0.1334 0.2286 0.1555 0.0579  0.0046  -0.0154 39  LYS A CA  
315  C  C   A LYS A 39  ? 0.2326 0.2049 0.0752 0.1005  0.0582  0.0073  39  LYS A C   
316  C  C   B LYS A 39  ? 0.1534 0.2349 0.1521 0.0083  -0.0838 -0.0255 39  LYS A C   
317  O  O   A LYS A 39  ? 0.1844 0.2230 0.0600 0.0283  -0.0232 0.0149  39  LYS A O   
318  O  O   B LYS A 39  ? 0.1273 0.2327 0.1453 0.0738  0.0196  -0.0057 39  LYS A O   
319  C  CB  A LYS A 39  ? 0.1381 0.2241 0.1302 0.0384  -0.0263 0.0320  39  LYS A CB  
320  C  CB  B LYS A 39  ? 0.1518 0.2637 0.1325 0.0564  -0.0386 -0.0082 39  LYS A CB  
321  C  CG  A LYS A 39  ? 0.2272 0.2450 0.1482 0.0677  -0.0194 0.0118  39  LYS A CG  
322  C  CG  B LYS A 39  ? 0.2320 0.2399 0.1444 0.0253  0.0071  0.0211  39  LYS A CG  
323  C  CD  A LYS A 39  ? 0.1577 0.2178 0.2731 0.0146  -0.0070 0.0340  39  LYS A CD  
324  C  CD  B LYS A 39  ? 0.2673 0.3581 0.1397 0.0647  -0.0414 -0.0410 39  LYS A CD  
325  C  CE  A LYS A 39  ? 0.1280 0.2216 0.2031 -0.0546 -0.0929 0.0200  39  LYS A CE  
326  C  CE  B LYS A 39  ? 0.1045 0.3551 0.3752 -0.0593 -0.0398 -0.1015 39  LYS A CE  
327  N  NZ  A LYS A 39  ? 0.1579 0.2947 0.2900 0.0401  -0.0051 0.1632  39  LYS A NZ  
328  N  NZ  B LYS A 39  ? 0.4661 0.4566 0.2067 -0.0061 0.1611  -0.0659 39  LYS A NZ  
329  N  N   . TYR A 40  ? 0.2462 0.2525 0.1372 0.0302  0.0430  0.0296  40  TYR A N   
330  C  CA  . TYR A 40  ? 0.2092 0.2069 0.1588 -0.0069 0.0628  0.0065  40  TYR A CA  
331  C  C   . TYR A 40  ? 0.1562 0.2266 0.1089 -0.0122 0.0240  0.0129  40  TYR A C   
332  O  O   . TYR A 40  ? 0.2186 0.2712 0.1027 0.0537  0.0313  -0.0190 40  TYR A O   
333  C  CB  . TYR A 40  ? 0.3061 0.3389 0.1848 -0.0776 0.0732  0.0794  40  TYR A CB  
334  C  CG  . TYR A 40  ? 0.2712 0.3378 0.1828 -0.0800 0.0838  0.0004  40  TYR A CG  
335  C  CD1 . TYR A 40  ? 0.2527 0.3162 0.1816 -0.0457 0.0456  -0.0329 40  TYR A CD1 
336  C  CD2 . TYR A 40  ? 0.3040 0.3562 0.2191 0.0089  0.0967  -0.0276 40  TYR A CD2 
337  C  CE1 . TYR A 40  ? 0.2351 0.4107 0.1843 -0.0307 0.0421  -0.0277 40  TYR A CE1 
338  C  CE2 . TYR A 40  ? 0.2665 0.5245 0.2065 0.0236  0.0977  0.0165  40  TYR A CE2 
339  C  CZ  . TYR A 40  ? 0.1990 0.5776 0.1778 -0.0947 0.0417  0.0183  40  TYR A CZ  
340  O  OH  . TYR A 40  ? 0.1855 0.6867 0.3003 -0.0008 0.0653  -0.0965 40  TYR A OH  
341  N  N   . ASP A 41  ? 0.1320 0.1929 0.1325 0.0284  0.0296  -0.0009 41  ASP A N   
342  C  CA  . ASP A 41  ? 0.1424 0.2110 0.1525 -0.0159 0.0199  -0.0009 41  ASP A CA  
343  C  C   . ASP A 41  ? 0.1550 0.2451 0.1498 0.0012  0.0280  -0.0261 41  ASP A C   
344  O  O   . ASP A 41  ? 0.1586 0.2682 0.1561 0.0239  0.0086  -0.0053 41  ASP A O   
345  C  CB  . ASP A 41  ? 0.1575 0.2081 0.1934 -0.0211 -0.0116 -0.0162 41  ASP A CB  
346  C  CG  . ASP A 41  ? 0.1264 0.2789 0.2555 -0.0200 -0.0194 -0.0389 41  ASP A CG  
347  O  OD1 . ASP A 41  ? 0.2306 0.2665 0.2320 0.0110  -0.0055 -0.0544 41  ASP A OD1 
348  O  OD2 . ASP A 41  ? 0.1936 0.3186 0.2582 -0.0705 -0.0510 -0.0113 41  ASP A OD2 
349  N  N   . PRO A 42  ? 0.1742 0.3294 0.1803 0.0479  0.0572  -0.0236 42  PRO A N   
350  C  CA  . PRO A 42  ? 0.1888 0.3322 0.2256 0.0425  0.0853  0.0072  42  PRO A CA  
351  C  C   . PRO A 42  ? 0.2423 0.3146 0.2719 0.1112  0.0856  0.0017  42  PRO A C   
352  O  O   . PRO A 42  ? 0.2563 0.5192 0.3723 0.1761  0.0788  0.0120  42  PRO A O   
353  C  CB  . PRO A 42  ? 0.2200 0.6637 0.2593 0.0310  0.1252  -0.0072 42  PRO A CB  
354  C  CG  . PRO A 42  ? 0.2453 0.4669 0.2421 0.0557  0.0700  -0.0369 42  PRO A CG  
355  C  CD  . PRO A 42  ? 0.2897 0.4050 0.1428 0.0791  0.0936  -0.0132 42  PRO A CD  
356  N  N   . SER A 43  ? 0.2530 0.3486 0.1625 0.0491  0.0198  -0.0274 43  SER A N   
357  C  CA  . SER A 43  ? 0.2620 0.3378 0.2737 0.0678  -0.0263 -0.0430 43  SER A CA  
358  C  C   . SER A 43  ? 0.2803 0.2737 0.2243 0.0615  -0.0015 -0.0395 43  SER A C   
359  O  O   . SER A 43  ? 0.3953 0.2975 0.3037 0.1235  -0.0218 0.0020  43  SER A O   
360  C  CB  . SER A 43  ? 0.2500 0.2927 0.3802 -0.0341 0.0348  -0.0125 43  SER A CB  
361  O  OG  . SER A 43  ? 0.2601 0.3457 0.3339 -0.0122 -0.0418 -0.0697 43  SER A OG  
362  N  N   . LEU A 44  ? 0.2389 0.3243 0.1674 0.0684  -0.0414 -0.0457 44  LEU A N   
363  C  CA  . LEU A 44  ? 0.1925 0.2987 0.1735 0.0471  -0.0458 0.0019  44  LEU A CA  
364  C  C   . LEU A 44  ? 0.1401 0.3567 0.2281 0.0137  -0.0061 0.0259  44  LEU A C   
365  O  O   . LEU A 44  ? 0.1710 0.5082 0.3207 -0.0447 -0.0075 0.0985  44  LEU A O   
366  C  CB  . LEU A 44  ? 0.1703 0.2617 0.1843 -0.0073 0.0089  -0.0255 44  LEU A CB  
367  C  CG  . LEU A 44  ? 0.1692 0.2372 0.1595 0.0009  -0.0171 0.0223  44  LEU A CG  
368  C  CD1 . LEU A 44  ? 0.2171 0.2658 0.1591 0.0168  0.0185  -0.0222 44  LEU A CD1 
369  C  CD2 . LEU A 44  ? 0.1679 0.2567 0.2313 -0.0258 0.0027  0.0086  44  LEU A CD2 
370  N  N   . LYS A 45  ? 0.1927 0.2604 0.2322 0.0379  -0.0266 0.0262  45  LYS A N   
371  C  CA  . LYS A 45  ? 0.1478 0.2502 0.2401 0.0250  -0.0272 -0.0092 45  LYS A CA  
372  C  C   . LYS A 45  ? 0.1311 0.2658 0.2164 0.0807  0.0099  -0.0013 45  LYS A C   
373  O  O   . LYS A 45  ? 0.1410 0.2721 0.2900 0.0312  0.0254  -0.0373 45  LYS A O   
374  C  CB  . LYS A 45  ? 0.2381 0.2496 0.2110 0.0775  -0.0176 -0.0209 45  LYS A CB  
375  C  CG  . LYS A 45  ? 0.2794 0.4500 0.2796 -0.0563 -0.0550 -0.1165 45  LYS A CG  
376  C  CD  . LYS A 45  ? 0.3128 0.3977 0.6880 -0.0839 -0.0956 -0.2088 45  LYS A CD  
377  N  N   . PRO A 46  ? 0.1025 0.2644 0.2751 -0.0174 0.0227  -0.0034 46  PRO A N   
378  C  CA  . PRO A 46  ? 0.1212 0.2918 0.2186 -0.0294 0.0194  0.0172  46  PRO A CA  
379  C  C   . PRO A 46  ? 0.1050 0.1947 0.1909 -0.0034 0.0217  0.0035  46  PRO A C   
380  O  O   . PRO A 46  ? 0.0710 0.2417 0.2435 -0.0188 -0.0172 0.0149  46  PRO A O   
381  C  CB  . PRO A 46  ? 0.1412 0.2998 0.2821 -0.0337 0.0133  0.0395  46  PRO A CB  
382  C  CG  . PRO A 46  ? 0.0632 0.4663 0.2976 -0.0164 -0.0085 -0.0276 46  PRO A CG  
383  C  CD  . PRO A 46  ? 0.1111 0.3326 0.3307 0.0446  0.0017  -0.0640 46  PRO A CD  
384  N  N   . LEU A 47  ? 0.1239 0.2540 0.2476 0.0201  0.0201  0.0041  47  LEU A N   
385  C  CA  . LEU A 47  ? 0.0779 0.2834 0.2380 -0.0490 -0.0175 0.0516  47  LEU A CA  
386  C  C   . LEU A 47  ? 0.0807 0.2679 0.3736 -0.0332 -0.0279 0.0976  47  LEU A C   
387  O  O   . LEU A 47  ? 0.1230 0.4140 0.6243 -0.0873 -0.0802 0.1907  47  LEU A O   
388  C  CB  . LEU A 47  ? 0.1911 0.4377 0.2805 0.1141  0.0895  0.0218  47  LEU A CB  
389  C  CG  . LEU A 47  ? 0.1773 0.3220 0.3974 -0.0263 0.0358  -0.0639 47  LEU A CG  
390  C  CD1 . LEU A 47  ? 0.1990 0.5743 0.5503 -0.0229 -0.0428 -0.0551 47  LEU A CD1 
391  C  CD2 . LEU A 47  ? 0.1403 0.3811 0.3994 -0.0536 0.0185  -0.0760 47  LEU A CD2 
392  N  N   . SER A 48  ? 0.0844 0.2254 0.1977 -0.0149 -0.0103 0.0197  48  SER A N   
393  C  CA  . SER A 48  ? 0.0928 0.2295 0.2051 0.0064  0.0062  0.0241  48  SER A CA  
394  C  C   . SER A 48  ? 0.0838 0.2263 0.2078 -0.0140 -0.0177 0.0148  48  SER A C   
395  O  O   . SER A 48  ? 0.0977 0.1972 0.1997 -0.0403 0.0035  -0.0156 48  SER A O   
396  C  CB  . SER A 48  ? 0.1243 0.2322 0.2284 -0.0273 -0.0099 0.0172  48  SER A CB  
397  O  OG  . SER A 48  ? 0.1358 0.2735 0.3219 0.0308  0.0196  0.0734  48  SER A OG  
398  N  N   . VAL A 49  ? 0.1315 0.1873 0.2031 -0.0438 -0.0094 0.0244  49  VAL A N   
399  C  CA  . VAL A 49  ? 0.1275 0.2247 0.2352 -0.0608 -0.0424 -0.0032 49  VAL A CA  
400  C  C   . VAL A 49  ? 0.1412 0.2205 0.2628 -0.0792 -0.0443 -0.0161 49  VAL A C   
401  O  O   . VAL A 49  ? 0.1803 0.3704 0.2878 -0.1360 -0.0819 0.0233  49  VAL A O   
402  C  CB  . VAL A 49  ? 0.1776 0.2322 0.2399 -0.0812 0.0392  -0.0419 49  VAL A CB  
403  C  CG1 . VAL A 49  ? 0.3523 0.2944 0.2453 -0.1172 0.0375  -0.0262 49  VAL A CG1 
404  C  CG2 . VAL A 49  ? 0.2090 0.2426 0.2828 -0.0748 0.0004  -0.0095 49  VAL A CG2 
405  N  N   . SER A 50  ? 0.1232 0.2561 0.2250 -0.0747 -0.0343 -0.0016 50  SER A N   
406  C  CA  . SER A 50  ? 0.1295 0.3306 0.2471 -0.0047 -0.0294 0.0020  50  SER A CA  
407  C  C   . SER A 50  ? 0.1005 0.3001 0.2180 -0.0025 -0.0532 -0.0051 50  SER A C   
408  O  O   . SER A 50  ? 0.2056 0.2526 0.2430 -0.0226 -0.0826 0.0238  50  SER A O   
409  C  CB  . SER A 50  ? 0.2209 0.3141 0.3193 -0.0416 0.0436  0.0466  50  SER A CB  
410  O  OG  . SER A 50  ? 0.1753 0.4319 0.3538 0.0082  -0.0052 -0.0097 50  SER A OG  
411  N  N   . TYR A 51  ? 0.1622 0.2455 0.2211 -0.0253 -0.0682 0.0022  51  TYR A N   
412  C  CA  . TYR A 51  ? 0.1245 0.2277 0.2365 -0.0296 -0.0916 -0.0052 51  TYR A CA  
413  C  C   . TYR A 51  ? 0.1913 0.2595 0.2528 0.0142  -0.0617 0.0663  51  TYR A C   
414  O  O   . TYR A 51  ? 0.1640 0.2910 0.2328 -0.0122 -0.0846 0.0219  51  TYR A O   
415  C  CB  . TYR A 51  ? 0.1255 0.2119 0.2329 -0.0255 -0.0851 -0.0125 51  TYR A CB  
416  C  CG  . TYR A 51  ? 0.1181 0.1976 0.1778 -0.0524 -0.0625 0.0144  51  TYR A CG  
417  C  CD1 . TYR A 51  ? 0.1444 0.2015 0.2124 -0.0547 -0.0861 0.0172  51  TYR A CD1 
418  C  CD2 . TYR A 51  ? 0.1473 0.1889 0.1467 -0.0276 -0.0325 0.0084  51  TYR A CD2 
419  C  CE1 . TYR A 51  ? 0.1201 0.1843 0.1500 -0.0370 -0.0487 0.0244  51  TYR A CE1 
420  C  CE2 . TYR A 51  ? 0.1340 0.1735 0.1661 -0.0535 -0.0501 -0.0043 51  TYR A CE2 
421  C  CZ  . TYR A 51  ? 0.1209 0.1780 0.1532 -0.0411 -0.0284 0.0013  51  TYR A CZ  
422  O  OH  . TYR A 51  ? 0.1210 0.1548 0.1740 -0.0203 -0.0351 -0.0096 51  TYR A OH  
423  N  N   . ASP A 52  ? 0.1192 0.3421 0.3503 -0.0458 -0.1124 0.0708  52  ASP A N   
424  C  CA  . ASP A 52  ? 0.1539 0.3773 0.3322 -0.0598 -0.0901 0.1149  52  ASP A CA  
425  C  C   . ASP A 52  ? 0.2284 0.3296 0.2552 -0.0127 -0.1128 0.0282  52  ASP A C   
426  O  O   . ASP A 52  ? 0.2998 0.2917 0.2547 0.0074  -0.1165 0.0204  52  ASP A O   
427  C  CB  . ASP A 52  ? 0.1717 0.4398 0.4896 -0.0005 -0.1186 0.0518  52  ASP A CB  
428  C  CG  . ASP A 52  ? 0.1782 0.4138 0.5501 0.0055  -0.1066 0.0259  52  ASP A CG  
429  O  OD1 . ASP A 52  ? 0.2040 0.6544 0.5493 0.0801  -0.0391 0.0384  52  ASP A OD1 
430  O  OD2 . ASP A 52  ? 0.6972 0.5133 0.9642 0.1819  -0.1359 0.2666  52  ASP A OD2 
431  N  N   . GLN A 53  ? 0.1846 0.3245 0.3915 -0.0031 -0.1123 0.0749  53  GLN A N   
432  C  CA  . GLN A 53  ? 0.2137 0.3098 0.3985 -0.0150 -0.0944 0.0589  53  GLN A CA  
433  C  C   . GLN A 53  ? 0.2275 0.2211 0.2617 -0.0431 -0.0697 0.0093  53  GLN A C   
434  O  O   . GLN A 53  ? 0.1841 0.2367 0.3010 -0.0115 -0.0680 0.0227  53  GLN A O   
435  C  CB  . GLN A 53  ? 0.3319 0.3193 0.4684 0.0063  0.0081  0.0036  53  GLN A CB  
436  C  CG  . GLN A 53  ? 0.2403 0.3308 0.8167 -0.0013 0.0059  0.1056  53  GLN A CG  
437  C  CD  . GLN A 53  ? 0.4559 0.7535 0.8042 0.0109  -0.0658 0.0649  53  GLN A CD  
438  O  OE1 . GLN A 53  ? 0.5643 0.8673 0.8414 0.2330  -0.0697 0.1908  53  GLN A OE1 
439  N  NE2 . GLN A 53  ? 0.5181 0.4106 0.7684 -0.0087 -0.0903 -0.1125 53  GLN A NE2 
440  N  N   . ALA A 54  ? 0.2603 0.1731 0.2724 -0.0453 -0.0732 0.0135  54  ALA A N   
441  C  CA  . ALA A 54  ? 0.2485 0.1814 0.2081 -0.0212 -0.0971 -0.0250 54  ALA A CA  
442  C  C   . ALA A 54  ? 0.3488 0.1862 0.2132 -0.0263 -0.1046 -0.0308 54  ALA A C   
443  O  O   . ALA A 54  ? 0.3256 0.3274 0.2439 -0.0647 -0.1046 -0.0695 54  ALA A O   
444  C  CB  . ALA A 54  ? 0.2777 0.1791 0.3283 0.0060  -0.0318 0.0072  54  ALA A CB  
445  N  N   . THR A 55  ? 0.2644 0.1561 0.1744 0.0225  -0.0778 0.0050  55  THR A N   
446  C  CA  . THR A 55  ? 0.2708 0.1927 0.1708 0.0758  -0.0884 0.0137  55  THR A CA  
447  C  C   . THR A 55  ? 0.2577 0.1255 0.1259 0.0006  -0.0776 0.0134  55  THR A C   
448  O  O   . THR A 55  ? 0.2407 0.1315 0.1530 0.0206  -0.0463 0.0199  55  THR A O   
449  C  CB  . THR A 55  ? 0.3833 0.2480 0.2055 0.0662  0.0265  0.0722  55  THR A CB  
450  O  OG1 . THR A 55  ? 0.4393 0.2099 0.4323 0.0848  -0.1345 -0.0032 55  THR A OG1 
451  C  CG2 . THR A 55  ? 0.5151 0.2867 0.1958 0.2219  0.0460  0.0697  55  THR A CG2 
452  N  N   . SER A 56  ? 0.2455 0.1573 0.1331 0.0366  -0.0637 0.0152  56  SER A N   
453  C  CA  . SER A 56  ? 0.2329 0.1604 0.1205 -0.0129 -0.0361 0.0197  56  SER A CA  
454  C  C   . SER A 56  ? 0.1823 0.1843 0.1532 0.0288  -0.0291 0.0170  56  SER A C   
455  O  O   . SER A 56  ? 0.2381 0.1826 0.1647 0.0397  -0.0399 0.0337  56  SER A O   
456  C  CB  . SER A 56  ? 0.2232 0.1708 0.1487 0.0086  -0.0375 -0.0016 56  SER A CB  
457  O  OG  . SER A 56  ? 0.2808 0.1740 0.1525 0.0258  -0.0895 0.0128  56  SER A OG  
458  N  N   . LEU A 57  ? 0.1476 0.1309 0.1051 0.0135  -0.0289 0.0319  57  LEU A N   
459  C  CA  . LEU A 57  ? 0.1870 0.1710 0.1658 0.0179  0.0025  0.0153  57  LEU A CA  
460  C  C   . LEU A 57  ? 0.1950 0.1814 0.1027 -0.0111 0.0104  0.0231  57  LEU A C   
461  O  O   . LEU A 57  ? 0.2329 0.1717 0.1297 0.0208  -0.0135 0.0201  57  LEU A O   
462  C  CB  . LEU A 57  ? 0.2572 0.2397 0.1861 -0.0580 -0.0073 0.0884  57  LEU A CB  
463  C  CG  . LEU A 57  ? 0.4389 0.2419 0.2459 0.0539  -0.0320 -0.0012 57  LEU A CG  
464  C  CD1 . LEU A 57  ? 0.4000 0.3234 0.2840 0.0491  0.0496  -0.0178 57  LEU A CD1 
465  C  CD2 . LEU A 57  ? 0.4742 0.2044 0.3574 0.0849  -0.0469 0.0653  57  LEU A CD2 
466  N  N   . ARG A 58  ? 0.3191 0.1834 0.1435 0.0741  -0.0309 0.0073  58  ARG A N   
467  C  CA  . ARG A 58  ? 0.3054 0.1683 0.1379 0.0091  -0.0336 0.0570  58  ARG A CA  
468  C  C   . ARG A 58  ? 0.1825 0.1658 0.1026 -0.0247 -0.0320 0.0248  58  ARG A C   
469  O  O   . ARG A 58  ? 0.2060 0.1681 0.1103 0.0089  0.0104  0.0079  58  ARG A O   
470  C  CB  . ARG A 58  ? 0.2582 0.2477 0.1782 0.0276  0.0066  -0.0262 58  ARG A CB  
471  C  CG  . ARG A 58  ? 0.2092 0.4672 0.3512 -0.0380 0.0958  0.0002  58  ARG A CG  
472  C  CD  . ARG A 58  ? 0.1604 0.2551 0.2843 -0.0633 0.0682  0.0476  58  ARG A CD  
473  N  NE  . ARG A 58  ? 0.1516 0.2487 0.2394 0.0100  -0.0008 0.0317  58  ARG A NE  
474  C  CZ  . ARG A 58  ? 0.1386 0.3483 0.1503 -0.0518 -0.0016 0.0710  58  ARG A CZ  
475  N  NH1 . ARG A 58  ? 0.3152 0.2437 0.2123 -0.0761 0.0502  0.0365  58  ARG A NH1 
476  N  NH2 . ARG A 58  ? 0.2496 0.2146 0.2555 -0.0462 0.0445  0.0714  58  ARG A NH2 
477  N  N   . ILE A 59  ? 0.3255 0.1588 0.0834 0.0283  0.0250  0.0116  59  ILE A N   
478  C  CA  . ILE A 59  ? 0.2130 0.1719 0.1159 -0.0223 -0.0046 0.0534  59  ILE A CA  
479  C  C   . ILE A 59  ? 0.2015 0.1018 0.1368 0.0064  -0.0476 0.0353  59  ILE A C   
480  O  O   . ILE A 59  ? 0.3754 0.1988 0.0763 0.0282  -0.0254 0.0276  59  ILE A O   
481  C  CB  . ILE A 59  ? 0.3565 0.1174 0.0893 0.0006  -0.0165 0.0168  59  ILE A CB  
482  C  CG1 . ILE A 59  ? 0.3384 0.1211 0.0837 0.0107  -0.0229 0.0168  59  ILE A CG1 
483  C  CG2 . ILE A 59  ? 0.3973 0.1377 0.0841 0.0251  -0.0646 0.0151  59  ILE A CG2 
484  C  CD1 . ILE A 59  ? 0.3583 0.1151 0.0950 0.0184  -0.0255 0.0140  59  ILE A CD1 
485  N  N   . LEU A 60  ? 0.1104 0.1586 0.2558 0.0109  -0.0659 -0.0285 60  LEU A N   
486  C  CA  . LEU A 60  ? 0.1961 0.1198 0.0858 0.0168  -0.0572 0.0016  60  LEU A CA  
487  C  C   . LEU A 60  ? 0.2619 0.1228 0.0948 -0.0012 -0.0015 -0.0234 60  LEU A C   
488  O  O   . LEU A 60  ? 0.2327 0.1532 0.0778 -0.0329 0.0160  0.0177  60  LEU A O   
489  C  CB  . LEU A 60  ? 0.1659 0.1654 0.1755 -0.0168 -0.0223 -0.0163 60  LEU A CB  
490  C  CG  . LEU A 60  ? 0.2133 0.1178 0.1356 0.0190  -0.0009 0.0234  60  LEU A CG  
491  C  CD1 . LEU A 60  ? 0.2396 0.1850 0.1622 -0.0590 0.0436  0.0105  60  LEU A CD1 
492  C  CD2 . LEU A 60  ? 0.2069 0.1365 0.1974 -0.0286 -0.0167 -0.0027 60  LEU A CD2 
493  N  N   . ASN A 61  ? 0.2227 0.1157 0.1333 -0.0212 0.0162  0.0270  61  ASN A N   
494  C  CA  . ASN A 61  ? 0.2177 0.1932 0.1072 -0.0561 0.0505  -0.0680 61  ASN A CA  
495  C  C   . ASN A 61  ? 0.2478 0.1663 0.0891 -0.0738 0.0421  -0.0070 61  ASN A C   
496  O  O   . ASN A 61  ? 0.3283 0.1464 0.0934 -0.0782 0.0496  0.0078  61  ASN A O   
497  C  CB  . ASN A 61  ? 0.2628 0.1342 0.1514 -0.0317 0.0185  -0.0242 61  ASN A CB  
498  C  CG  . ASN A 61  ? 0.2008 0.1879 0.0916 -0.0750 0.0379  -0.0570 61  ASN A CG  
499  O  OD1 . ASN A 61  ? 0.2644 0.1527 0.1365 -0.0819 0.0640  -0.0048 61  ASN A OD1 
500  N  ND2 . ASN A 61  ? 0.3095 0.1440 0.1181 -0.0768 0.0731  -0.0375 61  ASN A ND2 
501  N  N   . ASN A 62  ? 0.3086 0.1297 0.0814 -0.0759 0.0314  -0.0118 62  ASN A N   
502  C  CA  . ASN A 62  ? 0.1782 0.1913 0.1203 -0.0198 0.0047  -0.0085 62  ASN A CA  
503  C  C   . ASN A 62  ? 0.1379 0.1740 0.1212 -0.1005 0.0149  -0.0010 62  ASN A C   
504  O  O   . ASN A 62  ? 0.2491 0.2655 0.1654 -0.1069 0.0770  -0.0027 62  ASN A O   
505  C  CB  . ASN A 62  ? 0.3865 0.1232 0.1324 -0.1008 0.0285  -0.0077 62  ASN A CB  
506  C  CG  . ASN A 62  ? 0.2970 0.1688 0.0795 -0.0875 0.0339  -0.0350 62  ASN A CG  
507  O  OD1 . ASN A 62  ? 0.2270 0.1595 0.1172 -0.0762 0.0420  -0.0104 62  ASN A OD1 
508  N  ND2 . ASN A 62  ? 0.4290 0.1857 0.1277 -0.0345 0.0967  0.0051  62  ASN A ND2 
509  N  N   . GLY A 63  ? 0.2195 0.1850 0.1340 -0.0249 0.0263  0.0121  63  GLY A N   
510  C  CA  . GLY A 63  ? 0.1528 0.1807 0.0961 -0.0805 0.0268  0.0013  63  GLY A CA  
511  C  C   . GLY A 63  ? 0.2388 0.1485 0.1665 -0.0583 0.0408  -0.0284 63  GLY A C   
512  O  O   . GLY A 63  ? 0.1868 0.2142 0.1503 -0.0758 0.0647  -0.0416 63  GLY A O   
513  N  N   . HIS A 64  ? 0.1828 0.1636 0.1257 -0.0683 0.0729  -0.0247 64  HIS A N   
514  C  CA  . HIS A 64  ? 0.1828 0.1667 0.1089 -0.0666 0.0497  -0.0121 64  HIS A CA  
515  C  C   . HIS A 64  ? 0.1792 0.1325 0.1446 -0.0626 0.0748  -0.0113 64  HIS A C   
516  O  O   . HIS A 64  ? 0.1288 0.2211 0.2984 -0.0594 0.0374  0.0907  64  HIS A O   
517  C  CB  . HIS A 64  ? 0.1613 0.1870 0.1144 -0.0587 0.0293  -0.0228 64  HIS A CB  
518  C  CG  . HIS A 64  ? 0.1697 0.1690 0.1473 -0.0346 0.0517  -0.0223 64  HIS A CG  
519  N  ND1 . HIS A 64  ? 0.1746 0.2051 0.1584 -0.0496 0.0355  -0.0560 64  HIS A ND1 
520  C  CD2 . HIS A 64  ? 0.1843 0.2011 0.1796 -0.1022 0.0417  -0.0229 64  HIS A CD2 
521  C  CE1 . HIS A 64  ? 0.1832 0.2128 0.2295 -0.0465 0.0601  -0.0491 64  HIS A CE1 
522  N  NE2 . HIS A 64  ? 0.1830 0.2286 0.2243 -0.0951 0.0316  -0.0231 64  HIS A NE2 
523  N  N   . ALA A 65  ? 0.1559 0.1422 0.1104 -0.0556 0.0089  -0.0009 65  ALA A N   
524  C  CA  . ALA A 65  ? 0.1591 0.1444 0.1002 -0.0559 0.0280  -0.0081 65  ALA A CA  
525  C  C   . ALA A 65  ? 0.2117 0.1324 0.0631 -0.0502 0.0279  -0.0001 65  ALA A C   
526  O  O   . ALA A 65  ? 0.2390 0.1561 0.0938 -0.0617 0.0370  0.0027  65  ALA A O   
527  C  CB  . ALA A 65  ? 0.1602 0.1715 0.1033 -0.0409 0.0364  -0.0011 65  ALA A CB  
528  N  N   . PHE A 66  ? 0.1880 0.1193 0.1036 -0.0310 0.0247  0.0005  66  PHE A N   
529  C  CA  . PHE A 66  ? 0.2220 0.1307 0.0807 -0.0359 -0.0044 0.0126  66  PHE A CA  
530  C  C   . PHE A 66  ? 0.2238 0.1428 0.0603 -0.0233 -0.0119 0.0039  66  PHE A C   
531  O  O   . PHE A 66  ? 0.2363 0.1386 0.0677 -0.0352 0.0059  0.0061  66  PHE A O   
532  C  CB  . PHE A 66  ? 0.2182 0.1658 0.0880 -0.0468 -0.0109 0.0033  66  PHE A CB  
533  C  CG  . PHE A 66  ? 0.2177 0.1544 0.0741 -0.0407 -0.0111 -0.0171 66  PHE A CG  
534  C  CD1 . PHE A 66  ? 0.2353 0.1832 0.0664 -0.0320 -0.0156 -0.0002 66  PHE A CD1 
535  C  CD2 . PHE A 66  ? 0.2227 0.1643 0.0732 -0.0128 -0.0042 -0.0291 66  PHE A CD2 
536  C  CE1 . PHE A 66  ? 0.1911 0.1778 0.0917 -0.0197 -0.0287 -0.0108 66  PHE A CE1 
537  C  CE2 . PHE A 66  ? 0.2264 0.1656 0.0900 -0.0375 -0.0171 -0.0334 66  PHE A CE2 
538  C  CZ  . PHE A 66  ? 0.2103 0.1694 0.0972 -0.0219 -0.0140 -0.0269 66  PHE A CZ  
539  N  N   . ASN A 67  ? 0.2128 0.1248 0.0921 -0.0293 -0.0125 0.0268  67  ASN A N   
540  C  CA  . ASN A 67  ? 0.2083 0.1261 0.1232 -0.0438 0.0253  -0.0265 67  ASN A CA  
541  C  C   . ASN A 67  ? 0.1812 0.0986 0.1062 0.0128  -0.0624 0.0255  67  ASN A C   
542  O  O   . ASN A 67  ? 0.2752 0.1643 0.0966 0.0039  -0.0176 0.0340  67  ASN A O   
543  C  CB  . ASN A 67  ? 0.3101 0.1713 0.1203 -0.0801 0.0089  -0.0078 67  ASN A CB  
544  C  CG  . ASN A 67  ? 0.2407 0.1611 0.2410 -0.0768 0.0829  -0.0078 67  ASN A CG  
545  O  OD1 . ASN A 67  ? 0.3036 0.2464 0.1658 -0.1211 -0.0592 0.0374  67  ASN A OD1 
546  N  ND2 . ASN A 67  ? 0.2185 0.2116 0.3437 -0.0813 0.0291  -0.1131 67  ASN A ND2 
547  N  N   . VAL A 68  ? 0.1744 0.1753 0.1624 -0.0048 -0.0013 -0.0408 68  VAL A N   
548  C  CA  . VAL A 68  ? 0.1986 0.1546 0.0919 0.0785  -0.0423 0.0075  68  VAL A CA  
549  C  C   . VAL A 68  ? 0.2763 0.1325 0.0925 0.0449  -0.0039 0.0053  68  VAL A C   
550  O  O   . VAL A 68  ? 0.2850 0.1049 0.0785 0.0325  0.0001  0.0067  68  VAL A O   
551  C  CB  . VAL A 68  ? 0.2044 0.1307 0.1403 0.0148  -0.0211 0.0052  68  VAL A CB  
552  C  CG1 . VAL A 68  ? 0.2543 0.1636 0.1288 0.0381  -0.0697 0.0078  68  VAL A CG1 
553  C  CG2 . VAL A 68  ? 0.2836 0.1668 0.1089 0.0398  -0.0457 -0.0346 68  VAL A CG2 
554  N  N   . GLU A 69  ? 0.3001 0.1440 0.0868 0.0370  0.0165  0.0113  69  GLU A N   
555  C  CA  . GLU A 69  ? 0.2728 0.1566 0.1099 0.0287  0.0515  0.0055  69  GLU A CA  
556  C  C   . GLU A 69  ? 0.3200 0.1044 0.1297 0.0644  -0.0425 0.0198  69  GLU A C   
557  O  O   . GLU A 69  ? 0.2428 0.1584 0.1577 0.0284  -0.0096 0.0181  69  GLU A O   
558  C  CB  . GLU A 69  ? 0.1072 0.2471 0.2130 0.0346  0.0612  0.0421  69  GLU A CB  
559  C  CG  . GLU A 69  ? 0.0760 0.2712 0.2164 -0.0266 0.0221  0.0743  69  GLU A CG  
560  C  CD  . GLU A 69  ? 0.1288 0.1968 0.2141 0.0076  0.0328  0.0337  69  GLU A CD  
561  O  OE1 . GLU A 69  ? 0.2282 0.2214 0.2139 -0.0002 0.0341  0.0630  69  GLU A OE1 
562  O  OE2 . GLU A 69  ? 0.1480 0.2254 0.2363 -0.0480 0.0348  0.0308  69  GLU A OE2 
563  N  N   . PHE A 70  ? 0.2782 0.1004 0.1186 0.0222  0.0005  0.0071  70  PHE A N   
564  C  CA  . PHE A 70  ? 0.2352 0.1000 0.1306 0.0251  -0.0526 -0.0009 70  PHE A CA  
565  C  C   . PHE A 70  ? 0.2717 0.1129 0.1510 0.0293  -0.0463 0.0004  70  PHE A C   
566  O  O   . PHE A 70  ? 0.2653 0.1117 0.1769 0.0201  -0.0277 0.0259  70  PHE A O   
567  C  CB  . PHE A 70  ? 0.2460 0.1261 0.0956 0.0203  -0.0519 0.0100  70  PHE A CB  
568  C  CG  . PHE A 70  ? 0.2484 0.1050 0.1208 0.0298  -0.0789 0.0205  70  PHE A CG  
569  C  CD1 . PHE A 70  ? 0.2540 0.1069 0.1193 0.0384  -0.0563 0.0285  70  PHE A CD1 
570  C  CD2 . PHE A 70  ? 0.2507 0.1288 0.1108 0.0284  -0.0768 0.0144  70  PHE A CD2 
571  C  CE1 . PHE A 70  ? 0.2421 0.1338 0.1277 0.0304  -0.0277 0.0377  70  PHE A CE1 
572  C  CE2 . PHE A 70  ? 0.2370 0.1334 0.1160 0.0103  -0.0369 0.0247  70  PHE A CE2 
573  C  CZ  . PHE A 70  ? 0.2688 0.1227 0.1261 0.0175  -0.0336 0.0001  70  PHE A CZ  
574  N  N   . ASP A 71  ? 0.3068 0.1063 0.1943 0.0406  -0.0741 0.0403  71  ASP A N   
575  C  CA  . ASP A 71  ? 0.2714 0.1026 0.2115 0.0436  -0.0610 0.0362  71  ASP A CA  
576  C  C   . ASP A 71  ? 0.2137 0.0914 0.2773 -0.0089 -0.0108 0.0037  71  ASP A C   
577  O  O   . ASP A 71  ? 0.1992 0.1866 0.3457 -0.0383 -0.0262 -0.0469 71  ASP A O   
578  C  CB  . ASP A 71  ? 0.3425 0.1225 0.3337 0.0208  -0.1628 0.0726  71  ASP A CB  
579  C  CG  . ASP A 71  ? 0.4113 0.1582 0.3843 0.0281  -0.1830 0.0579  71  ASP A CG  
580  O  OD1 . ASP A 71  ? 0.3346 0.1343 0.3455 0.0531  -0.0804 0.0598  71  ASP A OD1 
581  O  OD2 . ASP A 71  ? 0.5618 0.1780 0.7835 0.0427  -0.3998 0.0521  71  ASP A OD2 
582  N  N   . ASP A 72  ? 0.1816 0.1018 0.2153 -0.0015 -0.0052 0.0310  72  ASP A N   
583  C  CA  . ASP A 72  ? 0.2148 0.1047 0.2207 -0.0196 0.0196  0.0032  72  ASP A CA  
584  C  C   . ASP A 72  ? 0.2191 0.1172 0.2705 -0.0020 0.0252  0.0019  72  ASP A C   
585  O  O   . ASP A 72  ? 0.2837 0.1182 0.2625 -0.0063 0.0367  -0.0046 72  ASP A O   
586  C  CB  . ASP A 72  ? 0.1654 0.1573 0.1972 0.0179  0.0563  0.0374  72  ASP A CB  
587  C  CG  . ASP A 72  ? 0.2135 0.1645 0.1557 0.0228  0.0120  0.0321  72  ASP A CG  
588  O  OD1 . ASP A 72  ? 0.2004 0.2270 0.1832 -0.0157 -0.0329 0.0591  72  ASP A OD1 
589  O  OD2 . ASP A 72  ? 0.2218 0.2257 0.1494 -0.0061 -0.0164 0.0290  72  ASP A OD2 
590  N  N   . SER A 73  ? 0.2424 0.0975 0.3041 -0.0026 0.0013  0.0342  73  SER A N   
591  C  CA  . SER A 73  ? 0.2656 0.1106 0.3494 -0.0223 0.0207  0.0322  73  SER A CA  
592  C  C   . SER A 73  ? 0.2529 0.1349 0.3203 -0.0201 0.0499  -0.0134 73  SER A C   
593  O  O   . SER A 73  ? 0.2939 0.1302 0.2705 0.0026  0.0089  0.0159  73  SER A O   
594  C  CB  . SER A 73  ? 0.3529 0.1550 0.3912 -0.0310 -0.0266 0.1116  73  SER A CB  
595  O  OG  . SER A 73  ? 0.3186 0.1473 0.2940 0.0392  0.0616  0.0660  73  SER A OG  
596  N  N   . GLN A 74  ? 0.2290 0.1395 0.5010 0.0212  0.0609  0.0358  74  GLN A N   
597  C  CA  . GLN A 74  ? 0.2761 0.1821 0.4143 0.0147  0.1018  0.0098  74  GLN A CA  
598  C  C   . GLN A 74  ? 0.2397 0.2563 0.2930 0.0270  -0.0087 -0.0163 74  GLN A C   
599  O  O   . GLN A 74  ? 0.2065 0.1936 0.2387 -0.0351 -0.0662 0.0212  74  GLN A O   
600  C  CB  . GLN A 74  ? 0.1884 0.2214 0.5201 -0.0088 -0.0013 0.0642  74  GLN A CB  
601  C  CG  . GLN A 74  ? 0.3096 0.2353 0.5534 -0.0420 0.0245  0.0868  74  GLN A CG  
602  C  CD  . GLN A 74  ? 0.3464 0.4602 0.6358 0.1614  -0.0543 -0.1348 74  GLN A CD  
603  O  OE1 . GLN A 74  ? 0.3272 0.4009 0.8616 0.1020  -0.1498 0.0850  74  GLN A OE1 
604  N  NE2 . GLN A 74  ? 0.3052 0.3339 0.5254 -0.0686 -0.0097 0.1220  74  GLN A NE2 
605  N  N   . ASP A 75  ? 0.3852 0.3504 0.2824 -0.1724 0.0835  -0.0861 75  ASP A N   
606  C  CA  . ASP A 75  ? 0.2563 0.2500 0.2565 -0.0554 -0.0066 -0.0539 75  ASP A CA  
607  C  C   . ASP A 75  ? 0.1970 0.3546 0.2954 -0.0160 -0.0348 -0.1142 75  ASP A C   
608  O  O   . ASP A 75  ? 0.1889 0.3932 0.4470 0.0487  -0.0242 0.0363  75  ASP A O   
609  C  CB  . ASP A 75  ? 0.4350 0.5289 0.3637 -0.2145 0.2053  -0.1013 75  ASP A CB  
610  C  CG  . ASP A 75  ? 0.4842 0.5496 0.7052 0.0697  0.0908  0.1603  75  ASP A CG  
611  O  OD1 . ASP A 75  ? 0.3490 0.7029 0.2812 -0.2216 0.0148  -0.0062 75  ASP A OD1 
612  O  OD2 . ASP A 75  ? 0.2745 0.4084 0.9406 0.0701  -0.0569 0.1577  75  ASP A OD2 
613  N  N   . LYS A 76  ? 0.1990 0.2277 0.2324 0.0005  -0.0543 0.0547  76  LYS A N   
614  C  CA  . LYS A 76  ? 0.2838 0.1640 0.3777 -0.0523 -0.0562 0.0294  76  LYS A CA  
615  C  C   . LYS A 76  ? 0.3125 0.2798 0.8290 -0.0359 -0.1864 0.2307  76  LYS A C   
616  O  O   . LYS A 76  ? 0.4016 0.4264 0.6930 -0.0958 -0.1114 0.1685  76  LYS A O   
617  C  CB  . LYS A 76  ? 0.3493 0.1803 0.3271 -0.0707 -0.1288 0.0420  76  LYS A CB  
618  C  CG  . LYS A 76  ? 0.6103 0.2090 0.4455 0.0195  -0.2978 0.0196  76  LYS A CG  
619  C  CD  . LYS A 76  ? 0.9469 0.2071 0.3688 -0.1105 -0.2546 0.0132  76  LYS A CD  
620  C  CE  . LYS A 76  ? 0.8295 0.2622 0.4173 0.1277  -0.2579 -0.0046 76  LYS A CE  
621  N  NZ  . LYS A 76  ? 0.3950 0.3502 0.4197 0.0034  -0.1804 -0.0446 76  LYS A NZ  
622  N  N   . ALA A 77  ? 0.2622 0.3466 0.3147 0.0394  -0.1754 0.0438  77  ALA A N   
623  C  CA  . ALA A 77  ? 0.1634 0.2425 0.1922 0.0196  -0.0785 0.0126  77  ALA A CA  
624  C  C   . ALA A 77  ? 0.0977 0.2058 0.2243 -0.0122 -0.0814 0.0034  77  ALA A C   
625  O  O   . ALA A 77  ? 0.1092 0.3364 0.3032 0.0182  -0.0671 -0.1220 77  ALA A O   
626  C  CB  . ALA A 77  ? 0.2467 0.1974 0.2178 0.0194  -0.1124 -0.0052 77  ALA A CB  
627  N  N   . VAL A 78  ? 0.1586 0.1742 0.1837 -0.0165 -0.0614 0.0073  78  VAL A N   
628  C  CA  . VAL A 78  ? 0.2090 0.1462 0.2058 -0.0089 -0.1035 0.0130  78  VAL A CA  
629  C  C   . VAL A 78  ? 0.0925 0.1376 0.2099 -0.0041 -0.0469 0.0047  78  VAL A C   
630  O  O   . VAL A 78  ? 0.1277 0.1726 0.2854 -0.0436 -0.0829 0.0177  78  VAL A O   
631  C  CB  . VAL A 78  ? 0.3723 0.1886 0.2870 0.0096  -0.0765 -0.0137 78  VAL A CB  
632  C  CG1 . VAL A 78  ? 0.4730 0.1645 0.3701 0.0376  -0.1377 0.0381  78  VAL A CG1 
633  C  CG2 . VAL A 78  ? 0.3513 0.2139 0.3075 0.0546  0.0098  0.0240  78  VAL A CG2 
634  N  N   . LEU A 79  ? 0.1035 0.1388 0.1699 -0.0018 -0.0269 0.0053  79  LEU A N   
635  C  CA  . LEU A 79  ? 0.1122 0.1536 0.1724 -0.0099 -0.0222 -0.0042 79  LEU A CA  
636  C  C   . LEU A 79  ? 0.1026 0.1573 0.1489 -0.0245 -0.0025 0.0035  79  LEU A C   
637  O  O   . LEU A 79  ? 0.1298 0.1710 0.1873 -0.0342 0.0157  -0.0373 79  LEU A O   
638  C  CB  . LEU A 79  ? 0.1051 0.1805 0.2013 0.0000  -0.0064 0.0233  79  LEU A CB  
639  C  CG  . LEU A 79  ? 0.1162 0.1615 0.1832 0.0065  0.0004  0.0058  79  LEU A CG  
640  C  CD1 . LEU A 79  ? 0.1002 0.2078 0.3735 -0.0240 0.0254  0.0616  79  LEU A CD1 
641  C  CD2 . LEU A 79  ? 0.1056 0.1765 0.1782 0.0109  0.0015  0.0018  79  LEU A CD2 
642  N  N   . LYS A 80  ? 0.1085 0.1839 0.1496 -0.0266 0.0143  -0.0136 80  LYS A N   
643  C  CA  . LYS A 80  ? 0.1313 0.1523 0.1889 -0.0140 0.0023  -0.0036 80  LYS A CA  
644  C  C   . LYS A 80  ? 0.0812 0.1607 0.2033 0.0087  0.0128  -0.0001 80  LYS A C   
645  O  O   . LYS A 80  ? 0.0968 0.1636 0.2047 -0.0233 0.0003  0.0018  80  LYS A O   
646  C  CB  . LYS A 80  ? 0.2099 0.1738 0.2657 0.0116  0.0100  0.0073  80  LYS A CB  
647  C  CG  . LYS A 80  ? 0.1313 0.2101 0.2741 0.0282  0.0262  0.0181  80  LYS A CG  
648  C  CD  . LYS A 80  ? 0.2182 0.2385 0.5137 0.0312  0.0062  0.0653  80  LYS A CD  
649  C  CE  . LYS A 80  ? 0.5392 0.4654 0.5026 -0.1928 0.1195  -0.0380 80  LYS A CE  
650  N  NZ  . LYS A 80  ? 0.8149 0.7585 0.6540 0.1099  0.1806  -0.0659 80  LYS A NZ  
651  N  N   . GLY A 81  ? 0.1458 0.1981 0.1846 0.0163  0.0292  -0.0031 81  GLY A N   
652  C  CA  . GLY A 81  ? 0.1282 0.2300 0.2263 0.0473  0.0495  0.0552  81  GLY A CA  
653  C  C   . GLY A 81  ? 0.1144 0.2037 0.2259 0.0468  0.0553  0.0292  81  GLY A C   
654  O  O   . GLY A 81  ? 0.1160 0.1862 0.2035 0.0009  0.0291  -0.0277 81  GLY A O   
655  N  N   . GLY A 82  ? 0.1192 0.2035 0.3376 0.0039  0.0454  0.0295  82  GLY A N   
656  C  CA  . GLY A 82  ? 0.1886 0.1848 0.3277 0.0328  0.0436  0.0294  82  GLY A CA  
657  C  C   . GLY A 82  ? 0.1764 0.2062 0.2425 0.0605  0.0847  0.0477  82  GLY A C   
658  O  O   . GLY A 82  ? 0.1773 0.3790 0.2564 0.1041  0.0794  0.0637  82  GLY A O   
659  N  N   . PRO A 83  ? 0.1613 0.1593 0.2186 0.0132  0.0466  0.0159  83  PRO A N   
660  C  CA  . PRO A 83  ? 0.1672 0.1889 0.1609 0.0457  0.0240  0.0134  83  PRO A CA  
661  C  C   . PRO A 83  ? 0.1606 0.2117 0.1787 0.0430  -0.0092 -0.0351 83  PRO A C   
662  O  O   . PRO A 83  ? 0.1893 0.2345 0.2065 0.0211  -0.0335 -0.0251 83  PRO A O   
663  C  CB  . PRO A 83  ? 0.1735 0.2216 0.1830 0.0523  -0.0163 0.0125  83  PRO A CB  
664  C  CG  . PRO A 83  ? 0.1239 0.1740 0.1744 0.0301  -0.0005 0.0130  83  PRO A CG  
665  C  CD  . PRO A 83  ? 0.1203 0.1509 0.2173 0.0046  0.0431  -0.0129 83  PRO A CD  
666  N  N   . LEU A 84  ? 0.1232 0.1762 0.1726 0.0333  0.0308  -0.0052 84  LEU A N   
667  C  CA  . LEU A 84  ? 0.1640 0.1465 0.1591 0.0249  0.0094  -0.0293 84  LEU A CA  
668  C  C   . LEU A 84  ? 0.1259 0.1904 0.2006 0.0629  -0.0179 -0.0435 84  LEU A C   
669  O  O   . LEU A 84  ? 0.1433 0.1963 0.2496 0.0543  0.0159  -0.0699 84  LEU A O   
670  C  CB  . LEU A 84  ? 0.0839 0.1401 0.1674 0.0301  0.0023  -0.0084 84  LEU A CB  
671  C  CG  . LEU A 84  ? 0.0834 0.1327 0.1559 0.0069  0.0264  -0.0212 84  LEU A CG  
672  C  CD1 . LEU A 84  ? 0.0981 0.1636 0.1652 0.0048  -0.0082 -0.0072 84  LEU A CD1 
673  C  CD2 . LEU A 84  ? 0.0847 0.1505 0.1728 -0.0040 0.0275  -0.0268 84  LEU A CD2 
674  N  N   . ASP A 85  ? 0.1947 0.1792 0.1923 0.0147  0.0001  -0.0732 85  ASP A N   
675  C  CA  . ASP A 85  ? 0.2793 0.1582 0.2636 -0.0370 0.0408  -0.0985 85  ASP A CA  
676  C  C   . ASP A 85  ? 0.2189 0.1451 0.3488 0.0128  0.0864  0.0126  85  ASP A C   
677  O  O   . ASP A 85  ? 0.2867 0.2777 0.2990 -0.0107 0.0939  -0.0521 85  ASP A O   
678  C  CB  . ASP A 85  ? 0.3687 0.2232 0.2655 0.0455  0.0251  -0.0783 85  ASP A CB  
679  C  CG  . ASP A 85  ? 0.5115 0.4113 0.4000 -0.1707 0.1823  0.1085  85  ASP A CG  
680  O  OD1 . ASP A 85  ? 0.4688 0.6497 0.4896 -0.1898 0.2082  -0.1136 85  ASP A OD1 
681  O  OD2 . ASP A 85  ? 0.5484 0.4713 0.7215 0.2200  -0.1280 -0.2155 85  ASP A OD2 
682  N  N   . GLY A 86  ? 0.3416 0.2302 0.3273 -0.0319 -0.0425 0.0325  86  GLY A N   
683  C  CA  . GLY A 86  ? 0.3124 0.3307 0.2085 -0.1109 0.0099  -0.0117 86  GLY A CA  
684  C  C   . GLY A 86  ? 0.3124 0.2823 0.2042 -0.0910 -0.0285 -0.0160 86  GLY A C   
685  O  O   . GLY A 86  ? 0.3896 0.3551 0.2363 -0.1995 -0.0326 0.0026  86  GLY A O   
686  N  N   A THR A 87  ? 0.1749 0.1668 0.2166 0.0040  0.0080  -0.0457 87  THR A N   
687  N  N   B THR A 87  ? 0.1622 0.1719 0.2203 0.0117  0.0229  -0.0510 87  THR A N   
688  C  CA  A THR A 87  ? 0.1351 0.1875 0.2010 0.0245  0.0144  -0.0433 87  THR A CA  
689  C  CA  B THR A 87  ? 0.1485 0.1828 0.2130 0.0329  0.0218  -0.0478 87  THR A CA  
690  C  C   A THR A 87  ? 0.0862 0.1264 0.1950 0.0092  -0.0114 -0.0348 87  THR A C   
691  C  C   B THR A 87  ? 0.0911 0.1268 0.1945 0.0114  -0.0121 -0.0365 87  THR A C   
692  O  O   A THR A 87  ? 0.1199 0.1178 0.2011 -0.0096 0.0125  -0.0274 87  THR A O   
693  O  O   B THR A 87  ? 0.1172 0.1168 0.2099 -0.0064 0.0049  -0.0308 87  THR A O   
694  C  CB  A THR A 87  ? 0.1167 0.1873 0.2663 0.0419  0.0089  -0.0670 87  THR A CB  
695  C  CB  B THR A 87  ? 0.1514 0.2408 0.2653 0.0526  -0.0255 -0.0743 87  THR A CB  
696  O  OG1 A THR A 87  ? 0.1435 0.1622 0.2121 0.0244  0.0054  0.0329  87  THR A OG1 
697  O  OG1 B THR A 87  ? 0.1992 0.3403 0.2935 0.0730  0.0210  -0.0429 87  THR A OG1 
698  C  CG2 A THR A 87  ? 0.1163 0.3567 0.2767 0.1232  -0.0288 -0.0908 87  THR A CG2 
699  C  CG2 B THR A 87  ? 0.2213 0.2816 0.2200 0.1382  -0.0628 -0.0522 87  THR A CG2 
700  N  N   . TYR A 88  ? 0.0871 0.1230 0.1728 0.0058  -0.0080 -0.0296 88  TYR A N   
701  C  CA  . TYR A 88  ? 0.0873 0.1304 0.1313 0.0144  -0.0031 -0.0156 88  TYR A CA  
702  C  C   . TYR A 88  ? 0.0947 0.1203 0.1550 0.0032  -0.0310 0.0039  88  TYR A C   
703  O  O   . TYR A 88  ? 0.1273 0.1868 0.1866 -0.0576 -0.0502 0.0050  88  TYR A O   
704  C  CB  . TYR A 88  ? 0.0993 0.1059 0.1507 0.0084  -0.0237 -0.0203 88  TYR A CB  
705  C  CG  . TYR A 88  ? 0.0833 0.0950 0.1302 -0.0104 0.0013  -0.0105 88  TYR A CG  
706  C  CD1 . TYR A 88  ? 0.1018 0.1187 0.1318 0.0051  -0.0006 -0.0118 88  TYR A CD1 
707  C  CD2 . TYR A 88  ? 0.0779 0.0920 0.1333 0.0116  -0.0102 -0.0042 88  TYR A CD2 
708  C  CE1 . TYR A 88  ? 0.0794 0.1280 0.1358 0.0048  0.0193  -0.0145 88  TYR A CE1 
709  C  CE2 . TYR A 88  ? 0.0862 0.0868 0.1202 -0.0015 0.0049  -0.0018 88  TYR A CE2 
710  C  CZ  . TYR A 88  ? 0.0889 0.1050 0.1270 -0.0036 -0.0052 -0.0175 88  TYR A CZ  
711  O  OH  . TYR A 88  ? 0.0896 0.1238 0.1168 -0.0033 -0.0041 -0.0267 88  TYR A OH  
712  N  N   A ARG A 89  ? 0.0766 0.0943 0.1214 0.0076  -0.0189 -0.0228 89  ARG A N   
713  N  N   B ARG A 89  ? 0.0972 0.1126 0.1440 0.0253  -0.0156 -0.0142 89  ARG A N   
714  C  CA  A ARG A 89  ? 0.1117 0.0853 0.0974 0.0117  -0.0049 0.0165  89  ARG A CA  
715  C  CA  B ARG A 89  ? 0.0945 0.1029 0.1537 0.0031  -0.0418 -0.0023 89  ARG A CA  
716  C  C   A ARG A 89  ? 0.0941 0.0829 0.0905 -0.0029 -0.0031 0.0038  89  ARG A C   
717  C  C   B ARG A 89  ? 0.0934 0.0726 0.1096 0.0062  -0.0289 0.0192  89  ARG A C   
718  O  O   A ARG A 89  ? 0.0842 0.0822 0.0759 -0.0055 0.0055  -0.0087 89  ARG A O   
719  O  O   B ARG A 89  ? 0.0812 0.0998 0.0957 0.0149  -0.0072 0.0133  89  ARG A O   
720  C  CB  A ARG A 89  ? 0.1175 0.0988 0.1017 -0.0048 -0.0017 0.0172  89  ARG A CB  
721  C  CB  B ARG A 89  ? 0.1029 0.0898 0.1907 0.0280  -0.0585 0.0152  89  ARG A CB  
722  C  CG  A ARG A 89  ? 0.1482 0.0957 0.1286 -0.0110 -0.0419 0.0168  89  ARG A CG  
723  C  CG  B ARG A 89  ? 0.2148 0.1722 0.2315 0.1013  -0.0787 -0.0576 89  ARG A CG  
724  C  CD  A ARG A 89  ? 0.1286 0.0896 0.1090 -0.0027 -0.0354 0.0031  89  ARG A CD  
725  C  CD  B ARG A 89  ? 0.1844 0.2107 0.3213 0.0619  -0.1665 0.0431  89  ARG A CD  
726  N  NE  A ARG A 89  ? 0.1065 0.0948 0.1079 -0.0166 -0.0340 0.0048  89  ARG A NE  
727  N  NE  B ARG A 89  ? 0.2917 0.2107 0.3365 0.0136  -0.2141 -0.0479 89  ARG A NE  
728  C  CZ  A ARG A 89  ? 0.1478 0.0880 0.1059 -0.0084 -0.0066 -0.0003 89  ARG A CZ  
729  C  CZ  B ARG A 89  ? 0.3410 0.2046 0.3971 0.0082  -0.1773 -0.0412 89  ARG A CZ  
730  N  NH1 A ARG A 89  ? 0.1038 0.1207 0.1460 -0.0342 0.0161  -0.0097 89  ARG A NH1 
731  N  NH1 B ARG A 89  ? 0.4192 0.1426 0.3680 0.0083  -0.2227 -0.0452 89  ARG A NH1 
732  N  NH2 A ARG A 89  ? 0.1327 0.1011 0.1129 0.0040  0.0044  0.0061  89  ARG A NH2 
733  N  NH2 B ARG A 89  ? 0.4917 0.2028 0.4517 0.0018  -0.1421 -0.1546 89  ARG A NH2 
734  N  N   . LEU A 90  ? 0.1150 0.0923 0.1108 -0.0047 -0.0315 0.0032  90  LEU A N   
735  C  CA  . LEU A 90  ? 0.1038 0.0934 0.0955 -0.0104 -0.0176 0.0010  90  LEU A CA  
736  C  C   . LEU A 90  ? 0.1309 0.1020 0.0927 -0.0079 -0.0314 0.0157  90  LEU A C   
737  O  O   . LEU A 90  ? 0.1399 0.1327 0.1214 0.0088  -0.0240 0.0390  90  LEU A O   
738  C  CB  . LEU A 90  ? 0.1246 0.1045 0.1154 -0.0138 -0.0291 0.0006  90  LEU A CB  
739  C  CG  . LEU A 90  ? 0.1388 0.1150 0.1094 -0.0234 -0.0351 0.0059  90  LEU A CG  
740  C  CD1 . LEU A 90  ? 0.1703 0.1029 0.1196 0.0006  -0.0144 -0.0030 90  LEU A CD1 
741  C  CD2 . LEU A 90  ? 0.1597 0.1785 0.1487 -0.0352 -0.0480 -0.0127 90  LEU A CD2 
742  N  N   . ILE A 91  ? 0.1428 0.0889 0.0882 0.0055  -0.0055 0.0065  91  ILE A N   
743  C  CA  . ILE A 91  ? 0.1157 0.0932 0.1024 -0.0073 0.0043  0.0061  91  ILE A CA  
744  C  C   . ILE A 91  ? 0.1365 0.0891 0.0848 -0.0036 -0.0133 0.0155  91  ILE A C   
745  O  O   . ILE A 91  ? 0.1602 0.0957 0.0765 -0.0139 -0.0118 0.0063  91  ILE A O   
746  C  CB  . ILE A 91  ? 0.1415 0.0954 0.0925 -0.0164 -0.0173 0.0055  91  ILE A CB  
747  C  CG1 . ILE A 91  ? 0.1909 0.1622 0.1153 -0.0756 -0.0047 0.0084  91  ILE A CG1 
748  C  CG2 . ILE A 91  ? 0.1604 0.1074 0.1024 -0.0106 -0.0212 0.0105  91  ILE A CG2 
749  C  CD1 . ILE A 91  ? 0.2249 0.2033 0.1588 -0.1081 0.0025  0.0050  91  ILE A CD1 
750  N  N   . GLN A 92  ? 0.1397 0.0871 0.0864 -0.0012 -0.0027 0.0127  92  GLN A N   
751  C  CA  . GLN A 92  ? 0.1744 0.0801 0.0762 0.0054  0.0016  0.0119  92  GLN A CA  
752  C  C   . GLN A 92  ? 0.1318 0.0851 0.0757 -0.0198 -0.0020 0.0089  92  GLN A C   
753  O  O   . GLN A 92  ? 0.1410 0.0929 0.0763 -0.0122 -0.0052 0.0052  92  GLN A O   
754  C  CB  . GLN A 92  ? 0.2105 0.1036 0.0841 -0.0074 0.0148  0.0077  92  GLN A CB  
755  C  CG  . GLN A 92  ? 0.1726 0.0946 0.1347 -0.0011 0.0094  0.0145  92  GLN A CG  
756  C  CD  . GLN A 92  ? 0.1758 0.1101 0.1038 -0.0216 0.0222  0.0023  92  GLN A CD  
757  O  OE1 . GLN A 92  ? 0.1916 0.1059 0.1216 0.0002  -0.0201 0.0135  92  GLN A OE1 
758  N  NE2 . GLN A 92  ? 0.1884 0.1370 0.1715 0.0175  0.0262  0.0262  92  GLN A NE2 
759  N  N   . PHE A 93  ? 0.1663 0.0763 0.0697 0.0020  -0.0174 0.0085  93  PHE A N   
760  C  CA  . PHE A 93  ? 0.1606 0.0806 0.0681 -0.0110 -0.0207 0.0078  93  PHE A CA  
761  C  C   . PHE A 93  ? 0.1505 0.0791 0.0603 -0.0122 -0.0210 0.0105  93  PHE A C   
762  O  O   . PHE A 93  ? 0.1988 0.0925 0.0633 -0.0065 -0.0061 0.0089  93  PHE A O   
763  C  CB  . PHE A 93  ? 0.1609 0.0998 0.0759 -0.0156 -0.0361 0.0119  93  PHE A CB  
764  C  CG  . PHE A 93  ? 0.1474 0.0995 0.0859 -0.0114 -0.0401 0.0055  93  PHE A CG  
765  C  CD1 . PHE A 93  ? 0.2114 0.0934 0.0875 -0.0144 -0.0430 -0.0041 93  PHE A CD1 
766  C  CD2 . PHE A 93  ? 0.2044 0.1093 0.1004 -0.0032 -0.0657 0.0257  93  PHE A CD2 
767  C  CE1 . PHE A 93  ? 0.2119 0.0908 0.1131 0.0136  -0.0562 -0.0054 93  PHE A CE1 
768  C  CE2 . PHE A 93  ? 0.2660 0.1291 0.1226 0.0317  -0.1061 -0.0097 93  PHE A CE2 
769  C  CZ  . PHE A 93  ? 0.2809 0.0986 0.1462 0.0212  -0.1102 -0.0069 93  PHE A CZ  
770  N  N   . HIS A 94  ? 0.1383 0.0769 0.0658 -0.0036 -0.0233 0.0069  94  HIS A N   
771  C  CA  . HIS A 94  ? 0.1349 0.0781 0.0703 -0.0097 -0.0152 0.0103  94  HIS A CA  
772  C  C   . HIS A 94  ? 0.0986 0.0851 0.0639 -0.0222 -0.0127 -0.0029 94  HIS A C   
773  O  O   . HIS A 94  ? 0.1156 0.0838 0.0693 -0.0026 -0.0029 0.0071  94  HIS A O   
774  C  CB  . HIS A 94  ? 0.1388 0.0966 0.0673 -0.0156 -0.0079 0.0060  94  HIS A CB  
775  C  CG  . HIS A 94  ? 0.1324 0.0836 0.0705 -0.0254 0.0079  0.0041  94  HIS A CG  
776  N  ND1 . HIS A 94  ? 0.1230 0.0937 0.0678 -0.0201 -0.0086 0.0009  94  HIS A ND1 
777  C  CD2 . HIS A 94  ? 0.1056 0.1038 0.0554 -0.0315 0.0017  0.0001  94  HIS A CD2 
778  C  CE1 . HIS A 94  ? 0.0905 0.0847 0.0853 -0.0080 0.0000  0.0049  94  HIS A CE1 
779  N  NE2 . HIS A 94  ? 0.1043 0.0867 0.0648 -0.0192 -0.0030 0.0011  94  HIS A NE2 
780  N  N   . PHE A 95  ? 0.1089 0.0820 0.0761 -0.0155 -0.0011 0.0003  95  PHE A N   
781  C  CA  . PHE A 95  ? 0.1027 0.0819 0.0837 -0.0064 0.0073  0.0053  95  PHE A CA  
782  C  C   . PHE A 95  ? 0.1099 0.0836 0.0739 -0.0100 0.0020  -0.0148 95  PHE A C   
783  O  O   . PHE A 95  ? 0.1010 0.1042 0.0876 -0.0166 0.0059  0.0070  95  PHE A O   
784  C  CB  . PHE A 95  ? 0.1072 0.0991 0.0873 -0.0237 -0.0131 -0.0055 95  PHE A CB  
785  C  CG  . PHE A 95  ? 0.1219 0.0900 0.0732 -0.0168 -0.0136 -0.0057 95  PHE A CG  
786  C  CD1 . PHE A 95  ? 0.1478 0.0977 0.0752 -0.0081 -0.0122 -0.0051 95  PHE A CD1 
787  C  CD2 . PHE A 95  ? 0.1111 0.1075 0.0966 -0.0284 -0.0077 -0.0212 95  PHE A CD2 
788  C  CE1 . PHE A 95  ? 0.1537 0.1171 0.0912 -0.0036 -0.0268 -0.0195 95  PHE A CE1 
789  C  CE2 . PHE A 95  ? 0.1218 0.1092 0.1045 -0.0005 -0.0135 -0.0249 95  PHE A CE2 
790  C  CZ  . PHE A 95  ? 0.1394 0.1114 0.1054 -0.0197 -0.0223 -0.0265 95  PHE A CZ  
791  N  N   . HIS A 96  ? 0.1026 0.0840 0.0710 -0.0079 -0.0025 -0.0010 96  HIS A N   
792  C  CA  . HIS A 96  ? 0.0970 0.0802 0.0728 -0.0041 0.0091  -0.0006 96  HIS A CA  
793  C  C   . HIS A 96  ? 0.0842 0.0898 0.0710 -0.0207 0.0039  0.0030  96  HIS A C   
794  O  O   . HIS A 96  ? 0.0923 0.0805 0.0838 -0.0197 0.0139  -0.0105 96  HIS A O   
795  C  CB  . HIS A 96  ? 0.0907 0.0898 0.0860 -0.0119 -0.0013 -0.0198 96  HIS A CB  
796  C  CG  . HIS A 96  ? 0.0848 0.0939 0.0682 -0.0114 0.0050  -0.0097 96  HIS A CG  
797  N  ND1 . HIS A 96  ? 0.0873 0.0898 0.1190 -0.0127 0.0167  -0.0163 96  HIS A ND1 
798  C  CD2 . HIS A 96  ? 0.0914 0.0787 0.0708 -0.0139 -0.0055 -0.0055 96  HIS A CD2 
799  C  CE1 . HIS A 96  ? 0.1022 0.0939 0.0991 -0.0103 0.0166  -0.0149 96  HIS A CE1 
800  N  NE2 . HIS A 96  ? 0.0986 0.0780 0.0802 -0.0137 0.0114  -0.0049 96  HIS A NE2 
801  N  N   . TRP A 97  ? 0.0970 0.0779 0.0736 -0.0110 0.0061  -0.0039 97  TRP A N   
802  C  CA  . TRP A 97  ? 0.0968 0.0785 0.0923 -0.0060 0.0058  -0.0151 97  TRP A CA  
803  C  C   . TRP A 97  ? 0.0905 0.0883 0.0822 -0.0164 0.0073  -0.0149 97  TRP A C   
804  O  O   . TRP A 97  ? 0.0966 0.0986 0.1092 -0.0125 0.0232  -0.0194 97  TRP A O   
805  C  CB  . TRP A 97  ? 0.1241 0.1016 0.0752 -0.0280 0.0152  -0.0189 97  TRP A CB  
806  C  CG  . TRP A 97  ? 0.1342 0.0930 0.0770 -0.0183 0.0050  -0.0105 97  TRP A CG  
807  C  CD1 . TRP A 97  ? 0.1433 0.1138 0.0896 -0.0238 0.0286  -0.0214 97  TRP A CD1 
808  C  CD2 . TRP A 97  ? 0.1419 0.0914 0.0688 -0.0209 0.0182  -0.0055 97  TRP A CD2 
809  N  NE1 . TRP A 97  ? 0.1821 0.1022 0.0945 -0.0244 0.0276  -0.0255 97  TRP A NE1 
810  C  CE2 . TRP A 97  ? 0.1453 0.1041 0.0858 -0.0357 0.0181  -0.0245 97  TRP A CE2 
811  C  CE3 . TRP A 97  ? 0.1471 0.0917 0.0805 -0.0121 -0.0079 -0.0031 97  TRP A CE3 
812  C  CZ2 . TRP A 97  ? 0.1672 0.1324 0.0831 -0.0358 0.0176  -0.0031 97  TRP A CZ2 
813  C  CZ3 . TRP A 97  ? 0.1555 0.1083 0.0810 -0.0321 0.0077  -0.0024 97  TRP A CZ3 
814  C  CH2 . TRP A 97  ? 0.2031 0.1015 0.0823 -0.0273 0.0189  -0.0053 97  TRP A CH2 
815  N  N   . GLY A 98  ? 0.1154 0.0851 0.0975 -0.0044 0.0172  -0.0145 98  GLY A N   
816  C  CA  . GLY A 98  ? 0.0950 0.1032 0.1026 -0.0008 0.0233  -0.0119 98  GLY A CA  
817  C  C   . GLY A 98  ? 0.1085 0.1085 0.1138 -0.0154 0.0172  -0.0252 98  GLY A C   
818  O  O   . GLY A 98  ? 0.1374 0.1063 0.1172 -0.0190 0.0152  -0.0250 98  GLY A O   
819  N  N   . SER A 99  ? 0.1306 0.1133 0.1121 -0.0143 0.0250  -0.0352 99  SER A N   
820  C  CA  . SER A 99  ? 0.1555 0.1189 0.1372 -0.0114 0.0337  -0.0453 99  SER A CA  
821  C  C   . SER A 99  ? 0.1600 0.1223 0.1311 -0.0044 0.0145  -0.0516 99  SER A C   
822  O  O   . SER A 99  ? 0.1753 0.1485 0.1448 -0.0153 0.0060  -0.0460 99  SER A O   
823  C  CB  . SER A 99  ? 0.1679 0.1397 0.1692 -0.0021 0.0337  -0.0623 99  SER A CB  
824  O  OG  . SER A 99  ? 0.1230 0.1386 0.2117 0.0044  0.0337  -0.0412 99  SER A OG  
825  N  N   . LEU A 100 ? 0.1187 0.1302 0.1333 -0.0087 0.0125  -0.0377 100 LEU A N   
826  C  CA  . LEU A 100 ? 0.1584 0.0988 0.1889 0.0137  0.0334  -0.0341 100 LEU A CA  
827  C  C   . LEU A 100 ? 0.1390 0.1013 0.1512 -0.0051 0.0054  -0.0190 100 LEU A C   
828  O  O   . LEU A 100 ? 0.1505 0.1122 0.1523 -0.0177 0.0268  -0.0300 100 LEU A O   
829  C  CB  . LEU A 100 ? 0.2655 0.2013 0.2634 0.0842  0.1018  0.0553  100 LEU A CB  
830  C  CG  . LEU A 100 ? 0.2103 0.3355 0.2955 0.0638  0.0084  0.0232  100 LEU A CG  
831  C  CD1 . LEU A 100 ? 0.2746 0.5739 0.3789 0.2109  -0.0347 0.0042  100 LEU A CD1 
832  C  CD2 . LEU A 100 ? 0.4055 0.2957 0.4128 -0.0580 0.1363  -0.1300 100 LEU A CD2 
833  N  N   . ASP A 101 ? 0.1351 0.1029 0.1864 -0.0052 -0.0092 -0.0115 101 ASP A N   
834  C  CA  . ASP A 101 ? 0.1114 0.1065 0.1713 -0.0041 0.0035  0.0067  101 ASP A CA  
835  C  C   . ASP A 101 ? 0.1338 0.1022 0.1704 -0.0038 0.0157  0.0078  101 ASP A C   
836  O  O   . ASP A 101 ? 0.1672 0.1469 0.1611 0.0175  0.0250  0.0099  101 ASP A O   
837  C  CB  . ASP A 101 ? 0.1530 0.1331 0.1728 -0.0351 -0.0089 0.0363  101 ASP A CB  
838  C  CG  . ASP A 101 ? 0.1289 0.1722 0.2178 -0.0210 -0.0227 0.0552  101 ASP A CG  
839  O  OD1 . ASP A 101 ? 0.1652 0.1537 0.1938 -0.0128 0.0017  0.0230  101 ASP A OD1 
840  O  OD2 . ASP A 101 ? 0.1749 0.2259 0.2507 -0.0741 -0.0304 0.0238  101 ASP A OD2 
841  N  N   . GLY A 102 ? 0.1424 0.1176 0.1785 -0.0178 0.0026  0.0273  102 GLY A N   
842  C  CA  . GLY A 102 ? 0.1401 0.1158 0.1708 -0.0118 -0.0042 0.0275  102 GLY A CA  
843  C  C   . GLY A 102 ? 0.1356 0.1167 0.1471 0.0074  0.0047  0.0146  102 GLY A C   
844  O  O   . GLY A 102 ? 0.1453 0.1232 0.1636 -0.0084 0.0232  0.0200  102 GLY A O   
845  N  N   A GLN A 103 ? 0.0975 0.1011 0.1494 -0.0066 0.0165  0.0064  103 GLN A N   
846  N  N   B GLN A 103 ? 0.1072 0.1070 0.1399 0.0002  0.0131  0.0093  103 GLN A N   
847  C  CA  A GLN A 103 ? 0.1146 0.1115 0.0930 -0.0013 -0.0036 0.0027  103 GLN A CA  
848  C  CA  B GLN A 103 ? 0.1072 0.1104 0.1081 0.0111  0.0070  0.0079  103 GLN A CA  
849  C  C   A GLN A 103 ? 0.0878 0.0992 0.0999 -0.0001 0.0220  -0.0055 103 GLN A C   
850  C  C   B GLN A 103 ? 0.0907 0.0986 0.0975 0.0002  0.0215  -0.0053 103 GLN A C   
851  O  O   A GLN A 103 ? 0.1108 0.0986 0.1004 0.0102  0.0132  -0.0064 103 GLN A O   
852  O  O   B GLN A 103 ? 0.1010 0.0964 0.1099 -0.0063 0.0122  -0.0122 103 GLN A O   
853  C  CB  A GLN A 103 ? 0.1181 0.0860 0.1183 0.0022  0.0208  0.0113  103 GLN A CB  
854  C  CB  B GLN A 103 ? 0.1041 0.2062 0.0901 0.0362  0.0108  0.0122  103 GLN A CB  
855  C  CG  A GLN A 103 ? 0.0937 0.1742 0.1200 0.0050  0.0348  -0.0141 103 GLN A CG  
856  C  CG  B GLN A 103 ? 0.1363 0.1263 0.1403 0.0344  0.0666  0.0125  103 GLN A CG  
857  C  CD  A GLN A 103 ? 0.1482 0.1555 0.1726 0.0260  0.0800  0.0299  103 GLN A CD  
858  C  CD  B GLN A 103 ? 0.1360 0.1243 0.1755 0.0034  0.0403  0.0129  103 GLN A CD  
859  O  OE1 A GLN A 103 ? 0.1579 0.1629 0.2166 0.0560  0.0716  0.0320  103 GLN A OE1 
860  O  OE1 B GLN A 103 ? 0.1491 0.1873 0.2464 0.0461  0.0642  0.0844  103 GLN A OE1 
861  N  NE2 A GLN A 103 ? 0.1270 0.1848 0.1812 0.0037  0.0272  0.0086  103 GLN A NE2 
862  N  NE2 B GLN A 103 ? 0.1352 0.1426 0.1667 0.0217  0.0397  -0.0335 103 GLN A NE2 
863  N  N   . GLY A 104 ? 0.0809 0.0956 0.0975 0.0085  0.0173  -0.0059 104 GLY A N   
864  C  CA  . GLY A 104 ? 0.0898 0.0963 0.0902 -0.0010 0.0103  0.0003  104 GLY A CA  
865  C  C   . GLY A 104 ? 0.0686 0.0950 0.0959 -0.0119 0.0044  0.0000  104 GLY A C   
866  O  O   . GLY A 104 ? 0.0787 0.1010 0.1050 -0.0122 0.0080  -0.0013 104 GLY A O   
867  N  N   . SER A 105 ? 0.0774 0.1051 0.0729 -0.0060 0.0062  -0.0083 105 SER A N   
868  C  CA  . SER A 105 ? 0.0770 0.0999 0.0816 -0.0190 0.0108  -0.0109 105 SER A CA  
869  C  C   . SER A 105 ? 0.0610 0.0826 0.0892 -0.0041 0.0122  0.0015  105 SER A C   
870  O  O   . SER A 105 ? 0.0878 0.0911 0.1002 0.0057  -0.0138 -0.0087 105 SER A O   
871  C  CB  . SER A 105 ? 0.0717 0.0878 0.0871 -0.0153 0.0029  0.0067  105 SER A CB  
872  O  OG  . SER A 105 ? 0.0772 0.0836 0.0941 -0.0051 0.0021  0.0016  105 SER A OG  
873  N  N   . GLU A 106 ? 0.0643 0.0880 0.0813 -0.0102 -0.0001 -0.0100 106 GLU A N   
874  C  CA  . GLU A 106 ? 0.0673 0.0898 0.0774 -0.0107 -0.0068 -0.0111 106 GLU A CA  
875  C  C   . GLU A 106 ? 0.0619 0.0868 0.0855 -0.0062 -0.0082 -0.0077 106 GLU A C   
876  O  O   . GLU A 106 ? 0.0716 0.0971 0.0916 0.0055  -0.0026 -0.0062 106 GLU A O   
877  C  CB  . GLU A 106 ? 0.0803 0.0884 0.0845 -0.0146 0.0089  -0.0044 106 GLU A CB  
878  C  CG  . GLU A 106 ? 0.1176 0.1054 0.1058 -0.0144 0.0311  -0.0057 106 GLU A CG  
879  C  CD  . GLU A 106 ? 0.0695 0.0914 0.0995 0.0000  0.0144  -0.0151 106 GLU A CD  
880  O  OE1 . GLU A 106 ? 0.0590 0.0986 0.0993 -0.0063 0.0013  -0.0117 106 GLU A OE1 
881  O  OE2 . GLU A 106 ? 0.0682 0.1248 0.1185 -0.0030 0.0194  -0.0233 106 GLU A OE2 
882  N  N   . HIS A 107 ? 0.0538 0.0878 0.0779 -0.0011 -0.0052 0.0012  107 HIS A N   
883  C  CA  . HIS A 107 ? 0.0681 0.0810 0.0697 0.0017  -0.0125 -0.0016 107 HIS A CA  
884  C  C   . HIS A 107 ? 0.0591 0.0959 0.0721 0.0082  0.0001  0.0002  107 HIS A C   
885  O  O   . HIS A 107 ? 0.0697 0.0916 0.0784 -0.0013 0.0000  -0.0003 107 HIS A O   
886  C  CB  . HIS A 107 ? 0.0664 0.0882 0.0824 0.0033  0.0018  -0.0038 107 HIS A CB  
887  C  CG  . HIS A 107 ? 0.0515 0.0896 0.0745 0.0089  -0.0005 -0.0066 107 HIS A CG  
888  N  ND1 . HIS A 107 ? 0.0754 0.0816 0.0813 0.0066  -0.0114 -0.0015 107 HIS A ND1 
889  C  CD2 . HIS A 107 ? 0.0529 0.0859 0.0834 0.0201  -0.0048 -0.0060 107 HIS A CD2 
890  C  CE1 . HIS A 107 ? 0.0650 0.0877 0.0829 0.0158  -0.0145 0.0003  107 HIS A CE1 
891  N  NE2 . HIS A 107 ? 0.0595 0.0907 0.0823 0.0126  -0.0142 -0.0161 107 HIS A NE2 
892  N  N   . THR A 108 ? 0.0724 0.0986 0.0860 -0.0004 -0.0016 0.0024  108 THR A N   
893  C  CA  . THR A 108 ? 0.0862 0.0765 0.0928 0.0119  0.0019  0.0003  108 THR A CA  
894  C  C   . THR A 108 ? 0.0769 0.0916 0.0802 0.0004  -0.0144 0.0019  108 THR A C   
895  O  O   . THR A 108 ? 0.0889 0.0925 0.0862 0.0018  -0.0066 0.0023  108 THR A O   
896  C  CB  . THR A 108 ? 0.0794 0.1095 0.1090 0.0188  -0.0192 -0.0075 108 THR A CB  
897  O  OG1 . THR A 108 ? 0.0943 0.1093 0.1056 0.0132  -0.0296 -0.0004 108 THR A OG1 
898  C  CG2 . THR A 108 ? 0.0811 0.1275 0.1101 0.0227  0.0035  0.0006  108 THR A CG2 
899  N  N   . VAL A 109 ? 0.0869 0.0916 0.0961 0.0022  -0.0102 0.0149  109 VAL A N   
900  C  CA  . VAL A 109 ? 0.1065 0.1114 0.0864 -0.0059 0.0068  0.0181  109 VAL A CA  
901  C  C   . VAL A 109 ? 0.0815 0.1081 0.1124 -0.0038 0.0071  0.0110  109 VAL A C   
902  O  O   . VAL A 109 ? 0.1047 0.1000 0.1074 0.0008  0.0053  0.0190  109 VAL A O   
903  C  CB  . VAL A 109 ? 0.0813 0.1174 0.1084 -0.0003 0.0010  0.0242  109 VAL A CB  
904  C  CG1 . VAL A 109 ? 0.1018 0.1424 0.1084 -0.0017 0.0125  0.0291  109 VAL A CG1 
905  C  CG2 . VAL A 109 ? 0.1038 0.1311 0.1394 0.0134  -0.0121 0.0337  109 VAL A CG2 
906  N  N   . ASP A 110 ? 0.1218 0.1205 0.0900 0.0300  0.0044  0.0187  110 ASP A N   
907  C  CA  . ASP A 110 ? 0.1410 0.1077 0.0999 0.0256  0.0092  0.0276  110 ASP A CA  
908  C  C   . ASP A 110 ? 0.1537 0.1029 0.1017 0.0074  -0.0055 0.0198  110 ASP A C   
909  O  O   . ASP A 110 ? 0.1543 0.1036 0.1225 0.0145  -0.0032 0.0251  110 ASP A O   
910  C  CB  . ASP A 110 ? 0.1875 0.1313 0.1066 0.0179  0.0342  0.0340  110 ASP A CB  
911  C  CG  . ASP A 110 ? 0.1789 0.1424 0.1200 0.0043  0.0158  0.0392  110 ASP A CG  
912  O  OD1 . ASP A 110 ? 0.2069 0.1509 0.1406 0.0222  0.0392  0.0337  110 ASP A OD1 
913  O  OD2 . ASP A 110 ? 0.1665 0.2013 0.1713 0.0178  0.0151  0.0205  110 ASP A OD2 
914  N  N   . LYS A 111 ? 0.1092 0.1126 0.1062 0.0217  -0.0176 0.0067  111 LYS A N   
915  C  CA  . LYS A 111 ? 0.1268 0.1149 0.1210 0.0287  -0.0152 0.0154  111 LYS A CA  
916  C  C   . LYS A 111 ? 0.1238 0.1099 0.0964 0.0158  -0.0037 0.0111  111 LYS A C   
917  O  O   . LYS A 111 ? 0.1270 0.1408 0.1300 0.0183  0.0115  -0.0061 111 LYS A O   
918  C  CB  . LYS A 111 ? 0.1471 0.1539 0.1289 0.0397  -0.0337 0.0229  111 LYS A CB  
919  C  CG  . LYS A 111 ? 0.2441 0.1816 0.1773 0.0805  -0.0841 0.0167  111 LYS A CG  
920  C  CD  . LYS A 111 ? 0.2119 0.2635 0.2101 0.0508  -0.0977 -0.0588 111 LYS A CD  
921  C  CE  . LYS A 111 ? 0.2567 0.2896 0.2663 0.0602  -0.1424 -0.0391 111 LYS A CE  
922  N  NZ  . LYS A 111 ? 0.3014 0.3483 0.3037 0.0877  -0.1296 -0.0071 111 LYS A NZ  
923  N  N   . LYS A 112 ? 0.1047 0.0977 0.1044 0.0124  -0.0099 0.0122  112 LYS A N   
924  C  CA  . LYS A 112 ? 0.1178 0.1183 0.0947 -0.0050 0.0055  0.0012  112 LYS A CA  
925  C  C   . LYS A 112 ? 0.0737 0.0995 0.1017 0.0084  -0.0166 0.0025  112 LYS A C   
926  O  O   . LYS A 112 ? 0.1071 0.0934 0.0898 0.0027  0.0000  0.0069  112 LYS A O   
927  C  CB  . LYS A 112 ? 0.1054 0.1351 0.1297 -0.0201 -0.0148 0.0054  112 LYS A CB  
928  C  CG  . LYS A 112 ? 0.0977 0.1733 0.1243 -0.0159 0.0135  -0.0187 112 LYS A CG  
929  C  CD  . LYS A 112 ? 0.1036 0.2056 0.1460 0.0031  -0.0138 0.0051  112 LYS A CD  
930  C  CE  . LYS A 112 ? 0.1749 0.1654 0.1661 -0.0011 -0.0451 -0.0025 112 LYS A CE  
931  N  NZ  . LYS A 112 ? 0.1821 0.1667 0.1744 -0.0079 -0.0197 0.0163  112 LYS A NZ  
932  N  N   A LYS A 113 ? 0.0930 0.1142 0.0876 0.0067  -0.0071 -0.0011 113 LYS A N   
933  N  N   B LYS A 113 ? 0.0905 0.1051 0.0934 0.0249  -0.0031 0.0092  113 LYS A N   
934  C  CA  A LYS A 113 ? 0.0887 0.0999 0.0977 0.0105  0.0025  0.0021  113 LYS A CA  
935  C  CA  B LYS A 113 ? 0.0729 0.1243 0.0930 0.0179  -0.0189 0.0250  113 LYS A CA  
936  C  C   A LYS A 113 ? 0.1068 0.0842 0.0984 0.0019  0.0083  0.0096  113 LYS A C   
937  C  C   B LYS A 113 ? 0.0801 0.0937 0.1051 0.0086  -0.0099 0.0006  113 LYS A C   
938  O  O   A LYS A 113 ? 0.1035 0.0877 0.1298 -0.0122 0.0074  0.0171  113 LYS A O   
939  O  O   B LYS A 113 ? 0.1022 0.0891 0.0984 0.0183  -0.0046 -0.0055 113 LYS A O   
940  C  CB  A LYS A 113 ? 0.0846 0.1052 0.1120 -0.0109 -0.0004 -0.0160 113 LYS A CB  
941  C  CB  B LYS A 113 ? 0.0930 0.1098 0.1164 0.0238  -0.0149 0.0087  113 LYS A CB  
942  C  CG  A LYS A 113 ? 0.0763 0.0907 0.1300 0.0120  -0.0038 0.0087  113 LYS A CG  
943  C  CG  B LYS A 113 ? 0.0920 0.1505 0.1132 0.0216  -0.0058 -0.0039 113 LYS A CG  
944  C  CD  A LYS A 113 ? 0.0869 0.1390 0.1613 -0.0052 0.0201  -0.0182 113 LYS A CD  
945  C  CD  B LYS A 113 ? 0.0950 0.0943 0.1817 0.0210  -0.0106 -0.0080 113 LYS A CD  
946  C  CE  A LYS A 113 ? 0.1123 0.1415 0.1807 0.0171  -0.0036 -0.0433 113 LYS A CE  
947  C  CE  B LYS A 113 ? 0.1297 0.1900 0.1686 0.0094  -0.0223 -0.0412 113 LYS A CE  
948  N  NZ  A LYS A 113 ? 0.0700 0.1992 0.1945 -0.0026 -0.0301 -0.0083 113 LYS A NZ  
949  N  NZ  B LYS A 113 ? 0.1812 0.1949 0.2518 0.0421  0.0563  -0.0096 113 LYS A NZ  
950  N  N   . TYR A 114 ? 0.0984 0.0913 0.0954 -0.0015 -0.0060 0.0057  114 TYR A N   
951  C  CA  . TYR A 114 ? 0.0896 0.1032 0.0925 0.0040  -0.0042 0.0055  114 TYR A CA  
952  C  C   . TYR A 114 ? 0.0795 0.0746 0.1029 0.0002  -0.0003 0.0026  114 TYR A C   
953  O  O   . TYR A 114 ? 0.0834 0.1070 0.1020 -0.0037 0.0070  -0.0040 114 TYR A O   
954  C  CB  . TYR A 114 ? 0.0750 0.0914 0.0996 0.0073  -0.0068 0.0021  114 TYR A CB  
955  C  CG  . TYR A 114 ? 0.0959 0.0853 0.1085 0.0120  -0.0114 0.0139  114 TYR A CG  
956  C  CD1 . TYR A 114 ? 0.1284 0.0966 0.1077 0.0199  0.0013  0.0109  114 TYR A CD1 
957  C  CD2 . TYR A 114 ? 0.0835 0.1070 0.1327 -0.0016 0.0006  0.0184  114 TYR A CD2 
958  C  CE1 . TYR A 114 ? 0.1694 0.1266 0.1068 0.0271  0.0124  0.0127  114 TYR A CE1 
959  C  CE2 . TYR A 114 ? 0.1004 0.1430 0.1471 -0.0022 0.0155  0.0114  114 TYR A CE2 
960  C  CZ  . TYR A 114 ? 0.1237 0.1480 0.1453 0.0140  0.0453  0.0236  114 TYR A CZ  
961  O  OH  . TYR A 114 ? 0.1999 0.2196 0.1970 -0.0032 0.1109  0.0062  114 TYR A OH  
962  N  N   . ALA A 115 ? 0.0930 0.0831 0.0974 -0.0190 -0.0089 0.0020  115 ALA A N   
963  C  CA  . ALA A 115 ? 0.0986 0.0812 0.1033 -0.0219 0.0121  -0.0047 115 ALA A CA  
964  C  C   . ALA A 115 ? 0.1061 0.0817 0.0893 -0.0109 0.0027  -0.0026 115 ALA A C   
965  O  O   . ALA A 115 ? 0.0974 0.0877 0.1102 -0.0170 0.0057  -0.0094 115 ALA A O   
966  C  CB  . ALA A 115 ? 0.1129 0.1038 0.1049 -0.0376 -0.0082 -0.0122 115 ALA A CB  
967  N  N   . ALA A 116 ? 0.0877 0.0722 0.0882 -0.0066 -0.0011 0.0002  116 ALA A N   
968  C  CA  . ALA A 116 ? 0.0941 0.0877 0.0867 -0.0076 0.0068  0.0048  116 ALA A CA  
969  C  C   . ALA A 116 ? 0.0864 0.0784 0.0714 -0.0079 -0.0058 0.0071  116 ALA A C   
970  O  O   . ALA A 116 ? 0.0820 0.0851 0.0839 -0.0113 -0.0005 0.0074  116 ALA A O   
971  C  CB  . ALA A 116 ? 0.1120 0.1102 0.0818 -0.0022 -0.0046 0.0010  116 ALA A CB  
972  N  N   . GLU A 117 ? 0.0908 0.0695 0.0842 -0.0034 -0.0037 0.0032  117 GLU A N   
973  C  CA  . GLU A 117 ? 0.0719 0.0763 0.0743 -0.0059 -0.0033 -0.0008 117 GLU A CA  
974  C  C   . GLU A 117 ? 0.0831 0.0889 0.0630 -0.0107 -0.0057 0.0011  117 GLU A C   
975  O  O   . GLU A 117 ? 0.0959 0.1036 0.0912 -0.0043 0.0124  0.0166  117 GLU A O   
976  C  CB  . GLU A 117 ? 0.0853 0.0840 0.0770 -0.0152 -0.0029 -0.0068 117 GLU A CB  
977  C  CG  . GLU A 117 ? 0.0807 0.1058 0.0762 -0.0032 -0.0162 -0.0004 117 GLU A CG  
978  C  CD  . GLU A 117 ? 0.0562 0.0866 0.0778 -0.0106 0.0055  0.0037  117 GLU A CD  
979  O  OE1 . GLU A 117 ? 0.0841 0.1043 0.0848 0.0041  -0.0111 -0.0013 117 GLU A OE1 
980  O  OE2 . GLU A 117 ? 0.0889 0.0995 0.0785 -0.0068 -0.0153 -0.0021 117 GLU A OE2 
981  N  N   . LEU A 118 ? 0.0749 0.0783 0.0716 -0.0027 -0.0098 0.0031  118 LEU A N   
982  C  CA  . LEU A 118 ? 0.0873 0.0804 0.0722 0.0003  -0.0179 0.0037  118 LEU A CA  
983  C  C   . LEU A 118 ? 0.0916 0.0779 0.0737 -0.0091 -0.0091 0.0054  118 LEU A C   
984  O  O   . LEU A 118 ? 0.0849 0.0783 0.0712 -0.0063 -0.0055 0.0006  118 LEU A O   
985  C  CB  . LEU A 118 ? 0.0869 0.0853 0.0916 -0.0066 -0.0249 0.0017  118 LEU A CB  
986  C  CG  . LEU A 118 ? 0.0921 0.1011 0.0974 0.0074  -0.0293 0.0145  118 LEU A CG  
987  C  CD1 . LEU A 118 ? 0.1318 0.0934 0.0905 -0.0013 -0.0372 0.0230  118 LEU A CD1 
988  C  CD2 . LEU A 118 ? 0.0925 0.1309 0.1221 0.0027  -0.0284 0.0011  118 LEU A CD2 
989  N  N   . HIS A 119 ? 0.0889 0.0655 0.0681 -0.0053 -0.0135 0.0017  119 HIS A N   
990  C  CA  . HIS A 119 ? 0.0757 0.0855 0.0696 -0.0141 -0.0072 -0.0008 119 HIS A CA  
991  C  C   . HIS A 119 ? 0.0744 0.0770 0.0588 -0.0165 -0.0141 0.0052  119 HIS A C   
992  O  O   . HIS A 119 ? 0.1069 0.0866 0.0703 -0.0038 -0.0050 0.0107  119 HIS A O   
993  C  CB  . HIS A 119 ? 0.0707 0.0798 0.0837 -0.0067 -0.0128 0.0037  119 HIS A CB  
994  C  CG  . HIS A 119 ? 0.0620 0.0780 0.0619 -0.0127 -0.0033 -0.0079 119 HIS A CG  
995  N  ND1 . HIS A 119 ? 0.0650 0.0839 0.0621 -0.0051 0.0009  -0.0003 119 HIS A ND1 
996  C  CD2 . HIS A 119 ? 0.0691 0.0871 0.0787 -0.0038 -0.0158 0.0040  119 HIS A CD2 
997  C  CE1 . HIS A 119 ? 0.0784 0.0939 0.0577 -0.0234 -0.0011 0.0016  119 HIS A CE1 
998  N  NE2 . HIS A 119 ? 0.0627 0.0919 0.0756 -0.0070 -0.0130 0.0114  119 HIS A NE2 
999  N  N   . LEU A 120 ? 0.0798 0.0731 0.0743 0.0015  -0.0146 -0.0006 120 LEU A N   
1000 C  CA  . LEU A 120 ? 0.0803 0.0718 0.1029 0.0046  -0.0220 0.0019  120 LEU A CA  
1001 C  C   . LEU A 120 ? 0.0774 0.0738 0.0633 0.0062  -0.0111 0.0062  120 LEU A C   
1002 O  O   . LEU A 120 ? 0.0734 0.0803 0.0729 -0.0095 -0.0096 -0.0022 120 LEU A O   
1003 C  CB  . LEU A 120 ? 0.0775 0.0963 0.0936 -0.0027 -0.0201 -0.0037 120 LEU A CB  
1004 C  CG  . LEU A 120 ? 0.1209 0.1108 0.1070 -0.0237 -0.0445 0.0005  120 LEU A CG  
1005 C  CD1 . LEU A 120 ? 0.1708 0.1417 0.1316 -0.0739 -0.0375 0.0129  120 LEU A CD1 
1006 C  CD2 . LEU A 120 ? 0.1277 0.1372 0.1205 -0.0054 -0.0671 -0.0089 120 LEU A CD2 
1007 N  N   . VAL A 121 ? 0.0721 0.0845 0.0840 -0.0098 -0.0066 0.0095  121 VAL A N   
1008 C  CA  . VAL A 121 ? 0.0848 0.0738 0.0875 -0.0139 -0.0083 0.0130  121 VAL A CA  
1009 C  C   . VAL A 121 ? 0.0811 0.0779 0.0878 -0.0134 -0.0022 -0.0024 121 VAL A C   
1010 O  O   . VAL A 121 ? 0.1060 0.0882 0.0859 0.0046  -0.0104 0.0084  121 VAL A O   
1011 C  CB  . VAL A 121 ? 0.0867 0.0818 0.0965 -0.0170 0.0063  -0.0005 121 VAL A CB  
1012 C  CG1 . VAL A 121 ? 0.0972 0.0984 0.1200 -0.0274 0.0001  0.0031  121 VAL A CG1 
1013 C  CG2 . VAL A 121 ? 0.1052 0.0873 0.1041 0.0013  0.0070  -0.0013 121 VAL A CG2 
1014 N  N   . HIS A 122 ? 0.0758 0.0785 0.0842 -0.0093 -0.0113 -0.0038 122 HIS A N   
1015 C  CA  . HIS A 122 ? 0.0875 0.0748 0.0878 -0.0035 -0.0076 -0.0017 122 HIS A CA  
1016 C  C   . HIS A 122 ? 0.0884 0.0889 0.0916 0.0019  -0.0055 0.0083  122 HIS A C   
1017 O  O   . HIS A 122 ? 0.0984 0.0857 0.1065 -0.0137 -0.0186 0.0086  122 HIS A O   
1018 C  CB  . HIS A 122 ? 0.0848 0.0846 0.1080 0.0018  -0.0098 -0.0020 122 HIS A CB  
1019 C  CG  . HIS A 122 ? 0.0721 0.0853 0.0948 -0.0092 -0.0058 0.0015  122 HIS A CG  
1020 N  ND1 . HIS A 122 ? 0.0702 0.0858 0.1076 -0.0048 -0.0050 0.0038  122 HIS A ND1 
1021 C  CD2 . HIS A 122 ? 0.0763 0.1171 0.1084 0.0000  -0.0218 -0.0060 122 HIS A CD2 
1022 C  CE1 . HIS A 122 ? 0.0677 0.1096 0.1208 -0.0037 -0.0109 -0.0048 122 HIS A CE1 
1023 N  NE2 . HIS A 122 ? 0.0793 0.1071 0.1218 -0.0111 -0.0091 0.0010  122 HIS A NE2 
1024 N  N   . TRP A 123 ? 0.0805 0.0747 0.0984 -0.0068 -0.0048 -0.0049 123 TRP A N   
1025 C  CA  . TRP A 123 ? 0.0873 0.0760 0.1031 -0.0107 -0.0083 -0.0049 123 TRP A CA  
1026 C  C   . TRP A 123 ? 0.0776 0.0829 0.1004 -0.0077 -0.0146 0.0020  123 TRP A C   
1027 O  O   . TRP A 123 ? 0.0831 0.0920 0.1252 0.0029  -0.0152 -0.0144 123 TRP A O   
1028 C  CB  . TRP A 123 ? 0.1087 0.1126 0.1133 -0.0261 -0.0020 0.0029  123 TRP A CB  
1029 C  CG  . TRP A 123 ? 0.1216 0.0943 0.1234 -0.0234 -0.0111 -0.0053 123 TRP A CG  
1030 C  CD1 . TRP A 123 ? 0.1751 0.0954 0.1072 -0.0230 -0.0188 -0.0009 123 TRP A CD1 
1031 C  CD2 . TRP A 123 ? 0.1658 0.0853 0.1149 -0.0132 0.0031  0.0030  123 TRP A CD2 
1032 N  NE1 . TRP A 123 ? 0.1778 0.0869 0.1307 -0.0071 -0.0272 0.0054  123 TRP A NE1 
1033 C  CE2 . TRP A 123 ? 0.1965 0.0770 0.1487 -0.0233 -0.0293 0.0096  123 TRP A CE2 
1034 C  CE3 . TRP A 123 ? 0.2180 0.0807 0.1270 -0.0311 0.0119  0.0001  123 TRP A CE3 
1035 C  CZ2 . TRP A 123 ? 0.2227 0.0851 0.1735 -0.0130 -0.0012 0.0011  123 TRP A CZ2 
1036 C  CZ3 . TRP A 123 ? 0.2761 0.0914 0.1480 -0.0219 -0.0038 0.0199  123 TRP A CZ3 
1037 C  CH2 . TRP A 123 ? 0.2893 0.0862 0.1674 -0.0137 -0.0168 0.0220  123 TRP A CH2 
1038 N  N   . ASN A 124 ? 0.0937 0.0855 0.1093 -0.0009 -0.0111 -0.0177 124 ASN A N   
1039 C  CA  . ASN A 124 ? 0.1049 0.0894 0.1086 0.0130  -0.0054 -0.0142 124 ASN A CA  
1040 C  C   . ASN A 124 ? 0.0972 0.1016 0.1095 0.0085  -0.0099 -0.0229 124 ASN A C   
1041 O  O   . ASN A 124 ? 0.1185 0.1026 0.1108 0.0081  -0.0029 -0.0089 124 ASN A O   
1042 C  CB  . ASN A 124 ? 0.1115 0.1038 0.1054 -0.0089 0.0038  -0.0122 124 ASN A CB  
1043 C  CG  . ASN A 124 ? 0.1157 0.0880 0.1196 0.0006  -0.0025 -0.0172 124 ASN A CG  
1044 O  OD1 . ASN A 124 ? 0.1268 0.1123 0.1408 0.0197  0.0060  -0.0207 124 ASN A OD1 
1045 N  ND2 . ASN A 124 ? 0.1609 0.1176 0.1144 -0.0010 0.0027  -0.0218 124 ASN A ND2 
1046 N  N   . THR A 125 ? 0.1112 0.0964 0.1412 0.0234  -0.0215 -0.0138 125 THR A N   
1047 C  CA  . THR A 125 ? 0.1255 0.0880 0.1735 0.0109  -0.0212 -0.0010 125 THR A CA  
1048 C  C   . THR A 125 ? 0.1491 0.0989 0.1602 0.0325  0.0114  -0.0033 125 THR A C   
1049 O  O   . THR A 125 ? 0.1769 0.1069 0.1706 0.0143  -0.0162 0.0119  125 THR A O   
1050 C  CB  . THR A 125 ? 0.1403 0.1521 0.2112 0.0059  -0.0513 0.0266  125 THR A CB  
1051 O  OG1 . THR A 125 ? 0.1879 0.1758 0.3015 0.0747  0.0505  0.0313  125 THR A OG1 
1052 C  CG2 . THR A 125 ? 0.1900 0.1478 0.2693 -0.0083 -0.0930 -0.0038 125 THR A CG2 
1053 N  N   . LYS A 126 ? 0.1611 0.0947 0.1390 0.0117  0.0143  -0.0239 127 LYS A N   
1054 C  CA  . LYS A 126 ? 0.1521 0.1144 0.1512 -0.0058 0.0122  -0.0317 127 LYS A CA  
1055 C  C   . LYS A 126 ? 0.1699 0.0798 0.1611 0.0021  0.0026  -0.0135 127 LYS A C   
1056 O  O   . LYS A 126 ? 0.1888 0.1142 0.1708 -0.0217 0.0176  -0.0362 127 LYS A O   
1057 C  CB  . LYS A 126 ? 0.2103 0.1564 0.1613 -0.0230 0.0000  -0.0252 127 LYS A CB  
1058 C  CG  . LYS A 126 ? 0.1961 0.1672 0.1516 -0.0208 -0.0236 -0.0095 127 LYS A CG  
1059 C  CD  . LYS A 126 ? 0.3131 0.2126 0.1771 -0.0578 0.0146  -0.0469 127 LYS A CD  
1060 C  CE  . LYS A 126 ? 0.1983 0.2544 0.5725 0.0618  -0.1108 -0.1391 127 LYS A CE  
1061 N  NZ  . LYS A 126 ? 0.8083 0.5468 0.4968 -0.1345 -0.2443 -0.1732 127 LYS A NZ  
1062 N  N   . TYR A 127 ? 0.1534 0.0857 0.1227 0.0004  -0.0145 -0.0151 128 TYR A N   
1063 C  CA  . TYR A 127 ? 0.1573 0.0968 0.1261 -0.0156 -0.0113 0.0081  128 TYR A CA  
1064 C  C   . TYR A 127 ? 0.1570 0.1038 0.1431 -0.0089 -0.0119 -0.0061 128 TYR A C   
1065 O  O   . TYR A 127 ? 0.1656 0.1004 0.1401 -0.0082 0.0142  -0.0102 128 TYR A O   
1066 C  CB  . TYR A 127 ? 0.1722 0.1036 0.1507 0.0082  0.0024  0.0010  128 TYR A CB  
1067 C  CG  . TYR A 127 ? 0.1178 0.1108 0.1252 -0.0023 -0.0099 -0.0139 128 TYR A CG  
1068 C  CD1 . TYR A 127 ? 0.1656 0.1065 0.1550 -0.0089 -0.0138 -0.0135 128 TYR A CD1 
1069 C  CD2 . TYR A 127 ? 0.1027 0.1149 0.1297 -0.0031 0.0012  -0.0002 128 TYR A CD2 
1070 C  CE1 . TYR A 127 ? 0.1681 0.1365 0.1469 -0.0010 -0.0281 -0.0277 128 TYR A CE1 
1071 C  CE2 . TYR A 127 ? 0.1004 0.1168 0.1254 -0.0033 -0.0059 -0.0233 128 TYR A CE2 
1072 C  CZ  . TYR A 127 ? 0.1724 0.1347 0.1374 0.0088  -0.0122 -0.0203 128 TYR A CZ  
1073 O  OH  . TYR A 127 ? 0.2067 0.1437 0.1388 0.0272  -0.0322 -0.0462 128 TYR A OH  
1074 N  N   . GLY A 128 ? 0.1460 0.0925 0.1333 -0.0156 -0.0003 0.0102  129 GLY A N   
1075 C  CA  . GLY A 128 ? 0.1940 0.1018 0.1437 0.0027  0.0305  0.0086  129 GLY A CA  
1076 C  C   . GLY A 128 ? 0.1825 0.1137 0.1205 0.0012  -0.0150 0.0299  129 GLY A C   
1077 O  O   . GLY A 128 ? 0.2626 0.1041 0.1356 0.0063  -0.0168 0.0219  129 GLY A O   
1078 N  N   . ASP A 129 ? 0.2106 0.1151 0.1219 0.0114  -0.0142 -0.0062 130 ASP A N   
1079 C  CA  . ASP A 129 ? 0.2812 0.1203 0.1122 0.0309  0.0031  0.0008  130 ASP A CA  
1080 C  C   . ASP A 129 ? 0.2347 0.1216 0.1149 0.0075  -0.0185 -0.0013 130 ASP A C   
1081 O  O   . ASP A 129 ? 0.2632 0.1248 0.1106 0.0281  -0.0131 -0.0023 130 ASP A O   
1082 C  CB  . ASP A 129 ? 0.2820 0.1800 0.1801 0.0612  0.0626  0.0325  130 ASP A CB  
1083 C  CG  . ASP A 129 ? 0.2531 0.1327 0.1654 0.0502  0.0386  0.0312  130 ASP A CG  
1084 O  OD1 . ASP A 129 ? 0.4796 0.1927 0.2815 -0.1037 -0.1600 -0.0041 130 ASP A OD1 
1085 O  OD2 . ASP A 129 ? 0.2879 0.2101 0.3357 0.0037  0.1617  0.0584  130 ASP A OD2 
1086 N  N   . PHE A 130 ? 0.2218 0.1114 0.1126 0.0102  0.0137  0.0066  131 PHE A N   
1087 C  CA  . PHE A 130 ? 0.1737 0.1049 0.1099 0.0001  -0.0156 -0.0041 131 PHE A CA  
1088 C  C   . PHE A 130 ? 0.1825 0.0945 0.1160 -0.0039 0.0293  0.0011  131 PHE A C   
1089 O  O   . PHE A 130 ? 0.1532 0.1160 0.1027 -0.0125 0.0006  0.0021  131 PHE A O   
1090 C  CB  . PHE A 130 ? 0.2067 0.1164 0.1120 0.0080  -0.0018 -0.0244 131 PHE A CB  
1091 C  CG  . PHE A 130 ? 0.1527 0.0993 0.1119 0.0054  0.0239  -0.0187 131 PHE A CG  
1092 C  CD1 . PHE A 130 ? 0.1737 0.1119 0.1056 -0.0296 -0.0004 -0.0147 131 PHE A CD1 
1093 C  CD2 . PHE A 130 ? 0.1988 0.1115 0.1643 -0.0036 0.0370  -0.0089 131 PHE A CD2 
1094 C  CE1 . PHE A 130 ? 0.1812 0.1227 0.1403 -0.0329 0.0122  -0.0184 131 PHE A CE1 
1095 C  CE2 . PHE A 130 ? 0.2537 0.1430 0.1927 0.0236  0.0521  0.0020  131 PHE A CE2 
1096 C  CZ  . PHE A 130 ? 0.1956 0.1503 0.1643 -0.0174 0.0120  -0.0190 131 PHE A CZ  
1097 N  N   . GLY A 131 ? 0.2186 0.1228 0.1259 -0.0243 0.0539  -0.0066 132 GLY A N   
1098 C  CA  . GLY A 131 ? 0.1997 0.1550 0.1627 -0.0527 0.0648  0.0013  132 GLY A CA  
1099 C  C   . GLY A 131 ? 0.2119 0.1532 0.1419 -0.0370 0.0581  0.0182  132 GLY A C   
1100 O  O   . GLY A 131 ? 0.1970 0.1397 0.2124 -0.0325 0.0454  -0.0348 132 GLY A O   
1101 N  N   . LYS A 132 ? 0.1778 0.1250 0.1602 -0.0476 0.0354  -0.0039 133 LYS A N   
1102 C  CA  . LYS A 132 ? 0.1701 0.1067 0.1548 -0.0252 0.0175  0.0037  133 LYS A CA  
1103 C  C   . LYS A 132 ? 0.1358 0.1033 0.1460 -0.0223 0.0117  -0.0100 133 LYS A C   
1104 O  O   . LYS A 132 ? 0.1397 0.1214 0.1383 -0.0252 0.0038  -0.0208 133 LYS A O   
1105 C  CB  . LYS A 132 ? 0.1334 0.1216 0.1873 -0.0153 -0.0068 -0.0018 133 LYS A CB  
1106 C  CG  . LYS A 132 ? 0.1600 0.1340 0.3141 -0.0183 -0.0113 0.0467  133 LYS A CG  
1107 C  CD  . LYS A 132 ? 0.1546 0.2031 0.4049 -0.0230 -0.0394 0.1132  133 LYS A CD  
1108 C  CE  . LYS A 132 ? 0.2531 0.1505 0.6794 -0.0933 -0.2148 0.0796  133 LYS A CE  
1109 N  NZ  . LYS A 132 ? 0.4537 0.3462 0.5470 -0.1048 -0.1763 -0.0060 133 LYS A NZ  
1110 N  N   . ALA A 133 ? 0.1361 0.1099 0.1266 -0.0494 0.0190  -0.0128 134 ALA A N   
1111 C  CA  . ALA A 133 ? 0.1243 0.1225 0.1081 -0.0283 -0.0086 -0.0032 134 ALA A CA  
1112 C  C   . ALA A 133 ? 0.1018 0.1220 0.0968 -0.0321 -0.0020 -0.0099 134 ALA A C   
1113 O  O   . ALA A 133 ? 0.0950 0.1383 0.1024 -0.0199 -0.0030 -0.0093 134 ALA A O   
1114 C  CB  . ALA A 133 ? 0.1114 0.1108 0.1099 -0.0292 -0.0122 -0.0035 134 ALA A CB  
1115 N  N   . VAL A 134 ? 0.1199 0.1099 0.1183 -0.0223 0.0139  -0.0098 135 VAL A N   
1116 C  CA  . VAL A 134 ? 0.1264 0.1266 0.1193 -0.0268 0.0148  0.0089  135 VAL A CA  
1117 C  C   . VAL A 134 ? 0.1106 0.1275 0.1306 -0.0166 0.0289  0.0012  135 VAL A C   
1118 O  O   . VAL A 134 ? 0.1096 0.1345 0.1491 -0.0064 0.0217  0.0013  135 VAL A O   
1119 C  CB  . VAL A 134 ? 0.1363 0.1329 0.1324 -0.0268 0.0356  -0.0133 135 VAL A CB  
1120 C  CG1 . VAL A 134 ? 0.1722 0.1518 0.1426 -0.0386 0.0106  -0.0165 135 VAL A CG1 
1121 C  CG2 . VAL A 134 ? 0.1552 0.1390 0.1505 -0.0280 0.0385  -0.0060 135 VAL A CG2 
1122 N  N   . GLN A 135 ? 0.1212 0.1203 0.1408 -0.0321 0.0134  -0.0173 136 GLN A N   
1123 C  CA  . GLN A 135 ? 0.1184 0.1428 0.1415 -0.0381 0.0131  -0.0280 136 GLN A CA  
1124 C  C   . GLN A 135 ? 0.1099 0.1390 0.1320 -0.0314 -0.0072 -0.0159 136 GLN A C   
1125 O  O   . GLN A 135 ? 0.1226 0.1993 0.1553 -0.0447 -0.0058 -0.0397 136 GLN A O   
1126 C  CB  . GLN A 135 ? 0.1252 0.1722 0.1609 -0.0647 -0.0158 -0.0016 136 GLN A CB  
1127 C  CG  . GLN A 135 ? 0.2047 0.2123 0.1879 -0.0835 0.0520  0.0173  136 GLN A CG  
1128 C  CD  . GLN A 135 ? 0.2029 0.2338 0.2410 -0.0425 -0.0120 -0.0026 136 GLN A CD  
1129 O  OE1 . GLN A 135 ? 0.3080 0.3167 0.2840 -0.1196 -0.0607 0.0217  136 GLN A OE1 
1130 N  NE2 . GLN A 135 ? 0.1958 0.2771 0.2714 -0.0506 0.0264  0.0579  136 GLN A NE2 
1131 N  N   . GLN A 136 ? 0.0921 0.1316 0.1284 -0.0212 0.0247  -0.0143 137 GLN A N   
1132 C  CA  . GLN A 136 ? 0.1108 0.1250 0.1153 -0.0153 -0.0085 -0.0313 137 GLN A CA  
1133 C  C   . GLN A 136 ? 0.0639 0.1467 0.1113 -0.0093 -0.0053 -0.0271 137 GLN A C   
1134 O  O   . GLN A 136 ? 0.1128 0.1158 0.1036 -0.0075 -0.0085 -0.0159 137 GLN A O   
1135 C  CB  . GLN A 136 ? 0.1223 0.1273 0.1178 0.0115  -0.0060 -0.0024 137 GLN A CB  
1136 C  CG  . GLN A 136 ? 0.2081 0.1525 0.1656 0.0234  0.0181  -0.0042 137 GLN A CG  
1137 C  CD  . GLN A 136 ? 0.1505 0.1828 0.3324 0.0122  0.0523  0.0476  137 GLN A CD  
1138 O  OE1 . GLN A 136 ? 0.2277 0.1803 0.3467 -0.0071 -0.0064 -0.1272 137 GLN A OE1 
1139 N  NE2 . GLN A 136 ? 0.2639 0.2857 0.5562 -0.0105 0.1265  0.1632  137 GLN A NE2 
1140 N  N   . PRO A 137 ? 0.0726 0.1464 0.1075 -0.0118 -0.0132 -0.0244 138 PRO A N   
1141 C  CA  . PRO A 137 ? 0.1103 0.1568 0.1075 0.0070  -0.0143 0.0017  138 PRO A CA  
1142 C  C   . PRO A 137 ? 0.1126 0.1541 0.0782 -0.0075 -0.0022 -0.0088 138 PRO A C   
1143 O  O   . PRO A 137 ? 0.1512 0.1494 0.1787 0.0001  -0.0074 0.0200  138 PRO A O   
1144 C  CB  . PRO A 137 ? 0.1760 0.1983 0.1004 -0.0010 -0.0135 -0.0047 138 PRO A CB  
1145 C  CG  . PRO A 137 ? 0.3353 0.2577 0.1112 -0.0324 -0.0478 -0.0139 138 PRO A CG  
1146 C  CD  . PRO A 137 ? 0.1643 0.2159 0.1088 -0.0555 -0.0317 -0.0383 138 PRO A CD  
1147 N  N   . ASP A 138 ? 0.0813 0.1465 0.0977 0.0002  -0.0095 -0.0122 139 ASP A N   
1148 C  CA  . ASP A 138 ? 0.0807 0.1451 0.1049 -0.0040 0.0027  -0.0174 139 ASP A CA  
1149 C  C   . ASP A 138 ? 0.0826 0.1084 0.0979 -0.0135 -0.0088 -0.0024 139 ASP A C   
1150 O  O   . ASP A 138 ? 0.0945 0.1193 0.1117 -0.0005 -0.0109 -0.0048 139 ASP A O   
1151 C  CB  . ASP A 138 ? 0.1360 0.1500 0.1217 0.0077  0.0247  -0.0154 139 ASP A CB  
1152 C  CG  . ASP A 138 ? 0.1244 0.1699 0.1221 0.0177  -0.0110 -0.0325 139 ASP A CG  
1153 O  OD1 . ASP A 138 ? 0.1518 0.1367 0.1315 0.0055  -0.0019 -0.0378 139 ASP A OD1 
1154 O  OD2 . ASP A 138 ? 0.1783 0.1961 0.1683 0.0240  0.0379  -0.0511 139 ASP A OD2 
1155 N  N   . GLY A 139 ? 0.0864 0.1024 0.0925 -0.0027 -0.0105 -0.0160 140 GLY A N   
1156 C  CA  . GLY A 139 ? 0.0974 0.1024 0.0925 -0.0167 -0.0140 -0.0050 140 GLY A CA  
1157 C  C   . GLY A 139 ? 0.0621 0.0916 0.0885 -0.0070 0.0013  0.0006  140 GLY A C   
1158 O  O   . GLY A 139 ? 0.1001 0.0883 0.0968 0.0027  -0.0153 -0.0049 140 GLY A O   
1159 N  N   . LEU A 140 ? 0.0739 0.0864 0.0866 0.0000  -0.0069 -0.0043 141 LEU A N   
1160 C  CA  . LEU A 140 ? 0.0710 0.0836 0.0824 -0.0122 -0.0004 -0.0132 141 LEU A CA  
1161 C  C   . LEU A 140 ? 0.0688 0.0788 0.0831 -0.0076 -0.0144 -0.0087 141 LEU A C   
1162 O  O   . LEU A 140 ? 0.0759 0.0862 0.0945 -0.0097 -0.0079 -0.0042 141 LEU A O   
1163 C  CB  . LEU A 140 ? 0.0746 0.0858 0.0925 -0.0096 -0.0026 -0.0128 141 LEU A CB  
1164 C  CG  . LEU A 140 ? 0.0877 0.1062 0.1144 0.0054  0.0168  -0.0037 141 LEU A CG  
1165 C  CD1 . LEU A 140 ? 0.0840 0.1045 0.1187 0.0034  0.0151  -0.0089 141 LEU A CD1 
1166 C  CD2 . LEU A 140 ? 0.1223 0.1098 0.1252 0.0272  0.0200  0.0048  141 LEU A CD2 
1167 N  N   . ALA A 141 ? 0.0672 0.0841 0.0919 -0.0088 -0.0093 -0.0013 142 ALA A N   
1168 C  CA  . ALA A 141 ? 0.0781 0.0782 0.0992 -0.0152 -0.0074 -0.0063 142 ALA A CA  
1169 C  C   . ALA A 141 ? 0.0673 0.0898 0.0864 -0.0131 -0.0081 0.0048  142 ALA A C   
1170 O  O   . ALA A 141 ? 0.0859 0.0946 0.0869 -0.0076 -0.0170 0.0060  142 ALA A O   
1171 C  CB  . ALA A 141 ? 0.0803 0.1220 0.1266 -0.0071 0.0133  -0.0011 142 ALA A CB  
1172 N  N   . VAL A 142 ? 0.0595 0.0859 0.0767 -0.0055 -0.0081 0.0059  143 VAL A N   
1173 C  CA  . VAL A 142 ? 0.0670 0.0925 0.0668 -0.0042 -0.0029 0.0026  143 VAL A CA  
1174 C  C   . VAL A 142 ? 0.0775 0.0835 0.0701 -0.0022 0.0000  -0.0006 143 VAL A C   
1175 O  O   . VAL A 142 ? 0.0724 0.0948 0.0717 -0.0059 -0.0115 0.0037  143 VAL A O   
1176 C  CB  . VAL A 142 ? 0.0611 0.1156 0.0836 0.0103  -0.0119 0.0054  143 VAL A CB  
1177 C  CG1 . VAL A 142 ? 0.0851 0.1433 0.0838 0.0234  -0.0185 -0.0186 143 VAL A CG1 
1178 C  CG2 . VAL A 142 ? 0.0771 0.1604 0.1124 -0.0118 -0.0055 0.0389  143 VAL A CG2 
1179 N  N   . LEU A 143 ? 0.0771 0.0721 0.0871 -0.0063 -0.0153 0.0040  144 LEU A N   
1180 C  CA  . LEU A 143 ? 0.0642 0.0841 0.0883 -0.0189 -0.0132 -0.0049 144 LEU A CA  
1181 C  C   . LEU A 143 ? 0.0697 0.0916 0.0748 -0.0236 -0.0106 0.0086  144 LEU A C   
1182 O  O   . LEU A 143 ? 0.1119 0.0950 0.0727 -0.0099 0.0035  0.0044  144 LEU A O   
1183 C  CB  . LEU A 143 ? 0.0891 0.1246 0.1015 -0.0178 -0.0261 0.0142  144 LEU A CB  
1184 C  CG  . LEU A 143 ? 0.0754 0.1329 0.1365 -0.0199 -0.0189 0.0002  144 LEU A CG  
1185 C  CD1 . LEU A 143 ? 0.1071 0.1756 0.1476 -0.0384 -0.0251 0.0361  144 LEU A CD1 
1186 C  CD2 . LEU A 143 ? 0.0709 0.1713 0.1672 -0.0074 -0.0228 0.0141  144 LEU A CD2 
1187 N  N   . GLY A 144 ? 0.0642 0.0790 0.0788 -0.0127 -0.0104 0.0059  145 GLY A N   
1188 C  CA  . GLY A 144 ? 0.0623 0.0894 0.0739 -0.0064 -0.0015 -0.0006 145 GLY A CA  
1189 C  C   . GLY A 144 ? 0.0482 0.0871 0.0778 -0.0052 -0.0160 0.0051  145 GLY A C   
1190 O  O   . GLY A 144 ? 0.0827 0.1007 0.0731 -0.0133 0.0038  -0.0002 145 GLY A O   
1191 N  N   . ILE A 145 ? 0.0616 0.0842 0.0731 -0.0024 -0.0142 -0.0029 146 ILE A N   
1192 C  CA  . ILE A 145 ? 0.0409 0.0868 0.0829 -0.0057 -0.0174 -0.0010 146 ILE A CA  
1193 C  C   . ILE A 145 ? 0.0659 0.0862 0.0714 -0.0100 -0.0186 0.0042  146 ILE A C   
1194 O  O   . ILE A 145 ? 0.0780 0.0779 0.0946 -0.0078 0.0001  0.0044  146 ILE A O   
1195 C  CB  . ILE A 145 ? 0.0639 0.0917 0.1168 0.0041  -0.0306 0.0000  146 ILE A CB  
1196 C  CG1 . ILE A 145 ? 0.0880 0.1163 0.1500 0.0331  -0.0464 0.0035  146 ILE A CG1 
1197 C  CG2 . ILE A 145 ? 0.0646 0.1238 0.1548 -0.0133 -0.0533 0.0022  146 ILE A CG2 
1198 C  CD1 . ILE A 145 ? 0.0822 0.1074 0.1338 0.0122  -0.0302 0.0127  146 ILE A CD1 
1199 N  N   . PHE A 146 ? 0.0752 0.0831 0.0701 -0.0038 -0.0132 0.0065  147 PHE A N   
1200 C  CA  . PHE A 146 ? 0.0705 0.0804 0.0829 0.0022  -0.0152 0.0044  147 PHE A CA  
1201 C  C   . PHE A 146 ? 0.0700 0.0807 0.0855 -0.0077 -0.0089 0.0029  147 PHE A C   
1202 O  O   . PHE A 146 ? 0.0730 0.0932 0.1056 -0.0002 -0.0175 -0.0100 147 PHE A O   
1203 C  CB  . PHE A 146 ? 0.0724 0.0911 0.0839 -0.0087 -0.0237 0.0210  147 PHE A CB  
1204 C  CG  . PHE A 146 ? 0.0577 0.0889 0.0750 -0.0074 -0.0125 0.0100  147 PHE A CG  
1205 C  CD1 . PHE A 146 ? 0.0659 0.0896 0.1002 0.0034  -0.0048 0.0050  147 PHE A CD1 
1206 C  CD2 . PHE A 146 ? 0.0955 0.0831 0.0900 -0.0058 -0.0168 0.0201  147 PHE A CD2 
1207 C  CE1 . PHE A 146 ? 0.0643 0.1013 0.0991 0.0005  -0.0174 0.0011  147 PHE A CE1 
1208 C  CE2 . PHE A 146 ? 0.0658 0.0977 0.0930 -0.0048 -0.0076 0.0085  147 PHE A CE2 
1209 C  CZ  . PHE A 146 ? 0.0664 0.0980 0.0980 -0.0044 -0.0026 0.0190  147 PHE A CZ  
1210 N  N   . LEU A 147 ? 0.0727 0.0842 0.0873 -0.0052 -0.0074 -0.0011 148 LEU A N   
1211 C  CA  . LEU A 147 ? 0.1122 0.0810 0.0789 -0.0156 -0.0214 -0.0044 148 LEU A CA  
1212 C  C   . LEU A 147 ? 0.0789 0.0902 0.0770 -0.0059 -0.0080 -0.0013 148 LEU A C   
1213 O  O   . LEU A 147 ? 0.0776 0.0943 0.1018 -0.0044 -0.0079 0.0055  148 LEU A O   
1214 C  CB  . LEU A 147 ? 0.1040 0.0885 0.0947 -0.0078 -0.0102 -0.0044 148 LEU A CB  
1215 C  CG  . LEU A 147 ? 0.1187 0.0845 0.1076 -0.0209 -0.0245 -0.0044 148 LEU A CG  
1216 C  CD1 . LEU A 147 ? 0.1604 0.0965 0.0869 -0.0081 -0.0318 0.0051  148 LEU A CD1 
1217 C  CD2 . LEU A 147 ? 0.1322 0.1358 0.0963 -0.0148 -0.0271 0.0058  148 LEU A CD2 
1218 N  N   . LYS A 148 ? 0.0893 0.0805 0.1142 -0.0172 -0.0131 -0.0083 149 LYS A N   
1219 C  CA  . LYS A 148 ? 0.1151 0.0829 0.1141 -0.0121 -0.0143 0.0033  149 LYS A CA  
1220 C  C   . LYS A 148 ? 0.0995 0.0941 0.1221 -0.0131 -0.0292 0.0005  149 LYS A C   
1221 O  O   . LYS A 148 ? 0.1220 0.1219 0.1139 0.0084  -0.0390 -0.0020 149 LYS A O   
1222 C  CB  . LYS A 148 ? 0.1345 0.1079 0.1041 -0.0168 -0.0168 0.0143  149 LYS A CB  
1223 C  CG  . LYS A 148 ? 0.1302 0.1376 0.1471 -0.0319 0.0011  0.0289  149 LYS A CG  
1224 C  CD  . LYS A 148 ? 0.1870 0.2551 0.1925 -0.0424 0.0361  0.0297  149 LYS A CD  
1225 C  CE  . LYS A 148 ? 0.2526 0.5049 0.2569 -0.0875 0.0586  0.0851  149 LYS A CE  
1226 N  NZ  . LYS A 148 ? 0.4870 0.8812 0.7011 -0.2288 0.1810  0.4745  149 LYS A NZ  
1227 N  N   . VAL A 149 ? 0.1187 0.0878 0.1264 -0.0074 -0.0154 -0.0109 150 VAL A N   
1228 C  CA  . VAL A 149 ? 0.1363 0.0889 0.1288 -0.0030 -0.0155 -0.0146 150 VAL A CA  
1229 C  C   . VAL A 149 ? 0.1559 0.1096 0.1095 -0.0140 -0.0244 -0.0034 150 VAL A C   
1230 O  O   . VAL A 149 ? 0.1715 0.1130 0.1510 -0.0190 -0.0317 0.0165  150 VAL A O   
1231 C  CB  . VAL A 149 ? 0.1376 0.1133 0.1261 0.0066  -0.0203 -0.0038 150 VAL A CB  
1232 C  CG1 . VAL A 149 ? 0.1927 0.1731 0.1313 -0.0003 -0.0364 -0.0206 150 VAL A CG1 
1233 C  CG2 . VAL A 149 ? 0.1144 0.1643 0.1810 -0.0048 -0.0027 0.0058  150 VAL A CG2 
1234 N  N   . GLY A 150 ? 0.1388 0.1115 0.1232 -0.0259 -0.0350 -0.0005 151 GLY A N   
1235 C  CA  . GLY A 150 ? 0.1410 0.1349 0.1650 -0.0387 -0.0494 0.0115  151 GLY A CA  
1236 C  C   . GLY A 150 ? 0.1372 0.1173 0.1561 -0.0209 -0.0295 0.0088  151 GLY A C   
1237 O  O   . GLY A 150 ? 0.1609 0.1349 0.1593 -0.0350 -0.0302 -0.0099 151 GLY A O   
1238 N  N   A SER A 151 ? 0.1286 0.1345 0.1832 -0.0216 -0.0416 -0.0017 152 SER A N   
1239 N  N   B SER A 151 ? 0.1223 0.1311 0.1767 -0.0190 -0.0496 0.0000  152 SER A N   
1240 C  CA  A SER A 151 ? 0.1625 0.1500 0.1870 -0.0294 -0.0531 0.0036  152 SER A CA  
1241 C  CA  B SER A 151 ? 0.1264 0.1553 0.1703 0.0064  -0.0359 -0.0119 152 SER A CA  
1242 C  C   A SER A 151 ? 0.1377 0.1119 0.1613 0.0035  -0.0242 -0.0408 152 SER A C   
1243 C  C   B SER A 151 ? 0.1713 0.1351 0.1568 -0.0166 -0.0643 -0.0282 152 SER A C   
1244 O  O   A SER A 151 ? 0.1131 0.1424 0.1584 -0.0139 -0.0204 -0.0298 152 SER A O   
1245 O  O   B SER A 151 ? 0.1092 0.1297 0.0995 -0.0036 -0.0055 -0.0248 152 SER A O   
1246 C  CB  A SER A 151 ? 0.1965 0.2878 0.3014 -0.0346 0.0394  -0.0488 152 SER A CB  
1247 C  CB  B SER A 151 ? 0.0708 0.1852 0.2108 0.0120  -0.0455 0.0182  152 SER A CB  
1248 O  OG  A SER A 151 ? 0.2083 0.3783 0.2480 -0.0389 -0.0107 -0.0391 152 SER A OG  
1249 O  OG  B SER A 151 ? 0.1342 0.2462 0.2998 -0.0399 -0.0118 0.0825  152 SER A OG  
1250 N  N   . ALA A 152 ? 0.1464 0.1295 0.1625 -0.0004 -0.0573 -0.0230 153 ALA A N   
1251 C  CA  . ALA A 152 ? 0.1873 0.1232 0.1478 0.0096  -0.0416 -0.0176 153 ALA A CA  
1252 C  C   . ALA A 152 ? 0.1473 0.1361 0.1349 0.0192  -0.0462 -0.0110 153 ALA A C   
1253 O  O   . ALA A 152 ? 0.1690 0.1465 0.1986 -0.0011 -0.0339 -0.0352 153 ALA A O   
1254 C  CB  . ALA A 152 ? 0.2282 0.2035 0.1494 0.0354  -0.0743 -0.0243 153 ALA A CB  
1255 N  N   . LYS A 153 ? 0.1900 0.1246 0.1480 -0.0042 -0.0524 0.0018  154 LYS A N   
1256 C  CA  . LYS A 153 ? 0.2333 0.1163 0.1523 0.0158  -0.0511 -0.0158 154 LYS A CA  
1257 C  C   . LYS A 153 ? 0.1570 0.1194 0.1546 0.0317  -0.0490 -0.0239 154 LYS A C   
1258 O  O   . LYS A 153 ? 0.1798 0.1494 0.1367 0.0059  -0.0681 -0.0157 154 LYS A O   
1259 C  CB  . LYS A 153 ? 0.2074 0.1090 0.1584 0.0029  -0.0567 -0.0062 154 LYS A CB  
1260 C  CG  . LYS A 153 ? 0.2626 0.1293 0.2240 0.0107  -0.1106 -0.0442 154 LYS A CG  
1261 C  CD  . LYS A 153 ? 0.3255 0.1473 0.1643 0.0458  -0.0668 -0.0218 154 LYS A CD  
1262 C  CE  . LYS A 153 ? 0.3114 0.2020 0.1794 0.0348  -0.0326 -0.0297 154 LYS A CE  
1263 N  NZ  . LYS A 153 ? 0.1726 0.1954 0.2724 0.0254  -0.0383 -0.0643 154 LYS A NZ  
1264 N  N   . PRO A 154 ? 0.2033 0.1591 0.1584 0.0206  -0.0700 -0.0154 155 PRO A N   
1265 C  CA  . PRO A 154 ? 0.2124 0.2008 0.1654 0.0017  -0.0797 0.0040  155 PRO A CA  
1266 C  C   . PRO A 154 ? 0.1954 0.2151 0.1324 0.0414  -0.0749 0.0058  155 PRO A C   
1267 O  O   . PRO A 154 ? 0.2707 0.2126 0.1658 0.0092  -0.0922 0.0337  155 PRO A O   
1268 C  CB  . PRO A 154 ? 0.1798 0.2200 0.2458 0.0228  -0.0933 0.0015  155 PRO A CB  
1269 C  CG  . PRO A 154 ? 0.1694 0.2913 0.2820 0.0179  -0.0502 -0.0018 155 PRO A CG  
1270 C  CD  . PRO A 154 ? 0.2259 0.2037 0.1893 0.0245  -0.0324 -0.0076 155 PRO A CD  
1271 N  N   . GLY A 155 ? 0.2133 0.1474 0.1861 0.0419  -0.0890 0.0044  156 GLY A N   
1272 C  CA  . GLY A 155 ? 0.3049 0.1516 0.2261 0.0365  -0.0447 0.0214  156 GLY A CA  
1273 C  C   . GLY A 155 ? 0.2911 0.1191 0.1656 0.0016  -0.0772 0.0239  156 GLY A C   
1274 O  O   . GLY A 155 ? 0.2954 0.1404 0.2508 0.0307  -0.0518 0.0299  156 GLY A O   
1275 N  N   . LEU A 156 ? 0.2239 0.1469 0.1685 0.0256  -0.0675 0.0020  157 LEU A N   
1276 C  CA  . LEU A 156 ? 0.2634 0.1117 0.1201 0.0034  -0.0694 -0.0111 157 LEU A CA  
1277 C  C   . LEU A 156 ? 0.2781 0.1212 0.1568 0.0013  -0.0905 -0.0163 157 LEU A C   
1278 O  O   . LEU A 156 ? 0.2628 0.1383 0.1217 0.0013  -0.0740 -0.0178 157 LEU A O   
1279 C  CB  . LEU A 156 ? 0.2119 0.1559 0.1473 -0.0228 -0.0814 0.0163  157 LEU A CB  
1280 C  CG  . LEU A 156 ? 0.2349 0.1537 0.1237 -0.0265 -0.0627 -0.0054 157 LEU A CG  
1281 C  CD1 . LEU A 156 ? 0.2634 0.1455 0.1474 -0.0383 -0.0757 0.0032  157 LEU A CD1 
1282 C  CD2 . LEU A 156 ? 0.2236 0.1783 0.1356 -0.0003 -0.0690 0.0153  157 LEU A CD2 
1283 N  N   . GLN A 157 ? 0.2448 0.1324 0.1358 -0.0265 -0.0839 -0.0001 158 GLN A N   
1284 C  CA  . GLN A 157 ? 0.2811 0.1570 0.1223 -0.0250 -0.0758 -0.0124 158 GLN A CA  
1285 C  C   . GLN A 157 ? 0.2678 0.1685 0.1289 -0.0019 -0.1008 -0.0093 158 GLN A C   
1286 O  O   . GLN A 157 ? 0.2621 0.1636 0.1426 -0.0240 -0.0745 -0.0206 158 GLN A O   
1287 C  CB  . GLN A 157 ? 0.3373 0.1462 0.1701 -0.0709 -0.0660 -0.0273 158 GLN A CB  
1288 C  CG  . GLN A 157 ? 0.3944 0.1694 0.1629 -0.0042 -0.0979 -0.0403 158 GLN A CG  
1289 C  CD  . GLN A 157 ? 0.3278 0.1361 0.1561 -0.0145 -0.0835 -0.0105 158 GLN A CD  
1290 O  OE1 . GLN A 157 ? 0.3229 0.1649 0.1401 -0.0037 -0.0878 -0.0139 158 GLN A OE1 
1291 N  NE2 . GLN A 157 ? 0.3725 0.1943 0.1505 -0.0594 -0.0701 -0.0282 158 GLN A NE2 
1292 N  N   A LYS A 158 ? 0.3125 0.1544 0.1340 -0.0019 -0.0991 0.0167  159 LYS A N   
1293 N  N   B LYS A 158 ? 0.3098 0.1527 0.1320 -0.0030 -0.0974 0.0165  159 LYS A N   
1294 C  CA  A LYS A 158 ? 0.2748 0.1595 0.1656 -0.0026 -0.1136 0.0215  159 LYS A CA  
1295 C  CA  B LYS A 158 ? 0.2742 0.1577 0.1641 -0.0018 -0.1153 0.0245  159 LYS A CA  
1296 C  C   A LYS A 158 ? 0.2771 0.1670 0.1151 0.0111  -0.0779 -0.0132 159 LYS A C   
1297 C  C   B LYS A 158 ? 0.2766 0.1690 0.1171 0.0110  -0.0771 -0.0171 159 LYS A C   
1298 O  O   A LYS A 158 ? 0.3001 0.1920 0.1277 -0.0105 -0.0847 0.0115  159 LYS A O   
1299 O  O   B LYS A 158 ? 0.3005 0.1904 0.1309 -0.0116 -0.0848 0.0072  159 LYS A O   
1300 C  CB  A LYS A 158 ? 0.3230 0.1658 0.2153 0.0122  -0.0746 0.0730  159 LYS A CB  
1301 C  CB  B LYS A 158 ? 0.3245 0.1708 0.2182 0.0122  -0.0699 0.0695  159 LYS A CB  
1302 C  CG  A LYS A 158 ? 0.3836 0.3693 0.2786 0.0913  -0.1061 0.0717  159 LYS A CG  
1303 C  CG  B LYS A 158 ? 0.3811 0.3368 0.2317 0.0736  -0.1245 0.0678  159 LYS A CG  
1304 C  CD  A LYS A 158 ? 0.3770 0.3289 0.7153 0.0149  -0.1769 0.0603  159 LYS A CD  
1305 C  CD  B LYS A 158 ? 0.3768 0.3420 0.7271 0.0433  -0.1512 0.0642  159 LYS A CD  
1306 C  CE  A LYS A 158 ? 0.4710 0.3164 0.3439 -0.0346 -0.1437 -0.0265 159 LYS A CE  
1307 C  CE  B LYS A 158 ? 0.4411 0.3526 0.4048 -0.0438 -0.1596 0.0634  159 LYS A CE  
1308 N  NZ  A LYS A 158 ? 0.7780 0.3479 0.2503 0.0203  -0.1351 -0.0784 159 LYS A NZ  
1309 N  NZ  B LYS A 158 ? 0.6067 0.3844 0.1992 0.0110  -0.0631 0.1060  159 LYS A NZ  
1310 N  N   . VAL A 159 ? 0.2982 0.1397 0.1101 0.0096  -0.0728 -0.0124 160 VAL A N   
1311 C  CA  . VAL A 159 ? 0.2798 0.1141 0.1163 -0.0023 -0.0669 -0.0111 160 VAL A CA  
1312 C  C   . VAL A 159 ? 0.2284 0.1169 0.1546 0.0110  -0.0839 -0.0072 160 VAL A C   
1313 O  O   . VAL A 159 ? 0.2803 0.1412 0.1462 -0.0017 -0.0746 -0.0151 160 VAL A O   
1314 C  CB  . VAL A 159 ? 0.2874 0.1205 0.1160 -0.0047 -0.0618 -0.0115 160 VAL A CB  
1315 C  CG1 . VAL A 159 ? 0.2779 0.1704 0.1361 -0.0220 -0.0854 -0.0004 160 VAL A CG1 
1316 C  CG2 . VAL A 159 ? 0.3362 0.1595 0.1237 0.0122  -0.0663 -0.0249 160 VAL A CG2 
1317 N  N   . VAL A 160 ? 0.2535 0.1106 0.1164 0.0066  -0.0562 -0.0131 161 VAL A N   
1318 C  CA  . VAL A 160 ? 0.3306 0.1132 0.1297 0.0150  -0.0239 0.0077  161 VAL A CA  
1319 C  C   . VAL A 160 ? 0.3172 0.1117 0.1489 -0.0250 -0.0357 -0.0266 161 VAL A C   
1320 O  O   . VAL A 160 ? 0.3194 0.1528 0.1580 -0.0139 -0.0063 -0.0179 161 VAL A O   
1321 C  CB  . VAL A 160 ? 0.4108 0.1688 0.1433 -0.0082 0.0529  -0.0263 161 VAL A CB  
1322 C  CG1 . VAL A 160 ? 0.3707 0.1699 0.2487 -0.0457 -0.0506 -0.0428 161 VAL A CG1 
1323 C  CG2 . VAL A 160 ? 0.3696 0.1719 0.1832 0.0337  0.0364  -0.0021 161 VAL A CG2 
1324 N  N   . ASP A 161 ? 0.3225 0.1731 0.1120 -0.0395 -0.0501 -0.0071 162 ASP A N   
1325 C  CA  . ASP A 161 ? 0.4298 0.2266 0.1177 -0.0767 -0.0857 -0.0215 162 ASP A CA  
1326 C  C   . ASP A 161 ? 0.3514 0.2570 0.1300 -0.0829 -0.0795 -0.0241 162 ASP A C   
1327 O  O   . ASP A 161 ? 0.5409 0.3098 0.1525 -0.1689 -0.0168 -0.0267 162 ASP A O   
1328 C  CB  . ASP A 161 ? 0.4802 0.2840 0.1455 -0.0893 -0.0708 -0.0466 162 ASP A CB  
1329 C  CG  . ASP A 161 ? 0.3494 0.2137 0.1365 -0.0043 -0.0388 -0.0097 162 ASP A CG  
1330 O  OD1 . ASP A 161 ? 0.3861 0.2491 0.2944 -0.0418 -0.1174 -0.0152 162 ASP A OD1 
1331 O  OD2 . ASP A 161 ? 0.3989 0.3602 0.2491 -0.0816 -0.1225 -0.0013 162 ASP A OD2 
1332 N  N   . VAL A 162 ? 0.4053 0.1956 0.1220 -0.0591 -0.1203 0.0115  163 VAL A N   
1333 C  CA  . VAL A 162 ? 0.3931 0.1904 0.1363 -0.0065 -0.0812 0.0243  163 VAL A CA  
1334 C  C   . VAL A 162 ? 0.3782 0.1428 0.1052 -0.0286 -0.0067 0.0215  163 VAL A C   
1335 O  O   . VAL A 162 ? 0.4647 0.1663 0.0981 -0.0622 -0.0042 0.0060  163 VAL A O   
1336 C  CB  . VAL A 162 ? 0.5367 0.1530 0.2240 -0.0219 -0.0928 0.0142  163 VAL A CB  
1337 C  CG1 . VAL A 162 ? 0.5188 0.1471 0.1654 0.0087  -0.0921 0.0001  163 VAL A CG1 
1338 C  CG2 . VAL A 162 ? 0.3005 0.2381 0.2115 0.0517  -0.0164 0.0553  163 VAL A CG2 
1339 N  N   . LEU A 163 ? 0.3607 0.1798 0.1124 -0.0390 -0.0477 0.0236  164 LEU A N   
1340 C  CA  . LEU A 163 ? 0.3765 0.1191 0.0945 -0.0266 0.0265  0.0023  164 LEU A CA  
1341 C  C   . LEU A 163 ? 0.3694 0.1708 0.1133 -0.0133 0.0138  0.0072  164 LEU A C   
1342 O  O   . LEU A 163 ? 0.3662 0.1663 0.1277 -0.0155 0.0480  0.0153  164 LEU A O   
1343 C  CB  . LEU A 163 ? 0.3033 0.1277 0.1163 -0.0352 -0.0097 0.0026  164 LEU A CB  
1344 C  CG  . LEU A 163 ? 0.3030 0.1349 0.0887 -0.0149 -0.0114 0.0110  164 LEU A CG  
1345 C  CD1 . LEU A 163 ? 0.3277 0.1338 0.1480 -0.0057 0.0017  0.0352  164 LEU A CD1 
1346 C  CD2 . LEU A 163 ? 0.2939 0.1579 0.0973 -0.0228 0.0026  -0.0080 164 LEU A CD2 
1347 N  N   . ASP A 164 ? 0.4781 0.1613 0.0867 -0.0485 0.0032  -0.0303 165 ASP A N   
1348 C  CA  . ASP A 164 ? 0.5061 0.1830 0.1487 -0.0471 0.0528  -0.0542 165 ASP A CA  
1349 C  C   . ASP A 164 ? 0.5145 0.2764 0.1099 -0.0041 0.0310  0.0001  165 ASP A C   
1350 O  O   . ASP A 164 ? 0.6090 0.2261 0.1947 0.0377  0.0798  -0.0043 165 ASP A O   
1351 C  CB  . ASP A 164 ? 0.6228 0.1787 0.2458 -0.1015 0.0238  -0.0762 165 ASP A CB  
1352 C  CG  . ASP A 164 ? 0.9227 0.5348 0.4796 0.0495  0.0377  0.0065  165 ASP A CG  
1353 O  OD1 . ASP A 164 ? 0.6440 0.7147 0.3048 -0.1813 -0.1576 -0.0167 165 ASP A OD1 
1354 O  OD2 . ASP A 164 ? 0.9047 1.1450 0.4431 -0.2046 0.2566  -0.0928 165 ASP A OD2 
1355 N  N   . SER A 165 ? 0.4307 0.2209 0.1071 -0.0355 0.0100  -0.0027 166 SER A N   
1356 C  CA  . SER A 165 ? 0.4052 0.2619 0.1115 -0.0897 0.0190  -0.0242 166 SER A CA  
1357 C  C   . SER A 165 ? 0.3095 0.1963 0.1135 -0.0399 0.0089  -0.0061 166 SER A C   
1358 O  O   . SER A 165 ? 0.5167 0.1823 0.1228 -0.0665 0.0088  0.0337  166 SER A O   
1359 C  CB  . SER A 165 ? 0.6013 0.2358 0.1913 -0.0077 0.0475  0.0226  166 SER A CB  
1360 O  OG  . SER A 165 ? 0.5360 0.2286 0.1783 -0.0245 0.0347  0.0210  166 SER A OG  
1361 N  N   . ILE A 166 ? 0.4474 0.1595 0.0773 -0.0883 -0.0066 0.0099  167 ILE A N   
1362 C  CA  . ILE A 166 ? 0.2610 0.1588 0.1555 -0.0263 0.0129  0.0321  167 ILE A CA  
1363 C  C   . ILE A 166 ? 0.2525 0.1828 0.0804 -0.0425 0.0050  -0.0454 167 ILE A C   
1364 O  O   . ILE A 166 ? 0.3488 0.1297 0.1092 -0.0578 0.0334  -0.0198 167 ILE A O   
1365 C  CB  . ILE A 166 ? 0.3847 0.1410 0.0859 -0.0673 0.0135  -0.0057 167 ILE A CB  
1366 C  CG1 . ILE A 166 ? 0.3256 0.1415 0.0945 -0.0592 0.0263  -0.0111 167 ILE A CG1 
1367 C  CG2 . ILE A 166 ? 0.4496 0.1322 0.1329 -0.0462 0.0025  0.0159  167 ILE A CG2 
1368 C  CD1 . ILE A 166 ? 0.3273 0.1439 0.1050 -0.0402 0.0285  -0.0190 167 ILE A CD1 
1369 N  N   . LYS A 167 ? 0.3227 0.1410 0.1250 -0.0416 0.0403  -0.0059 168 LYS A N   
1370 C  CA  . LYS A 167 ? 0.2419 0.2144 0.1252 -0.0221 0.0233  -0.0587 168 LYS A CA  
1371 C  C   . LYS A 167 ? 0.2546 0.1974 0.1002 -0.0149 0.0675  0.0293  168 LYS A C   
1372 O  O   . LYS A 167 ? 0.2737 0.1424 0.1333 -0.0782 0.0324  -0.0359 168 LYS A O   
1373 C  CB  . LYS A 167 ? 0.3685 0.1738 0.1140 -0.0307 0.0068  -0.0429 168 LYS A CB  
1374 C  CG  . LYS A 167 ? 0.3046 0.1882 0.1627 -0.0487 0.0245  -0.0785 168 LYS A CG  
1375 C  CD  . LYS A 167 ? 0.4270 0.2722 0.2661 -0.0003 0.0164  -0.1298 168 LYS A CD  
1376 C  CE  . LYS A 167 ? 0.4299 0.4432 0.3088 0.0122  -0.0528 -0.1444 168 LYS A CE  
1377 N  NZ  . LYS A 167 ? 0.6765 0.3649 0.3334 0.0148  0.0326  -0.1096 168 LYS A NZ  
1378 N  N   . THR A 168 ? 0.2114 0.1597 0.1527 -0.0291 0.0096  0.0234  169 THR A N   
1379 C  CA  . THR A 168 ? 0.2200 0.1882 0.1098 0.0293  0.0307  -0.0002 169 THR A CA  
1380 C  C   . THR A 168 ? 0.1480 0.2085 0.0928 0.0229  0.0295  0.0262  169 THR A C   
1381 O  O   . THR A 168 ? 0.2638 0.1433 0.1555 -0.0480 0.0490  0.0024  169 THR A O   
1382 C  CB  . THR A 168 ? 0.2882 0.1986 0.1428 0.0075  0.0240  -0.0325 169 THR A CB  
1383 O  OG1 . THR A 168 ? 0.3612 0.2119 0.1208 -0.0695 0.0662  -0.0001 169 THR A OG1 
1384 C  CG2 . THR A 168 ? 0.3428 0.1945 0.1516 -0.0857 0.1161  -0.0359 169 THR A CG2 
1385 N  N   . LYS A 169 ? 0.2660 0.1983 0.1342 -0.0936 0.1016  -0.0051 170 LYS A N   
1386 C  CA  . LYS A 169 ? 0.2484 0.1654 0.1726 -0.0158 0.0619  -0.0198 170 LYS A CA  
1387 C  C   . LYS A 169 ? 0.2532 0.2338 0.1491 -0.0416 0.1066  0.0601  170 LYS A C   
1388 O  O   . LYS A 169 ? 0.3079 0.2498 0.1487 -0.0515 0.0655  0.0023  170 LYS A O   
1389 C  CB  . LYS A 169 ? 0.2383 0.1444 0.1304 0.0120  0.0776  -0.0003 170 LYS A CB  
1390 C  CG  . LYS A 169 ? 0.2317 0.1913 0.2379 -0.0022 0.0106  0.0026  170 LYS A CG  
1391 C  CD  . LYS A 169 ? 0.2194 0.2426 0.2367 0.0447  0.0541  -0.0546 170 LYS A CD  
1392 C  CE  . LYS A 169 ? 0.1873 0.3401 0.5422 0.0428  -0.0944 -0.0961 170 LYS A CE  
1393 N  NZ  . LYS A 169 ? 0.5786 0.6843 0.4896 -0.3522 0.1375  -0.2408 170 LYS A NZ  
1394 N  N   . GLY A 170 ? 0.3795 0.1417 0.1577 -0.1147 0.0603  -0.0011 171 GLY A N   
1395 C  CA  . GLY A 170 ? 0.1634 0.1622 0.3416 -0.0289 0.0116  0.0671  171 GLY A CA  
1396 C  C   . GLY A 170 ? 0.2268 0.2028 0.1640 -0.0728 0.0062  0.0420  171 GLY A C   
1397 O  O   . GLY A 170 ? 0.3683 0.1808 0.2205 -0.0959 -0.0125 0.0596  171 GLY A O   
1398 N  N   . LYS A 171 ? 0.2329 0.1190 0.2056 -0.0515 0.0381  0.0431  172 LYS A N   
1399 C  CA  . LYS A 171 ? 0.1232 0.1571 0.3867 0.0086  0.0025  0.0439  172 LYS A CA  
1400 C  C   . LYS A 171 ? 0.1985 0.2295 0.1430 0.0664  -0.0108 -0.0785 172 LYS A C   
1401 O  O   . LYS A 171 ? 0.3000 0.1943 0.0961 -0.0334 0.0299  0.0203  172 LYS A O   
1402 C  CB  . LYS A 171 ? 0.3614 0.2017 0.1144 -0.0856 0.0718  -0.0409 172 LYS A CB  
1403 C  CG  . LYS A 171 ? 0.3804 0.2143 0.2349 -0.0719 0.0551  -0.0460 172 LYS A CG  
1404 C  CD  . LYS A 171 ? 0.4448 0.2458 0.3317 -0.1054 -0.0072 -0.0746 172 LYS A CD  
1405 C  CE  . LYS A 171 ? 0.4771 0.4881 0.2640 -0.0920 0.0117  -0.0348 172 LYS A CE  
1406 N  NZ  . LYS A 171 ? 0.7258 0.2748 0.2460 -0.0727 0.1445  0.0012  172 LYS A NZ  
1407 N  N   . SER A 172 ? 0.1081 0.2090 0.2911 0.0025  -0.0279 0.0985  173 SER A N   
1408 C  CA  . SER A 172 ? 0.0623 0.1934 0.3768 0.0058  -0.0083 0.0254  173 SER A CA  
1409 C  C   . SER A 172 ? 0.1169 0.1719 0.1670 0.0216  -0.0135 0.0701  173 SER A C   
1410 O  O   . SER A 172 ? 0.2491 0.2716 0.1250 0.0231  -0.0190 0.0245  173 SER A O   
1411 C  CB  . SER A 172 ? 0.2477 0.1913 0.1866 0.0008  -0.0087 0.0086  173 SER A CB  
1412 O  OG  . SER A 172 ? 0.5592 0.2035 0.1929 -0.0004 0.0695  0.0430  173 SER A OG  
1413 N  N   . ALA A 173 ? 0.1149 0.2001 0.3319 0.0633  -0.0377 -0.0532 174 ALA A N   
1414 C  CA  . ALA A 173 ? 0.2010 0.2892 0.1528 0.0591  -0.0306 0.0916  174 ALA A CA  
1415 C  C   . ALA A 173 ? 0.0591 0.2608 0.2178 0.0278  -0.0471 0.0258  174 ALA A C   
1416 O  O   . ALA A 173 ? 0.2345 0.2155 0.1128 0.0289  -0.0137 0.0042  174 ALA A O   
1417 C  CB  . ALA A 173 ? 0.4347 0.2351 0.1765 0.1203  -0.0059 -0.0311 174 ALA A CB  
1418 N  N   . ASP A 174 ? 0.1244 0.3814 0.1740 0.0278  0.0106  0.1276  175 ASP A N   
1419 C  CA  . ASP A 174 ? 0.2842 0.2554 0.1516 0.0608  0.0586  0.0630  175 ASP A CA  
1420 C  C   . ASP A 174 ? 0.2665 0.2234 0.1609 0.0660  -0.0198 0.0115  175 ASP A C   
1421 O  O   . ASP A 174 ? 0.5619 0.2611 0.2017 0.0545  0.0350  -0.0736 175 ASP A O   
1422 C  CB  . ASP A 174 ? 0.3041 0.3723 0.3161 0.1419  0.0049  0.1332  175 ASP A CB  
1423 C  CG  . ASP A 174 ? 0.6866 0.4478 0.2797 -0.0069 0.0526  0.0025  175 ASP A CG  
1424 O  OD1 . ASP A 174 ? 0.9786 0.6176 0.2338 0.0220  -0.1560 -0.0402 175 ASP A OD1 
1425 O  OD2 . ASP A 174 ? 0.3668 0.5661 0.3026 -0.0241 -0.0009 0.0699  175 ASP A OD2 
1426 N  N   . PHE A 175 ? 0.3298 0.2182 0.1254 0.0234  -0.0136 -0.0111 176 PHE A N   
1427 C  CA  . PHE A 175 ? 0.3289 0.2376 0.1552 0.0734  -0.0077 0.0820  176 PHE A CA  
1428 C  C   . PHE A 175 ? 0.3602 0.1588 0.1516 0.0480  -0.0776 -0.0281 176 PHE A C   
1429 O  O   . PHE A 175 ? 0.4656 0.2270 0.1235 0.1118  -0.1146 -0.0201 176 PHE A O   
1430 C  CB  . PHE A 175 ? 0.4241 0.1618 0.1395 0.0497  -0.0401 0.0334  176 PHE A CB  
1431 C  CG  . PHE A 175 ? 0.4125 0.1573 0.1279 0.0491  -0.0545 -0.0008 176 PHE A CG  
1432 C  CD1 . PHE A 175 ? 0.4799 0.1365 0.1713 0.0206  -0.0228 -0.0030 176 PHE A CD1 
1433 C  CD2 . PHE A 175 ? 0.4315 0.1392 0.1324 0.0573  -0.0543 0.0324  176 PHE A CD2 
1434 C  CE1 . PHE A 175 ? 0.4613 0.1449 0.1668 0.0269  -0.0291 -0.0010 176 PHE A CE1 
1435 C  CE2 . PHE A 175 ? 0.4032 0.1683 0.1726 0.0429  -0.1075 0.0155  176 PHE A CE2 
1436 C  CZ  . PHE A 175 ? 0.4766 0.1439 0.1622 0.0436  -0.0747 -0.0076 176 PHE A CZ  
1437 N  N   . THR A 176 ? 0.3883 0.2313 0.0884 0.0156  -0.0886 0.0383  177 THR A N   
1438 C  CA  . THR A 176 ? 0.3564 0.1609 0.1284 0.0467  -0.0449 0.0268  177 THR A CA  
1439 C  C   . THR A 176 ? 0.2845 0.1295 0.1401 0.0286  -0.0763 0.0623  177 THR A C   
1440 O  O   . THR A 176 ? 0.4399 0.1304 0.1131 -0.0088 -0.0859 0.0291  177 THR A O   
1441 C  CB  . THR A 176 ? 0.3990 0.1823 0.1455 -0.0333 -0.1262 0.0508  177 THR A CB  
1442 O  OG1 . THR A 176 ? 0.5327 0.2186 0.1289 0.0807  -0.0951 0.0345  177 THR A OG1 
1443 C  CG2 . THR A 176 ? 0.3813 0.2315 0.3327 -0.0414 -0.1371 0.1571  177 THR A CG2 
1444 N  N   . ASN A 177 ? 0.2687 0.1713 0.1151 0.0595  -0.0881 -0.0010 178 ASN A N   
1445 C  CA  . ASN A 177 ? 0.3072 0.1597 0.1787 0.0041  -0.0943 0.0363  178 ASN A CA  
1446 C  C   . ASN A 177 ? 0.3533 0.1692 0.1424 0.0022  -0.0998 0.0372  178 ASN A C   
1447 O  O   . ASN A 177 ? 0.4292 0.2042 0.2834 -0.0463 -0.1911 0.1145  178 ASN A O   
1448 C  CB  . ASN A 177 ? 0.3243 0.1625 0.2073 -0.0069 -0.1449 0.0542  178 ASN A CB  
1449 C  CG  . ASN A 177 ? 0.3736 0.1541 0.1453 0.0282  -0.0922 0.0273  178 ASN A CG  
1450 O  OD1 . ASN A 177 ? 0.3794 0.1731 0.2363 0.0370  -0.0671 0.0526  178 ASN A OD1 
1451 N  ND2 . ASN A 177 ? 0.3328 0.1753 0.1589 -0.0111 -0.1206 0.0519  178 ASN A ND2 
1452 N  N   . PHE A 178 ? 0.3844 0.1288 0.1079 0.0198  -0.1020 0.0210  179 PHE A N   
1453 C  CA  . PHE A 178 ? 0.3518 0.1257 0.1273 0.0004  -0.0854 0.0303  179 PHE A CA  
1454 C  C   . PHE A 178 ? 0.2671 0.1372 0.1193 0.0190  -0.0936 0.0104  179 PHE A C   
1455 O  O   . PHE A 178 ? 0.3145 0.1439 0.1156 0.0040  -0.0825 0.0165  179 PHE A O   
1456 C  CB  . PHE A 178 ? 0.3536 0.1390 0.1056 0.0170  -0.0364 0.0370  179 PHE A CB  
1457 C  CG  . PHE A 178 ? 0.3626 0.1219 0.1181 -0.0010 -0.0466 0.0330  179 PHE A CG  
1458 C  CD1 . PHE A 178 ? 0.3903 0.1356 0.1212 0.0335  -0.0538 0.0196  179 PHE A CD1 
1459 C  CD2 . PHE A 178 ? 0.2637 0.1462 0.1068 0.0290  -0.0376 0.0323  179 PHE A CD2 
1460 C  CE1 . PHE A 178 ? 0.4188 0.1295 0.1491 0.0147  -0.0860 0.0320  179 PHE A CE1 
1461 C  CE2 . PHE A 178 ? 0.2491 0.1252 0.1435 0.0097  -0.0618 0.0265  179 PHE A CE2 
1462 C  CZ  . PHE A 178 ? 0.3610 0.1268 0.1166 0.0406  -0.0423 0.0354  179 PHE A CZ  
1463 N  N   . ASP A 179 ? 0.2718 0.1530 0.1379 0.0122  -0.0943 0.0285  180 ASP A N   
1464 C  CA  . ASP A 179 ? 0.2433 0.1618 0.1638 0.0201  -0.0928 0.0422  180 ASP A CA  
1465 C  C   . ASP A 179 ? 0.2135 0.1324 0.1424 0.0111  -0.0820 0.0074  180 ASP A C   
1466 O  O   . ASP A 179 ? 0.2439 0.1259 0.1244 -0.0026 -0.0784 0.0076  180 ASP A O   
1467 C  CB  . ASP A 179 ? 0.2257 0.2270 0.2049 0.0237  -0.1242 0.0490  180 ASP A CB  
1468 C  CG  . ASP A 179 ? 0.1943 0.2505 0.2198 0.0103  -0.1217 0.0555  180 ASP A CG  
1469 O  OD1 . ASP A 179 ? 0.2430 0.1704 0.2141 0.0243  -0.0991 0.0367  180 ASP A OD1 
1470 O  OD2 . ASP A 179 ? 0.1972 0.4476 0.3195 -0.0465 -0.1277 0.0234  180 ASP A OD2 
1471 N  N   . PRO A 180 ? 0.1927 0.1329 0.1122 -0.0046 -0.0661 0.0203  181 PRO A N   
1472 C  CA  . PRO A 180 ? 0.1532 0.1388 0.1440 0.0094  -0.0706 0.0254  181 PRO A CA  
1473 C  C   . PRO A 180 ? 0.1661 0.1381 0.1194 0.0209  -0.0454 0.0127  181 PRO A C   
1474 O  O   . PRO A 180 ? 0.1449 0.1446 0.1266 0.0079  -0.0419 0.0273  181 PRO A O   
1475 C  CB  . PRO A 180 ? 0.1582 0.1771 0.1467 0.0037  -0.0641 0.0193  181 PRO A CB  
1476 C  CG  . PRO A 180 ? 0.1967 0.1652 0.1367 -0.0085 -0.0704 0.0062  181 PRO A CG  
1477 C  CD  . PRO A 180 ? 0.2220 0.1476 0.1264 0.0052  -0.0683 0.0196  181 PRO A CD  
1478 N  N   . ARG A 181 ? 0.1548 0.1467 0.1223 0.0223  -0.0528 0.0196  182 ARG A N   
1479 C  CA  . ARG A 181 ? 0.1523 0.1442 0.1632 0.0100  -0.0468 0.0073  182 ARG A CA  
1480 C  C   . ARG A 181 ? 0.1652 0.1571 0.1755 0.0140  -0.0925 0.0142  182 ARG A C   
1481 O  O   . ARG A 181 ? 0.1658 0.1737 0.1823 0.0107  -0.0569 0.0277  182 ARG A O   
1482 C  CB  . ARG A 181 ? 0.1259 0.1834 0.1882 0.0093  -0.0646 0.0219  182 ARG A CB  
1483 C  CG  . ARG A 181 ? 0.1613 0.1667 0.2117 -0.0050 -0.0158 0.0006  182 ARG A CG  
1484 C  CD  . ARG A 181 ? 0.1884 0.2381 0.2645 0.0463  0.0351  0.0454  182 ARG A CD  
1485 N  NE  . ARG A 181 ? 0.1898 0.2209 0.2814 -0.0082 -0.0425 0.0805  182 ARG A NE  
1486 C  CZ  . ARG A 181 ? 0.1532 0.2764 0.3631 0.0407  0.0356  0.0775  182 ARG A CZ  
1487 N  NH1 . ARG A 181 ? 0.1988 0.3030 0.4350 0.0249  0.0560  0.1046  182 ARG A NH1 
1488 N  NH2 . ARG A 181 ? 0.2035 0.3888 0.3610 0.0228  -0.0272 0.1743  182 ARG A NH2 
1489 N  N   . GLY A 182 ? 0.1674 0.1571 0.1697 0.0097  -0.1025 0.0100  183 GLY A N   
1490 C  CA  . GLY A 182 ? 0.2478 0.1235 0.1918 0.0011  -0.1295 0.0182  183 GLY A CA  
1491 C  C   . GLY A 182 ? 0.2518 0.1354 0.1895 0.0227  -0.1226 0.0013  183 GLY A C   
1492 O  O   . GLY A 182 ? 0.2828 0.1254 0.2223 0.0229  -0.1296 -0.0037 183 GLY A O   
1493 N  N   . LEU A 183 ? 0.2040 0.1394 0.1275 0.0159  -0.0797 -0.0029 184 LEU A N   
1494 C  CA  . LEU A 183 ? 0.2322 0.1203 0.1442 0.0174  -0.1035 0.0043  184 LEU A CA  
1495 C  C   . LEU A 183 ? 0.1979 0.1300 0.1275 -0.0032 -0.0804 0.0013  184 LEU A C   
1496 O  O   . LEU A 183 ? 0.1701 0.1600 0.1634 0.0091  -0.0627 0.0318  184 LEU A O   
1497 C  CB  . LEU A 183 ? 0.2157 0.1413 0.1205 0.0451  -0.0462 0.0029  184 LEU A CB  
1498 C  CG  . LEU A 183 ? 0.2575 0.1726 0.1183 0.0528  -0.0444 0.0132  184 LEU A CG  
1499 C  CD1 . LEU A 183 ? 0.2775 0.2433 0.1482 0.0662  -0.0834 0.0507  184 LEU A CD1 
1500 C  CD2 . LEU A 183 ? 0.3435 0.1992 0.1491 0.0713  -0.0109 -0.0374 184 LEU A CD2 
1501 N  N   . LEU A 184 ? 0.1927 0.1358 0.1334 0.0309  -0.0685 -0.0061 185 LEU A N   
1502 C  CA  . LEU A 184 ? 0.1282 0.1372 0.1519 -0.0330 -0.0721 0.0277  185 LEU A CA  
1503 C  C   . LEU A 184 ? 0.1914 0.1365 0.1844 -0.0450 -0.0998 0.0403  185 LEU A C   
1504 O  O   . LEU A 184 ? 0.3310 0.2162 0.3455 -0.1404 -0.2615 0.1257  185 LEU A O   
1505 C  CB  . LEU A 184 ? 0.0905 0.1582 0.1765 -0.0315 -0.0398 0.0259  185 LEU A CB  
1506 C  CG  . LEU A 184 ? 0.0648 0.1541 0.1498 -0.0034 -0.0137 0.0197  185 LEU A CG  
1507 C  CD1 . LEU A 184 ? 0.1072 0.1629 0.1877 0.0100  -0.0221 0.0089  185 LEU A CD1 
1508 C  CD2 . LEU A 184 ? 0.0840 0.1785 0.2010 -0.0185 -0.0413 0.0118  185 LEU A CD2 
1509 N  N   . PRO A 185 ? 0.1164 0.1421 0.1555 -0.0104 -0.0730 0.0263  186 PRO A N   
1510 C  CA  . PRO A 185 ? 0.1478 0.1306 0.1801 0.0066  -0.0456 0.0446  186 PRO A CA  
1511 C  C   . PRO A 185 ? 0.1338 0.1237 0.2261 0.0039  -0.0917 0.0270  186 PRO A C   
1512 O  O   . PRO A 185 ? 0.0638 0.1347 0.3890 0.0004  -0.0772 0.0457  186 PRO A O   
1513 C  CB  . PRO A 185 ? 0.0992 0.1473 0.1677 0.0128  -0.0389 0.0131  186 PRO A CB  
1514 C  CG  . PRO A 185 ? 0.0716 0.1505 0.1498 0.0153  -0.0343 0.0082  186 PRO A CG  
1515 C  CD  . PRO A 185 ? 0.0873 0.1368 0.1123 0.0023  -0.0264 0.0086  186 PRO A CD  
1516 N  N   . GLU A 186 ? 0.1372 0.1376 0.2175 -0.0163 -0.0477 0.0283  187 GLU A N   
1517 C  CA  . GLU A 186 ? 0.1000 0.1652 0.2791 -0.0280 -0.0542 0.0244  187 GLU A CA  
1518 C  C   . GLU A 186 ? 0.0602 0.1685 0.2600 -0.0170 -0.0215 0.0223  187 GLU A C   
1519 O  O   . GLU A 186 ? 0.0724 0.1990 0.3285 0.0159  -0.0184 0.0183  187 GLU A O   
1520 C  CB  . GLU A 186 ? 0.1315 0.2029 0.3861 -0.0705 -0.1368 0.0465  187 GLU A CB  
1521 C  CG  . GLU A 186 ? 0.2656 0.3959 0.6413 -0.0308 -0.0273 0.1430  187 GLU A CG  
1522 C  CD  . GLU A 186 ? 0.2175 0.4027 0.5467 -0.0003 0.0342  -0.0668 187 GLU A CD  
1523 O  OE1 . GLU A 186 ? 0.1324 0.2239 0.5440 -0.0441 -0.0036 -0.0476 187 GLU A OE1 
1524 O  OE2 . GLU A 186 ? 0.3855 0.4248 0.6721 0.1606  0.1733  0.1934  187 GLU A OE2 
1525 N  N   . SER A 187 ? 0.0536 0.1636 0.2309 -0.0231 -0.0259 0.0140  188 SER A N   
1526 C  CA  . SER A 187 ? 0.0798 0.1424 0.2530 -0.0173 0.0198  0.0113  188 SER A CA  
1527 C  C   . SER A 187 ? 0.0629 0.1510 0.2083 -0.0004 -0.0009 0.0154  188 SER A C   
1528 O  O   . SER A 187 ? 0.0623 0.1862 0.2358 -0.0132 -0.0006 -0.0138 188 SER A O   
1529 C  CB  . SER A 187 ? 0.1381 0.1624 0.2496 -0.0322 0.0159  0.0149  188 SER A CB  
1530 O  OG  . SER A 187 ? 0.0943 0.2092 0.2537 -0.0322 0.0139  0.0295  188 SER A OG  
1531 N  N   . LEU A 188 ? 0.0556 0.1751 0.2069 -0.0173 0.0016  -0.0026 189 LEU A N   
1532 C  CA  . LEU A 188 ? 0.0535 0.1631 0.2051 -0.0040 -0.0064 -0.0016 189 LEU A CA  
1533 C  C   . LEU A 188 ? 0.0792 0.1376 0.1864 0.0006  0.0110  -0.0157 189 LEU A C   
1534 O  O   . LEU A 188 ? 0.1135 0.1785 0.1913 -0.0121 -0.0148 -0.0312 189 LEU A O   
1535 C  CB  . LEU A 188 ? 0.0972 0.1798 0.2241 -0.0119 -0.0063 -0.0017 189 LEU A CB  
1536 C  CG  . LEU A 188 ? 0.1018 0.2044 0.2807 -0.0115 -0.0031 0.0668  189 LEU A CG  
1537 C  CD1 . LEU A 188 ? 0.1489 0.2049 0.3157 -0.0334 -0.0113 0.0576  189 LEU A CD1 
1538 C  CD2 . LEU A 188 ? 0.1051 0.2781 0.2471 -0.0035 -0.0234 0.0363  189 LEU A CD2 
1539 N  N   . ASP A 189 ? 0.0644 0.1588 0.1692 -0.0052 0.0103  -0.0221 190 ASP A N   
1540 C  CA  . ASP A 189 ? 0.0737 0.1873 0.1555 -0.0329 0.0292  -0.0257 190 ASP A CA  
1541 C  C   . ASP A 189 ? 0.0735 0.1356 0.1266 -0.0250 0.0152  -0.0011 190 ASP A C   
1542 O  O   . ASP A 189 ? 0.0644 0.1424 0.1252 -0.0059 -0.0026 -0.0067 190 ASP A O   
1543 C  CB  . ASP A 189 ? 0.1225 0.2380 0.1794 -0.1054 0.0290  0.0244  190 ASP A CB  
1544 C  CG  . ASP A 189 ? 0.1349 0.3226 0.1780 -0.0618 0.0080  0.0122  190 ASP A CG  
1545 O  OD1 . ASP A 189 ? 0.1674 0.4417 0.3194 -0.0668 0.1078  -0.0534 190 ASP A OD1 
1546 O  OD2 . ASP A 189 ? 0.1620 0.4979 0.3465 -0.1166 -0.0052 0.1159  190 ASP A OD2 
1547 N  N   . TYR A 190 ? 0.0691 0.1465 0.1168 -0.0120 0.0093  0.0003  191 TYR A N   
1548 C  CA  . TYR A 190 ? 0.0737 0.1453 0.1032 -0.0274 -0.0008 0.0103  191 TYR A CA  
1549 C  C   . TYR A 190 ? 0.0893 0.1097 0.0932 -0.0140 0.0277  0.0008  191 TYR A C   
1550 O  O   . TYR A 190 ? 0.1000 0.1426 0.0932 -0.0130 0.0273  -0.0001 191 TYR A O   
1551 C  CB  . TYR A 190 ? 0.0930 0.1474 0.0971 -0.0084 -0.0020 0.0124  191 TYR A CB  
1552 C  CG  . TYR A 190 ? 0.0884 0.1410 0.1002 -0.0155 0.0081  0.0269  191 TYR A CG  
1553 C  CD1 . TYR A 190 ? 0.0813 0.1392 0.1158 -0.0086 0.0079  0.0150  191 TYR A CD1 
1554 C  CD2 . TYR A 190 ? 0.0902 0.1539 0.1250 0.0026  0.0111  0.0059  191 TYR A CD2 
1555 C  CE1 . TYR A 190 ? 0.1079 0.1534 0.1205 -0.0163 0.0089  0.0136  191 TYR A CE1 
1556 C  CE2 . TYR A 190 ? 0.0921 0.1507 0.1439 -0.0115 -0.0017 -0.0009 191 TYR A CE2 
1557 C  CZ  . TYR A 190 ? 0.1293 0.1399 0.1191 -0.0080 0.0039  0.0025  191 TYR A CZ  
1558 O  OH  . TYR A 190 ? 0.1309 0.1593 0.1570 0.0029  -0.0081 -0.0204 191 TYR A OH  
1559 N  N   . TRP A 191 ? 0.0732 0.1117 0.0867 -0.0076 -0.0005 -0.0017 192 TRP A N   
1560 C  CA  . TRP A 191 ? 0.0790 0.1077 0.0871 -0.0020 0.0141  0.0087  192 TRP A CA  
1561 C  C   . TRP A 191 ? 0.0683 0.1172 0.0715 -0.0006 0.0023  0.0035  192 TRP A C   
1562 O  O   . TRP A 191 ? 0.1010 0.1186 0.0809 -0.0206 0.0034  0.0039  192 TRP A O   
1563 C  CB  . TRP A 191 ? 0.0826 0.1115 0.0984 -0.0051 0.0063  -0.0012 192 TRP A CB  
1564 C  CG  . TRP A 191 ? 0.1072 0.1105 0.0836 0.0104  0.0022  0.0130  192 TRP A CG  
1565 C  CD1 . TRP A 191 ? 0.1399 0.1219 0.1051 0.0051  0.0059  0.0016  192 TRP A CD1 
1566 C  CD2 . TRP A 191 ? 0.0704 0.1122 0.1126 0.0116  -0.0006 0.0132  192 TRP A CD2 
1567 N  NE1 . TRP A 191 ? 0.1532 0.1259 0.1157 -0.0016 0.0178  0.0286  192 TRP A NE1 
1568 C  CE2 . TRP A 191 ? 0.1252 0.1159 0.1181 0.0013  -0.0058 0.0114  192 TRP A CE2 
1569 C  CE3 . TRP A 191 ? 0.0532 0.1399 0.1141 0.0093  0.0061  0.0039  192 TRP A CE3 
1570 C  CZ2 . TRP A 191 ? 0.1112 0.1244 0.1670 0.0218  -0.0205 0.0084  192 TRP A CZ2 
1571 C  CZ3 . TRP A 191 ? 0.0871 0.1336 0.1428 -0.0052 0.0102  -0.0239 192 TRP A CZ3 
1572 C  CH2 . TRP A 191 ? 0.1074 0.1449 0.1661 0.0093  -0.0064 -0.0244 192 TRP A CH2 
1573 N  N   . THR A 192 ? 0.0731 0.1029 0.0738 -0.0042 -0.0013 0.0041  193 THR A N   
1574 C  CA  . THR A 192 ? 0.0772 0.1004 0.0851 -0.0050 -0.0087 -0.0040 193 THR A CA  
1575 C  C   . THR A 192 ? 0.0791 0.0977 0.0760 -0.0038 0.0016  0.0050  193 THR A C   
1576 O  O   . THR A 192 ? 0.0811 0.1315 0.0723 -0.0039 0.0008  -0.0001 193 THR A O   
1577 C  CB  . THR A 192 ? 0.0919 0.1068 0.0858 0.0039  0.0037  0.0001  193 THR A CB  
1578 O  OG1 . THR A 192 ? 0.0816 0.1089 0.0961 0.0016  0.0044  -0.0033 193 THR A OG1 
1579 C  CG2 . THR A 192 ? 0.1041 0.1363 0.0875 0.0167  0.0147  -0.0083 193 THR A CG2 
1580 N  N   . TYR A 193 ? 0.0629 0.1036 0.0823 0.0001  -0.0104 0.0000  194 TYR A N   
1581 C  CA  . TYR A 193 ? 0.0769 0.1115 0.0758 -0.0058 -0.0161 0.0025  194 TYR A CA  
1582 C  C   . TYR A 193 ? 0.0626 0.1140 0.0633 0.0031  -0.0076 -0.0070 194 TYR A C   
1583 O  O   . TYR A 193 ? 0.0700 0.1106 0.0767 0.0029  -0.0125 -0.0021 194 TYR A O   
1584 C  CB  . TYR A 193 ? 0.0896 0.1169 0.0759 0.0114  -0.0125 -0.0084 194 TYR A CB  
1585 C  CG  . TYR A 193 ? 0.0684 0.0927 0.0928 0.0082  -0.0074 -0.0008 194 TYR A CG  
1586 C  CD1 . TYR A 193 ? 0.0813 0.0982 0.0810 0.0033  -0.0153 0.0006  194 TYR A CD1 
1587 C  CD2 . TYR A 193 ? 0.0744 0.1036 0.0928 0.0021  -0.0232 -0.0120 194 TYR A CD2 
1588 C  CE1 . TYR A 193 ? 0.0616 0.0855 0.0979 0.0062  -0.0104 0.0039  194 TYR A CE1 
1589 C  CE2 . TYR A 193 ? 0.0719 0.1038 0.1002 0.0210  -0.0166 -0.0079 194 TYR A CE2 
1590 C  CZ  . TYR A 193 ? 0.0560 0.0904 0.0785 0.0103  -0.0152 0.0068  194 TYR A CZ  
1591 O  OH  . TYR A 193 ? 0.0671 0.1029 0.0859 0.0027  -0.0039 -0.0054 194 TYR A OH  
1592 N  N   . PRO A 194 ? 0.0573 0.1144 0.0789 0.0026  -0.0181 -0.0093 195 PRO A N   
1593 C  CA  . PRO A 194 ? 0.0732 0.1106 0.0864 0.0043  0.0000  -0.0248 195 PRO A CA  
1594 C  C   . PRO A 194 ? 0.0581 0.0957 0.0871 -0.0088 -0.0152 -0.0094 195 PRO A C   
1595 O  O   . PRO A 194 ? 0.0844 0.1205 0.0824 0.0160  -0.0196 -0.0016 195 PRO A O   
1596 C  CB  . PRO A 194 ? 0.1054 0.1324 0.0923 -0.0013 -0.0108 -0.0230 195 PRO A CB  
1597 C  CG  . PRO A 194 ? 0.1154 0.1455 0.0950 -0.0142 -0.0099 -0.0261 195 PRO A CG  
1598 C  CD  . PRO A 194 ? 0.0971 0.1390 0.0732 -0.0201 -0.0138 -0.0222 195 PRO A CD  
1599 N  N   . GLY A 195 ? 0.0593 0.0999 0.0793 0.0052  -0.0104 -0.0168 196 GLY A N   
1600 C  CA  . GLY A 195 ? 0.0651 0.1045 0.0820 0.0077  -0.0036 -0.0065 196 GLY A CA  
1601 C  C   . GLY A 195 ? 0.0591 0.0983 0.0923 -0.0046 -0.0076 -0.0155 196 GLY A C   
1602 O  O   . GLY A 195 ? 0.0685 0.0975 0.0938 -0.0017 -0.0061 -0.0162 196 GLY A O   
1603 N  N   . SER A 196 ? 0.0497 0.1022 0.0860 0.0050  -0.0076 -0.0137 197 SER A N   
1604 C  CA  . SER A 196 ? 0.0406 0.1124 0.0981 -0.0110 0.0001  -0.0176 197 SER A CA  
1605 C  C   . SER A 196 ? 0.0429 0.0818 0.0934 -0.0019 -0.0176 -0.0013 197 SER A C   
1606 O  O   . SER A 196 ? 0.0477 0.0961 0.0952 -0.0029 -0.0020 -0.0134 197 SER A O   
1607 C  CB  . SER A 196 ? 0.0514 0.1096 0.1185 -0.0055 -0.0143 -0.0165 197 SER A CB  
1608 O  OG  . SER A 196 ? 0.0438 0.0959 0.1230 -0.0022 -0.0083 -0.0126 197 SER A OG  
1609 N  N   . LEU A 197 ? 0.0441 0.0977 0.0877 0.0015  0.0046  -0.0138 198 LEU A N   
1610 C  CA  . LEU A 197 ? 0.0656 0.0907 0.0904 -0.0146 0.0032  -0.0138 198 LEU A CA  
1611 C  C   . LEU A 197 ? 0.0431 0.0995 0.1013 -0.0074 0.0043  -0.0176 198 LEU A C   
1612 O  O   . LEU A 197 ? 0.0511 0.1144 0.1067 -0.0046 -0.0013 -0.0212 198 LEU A O   
1613 C  CB  . LEU A 197 ? 0.0838 0.1078 0.1120 -0.0093 0.0122  -0.0100 198 LEU A CB  
1614 C  CG  . LEU A 197 ? 0.1102 0.1733 0.2133 0.0452  0.0721  0.0625  198 LEU A CG  
1615 C  CD1 . LEU A 197 ? 0.1219 0.1327 0.2013 -0.0024 0.0467  0.0105  198 LEU A CD1 
1616 C  CD2 . LEU A 197 ? 0.1225 0.2392 0.2335 0.0450  0.0898  0.1062  198 LEU A CD2 
1617 N  N   . THR A 198 ? 0.0422 0.0943 0.0952 -0.0001 -0.0012 -0.0150 199 THR A N   
1618 C  CA  . THR A 198 ? 0.0533 0.0975 0.1289 -0.0044 0.0179  -0.0204 199 THR A CA  
1619 C  C   . THR A 198 ? 0.0372 0.1102 0.1193 -0.0152 -0.0013 -0.0198 199 THR A C   
1620 O  O   . THR A 198 ? 0.0537 0.1076 0.1356 0.0017  0.0119  -0.0154 199 THR A O   
1621 C  CB  . THR A 198 ? 0.0653 0.1011 0.0986 -0.0140 0.0050  -0.0199 199 THR A CB  
1622 O  OG1 . THR A 198 ? 0.0682 0.0961 0.0900 -0.0077 0.0018  -0.0119 199 THR A OG1 
1623 C  CG2 . THR A 198 ? 0.0499 0.1196 0.1024 0.0000  0.0108  -0.0168 199 THR A CG2 
1624 N  N   . THR A 199 ? 0.0692 0.1164 0.1135 -0.0126 0.0217  -0.0155 200 THR A N   
1625 C  CA  . THR A 199 ? 0.0581 0.1345 0.1320 -0.0268 0.0239  -0.0215 200 THR A CA  
1626 C  C   . THR A 199 ? 0.0731 0.1255 0.1185 -0.0200 0.0286  -0.0268 200 THR A C   
1627 O  O   . THR A 199 ? 0.0648 0.1257 0.1460 -0.0278 0.0215  -0.0394 200 THR A O   
1628 C  CB  . THR A 199 ? 0.0900 0.1358 0.1259 -0.0274 0.0105  -0.0190 200 THR A CB  
1629 O  OG1 . THR A 199 ? 0.1983 0.1302 0.1309 0.0071  -0.0047 -0.0197 200 THR A OG1 
1630 C  CG2 . THR A 199 ? 0.0853 0.1449 0.1307 -0.0352 0.0140  -0.0227 200 THR A CG2 
1631 N  N   . PRO A 200 ? 0.0754 0.1302 0.1430 -0.0227 0.0345  -0.0227 201 PRO A N   
1632 C  CA  . PRO A 200 ? 0.0672 0.1478 0.1480 -0.0251 0.0226  -0.0013 201 PRO A CA  
1633 C  C   . PRO A 200 ? 0.1266 0.1388 0.1444 -0.0220 0.0238  -0.0214 201 PRO A C   
1634 O  O   . PRO A 200 ? 0.1544 0.1773 0.1453 -0.0133 0.0066  -0.0270 201 PRO A O   
1635 C  CB  . PRO A 200 ? 0.0832 0.1749 0.1873 -0.0273 0.0254  -0.0135 201 PRO A CB  
1636 C  CG  . PRO A 200 ? 0.0814 0.1731 0.1990 -0.0436 0.0526  -0.0365 201 PRO A CG  
1637 C  CD  . PRO A 200 ? 0.0675 0.1690 0.1667 -0.0055 0.0304  -0.0439 201 PRO A CD  
1638 N  N   . PRO A 201 ? 0.0991 0.1442 0.1390 -0.0303 0.0277  -0.0144 202 PRO A N   
1639 C  CA  . PRO A 201 ? 0.1078 0.1234 0.1456 -0.0272 0.0170  -0.0098 202 PRO A CA  
1640 C  C   . PRO A 201 ? 0.0710 0.1302 0.1433 -0.0237 0.0142  -0.0283 202 PRO A C   
1641 O  O   . PRO A 201 ? 0.0730 0.1349 0.1641 -0.0308 0.0152  -0.0155 202 PRO A O   
1642 C  CB  . PRO A 201 ? 0.1677 0.1410 0.1949 -0.0471 0.0157  -0.0021 202 PRO A CB  
1643 C  CG  . PRO A 201 ? 0.1791 0.1385 0.2006 -0.0122 0.0043  -0.0244 202 PRO A CG  
1644 C  CD  . PRO A 201 ? 0.1699 0.1548 0.1390 -0.0089 0.0225  -0.0153 202 PRO A CD  
1645 N  N   . LEU A 202 ? 0.0632 0.1205 0.1342 -0.0230 0.0168  -0.0171 203 LEU A N   
1646 C  CA  . LEU A 202 ? 0.0563 0.1117 0.1358 -0.0072 0.0037  -0.0222 203 LEU A CA  
1647 C  C   . LEU A 202 ? 0.0562 0.1102 0.1248 -0.0243 -0.0027 -0.0053 203 LEU A C   
1648 O  O   . LEU A 202 ? 0.0634 0.1112 0.1223 -0.0017 -0.0044 -0.0178 203 LEU A O   
1649 C  CB  . LEU A 202 ? 0.0441 0.1273 0.1476 -0.0009 -0.0111 -0.0378 203 LEU A CB  
1650 C  CG  . LEU A 202 ? 0.0469 0.1183 0.1552 -0.0003 0.0000  -0.0265 203 LEU A CG  
1651 C  CD1 . LEU A 202 ? 0.0455 0.1604 0.2152 0.0051  0.0002  -0.0214 203 LEU A CD1 
1652 C  CD2 . LEU A 202 ? 0.0569 0.1320 0.1668 -0.0066 -0.0040 -0.0381 203 LEU A CD2 
1653 N  N   . LEU A 203 ? 0.0544 0.1060 0.1444 0.0013  -0.0027 -0.0161 204 LEU A N   
1654 C  CA  . LEU A 203 ? 0.0710 0.1029 0.1412 -0.0137 0.0008  -0.0220 204 LEU A CA  
1655 C  C   . LEU A 203 ? 0.0666 0.0934 0.1374 -0.0035 0.0077  -0.0156 204 LEU A C   
1656 O  O   . LEU A 203 ? 0.0706 0.1126 0.1207 -0.0143 -0.0083 -0.0160 204 LEU A O   
1657 C  CB  . LEU A 203 ? 0.0741 0.1157 0.1625 -0.0254 0.0121  -0.0033 204 LEU A CB  
1658 C  CG  . LEU A 203 ? 0.1288 0.1238 0.1805 -0.0032 0.0368  -0.0079 204 LEU A CG  
1659 C  CD1 . LEU A 203 ? 0.1358 0.1521 0.2090 0.0098  0.0556  0.0298  204 LEU A CD1 
1660 C  CD2 . LEU A 203 ? 0.1054 0.1817 0.3040 -0.0613 0.0026  0.0210  204 LEU A CD2 
1661 N  N   . GLU A 204 ? 0.0776 0.1199 0.1311 -0.0182 0.0047  -0.0331 205 GLU A N   
1662 C  CA  . GLU A 204 ? 0.0774 0.1205 0.1156 0.0073  -0.0254 -0.0261 205 GLU A CA  
1663 C  C   . GLU A 204 ? 0.0723 0.1065 0.1114 -0.0108 -0.0223 -0.0272 205 GLU A C   
1664 O  O   . GLU A 204 ? 0.0991 0.1570 0.1302 0.0127  -0.0340 -0.0509 205 GLU A O   
1665 C  CB  . GLU A 204 ? 0.0750 0.1394 0.1415 0.0131  -0.0289 -0.0290 205 GLU A CB  
1666 C  CG  . GLU A 204 ? 0.0932 0.1370 0.1476 0.0060  -0.0302 -0.0346 205 GLU A CG  
1667 C  CD  . GLU A 204 ? 0.1008 0.1376 0.1392 -0.0089 -0.0292 -0.0223 205 GLU A CD  
1668 O  OE1 . GLU A 204 ? 0.1194 0.1667 0.1834 0.0156  -0.0695 -0.0510 205 GLU A OE1 
1669 O  OE2 . GLU A 204 ? 0.0886 0.1449 0.1618 -0.0080 -0.0485 -0.0212 205 GLU A OE2 
1670 N  N   . CYS A 205 ? 0.0560 0.1020 0.1221 -0.0061 -0.0134 -0.0193 206 CYS A N   
1671 C  CA  . CYS A 205 ? 0.0619 0.0975 0.1192 -0.0006 -0.0135 -0.0132 206 CYS A CA  
1672 C  C   . CYS A 205 ? 0.0572 0.0961 0.1016 0.0092  -0.0174 -0.0234 206 CYS A C   
1673 O  O   . CYS A 205 ? 0.0774 0.0965 0.1460 0.0002  -0.0277 0.0024  206 CYS A O   
1674 C  CB  . CYS A 205 ? 0.0947 0.1060 0.1130 -0.0183 -0.0046 -0.0027 206 CYS A CB  
1675 S  SG  . CYS A 205 ? 0.1133 0.1172 0.1149 -0.0026 -0.0065 -0.0080 206 CYS A SG  
1676 N  N   . VAL A 206 ? 0.0610 0.0898 0.1103 -0.0091 -0.0149 -0.0036 207 VAL A N   
1677 C  CA  . VAL A 206 ? 0.0450 0.0977 0.1034 -0.0059 -0.0071 0.0009  207 VAL A CA  
1678 C  C   . VAL A 206 ? 0.0554 0.0864 0.0982 0.0102  -0.0172 0.0003  207 VAL A C   
1679 O  O   . VAL A 206 ? 0.0621 0.1221 0.1133 0.0021  -0.0168 0.0177  207 VAL A O   
1680 C  CB  . VAL A 206 ? 0.0541 0.1067 0.1034 -0.0109 0.0006  -0.0095 207 VAL A CB  
1681 C  CG1 . VAL A 206 ? 0.0503 0.0981 0.1156 -0.0092 -0.0122 -0.0145 207 VAL A CG1 
1682 C  CG2 . VAL A 206 ? 0.0671 0.1250 0.1169 -0.0048 0.0125  -0.0032 207 VAL A CG2 
1683 N  N   . THR A 207 ? 0.0534 0.0828 0.0936 -0.0054 -0.0115 -0.0081 208 THR A N   
1684 C  CA  . THR A 207 ? 0.0611 0.1002 0.0838 0.0017  -0.0046 -0.0048 208 THR A CA  
1685 C  C   . THR A 207 ? 0.0651 0.0905 0.0656 -0.0074 0.0000  0.0042  208 THR A C   
1686 O  O   . THR A 207 ? 0.0610 0.0996 0.0880 0.0019  -0.0196 -0.0042 208 THR A O   
1687 C  CB  . THR A 207 ? 0.0785 0.1027 0.0971 -0.0022 -0.0035 -0.0108 208 THR A CB  
1688 O  OG1 . THR A 207 ? 0.0927 0.1063 0.1026 0.0036  -0.0016 -0.0170 208 THR A OG1 
1689 C  CG2 . THR A 207 ? 0.0895 0.1192 0.1193 -0.0046 0.0044  0.0116  208 THR A CG2 
1690 N  N   . TRP A 208 ? 0.0598 0.0844 0.0741 -0.0024 -0.0064 -0.0015 209 TRP A N   
1691 C  CA  . TRP A 208 ? 0.0537 0.0857 0.0793 -0.0035 -0.0085 -0.0082 209 TRP A CA  
1692 C  C   . TRP A 208 ? 0.0561 0.0878 0.0651 0.0039  0.0013  -0.0055 209 TRP A C   
1693 O  O   . TRP A 208 ? 0.0595 0.1043 0.0723 -0.0061 0.0017  -0.0032 209 TRP A O   
1694 C  CB  . TRP A 208 ? 0.0465 0.0961 0.0762 0.0095  -0.0050 0.0040  209 TRP A CB  
1695 C  CG  . TRP A 208 ? 0.0457 0.0904 0.0817 0.0057  -0.0066 -0.0012 209 TRP A CG  
1696 C  CD1 . TRP A 208 ? 0.0444 0.0948 0.0947 0.0044  -0.0079 0.0061  209 TRP A CD1 
1697 C  CD2 . TRP A 208 ? 0.0362 0.0878 0.0895 0.0111  -0.0046 -0.0043 209 TRP A CD2 
1698 N  NE1 . TRP A 208 ? 0.0456 0.0966 0.0982 -0.0060 0.0011  -0.0065 209 TRP A NE1 
1699 C  CE2 . TRP A 208 ? 0.0444 0.0869 0.0911 0.0070  -0.0048 -0.0055 209 TRP A CE2 
1700 C  CE3 . TRP A 208 ? 0.0518 0.0853 0.0719 0.0041  -0.0146 0.0019  209 TRP A CE3 
1701 C  CZ2 . TRP A 208 ? 0.0525 0.0943 0.0995 0.0181  0.0092  -0.0016 209 TRP A CZ2 
1702 C  CZ3 . TRP A 208 ? 0.0635 0.1135 0.0773 0.0098  -0.0024 0.0092  209 TRP A CZ3 
1703 C  CH2 . TRP A 208 ? 0.0587 0.0995 0.0989 0.0118  0.0076  -0.0002 209 TRP A CH2 
1704 N  N   . ILE A 209 ? 0.0451 0.0841 0.0818 -0.0047 -0.0038 -0.0074 210 ILE A N   
1705 C  CA  . ILE A 209 ? 0.0450 0.0950 0.0853 -0.0043 -0.0096 -0.0024 210 ILE A CA  
1706 C  C   . ILE A 209 ? 0.0406 0.0961 0.0735 -0.0069 0.0013  -0.0005 210 ILE A C   
1707 O  O   . ILE A 209 ? 0.0832 0.1002 0.0713 -0.0086 -0.0029 0.0035  210 ILE A O   
1708 C  CB  . ILE A 209 ? 0.0403 0.1015 0.1158 -0.0051 -0.0059 -0.0013 210 ILE A CB  
1709 C  CG1 . ILE A 209 ? 0.0553 0.1095 0.1446 0.0061  -0.0062 -0.0221 210 ILE A CG1 
1710 C  CG2 . ILE A 209 ? 0.0438 0.1413 0.1327 0.0050  -0.0008 0.0071  210 ILE A CG2 
1711 C  CD1 . ILE A 209 ? 0.0695 0.1115 0.1932 0.0199  0.0051  0.0064  210 ILE A CD1 
1712 N  N   . VAL A 210 ? 0.0518 0.0871 0.0813 -0.0041 -0.0001 0.0058  211 VAL A N   
1713 C  CA  . VAL A 210 ? 0.0480 0.0880 0.0739 -0.0111 0.0005  -0.0040 211 VAL A CA  
1714 C  C   . VAL A 210 ? 0.0617 0.0882 0.0771 0.0019  0.0063  0.0077  211 VAL A C   
1715 O  O   . VAL A 210 ? 0.0712 0.1065 0.0814 -0.0144 0.0027  0.0038  211 VAL A O   
1716 C  CB  . VAL A 210 ? 0.0450 0.1020 0.1024 0.0037  -0.0043 0.0055  211 VAL A CB  
1717 C  CG1 . VAL A 210 ? 0.0977 0.0889 0.1022 0.0009  -0.0074 -0.0006 211 VAL A CG1 
1718 C  CG2 . VAL A 210 ? 0.0612 0.1202 0.1029 -0.0050 -0.0042 -0.0053 211 VAL A CG2 
1719 N  N   . LEU A 211 ? 0.0481 0.1078 0.0907 -0.0075 -0.0127 -0.0030 212 LEU A N   
1720 C  CA  . LEU A 211 ? 0.0500 0.1045 0.0971 -0.0144 -0.0088 -0.0043 212 LEU A CA  
1721 C  C   . LEU A 211 ? 0.0392 0.1110 0.0975 -0.0185 -0.0144 0.0103  212 LEU A C   
1722 O  O   . LEU A 211 ? 0.0732 0.1108 0.1002 -0.0043 -0.0059 -0.0005 212 LEU A O   
1723 C  CB  . LEU A 211 ? 0.0631 0.1209 0.1084 -0.0121 -0.0145 0.0034  212 LEU A CB  
1724 C  CG  . LEU A 211 ? 0.0695 0.1259 0.1211 -0.0067 -0.0108 0.0068  212 LEU A CG  
1725 C  CD1 . LEU A 211 ? 0.0738 0.1893 0.1679 -0.0245 -0.0593 0.0258  212 LEU A CD1 
1726 C  CD2 . LEU A 211 ? 0.0758 0.1421 0.1500 0.0182  0.0121  0.0031  212 LEU A CD2 
1727 N  N   A LYS A 212 ? 0.0757 0.1189 0.1117 -0.0305 -0.0034 0.0165  213 LYS A N   
1728 N  N   B LYS A 212 ? 0.0652 0.1122 0.1047 -0.0218 -0.0047 0.0095  213 LYS A N   
1729 C  CA  A LYS A 212 ? 0.1072 0.1160 0.0963 -0.0083 0.0190  0.0058  213 LYS A CA  
1730 C  CA  B LYS A 212 ? 0.0696 0.1094 0.0996 -0.0006 0.0113  0.0087  213 LYS A CA  
1731 C  C   A LYS A 212 ? 0.0752 0.1128 0.0904 -0.0175 0.0031  0.0163  213 LYS A C   
1732 C  C   B LYS A 212 ? 0.0622 0.1083 0.1020 -0.0199 0.0003  0.0159  213 LYS A C   
1733 O  O   A LYS A 212 ? 0.0868 0.1270 0.1284 -0.0015 0.0087  0.0138  213 LYS A O   
1734 O  O   B LYS A 212 ? 0.0769 0.1171 0.0819 -0.0002 -0.0260 -0.0048 213 LYS A O   
1735 C  CB  A LYS A 212 ? 0.1631 0.1041 0.0977 -0.0232 0.0457  -0.0030 213 LYS A CB  
1736 C  CB  B LYS A 212 ? 0.0506 0.1381 0.1042 -0.0195 0.0162  0.0006  213 LYS A CB  
1737 C  CG  A LYS A 212 ? 0.2213 0.1288 0.0889 -0.0610 -0.0225 -0.0061 213 LYS A CG  
1738 C  CG  B LYS A 212 ? 0.1641 0.1293 0.1674 0.0337  0.0389  0.0211  213 LYS A CG  
1739 C  CD  A LYS A 212 ? 0.2115 0.2279 0.1708 -0.0976 0.0022  0.0041  213 LYS A CD  
1740 C  CD  B LYS A 212 ? 0.1537 0.2284 0.1514 -0.0216 0.0308  0.0605  213 LYS A CD  
1741 C  CE  A LYS A 212 ? 0.2270 0.2760 0.3028 -0.0996 0.0150  0.0183  213 LYS A CE  
1742 C  CE  B LYS A 212 ? 0.2836 0.2471 0.2259 -0.0331 0.1012  0.0884  213 LYS A CE  
1743 N  NZ  A LYS A 212 ? 0.3937 0.4950 0.4207 0.0217  0.0819  0.0504  213 LYS A NZ  
1744 N  NZ  B LYS A 212 ? 0.5793 0.3732 0.2432 -0.1729 0.1357  0.0684  213 LYS A NZ  
1745 N  N   A GLU A 213 ? 0.0670 0.1183 0.1079 -0.0103 -0.0100 0.0165  214 GLU A N   
1746 N  N   B GLU A 213 ? 0.0707 0.1186 0.1097 -0.0077 -0.0140 0.0172  214 GLU A N   
1747 C  CA  A GLU A 213 ? 0.0552 0.1193 0.1284 -0.0223 -0.0081 0.0036  214 GLU A CA  
1748 C  CA  B GLU A 213 ? 0.0658 0.1164 0.1295 -0.0161 -0.0102 0.0068  214 GLU A CA  
1749 C  C   A GLU A 213 ? 0.0500 0.1040 0.1212 -0.0151 -0.0153 0.0149  214 GLU A C   
1750 C  C   B GLU A 213 ? 0.0546 0.1066 0.1218 -0.0174 -0.0179 0.0142  214 GLU A C   
1751 O  O   A GLU A 213 ? 0.0494 0.1111 0.1270 -0.0012 -0.0155 0.0154  214 GLU A O   
1752 O  O   B GLU A 213 ? 0.0605 0.1130 0.1284 -0.0043 -0.0161 0.0147  214 GLU A O   
1753 C  CB  A GLU A 213 ? 0.0560 0.1512 0.1320 -0.0226 -0.0131 0.0073  214 GLU A CB  
1754 C  CB  B GLU A 213 ? 0.0637 0.1489 0.1320 -0.0234 -0.0130 0.0126  214 GLU A CB  
1755 C  CG  A GLU A 213 ? 0.0878 0.1807 0.1857 -0.0407 -0.0468 0.0031  214 GLU A CG  
1756 C  CG  B GLU A 213 ? 0.1056 0.1850 0.1895 -0.0458 -0.0400 0.0017  214 GLU A CG  
1757 C  CD  A GLU A 213 ? 0.0936 0.2264 0.1487 -0.0380 -0.0595 -0.0100 214 GLU A CD  
1758 C  CD  B GLU A 213 ? 0.1169 0.2385 0.2399 -0.0542 -0.0425 0.0102  214 GLU A CD  
1759 O  OE1 A GLU A 213 ? 0.0423 0.1087 0.2568 -0.0161 -0.0594 0.0138  214 GLU A OE1 
1760 O  OE1 B GLU A 213 ? 0.1377 0.1577 0.3407 -0.0226 -0.0680 0.0476  214 GLU A OE1 
1761 O  OE2 A GLU A 213 ? 0.1141 0.3107 0.3814 -0.0428 -0.0588 -0.1564 214 GLU A OE2 
1762 O  OE2 B GLU A 213 ? 0.3436 0.4278 0.3831 0.0326  0.0805  -0.0618 214 GLU A OE2 
1763 N  N   . PRO A 214 ? 0.0904 0.1120 0.0975 -0.0070 -0.0078 0.0151  215 PRO A N   
1764 C  CA  . PRO A 214 ? 0.0835 0.1067 0.1060 0.0079  -0.0141 0.0077  215 PRO A CA  
1765 C  C   . PRO A 214 ? 0.0883 0.1101 0.1111 -0.0227 -0.0263 -0.0082 215 PRO A C   
1766 O  O   . PRO A 214 ? 0.1061 0.1703 0.1235 -0.0356 -0.0390 0.0190  215 PRO A O   
1767 C  CB  . PRO A 214 ? 0.0895 0.1104 0.1282 0.0020  -0.0109 0.0048  215 PRO A CB  
1768 C  CG  . PRO A 214 ? 0.1577 0.1613 0.1850 -0.0301 0.0173  0.0011  215 PRO A CG  
1769 C  CD  . PRO A 214 ? 0.1102 0.0946 0.1552 -0.0092 0.0160  0.0094  215 PRO A CD  
1770 N  N   . ILE A 215 ? 0.1041 0.1086 0.0939 -0.0031 -0.0201 -0.0039 216 ILE A N   
1771 C  CA  . ILE A 215 ? 0.1097 0.1027 0.1051 0.0113  -0.0311 -0.0196 216 ILE A CA  
1772 C  C   . ILE A 215 ? 0.0968 0.1078 0.1165 -0.0067 -0.0281 -0.0055 216 ILE A C   
1773 O  O   . ILE A 215 ? 0.1041 0.1061 0.1464 0.0019  -0.0240 -0.0111 216 ILE A O   
1774 C  CB  . ILE A 215 ? 0.1437 0.1011 0.1135 0.0094  -0.0260 -0.0084 216 ILE A CB  
1775 C  CG1 . ILE A 215 ? 0.1589 0.1264 0.1038 0.0064  -0.0148 0.0030  216 ILE A CG1 
1776 C  CG2 . ILE A 215 ? 0.1738 0.1322 0.1270 0.0366  -0.0499 -0.0255 216 ILE A CG2 
1777 C  CD1 . ILE A 215 ? 0.1985 0.1221 0.1325 -0.0074 -0.0368 0.0139  216 ILE A CD1 
1778 N  N   . SER A 216 ? 0.0963 0.1200 0.1315 -0.0029 -0.0292 -0.0297 217 SER A N   
1779 C  CA  . SER A 216 ? 0.0990 0.1280 0.1268 -0.0001 -0.0335 -0.0295 217 SER A CA  
1780 C  C   . SER A 216 ? 0.1165 0.0968 0.1178 -0.0005 -0.0399 -0.0125 217 SER A C   
1781 O  O   . SER A 216 ? 0.1212 0.1383 0.1415 0.0083  -0.0428 -0.0115 217 SER A O   
1782 C  CB  . SER A 216 ? 0.2380 0.1103 0.1604 -0.0392 0.0275  -0.0089 217 SER A CB  
1783 O  OG  . SER A 216 ? 0.2299 0.2169 0.1967 -0.0270 -0.0207 0.0079  217 SER A OG  
1784 N  N   . VAL A 217 ? 0.1284 0.0883 0.1229 -0.0152 -0.0292 -0.0153 218 VAL A N   
1785 C  CA  . VAL A 217 ? 0.1442 0.0941 0.1069 -0.0135 -0.0273 -0.0105 218 VAL A CA  
1786 C  C   . VAL A 217 ? 0.1343 0.1015 0.1011 -0.0181 -0.0223 -0.0051 218 VAL A C   
1787 O  O   . VAL A 217 ? 0.1284 0.1027 0.1230 -0.0217 -0.0303 -0.0068 218 VAL A O   
1788 C  CB  . VAL A 217 ? 0.1318 0.0790 0.1627 -0.0204 -0.0458 -0.0059 218 VAL A CB  
1789 C  CG1 . VAL A 217 ? 0.1606 0.1035 0.1498 -0.0243 -0.0326 -0.0173 218 VAL A CG1 
1790 C  CG2 . VAL A 217 ? 0.1361 0.1068 0.2126 -0.0092 -0.0364 -0.0033 218 VAL A CG2 
1791 N  N   . SER A 218 ? 0.1532 0.0950 0.1086 -0.0190 -0.0316 -0.0214 219 SER A N   
1792 C  CA  . SER A 218 ? 0.1442 0.0927 0.1354 -0.0118 -0.0287 -0.0264 219 SER A CA  
1793 C  C   . SER A 218 ? 0.1487 0.0928 0.1208 -0.0142 -0.0240 -0.0079 219 SER A C   
1794 O  O   . SER A 218 ? 0.1500 0.0996 0.1322 -0.0150 -0.0192 -0.0089 219 SER A O   
1795 C  CB  . SER A 218 ? 0.1636 0.1154 0.1184 -0.0037 -0.0373 -0.0163 219 SER A CB  
1796 O  OG  . SER A 218 ? 0.2137 0.1099 0.1322 -0.0144 -0.0303 -0.0068 219 SER A OG  
1797 N  N   A SER A 219 ? 0.1473 0.0880 0.1424 -0.0130 -0.0305 -0.0049 220 SER A N   
1798 N  N   B SER A 219 ? 0.1537 0.0873 0.1516 -0.0157 -0.0326 -0.0089 220 SER A N   
1799 C  CA  A SER A 219 ? 0.1658 0.0866 0.1755 0.0010  -0.0053 0.0085  220 SER A CA  
1800 C  CA  B SER A 219 ? 0.1782 0.1053 0.1785 -0.0060 -0.0085 -0.0001 220 SER A CA  
1801 C  C   A SER A 219 ? 0.1717 0.1002 0.1746 -0.0104 -0.0002 0.0034  220 SER A C   
1802 C  C   B SER A 219 ? 0.1703 0.0802 0.1918 -0.0177 -0.0043 0.0010  220 SER A C   
1803 O  O   A SER A 219 ? 0.1710 0.1146 0.1925 -0.0094 0.0185  0.0157  220 SER A O   
1804 O  O   B SER A 219 ? 0.1729 0.1077 0.2238 -0.0253 0.0163  -0.0033 220 SER A O   
1805 C  CB  A SER A 219 ? 0.1266 0.1034 0.2243 -0.0253 0.0027  0.0124  220 SER A CB  
1806 C  CB  B SER A 219 ? 0.1792 0.1392 0.1927 -0.0077 -0.0137 0.0088  220 SER A CB  
1807 O  OG  A SER A 219 ? 0.1805 0.0965 0.1780 0.0008  0.0000  -0.0231 220 SER A OG  
1808 O  OG  B SER A 219 ? 0.1893 0.1550 0.2511 -0.0197 0.0219  0.0048  220 SER A OG  
1809 N  N   . GLU A 220 ? 0.1746 0.1022 0.1430 0.0013  0.0009  -0.0108 221 GLU A N   
1810 C  CA  . GLU A 220 ? 0.2107 0.1185 0.1643 -0.0176 -0.0195 -0.0204 221 GLU A CA  
1811 C  C   . GLU A 220 ? 0.2191 0.1268 0.1178 -0.0104 0.0000  -0.0009 221 GLU A C   
1812 O  O   . GLU A 220 ? 0.2083 0.1444 0.1465 -0.0043 0.0211  -0.0159 221 GLU A O   
1813 C  CB  . GLU A 220 ? 0.2876 0.1794 0.1568 -0.0423 -0.0367 -0.0449 221 GLU A CB  
1814 C  CG  . GLU A 220 ? 0.3628 0.2207 0.2245 -0.0740 -0.0467 -0.0920 221 GLU A CG  
1815 C  CD  . GLU A 220 ? 0.3386 0.1864 0.2232 -0.0683 -0.0245 -0.0867 221 GLU A CD  
1816 O  OE1 . GLU A 220 ? 0.3106 0.1767 0.2615 -0.0890 0.0146  -0.0553 221 GLU A OE1 
1817 O  OE2 . GLU A 220 ? 0.5312 0.2977 0.4314 -0.1782 0.1235  -0.1986 221 GLU A OE2 
1818 N  N   . GLN A 221 ? 0.1758 0.1074 0.1437 -0.0152 -0.0201 -0.0087 222 GLN A N   
1819 C  CA  . GLN A 221 ? 0.1886 0.1027 0.1361 -0.0125 -0.0183 -0.0140 222 GLN A CA  
1820 C  C   . GLN A 221 ? 0.1588 0.1079 0.1336 0.0041  -0.0046 0.0212  222 GLN A C   
1821 O  O   . GLN A 221 ? 0.2046 0.1252 0.1254 -0.0276 0.0074  0.0173  222 GLN A O   
1822 C  CB  . GLN A 221 ? 0.1760 0.1293 0.1097 -0.0216 -0.0403 -0.0148 222 GLN A CB  
1823 C  CG  . GLN A 221 ? 0.1983 0.1207 0.1010 -0.0190 -0.0357 -0.0026 222 GLN A CG  
1824 C  CD  . GLN A 221 ? 0.1570 0.1146 0.1284 -0.0071 -0.0434 -0.0084 222 GLN A CD  
1825 O  OE1 . GLN A 221 ? 0.1575 0.1151 0.1293 -0.0085 -0.0343 -0.0114 222 GLN A OE1 
1826 N  NE2 . GLN A 221 ? 0.1640 0.1273 0.1435 -0.0051 -0.0480 0.0058  222 GLN A NE2 
1827 N  N   A VAL A 222 ? 0.1701 0.1054 0.1237 -0.0275 -0.0178 0.0184  223 VAL A N   
1828 N  N   B VAL A 222 ? 0.1821 0.1123 0.1394 -0.0144 -0.0309 0.0179  223 VAL A N   
1829 C  CA  A VAL A 222 ? 0.1446 0.1388 0.1320 -0.0283 -0.0131 0.0233  223 VAL A CA  
1830 C  CA  B VAL A 222 ? 0.1521 0.1379 0.1546 -0.0269 -0.0044 0.0195  223 VAL A CA  
1831 C  C   A VAL A 222 ? 0.1665 0.1081 0.1453 -0.0041 0.0033  0.0155  223 VAL A C   
1832 C  C   B VAL A 222 ? 0.1606 0.1185 0.1561 -0.0271 0.0017  0.0089  223 VAL A C   
1833 O  O   A VAL A 222 ? 0.1949 0.1135 0.1451 -0.0284 0.0006  0.0359  223 VAL A O   
1834 O  O   B VAL A 222 ? 0.1403 0.1521 0.1713 -0.0251 -0.0089 0.0477  223 VAL A O   
1835 C  CB  A VAL A 222 ? 0.1491 0.1422 0.1275 -0.0285 -0.0154 0.0218  223 VAL A CB  
1836 C  CB  B VAL A 222 ? 0.1841 0.2117 0.1699 0.0262  0.0118  0.0445  223 VAL A CB  
1837 C  CG1 A VAL A 222 ? 0.1087 0.1372 0.1582 -0.0543 -0.0491 0.0628  223 VAL A CG1 
1838 C  CG1 B VAL A 222 ? 0.1458 0.2642 0.1782 0.0240  0.0488  0.0416  223 VAL A CG1 
1839 C  CG2 A VAL A 222 ? 0.1340 0.1476 0.1952 0.0150  -0.0427 -0.0276 223 VAL A CG2 
1840 C  CG2 B VAL A 222 ? 0.1417 0.2545 0.2338 0.0434  -0.0005 0.0044  223 VAL A CG2 
1841 N  N   . LEU A 223 ? 0.1703 0.1252 0.1676 -0.0107 0.0079  0.0030  224 LEU A N   
1842 C  CA  . LEU A 223 ? 0.1914 0.1356 0.1900 -0.0201 0.0333  -0.0089 224 LEU A CA  
1843 C  C   . LEU A 223 ? 0.1929 0.1557 0.1467 -0.0317 0.0170  -0.0267 224 LEU A C   
1844 O  O   . LEU A 223 ? 0.1879 0.1843 0.1990 -0.0131 0.0251  -0.0245 224 LEU A O   
1845 C  CB  . LEU A 223 ? 0.2169 0.1439 0.2311 -0.0146 0.0308  -0.0403 224 LEU A CB  
1846 C  CG  . LEU A 223 ? 0.3890 0.1907 0.3128 -0.0274 0.0586  -0.0378 224 LEU A CG  
1847 C  CD1 . LEU A 223 ? 0.3456 0.1841 0.3845 -0.0019 0.0104  -0.0313 224 LEU A CD1 
1848 C  CD2 . LEU A 223 ? 0.4126 0.1979 0.5680 0.0468  0.1142  -0.0229 224 LEU A CD2 
1849 N  N   . LYS A 224 ? 0.2542 0.1406 0.1307 -0.0181 0.0016  0.0011  225 LYS A N   
1850 C  CA  . LYS A 224 ? 0.2022 0.1742 0.1465 -0.0178 0.0279  0.0053  225 LYS A CA  
1851 C  C   . LYS A 224 ? 0.2135 0.1579 0.1119 -0.0091 0.0214  0.0155  225 LYS A C   
1852 O  O   . LYS A 224 ? 0.2085 0.1552 0.1214 -0.0251 0.0337  0.0018  225 LYS A O   
1853 C  CB  . LYS A 224 ? 0.2331 0.2213 0.1905 0.0151  -0.0099 0.0531  225 LYS A CB  
1854 C  CG  . LYS A 224 ? 0.2821 0.2973 0.2153 -0.0190 -0.0395 0.0015  225 LYS A CG  
1855 C  CD  . LYS A 224 ? 0.3828 0.2053 0.2836 0.0179  -0.0567 -0.0153 225 LYS A CD  
1856 C  CE  . LYS A 224 ? 0.3507 0.3265 0.3676 -0.0179 0.0141  -0.1190 225 LYS A CE  
1857 N  NZ  . LYS A 224 ? 0.3449 0.3424 0.5664 0.0259  -0.0242 -0.0669 225 LYS A NZ  
1858 N  N   . PHE A 225 ? 0.2112 0.1374 0.1069 -0.0161 0.0175  0.0073  226 PHE A N   
1859 C  CA  . PHE A 225 ? 0.1801 0.1245 0.1083 -0.0163 0.0403  0.0016  226 PHE A CA  
1860 C  C   . PHE A 225 ? 0.1773 0.1117 0.1203 -0.0273 0.0286  0.0034  226 PHE A C   
1861 O  O   . PHE A 225 ? 0.1938 0.1239 0.1158 -0.0309 0.0357  -0.0171 226 PHE A O   
1862 C  CB  . PHE A 225 ? 0.1907 0.1245 0.1133 -0.0199 0.0345  -0.0050 226 PHE A CB  
1863 C  CG  . PHE A 225 ? 0.1893 0.1135 0.1259 -0.0462 0.0392  -0.0298 226 PHE A CG  
1864 C  CD1 . PHE A 225 ? 0.2367 0.2354 0.1805 0.0271  0.0543  0.0279  226 PHE A CD1 
1865 C  CD2 . PHE A 225 ? 0.2353 0.2069 0.1589 -0.0217 0.0252  -0.0449 226 PHE A CD2 
1866 C  CE1 . PHE A 225 ? 0.2972 0.2257 0.1923 0.0466  0.0763  0.0263  226 PHE A CE1 
1867 C  CE2 . PHE A 225 ? 0.1816 0.2415 0.2173 -0.0386 0.0229  -0.1138 226 PHE A CE2 
1868 C  CZ  . PHE A 225 ? 0.1862 0.1690 0.2132 -0.0514 0.0221  -0.0536 226 PHE A CZ  
1869 N  N   . ARG A 226 ? 0.1564 0.1246 0.1112 -0.0091 0.0108  -0.0029 227 ARG A N   
1870 C  CA  . ARG A 226 ? 0.1629 0.1399 0.1277 -0.0252 0.0303  -0.0010 227 ARG A CA  
1871 C  C   . ARG A 226 ? 0.1958 0.1147 0.1527 -0.0277 0.0337  -0.0084 227 ARG A C   
1872 O  O   . ARG A 226 ? 0.2020 0.1552 0.1487 -0.0196 0.0343  -0.0142 227 ARG A O   
1873 C  CB  . ARG A 226 ? 0.2076 0.1259 0.1214 -0.0143 0.0270  0.0012  227 ARG A CB  
1874 C  CG  . ARG A 226 ? 0.1749 0.1275 0.1313 -0.0244 0.0290  0.0097  227 ARG A CG  
1875 C  CD  . ARG A 226 ? 0.2615 0.1209 0.1492 -0.0174 0.0272  0.0218  227 ARG A CD  
1876 N  NE  . ARG A 226 ? 0.1753 0.1208 0.1212 -0.0533 -0.0138 -0.0089 227 ARG A NE  
1877 C  CZ  . ARG A 226 ? 0.1857 0.1392 0.1232 -0.0563 -0.0040 -0.0264 227 ARG A CZ  
1878 N  NH1 . ARG A 226 ? 0.2220 0.1764 0.1902 -0.0748 -0.0194 -0.0486 227 ARG A NH1 
1879 N  NH2 . ARG A 226 ? 0.2231 0.1519 0.1333 -0.0638 0.0201  0.0006  227 ARG A NH2 
1880 N  N   . LYS A 227 ? 0.1834 0.1259 0.1011 -0.0285 0.0285  -0.0280 228 LYS A N   
1881 C  CA  . LYS A 227 ? 0.2173 0.1451 0.1147 -0.0511 0.0454  -0.0407 228 LYS A CA  
1882 C  C   . LYS A 227 ? 0.2327 0.1394 0.0971 -0.0402 0.0558  -0.0228 228 LYS A C   
1883 O  O   . LYS A 227 ? 0.2870 0.1755 0.1133 -0.0706 0.0604  -0.0309 228 LYS A O   
1884 C  CB  . LYS A 227 ? 0.2854 0.1985 0.1088 -0.0829 0.0307  -0.0525 228 LYS A CB  
1885 C  CG  . LYS A 227 ? 0.2970 0.2119 0.1751 -0.0999 0.0621  -0.0495 228 LYS A CG  
1886 C  CD  . LYS A 227 ? 0.3953 0.3177 0.3061 -0.1640 -0.0215 -0.0726 228 LYS A CD  
1887 N  N   . LEU A 228 ? 0.2394 0.1320 0.1072 -0.0751 0.0476  -0.0405 229 LEU A N   
1888 C  CA  . LEU A 228 ? 0.1956 0.1469 0.1230 -0.0735 0.0309  -0.0333 229 LEU A CA  
1889 C  C   . LEU A 228 ? 0.2451 0.1235 0.1027 -0.0625 0.0374  -0.0416 229 LEU A C   
1890 O  O   . LEU A 228 ? 0.1976 0.1512 0.1207 -0.0484 0.0675  -0.0477 229 LEU A O   
1891 C  CB  . LEU A 228 ? 0.2588 0.1390 0.0922 -0.0825 0.0378  -0.0293 229 LEU A CB  
1892 C  CG  . LEU A 228 ? 0.2331 0.1622 0.1050 -0.0356 0.0316  -0.0066 229 LEU A CG  
1893 C  CD1 . LEU A 228 ? 0.2543 0.1638 0.1098 -0.0480 0.0449  -0.0357 229 LEU A CD1 
1894 C  CD2 . LEU A 228 ? 0.3051 0.1480 0.1219 -0.0120 0.0405  0.0286  229 LEU A CD2 
1895 N  N   . ASN A 229 ? 0.2078 0.1661 0.1130 -0.0741 0.0631  -0.0317 230 ASN A N   
1896 C  CA  . ASN A 229 ? 0.2475 0.1593 0.0747 -0.0269 0.0347  -0.0446 230 ASN A CA  
1897 C  C   . ASN A 229 ? 0.1615 0.2239 0.1444 0.0004  0.0794  0.0030  230 ASN A C   
1898 O  O   . ASN A 229 ? 0.2675 0.1787 0.1421 -0.0578 0.0527  -0.0510 230 ASN A O   
1899 C  CB  . ASN A 229 ? 0.2716 0.1778 0.1239 -0.0848 0.0757  -0.0464 230 ASN A CB  
1900 C  CG  . ASN A 229 ? 0.3227 0.2268 0.1075 -0.0923 0.0679  -0.0648 230 ASN A CG  
1901 O  OD1 . ASN A 229 ? 0.4200 0.2240 0.1234 -0.0680 0.1028  -0.0506 230 ASN A OD1 
1902 N  ND2 . ASN A 229 ? 0.2912 0.1726 0.1509 -0.0849 0.0587  -0.0602 230 ASN A ND2 
1903 N  N   . PHE A 230 ? 0.1905 0.1503 0.1383 -0.0597 0.0814  -0.0358 231 PHE A N   
1904 C  CA  . PHE A 230 ? 0.1597 0.1665 0.1812 -0.0576 0.0122  -0.0074 231 PHE A CA  
1905 C  C   . PHE A 230 ? 0.2509 0.2060 0.2004 -0.1260 0.1123  -0.0748 231 PHE A C   
1906 O  O   . PHE A 230 ? 0.2839 0.2055 0.1704 -0.1293 0.1047  -0.0449 231 PHE A O   
1907 C  CB  . PHE A 230 ? 0.1807 0.1861 0.1631 -0.0621 0.0925  -0.0326 231 PHE A CB  
1908 C  CG  . PHE A 230 ? 0.1773 0.1780 0.1663 -0.0601 0.0572  -0.0223 231 PHE A CG  
1909 C  CD1 . PHE A 230 ? 0.2178 0.1983 0.1392 -0.0866 0.0703  -0.0407 231 PHE A CD1 
1910 C  CD2 . PHE A 230 ? 0.1747 0.2403 0.1217 0.0073  0.0485  -0.0418 231 PHE A CD2 
1911 C  CE1 . PHE A 230 ? 0.2146 0.1864 0.1875 -0.0765 0.0568  -0.0612 231 PHE A CE1 
1912 C  CE2 . PHE A 230 ? 0.2040 0.2042 0.1731 -0.0646 0.0514  -0.0497 231 PHE A CE2 
1913 C  CZ  . PHE A 230 ? 0.2097 0.2286 0.1010 -0.0637 0.0484  -0.0276 231 PHE A CZ  
1914 N  N   . ASN A 231 ? 0.2769 0.2302 0.1552 -0.1077 0.1215  -0.0559 232 ASN A N   
1915 C  CA  . ASN A 231 ? 0.1575 0.2128 0.1825 -0.0728 0.0624  -0.0618 232 ASN A CA  
1916 C  C   . ASN A 231 ? 0.1223 0.2609 0.1422 0.0408  -0.0038 -0.0432 232 ASN A C   
1917 O  O   . ASN A 231 ? 0.2581 0.2115 0.1882 -0.0812 0.0709  -0.0496 232 ASN A O   
1918 C  CB  . ASN A 231 ? 0.2592 0.2078 0.2214 -0.0819 0.1215  -0.0474 232 ASN A CB  
1919 C  CG  . ASN A 231 ? 0.2850 0.2171 0.2410 -0.0929 0.1136  -0.0122 232 ASN A CG  
1920 O  OD1 . ASN A 231 ? 0.4466 0.2117 0.2223 -0.1052 0.1336  -0.1039 232 ASN A OD1 
1921 N  ND2 . ASN A 231 ? 0.4079 0.2619 0.1927 -0.0974 0.1069  -0.0893 232 ASN A ND2 
1922 N  N   . GLY A 232 ? 0.2543 0.1864 0.1922 -0.0015 0.0465  -0.0304 233 GLY A N   
1923 C  CA  . GLY A 232 ? 0.2151 0.2426 0.1469 0.0048  0.0504  0.0204  233 GLY A CA  
1924 C  C   . GLY A 232 ? 0.1606 0.1922 0.2126 -0.0019 -0.0296 -0.0093 233 GLY A C   
1925 O  O   . GLY A 232 ? 0.2437 0.3234 0.2273 0.0388  0.1170  0.0947  233 GLY A O   
1926 N  N   . GLU A 233 ? 0.1907 0.2279 0.1816 -0.0250 0.0359  -0.0119 234 GLU A N   
1927 C  CA  . GLU A 233 ? 0.1879 0.2139 0.1634 0.0066  0.0044  -0.0273 234 GLU A CA  
1928 C  C   . GLU A 233 ? 0.2083 0.2428 0.2394 0.0209  0.0005  -0.0055 234 GLU A C   
1929 O  O   . GLU A 233 ? 0.2728 0.3170 0.1808 -0.0436 0.0713  0.0054  234 GLU A O   
1930 C  CB  . GLU A 233 ? 0.2475 0.2308 0.1794 0.0421  0.0058  0.0203  234 GLU A CB  
1931 C  CG  . GLU A 233 ? 0.2513 0.3352 0.1627 -0.0570 0.0203  -0.0227 234 GLU A CG  
1932 C  CD  . GLU A 233 ? 0.2791 0.4346 0.3447 0.0435  0.1384  -0.0069 234 GLU A CD  
1933 O  OE1 . GLU A 233 ? 0.4130 0.3714 0.3267 -0.0609 0.1575  0.0234  234 GLU A OE1 
1934 O  OE2 . GLU A 233 ? 0.4265 0.4511 0.3107 0.0318  0.0373  -0.0423 234 GLU A OE2 
1935 N  N   . GLY A 234 ? 0.3967 0.2732 0.2388 -0.0149 0.1236  -0.0599 235 GLY A N   
1936 C  CA  . GLY A 234 ? 0.3540 0.3386 0.2162 0.0556  0.0653  0.0619  235 GLY A CA  
1937 C  C   . GLY A 234 ? 0.2957 0.3524 0.1920 0.0841  0.0795  0.0485  235 GLY A C   
1938 O  O   . GLY A 234 ? 0.3312 0.6873 0.3043 0.1028  0.1340  0.0841  235 GLY A O   
1939 N  N   . GLU A 235 ? 0.2295 0.3404 0.2338 0.0389  0.1208  -0.0099 236 GLU A N   
1940 C  CA  . GLU A 235 ? 0.2451 0.2019 0.2022 0.0791  0.0772  0.0619  236 GLU A CA  
1941 C  C   . GLU A 235 ? 0.2331 0.3188 0.2349 0.0361  0.0505  -0.0238 236 GLU A C   
1942 O  O   . GLU A 235 ? 0.2658 0.3370 0.2581 -0.0352 0.0621  -0.0218 236 GLU A O   
1943 C  CB  . GLU A 235 ? 0.3520 0.2784 0.2865 0.0073  0.1720  -0.0044 236 GLU A CB  
1944 C  CG  . GLU A 235 ? 0.3517 0.2508 0.3067 -0.0250 0.1569  -0.0036 236 GLU A CG  
1945 C  CD  . GLU A 235 ? 0.4950 0.3741 0.3366 -0.2199 0.1844  -0.0354 236 GLU A CD  
1946 O  OE1 . GLU A 235 ? 0.2626 0.3407 0.3547 -0.0915 0.1158  0.0142  236 GLU A OE1 
1947 O  OE2 . GLU A 235 ? 0.5272 0.3546 0.5090 -0.1736 0.3227  -0.0768 236 GLU A OE2 
1948 N  N   . PRO A 236 ? 0.1656 0.2671 0.2795 0.0176  0.0785  0.0889  237 PRO A N   
1949 C  CA  . PRO A 236 ? 0.3161 0.2958 0.3171 0.0267  0.1925  0.0339  237 PRO A CA  
1950 C  C   . PRO A 236 ? 0.4605 0.2798 0.2457 -0.1037 0.2701  -0.0782 237 PRO A C   
1951 O  O   . PRO A 236 ? 0.4004 0.3070 0.3739 -0.1342 0.2039  -0.1162 237 PRO A O   
1952 C  CB  . PRO A 236 ? 0.3089 0.4623 0.3833 0.1268  0.1506  0.1620  237 PRO A CB  
1953 C  CG  . PRO A 236 ? 0.6003 0.4666 0.3912 0.0881  0.0244  0.1556  237 PRO A CG  
1954 C  CD  . PRO A 236 ? 0.2839 0.4467 0.3585 -0.0215 0.0293  0.0728  237 PRO A CD  
1955 N  N   . GLU A 237 ? 0.3847 0.2284 0.2390 -0.0578 0.1812  -0.0403 238 GLU A N   
1956 C  CA  . GLU A 237 ? 0.3629 0.2886 0.1485 -0.0801 0.1423  -0.0526 238 GLU A CA  
1957 C  C   . GLU A 237 ? 0.2927 0.2574 0.2081 -0.0995 0.1285  -0.0366 238 GLU A C   
1958 O  O   . GLU A 237 ? 0.2184 0.3076 0.1374 -0.0723 0.0541  -0.0510 238 GLU A O   
1959 C  CB  . GLU A 237 ? 0.3560 0.1981 0.1510 -0.0051 0.0538  -0.0333 238 GLU A CB  
1960 C  CG  . GLU A 237 ? 0.2865 0.2772 0.1927 -0.0432 0.0342  -0.0812 238 GLU A CG  
1961 C  CD  . GLU A 237 ? 0.2636 0.1825 0.1347 -0.0133 0.0115  -0.0276 238 GLU A CD  
1962 O  OE1 . GLU A 237 ? 0.3560 0.2496 0.2994 0.0746  -0.1092 -0.0995 238 GLU A OE1 
1963 O  OE2 . GLU A 237 ? 0.2805 0.1995 0.1783 -0.0044 0.0107  -0.0538 238 GLU A OE2 
1964 N  N   . GLU A 238 ? 0.2313 0.2570 0.1670 -0.1196 0.1128  -0.0756 239 GLU A N   
1965 C  CA  . GLU A 238 ? 0.2033 0.3731 0.1636 -0.1590 0.1046  -0.0993 239 GLU A CA  
1966 C  C   . GLU A 238 ? 0.1471 0.2324 0.1313 -0.0832 0.0514  -0.0271 239 GLU A C   
1967 O  O   . GLU A 238 ? 0.3160 0.2157 0.1746 -0.1117 0.1057  -0.0480 239 GLU A O   
1968 C  CB  . GLU A 238 ? 0.3242 0.5277 0.2178 -0.2961 0.1339  -0.1709 239 GLU A CB  
1969 C  CG  . GLU A 238 ? 0.4297 0.6871 0.3085 -0.2031 0.1295  -0.0693 239 GLU A CG  
1970 C  CD  . GLU A 238 ? 0.2698 0.3738 0.3610 0.1855  0.1152  0.1040  239 GLU A CD  
1971 O  OE1 . GLU A 238 ? 0.2886 0.4201 0.3493 0.0102  -0.0221 0.0268  239 GLU A OE1 
1972 O  OE2 . GLU A 238 ? 0.2518 0.8542 0.2953 -0.1489 0.0781  -0.1991 239 GLU A OE2 
1973 N  N   . LEU A 239 ? 0.1604 0.2171 0.1199 -0.0650 0.0623  -0.0593 240 LEU A N   
1974 C  CA  . LEU A 239 ? 0.1318 0.1958 0.1211 -0.0590 0.0478  -0.0238 240 LEU A CA  
1975 C  C   . LEU A 239 ? 0.1776 0.1636 0.0974 -0.0713 0.0339  -0.0184 240 LEU A C   
1976 O  O   . LEU A 239 ? 0.1523 0.1970 0.1358 -0.0552 0.0675  -0.0277 240 LEU A O   
1977 C  CB  . LEU A 239 ? 0.1566 0.1611 0.1361 -0.0129 0.0333  -0.0227 240 LEU A CB  
1978 C  CG  . LEU A 239 ? 0.1460 0.1394 0.1742 -0.0219 0.0010  -0.0364 240 LEU A CG  
1979 C  CD1 . LEU A 239 ? 0.1886 0.1338 0.3165 0.0017  -0.0377 -0.0302 240 LEU A CD1 
1980 C  CD2 . LEU A 239 ? 0.2144 0.1597 0.1706 0.0083  0.0108  -0.0447 240 LEU A CD2 
1981 N  N   . MET A 240 ? 0.1837 0.1566 0.1273 -0.0405 0.0726  -0.0310 241 MET A N   
1982 C  CA  . MET A 240 ? 0.2108 0.1740 0.0966 -0.0538 0.0810  -0.0302 241 MET A CA  
1983 C  C   . MET A 240 ? 0.1625 0.1751 0.0993 -0.0577 0.0291  -0.0326 241 MET A C   
1984 O  O   . MET A 240 ? 0.1546 0.1598 0.1084 -0.0531 0.0378  -0.0234 241 MET A O   
1985 C  CB  . MET A 240 ? 0.2182 0.1277 0.1313 -0.0346 0.0685  -0.0261 241 MET A CB  
1986 C  CG  . MET A 240 ? 0.1853 0.2439 0.1121 -0.0704 0.0794  -0.0614 241 MET A CG  
1987 S  SD  . MET A 240 ? 0.2525 0.1318 0.1383 -0.0523 0.0719  -0.0245 241 MET A SD  
1988 C  CE  . MET A 240 ? 0.2721 0.1591 0.1417 -0.0717 0.0907  -0.0146 241 MET A CE  
1989 N  N   . VAL A 241 ? 0.1553 0.1377 0.1201 -0.0427 0.0579  -0.0409 242 VAL A N   
1990 C  CA  . VAL A 241 ? 0.1503 0.1270 0.1007 -0.0445 0.0548  -0.0366 242 VAL A CA  
1991 C  C   . VAL A 241 ? 0.1372 0.1178 0.1184 -0.0359 0.0425  -0.0414 242 VAL A C   
1992 O  O   . VAL A 241 ? 0.1376 0.1580 0.1175 -0.0406 0.0529  -0.0441 242 VAL A O   
1993 C  CB  . VAL A 241 ? 0.1365 0.1315 0.1324 -0.0223 0.0543  -0.0384 242 VAL A CB  
1994 C  CG1 . VAL A 241 ? 0.1656 0.1467 0.1478 -0.0507 0.0377  -0.0570 242 VAL A CG1 
1995 C  CG2 . VAL A 241 ? 0.1879 0.1261 0.1611 -0.0299 0.0804  -0.0502 242 VAL A CG2 
1996 N  N   . ASP A 242 ? 0.1302 0.1110 0.0977 -0.0319 0.0446  -0.0370 243 ASP A N   
1997 C  CA  . ASP A 242 ? 0.1124 0.1117 0.1223 -0.0039 0.0264  -0.0411 243 ASP A CA  
1998 C  C   . ASP A 242 ? 0.1189 0.1219 0.0975 -0.0425 0.0341  -0.0345 243 ASP A C   
1999 O  O   . ASP A 242 ? 0.1158 0.1324 0.1600 -0.0399 0.0367  -0.0392 243 ASP A O   
2000 C  CB  . ASP A 242 ? 0.1129 0.1234 0.1279 -0.0184 0.0250  -0.0322 243 ASP A CB  
2001 C  CG  . ASP A 242 ? 0.1172 0.1284 0.1462 -0.0086 0.0294  -0.0423 243 ASP A CG  
2002 O  OD1 . ASP A 242 ? 0.1060 0.1128 0.1351 -0.0036 0.0277  -0.0209 243 ASP A OD1 
2003 O  OD2 . ASP A 242 ? 0.1212 0.1361 0.1769 0.0044  0.0365  -0.0411 243 ASP A OD2 
2004 N  N   . ASN A 243 ? 0.1227 0.0930 0.1088 -0.0175 0.0420  -0.0326 244 ASN A N   
2005 C  CA  . ASN A 243 ? 0.1254 0.0932 0.1153 -0.0274 0.0370  -0.0357 244 ASN A CA  
2006 C  C   . ASN A 243 ? 0.0652 0.1031 0.1044 -0.0195 0.0252  -0.0114 244 ASN A C   
2007 O  O   . ASN A 243 ? 0.1135 0.1093 0.1047 0.0018  0.0361  -0.0151 244 ASN A O   
2008 C  CB  . ASN A 243 ? 0.1273 0.1173 0.0991 -0.0466 0.0359  -0.0134 244 ASN A CB  
2009 C  CG  . ASN A 243 ? 0.1191 0.1219 0.1029 -0.0606 0.0407  -0.0178 244 ASN A CG  
2010 O  OD1 . ASN A 243 ? 0.1036 0.1277 0.1286 -0.0350 0.0323  0.0025  244 ASN A OD1 
2011 N  ND2 . ASN A 243 ? 0.1728 0.1570 0.1891 -0.0590 0.0109  0.0599  244 ASN A ND2 
2012 N  N   . TRP A 244 ? 0.0959 0.0932 0.1010 -0.0161 0.0309  -0.0249 245 TRP A N   
2013 C  CA  . TRP A 244 ? 0.0632 0.1129 0.0996 -0.0176 0.0166  -0.0193 245 TRP A CA  
2014 C  C   . TRP A 244 ? 0.0730 0.1004 0.1089 -0.0113 0.0193  -0.0142 245 TRP A C   
2015 O  O   . TRP A 244 ? 0.0796 0.1241 0.1455 0.0070  0.0074  -0.0396 245 TRP A O   
2016 C  CB  . TRP A 244 ? 0.0842 0.0977 0.1032 -0.0061 0.0244  -0.0214 245 TRP A CB  
2017 C  CG  . TRP A 244 ? 0.0716 0.1033 0.1076 -0.0057 0.0192  -0.0065 245 TRP A CG  
2018 C  CD1 . TRP A 244 ? 0.1009 0.0984 0.1163 -0.0043 0.0341  -0.0183 245 TRP A CD1 
2019 C  CD2 . TRP A 244 ? 0.0625 0.1119 0.1098 -0.0086 0.0234  -0.0142 245 TRP A CD2 
2020 N  NE1 . TRP A 244 ? 0.0950 0.1066 0.1154 -0.0111 0.0271  -0.0076 245 TRP A NE1 
2021 C  CE2 . TRP A 244 ? 0.0772 0.0990 0.1180 0.0027  0.0232  -0.0016 245 TRP A CE2 
2022 C  CE3 . TRP A 244 ? 0.0970 0.1094 0.1223 -0.0147 0.0082  -0.0140 245 TRP A CE3 
2023 C  CZ2 . TRP A 244 ? 0.1044 0.1099 0.1483 0.0100  0.0211  -0.0098 245 TRP A CZ2 
2024 C  CZ3 . TRP A 244 ? 0.1115 0.1320 0.1439 0.0013  0.0071  0.0033  245 TRP A CZ3 
2025 C  CH2 . TRP A 244 ? 0.1150 0.1349 0.1444 0.0275  0.0268  0.0103  245 TRP A CH2 
2026 N  N   . ARG A 245 ? 0.0809 0.1090 0.0980 -0.0134 0.0136  -0.0271 246 ARG A N   
2027 C  CA  . ARG A 245 ? 0.0761 0.1104 0.1133 -0.0031 0.0155  -0.0192 246 ARG A CA  
2028 C  C   . ARG A 245 ? 0.0529 0.1146 0.1061 0.0088  -0.0053 -0.0354 246 ARG A C   
2029 O  O   . ARG A 245 ? 0.0680 0.1223 0.1232 0.0035  -0.0017 -0.0192 246 ARG A O   
2030 C  CB  . ARG A 245 ? 0.0555 0.1115 0.1168 -0.0011 -0.0065 -0.0298 246 ARG A CB  
2031 C  CG  . ARG A 245 ? 0.0356 0.1180 0.1456 0.0008  -0.0017 -0.0288 246 ARG A CG  
2032 C  CD  . ARG A 245 ? 0.0384 0.1203 0.1379 -0.0201 0.0078  -0.0358 246 ARG A CD  
2033 N  NE  . ARG A 245 ? 0.0476 0.1336 0.1482 -0.0209 0.0050  -0.0379 246 ARG A NE  
2034 C  CZ  . ARG A 245 ? 0.0590 0.1302 0.1205 -0.0225 0.0086  -0.0308 246 ARG A CZ  
2035 N  NH1 . ARG A 245 ? 0.0743 0.1306 0.1291 -0.0111 0.0155  -0.0290 246 ARG A NH1 
2036 N  NH2 . ARG A 245 ? 0.0670 0.1408 0.1695 -0.0274 -0.0081 -0.0154 246 ARG A NH2 
2037 N  N   A PRO A 246 ? 0.0717 0.1108 0.1293 0.0099  0.0054  -0.0089 247 PRO A N   
2038 N  N   B PRO A 246 ? 0.0721 0.1142 0.1263 0.0140  0.0076  -0.0124 247 PRO A N   
2039 C  CA  A PRO A 246 ? 0.0847 0.1181 0.1199 0.0054  -0.0082 -0.0102 247 PRO A CA  
2040 C  CA  B PRO A 246 ? 0.0892 0.1230 0.1165 0.0115  -0.0111 -0.0044 247 PRO A CA  
2041 C  C   A PRO A 246 ? 0.0756 0.1045 0.1248 0.0148  -0.0095 -0.0079 247 PRO A C   
2042 C  C   B PRO A 246 ? 0.0747 0.1044 0.1252 0.0126  -0.0130 -0.0063 247 PRO A C   
2043 O  O   A PRO A 246 ? 0.0675 0.1241 0.1257 0.0066  -0.0077 -0.0186 247 PRO A O   
2044 O  O   B PRO A 246 ? 0.0675 0.1284 0.1309 0.0005  -0.0156 -0.0129 247 PRO A O   
2045 C  CB  A PRO A 246 ? 0.1096 0.1455 0.1512 0.0468  0.0172  -0.0331 247 PRO A CB  
2046 C  CB  B PRO A 246 ? 0.1090 0.1237 0.1817 0.0257  -0.0122 -0.0333 247 PRO A CB  
2047 C  CG  A PRO A 246 ? 0.0615 0.1460 0.1683 0.0093  0.0273  0.0170  247 PRO A CG  
2048 C  CG  B PRO A 246 ? 0.0977 0.1679 0.2593 0.0512  -0.0013 0.0216  247 PRO A CG  
2049 C  CD  A PRO A 246 ? 0.0526 0.1171 0.1539 0.0139  -0.0265 -0.0179 247 PRO A CD  
2050 C  CD  B PRO A 246 ? 0.0717 0.1595 0.1519 0.0447  -0.0188 -0.0528 247 PRO A CD  
2051 N  N   . ALA A 247 ? 0.0806 0.1250 0.1207 0.0127  -0.0065 -0.0053 248 ALA A N   
2052 C  CA  . ALA A 247 ? 0.0955 0.1190 0.1259 0.0063  -0.0074 -0.0016 248 ALA A CA  
2053 C  C   . ALA A 247 ? 0.0697 0.1275 0.1186 0.0286  -0.0168 0.0039  248 ALA A C   
2054 O  O   . ALA A 247 ? 0.0893 0.1388 0.1437 0.0388  -0.0229 -0.0011 248 ALA A O   
2055 C  CB  . ALA A 247 ? 0.1200 0.1498 0.1462 -0.0122 0.0255  0.0035  248 ALA A CB  
2056 N  N   . GLN A 248 ? 0.0687 0.1165 0.1320 0.0152  -0.0195 -0.0072 249 GLN A N   
2057 C  CA  . GLN A 248 ? 0.0555 0.1446 0.1291 0.0104  -0.0303 -0.0035 249 GLN A CA  
2058 C  C   . GLN A 248 ? 0.0783 0.1361 0.1358 0.0124  -0.0403 0.0115  249 GLN A C   
2059 O  O   . GLN A 248 ? 0.0988 0.1399 0.1388 0.0156  -0.0184 0.0000  249 GLN A O   
2060 C  CB  . GLN A 248 ? 0.0973 0.1300 0.1505 -0.0027 -0.0252 -0.0144 249 GLN A CB  
2061 C  CG  . GLN A 248 ? 0.0826 0.1498 0.1367 0.0034  -0.0282 0.0018  249 GLN A CG  
2062 C  CD  . GLN A 248 ? 0.0671 0.1685 0.1555 -0.0263 -0.0077 -0.0026 249 GLN A CD  
2063 O  OE1 . GLN A 248 ? 0.0823 0.2101 0.1841 -0.0274 -0.0113 -0.0359 249 GLN A OE1 
2064 N  NE2 . GLN A 248 ? 0.1250 0.1717 0.1559 -0.0089 -0.0055 -0.0152 249 GLN A NE2 
2065 N  N   . PRO A 249 ? 0.1099 0.1834 0.1399 0.0385  -0.0392 -0.0172 250 PRO A N   
2066 C  CA  . PRO A 249 ? 0.1286 0.2207 0.1385 0.0380  -0.0440 -0.0229 250 PRO A CA  
2067 C  C   . PRO A 249 ? 0.1363 0.1465 0.1155 0.0155  -0.0508 -0.0033 250 PRO A C   
2068 O  O   . PRO A 249 ? 0.1071 0.1611 0.1453 0.0280  -0.0466 0.0055  250 PRO A O   
2069 C  CB  . PRO A 249 ? 0.0966 0.2901 0.1859 0.0592  -0.0594 -0.0214 250 PRO A CB  
2070 C  CG  . PRO A 249 ? 0.1636 0.3287 0.1645 0.0174  -0.0634 -0.0414 250 PRO A CG  
2071 C  CD  . PRO A 249 ? 0.0664 0.3064 0.1916 0.0508  -0.0741 -0.0134 250 PRO A CD  
2072 N  N   . LEU A 250 ? 0.1724 0.1595 0.1129 0.0438  -0.0141 0.0089  251 LEU A N   
2073 C  CA  . LEU A 250 ? 0.1388 0.1394 0.1236 -0.0027 -0.0198 -0.0137 251 LEU A CA  
2074 C  C   . LEU A 250 ? 0.1430 0.1372 0.1227 0.0240  -0.0519 0.0173  251 LEU A C   
2075 O  O   . LEU A 250 ? 0.1273 0.1473 0.1430 0.0188  -0.0560 -0.0003 251 LEU A O   
2076 C  CB  . LEU A 250 ? 0.1794 0.1658 0.1518 -0.0021 -0.0133 0.0095  251 LEU A CB  
2077 C  CG  . LEU A 250 ? 0.1473 0.1970 0.1480 -0.0223 0.0172  -0.0145 251 LEU A CG  
2078 C  CD1 . LEU A 250 ? 0.1092 0.2103 0.1636 0.0019  -0.0188 -0.0336 251 LEU A CD1 
2079 C  CD2 . LEU A 250 ? 0.2734 0.1857 0.1907 -0.0328 0.0494  -0.0344 251 LEU A CD2 
2080 N  N   . LYS A 251 ? 0.1561 0.1841 0.1284 0.0484  -0.0560 -0.0022 252 LYS A N   
2081 C  CA  . LYS A 251 ? 0.1557 0.2035 0.1304 0.0493  -0.0637 -0.0150 252 LYS A CA  
2082 C  C   . LYS A 251 ? 0.1509 0.2026 0.1981 0.0035  -0.0713 -0.0227 252 LYS A C   
2083 O  O   . LYS A 251 ? 0.1961 0.2288 0.1747 -0.0003 -0.0223 -0.0272 252 LYS A O   
2084 C  CB  . LYS A 251 ? 0.2200 0.2132 0.1738 -0.0055 -0.0749 -0.0223 252 LYS A CB  
2085 C  CG  . LYS A 251 ? 0.1929 0.2532 0.2827 0.0260  -0.0171 -0.0114 252 LYS A CG  
2086 C  CD  . LYS A 251 ? 0.1658 0.2902 0.2827 0.0148  -0.0391 -0.0243 252 LYS A CD  
2087 C  CE  . LYS A 251 ? 0.1406 0.3648 0.5906 0.0644  0.0465  0.0292  252 LYS A CE  
2088 N  NZ  . LYS A 251 ? 0.1448 0.3747 0.5373 0.0165  -0.0289 0.0050  252 LYS A NZ  
2089 N  N   . ASN A 252 ? 0.1832 0.1949 0.1268 0.0211  -0.0634 -0.0273 253 ASN A N   
2090 C  CA  . ASN A 252 ? 0.1773 0.3772 0.1782 0.0447  -0.0700 -0.0988 253 ASN A CA  
2091 C  C   . ASN A 252 ? 0.2010 0.2649 0.2482 0.0989  -0.0516 -0.0598 253 ASN A C   
2092 O  O   . ASN A 252 ? 0.2272 0.2692 0.2354 0.0519  0.0010  -0.0354 253 ASN A O   
2093 C  CB  . ASN A 252 ? 0.2486 0.4863 0.2664 0.0216  -0.0935 -0.1606 253 ASN A CB  
2094 C  CG  . ASN A 252 ? 0.2207 0.4061 0.3317 -0.0111 -0.0197 -0.1110 253 ASN A CG  
2095 O  OD1 . ASN A 252 ? 0.4504 0.5349 0.2743 -0.1037 0.0126  0.0460  253 ASN A OD1 
2096 N  ND2 . ASN A 252 ? 0.5993 0.4753 0.5413 -0.1315 -0.1592 -0.2066 253 ASN A ND2 
2097 N  N   . ARG A 253 ? 0.1270 0.2860 0.1034 0.0326  -0.0256 0.0162  254 ARG A N   
2098 C  CA  . ARG A 253 ? 0.1196 0.1792 0.0968 0.0322  -0.0312 -0.0080 254 ARG A CA  
2099 C  C   . ARG A 253 ? 0.1593 0.1534 0.1385 0.0148  -0.0059 -0.0221 254 ARG A C   
2100 O  O   . ARG A 253 ? 0.2256 0.1979 0.2784 0.0765  0.0961  0.0637  254 ARG A O   
2101 C  CB  . ARG A 253 ? 0.1377 0.1607 0.0871 0.0255  -0.0153 -0.0135 254 ARG A CB  
2102 C  CG  . ARG A 253 ? 0.1494 0.1349 0.1108 0.0091  -0.0210 0.0006  254 ARG A CG  
2103 C  CD  . ARG A 253 ? 0.1243 0.1446 0.0914 0.0192  -0.0133 -0.0228 254 ARG A CD  
2104 N  NE  . ARG A 253 ? 0.1090 0.1282 0.1045 0.0206  -0.0237 -0.0094 254 ARG A NE  
2105 C  CZ  . ARG A 253 ? 0.0700 0.1160 0.0977 0.0048  -0.0110 -0.0060 254 ARG A CZ  
2106 N  NH1 . ARG A 253 ? 0.0564 0.1162 0.1065 0.0080  -0.0330 -0.0067 254 ARG A NH1 
2107 N  NH2 . ARG A 253 ? 0.0932 0.1218 0.0950 0.0166  -0.0363 -0.0157 254 ARG A NH2 
2108 N  N   . GLN A 254 ? 0.1255 0.1967 0.1178 0.0254  -0.0245 -0.0389 255 GLN A N   
2109 C  CA  . GLN A 254 ? 0.1505 0.2092 0.1174 0.0145  -0.0243 -0.0376 255 GLN A CA  
2110 C  C   . GLN A 254 ? 0.1322 0.1699 0.1374 0.0052  -0.0289 -0.0095 255 GLN A C   
2111 O  O   . GLN A 254 ? 0.2191 0.1422 0.2004 -0.0044 -0.0704 -0.0060 255 GLN A O   
2112 C  CB  . GLN A 254 ? 0.2069 0.2498 0.1162 0.0098  -0.0195 -0.0356 255 GLN A CB  
2113 C  CG  . GLN A 254 ? 0.3191 0.3425 0.2763 -0.0011 0.0164  -0.0226 255 GLN A CG  
2114 C  CD  . GLN A 254 ? 0.3929 0.4935 0.3407 -0.0684 -0.0446 0.0413  255 GLN A CD  
2115 O  OE1 . GLN A 254 ? 0.4590 0.3880 0.3435 0.0336  0.0232  -0.0255 255 GLN A OE1 
2116 N  NE2 . GLN A 254 ? 0.5287 0.5653 0.3304 0.0955  0.0187  0.1243  255 GLN A NE2 
2117 N  N   . ILE A 255 ? 0.1311 0.1428 0.0995 0.0116  -0.0196 -0.0001 256 ILE A N   
2118 C  CA  . ILE A 255 ? 0.1049 0.1419 0.1000 0.0184  -0.0159 -0.0067 256 ILE A CA  
2119 C  C   . ILE A 255 ? 0.1340 0.1401 0.0858 0.0155  0.0100  0.0201  256 ILE A C   
2120 O  O   . ILE A 255 ? 0.1530 0.1548 0.1178 0.0359  0.0142  0.0287  256 ILE A O   
2121 C  CB  . ILE A 255 ? 0.1318 0.1286 0.1056 0.0140  -0.0053 -0.0057 256 ILE A CB  
2122 C  CG1 . ILE A 255 ? 0.1219 0.1483 0.1374 0.0172  0.0058  -0.0106 256 ILE A CG1 
2123 C  CG2 . ILE A 255 ? 0.1158 0.1652 0.1117 -0.0001 -0.0104 -0.0047 256 ILE A CG2 
2124 C  CD1 . ILE A 255 ? 0.1562 0.1546 0.1467 0.0081  0.0226  -0.0236 256 ILE A CD1 
2125 N  N   . LYS A 256 ? 0.1099 0.1377 0.0722 0.0159  -0.0047 0.0068  257 LYS A N   
2126 C  CA  . LYS A 256 ? 0.1011 0.1514 0.0868 -0.0032 0.0184  0.0111  257 LYS A CA  
2127 C  C   . LYS A 256 ? 0.1173 0.1379 0.0791 -0.0002 0.0044  0.0097  257 LYS A C   
2128 O  O   . LYS A 256 ? 0.1487 0.1941 0.0723 -0.0554 0.0140  0.0052  257 LYS A O   
2129 C  CB  . LYS A 256 ? 0.1329 0.1469 0.1252 -0.0013 0.0227  -0.0170 257 LYS A CB  
2130 C  CG  . LYS A 256 ? 0.2283 0.1990 0.1663 -0.0302 0.0163  -0.0412 257 LYS A CG  
2131 C  CD  . LYS A 256 ? 0.3091 0.2403 0.2444 0.0121  0.0164  -0.0637 257 LYS A CD  
2132 C  CE  . LYS A 256 ? 0.4322 0.3480 0.3203 -0.1380 -0.0335 -0.1575 257 LYS A CE  
2133 N  NZ  . LYS A 256 ? 0.3338 0.3283 0.3750 0.0037  -0.0565 -0.0913 257 LYS A NZ  
2134 N  N   . ALA A 257 ? 0.1027 0.1686 0.0932 -0.0077 0.0186  0.0120  258 ALA A N   
2135 C  CA  . ALA A 257 ? 0.0842 0.1613 0.1232 -0.0019 -0.0047 0.0106  258 ALA A CA  
2136 C  C   . ALA A 257 ? 0.0923 0.1771 0.0990 -0.0170 0.0270  0.0016  258 ALA A C   
2137 O  O   . ALA A 257 ? 0.1358 0.1904 0.1002 0.0089  0.0274  0.0027  258 ALA A O   
2138 C  CB  . ALA A 257 ? 0.1681 0.1685 0.1453 -0.0140 0.0286  0.0168  258 ALA A CB  
2139 N  N   . SER A 258 ? 0.0934 0.1613 0.1135 -0.0054 0.0089  0.0069  259 SER A N   
2140 C  CA  . SER A 258 ? 0.0992 0.1855 0.1476 0.0076  0.0253  -0.0025 259 SER A CA  
2141 C  C   . SER A 258 ? 0.0908 0.1993 0.1546 -0.0258 0.0280  -0.0099 259 SER A C   
2142 O  O   . SER A 258 ? 0.1126 0.2933 0.1902 0.0160  0.0409  0.0124  259 SER A O   
2143 C  CB  . SER A 258 ? 0.1422 0.1771 0.1446 -0.0133 -0.0089 -0.0006 259 SER A CB  
2144 O  OG  . SER A 258 ? 0.0948 0.1891 0.1225 -0.0048 0.0233  0.0010  259 SER A OG  
2145 N  N   . PHE A 259 ? 0.1437 0.1934 0.1530 -0.0402 0.0581  -0.0024 260 PHE A N   
2146 C  CA  . PHE A 259 ? 0.1764 0.2108 0.1871 -0.0460 0.0554  0.0402  260 PHE A CA  
2147 C  C   . PHE A 259 ? 0.2058 0.2655 0.1821 -0.0336 0.0668  0.0287  260 PHE A C   
2148 O  O   . PHE A 259 ? 0.2624 0.2200 0.2150 -0.0510 0.0079  0.0783  260 PHE A O   
2149 C  CB  . PHE A 259 ? 0.1401 0.2412 0.2268 -0.0505 0.0335  -0.0310 260 PHE A CB  
2150 C  CG  . PHE A 259 ? 0.1383 0.2074 0.1992 -0.0417 0.0064  0.0198  260 PHE A CG  
2151 C  CD1 . PHE A 259 ? 0.1403 0.1893 0.1376 -0.0438 -0.0131 0.0031  260 PHE A CD1 
2152 C  CD2 . PHE A 259 ? 0.2268 0.2196 0.2507 -0.0289 0.0339  0.0502  260 PHE A CD2 
2153 C  CE1 . PHE A 259 ? 0.1647 0.1902 0.2098 -0.0245 0.0107  -0.0201 260 PHE A CE1 
2154 C  CE2 . PHE A 259 ? 0.1945 0.2169 0.2828 -0.0326 -0.0111 0.0586  260 PHE A CE2 
2155 C  CZ  . PHE A 259 ? 0.1970 0.2074 0.3073 -0.0303 0.0105  -0.0189 260 PHE A CZ  
2156 N  N   . LYS A 260 ? 0.4218 0.4001 0.2503 -0.1714 0.0981  0.0973  261 LYS A N   
2157 C  CA  . LYS A 260 ? 0.5798 0.5853 0.2597 -0.1041 -0.1638 0.0993  261 LYS A CA  
2158 C  CB  . LYS A 260 ? 0.8557 0.5416 0.6347 -0.1648 0.1662  0.1271  261 LYS A CB  
2159 ZN ZN  . ZN  B .   ? 0.0746 0.0846 0.0717 -0.0122 0.0017  -0.0058 301 ZN  A ZN  
2160 S  S   . DMS C .   ? 0.1821 0.2297 0.2565 -0.0155 0.0412  -0.0350 302 DMS A S   
2161 O  O   . DMS C .   ? 0.1914 0.3080 0.5497 -0.0184 0.0622  -0.0175 302 DMS A O   
2162 C  C1  . DMS C .   ? 0.2449 0.1895 0.2385 0.0121  0.0541  -0.0683 302 DMS A C1  
2163 C  C2  . DMS C .   ? 0.1577 0.2453 0.2342 0.0464  -0.0070 -0.0694 302 DMS A C2  
2164 N  N1  . BCN D .   ? 0.3312 0.3809 0.3741 -0.0116 -0.0306 -0.0696 303 BCN A N1  
2165 C  C1  . BCN D .   ? 0.2205 0.5087 0.2632 -0.1775 -0.0128 0.0724  303 BCN A C1  
2166 C  C2  . BCN D .   ? 0.2417 0.4860 0.3519 -0.1336 0.0511  0.1165  303 BCN A C2  
2167 O  O21 . BCN D .   ? 0.4051 0.3697 0.4422 -0.1145 0.0635  0.1235  303 BCN A O21 
2168 O  O22 . BCN D .   ? 0.3587 0.3596 0.3987 -0.1101 -0.0346 0.0601  303 BCN A O22 
2169 C  C3  . BCN D .   ? 0.2541 0.1993 0.2908 -0.0425 0.0330  0.0593  303 BCN A C3  
2170 C  C4  . BCN D .   ? 0.6251 0.5172 0.3615 -0.0145 0.1010  -0.1483 303 BCN A C4  
2171 O  O4  . BCN D .   ? 0.3222 0.3285 0.4020 -0.1219 0.0815  -0.0307 303 BCN A O4  
2172 C  C5  . BCN D .   ? 0.1934 0.1871 0.2477 -0.0066 0.0366  0.0361  303 BCN A C5  
2173 C  C6  . BCN D .   ? 0.6167 0.3345 0.4723 -0.0259 -0.1303 -0.0443 303 BCN A C6  
2174 O  O6  . BCN D .   ? 0.5497 0.3996 0.5283 -0.2027 -0.0273 0.1596  303 BCN A O6  
2175 C  C5  . ENN E .   ? 0.0869 0.1203 0.0923 -0.0276 -0.0002 -0.0055 304 ENN A C5  
2176 C  C4  . ENN E .   ? 0.1322 0.1166 0.1124 -0.0228 0.0199  0.0089  304 ENN A C4  
2177 C  C6  . ENN E .   ? 0.0685 0.1090 0.1036 -0.0232 0.0044  -0.0118 304 ENN A C6  
2178 C  C2  . ENN E .   ? 0.1336 0.1133 0.1198 -0.0257 0.0203  0.0009  304 ENN A C2  
2179 O  O14 . ENN E .   ? 0.1704 0.2119 0.1512 0.0126  0.0356  0.0171  304 ENN A O14 
2180 C  C13 . ENN E .   ? 0.1631 0.1762 0.1200 -0.0216 0.0398  0.0222  304 ENN A C13 
2181 N  N15 . ENN E .   ? 0.2037 0.2092 0.1298 0.0337  0.0539  -0.0026 304 ENN A N15 
2182 C  C16 . ENN E .   ? 0.2737 0.3368 0.1893 0.0630  0.1401  0.0623  304 ENN A C16 
2183 C  C17 . ENN E .   ? 0.2839 0.4326 0.2028 0.0756  0.1298  0.0409  304 ENN A C17 
2184 C  C18 . ENN E .   ? 0.5585 0.5078 0.7553 0.1381  0.0772  -0.0869 304 ENN A C18 
2185 C  C19 . ENN E .   ? 0.6123 0.6878 0.5259 0.0355  0.1576  -0.2131 304 ENN A C19 
2186 C  C3  . ENN E .   ? 0.1212 0.1291 0.1424 -0.0237 0.0317  0.0108  304 ENN A C3  
2187 CL CL1 . ENN E .   ? 0.4770 0.3301 0.3474 -0.0769 0.0531  0.0491  304 ENN A CL1 
2188 C  C1  . ENN E .   ? 0.1097 0.1043 0.1077 -0.0253 0.0134  -0.0079 304 ENN A C1  
2189 CL CL2 . ENN E .   ? 0.0984 0.1010 0.1318 -0.0069 0.0158  -0.0219 304 ENN A CL2 
2190 S  S7  . ENN E .   ? 0.0642 0.0878 0.0859 -0.0126 -0.0012 -0.0116 304 ENN A S7  
2191 O  O9  . ENN E .   ? 0.0534 0.1038 0.0913 -0.0015 -0.0032 -0.0184 304 ENN A O9  
2192 O  O10 . ENN E .   ? 0.0605 0.0901 0.0896 -0.0113 -0.0058 -0.0082 304 ENN A O10 
2193 N  N8  . ENN E .   ? 0.0612 0.0877 0.0878 -0.0126 -0.0043 -0.0182 304 ENN A N8  
2194 O  O   . HOH F .   ? 0.2306 0.2647 0.4150 -0.0273 -0.1127 0.0029  401 HOH A O   
2195 O  O   . HOH F .   ? 0.2814 0.2162 0.3042 0.0167  0.0413  0.0894  402 HOH A O   
2196 O  O   . HOH F .   ? 0.2954 0.3177 0.4272 -0.0334 -0.0322 0.0873  403 HOH A O   
2197 O  O   . HOH F .   ? 0.1785 0.1780 0.1967 -0.0122 -0.0228 0.0205  404 HOH A O   
2198 O  O   . HOH F .   ? 0.5137 0.1306 0.1722 0.0284  -0.1570 0.0061  405 HOH A O   
2199 O  O   . HOH F .   ? 0.2734 0.1866 0.3555 -0.0266 -0.0365 -0.0089 406 HOH A O   
2200 O  O   . HOH F .   ? 0.5357 0.5001 0.3511 -0.0719 0.0073  0.0666  407 HOH A O   
2201 O  O   . HOH F .   ? 0.2956 0.5452 0.2573 -0.0041 -0.0001 0.0603  408 HOH A O   
2202 O  O   . HOH F .   ? 0.5233 0.3281 0.5230 0.0409  -0.3319 -0.1597 409 HOH A O   
2203 O  O   . HOH F .   ? 0.4215 0.2549 0.2187 0.0489  0.0337  0.0391  410 HOH A O   
2204 O  O   . HOH F .   ? 0.5085 0.5622 0.4037 -0.0016 -0.1119 -0.1202 411 HOH A O   
2205 O  O   . HOH F .   ? 0.5728 0.5511 0.3573 0.0634  0.0303  -0.0318 412 HOH A O   
2206 O  O   . HOH F .   ? 0.4111 0.2991 0.5251 -0.0725 -0.0948 0.0707  413 HOH A O   
2207 O  O   . HOH F .   ? 0.2621 0.1313 0.1970 -0.0096 -0.0144 -0.0049 414 HOH A O   
2208 O  O   . HOH F .   ? 0.2399 0.9064 0.3661 0.0358  0.0396  0.0627  415 HOH A O   
2209 O  O   . HOH F .   ? 0.5643 0.3249 0.4713 0.0597  0.1582  -0.0433 416 HOH A O   
2210 O  O   . HOH F .   ? 0.3978 0.4374 0.2857 -0.1693 0.1735  -0.1349 417 HOH A O   
2211 O  O   . HOH F .   ? 0.3291 0.4130 0.3658 -0.0569 0.0596  -0.0036 418 HOH A O   
2212 O  O   . HOH F .   ? 0.3495 0.4210 0.5705 -0.0441 0.2314  0.0291  419 HOH A O   
2213 O  O   . HOH F .   ? 0.4070 0.4233 0.3825 0.0093  0.0424  -0.0333 420 HOH A O   
2214 O  O   . HOH F .   ? 1.0226 0.4077 0.2962 0.1164  -0.0683 -0.0078 421 HOH A O   
2215 O  O   . HOH F .   ? 0.3934 0.3228 0.4467 -0.0724 0.1594  0.0406  422 HOH A O   
2216 O  O   . HOH F .   ? 0.4679 0.2930 0.4450 0.1685  -0.0079 -0.0615 423 HOH A O   
2217 O  O   . HOH F .   ? 0.1981 0.8734 0.4221 0.0130  -0.0387 -0.2176 424 HOH A O   
2218 O  O   . HOH F .   ? 1.5362 1.9689 0.4237 0.9975  -0.6027 -0.6246 425 HOH A O   
2219 O  O   . HOH F .   ? 0.2958 0.2299 0.4441 -0.0011 -0.0588 0.0110  426 HOH A O   
2220 O  O   . HOH F .   ? 0.4334 0.3116 0.6617 -0.0968 0.1239  0.1010  427 HOH A O   
2221 O  O   . HOH F .   ? 0.2646 0.3356 0.4731 -0.0951 -0.0714 0.1140  428 HOH A O   
2222 O  O   . HOH F .   ? 0.5222 0.3124 0.2963 -0.0712 0.1074  -0.1021 429 HOH A O   
2223 O  O   . HOH F .   ? 0.4285 0.2931 0.6506 -0.1031 0.0596  -0.0765 430 HOH A O   
2224 O  O   . HOH F .   ? 0.2042 0.7277 0.2448 0.0935  -0.0038 -0.0323 431 HOH A O   
2225 O  O   . HOH F .   ? 0.0993 0.1176 0.1247 -0.0145 0.0222  -0.0245 432 HOH A O   
2226 O  O   . HOH F .   ? 0.5030 0.3550 0.3209 -0.1010 0.0798  -0.0113 433 HOH A O   
2227 O  O   . HOH F .   ? 0.6545 0.2556 0.1315 -0.0454 0.0293  -0.0004 434 HOH A O   
2228 O  O   . HOH F .   ? 0.3134 0.2561 0.3407 -0.0450 0.0927  -0.0863 435 HOH A O   
2229 O  O   . HOH F .   ? 0.1695 0.1126 0.0713 -0.0275 0.0065  -0.0010 436 HOH A O   
2230 O  O   . HOH F .   ? 0.5360 0.2491 0.2667 -0.0403 -0.0199 -0.0662 437 HOH A O   
2231 O  O   . HOH F .   ? 0.2782 0.2132 0.2130 -0.0917 -0.0471 -0.0009 438 HOH A O   
2232 O  O   . HOH F .   ? 0.2051 0.2008 0.2974 0.0168  -0.1426 -0.0609 439 HOH A O   
2233 O  O   . HOH F .   ? 0.9305 0.3331 0.5774 -0.0899 0.1550  0.0399  440 HOH A O   
2234 O  O   . HOH F .   ? 0.9507 0.2967 0.4719 -0.0923 0.0211  -0.0440 441 HOH A O   
2235 O  O   . HOH F .   ? 0.3545 0.4164 0.4716 -0.0256 0.0554  0.0006  442 HOH A O   
2236 O  O   . HOH F .   ? 0.2653 0.2990 0.1961 -0.0719 0.0784  0.0084  443 HOH A O   
2237 O  O   . HOH F .   ? 0.3480 0.2124 0.1460 -0.0627 0.0806  0.0049  444 HOH A O   
2238 O  O   . HOH F .   ? 0.1821 0.2209 0.1801 0.0146  -0.0430 0.0023  445 HOH A O   
2239 O  O   . HOH F .   ? 0.4401 0.2527 0.1922 0.0100  0.0805  0.0561  446 HOH A O   
2240 O  O   . HOH F .   ? 0.4383 0.2771 0.3892 -0.0156 -0.1115 0.0610  447 HOH A O   
2241 O  O   . HOH F .   ? 0.1500 0.3188 0.3881 0.0214  0.0190  -0.0113 448 HOH A O   
2242 O  O   . HOH F .   ? 0.2191 0.5622 0.4382 0.0416  0.0806  -0.0384 449 HOH A O   
2243 O  O   . HOH F .   ? 0.2965 0.3538 0.3105 -0.1184 0.1388  -0.1538 450 HOH A O   
2244 O  O   . HOH F .   ? 0.1586 0.2861 0.2678 0.0203  -0.0019 0.0221  451 HOH A O   
2245 O  O   . HOH F .   ? 0.5310 0.5752 0.2107 0.0218  0.0967  -0.0951 452 HOH A O   
2246 O  O   . HOH F .   ? 0.6241 0.3546 0.2067 -0.2078 0.0906  -0.0882 453 HOH A O   
2247 O  O   . HOH F .   ? 0.3005 0.2645 0.2026 0.0271  0.0277  0.0023  454 HOH A O   
2248 O  O   . HOH F .   ? 0.1104 0.1137 0.1056 -0.0067 0.0020  -0.0128 455 HOH A O   
2249 O  O   . HOH F .   ? 0.4242 0.4341 0.3662 0.0436  -0.0317 0.0666  456 HOH A O   
2250 O  O   . HOH F .   ? 0.2065 0.6154 0.3050 -0.0756 -0.0192 -0.0403 457 HOH A O   
2251 O  O   . HOH F .   ? 0.5292 0.8305 0.1706 -0.0347 0.0133  0.0820  458 HOH A O   
2252 O  O   . HOH F .   ? 0.3134 0.3120 0.6308 -0.1128 -0.1376 0.0168  459 HOH A O   
2253 O  O   . HOH F .   ? 0.5600 0.3793 0.3094 -0.0130 -0.0436 -0.0329 460 HOH A O   
2254 O  O   . HOH F .   ? 0.1934 0.2225 0.2426 -0.0201 -0.0082 0.0205  461 HOH A O   
2255 O  O   . HOH F .   ? 0.2588 0.2973 0.3050 0.0143  -0.0810 -0.1570 462 HOH A O   
2256 O  O   . HOH F .   ? 0.3571 0.4003 0.3738 -0.0663 0.0286  -0.0177 463 HOH A O   
2257 O  O   . HOH F .   ? 0.1873 0.2074 0.2254 0.0139  0.0150  0.0475  464 HOH A O   
2258 O  O   . HOH F .   ? 0.4186 0.2182 0.1900 -0.0765 -0.0319 0.0535  465 HOH A O   
2259 O  O   . HOH F .   ? 0.3410 0.2168 0.3662 -0.0385 0.0457  -0.0293 466 HOH A O   
2260 O  O   . HOH F .   ? 0.1776 0.2142 0.2583 0.0140  0.0099  -0.0317 467 HOH A O   
2261 O  O   . HOH F .   ? 0.1242 1.4031 1.5391 -0.0094 -0.1285 0.7533  468 HOH A O   
2262 O  O   . HOH F .   ? 0.1221 0.1207 0.1205 -0.0094 0.0178  -0.0122 469 HOH A O   
2263 O  O   . HOH F .   ? 0.5960 0.2890 0.1322 -0.0054 -0.0582 0.0027  470 HOH A O   
2264 O  O   . HOH F .   ? 0.3203 0.2444 0.1552 -0.0245 -0.0716 0.0177  471 HOH A O   
2265 O  O   . HOH F .   ? 0.2361 0.3762 0.3419 0.0193  -0.1232 -0.0659 472 HOH A O   
2266 O  O   . HOH F .   ? 0.3106 0.2638 0.3398 0.0292  -0.0840 0.0871  473 HOH A O   
2267 O  O   . HOH F .   ? 0.1997 0.4633 0.3773 -0.0366 0.0856  0.0083  474 HOH A O   
2268 O  O   . HOH F .   ? 0.3820 0.4381 0.4000 -0.0065 -0.0823 -0.2180 475 HOH A O   
2269 O  O   . HOH F .   ? 0.4618 0.2751 0.2605 -0.0815 -0.1731 -0.0196 476 HOH A O   
2270 O  O   . HOH F .   ? 0.9130 1.6874 2.8611 -0.8071 0.7522  -1.1740 477 HOH A O   
2271 O  O   . HOH F .   ? 0.8129 0.8032 0.3142 0.0401  0.0193  -0.0796 478 HOH A O   
2272 O  O   . HOH F .   ? 0.1805 0.2584 0.3004 -0.0047 0.0639  0.0797  479 HOH A O   
2273 O  O   . HOH F .   ? 0.4008 0.3177 0.5874 -0.0924 -0.0801 -0.0434 480 HOH A O   
2274 O  O   . HOH F .   ? 0.1516 0.3347 0.3910 0.0759  0.0168  0.0317  481 HOH A O   
2275 O  O   . HOH F .   ? 0.7207 0.5793 0.4113 0.2256  -0.0708 0.0100  482 HOH A O   
2276 O  O   . HOH F .   ? 0.2013 0.3867 0.2236 0.0601  0.0513  -0.0178 483 HOH A O   
2277 O  O   . HOH F .   ? 0.0961 0.1791 0.1873 0.0228  -0.0142 0.0116  484 HOH A O   
2278 O  O   . HOH F .   ? 0.0961 0.1126 0.1165 0.0084  -0.0083 -0.0105 485 HOH A O   
2279 O  O   . HOH F .   ? 0.3686 0.4760 0.3279 -0.0416 -0.0817 -0.0452 486 HOH A O   
2280 O  O   . HOH F .   ? 0.5583 1.2634 0.7452 0.0693  0.1206  -0.0516 487 HOH A O   
2281 O  O   . HOH F .   ? 0.0988 0.1588 0.1356 0.0020  -0.0392 0.0168  488 HOH A O   
2282 O  O   . HOH F .   ? 0.1415 0.1412 0.1518 -0.0006 0.0068  0.0013  489 HOH A O   
2283 O  O   . HOH F .   ? 0.1121 0.3265 0.2797 0.0290  -0.0244 0.0903  490 HOH A O   
2284 O  O   . HOH F .   ? 0.2979 0.5616 0.2234 -0.0573 -0.1011 0.1228  491 HOH A O   
2285 O  O   . HOH F .   ? 0.2026 0.2509 0.1880 -0.0022 0.0761  -0.0525 492 HOH A O   
2286 O  O   . HOH F .   ? 0.0825 0.1370 0.1169 0.0256  -0.0098 -0.0052 493 HOH A O   
2287 O  O   . HOH F .   ? 0.3477 0.6366 0.6249 -0.0943 0.0588  0.0229  494 HOH A O   
2288 O  O   . HOH F .   ? 0.3305 0.2951 0.3823 0.0064  0.2070  0.0146  495 HOH A O   
2289 O  O   . HOH F .   ? 0.2446 0.2785 0.3162 -0.0061 -0.0427 0.1370  496 HOH A O   
2290 O  O   . HOH F .   ? 0.3371 0.2954 0.4706 -0.1676 0.0188  0.0693  497 HOH A O   
2291 O  O   . HOH F .   ? 0.2480 0.3058 0.2295 -0.0148 0.0359  -0.0167 498 HOH A O   
2292 O  O   . HOH F .   ? 0.0743 0.1168 0.0966 -0.0062 0.0130  0.0005  499 HOH A O   
2293 O  O   . HOH F .   ? 0.3756 0.3888 0.3360 0.1030  0.0044  -0.0342 500 HOH A O   
2294 O  O   . HOH F .   ? 0.7942 0.4562 0.4733 0.2312  0.1810  0.0388  501 HOH A O   
2295 O  O   . HOH F .   ? 0.3208 0.4807 0.6103 -0.0847 0.1253  -0.0584 502 HOH A O   
2296 O  O   . HOH F .   ? 0.3491 0.3726 0.3675 0.0525  0.0394  -0.0240 503 HOH A O   
2297 O  O   . HOH F .   ? 0.5130 0.3331 0.2859 0.0230  -0.0229 0.1016  504 HOH A O   
2298 O  O   . HOH F .   ? 0.3018 0.4592 0.3398 0.0531  0.1502  -0.0392 505 HOH A O   
2299 O  O   . HOH F .   ? 0.1857 0.2455 0.1650 0.0071  -0.0452 0.0156  506 HOH A O   
2300 O  O   . HOH F .   ? 0.2324 0.2937 0.1773 -0.0446 -0.0182 -0.0719 507 HOH A O   
2301 O  O   . HOH F .   ? 0.1679 0.1762 0.2508 0.0166  0.0073  -0.0218 508 HOH A O   
2302 O  O   . HOH F .   ? 0.0604 0.1694 0.2065 -0.0065 -0.0069 -0.0403 509 HOH A O   
2303 O  O   . HOH F .   ? 0.6082 0.1913 0.9501 -0.1712 -0.2269 0.0840  510 HOH A O   
2304 O  O   . HOH F .   ? 1.3013 0.7378 0.3914 0.0290  -0.3261 0.0065  511 HOH A O   
2305 O  O   . HOH F .   ? 0.3333 0.2759 0.1909 -0.1011 0.1151  -0.0670 512 HOH A O   
2306 O  O   . HOH F .   ? 0.3115 0.2044 0.3641 0.0807  -0.0933 -0.0083 513 HOH A O   
2307 O  O   . HOH F .   ? 0.1771 0.1455 0.1636 -0.0333 -0.0292 -0.0019 514 HOH A O   
2308 O  O   . HOH F .   ? 0.4145 0.4427 0.4620 -0.0403 -0.0113 -0.0059 515 HOH A O   
2309 O  O   . HOH F .   ? 0.2063 0.2089 0.3034 -0.0467 0.0570  -0.0431 516 HOH A O   
2310 O  O   . HOH F .   ? 0.4075 0.2453 0.1913 -0.0793 0.1140  -0.1030 517 HOH A O   
2311 O  O   . HOH F .   ? 0.3856 0.2787 0.3802 0.0131  0.0096  0.0367  518 HOH A O   
2312 O  O   . HOH F .   ? 0.1038 0.1582 0.2934 -0.0157 0.0013  0.0143  519 HOH A O   
2313 O  O   . HOH F .   ? 0.5833 0.6743 0.3092 -0.0538 0.0367  -0.0739 520 HOH A O   
2314 O  O   . HOH F .   ? 0.2450 0.1895 0.1816 -0.0027 -0.0495 0.0008  521 HOH A O   
2315 O  O   . HOH F .   ? 0.4301 0.4075 0.2106 -0.0280 -0.0665 -0.0690 522 HOH A O   
2316 O  O   . HOH F .   ? 0.1753 0.5781 0.4543 -0.0853 -0.1101 -0.1026 523 HOH A O   
2317 O  O   . HOH F .   ? 0.3776 0.2860 0.2549 -0.0207 0.0425  -0.0288 524 HOH A O   
2318 O  O   . HOH F .   ? 0.8415 0.2353 0.1527 -0.0325 0.0476  0.0004  525 HOH A O   
2319 O  O   . HOH F .   ? 0.3015 0.2081 0.2333 -0.0488 0.0139  -0.0125 526 HOH A O   
2320 O  O   . HOH F .   ? 0.4327 0.4361 0.4396 -0.0435 -0.0584 -0.0075 527 HOH A O   
2321 O  O   . HOH F .   ? 0.4075 0.3845 0.8827 0.0485  0.1451  0.1002  528 HOH A O   
2322 O  O   . HOH F .   ? 0.3025 0.5090 0.1462 0.1260  -0.0938 -0.0422 529 HOH A O   
2323 O  O   . HOH F .   ? 0.0833 0.3222 0.3818 -0.0192 -0.0088 0.0619  530 HOH A O   
2324 O  O   . HOH F .   ? 0.1060 0.1329 0.1491 0.0175  -0.0240 0.0122  531 HOH A O   
2325 O  O   . HOH F .   ? 0.3230 0.4996 0.6630 -0.1609 0.1183  0.1238  532 HOH A O   
2326 O  O   . HOH F .   ? 0.2390 0.2218 0.3493 -0.0111 0.0077  -0.0479 533 HOH A O   
2327 O  O   . HOH F .   ? 0.2801 0.1295 0.1717 0.0063  -0.0817 0.0019  534 HOH A O   
2328 O  O   . HOH F .   ? 0.2363 0.5290 0.3527 -0.0565 0.0039  -0.0845 535 HOH A O   
2329 O  O   . HOH F .   ? 0.4102 0.1672 0.1738 0.0103  -0.1322 0.0111  536 HOH A O   
2330 O  O   . HOH F .   ? 0.4867 0.4014 0.6359 0.1342  0.1621  -0.1018 537 HOH A O   
2331 O  O   . HOH F .   ? 0.2951 0.2168 0.2861 -0.0055 -0.0873 -0.0075 538 HOH A O   
2332 O  O   . HOH F .   ? 0.1983 0.1850 0.1929 -0.0064 -0.0332 -0.0233 539 HOH A O   
2333 O  O   . HOH F .   ? 0.3166 0.3714 0.2065 0.0328  0.0763  0.1010  540 HOH A O   
2334 O  O   . HOH F .   ? 0.3984 0.3375 0.4511 -0.1753 -0.0100 -0.0598 541 HOH A O   
2335 O  O   . HOH F .   ? 0.2214 0.1636 0.1798 -0.0076 0.0179  0.0111  542 HOH A O   
2336 O  O   . HOH F .   ? 0.1232 0.1782 0.3102 -0.0377 -0.0600 0.0080  543 HOH A O   
2337 O  O   . HOH F .   ? 0.4979 0.2284 0.1731 0.0413  0.0735  0.0350  544 HOH A O   
2338 O  O   . HOH F .   ? 0.3121 0.6383 0.4214 -0.0697 0.0510  0.2517  545 HOH A O   
2339 O  O   . HOH F .   ? 0.4049 0.2417 0.8983 0.0540  -0.0724 0.0697  546 HOH A O   
2340 O  O   . HOH F .   ? 0.2103 0.1753 0.1609 0.0102  -0.0638 0.0051  547 HOH A O   
2341 O  O   . HOH F .   ? 0.3051 0.1898 0.2148 0.0479  -0.1055 -0.0131 548 HOH A O   
2342 O  O   . HOH F .   ? 0.4064 0.2517 0.2816 0.0421  0.1865  -0.0326 549 HOH A O   
2343 O  O   . HOH F .   ? 0.1537 0.3278 0.1656 -0.0029 0.0113  -0.0147 550 HOH A O   
2344 O  O   . HOH F .   ? 0.2182 0.2423 0.1864 0.0330  0.0003  0.0289  551 HOH A O   
2345 O  O   . HOH F .   ? 0.1634 0.1744 0.1483 -0.0121 -0.0151 0.0119  552 HOH A O   
2346 O  O   . HOH F .   ? 0.1327 0.1394 0.1846 0.0229  -0.0039 0.0072  553 HOH A O   
2347 O  O   . HOH F .   ? 0.0564 0.2067 0.2496 0.0146  0.0157  -0.0476 554 HOH A O   
2348 O  O   . HOH F .   ? 0.2053 0.3731 0.3230 -0.0236 -0.0438 0.0348  555 HOH A O   
2349 O  O   . HOH F .   ? 0.2196 0.1900 0.2139 0.0244  0.0277  0.0941  556 HOH A O   
2350 O  O   . HOH F .   ? 0.2308 0.2979 0.3775 0.0157  0.0807  -0.0386 557 HOH A O   
2351 O  O   . HOH F .   ? 0.1817 0.1401 0.1428 0.0247  -0.0230 0.0032  558 HOH A O   
2352 O  O   . HOH F .   ? 0.2685 0.5874 0.3199 -0.0560 -0.0728 0.1706  559 HOH A O   
2353 O  O   . HOH F .   ? 0.2749 0.5245 0.4939 -0.3342 0.0642  -0.0647 560 HOH A O   
2354 O  O   . HOH F .   ? 0.1264 0.1719 0.1922 -0.0051 0.0252  -0.0036 561 HOH A O   
2355 O  O   . HOH F .   ? 0.2259 0.2283 0.4946 0.0067  -0.0165 -0.1117 562 HOH A O   
2356 O  O   . HOH F .   ? 0.2460 0.2363 0.1471 0.0392  -0.0396 -0.0209 563 HOH A O   
2357 O  O   . HOH F .   ? 0.6343 0.3586 0.4742 0.0509  -0.1675 -0.1341 564 HOH A O   
2358 O  O   . HOH F .   ? 0.2910 0.6891 0.6109 0.1032  -0.0899 -0.2493 565 HOH A O   
2359 O  O   . HOH F .   ? 0.2426 0.3164 0.3687 0.0831  0.0639  0.0446  566 HOH A O   
2360 O  O   . HOH F .   ? 0.3714 0.2973 0.3930 0.0583  -0.0514 0.0069  567 HOH A O   
2361 O  O   . HOH F .   ? 0.3414 0.2317 0.4034 -0.0305 0.0020  0.1338  568 HOH A O   
2362 O  O   . HOH F .   ? 0.2092 0.1706 0.6742 0.0032  0.0994  -0.0650 569 HOH A O   
2363 O  O   . HOH F .   ? 0.1958 0.2903 0.2911 0.0135  -0.0057 0.0215  570 HOH A O   
2364 O  O   . HOH F .   ? 0.2482 0.4181 0.3131 -0.0601 -0.1130 0.0580  571 HOH A O   
2365 O  O   . HOH F .   ? 0.6327 0.3301 0.2150 -0.1412 0.0524  -0.1004 572 HOH A O   
2366 O  O   . HOH F .   ? 0.3238 0.4842 0.5578 0.1193  0.0970  0.0721  573 HOH A O   
2367 O  O   . HOH F .   ? 0.0950 0.3649 0.3921 0.0299  -0.0323 0.1081  574 HOH A O   
2368 O  O   . HOH F .   ? 0.4023 0.3702 0.3658 0.0662  0.1305  0.0744  575 HOH A O   
2369 O  O   . HOH F .   ? 0.2552 0.2800 0.6455 -0.1003 0.0301  0.0251  576 HOH A O   
2370 O  O   . HOH F .   ? 0.3254 0.1889 0.2539 0.0626  0.0238  0.0234  577 HOH A O   
2371 O  O   . HOH F .   ? 0.2771 0.1821 0.2833 0.0159  -0.0493 -0.0352 578 HOH A O   
2372 O  O   . HOH F .   ? 0.3774 0.3480 0.2097 0.2127  -0.0212 0.0544  579 HOH A O   
2373 O  O   . HOH F .   ? 0.1905 0.3121 0.2257 -0.0165 -0.0567 -0.0166 580 HOH A O   
2374 O  O   . HOH F .   ? 0.0992 0.2284 0.1625 -0.0201 -0.0466 0.0353  581 HOH A O   
2375 O  O   . HOH F .   ? 0.1399 0.2329 0.2437 -0.0034 0.0186  -0.0184 582 HOH A O   
2376 O  O   . HOH F .   ? 0.2633 0.2748 0.1958 0.0189  0.0296  -0.0205 583 HOH A O   
2377 O  O   . HOH F .   ? 0.1963 0.1843 0.2772 -0.0917 -0.0494 -0.0445 584 HOH A O   
2378 O  O   . HOH F .   ? 0.0917 0.1897 0.3109 -0.0089 -0.0136 -0.0041 585 HOH A O   
2379 O  O   . HOH F .   ? 0.1934 0.2056 0.2207 -0.0012 -0.0418 -0.0864 586 HOH A O   
2380 O  O   . HOH F .   ? 0.4781 0.4988 0.4049 -0.0339 0.0138  -0.1713 587 HOH A O   
2381 O  O   . HOH F .   ? 0.2288 0.3591 0.4348 0.1207  0.0504  0.0084  588 HOH A O   
2382 O  O   . HOH F .   ? 0.5836 0.2186 0.2128 -0.1053 -0.1575 -0.0071 589 HOH A O   
2383 O  O   . HOH F .   ? 0.5488 0.3783 0.3712 0.0147  0.0479  -0.0103 590 HOH A O   
2384 O  O   . HOH F .   ? 0.3308 0.1862 0.2274 0.0453  -0.0284 -0.0320 591 HOH A O   
2385 O  O   . HOH F .   ? 0.1879 0.3368 0.4896 0.0200  0.0991  0.0820  592 HOH A O   
2386 O  O   . HOH F .   ? 0.2548 0.2139 0.2097 0.0563  -0.0361 0.0310  593 HOH A O   
2387 O  O   . HOH F .   ? 0.4188 0.3212 0.4900 0.0820  -0.0162 0.0300  594 HOH A O   
2388 O  O   . HOH F .   ? 0.5080 0.7173 0.3472 -0.0274 0.0590  -0.1717 595 HOH A O   
2389 O  O   . HOH F .   ? 0.2933 0.2365 0.1568 0.0488  -0.0251 0.0091  596 HOH A O   
2390 O  O   . HOH F .   ? 0.4106 0.5209 0.4605 0.0547  0.1324  0.2132  597 HOH A O   
2391 O  O   . HOH F .   ? 0.4215 0.1976 0.3017 0.0873  0.0512  0.0895  598 HOH A O   
2392 O  O   . HOH F .   ? 0.0948 0.1176 0.1573 0.0166  -0.0124 -0.0072 599 HOH A O   
2393 O  O   . HOH F .   ? 0.3134 0.3694 0.3177 -0.0065 -0.0908 0.0596  600 HOH A O   
2394 O  O   . HOH F .   ? 0.3419 0.4096 0.4207 0.0294  -0.0423 0.0184  601 HOH A O   
2395 O  O   . HOH F .   ? 0.3125 0.2489 0.5182 0.0774  0.1313  0.1091  602 HOH A O   
2396 O  O   . HOH F .   ? 0.1999 0.2392 0.3520 0.1018  -0.0097 -0.0348 603 HOH A O   
2397 O  O   . HOH F .   ? 0.1634 0.3087 0.3015 0.0946  -0.0891 -0.0205 604 HOH A O   
2398 O  O   . HOH F .   ? 0.2485 0.2317 0.3246 0.0695  0.0254  0.0385  605 HOH A O   
2399 O  O   . HOH F .   ? 0.7552 0.5330 0.6353 -0.1324 -0.1636 0.0518  606 HOH A O   
2400 O  O   . HOH F .   ? 0.3828 0.3816 0.2999 -0.1548 0.0785  0.0429  607 HOH A O   
2401 O  O   . HOH F .   ? 0.4594 0.4424 0.1595 0.0021  0.0513  0.0558  608 HOH A O   
2402 O  O   . HOH F .   ? 0.4266 0.3474 0.2529 -0.0480 -0.0039 0.0488  609 HOH A O   
2403 O  O   . HOH F .   ? 0.5855 0.4508 0.1532 0.1461  -0.0044 0.0449  610 HOH A O   
2404 O  O   . HOH F .   ? 0.6039 0.3198 0.1868 -0.1719 0.0377  -0.0803 611 HOH A O   
2405 O  O   . HOH F .   ? 0.3614 0.4780 0.6025 0.1556  -0.1760 -0.0839 612 HOH A O   
2406 O  O   . HOH F .   ? 0.4662 0.7068 0.6523 0.1824  0.2101  0.1085  613 HOH A O   
2407 O  O   . HOH F .   ? 0.4907 0.4414 0.4567 -0.0032 0.0333  -0.0261 614 HOH A O   
2408 O  O   . HOH F .   ? 0.3520 0.2588 0.2743 -0.0606 0.0325  0.0550  615 HOH A O   
2409 O  O   . HOH F .   ? 0.2957 0.5407 0.3904 0.0612  -0.0919 -0.1187 616 HOH A O   
2410 O  O   . HOH F .   ? 0.5324 0.4158 0.3581 0.1152  -0.0109 0.1214  617 HOH A O   
2411 O  O   . HOH F .   ? 0.3798 0.1952 0.2464 -0.0222 -0.0690 0.0287  618 HOH A O   
2412 O  O   . HOH F .   ? 0.5039 0.3154 0.5913 -0.0468 0.0140  0.1678  619 HOH A O   
2413 O  O   . HOH F .   ? 0.7294 0.3288 0.3312 -0.1790 0.0248  -0.0588 620 HOH A O   
2414 O  O   . HOH F .   ? 0.2040 0.3447 0.3215 -0.0416 -0.0307 0.0447  621 HOH A O   
2415 O  O   . HOH F .   ? 0.3580 0.4191 1.0987 -0.0143 -0.2054 0.1905  622 HOH A O   
2416 O  O   . HOH F .   ? 0.1347 0.4572 0.4814 -0.0636 -0.0461 0.0237  623 HOH A O   
2417 O  O   . HOH F .   ? 0.4831 0.1667 0.2176 -0.0642 -0.0873 -0.0211 624 HOH A O   
2418 O  O   . HOH F .   ? 0.5086 0.3456 0.2828 -0.0055 0.0498  -0.0184 625 HOH A O   
2419 O  O   . HOH F .   ? 0.4665 0.3289 0.1862 -0.0811 -0.0602 -0.0105 626 HOH A O   
2420 O  O   . HOH F .   ? 0.6333 0.2037 0.2957 -0.0686 0.1547  0.0098  627 HOH A O   
2421 O  O   . HOH F .   ? 0.4032 0.8600 0.4021 -0.1455 -0.0257 -0.2633 628 HOH A O   
2422 O  O   . HOH F .   ? 0.4087 0.3462 0.3403 0.0462  -0.0436 0.0274  629 HOH A O   
2423 O  O   . HOH F .   ? 0.2168 0.2980 0.4454 -0.0548 0.1317  -0.0736 630 HOH A O   
2424 O  O   . HOH F .   ? 0.6190 0.3784 0.4256 0.0006  0.3001  -0.0475 631 HOH A O   
2425 O  O   . HOH F .   ? 0.2128 0.4517 0.2367 0.0614  0.0436  0.0223  632 HOH A O   
2426 O  O   . HOH F .   ? 0.3024 0.3282 0.5468 -0.0812 -0.0749 0.0432  633 HOH A O   
2427 O  O   . HOH F .   ? 0.3445 0.4835 0.5576 0.1473  0.0510  0.0635  634 HOH A O   
2428 O  O   . HOH F .   ? 0.1232 0.1277 0.1491 -0.0021 -0.0253 -0.0071 635 HOH A O   
2429 O  O   . HOH F .   ? 0.5291 0.4101 0.4048 -0.0129 0.0325  -0.0108 636 HOH A O   
2430 O  O   . HOH F .   ? 0.7311 0.3458 0.4842 0.1744  0.3447  0.1311  637 HOH A O   
2431 O  O   . HOH F .   ? 0.3843 0.4384 0.3816 -0.0456 -0.1233 -0.1376 638 HOH A O   
2432 O  O   . HOH F .   ? 0.5064 0.4079 0.2435 0.0450  0.0586  0.0241  639 HOH A O   
2433 O  O   . HOH F .   ? 0.3338 0.3148 0.3514 0.0075  -0.0632 -0.0447 640 HOH A O   
2434 O  O   . HOH F .   ? 1.0537 0.5098 0.4871 0.2300  0.0757  0.1416  641 HOH A O   
2435 O  O   . HOH F .   ? 0.4345 0.2337 0.6213 -0.0574 0.0092  0.0581  642 HOH A O   
2436 O  O   . HOH F .   ? 0.3493 0.6686 0.3577 -0.2024 -0.0823 0.0055  643 HOH A O   
2437 O  O   . HOH F .   ? 1.1440 0.6673 0.4011 -0.1671 -0.1398 0.0174  644 HOH A O   
2438 O  O   . HOH F .   ? 0.2866 0.3676 0.5764 0.0529  0.0100  0.0183  645 HOH A O   
2439 O  O   . HOH F .   ? 0.1995 0.2002 0.1785 -0.0381 0.0178  0.0219  646 HOH A O   
2440 O  O   . HOH F .   ? 0.1525 0.1239 0.1835 0.0043  -0.0243 -0.0253 647 HOH A O   
2441 O  O   . HOH F .   ? 0.3495 0.7853 0.5802 -0.0703 0.0546  0.2829  648 HOH A O   
2442 O  O   . HOH F .   ? 0.3276 0.3872 0.5014 0.1910  -0.1657 -0.1490 649 HOH A O   
2443 O  O   . HOH F .   ? 0.5414 0.3124 0.3292 -0.0673 0.0703  0.0353  650 HOH A O   
2444 O  O   . HOH F .   ? 0.3678 0.3240 0.1895 -0.0499 0.0624  0.0778  651 HOH A O   
2445 O  O   . HOH F .   ? 0.6293 0.2672 0.7164 0.0277  -0.1340 0.1225  652 HOH A O   
2446 O  O   . HOH F .   ? 0.3673 0.3996 0.4536 0.0055  -0.0468 -0.0323 653 HOH A O   
2447 O  O   . HOH F .   ? 0.3452 0.5341 0.3743 -0.0754 -0.0812 0.1058  654 HOH A O   
2448 O  O   . HOH F .   ? 0.2962 0.5612 0.3153 -0.0509 0.0278  0.2232  655 HOH A O   
2449 O  O   . HOH F .   ? 0.3832 0.3883 0.3352 0.1233  0.0078  0.0837  656 HOH A O   
2450 O  O   . HOH F .   ? 0.3786 0.2010 0.4680 -0.0206 0.0417  0.0754  657 HOH A O   
2451 O  O   . HOH F .   ? 0.3811 0.4112 0.3222 0.0643  0.0944  0.0763  658 HOH A O   
2452 O  O   . HOH F .   ? 0.3213 0.2849 0.2340 -0.0050 -0.1032 -0.0272 659 HOH A O   
2453 O  O   . HOH F .   ? 0.3158 0.4001 0.2555 -0.1309 -0.0362 0.0259  660 HOH A O   
2454 O  O   . HOH F .   ? 0.5773 0.3549 0.3213 -0.0114 0.0675  -0.0238 661 HOH A O   
2455 O  O   . HOH F .   ? 0.4229 0.4161 0.3808 -0.0763 0.0139  -0.0545 662 HOH A O   
2456 O  O   . HOH F .   ? 0.3257 0.2513 0.3727 0.0744  -0.2350 -0.0328 663 HOH A O   
2457 O  O   . HOH F .   ? 0.1674 0.2799 0.3237 0.0731  0.0592  0.0183  664 HOH A O   
2458 O  O   . HOH F .   ? 0.2913 0.4482 0.6438 0.0590  -0.0719 -0.0158 665 HOH A O   
2459 O  O   . HOH F .   ? 0.3903 0.4954 0.4127 0.0271  0.1070  -0.0985 666 HOH A O   
2460 O  O   . HOH F .   ? 0.5079 0.3114 0.3431 0.0120  0.0373  0.0622  667 HOH A O   
2461 O  O   . HOH F .   ? 0.2978 0.3943 0.3407 0.0370  0.0195  0.0854  668 HOH A O   
2462 O  O   . HOH F .   ? 0.4277 0.4315 0.4683 0.0443  0.0524  -0.0035 669 HOH A O   
2463 O  O   . HOH F .   ? 0.4335 0.4400 0.3788 0.0307  0.0194  0.0009  670 HOH A O   
2464 O  O   . HOH F .   ? 0.2403 0.2811 0.4021 0.0461  -0.0081 0.0784  671 HOH A O   
2465 O  O   . HOH F .   ? 0.3251 0.8038 0.4066 0.0631  -0.0053 0.1556  672 HOH A O   
2466 O  O   . HOH F .   ? 0.2617 0.3653 0.2896 0.1521  -0.0507 -0.0051 673 HOH A O   
2467 O  O   . HOH F .   ? 0.4180 0.3772 0.4045 0.0517  -0.0089 0.0345  674 HOH A O   
2468 O  O   . HOH F .   ? 0.2236 0.3334 0.2437 -0.0214 0.0332  -0.0128 675 HOH A O   
2469 O  O   . HOH F .   ? 0.2067 0.2137 0.2940 0.0192  -0.0761 -0.0120 676 HOH A O   
2470 O  O   . HOH F .   ? 0.5401 0.3753 0.3856 -0.0521 0.1436  -0.0839 677 HOH A O   
2471 O  O   . HOH F .   ? 0.3922 0.4183 0.4230 0.0839  -0.0215 0.0328  678 HOH A O   
2472 O  O   . HOH F .   ? 0.2931 0.2615 0.2216 -0.0774 -0.0416 -0.0208 679 HOH A O   
2473 O  O   . HOH F .   ? 0.4417 0.3040 0.3416 -0.0861 0.0877  0.0222  680 HOH A O   
2474 O  O   . HOH F .   ? 0.3767 0.5401 0.3231 0.0171  0.1012  0.1057  681 HOH A O   
2475 O  O   . HOH F .   ? 0.4086 0.5655 0.2482 0.0250  -0.0965 0.0509  682 HOH A O   
2476 O  O   . HOH F .   ? 0.3285 0.5005 0.4478 0.0802  0.0376  -0.0604 683 HOH A O   
2477 O  O   . HOH F .   ? 0.1670 0.3265 0.3274 0.0119  -0.0152 -0.0048 684 HOH A O   
2478 O  O   . HOH F .   ? 0.8724 0.3391 0.2992 -0.1390 -0.1446 0.0752  685 HOH A O   
2479 O  O   . HOH F .   ? 0.1893 0.3346 0.5049 -0.0763 0.0311  0.0128  686 HOH A O   
2480 O  O   . HOH F .   ? 0.5240 0.4637 0.4442 -0.0218 0.0145  0.0867  687 HOH A O   
2481 O  O   . HOH F .   ? 0.2615 0.3215 0.2148 -0.0884 0.0365  0.0351  688 HOH A O   
2482 O  O   . HOH F .   ? 0.4463 0.2518 0.3290 0.0281  -0.0766 -0.0168 689 HOH A O   
2483 O  O   . HOH F .   ? 0.3880 0.3177 0.2277 -0.0309 -0.0115 0.0502  690 HOH A O   
2484 O  O   . HOH F .   ? 0.3944 0.5432 0.7465 0.0796  0.0119  0.0535  691 HOH A O   
2485 O  O   . HOH F .   ? 0.1422 0.3432 0.5969 -0.0008 -0.0464 0.0412  692 HOH A O   
2486 O  O   . HOH F .   ? 0.3064 0.2561 0.3651 -0.0085 0.0432  -0.0200 693 HOH A O   
2487 O  O   . HOH F .   ? 0.1291 0.1160 0.1593 -0.0117 -0.0089 0.0073  694 HOH A O   
2488 O  O   . HOH F .   ? 0.4109 0.4209 0.1898 -0.0876 0.0216  0.0709  695 HOH A O   
2489 O  O   . HOH F .   ? 0.4362 0.3704 0.2166 0.0677  -0.0176 -0.0988 696 HOH A O   
2490 O  O   . HOH F .   ? 0.3518 0.3995 0.4538 -0.0350 -0.0259 0.0706  697 HOH A O   
2491 O  O   . HOH F .   ? 0.3585 0.5382 0.4003 0.1070  0.0100  -0.2410 698 HOH A O   
2492 O  O   . HOH F .   ? 0.4527 0.4788 0.3367 0.0197  -0.0631 0.0176  699 HOH A O   
2493 O  O   . HOH F .   ? 0.4261 0.4273 0.5007 0.0291  -0.0714 0.0174  700 HOH A O   
2494 O  O   . HOH F .   ? 0.4139 0.3779 0.4133 0.0545  0.0944  -0.0898 701 HOH A O   
2495 O  O   . HOH F .   ? 0.3184 0.4688 0.2236 0.0534  0.0306  0.0042  702 HOH A O   
2496 O  O   . HOH F .   ? 0.3732 0.4526 0.4982 0.0735  0.0491  0.0644  703 HOH A O   
2497 O  O   . HOH F .   ? 0.2858 0.5224 0.3031 -0.0118 0.1184  0.0538  704 HOH A O   
2498 O  O   . HOH F .   ? 0.2500 0.1895 0.1884 0.0179  -0.0436 -0.0186 705 HOH A O   
2499 O  O   . HOH F .   ? 0.4542 0.4643 0.3049 -0.1269 -0.1349 -0.0807 706 HOH A O   
2500 O  O   . HOH F .   ? 0.4771 0.2444 0.5813 -0.0745 -0.0871 0.1209  707 HOH A O   
2501 O  O   . HOH F .   ? 0.1512 0.2329 0.2399 0.0300  -0.0639 0.0116  708 HOH A O   
2502 O  O   . HOH F .   ? 0.4997 0.5046 0.4111 -0.0130 0.0719  -0.0577 709 HOH A O   
2503 O  O   . HOH F .   ? 0.6822 0.5536 0.5968 0.2742  -0.0325 -0.2275 710 HOH A O   
2504 O  O   . HOH F .   ? 0.3071 0.2583 0.5219 0.0312  0.0981  0.0546  711 HOH A O   
2505 O  O   . HOH F .   ? 0.4596 0.3016 0.4884 -0.1388 0.1714  -0.0635 712 HOH A O   
2506 O  O   . HOH F .   ? 0.6729 0.5136 0.3692 -0.1527 -0.1688 0.0407  713 HOH A O   
2507 O  O   . HOH F .   ? 0.4702 0.3001 0.3430 0.0277  0.0021  -0.0504 714 HOH A O   
2508 O  O   . HOH F .   ? 0.5299 0.3969 0.6087 -0.1626 -0.0089 0.0528  715 HOH A O   
2509 O  O   . HOH F .   ? 0.3393 0.3700 0.5274 -0.0329 -0.0044 0.0801  716 HOH A O   
2510 O  O   . HOH F .   ? 0.4169 0.3470 0.4119 -0.0453 0.0270  -0.0250 717 HOH A O   
2511 O  O   . HOH F .   ? 0.4081 0.3717 0.3822 0.0033  0.0030  -0.0132 718 HOH A O   
2512 O  O   . HOH F .   ? 0.3436 0.4056 0.6032 -0.0217 0.0261  -0.1659 719 HOH A O   
2513 O  O   . HOH F .   ? 0.3361 0.2832 0.4151 -0.0970 0.0078  0.0077  720 HOH A O   
2514 O  O   . HOH F .   ? 0.2223 0.1931 0.3392 -0.0296 0.1079  -0.0526 721 HOH A O   
2515 O  O   . HOH F .   ? 0.4738 0.4505 0.3183 0.0335  -0.0309 0.0420  722 HOH A O   
2516 O  O   . HOH F .   ? 0.2187 0.3855 0.5224 -0.0824 0.0321  -0.1323 723 HOH A O   
2517 O  O   . HOH F .   ? 0.2254 0.5194 0.4306 -0.1098 0.0783  0.0063  724 HOH A O   
2518 O  O   . HOH F .   ? 0.2349 0.3793 0.3902 -0.1310 0.0215  -0.1060 725 HOH A O   
2519 O  O   . HOH F .   ? 0.2956 0.4435 0.4390 -0.0392 0.0346  0.0557  726 HOH A O   
2520 O  O   . HOH F .   ? 0.2916 0.2708 0.2935 0.0851  -0.0434 -0.0807 727 HOH A O   
2521 O  O   . HOH F .   ? 0.4265 0.4373 0.4374 -0.0207 0.0225  0.0039  728 HOH A O   
# 
