data_7NZX
# 
_entry.id   7NZX 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.384 
_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   7NZX         pdb_00007nzx 10.2210/pdb7nzx/pdb 
WWPDB D_1292114824 ?            ?                   
# 
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 2022-04-13 
2 'Structure model' 1 1 2024-01-31 
# 
_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' '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' pdbx_initial_refinement_model 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        7NZX 
_pdbx_database_status.recvd_initial_deposition_date   2021-03-24 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
PDB 'PDB entry for the same citation' 7NZR unspecified 
PDB 'PDB entry for the same citation' 7NZS unspecified 
PDB 'PDB entry for the same citation' 7NZT unspecified 
PDB 'PDB entry for the same citation' 7NZU unspecified 
PDB 'PDB entry for the same citation' 7NZW unspecified 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Smirnov, A.'  1 0000-0001-5080-9367 
'Manakova, E.' 2 0000-0002-6027-2265 
'Grazulis, S.' 3 0000-0002-7928-5218 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Crystal structure of chimeric carbonic anhydrase VA' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
_citation_author.citation_id        primary 
_citation_author.name               'Smirnov, A.' 
_citation_author.ordinal            1 
_citation_author.identifier_ORCID   0000-0001-5080-9367 
# 
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'                                               29377.160 1   4.2.1.1 
'N62T, H64Y, A65L, N67Q, I91K, F130Y, L203T' ? ? 
2 non-polymer syn 'ZINC ION'                                                           65.409    1   ?       ? ? ? 
3 non-polymer syn '2,3,5,6-tetrafluoro-4-[(2-hydroxyethyl)sulfonyl]benzenesulfonamide' 337.268   1   ?       ? ? ? 
4 non-polymer syn BICINE                                                               163.172   1   ?       ? ? ? 
5 non-polymer syn 'DIMETHYL SULFOXIDE'                                                 78.133    1   ?       ? ? ? 
6 non-polymer syn 'SODIUM ION'                                                         22.990    1   ?       ? ? ? 
7 water       nat water                                                                18.015    300 ?       ? ? ? 
# 
_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       
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNTGYLFQVEFDDSQDKAVLK
GGPLDGTYRLKQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDYGKAVQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLTECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNTGYLFQVEFDDSQDKAVLK
GGPLDGTYRLKQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDYGKAVQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLTECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
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 '2,3,5,6-tetrafluoro-4-[(2-hydroxyethyl)sulfonyl]benzenesulfonamide' V13 
4 BICINE                                                               BCN 
5 'DIMETHYL SULFOXIDE'                                                 DMS 
6 'SODIUM ION'                                                         NA  
7 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  THR n 
1 63  GLY n 
1 64  TYR n 
1 65  LEU n 
1 66  PHE n 
1 67  GLN 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  LYS 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 TYR 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 THR 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 BL21(DE3)' 
_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               ? 
_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  
GLN 'L-peptide linking' y GLUTAMINE                                                            ? 'C5 H10 N2 O3'     146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                                                      ? 'C5 H9 N O4'       147.129 
GLY 'peptide linking'   y GLYCINE                                                              ? 'C2 H5 N O2'       75.067  
HIS 'L-peptide linking' y HISTIDINE                                                            ? 'C6 H10 N3 O2 1'   156.162 
HOH non-polymer         . WATER                                                                ? 'H2 O'             18.015  
ILE 'L-peptide linking' y ISOLEUCINE                                                           ? 'C6 H13 N O2'      131.173 
LEU 'L-peptide linking' y LEUCINE                                                              ? 'C6 H13 N O2'      131.173 
LYS 'L-peptide linking' y LYSINE                                                               ? 'C6 H15 N2 O2 1'   147.195 
MET 'L-peptide linking' y METHIONINE                                                           ? 'C5 H11 N O2 S'    149.211 
NA  non-polymer         . 'SODIUM ION'                                                         ? 'Na 1'             22.990  
PHE 'L-peptide linking' y PHENYLALANINE                                                        ? 'C9 H11 N O2'      165.189 
PRO 'L-peptide linking' y PROLINE                                                              ? 'C5 H9 N O2'       115.130 
SER 'L-peptide linking' y SERINE                                                               ? 'C3 H7 N O3'       105.093 
THR 'L-peptide linking' y THREONINE                                                            ? 'C4 H9 N O3'       119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                                           ? 'C11 H12 N2 O2'    204.225 
TYR 'L-peptide linking' y TYROSINE                                                             ? 'C9 H11 N O3'      181.189 
V13 non-polymer         . '2,3,5,6-tetrafluoro-4-[(2-hydroxyethyl)sulfonyl]benzenesulfonamide' ? 'C8 H7 F4 N O5 S2' 337.268 
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   3   HIS HIS 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  THR 62  62  62  THR THR A . n 
A 1 63  GLY 63  63  63  GLY GLY A . n 
A 1 64  TYR 64  64  64  TYR TYR A . n 
A 1 65  LEU 65  65  65  LEU LEU A . n 
A 1 66  PHE 66  66  66  PHE PHE A . n 
A 1 67  GLN 67  67  67  GLN GLN 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  LYS 91  91  91  LYS LYS 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 126 126 126 LYS LYS A . n 
A 1 127 TYR 127 127 127 TYR TYR A . n 
A 1 128 GLY 128 128 128 GLY GLY A . n 
A 1 129 ASP 129 129 129 ASP ASP A . n 
A 1 130 TYR 130 130 130 TYR TYR A . n 
A 1 131 GLY 131 131 131 GLY GLY A . n 
A 1 132 LYS 132 132 132 LYS LYS A . n 
A 1 133 ALA 133 133 133 ALA ALA A . n 
A 1 134 VAL 134 134 134 VAL VAL A . n 
A 1 135 GLN 135 135 135 GLN GLN A . n 
A 1 136 GLN 136 136 136 GLN GLN A . n 
A 1 137 PRO 137 137 137 PRO PRO A . n 
A 1 138 ASP 138 138 138 ASP ASP A . n 
A 1 139 GLY 139 139 139 GLY GLY A . n 
A 1 140 LEU 140 140 140 LEU LEU A . n 
A 1 141 ALA 141 141 141 ALA ALA A . n 
A 1 142 VAL 142 142 142 VAL VAL A . n 
A 1 143 LEU 143 143 143 LEU LEU A . n 
A 1 144 GLY 144 144 144 GLY GLY A . n 
A 1 145 ILE 145 145 145 ILE ILE A . n 
A 1 146 PHE 146 146 146 PHE PHE A . n 
A 1 147 LEU 147 147 147 LEU LEU A . n 
A 1 148 LYS 148 148 148 LYS LYS A . n 
A 1 149 VAL 149 149 149 VAL VAL A . n 
A 1 150 GLY 150 150 150 GLY GLY A . n 
A 1 151 SER 151 151 151 SER SER A . n 
A 1 152 ALA 152 152 152 ALA ALA A . n 
A 1 153 LYS 153 153 153 LYS LYS A . n 
A 1 154 PRO 154 154 154 PRO PRO A . n 
A 1 155 GLY 155 155 155 GLY GLY A . n 
A 1 156 LEU 156 156 156 LEU LEU A . n 
A 1 157 GLN 157 157 157 GLN GLN A . n 
A 1 158 LYS 158 158 158 LYS LYS A . n 
A 1 159 VAL 159 159 159 VAL VAL A . n 
A 1 160 VAL 160 160 160 VAL VAL A . n 
A 1 161 ASP 161 161 161 ASP ASP A . n 
A 1 162 VAL 162 162 162 VAL VAL A . n 
A 1 163 LEU 163 163 163 LEU LEU A . n 
A 1 164 ASP 164 164 164 ASP ASP A . n 
A 1 165 SER 165 165 165 SER SER A . n 
A 1 166 ILE 166 166 166 ILE ILE A . n 
A 1 167 LYS 167 167 167 LYS LYS A . n 
A 1 168 THR 168 168 168 THR THR A . n 
A 1 169 LYS 169 169 169 LYS LYS A . n 
A 1 170 GLY 170 170 170 GLY GLY A . n 
A 1 171 LYS 171 171 171 LYS LYS A . n 
A 1 172 SER 172 172 172 SER SER A . n 
A 1 173 ALA 173 173 173 ALA ALA A . n 
A 1 174 ASP 174 174 174 ASP ASP A . n 
A 1 175 PHE 175 175 175 PHE PHE A . n 
A 1 176 THR 176 176 176 THR THR A . n 
A 1 177 ASN 177 177 177 ASN ASN A . n 
A 1 178 PHE 178 178 178 PHE PHE A . n 
A 1 179 ASP 179 179 179 ASP ASP A . n 
A 1 180 PRO 180 180 180 PRO PRO A . n 
A 1 181 ARG 181 181 181 ARG ARG A . n 
A 1 182 GLY 182 182 182 GLY GLY A . n 
A 1 183 LEU 183 183 183 LEU LEU A . n 
A 1 184 LEU 184 184 184 LEU LEU A . n 
A 1 185 PRO 185 185 185 PRO PRO A . n 
A 1 186 GLU 186 186 186 GLU GLU A . n 
A 1 187 SER 187 187 187 SER SER A . n 
A 1 188 LEU 188 188 188 LEU LEU A . n 
A 1 189 ASP 189 189 189 ASP ASP A . n 
A 1 190 TYR 190 190 190 TYR TYR A . n 
A 1 191 TRP 191 191 191 TRP TRP A . n 
A 1 192 THR 192 192 192 THR THR A . n 
A 1 193 TYR 193 193 193 TYR TYR A . n 
A 1 194 PRO 194 194 194 PRO PRO A . n 
A 1 195 GLY 195 195 195 GLY GLY A . n 
A 1 196 SER 196 196 196 SER SER A . n 
A 1 197 LEU 197 197 197 LEU LEU A . n 
A 1 198 THR 198 198 198 THR THR A . n 
A 1 199 THR 199 199 199 THR THR A . n 
A 1 200 PRO 200 200 200 PRO PRO A . n 
A 1 201 PRO 201 201 201 PRO PRO A . n 
A 1 202 LEU 202 202 202 LEU LEU A . n 
A 1 203 THR 203 203 203 THR THR A . n 
A 1 204 GLU 204 204 204 GLU GLU A . n 
A 1 205 CYS 205 205 205 CYS CYS A . n 
A 1 206 VAL 206 206 206 VAL VAL A . n 
A 1 207 THR 207 207 207 THR THR A . n 
A 1 208 TRP 208 208 208 TRP TRP A . n 
A 1 209 ILE 209 209 209 ILE ILE A . n 
A 1 210 VAL 210 210 210 VAL VAL A . n 
A 1 211 LEU 211 211 211 LEU LEU A . n 
A 1 212 LYS 212 212 212 LYS LYS A . n 
A 1 213 GLU 213 213 213 GLU GLU A . n 
A 1 214 PRO 214 214 214 PRO PRO A . n 
A 1 215 ILE 215 215 215 ILE ILE A . n 
A 1 216 SER 216 216 216 SER SER A . n 
A 1 217 VAL 217 217 217 VAL VAL A . n 
A 1 218 SER 218 218 218 SER SER A . n 
A 1 219 SER 219 219 219 SER SER A . n 
A 1 220 GLU 220 220 220 GLU GLU A . n 
A 1 221 GLN 221 221 221 GLN GLN A . n 
A 1 222 VAL 222 222 222 VAL VAL A . n 
A 1 223 LEU 223 223 223 LEU LEU A . n 
A 1 224 LYS 224 224 224 LYS LYS A . n 
A 1 225 PHE 225 225 225 PHE PHE A . n 
A 1 226 ARG 226 226 226 ARG ARG A . n 
A 1 227 LYS 227 227 227 LYS LYS A . n 
A 1 228 LEU 228 228 228 LEU LEU A . n 
A 1 229 ASN 229 229 229 ASN ASN A . n 
A 1 230 PHE 230 230 230 PHE PHE A . n 
A 1 231 ASN 231 231 231 ASN ASN A . n 
A 1 232 GLY 232 232 232 GLY GLY A . n 
A 1 233 GLU 233 233 233 GLU GLU A . n 
A 1 234 GLY 234 234 234 GLY GLY A . n 
A 1 235 GLU 235 235 235 GLU GLU A . n 
A 1 236 PRO 236 236 236 PRO PRO A . n 
A 1 237 GLU 237 237 237 GLU GLU A . n 
A 1 238 GLU 238 238 238 GLU GLU A . n 
A 1 239 LEU 239 239 239 LEU LEU A . n 
A 1 240 MET 240 240 240 MET MET A . n 
A 1 241 VAL 241 241 241 VAL VAL A . n 
A 1 242 ASP 242 242 242 ASP ASP A . n 
A 1 243 ASN 243 243 243 ASN ASN A . n 
A 1 244 TRP 244 244 244 TRP TRP A . n 
A 1 245 ARG 245 245 245 ARG ARG A . n 
A 1 246 PRO 246 246 246 PRO PRO A . n 
A 1 247 ALA 247 247 247 ALA ALA A . n 
A 1 248 GLN 248 248 248 GLN GLN A . n 
A 1 249 PRO 249 249 249 PRO PRO A . n 
A 1 250 LEU 250 250 250 LEU LEU A . n 
A 1 251 LYS 251 251 251 LYS LYS A . n 
A 1 252 ASN 252 252 252 ASN ASN A . n 
A 1 253 ARG 253 253 253 ARG ARG A . n 
A 1 254 GLN 254 254 254 GLN GLN A . n 
A 1 255 ILE 255 255 255 ILE ILE A . n 
A 1 256 LYS 256 256 256 LYS LYS A . n 
A 1 257 ALA 257 257 257 ALA ALA A . n 
A 1 258 SER 258 258 258 SER SER A . n 
A 1 259 PHE 259 259 259 PHE PHE A . n 
A 1 260 LYS 260 260 260 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 V13 1   302 1   V13 V13 A . 
D 4 BCN 1   303 1   BCN BCN A . 
E 5 DMS 1   304 2   DMS DMS A . 
F 6 NA  1   305 1   NA  NA  A . 
G 7 HOH 1   401 263 HOH HOH A . 
G 7 HOH 2   402 248 HOH HOH A . 
G 7 HOH 3   403 183 HOH HOH A . 
G 7 HOH 4   404 252 HOH HOH A . 
G 7 HOH 5   405 227 HOH HOH A . 
G 7 HOH 6   406 290 HOH HOH A . 
G 7 HOH 7   407 204 HOH HOH A . 
G 7 HOH 8   408 119 HOH HOH A . 
G 7 HOH 9   409 216 HOH HOH A . 
G 7 HOH 10  410 129 HOH HOH A . 
G 7 HOH 11  411 229 HOH HOH A . 
G 7 HOH 12  412 141 HOH HOH A . 
G 7 HOH 13  413 288 HOH HOH A . 
G 7 HOH 14  414 151 HOH HOH A . 
G 7 HOH 15  415 62  HOH HOH A . 
G 7 HOH 16  416 38  HOH HOH A . 
G 7 HOH 17  417 143 HOH HOH A . 
G 7 HOH 18  418 187 HOH HOH A . 
G 7 HOH 19  419 272 HOH HOH A . 
G 7 HOH 20  420 121 HOH HOH A . 
G 7 HOH 21  421 167 HOH HOH A . 
G 7 HOH 22  422 236 HOH HOH A . 
G 7 HOH 23  423 262 HOH HOH A . 
G 7 HOH 24  424 148 HOH HOH A . 
G 7 HOH 25  425 133 HOH HOH A . 
G 7 HOH 26  426 218 HOH HOH A . 
G 7 HOH 27  427 213 HOH HOH A . 
G 7 HOH 28  428 297 HOH HOH A . 
G 7 HOH 29  429 241 HOH HOH A . 
G 7 HOH 30  430 14  HOH HOH A . 
G 7 HOH 31  431 81  HOH HOH A . 
G 7 HOH 32  432 155 HOH HOH A . 
G 7 HOH 33  433 112 HOH HOH A . 
G 7 HOH 34  434 57  HOH HOH A . 
G 7 HOH 35  435 20  HOH HOH A . 
G 7 HOH 36  436 3   HOH HOH A . 
G 7 HOH 37  437 87  HOH HOH A . 
G 7 HOH 38  438 179 HOH HOH A . 
G 7 HOH 39  439 300 HOH HOH A . 
G 7 HOH 40  440 223 HOH HOH A . 
G 7 HOH 41  441 165 HOH HOH A . 
G 7 HOH 42  442 61  HOH HOH A . 
G 7 HOH 43  443 24  HOH HOH A . 
G 7 HOH 44  444 44  HOH HOH A . 
G 7 HOH 45  445 298 HOH HOH A . 
G 7 HOH 46  446 203 HOH HOH A . 
G 7 HOH 47  447 240 HOH HOH A . 
G 7 HOH 48  448 11  HOH HOH A . 
G 7 HOH 49  449 156 HOH HOH A . 
G 7 HOH 50  450 101 HOH HOH A . 
G 7 HOH 51  451 269 HOH HOH A . 
G 7 HOH 52  452 256 HOH HOH A . 
G 7 HOH 53  453 162 HOH HOH A . 
G 7 HOH 54  454 9   HOH HOH A . 
G 7 HOH 55  455 19  HOH HOH A . 
G 7 HOH 56  456 257 HOH HOH A . 
G 7 HOH 57  457 92  HOH HOH A . 
G 7 HOH 58  458 117 HOH HOH A . 
G 7 HOH 59  459 188 HOH HOH A . 
G 7 HOH 60  460 253 HOH HOH A . 
G 7 HOH 61  461 73  HOH HOH A . 
G 7 HOH 62  462 31  HOH HOH A . 
G 7 HOH 63  463 123 HOH HOH A . 
G 7 HOH 64  464 220 HOH HOH A . 
G 7 HOH 65  465 181 HOH HOH A . 
G 7 HOH 66  466 283 HOH HOH A . 
G 7 HOH 67  467 266 HOH HOH A . 
G 7 HOH 68  468 120 HOH HOH A . 
G 7 HOH 69  469 40  HOH HOH A . 
G 7 HOH 70  470 157 HOH HOH A . 
G 7 HOH 71  471 150 HOH HOH A . 
G 7 HOH 72  472 200 HOH HOH A . 
G 7 HOH 73  473 158 HOH HOH A . 
G 7 HOH 74  474 10  HOH HOH A . 
G 7 HOH 75  475 245 HOH HOH A . 
G 7 HOH 76  476 149 HOH HOH A . 
G 7 HOH 77  477 244 HOH HOH A . 
G 7 HOH 78  478 63  HOH HOH A . 
G 7 HOH 79  479 85  HOH HOH A . 
G 7 HOH 80  480 267 HOH HOH A . 
G 7 HOH 81  481 12  HOH HOH A . 
G 7 HOH 82  482 56  HOH HOH A . 
G 7 HOH 83  483 299 HOH HOH A . 
G 7 HOH 84  484 29  HOH HOH A . 
G 7 HOH 85  485 95  HOH HOH A . 
G 7 HOH 86  486 89  HOH HOH A . 
G 7 HOH 87  487 49  HOH HOH A . 
G 7 HOH 88  488 199 HOH HOH A . 
G 7 HOH 89  489 97  HOH HOH A . 
G 7 HOH 90  490 96  HOH HOH A . 
G 7 HOH 91  491 152 HOH HOH A . 
G 7 HOH 92  492 196 HOH HOH A . 
G 7 HOH 93  493 136 HOH HOH A . 
G 7 HOH 94  494 39  HOH HOH A . 
G 7 HOH 95  495 108 HOH HOH A . 
G 7 HOH 96  496 13  HOH HOH A . 
G 7 HOH 97  497 47  HOH HOH A . 
G 7 HOH 98  498 1   HOH HOH A . 
G 7 HOH 99  499 102 HOH HOH A . 
G 7 HOH 100 500 8   HOH HOH A . 
G 7 HOH 101 501 110 HOH HOH A . 
G 7 HOH 102 502 15  HOH HOH A . 
G 7 HOH 103 503 4   HOH HOH A . 
G 7 HOH 104 504 46  HOH HOH A . 
G 7 HOH 105 505 88  HOH HOH A . 
G 7 HOH 106 506 66  HOH HOH A . 
G 7 HOH 107 507 207 HOH HOH A . 
G 7 HOH 108 508 285 HOH HOH A . 
G 7 HOH 109 509 21  HOH HOH A . 
G 7 HOH 110 510 76  HOH HOH A . 
G 7 HOH 111 511 69  HOH HOH A . 
G 7 HOH 112 512 83  HOH HOH A . 
G 7 HOH 113 513 113 HOH HOH A . 
G 7 HOH 114 514 42  HOH HOH A . 
G 7 HOH 115 515 28  HOH HOH A . 
G 7 HOH 116 516 93  HOH HOH A . 
G 7 HOH 117 517 53  HOH HOH A . 
G 7 HOH 118 518 91  HOH HOH A . 
G 7 HOH 119 519 67  HOH HOH A . 
G 7 HOH 120 520 106 HOH HOH A . 
G 7 HOH 121 521 276 HOH HOH A . 
G 7 HOH 122 522 77  HOH HOH A . 
G 7 HOH 123 523 215 HOH HOH A . 
G 7 HOH 124 524 6   HOH HOH A . 
G 7 HOH 125 525 111 HOH HOH A . 
G 7 HOH 126 526 52  HOH HOH A . 
G 7 HOH 127 527 35  HOH HOH A . 
G 7 HOH 128 528 226 HOH HOH A . 
G 7 HOH 129 529 186 HOH HOH A . 
G 7 HOH 130 530 228 HOH HOH A . 
G 7 HOH 131 531 84  HOH HOH A . 
G 7 HOH 132 532 59  HOH HOH A . 
G 7 HOH 133 533 37  HOH HOH A . 
G 7 HOH 134 534 128 HOH HOH A . 
G 7 HOH 135 535 107 HOH HOH A . 
G 7 HOH 136 536 36  HOH HOH A . 
G 7 HOH 137 537 17  HOH HOH A . 
G 7 HOH 138 538 43  HOH HOH A . 
G 7 HOH 139 539 164 HOH HOH A . 
G 7 HOH 140 540 287 HOH HOH A . 
G 7 HOH 141 541 206 HOH HOH A . 
G 7 HOH 142 542 90  HOH HOH A . 
G 7 HOH 143 543 30  HOH HOH A . 
G 7 HOH 144 544 99  HOH HOH A . 
G 7 HOH 145 545 2   HOH HOH A . 
G 7 HOH 146 546 208 HOH HOH A . 
G 7 HOH 147 547 82  HOH HOH A . 
G 7 HOH 148 548 23  HOH HOH A . 
G 7 HOH 149 549 27  HOH HOH A . 
G 7 HOH 150 550 7   HOH HOH A . 
G 7 HOH 151 551 32  HOH HOH A . 
G 7 HOH 152 552 72  HOH HOH A . 
G 7 HOH 153 553 45  HOH HOH A . 
G 7 HOH 154 554 34  HOH HOH A . 
G 7 HOH 155 555 131 HOH HOH A . 
G 7 HOH 156 556 25  HOH HOH A . 
G 7 HOH 157 557 138 HOH HOH A . 
G 7 HOH 158 558 100 HOH HOH A . 
G 7 HOH 159 559 16  HOH HOH A . 
G 7 HOH 160 560 134 HOH HOH A . 
G 7 HOH 161 561 78  HOH HOH A . 
G 7 HOH 162 562 142 HOH HOH A . 
G 7 HOH 163 563 132 HOH HOH A . 
G 7 HOH 164 564 124 HOH HOH A . 
G 7 HOH 165 565 279 HOH HOH A . 
G 7 HOH 166 566 50  HOH HOH A . 
G 7 HOH 167 567 274 HOH HOH A . 
G 7 HOH 168 568 26  HOH HOH A . 
G 7 HOH 169 569 94  HOH HOH A . 
G 7 HOH 170 570 86  HOH HOH A . 
G 7 HOH 171 571 74  HOH HOH A . 
G 7 HOH 172 572 161 HOH HOH A . 
G 7 HOH 173 573 168 HOH HOH A . 
G 7 HOH 174 574 68  HOH HOH A . 
G 7 HOH 175 575 194 HOH HOH A . 
G 7 HOH 176 576 51  HOH HOH A . 
G 7 HOH 177 577 295 HOH HOH A . 
G 7 HOH 178 578 5   HOH HOH A . 
G 7 HOH 179 579 75  HOH HOH A . 
G 7 HOH 180 580 80  HOH HOH A . 
G 7 HOH 181 581 105 HOH HOH A . 
G 7 HOH 182 582 160 HOH HOH A . 
G 7 HOH 183 583 144 HOH HOH A . 
G 7 HOH 184 584 64  HOH HOH A . 
G 7 HOH 185 585 70  HOH HOH A . 
G 7 HOH 186 586 201 HOH HOH A . 
G 7 HOH 187 587 195 HOH HOH A . 
G 7 HOH 188 588 190 HOH HOH A . 
G 7 HOH 189 589 18  HOH HOH A . 
G 7 HOH 190 590 286 HOH HOH A . 
G 7 HOH 191 591 116 HOH HOH A . 
G 7 HOH 192 592 209 HOH HOH A . 
G 7 HOH 193 593 65  HOH HOH A . 
G 7 HOH 194 594 41  HOH HOH A . 
G 7 HOH 195 595 278 HOH HOH A . 
G 7 HOH 196 596 180 HOH HOH A . 
G 7 HOH 197 597 126 HOH HOH A . 
G 7 HOH 198 598 275 HOH HOH A . 
G 7 HOH 199 599 258 HOH HOH A . 
G 7 HOH 200 600 140 HOH HOH A . 
G 7 HOH 201 601 224 HOH HOH A . 
G 7 HOH 202 602 33  HOH HOH A . 
G 7 HOH 203 603 243 HOH HOH A . 
G 7 HOH 204 604 235 HOH HOH A . 
G 7 HOH 205 605 109 HOH HOH A . 
G 7 HOH 206 606 103 HOH HOH A . 
G 7 HOH 207 607 122 HOH HOH A . 
G 7 HOH 208 608 189 HOH HOH A . 
G 7 HOH 209 609 289 HOH HOH A . 
G 7 HOH 210 610 254 HOH HOH A . 
G 7 HOH 211 611 104 HOH HOH A . 
G 7 HOH 212 612 54  HOH HOH A . 
G 7 HOH 213 613 211 HOH HOH A . 
G 7 HOH 214 614 182 HOH HOH A . 
G 7 HOH 215 615 221 HOH HOH A . 
G 7 HOH 216 616 292 HOH HOH A . 
G 7 HOH 217 617 60  HOH HOH A . 
G 7 HOH 218 618 127 HOH HOH A . 
G 7 HOH 219 619 230 HOH HOH A . 
G 7 HOH 220 620 130 HOH HOH A . 
G 7 HOH 221 621 282 HOH HOH A . 
G 7 HOH 222 622 191 HOH HOH A . 
G 7 HOH 223 623 242 HOH HOH A . 
G 7 HOH 224 624 249 HOH HOH A . 
G 7 HOH 225 625 261 HOH HOH A . 
G 7 HOH 226 626 205 HOH HOH A . 
G 7 HOH 227 627 153 HOH HOH A . 
G 7 HOH 228 628 198 HOH HOH A . 
G 7 HOH 229 629 239 HOH HOH A . 
G 7 HOH 230 630 159 HOH HOH A . 
G 7 HOH 231 631 291 HOH HOH A . 
G 7 HOH 232 632 280 HOH HOH A . 
G 7 HOH 233 633 247 HOH HOH A . 
G 7 HOH 234 634 184 HOH HOH A . 
G 7 HOH 235 635 232 HOH HOH A . 
G 7 HOH 236 636 166 HOH HOH A . 
G 7 HOH 237 637 48  HOH HOH A . 
G 7 HOH 238 638 296 HOH HOH A . 
G 7 HOH 239 639 234 HOH HOH A . 
G 7 HOH 240 640 202 HOH HOH A . 
G 7 HOH 241 641 79  HOH HOH A . 
G 7 HOH 242 642 231 HOH HOH A . 
G 7 HOH 243 643 293 HOH HOH A . 
G 7 HOH 244 644 281 HOH HOH A . 
G 7 HOH 245 645 114 HOH HOH A . 
G 7 HOH 246 646 273 HOH HOH A . 
G 7 HOH 247 647 217 HOH HOH A . 
G 7 HOH 248 648 192 HOH HOH A . 
G 7 HOH 249 649 271 HOH HOH A . 
G 7 HOH 250 650 246 HOH HOH A . 
G 7 HOH 251 651 250 HOH HOH A . 
G 7 HOH 252 652 154 HOH HOH A . 
G 7 HOH 253 653 170 HOH HOH A . 
G 7 HOH 254 654 233 HOH HOH A . 
G 7 HOH 255 655 268 HOH HOH A . 
G 7 HOH 256 656 222 HOH HOH A . 
G 7 HOH 257 657 58  HOH HOH A . 
G 7 HOH 258 658 55  HOH HOH A . 
G 7 HOH 259 659 270 HOH HOH A . 
G 7 HOH 260 660 125 HOH HOH A . 
G 7 HOH 261 661 139 HOH HOH A . 
G 7 HOH 262 662 210 HOH HOH A . 
G 7 HOH 263 663 225 HOH HOH A . 
G 7 HOH 264 664 185 HOH HOH A . 
G 7 HOH 265 665 146 HOH HOH A . 
G 7 HOH 266 666 238 HOH HOH A . 
G 7 HOH 267 667 277 HOH HOH A . 
G 7 HOH 268 668 284 HOH HOH A . 
G 7 HOH 269 669 255 HOH HOH A . 
G 7 HOH 270 670 71  HOH HOH A . 
G 7 HOH 271 671 260 HOH HOH A . 
G 7 HOH 272 672 259 HOH HOH A . 
G 7 HOH 273 673 172 HOH HOH A . 
G 7 HOH 274 674 173 HOH HOH A . 
G 7 HOH 275 675 174 HOH HOH A . 
G 7 HOH 276 676 214 HOH HOH A . 
G 7 HOH 277 677 163 HOH HOH A . 
G 7 HOH 278 678 137 HOH HOH A . 
G 7 HOH 279 679 197 HOH HOH A . 
G 7 HOH 280 680 147 HOH HOH A . 
G 7 HOH 281 681 294 HOH HOH A . 
G 7 HOH 282 682 22  HOH HOH A . 
G 7 HOH 283 683 177 HOH HOH A . 
G 7 HOH 284 684 169 HOH HOH A . 
G 7 HOH 285 685 237 HOH HOH A . 
G 7 HOH 286 686 265 HOH HOH A . 
G 7 HOH 287 687 178 HOH HOH A . 
G 7 HOH 288 688 193 HOH HOH A . 
G 7 HOH 289 689 171 HOH HOH A . 
G 7 HOH 290 690 212 HOH HOH A . 
G 7 HOH 291 691 145 HOH HOH A . 
G 7 HOH 292 692 219 HOH HOH A . 
G 7 HOH 293 693 118 HOH HOH A . 
G 7 HOH 294 694 135 HOH HOH A . 
G 7 HOH 295 695 115 HOH HOH A . 
G 7 HOH 296 696 264 HOH HOH A . 
G 7 HOH 297 697 251 HOH HOH A . 
G 7 HOH 298 698 98  HOH HOH A . 
G 7 HOH 299 699 176 HOH HOH A . 
G 7 HOH 300 700 175 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  ? NZ ? A LYS 45  NZ 
6  1 Y 1 A LYS 80  ? NZ ? A LYS 80  NZ 
7  1 Y 1 A LYS 158 ? CD ? A LYS 158 CD 
8  1 Y 1 A LYS 158 ? CE ? A LYS 158 CE 
9  1 Y 1 A LYS 158 ? NZ ? A LYS 158 NZ 
10 1 Y 1 A LYS 169 ? NZ ? A LYS 169 NZ 
11 1 Y 1 A LYS 256 ? CE ? A LYS 256 CE 
12 1 Y 1 A LYS 256 ? NZ ? A LYS 256 NZ 
13 1 Y 1 A LYS 260 ? CG ? A LYS 260 CG 
14 1 Y 1 A LYS 260 ? CD ? A LYS 260 CD 
15 1 Y 1 A LYS 260 ? CE ? A LYS 260 CE 
16 1 Y 1 A LYS 260 ? 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 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? SCALA       ? ? ? 3.3.22   1 
? refinement        ? ? ? ? ? ? ? ? ? ? ? REFMAC      ? ? ? 5.8.0232 2 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? 3.27     3 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? XDS         ? ? ? .        4 
? phasing           ? ? ? ? ? ? ? ? ? ? ? MOLREP      ? ? ? .        5 
? 'model building'  ? ? ? ? ? ? ? ? ? ? ? Coot        ? ? ? .        6 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   104.130 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     7NZX 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     42.159 
_cell.length_a_esd                 ? 
_cell.length_b                     41.334 
_cell.length_b_esd                 ? 
_cell.length_c                     71.548 
_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                         7NZX 
_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                   7NZX 
_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            2.06 
_exptl_crystal.density_method              ? 
_exptl_crystal.density_percent_sol         40.23 
_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              ? 
_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 was 0.1M sodium BICINE, pH 9, 0.2 M ammonium sulfate and 2M sodium malonate pH 7 made from 1M sodium BICINE and 3.4M sodium malonate
;
_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.pdbx_serial_crystal_experiment   N 
# 
_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_detector.pdbx_frequency               ? 
# 
_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   0.97630 
_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 P13 (MX1)' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97630 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   'P13 (MX1)' 
_diffrn_source.pdbx_synchrotron_site       'PETRA III, EMBL c/o DESY' 
# 
_reflns.B_iso_Wilson_estimate            ? 
_reflns.entry_id                         7NZX 
_reflns.data_reduction_details           ? 
_reflns.data_reduction_method            ? 
_reflns.d_resolution_high                1.328 
_reflns.d_resolution_low                 69.384 
_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                       53846 
_reflns.number_obs                       53846 
_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             97.300 
_reflns.R_free_details                   ? 
_reflns.Rmerge_F_all                     ? 
_reflns.Rmerge_F_obs                     ? 
_reflns.Friedel_coverage                 ? 
_reflns.number_gt                        ? 
_reflns.threshold_expression             ? 
_reflns.pdbx_redundancy                  6.600 
_reflns.pdbx_Rmerge_I_obs                ? 
_reflns.pdbx_Rmerge_I_all                ? 
_reflns.pdbx_Rsym_value                  0.046 
_reflns.pdbx_netI_over_av_sigmaI         6.000 
_reflns.pdbx_netI_over_sigmaI            20.400 
_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                  0.056 
_reflns.pdbx_Rpim_I_all                  0.021 
_reflns.pdbx_d_opt                       ? 
_reflns.pdbx_number_measured_all         357152 
_reflns.pdbx_diffrn_id                   1 
_reflns.pdbx_ordinal                     1 
_reflns.pdbx_CC_half                     ? 
_reflns.pdbx_CC_star                     ? 
_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_CC_star 
_reflns_shell.pdbx_R_split 
1.330 1.400  ? 3.400  39203 ? ? ? 6872 85.600 ? ? ? ? 0.217 ? ? ? ? ? ? ? ? 5.700 0.217 ? ? 6.500  0.263 0.107 ? 1  1 ? ? ? 
1.400 1.480  ? 4.500  51004 ? ? ? 7506 99.200 ? ? ? ? 0.164 ? ? ? ? ? ? ? ? 6.800 0.164 ? ? 9.100  0.196 0.074 ? 2  1 ? ? ? 
1.480 1.590  ? 6.400  46644 ? ? ? 7111 99.200 ? ? ? ? 0.112 ? ? ? ? ? ? ? ? 6.600 0.112 ? ? 12.000 0.137 0.053 ? 3  1 ? ? ? 
1.590 1.710  ? 8.400  45627 ? ? ? 6621 99.400 ? ? ? ? 0.084 ? ? ? ? ? ? ? ? 6.900 0.084 ? ? 15.900 0.104 0.039 ? 4  1 ? ? ? 
1.710 1.880  ? 10.800 40052 ? ? ? 6088 99.200 ? ? ? ? 0.063 ? ? ? ? ? ? ? ? 6.600 0.063 ? ? 20.200 0.078 0.030 ? 5  1 ? ? ? 
1.880 2.100  ? 13.800 38677 ? ? ? 5538 99.600 ? ? ? ? 0.047 ? ? ? ? ? ? ? ? 7.000 0.047 ? ? 27.500 0.059 0.022 ? 6  1 ? ? ? 
2.100 2.420  ? 15.200 32541 ? ? ? 4870 99.200 ? ? ? ? 0.041 ? ? ? ? ? ? ? ? 6.700 0.041 ? ? 31.900 0.051 0.020 ? 7  1 ? ? ? 
2.420 2.970  ? 15.800 29509 ? ? ? 4177 99.800 ? ? ? ? 0.038 ? ? ? ? ? ? ? ? 7.100 0.038 ? ? 36.700 0.047 0.017 ? 8  1 ? ? ? 
2.970 4.200  ? 13.400 21820 ? ? ? 3241 99.300 ? ? ? ? 0.038 ? ? ? ? ? ? ? ? 6.700 0.038 ? ? 41.000 0.045 0.017 ? 9  1 ? ? ? 
4.200 69.384 ? 10.500 12075 ? ? ? 1822 99.400 ? ? ? ? 0.043 ? ? ? ? ? ? ? ? 6.600 0.043 ? ? 41.600 0.051 0.020 ? 10 1 ? ? ? 
# 
_refine.aniso_B[1][1]                            -0.4900 
_refine.aniso_B[1][2]                            0.0000 
_refine.aniso_B[1][3]                            -0.1400 
_refine.aniso_B[2][2]                            0.3300 
_refine.aniso_B[2][3]                            0.0000 
_refine.aniso_B[3][3]                            0.2100 
_refine.B_iso_max                                117.790 
_refine.B_iso_mean                               19.6940 
_refine.B_iso_min                                7.370 
_refine.correlation_coeff_Fo_to_Fc               0.9790 
_refine.correlation_coeff_Fo_to_Fc_free          0.9690 
_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                                 7NZX 
_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                            1.3300 
_refine.ls_d_res_low                             69.3800 
_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                     48495 
_refine.ls_number_reflns_R_free                  5334 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    97.2500 
_refine.ls_percent_reflns_R_free                 9.9000 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1288 
_refine.ls_R_factor_R_free                       0.1703 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1242 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          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       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.0530 
_refine.pdbx_overall_ESU_R_Free                  0.0540 
_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             ? 
_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                         final 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.3300 
_refine_hist.d_res_low                        69.3800 
_refine_hist.number_atoms_solvent             300 
_refine_hist.number_atoms_total               2406 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       258 
_refine_hist.pdbx_B_iso_mean_ligand           29.17 
_refine_hist.pdbx_B_iso_mean_solvent          32.95 
_refine_hist.pdbx_number_atoms_protein        2049 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         57 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.017  0.012  2267 ? r_bond_refined_d       ? ? 
'X-RAY DIFFRACTION' ? 2.332  1.666  3108 ? r_angle_refined_deg    ? ? 
'X-RAY DIFFRACTION' ? 6.971  5.000  279  ? r_dihedral_angle_1_deg ? ? 
'X-RAY DIFFRACTION' ? 34.524 23.874 111  ? r_dihedral_angle_2_deg ? ? 
'X-RAY DIFFRACTION' ? 13.043 15.000 357  ? r_dihedral_angle_3_deg ? ? 
'X-RAY DIFFRACTION' ? 21.989 15.000 7    ? r_dihedral_angle_4_deg ? ? 
'X-RAY DIFFRACTION' ? 0.158  0.200  273  ? r_chiral_restr         ? ? 
'X-RAY DIFFRACTION' ? 0.015  0.020  1799 ? r_gen_planes_refined   ? ? 
'X-RAY DIFFRACTION' ? 7.255  3.000  2267 ? r_rigid_bond_restr     ? ? 
'X-RAY DIFFRACTION' ? 26.904 5.000  175  ? r_sphericity_free      ? ? 
'X-RAY DIFFRACTION' ? 16.598 5.000  2321 ? r_sphericity_bonded    ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.330 
_refine_ls_shell.d_res_low                        1.3630 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             336 
_refine_ls_shell.number_reflns_R_work             2683 
_refine_ls_shell.percent_reflns_obs               73.7600 
_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                  0.2040 
_refine_ls_shell.R_factor_R_free_error            0.0000 
_refine_ls_shell.R_factor_R_work                  0.1470 
_refine_ls_shell.redundancy_reflns_all            ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.wR_factor_all                    ? 
_refine_ls_shell.wR_factor_obs                    ? 
_refine_ls_shell.wR_factor_R_free                 ? 
_refine_ls_shell.wR_factor_R_work                 ? 
_refine_ls_shell.pdbx_R_complete                  ? 
_refine_ls_shell.pdbx_total_number_of_bins_used   ? 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
# 
_struct.entry_id                     7NZX 
_struct.title                        
'Crystal structure of chimeric carbonic anhydrase VA with 2,3,5,6-tetrafluoro-4-[(2-hydroxyethyl)sulfonyl]benzenesulfonamide' 
_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        7NZX 
_struct_keywords.text            
'drug design, carbonic anhydrase, benzenesulfonamide, metal-binding, lyase-lyase inhibitor complex, 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 ? 
G N N 7 ? 
# 
_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              7NZX 
_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       260 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 7NZX THR A 62  ? UNP P00918 ASN 62  'engineered mutation' 62  1 
1 7NZX TYR A 64  ? UNP P00918 HIS 64  'engineered mutation' 64  2 
1 7NZX LEU A 65  ? UNP P00918 ALA 65  'engineered mutation' 65  3 
1 7NZX GLN A 67  ? UNP P00918 ASN 67  'engineered mutation' 67  4 
1 7NZX LYS A 91  ? UNP P00918 ILE 91  'engineered mutation' 91  5 
1 7NZX TYR A 130 ? UNP P00918 PHE 130 'engineered mutation' 130 6 
1 7NZX THR A 203 ? UNP P00918 LEU 203 'engineered mutation' 203 7 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   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)' 620   ? 
1 MORE         -1    ? 
1 'SSA (A^2)'  11410 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G 
# 
_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 126 GLY A 128 5 ? 3 
HELX_P HELX_P4 AA4 ASP A 129 ? VAL A 134 ? ASP A 129 VAL A 134 1 ? 6 
HELX_P HELX_P5 AA5 LYS A 153 ? GLY A 155 ? LYS A 153 GLY A 155 5 ? 3 
HELX_P HELX_P6 AA6 LEU A 156 ? LEU A 163 ? LEU A 156 LEU A 163 1 ? 8 
HELX_P HELX_P7 AA7 ASP A 164 ? LYS A 167 ? ASP A 164 LYS A 167 5 ? 4 
HELX_P HELX_P8 AA8 ASP A 179 ? LEU A 184 ? ASP A 179 LEU A 184 5 ? 6 
HELX_P HELX_P9 AA9 SER A 218 ? ARG A 226 ? SER A 218 ARG A 226 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 SER 73  OG  ? ? ? 1_555 F NA  . NA  ? ? A SER 73  A NA  305 1_555 ? ? ? ? ? ? ? 2.213 ? ? 
metalc2  metalc ? ? A HIS 94  NE2 ? ? ? 1_555 B ZN  . ZN  ? ? A HIS 94  A ZN  301 1_555 ? ? ? ? ? ? ? 2.006 ? ? 
metalc3  metalc ? ? A HIS 96  NE2 ? ? ? 1_555 B ZN  . ZN  ? ? A HIS 96  A ZN  301 1_555 ? ? ? ? ? ? ? 2.006 ? ? 
metalc4  metalc ? ? A HIS 119 ND1 ? ? ? 1_555 B ZN  . ZN  ? ? A HIS 119 A ZN  301 1_555 ? ? ? ? ? ? ? 2.027 ? ? 
metalc5  metalc ? ? A SER 219 OG  ? ? ? 1_555 F NA  . NA  ? ? A SER 219 A NA  305 1_545 ? ? ? ? ? ? ? 2.473 ? ? 
metalc6  metalc ? ? B ZN  .   ZN  ? ? ? 1_555 C V13 . S7  B ? A ZN  301 A V13 302 1_555 ? ? ? ? ? ? ? 2.997 ? ? 
metalc7  metalc ? ? B ZN  .   ZN  ? ? ? 1_555 C V13 . N10 A ? A ZN  301 A V13 302 1_555 ? ? ? ? ? ? ? 1.920 ? ? 
metalc8  metalc ? ? B ZN  .   ZN  ? ? ? 1_555 C V13 . N10 B ? A ZN  301 A V13 302 1_555 ? ? ? ? ? ? ? 1.886 ? ? 
metalc9  metalc ? ? F NA  .   NA  ? ? ? 1_555 G HOH . O   ? ? A NA  305 A HOH 469 1_565 ? ? ? ? ? ? ? 2.123 ? ? 
metalc10 metalc ? ? F NA  .   NA  ? ? ? 1_555 G HOH . O   ? ? A NA  305 A HOH 488 1_555 ? ? ? ? ? ? ? 2.431 ? ? 
metalc11 metalc ? ? F NA  .   NA  ? ? ? 1_555 G HOH . O   ? ? A NA  305 A HOH 536 1_565 ? ? ? ? ? ? ? 2.562 ? ? 
metalc12 metalc ? ? F NA  .   NA  ? ? ? 1_555 G HOH . O   ? ? A NA  305 A HOH 614 1_555 ? ? ? ? ? ? ? 2.083 ? ? 
# 
_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  OG  ? A SER 73  ? A SER 73  ? 1_555 NA ? F NA . ? A NA 305 ? 1_555 OG  ? A SER 219 ? A SER 219 ? 1_555 39.3  ? 
2  OG  ? A SER 73  ? A SER 73  ? 1_555 NA ? F NA . ? A NA 305 ? 1_555 O   ? G HOH .   ? A HOH 469 ? 1_565 162.1 ? 
3  OG  ? A SER 219 ? A SER 219 ? 1_555 NA ? F NA . ? A NA 305 ? 1_555 O   ? G HOH .   ? A HOH 469 ? 1_565 129.0 ? 
4  OG  ? A SER 73  ? A SER 73  ? 1_555 NA ? F NA . ? A NA 305 ? 1_555 O   ? G HOH .   ? A HOH 488 ? 1_555 76.1  ? 
5  OG  ? A SER 219 ? A SER 219 ? 1_555 NA ? F NA . ? A NA 305 ? 1_555 O   ? G HOH .   ? A HOH 488 ? 1_555 45.2  ? 
6  O   ? G HOH .   ? A HOH 469 ? 1_565 NA ? F NA . ? A NA 305 ? 1_555 O   ? G HOH .   ? A HOH 488 ? 1_555 87.5  ? 
7  OG  ? A SER 73  ? A SER 73  ? 1_555 NA ? F NA . ? A NA 305 ? 1_555 O   ? G HOH .   ? A HOH 536 ? 1_565 97.7  ? 
8  OG  ? A SER 219 ? A SER 219 ? 1_555 NA ? F NA . ? A NA 305 ? 1_555 O   ? G HOH .   ? A HOH 536 ? 1_565 129.6 ? 
9  O   ? G HOH .   ? A HOH 469 ? 1_565 NA ? F NA . ? A NA 305 ? 1_555 O   ? G HOH .   ? A HOH 536 ? 1_565 83.2  ? 
10 O   ? G HOH .   ? A HOH 488 ? 1_555 NA ? F NA . ? A NA 305 ? 1_555 O   ? G HOH .   ? A HOH 536 ? 1_565 116.9 ? 
11 OG  ? A SER 73  ? A SER 73  ? 1_555 NA ? F NA . ? A NA 305 ? 1_555 O   ? G HOH .   ? A HOH 614 ? 1_555 90.0  ? 
12 OG  ? A SER 219 ? A SER 219 ? 1_555 NA ? F NA . ? A NA 305 ? 1_555 O   ? G HOH .   ? A HOH 614 ? 1_555 66.6  ? 
13 O   ? G HOH .   ? A HOH 469 ? 1_565 NA ? F NA . ? A NA 305 ? 1_555 O   ? G HOH .   ? A HOH 614 ? 1_555 95.4  ? 
14 O   ? G HOH .   ? A HOH 488 ? 1_555 NA ? F NA . ? A NA 305 ? 1_555 O   ? G HOH .   ? A HOH 614 ? 1_555 83.8  ? 
15 O   ? G HOH .   ? A HOH 536 ? 1_565 NA ? F NA . ? A NA 305 ? 1_555 O   ? G HOH .   ? A HOH 614 ? 1_555 159.1 ? 
16 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_555 104.2 ? 
17 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_555 109.9 ? 
18 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_555 101.3 ? 
19 NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 S7  B C V13 .   ? A V13 302 ? 1_555 96.1  ? 
20 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 S7  B C V13 .   ? A V13 302 ? 1_555 140.7 ? 
21 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 S7  B C V13 .   ? A V13 302 ? 1_555 102.8 ? 
22 NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N10 A C V13 .   ? A V13 302 ? 1_555 110.6 ? 
23 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N10 A C V13 .   ? A V13 302 ? 1_555 113.6 ? 
24 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N10 A C V13 .   ? A V13 302 ? 1_555 116.3 ? 
25 S7  B C V13 .   ? A V13 302 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N10 A C V13 .   ? A V13 302 ? 1_555 27.1  ? 
26 NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N10 B C V13 .   ? A V13 302 ? 1_555 116.4 ? 
27 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N10 B C V13 .   ? A V13 302 ? 1_555 113.1 ? 
28 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N10 B C V13 .   ? A V13 302 ? 1_555 110.7 ? 
29 S7  B C V13 .   ? A V13 302 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N10 B C V13 .   ? A V13 302 ? 1_555 28.4  ? 
30 N10 A C V13 .   ? A V13 302 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N10 B C V13 .   ? A V13 302 ? 1_555 6.4   ? 
# 
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 -1.92 
2 PRO 200 A . ? PRO 200 A PRO 201 A ? PRO 201 A 1 11.28 
# 
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 256 ALA A 257 
AA2 3  TYR A 190 ? GLY A 195 ? TYR A 190 GLY A 195 
AA2 4  VAL A 206 ? LEU A 211 ? VAL A 206 LEU A 211 
AA2 5  LEU A 140 ? VAL A 149 ? LEU A 140 VAL A 149 
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 172 ASP A 174 
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 140 VAL A 149 
AA3 6  ILE A 215 ? VAL A 217 ? ILE A 215 VAL A 217 
# 
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 257 
AA2 2 3  O LYS A 256 ? O LYS A 256 N THR A 192 ? N THR A 192 
AA2 3 4  N GLY A 195 ? N GLY A 195 O VAL A 206 ? O VAL A 206 
AA2 4 5  O ILE A 209 ? O ILE A 209 N GLY A 144 ? N GLY A 144 
AA2 5 6  O ILE A 145 ? O ILE A 145 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 LEU A 57  ? N LEU A 57  
AA2 9 10 N ILE A 59  ? N ILE A 59  O ALA A 173 ? O ALA A 173 
AA3 1 2  N SER A 50  ? N SER A 50  O VAL A 78  ? O VAL A 78  
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 145 
AA3 5 6  N PHE A 146 ? N PHE A 146 O ILE A 215 ? O ILE A 215 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   OH 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   TYR 
_pdbx_validate_close_contact.auth_seq_id_1    130 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   O19 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   V13 
_pdbx_validate_close_contact.auth_seq_id_2    302 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   A 
_pdbx_validate_close_contact.dist             2.13 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             C 
_pdbx_validate_rmsd_angle.auth_asym_id_1             A 
_pdbx_validate_rmsd_angle.auth_comp_id_1             PHE 
_pdbx_validate_rmsd_angle.auth_seq_id_1              259 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             N 
_pdbx_validate_rmsd_angle.auth_asym_id_2             A 
_pdbx_validate_rmsd_angle.auth_comp_id_2             LYS 
_pdbx_validate_rmsd_angle.auth_seq_id_2              260 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             CA 
_pdbx_validate_rmsd_angle.auth_asym_id_3             A 
_pdbx_validate_rmsd_angle.auth_comp_id_3             LYS 
_pdbx_validate_rmsd_angle.auth_seq_id_3              260 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                139.81 
_pdbx_validate_rmsd_angle.angle_target_value         121.70 
_pdbx_validate_rmsd_angle.angle_deviation            18.11 
_pdbx_validate_rmsd_angle.angle_standard_deviation   2.50 
_pdbx_validate_rmsd_angle.linker_flag                Y 
# 
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  ? ? -141.58 18.14   
2  1 ARG A 27  ? ? -140.97 51.16   
3  1 LEU A 65  ? ? -172.30 -176.24 
4  1 ASP A 75  ? B -67.79  97.76   
5  1 LYS A 76  ? ? -95.15  -81.37  
6  1 LYS A 76  ? ? -117.12 -81.37  
7  1 LYS A 111 ? ? 73.98   -2.24   
8  1 ASN A 243 ? ? -94.08  46.22   
9  1 LYS A 251 ? ? 56.86   -135.17 
10 1 ASN A 252 ? ? -96.90  58.52   
# 
_pdbx_entry_details.entry_id                 7NZX 
_pdbx_entry_details.has_ligand_of_interest   Y 
_pdbx_entry_details.compound_details         ? 
_pdbx_entry_details.source_details           ? 
_pdbx_entry_details.nonpolymer_details       ? 
_pdbx_entry_details.sequence_details         ? 
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      A 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       700 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   6.46 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A MET 1 ? A MET 1 
2 1 Y 1 A SER 2 ? A SER 2 
# 
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 
GLN N    N  N N 122 
GLN CA   C  N S 123 
GLN C    C  N N 124 
GLN O    O  N N 125 
GLN CB   C  N N 126 
GLN CG   C  N N 127 
GLN CD   C  N N 128 
GLN OE1  O  N N 129 
GLN NE2  N  N N 130 
GLN OXT  O  N N 131 
GLN H    H  N N 132 
GLN H2   H  N N 133 
GLN HA   H  N N 134 
GLN HB2  H  N N 135 
GLN HB3  H  N N 136 
GLN HG2  H  N N 137 
GLN HG3  H  N N 138 
GLN HE21 H  N N 139 
GLN HE22 H  N N 140 
GLN HXT  H  N N 141 
GLU N    N  N N 142 
GLU CA   C  N S 143 
GLU C    C  N N 144 
GLU O    O  N N 145 
GLU CB   C  N N 146 
GLU CG   C  N N 147 
GLU CD   C  N N 148 
GLU OE1  O  N N 149 
GLU OE2  O  N N 150 
GLU OXT  O  N N 151 
GLU H    H  N N 152 
GLU H2   H  N N 153 
GLU HA   H  N N 154 
GLU HB2  H  N N 155 
GLU HB3  H  N N 156 
GLU HG2  H  N N 157 
GLU HG3  H  N N 158 
GLU HE2  H  N N 159 
GLU HXT  H  N N 160 
GLY N    N  N N 161 
GLY CA   C  N N 162 
GLY C    C  N N 163 
GLY O    O  N N 164 
GLY OXT  O  N N 165 
GLY H    H  N N 166 
GLY H2   H  N N 167 
GLY HA2  H  N N 168 
GLY HA3  H  N N 169 
GLY HXT  H  N N 170 
HIS N    N  N N 171 
HIS CA   C  N S 172 
HIS C    C  N N 173 
HIS O    O  N N 174 
HIS CB   C  N N 175 
HIS CG   C  Y N 176 
HIS ND1  N  Y N 177 
HIS CD2  C  Y N 178 
HIS CE1  C  Y N 179 
HIS NE2  N  Y N 180 
HIS OXT  O  N N 181 
HIS H    H  N N 182 
HIS H2   H  N N 183 
HIS HA   H  N N 184 
HIS HB2  H  N N 185 
HIS HB3  H  N N 186 
HIS HD1  H  N N 187 
HIS HD2  H  N N 188 
HIS HE1  H  N N 189 
HIS HE2  H  N N 190 
HIS HXT  H  N N 191 
HOH O    O  N N 192 
HOH H1   H  N N 193 
HOH H2   H  N N 194 
ILE N    N  N N 195 
ILE CA   C  N S 196 
ILE C    C  N N 197 
ILE O    O  N N 198 
ILE CB   C  N S 199 
ILE CG1  C  N N 200 
ILE CG2  C  N N 201 
ILE CD1  C  N N 202 
ILE OXT  O  N N 203 
ILE H    H  N N 204 
ILE H2   H  N N 205 
ILE HA   H  N N 206 
ILE HB   H  N N 207 
ILE HG12 H  N N 208 
ILE HG13 H  N N 209 
ILE HG21 H  N N 210 
ILE HG22 H  N N 211 
ILE HG23 H  N N 212 
ILE HD11 H  N N 213 
ILE HD12 H  N N 214 
ILE HD13 H  N N 215 
ILE HXT  H  N N 216 
LEU N    N  N N 217 
LEU CA   C  N S 218 
LEU C    C  N N 219 
LEU O    O  N N 220 
LEU CB   C  N N 221 
LEU CG   C  N N 222 
LEU CD1  C  N N 223 
LEU CD2  C  N N 224 
LEU OXT  O  N N 225 
LEU H    H  N N 226 
LEU H2   H  N N 227 
LEU HA   H  N N 228 
LEU HB2  H  N N 229 
LEU HB3  H  N N 230 
LEU HG   H  N N 231 
LEU HD11 H  N N 232 
LEU HD12 H  N N 233 
LEU HD13 H  N N 234 
LEU HD21 H  N N 235 
LEU HD22 H  N N 236 
LEU HD23 H  N N 237 
LEU HXT  H  N N 238 
LYS N    N  N N 239 
LYS CA   C  N S 240 
LYS C    C  N N 241 
LYS O    O  N N 242 
LYS CB   C  N N 243 
LYS CG   C  N N 244 
LYS CD   C  N N 245 
LYS CE   C  N N 246 
LYS NZ   N  N N 247 
LYS OXT  O  N N 248 
LYS H    H  N N 249 
LYS H2   H  N N 250 
LYS HA   H  N N 251 
LYS HB2  H  N N 252 
LYS HB3  H  N N 253 
LYS HG2  H  N N 254 
LYS HG3  H  N N 255 
LYS HD2  H  N N 256 
LYS HD3  H  N N 257 
LYS HE2  H  N N 258 
LYS HE3  H  N N 259 
LYS HZ1  H  N N 260 
LYS HZ2  H  N N 261 
LYS HZ3  H  N N 262 
LYS HXT  H  N N 263 
MET N    N  N N 264 
MET CA   C  N S 265 
MET C    C  N N 266 
MET O    O  N N 267 
MET CB   C  N N 268 
MET CG   C  N N 269 
MET SD   S  N N 270 
MET CE   C  N N 271 
MET OXT  O  N N 272 
MET H    H  N N 273 
MET H2   H  N N 274 
MET HA   H  N N 275 
MET HB2  H  N N 276 
MET HB3  H  N N 277 
MET HG2  H  N N 278 
MET HG3  H  N N 279 
MET HE1  H  N N 280 
MET HE2  H  N N 281 
MET HE3  H  N N 282 
MET HXT  H  N N 283 
NA  NA   NA N N 284 
PHE N    N  N N 285 
PHE CA   C  N S 286 
PHE C    C  N N 287 
PHE O    O  N N 288 
PHE CB   C  N N 289 
PHE CG   C  Y N 290 
PHE CD1  C  Y N 291 
PHE CD2  C  Y N 292 
PHE CE1  C  Y N 293 
PHE CE2  C  Y N 294 
PHE CZ   C  Y N 295 
PHE OXT  O  N N 296 
PHE H    H  N N 297 
PHE H2   H  N N 298 
PHE HA   H  N N 299 
PHE HB2  H  N N 300 
PHE HB3  H  N N 301 
PHE HD1  H  N N 302 
PHE HD2  H  N N 303 
PHE HE1  H  N N 304 
PHE HE2  H  N N 305 
PHE HZ   H  N N 306 
PHE HXT  H  N N 307 
PRO N    N  N N 308 
PRO CA   C  N S 309 
PRO C    C  N N 310 
PRO O    O  N N 311 
PRO CB   C  N N 312 
PRO CG   C  N N 313 
PRO CD   C  N N 314 
PRO OXT  O  N N 315 
PRO H    H  N N 316 
PRO HA   H  N N 317 
PRO HB2  H  N N 318 
PRO HB3  H  N N 319 
PRO HG2  H  N N 320 
PRO HG3  H  N N 321 
PRO HD2  H  N N 322 
PRO HD3  H  N N 323 
PRO HXT  H  N N 324 
SER N    N  N N 325 
SER CA   C  N S 326 
SER C    C  N N 327 
SER O    O  N N 328 
SER CB   C  N N 329 
SER OG   O  N N 330 
SER OXT  O  N N 331 
SER H    H  N N 332 
SER H2   H  N N 333 
SER HA   H  N N 334 
SER HB2  H  N N 335 
SER HB3  H  N N 336 
SER HG   H  N N 337 
SER HXT  H  N N 338 
THR N    N  N N 339 
THR CA   C  N S 340 
THR C    C  N N 341 
THR O    O  N N 342 
THR CB   C  N R 343 
THR OG1  O  N N 344 
THR CG2  C  N N 345 
THR OXT  O  N N 346 
THR H    H  N N 347 
THR H2   H  N N 348 
THR HA   H  N N 349 
THR HB   H  N N 350 
THR HG1  H  N N 351 
THR HG21 H  N N 352 
THR HG22 H  N N 353 
THR HG23 H  N N 354 
THR HXT  H  N N 355 
TRP N    N  N N 356 
TRP CA   C  N S 357 
TRP C    C  N N 358 
TRP O    O  N N 359 
TRP CB   C  N N 360 
TRP CG   C  Y N 361 
TRP CD1  C  Y N 362 
TRP CD2  C  Y N 363 
TRP NE1  N  Y N 364 
TRP CE2  C  Y N 365 
TRP CE3  C  Y N 366 
TRP CZ2  C  Y N 367 
TRP CZ3  C  Y N 368 
TRP CH2  C  Y N 369 
TRP OXT  O  N N 370 
TRP H    H  N N 371 
TRP H2   H  N N 372 
TRP HA   H  N N 373 
TRP HB2  H  N N 374 
TRP HB3  H  N N 375 
TRP HD1  H  N N 376 
TRP HE1  H  N N 377 
TRP HE3  H  N N 378 
TRP HZ2  H  N N 379 
TRP HZ3  H  N N 380 
TRP HH2  H  N N 381 
TRP HXT  H  N N 382 
TYR N    N  N N 383 
TYR CA   C  N S 384 
TYR C    C  N N 385 
TYR O    O  N N 386 
TYR CB   C  N N 387 
TYR CG   C  Y N 388 
TYR CD1  C  Y N 389 
TYR CD2  C  Y N 390 
TYR CE1  C  Y N 391 
TYR CE2  C  Y N 392 
TYR CZ   C  Y N 393 
TYR OH   O  N N 394 
TYR OXT  O  N N 395 
TYR H    H  N N 396 
TYR H2   H  N N 397 
TYR HA   H  N N 398 
TYR HB2  H  N N 399 
TYR HB3  H  N N 400 
TYR HD1  H  N N 401 
TYR HD2  H  N N 402 
TYR HE1  H  N N 403 
TYR HE2  H  N N 404 
TYR HH   H  N N 405 
TYR HXT  H  N N 406 
V13 O20  O  N N 407 
V13 S15  S  N N 408 
V13 O19  O  N N 409 
V13 C16  C  N N 410 
V13 C17  C  N N 411 
V13 O18  O  N N 412 
V13 C1   C  Y N 413 
V13 C6   C  Y N 414 
V13 F11  F  N N 415 
V13 C5   C  Y N 416 
V13 F12  F  N N 417 
V13 C4   C  Y N 418 
V13 S7   S  N N 419 
V13 O9   O  N N 420 
V13 N10  N  N N 421 
V13 O8   O  N N 422 
V13 C3   C  Y N 423 
V13 F13  F  N N 424 
V13 C2   C  Y N 425 
V13 F14  F  N N 426 
V13 H1   H  N N 427 
V13 H2   H  N N 428 
V13 H3   H  N N 429 
V13 H4   H  N N 430 
V13 H5   H  N N 431 
V13 H6   H  N N 432 
V13 H7   H  N N 433 
VAL N    N  N N 434 
VAL CA   C  N S 435 
VAL C    C  N N 436 
VAL O    O  N N 437 
VAL CB   C  N N 438 
VAL CG1  C  N N 439 
VAL CG2  C  N N 440 
VAL OXT  O  N N 441 
VAL H    H  N N 442 
VAL H2   H  N N 443 
VAL HA   H  N N 444 
VAL HB   H  N N 445 
VAL HG11 H  N N 446 
VAL HG12 H  N N 447 
VAL HG13 H  N N 448 
VAL HG21 H  N N 449 
VAL HG22 H  N N 450 
VAL HG23 H  N N 451 
VAL HXT  H  N N 452 
ZN  ZN   ZN N N 453 
# 
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 
GLN N   CA   sing N N 115 
GLN N   H    sing N N 116 
GLN N   H2   sing N N 117 
GLN CA  C    sing N N 118 
GLN CA  CB   sing N N 119 
GLN CA  HA   sing N N 120 
GLN C   O    doub N N 121 
GLN C   OXT  sing N N 122 
GLN CB  CG   sing N N 123 
GLN CB  HB2  sing N N 124 
GLN CB  HB3  sing N N 125 
GLN CG  CD   sing N N 126 
GLN CG  HG2  sing N N 127 
GLN CG  HG3  sing N N 128 
GLN CD  OE1  doub N N 129 
GLN CD  NE2  sing N N 130 
GLN NE2 HE21 sing N N 131 
GLN NE2 HE22 sing N N 132 
GLN OXT HXT  sing N N 133 
GLU N   CA   sing N N 134 
GLU N   H    sing N N 135 
GLU N   H2   sing N N 136 
GLU CA  C    sing N N 137 
GLU CA  CB   sing N N 138 
GLU CA  HA   sing N N 139 
GLU C   O    doub N N 140 
GLU C   OXT  sing N N 141 
GLU CB  CG   sing N N 142 
GLU CB  HB2  sing N N 143 
GLU CB  HB3  sing N N 144 
GLU CG  CD   sing N N 145 
GLU CG  HG2  sing N N 146 
GLU CG  HG3  sing N N 147 
GLU CD  OE1  doub N N 148 
GLU CD  OE2  sing N N 149 
GLU OE2 HE2  sing N N 150 
GLU OXT HXT  sing N N 151 
GLY N   CA   sing N N 152 
GLY N   H    sing N N 153 
GLY N   H2   sing N N 154 
GLY CA  C    sing N N 155 
GLY CA  HA2  sing N N 156 
GLY CA  HA3  sing N N 157 
GLY C   O    doub N N 158 
GLY C   OXT  sing N N 159 
GLY OXT HXT  sing N N 160 
HIS N   CA   sing N N 161 
HIS N   H    sing N N 162 
HIS N   H2   sing N N 163 
HIS CA  C    sing N N 164 
HIS CA  CB   sing N N 165 
HIS CA  HA   sing N N 166 
HIS C   O    doub N N 167 
HIS C   OXT  sing N N 168 
HIS CB  CG   sing N N 169 
HIS CB  HB2  sing N N 170 
HIS CB  HB3  sing N N 171 
HIS CG  ND1  sing Y N 172 
HIS CG  CD2  doub Y N 173 
HIS ND1 CE1  doub Y N 174 
HIS ND1 HD1  sing N N 175 
HIS CD2 NE2  sing Y N 176 
HIS CD2 HD2  sing N N 177 
HIS CE1 NE2  sing Y N 178 
HIS CE1 HE1  sing N N 179 
HIS NE2 HE2  sing N N 180 
HIS OXT HXT  sing N N 181 
HOH O   H1   sing N N 182 
HOH O   H2   sing N N 183 
ILE N   CA   sing N N 184 
ILE N   H    sing N N 185 
ILE N   H2   sing N N 186 
ILE CA  C    sing N N 187 
ILE CA  CB   sing N N 188 
ILE CA  HA   sing N N 189 
ILE C   O    doub N N 190 
ILE C   OXT  sing N N 191 
ILE CB  CG1  sing N N 192 
ILE CB  CG2  sing N N 193 
ILE CB  HB   sing N N 194 
ILE CG1 CD1  sing N N 195 
ILE CG1 HG12 sing N N 196 
ILE CG1 HG13 sing N N 197 
ILE CG2 HG21 sing N N 198 
ILE CG2 HG22 sing N N 199 
ILE CG2 HG23 sing N N 200 
ILE CD1 HD11 sing N N 201 
ILE CD1 HD12 sing N N 202 
ILE CD1 HD13 sing N N 203 
ILE OXT HXT  sing N N 204 
LEU N   CA   sing N N 205 
LEU N   H    sing N N 206 
LEU N   H2   sing N N 207 
LEU CA  C    sing N N 208 
LEU CA  CB   sing N N 209 
LEU CA  HA   sing N N 210 
LEU C   O    doub N N 211 
LEU C   OXT  sing N N 212 
LEU CB  CG   sing N N 213 
LEU CB  HB2  sing N N 214 
LEU CB  HB3  sing N N 215 
LEU CG  CD1  sing N N 216 
LEU CG  CD2  sing N N 217 
LEU CG  HG   sing N N 218 
LEU CD1 HD11 sing N N 219 
LEU CD1 HD12 sing N N 220 
LEU CD1 HD13 sing N N 221 
LEU CD2 HD21 sing N N 222 
LEU CD2 HD22 sing N N 223 
LEU CD2 HD23 sing N N 224 
LEU OXT HXT  sing N N 225 
LYS N   CA   sing N N 226 
LYS N   H    sing N N 227 
LYS N   H2   sing N N 228 
LYS CA  C    sing N N 229 
LYS CA  CB   sing N N 230 
LYS CA  HA   sing N N 231 
LYS C   O    doub N N 232 
LYS C   OXT  sing N N 233 
LYS CB  CG   sing N N 234 
LYS CB  HB2  sing N N 235 
LYS CB  HB3  sing N N 236 
LYS CG  CD   sing N N 237 
LYS CG  HG2  sing N N 238 
LYS CG  HG3  sing N N 239 
LYS CD  CE   sing N N 240 
LYS CD  HD2  sing N N 241 
LYS CD  HD3  sing N N 242 
LYS CE  NZ   sing N N 243 
LYS CE  HE2  sing N N 244 
LYS CE  HE3  sing N N 245 
LYS NZ  HZ1  sing N N 246 
LYS NZ  HZ2  sing N N 247 
LYS NZ  HZ3  sing N N 248 
LYS OXT HXT  sing N N 249 
MET N   CA   sing N N 250 
MET N   H    sing N N 251 
MET N   H2   sing N N 252 
MET CA  C    sing N N 253 
MET CA  CB   sing N N 254 
MET CA  HA   sing N N 255 
MET C   O    doub N N 256 
MET C   OXT  sing N N 257 
MET CB  CG   sing N N 258 
MET CB  HB2  sing N N 259 
MET CB  HB3  sing N N 260 
MET CG  SD   sing N N 261 
MET CG  HG2  sing N N 262 
MET CG  HG3  sing N N 263 
MET SD  CE   sing N N 264 
MET CE  HE1  sing N N 265 
MET CE  HE2  sing N N 266 
MET CE  HE3  sing N N 267 
MET OXT HXT  sing N N 268 
PHE N   CA   sing N N 269 
PHE N   H    sing N N 270 
PHE N   H2   sing N N 271 
PHE CA  C    sing N N 272 
PHE CA  CB   sing N N 273 
PHE CA  HA   sing N N 274 
PHE C   O    doub N N 275 
PHE C   OXT  sing N N 276 
PHE CB  CG   sing N N 277 
PHE CB  HB2  sing N N 278 
PHE CB  HB3  sing N N 279 
PHE CG  CD1  doub Y N 280 
PHE CG  CD2  sing Y N 281 
PHE CD1 CE1  sing Y N 282 
PHE CD1 HD1  sing N N 283 
PHE CD2 CE2  doub Y N 284 
PHE CD2 HD2  sing N N 285 
PHE CE1 CZ   doub Y N 286 
PHE CE1 HE1  sing N N 287 
PHE CE2 CZ   sing Y N 288 
PHE CE2 HE2  sing N N 289 
PHE CZ  HZ   sing N N 290 
PHE OXT HXT  sing N N 291 
PRO N   CA   sing N N 292 
PRO N   CD   sing N N 293 
PRO N   H    sing N N 294 
PRO CA  C    sing N N 295 
PRO CA  CB   sing N N 296 
PRO CA  HA   sing N N 297 
PRO C   O    doub N N 298 
PRO C   OXT  sing N N 299 
PRO CB  CG   sing N N 300 
PRO CB  HB2  sing N N 301 
PRO CB  HB3  sing N N 302 
PRO CG  CD   sing N N 303 
PRO CG  HG2  sing N N 304 
PRO CG  HG3  sing N N 305 
PRO CD  HD2  sing N N 306 
PRO CD  HD3  sing N N 307 
PRO OXT HXT  sing N N 308 
SER N   CA   sing N N 309 
SER N   H    sing N N 310 
SER N   H2   sing N N 311 
SER CA  C    sing N N 312 
SER CA  CB   sing N N 313 
SER CA  HA   sing N N 314 
SER C   O    doub N N 315 
SER C   OXT  sing N N 316 
SER CB  OG   sing N N 317 
SER CB  HB2  sing N N 318 
SER CB  HB3  sing N N 319 
SER OG  HG   sing N N 320 
SER OXT HXT  sing N N 321 
THR N   CA   sing N N 322 
THR N   H    sing N N 323 
THR N   H2   sing N N 324 
THR CA  C    sing N N 325 
THR CA  CB   sing N N 326 
THR CA  HA   sing N N 327 
THR C   O    doub N N 328 
THR C   OXT  sing N N 329 
THR CB  OG1  sing N N 330 
THR CB  CG2  sing N N 331 
THR CB  HB   sing N N 332 
THR OG1 HG1  sing N N 333 
THR CG2 HG21 sing N N 334 
THR CG2 HG22 sing N N 335 
THR CG2 HG23 sing N N 336 
THR OXT HXT  sing N N 337 
TRP N   CA   sing N N 338 
TRP N   H    sing N N 339 
TRP N   H2   sing N N 340 
TRP CA  C    sing N N 341 
TRP CA  CB   sing N N 342 
TRP CA  HA   sing N N 343 
TRP C   O    doub N N 344 
TRP C   OXT  sing N N 345 
TRP CB  CG   sing N N 346 
TRP CB  HB2  sing N N 347 
TRP CB  HB3  sing N N 348 
TRP CG  CD1  doub Y N 349 
TRP CG  CD2  sing Y N 350 
TRP CD1 NE1  sing Y N 351 
TRP CD1 HD1  sing N N 352 
TRP CD2 CE2  doub Y N 353 
TRP CD2 CE3  sing Y N 354 
TRP NE1 CE2  sing Y N 355 
TRP NE1 HE1  sing N N 356 
TRP CE2 CZ2  sing Y N 357 
TRP CE3 CZ3  doub Y N 358 
TRP CE3 HE3  sing N N 359 
TRP CZ2 CH2  doub Y N 360 
TRP CZ2 HZ2  sing N N 361 
TRP CZ3 CH2  sing Y N 362 
TRP CZ3 HZ3  sing N N 363 
TRP CH2 HH2  sing N N 364 
TRP OXT HXT  sing N N 365 
TYR N   CA   sing N N 366 
TYR N   H    sing N N 367 
TYR N   H2   sing N N 368 
TYR CA  C    sing N N 369 
TYR CA  CB   sing N N 370 
TYR CA  HA   sing N N 371 
TYR C   O    doub N N 372 
TYR C   OXT  sing N N 373 
TYR CB  CG   sing N N 374 
TYR CB  HB2  sing N N 375 
TYR CB  HB3  sing N N 376 
TYR CG  CD1  doub Y N 377 
TYR CG  CD2  sing Y N 378 
TYR CD1 CE1  sing Y N 379 
TYR CD1 HD1  sing N N 380 
TYR CD2 CE2  doub Y N 381 
TYR CD2 HD2  sing N N 382 
TYR CE1 CZ   doub Y N 383 
TYR CE1 HE1  sing N N 384 
TYR CE2 CZ   sing Y N 385 
TYR CE2 HE2  sing N N 386 
TYR CZ  OH   sing N N 387 
TYR OH  HH   sing N N 388 
TYR OXT HXT  sing N N 389 
V13 C17 C16  sing N N 390 
V13 C17 O18  sing N N 391 
V13 F11 C6   sing N N 392 
V13 O20 S15  doub N N 393 
V13 C16 S15  sing N N 394 
V13 S15 C1   sing N N 395 
V13 S15 O19  doub N N 396 
V13 F12 C5   sing N N 397 
V13 C6  C5   doub Y N 398 
V13 C6  C1   sing Y N 399 
V13 C5  C4   sing Y N 400 
V13 C1  C2   doub Y N 401 
V13 C2  F14  sing N N 402 
V13 C2  C3   sing Y N 403 
V13 C4  C3   doub Y N 404 
V13 C4  S7   sing N N 405 
V13 O8  S7   doub N N 406 
V13 O9  S7   doub N N 407 
V13 C3  F13  sing N N 408 
V13 S7  N10  sing N N 409 
V13 C16 H1   sing N N 410 
V13 C16 H2   sing N N 411 
V13 C17 H3   sing N N 412 
V13 C17 H4   sing N N 413 
V13 O18 H5   sing N N 414 
V13 N10 H6   sing N N 415 
V13 N10 H7   sing N N 416 
VAL N   CA   sing N N 417 
VAL N   H    sing N N 418 
VAL N   H2   sing N N 419 
VAL CA  C    sing N N 420 
VAL CA  CB   sing N N 421 
VAL CA  HA   sing N N 422 
VAL C   O    doub N N 423 
VAL C   OXT  sing N N 424 
VAL CB  CG1  sing N N 425 
VAL CB  CG2  sing N N 426 
VAL CB  HB   sing N N 427 
VAL CG1 HG11 sing N N 428 
VAL CG1 HG12 sing N N 429 
VAL CG1 HG13 sing N N 430 
VAL CG2 HG21 sing N N 431 
VAL CG2 HG22 sing N N 432 
VAL CG2 HG23 sing N N 433 
VAL OXT HXT  sing N N 434 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        V13 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   V13 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
_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                    7NZX 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.fract_transf_matrix[1][1]   0.023720 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.005970 
_atom_sites.fract_transf_matrix[2][1]   -0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.024193 
_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]   0.014413 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
F  
N  
NA 
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   . HIS A 1 3   ? 34.714  1.603   6.478   1.00 37.40  ? 3   HIS A N   1 
ATOM   2    C  CA  . HIS A 1 3   ? 34.455  0.646   7.659   1.00 47.82  ? 3   HIS A CA  1 
ATOM   3    C  C   . HIS A 1 3   ? 33.463  1.301   8.619   1.00 47.43  ? 3   HIS A C   1 
ATOM   4    O  O   . HIS A 1 3   ? 33.802  1.576   9.791   1.00 48.61  ? 3   HIS A O   1 
ATOM   5    C  CB  . HIS A 1 3   ? 35.759  0.212   8.360   1.00 41.78  ? 3   HIS A CB  1 
ATOM   6    C  CG  . HIS A 1 3   ? 35.603  -1.021  9.191   1.00 34.81  ? 3   HIS A CG  1 
ATOM   7    N  ND1 . HIS A 1 3   ? 35.323  -0.973  10.578  1.00 36.57  ? 3   HIS A ND1 1 
ATOM   8    C  CD2 . HIS A 1 3   ? 35.708  -2.339  8.868   1.00 36.29  ? 3   HIS A CD2 1 
ATOM   9    C  CE1 . HIS A 1 3   ? 35.277  -2.215  11.050  1.00 36.18  ? 3   HIS A CE1 1 
ATOM   10   N  NE2 . HIS A 1 3   ? 35.508  -3.077  10.022  1.00 39.86  ? 3   HIS A NE2 1 
ATOM   11   N  N   . HIS A 1 4   ? 32.273  1.572   8.050   1.00 63.87  ? 4   HIS A N   1 
ATOM   12   C  CA  . HIS A 1 4   ? 31.123  2.053   8.801   1.00 47.17  ? 4   HIS A CA  1 
ATOM   13   C  C   . HIS A 1 4   ? 30.586  0.885   9.632   1.00 41.78  ? 4   HIS A C   1 
ATOM   14   O  O   . HIS A 1 4   ? 30.883  -0.275  9.416   1.00 28.96  ? 4   HIS A O   1 
ATOM   15   C  CB  . HIS A 1 4   ? 30.020  2.708   7.869   1.00 57.05  ? 4   HIS A CB  1 
ATOM   16   C  CG  . HIS A 1 4   ? 29.544  4.065   8.482   1.00 86.69  ? 4   HIS A CG  1 
ATOM   17   N  ND1 . HIS A 1 4   ? 28.240  4.507   8.374   1.00 98.19  ? 4   HIS A ND1 1 
ATOM   18   C  CD2 . HIS A 1 4   ? 30.209  5.012   9.178   1.00 96.91  ? 4   HIS A CD2 1 
ATOM   19   C  CE1 . HIS A 1 4   ? 28.121  5.672   8.978   1.00 117.79 ? 4   HIS A CE1 1 
ATOM   20   N  NE2 . HIS A 1 4   ? 29.316  6.004   9.480   1.00 105.09 ? 4   HIS A NE2 1 
ATOM   21   N  N   . TRP A 1 5   ? 29.714  1.208   10.544  1.00 21.86  ? 5   TRP A N   1 
ATOM   22   C  CA  . TRP A 1 5   ? 29.032  0.215   11.354  1.00 18.59  ? 5   TRP A CA  1 
ATOM   23   C  C   . TRP A 1 5   ? 28.054  -0.615  10.537  1.00 21.24  ? 5   TRP A C   1 
ATOM   24   O  O   . TRP A 1 5   ? 27.542  -0.163  9.508   1.00 19.32  ? 5   TRP A O   1 
ATOM   25   C  CB  . TRP A 1 5   ? 28.285  0.891   12.498  1.00 16.48  ? 5   TRP A CB  1 
ATOM   26   C  CG  . TRP A 1 5   ? 27.106  1.739   12.095  1.00 16.23  ? 5   TRP A CG  1 
ATOM   27   C  CD1 . TRP A 1 5   ? 27.116  3.054   11.725  1.00 21.33  ? 5   TRP A CD1 1 
ATOM   28   C  CD2 . TRP A 1 5   ? 25.744  1.317   12.033  1.00 14.80  ? 5   TRP A CD2 1 
ATOM   29   N  NE1 . TRP A 1 5   ? 25.852  3.482   11.417  1.00 20.64  ? 5   TRP A NE1 1 
ATOM   30   C  CE2 . TRP A 1 5   ? 24.990  2.431   11.588  1.00 15.83  ? 5   TRP A CE2 1 
ATOM   31   C  CE3 . TRP A 1 5   ? 25.133  0.075   12.282  1.00 15.71  ? 5   TRP A CE3 1 
ATOM   32   C  CZ2 . TRP A 1 5   ? 23.598  2.360   11.520  1.00 20.74  ? 5   TRP A CZ2 1 
ATOM   33   C  CZ3 . TRP A 1 5   ? 23.751  -0.014  12.139  1.00 18.94  ? 5   TRP A CZ3 1 
ATOM   34   C  CH2 . TRP A 1 5   ? 23.005  1.120   11.739  1.00 18.38  ? 5   TRP A CH2 1 
ATOM   35   N  N   . GLY A 1 6   ? 27.745  -1.804  11.036  1.00 18.08  ? 6   GLY A N   1 
ATOM   36   C  CA  . GLY A 1 6   ? 26.671  -2.596  10.426  1.00 19.04  ? 6   GLY A CA  1 
ATOM   37   C  C   . GLY A 1 6   ? 26.316  -3.757  11.344  1.00 19.32  ? 6   GLY A C   1 
ATOM   38   O  O   . GLY A 1 6   ? 26.332  -3.576  12.564  1.00 19.30  ? 6   GLY A O   1 
ATOM   39   N  N   . TYR A 1 7   ? 25.983  -4.913  10.759  1.00 21.37  ? 7   TYR A N   1 
ATOM   40   C  CA  . TYR A 1 7   ? 25.561  -6.073  11.532  1.00 24.43  ? 7   TYR A CA  1 
ATOM   41   C  C   . TYR A 1 7   ? 26.577  -7.239  11.591  1.00 31.49  ? 7   TYR A C   1 
ATOM   42   O  O   . TYR A 1 7   ? 26.372  -8.230  12.367  1.00 27.99  ? 7   TYR A O   1 
ATOM   43   C  CB  . TYR A 1 7   ? 24.063  -6.369  11.282  1.00 20.84  ? 7   TYR A CB  1 
ATOM   44   C  CG  . TYR A 1 7   ? 23.190  -5.232  11.793  1.00 14.68  ? 7   TYR A CG  1 
ATOM   45   C  CD1 . TYR A 1 7   ? 22.767  -5.237  13.110  1.00 13.85  ? 7   TYR A CD1 1 
ATOM   46   C  CD2 . TYR A 1 7   ? 22.740  -4.222  10.961  1.00 15.50  ? 7   TYR A CD2 1 
ATOM   47   C  CE1 . TYR A 1 7   ? 21.949  -4.243  13.608  1.00 13.38  ? 7   TYR A CE1 1 
ATOM   48   C  CE2 . TYR A 1 7   ? 21.920  -3.216  11.443  1.00 13.17  ? 7   TYR A CE2 1 
ATOM   49   C  CZ  . TYR A 1 7   ? 21.527  -3.231  12.769  1.00 11.99  ? 7   TYR A CZ  1 
ATOM   50   O  OH  . TYR A 1 7   ? 20.718  -2.263  13.271  1.00 13.29  ? 7   TYR A OH  1 
ATOM   51   N  N   . GLY A 1 8   ? 27.702  -7.166  10.829  1.00 32.59  ? 8   GLY A N   1 
ATOM   52   C  CA  . GLY A 1 8   ? 28.634  -8.326  10.693  1.00 26.71  ? 8   GLY A CA  1 
ATOM   53   C  C   . GLY A 1 8   ? 29.664  -8.557  11.815  1.00 28.63  ? 8   GLY A C   1 
ATOM   54   O  O   . GLY A 1 8   ? 29.780  -7.851  12.872  1.00 29.56  ? 8   GLY A O   1 
ATOM   55   N  N   . LYS A 1 9   ? 30.474  -9.635  11.653  1.00 31.39  ? 9   LYS A N   1 
ATOM   56   C  CA  . LYS A 1 9   ? 31.475  -9.997  12.660  1.00 37.49  ? 9   LYS A CA  1 
ATOM   57   C  C   . LYS A 1 9   ? 32.391  -8.802  12.890  1.00 32.80  ? 9   LYS A C   1 
ATOM   58   O  O   . LYS A 1 9   ? 32.920  -8.640  14.002  1.00 34.92  ? 9   LYS A O   1 
ATOM   59   C  CB  . LYS A 1 9   ? 32.447  -11.094 12.225  1.00 37.76  ? 9   LYS A CB  1 
ATOM   60   N  N   . HIS A 1 10  ? 32.480  -7.890  11.794  1.00 47.86  ? 10  HIS A N   1 
ATOM   61   C  CA  . HIS A 1 10  ? 33.692  -7.078  11.794  1.00 50.72  ? 10  HIS A CA  1 
ATOM   62   C  C   . HIS A 1 10  ? 33.179  -5.684  12.075  1.00 31.79  ? 10  HIS A C   1 
ATOM   63   O  O   . HIS A 1 10  ? 33.982  -4.904  12.527  1.00 26.83  ? 10  HIS A O   1 
ATOM   64   C  CB  . HIS A 1 10  ? 34.640  -7.129  10.465  1.00 52.27  ? 10  HIS A CB  1 
ATOM   65   C  CG  . HIS A 1 10  ? 34.943  -8.450  10.017  1.00 69.33  ? 10  HIS A CG  1 
ATOM   66   N  ND1 . HIS A 1 10  ? 35.985  -9.188  10.545  1.00 107.96 ? 10  HIS A ND1 1 
ATOM   67   C  CD2 . HIS A 1 10  ? 34.365  -9.229  9.078   1.00 111.94 ? 10  HIS A CD2 1 
ATOM   68   C  CE1 . HIS A 1 10  ? 36.035  -10.363 9.950   1.00 91.38  ? 10  HIS A CE1 1 
ATOM   69   N  NE2 . HIS A 1 10  ? 35.050  -10.413 9.046   1.00 110.53 ? 10  HIS A NE2 1 
ATOM   70   N  N   . ASN A 1 11  ? 31.840  -5.481  11.942  1.00 27.72  ? 11  ASN A N   1 
ATOM   71   C  CA  . ASN A 1 11  ? 31.403  -4.121  12.217  1.00 19.66  ? 11  ASN A CA  1 
ATOM   72   C  C   . ASN A 1 11  ? 30.048  -4.112  12.967  1.00 21.89  ? 11  ASN A C   1 
ATOM   73   O  O   . ASN A 1 11  ? 29.406  -3.068  13.065  1.00 20.59  ? 11  ASN A O   1 
ATOM   74   C  CB  . ASN A 1 11  ? 31.219  -3.330  10.919  1.00 17.90  ? 11  ASN A CB  1 
ATOM   75   C  CG  . ASN A 1 11  ? 30.147  -3.914  10.021  1.00 21.60  ? 11  ASN A CG  1 
ATOM   76   O  OD1 . ASN A 1 11  ? 29.479  -4.908  10.382  1.00 24.83  ? 11  ASN A OD1 1 
ATOM   77   N  ND2 . ASN A 1 11  ? 29.912  -3.278  8.872   1.00 25.71  ? 11  ASN A ND2 1 
ATOM   78   N  N   . GLY A 1 12  ? 29.661  -5.241  13.575  1.00 20.42  ? 12  GLY A N   1 
ATOM   79   C  CA  . GLY A 1 12  ? 28.356  -5.422  14.211  1.00 18.16  ? 12  GLY A CA  1 
ATOM   80   C  C   . GLY A 1 12  ? 28.334  -4.835  15.615  1.00 17.63  ? 12  GLY A C   1 
ATOM   81   O  O   . GLY A 1 12  ? 29.233  -4.118  16.072  1.00 17.76  ? 12  GLY A O   1 
ATOM   82   N  N   . PRO A 1 13  ? 27.236  -5.131  16.341  1.00 15.23  ? 13  PRO A N   1 
ATOM   83   C  CA  . PRO A 1 13  ? 26.990  -4.527  17.645  1.00 14.98  ? 13  PRO A CA  1 
ATOM   84   C  C   . PRO A 1 13  ? 28.134  -4.532  18.631  1.00 15.11  ? 13  PRO A C   1 
ATOM   85   O  O   . PRO A 1 13  ? 28.261  -3.567  19.377  1.00 15.84  ? 13  PRO A O   1 
ATOM   86   C  CB  . PRO A 1 13  ? 25.796  -5.314  18.161  1.00 16.58  ? 13  PRO A CB  1 
ATOM   87   C  CG  . PRO A 1 13  ? 24.992  -5.592  16.887  1.00 16.46  ? 13  PRO A CG  1 
ATOM   88   C  CD  . PRO A 1 13  ? 26.074  -5.872  15.834  1.00 16.22  ? 13  PRO A CD  1 
ATOM   89   N  N   . GLU A 1 14  ? 28.983  -5.555  18.617  1.00 16.34  ? 14  GLU A N   1 
ATOM   90   C  CA  . GLU A 1 14  ? 30.036  -5.645  19.609  1.00 18.49  ? 14  GLU A CA  1 
ATOM   91   C  C   . GLU A 1 14  ? 31.150  -4.654  19.267  1.00 17.00  ? 14  GLU A C   1 
ATOM   92   O  O   . GLU A 1 14  ? 32.061  -4.473  20.085  1.00 19.17  ? 14  GLU A O   1 
ATOM   93   C  CB  . GLU A 1 14  ? 30.528  -7.090  19.662  1.00 24.87  ? 14  GLU A CB  1 
ATOM   94   C  CG  . GLU A 1 14  ? 31.083  -7.576  18.309  1.00 26.74  ? 14  GLU A CG  1 
ATOM   95   C  CD  . GLU A 1 14  ? 30.347  -8.155  17.087  1.00 30.22  ? 14  GLU A CD  1 
ATOM   96   O  OE1 . GLU A 1 14  ? 29.180  -7.774  16.867  1.00 24.07  ? 14  GLU A OE1 1 
ATOM   97   O  OE2 . GLU A 1 14  ? 30.950  -8.980  16.372  1.00 32.12  ? 14  GLU A OE2 1 
ATOM   98   N  N   . HIS A 1 15  ? 31.131  -4.081  18.047  1.00 16.63  ? 15  HIS A N   1 
ATOM   99   C  CA  . HIS A 1 15  ? 32.140  -3.089  17.687  1.00 16.57  ? 15  HIS A CA  1 
ATOM   100  C  C   . HIS A 1 15  ? 31.680  -1.640  17.831  1.00 14.92  ? 15  HIS A C   1 
ATOM   101  O  O   . HIS A 1 15  ? 32.514  -0.717  17.805  1.00 16.72  ? 15  HIS A O   1 
ATOM   102  C  CB  . HIS A 1 15  ? 32.533  -3.265  16.224  1.00 16.13  ? 15  HIS A CB  1 
ATOM   103  C  CG  . HIS A 1 15  ? 33.234  -4.541  15.966  1.00 18.04  ? 15  HIS A CG  1 
ATOM   104  N  ND1 . HIS A 1 15  ? 34.600  -4.636  16.104  1.00 22.39  ? 15  HIS A ND1 1 
ATOM   105  C  CD2 . HIS A 1 15  ? 32.748  -5.745  15.612  1.00 18.91  ? 15  HIS A CD2 1 
ATOM   106  C  CE1 . HIS A 1 15  ? 34.954  -5.880  15.868  1.00 23.96  ? 15  HIS A CE1 1 
ATOM   107  N  NE2 . HIS A 1 15  ? 33.865  -6.589  15.561  1.00 25.59  ? 15  HIS A NE2 1 
ATOM   108  N  N   . TRP A 1 16  ? 30.375  -1.378  17.968  1.00 14.97  ? 16  TRP A N   1 
ATOM   109  C  CA  . TRP A 1 16  ? 29.879  -0.016  17.861  1.00 13.49  ? 16  TRP A CA  1 
ATOM   110  C  C   . TRP A 1 16  ? 30.435  0.925   18.928  1.00 14.16  ? 16  TRP A C   1 
ATOM   111  O  O   . TRP A 1 16  ? 30.567  2.118   18.703  1.00 14.77  ? 16  TRP A O   1 
ATOM   112  C  CB  . TRP A 1 16  ? 28.344  -0.079  18.025  1.00 13.85  ? 16  TRP A CB  1 
ATOM   113  C  CG  . TRP A 1 16  ? 27.696  -0.773  16.859  1.00 13.43  ? 16  TRP A CG  1 
ATOM   114  C  CD1 . TRP A 1 16  ? 28.242  -1.235  15.682  1.00 14.33  ? 16  TRP A CD1 1 
ATOM   115  C  CD2 . TRP A 1 16  ? 26.300  -1.103  16.783  1.00 13.13  ? 16  TRP A CD2 1 
ATOM   116  N  NE1 . TRP A 1 16  ? 27.266  -1.824  14.906  1.00 13.76  ? 16  TRP A NE1 1 
ATOM   117  C  CE2 . TRP A 1 16  ? 26.062  -1.744  15.551  1.00 13.07  ? 16  TRP A CE2 1 
ATOM   118  C  CE3 . TRP A 1 16  ? 25.245  -0.907  17.668  1.00 13.21  ? 16  TRP A CE3 1 
ATOM   119  C  CZ2 . TRP A 1 16  ? 24.797  -2.188  15.164  1.00 14.25  ? 16  TRP A CZ2 1 
ATOM   120  C  CZ3 . TRP A 1 16  ? 23.998  -1.366  17.290  1.00 12.51  ? 16  TRP A CZ3 1 
ATOM   121  C  CH2 . TRP A 1 16  ? 23.772  -1.991  16.064  1.00 13.83  ? 16  TRP A CH2 1 
ATOM   122  N  N   . HIS A 1 17  ? 30.809  0.388   20.083  1.00 13.97  ? 17  HIS A N   1 
ATOM   123  C  CA  . HIS A 1 17  ? 31.306  1.204   21.180  1.00 15.18  ? 17  HIS A CA  1 
ATOM   124  C  C   . HIS A 1 17  ? 32.576  1.973   20.774  1.00 17.65  ? 17  HIS A C   1 
ATOM   125  O  O   . HIS A 1 17  ? 32.813  3.041   21.339  1.00 17.36  ? 17  HIS A O   1 
ATOM   126  C  CB  . HIS A 1 17  ? 31.594  0.422   22.488  1.00 14.86  ? 17  HIS A CB  1 
ATOM   127  C  CG  . HIS A 1 17  ? 32.783  -0.460  22.389  1.00 17.75  ? 17  HIS A CG  1 
ATOM   128  N  ND1 . HIS A 1 17  ? 34.008  -0.106  22.903  1.00 20.63  ? 17  HIS A ND1 1 
ATOM   129  C  CD2 . HIS A 1 17  ? 32.945  -1.610  21.708  1.00 17.34  ? 17  HIS A CD2 1 
ATOM   130  C  CE1 . HIS A 1 17  ? 34.864  -1.064  22.616  1.00 21.86  ? 17  HIS A CE1 1 
ATOM   131  N  NE2 . HIS A 1 17  ? 34.283  -1.987  21.895  1.00 20.20  ? 17  HIS A NE2 1 
ATOM   132  N  N   . LYS A 1 18  ? 33.336  1.498   19.771  1.00 16.55  ? 18  LYS A N   1 
ATOM   133  C  CA  . LYS A 1 18  ? 34.569  2.238   19.526  1.00 19.07  ? 18  LYS A CA  1 
ATOM   134  C  C   . LYS A 1 18  ? 34.265  3.584   18.851  1.00 21.48  ? 18  LYS A C   1 
ATOM   135  O  O   . LYS A 1 18  ? 34.910  4.601   19.139  1.00 27.21  ? 18  LYS A O   1 
ATOM   136  C  CB  . LYS A 1 18  ? 35.437  1.384   18.631  1.00 21.53  ? 18  LYS A CB  1 
ATOM   137  C  CG  . LYS A 1 18  ? 36.043  0.162   19.316  1.00 19.29  ? 18  LYS A CG  1 
ATOM   138  C  CD  . LYS A 1 18  ? 36.775  -0.767  18.332  1.00 20.12  ? 18  LYS A CD  1 
ATOM   139  C  CE  . LYS A 1 18  ? 35.761  -1.730  17.695  1.00 20.02  ? 18  LYS A CE  1 
ATOM   140  N  NZ  . LYS A 1 18  ? 36.421  -2.518  16.600  1.00 19.41  ? 18  LYS A NZ  1 
ATOM   141  N  N   . ASP A 1 19  ? 33.247  3.672   17.973  1.00 19.19  ? 19  ASP A N   1 
ATOM   142  C  CA  . ASP A 1 19  ? 32.855  4.943   17.398  1.00 18.94  ? 19  ASP A CA  1 
ATOM   143  C  C   . ASP A 1 19  ? 31.769  5.635   18.232  1.00 18.13  ? 19  ASP A C   1 
ATOM   144  O  O   . ASP A 1 19  ? 31.647  6.864   18.166  1.00 20.75  ? 19  ASP A O   1 
ATOM   145  C  CB  . ASP A 1 19  ? 32.319  4.817   15.971  1.00 21.47  ? 19  ASP A CB  1 
ATOM   146  C  CG  . ASP A 1 19  ? 33.374  4.834   14.883  1.00 27.42  ? 19  ASP A CG  1 
ATOM   147  O  OD1 . ASP A 1 19  ? 34.355  5.556   15.038  1.00 31.84  ? 19  ASP A OD1 1 
ATOM   148  O  OD2 . ASP A 1 19  ? 33.227  4.031   13.949  1.00 47.03  ? 19  ASP A OD2 1 
ATOM   149  N  N   . PHE A 1 20  ? 31.034  4.867   19.056  1.00 16.40  ? 20  PHE A N   1 
ATOM   150  C  CA  . PHE A 1 20  ? 29.900  5.423   19.775  1.00 16.92  ? 20  PHE A CA  1 
ATOM   151  C  C   . PHE A 1 20  ? 30.006  4.936   21.213  1.00 17.67  ? 20  PHE A C   1 
ATOM   152  O  O   . PHE A 1 20  ? 29.352  3.944   21.566  1.00 15.17  ? 20  PHE A O   1 
ATOM   153  C  CB  . PHE A 1 20  ? 28.580  4.946   19.125  1.00 16.62  ? 20  PHE A CB  1 
ATOM   154  C  CG  . PHE A 1 20  ? 28.528  5.342   17.663  1.00 16.52  ? 20  PHE A CG  1 
ATOM   155  C  CD1 . PHE A 1 20  ? 28.190  6.648   17.294  1.00 19.87  ? 20  PHE A CD1 1 
ATOM   156  C  CD2 . PHE A 1 20  ? 28.883  4.418   16.668  1.00 18.20  ? 20  PHE A CD2 1 
ATOM   157  C  CE1 . PHE A 1 20  ? 28.210  7.013   15.940  1.00 21.59  ? 20  PHE A CE1 1 
ATOM   158  C  CE2 . PHE A 1 20  ? 28.899  4.771   15.329  1.00 18.45  ? 20  PHE A CE2 1 
ATOM   159  C  CZ  . PHE A 1 20  ? 28.549  6.069   14.966  1.00 21.71  ? 20  PHE A CZ  1 
ATOM   160  N  N   . PRO A 1 21  ? 30.824  5.577   22.061  1.00 17.41  ? 21  PRO A N   1 
ATOM   161  C  CA  . PRO A 1 21  ? 31.100  5.067   23.404  1.00 16.93  ? 21  PRO A CA  1 
ATOM   162  C  C   . PRO A 1 21  ? 29.859  4.941   24.279  1.00 16.75  ? 21  PRO A C   1 
ATOM   163  O  O   . PRO A 1 21  ? 29.870  4.166   25.227  1.00 16.82  ? 21  PRO A O   1 
ATOM   164  C  CB  . PRO A 1 21  ? 32.133  6.066   24.028  1.00 21.93  ? 21  PRO A CB  1 
ATOM   165  C  CG  . PRO A 1 21  ? 32.231  7.182   23.003  1.00 30.09  ? 21  PRO A CG  1 
ATOM   166  C  CD  . PRO A 1 21  ? 31.732  6.661   21.662  1.00 20.31  ? 21  PRO A CD  1 
ATOM   167  N  N   . ILE A 1 22  ? 28.794  5.701   23.967  1.00 15.55  ? 22  ILE A N   1 
ATOM   168  C  CA  . ILE A 1 22  ? 27.542  5.558   24.701  1.00 14.99  ? 22  ILE A CA  1 
ATOM   169  C  C   . ILE A 1 22  ? 26.943  4.156   24.529  1.00 13.11  ? 22  ILE A C   1 
ATOM   170  O  O   . ILE A 1 22  ? 26.039  3.806   25.283  1.00 14.34  ? 22  ILE A O   1 
ATOM   171  C  CB  . ILE A 1 22  ? 26.531  6.642   24.268  1.00 14.24  ? 22  ILE A CB  1 
ATOM   172  C  CG1 . ILE A 1 22  ? 25.448  6.926   25.311  1.00 17.44  ? 22  ILE A CG1 1 
ATOM   173  C  CG2 . ILE A 1 22  ? 25.930  6.353   22.864  1.00 14.92  ? 22  ILE A CG2 1 
ATOM   174  C  CD1 . ILE A 1 22  ? 25.974  7.448   26.613  1.00 21.52  ? 22  ILE A CD1 1 
ATOM   175  N  N   . ALA A 1 23  ? 27.470  3.330   23.597  1.00 14.05  ? 23  ALA A N   1 
ATOM   176  C  CA  . ALA A 1 23  ? 27.021  1.947   23.488  1.00 14.20  ? 23  ALA A CA  1 
ATOM   177  C  C   . ALA A 1 23  ? 27.143  1.223   24.831  1.00 13.08  ? 23  ALA A C   1 
ATOM   178  O  O   . ALA A 1 23  ? 26.414  0.271   25.038  1.00 14.15  ? 23  ALA A O   1 
ATOM   179  C  CB  . ALA A 1 23  ? 27.843  1.223   22.455  1.00 14.39  ? 23  ALA A CB  1 
ATOM   180  N  N   . LYS A 1 24  ? 28.051  1.683   25.747  1.00 14.84  ? 24  LYS A N   1 
ATOM   181  C  CA  . LYS A 1 24  ? 28.244  1.064   27.064  1.00 15.25  ? 24  LYS A CA  1 
ATOM   182  C  C   . LYS A 1 24  ? 27.616  1.966   28.147  1.00 17.05  ? 24  LYS A C   1 
ATOM   183  O  O   . LYS A 1 24  ? 27.980  1.841   29.330  1.00 19.89  ? 24  LYS A O   1 
ATOM   184  C  CB  . LYS A 1 24  ? 29.730  0.856   27.343  1.00 16.50  ? 24  LYS A CB  1 
ATOM   185  C  CG  . LYS A 1 24  ? 30.310  -0.156  26.378  1.00 19.29  ? 24  LYS A CG  1 
ATOM   186  C  CD  . LYS A 1 24  ? 31.758  -0.349  26.746  1.00 22.58  ? 24  LYS A CD  1 
ATOM   187  C  CE  . LYS A 1 24  ? 32.515  -1.257  25.826  1.00 25.30  ? 24  LYS A CE  1 
ATOM   188  N  NZ  . LYS A 1 24  ? 32.177  -2.642  26.159  1.00 29.62  ? 24  LYS A NZ  1 
ATOM   189  N  N   . GLY A 1 25  ? 26.562  2.723   27.754  1.00 16.34  ? 25  GLY A N   1 
ATOM   190  C  CA  . GLY A 1 25  ? 25.935  3.701   28.651  1.00 15.83  ? 25  GLY A CA  1 
ATOM   191  C  C   . GLY A 1 25  ? 24.963  3.065   29.634  1.00 15.61  ? 25  GLY A C   1 
ATOM   192  O  O   . GLY A 1 25  ? 24.793  1.846   29.720  1.00 14.50  ? 25  GLY A O   1 
ATOM   193  N  N   . GLU A 1 26  ? 24.305  3.951   30.376  1.00 16.13  ? 26  GLU A N   1 
ATOM   194  C  CA  . GLU A 1 26  ? 23.458  3.517   31.464  1.00 18.19  ? 26  GLU A CA  1 
ATOM   195  C  C   . GLU A 1 26  ? 22.011  3.317   31.059  1.00 14.10  ? 26  GLU A C   1 
ATOM   196  O  O   . GLU A 1 26  ? 21.228  2.787   31.861  1.00 16.03  ? 26  GLU A O   1 
ATOM   197  C  CB  . GLU A 1 26  ? 23.494  4.557   32.588  1.00 21.83  ? 26  GLU A CB  1 
ATOM   198  C  CG  . GLU A 1 26  ? 24.924  4.713   33.153  1.00 28.92  ? 26  GLU A CG  1 
ATOM   199  C  CD  . GLU A 1 26  ? 25.585  3.472   33.762  1.00 33.83  ? 26  GLU A CD  1 
ATOM   200  O  OE1 . GLU A 1 26  ? 24.902  2.725   34.524  1.00 37.46  ? 26  GLU A OE1 1 
ATOM   201  O  OE2 . GLU A 1 26  ? 26.768  3.219   33.412  1.00 44.06  ? 26  GLU A OE2 1 
ATOM   202  N  N   . ARG A 1 27  ? 21.638  3.672   29.819  1.00 12.45  ? 27  ARG A N   1 
ATOM   203  C  CA  . ARG A 1 27  ? 20.236  3.517   29.422  1.00 12.00  ? 27  ARG A CA  1 
ATOM   204  C  C   . ARG A 1 27  ? 20.150  3.028   27.976  1.00 10.44  ? 27  ARG A C   1 
ATOM   205  O  O   . ARG A 1 27  ? 19.471  3.591   27.120  1.00 11.24  ? 27  ARG A O   1 
ATOM   206  C  CB  . ARG A 1 27  ? 19.343  4.735   29.707  1.00 15.04  ? 27  ARG A CB  1 
ATOM   207  C  CG  . ARG A 1 27  ? 19.793  6.016   29.049  1.00 18.84  ? 27  ARG A CG  1 
ATOM   208  C  CD  . ARG A 1 27  ? 18.852  7.212   29.233  1.00 24.83  ? 27  ARG A CD  1 
ATOM   209  N  NE  . ARG A 1 27  ? 17.648  7.150   28.372  1.00 18.51  ? 27  ARG A NE  1 
ATOM   210  C  CZ  . ARG A 1 27  ? 16.761  8.130   28.245  1.00 14.29  ? 27  ARG A CZ  1 
ATOM   211  N  NH1 . ARG A 1 27  ? 16.922  9.259   28.915  1.00 15.72  ? 27  ARG A NH1 1 
ATOM   212  N  NH2 . ARG A 1 27  ? 15.717  7.980   27.450  1.00 18.22  ? 27  ARG A NH2 1 
ATOM   213  N  N   . GLN A 1 28  ? 20.883  1.945   27.665  1.00 10.17  ? 28  GLN A N   1 
ATOM   214  C  CA  . GLN A 1 28  ? 20.937  1.417   26.313  1.00 9.41   ? 28  GLN A CA  1 
ATOM   215  C  C   . GLN A 1 28  ? 19.773  0.481   26.014  1.00 8.96   ? 28  GLN A C   1 
ATOM   216  O  O   . GLN A 1 28  ? 19.259  -0.202  26.914  1.00 10.19  ? 28  GLN A O   1 
ATOM   217  C  CB  . GLN A 1 28  ? 22.278  0.719   26.084  1.00 9.85   ? 28  GLN A CB  1 
ATOM   218  C  CG  . GLN A 1 28  ? 23.417  1.739   26.017  1.00 11.13  ? 28  GLN A CG  1 
ATOM   219  C  CD  . GLN A 1 28  ? 23.330  2.557   24.747  1.00 11.18  ? 28  GLN A CD  1 
ATOM   220  O  OE1 . GLN A 1 28  ? 23.511  2.006   23.658  1.00 11.69  ? 28  GLN A OE1 1 
ATOM   221  N  NE2 . GLN A 1 28  ? 22.973  3.836   24.825  1.00 11.36  ? 28  GLN A NE2 1 
ATOM   222  N  N   . SER A 1 29  ? 19.396  0.431   24.729  1.00 9.13   ? 29  SER A N   1 
ATOM   223  C  CA  . SER A 1 29  ? 18.327  -0.450  24.267  1.00 8.41   ? 29  SER A CA  1 
ATOM   224  C  C   . SER A 1 29  ? 18.853  -1.299  23.153  1.00 8.62   ? 29  SER A C   1 
ATOM   225  O  O   . SER A 1 29  ? 19.811  -0.968  22.463  1.00 9.74   ? 29  SER A O   1 
ATOM   226  C  CB  . SER A 1 29  ? 17.171  0.410   23.707  1.00 8.79   ? 29  SER A CB  1 
ATOM   227  O  OG  . SER A 1 29  ? 16.586  1.147   24.791  1.00 9.18   ? 29  SER A OG  1 
ATOM   228  N  N   . PRO A 1 30  ? 18.218  -2.434  22.854  1.00 8.37   ? 30  PRO A N   1 
ATOM   229  C  CA  . PRO A 1 30  ? 17.039  -2.977  23.551  1.00 8.74   ? 30  PRO A CA  1 
ATOM   230  C  C   . PRO A 1 30  ? 17.441  -3.655  24.875  1.00 8.52   ? 30  PRO A C   1 
ATOM   231  O  O   . PRO A 1 30  ? 18.629  -3.698  25.208  1.00 9.69   ? 30  PRO A O   1 
ATOM   232  C  CB  . PRO A 1 30  ? 16.507  -3.969  22.532  1.00 8.16   ? 30  PRO A CB  1 
ATOM   233  C  CG  . PRO A 1 30  ? 17.784  -4.551  21.964  1.00 8.57   ? 30  PRO A CG  1 
ATOM   234  C  CD  . PRO A 1 30  ? 18.676  -3.342  21.783  1.00 8.59   ? 30  PRO A CD  1 
ATOM   235  N  N   . VAL A 1 31  ? 16.443  -4.212  25.557  1.00 9.05   ? 31  VAL A N   1 
ATOM   236  C  CA  . VAL A 1 31  ? 16.641  -4.942  26.783  1.00 9.13   ? 31  VAL A CA  1 
ATOM   237  C  C   . VAL A 1 31  ? 15.749  -6.177  26.736  1.00 9.42   ? 31  VAL A C   1 
ATOM   238  O  O   . VAL A 1 31  ? 14.792  -6.241  25.967  1.00 9.92   ? 31  VAL A O   1 
ATOM   239  C  CB  . VAL A 1 31  ? 16.315  -4.116  28.036  1.00 9.88   ? 31  VAL A CB  1 
ATOM   240  C  CG1 . VAL A 1 31  ? 17.223  -2.897  28.141  1.00 11.55  ? 31  VAL A CG1 1 
ATOM   241  C  CG2 . VAL A 1 31  ? 14.847  -3.709  28.095  1.00 10.59  ? 31  VAL A CG2 1 
ATOM   242  N  N   . ASP A 1 32  ? 16.107  -7.152  27.601  1.00 9.73   ? 32  ASP A N   1 
ATOM   243  C  CA  . ASP A 1 32  ? 15.196  -8.229  27.893  1.00 9.95   ? 32  ASP A CA  1 
ATOM   244  C  C   . ASP A 1 32  ? 14.122  -7.700  28.850  1.00 9.50   ? 32  ASP A C   1 
ATOM   245  O  O   . ASP A 1 32  ? 14.436  -7.048  29.876  1.00 12.02  ? 32  ASP A O   1 
ATOM   246  C  CB  . ASP A 1 32  ? 15.924  -9.418  28.495  1.00 11.72  ? 32  ASP A CB  1 
ATOM   247  C  CG  . ASP A 1 32  ? 14.964  -10.581 28.785  1.00 11.99  ? 32  ASP A CG  1 
ATOM   248  O  OD1 . ASP A 1 32  ? 14.281  -11.049 27.855  1.00 11.39  ? 32  ASP A OD1 1 
ATOM   249  O  OD2 . ASP A 1 32  ? 14.935  -10.986 29.951  1.00 14.75  ? 32  ASP A OD2 1 
ATOM   250  N  N   . ILE A 1 33  ? 12.858  -8.004  28.548  1.00 10.03  ? 33  ILE A N   1 
ATOM   251  C  CA  . ILE A 1 33  ? 11.747  -7.624  29.429  1.00 12.15  ? 33  ILE A CA  1 
ATOM   252  C  C   . ILE A 1 33  ? 11.459  -8.880  30.255  1.00 12.35  ? 33  ILE A C   1 
ATOM   253  O  O   . ILE A 1 33  ? 10.912  -9.899  29.790  1.00 13.17  ? 33  ILE A O   1 
ATOM   254  C  CB  . ILE A 1 33  ? 10.550  -7.212  28.599  1.00 11.64  ? 33  ILE A CB  1 
ATOM   255  C  CG1 . ILE A 1 33  ? 10.908  -5.969  27.777  1.00 11.57  ? 33  ILE A CG1 1 
ATOM   256  C  CG2 . ILE A 1 33  ? 9.375   -6.939  29.503  1.00 12.20  ? 33  ILE A CG2 1 
ATOM   257  C  CD1 . ILE A 1 33  ? 9.884   -5.649  26.664  1.00 15.16  ? 33  ILE A CD1 1 
ATOM   258  N  N   . ASP A 1 34  ? 11.846  -8.825  31.528  1.00 12.91  ? 34  ASP A N   1 
ATOM   259  C  CA  . ASP A 1 34  ? 11.546  -9.901  32.483  1.00 14.78  ? 34  ASP A CA  1 
ATOM   260  C  C   . ASP A 1 34  ? 10.124  -9.624  32.995  1.00 13.40  ? 34  ASP A C   1 
ATOM   261  O  O   . ASP A 1 34  ? 9.880   -8.674  33.734  1.00 17.82  ? 34  ASP A O   1 
ATOM   262  C  CB  . ASP A 1 34  ? 12.644  -9.916  33.586  1.00 17.12  ? 34  ASP A CB  1 
ATOM   263  C  CG  . ASP A 1 34  ? 12.431  -10.920 34.765  1.00 22.11  ? 34  ASP A CG  1 
ATOM   264  O  OD1 . ASP A 1 34  ? 11.315  -11.320 34.978  1.00 22.68  ? 34  ASP A OD1 1 
ATOM   265  O  OD2 . ASP A 1 34  ? 13.387  -11.142 35.561  1.00 32.74  ? 34  ASP A OD2 1 
ATOM   266  N  N   . THR A 1 35  ? 9.150   -10.427 32.529  1.00 15.98  ? 35  THR A N   1 
ATOM   267  C  CA  . THR A 1 35  ? 7.762   -10.137 32.781  1.00 18.49  ? 35  THR A CA  1 
ATOM   268  C  C   . THR A 1 35  ? 7.415   -10.258 34.243  1.00 19.72  ? 35  THR A C   1 
ATOM   269  O  O   . THR A 1 35  ? 6.483   -9.594  34.705  1.00 21.41  ? 35  THR A O   1 
ATOM   270  C  CB  . THR A 1 35  ? 6.863   -11.049 31.957  1.00 21.76  ? 35  THR A CB  1 
ATOM   271  O  OG1 . THR A 1 35  ? 7.060   -12.376 32.446  1.00 21.24  ? 35  THR A OG1 1 
ATOM   272  C  CG2 . THR A 1 35  ? 7.122   -10.935 30.471  1.00 24.31  ? 35  THR A CG2 1 
ATOM   273  N  N   . HIS A 1 36  ? 8.196   -11.065 34.972  1.00 21.35  ? 36  HIS A N   1 
ATOM   274  C  CA  . HIS A 1 36  ? 7.949   -11.291 36.398  1.00 22.54  ? 36  HIS A CA  1 
ATOM   275  C  C   . HIS A 1 36  ? 8.414   -10.114 37.215  1.00 27.38  ? 36  HIS A C   1 
ATOM   276  O  O   . HIS A 1 36  ? 7.739   -9.823  38.191  1.00 36.36  ? 36  HIS A O   1 
ATOM   277  C  CB  . HIS A 1 36  ? 8.581   -12.623 36.842  1.00 27.27  ? 36  HIS A CB  1 
ATOM   278  C  CG  . HIS A 1 36  ? 7.909   -13.726 36.099  1.00 28.27  ? 36  HIS A CG  1 
ATOM   279  N  ND1 . HIS A 1 36  ? 8.521   -14.421 34.968  1.00 34.53  ? 36  HIS A ND1 1 
ATOM   280  C  CD2 . HIS A 1 36  ? 6.608   -14.130 36.181  1.00 31.59  ? 36  HIS A CD2 1 
ATOM   281  C  CE1 . HIS A 1 36  ? 7.657   -15.272 34.470  1.00 42.56  ? 36  HIS A CE1 1 
ATOM   282  N  NE2 . HIS A 1 36  ? 6.491   -15.152 35.184  1.00 43.29  ? 36  HIS A NE2 1 
ATOM   283  N  N   . THR A 1 37  ? 9.483   -9.436  36.800  1.00 23.48  ? 37  THR A N   1 
ATOM   284  C  CA  . THR A 1 37  ? 9.954   -8.270  37.538  1.00 25.25  ? 37  THR A CA  1 
ATOM   285  C  C   . THR A 1 37  ? 9.461   -6.918  37.035  1.00 20.07  ? 37  THR A C   1 
ATOM   286  O  O   . THR A 1 37  ? 9.586   -5.958  37.799  1.00 29.90  ? 37  THR A O   1 
ATOM   287  C  CB  . THR A 1 37  ? 11.460  -8.245  37.775  1.00 42.29  ? 37  THR A CB  1 
ATOM   288  O  OG1 . THR A 1 37  ? 12.264  -7.685  36.675  1.00 69.02  ? 37  THR A OG1 1 
ATOM   289  C  CG2 . THR A 1 37  ? 11.929  -9.654  38.031  1.00 29.83  ? 37  THR A CG2 1 
ATOM   290  N  N   . ALA A 1 38  ? 8.760   -6.845  35.901  1.00 19.81  ? 38  ALA A N   1 
ATOM   291  C  CA  . ALA A 1 38  ? 8.183   -5.580  35.489  1.00 20.33  ? 38  ALA A CA  1 
ATOM   292  C  C   . ALA A 1 38  ? 7.059   -5.301  36.459  1.00 22.68  ? 38  ALA A C   1 
ATOM   293  O  O   . ALA A 1 38  ? 6.365   -6.227  36.861  1.00 29.80  ? 38  ALA A O   1 
ATOM   294  C  CB  . ALA A 1 38  ? 7.657   -5.713  34.106  1.00 17.38  ? 38  ALA A CB  1 
ATOM   295  N  N   . LYS A 1 39  ? 6.937   -4.071  36.930  1.00 22.24  ? 39  LYS A N   1 
ATOM   296  C  CA  . LYS A 1 39  ? 5.931   -3.720  37.933  1.00 24.75  ? 39  LYS A CA  1 
ATOM   297  C  C   . LYS A 1 39  ? 4.746   -3.065  37.230  1.00 17.04  ? 39  LYS A C   1 
ATOM   298  O  O   . LYS A 1 39  ? 4.937   -2.047  36.542  1.00 16.50  ? 39  LYS A O   1 
ATOM   299  C  CB  . LYS A 1 39  ? 6.621   -2.734  38.884  1.00 32.60  ? 39  LYS A CB  1 
ATOM   300  C  CG  . LYS A 1 39  ? 5.778   -1.731  39.640  1.00 44.28  ? 39  LYS A CG  1 
ATOM   301  C  CD  . LYS A 1 39  ? 5.769   -2.152  41.076  1.00 32.63  ? 39  LYS A CD  1 
ATOM   302  C  CE  . LYS A 1 39  ? 5.070   -1.089  41.921  1.00 39.46  ? 39  LYS A CE  1 
ATOM   303  N  NZ  . LYS A 1 39  ? 4.838   -1.730  43.236  1.00 39.37  ? 39  LYS A NZ  1 
ATOM   304  N  N   . TYR A 1 40  ? 3.530   -3.557  37.508  1.00 19.97  ? 40  TYR A N   1 
ATOM   305  C  CA  . TYR A 1 40  ? 2.295   -2.868  37.180  1.00 19.62  ? 40  TYR A CA  1 
ATOM   306  C  C   . TYR A 1 40  ? 2.365   -1.483  37.793  1.00 17.50  ? 40  TYR A C   1 
ATOM   307  O  O   . TYR A 1 40  ? 2.552   -1.310  39.025  1.00 21.03  ? 40  TYR A O   1 
ATOM   308  C  CB  . TYR A 1 40  ? 1.025   -3.624  37.584  1.00 22.75  ? 40  TYR A CB  1 
ATOM   309  C  CG  . TYR A 1 40  ? -0.242  -2.818  37.467  1.00 28.52  ? 40  TYR A CG  1 
ATOM   310  C  CD1 . TYR A 1 40  ? -0.665  -2.335  36.238  1.00 24.66  ? 40  TYR A CD1 1 
ATOM   311  C  CD2 . TYR A 1 40  ? -1.066  -2.585  38.578  1.00 38.61  ? 40  TYR A CD2 1 
ATOM   312  C  CE1 . TYR A 1 40  ? -1.824  -1.592  36.111  1.00 32.05  ? 40  TYR A CE1 1 
ATOM   313  C  CE2 . TYR A 1 40  ? -2.230  -1.834  38.473  1.00 44.24  ? 40  TYR A CE2 1 
ATOM   314  C  CZ  . TYR A 1 40  ? -2.620  -1.361  37.230  1.00 39.79  ? 40  TYR A CZ  1 
ATOM   315  O  OH  . TYR A 1 40  ? -3.727  -0.598  37.057  1.00 46.25  ? 40  TYR A OH  1 
ATOM   316  N  N   . ASP A 1 41  ? 2.091   -0.480  36.959  1.00 17.32  ? 41  ASP A N   1 
ATOM   317  C  CA  . ASP A 1 41  ? 2.069   0.895   37.453  1.00 17.69  ? 41  ASP A CA  1 
ATOM   318  C  C   . ASP A 1 41  ? 0.690   1.487   37.222  1.00 24.83  ? 41  ASP A C   1 
ATOM   319  O  O   . ASP A 1 41  ? 0.360   1.835   36.102  1.00 20.35  ? 41  ASP A O   1 
ATOM   320  C  CB  . ASP A 1 41  ? 3.101   1.738   36.690  1.00 19.93  ? 41  ASP A CB  1 
ATOM   321  C  CG  . ASP A 1 41  ? 3.262   3.142   37.229  1.00 27.58  ? 41  ASP A CG  1 
ATOM   322  O  OD1 . ASP A 1 41  ? 2.376   3.601   37.955  1.00 26.51  ? 41  ASP A OD1 1 
ATOM   323  O  OD2 . ASP A 1 41  ? 4.303   3.780   36.882  1.00 29.90  ? 41  ASP A OD2 1 
ATOM   324  N  N   . PRO A 1 42  ? -0.132  1.611   38.285  1.00 27.13  ? 42  PRO A N   1 
ATOM   325  C  CA  . PRO A 1 42  ? -1.506  2.098   38.123  1.00 28.87  ? 42  PRO A CA  1 
ATOM   326  C  C   . PRO A 1 42  ? -1.565  3.575   37.738  1.00 35.32  ? 42  PRO A C   1 
ATOM   327  O  O   . PRO A 1 42  ? -2.619  4.022   37.266  1.00 46.41  ? 42  PRO A O   1 
ATOM   328  C  CB  . PRO A 1 42  ? -2.137  1.786   39.486  1.00 36.35  ? 42  PRO A CB  1 
ATOM   329  C  CG  . PRO A 1 42  ? -0.954  1.828   40.423  1.00 33.63  ? 42  PRO A CG  1 
ATOM   330  C  CD  . PRO A 1 42  ? 0.170   1.161   39.660  1.00 32.75  ? 42  PRO A CD  1 
ATOM   331  N  N   . SER A 1 43  ? -0.423  4.309   37.851  1.00 27.71  ? 43  SER A N   1 
ATOM   332  C  CA  . SER A 1 43  ? -0.453  5.710   37.403  1.00 32.22  ? 43  SER A CA  1 
ATOM   333  C  C   . SER A 1 43  ? -0.258  5.877   35.890  1.00 30.53  ? 43  SER A C   1 
ATOM   334  O  O   . SER A 1 43  ? -0.483  6.969   35.355  1.00 42.12  ? 43  SER A O   1 
ATOM   335  C  CB  . SER A 1 43  ? 0.540   6.559   38.107  1.00 34.23  ? 43  SER A CB  1 
ATOM   336  O  OG  . SER A 1 43  ? 1.840   6.133   37.795  1.00 40.38  ? 43  SER A OG  1 
ATOM   337  N  N   . LEU A 1 44  ? 0.139   4.824   35.180  1.00 28.12  ? 44  LEU A N   1 
ATOM   338  C  CA  . LEU A 1 44  ? 0.294   4.916   33.733  1.00 24.55  ? 44  LEU A CA  1 
ATOM   339  C  C   . LEU A 1 44  ? -1.072  5.101   33.110  1.00 34.22  ? 44  LEU A C   1 
ATOM   340  O  O   . LEU A 1 44  ? -2.058  4.541   33.564  1.00 35.17  ? 44  LEU A O   1 
ATOM   341  C  CB  . LEU A 1 44  ? 0.897   3.629   33.179  1.00 25.78  ? 44  LEU A CB  1 
ATOM   342  C  CG  . LEU A 1 44  ? 2.383   3.440   33.377  1.00 20.33  ? 44  LEU A CG  1 
ATOM   343  C  CD1 . LEU A 1 44  ? 2.770   2.060   32.913  1.00 21.29  ? 44  LEU A CD1 1 
ATOM   344  C  CD2 . LEU A 1 44  ? 3.136   4.482   32.595  1.00 18.62  ? 44  LEU A CD2 1 
ATOM   345  N  N   . LYS A 1 45  ? -1.079  5.804   31.989  1.00 36.55  ? 45  LYS A N   1 
ATOM   346  C  CA  . LYS A 1 45  ? -2.293  5.826   31.196  1.00 30.05  ? 45  LYS A CA  1 
ATOM   347  C  C   . LYS A 1 45  ? -2.329  4.842   30.056  1.00 29.19  ? 45  LYS A C   1 
ATOM   348  O  O   . LYS A 1 45  ? -1.357  4.097   29.738  1.00 37.15  ? 45  LYS A O   1 
ATOM   349  C  CB  . LYS A 1 45  ? -2.691  7.208   30.767  1.00 27.14  ? 45  LYS A CB  1 
ATOM   350  C  CG  . LYS A 1 45  ? -2.437  8.202   31.893  1.00 28.21  ? 45  LYS A CG  1 
ATOM   351  C  CD  . LYS A 1 45  ? -2.195  9.605   31.416  1.00 35.25  ? 45  LYS A CD  1 
ATOM   352  C  CE  . LYS A 1 45  ? -1.842  10.543  32.558  1.00 45.12  ? 45  LYS A CE  1 
ATOM   353  N  N   . PRO A 1 46  ? -3.580  4.697   29.511  1.00 26.60  ? 46  PRO A N   1 
ATOM   354  C  CA  . PRO A 1 46  ? -3.758  3.986   28.252  1.00 29.92  ? 46  PRO A CA  1 
ATOM   355  C  C   . PRO A 1 46  ? -3.036  4.929   27.297  1.00 23.64  ? 46  PRO A C   1 
ATOM   356  O  O   . PRO A 1 46  ? -3.014  6.176   27.435  1.00 28.41  ? 46  PRO A O   1 
ATOM   357  C  CB  . PRO A 1 46  ? -5.270  4.055   27.974  1.00 27.46  ? 46  PRO A CB  1 
ATOM   358  C  CG  . PRO A 1 46  ? -5.842  4.241   29.374  1.00 34.08  ? 46  PRO A CG  1 
ATOM   359  C  CD  . PRO A 1 46  ? -4.855  5.152   30.078  1.00 34.28  ? 46  PRO A CD  1 
ATOM   360  N  N   . LEU A 1 47  ? -2.480  4.227   26.325  1.00 26.60  ? 47  LEU A N   1 
ATOM   361  C  CA  . LEU A 1 47  ? -1.749  4.939   25.345  1.00 24.96  ? 47  LEU A CA  1 
ATOM   362  C  C   . LEU A 1 47  ? -2.855  5.548   24.476  1.00 25.50  ? 47  LEU A C   1 
ATOM   363  O  O   . LEU A 1 47  ? -3.949  5.010   24.365  1.00 26.57  ? 47  LEU A O   1 
ATOM   364  C  CB  . LEU A 1 47  ? -1.046  3.806   24.637  1.00 34.47  ? 47  LEU A CB  1 
ATOM   365  C  CG  . LEU A 1 47  ? 0.156   4.170   23.816  1.00 35.89  ? 47  LEU A CG  1 
ATOM   366  C  CD1 . LEU A 1 47  ? 1.175   4.878   24.707  1.00 28.22  ? 47  LEU A CD1 1 
ATOM   367  C  CD2 . LEU A 1 47  ? 0.650   2.856   23.181  1.00 35.12  ? 47  LEU A CD2 1 
ATOM   368  N  N   . SER A 1 48  ? -2.559  6.666   23.857  1.00 16.77  ? 48  SER A N   1 
ATOM   369  C  CA  . SER A 1 48  ? -3.412  7.297   22.854  1.00 15.22  ? 48  SER A CA  1 
ATOM   370  C  C   . SER A 1 48  ? -2.636  7.262   21.541  1.00 14.96  ? 48  SER A C   1 
ATOM   371  O  O   . SER A 1 48  ? -1.630  7.967   21.367  1.00 16.25  ? 48  SER A O   1 
ATOM   372  C  CB  . SER A 1 48  ? -3.744  8.757   23.240  1.00 16.75  ? 48  SER A CB  1 
ATOM   373  O  OG  . SER A 1 48  ? -4.436  9.407   22.211  1.00 22.21  ? 48  SER A OG  1 
ATOM   374  N  N   . VAL A 1 49  ? -3.080  6.430   20.643  1.00 16.91  ? 49  VAL A N   1 
ATOM   375  C  CA  . VAL A 1 49  ? -2.480  6.308   19.344  1.00 16.20  ? 49  VAL A CA  1 
ATOM   376  C  C   . VAL A 1 49  ? -3.444  6.923   18.333  1.00 20.16  ? 49  VAL A C   1 
ATOM   377  O  O   . VAL A 1 49  ? -4.520  6.387   18.121  1.00 26.08  ? 49  VAL A O   1 
ATOM   378  C  CB  . VAL A 1 49  ? -2.217  4.832   19.006  1.00 21.45  ? 49  VAL A CB  1 
ATOM   379  C  CG1 . VAL A 1 49  ? -1.519  4.740   17.673  1.00 25.29  ? 49  VAL A CG1 1 
ATOM   380  C  CG2 . VAL A 1 49  ? -1.362  4.202   20.090  1.00 22.42  ? 49  VAL A CG2 1 
ATOM   381  N  N   . SER A 1 50  ? -3.079  8.055   17.741  1.00 18.00  ? 50  SER A N   1 
ATOM   382  C  CA  . SER A 1 50  ? -4.065  8.784   16.936  1.00 19.47  ? 50  SER A CA  1 
ATOM   383  C  C   . SER A 1 50  ? -3.468  8.874   15.540  1.00 15.77  ? 50  SER A C   1 
ATOM   384  O  O   . SER A 1 50  ? -2.751  9.806   15.245  1.00 17.31  ? 50  SER A O   1 
ATOM   385  C  CB  . SER A 1 50  ? -4.465  10.186  17.469  1.00 23.30  ? 50  SER A CB  1 
ATOM   386  O  OG  . SER A 1 50  ? -5.084  10.054  18.729  1.00 32.06  ? 50  SER A OG  1 
ATOM   387  N  N   . TYR A 1 51  ? -3.698  7.873   14.700  1.00 17.52  ? 51  TYR A N   1 
ATOM   388  C  CA  . TYR A 1 51  ? -3.141  7.783   13.380  1.00 15.85  ? 51  TYR A CA  1 
ATOM   389  C  C   . TYR A 1 51  ? -4.125  8.045   12.246  1.00 17.47  ? 51  TYR A C   1 
ATOM   390  O  O   . TYR A 1 51  ? -3.756  7.810   11.079  1.00 19.18  ? 51  TYR A O   1 
ATOM   391  C  CB  . TYR A 1 51  ? -2.489  6.403   13.198  1.00 15.56  ? 51  TYR A CB  1 
ATOM   392  C  CG  . TYR A 1 51  ? -1.221  6.090   13.952  1.00 14.56  ? 51  TYR A CG  1 
ATOM   393  C  CD1 . TYR A 1 51  ? -0.531  7.049   14.672  1.00 15.68  ? 51  TYR A CD1 1 
ATOM   394  C  CD2 . TYR A 1 51  ? -0.755  4.784   14.040  1.00 13.01  ? 51  TYR A CD2 1 
ATOM   395  C  CE1 . TYR A 1 51  ? 0.686   6.746   15.309  1.00 13.70  ? 51  TYR A CE1 1 
ATOM   396  C  CE2 . TYR A 1 51  ? 0.441   4.461   14.667  1.00 13.67  ? 51  TYR A CE2 1 
ATOM   397  C  CZ  . TYR A 1 51  ? 1.147   5.437   15.348  1.00 12.25  ? 51  TYR A CZ  1 
ATOM   398  O  OH  . TYR A 1 51  ? 2.295   5.100   16.008  1.00 13.69  ? 51  TYR A OH  1 
ATOM   399  N  N   A ASP A 1 52  ? -5.335  8.542   12.586  0.50 22.05  ? 52  ASP A N   1 
ATOM   400  N  N   B ASP A 1 52  ? -5.357  8.510   12.557  0.50 22.16  ? 52  ASP A N   1 
ATOM   401  C  CA  A ASP A 1 52  ? -6.385  8.780   11.608  0.50 23.07  ? 52  ASP A CA  1 
ATOM   402  C  CA  B ASP A 1 52  ? -6.367  8.738   11.529  0.50 24.45  ? 52  ASP A CA  1 
ATOM   403  C  C   A ASP A 1 52  ? -5.947  9.694   10.464  0.50 22.13  ? 52  ASP A C   1 
ATOM   404  C  C   B ASP A 1 52  ? -5.850  9.637   10.403  0.50 22.76  ? 52  ASP A C   1 
ATOM   405  O  O   A ASP A 1 52  ? -6.372  9.514   9.319   0.50 24.20  ? 52  ASP A O   1 
ATOM   406  O  O   B ASP A 1 52  ? -6.136  9.416   9.219   0.50 26.15  ? 52  ASP A O   1 
ATOM   407  C  CB  A ASP A 1 52  ? -7.698  9.175   12.302  0.50 22.41  ? 52  ASP A CB  1 
ATOM   408  C  CB  B ASP A 1 52  ? -7.674  9.274   12.137  0.50 26.07  ? 52  ASP A CB  1 
ATOM   409  C  CG  A ASP A 1 52  ? -7.519  10.171  13.435  0.50 24.85  ? 52  ASP A CG  1 
ATOM   410  C  CG  B ASP A 1 52  ? -8.824  9.365   11.137  0.50 29.01  ? 52  ASP A CG  1 
ATOM   411  O  OD1 A ASP A 1 52  ? -6.678  9.896   14.373  0.50 24.97  ? 52  ASP A OD1 1 
ATOM   412  O  OD1 B ASP A 1 52  ? -9.168  8.324   10.499  0.50 30.53  ? 52  ASP A OD1 1 
ATOM   413  O  OD2 A ASP A 1 52  ? -8.189  11.208  13.384  0.50 34.78  ? 52  ASP A OD2 1 
ATOM   414  O  OD2 B ASP A 1 52  ? -9.352  10.480  10.981  0.50 43.73  ? 52  ASP A OD2 1 
ATOM   415  N  N   . GLN A 1 53  ? -5.097  10.676  10.746  1.00 22.39  ? 53  GLN A N   1 
ATOM   416  C  CA  . GLN A 1 53  ? -4.684  11.634  9.708   1.00 25.49  ? 53  GLN A CA  1 
ATOM   417  C  C   . GLN A 1 53  ? -3.260  11.395  9.214   1.00 22.49  ? 53  GLN A C   1 
ATOM   418  O  O   . GLN A 1 53  ? -2.667  12.259  8.587   1.00 23.42  ? 53  GLN A O   1 
ATOM   419  C  CB  . GLN A 1 53  ? -4.958  13.090  10.151  1.00 39.19  ? 53  GLN A CB  1 
ATOM   420  C  CG  . GLN A 1 53  ? -6.444  13.409  10.427  1.00 54.37  ? 53  GLN A CG  1 
ATOM   421  C  CD  . GLN A 1 53  ? -7.181  13.347  9.065   1.00 62.56  ? 53  GLN A CD  1 
ATOM   422  O  OE1 . GLN A 1 53  ? -6.599  13.596  7.949   1.00 77.62  ? 53  GLN A OE1 1 
ATOM   423  N  NE2 . GLN A 1 53  ? -8.482  13.021  9.165   1.00 73.38  ? 53  GLN A NE2 1 
ATOM   424  N  N   . ALA A 1 54  ? -2.727  10.211  9.467   1.00 18.70  ? 54  ALA A N   1 
ATOM   425  C  CA  . ALA A 1 54  ? -1.354  9.933   9.065   1.00 16.46  ? 54  ALA A CA  1 
ATOM   426  C  C   . ALA A 1 54  ? -1.219  10.065  7.554   1.00 19.16  ? 54  ALA A C   1 
ATOM   427  O  O   . ALA A 1 54  ? -2.051  9.555   6.785   1.00 24.85  ? 54  ALA A O   1 
ATOM   428  C  CB  . ALA A 1 54  ? -0.902  8.531   9.491   1.00 18.28  ? 54  ALA A CB  1 
ATOM   429  N  N   . THR A 1 55  ? -0.097  10.641  7.133   1.00 16.10  ? 55  THR A N   1 
ATOM   430  C  CA  . THR A 1 55  ? 0.202   10.891  5.719   1.00 18.18  ? 55  THR A CA  1 
ATOM   431  C  C   . THR A 1 55  ? 1.530   10.220  5.382   1.00 14.13  ? 55  THR A C   1 
ATOM   432  O  O   . THR A 1 55  ? 2.591   10.785  5.645   1.00 14.84  ? 55  THR A O   1 
ATOM   433  C  CB  . THR A 1 55  ? 0.318   12.392  5.335   1.00 20.96  ? 55  THR A CB  1 
ATOM   434  O  OG1 . THR A 1 55  ? -0.907  13.029  5.674   1.00 30.80  ? 55  THR A OG1 1 
ATOM   435  C  CG2 . THR A 1 55  ? 0.559   12.438  3.843   1.00 29.69  ? 55  THR A CG2 1 
ATOM   436  N  N   . SER A 1 56  ? 1.483   8.997   4.863   1.00 14.83  ? 56  SER A N   1 
ATOM   437  C  CA  . SER A 1 56  ? 2.751   8.387   4.491   1.00 13.20  ? 56  SER A CA  1 
ATOM   438  C  C   . SER A 1 56  ? 3.270   9.051   3.212   1.00 15.45  ? 56  SER A C   1 
ATOM   439  O  O   . SER A 1 56  ? 2.499   9.513   2.391   1.00 16.84  ? 56  SER A O   1 
ATOM   440  C  CB  . SER A 1 56  ? 2.663   6.892   4.346   1.00 15.22  ? 56  SER A CB  1 
ATOM   441  O  OG  . SER A 1 56  ? 1.807   6.550   3.254   1.00 17.09  ? 56  SER A OG  1 
ATOM   442  N  N   . LEU A 1 57  ? 4.588   9.021   3.015   1.00 14.18  ? 57  LEU A N   1 
ATOM   443  C  CA  . LEU A 1 57  ? 5.103   9.639   1.808   1.00 18.87  ? 57  LEU A CA  1 
ATOM   444  C  C   . LEU A 1 57  ? 5.956   8.665   0.999   1.00 16.67  ? 57  LEU A C   1 
ATOM   445  O  O   . LEU A 1 57  ? 5.895   8.652   -0.224  1.00 16.92  ? 57  LEU A O   1 
ATOM   446  C  CB  . LEU A 1 57  ? 5.949   10.818  2.232   1.00 21.38  ? 57  LEU A CB  1 
ATOM   447  C  CG  . LEU A 1 57  ? 5.156   12.023  2.802   1.00 23.74  ? 57  LEU A CG  1 
ATOM   448  C  CD1 . LEU A 1 57  ? 6.113   13.133  3.241   1.00 30.46  ? 57  LEU A CD1 1 
ATOM   449  C  CD2 . LEU A 1 57  ? 4.070   12.606  1.860   1.00 33.03  ? 57  LEU A CD2 1 
ATOM   450  N  N   . ARG A 1 58  ? 6.862   7.910   1.637   1.00 14.81  ? 58  ARG A N   1 
ATOM   451  C  CA  . ARG A 1 58  ? 7.965   7.281   0.933   1.00 13.96  ? 58  ARG A CA  1 
ATOM   452  C  C   . ARG A 1 58  ? 8.468   6.066   1.697   1.00 13.73  ? 58  ARG A C   1 
ATOM   453  O  O   . ARG A 1 58  ? 8.336   6.035   2.911   1.00 16.11  ? 58  ARG A O   1 
ATOM   454  C  CB  . ARG A 1 58  ? 9.114   8.262   0.755   1.00 18.88  ? 58  ARG A CB  1 
ATOM   455  C  CG  . ARG A 1 58  ? 10.183  7.788   -0.201  1.00 22.43  ? 58  ARG A CG  1 
ATOM   456  C  CD  . ARG A 1 58  ? 11.117  8.967   -0.401  1.00 20.93  ? 58  ARG A CD  1 
ATOM   457  N  NE  . ARG A 1 58  ? 11.949  9.125   0.798   1.00 17.41  ? 58  ARG A NE  1 
ATOM   458  C  CZ  . ARG A 1 58  ? 13.279  9.304   0.800   1.00 17.35  ? 58  ARG A CZ  1 
ATOM   459  N  NH1 . ARG A 1 58  ? 13.921  9.575   -0.314  1.00 20.89  ? 58  ARG A NH1 1 
ATOM   460  N  NH2 . ARG A 1 58  ? 13.916  9.347   1.955   1.00 17.06  ? 58  ARG A NH2 1 
ATOM   461  N  N   . ILE A 1 59  ? 9.023   5.083   1.017   1.00 12.70  ? 59  ILE A N   1 
ATOM   462  C  CA  . ILE A 1 59  ? 9.677   3.947   1.640   1.00 12.53  ? 59  ILE A CA  1 
ATOM   463  C  C   . ILE A 1 59  ? 11.104  3.960   1.141   1.00 12.31  ? 59  ILE A C   1 
ATOM   464  O  O   . ILE A 1 59  ? 11.352  4.225   -0.038  1.00 14.76  ? 59  ILE A O   1 
ATOM   465  C  CB  . ILE A 1 59  ? 8.917   2.644   1.365   1.00 12.74  ? 59  ILE A CB  1 
ATOM   466  C  CG1 . ILE A 1 59  ? 9.456   1.511   2.255   1.00 13.16  ? 59  ILE A CG1 1 
ATOM   467  C  CG2 . ILE A 1 59  ? 8.905   2.249   -0.138  1.00 15.30  ? 59  ILE A CG2 1 
ATOM   468  C  CD1 . ILE A 1 59  ? 8.558   0.269   2.146   1.00 16.15  ? 59  ILE A CD1 1 
ATOM   469  N  N   . LEU A 1 60  ? 12.047  3.656   2.049   1.00 13.51  ? 60  LEU A N   1 
ATOM   470  C  CA  . LEU A 1 60  ? 13.460  3.811   1.726   1.00 11.70  ? 60  LEU A CA  1 
ATOM   471  C  C   . LEU A 1 60  ? 14.233  2.626   2.312   1.00 12.18  ? 60  LEU A C   1 
ATOM   472  O  O   . LEU A 1 60  ? 14.032  2.263   3.479   1.00 12.25  ? 60  LEU A O   1 
ATOM   473  C  CB  . LEU A 1 60  ? 13.937  5.099   2.437   1.00 14.43  ? 60  LEU A CB  1 
ATOM   474  C  CG  . LEU A 1 60  ? 15.454  5.355   2.421   1.00 15.37  ? 60  LEU A CG  1 
ATOM   475  C  CD1 . LEU A 1 60  ? 15.960  5.608   1.006   1.00 16.58  ? 60  LEU A CD1 1 
ATOM   476  C  CD2 . LEU A 1 60  ? 15.860  6.511   3.317   1.00 14.91  ? 60  LEU A CD2 1 
ATOM   477  N  N   . ASN A 1 61  ? 15.154  2.084   1.521   1.00 11.79  ? 61  ASN A N   1 
ATOM   478  C  CA  . ASN A 1 61  ? 16.131  1.103   1.977   1.00 11.18  ? 61  ASN A CA  1 
ATOM   479  C  C   . ASN A 1 61  ? 17.328  1.953   2.424   1.00 12.70  ? 61  ASN A C   1 
ATOM   480  O  O   . ASN A 1 61  ? 17.964  2.595   1.607   1.00 12.73  ? 61  ASN A O   1 
ATOM   481  C  CB  . ASN A 1 61  ? 16.493  0.140   0.847   1.00 12.08  ? 61  ASN A CB  1 
ATOM   482  C  CG  . ASN A 1 61  ? 17.568  -0.842  1.252   1.00 11.24  ? 61  ASN A CG  1 
ATOM   483  O  OD1 . ASN A 1 61  ? 18.400  -0.584  2.144   1.00 13.50  ? 61  ASN A OD1 1 
ATOM   484  N  ND2 . ASN A 1 61  ? 17.518  -2.009  0.650   1.00 14.04  ? 61  ASN A ND2 1 
ATOM   485  N  N   . THR A 1 62  ? 17.642  1.965   3.734   1.00 13.10  ? 62  THR A N   1 
ATOM   486  C  CA  . THR A 1 62  ? 18.673  2.861   4.281   1.00 12.61  ? 62  THR A CA  1 
ATOM   487  C  C   . THR A 1 62  ? 20.028  2.172   4.222   1.00 13.21  ? 62  THR A C   1 
ATOM   488  O  O   . THR A 1 62  ? 21.064  2.791   4.575   1.00 16.26  ? 62  THR A O   1 
ATOM   489  C  CB  . THR A 1 62  ? 18.401  3.179   5.774   1.00 13.30  ? 62  THR A CB  1 
ATOM   490  O  OG1 . THR A 1 62  ? 18.534  1.924   6.471   1.00 12.84  ? 62  THR A OG1 1 
ATOM   491  C  CG2 . THR A 1 62  ? 17.054  3.824   6.012   1.00 15.29  ? 62  THR A CG2 1 
ATOM   492  N  N   . GLY A 1 63  ? 20.095  0.866   3.814   1.00 12.08  ? 63  GLY A N   1 
ATOM   493  C  CA  . GLY A 1 63  ? 21.320  0.095   3.907   1.00 12.59  ? 63  GLY A CA  1 
ATOM   494  C  C   . GLY A 1 63  ? 21.405  -0.703  5.209   1.00 12.78  ? 63  GLY A C   1 
ATOM   495  O  O   . GLY A 1 63  ? 22.250  -1.615  5.327   1.00 14.19  ? 63  GLY A O   1 
ATOM   496  N  N   A TYR A 1 64  ? 20.485  -0.421  6.143   0.50 11.89  ? 64  TYR A N   1 
ATOM   497  N  N   B TYR A 1 64  ? 20.542  -0.407  6.205   0.50 12.56  ? 64  TYR A N   1 
ATOM   498  C  CA  A TYR A 1 64  ? 20.487  -1.080  7.439   0.50 12.56  ? 64  TYR A CA  1 
ATOM   499  C  CA  B TYR A 1 64  ? 20.522  -1.199  7.442   0.50 12.65  ? 64  TYR A CA  1 
ATOM   500  C  C   A TYR A 1 64  ? 19.135  -1.725  7.702   0.50 11.05  ? 64  TYR A C   1 
ATOM   501  C  C   B TYR A 1 64  ? 19.119  -1.699  7.772   0.50 11.62  ? 64  TYR A C   1 
ATOM   502  O  O   A TYR A 1 64  ? 19.045  -2.688  8.447   0.50 14.56  ? 64  TYR A O   1 
ATOM   503  O  O   B TYR A 1 64  ? 18.983  -2.502  8.689   0.50 14.58  ? 64  TYR A O   1 
ATOM   504  C  CB  A TYR A 1 64  ? 20.820  -0.069  8.540   0.50 14.51  ? 64  TYR A CB  1 
ATOM   505  C  CB  B TYR A 1 64  ? 21.041  -0.463  8.695   0.50 12.78  ? 64  TYR A CB  1 
ATOM   506  C  CG  A TYR A 1 64  ? 22.222  0.482   8.441   0.50 14.94  ? 64  TYR A CG  1 
ATOM   507  C  CG  B TYR A 1 64  ? 20.702  1.007   8.767   0.50 16.44  ? 64  TYR A CG  1 
ATOM   508  C  CD1 A TYR A 1 64  ? 23.294  -0.335  8.746   0.50 18.23  ? 64  TYR A CD1 1 
ATOM   509  C  CD1 B TYR A 1 64  ? 21.505  1.948   8.149   0.50 15.48  ? 64  TYR A CD1 1 
ATOM   510  C  CD2 A TYR A 1 64  ? 22.504  1.748   7.953   0.50 14.05  ? 64  TYR A CD2 1 
ATOM   511  C  CD2 B TYR A 1 64  ? 19.556  1.481   9.403   0.50 19.96  ? 64  TYR A CD2 1 
ATOM   512  C  CE1 A TYR A 1 64  ? 24.606  0.098   8.722   0.50 16.55  ? 64  TYR A CE1 1 
ATOM   513  C  CE1 B TYR A 1 64  ? 21.211  3.305   8.190   0.50 21.04  ? 64  TYR A CE1 1 
ATOM   514  C  CE2 A TYR A 1 64  ? 23.815  2.210   7.897   0.50 18.22  ? 64  TYR A CE2 1 
ATOM   515  C  CE2 B TYR A 1 64  ? 19.166  2.818   9.328   0.50 16.11  ? 64  TYR A CE2 1 
ATOM   516  C  CZ  A TYR A 1 64  ? 24.852  1.377   8.283   0.50 20.75  ? 64  TYR A CZ  1 
ATOM   517  C  CZ  B TYR A 1 64  ? 20.053  3.744   8.806   0.50 18.81  ? 64  TYR A CZ  1 
ATOM   518  O  OH  A TYR A 1 64  ? 26.134  1.816   8.226   0.50 26.02  ? 64  TYR A OH  1 
ATOM   519  O  OH  B TYR A 1 64  ? 19.833  5.094   8.738   0.50 21.30  ? 64  TYR A OH  1 
ATOM   520  N  N   . LEU A 1 65  ? 18.085  -1.204  7.092   1.00 11.57  ? 65  LEU A N   1 
ATOM   521  C  CA  . LEU A 1 65  ? 16.714  -1.602  7.310   1.00 11.34  ? 65  LEU A CA  1 
ATOM   522  C  C   . LEU A 1 65  ? 15.896  -0.933  6.186   1.00 11.11  ? 65  LEU A C   1 
ATOM   523  O  O   . LEU A 1 65  ? 16.491  -0.333  5.283   1.00 11.69  ? 65  LEU A O   1 
ATOM   524  C  CB  . LEU A 1 65  ? 16.202  -1.245  8.722   1.00 12.53  ? 65  LEU A CB  1 
ATOM   525  C  CG  . LEU A 1 65  ? 16.481  0.178   9.204   1.00 13.09  ? 65  LEU A CG  1 
ATOM   526  C  CD1 . LEU A 1 65  ? 15.670  1.189   8.413   1.00 13.70  ? 65  LEU A CD1 1 
ATOM   527  C  CD2 . LEU A 1 65  ? 16.168  0.304   10.686  1.00 19.42  ? 65  LEU A CD2 1 
ATOM   528  N  N   . PHE A 1 66  ? 14.578  -1.074  6.193   1.00 11.44  ? 66  PHE A N   1 
ATOM   529  C  CA  . PHE A 1 66  ? 13.741  -0.185  5.397   1.00 10.97  ? 66  PHE A CA  1 
ATOM   530  C  C   . PHE A 1 66  ? 12.809  0.582   6.323   1.00 10.56  ? 66  PHE A C   1 
ATOM   531  O  O   . PHE A 1 66  ? 12.467  0.105   7.401   1.00 11.90  ? 66  PHE A O   1 
ATOM   532  C  CB  . PHE A 1 66  ? 12.995  -0.993  4.299   1.00 12.64  ? 66  PHE A CB  1 
ATOM   533  C  CG  . PHE A 1 66  ? 11.830  -1.789  4.819   1.00 11.18  ? 66  PHE A CG  1 
ATOM   534  C  CD1 . PHE A 1 66  ? 10.575  -1.242  4.977   1.00 13.03  ? 66  PHE A CD1 1 
ATOM   535  C  CD2 . PHE A 1 66  ? 12.023  -3.137  5.160   1.00 12.63  ? 66  PHE A CD2 1 
ATOM   536  C  CE1 . PHE A 1 66  ? 9.563   -2.007  5.519   1.00 12.86  ? 66  PHE A CE1 1 
ATOM   537  C  CE2 . PHE A 1 66  ? 10.973  -3.921  5.632   1.00 12.03  ? 66  PHE A CE2 1 
ATOM   538  C  CZ  . PHE A 1 66  ? 9.731   -3.364  5.739   1.00 11.71  ? 66  PHE A CZ  1 
ATOM   539  N  N   . GLN A 1 67  ? 12.449  1.772   5.869   1.00 11.80  ? 67  GLN A N   1 
ATOM   540  C  CA  . GLN A 1 67  ? 11.608  2.612   6.682   1.00 13.08  ? 67  GLN A CA  1 
ATOM   541  C  C   . GLN A 1 67  ? 10.562  3.277   5.809   1.00 11.19  ? 67  GLN A C   1 
ATOM   542  O  O   . GLN A 1 67  ? 10.810  3.660   4.656   1.00 13.61  ? 67  GLN A O   1 
ATOM   543  C  CB  . GLN A 1 67  ? 12.376  3.684   7.449   1.00 15.42  ? 67  GLN A CB  1 
ATOM   544  C  CG  . GLN A 1 67  ? 13.112  4.621   6.571   1.00 15.60  ? 67  GLN A CG  1 
ATOM   545  C  CD  . GLN A 1 67  ? 14.013  5.540   7.340   1.00 22.53  ? 67  GLN A CD  1 
ATOM   546  O  OE1 . GLN A 1 67  ? 14.675  5.143   8.298   1.00 24.45  ? 67  GLN A OE1 1 
ATOM   547  N  NE2 . GLN A 1 67  ? 14.056  6.795   6.919   1.00 24.99  ? 67  GLN A NE2 1 
ATOM   548  N  N   . VAL A 1 68  ? 9.386   3.441   6.386   1.00 12.37  ? 68  VAL A N   1 
ATOM   549  C  CA  . VAL A 1 68  ? 8.302   4.180   5.758   1.00 13.69  ? 68  VAL A CA  1 
ATOM   550  C  C   . VAL A 1 68  ? 8.239   5.527   6.477   1.00 13.64  ? 68  VAL A C   1 
ATOM   551  O  O   . VAL A 1 68  ? 8.080   5.557   7.703   1.00 13.07  ? 68  VAL A O   1 
ATOM   552  C  CB  . VAL A 1 68  ? 6.964   3.418   5.879   1.00 13.84  ? 68  VAL A CB  1 
ATOM   553  C  CG1 . VAL A 1 68  ? 5.790   4.321   5.467   1.00 14.24  ? 68  VAL A CG1 1 
ATOM   554  C  CG2 . VAL A 1 68  ? 7.003   2.126   5.060   1.00 14.10  ? 68  VAL A CG2 1 
ATOM   555  N  N   . GLU A 1 69  ? 8.323   6.589   5.704   1.00 13.02  ? 69  GLU A N   1 
ATOM   556  C  CA  . GLU A 1 69  ? 8.372   7.928   6.253   1.00 11.87  ? 69  GLU A CA  1 
ATOM   557  C  C   . GLU A 1 69  ? 7.005   8.612   6.121   1.00 13.17  ? 69  GLU A C   1 
ATOM   558  O  O   . GLU A 1 69  ? 6.269   8.401   5.128   1.00 14.66  ? 69  GLU A O   1 
ATOM   559  C  CB  . GLU A 1 69  ? 9.352   8.742   5.441   1.00 14.27  ? 69  GLU A CB  1 
ATOM   560  C  CG  . GLU A 1 69  ? 10.746  8.143   5.507   1.00 15.93  ? 69  GLU A CG  1 
ATOM   561  C  CD  . GLU A 1 69  ? 11.716  8.612   4.453   1.00 16.78  ? 69  GLU A CD  1 
ATOM   562  O  OE1 . GLU A 1 69  ? 12.913  8.324   4.603   1.00 24.50  ? 69  GLU A OE1 1 
ATOM   563  O  OE2 . GLU A 1 69  ? 11.232  9.307   3.527   1.00 21.24  ? 69  GLU A OE2 1 
ATOM   564  N  N   . PHE A 1 70  ? 6.727   9.519   7.073   1.00 12.72  ? 70  PHE A N   1 
ATOM   565  C  CA  . PHE A 1 70  ? 5.473   10.250  7.115   1.00 12.72  ? 70  PHE A CA  1 
ATOM   566  C  C   . PHE A 1 70  ? 5.755   11.736  7.010   1.00 13.51  ? 70  PHE A C   1 
ATOM   567  O  O   . PHE A 1 70  ? 6.803   12.226  7.396   1.00 14.88  ? 70  PHE A O   1 
ATOM   568  C  CB  . PHE A 1 70  ? 4.716   9.911   8.409   1.00 12.65  ? 70  PHE A CB  1 
ATOM   569  C  CG  . PHE A 1 70  ? 4.172   8.513   8.403   1.00 12.50  ? 70  PHE A CG  1 
ATOM   570  C  CD1 . PHE A 1 70  ? 4.998   7.422   8.620   1.00 12.85  ? 70  PHE A CD1 1 
ATOM   571  C  CD2 . PHE A 1 70  ? 2.852   8.275   8.068   1.00 13.23  ? 70  PHE A CD2 1 
ATOM   572  C  CE1 . PHE A 1 70  ? 4.509   6.116   8.532   1.00 15.94  ? 70  PHE A CE1 1 
ATOM   573  C  CE2 . PHE A 1 70  ? 2.361   6.977   7.985   1.00 13.84  ? 70  PHE A CE2 1 
ATOM   574  C  CZ  . PHE A 1 70  ? 3.201   5.880   8.203   1.00 13.58  ? 70  PHE A CZ  1 
ATOM   575  N  N   . ASP A 1 71  ? 4.713   12.466  6.587   1.00 16.33  ? 71  ASP A N   1 
ATOM   576  C  CA  . ASP A 1 71  ? 4.779   13.910  6.691   1.00 16.76  ? 71  ASP A CA  1 
ATOM   577  C  C   . ASP A 1 71  ? 4.579   14.309  8.153   1.00 15.10  ? 71  ASP A C   1 
ATOM   578  O  O   . ASP A 1 71  ? 3.470   14.139  8.722   1.00 22.05  ? 71  ASP A O   1 
ATOM   579  C  CB  . ASP A 1 71  ? 3.589   14.507  5.918   1.00 21.27  ? 71  ASP A CB  1 
ATOM   580  C  CG  . ASP A 1 71  ? 3.525   16.032  6.040   1.00 23.18  ? 71  ASP A CG  1 
ATOM   581  O  OD1 . ASP A 1 71  ? 4.473   16.607  6.537   1.00 23.08  ? 71  ASP A OD1 1 
ATOM   582  O  OD2 . ASP A 1 71  ? 2.472   16.577  5.781   1.00 25.86  ? 71  ASP A OD2 1 
ATOM   583  N  N   . ASP A 1 72  ? 5.640   14.762  8.823   1.00 15.83  ? 72  ASP A N   1 
ATOM   584  C  CA  . ASP A 1 72  ? 5.555   15.165  10.213  1.00 16.28  ? 72  ASP A CA  1 
ATOM   585  C  C   . ASP A 1 72  ? 5.754   16.690  10.298  1.00 18.64  ? 72  ASP A C   1 
ATOM   586  O  O   . ASP A 1 72  ? 6.315   17.182  11.278  1.00 20.03  ? 72  ASP A O   1 
ATOM   587  C  CB  . ASP A 1 72  ? 6.631   14.442  11.032  1.00 17.15  ? 72  ASP A CB  1 
ATOM   588  C  CG  . ASP A 1 72  ? 8.068   14.709  10.601  1.00 18.08  ? 72  ASP A CG  1 
ATOM   589  O  OD1 . ASP A 1 72  ? 8.264   15.256  9.470   1.00 21.67  ? 72  ASP A OD1 1 
ATOM   590  O  OD2 . ASP A 1 72  ? 8.993   14.196  11.289  1.00 19.81  ? 72  ASP A OD2 1 
ATOM   591  N  N   . SER A 1 73  ? 5.373   17.416  9.236   1.00 19.68  ? 73  SER A N   1 
ATOM   592  C  CA  . SER A 1 73  ? 5.486   18.901  9.242   1.00 19.47  ? 73  SER A CA  1 
ATOM   593  C  C   . SER A 1 73  ? 4.276   19.587  9.898   1.00 26.15  ? 73  SER A C   1 
ATOM   594  O  O   . SER A 1 73  ? 4.212   20.797  10.030  1.00 30.93  ? 73  SER A O   1 
ATOM   595  C  CB  . SER A 1 73  ? 5.689   19.352  7.816   1.00 21.14  ? 73  SER A CB  1 
ATOM   596  O  OG  . SER A 1 73  ? 4.407   19.331  7.140   1.00 19.90  ? 73  SER A OG  1 
ATOM   597  N  N   . GLN A 1 74  ? 3.320   18.795  10.406  1.00 22.73  ? 74  GLN A N   1 
ATOM   598  C  CA  . GLN A 1 74  ? 2.110   19.254  11.078  1.00 27.12  ? 74  GLN A CA  1 
ATOM   599  C  C   . GLN A 1 74  ? 1.645   18.116  11.980  1.00 22.99  ? 74  GLN A C   1 
ATOM   600  O  O   . GLN A 1 74  ? 2.056   16.983  11.743  1.00 20.38  ? 74  GLN A O   1 
ATOM   601  C  CB  . GLN A 1 74  ? 0.985   19.334  10.027  1.00 32.91  ? 74  GLN A CB  1 
ATOM   602  C  CG  . GLN A 1 74  ? 0.947   20.609  9.223   1.00 43.12  ? 74  GLN A CG  1 
ATOM   603  C  CD  . GLN A 1 74  ? -0.407  20.586  8.569   1.00 44.26  ? 74  GLN A CD  1 
ATOM   604  O  OE1 . GLN A 1 74  ? -1.394  20.993  9.180   1.00 51.65  ? 74  GLN A OE1 1 
ATOM   605  N  NE2 . GLN A 1 74  ? -0.461  20.021  7.370   1.00 38.06  ? 74  GLN A NE2 1 
ATOM   606  N  N   A ASP A 1 75  ? 0.739   18.392  12.936  0.50 28.02  ? 75  ASP A N   1 
ATOM   607  N  N   B ASP A 1 75  ? 0.832   18.486  12.966  0.50 29.11  ? 75  ASP A N   1 
ATOM   608  C  CA  A ASP A 1 75  ? 0.358   17.438  13.975  0.50 27.60  ? 75  ASP A CA  1 
ATOM   609  C  CA  B ASP A 1 75  ? 0.217   17.566  13.893  0.50 30.37  ? 75  ASP A CA  1 
ATOM   610  C  C   A ASP A 1 75  ? -0.759  16.519  13.492  0.50 28.22  ? 75  ASP A C   1 
ATOM   611  C  C   B ASP A 1 75  ? -0.790  16.726  13.112  0.50 30.41  ? 75  ASP A C   1 
ATOM   612  O  O   A ASP A 1 75  ? -1.923  16.674  13.850  0.50 41.49  ? 75  ASP A O   1 
ATOM   613  O  O   B ASP A 1 75  ? -1.902  17.183  12.844  0.50 28.13  ? 75  ASP A O   1 
ATOM   614  C  CB  A ASP A 1 75  ? -0.112  18.119  15.259  0.50 28.85  ? 75  ASP A CB  1 
ATOM   615  C  CB  B ASP A 1 75  ? -0.417  18.356  15.042  0.50 39.83  ? 75  ASP A CB  1 
ATOM   616  C  CG  A ASP A 1 75  ? 0.885   18.079  16.397  0.50 23.15  ? 75  ASP A CG  1 
ATOM   617  C  CG  B ASP A 1 75  ? -1.083  17.427  16.105  0.50 41.38  ? 75  ASP A CG  1 
ATOM   618  O  OD1 A ASP A 1 75  ? 1.843   17.272  16.313  0.50 33.94  ? 75  ASP A OD1 1 
ATOM   619  O  OD1 B ASP A 1 75  ? -1.214  16.232  15.779  0.50 52.30  ? 75  ASP A OD1 1 
ATOM   620  O  OD2 A ASP A 1 75  ? 0.681   18.829  17.358  0.50 30.18  ? 75  ASP A OD2 1 
ATOM   621  O  OD2 B ASP A 1 75  ? -1.490  17.909  17.225  0.50 53.89  ? 75  ASP A OD2 1 
ATOM   622  N  N   . LYS A 1 76  ? -0.372  15.521  12.713  1.00 23.33  ? 76  LYS A N   1 
ATOM   623  C  CA  . LYS A 1 76  ? -1.298  14.575  12.103  1.00 28.36  ? 76  LYS A CA  1 
ATOM   624  C  C   . LYS A 1 76  ? -1.437  13.319  12.949  1.00 33.98  ? 76  LYS A C   1 
ATOM   625  O  O   . LYS A 1 76  ? -2.360  13.138  13.733  1.00 40.23  ? 76  LYS A O   1 
ATOM   626  C  CB  . LYS A 1 76  ? -0.752  14.276  10.707  1.00 26.80  ? 76  LYS A CB  1 
ATOM   627  C  CG  . LYS A 1 76  ? -1.068  15.401  9.725   1.00 29.00  ? 76  LYS A CG  1 
ATOM   628  C  CD  . LYS A 1 76  ? -0.392  15.258  8.372   1.00 31.38  ? 76  LYS A CD  1 
ATOM   629  C  CE  . LYS A 1 76  ? -0.934  16.225  7.328   1.00 24.64  ? 76  LYS A CE  1 
ATOM   630  N  NZ  . LYS A 1 76  ? -0.231  16.070  6.041   1.00 34.42  ? 76  LYS A NZ  1 
ATOM   631  N  N   . ALA A 1 77  ? -0.481  12.461  12.773  1.00 26.66  ? 77  ALA A N   1 
ATOM   632  C  CA  . ALA A 1 77  ? -0.463  11.190  13.482  1.00 24.73  ? 77  ALA A CA  1 
ATOM   633  C  C   . ALA A 1 77  ? 0.363   11.406  14.748  1.00 21.84  ? 77  ALA A C   1 
ATOM   634  O  O   . ALA A 1 77  ? 1.528   11.810  14.647  1.00 25.17  ? 77  ALA A O   1 
ATOM   635  C  CB  . ALA A 1 77  ? 0.233   10.247  12.547  1.00 27.77  ? 77  ALA A CB  1 
ATOM   636  N  N   . VAL A 1 78  ? -0.215  11.186  15.927  1.00 16.30  ? 78  VAL A N   1 
ATOM   637  C  CA  . VAL A 1 78  ? 0.533   11.448  17.141  1.00 17.32  ? 78  VAL A CA  1 
ATOM   638  C  C   . VAL A 1 78  ? 0.271   10.359  18.166  1.00 16.31  ? 78  VAL A C   1 
ATOM   639  O  O   . VAL A 1 78  ? -0.752  9.671   18.161  1.00 18.82  ? 78  VAL A O   1 
ATOM   640  C  CB  . VAL A 1 78  ? 0.236   12.821  17.721  1.00 24.30  ? 78  VAL A CB  1 
ATOM   641  C  CG1 . VAL A 1 78  ? 0.404   13.973  16.753  1.00 23.68  ? 78  VAL A CG1 1 
ATOM   642  C  CG2 . VAL A 1 78  ? -1.131  12.811  18.272  1.00 22.20  ? 78  VAL A CG2 1 
ATOM   643  N  N   . LEU A 1 79  ? 1.240   10.211  19.045  1.00 13.93  ? 79  LEU A N   1 
ATOM   644  C  CA  . LEU A 1 79  ? 1.243   9.321   20.181  1.00 13.60  ? 79  LEU A CA  1 
ATOM   645  C  C   . LEU A 1 79  ? 1.265   10.195  21.421  1.00 13.75  ? 79  LEU A C   1 
ATOM   646  O  O   . LEU A 1 79  ? 2.097   11.124  21.533  1.00 15.20  ? 79  LEU A O   1 
ATOM   647  C  CB  . LEU A 1 79  ? 2.478   8.416   20.071  1.00 14.55  ? 79  LEU A CB  1 
ATOM   648  C  CG  . LEU A 1 79  ? 2.590   7.372   21.158  1.00 14.19  ? 79  LEU A CG  1 
ATOM   649  C  CD1 . LEU A 1 79  ? 1.494   6.333   21.032  1.00 19.10  ? 79  LEU A CD1 1 
ATOM   650  C  CD2 . LEU A 1 79  ? 3.957   6.704   21.060  1.00 15.26  ? 79  LEU A CD2 1 
ATOM   651  N  N   . LYS A 1 80  ? 0.393   9.895   22.365  1.00 15.01  ? 80  LYS A N   1 
ATOM   652  C  CA  . LYS A 1 80  ? 0.380   10.604  23.634  1.00 15.03  ? 80  LYS A CA  1 
ATOM   653  C  C   . LYS A 1 80  ? -0.102  9.669   24.724  1.00 13.81  ? 80  LYS A C   1 
ATOM   654  O  O   . LYS A 1 80  ? -0.463  8.509   24.430  1.00 15.74  ? 80  LYS A O   1 
ATOM   655  C  CB  . LYS A 1 80  ? -0.409  11.909  23.619  1.00 22.05  ? 80  LYS A CB  1 
ATOM   656  C  CG  . LYS A 1 80  ? -1.902  11.740  23.413  1.00 27.91  ? 80  LYS A CG  1 
ATOM   657  C  CD  . LYS A 1 80  ? -2.636  13.108  23.309  1.00 31.86  ? 80  LYS A CD  1 
ATOM   658  C  CE  . LYS A 1 80  ? -1.896  14.108  22.437  1.00 36.93  ? 80  LYS A CE  1 
ATOM   659  N  N   . GLY A 1 81  ? -0.123  10.171  25.947  1.00 16.28  ? 81  GLY A N   1 
ATOM   660  C  CA  . GLY A 1 81  ? -0.611  9.354   27.052  1.00 17.95  ? 81  GLY A CA  1 
ATOM   661  C  C   . GLY A 1 81  ? 0.404   8.284   27.420  1.00 18.08  ? 81  GLY A C   1 
ATOM   662  O  O   . GLY A 1 81  ? 1.589   8.434   27.179  1.00 17.59  ? 81  GLY A O   1 
ATOM   663  N  N   . GLY A 1 82  ? -0.052  7.233   28.085  1.00 21.68  ? 82  GLY A N   1 
ATOM   664  C  CA  . GLY A 1 82  ? 0.887   6.257   28.598  1.00 26.80  ? 82  GLY A CA  1 
ATOM   665  C  C   . GLY A 1 82  ? 1.848   6.911   29.567  1.00 25.90  ? 82  GLY A C   1 
ATOM   666  O  O   . GLY A 1 82  ? 1.416   7.692   30.429  1.00 26.55  ? 82  GLY A O   1 
ATOM   667  N  N   . PRO A 1 83  ? 3.183   6.678   29.393  1.00 19.20  ? 83  PRO A N   1 
ATOM   668  C  CA  . PRO A 1 83  ? 4.175   7.305   30.247  1.00 19.41  ? 83  PRO A CA  1 
ATOM   669  C  C   . PRO A 1 83  ? 4.529   8.714   29.806  1.00 17.12  ? 83  PRO A C   1 
ATOM   670  O  O   . PRO A 1 83  ? 5.307   9.359   30.490  1.00 22.78  ? 83  PRO A O   1 
ATOM   671  C  CB  . PRO A 1 83  ? 5.387   6.374   30.045  1.00 18.28  ? 83  PRO A CB  1 
ATOM   672  C  CG  . PRO A 1 83  ? 5.285   5.992   28.589  1.00 17.38  ? 83  PRO A CG  1 
ATOM   673  C  CD  . PRO A 1 83  ? 3.800   5.788   28.371  1.00 17.39  ? 83  PRO A CD  1 
ATOM   674  N  N   . LEU A 1 84  ? 3.928   9.132   28.669  1.00 15.87  ? 84  LEU A N   1 
ATOM   675  C  CA  . LEU A 1 84  ? 4.452   10.308  27.998  1.00 15.80  ? 84  LEU A CA  1 
ATOM   676  C  C   . LEU A 1 84  ? 3.847   11.575  28.603  1.00 18.57  ? 84  LEU A C   1 
ATOM   677  O  O   . LEU A 1 84  ? 2.636   11.596  28.869  1.00 20.98  ? 84  LEU A O   1 
ATOM   678  C  CB  . LEU A 1 84  ? 4.192   10.237  26.485  1.00 14.20  ? 84  LEU A CB  1 
ATOM   679  C  CG  . LEU A 1 84  ? 4.760   9.005   25.801  1.00 13.41  ? 84  LEU A CG  1 
ATOM   680  C  CD1 . LEU A 1 84  ? 4.251   8.912   24.353  1.00 16.01  ? 84  LEU A CD1 1 
ATOM   681  C  CD2 . LEU A 1 84  ? 6.309   9.001   25.865  1.00 14.11  ? 84  LEU A CD2 1 
ATOM   682  N  N   . ASP A 1 85  ? 4.673   12.636  28.627  1.00 19.82  ? 85  ASP A N   1 
ATOM   683  C  CA  . ASP A 1 85  ? 4.224   14.000  28.854  1.00 23.08  ? 85  ASP A CA  1 
ATOM   684  C  C   . ASP A 1 85  ? 4.149   14.609  27.457  1.00 22.05  ? 85  ASP A C   1 
ATOM   685  O  O   . ASP A 1 85  ? 5.129   14.599  26.696  1.00 29.37  ? 85  ASP A O   1 
ATOM   686  C  CB  . ASP A 1 85  ? 5.101   14.725  29.901  1.00 25.27  ? 85  ASP A CB  1 
ATOM   687  C  CG  . ASP A 1 85  ? 5.038   14.195  31.339  1.00 30.85  ? 85  ASP A CG  1 
ATOM   688  O  OD1 . ASP A 1 85  ? 3.952   13.728  31.782  1.00 39.86  ? 85  ASP A OD1 1 
ATOM   689  O  OD2 . ASP A 1 85  ? 6.089   14.258  32.048  1.00 33.75  ? 85  ASP A OD2 1 
ATOM   690  N  N   . GLY A 1 86  ? 3.052   15.295  27.158  1.00 30.31  ? 86  GLY A N   1 
ATOM   691  C  CA  . GLY A 1 86  ? 2.942   16.029  25.904  1.00 24.05  ? 86  GLY A CA  1 
ATOM   692  C  C   . GLY A 1 86  ? 2.708   15.140  24.671  1.00 21.78  ? 86  GLY A C   1 
ATOM   693  O  O   . GLY A 1 86  ? 2.137   14.073  24.761  1.00 27.59  ? 86  GLY A O   1 
ATOM   694  N  N   . THR A 1 87  ? 3.109   15.594  23.477  1.00 21.20  ? 87  THR A N   1 
ATOM   695  C  CA  . THR A 1 87  ? 2.613   15.061  22.224  1.00 22.47  ? 87  THR A CA  1 
ATOM   696  C  C   . THR A 1 87  ? 3.835   14.640  21.425  1.00 16.31  ? 87  THR A C   1 
ATOM   697  O  O   . THR A 1 87  ? 4.779   15.433  21.234  1.00 17.63  ? 87  THR A O   1 
ATOM   698  C  CB  . THR A 1 87  ? 1.838   16.168  21.471  1.00 30.93  ? 87  THR A CB  1 
ATOM   699  O  OG1 . THR A 1 87  ? 0.615   16.304  22.195  1.00 34.73  ? 87  THR A OG1 1 
ATOM   700  C  CG2 . THR A 1 87  ? 1.502   15.786  20.036  1.00 29.13  ? 87  THR A CG2 1 
ATOM   701  N  N   . TYR A 1 88  ? 3.770   13.450  20.843  1.00 13.55  ? 88  TYR A N   1 
ATOM   702  C  CA  . TYR A 1 88  ? 4.863   12.944  20.037  1.00 13.78  ? 88  TYR A CA  1 
ATOM   703  C  C   . TYR A 1 88  ? 4.344   12.651  18.632  1.00 12.32  ? 88  TYR A C   1 
ATOM   704  O  O   . TYR A 1 88  ? 3.371   11.964  18.476  1.00 16.70  ? 88  TYR A O   1 
ATOM   705  C  CB  . TYR A 1 88  ? 5.485   11.712  20.651  1.00 13.04  ? 88  TYR A CB  1 
ATOM   706  C  CG  . TYR A 1 88  ? 6.274   11.948  21.911  1.00 11.19  ? 88  TYR A CG  1 
ATOM   707  C  CD1 . TYR A 1 88  ? 5.664   12.343  23.107  1.00 13.41  ? 88  TYR A CD1 1 
ATOM   708  C  CD2 . TYR A 1 88  ? 7.652   11.732  21.894  1.00 12.02  ? 88  TYR A CD2 1 
ATOM   709  C  CE1 . TYR A 1 88  ? 6.409   12.488  24.265  1.00 12.87  ? 88  TYR A CE1 1 
ATOM   710  C  CE2 . TYR A 1 88  ? 8.400   11.910  23.034  1.00 11.14  ? 88  TYR A CE2 1 
ATOM   711  C  CZ  . TYR A 1 88  ? 7.785   12.258  24.225  1.00 11.22  ? 88  TYR A CZ  1 
ATOM   712  O  OH  . TYR A 1 88  ? 8.537   12.352  25.351  1.00 13.50  ? 88  TYR A OH  1 
ATOM   713  N  N   . ARG A 1 89  ? 5.001   13.196  17.614  1.00 12.28  ? 89  ARG A N   1 
ATOM   714  C  CA  . ARG A 1 89  ? 4.542   13.091  16.240  1.00 12.92  ? 89  ARG A CA  1 
ATOM   715  C  C   . ARG A 1 89  ? 5.211   11.947  15.515  1.00 10.57  ? 89  ARG A C   1 
ATOM   716  O  O   . ARG A 1 89  ? 6.432   11.754  15.611  1.00 10.85  ? 89  ARG A O   1 
ATOM   717  C  CB  . ARG A 1 89  ? 4.920   14.398  15.550  1.00 16.39  ? 89  ARG A CB  1 
ATOM   718  C  CG  . ARG A 1 89  ? 4.187   14.576  14.243  1.00 20.04  ? 89  ARG A CG  1 
ATOM   719  C  CD  . ARG A 1 89  ? 4.549   15.984  13.753  1.00 20.43  ? 89  ARG A CD  1 
ATOM   720  N  NE  . ARG A 1 89  ? 3.892   17.046  14.538  1.00 23.30  ? 89  ARG A NE  1 
ATOM   721  C  CZ  . ARG A 1 89  ? 4.067   18.352  14.369  1.00 22.61  ? 89  ARG A CZ  1 
ATOM   722  N  NH1 . ARG A 1 89  ? 4.932   18.755  13.449  1.00 24.61  ? 89  ARG A NH1 1 
ATOM   723  N  NH2 . ARG A 1 89  ? 3.394   19.231  15.121  1.00 22.29  ? 89  ARG A NH2 1 
ATOM   724  N  N   . LEU A 1 90  ? 4.396   11.173  14.791  1.00 11.79  ? 90  LEU A N   1 
ATOM   725  C  CA  . LEU A 1 90  ? 4.959   10.046  14.056  1.00 11.49  ? 90  LEU A CA  1 
ATOM   726  C  C   . LEU A 1 90  ? 5.828   10.542  12.915  1.00 11.21  ? 90  LEU A C   1 
ATOM   727  O  O   . LEU A 1 90  ? 5.346   11.291  12.058  1.00 14.48  ? 90  LEU A O   1 
ATOM   728  C  CB  . LEU A 1 90  ? 3.853   9.175   13.499  1.00 13.00  ? 90  LEU A CB  1 
ATOM   729  C  CG  . LEU A 1 90  ? 4.267   8.001   12.592  1.00 13.41  ? 90  LEU A CG  1 
ATOM   730  C  CD1 . LEU A 1 90  ? 4.981   6.909   13.398  1.00 14.50  ? 90  LEU A CD1 1 
ATOM   731  C  CD2 . LEU A 1 90  ? 3.007   7.361   11.975  1.00 17.58  ? 90  LEU A CD2 1 
ATOM   732  N  N   . LYS A 1 91  ? 7.060   10.064  12.810  1.00 10.90  ? 91  LYS A N   1 
ATOM   733  C  CA  . LYS A 1 91  ? 8.000   10.405  11.760  1.00 11.42  ? 91  LYS A CA  1 
ATOM   734  C  C   . LYS A 1 91  ? 8.154   9.276   10.758  1.00 10.85  ? 91  LYS A C   1 
ATOM   735  O  O   . LYS A 1 91  ? 8.196   9.501   9.557   1.00 11.30  ? 91  LYS A O   1 
ATOM   736  C  CB  . LYS A 1 91  ? 9.362   10.795  12.332  1.00 13.51  ? 91  LYS A CB  1 
ATOM   737  C  CG  . LYS A 1 91  ? 10.480  11.042  11.312  1.00 15.18  ? 91  LYS A CG  1 
ATOM   738  C  CD  . LYS A 1 91  ? 11.825  11.457  11.913  1.00 22.35  ? 91  LYS A CD  1 
ATOM   739  C  CE  . LYS A 1 91  ? 12.925  11.679  10.867  1.00 28.77  ? 91  LYS A CE  1 
ATOM   740  N  NZ  . LYS A 1 91  ? 12.517  12.670  9.838   1.00 44.74  ? 91  LYS A NZ  1 
ATOM   741  N  N   . GLN A 1 92  ? 8.316   8.023   11.246  1.00 10.56  ? 92  GLN A N   1 
ATOM   742  C  CA  . GLN A 1 92  ? 8.645   6.914   10.367  1.00 10.21  ? 92  GLN A CA  1 
ATOM   743  C  C   . GLN A 1 92  ? 8.370   5.644   11.131  1.00 10.29  ? 92  GLN A C   1 
ATOM   744  O  O   . GLN A 1 92  ? 8.338   5.650   12.362  1.00 10.33  ? 92  GLN A O   1 
ATOM   745  C  CB  . GLN A 1 92  ? 10.118  6.936   9.899   1.00 11.78  ? 92  GLN A CB  1 
ATOM   746  C  CG  . GLN A 1 92  ? 11.144  7.060   11.040  1.00 12.63  ? 92  GLN A CG  1 
ATOM   747  C  CD  . GLN A 1 92  ? 11.946  5.824   11.273  1.00 13.01  ? 92  GLN A CD  1 
ATOM   748  O  OE1 . GLN A 1 92  ? 11.422  4.711   11.235  1.00 13.10  ? 92  GLN A OE1 1 
ATOM   749  N  NE2 . GLN A 1 92  ? 13.157  6.034   11.803  1.00 20.38  ? 92  GLN A NE2 1 
ATOM   750  N  N   . PHE A 1 93  ? 8.228   4.548   10.379  1.00 10.12  ? 93  PHE A N   1 
ATOM   751  C  CA  . PHE A 1 93  ? 8.318   3.245   11.018  1.00 9.98   ? 93  PHE A CA  1 
ATOM   752  C  C   . PHE A 1 93  ? 9.324   2.423   10.256  1.00 9.22   ? 93  PHE A C   1 
ATOM   753  O  O   . PHE A 1 93  ? 9.542   2.605   9.063   1.00 11.09  ? 93  PHE A O   1 
ATOM   754  C  CB  . PHE A 1 93  ? 6.964   2.553   11.238  1.00 10.34  ? 93  PHE A CB  1 
ATOM   755  C  CG  . PHE A 1 93  ? 6.259   2.070   9.995   1.00 10.32  ? 93  PHE A CG  1 
ATOM   756  C  CD1 . PHE A 1 93  ? 6.651   0.939   9.295   1.00 11.14  ? 93  PHE A CD1 1 
ATOM   757  C  CD2 . PHE A 1 93  ? 5.111   2.739   9.563   1.00 11.86  ? 93  PHE A CD2 1 
ATOM   758  C  CE1 . PHE A 1 93  ? 6.014   0.527   8.127   1.00 12.91  ? 93  PHE A CE1 1 
ATOM   759  C  CE2 . PHE A 1 93  ? 4.475   2.334   8.405   1.00 12.01  ? 93  PHE A CE2 1 
ATOM   760  C  CZ  . PHE A 1 93  ? 4.889   1.226   7.718   1.00 11.87  ? 93  PHE A CZ  1 
ATOM   761  N  N   . HIS A 1 94  ? 9.816   1.370   10.933  1.00 8.95   ? 94  HIS A N   1 
ATOM   762  C  CA  . HIS A 1 94  ? 10.776  0.467   10.317  1.00 8.79   ? 94  HIS A CA  1 
ATOM   763  C  C   . HIS A 1 94  ? 10.729  -0.852  11.054  1.00 8.20   ? 94  HIS A C   1 
ATOM   764  O  O   . HIS A 1 94  ? 10.052  -0.970  12.073  1.00 9.52   ? 94  HIS A O   1 
ATOM   765  C  CB  . HIS A 1 94  ? 12.229  1.055   10.311  1.00 9.96   ? 94  HIS A CB  1 
ATOM   766  C  CG  . HIS A 1 94  ? 12.673  1.300   11.704  1.00 8.52   ? 94  HIS A CG  1 
ATOM   767  N  ND1 . HIS A 1 94  ? 12.536  2.503   12.374  1.00 9.36   ? 94  HIS A ND1 1 
ATOM   768  C  CD2 . HIS A 1 94  ? 13.283  0.446   12.585  1.00 9.25   ? 94  HIS A CD2 1 
ATOM   769  C  CE1 . HIS A 1 94  ? 13.031  2.400   13.607  1.00 9.06   ? 94  HIS A CE1 1 
ATOM   770  N  NE2 . HIS A 1 94  ? 13.546  1.124   13.755  1.00 8.50   ? 94  HIS A NE2 1 
ATOM   771  N  N   . PHE A 1 95  ? 11.469  -1.826  10.542  1.00 8.94   ? 95  PHE A N   1 
ATOM   772  C  CA  . PHE A 1 95  ? 11.537  -3.133  11.161  1.00 8.42   ? 95  PHE A CA  1 
ATOM   773  C  C   . PHE A 1 95  ? 12.986  -3.552  11.327  1.00 9.40   ? 95  PHE A C   1 
ATOM   774  O  O   . PHE A 1 95  ? 13.883  -3.137  10.606  1.00 10.42  ? 95  PHE A O   1 
ATOM   775  C  CB  . PHE A 1 95  ? 10.841  -4.194  10.273  1.00 9.98   ? 95  PHE A CB  1 
ATOM   776  C  CG  . PHE A 1 95  ? 9.376   -3.926  10.001  1.00 9.72   ? 95  PHE A CG  1 
ATOM   777  C  CD1 . PHE A 1 95  ? 8.970   -3.060  8.986   1.00 10.00  ? 95  PHE A CD1 1 
ATOM   778  C  CD2 . PHE A 1 95  ? 8.391   -4.624  10.690  1.00 10.52  ? 95  PHE A CD2 1 
ATOM   779  C  CE1 . PHE A 1 95  ? 7.623   -2.865  8.709   1.00 11.00  ? 95  PHE A CE1 1 
ATOM   780  C  CE2 . PHE A 1 95  ? 7.040   -4.427  10.425  1.00 11.24  ? 95  PHE A CE2 1 
ATOM   781  C  CZ  . PHE A 1 95  ? 6.673   -3.525  9.424   1.00 11.90  ? 95  PHE A CZ  1 
ATOM   782  N  N   . HIS A 1 96  ? 13.155  -4.511  12.248  1.00 9.58   ? 96  HIS A N   1 
ATOM   783  C  CA  . HIS A 1 96  ? 14.359  -5.327  12.399  1.00 9.20   ? 96  HIS A CA  1 
ATOM   784  C  C   . HIS A 1 96  ? 13.902  -6.782  12.298  1.00 9.28   ? 96  HIS A C   1 
ATOM   785  O  O   . HIS A 1 96  ? 12.810  -7.103  12.780  1.00 9.87   ? 96  HIS A O   1 
ATOM   786  C  CB  . HIS A 1 96  ? 15.095  -5.116  13.763  1.00 9.03   ? 96  HIS A CB  1 
ATOM   787  C  CG  . HIS A 1 96  ? 15.328  -3.665  14.065  1.00 8.42   ? 96  HIS A CG  1 
ATOM   788  N  ND1 . HIS A 1 96  ? 16.535  -3.040  13.792  1.00 9.16   ? 96  HIS A ND1 1 
ATOM   789  C  CD2 . HIS A 1 96  ? 14.458  -2.717  14.493  1.00 8.87   ? 96  HIS A CD2 1 
ATOM   790  C  CE1 . HIS A 1 96  ? 16.427  -1.730  14.151  1.00 9.94   ? 96  HIS A CE1 1 
ATOM   791  N  NE2 . HIS A 1 96  ? 15.140  -1.492  14.554  1.00 8.72   ? 96  HIS A NE2 1 
ATOM   792  N  N   . TRP A 1 97  ? 14.711  -7.652  11.677  1.00 9.49   ? 97  TRP A N   1 
ATOM   793  C  CA  . TRP A 1 97  ? 14.276  -9.032  11.520  1.00 9.34   ? 97  TRP A CA  1 
ATOM   794  C  C   . TRP A 1 97  ? 15.482  -9.940  11.392  1.00 9.02   ? 97  TRP A C   1 
ATOM   795  O  O   . TRP A 1 97  ? 16.651  -9.540  11.300  1.00 9.76   ? 97  TRP A O   1 
ATOM   796  C  CB  . TRP A 1 97  ? 13.374  -9.173  10.293  1.00 10.46  ? 97  TRP A CB  1 
ATOM   797  C  CG  . TRP A 1 97  ? 14.028  -8.772  9.005   1.00 9.37   ? 97  TRP A CG  1 
ATOM   798  C  CD1 . TRP A 1 97  ? 14.728  -9.600  8.162   1.00 10.32  ? 97  TRP A CD1 1 
ATOM   799  C  CD2 . TRP A 1 97  ? 14.104  -7.456  8.418   1.00 10.00  ? 97  TRP A CD2 1 
ATOM   800  N  NE1 . TRP A 1 97  ? 15.199  -8.926  7.062   1.00 12.00  ? 97  TRP A NE1 1 
ATOM   801  C  CE2 . TRP A 1 97  ? 14.854  -7.590  7.224   1.00 10.90  ? 97  TRP A CE2 1 
ATOM   802  C  CE3 . TRP A 1 97  ? 13.632  -6.166  8.780   1.00 10.41  ? 97  TRP A CE3 1 
ATOM   803  C  CZ2 . TRP A 1 97  ? 15.089  -6.520  6.356   1.00 11.76  ? 97  TRP A CZ2 1 
ATOM   804  C  CZ3 . TRP A 1 97  ? 13.883  -5.082  7.944   1.00 11.03  ? 97  TRP A CZ3 1 
ATOM   805  C  CH2 . TRP A 1 97  ? 14.611  -5.284  6.759   1.00 12.48  ? 97  TRP A CH2 1 
ATOM   806  N  N   . GLY A 1 98  ? 15.141  -11.247 11.400  1.00 9.47   ? 98  GLY A N   1 
ATOM   807  C  CA  . GLY A 1 98  ? 16.149  -12.281 11.469  1.00 9.71   ? 98  GLY A CA  1 
ATOM   808  C  C   . GLY A 1 98  ? 16.380  -13.002 10.144  1.00 10.64  ? 98  GLY A C   1 
ATOM   809  O  O   . GLY A 1 98  ? 15.679  -12.827 9.149   1.00 11.74  ? 98  GLY A O   1 
ATOM   810  N  N   . SER A 1 99  ? 17.387  -13.886 10.177  1.00 11.12  ? 99  SER A N   1 
ATOM   811  C  CA  . SER A 1 99  ? 17.616  -14.808 9.065   1.00 11.92  ? 99  SER A CA  1 
ATOM   812  C  C   . SER A 1 99  ? 16.729  -16.064 9.177   1.00 12.00  ? 99  SER A C   1 
ATOM   813  O  O   . SER A 1 99  ? 16.601  -16.796 8.208   1.00 15.70  ? 99  SER A O   1 
ATOM   814  C  CB  . SER A 1 99  ? 19.075  -15.123 9.001   1.00 13.89  ? 99  SER A CB  1 
ATOM   815  O  OG  . SER A 1 99  ? 19.529  -15.667 10.266  1.00 14.51  ? 99  SER A OG  1 
ATOM   816  N  N   . LEU A 1 100 ? 16.139  -16.286 10.366  1.00 11.48  ? 100 LEU A N   1 
ATOM   817  C  CA  . LEU A 1 100 ? 15.358  -17.453 10.715  1.00 12.89  ? 100 LEU A CA  1 
ATOM   818  C  C   . LEU A 1 100 ? 14.210  -16.984 11.577  1.00 11.86  ? 100 LEU A C   1 
ATOM   819  O  O   . LEU A 1 100 ? 14.347  -15.962 12.256  1.00 12.65  ? 100 LEU A O   1 
ATOM   820  C  CB  . LEU A 1 100 ? 16.152  -18.399 11.613  1.00 16.80  ? 100 LEU A CB  1 
ATOM   821  C  CG  . LEU A 1 100 ? 17.480  -18.852 11.010  1.00 19.42  ? 100 LEU A CG  1 
ATOM   822  C  CD1 . LEU A 1 100 ? 18.384  -19.449 12.098  1.00 28.52  ? 100 LEU A CD1 1 
ATOM   823  C  CD2 . LEU A 1 100 ? 17.114  -19.930 9.992   1.00 23.69  ? 100 LEU A CD2 1 
ATOM   824  N  N   . ASP A 1 101 ? 13.115  -17.717 11.608  1.00 14.08  ? 101 ASP A N   1 
ATOM   825  C  CA  . ASP A 1 101 ? 11.939  -17.248 12.307  1.00 13.89  ? 101 ASP A CA  1 
ATOM   826  C  C   . ASP A 1 101 ? 12.192  -17.126 13.810  1.00 13.84  ? 101 ASP A C   1 
ATOM   827  O  O   . ASP A 1 101 ? 11.511  -16.384 14.467  1.00 16.78  ? 101 ASP A O   1 
ATOM   828  C  CB  . ASP A 1 101 ? 10.732  -18.168 12.081  1.00 16.26  ? 101 ASP A CB  1 
ATOM   829  C  CG  . ASP A 1 101 ? 10.256  -18.224 10.645  1.00 17.47  ? 101 ASP A CG  1 
ATOM   830  O  OD1 . ASP A 1 101 ? 10.629  -17.381 9.793   1.00 15.33  ? 101 ASP A OD1 1 
ATOM   831  O  OD2 . ASP A 1 101 ? 9.453   -19.103 10.373  1.00 21.44  ? 101 ASP A OD2 1 
ATOM   832  N  N   . GLY A 1 102 ? 13.175  -17.867 14.364  1.00 15.67  ? 102 GLY A N   1 
ATOM   833  C  CA  . GLY A 1 102 ? 13.511  -17.876 15.776  1.00 17.41  ? 102 GLY A CA  1 
ATOM   834  C  C   . GLY A 1 102 ? 14.321  -16.681 16.290  1.00 15.49  ? 102 GLY A C   1 
ATOM   835  O  O   . GLY A 1 102 ? 14.708  -16.665 17.476  1.00 15.42  ? 102 GLY A O   1 
ATOM   836  N  N   . GLN A 1 103 ? 14.636  -15.691 15.434  1.00 12.33  ? 103 GLN A N   1 
ATOM   837  C  CA  . GLN A 1 103 ? 15.349  -14.524 15.928  1.00 11.10  ? 103 GLN A CA  1 
ATOM   838  C  C   . GLN A 1 103 ? 14.967  -13.354 15.037  1.00 9.97   ? 103 GLN A C   1 
ATOM   839  O  O   . GLN A 1 103 ? 14.473  -13.542 13.934  1.00 11.29  ? 103 GLN A O   1 
ATOM   840  C  CB  . GLN A 1 103 ? 16.853  -14.747 15.899  1.00 12.53  ? 103 GLN A CB  1 
ATOM   841  C  CG  . GLN A 1 103 ? 17.374  -15.058 14.476  1.00 12.94  ? 103 GLN A CG  1 
ATOM   842  C  CD  . GLN A 1 103 ? 18.758  -15.646 14.490  1.00 15.85  ? 103 GLN A CD  1 
ATOM   843  O  OE1 . GLN A 1 103 ? 18.921  -16.649 15.134  1.00 25.51  ? 103 GLN A OE1 1 
ATOM   844  N  NE2 . GLN A 1 103 ? 19.750  -15.128 13.828  1.00 15.40  ? 103 GLN A NE2 1 
ATOM   845  N  N   . GLY A 1 104 ? 15.327  -12.137 15.489  1.00 9.30   ? 104 GLY A N   1 
ATOM   846  C  CA  . GLY A 1 104 ? 15.056  -10.975 14.657  1.00 9.43   ? 104 GLY A CA  1 
ATOM   847  C  C   . GLY A 1 104 ? 14.601  -9.800  15.517  1.00 8.64   ? 104 GLY A C   1 
ATOM   848  O  O   . GLY A 1 104 ? 14.834  -8.652  15.139  1.00 10.66  ? 104 GLY A O   1 
ATOM   849  N  N   . SER A 1 105 ? 13.877  -10.047 16.632  1.00 8.93   ? 105 SER A N   1 
ATOM   850  C  CA  . SER A 1 105 ? 13.498  -8.939  17.490  1.00 8.56   ? 105 SER A CA  1 
ATOM   851  C  C   . SER A 1 105 ? 14.693  -8.404  18.258  1.00 8.50   ? 105 SER A C   1 
ATOM   852  O  O   . SER A 1 105 ? 15.730  -9.045  18.416  1.00 8.99   ? 105 SER A O   1 
ATOM   853  C  CB  . SER A 1 105 ? 12.389  -9.261  18.429  1.00 8.77   ? 105 SER A CB  1 
ATOM   854  O  OG  . SER A 1 105 ? 12.762  -10.266 19.379  1.00 9.34   ? 105 SER A OG  1 
ATOM   855  N  N   . GLU A 1 106 ? 14.565  -7.140  18.641  1.00 8.62   ? 106 GLU A N   1 
ATOM   856  C  CA  . GLU A 1 106 ? 15.572  -6.421  19.438  1.00 8.00   ? 106 GLU A CA  1 
ATOM   857  C  C   . GLU A 1 106 ? 15.261  -6.618  20.926  1.00 7.57   ? 106 GLU A C   1 
ATOM   858  O  O   . GLU A 1 106 ? 16.049  -7.198  21.681  1.00 8.61   ? 106 GLU A O   1 
ATOM   859  C  CB  . GLU A 1 106 ? 15.634  -4.940  19.026  1.00 8.83   ? 106 GLU A CB  1 
ATOM   860  C  CG  . GLU A 1 106 ? 15.981  -4.814  17.555  1.00 9.56   ? 106 GLU A CG  1 
ATOM   861  C  CD  . GLU A 1 106 ? 16.720  -3.533  17.275  1.00 8.01   ? 106 GLU A CD  1 
ATOM   862  O  OE1 . GLU A 1 106 ? 16.133  -2.447  17.496  1.00 8.73   ? 106 GLU A OE1 1 
ATOM   863  O  OE2 . GLU A 1 106 ? 17.888  -3.614  16.872  1.00 9.82   ? 106 GLU A OE2 1 
ATOM   864  N  N   . HIS A 1 107 ? 14.073  -6.189  21.342  1.00 7.86   ? 107 HIS A N   1 
ATOM   865  C  CA  . HIS A 1 107 ? 13.637  -6.582  22.670  1.00 8.41   ? 107 HIS A CA  1 
ATOM   866  C  C   . HIS A 1 107 ? 13.333  -8.070  22.687  1.00 8.32   ? 107 HIS A C   1 
ATOM   867  O  O   . HIS A 1 107 ? 12.980  -8.684  21.676  1.00 9.32   ? 107 HIS A O   1 
ATOM   868  C  CB  . HIS A 1 107 ? 12.387  -5.779  23.057  1.00 8.46   ? 107 HIS A CB  1 
ATOM   869  C  CG  . HIS A 1 107 ? 12.688  -4.342  23.235  1.00 7.57   ? 107 HIS A CG  1 
ATOM   870  N  ND1 . HIS A 1 107 ? 12.634  -3.448  22.169  1.00 7.86   ? 107 HIS A ND1 1 
ATOM   871  C  CD2 . HIS A 1 107 ? 13.148  -3.630  24.285  1.00 7.92   ? 107 HIS A CD2 1 
ATOM   872  C  CE1 . HIS A 1 107 ? 13.026  -2.236  22.622  1.00 9.01   ? 107 HIS A CE1 1 
ATOM   873  N  NE2 . HIS A 1 107 ? 13.378  -2.314  23.894  1.00 8.47   ? 107 HIS A NE2 1 
ATOM   874  N  N   . THR A 1 108 ? 13.434  -8.646  23.889  1.00 9.12   ? 108 THR A N   1 
ATOM   875  C  CA  . THR A 1 108 ? 13.047  -10.038 24.123  1.00 9.26   ? 108 THR A CA  1 
ATOM   876  C  C   . THR A 1 108 ? 12.111  -10.016 25.312  1.00 8.76   ? 108 THR A C   1 
ATOM   877  O  O   . THR A 1 108 ? 12.080  -9.075  26.117  1.00 9.84   ? 108 THR A O   1 
ATOM   878  C  CB  . THR A 1 108 ? 14.269  -10.955 24.319  1.00 9.67   ? 108 THR A CB  1 
ATOM   879  O  OG1 . THR A 1 108 ? 15.087  -10.445 25.385  1.00 10.40  ? 108 THR A OG1 1 
ATOM   880  C  CG2 . THR A 1 108 ? 15.115  -11.021 23.049  1.00 10.62  ? 108 THR A CG2 1 
ATOM   881  N  N   . VAL A 1 109 ? 11.354  -11.102 25.481  1.00 10.29  ? 109 VAL A N   1 
ATOM   882  C  CA  . VAL A 1 109 ? 10.371  -11.214 26.560  1.00 11.64  ? 109 VAL A CA  1 
ATOM   883  C  C   . VAL A 1 109 ? 10.708  -12.511 27.299  1.00 11.63  ? 109 VAL A C   1 
ATOM   884  O  O   . VAL A 1 109 ? 10.535  -13.597 26.719  1.00 12.73  ? 109 VAL A O   1 
ATOM   885  C  CB  . VAL A 1 109 ? 8.915   -11.202 26.002  1.00 11.74  ? 109 VAL A CB  1 
ATOM   886  C  CG1 . VAL A 1 109 ? 7.897   -11.357 27.119  1.00 14.49  ? 109 VAL A CG1 1 
ATOM   887  C  CG2 . VAL A 1 109 ? 8.640   -9.902  25.234  1.00 12.74  ? 109 VAL A CG2 1 
ATOM   888  N  N   . ASP A 1 110 ? 11.166  -12.386 28.536  1.00 12.61  ? 110 ASP A N   1 
ATOM   889  C  CA  . ASP A 1 110 ? 11.623  -13.583 29.248  1.00 13.09  ? 110 ASP A CA  1 
ATOM   890  C  C   . ASP A 1 110 ? 12.591  -14.391 28.369  1.00 13.61  ? 110 ASP A C   1 
ATOM   891  O  O   . ASP A 1 110 ? 12.513  -15.644 28.287  1.00 16.29  ? 110 ASP A O   1 
ATOM   892  C  CB  . ASP A 1 110 ? 10.446  -14.452 29.737  1.00 17.05  ? 110 ASP A CB  1 
ATOM   893  C  CG  . ASP A 1 110 ? 9.612   -13.676 30.749  1.00 18.09  ? 110 ASP A CG  1 
ATOM   894  O  OD1 . ASP A 1 110 ? 10.201  -12.780 31.461  1.00 19.32  ? 110 ASP A OD1 1 
ATOM   895  O  OD2 . ASP A 1 110 ? 8.403   -13.970 30.823  1.00 22.71  ? 110 ASP A OD2 1 
ATOM   896  N  N   . LYS A 1 111 ? 13.495  -13.683 27.656  1.00 12.66  ? 111 LYS A N   1 
ATOM   897  C  CA  . LYS A 1 111 ? 14.562  -14.178 26.789  1.00 13.38  ? 111 LYS A CA  1 
ATOM   898  C  C   . LYS A 1 111 ? 13.985  -14.715 25.469  1.00 12.92  ? 111 LYS A C   1 
ATOM   899  O  O   . LYS A 1 111 ? 14.758  -15.054 24.577  1.00 15.71  ? 111 LYS A O   1 
ATOM   900  C  CB  . LYS A 1 111 ? 15.487  -15.218 27.460  1.00 15.87  ? 111 LYS A CB  1 
ATOM   901  C  CG  . LYS A 1 111 ? 16.193  -14.641 28.702  1.00 19.60  ? 111 LYS A CG  1 
ATOM   902  C  CD  . LYS A 1 111 ? 17.166  -13.500 28.333  1.00 21.10  ? 111 LYS A CD  1 
ATOM   903  C  CE  . LYS A 1 111 ? 17.872  -12.880 29.524  1.00 24.34  ? 111 LYS A CE  1 
ATOM   904  N  NZ  . LYS A 1 111 ? 19.086  -13.688 29.705  1.00 33.94  ? 111 LYS A NZ  1 
ATOM   905  N  N   . LYS A 1 112 ? 12.660  -14.721 25.277  1.00 12.45  ? 112 LYS A N   1 
ATOM   906  C  CA  . LYS A 1 112 ? 12.115  -15.094 23.960  1.00 14.41  ? 112 LYS A CA  1 
ATOM   907  C  C   . LYS A 1 112 ? 12.416  -14.033 22.891  1.00 12.27  ? 112 LYS A C   1 
ATOM   908  O  O   . LYS A 1 112 ? 12.110  -12.859 23.080  1.00 11.77  ? 112 LYS A O   1 
ATOM   909  C  CB  . LYS A 1 112 ? 10.576  -15.190 24.040  1.00 15.86  ? 112 LYS A CB  1 
ATOM   910  C  CG  . LYS A 1 112 ? 9.888   -15.665 22.773  1.00 16.22  ? 112 LYS A CG  1 
ATOM   911  C  CD  . LYS A 1 112 ? 8.413   -15.669 22.906  1.00 20.99  ? 112 LYS A CD  1 
ATOM   912  C  CE  . LYS A 1 112 ? 7.813   -15.781 21.540  1.00 22.34  ? 112 LYS A CE  1 
ATOM   913  N  NZ  . LYS A 1 112 ? 7.970   -17.145 21.018  1.00 21.07  ? 112 LYS A NZ  1 
ATOM   914  N  N   A LYS A 1 113 ? 12.918  -14.499 21.748  0.50 12.34  ? 113 LYS A N   1 
ATOM   915  N  N   B LYS A 1 113 ? 12.965  -14.478 21.756  0.50 12.50  ? 113 LYS A N   1 
ATOM   916  C  CA  A LYS A 1 113 ? 13.099  -13.681 20.568  0.50 11.68  ? 113 LYS A CA  1 
ATOM   917  C  CA  B LYS A 1 113 ? 13.157  -13.673 20.563  0.50 11.64  ? 113 LYS A CA  1 
ATOM   918  C  C   A LYS A 1 113 ? 11.947  -13.921 19.603  0.50 11.24  ? 113 LYS A C   1 
ATOM   919  C  C   B LYS A 1 113 ? 12.006  -13.916 19.586  0.50 11.07  ? 113 LYS A C   1 
ATOM   920  O  O   A LYS A 1 113 ? 11.513  -15.045 19.367  0.50 14.63  ? 113 LYS A O   1 
ATOM   921  O  O   B LYS A 1 113 ? 11.623  -15.055 19.329  0.50 15.13  ? 113 LYS A O   1 
ATOM   922  C  CB  A LYS A 1 113 ? 14.406  -14.019 19.848  0.50 13.35  ? 113 LYS A CB  1 
ATOM   923  C  CB  B LYS A 1 113 ? 14.475  -14.029 19.863  0.50 13.36  ? 113 LYS A CB  1 
ATOM   924  C  CG  A LYS A 1 113 ? 15.631  -13.783 20.693  0.50 12.84  ? 113 LYS A CG  1 
ATOM   925  C  CG  B LYS A 1 113 ? 15.708  -13.680 20.665  0.50 13.60  ? 113 LYS A CG  1 
ATOM   926  C  CD  A LYS A 1 113 ? 16.871  -14.363 19.991  0.50 12.73  ? 113 LYS A CD  1 
ATOM   927  C  CD  B LYS A 1 113 ? 17.006  -14.259 20.063  0.50 13.94  ? 113 LYS A CD  1 
ATOM   928  C  CE  A LYS A 1 113 ? 18.171  -13.861 20.587  0.50 14.70  ? 113 LYS A CE  1 
ATOM   929  C  CE  B LYS A 1 113 ? 18.219  -13.670 20.769  0.50 15.77  ? 113 LYS A CE  1 
ATOM   930  N  NZ  A LYS A 1 113 ? 18.547  -14.693 21.751  0.50 19.62  ? 113 LYS A NZ  1 
ATOM   931  N  NZ  B LYS A 1 113 ? 19.480  -14.412 20.539  0.50 20.48  ? 113 LYS A NZ  1 
ATOM   932  N  N   . TYR A 1 114 ? 11.468  -12.841 19.009  1.00 10.86  ? 114 TYR A N   1 
ATOM   933  C  CA  . TYR A 1 114 ? 10.441  -12.922 17.970  1.00 10.59  ? 114 TYR A CA  1 
ATOM   934  C  C   . TYR A 1 114 ? 11.105  -12.825 16.618  1.00 10.89  ? 114 TYR A C   1 
ATOM   935  O  O   . TYR A 1 114 ? 12.304  -12.557 16.509  1.00 11.13  ? 114 TYR A O   1 
ATOM   936  C  CB  . TYR A 1 114 ? 9.398   -11.799 18.121  1.00 10.20  ? 114 TYR A CB  1 
ATOM   937  C  CG  . TYR A 1 114 ? 8.480   -12.014 19.286  1.00 10.43  ? 114 TYR A CG  1 
ATOM   938  C  CD1 . TYR A 1 114 ? 8.785   -11.575 20.570  1.00 12.65  ? 114 TYR A CD1 1 
ATOM   939  C  CD2 . TYR A 1 114 ? 7.310   -12.701 19.098  1.00 11.72  ? 114 TYR A CD2 1 
ATOM   940  C  CE1 . TYR A 1 114 ? 7.936   -11.801 21.642  1.00 13.90  ? 114 TYR A CE1 1 
ATOM   941  C  CE2 . TYR A 1 114 ? 6.438   -12.925 20.182  1.00 14.75  ? 114 TYR A CE2 1 
ATOM   942  C  CZ  . TYR A 1 114 ? 6.750   -12.453 21.439  1.00 15.38  ? 114 TYR A CZ  1 
ATOM   943  O  OH  . TYR A 1 114 ? 5.904   -12.589 22.526  1.00 19.67  ? 114 TYR A OH  1 
ATOM   944  N  N   . ALA A 1 115 ? 10.341  -13.097 15.566  1.00 11.30  ? 115 ALA A N   1 
ATOM   945  C  CA  . ALA A 1 115 ? 10.898  -13.150 14.201  1.00 10.77  ? 115 ALA A CA  1 
ATOM   946  C  C   . ALA A 1 115 ? 11.253  -11.748 13.715  1.00 11.51  ? 115 ALA A C   1 
ATOM   947  O  O   . ALA A 1 115 ? 12.124  -11.599 12.835  1.00 11.81  ? 115 ALA A O   1 
ATOM   948  C  CB  . ALA A 1 115 ? 9.853   -13.748 13.272  1.00 12.46  ? 115 ALA A CB  1 
ATOM   949  N  N   . ALA A 1 116 ? 10.629  -10.701 14.269  1.00 10.33  ? 116 ALA A N   1 
ATOM   950  C  CA  . ALA A 1 116 ? 10.901  -9.329  13.816  1.00 9.62   ? 116 ALA A CA  1 
ATOM   951  C  C   . ALA A 1 116 ? 10.324  -8.401  14.850  1.00 9.14   ? 116 ALA A C   1 
ATOM   952  O  O   . ALA A 1 116 ? 9.612   -8.825  15.734  1.00 9.11   ? 116 ALA A O   1 
ATOM   953  C  CB  . ALA A 1 116 ? 10.361  -9.063  12.392  1.00 11.05  ? 116 ALA A CB  1 
ATOM   954  N  N   . GLU A 1 117 ? 10.637  -7.128  14.672  1.00 9.07   ? 117 GLU A N   1 
ATOM   955  C  CA  . GLU A 1 117 ? 10.136  -6.081  15.563  1.00 8.49   ? 117 GLU A CA  1 
ATOM   956  C  C   . GLU A 1 117 ? 9.924   -4.824  14.720  1.00 8.09   ? 117 GLU A C   1 
ATOM   957  O  O   . GLU A 1 117 ? 10.806  -4.396  13.982  1.00 9.50   ? 117 GLU A O   1 
ATOM   958  C  CB  . GLU A 1 117 ? 11.115  -5.822  16.727  1.00 9.18   ? 117 GLU A CB  1 
ATOM   959  C  CG  . GLU A 1 117 ? 10.498  -4.976  17.833  1.00 9.76   ? 117 GLU A CG  1 
ATOM   960  C  CD  . GLU A 1 117 ? 11.442  -4.891  19.013  1.00 8.77   ? 117 GLU A CD  1 
ATOM   961  O  OE1 . GLU A 1 117 ? 12.120  -5.893  19.326  1.00 9.31   ? 117 GLU A OE1 1 
ATOM   962  O  OE2 . GLU A 1 117 ? 11.468  -3.857  19.733  1.00 9.48   ? 117 GLU A OE2 1 
ATOM   963  N  N   . LEU A 1 118 ? 8.725   -4.274  14.856  1.00 8.61   ? 118 LEU A N   1 
ATOM   964  C  CA  . LEU A 1 118 ? 8.311   -3.024  14.224  1.00 7.85   ? 118 LEU A CA  1 
ATOM   965  C  C   . LEU A 1 118 ? 8.504   -1.903  15.235  1.00 8.48   ? 118 LEU A C   1 
ATOM   966  O  O   . LEU A 1 118 ? 8.071   -1.981  16.379  1.00 8.40   ? 118 LEU A O   1 
ATOM   967  C  CB  . LEU A 1 118 ? 6.802   -3.194  13.912  1.00 9.51   ? 118 LEU A CB  1 
ATOM   968  C  CG  . LEU A 1 118 ? 5.991   -1.892  13.598  1.00 9.72   ? 118 LEU A CG  1 
ATOM   969  C  CD1 . LEU A 1 118 ? 6.525   -1.189  12.370  1.00 10.70  ? 118 LEU A CD1 1 
ATOM   970  C  CD2 . LEU A 1 118 ? 4.543   -2.316  13.309  1.00 11.45  ? 118 LEU A CD2 1 
ATOM   971  N  N   . HIS A 1 119 ? 9.129   -0.830  14.733  1.00 8.38   ? 119 HIS A N   1 
ATOM   972  C  CA  . HIS A 1 119 ? 9.352   0.361   15.555  1.00 8.57   ? 119 HIS A CA  1 
ATOM   973  C  C   . HIS A 1 119 ? 8.668   1.555   14.887  1.00 7.98   ? 119 HIS A C   1 
ATOM   974  O  O   . HIS A 1 119 ? 8.998   1.880   13.732  1.00 9.29   ? 119 HIS A O   1 
ATOM   975  C  CB  . HIS A 1 119 ? 10.857  0.647   15.663  1.00 8.11   ? 119 HIS A CB  1 
ATOM   976  C  CG  . HIS A 1 119 ? 11.504  -0.360  16.516  1.00 7.77   ? 119 HIS A CG  1 
ATOM   977  N  ND1 . HIS A 1 119 ? 12.890  -0.577  16.509  1.00 8.50   ? 119 HIS A ND1 1 
ATOM   978  C  CD2 . HIS A 1 119 ? 10.966  -1.181  17.466  1.00 8.19   ? 119 HIS A CD2 1 
ATOM   979  C  CE1 . HIS A 1 119 ? 13.178  -1.520  17.418  1.00 8.58   ? 119 HIS A CE1 1 
ATOM   980  N  NE2 . HIS A 1 119 ? 12.037  -1.893  18.025  1.00 8.71   ? 119 HIS A NE2 1 
ATOM   981  N  N   . LEU A 1 120 ? 7.697   2.189   15.569  1.00 8.34   ? 120 LEU A N   1 
ATOM   982  C  CA  . LEU A 1 120 ? 7.056   3.421   15.114  1.00 8.68   ? 120 LEU A CA  1 
ATOM   983  C  C   . LEU A 1 120 ? 7.709   4.573   15.902  1.00 8.02   ? 120 LEU A C   1 
ATOM   984  O  O   . LEU A 1 120 ? 7.626   4.599   17.115  1.00 8.44   ? 120 LEU A O   1 
ATOM   985  C  CB  . LEU A 1 120 ? 5.560   3.332   15.287  1.00 9.33   ? 120 LEU A CB  1 
ATOM   986  C  CG  . LEU A 1 120 ? 4.864   2.253   14.446  1.00 10.19  ? 120 LEU A CG  1 
ATOM   987  C  CD1 . LEU A 1 120 ? 4.144   1.246   15.342  1.00 14.56  ? 120 LEU A CD1 1 
ATOM   988  C  CD2 . LEU A 1 120 ? 3.912   2.913   13.478  1.00 12.35  ? 120 LEU A CD2 1 
ATOM   989  N  N   . VAL A 1 121 ? 8.444   5.417   15.171  1.00 9.54   ? 121 VAL A N   1 
ATOM   990  C  CA  . VAL A 1 121 ? 9.283   6.428   15.813  1.00 8.87   ? 121 VAL A CA  1 
ATOM   991  C  C   . VAL A 1 121 ? 8.566   7.768   15.826  1.00 9.60   ? 121 VAL A C   1 
ATOM   992  O  O   . VAL A 1 121 ? 8.149   8.261   14.765  1.00 10.82  ? 121 VAL A O   1 
ATOM   993  C  CB  . VAL A 1 121 ? 10.600  6.534   15.016  1.00 9.26   ? 121 VAL A CB  1 
ATOM   994  C  CG1 . VAL A 1 121 ? 11.550  7.589   15.635  1.00 11.46  ? 121 VAL A CG1 1 
ATOM   995  C  CG2 . VAL A 1 121 ? 11.282  5.145   14.861  1.00 10.79  ? 121 VAL A CG2 1 
ATOM   996  N  N   . HIS A 1 122 ? 8.491   8.364   17.024  1.00 8.64   ? 122 HIS A N   1 
ATOM   997  C  CA  . HIS A 1 122 ? 7.797   9.612   17.220  1.00 9.25   ? 122 HIS A CA  1 
ATOM   998  C  C   . HIS A 1 122 ? 8.701   10.593  17.930  1.00 9.76   ? 122 HIS A C   1 
ATOM   999  O  O   . HIS A 1 122 ? 9.445   10.196  18.791  1.00 11.21  ? 122 HIS A O   1 
ATOM   1000 C  CB  . HIS A 1 122 ? 6.517   9.439   18.059  1.00 10.69  ? 122 HIS A CB  1 
ATOM   1001 C  CG  . HIS A 1 122 ? 5.638   8.316   17.655  1.00 9.70   ? 122 HIS A CG  1 
ATOM   1002 N  ND1 . HIS A 1 122 ? 5.952   6.988   17.926  1.00 10.16  ? 122 HIS A ND1 1 
ATOM   1003 C  CD2 . HIS A 1 122 ? 4.418   8.293   17.084  1.00 10.64  ? 122 HIS A CD2 1 
ATOM   1004 C  CE1 . HIS A 1 122 ? 4.940   6.222   17.540  1.00 10.71  ? 122 HIS A CE1 1 
ATOM   1005 N  NE2 . HIS A 1 122 ? 3.976   6.971   16.975  1.00 10.55  ? 122 HIS A NE2 1 
ATOM   1006 N  N   . TRP A 1 123 ? 8.562   11.884  17.642  1.00 9.60   ? 123 TRP A N   1 
ATOM   1007 C  CA  . TRP A 1 123 ? 9.387   12.870  18.326  1.00 9.69   ? 123 TRP A CA  1 
ATOM   1008 C  C   . TRP A 1 123 ? 8.537   13.894  19.064  1.00 9.89   ? 123 TRP A C   1 
ATOM   1009 O  O   . TRP A 1 123 ? 7.415   14.234  18.653  1.00 10.52  ? 123 TRP A O   1 
ATOM   1010 C  CB  . TRP A 1 123 ? 10.373  13.570  17.378  1.00 11.87  ? 123 TRP A CB  1 
ATOM   1011 C  CG  . TRP A 1 123 ? 9.737   14.210  16.198  1.00 12.26  ? 123 TRP A CG  1 
ATOM   1012 C  CD1 . TRP A 1 123 ? 9.509   13.570  15.000  1.00 13.21  ? 123 TRP A CD1 1 
ATOM   1013 C  CD2 . TRP A 1 123 ? 9.337   15.567  16.034  1.00 13.42  ? 123 TRP A CD2 1 
ATOM   1014 N  NE1 . TRP A 1 123 ? 8.979   14.460  14.112  1.00 14.29  ? 123 TRP A NE1 1 
ATOM   1015 C  CE2 . TRP A 1 123 ? 8.859   15.693  14.698  1.00 15.11  ? 123 TRP A CE2 1 
ATOM   1016 C  CE3 . TRP A 1 123 ? 9.333   16.706  16.887  1.00 14.99  ? 123 TRP A CE3 1 
ATOM   1017 C  CZ2 . TRP A 1 123 ? 8.339   16.897  14.200  1.00 17.51  ? 123 TRP A CZ2 1 
ATOM   1018 C  CZ3 . TRP A 1 123 ? 8.842   17.884  16.356  1.00 18.83  ? 123 TRP A CZ3 1 
ATOM   1019 C  CH2 . TRP A 1 123 ? 8.346   17.978  15.050  1.00 18.10  ? 123 TRP A CH2 1 
ATOM   1020 N  N   . ASN A 1 124 ? 9.075   14.340  20.219  1.00 10.39  ? 124 ASN A N   1 
ATOM   1021 C  CA  . ASN A 1 124 ? 8.365   15.244  21.116  1.00 11.92  ? 124 ASN A CA  1 
ATOM   1022 C  C   . ASN A 1 124 ? 8.245   16.626  20.473  1.00 12.25  ? 124 ASN A C   1 
ATOM   1023 O  O   . ASN A 1 124 ? 9.251   17.305  20.229  1.00 11.43  ? 124 ASN A O   1 
ATOM   1024 C  CB  . ASN A 1 124 ? 9.187   15.286  22.393  1.00 12.10  ? 124 ASN A CB  1 
ATOM   1025 C  CG  . ASN A 1 124 ? 8.424   15.914  23.531  1.00 14.64  ? 124 ASN A CG  1 
ATOM   1026 O  OD1 . ASN A 1 124 ? 7.610   16.809  23.276  1.00 14.99  ? 124 ASN A OD1 1 
ATOM   1027 N  ND2 . ASN A 1 124 ? 8.707   15.436  24.736  1.00 15.75  ? 124 ASN A ND2 1 
ATOM   1028 N  N   . THR A 1 125 ? 6.995   17.051  20.201  1.00 13.27  ? 125 THR A N   1 
ATOM   1029 C  CA  . THR A 1 125 ? 6.818   18.333  19.489  1.00 15.00  ? 125 THR A CA  1 
ATOM   1030 C  C   . THR A 1 125 ? 7.352   19.515  20.305  1.00 15.31  ? 125 THR A C   1 
ATOM   1031 O  O   . THR A 1 125 ? 7.451   20.591  19.703  1.00 16.27  ? 125 THR A O   1 
ATOM   1032 C  CB  . THR A 1 125 ? 5.369   18.480  19.024  1.00 19.94  ? 125 THR A CB  1 
ATOM   1033 O  OG1 . THR A 1 125 ? 4.559   18.503  20.195  1.00 24.15  ? 125 THR A OG1 1 
ATOM   1034 C  CG2 . THR A 1 125 ? 4.957   17.357  18.078  1.00 20.59  ? 125 THR A CG2 1 
ATOM   1035 N  N   . LYS A 1 126 ? 7.511   19.420  21.613  1.00 14.06  ? 126 LYS A N   1 
ATOM   1036 C  CA  . LYS A 1 126 ? 8.073   20.546  22.404  1.00 15.82  ? 126 LYS A CA  1 
ATOM   1037 C  C   . LYS A 1 126 ? 9.449   20.961  21.875  1.00 15.20  ? 126 LYS A C   1 
ATOM   1038 O  O   . LYS A 1 126 ? 9.859   22.070  22.125  1.00 19.40  ? 126 LYS A O   1 
ATOM   1039 C  CB  . LYS A 1 126 ? 8.020   20.232  23.892  1.00 18.56  ? 126 LYS A CB  1 
ATOM   1040 C  CG  . LYS A 1 126 ? 9.183   19.460  24.476  1.00 20.55  ? 126 LYS A CG  1 
ATOM   1041 C  CD  . LYS A 1 126 ? 9.062   19.017  25.975  1.00 26.89  ? 126 LYS A CD  1 
ATOM   1042 C  CE  . LYS A 1 126 ? 9.464   20.135  26.906  1.00 30.75  ? 126 LYS A CE  1 
ATOM   1043 N  NZ  . LYS A 1 126 ? 9.295   19.714  28.326  1.00 37.42  ? 126 LYS A NZ  1 
ATOM   1044 N  N   . TYR A 1 127 ? 10.129  20.086  21.116  1.00 13.93  ? 127 TYR A N   1 
ATOM   1045 C  CA  . TYR A 1 127 ? 11.472  20.365  20.615  1.00 13.27  ? 127 TYR A CA  1 
ATOM   1046 C  C   . TYR A 1 127 ? 11.484  20.828  19.159  1.00 14.22  ? 127 TYR A C   1 
ATOM   1047 O  O   . TYR A 1 127 ? 12.568  21.127  18.604  1.00 15.15  ? 127 TYR A O   1 
ATOM   1048 C  CB  . TYR A 1 127 ? 12.468  19.217  20.844  1.00 13.95  ? 127 TYR A CB  1 
ATOM   1049 C  CG  . TYR A 1 127 ? 12.558  18.872  22.290  1.00 14.24  ? 127 TYR A CG  1 
ATOM   1050 C  CD1 . TYR A 1 127 ? 12.956  19.823  23.209  1.00 15.52  ? 127 TYR A CD1 1 
ATOM   1051 C  CD2 . TYR A 1 127 ? 12.241  17.593  22.750  1.00 13.17  ? 127 TYR A CD2 1 
ATOM   1052 C  CE1 . TYR A 1 127 ? 13.016  19.500  24.564  1.00 17.87  ? 127 TYR A CE1 1 
ATOM   1053 C  CE2 . TYR A 1 127 ? 12.336  17.232  24.098  1.00 14.14  ? 127 TYR A CE2 1 
ATOM   1054 C  CZ  . TYR A 1 127 ? 12.746  18.220  24.990  1.00 16.37  ? 127 TYR A CZ  1 
ATOM   1055 O  OH  . TYR A 1 127 ? 12.816  17.954  26.318  1.00 19.59  ? 127 TYR A OH  1 
ATOM   1056 N  N   . GLY A 1 128 ? 10.296  20.943  18.545  1.00 13.67  ? 128 GLY A N   1 
ATOM   1057 C  CA  . GLY A 1 128 ? 10.256  21.684  17.289  1.00 13.89  ? 128 GLY A CA  1 
ATOM   1058 C  C   . GLY A 1 128 ? 10.601  20.848  16.050  1.00 15.65  ? 128 GLY A C   1 
ATOM   1059 O  O   . GLY A 1 128 ? 9.903   20.966  15.064  1.00 16.24  ? 128 GLY A O   1 
ATOM   1060 N  N   A ASP A 1 129 ? 11.622  19.997  16.096  0.50 15.62  ? 129 ASP A N   1 
ATOM   1061 N  N   B ASP A 1 129 ? 11.734  20.104  16.091  0.50 16.45  ? 129 ASP A N   1 
ATOM   1062 C  CA  A ASP A 1 129 ? 11.721  19.007  15.034  0.50 15.44  ? 129 ASP A CA  1 
ATOM   1063 C  CA  B ASP A 1 129 ? 12.208  19.272  14.979  0.50 16.35  ? 129 ASP A CA  1 
ATOM   1064 C  C   A ASP A 1 129 ? 12.525  17.859  15.605  0.50 15.73  ? 129 ASP A C   1 
ATOM   1065 C  C   B ASP A 1 129 ? 12.790  17.969  15.538  0.50 16.93  ? 129 ASP A C   1 
ATOM   1066 O  O   A ASP A 1 129 ? 12.989  17.888  16.760  0.50 16.96  ? 129 ASP A O   1 
ATOM   1067 O  O   B ASP A 1 129 ? 13.275  17.934  16.692  0.50 15.59  ? 129 ASP A O   1 
ATOM   1068 C  CB  A ASP A 1 129 ? 12.298  19.538  13.715  0.50 15.23  ? 129 ASP A CB  1 
ATOM   1069 C  CB  B ASP A 1 129 ? 13.088  20.039  13.961  0.50 16.81  ? 129 ASP A CB  1 
ATOM   1070 C  CG  A ASP A 1 129 ? 13.665  20.138  13.944  0.50 12.34  ? 129 ASP A CG  1 
ATOM   1071 C  CG  B ASP A 1 129 ? 14.505  20.397  14.417  0.50 19.51  ? 129 ASP A CG  1 
ATOM   1072 O  OD1 A ASP A 1 129 ? 14.176  19.982  15.086  0.50 18.36  ? 129 ASP A OD1 1 
ATOM   1073 O  OD1 B ASP A 1 129 ? 15.323  19.506  14.678  0.50 19.38  ? 129 ASP A OD1 1 
ATOM   1074 O  OD2 A ASP A 1 129 ? 14.173  20.802  13.073  0.50 17.41  ? 129 ASP A OD2 1 
ATOM   1075 O  OD2 B ASP A 1 129 ? 14.794  21.571  14.471  0.50 17.03  ? 129 ASP A OD2 1 
ATOM   1076 N  N   . TYR A 1 130 ? 12.747  16.893  14.726  1.00 17.79  ? 130 TYR A N   1 
ATOM   1077 C  CA  . TYR A 1 130 ? 13.395  15.660  15.118  1.00 15.64  ? 130 TYR A CA  1 
ATOM   1078 C  C   . TYR A 1 130 ? 14.857  15.846  15.513  1.00 16.99  ? 130 TYR A C   1 
ATOM   1079 O  O   . TYR A 1 130 ? 15.334  15.253  16.476  1.00 15.10  ? 130 TYR A O   1 
ATOM   1080 C  CB  . TYR A 1 130 ? 13.244  14.670  13.976  1.00 17.52  ? 130 TYR A CB  1 
ATOM   1081 C  CG  . TYR A 1 130 ? 13.976  13.385  14.226  1.00 16.74  ? 130 TYR A CG  1 
ATOM   1082 C  CD1 . TYR A 1 130 ? 15.314  13.241  13.860  1.00 20.76  ? 130 TYR A CD1 1 
ATOM   1083 C  CD2 . TYR A 1 130 ? 13.325  12.309  14.797  1.00 17.13  ? 130 TYR A CD2 1 
ATOM   1084 C  CE1 . TYR A 1 130 ? 15.982  12.044  14.048  1.00 22.51  ? 130 TYR A CE1 1 
ATOM   1085 C  CE2 . TYR A 1 130 ? 13.979  11.122  14.961  1.00 20.17  ? 130 TYR A CE2 1 
ATOM   1086 C  CZ  . TYR A 1 130 ? 15.298  11.001  14.632  1.00 22.89  ? 130 TYR A CZ  1 
ATOM   1087 O  OH  . TYR A 1 130 ? 15.795  9.755   14.905  1.00 35.42  ? 130 TYR A OH  1 
ATOM   1088 N  N   . GLY A 1 131 ? 15.605  16.614  14.697  1.00 18.47  ? 131 GLY A N   1 
ATOM   1089 C  CA  . GLY A 1 131 ? 17.022  16.779  14.992  1.00 20.76  ? 131 GLY A CA  1 
ATOM   1090 C  C   . GLY A 1 131 ? 17.288  17.391  16.366  1.00 17.98  ? 131 GLY A C   1 
ATOM   1091 O  O   . GLY A 1 131 ? 18.312  17.081  17.008  1.00 19.98  ? 131 GLY A O   1 
ATOM   1092 N  N   . LYS A 1 132 ? 16.391  18.291  16.833  1.00 17.63  ? 132 LYS A N   1 
ATOM   1093 C  CA  . LYS A 1 132 ? 16.525  18.835  18.184  1.00 16.93  ? 132 LYS A CA  1 
ATOM   1094 C  C   . LYS A 1 132 ? 16.075  17.792  19.206  1.00 15.09  ? 132 LYS A C   1 
ATOM   1095 O  O   . LYS A 1 132 ? 16.613  17.671  20.304  1.00 19.03  ? 132 LYS A O   1 
ATOM   1096 C  CB  . LYS A 1 132 ? 15.785  20.180  18.286  1.00 17.88  ? 132 LYS A CB  1 
ATOM   1097 C  CG  . LYS A 1 132 ? 16.476  21.451  17.739  1.00 25.70  ? 132 LYS A CG  1 
ATOM   1098 C  CD  . LYS A 1 132 ? 17.578  21.902  18.775  1.00 36.62  ? 132 LYS A CD  1 
ATOM   1099 C  CE  . LYS A 1 132 ? 18.079  23.309  18.498  1.00 50.35  ? 132 LYS A CE  1 
ATOM   1100 N  NZ  . LYS A 1 132 ? 19.570  23.351  18.513  1.00 59.09  ? 132 LYS A NZ  1 
ATOM   1101 N  N   . ALA A 1 133 ? 15.007  17.065  18.862  1.00 13.36  ? 133 ALA A N   1 
ATOM   1102 C  CA  . ALA A 1 133 ? 14.440  16.117  19.801  1.00 13.01  ? 133 ALA A CA  1 
ATOM   1103 C  C   . ALA A 1 133 ? 15.436  15.024  20.160  1.00 14.30  ? 133 ALA A C   1 
ATOM   1104 O  O   . ALA A 1 133 ? 15.486  14.609  21.297  1.00 14.65  ? 133 ALA A O   1 
ATOM   1105 C  CB  . ALA A 1 133 ? 13.138  15.505  19.218  1.00 12.06  ? 133 ALA A CB  1 
ATOM   1106 N  N   . VAL A 1 134 ? 16.243  14.568  19.212  1.00 15.47  ? 134 VAL A N   1 
ATOM   1107 C  CA  . VAL A 1 134 ? 17.167  13.472  19.540  1.00 20.12  ? 134 VAL A CA  1 
ATOM   1108 C  C   . VAL A 1 134 ? 18.322  13.965  20.383  1.00 22.22  ? 134 VAL A C   1 
ATOM   1109 O  O   . VAL A 1 134 ? 19.015  13.106  20.898  1.00 29.13  ? 134 VAL A O   1 
ATOM   1110 C  CB  . VAL A 1 134 ? 17.761  12.812  18.297  1.00 24.48  ? 134 VAL A CB  1 
ATOM   1111 C  CG1 . VAL A 1 134 ? 16.631  12.318  17.452  1.00 20.32  ? 134 VAL A CG1 1 
ATOM   1112 C  CG2 . VAL A 1 134 ? 18.617  13.789  17.477  1.00 25.74  ? 134 VAL A CG2 1 
ATOM   1113 N  N   . GLN A 1 135 ? 18.382  15.265  20.664  1.00 24.21  ? 135 GLN A N   1 
ATOM   1114 C  CA  . GLN A 1 135 ? 19.385  15.755  21.618  1.00 29.38  ? 135 GLN A CA  1 
ATOM   1115 C  C   . GLN A 1 135 ? 18.832  15.781  23.047  1.00 24.72  ? 135 GLN A C   1 
ATOM   1116 O  O   . GLN A 1 135 ? 19.487  16.265  23.997  1.00 26.44  ? 135 GLN A O   1 
ATOM   1117 C  CB  . GLN A 1 135 ? 19.945  17.106  21.140  1.00 32.31  ? 135 GLN A CB  1 
ATOM   1118 C  CG  . GLN A 1 135 ? 20.592  16.908  19.704  1.00 42.43  ? 135 GLN A CG  1 
ATOM   1119 C  CD  . GLN A 1 135 ? 20.876  18.368  19.260  1.00 63.96  ? 135 GLN A CD  1 
ATOM   1120 O  OE1 . GLN A 1 135 ? 20.437  18.822  18.121  1.00 40.89  ? 135 GLN A OE1 1 
ATOM   1121 N  NE2 . GLN A 1 135 ? 21.473  19.138  20.288  1.00 62.82  ? 135 GLN A NE2 1 
ATOM   1122 N  N   . GLN A 1 136 ? 17.633  15.215  23.235  1.00 18.51  ? 136 GLN A N   1 
ATOM   1123 C  CA  . GLN A 1 136 ? 17.008  15.401  24.536  1.00 15.21  ? 136 GLN A CA  1 
ATOM   1124 C  C   . GLN A 1 136 ? 16.721  14.048  25.160  1.00 13.74  ? 136 GLN A C   1 
ATOM   1125 O  O   . GLN A 1 136 ? 16.365  13.110  24.425  1.00 13.32  ? 136 GLN A O   1 
ATOM   1126 C  CB  . GLN A 1 136 ? 15.699  16.174  24.430  1.00 16.85  ? 136 GLN A CB  1 
ATOM   1127 C  CG  . GLN A 1 136 ? 15.772  17.392  23.518  1.00 19.23  ? 136 GLN A CG  1 
ATOM   1128 C  CD  . GLN A 1 136 ? 16.803  18.374  23.949  1.00 21.63  ? 136 GLN A CD  1 
ATOM   1129 O  OE1 . GLN A 1 136 ? 17.013  18.620  25.137  1.00 24.22  ? 136 GLN A OE1 1 
ATOM   1130 N  NE2 . GLN A 1 136 ? 17.324  19.078  22.957  1.00 29.28  ? 136 GLN A NE2 1 
ATOM   1131 N  N   A PRO A 1 137 ? 16.728  13.941  26.508  0.50 15.10  ? 137 PRO A N   1 
ATOM   1132 N  N   B PRO A 1 137 ? 16.829  13.922  26.505  0.50 15.32  ? 137 PRO A N   1 
ATOM   1133 C  CA  A PRO A 1 137 ? 16.522  12.632  27.109  0.50 14.28  ? 137 PRO A CA  1 
ATOM   1134 C  CA  B PRO A 1 137 ? 16.540  12.630  27.108  0.50 14.40  ? 137 PRO A CA  1 
ATOM   1135 C  C   A PRO A 1 137 ? 15.111  12.116  26.900  0.50 13.77  ? 137 PRO A C   1 
ATOM   1136 C  C   B PRO A 1 137 ? 15.129  12.122  26.884  0.50 13.70  ? 137 PRO A C   1 
ATOM   1137 O  O   A PRO A 1 137 ? 14.895  10.904  26.985  0.50 16.25  ? 137 PRO A O   1 
ATOM   1138 O  O   B PRO A 1 137 ? 14.940  10.907  26.962  0.50 16.23  ? 137 PRO A O   1 
ATOM   1139 C  CB  A PRO A 1 137 ? 16.802  12.878  28.593  0.50 18.73  ? 137 PRO A CB  1 
ATOM   1140 C  CB  B PRO A 1 137 ? 16.789  12.861  28.598  0.50 18.41  ? 137 PRO A CB  1 
ATOM   1141 C  CG  A PRO A 1 137 ? 16.549  14.352  28.771  0.50 21.54  ? 137 PRO A CG  1 
ATOM   1142 C  CG  B PRO A 1 137 ? 17.812  13.958  28.607  0.50 20.69  ? 137 PRO A CG  1 
ATOM   1143 C  CD  A PRO A 1 137 ? 17.037  15.007  27.491  0.50 18.55  ? 137 PRO A CD  1 
ATOM   1144 C  CD  B PRO A 1 137 ? 17.428  14.888  27.461  0.50 18.42  ? 137 PRO A CD  1 
ATOM   1145 N  N   . ASP A 1 138 ? 14.174  13.039  26.628  1.00 13.25  ? 138 ASP A N   1 
ATOM   1146 C  CA  . ASP A 1 138 ? 12.771  12.670  26.389  1.00 13.42  ? 138 ASP A CA  1 
ATOM   1147 C  C   . ASP A 1 138 ? 12.367  13.097  24.980  1.00 11.89  ? 138 ASP A C   1 
ATOM   1148 O  O   . ASP A 1 138 ? 11.229  13.510  24.710  1.00 13.38  ? 138 ASP A O   1 
ATOM   1149 C  CB  . ASP A 1 138 ? 11.859  13.348  27.424  1.00 15.85  ? 138 ASP A CB  1 
ATOM   1150 C  CG  . ASP A 1 138 ? 11.898  14.838  27.426  1.00 16.00  ? 138 ASP A CG  1 
ATOM   1151 O  OD1 . ASP A 1 138 ? 12.826  15.393  26.811  1.00 17.12  ? 138 ASP A OD1 1 
ATOM   1152 O  OD2 . ASP A 1 138 ? 11.011  15.427  28.114  1.00 18.73  ? 138 ASP A OD2 1 
ATOM   1153 N  N   . GLY A 1 139 ? 13.296  12.996  24.022  1.00 10.72  ? 139 GLY A N   1 
ATOM   1154 C  CA  . GLY A 1 139 ? 13.032  13.496  22.676  1.00 10.40  ? 139 GLY A CA  1 
ATOM   1155 C  C   . GLY A 1 139 ? 12.170  12.553  21.840  1.00 9.61   ? 139 GLY A C   1 
ATOM   1156 O  O   . GLY A 1 139 ? 11.445  13.053  20.987  1.00 10.38  ? 139 GLY A O   1 
ATOM   1157 N  N   . LEU A 1 140 ? 12.351  11.238  21.997  1.00 9.62   ? 140 LEU A N   1 
ATOM   1158 C  CA  . LEU A 1 140 ? 11.645  10.294  21.146  1.00 8.26   ? 140 LEU A CA  1 
ATOM   1159 C  C   . LEU A 1 140 ? 10.795  9.375   21.990  1.00 8.42   ? 140 LEU A C   1 
ATOM   1160 O  O   . LEU A 1 140 ? 11.115  9.094   23.142  1.00 9.11   ? 140 LEU A O   1 
ATOM   1161 C  CB  . LEU A 1 140 ? 12.654  9.451   20.353  1.00 9.87   ? 140 LEU A CB  1 
ATOM   1162 C  CG  . LEU A 1 140 ? 13.491  10.118  19.288  1.00 12.71  ? 140 LEU A CG  1 
ATOM   1163 C  CD1 . LEU A 1 140 ? 14.274  9.105   18.501  1.00 14.41  ? 140 LEU A CD1 1 
ATOM   1164 C  CD2 . LEU A 1 140 ? 12.871  11.193  18.465  1.00 17.08  ? 140 LEU A CD2 1 
ATOM   1165 N  N   . ALA A 1 141 ? 9.727   8.879   21.335  1.00 9.10   ? 141 ALA A N   1 
ATOM   1166 C  CA  . ALA A 1 141 ? 8.958   7.770   21.874  1.00 9.62   ? 141 ALA A CA  1 
ATOM   1167 C  C   . ALA A 1 141 ? 8.868   6.767   20.739  1.00 8.52   ? 141 ALA A C   1 
ATOM   1168 O  O   . ALA A 1 141 ? 8.441   7.103   19.641  1.00 9.61   ? 141 ALA A O   1 
ATOM   1169 C  CB  . ALA A 1 141 ? 7.562   8.237   22.316  1.00 10.81  ? 141 ALA A CB  1 
ATOM   1170 N  N   . VAL A 1 142 ? 9.381   5.548   21.021  1.00 8.89   ? 142 VAL A N   1 
ATOM   1171 C  CA  . VAL A 1 142 ? 9.321   4.508   20.007  1.00 9.07   ? 142 VAL A CA  1 
ATOM   1172 C  C   . VAL A 1 142 ? 8.331   3.444   20.498  1.00 8.37   ? 142 VAL A C   1 
ATOM   1173 O  O   . VAL A 1 142 ? 8.465   2.930   21.609  1.00 8.64   ? 142 VAL A O   1 
ATOM   1174 C  CB  . VAL A 1 142 ? 10.691  3.919   19.628  1.00 7.99   ? 142 VAL A CB  1 
ATOM   1175 C  CG1 . VAL A 1 142 ? 10.493  2.899   18.498  1.00 9.33   ? 142 VAL A CG1 1 
ATOM   1176 C  CG2 . VAL A 1 142 ? 11.651  5.009   19.182  1.00 10.40  ? 142 VAL A CG2 1 
ATOM   1177 N  N   . LEU A 1 143 ? 7.322   3.179   19.661  1.00 8.61   ? 143 LEU A N   1 
ATOM   1178 C  CA  . LEU A 1 143 ? 6.345   2.138   19.915  1.00 8.08   ? 143 LEU A CA  1 
ATOM   1179 C  C   . LEU A 1 143 ? 6.855   0.874   19.217  1.00 8.59   ? 143 LEU A C   1 
ATOM   1180 O  O   . LEU A 1 143 ? 7.023   0.850   18.005  1.00 9.56   ? 143 LEU A O   1 
ATOM   1181 C  CB  . LEU A 1 143 ? 4.987   2.616   19.369  1.00 11.09  ? 143 LEU A CB  1 
ATOM   1182 C  CG  . LEU A 1 143 ? 3.833   1.652   19.534  1.00 12.05  ? 143 LEU A CG  1 
ATOM   1183 C  CD1 . LEU A 1 143 ? 3.582   1.340   21.006  1.00 13.64  ? 143 LEU A CD1 1 
ATOM   1184 C  CD2 . LEU A 1 143 ? 2.566   2.252   18.944  1.00 13.60  ? 143 LEU A CD2 1 
ATOM   1185 N  N   . GLY A 1 144 ? 7.137   -0.153  20.024  1.00 8.31   ? 144 GLY A N   1 
ATOM   1186 C  CA  . GLY A 1 144 ? 7.676   -1.416  19.514  1.00 8.44   ? 144 GLY A CA  1 
ATOM   1187 C  C   . GLY A 1 144 ? 6.606   -2.502  19.512  1.00 7.37   ? 144 GLY A C   1 
ATOM   1188 O  O   . GLY A 1 144 ? 5.879   -2.645  20.486  1.00 9.82   ? 144 GLY A O   1 
ATOM   1189 N  N   . ILE A 1 145 ? 6.551   -3.254  18.408  1.00 8.40   ? 145 ILE A N   1 
ATOM   1190 C  CA  . ILE A 1 145 ? 5.541   -4.310  18.246  1.00 8.44   ? 145 ILE A CA  1 
ATOM   1191 C  C   . ILE A 1 145 ? 6.280   -5.517  17.722  1.00 8.75   ? 145 ILE A C   1 
ATOM   1192 O  O   . ILE A 1 145 ? 6.974   -5.475  16.708  1.00 9.40   ? 145 ILE A O   1 
ATOM   1193 C  CB  . ILE A 1 145 ? 4.432   -3.830  17.289  1.00 9.11   ? 145 ILE A CB  1 
ATOM   1194 C  CG1 . ILE A 1 145 ? 3.799   -2.544  17.806  1.00 11.61  ? 145 ILE A CG1 1 
ATOM   1195 C  CG2 . ILE A 1 145 ? 3.434   -4.956  17.045  1.00 12.03  ? 145 ILE A CG2 1 
ATOM   1196 C  CD1 . ILE A 1 145 ? 2.737   -1.901  16.851  1.00 11.54  ? 145 ILE A CD1 1 
ATOM   1197 N  N   . PHE A 1 146 ? 6.095   -6.641  18.420  1.00 8.45   ? 146 PHE A N   1 
ATOM   1198 C  CA  . PHE A 1 146 ? 6.704   -7.893  18.005  1.00 8.72   ? 146 PHE A CA  1 
ATOM   1199 C  C   . PHE A 1 146 ? 5.964   -8.522  16.821  1.00 9.24   ? 146 PHE A C   1 
ATOM   1200 O  O   . PHE A 1 146 ? 4.726   -8.421  16.767  1.00 10.13  ? 146 PHE A O   1 
ATOM   1201 C  CB  . PHE A 1 146 ? 6.725   -8.861  19.166  1.00 9.76   ? 146 PHE A CB  1 
ATOM   1202 C  CG  . PHE A 1 146 ? 7.557   -8.385  20.314  1.00 8.14   ? 146 PHE A CG  1 
ATOM   1203 C  CD1 . PHE A 1 146 ? 8.944   -8.230  20.141  1.00 9.66   ? 146 PHE A CD1 1 
ATOM   1204 C  CD2 . PHE A 1 146 ? 7.008   -8.177  21.564  1.00 9.02   ? 146 PHE A CD2 1 
ATOM   1205 C  CE1 . PHE A 1 146 ? 9.751   -7.807  21.200  1.00 9.27   ? 146 PHE A CE1 1 
ATOM   1206 C  CE2 . PHE A 1 146 ? 7.807   -7.740  22.629  1.00 8.96   ? 146 PHE A CE2 1 
ATOM   1207 C  CZ  . PHE A 1 146 ? 9.187   -7.598  22.445  1.00 8.96   ? 146 PHE A CZ  1 
ATOM   1208 N  N   . LEU A 1 147 ? 6.715   -9.189  15.948  1.00 10.11  ? 147 LEU A N   1 
ATOM   1209 C  CA  . LEU A 1 147 ? 6.095   -9.979  14.878  1.00 9.73   ? 147 LEU A CA  1 
ATOM   1210 C  C   . LEU A 1 147 ? 6.428   -11.445 15.148  1.00 9.25   ? 147 LEU A C   1 
ATOM   1211 O  O   . LEU A 1 147 ? 7.595   -11.841 15.277  1.00 10.89  ? 147 LEU A O   1 
ATOM   1212 C  CB  . LEU A 1 147 ? 6.670   -9.608  13.512  1.00 10.20  ? 147 LEU A CB  1 
ATOM   1213 C  CG  . LEU A 1 147 ? 6.071   -8.350  12.856  1.00 10.11  ? 147 LEU A CG  1 
ATOM   1214 C  CD1 . LEU A 1 147 ? 6.271   -7.089  13.704  1.00 12.03  ? 147 LEU A CD1 1 
ATOM   1215 C  CD2 . LEU A 1 147 ? 6.707   -8.139  11.480  1.00 12.33  ? 147 LEU A CD2 1 
ATOM   1216 N  N   . LYS A 1 148 ? 5.370   -12.296 15.110  1.00 10.66  ? 148 LYS A N   1 
ATOM   1217 C  CA  . LYS A 1 148 ? 5.578   -13.743 15.099  1.00 10.65  ? 148 LYS A CA  1 
ATOM   1218 C  C   . LYS A 1 148 ? 5.068   -14.277 13.774  1.00 12.22  ? 148 LYS A C   1 
ATOM   1219 O  O   . LYS A 1 148 ? 4.231   -13.666 13.101  1.00 13.73  ? 148 LYS A O   1 
ATOM   1220 C  CB  . LYS A 1 148 ? 4.828   -14.405 16.270  1.00 14.39  ? 148 LYS A CB  1 
ATOM   1221 C  CG  . LYS A 1 148 ? 3.316   -14.303 16.197  1.00 15.01  ? 148 LYS A CG  1 
ATOM   1222 C  CD  . LYS A 1 148 ? 2.727   -15.026 17.423  1.00 19.96  ? 148 LYS A CD  1 
ATOM   1223 C  CE  . LYS A 1 148 ? 1.222   -15.045 17.334  1.00 28.59  ? 148 LYS A CE  1 
ATOM   1224 N  NZ  . LYS A 1 148 ? 0.690   -15.888 18.430  1.00 40.08  ? 148 LYS A NZ  1 
ATOM   1225 N  N   . VAL A 1 149 ? 5.598   -15.427 13.348  1.00 12.36  ? 149 VAL A N   1 
ATOM   1226 C  CA  . VAL A 1 149 ? 5.195   -16.004 12.079  1.00 12.17  ? 149 VAL A CA  1 
ATOM   1227 C  C   . VAL A 1 149 ? 3.991   -16.915 12.303  1.00 13.43  ? 149 VAL A C   1 
ATOM   1228 O  O   . VAL A 1 149 ? 4.037   -17.863 13.088  1.00 14.76  ? 149 VAL A O   1 
ATOM   1229 C  CB  . VAL A 1 149 ? 6.397   -16.758 11.501  1.00 13.37  ? 149 VAL A CB  1 
ATOM   1230 C  CG1 . VAL A 1 149 ? 5.987   -17.569 10.267  1.00 16.60  ? 149 VAL A CG1 1 
ATOM   1231 C  CG2 . VAL A 1 149 ? 7.509   -15.768 11.143  1.00 15.23  ? 149 VAL A CG2 1 
ATOM   1232 N  N   . GLY A 1 150 ? 2.942   -16.658 11.548  1.00 13.15  ? 150 GLY A N   1 
ATOM   1233 C  CA  . GLY A 1 150 ? 1.759   -17.514 11.561  1.00 15.17  ? 150 GLY A CA  1 
ATOM   1234 C  C   . GLY A 1 150 ? 0.855   -17.084 10.429  1.00 14.30  ? 150 GLY A C   1 
ATOM   1235 O  O   . GLY A 1 150 ? 1.246   -17.195 9.299   1.00 14.82  ? 150 GLY A O   1 
ATOM   1236 N  N   A SER A 1 151 ? -0.350  -16.593 10.748  0.50 13.81  ? 151 SER A N   1 
ATOM   1237 N  N   B SER A 1 151 ? -0.325  -16.553 10.767  0.50 14.37  ? 151 SER A N   1 
ATOM   1238 C  CA  A SER A 1 151 ? -1.267  -16.040 9.753   0.50 15.03  ? 151 SER A CA  1 
ATOM   1239 C  CA  B SER A 1 151 ? -1.209  -15.975 9.763   0.50 16.22  ? 151 SER A CA  1 
ATOM   1240 C  C   A SER A 1 151 ? -0.682  -14.742 9.186   0.50 13.21  ? 151 SER A C   1 
ATOM   1241 C  C   B SER A 1 151 ? -0.584  -14.717 9.165   0.50 13.99  ? 151 SER A C   1 
ATOM   1242 O  O   A SER A 1 151 ? -0.020  -13.993 9.898   0.50 14.13  ? 151 SER A O   1 
ATOM   1243 O  O   B SER A 1 151 ? 0.193   -14.008 9.813   0.50 14.51  ? 151 SER A O   1 
ATOM   1244 C  CB  A SER A 1 151 ? -2.622  -15.803 10.361  0.50 17.97  ? 151 SER A CB  1 
ATOM   1245 C  CB  B SER A 1 151 ? -2.593  -15.719 10.294  0.50 20.42  ? 151 SER A CB  1 
ATOM   1246 O  OG  A SER A 1 151 ? -2.549  -14.660 11.203  0.50 22.62  ? 151 SER A OG  1 
ATOM   1247 O  OG  B SER A 1 151 ? -3.137  -16.913 10.821  0.50 21.45  ? 151 SER A OG  1 
ATOM   1248 N  N   . ALA A 1 152 ? -0.924  -14.437 7.911   1.00 13.20  ? 152 ALA A N   1 
ATOM   1249 C  CA  . ALA A 1 152 ? -0.587  -13.149 7.307   1.00 13.13  ? 152 ALA A CA  1 
ATOM   1250 C  C   . ALA A 1 152 ? -1.216  -11.953 8.002   1.00 13.13  ? 152 ALA A C   1 
ATOM   1251 O  O   . ALA A 1 152 ? -2.356  -12.047 8.445   1.00 16.14  ? 152 ALA A O   1 
ATOM   1252 C  CB  . ALA A 1 152 ? -1.004  -13.164 5.836   1.00 16.17  ? 152 ALA A CB  1 
ATOM   1253 N  N   . LYS A 1 153 ? -0.486  -10.839 7.946   1.00 14.74  ? 153 LYS A N   1 
ATOM   1254 C  CA  . LYS A 1 153 ? -1.068  -9.591  8.391   1.00 15.11  ? 153 LYS A CA  1 
ATOM   1255 C  C   . LYS A 1 153 ? -1.493  -8.822  7.151   1.00 16.00  ? 153 LYS A C   1 
ATOM   1256 O  O   . LYS A 1 153 ? -0.659  -8.332  6.388   1.00 14.99  ? 153 LYS A O   1 
ATOM   1257 C  CB  . LYS A 1 153 ? -0.033  -8.782  9.178   1.00 13.83  ? 153 LYS A CB  1 
ATOM   1258 C  CG  . LYS A 1 153 ? -0.566  -7.582  10.005  1.00 16.28  ? 153 LYS A CG  1 
ATOM   1259 C  CD  . LYS A 1 153 ? -1.507  -7.938  11.161  1.00 18.64  ? 153 LYS A CD  1 
ATOM   1260 C  CE  . LYS A 1 153 ? -1.780  -6.786  12.085  1.00 22.71  ? 153 LYS A CE  1 
ATOM   1261 N  NZ  . LYS A 1 153 ? -2.828  -7.168  13.066  1.00 30.26  ? 153 LYS A NZ  1 
ATOM   1262 N  N   . PRO A 1 154 ? -2.813  -8.687  6.899   1.00 15.52  ? 154 PRO A N   1 
ATOM   1263 C  CA  . PRO A 1 154 ? -3.239  -8.086  5.632   1.00 17.02  ? 154 PRO A CA  1 
ATOM   1264 C  C   . PRO A 1 154 ? -2.718  -6.645  5.482   1.00 17.18  ? 154 PRO A C   1 
ATOM   1265 O  O   . PRO A 1 154 ? -2.288  -6.258  4.404   1.00 18.46  ? 154 PRO A O   1 
ATOM   1266 C  CB  . PRO A 1 154 ? -4.760  -8.096  5.829   1.00 20.52  ? 154 PRO A CB  1 
ATOM   1267 C  CG  . PRO A 1 154 ? -5.016  -9.329  6.674   1.00 19.91  ? 154 PRO A CG  1 
ATOM   1268 C  CD  . PRO A 1 154 ? -3.907  -9.283  7.701   1.00 17.97  ? 154 PRO A CD  1 
ATOM   1269 N  N   . GLY A 1 155 ? -2.633  -5.890  6.597   1.00 15.87  ? 155 GLY A N   1 
ATOM   1270 C  CA  . GLY A 1 155 ? -2.254  -4.487  6.552   1.00 17.74  ? 155 GLY A CA  1 
ATOM   1271 C  C   . GLY A 1 155 ? -0.769  -4.345  6.276   1.00 15.76  ? 155 GLY A C   1 
ATOM   1272 O  O   . GLY A 1 155 ? -0.325  -3.243  6.066   1.00 20.11  ? 155 GLY A O   1 
ATOM   1273 N  N   . LEU A 1 156 ? 0.018   -5.418  6.360   1.00 14.55  ? 156 LEU A N   1 
ATOM   1274 C  CA  . LEU A 1 156 ? 1.435   -5.436  5.996   1.00 13.36  ? 156 LEU A CA  1 
ATOM   1275 C  C   . LEU A 1 156 ? 1.680   -5.641  4.501   1.00 13.79  ? 156 LEU A C   1 
ATOM   1276 O  O   . LEU A 1 156 ? 2.776   -5.380  3.997   1.00 13.48  ? 156 LEU A O   1 
ATOM   1277 C  CB  . LEU A 1 156 ? 2.195   -6.490  6.798   1.00 13.48  ? 156 LEU A CB  1 
ATOM   1278 C  CG  . LEU A 1 156 ? 3.724   -6.533  6.631   1.00 11.82  ? 156 LEU A CG  1 
ATOM   1279 C  CD1 . LEU A 1 156 ? 4.408   -5.207  7.058   1.00 14.15  ? 156 LEU A CD1 1 
ATOM   1280 C  CD2 . LEU A 1 156 ? 4.277   -7.644  7.484   1.00 13.80  ? 156 LEU A CD2 1 
ATOM   1281 N  N   . GLN A 1 157 ? 0.717   -6.211  3.780   1.00 14.21  ? 157 GLN A N   1 
ATOM   1282 C  CA  . GLN A 1 157 ? 1.025   -6.676  2.414   1.00 15.82  ? 157 GLN A CA  1 
ATOM   1283 C  C   . GLN A 1 157 ? 1.433   -5.516  1.499   1.00 16.30  ? 157 GLN A C   1 
ATOM   1284 O  O   . GLN A 1 157 ? 2.319   -5.744  0.682   1.00 15.85  ? 157 GLN A O   1 
ATOM   1285 C  CB  . GLN A 1 157 ? -0.104  -7.546  1.852   1.00 17.83  ? 157 GLN A CB  1 
ATOM   1286 C  CG  . GLN A 1 157 ? 0.270   -8.309  0.560   1.00 19.45  ? 157 GLN A CG  1 
ATOM   1287 C  CD  . GLN A 1 157 ? 1.422   -9.258  0.805   1.00 16.64  ? 157 GLN A CD  1 
ATOM   1288 O  OE1 . GLN A 1 157 ? 1.542   -9.845  1.900   1.00 18.48  ? 157 GLN A OE1 1 
ATOM   1289 N  NE2 . GLN A 1 157 ? 2.270   -9.461  -0.206  1.00 18.58  ? 157 GLN A NE2 1 
ATOM   1290 N  N   . LYS A 1 158 ? 0.846   -4.309  1.624   1.00 15.97  ? 158 LYS A N   1 
ATOM   1291 C  CA  . LYS A 1 158 ? 1.264   -3.207  0.753   1.00 16.89  ? 158 LYS A CA  1 
ATOM   1292 C  C   . LYS A 1 158 ? 2.758   -2.904  0.904   1.00 14.49  ? 158 LYS A C   1 
ATOM   1293 O  O   . LYS A 1 158 ? 3.465   -2.564  -0.032  1.00 16.01  ? 158 LYS A O   1 
ATOM   1294 C  CB  . LYS A 1 158 ? 0.369   -1.977  0.946   1.00 19.64  ? 158 LYS A CB  1 
ATOM   1295 C  CG  . LYS A 1 158 ? -0.965  -2.070  0.204   1.00 25.94  ? 158 LYS A CG  1 
ATOM   1296 N  N   . VAL A 1 159 ? 3.258   -3.056  2.136   1.00 13.33  ? 159 VAL A N   1 
ATOM   1297 C  CA  . VAL A 1 159 ? 4.657   -2.855  2.407   1.00 12.37  ? 159 VAL A CA  1 
ATOM   1298 C  C   . VAL A 1 159 ? 5.484   -3.949  1.749   1.00 14.62  ? 159 VAL A C   1 
ATOM   1299 O  O   . VAL A 1 159 ? 6.435   -3.702  1.028   1.00 14.27  ? 159 VAL A O   1 
ATOM   1300 C  CB  . VAL A 1 159 ? 4.906   -2.869  3.911   1.00 12.74  ? 159 VAL A CB  1 
ATOM   1301 C  CG1 . VAL A 1 159 ? 6.450   -2.844  4.188   1.00 14.87  ? 159 VAL A CG1 1 
ATOM   1302 C  CG2 . VAL A 1 159 ? 4.218   -1.705  4.575   1.00 15.28  ? 159 VAL A CG2 1 
ATOM   1303 N  N   . VAL A 1 160 ? 5.121   -5.203  1.993   1.00 13.22  ? 160 VAL A N   1 
ATOM   1304 C  CA  . VAL A 1 160 ? 5.842   -6.340  1.429   1.00 15.80  ? 160 VAL A CA  1 
ATOM   1305 C  C   . VAL A 1 160 ? 5.929   -6.224  -0.084  1.00 16.12  ? 160 VAL A C   1 
ATOM   1306 O  O   . VAL A 1 160 ? 6.971   -6.507  -0.681  1.00 16.28  ? 160 VAL A O   1 
ATOM   1307 C  CB  . VAL A 1 160 ? 5.197   -7.699  1.899   1.00 17.83  ? 160 VAL A CB  1 
ATOM   1308 C  CG1 . VAL A 1 160 ? 5.543   -8.940  1.072   1.00 19.90  ? 160 VAL A CG1 1 
ATOM   1309 C  CG2 . VAL A 1 160 ? 5.464   -7.852  3.421   1.00 20.08  ? 160 VAL A CG2 1 
ATOM   1310 N  N   . ASP A 1 161 ? 4.817   -5.801  -0.720  1.00 15.83  ? 161 ASP A N   1 
ATOM   1311 C  CA  . ASP A 1 161 ? 4.841   -5.914  -2.175  1.00 19.30  ? 161 ASP A CA  1 
ATOM   1312 C  C   . ASP A 1 161 ? 5.664   -4.830  -2.840  1.00 20.26  ? 161 ASP A C   1 
ATOM   1313 O  O   . ASP A 1 161 ? 5.982   -4.982  -4.011  1.00 27.54  ? 161 ASP A O   1 
ATOM   1314 C  CB  . ASP A 1 161 ? 3.429   -5.825  -2.684  1.00 22.44  ? 161 ASP A CB  1 
ATOM   1315 C  CG  . ASP A 1 161 ? 2.788   -7.200  -2.617  1.00 21.94  ? 161 ASP A CG  1 
ATOM   1316 O  OD1 . ASP A 1 161 ? 3.545   -8.243  -2.736  1.00 27.81  ? 161 ASP A OD1 1 
ATOM   1317 O  OD2 . ASP A 1 161 ? 1.619   -7.213  -2.337  1.00 27.59  ? 161 ASP A OD2 1 
ATOM   1318 N  N   . VAL A 1 162 ? 6.048   -3.760  -2.136  1.00 18.36  ? 162 VAL A N   1 
ATOM   1319 C  CA  . VAL A 1 162 ? 6.848   -2.692  -2.746  1.00 17.91  ? 162 VAL A CA  1 
ATOM   1320 C  C   . VAL A 1 162 ? 8.325   -2.981  -2.513  1.00 16.53  ? 162 VAL A C   1 
ATOM   1321 O  O   . VAL A 1 162 ? 9.185   -2.289  -3.012  1.00 16.65  ? 162 VAL A O   1 
ATOM   1322 C  CB  . VAL A 1 162 ? 6.481   -1.311  -2.140  1.00 19.12  ? 162 VAL A CB  1 
ATOM   1323 C  CG1 . VAL A 1 162 ? 7.009   -1.076  -0.742  1.00 20.51  ? 162 VAL A CG1 1 
ATOM   1324 C  CG2 . VAL A 1 162 ? 6.792   -0.060  -2.995  1.00 19.58  ? 162 VAL A CG2 1 
ATOM   1325 N  N   . LEU A 1 163 ? 8.664   -3.987  -1.686  1.00 15.29  ? 163 LEU A N   1 
ATOM   1326 C  CA  . LEU A 1 163 ? 10.086  -4.178  -1.338  1.00 13.95  ? 163 LEU A CA  1 
ATOM   1327 C  C   . LEU A 1 163 ? 11.001  -4.525  -2.519  1.00 16.31  ? 163 LEU A C   1 
ATOM   1328 O  O   . LEU A 1 163 ? 12.193  -4.142  -2.548  1.00 17.06  ? 163 LEU A O   1 
ATOM   1329 C  CB  . LEU A 1 163 ? 10.288  -5.208  -0.242  1.00 14.98  ? 163 LEU A CB  1 
ATOM   1330 C  CG  . LEU A 1 163 ? 9.633   -4.859  1.101   1.00 13.67  ? 163 LEU A CG  1 
ATOM   1331 C  CD1 . LEU A 1 163 ? 9.885   -5.971  2.137   1.00 16.75  ? 163 LEU A CD1 1 
ATOM   1332 C  CD2 . LEU A 1 163 ? 10.206  -3.560  1.642   1.00 14.93  ? 163 LEU A CD2 1 
ATOM   1333 N  N   . ASP A 1 164 ? 10.457  -5.251  -3.514  1.00 18.92  ? 164 ASP A N   1 
ATOM   1334 C  CA  . ASP A 1 164 ? 11.263  -5.520  -4.705  1.00 22.37  ? 164 ASP A CA  1 
ATOM   1335 C  C   . ASP A 1 164 ? 11.680  -4.217  -5.413  1.00 21.66  ? 164 ASP A C   1 
ATOM   1336 O  O   . ASP A 1 164 ? 12.645  -4.283  -6.161  1.00 25.03  ? 164 ASP A O   1 
ATOM   1337 C  CB  . ASP A 1 164 ? 10.599  -6.515  -5.659  1.00 32.96  ? 164 ASP A CB  1 
ATOM   1338 C  CG  . ASP A 1 164 ? 9.623   -5.747  -6.497  1.00 41.00  ? 164 ASP A CG  1 
ATOM   1339 O  OD1 . ASP A 1 164 ? 8.688   -5.233  -5.900  1.00 39.51  ? 164 ASP A OD1 1 
ATOM   1340 O  OD2 . ASP A 1 164 ? 9.850   -5.620  -7.737  1.00 56.69  ? 164 ASP A OD2 1 
ATOM   1341 N  N   . SER A 1 165 ? 11.017  -3.063  -5.182  1.00 18.29  ? 165 SER A N   1 
ATOM   1342 C  CA  . SER A 1 165 ? 11.379  -1.814  -5.860  1.00 17.60  ? 165 SER A CA  1 
ATOM   1343 C  C   . SER A 1 165 ? 12.430  -1.045  -5.064  1.00 16.84  ? 165 SER A C   1 
ATOM   1344 O  O   . SER A 1 165 ? 12.985  -0.069  -5.561  1.00 18.43  ? 165 SER A O   1 
ATOM   1345 C  CB  . SER A 1 165 ? 10.144  -0.998  -6.136  1.00 21.95  ? 165 SER A CB  1 
ATOM   1346 O  OG  . SER A 1 165 ? 9.655   -0.420  -4.934  1.00 21.19  ? 165 SER A OG  1 
ATOM   1347 N  N   . ILE A 1 166 ? 12.705  -1.522  -3.849  1.00 15.36  ? 166 ILE A N   1 
ATOM   1348 C  CA  . ILE A 1 166 ? 13.728  -0.881  -3.018  1.00 14.80  ? 166 ILE A CA  1 
ATOM   1349 C  C   . ILE A 1 166 ? 14.809  -1.877  -2.547  1.00 14.03  ? 166 ILE A C   1 
ATOM   1350 O  O   . ILE A 1 166 ? 15.176  -1.902  -1.385  1.00 15.04  ? 166 ILE A O   1 
ATOM   1351 C  CB  . ILE A 1 166 ? 13.131  -0.036  -1.857  1.00 13.20  ? 166 ILE A CB  1 
ATOM   1352 C  CG1 . ILE A 1 166 ? 12.280  -0.881  -0.912  1.00 13.33  ? 166 ILE A CG1 1 
ATOM   1353 C  CG2 . ILE A 1 166 ? 12.385  1.215   -2.375  1.00 15.84  ? 166 ILE A CG2 1 
ATOM   1354 C  CD1 . ILE A 1 166 ? 12.280  -0.298  0.474   1.00 14.73  ? 166 ILE A CD1 1 
ATOM   1355 N  N   . LYS A 1 167 ? 15.209  -2.805  -3.423  1.00 14.93  ? 167 LYS A N   1 
ATOM   1356 C  CA  . LYS A 1 167 ? 16.016  -3.934  -2.997  1.00 14.56  ? 167 LYS A CA  1 
ATOM   1357 C  C   . LYS A 1 167 ? 17.320  -3.506  -2.323  1.00 13.34  ? 167 LYS A C   1 
ATOM   1358 O  O   . LYS A 1 167 ? 17.749  -4.159  -1.383  1.00 14.21  ? 167 LYS A O   1 
ATOM   1359 C  CB  . LYS A 1 167 ? 16.301  -4.856  -4.201  1.00 16.34  ? 167 LYS A CB  1 
ATOM   1360 C  CG  . LYS A 1 167 ? 17.063  -6.117  -3.826  1.00 17.97  ? 167 LYS A CG  1 
ATOM   1361 C  CD  . LYS A 1 167 ? 17.361  -7.013  -5.044  1.00 23.83  ? 167 LYS A CD  1 
ATOM   1362 C  CE  . LYS A 1 167 ? 18.163  -8.263  -4.698  1.00 31.24  ? 167 LYS A CE  1 
ATOM   1363 N  NZ  . LYS A 1 167 ? 18.190  -9.244  -5.840  1.00 45.51  ? 167 LYS A NZ  1 
ATOM   1364 N  N   . THR A 1 168 ? 17.939  -2.440  -2.842  1.00 13.60  ? 168 THR A N   1 
ATOM   1365 C  CA  . THR A 1 168 ? 19.307  -2.125  -2.477  1.00 14.26  ? 168 THR A CA  1 
ATOM   1366 C  C   . THR A 1 168 ? 19.360  -0.747  -1.797  1.00 12.09  ? 168 THR A C   1 
ATOM   1367 O  O   . THR A 1 168 ? 18.444  0.102   -1.899  1.00 14.75  ? 168 THR A O   1 
ATOM   1368 C  CB  . THR A 1 168 ? 20.238  -2.150  -3.725  1.00 14.97  ? 168 THR A CB  1 
ATOM   1369 O  OG1 . THR A 1 168 ? 19.617  -1.332  -4.720  1.00 16.72  ? 168 THR A OG1 1 
ATOM   1370 C  CG2 . THR A 1 168 ? 20.417  -3.592  -4.183  1.00 17.05  ? 168 THR A CG2 1 
ATOM   1371 N  N   . LYS A 1 169 ? 20.426  -0.618  -1.035  1.00 14.60  ? 169 LYS A N   1 
ATOM   1372 C  CA  . LYS A 1 169 ? 20.686  0.569   -0.224  1.00 13.92  ? 169 LYS A CA  1 
ATOM   1373 C  C   . LYS A 1 169 ? 20.610  1.865   -1.019  1.00 13.71  ? 169 LYS A C   1 
ATOM   1374 O  O   . LYS A 1 169 ? 21.179  1.949   -2.125  1.00 17.70  ? 169 LYS A O   1 
ATOM   1375 C  CB  . LYS A 1 169 ? 22.140  0.461   0.277   1.00 14.70  ? 169 LYS A CB  1 
ATOM   1376 C  CG  . LYS A 1 169 ? 22.649  1.707   1.067   1.00 17.72  ? 169 LYS A CG  1 
ATOM   1377 C  CD  . LYS A 1 169 ? 23.943  1.550   1.802   1.00 19.27  ? 169 LYS A CD  1 
ATOM   1378 C  CE  . LYS A 1 169 ? 24.429  2.760   2.583   1.00 39.47  ? 169 LYS A CE  1 
ATOM   1379 N  N   . GLY A 1 170 ? 19.763  2.795   -0.530  1.00 14.93  ? 170 GLY A N   1 
ATOM   1380 C  CA  . GLY A 1 170 ? 19.624  4.109   -1.151  1.00 16.85  ? 170 GLY A CA  1 
ATOM   1381 C  C   . GLY A 1 170 ? 18.430  4.205   -2.108  1.00 18.57  ? 170 GLY A C   1 
ATOM   1382 O  O   . GLY A 1 170 ? 18.086  5.302   -2.566  1.00 20.57  ? 170 GLY A O   1 
ATOM   1383 N  N   . LYS A 1 171 ? 17.799  3.066   -2.452  1.00 15.79  ? 171 LYS A N   1 
ATOM   1384 C  CA  . LYS A 1 171 ? 16.542  3.078   -3.204  1.00 17.10  ? 171 LYS A CA  1 
ATOM   1385 C  C   . LYS A 1 171 ? 15.371  3.537   -2.357  1.00 14.42  ? 171 LYS A C   1 
ATOM   1386 O  O   . LYS A 1 171 ? 15.221  3.077   -1.226  1.00 15.36  ? 171 LYS A O   1 
ATOM   1387 C  CB  . LYS A 1 171 ? 16.307  1.721   -3.879  1.00 16.45  ? 171 LYS A CB  1 
ATOM   1388 C  CG  . LYS A 1 171 ? 17.343  1.445   -4.972  1.00 21.86  ? 171 LYS A CG  1 
ATOM   1389 C  CD  . LYS A 1 171 ? 16.972  0.244   -5.873  1.00 30.09  ? 171 LYS A CD  1 
ATOM   1390 C  CE  . LYS A 1 171 ? 16.334  0.670   -7.205  1.00 51.23  ? 171 LYS A CE  1 
ATOM   1391 N  NZ  . LYS A 1 171 ? 15.483  -0.376  -7.880  1.00 44.16  ? 171 LYS A NZ  1 
ATOM   1392 N  N   . SER A 1 172 ? 14.504  4.360   -2.909  1.00 15.00  ? 172 SER A N   1 
ATOM   1393 C  CA  . SER A 1 172 ? 13.239  4.804   -2.346  1.00 17.10  ? 172 SER A CA  1 
ATOM   1394 C  C   . SER A 1 172 ? 12.142  4.608   -3.389  1.00 14.50  ? 172 SER A C   1 
ATOM   1395 O  O   . SER A 1 172 ? 12.361  4.564   -4.630  1.00 19.18  ? 172 SER A O   1 
ATOM   1396 C  CB  . SER A 1 172 ? 13.316  6.235   -1.812  1.00 17.19  ? 172 SER A CB  1 
ATOM   1397 O  OG  . SER A 1 172 ? 13.521  7.134   -2.878  1.00 19.96  ? 172 SER A OG  1 
ATOM   1398 N  N   . ALA A 1 173 ? 10.903  4.615   -2.864  1.00 17.93  ? 173 ALA A N   1 
ATOM   1399 C  CA  . ALA A 1 173 ? 9.736   4.596   -3.753  1.00 17.03  ? 173 ALA A CA  1 
ATOM   1400 C  C   . ALA A 1 173 ? 8.607   5.377   -3.088  1.00 17.78  ? 173 ALA A C   1 
ATOM   1401 O  O   . ALA A 1 173 ? 8.515   5.453   -1.854  1.00 15.11  ? 173 ALA A O   1 
ATOM   1402 C  CB  . ALA A 1 173 ? 9.325   3.149   -3.964  1.00 20.58  ? 173 ALA A CB  1 
ATOM   1403 N  N   . ASP A 1 174 ? 7.738   5.981   -3.895  1.00 19.11  ? 174 ASP A N   1 
ATOM   1404 C  CA  . ASP A 1 174 ? 6.556   6.619   -3.356  1.00 19.38  ? 174 ASP A CA  1 
ATOM   1405 C  C   . ASP A 1 174 ? 5.777   5.581   -2.572  1.00 19.81  ? 174 ASP A C   1 
ATOM   1406 O  O   . ASP A 1 174 ? 5.697   4.394   -2.911  1.00 21.08  ? 174 ASP A O   1 
ATOM   1407 C  CB  . ASP A 1 174 ? 5.736   7.316   -4.461  1.00 24.57  ? 174 ASP A CB  1 
ATOM   1408 C  CG  . ASP A 1 174 ? 6.505   8.437   -5.197  1.00 40.07  ? 174 ASP A CG  1 
ATOM   1409 O  OD1 . ASP A 1 174 ? 7.152   9.319   -4.546  1.00 48.01  ? 174 ASP A OD1 1 
ATOM   1410 O  OD2 . ASP A 1 174 ? 6.470   8.456   -6.461  1.00 44.29  ? 174 ASP A OD2 1 
ATOM   1411 N  N   . PHE A 1 175 ? 5.278   6.039   -1.430  1.00 16.18  ? 175 PHE A N   1 
ATOM   1412 C  CA  . PHE A 1 175 ? 4.504   5.162   -0.579  1.00 16.24  ? 175 PHE A CA  1 
ATOM   1413 C  C   . PHE A 1 175 ? 3.439   5.961   0.130   1.00 16.80  ? 175 PHE A C   1 
ATOM   1414 O  O   . PHE A 1 175 ? 3.462   6.087   1.343   1.00 19.98  ? 175 PHE A O   1 
ATOM   1415 C  CB  . PHE A 1 175 ? 5.449   4.353   0.296   1.00 16.97  ? 175 PHE A CB  1 
ATOM   1416 C  CG  . PHE A 1 175 ? 4.839   3.080   0.810   1.00 14.99  ? 175 PHE A CG  1 
ATOM   1417 C  CD1 . PHE A 1 175 ? 4.608   2.011   -0.035  1.00 16.35  ? 175 PHE A CD1 1 
ATOM   1418 C  CD2 . PHE A 1 175 ? 4.400   2.969   2.129   1.00 15.86  ? 175 PHE A CD2 1 
ATOM   1419 C  CE1 . PHE A 1 175 ? 4.026   0.862   0.461   1.00 18.83  ? 175 PHE A CE1 1 
ATOM   1420 C  CE2 . PHE A 1 175 ? 3.881   1.767   2.650   1.00 17.27  ? 175 PHE A CE2 1 
ATOM   1421 C  CZ  . PHE A 1 175 ? 3.658   0.718   1.782   1.00 16.74  ? 175 PHE A CZ  1 
ATOM   1422 N  N   . THR A 1 176 ? 2.511   6.488   -0.657  1.00 16.63  ? 176 THR A N   1 
ATOM   1423 C  CA  . THR A 1 176 ? 1.450   7.309   -0.113  1.00 14.82  ? 176 THR A CA  1 
ATOM   1424 C  C   . THR A 1 176 ? 0.268   6.479   0.321   1.00 13.25  ? 176 THR A C   1 
ATOM   1425 O  O   . THR A 1 176 ? 0.096   5.337   -0.140  1.00 15.16  ? 176 THR A O   1 
ATOM   1426 C  CB  . THR A 1 176 ? 1.055   8.379   -1.132  1.00 17.10  ? 176 THR A CB  1 
ATOM   1427 O  OG1 . THR A 1 176 ? 0.650   7.766   -2.359  1.00 23.46  ? 176 THR A OG1 1 
ATOM   1428 C  CG2 . THR A 1 176 ? 2.166   9.396   -1.308  1.00 25.76  ? 176 THR A CG2 1 
ATOM   1429 N  N   . ASN A 1 177 ? -0.568  7.060   1.182   1.00 14.46  ? 177 ASN A N   1 
ATOM   1430 C  CA  . ASN A 1 177 ? -1.853  6.506   1.568   1.00 14.33  ? 177 ASN A CA  1 
ATOM   1431 C  C   . ASN A 1 177 ? -1.749  5.180   2.318   1.00 14.59  ? 177 ASN A C   1 
ATOM   1432 O  O   . ASN A 1 177 ? -2.656  4.361   2.218   1.00 19.98  ? 177 ASN A O   1 
ATOM   1433 C  CB  . ASN A 1 177 ? -2.767  6.433   0.356   1.00 16.74  ? 177 ASN A CB  1 
ATOM   1434 C  CG  . ASN A 1 177 ? -2.983  7.789   -0.281  1.00 17.49  ? 177 ASN A CG  1 
ATOM   1435 O  OD1 . ASN A 1 177 ? -3.610  8.651   0.321   1.00 20.87  ? 177 ASN A OD1 1 
ATOM   1436 N  ND2 . ASN A 1 177 ? -2.372  7.995   -1.423  1.00 17.26  ? 177 ASN A ND2 1 
ATOM   1437 N  N   . PHE A 1 178 ? -0.636  4.956   3.002   1.00 13.89  ? 178 PHE A N   1 
ATOM   1438 C  CA  . PHE A 1 178 ? -0.550  3.729   3.777   1.00 14.10  ? 178 PHE A CA  1 
ATOM   1439 C  C   . PHE A 1 178 ? -1.019  4.013   5.197   1.00 14.21  ? 178 PHE A C   1 
ATOM   1440 O  O   . PHE A 1 178 ? -0.572  5.000   5.798   1.00 15.30  ? 178 PHE A O   1 
ATOM   1441 C  CB  . PHE A 1 178 ? 0.916   3.282   3.821   1.00 14.42  ? 178 PHE A CB  1 
ATOM   1442 C  CG  . PHE A 1 178 ? 1.047   2.044   4.674   1.00 15.10  ? 178 PHE A CG  1 
ATOM   1443 C  CD1 . PHE A 1 178 ? 0.672   0.816   4.145   1.00 16.19  ? 178 PHE A CD1 1 
ATOM   1444 C  CD2 . PHE A 1 178 ? 1.458   2.088   6.010   1.00 13.71  ? 178 PHE A CD2 1 
ATOM   1445 C  CE1 . PHE A 1 178 ? 0.701   -0.338  4.912   1.00 18.09  ? 178 PHE A CE1 1 
ATOM   1446 C  CE2 . PHE A 1 178 ? 1.499   0.927   6.796   1.00 14.41  ? 178 PHE A CE2 1 
ATOM   1447 C  CZ  . PHE A 1 178 ? 1.116   -0.279  6.239   1.00 14.70  ? 178 PHE A CZ  1 
ATOM   1448 N  N   . ASP A 1 179 ? -1.890  3.191   5.736   1.00 15.35  ? 179 ASP A N   1 
ATOM   1449 C  CA  . ASP A 1 179 ? -2.433  3.405   7.063   1.00 15.23  ? 179 ASP A CA  1 
ATOM   1450 C  C   . ASP A 1 179 ? -1.742  2.524   8.082   1.00 13.07  ? 179 ASP A C   1 
ATOM   1451 O  O   . ASP A 1 179 ? -1.961  1.314   8.131   1.00 14.40  ? 179 ASP A O   1 
ATOM   1452 C  CB  . ASP A 1 179 ? -3.937  3.116   7.015   1.00 17.55  ? 179 ASP A CB  1 
ATOM   1453 C  CG  . ASP A 1 179 ? -4.703  3.457   8.270   1.00 18.36  ? 179 ASP A CG  1 
ATOM   1454 O  OD1 . ASP A 1 179 ? -4.046  3.673   9.306   1.00 16.28  ? 179 ASP A OD1 1 
ATOM   1455 O  OD2 . ASP A 1 179 ? -5.921  3.531   8.174   1.00 29.09  ? 179 ASP A OD2 1 
ATOM   1456 N  N   . PRO A 1 180 ? -0.931  3.100   8.993   1.00 11.83  ? 180 PRO A N   1 
ATOM   1457 C  CA  . PRO A 1 180 ? -0.177  2.263   9.933   1.00 12.18  ? 180 PRO A CA  1 
ATOM   1458 C  C   . PRO A 1 180 ? -1.064  1.662   11.020  1.00 12.44  ? 180 PRO A C   1 
ATOM   1459 O  O   . PRO A 1 180 ? -0.627  0.741   11.716  1.00 13.51  ? 180 PRO A O   1 
ATOM   1460 C  CB  . PRO A 1 180 ? 0.824   3.271   10.517  1.00 14.14  ? 180 PRO A CB  1 
ATOM   1461 C  CG  . PRO A 1 180 ? 0.149   4.629   10.375  1.00 13.54  ? 180 PRO A CG  1 
ATOM   1462 C  CD  . PRO A 1 180 ? -0.601  4.532   9.059   1.00 13.61  ? 180 PRO A CD  1 
ATOM   1463 N  N   . ARG A 1 181 ? -2.344  2.034   11.050  1.00 12.28  ? 181 ARG A N   1 
ATOM   1464 C  CA  . ARG A 1 181 ? -3.253  1.367   11.990  1.00 13.75  ? 181 ARG A CA  1 
ATOM   1465 C  C   . ARG A 1 181 ? -3.384  -0.118  11.675  1.00 14.24  ? 181 ARG A C   1 
ATOM   1466 O  O   . ARG A 1 181 ? -3.719  -0.901  12.560  1.00 15.07  ? 181 ARG A O   1 
ATOM   1467 C  CB  . ARG A 1 181 ? -4.629  2.035   11.994  1.00 15.61  ? 181 ARG A CB  1 
ATOM   1468 C  CG  . ARG A 1 181 ? -4.536  3.434   12.581  1.00 16.00  ? 181 ARG A CG  1 
ATOM   1469 C  CD  . ARG A 1 181 ? -5.860  4.137   12.526  1.00 16.97  ? 181 ARG A CD  1 
ATOM   1470 N  NE  . ARG A 1 181 ? -6.234  4.407   11.143  1.00 17.77  ? 181 ARG A NE  1 
ATOM   1471 C  CZ  . ARG A 1 181 ? -7.287  5.152   10.812  1.00 18.35  ? 181 ARG A CZ  1 
ATOM   1472 N  NH1 . ARG A 1 181 ? -8.057  5.636   11.779  1.00 23.21  ? 181 ARG A NH1 1 
ATOM   1473 N  NH2 . ARG A 1 181 ? -7.552  5.351   9.535   1.00 22.55  ? 181 ARG A NH2 1 
ATOM   1474 N  N   . GLY A 1 182 ? -3.204  -0.484  10.405  1.00 13.41  ? 182 GLY A N   1 
ATOM   1475 C  CA  . GLY A 1 182 ? -3.286  -1.883  10.025  1.00 15.55  ? 182 GLY A CA  1 
ATOM   1476 C  C   . GLY A 1 182 ? -2.136  -2.772  10.541  1.00 13.68  ? 182 GLY A C   1 
ATOM   1477 O  O   . GLY A 1 182 ? -2.141  -3.978  10.268  1.00 17.49  ? 182 GLY A O   1 
ATOM   1478 N  N   . LEU A 1 183 ? -1.140  -2.170  11.229  1.00 13.42  ? 183 LEU A N   1 
ATOM   1479 C  CA  . LEU A 1 183 ? -0.006  -2.893  11.752  1.00 13.59  ? 183 LEU A CA  1 
ATOM   1480 C  C   . LEU A 1 183 ? -0.136  -3.116  13.269  1.00 11.73  ? 183 LEU A C   1 
ATOM   1481 O  O   . LEU A 1 183 ? 0.769   -3.705  13.898  1.00 14.65  ? 183 LEU A O   1 
ATOM   1482 C  CB  . LEU A 1 183 ? 1.310   -2.176  11.446  1.00 13.41  ? 183 LEU A CB  1 
ATOM   1483 C  CG  . LEU A 1 183 ? 1.606   -2.049  9.946   1.00 13.29  ? 183 LEU A CG  1 
ATOM   1484 C  CD1 . LEU A 1 183 ? 2.829   -1.212  9.748   1.00 16.69  ? 183 LEU A CD1 1 
ATOM   1485 C  CD2 . LEU A 1 183 ? 1.686   -3.400  9.276   1.00 18.16  ? 183 LEU A CD2 1 
ATOM   1486 N  N   . LEU A 1 184 ? -1.228  -2.631  13.902  1.00 13.31  ? 184 LEU A N   1 
ATOM   1487 C  CA  . LEU A 1 184 ? -1.343  -2.653  15.358  1.00 13.32  ? 184 LEU A CA  1 
ATOM   1488 C  C   . LEU A 1 184 ? -2.116  -3.890  15.832  1.00 16.10  ? 184 LEU A C   1 
ATOM   1489 O  O   . LEU A 1 184 ? -3.123  -4.317  15.267  1.00 23.19  ? 184 LEU A O   1 
ATOM   1490 C  CB  . LEU A 1 184 ? -2.133  -1.431  15.832  1.00 13.58  ? 184 LEU A CB  1 
ATOM   1491 C  CG  . LEU A 1 184 ? -1.546  -0.072  15.427  1.00 12.85  ? 184 LEU A CG  1 
ATOM   1492 C  CD1 . LEU A 1 184 ? -2.449  1.043   15.918  1.00 15.99  ? 184 LEU A CD1 1 
ATOM   1493 C  CD2 . LEU A 1 184 ? -0.138  0.068   15.946  1.00 15.59  ? 184 LEU A CD2 1 
ATOM   1494 N  N   . PRO A 1 185 ? -1.687  -4.494  16.950  1.00 14.10  ? 185 PRO A N   1 
ATOM   1495 C  CA  . PRO A 1 185 ? -2.424  -5.649  17.492  1.00 13.64  ? 185 PRO A CA  1 
ATOM   1496 C  C   . PRO A 1 185 ? -3.710  -5.152  18.137  1.00 14.45  ? 185 PRO A C   1 
ATOM   1497 O  O   . PRO A 1 185 ? -3.950  -3.932  18.186  1.00 16.70  ? 185 PRO A O   1 
ATOM   1498 C  CB  . PRO A 1 185 ? -1.485  -6.224  18.535  1.00 13.71  ? 185 PRO A CB  1 
ATOM   1499 C  CG  . PRO A 1 185 ? -0.706  -5.004  18.987  1.00 11.92  ? 185 PRO A CG  1 
ATOM   1500 C  CD  . PRO A 1 185 ? -0.536  -4.081  17.768  1.00 11.49  ? 185 PRO A CD  1 
ATOM   1501 N  N   . GLU A 1 186 ? -4.554  -6.053  18.645  1.00 15.30  ? 186 GLU A N   1 
ATOM   1502 C  CA  . GLU A 1 186 ? -5.824  -5.663  19.239  1.00 16.30  ? 186 GLU A CA  1 
ATOM   1503 C  C   . GLU A 1 186 ? -5.565  -4.891  20.517  1.00 14.84  ? 186 GLU A C   1 
ATOM   1504 O  O   . GLU A 1 186 ? -6.180  -3.845  20.760  1.00 18.35  ? 186 GLU A O   1 
ATOM   1505 C  CB  . GLU A 1 186 ? -6.649  -6.893  19.639  1.00 25.29  ? 186 GLU A CB  1 
ATOM   1506 C  CG  . GLU A 1 186 ? -7.307  -7.555  18.486  1.00 34.71  ? 186 GLU A CG  1 
ATOM   1507 C  CD  . GLU A 1 186 ? -8.049  -8.789  18.993  1.00 31.64  ? 186 GLU A CD  1 
ATOM   1508 O  OE1 . GLU A 1 186 ? -8.392  -9.635  18.168  1.00 44.59  ? 186 GLU A OE1 1 
ATOM   1509 O  OE2 . GLU A 1 186 ? -8.213  -8.880  20.232  1.00 26.76  ? 186 GLU A OE2 1 
ATOM   1510 N  N   . SER A 1 187 ? -4.669  -5.413  21.367  1.00 14.84  ? 187 SER A N   1 
ATOM   1511 C  CA  . SER A 1 187 ? -4.473  -4.770  22.651  1.00 14.33  ? 187 SER A CA  1 
ATOM   1512 C  C   . SER A 1 187 ? -3.333  -3.763  22.610  1.00 13.50  ? 187 SER A C   1 
ATOM   1513 O  O   . SER A 1 187 ? -2.301  -4.014  21.969  1.00 15.93  ? 187 SER A O   1 
ATOM   1514 C  CB  . SER A 1 187 ? -4.088  -5.858  23.666  1.00 15.45  ? 187 SER A CB  1 
ATOM   1515 O  OG  . SER A 1 187 ? -3.827  -5.294  24.959  1.00 16.75  ? 187 SER A OG  1 
ATOM   1516 N  N   . LEU A 1 188 ? -3.529  -2.677  23.369  1.00 14.24  ? 188 LEU A N   1 
ATOM   1517 C  CA  . LEU A 1 188 ? -2.462  -1.700  23.605  1.00 15.56  ? 188 LEU A CA  1 
ATOM   1518 C  C   . LEU A 1 188 ? -1.782  -1.841  24.969  1.00 13.43  ? 188 LEU A C   1 
ATOM   1519 O  O   . LEU A 1 188 ? -1.082  -0.937  25.411  1.00 16.37  ? 188 LEU A O   1 
ATOM   1520 C  CB  . LEU A 1 188 ? -2.966  -0.265  23.428  1.00 18.48  ? 188 LEU A CB  1 
ATOM   1521 C  CG  . LEU A 1 188 ? -3.408  0.088   22.002  1.00 19.91  ? 188 LEU A CG  1 
ATOM   1522 C  CD1 . LEU A 1 188 ? -3.954  1.510   21.879  1.00 22.19  ? 188 LEU A CD1 1 
ATOM   1523 C  CD2 . LEU A 1 188 ? -2.290  -0.188  20.971  1.00 21.57  ? 188 LEU A CD2 1 
ATOM   1524 N  N   . ASP A 1 189 ? -1.916  -3.028  25.610  1.00 13.86  ? 189 ASP A N   1 
ATOM   1525 C  CA  . ASP A 1 189 ? -1.169  -3.284  26.822  1.00 14.47  ? 189 ASP A CA  1 
ATOM   1526 C  C   . ASP A 1 189 ? 0.339   -3.211  26.522  1.00 12.70  ? 189 ASP A C   1 
ATOM   1527 O  O   . ASP A 1 189 ? 0.759   -3.700  25.460  1.00 11.79  ? 189 ASP A O   1 
ATOM   1528 C  CB  . ASP A 1 189 ? -1.533  -4.636  27.415  1.00 17.25  ? 189 ASP A CB  1 
ATOM   1529 C  CG  . ASP A 1 189 ? -2.899  -4.741  28.083  1.00 22.21  ? 189 ASP A CG  1 
ATOM   1530 O  OD1 . ASP A 1 189 ? -3.477  -3.667  28.280  1.00 27.05  ? 189 ASP A OD1 1 
ATOM   1531 O  OD2 . ASP A 1 189 ? -3.309  -5.889  28.363  1.00 28.27  ? 189 ASP A OD2 1 
ATOM   1532 N  N   . TYR A 1 190 ? 1.121   -2.582  27.412  1.00 11.68  ? 190 TYR A N   1 
ATOM   1533 C  CA  . TYR A 1 190 ? 2.513   -2.332  27.075  1.00 11.18  ? 190 TYR A CA  1 
ATOM   1534 C  C   . TYR A 1 190 ? 3.421   -2.367  28.290  1.00 10.56  ? 190 TYR A C   1 
ATOM   1535 O  O   . TYR A 1 190 ? 2.959   -2.279  29.442  1.00 12.23  ? 190 TYR A O   1 
ATOM   1536 C  CB  . TYR A 1 190 ? 2.614   -0.976  26.348  1.00 11.79  ? 190 TYR A CB  1 
ATOM   1537 C  CG  . TYR A 1 190 ? 2.280   0.217   27.219  1.00 11.74  ? 190 TYR A CG  1 
ATOM   1538 C  CD1 . TYR A 1 190 ? 3.203   0.807   28.099  1.00 12.30  ? 190 TYR A CD1 1 
ATOM   1539 C  CD2 . TYR A 1 190 ? 0.992   0.736   27.209  1.00 12.54  ? 190 TYR A CD2 1 
ATOM   1540 C  CE1 . TYR A 1 190 ? 2.827   1.851   28.947  1.00 11.84  ? 190 TYR A CE1 1 
ATOM   1541 C  CE2 . TYR A 1 190 ? 0.636   1.827   27.983  1.00 13.21  ? 190 TYR A CE2 1 
ATOM   1542 C  CZ  . TYR A 1 190 ? 1.542   2.369   28.884  1.00 11.86  ? 190 TYR A CZ  1 
ATOM   1543 O  OH  . TYR A 1 190 ? 1.229   3.415   29.677  1.00 14.06  ? 190 TYR A OH  1 
ATOM   1544 N  N   . TRP A 1 191 ? 4.708   -2.515  27.974  1.00 9.93   ? 191 TRP A N   1 
ATOM   1545 C  CA  . TRP A 1 191 ? 5.771   -2.238  28.948  1.00 10.53  ? 191 TRP A CA  1 
ATOM   1546 C  C   . TRP A 1 191 ? 6.479   -0.958  28.525  1.00 10.49  ? 191 TRP A C   1 
ATOM   1547 O  O   . TRP A 1 191 ? 6.516   -0.648  27.344  1.00 10.99  ? 191 TRP A O   1 
ATOM   1548 C  CB  . TRP A 1 191 ? 6.780   -3.389  28.943  1.00 11.04  ? 191 TRP A CB  1 
ATOM   1549 C  CG  . TRP A 1 191 ? 6.268   -4.708  29.361  1.00 10.53  ? 191 TRP A CG  1 
ATOM   1550 C  CD1 . TRP A 1 191 ? 6.052   -5.116  30.662  1.00 12.92  ? 191 TRP A CD1 1 
ATOM   1551 C  CD2 . TRP A 1 191 ? 5.991   -5.837  28.485  1.00 9.94   ? 191 TRP A CD2 1 
ATOM   1552 N  NE1 . TRP A 1 191 ? 5.606   -6.433  30.634  1.00 14.29  ? 191 TRP A NE1 1 
ATOM   1553 C  CE2 . TRP A 1 191 ? 5.566   -6.889  29.334  1.00 11.17  ? 191 TRP A CE2 1 
ATOM   1554 C  CE3 . TRP A 1 191 ? 6.072   -6.057  27.087  1.00 11.42  ? 191 TRP A CE3 1 
ATOM   1555 C  CZ2 . TRP A 1 191 ? 5.271   -8.149  28.814  1.00 13.50  ? 191 TRP A CZ2 1 
ATOM   1556 C  CZ3 . TRP A 1 191 ? 5.809   -7.320  26.600  1.00 11.84  ? 191 TRP A CZ3 1 
ATOM   1557 C  CH2 . TRP A 1 191 ? 5.361   -8.324  27.454  1.00 14.76  ? 191 TRP A CH2 1 
ATOM   1558 N  N   . THR A 1 192 ? 7.037   -0.229  29.491  1.00 9.81   ? 192 THR A N   1 
ATOM   1559 C  CA  . THR A 1 192 ? 7.759   0.987   29.154  1.00 10.12  ? 192 THR A CA  1 
ATOM   1560 C  C   . THR A 1 192 ? 8.999   1.127   30.009  1.00 9.40   ? 192 THR A C   1 
ATOM   1561 O  O   . THR A 1 192 ? 9.008   0.754   31.199  1.00 10.54  ? 192 THR A O   1 
ATOM   1562 C  CB  . THR A 1 192 ? 6.836   2.204   29.274  1.00 10.16  ? 192 THR A CB  1 
ATOM   1563 O  OG1 . THR A 1 192 ? 7.541   3.361   28.817  1.00 10.58  ? 192 THR A OG1 1 
ATOM   1564 C  CG2 . THR A 1 192 ? 6.257   2.463   30.649  1.00 11.36  ? 192 THR A CG2 1 
ATOM   1565 N  N   . TYR A 1 193 ? 10.043  1.725   29.431  1.00 9.71   ? 193 TYR A N   1 
ATOM   1566 C  CA  . TYR A 1 193 ? 11.285  1.995   30.161  1.00 10.39  ? 193 TYR A CA  1 
ATOM   1567 C  C   . TYR A 1 193 ? 12.058  3.062   29.406  1.00 9.64   ? 193 TYR A C   1 
ATOM   1568 O  O   . TYR A 1 193 ? 11.825  3.237   28.197  1.00 9.54   ? 193 TYR A O   1 
ATOM   1569 C  CB  . TYR A 1 193 ? 12.109  0.689   30.338  1.00 10.49  ? 193 TYR A CB  1 
ATOM   1570 C  CG  . TYR A 1 193 ? 12.766  0.257   29.052  1.00 8.44   ? 193 TYR A CG  1 
ATOM   1571 C  CD1 . TYR A 1 193 ? 12.085  -0.487  28.073  1.00 9.29   ? 193 TYR A CD1 1 
ATOM   1572 C  CD2 . TYR A 1 193 ? 14.115  0.563   28.860  1.00 9.50   ? 193 TYR A CD2 1 
ATOM   1573 C  CE1 . TYR A 1 193 ? 12.721  -0.847  26.900  1.00 8.84   ? 193 TYR A CE1 1 
ATOM   1574 C  CE2 . TYR A 1 193 ? 14.745  0.251   27.665  1.00 9.98   ? 193 TYR A CE2 1 
ATOM   1575 C  CZ  . TYR A 1 193 ? 14.038  -0.440  26.695  1.00 8.89   ? 193 TYR A CZ  1 
ATOM   1576 O  OH  . TYR A 1 193 ? 14.686  -0.735  25.531  1.00 8.64   ? 193 TYR A OH  1 
ATOM   1577 N  N   . PRO A 1 194 ? 13.006  3.745   30.073  1.00 9.99   ? 194 PRO A N   1 
ATOM   1578 C  CA  . PRO A 1 194 ? 13.835  4.726   29.365  1.00 10.47  ? 194 PRO A CA  1 
ATOM   1579 C  C   . PRO A 1 194 ? 15.023  4.061   28.719  1.00 9.58   ? 194 PRO A C   1 
ATOM   1580 O  O   . PRO A 1 194 ? 15.760  3.306   29.363  1.00 11.20  ? 194 PRO A O   1 
ATOM   1581 C  CB  . PRO A 1 194 ? 14.312  5.633   30.502  1.00 12.31  ? 194 PRO A CB  1 
ATOM   1582 C  CG  . PRO A 1 194 ? 14.355  4.744   31.726  1.00 12.34  ? 194 PRO A CG  1 
ATOM   1583 C  CD  . PRO A 1 194 ? 13.175  3.800   31.537  1.00 12.82  ? 194 PRO A CD  1 
ATOM   1584 N  N   . GLY A 1 195 ? 15.279  4.414   27.459  1.00 9.57   ? 195 GLY A N   1 
ATOM   1585 C  CA  . GLY A 1 195 ? 16.360  3.761   26.723  1.00 10.17  ? 195 GLY A CA  1 
ATOM   1586 C  C   . GLY A 1 195 ? 16.909  4.660   25.643  1.00 8.37   ? 195 GLY A C   1 
ATOM   1587 O  O   . GLY A 1 195 ? 17.036  5.886   25.804  1.00 9.48   ? 195 GLY A O   1 
ATOM   1588 N  N   . SER A 1 196 ? 17.316  3.987   24.564  1.00 8.78   ? 196 SER A N   1 
ATOM   1589 C  CA  . SER A 1 196 ? 18.161  4.606   23.587  1.00 9.34   ? 196 SER A CA  1 
ATOM   1590 C  C   . SER A 1 196 ? 17.721  4.213   22.183  1.00 8.64   ? 196 SER A C   1 
ATOM   1591 O  O   . SER A 1 196 ? 16.951  3.269   21.992  1.00 8.84   ? 196 SER A O   1 
ATOM   1592 C  CB  . SER A 1 196 ? 19.635  4.193   23.776  1.00 9.79   ? 196 SER A CB  1 
ATOM   1593 O  OG  . SER A 1 196 ? 19.868  2.845   23.290  1.00 9.73   ? 196 SER A OG  1 
ATOM   1594 N  N   . LEU A 1 197 ? 18.280  4.900   21.166  1.00 9.02   ? 197 LEU A N   1 
ATOM   1595 C  CA  . LEU A 1 197 ? 18.332  4.341   19.832  1.00 9.12   ? 197 LEU A CA  1 
ATOM   1596 C  C   . LEU A 1 197 ? 18.983  2.981   19.892  1.00 8.76   ? 197 LEU A C   1 
ATOM   1597 O  O   . LEU A 1 197 ? 20.020  2.839   20.554  1.00 9.83   ? 197 LEU A O   1 
ATOM   1598 C  CB  . LEU A 1 197 ? 19.095  5.313   18.897  1.00 10.07  ? 197 LEU A CB  1 
ATOM   1599 C  CG  . LEU A 1 197 ? 18.537  6.736   18.835  1.00 12.69  ? 197 LEU A CG  1 
ATOM   1600 C  CD1 . LEU A 1 197 ? 19.451  7.551   17.931  1.00 15.80  ? 197 LEU A CD1 1 
ATOM   1601 C  CD2 . LEU A 1 197 ? 17.118  6.776   18.263  1.00 15.85  ? 197 LEU A CD2 1 
ATOM   1602 N  N   . THR A 1 198 ? 18.533  2.048   19.016  1.00 8.84   ? 198 THR A N   1 
ATOM   1603 C  CA  . THR A 1 198 ? 19.173  0.742   18.992  1.00 8.95   ? 198 THR A CA  1 
ATOM   1604 C  C   . THR A 1 198 ? 20.209  0.630   17.874  1.00 9.55   ? 198 THR A C   1 
ATOM   1605 O  O   . THR A 1 198 ? 20.809  -0.446  17.713  1.00 10.31  ? 198 THR A O   1 
ATOM   1606 C  CB  . THR A 1 198 ? 18.167  -0.395  18.865  1.00 8.61   ? 198 THR A CB  1 
ATOM   1607 O  OG1 . THR A 1 198 ? 17.600  -0.275  17.547  1.00 8.47   ? 198 THR A OG1 1 
ATOM   1608 C  CG2 . THR A 1 198 ? 17.118  -0.387  19.953  1.00 8.94   ? 198 THR A CG2 1 
ATOM   1609 N  N   . THR A 1 199 ? 20.392  1.705   17.071  1.00 11.53  ? 199 THR A N   1 
ATOM   1610 C  CA  . THR A 1 199 ? 21.476  1.720   16.106  1.00 12.91  ? 199 THR A CA  1 
ATOM   1611 C  C   . THR A 1 199 ? 22.335  2.927   16.431  1.00 12.79  ? 199 THR A C   1 
ATOM   1612 O  O   . THR A 1 199 ? 21.866  3.899   17.059  1.00 12.99  ? 199 THR A O   1 
ATOM   1613 C  CB  . THR A 1 199 ? 20.949  1.992   14.690  1.00 14.83  ? 199 THR A CB  1 
ATOM   1614 O  OG1 . THR A 1 199 ? 20.299  3.258   14.582  1.00 21.73  ? 199 THR A OG1 1 
ATOM   1615 C  CG2 . THR A 1 199 ? 20.004  0.913   14.220  1.00 14.01  ? 199 THR A CG2 1 
ATOM   1616 N  N   . PRO A 1 200 ? 23.587  2.970   15.951  1.00 13.04  ? 200 PRO A N   1 
ATOM   1617 C  CA  . PRO A 1 200 ? 24.370  4.205   16.080  1.00 14.05  ? 200 PRO A CA  1 
ATOM   1618 C  C   . PRO A 1 200 ? 23.519  5.365   15.574  1.00 14.02  ? 200 PRO A C   1 
ATOM   1619 O  O   . PRO A 1 200 ? 22.792  5.251   14.579  1.00 15.81  ? 200 PRO A O   1 
ATOM   1620 C  CB  . PRO A 1 200 ? 25.539  3.895   15.134  1.00 15.09  ? 200 PRO A CB  1 
ATOM   1621 C  CG  . PRO A 1 200 ? 25.761  2.415   15.344  1.00 15.03  ? 200 PRO A CG  1 
ATOM   1622 C  CD  . PRO A 1 200 ? 24.338  1.864   15.304  1.00 15.37  ? 200 PRO A CD  1 
ATOM   1623 N  N   . PRO A 1 201 ? 23.549  6.538   16.229  1.00 13.25  ? 201 PRO A N   1 
ATOM   1624 C  CA  . PRO A 1 201 ? 24.536  6.871   17.281  1.00 13.56  ? 201 PRO A CA  1 
ATOM   1625 C  C   . PRO A 1 201 ? 24.177  6.422   18.707  1.00 12.71  ? 201 PRO A C   1 
ATOM   1626 O  O   . PRO A 1 201 ? 24.858  6.803   19.640  1.00 13.69  ? 201 PRO A O   1 
ATOM   1627 C  CB  . PRO A 1 201 ? 24.563  8.399   17.193  1.00 15.29  ? 201 PRO A CB  1 
ATOM   1628 C  CG  . PRO A 1 201 ? 23.163  8.765   16.753  1.00 17.11  ? 201 PRO A CG  1 
ATOM   1629 C  CD  . PRO A 1 201 ? 22.745  7.695   15.768  1.00 14.82  ? 201 PRO A CD  1 
ATOM   1630 N  N   . LEU A 1 202 ? 23.094  5.648   18.870  1.00 11.65  ? 202 LEU A N   1 
ATOM   1631 C  CA  . LEU A 1 202 ? 22.798  4.986   20.143  1.00 11.89  ? 202 LEU A CA  1 
ATOM   1632 C  C   . LEU A 1 202 ? 22.462  6.015   21.229  1.00 11.13  ? 202 LEU A C   1 
ATOM   1633 O  O   . LEU A 1 202 ? 22.491  5.731   22.419  1.00 11.29  ? 202 LEU A O   1 
ATOM   1634 C  CB  . LEU A 1 202 ? 23.974  4.113   20.628  1.00 11.46  ? 202 LEU A CB  1 
ATOM   1635 C  CG  . LEU A 1 202 ? 24.298  2.946   19.653  1.00 11.44  ? 202 LEU A CG  1 
ATOM   1636 C  CD1 . LEU A 1 202 ? 25.588  2.288   20.094  1.00 13.33  ? 202 LEU A CD1 1 
ATOM   1637 C  CD2 . LEU A 1 202 ? 23.180  1.897   19.561  1.00 13.94  ? 202 LEU A CD2 1 
ATOM   1638 N  N   . THR A 1 203 ? 21.972  7.164   20.803  1.00 12.19  ? 203 THR A N   1 
ATOM   1639 C  CA  . THR A 1 203 ? 21.657  8.268   21.707  1.00 12.46  ? 203 THR A CA  1 
ATOM   1640 C  C   . THR A 1 203 ? 20.586  7.855   22.729  1.00 11.32  ? 203 THR A C   1 
ATOM   1641 O  O   . THR A 1 203 ? 19.575  7.214   22.387  1.00 11.17  ? 203 THR A O   1 
ATOM   1642 C  CB  . THR A 1 203 ? 21.121  9.457   20.888  1.00 15.72  ? 203 THR A CB  1 
ATOM   1643 O  OG1 . THR A 1 203 ? 22.044  9.665   19.813  1.00 18.62  ? 203 THR A OG1 1 
ATOM   1644 C  CG2 . THR A 1 203 ? 20.996  10.702  21.730  1.00 17.58  ? 203 THR A CG2 1 
ATOM   1645 N  N   . GLU A 1 204 ? 20.733  8.320   23.958  1.00 12.85  ? 204 GLU A N   1 
ATOM   1646 C  CA  . GLU A 1 204 ? 19.848  7.946   25.042  1.00 12.40  ? 204 GLU A CA  1 
ATOM   1647 C  C   . GLU A 1 204 ? 18.683  8.929   25.123  1.00 12.02  ? 204 GLU A C   1 
ATOM   1648 O  O   . GLU A 1 204 ? 18.553  9.664   26.119  1.00 14.36  ? 204 GLU A O   1 
ATOM   1649 C  CB  . GLU A 1 204 ? 20.644  7.778   26.347  1.00 13.35  ? 204 GLU A CB  1 
ATOM   1650 C  CG  . GLU A 1 204 ? 21.593  6.596   26.200  1.00 13.25  ? 204 GLU A CG  1 
ATOM   1651 C  CD  . GLU A 1 204 ? 22.460  6.334   27.429  1.00 15.20  ? 204 GLU A CD  1 
ATOM   1652 O  OE1 . GLU A 1 204 ? 22.700  7.253   28.257  1.00 19.17  ? 204 GLU A OE1 1 
ATOM   1653 O  OE2 . GLU A 1 204 ? 22.886  5.169   27.614  1.00 13.64  ? 204 GLU A OE2 1 
ATOM   1654 N  N   . CYS A 1 205 ? 17.825  8.906   24.120  1.00 9.87   ? 205 CYS A N   1 
ATOM   1655 C  CA  . CYS A 1 205 ? 16.803  9.908   23.953  1.00 10.33  ? 205 CYS A CA  1 
ATOM   1656 C  C   . CYS A 1 205 ? 15.424  9.302   23.807  1.00 9.53   ? 205 CYS A C   1 
ATOM   1657 O  O   . CYS A 1 205 ? 14.495  9.996   23.412  1.00 10.40  ? 205 CYS A O   1 
ATOM   1658 C  CB  . CYS A 1 205 ? 17.066  10.760  22.710  1.00 10.76  ? 205 CYS A CB  1 
ATOM   1659 S  SG  . CYS A 1 205 ? 17.194  9.817   21.178  1.00 12.66  ? 205 CYS A SG  1 
ATOM   1660 N  N   . VAL A 1 206 ? 15.274  7.997   24.127  1.00 9.99   ? 206 VAL A N   1 
ATOM   1661 C  CA  . VAL A 1 206 ? 14.039  7.267   23.782  1.00 8.84   ? 206 VAL A CA  1 
ATOM   1662 C  C   . VAL A 1 206 ? 13.268  6.830   25.011  1.00 8.86   ? 206 VAL A C   1 
ATOM   1663 O  O   . VAL A 1 206 ? 13.824  6.159   25.892  1.00 10.76  ? 206 VAL A O   1 
ATOM   1664 C  CB  . VAL A 1 206 ? 14.312  6.031   22.922  1.00 8.84   ? 206 VAL A CB  1 
ATOM   1665 C  CG1 . VAL A 1 206 ? 12.983  5.359   22.572  1.00 9.99   ? 206 VAL A CG1 1 
ATOM   1666 C  CG2 . VAL A 1 206 ? 15.060  6.411   21.613  1.00 11.67  ? 206 VAL A CG2 1 
ATOM   1667 N  N   . THR A 1 207 ? 11.958  7.150   25.054  1.00 8.44   ? 207 THR A N   1 
ATOM   1668 C  CA  . THR A 1 207 ? 11.033  6.427   25.926  1.00 9.22   ? 207 THR A CA  1 
ATOM   1669 C  C   . THR A 1 207 ? 10.452  5.266   25.104  1.00 8.50   ? 207 THR A C   1 
ATOM   1670 O  O   . THR A 1 207 ? 9.812   5.490   24.067  1.00 9.57   ? 207 THR A O   1 
ATOM   1671 C  CB  . THR A 1 207 ? 9.839   7.286   26.360  1.00 9.46   ? 207 THR A CB  1 
ATOM   1672 O  OG1 . THR A 1 207 ? 10.372  8.421   27.069  1.00 11.11  ? 207 THR A OG1 1 
ATOM   1673 C  CG2 . THR A 1 207 ? 8.931   6.508   27.273  1.00 11.45  ? 207 THR A CG2 1 
ATOM   1674 N  N   . TRP A 1 208 ? 10.800  4.055   25.534  1.00 8.47   ? 208 TRP A N   1 
ATOM   1675 C  CA  . TRP A 1 208 ? 10.347  2.869   24.822  1.00 8.11   ? 208 TRP A CA  1 
ATOM   1676 C  C   . TRP A 1 208 ? 8.973   2.448   25.341  1.00 7.99   ? 208 TRP A C   1 
ATOM   1677 O  O   . TRP A 1 208 ? 8.764   2.394   26.554  1.00 9.03   ? 208 TRP A O   1 
ATOM   1678 C  CB  . TRP A 1 208 ? 11.344  1.707   25.029  1.00 8.09   ? 208 TRP A CB  1 
ATOM   1679 C  CG  . TRP A 1 208 ? 12.468  1.802   24.059  1.00 7.38   ? 208 TRP A CG  1 
ATOM   1680 C  CD1 . TRP A 1 208 ? 13.694  2.406   24.241  1.00 8.83   ? 208 TRP A CD1 1 
ATOM   1681 C  CD2 . TRP A 1 208 ? 12.404  1.412   22.677  1.00 8.43   ? 208 TRP A CD2 1 
ATOM   1682 N  NE1 . TRP A 1 208 ? 14.381  2.359   23.075  1.00 9.29   ? 208 TRP A NE1 1 
ATOM   1683 C  CE2 . TRP A 1 208 ? 13.615  1.797   22.084  1.00 8.34   ? 208 TRP A CE2 1 
ATOM   1684 C  CE3 . TRP A 1 208 ? 11.431  0.756   21.911  1.00 8.62   ? 208 TRP A CE3 1 
ATOM   1685 C  CZ2 . TRP A 1 208 ? 13.889  1.533   20.757  1.00 8.90   ? 208 TRP A CZ2 1 
ATOM   1686 C  CZ3 . TRP A 1 208 ? 11.693  0.511   20.580  1.00 8.80   ? 208 TRP A CZ3 1 
ATOM   1687 C  CH2 . TRP A 1 208 ? 12.908  0.892   20.009  1.00 9.60   ? 208 TRP A CH2 1 
ATOM   1688 N  N   . ILE A 1 209 ? 8.074   2.104   24.426  1.00 7.90   ? 209 ILE A N   1 
ATOM   1689 C  CA  . ILE A 1 209 ? 6.758   1.580   24.779  1.00 8.42   ? 209 ILE A CA  1 
ATOM   1690 C  C   . ILE A 1 209 ? 6.639   0.337   23.904  1.00 8.72   ? 209 ILE A C   1 
ATOM   1691 O  O   . ILE A 1 209 ? 6.553   0.421   22.688  1.00 9.25   ? 209 ILE A O   1 
ATOM   1692 C  CB  . ILE A 1 209 ? 5.681   2.609   24.425  1.00 10.18  ? 209 ILE A CB  1 
ATOM   1693 C  CG1 . ILE A 1 209 ? 5.898   3.876   25.273  1.00 10.93  ? 209 ILE A CG1 1 
ATOM   1694 C  CG2 . ILE A 1 209 ? 4.290   1.998   24.705  1.00 11.51  ? 209 ILE A CG2 1 
ATOM   1695 C  CD1 . ILE A 1 209 ? 5.079   5.052   24.766  1.00 14.40  ? 209 ILE A CD1 1 
ATOM   1696 N  N   . VAL A 1 210 ? 6.679   -0.834  24.549  1.00 8.49   ? 210 VAL A N   1 
ATOM   1697 C  CA  . VAL A 1 210 ? 6.711   -2.125  23.812  1.00 7.66   ? 210 VAL A CA  1 
ATOM   1698 C  C   . VAL A 1 210 ? 5.390   -2.832  24.096  1.00 8.34   ? 210 VAL A C   1 
ATOM   1699 O  O   . VAL A 1 210 ? 5.064   -3.130  25.242  1.00 9.66   ? 210 VAL A O   1 
ATOM   1700 C  CB  . VAL A 1 210 ? 7.918   -2.966  24.252  1.00 8.04   ? 210 VAL A CB  1 
ATOM   1701 C  CG1 . VAL A 1 210 ? 7.867   -4.323  23.502  1.00 9.41   ? 210 VAL A CG1 1 
ATOM   1702 C  CG2 . VAL A 1 210 ? 9.212   -2.232  24.011  1.00 9.50   ? 210 VAL A CG2 1 
ATOM   1703 N  N   . LEU A 1 211 ? 4.624   -3.101  23.027  1.00 9.19   ? 211 LEU A N   1 
ATOM   1704 C  CA  . LEU A 1 211 ? 3.340   -3.747  23.208  1.00 9.52   ? 211 LEU A CA  1 
ATOM   1705 C  C   . LEU A 1 211 ? 3.520   -5.217  23.580  1.00 9.81   ? 211 LEU A C   1 
ATOM   1706 O  O   . LEU A 1 211 ? 4.377   -5.927  23.035  1.00 10.23  ? 211 LEU A O   1 
ATOM   1707 C  CB  . LEU A 1 211 ? 2.540   -3.624  21.900  1.00 10.32  ? 211 LEU A CB  1 
ATOM   1708 C  CG  . LEU A 1 211 ? 2.123   -2.187  21.502  1.00 11.37  ? 211 LEU A CG  1 
ATOM   1709 C  CD1 . LEU A 1 211 ? 1.089   -2.233  20.358  1.00 14.67  ? 211 LEU A CD1 1 
ATOM   1710 C  CD2 . LEU A 1 211 ? 1.628   -1.394  22.678  1.00 13.84  ? 211 LEU A CD2 1 
ATOM   1711 N  N   . LYS A 1 212 ? 2.664   -5.705  24.480  1.00 10.74  ? 212 LYS A N   1 
ATOM   1712 C  CA  . LYS A 1 212 ? 2.767   -7.117  24.867  1.00 11.58  ? 212 LYS A CA  1 
ATOM   1713 C  C   . LYS A 1 212 ? 2.269   -8.055  23.777  1.00 11.67  ? 212 LYS A C   1 
ATOM   1714 O  O   . LYS A 1 212 ? 2.797   -9.136  23.635  1.00 13.57  ? 212 LYS A O   1 
ATOM   1715 C  CB  . LYS A 1 212 ? 1.892   -7.286  26.113  1.00 14.00  ? 212 LYS A CB  1 
ATOM   1716 C  CG  . LYS A 1 212 ? 1.775   -8.727  26.642  1.00 19.52  ? 212 LYS A CG  1 
ATOM   1717 C  CD  . LYS A 1 212 ? 0.856   -8.837  27.903  1.00 31.06  ? 212 LYS A CD  1 
ATOM   1718 C  CE  . LYS A 1 212 ? 0.731   -10.168 28.661  1.00 37.60  ? 212 LYS A CE  1 
ATOM   1719 N  NZ  . LYS A 1 212 ? 1.256   -11.339 27.933  1.00 56.08  ? 212 LYS A NZ  1 
ATOM   1720 N  N   A GLU A 1 213 ? 1.240   -7.661  23.037  0.50 10.05  ? 213 GLU A N   1 
ATOM   1721 N  N   B GLU A 1 213 ? 1.204   -7.690  23.062  0.50 10.11  ? 213 GLU A N   1 
ATOM   1722 C  CA  A GLU A 1 213 ? 0.605   -8.557  22.078  0.50 11.37  ? 213 GLU A CA  1 
ATOM   1723 C  CA  B GLU A 1 213 ? 0.622   -8.605  22.086  0.50 11.43  ? 213 GLU A CA  1 
ATOM   1724 C  C   A GLU A 1 213 ? 1.361   -8.470  20.745  0.50 10.41  ? 213 GLU A C   1 
ATOM   1725 C  C   B GLU A 1 213 ? 1.381   -8.472  20.762  0.50 10.42  ? 213 GLU A C   1 
ATOM   1726 O  O   A GLU A 1 213 ? 1.427   -7.410  20.122  0.50 11.10  ? 213 GLU A O   1 
ATOM   1727 O  O   B GLU A 1 213 ? 1.454   -7.396  20.168  0.50 10.93  ? 213 GLU A O   1 
ATOM   1728 C  CB  A GLU A 1 213 ? -0.849  -8.119  21.877  0.50 11.64  ? 213 GLU A CB  1 
ATOM   1729 C  CB  B GLU A 1 213 ? -0.850  -8.306  21.785  0.50 12.10  ? 213 GLU A CB  1 
ATOM   1730 C  CG  A GLU A 1 213 ? -1.611  -9.040  20.939  0.50 14.89  ? 213 GLU A CG  1 
ATOM   1731 C  CG  B GLU A 1 213 ? -1.442  -9.354  20.837  0.50 13.54  ? 213 GLU A CG  1 
ATOM   1732 C  CD  A GLU A 1 213 ? -3.027  -8.557  20.637  0.50 15.25  ? 213 GLU A CD  1 
ATOM   1733 C  CD  B GLU A 1 213 ? -2.927  -9.198  20.550  0.50 15.17  ? 213 GLU A CD  1 
ATOM   1734 O  OE1 A GLU A 1 213 ? -3.678  -8.015  21.576  0.50 15.02  ? 213 GLU A OE1 1 
ATOM   1735 O  OE1 B GLU A 1 213 ? -3.514  -8.160  20.937  0.50 13.14  ? 213 GLU A OE1 1 
ATOM   1736 O  OE2 A GLU A 1 213 ? -3.480  -8.722  19.468  0.50 16.51  ? 213 GLU A OE2 1 
ATOM   1737 O  OE2 B GLU A 1 213 ? -3.520  -10.116 19.972  0.50 17.48  ? 213 GLU A OE2 1 
ATOM   1738 N  N   . PRO A 1 214 ? 1.988   -9.564  20.251  1.00 10.76  ? 214 PRO A N   1 
ATOM   1739 C  CA  . PRO A 1 214 ? 2.639   -9.508  18.945  1.00 10.28  ? 214 PRO A CA  1 
ATOM   1740 C  C   . PRO A 1 214 ? 1.571   -9.497  17.850  1.00 11.15  ? 214 PRO A C   1 
ATOM   1741 O  O   . PRO A 1 214 ? 0.426   -9.891  18.055  1.00 13.46  ? 214 PRO A O   1 
ATOM   1742 C  CB  . PRO A 1 214 ? 3.395   -10.856 18.861  1.00 12.16  ? 214 PRO A CB  1 
ATOM   1743 C  CG  . PRO A 1 214 ? 2.554   -11.775 19.709  1.00 19.63  ? 214 PRO A CG  1 
ATOM   1744 C  CD  . PRO A 1 214 ? 2.041   -10.906 20.862  1.00 13.12  ? 214 PRO A CD  1 
ATOM   1745 N  N   . ILE A 1 215 ? 1.981   -9.028  16.678  1.00 10.71  ? 215 ILE A N   1 
ATOM   1746 C  CA  . ILE A 1 215 ? 1.168   -9.290  15.490  1.00 11.39  ? 215 ILE A CA  1 
ATOM   1747 C  C   . ILE A 1 215 ? 1.698   -10.533 14.791  1.00 11.44  ? 215 ILE A C   1 
ATOM   1748 O  O   . ILE A 1 215 ? 2.878   -10.885 14.914  1.00 12.60  ? 215 ILE A O   1 
ATOM   1749 C  CB  . ILE A 1 215 ? 1.116   -8.087  14.540  1.00 11.58  ? 215 ILE A CB  1 
ATOM   1750 C  CG1 . ILE A 1 215 ? 2.507   -7.704  14.026  1.00 12.38  ? 215 ILE A CG1 1 
ATOM   1751 C  CG2 . ILE A 1 215 ? 0.391   -6.946  15.249  1.00 12.84  ? 215 ILE A CG2 1 
ATOM   1752 C  CD1 . ILE A 1 215 ? 2.457   -6.691  12.851  1.00 13.95  ? 215 ILE A CD1 1 
ATOM   1753 N  N   A SER A 1 216 ? 0.780   -11.194 14.067  0.50 12.39  ? 216 SER A N   1 
ATOM   1754 N  N   B SER A 1 216 ? 0.793   -11.225 14.112  0.50 12.58  ? 216 SER A N   1 
ATOM   1755 C  CA  A SER A 1 216 ? 1.105   -12.347 13.229  0.50 11.94  ? 216 SER A CA  1 
ATOM   1756 C  CA  B SER A 1 216 ? 1.222   -12.377 13.339  0.50 12.79  ? 216 SER A CA  1 
ATOM   1757 C  C   A SER A 1 216 ? 1.376   -11.884 11.799  0.50 11.47  ? 216 SER A C   1 
ATOM   1758 C  C   B SER A 1 216 ? 1.370   -11.960 11.872  0.50 10.95  ? 216 SER A C   1 
ATOM   1759 O  O   A SER A 1 216 ? 0.588   -11.122 11.222  0.50 12.97  ? 216 SER A O   1 
ATOM   1760 O  O   B SER A 1 216 ? 0.487   -11.266 11.353  0.50 12.59  ? 216 SER A O   1 
ATOM   1761 C  CB  A SER A 1 216 ? 0.004   -13.402 13.234  0.50 13.16  ? 216 SER A CB  1 
ATOM   1762 C  CB  B SER A 1 216 ? 0.208   -13.465 13.503  0.50 17.64  ? 216 SER A CB  1 
ATOM   1763 O  OG  A SER A 1 216 ? -0.043  -13.976 14.526  0.50 14.53  ? 216 SER A OG  1 
ATOM   1764 O  OG  B SER A 1 216 ? 0.470   -14.495 12.598  0.50 21.23  ? 216 SER A OG  1 
ATOM   1765 N  N   . VAL A 1 217 ? 2.484   -12.374 11.232  1.00 12.31  ? 217 VAL A N   1 
ATOM   1766 C  CA  . VAL A 1 217 ? 2.730   -12.169 9.810   1.00 11.35  ? 217 VAL A CA  1 
ATOM   1767 C  C   . VAL A 1 217 ? 2.989   -13.538 9.208   1.00 11.74  ? 217 VAL A C   1 
ATOM   1768 O  O   . VAL A 1 217 ? 3.370   -14.480 9.928   1.00 11.84  ? 217 VAL A O   1 
ATOM   1769 C  CB  . VAL A 1 217 ? 3.925   -11.224 9.582   1.00 12.59  ? 217 VAL A CB  1 
ATOM   1770 C  CG1 . VAL A 1 217 ? 3.688   -9.902  10.305  1.00 13.00  ? 217 VAL A CG1 1 
ATOM   1771 C  CG2 . VAL A 1 217 ? 5.210   -11.854 10.095  1.00 13.71  ? 217 VAL A CG2 1 
ATOM   1772 N  N   . SER A 1 218 ? 2.834   -13.671 7.906   1.00 11.70  ? 218 SER A N   1 
ATOM   1773 C  CA  . SER A 1 218 ? 3.063   -14.988 7.336   1.00 11.76  ? 218 SER A CA  1 
ATOM   1774 C  C   . SER A 1 218 ? 4.535   -15.260 7.078   1.00 12.09  ? 218 SER A C   1 
ATOM   1775 O  O   . SER A 1 218 ? 5.359   -14.335 6.930   1.00 12.22  ? 218 SER A O   1 
ATOM   1776 C  CB  . SER A 1 218 ? 2.273   -15.222 6.109   1.00 12.88  ? 218 SER A CB  1 
ATOM   1777 O  OG  . SER A 1 218 ? 2.717   -14.314 5.110   1.00 13.58  ? 218 SER A OG  1 
ATOM   1778 N  N   . SER A 1 219 ? 4.882   -16.548 6.908   1.00 12.05  ? 219 SER A N   1 
ATOM   1779 C  CA  . SER A 1 219 ? 6.231   -16.913 6.539   1.00 13.05  ? 219 SER A CA  1 
ATOM   1780 C  C   . SER A 1 219 ? 6.601   -16.205 5.228   1.00 12.78  ? 219 SER A C   1 
ATOM   1781 O  O   . SER A 1 219 ? 7.749   -15.734 5.066   1.00 15.20  ? 219 SER A O   1 
ATOM   1782 C  CB  . SER A 1 219 ? 6.406   -18.450 6.478   1.00 17.74  ? 219 SER A CB  1 
ATOM   1783 O  OG  . SER A 1 219 ? 5.458   -19.013 5.578   1.00 21.51  ? 219 SER A OG  1 
ATOM   1784 N  N   . GLU A 1 220 ? 5.647   -16.081 4.277   1.00 13.50  ? 220 GLU A N   1 
ATOM   1785 C  CA  . GLU A 1 220 ? 5.989   -15.468 3.007   1.00 14.85  ? 220 GLU A CA  1 
ATOM   1786 C  C   . GLU A 1 220 ? 6.245   -13.973 3.188   1.00 13.98  ? 220 GLU A C   1 
ATOM   1787 O  O   . GLU A 1 220 ? 7.095   -13.397 2.469   1.00 15.27  ? 220 GLU A O   1 
ATOM   1788 C  CB  . GLU A 1 220 ? 4.839   -15.648 2.026   1.00 16.99  ? 220 GLU A CB  1 
ATOM   1789 C  CG  . GLU A 1 220 ? 4.616   -17.121 1.609   1.00 20.48  ? 220 GLU A CG  1 
ATOM   1790 C  CD  . GLU A 1 220 ? 3.729   -17.921 2.554   1.00 22.82  ? 220 GLU A CD  1 
ATOM   1791 O  OE1 . GLU A 1 220 ? 3.163   -17.392 3.509   1.00 19.01  ? 220 GLU A OE1 1 
ATOM   1792 O  OE2 . GLU A 1 220 ? 3.569   -19.137 2.309   1.00 33.00  ? 220 GLU A OE2 1 
ATOM   1793 N  N   . GLN A 1 221 ? 5.505   -13.306 4.118   1.00 12.84  ? 221 GLN A N   1 
ATOM   1794 C  CA  . GLN A 1 221 ? 5.750   -11.885 4.314   1.00 11.69  ? 221 GLN A CA  1 
ATOM   1795 C  C   . GLN A 1 221 ? 7.174   -11.632 4.845   1.00 12.03  ? 221 GLN A C   1 
ATOM   1796 O  O   . GLN A 1 221 ? 7.901   -10.780 4.344   1.00 11.78  ? 221 GLN A O   1 
ATOM   1797 C  CB  . GLN A 1 221 ? 4.686   -11.335 5.231   1.00 13.11  ? 221 GLN A CB  1 
ATOM   1798 C  CG  . GLN A 1 221 ? 3.347   -11.173 4.532   1.00 12.95  ? 221 GLN A CG  1 
ATOM   1799 C  CD  . GLN A 1 221 ? 2.218   -10.661 5.412   1.00 13.15  ? 221 GLN A CD  1 
ATOM   1800 O  OE1 . GLN A 1 221 ? 2.138   -11.054 6.573   1.00 12.39  ? 221 GLN A OE1 1 
ATOM   1801 N  NE2 . GLN A 1 221 ? 1.374   -9.806  4.845   1.00 13.60  ? 221 GLN A NE2 1 
ATOM   1802 N  N   . VAL A 1 222 ? 7.609   -12.418 5.844   1.00 12.52  ? 222 VAL A N   1 
ATOM   1803 C  CA  . VAL A 1 222 ? 8.931   -12.165 6.418   1.00 12.91  ? 222 VAL A CA  1 
ATOM   1804 C  C   . VAL A 1 222 ? 10.011  -12.636 5.438   1.00 13.73  ? 222 VAL A C   1 
ATOM   1805 O  O   . VAL A 1 222 ? 11.097  -12.043 5.377   1.00 13.80  ? 222 VAL A O   1 
ATOM   1806 C  CB  . VAL A 1 222 ? 9.088   -12.743 7.849   1.00 15.79  ? 222 VAL A CB  1 
ATOM   1807 C  CG1 . VAL A 1 222 ? 9.006   -14.226 7.927   1.00 18.78  ? 222 VAL A CG1 1 
ATOM   1808 C  CG2 . VAL A 1 222 ? 10.345  -12.208 8.551   1.00 19.18  ? 222 VAL A CG2 1 
ATOM   1809 N  N   A LEU A 1 223 ? 9.723   -13.665 4.618   0.50 13.35  ? 223 LEU A N   1 
ATOM   1810 N  N   B LEU A 1 223 ? 9.685   -13.660 4.641   0.50 13.11  ? 223 LEU A N   1 
ATOM   1811 C  CA  A LEU A 1 223 ? 10.743  -14.089 3.667   0.50 17.00  ? 223 LEU A CA  1 
ATOM   1812 C  CA  B LEU A 1 223 ? 10.632  -14.095 3.635   0.50 15.84  ? 223 LEU A CA  1 
ATOM   1813 C  C   A LEU A 1 223 ? 11.023  -12.975 2.661   0.50 14.35  ? 223 LEU A C   1 
ATOM   1814 C  C   B LEU A 1 223 ? 11.020  -12.933 2.740   0.50 13.74  ? 223 LEU A C   1 
ATOM   1815 O  O   A LEU A 1 223 ? 12.159  -12.862 2.181   0.50 14.72  ? 223 LEU A O   1 
ATOM   1816 O  O   B LEU A 1 223 ? 12.202  -12.761 2.419   0.50 14.89  ? 223 LEU A O   1 
ATOM   1817 C  CB  A LEU A 1 223 ? 10.412  -15.455 3.027   0.50 23.64  ? 223 LEU A CB  1 
ATOM   1818 C  CB  B LEU A 1 223 ? 10.049  -15.288 2.869   0.50 15.70  ? 223 LEU A CB  1 
ATOM   1819 C  CG  A LEU A 1 223 ? 9.818   -15.496 1.625   0.50 31.84  ? 223 LEU A CG  1 
ATOM   1820 C  CG  B LEU A 1 223 ? 10.385  -16.573 3.619   0.50 21.34  ? 223 LEU A CG  1 
ATOM   1821 C  CD1 A LEU A 1 223 ? 10.857  -15.176 0.575   0.50 25.88  ? 223 LEU A CD1 1 
ATOM   1822 C  CD1 B LEU A 1 223 ? 9.404   -17.665 3.231   0.50 22.74  ? 223 LEU A CD1 1 
ATOM   1823 C  CD2 A LEU A 1 223 ? 9.250   -16.882 1.353   0.50 36.25  ? 223 LEU A CD2 1 
ATOM   1824 C  CD2 B LEU A 1 223 ? 11.812  -16.966 3.317   0.50 23.82  ? 223 LEU A CD2 1 
ATOM   1825 N  N   . LYS A 1 224 ? 10.035  -12.093 2.389   1.00 13.49  ? 224 LYS A N   1 
ATOM   1826 C  CA  . LYS A 1 224 ? 10.251  -10.967 1.467   1.00 14.76  ? 224 LYS A CA  1 
ATOM   1827 C  C   . LYS A 1 224 ? 11.108  -9.893  2.131   1.00 12.69  ? 224 LYS A C   1 
ATOM   1828 O  O   . LYS A 1 224 ? 11.946  -9.290  1.473   1.00 13.64  ? 224 LYS A O   1 
ATOM   1829 C  CB  . LYS A 1 224 ? 8.902   -10.496 0.899   1.00 17.16  ? 224 LYS A CB  1 
ATOM   1830 C  CG  . LYS A 1 224 ? 8.303   -11.576 -0.032  1.00 20.48  ? 224 LYS A CG  1 
ATOM   1831 C  CD  . LYS A 1 224 ? 7.033   -11.318 -0.762  1.00 26.11  ? 224 LYS A CD  1 
ATOM   1832 C  CE  . LYS A 1 224 ? 6.552   -12.435 -1.700  1.00 31.13  ? 224 LYS A CE  1 
ATOM   1833 N  NZ  . LYS A 1 224 ? 5.308   -12.078 -2.439  1.00 28.95  ? 224 LYS A NZ  1 
ATOM   1834 N  N   . PHE A 1 225 ? 10.996  -9.704  3.456   1.00 11.34  ? 225 PHE A N   1 
ATOM   1835 C  CA  . PHE A 1 225 ? 11.974  -8.845  4.126   1.00 11.14  ? 225 PHE A CA  1 
ATOM   1836 C  C   . PHE A 1 225 ? 13.401  -9.317  3.918   1.00 11.14  ? 225 PHE A C   1 
ATOM   1837 O  O   . PHE A 1 225 ? 14.310  -8.499  3.694   1.00 12.34  ? 225 PHE A O   1 
ATOM   1838 C  CB  . PHE A 1 225 ? 11.777  -8.808  5.651   1.00 11.68  ? 225 PHE A CB  1 
ATOM   1839 C  CG  . PHE A 1 225 ? 10.524  -8.144  6.230   1.00 11.99  ? 225 PHE A CG  1 
ATOM   1840 C  CD1 . PHE A 1 225 ? 9.483   -7.638  5.444   1.00 13.28  ? 225 PHE A CD1 1 
ATOM   1841 C  CD2 . PHE A 1 225 ? 10.467  -7.891  7.611   1.00 12.91  ? 225 PHE A CD2 1 
ATOM   1842 C  CE1 . PHE A 1 225 ? 8.405   -6.988  6.035   1.00 14.78  ? 225 PHE A CE1 1 
ATOM   1843 C  CE2 . PHE A 1 225 ? 9.374   -7.290  8.203   1.00 14.17  ? 225 PHE A CE2 1 
ATOM   1844 C  CZ  . PHE A 1 225 ? 8.377   -6.794  7.402   1.00 13.65  ? 225 PHE A CZ  1 
ATOM   1845 N  N   . ARG A 1 226 ? 13.610  -10.653 3.940   1.00 11.49  ? 226 ARG A N   1 
ATOM   1846 C  CA  . ARG A 1 226 ? 14.959  -11.234 3.880   1.00 12.16  ? 226 ARG A CA  1 
ATOM   1847 C  C   . ARG A 1 226 ? 15.509  -11.247 2.459   1.00 12.29  ? 226 ARG A C   1 
ATOM   1848 O  O   . ARG A 1 226 ? 16.679  -11.619 2.307   1.00 14.84  ? 226 ARG A O   1 
ATOM   1849 C  CB  . ARG A 1 226 ? 14.882  -12.682 4.401   1.00 13.69  ? 226 ARG A CB  1 
ATOM   1850 C  CG  . ARG A 1 226 ? 14.422  -12.785 5.853   1.00 13.06  ? 226 ARG A CG  1 
ATOM   1851 C  CD  . ARG A 1 226 ? 14.497  -14.220 6.293   1.00 14.85  ? 226 ARG A CD  1 
ATOM   1852 N  NE  . ARG A 1 226 ? 13.910  -14.412 7.619   1.00 13.91  ? 226 ARG A NE  1 
ATOM   1853 C  CZ  . ARG A 1 226 ? 12.960  -15.299 7.917   1.00 13.41  ? 226 ARG A CZ  1 
ATOM   1854 N  NH1 . ARG A 1 226 ? 12.476  -16.091 6.976   1.00 17.82  ? 226 ARG A NH1 1 
ATOM   1855 N  NH2 . ARG A 1 226 ? 12.501  -15.387 9.153   1.00 14.06  ? 226 ARG A NH2 1 
ATOM   1856 N  N   . LYS A 1 227 ? 14.731  -10.783 1.448   1.00 12.66  ? 227 LYS A N   1 
ATOM   1857 C  CA  . LYS A 1 227 ? 15.283  -10.639 0.100   1.00 14.35  ? 227 LYS A CA  1 
ATOM   1858 C  C   . LYS A 1 227 ? 15.870  -9.249  -0.148  1.00 13.83  ? 227 LYS A C   1 
ATOM   1859 O  O   . LYS A 1 227 ? 16.496  -9.022  -1.166  1.00 16.51  ? 227 LYS A O   1 
ATOM   1860 C  CB  . LYS A 1 227 ? 14.188  -10.917 -0.915  1.00 15.85  ? 227 LYS A CB  1 
ATOM   1861 C  CG  . LYS A 1 227 ? 13.744  -12.364 -0.893  1.00 19.78  ? 227 LYS A CG  1 
ATOM   1862 C  CD  . LYS A 1 227 ? 12.617  -12.660 -1.947  1.00 31.24  ? 227 LYS A CD  1 
ATOM   1863 C  CE  . LYS A 1 227 ? 13.056  -12.648 -3.397  1.00 41.26  ? 227 LYS A CE  1 
ATOM   1864 N  NZ  . LYS A 1 227 ? 11.920  -12.909 -4.317  1.00 60.67  ? 227 LYS A NZ  1 
ATOM   1865 N  N   . LEU A 1 228 ? 15.641  -8.299  0.779   1.00 13.49  ? 228 LEU A N   1 
ATOM   1866 C  CA  . LEU A 1 228 ? 16.275  -7.012  0.691   1.00 12.77  ? 228 LEU A CA  1 
ATOM   1867 C  C   . LEU A 1 228 ? 17.779  -7.208  0.796   1.00 13.88  ? 228 LEU A C   1 
ATOM   1868 O  O   . LEU A 1 228 ? 18.289  -8.260  1.241   1.00 13.78  ? 228 LEU A O   1 
ATOM   1869 C  CB  . LEU A 1 228 ? 15.768  -6.106  1.802   1.00 13.23  ? 228 LEU A CB  1 
ATOM   1870 C  CG  . LEU A 1 228 ? 14.349  -5.602  1.644   1.00 13.63  ? 228 LEU A CG  1 
ATOM   1871 C  CD1 . LEU A 1 228 ? 13.909  -4.993  2.949   1.00 14.28  ? 228 LEU A CD1 1 
ATOM   1872 C  CD2 . LEU A 1 228 ? 14.289  -4.573  0.503   1.00 15.12  ? 228 LEU A CD2 1 
ATOM   1873 N  N   . ASN A 1 229 ? 18.502  -6.143  0.428   1.00 13.37  ? 229 ASN A N   1 
ATOM   1874 C  CA  . ASN A 1 229 ? 19.953  -6.177  0.436   1.00 13.03  ? 229 ASN A CA  1 
ATOM   1875 C  C   . ASN A 1 229 ? 20.519  -5.026  1.266   1.00 14.42  ? 229 ASN A C   1 
ATOM   1876 O  O   . ASN A 1 229 ? 20.022  -3.890  1.180   1.00 14.79  ? 229 ASN A O   1 
ATOM   1877 C  CB  . ASN A 1 229 ? 20.503  -5.929  -0.972  1.00 16.15  ? 229 ASN A CB  1 
ATOM   1878 C  CG  . ASN A 1 229 ? 20.470  -7.099  -1.923  1.00 16.97  ? 229 ASN A CG  1 
ATOM   1879 O  OD1 . ASN A 1 229 ? 20.999  -6.978  -3.033  1.00 20.56  ? 229 ASN A OD1 1 
ATOM   1880 N  ND2 . ASN A 1 229 ? 19.849  -8.208  -1.554  1.00 17.14  ? 229 ASN A ND2 1 
ATOM   1881 N  N   . PHE A 1 230 ? 21.583  -5.329  2.028   1.00 12.66  ? 230 PHE A N   1 
ATOM   1882 C  CA  . PHE A 1 230 ? 22.307  -4.263  2.709   1.00 12.82  ? 230 PHE A CA  1 
ATOM   1883 C  C   . PHE A 1 230 ? 23.163  -3.451  1.766   1.00 15.37  ? 230 PHE A C   1 
ATOM   1884 O  O   . PHE A 1 230 ? 23.376  -2.262  1.969   1.00 16.87  ? 230 PHE A O   1 
ATOM   1885 C  CB  . PHE A 1 230 ? 23.307  -4.878  3.675   1.00 13.74  ? 230 PHE A CB  1 
ATOM   1886 C  CG  . PHE A 1 230 ? 22.793  -5.449  4.995   1.00 13.97  ? 230 PHE A CG  1 
ATOM   1887 C  CD1 . PHE A 1 230 ? 22.067  -4.689  5.892   1.00 14.09  ? 230 PHE A CD1 1 
ATOM   1888 C  CD2 . PHE A 1 230 ? 23.087  -6.782  5.333   1.00 13.85  ? 230 PHE A CD2 1 
ATOM   1889 C  CE1 . PHE A 1 230 ? 21.653  -5.237  7.104   1.00 14.99  ? 230 PHE A CE1 1 
ATOM   1890 C  CE2 . PHE A 1 230 ? 22.682  -7.342  6.545   1.00 14.95  ? 230 PHE A CE2 1 
ATOM   1891 C  CZ  . PHE A 1 230 ? 21.983  -6.555  7.440   1.00 13.59  ? 230 PHE A CZ  1 
ATOM   1892 N  N   . ASN A 1 231 ? 23.638  -4.077  0.710   1.00 13.66  ? 231 ASN A N   1 
ATOM   1893 C  CA  . ASN A 1 231 ? 24.483  -3.447  -0.314  1.00 14.16  ? 231 ASN A CA  1 
ATOM   1894 C  C   . ASN A 1 231 ? 23.688  -2.536  -1.239  1.00 14.90  ? 231 ASN A C   1 
ATOM   1895 O  O   . ASN A 1 231 ? 22.478  -2.623  -1.399  1.00 15.75  ? 231 ASN A O   1 
ATOM   1896 C  CB  . ASN A 1 231 ? 25.187  -4.525  -1.133  1.00 15.09  ? 231 ASN A CB  1 
ATOM   1897 C  CG  . ASN A 1 231 ? 24.134  -5.424  -1.727  1.00 14.34  ? 231 ASN A CG  1 
ATOM   1898 O  OD1 . ASN A 1 231 ? 23.652  -6.342  -1.066  1.00 16.42  ? 231 ASN A OD1 1 
ATOM   1899 N  ND2 . ASN A 1 231 ? 23.841  -5.215  -3.008  1.00 16.72  ? 231 ASN A ND2 1 
ATOM   1900 N  N   . GLY A 1 232 ? 24.440  -1.619  -1.892  1.00 15.18  ? 232 GLY A N   1 
ATOM   1901 C  CA  . GLY A 1 232 ? 23.948  -0.815  -3.004  1.00 14.86  ? 232 GLY A CA  1 
ATOM   1902 C  C   . GLY A 1 232 ? 23.837  -1.639  -4.263  1.00 15.28  ? 232 GLY A C   1 
ATOM   1903 O  O   . GLY A 1 232 ? 24.541  -2.661  -4.407  1.00 16.01  ? 232 GLY A O   1 
ATOM   1904 N  N   . GLU A 1 233 ? 23.077  -1.109  -5.223  1.00 15.49  ? 233 GLU A N   1 
ATOM   1905 C  CA  . GLU A 1 233 ? 23.049  -1.653  -6.577  1.00 15.03  ? 233 GLU A CA  1 
ATOM   1906 C  C   . GLU A 1 233 ? 24.456  -1.769  -7.147  1.00 16.84  ? 233 GLU A C   1 
ATOM   1907 O  O   . GLU A 1 233 ? 25.280  -0.891  -7.013  1.00 18.11  ? 233 GLU A O   1 
ATOM   1908 C  CB  . GLU A 1 233 ? 22.170  -0.761  -7.457  1.00 16.39  ? 233 GLU A CB  1 
ATOM   1909 C  CG  . GLU A 1 233 ? 21.868  -1.350  -8.851  1.00 17.79  ? 233 GLU A CG  1 
ATOM   1910 C  CD  . GLU A 1 233 ? 21.015  -0.440  -9.699  1.00 24.88  ? 233 GLU A CD  1 
ATOM   1911 O  OE1 . GLU A 1 233 ? 20.767  0.749   -9.276  1.00 26.04  ? 233 GLU A OE1 1 
ATOM   1912 O  OE2 . GLU A 1 233 ? 20.724  -0.863  -10.809 1.00 29.67  ? 233 GLU A OE2 1 
ATOM   1913 N  N   . GLY A 1 234 ? 24.710  -2.896  -7.771  1.00 22.28  ? 234 GLY A N   1 
ATOM   1914 C  CA  . GLY A 1 234 ? 25.978  -3.051  -8.481  1.00 22.84  ? 234 GLY A CA  1 
ATOM   1915 C  C   . GLY A 1 234 ? 27.129  -3.449  -7.557  1.00 21.17  ? 234 GLY A C   1 
ATOM   1916 O  O   . GLY A 1 234 ? 28.296  -3.441  -7.972  1.00 30.59  ? 234 GLY A O   1 
ATOM   1917 N  N   . GLU A 1 235 ? 26.802  -3.785  -6.279  1.00 20.02  ? 235 GLU A N   1 
ATOM   1918 C  CA  . GLU A 1 235 ? 27.802  -4.288  -5.342  1.00 19.34  ? 235 GLU A CA  1 
ATOM   1919 C  C   . GLU A 1 235 ? 27.421  -5.723  -5.018  1.00 21.39  ? 235 GLU A C   1 
ATOM   1920 O  O   . GLU A 1 235 ? 26.274  -6.168  -5.273  1.00 23.01  ? 235 GLU A O   1 
ATOM   1921 C  CB  . GLU A 1 235 ? 27.754  -3.517  -4.005  1.00 20.07  ? 235 GLU A CB  1 
ATOM   1922 C  CG  . GLU A 1 235 ? 28.024  -2.037  -4.162  1.00 20.33  ? 235 GLU A CG  1 
ATOM   1923 C  CD  . GLU A 1 235 ? 27.790  -1.175  -2.943  1.00 31.71  ? 235 GLU A CD  1 
ATOM   1924 O  OE1 . GLU A 1 235 ? 27.222  -1.655  -1.948  1.00 25.58  ? 235 GLU A OE1 1 
ATOM   1925 O  OE2 . GLU A 1 235 ? 28.233  -0.024  -2.960  1.00 40.38  ? 235 GLU A OE2 1 
ATOM   1926 N  N   . PRO A 1 236 ? 28.366  -6.514  -4.475  1.00 19.00  ? 236 PRO A N   1 
ATOM   1927 C  CA  . PRO A 1 236 ? 28.090  -7.899  -4.170  1.00 19.62  ? 236 PRO A CA  1 
ATOM   1928 C  C   . PRO A 1 236 ? 26.904  -7.989  -3.207  1.00 17.64  ? 236 PRO A C   1 
ATOM   1929 O  O   . PRO A 1 236 ? 26.713  -7.155  -2.311  1.00 16.84  ? 236 PRO A O   1 
ATOM   1930 C  CB  . PRO A 1 236 ? 29.379  -8.379  -3.513  1.00 21.71  ? 236 PRO A CB  1 
ATOM   1931 C  CG  . PRO A 1 236 ? 30.478  -7.442  -4.043  1.00 22.10  ? 236 PRO A CG  1 
ATOM   1932 C  CD  . PRO A 1 236 ? 29.752  -6.117  -4.136  1.00 22.27  ? 236 PRO A CD  1 
ATOM   1933 N  N   A GLU A 1 237 ? 26.064  -9.003  -3.414  0.50 17.78  ? 237 GLU A N   1 
ATOM   1934 N  N   B GLU A 1 237 ? 26.188  -9.098  -3.331  0.50 18.92  ? 237 GLU A N   1 
ATOM   1935 C  CA  A GLU A 1 237 ? 24.806  -9.117  -2.693  0.50 16.48  ? 237 GLU A CA  1 
ATOM   1936 C  CA  B GLU A 1 237 ? 24.917  -9.256  -2.658  0.50 17.86  ? 237 GLU A CA  1 
ATOM   1937 C  C   A GLU A 1 237 ? 25.040  -9.648  -1.280  0.50 16.54  ? 237 GLU A C   1 
ATOM   1938 C  C   B GLU A 1 237 ? 25.176  -9.640  -1.208  0.50 17.31  ? 237 GLU A C   1 
ATOM   1939 O  O   A GLU A 1 237 ? 25.542  -10.753 -1.109  0.50 16.89  ? 237 GLU A O   1 
ATOM   1940 O  O   B GLU A 1 237 ? 25.866  -10.622 -0.947  0.50 18.49  ? 237 GLU A O   1 
ATOM   1941 C  CB  A GLU A 1 237 ? 23.817  -10.056 -3.398  0.50 18.74  ? 237 GLU A CB  1 
ATOM   1942 C  CB  B GLU A 1 237 ? 24.077  -10.341 -3.342  0.50 19.39  ? 237 GLU A CB  1 
ATOM   1943 C  CG  A GLU A 1 237 ? 22.424  -10.005 -2.745  0.50 17.72  ? 237 GLU A CG  1 
ATOM   1944 C  CG  B GLU A 1 237 ? 22.713  -10.525 -2.656  0.50 23.48  ? 237 GLU A CG  1 
ATOM   1945 C  CD  A GLU A 1 237 ? 21.295  -10.907 -3.224  0.50 19.54  ? 237 GLU A CD  1 
ATOM   1946 C  CD  B GLU A 1 237 ? 21.513  -10.921 -3.511  0.50 24.58  ? 237 GLU A CD  1 
ATOM   1947 O  OE1 A GLU A 1 237 ? 21.515  -12.150 -3.323  0.50 22.58  ? 237 GLU A OE1 1 
ATOM   1948 O  OE1 B GLU A 1 237 ? 21.684  -11.231 -4.703  0.50 26.57  ? 237 GLU A OE1 1 
ATOM   1949 O  OE2 A GLU A 1 237 ? 20.158  -10.369 -3.446  0.50 20.61  ? 237 GLU A OE2 1 
ATOM   1950 O  OE2 B GLU A 1 237 ? 20.378  -10.925 -2.971  0.50 28.54  ? 237 GLU A OE2 1 
ATOM   1951 N  N   . GLU A 1 238 ? 24.549  -8.891  -0.302  1.00 16.87  ? 238 GLU A N   1 
ATOM   1952 C  CA  . GLU A 1 238 ? 24.569  -9.196  1.118   1.00 17.60  ? 238 GLU A CA  1 
ATOM   1953 C  C   . GLU A 1 238 ? 23.124  -9.128  1.599   1.00 13.10  ? 238 GLU A C   1 
ATOM   1954 O  O   . GLU A 1 238 ? 22.560  -8.023  1.657   1.00 16.39  ? 238 GLU A O   1 
ATOM   1955 C  CB  . GLU A 1 238 ? 25.377  -8.163  1.909   1.00 24.97  ? 238 GLU A CB  1 
ATOM   1956 C  CG  . GLU A 1 238 ? 26.889  -8.015  1.650   1.00 26.41  ? 238 GLU A CG  1 
ATOM   1957 C  CD  . GLU A 1 238 ? 27.532  -6.842  2.421   1.00 51.63  ? 238 GLU A CD  1 
ATOM   1958 O  OE1 . GLU A 1 238 ? 27.505  -5.694  1.904   1.00 49.06  ? 238 GLU A OE1 1 
ATOM   1959 O  OE2 . GLU A 1 238 ? 28.033  -7.053  3.559   1.00 66.24  ? 238 GLU A OE2 1 
ATOM   1960 N  N   . LEU A 1 239 ? 22.458  -10.293 1.829   1.00 15.62  ? 239 LEU A N   1 
ATOM   1961 C  CA  . LEU A 1 239 ? 21.056  -10.220 2.202   1.00 13.31  ? 239 LEU A CA  1 
ATOM   1962 C  C   . LEU A 1 239 ? 20.900  -9.444  3.509   1.00 12.54  ? 239 LEU A C   1 
ATOM   1963 O  O   . LEU A 1 239 ? 21.637  -9.646  4.483   1.00 12.80  ? 239 LEU A O   1 
ATOM   1964 C  CB  . LEU A 1 239 ? 20.492  -11.623 2.388   1.00 12.53  ? 239 LEU A CB  1 
ATOM   1965 C  CG  . LEU A 1 239 ? 20.475  -12.453 1.112   1.00 14.94  ? 239 LEU A CG  1 
ATOM   1966 C  CD1 . LEU A 1 239 ? 20.072  -13.892 1.402   1.00 20.78  ? 239 LEU A CD1 1 
ATOM   1967 C  CD2 . LEU A 1 239 ? 19.581  -11.863 0.051   1.00 16.02  ? 239 LEU A CD2 1 
ATOM   1968 N  N   . MET A 1 240 ? 19.837  -8.653  3.539   1.00 12.22  ? 240 MET A N   1 
ATOM   1969 C  CA  . MET A 1 240 ? 19.558  -7.836  4.712   1.00 12.00  ? 240 MET A CA  1 
ATOM   1970 C  C   . MET A 1 240 ? 18.760  -8.741  5.667   1.00 11.42  ? 240 MET A C   1 
ATOM   1971 O  O   . MET A 1 240 ? 17.551  -8.920  5.555   1.00 12.16  ? 240 MET A O   1 
ATOM   1972 C  CB  . MET A 1 240 ? 18.704  -6.643  4.298   1.00 13.16  ? 240 MET A CB  1 
ATOM   1973 C  CG  . MET A 1 240 ? 18.418  -5.637  5.484   1.00 11.76  ? 240 MET A CG  1 
ATOM   1974 S  SD  . MET A 1 240 ? 17.497  -4.231  5.053   1.00 13.53  ? 240 MET A SD  1 
ATOM   1975 C  CE  . MET A 1 240 ? 18.763  -3.230  4.274   1.00 13.76  ? 240 MET A CE  1 
ATOM   1976 N  N   . VAL A 1 241 ? 19.512  -9.340  6.594   1.00 10.33  ? 241 VAL A N   1 
ATOM   1977 C  CA  . VAL A 1 241 ? 18.964  -10.210 7.651   1.00 10.90  ? 241 VAL A CA  1 
ATOM   1978 C  C   . VAL A 1 241 ? 19.729  -9.943  8.932   1.00 10.80  ? 241 VAL A C   1 
ATOM   1979 O  O   . VAL A 1 241 ? 20.895  -9.538  8.864   1.00 11.18  ? 241 VAL A O   1 
ATOM   1980 C  CB  . VAL A 1 241 ? 19.052  -11.710 7.263   1.00 10.86  ? 241 VAL A CB  1 
ATOM   1981 C  CG1 . VAL A 1 241 ? 18.124  -12.020 6.076   1.00 12.30  ? 241 VAL A CG1 1 
ATOM   1982 C  CG2 . VAL A 1 241 ? 20.532  -12.124 7.013   1.00 13.10  ? 241 VAL A CG2 1 
ATOM   1983 N  N   . ASP A 1 242 ? 19.103  -10.244 10.065  1.00 9.97   ? 242 ASP A N   1 
ATOM   1984 C  CA  . ASP A 1 242 ? 19.802  -10.107 11.342  1.00 10.34  ? 242 ASP A CA  1 
ATOM   1985 C  C   . ASP A 1 242 ? 20.278  -8.690  11.598  1.00 9.92   ? 242 ASP A C   1 
ATOM   1986 O  O   . ASP A 1 242 ? 21.399  -8.476  12.080  1.00 11.52  ? 242 ASP A O   1 
ATOM   1987 C  CB  . ASP A 1 242 ? 20.867  -11.172 11.572  1.00 10.71  ? 242 ASP A CB  1 
ATOM   1988 C  CG  . ASP A 1 242 ? 20.266  -12.575 11.633  1.00 11.05  ? 242 ASP A CG  1 
ATOM   1989 O  OD1 . ASP A 1 242 ? 19.205  -12.729 12.292  1.00 10.93  ? 242 ASP A OD1 1 
ATOM   1990 O  OD2 . ASP A 1 242 ? 20.857  -13.485 10.976  1.00 12.79  ? 242 ASP A OD2 1 
ATOM   1991 N  N   . ASN A 1 243 ? 19.409  -7.726  11.301  1.00 9.64   ? 243 ASN A N   1 
ATOM   1992 C  CA  . ASN A 1 243 ? 19.693  -6.296  11.534  1.00 10.07  ? 243 ASN A CA  1 
ATOM   1993 C  C   . ASN A 1 243 ? 19.144  -5.864  12.885  1.00 8.76   ? 243 ASN A C   1 
ATOM   1994 O  O   . ASN A 1 243 ? 18.438  -4.872  12.978  1.00 10.55  ? 243 ASN A O   1 
ATOM   1995 C  CB  . ASN A 1 243 ? 19.190  -5.448  10.369  1.00 10.61  ? 243 ASN A CB  1 
ATOM   1996 C  CG  . ASN A 1 243 ? 17.726  -5.626  10.104  1.00 9.79   ? 243 ASN A CG  1 
ATOM   1997 O  OD1 . ASN A 1 243 ? 17.061  -6.499  10.650  1.00 11.72  ? 243 ASN A OD1 1 
ATOM   1998 N  ND2 . ASN A 1 243 ? 17.188  -4.759  9.265   1.00 13.65  ? 243 ASN A ND2 1 
ATOM   1999 N  N   . TRP A 1 244 ? 19.385  -6.656  13.942  1.00 8.80   ? 244 TRP A N   1 
ATOM   2000 C  CA  . TRP A 1 244 ? 18.929  -6.404  15.293  1.00 8.74   ? 244 TRP A CA  1 
ATOM   2001 C  C   . TRP A 1 244 ? 20.124  -6.313  16.229  1.00 9.90   ? 244 TRP A C   1 
ATOM   2002 O  O   . TRP A 1 244 ? 21.107  -7.036  16.063  1.00 10.08  ? 244 TRP A O   1 
ATOM   2003 C  CB  . TRP A 1 244 ? 17.951  -7.489  15.758  1.00 8.65   ? 244 TRP A CB  1 
ATOM   2004 C  CG  . TRP A 1 244 ? 18.422  -8.898  15.575  1.00 8.82   ? 244 TRP A CG  1 
ATOM   2005 C  CD1 . TRP A 1 244 ? 18.301  -9.631  14.426  1.00 10.01  ? 244 TRP A CD1 1 
ATOM   2006 C  CD2 . TRP A 1 244 ? 19.021  -9.766  16.541  1.00 8.99   ? 244 TRP A CD2 1 
ATOM   2007 N  NE1 . TRP A 1 244 ? 18.818  -10.910 14.597  1.00 9.50   ? 244 TRP A NE1 1 
ATOM   2008 C  CE2 . TRP A 1 244 ? 19.277  -11.016 15.893  1.00 9.51   ? 244 TRP A CE2 1 
ATOM   2009 C  CE3 . TRP A 1 244 ? 19.371  -9.614  17.899  1.00 10.96  ? 244 TRP A CE3 1 
ATOM   2010 C  CZ2 . TRP A 1 244 ? 19.824  -12.113 16.581  1.00 10.82  ? 244 TRP A CZ2 1 
ATOM   2011 C  CZ3 . TRP A 1 244 ? 19.870  -10.710 18.590  1.00 11.67  ? 244 TRP A CZ3 1 
ATOM   2012 C  CH2 . TRP A 1 244 ? 20.149  -11.898 17.897  1.00 12.28  ? 244 TRP A CH2 1 
ATOM   2013 N  N   . ARG A 1 245 ? 20.002  -5.403  17.182  1.00 9.48   ? 245 ARG A N   1 
ATOM   2014 C  CA  . ARG A 1 245 ? 20.971  -5.345  18.286  1.00 8.91   ? 245 ARG A CA  1 
ATOM   2015 C  C   . ARG A 1 245 ? 20.505  -6.276  19.400  1.00 8.97   ? 245 ARG A C   1 
ATOM   2016 O  O   . ARG A 1 245 ? 19.325  -6.256  19.751  1.00 10.07  ? 245 ARG A O   1 
ATOM   2017 C  CB  . ARG A 1 245 ? 21.053  -3.899  18.788  1.00 9.55   ? 245 ARG A CB  1 
ATOM   2018 C  CG  . ARG A 1 245 ? 22.205  -3.683  19.749  1.00 9.76   ? 245 ARG A CG  1 
ATOM   2019 C  CD  . ARG A 1 245 ? 22.123  -2.333  20.444  1.00 10.63  ? 245 ARG A CD  1 
ATOM   2020 N  NE  . ARG A 1 245 ? 23.369  -2.047  21.170  1.00 10.78  ? 245 ARG A NE  1 
ATOM   2021 C  CZ  . ARG A 1 245 ? 23.553  -1.032  22.003  1.00 9.90   ? 245 ARG A CZ  1 
ATOM   2022 N  NH1 . ARG A 1 245 ? 22.537  -0.224  22.367  1.00 11.61  ? 245 ARG A NH1 1 
ATOM   2023 N  NH2 . ARG A 1 245 ? 24.793  -0.798  22.489  1.00 11.98  ? 245 ARG A NH2 1 
ATOM   2024 N  N   . PRO A 1 246 ? 21.417  -7.056  20.012  1.00 10.42  ? 246 PRO A N   1 
ATOM   2025 C  CA  . PRO A 1 246 ? 21.026  -7.881  21.153  1.00 11.00  ? 246 PRO A CA  1 
ATOM   2026 C  C   . PRO A 1 246 ? 20.644  -7.056  22.379  1.00 9.78   ? 246 PRO A C   1 
ATOM   2027 O  O   . PRO A 1 246 ? 20.995  -5.877  22.516  1.00 11.08  ? 246 PRO A O   1 
ATOM   2028 C  CB  . PRO A 1 246 ? 22.255  -8.740  21.465  1.00 15.02  ? 246 PRO A CB  1 
ATOM   2029 C  CG  . PRO A 1 246 ? 23.102  -8.637  20.202  1.00 18.80  ? 246 PRO A CG  1 
ATOM   2030 C  CD  . PRO A 1 246 ? 22.824  -7.266  19.614  1.00 13.06  ? 246 PRO A CD  1 
ATOM   2031 N  N   . ALA A 1 247 ? 19.974  -7.726  23.319  1.00 10.59  ? 247 ALA A N   1 
ATOM   2032 C  CA  . ALA A 1 247 ? 19.613  -7.079  24.592  1.00 9.61   ? 247 ALA A CA  1 
ATOM   2033 C  C   . ALA A 1 247 ? 20.859  -6.565  25.310  1.00 10.12  ? 247 ALA A C   1 
ATOM   2034 O  O   . ALA A 1 247 ? 21.906  -7.245  25.374  1.00 12.21  ? 247 ALA A O   1 
ATOM   2035 C  CB  . ALA A 1 247 ? 18.859  -8.109  25.432  1.00 12.31  ? 247 ALA A CB  1 
ATOM   2036 N  N   . GLN A 1 248 ? 20.697  -5.390  25.908  1.00 9.66   ? 248 GLN A N   1 
ATOM   2037 C  CA  . GLN A 1 248 ? 21.763  -4.695  26.620  1.00 10.44  ? 248 GLN A CA  1 
ATOM   2038 C  C   . GLN A 1 248 ? 21.477  -4.730  28.109  1.00 10.66  ? 248 GLN A C   1 
ATOM   2039 O  O   . GLN A 1 248 ? 20.318  -4.922  28.513  1.00 11.72  ? 248 GLN A O   1 
ATOM   2040 C  CB  . GLN A 1 248 ? 21.857  -3.260  26.133  1.00 11.34  ? 248 GLN A CB  1 
ATOM   2041 C  CG  . GLN A 1 248 ? 22.169  -3.188  24.618  1.00 11.30  ? 248 GLN A CG  1 
ATOM   2042 C  CD  . GLN A 1 248 ? 23.488  -3.874  24.293  1.00 12.54  ? 248 GLN A CD  1 
ATOM   2043 O  OE1 . GLN A 1 248 ? 24.550  -3.613  24.892  1.00 15.35  ? 248 GLN A OE1 1 
ATOM   2044 N  NE2 . GLN A 1 248 ? 23.466  -4.824  23.355  1.00 13.51  ? 248 GLN A NE2 1 
ATOM   2045 N  N   . PRO A 1 249 ? 22.468  -4.454  28.987  1.00 13.71  ? 249 PRO A N   1 
ATOM   2046 C  CA  . PRO A 1 249 ? 22.219  -4.529  30.411  1.00 16.20  ? 249 PRO A CA  1 
ATOM   2047 C  C   . PRO A 1 249 ? 21.198  -3.500  30.898  1.00 12.83  ? 249 PRO A C   1 
ATOM   2048 O  O   . PRO A 1 249 ? 21.211  -2.318  30.504  1.00 13.85  ? 249 PRO A O   1 
ATOM   2049 C  CB  . PRO A 1 249 ? 23.634  -4.197  30.969  1.00 20.13  ? 249 PRO A CB  1 
ATOM   2050 C  CG  . PRO A 1 249 ? 24.593  -4.629  29.953  1.00 20.83  ? 249 PRO A CG  1 
ATOM   2051 C  CD  . PRO A 1 249 ? 23.878  -4.242  28.637  1.00 16.63  ? 249 PRO A CD  1 
ATOM   2052 N  N   . LEU A 1 250 ? 20.276  -3.954  31.739  1.00 14.59  ? 250 LEU A N   1 
ATOM   2053 C  CA  . LEU A 1 250 ? 19.230  -3.089  32.222  1.00 13.41  ? 250 LEU A CA  1 
ATOM   2054 C  C   . LEU A 1 250 ? 19.764  -2.021  33.175  1.00 14.62  ? 250 LEU A C   1 
ATOM   2055 O  O   . LEU A 1 250 ? 19.252  -0.892  33.272  1.00 14.98  ? 250 LEU A O   1 
ATOM   2056 C  CB  . LEU A 1 250 ? 18.187  -3.961  32.919  1.00 15.34  ? 250 LEU A CB  1 
ATOM   2057 C  CG  . LEU A 1 250 ? 16.911  -3.240  33.345  1.00 16.25  ? 250 LEU A CG  1 
ATOM   2058 C  CD1 . LEU A 1 250 ? 16.144  -2.678  32.126  1.00 15.14  ? 250 LEU A CD1 1 
ATOM   2059 C  CD2 . LEU A 1 250 ? 16.025  -4.206  34.170  1.00 19.22  ? 250 LEU A CD2 1 
ATOM   2060 N  N   . LYS A 1 251 ? 20.852  -2.323  33.872  1.00 16.32  ? 251 LYS A N   1 
ATOM   2061 C  CA  . LYS A 1 251 ? 21.491  -1.348  34.760  1.00 16.05  ? 251 LYS A CA  1 
ATOM   2062 C  C   . LYS A 1 251 ? 20.487  -0.847  35.795  1.00 20.82  ? 251 LYS A C   1 
ATOM   2063 O  O   . LYS A 1 251 ? 19.834  -1.675  36.388  1.00 25.97  ? 251 LYS A O   1 
ATOM   2064 C  CB  . LYS A 1 251 ? 22.286  -0.300  33.990  1.00 18.84  ? 251 LYS A CB  1 
ATOM   2065 C  CG  . LYS A 1 251 ? 23.403  -0.963  33.209  1.00 23.97  ? 251 LYS A CG  1 
ATOM   2066 C  CD  . LYS A 1 251 ? 24.396  -0.020  32.665  1.00 28.37  ? 251 LYS A CD  1 
ATOM   2067 C  CE  . LYS A 1 251 ? 25.655  -0.750  32.273  1.00 28.14  ? 251 LYS A CE  1 
ATOM   2068 N  NZ  . LYS A 1 251 ? 26.381  0.066   31.259  1.00 29.01  ? 251 LYS A NZ  1 
ATOM   2069 N  N   . ASN A 1 252 ? 20.437  0.447   36.039  1.00 20.33  ? 252 ASN A N   1 
ATOM   2070 C  CA  . ASN A 1 252 ? 19.607  0.939   37.108  1.00 33.07  ? 252 ASN A CA  1 
ATOM   2071 C  C   . ASN A 1 252 ? 18.272  1.401   36.531  1.00 35.50  ? 252 ASN A C   1 
ATOM   2072 O  O   . ASN A 1 252 ? 17.984  2.621   36.634  1.00 38.85  ? 252 ASN A O   1 
ATOM   2073 C  CB  . ASN A 1 252 ? 20.303  2.116   37.798  1.00 37.90  ? 252 ASN A CB  1 
ATOM   2074 C  CG  . ASN A 1 252 ? 19.497  2.664   38.966  1.00 49.26  ? 252 ASN A CG  1 
ATOM   2075 O  OD1 . ASN A 1 252 ? 18.923  1.881   39.738  1.00 57.45  ? 252 ASN A OD1 1 
ATOM   2076 N  ND2 . ASN A 1 252 ? 19.393  3.994   39.082  1.00 39.55  ? 252 ASN A ND2 1 
ATOM   2077 N  N   . ARG A 1 253 ? 17.551  0.464   35.856  1.00 17.19  ? 253 ARG A N   1 
ATOM   2078 C  CA  . ARG A 1 253 ? 16.269  0.809   35.303  1.00 14.88  ? 253 ARG A CA  1 
ATOM   2079 C  C   . ARG A 1 253 ? 15.180  -0.144  35.753  1.00 15.15  ? 253 ARG A C   1 
ATOM   2080 O  O   . ARG A 1 253 ? 15.456  -1.300  36.010  1.00 20.08  ? 253 ARG A O   1 
ATOM   2081 C  CB  . ARG A 1 253 ? 16.327  0.859   33.777  1.00 13.09  ? 253 ARG A CB  1 
ATOM   2082 C  CG  . ARG A 1 253 ? 17.194  2.018   33.276  1.00 12.90  ? 253 ARG A CG  1 
ATOM   2083 C  CD  . ARG A 1 253 ? 17.270  1.946   31.762  1.00 12.19  ? 253 ARG A CD  1 
ATOM   2084 N  NE  . ARG A 1 253 ? 18.101  0.807   31.313  1.00 12.02  ? 253 ARG A NE  1 
ATOM   2085 C  CZ  . ARG A 1 253 ? 18.375  0.571   30.034  1.00 9.75   ? 253 ARG A CZ  1 
ATOM   2086 N  NH1 . ARG A 1 253 ? 17.759  1.265   29.069  1.00 10.59  ? 253 ARG A NH1 1 
ATOM   2087 N  NH2 . ARG A 1 253 ? 19.204  -0.419  29.733  1.00 10.84  ? 253 ARG A NH2 1 
ATOM   2088 N  N   . GLN A 1 254 ? 13.954  0.346   35.820  1.00 15.05  ? 254 GLN A N   1 
ATOM   2089 C  CA  . GLN A 1 254 ? 12.771  -0.472  36.076  1.00 18.13  ? 254 GLN A CA  1 
ATOM   2090 C  C   . GLN A 1 254 ? 11.900  -0.439  34.833  1.00 15.82  ? 254 GLN A C   1 
ATOM   2091 O  O   . GLN A 1 254 ? 11.711  0.622   34.198  1.00 20.06  ? 254 GLN A O   1 
ATOM   2092 C  CB  . GLN A 1 254 ? 11.974  0.143   37.235  1.00 22.57  ? 254 GLN A CB  1 
ATOM   2093 C  CG  . GLN A 1 254 ? 12.681  -0.074  38.567  1.00 29.61  ? 254 GLN A CG  1 
ATOM   2094 C  CD  . GLN A 1 254 ? 11.659  -0.127  39.679  1.00 47.98  ? 254 GLN A CD  1 
ATOM   2095 O  OE1 . GLN A 1 254 ? 11.410  -1.179  40.278  1.00 66.90  ? 254 GLN A OE1 1 
ATOM   2096 N  NE2 . GLN A 1 254 ? 11.000  0.999   39.907  1.00 47.24  ? 254 GLN A NE2 1 
ATOM   2097 N  N   . ILE A 1 255 ? 11.385  -1.588  34.449  1.00 13.81  ? 255 ILE A N   1 
ATOM   2098 C  CA  . ILE A 1 255 ? 10.444  -1.677  33.364  1.00 12.35  ? 255 ILE A CA  1 
ATOM   2099 C  C   . ILE A 1 255 ? 9.060   -1.693  34.019  1.00 12.81  ? 255 ILE A C   1 
ATOM   2100 O  O   . ILE A 1 255 ? 8.812   -2.435  34.972  1.00 15.41  ? 255 ILE A O   1 
ATOM   2101 C  CB  . ILE A 1 255 ? 10.667  -2.959  32.543  1.00 11.53  ? 255 ILE A CB  1 
ATOM   2102 C  CG1 . ILE A 1 255 ? 12.111  -2.972  31.966  1.00 13.69  ? 255 ILE A CG1 1 
ATOM   2103 C  CG2 . ILE A 1 255 ? 9.568   -3.031  31.452  1.00 14.08  ? 255 ILE A CG2 1 
ATOM   2104 C  CD1 . ILE A 1 255 ? 12.396  -4.203  31.127  1.00 15.18  ? 255 ILE A CD1 1 
ATOM   2105 N  N   . LYS A 1 256 ? 8.181   -0.799  33.561  1.00 12.55  ? 256 LYS A N   1 
ATOM   2106 C  CA  . LYS A 1 256 ? 6.826   -0.703  34.095  1.00 12.48  ? 256 LYS A CA  1 
ATOM   2107 C  C   . LYS A 1 256 ? 5.844   -1.342  33.148  1.00 11.98  ? 256 LYS A C   1 
ATOM   2108 O  O   . LYS A 1 256 ? 6.002   -1.209  31.938  1.00 14.27  ? 256 LYS A O   1 
ATOM   2109 C  CB  . LYS A 1 256 ? 6.529   0.787   34.359  1.00 15.64  ? 256 LYS A CB  1 
ATOM   2110 C  CG  . LYS A 1 256 ? 7.439   1.380   35.440  1.00 22.35  ? 256 LYS A CG  1 
ATOM   2111 C  CD  . LYS A 1 256 ? 7.215   2.824   35.728  1.00 29.11  ? 256 LYS A CD  1 
ATOM   2112 N  N   . ALA A 1 257 ? 4.812   -1.966  33.683  1.00 13.39  ? 257 ALA A N   1 
ATOM   2113 C  CA  . ALA A 1 257 ? 3.736   -2.587  32.917  1.00 13.31  ? 257 ALA A CA  1 
ATOM   2114 C  C   . ALA A 1 257 ? 2.463   -1.762  33.044  1.00 11.79  ? 257 ALA A C   1 
ATOM   2115 O  O   . ALA A 1 257 ? 2.139   -1.293  34.143  1.00 15.34  ? 257 ALA A O   1 
ATOM   2116 C  CB  . ALA A 1 257 ? 3.500   -4.049  33.327  1.00 15.50  ? 257 ALA A CB  1 
ATOM   2117 N  N   . SER A 1 258 ? 1.759   -1.621  31.929  1.00 12.80  ? 258 SER A N   1 
ATOM   2118 C  CA  . SER A 1 258 ? 0.497   -0.865  31.929  1.00 14.51  ? 258 SER A CA  1 
ATOM   2119 C  C   . SER A 1 258 ? -0.679  -1.729  32.378  1.00 15.85  ? 258 SER A C   1 
ATOM   2120 O  O   . SER A 1 258 ? -1.776  -1.186  32.509  1.00 21.36  ? 258 SER A O   1 
ATOM   2121 C  CB  . SER A 1 258 ? 0.195   -0.352  30.538  1.00 14.23  ? 258 SER A CB  1 
ATOM   2122 O  OG  . SER A 1 258 ? -0.254  -1.423  29.723  1.00 14.03  ? 258 SER A OG  1 
ATOM   2123 N  N   . PHE A 1 259 ? -0.404  -3.023  32.529  1.00 16.22  ? 259 PHE A N   1 
ATOM   2124 C  CA  . PHE A 1 259 ? -1.478  -4.003  32.784  1.00 19.17  ? 259 PHE A CA  1 
ATOM   2125 C  C   . PHE A 1 259 ? -1.167  -4.945  33.946  1.00 26.76  ? 259 PHE A C   1 
ATOM   2126 O  O   . PHE A 1 259 ? 0.012   -5.058  34.338  1.00 25.04  ? 259 PHE A O   1 
ATOM   2127 C  CB  . PHE A 1 259 ? -1.615  -4.889  31.541  1.00 19.28  ? 259 PHE A CB  1 
ATOM   2128 C  CG  . PHE A 1 259 ? -0.338  -5.605  31.169  1.00 18.48  ? 259 PHE A CG  1 
ATOM   2129 C  CD1 . PHE A 1 259 ? 0.653   -4.957  30.432  1.00 15.36  ? 259 PHE A CD1 1 
ATOM   2130 C  CD2 . PHE A 1 259 ? -0.124  -6.920  31.575  1.00 23.88  ? 259 PHE A CD2 1 
ATOM   2131 C  CE1 . PHE A 1 259 ? 1.831   -5.622  30.100  1.00 18.13  ? 259 PHE A CE1 1 
ATOM   2132 C  CE2 . PHE A 1 259 ? 1.080   -7.562  31.272  1.00 26.86  ? 259 PHE A CE2 1 
ATOM   2133 C  CZ  . PHE A 1 259 ? 2.041   -6.911  30.518  1.00 21.72  ? 259 PHE A CZ  1 
ATOM   2134 N  N   . LYS A 1 260 ? -2.285  -5.671  34.216  1.00 40.98  ? 260 LYS A N   1 
ATOM   2135 C  CA  . LYS A 1 260 ? -2.745  -6.773  35.126  1.00 55.54  ? 260 LYS A CA  1 
ATOM   2136 C  C   . LYS A 1 260 ? -1.900  -6.872  36.378  1.00 66.57  ? 260 LYS A C   1 
ATOM   2137 O  O   . LYS A 1 260 ? -0.899  -7.622  36.386  1.00 79.66  ? 260 LYS A O   1 
ATOM   2138 C  CB  . LYS A 1 260 ? -2.751  -8.109  34.375  1.00 75.18  ? 260 LYS A CB  1 
ATOM   2139 O  OXT . LYS A 1 260 ? -2.312  -6.208  37.327  1.00 65.15  ? 260 LYS A OXT 1 
HETATM 2140 ZN ZN  . ZN  B 2 .   ? 14.355  0.182   15.331  1.00 9.01   ? 301 ZN  A ZN  1 
HETATM 2141 O  O20 A V13 C 3 .   ? 19.544  7.617   14.048  0.50 29.95  ? 302 V13 A O20 1 
HETATM 2142 O  O20 B V13 C 3 .   ? 16.213  6.421   11.013  0.50 33.61  ? 302 V13 A O20 1 
HETATM 2143 S  S15 A V13 C 3 .   ? 18.090  7.850   14.082  0.50 22.69  ? 302 V13 A S15 1 
HETATM 2144 S  S15 B V13 C 3 .   ? 17.320  6.182   12.028  0.50 31.07  ? 302 V13 A S15 1 
HETATM 2145 O  O19 A V13 C 3 .   ? 17.843  9.212   14.698  0.50 43.38  ? 302 V13 A O19 1 
HETATM 2146 O  O19 B V13 C 3 .   ? 18.422  5.359   11.500  0.50 32.25  ? 302 V13 A O19 1 
HETATM 2147 C  C16 A V13 C 3 .   ? 17.283  7.983   12.471  0.50 27.48  ? 302 V13 A C16 1 
HETATM 2148 C  C16 B V13 C 3 .   ? 18.068  7.825   12.365  0.50 52.73  ? 302 V13 A C16 1 
HETATM 2149 C  C17 A V13 C 3 .   ? 15.822  7.420   12.429  0.50 16.37  ? 302 V13 A C17 1 
HETATM 2150 C  C17 B V13 C 3 .   ? 18.540  8.012   13.796  0.50 62.81  ? 302 V13 A C17 1 
HETATM 2151 O  O18 A V13 C 3 .   ? 14.713  8.357   12.577  0.50 25.89  ? 302 V13 A O18 1 
HETATM 2152 O  O18 B V13 C 3 .   ? 19.687  6.844   13.996  0.50 69.02  ? 302 V13 A O18 1 
HETATM 2153 C  C1  A V13 C 3 .   ? 17.312  6.434   14.879  0.50 17.28  ? 302 V13 A C1  1 
HETATM 2154 C  C1  B V13 C 3 .   ? 16.589  5.248   13.352  0.50 20.61  ? 302 V13 A C1  1 
HETATM 2155 C  C6  A V13 C 3 .   ? 18.060  5.321   15.346  0.50 13.40  ? 302 V13 A C6  1 
HETATM 2156 C  C6  B V13 C 3 .   ? 15.877  5.826   14.394  0.50 17.88  ? 302 V13 A C6  1 
HETATM 2157 F  F11 A V13 C 3 .   ? 19.415  5.346   15.317  0.50 18.23  ? 302 V13 A F11 1 
HETATM 2158 F  F11 B V13 C 3 .   ? 15.543  7.122   14.413  0.50 28.74  ? 302 V13 A F11 1 
HETATM 2159 C  C5  A V13 C 3 .   ? 17.419  4.220   15.901  0.50 13.38  ? 302 V13 A C5  1 
HETATM 2160 C  C5  B V13 C 3 .   ? 15.404  5.010   15.423  0.50 12.42  ? 302 V13 A C5  1 
HETATM 2161 F  F12 A V13 C 3 .   ? 18.215  3.249   16.355  0.50 13.81  ? 302 V13 A F12 1 
HETATM 2162 F  F12 B V13 C 3 .   ? 14.672  5.520   16.431  0.50 11.82  ? 302 V13 A F12 1 
HETATM 2163 C  C4  A V13 C 3 .   ? 16.013  4.097   15.997  0.50 14.22  ? 302 V13 A C4  1 
HETATM 2164 C  C4  B V13 C 3 .   ? 15.711  3.649   15.439  0.50 9.30   ? 302 V13 A C4  1 
HETATM 2165 S  S7  A V13 C 3 .   ? 15.214  2.714   16.830  0.50 9.91   ? 302 V13 A S7  1 
HETATM 2166 S  S7  B V13 C 3 .   ? 15.171  2.662   16.802  0.50 9.26   ? 302 V13 A S7  1 
HETATM 2167 O  O9  A V13 C 3 .   ? 13.789  2.889   16.724  0.50 9.51   ? 302 V13 A O9  1 
HETATM 2168 O  O9  B V13 C 3 .   ? 13.745  2.837   16.789  0.50 10.26  ? 302 V13 A O9  1 
HETATM 2169 N  N10 A V13 C 3 .   ? 15.647  1.307   16.199  0.50 11.11  ? 302 V13 A N10 1 
HETATM 2170 N  N10 B V13 C 3 .   ? 15.590  1.172   16.356  0.50 13.18  ? 302 V13 A N10 1 
HETATM 2171 O  O8  A V13 C 3 .   ? 15.836  2.938   18.110  0.50 11.60  ? 302 V13 A O8  1 
HETATM 2172 O  O8  B V13 C 3 .   ? 15.893  3.045   17.980  0.50 8.67   ? 302 V13 A O8  1 
HETATM 2173 C  C3  A V13 C 3 .   ? 15.298  5.216   15.582  0.50 17.37  ? 302 V13 A C3  1 
HETATM 2174 C  C3  B V13 C 3 .   ? 16.441  3.130   14.351  0.50 13.11  ? 302 V13 A C3  1 
HETATM 2175 F  F13 A V13 C 3 .   ? 13.974  5.238   15.673  0.50 22.07  ? 302 V13 A F13 1 
HETATM 2176 F  F13 B V13 C 3 .   ? 16.799  1.865   14.206  0.50 17.31  ? 302 V13 A F13 1 
HETATM 2177 C  C2  A V13 C 3 .   ? 15.890  6.329   14.980  0.50 19.69  ? 302 V13 A C2  1 
HETATM 2178 C  C2  B V13 C 3 .   ? 16.906  3.944   13.356  0.50 19.04  ? 302 V13 A C2  1 
HETATM 2179 F  F14 A V13 C 3 .   ? 15.013  7.305   14.627  0.50 21.88  ? 302 V13 A F14 1 
HETATM 2180 F  F14 B V13 C 3 .   ? 17.573  3.385   12.341  0.50 25.05  ? 302 V13 A F14 1 
HETATM 2181 N  N1  . BCN D 4 .   ? 0.682   -12.668 23.286  1.00 39.53  ? 303 BCN A N1  1 
HETATM 2182 C  C1  . BCN D 4 .   ? 1.357   -12.237 24.538  1.00 32.88  ? 303 BCN A C1  1 
HETATM 2183 C  C2  . BCN D 4 .   ? 1.245   -13.249 25.695  1.00 52.50  ? 303 BCN A C2  1 
HETATM 2184 O  O21 . BCN D 4 .   ? 0.178   -13.930 25.852  1.00 58.20  ? 303 BCN A O21 1 
HETATM 2185 O  O22 . BCN D 4 .   ? 2.222   -13.297 26.454  1.00 47.98  ? 303 BCN A O22 1 
HETATM 2186 C  C3  . BCN D 4 .   ? 0.872   -14.084 22.936  1.00 49.75  ? 303 BCN A C3  1 
HETATM 2187 C  C4  . BCN D 4 .   ? 1.526   -14.346 21.613  1.00 42.00  ? 303 BCN A C4  1 
HETATM 2188 O  O4  . BCN D 4 .   ? 0.575   -14.629 20.590  1.00 49.93  ? 303 BCN A O4  1 
HETATM 2189 C  C5  . BCN D 4 .   ? -0.603  -11.999 22.976  1.00 32.39  ? 303 BCN A C5  1 
HETATM 2190 C  C6  . BCN D 4 .   ? -1.622  -11.657 24.058  1.00 47.00  ? 303 BCN A C6  1 
HETATM 2191 O  O6  . BCN D 4 .   ? -1.267  -10.503 24.831  1.00 29.80  ? 303 BCN A O6  1 
HETATM 2192 S  S   . DMS E 5 .   ? 22.424  -9.806  14.962  1.00 27.62  ? 304 DMS A S   1 
HETATM 2193 O  O   . DMS E 5 .   ? 23.059  -11.172 14.496  1.00 38.29  ? 304 DMS A O   1 
HETATM 2194 C  C1  . DMS E 5 .   ? 23.594  -8.669  14.325  1.00 34.52  ? 304 DMS A C1  1 
HETATM 2195 C  C2  . DMS E 5 .   ? 22.791  -9.621  16.697  1.00 24.13  ? 304 DMS A C2  1 
HETATM 2196 NA NA  . NA  F 6 .   ? 3.424   21.010  6.086   1.00 25.07  ? 305 NA  A NA  1 
HETATM 2197 O  O   . HOH G 7 .   ? -4.468  -8.798  17.479  1.00 32.74  ? 401 HOH A O   1 
HETATM 2198 O  O   . HOH G 7 .   ? -7.342  8.215   15.668  1.00 55.55  ? 402 HOH A O   1 
HETATM 2199 O  O   . HOH G 7 .   ? 10.120  -13.214 33.964  1.00 28.97  ? 403 HOH A O   1 
HETATM 2200 O  O   . HOH G 7 .   ? 27.543  -0.700  0.083   1.00 39.80  ? 404 HOH A O   1 
HETATM 2201 O  O   . HOH G 7 .   ? 2.345   19.424  18.786  1.00 32.08  ? 405 HOH A O   1 
HETATM 2202 O  O   . HOH G 7 .   ? 33.759  1.535   12.063  1.00 47.16  ? 406 HOH A O   1 
HETATM 2203 O  O   . HOH G 7 .   ? -5.734  -10.791 19.979  1.00 45.58  ? 407 HOH A O   1 
HETATM 2204 O  O   . HOH G 7 .   ? 4.217   -12.122 26.313  1.00 24.46  ? 408 HOH A O   1 
HETATM 2205 O  O   . HOH G 7 .   ? 18.557  -17.049 21.817  1.00 38.19  ? 409 HOH A O   1 
HETATM 2206 O  O   . HOH G 7 .   ? 14.983  -9.644  36.464  1.00 41.36  ? 410 HOH A O   1 
HETATM 2207 O  O   . HOH G 7 .   ? 17.172  5.689   8.927   1.00 51.98  ? 411 HOH A O   1 
HETATM 2208 O  O   . HOH G 7 .   ? -2.944  -1.571  29.371  1.00 30.54  ? 412 HOH A O   1 
HETATM 2209 O  O   . HOH G 7 .   ? -2.762  -12.432 20.124  1.00 48.32  ? 413 HOH A O   1 
HETATM 2210 O  O   . HOH G 7 .   ? 11.603  14.776  10.674  1.00 32.56  ? 414 HOH A O   1 
HETATM 2211 O  O   . HOH G 7 .   ? 20.087  25.691  18.006  1.00 35.55  ? 415 HOH A O   1 
HETATM 2212 O  O   . HOH G 7 .   ? 25.602  -0.746  29.081  1.00 24.84  ? 416 HOH A O   1 
HETATM 2213 O  O   . HOH G 7 .   ? 7.332   -3.196  -6.181  1.00 45.05  ? 417 HOH A O   1 
HETATM 2214 O  O   . HOH G 7 .   ? 5.599   -8.433  37.687  1.00 38.48  ? 418 HOH A O   1 
HETATM 2215 O  O   . HOH G 7 .   ? 24.133  -7.148  26.526  1.00 48.93  ? 419 HOH A O   1 
HETATM 2216 O  O   . HOH G 7 .   ? 0.035   -5.321  -1.837  1.00 35.96  ? 420 HOH A O   1 
HETATM 2217 O  O   . HOH G 7 .   ? -4.699  8.013   27.023  1.00 30.13  ? 421 HOH A O   1 
HETATM 2218 O  O   . HOH G 7 .   ? 23.039  3.464   36.085  1.00 53.39  ? 422 HOH A O   1 
HETATM 2219 O  O   . HOH G 7 .   ? 21.604  -7.720  -5.388  1.00 40.73  ? 423 HOH A O   1 
HETATM 2220 O  O   . HOH G 7 .   ? 6.930   -6.983  -5.311  1.00 39.17  ? 424 HOH A O   1 
HETATM 2221 O  O   . HOH G 7 .   ? 0.749   10.364  30.076  1.00 30.02  ? 425 HOH A O   1 
HETATM 2222 O  O   . HOH G 7 .   ? 8.309   -20.397 8.488   1.00 37.73  ? 426 HOH A O   1 
HETATM 2223 O  O   . HOH G 7 .   ? -1.684  -12.977 16.216  1.00 39.16  ? 427 HOH A O   1 
HETATM 2224 O  O   . HOH G 7 .   ? 25.517  1.048   -5.342  1.00 34.52  ? 428 HOH A O   1 
HETATM 2225 O  O   . HOH G 7 .   ? 6.203   4.479   38.470  1.00 35.51  ? 429 HOH A O   1 
HETATM 2226 O  O   . HOH G 7 .   ? -4.236  11.443  13.254  1.00 32.29  ? 430 HOH A O   1 
HETATM 2227 O  O   . HOH G 7 .   ? 8.541   15.006  31.821  1.00 27.49  ? 431 HOH A O   1 
HETATM 2228 O  O   . HOH G 7 .   ? 4.711   -13.361 32.846  1.00 42.30  ? 432 HOH A O   1 
HETATM 2229 O  O   . HOH G 7 .   ? 8.947   14.318  29.200  1.00 28.23  ? 433 HOH A O   1 
HETATM 2230 O  O   . HOH G 7 .   ? 6.817   -14.715 28.925  1.00 29.45  ? 434 HOH A O   1 
HETATM 2231 O  O   . HOH G 7 .   ? 14.728  -2.767  -6.392  1.00 24.90  ? 435 HOH A O   1 
HETATM 2232 O  O   . HOH G 7 .   ? 19.930  -2.312  15.751  1.00 10.58  ? 436 HOH A O   1 
HETATM 2233 O  O   . HOH G 7 .   ? 23.188  9.759   27.715  1.00 26.23  ? 437 HOH A O   1 
HETATM 2234 O  O   . HOH G 7 .   ? -3.024  10.565  20.344  1.00 24.38  ? 438 HOH A O   1 
HETATM 2235 O  O   . HOH G 7 .   ? 16.384  8.735   9.802   1.00 34.49  ? 439 HOH A O   1 
HETATM 2236 O  O   . HOH G 7 .   ? -6.129  -5.817  26.094  1.00 34.34  ? 440 HOH A O   1 
HETATM 2237 O  O   . HOH G 7 .   ? 7.040   16.735  6.008   1.00 62.37  ? 441 HOH A O   1 
HETATM 2238 O  O   . HOH G 7 .   ? 12.259  2.539   -6.299  1.00 32.64  ? 442 HOH A O   1 
HETATM 2239 O  O   . HOH G 7 .   ? 1.269   -15.097 3.057   1.00 25.21  ? 443 HOH A O   1 
HETATM 2240 O  O   . HOH G 7 .   ? 16.397  -10.152 31.980  1.00 22.59  ? 444 HOH A O   1 
HETATM 2241 O  O   . HOH G 7 .   ? 22.661  -13.911 -1.725  1.00 42.14  ? 445 HOH A O   1 
HETATM 2242 O  O   . HOH G 7 .   ? 10.243  -3.427  38.175  1.00 60.86  ? 446 HOH A O   1 
HETATM 2243 O  O   . HOH G 7 .   ? 12.319  -13.067 33.015  1.00 57.60  ? 447 HOH A O   1 
HETATM 2244 O  O   . HOH G 7 .   ? 10.669  10.530  25.495  1.00 13.37  ? 448 HOH A O   1 
HETATM 2245 O  O   . HOH G 7 .   ? 25.162  -1.405  3.731   1.00 41.06  ? 449 HOH A O   1 
HETATM 2246 O  O   . HOH G 7 .   ? 22.945  -13.842 9.373   1.00 27.35  ? 450 HOH A O   1 
HETATM 2247 O  O   . HOH G 7 .   ? 24.515  -11.062 12.276  1.00 49.57  ? 451 HOH A O   1 
HETATM 2248 O  O   . HOH G 7 .   ? 15.448  18.933  27.275  1.00 50.30  ? 452 HOH A O   1 
HETATM 2249 O  O   . HOH G 7 .   ? 12.188  7.774   28.918  1.00 24.26  ? 453 HOH A O   1 
HETATM 2250 O  O   . HOH G 7 .   ? 24.584  6.773   30.090  1.00 22.00  ? 454 HOH A O   1 
HETATM 2251 O  O   . HOH G 7 .   ? 21.071  0.909   -4.614  1.00 17.13  ? 455 HOH A O   1 
HETATM 2252 O  O   . HOH G 7 .   ? 17.035  22.693  15.403  1.00 36.70  ? 456 HOH A O   1 
HETATM 2253 O  O   . HOH G 7 .   ? 23.540  -11.413 5.123   1.00 21.96  ? 457 HOH A O   1 
HETATM 2254 O  O   . HOH G 7 .   ? 32.783  1.391   16.178  1.00 30.77  ? 458 HOH A O   1 
HETATM 2255 O  O   . HOH G 7 .   ? 22.893  -14.075 -4.574  1.00 29.24  ? 459 HOH A O   1 
HETATM 2256 O  O   . HOH G 7 .   ? 8.859   12.672  5.739   1.00 36.35  ? 460 HOH A O   1 
HETATM 2257 O  O   . HOH G 7 .   ? 20.892  2.823   34.524  1.00 35.31  ? 461 HOH A O   1 
HETATM 2258 O  O   . HOH G 7 .   ? 25.337  -1.699  26.605  1.00 20.07  ? 462 HOH A O   1 
HETATM 2259 O  O   . HOH G 7 .   ? 32.649  -5.464  22.512  1.00 31.64  ? 463 HOH A O   1 
HETATM 2260 O  O   . HOH G 7 .   ? 5.467   5.453   35.125  1.00 38.01  ? 464 HOH A O   1 
HETATM 2261 O  O   . HOH G 7 .   ? 11.272  3.453   38.835  1.00 36.32  ? 465 HOH A O   1 
HETATM 2262 O  O   . HOH G 7 .   ? -4.399  -7.783  15.165  1.00 35.56  ? 466 HOH A O   1 
HETATM 2263 O  O   . HOH G 7 .   ? -6.133  -3.579  27.827  1.00 41.21  ? 467 HOH A O   1 
HETATM 2264 O  O   . HOH G 7 .   ? -5.223  5.602   15.639  1.00 28.47  ? 468 HOH A O   1 
HETATM 2265 O  O   . HOH G 7 .   ? 1.942   -19.050 5.257   1.00 23.75  ? 469 HOH A O   1 
HETATM 2266 O  O   . HOH G 7 .   ? 16.539  -14.049 1.129   1.00 35.11  ? 470 HOH A O   1 
HETATM 2267 O  O   . HOH G 7 .   ? -4.781  -4.228  13.132  1.00 33.58  ? 471 HOH A O   1 
HETATM 2268 O  O   . HOH G 7 .   ? -6.726  8.077   21.648  1.00 35.06  ? 472 HOH A O   1 
HETATM 2269 O  O   . HOH G 7 .   ? 2.536   -10.620 -3.573  1.00 26.42  ? 473 HOH A O   1 
HETATM 2270 O  O   . HOH G 7 .   ? 13.117  -13.595 11.286  1.00 12.99  ? 474 HOH A O   1 
HETATM 2271 O  O   . HOH G 7 .   ? -4.457  0.973   34.966  1.00 37.20  ? 475 HOH A O   1 
HETATM 2272 O  O   . HOH G 7 .   ? 13.376  -3.018  39.908  1.00 33.48  ? 476 HOH A O   1 
HETATM 2273 O  O   . HOH G 7 .   ? -2.059  2.007   34.551  1.00 42.46  ? 477 HOH A O   1 
HETATM 2274 O  O   . HOH G 7 .   ? 14.310  23.026  19.477  1.00 20.68  ? 478 HOH A O   1 
HETATM 2275 O  O   . HOH G 7 .   ? 13.901  -14.886 1.655   1.00 22.93  ? 479 HOH A O   1 
HETATM 2276 O  O   . HOH G 7 .   ? 19.900  0.572   -12.971 1.00 43.91  ? 480 HOH A O   1 
HETATM 2277 O  O   . HOH G 7 .   ? 18.573  -6.940  29.061  1.00 13.07  ? 481 HOH A O   1 
HETATM 2278 O  O   . HOH G 7 .   ? 5.076   -10.427 24.384  1.00 16.14  ? 482 HOH A O   1 
HETATM 2279 O  O   . HOH G 7 .   ? 14.894  3.838   10.681  1.00 33.10  ? 483 HOH A O   1 
HETATM 2280 O  O   . HOH G 7 .   ? 0.993   12.648  26.785  1.00 23.67  ? 484 HOH A O   1 
HETATM 2281 O  O   . HOH G 7 .   ? 19.714  10.803  28.309  1.00 42.17  ? 485 HOH A O   1 
HETATM 2282 O  O   . HOH G 7 .   ? 2.424   -19.224 14.818  1.00 27.10  ? 486 HOH A O   1 
HETATM 2283 O  O   . HOH G 7 .   ? 26.587  8.796   20.338  1.00 19.09  ? 487 HOH A O   1 
HETATM 2284 O  O   . HOH G 7 .   ? 1.791   19.213  5.974   1.00 32.55  ? 488 HOH A O   1 
HETATM 2285 O  O   . HOH G 7 .   ? 18.818  -1.381  11.521  1.00 23.09  ? 489 HOH A O   1 
HETATM 2286 O  O   . HOH G 7 .   ? 3.866   -14.353 22.095  1.00 29.87  ? 490 HOH A O   1 
HETATM 2287 O  O   . HOH G 7 .   ? 7.037   -18.929 3.352   1.00 36.78  ? 491 HOH A O   1 
HETATM 2288 O  O   . HOH G 7 .   ? 28.048  -1.806  30.175  1.00 37.52  ? 492 HOH A O   1 
HETATM 2289 O  O   . HOH G 7 .   ? 9.214   11.124  3.226   1.00 24.51  ? 493 HOH A O   1 
HETATM 2290 O  O   . HOH G 7 .   ? 14.197  -13.086 31.536  1.00 25.70  ? 494 HOH A O   1 
HETATM 2291 O  O   . HOH G 7 .   ? -2.096  -9.348  17.146  1.00 31.09  ? 495 HOH A O   1 
HETATM 2292 O  O   . HOH G 7 .   ? 17.591  -9.290  20.825  1.00 11.38  ? 496 HOH A O   1 
HETATM 2293 O  O   . HOH G 7 .   ? -0.197  9.708   1.965   1.00 18.10  ? 497 HOH A O   1 
HETATM 2294 O  O   . HOH G 7 .   ? 4.086   -6.547  20.383  1.00 10.47  ? 498 HOH A O   1 
HETATM 2295 O  O   . HOH G 7 .   ? 7.375   22.011  15.234  1.00 21.92  ? 499 HOH A O   1 
HETATM 2296 O  O   . HOH G 7 .   ? 16.553  -11.627 17.998  1.00 10.82  ? 500 HOH A O   1 
HETATM 2297 O  O   . HOH G 7 .   ? 16.831  -6.769  31.183  1.00 23.92  ? 501 HOH A O   1 
HETATM 2298 O  O   . HOH G 7 .   ? 7.490   12.279  27.886  1.00 18.40  ? 502 HOH A O   1 
HETATM 2299 O  O   . HOH G 7 .   ? -0.459  -5.342  23.628  1.00 14.84  ? 503 HOH A O   1 
HETATM 2300 O  O   . HOH G 7 .   ? 17.389  -10.961 -2.896  1.00 30.90  ? 504 HOH A O   1 
HETATM 2301 O  O   . HOH G 7 .   ? 21.414  -17.597 10.788  1.00 30.19  ? 505 HOH A O   1 
HETATM 2302 O  O   . HOH G 7 .   ? -5.166  4.696   21.091  1.00 25.18  ? 506 HOH A O   1 
HETATM 2303 O  O   . HOH G 7 .   ? 27.284  -9.372  15.677  1.00 40.52  ? 507 HOH A O   1 
HETATM 2304 O  O   . HOH G 7 .   ? 12.140  6.389   -6.678  1.00 36.84  ? 508 HOH A O   1 
HETATM 2305 O  O   . HOH G 7 .   ? 29.746  -2.095  21.167  1.00 16.01  ? 509 HOH A O   1 
HETATM 2306 O  O   . HOH G 7 .   ? 34.536  1.991   24.610  1.00 24.31  ? 510 HOH A O   1 
HETATM 2307 O  O   . HOH G 7 .   ? 6.431   -16.816 18.748  1.00 17.76  ? 511 HOH A O   1 
HETATM 2308 O  O   . HOH G 7 .   ? 14.459  -3.495  37.362  1.00 21.83  ? 512 HOH A O   1 
HETATM 2309 O  O   . HOH G 7 .   ? -0.574  -12.386 18.705  1.00 41.89  ? 513 HOH A O   1 
HETATM 2310 O  O   . HOH G 7 .   ? 1.347   -2.317  41.302  1.00 36.84  ? 514 HOH A O   1 
HETATM 2311 O  O   . HOH G 7 .   ? -1.697  -4.063  2.828   1.00 23.76  ? 515 HOH A O   1 
HETATM 2312 O  O   . HOH G 7 .   ? 10.548  23.720  20.012  1.00 22.81  ? 516 HOH A O   1 
HETATM 2313 O  O   . HOH G 7 .   ? -3.819  -5.864  9.124   1.00 21.72  ? 517 HOH A O   1 
HETATM 2314 O  O   . HOH G 7 .   ? 5.065   17.798  23.762  1.00 27.88  ? 518 HOH A O   1 
HETATM 2315 O  O   . HOH G 7 .   ? 28.561  -5.853  -0.704  1.00 23.31  ? 519 HOH A O   1 
HETATM 2316 O  O   . HOH G 7 .   ? 5.771   21.392  13.253  1.00 23.81  ? 520 HOH A O   1 
HETATM 2317 O  O   . HOH G 7 .   ? 28.183  5.273   32.194  1.00 39.98  ? 521 HOH A O   1 
HETATM 2318 O  O   . HOH G 7 .   ? 2.652   -2.006  -2.628  1.00 28.89  ? 522 HOH A O   1 
HETATM 2319 O  O   . HOH G 7 .   ? 21.403  21.568  17.430  1.00 49.46  ? 523 HOH A O   1 
HETATM 2320 O  O   . HOH G 7 .   ? 17.328  -14.038 24.286  1.00 15.30  ? 524 HOH A O   1 
HETATM 2321 O  O   . HOH G 7 .   ? 12.727  -13.727 36.341  1.00 32.33  ? 525 HOH A O   1 
HETATM 2322 O  O   . HOH G 7 .   ? 22.324  -9.975  25.041  1.00 24.13  ? 526 HOH A O   1 
HETATM 2323 O  O   . HOH G 7 .   ? 9.967   -17.517 7.093   1.00 27.77  ? 527 HOH A O   1 
HETATM 2324 O  O   . HOH G 7 .   ? -0.492  21.357  17.375  1.00 37.62  ? 528 HOH A O   1 
HETATM 2325 O  O   . HOH G 7 .   ? -2.461  -16.190 6.384   1.00 34.65  ? 529 HOH A O   1 
HETATM 2326 O  O   . HOH G 7 .   ? 20.113  10.715  15.295  1.00 36.29  ? 530 HOH A O   1 
HETATM 2327 O  O   . HOH G 7 .   ? 36.484  -0.650  14.532  1.00 26.42  ? 531 HOH A O   1 
HETATM 2328 O  O   . HOH G 7 .   ? -2.297  -11.422 11.386  1.00 21.83  ? 532 HOH A O   1 
HETATM 2329 O  O   . HOH G 7 .   ? 8.121   -14.994 26.639  1.00 20.33  ? 533 HOH A O   1 
HETATM 2330 O  O   . HOH G 7 .   ? 35.113  7.389   19.228  1.00 36.01  ? 534 HOH A O   1 
HETATM 2331 O  O   . HOH G 7 .   ? 20.737  11.258  17.917  1.00 35.16  ? 535 HOH A O   1 
HETATM 2332 O  O   . HOH G 7 .   ? 3.250   -18.724 8.079   1.00 17.41  ? 536 HOH A O   1 
HETATM 2333 O  O   . HOH G 7 .   ? 9.170   4.606   30.731  1.00 17.97  ? 537 HOH A O   1 
HETATM 2334 O  O   . HOH G 7 .   ? 6.166   22.072  17.697  1.00 22.20  ? 538 HOH A O   1 
HETATM 2335 O  O   . HOH G 7 .   ? 4.437   7.117   -7.855  1.00 31.97  ? 539 HOH A O   1 
HETATM 2336 O  O   . HOH G 7 .   ? -1.497  -7.773  25.436  1.00 28.12  ? 540 HOH A O   1 
HETATM 2337 O  O   . HOH G 7 .   ? 10.230  2.943   33.656  1.00 36.19  ? 541 HOH A O   1 
HETATM 2338 O  O   . HOH G 7 .   ? 19.077  -2.725  -7.096  1.00 30.00  ? 542 HOH A O   1 
HETATM 2339 O  O   . HOH G 7 .   ? 13.707  -6.870  32.581  1.00 19.31  ? 543 HOH A O   1 
HETATM 2340 O  O   . HOH G 7 .   ? -2.143  -1.205  6.902   1.00 28.21  ? 544 HOH A O   1 
HETATM 2341 O  O   . HOH G 7 .   ? -0.993  7.639   4.932   1.00 18.35  ? 545 HOH A O   1 
HETATM 2342 O  O   . HOH G 7 .   ? 8.110   -7.145  -3.169  1.00 29.84  ? 546 HOH A O   1 
HETATM 2343 O  O   . HOH G 7 .   ? 15.281  9.632   5.366   1.00 23.06  ? 547 HOH A O   1 
HETATM 2344 O  O   . HOH G 7 .   ? 2.965   12.614  11.364  1.00 23.84  ? 548 HOH A O   1 
HETATM 2345 O  O   . HOH G 7 .   ? -1.091  -16.609 13.600  1.00 25.87  ? 549 HOH A O   1 
HETATM 2346 O  O   . HOH G 7 .   ? 17.724  -11.386 25.115  1.00 12.60  ? 550 HOH A O   1 
HETATM 2347 O  O   . HOH G 7 .   ? 4.887   -8.079  32.952  1.00 22.35  ? 551 HOH A O   1 
HETATM 2348 O  O   . HOH G 7 .   ? 5.399   10.843  -1.918  1.00 34.05  ? 552 HOH A O   1 
HETATM 2349 O  O   . HOH G 7 .   ? 20.758  -18.777 14.977  1.00 38.82  ? 553 HOH A O   1 
HETATM 2350 O  O   . HOH G 7 .   ? 32.344  3.105   26.077  1.00 28.70  ? 554 HOH A O   1 
HETATM 2351 O  O   . HOH G 7 .   ? 24.453  10.540  20.999  1.00 32.51  ? 555 HOH A O   1 
HETATM 2352 O  O   . HOH G 7 .   ? 1.705   11.945  8.982   1.00 16.38  ? 556 HOH A O   1 
HETATM 2353 O  O   . HOH G 7 .   ? -2.923  1.693   1.309   1.00 32.37  ? 557 HOH A O   1 
HETATM 2354 O  O   . HOH G 7 .   ? 22.902  9.945   24.821  1.00 26.15  ? 558 HOH A O   1 
HETATM 2355 O  O   . HOH G 7 .   ? 26.011  -3.105  21.075  1.00 15.93  ? 559 HOH A O   1 
HETATM 2356 O  O   . HOH G 7 .   ? 7.500   1.088   -6.030  1.00 29.70  ? 560 HOH A O   1 
HETATM 2357 O  O   . HOH G 7 .   ? 7.486   16.054  27.367  1.00 29.19  ? 561 HOH A O   1 
HETATM 2358 O  O   . HOH G 7 .   ? -2.792  1.056   26.520  1.00 27.43  ? 562 HOH A O   1 
HETATM 2359 O  O   . HOH G 7 .   ? 35.022  3.873   22.938  1.00 26.96  ? 563 HOH A O   1 
HETATM 2360 O  O   . HOH G 7 .   ? -5.162  -5.634  30.525  1.00 40.64  ? 564 HOH A O   1 
HETATM 2361 O  O   . HOH G 7 .   ? -4.873  9.936   6.509   1.00 38.51  ? 565 HOH A O   1 
HETATM 2362 O  O   . HOH G 7 .   ? 23.703  -9.589  9.413   1.00 21.56  ? 566 HOH A O   1 
HETATM 2363 O  O   . HOH G 7 .   ? -4.596  -1.423  32.082  1.00 48.16  ? 567 HOH A O   1 
HETATM 2364 O  O   . HOH G 7 .   ? 11.691  -8.179  -1.153  1.00 27.24  ? 568 HOH A O   1 
HETATM 2365 O  O   . HOH G 7 .   ? -5.672  -2.158  25.195  1.00 26.82  ? 569 HOH A O   1 
HETATM 2366 O  O   . HOH G 7 .   ? 8.168   5.454   -6.676  1.00 24.97  ? 570 HOH A O   1 
HETATM 2367 O  O   . HOH G 7 .   ? 7.795   -16.613 14.751  1.00 19.77  ? 571 HOH A O   1 
HETATM 2368 O  O   . HOH G 7 .   ? 13.956  -6.698  -6.981  1.00 35.44  ? 572 HOH A O   1 
HETATM 2369 O  O   . HOH G 7 .   ? 9.890   13.874  7.540   1.00 37.49  ? 573 HOH A O   1 
HETATM 2370 O  O   . HOH G 7 .   ? 11.968  -3.969  35.956  1.00 22.43  ? 574 HOH A O   1 
HETATM 2371 O  O   . HOH G 7 .   ? 24.208  -2.508  7.242   1.00 36.06  ? 575 HOH A O   1 
HETATM 2372 O  O   . HOH G 7 .   ? 20.891  -12.411 22.070  1.00 22.04  ? 576 HOH A O   1 
HETATM 2373 O  O   . HOH G 7 .   ? 10.553  22.721  24.857  1.00 31.72  ? 577 HOH A O   1 
HETATM 2374 O  O   . HOH G 7 .   ? 22.371  0.228   29.465  1.00 15.59  ? 578 HOH A O   1 
HETATM 2375 O  O   . HOH G 7 .   ? 20.481  -6.746  32.503  1.00 25.15  ? 579 HOH A O   1 
HETATM 2376 O  O   . HOH G 7 .   ? 11.605  17.147  12.070  1.00 27.07  ? 580 HOH A O   1 
HETATM 2377 O  O   . HOH G 7 .   ? 26.077  -5.578  22.331  1.00 31.93  ? 581 HOH A O   1 
HETATM 2378 O  O   . HOH G 7 .   ? -3.795  6.612   8.433   1.00 38.12  ? 582 HOH A O   1 
HETATM 2379 O  O   . HOH G 7 .   ? 19.468  6.329   -4.911  1.00 30.95  ? 583 HOH A O   1 
HETATM 2380 O  O   . HOH G 7 .   ? -1.859  -9.951  14.105  1.00 22.69  ? 584 HOH A O   1 
HETATM 2381 O  O   . HOH G 7 .   ? 34.226  -3.978  24.569  1.00 28.77  ? 585 HOH A O   1 
HETATM 2382 O  O   . HOH G 7 .   ? 15.120  17.727  12.044  1.00 38.45  ? 586 HOH A O   1 
HETATM 2383 O  O   . HOH G 7 .   ? 10.995  7.951   -4.089  1.00 35.15  ? 587 HOH A O   1 
HETATM 2384 O  O   . HOH G 7 .   ? 12.596  -18.050 26.632  1.00 29.25  ? 588 HOH A O   1 
HETATM 2385 O  O   . HOH G 7 .   ? 19.016  -10.443 22.792  1.00 11.64  ? 589 HOH A O   1 
HETATM 2386 O  O   . HOH G 7 .   ? 8.572   11.728  -5.429  1.00 39.34  ? 590 HOH A O   1 
HETATM 2387 O  O   . HOH G 7 .   ? 32.731  -2.047  7.983   1.00 48.68  ? 591 HOH A O   1 
HETATM 2388 O  O   . HOH G 7 .   ? -0.842  21.465  12.035  1.00 39.33  ? 592 HOH A O   1 
HETATM 2389 O  O   . HOH G 7 .   ? 23.883  3.122   -2.112  1.00 33.76  ? 593 HOH A O   1 
HETATM 2390 O  O   . HOH G 7 .   ? -3.000  1.067   4.017   1.00 22.81  ? 594 HOH A O   1 
HETATM 2391 O  O   . HOH G 7 .   ? 4.039   -9.902  36.327  1.00 41.84  ? 595 HOH A O   1 
HETATM 2392 O  O   . HOH G 7 .   ? 8.532   -16.678 31.985  1.00 31.78  ? 596 HOH A O   1 
HETATM 2393 O  O   . HOH G 7 .   ? 8.422   9.737   28.866  1.00 29.27  ? 597 HOH A O   1 
HETATM 2394 O  O   . HOH G 7 .   ? 31.647  8.619   15.778  1.00 39.45  ? 598 HOH A O   1 
HETATM 2395 O  O   . HOH G 7 .   ? 0.073   -17.878 6.650   1.00 26.21  ? 599 HOH A O   1 
HETATM 2396 O  O   . HOH G 7 .   ? 25.468  -4.967  7.826   1.00 29.23  ? 600 HOH A O   1 
HETATM 2397 O  O   . HOH G 7 .   ? 22.625  -15.811 13.452  1.00 43.83  ? 601 HOH A O   1 
HETATM 2398 O  O   . HOH G 7 .   ? 12.960  -17.477 21.675  1.00 21.50  ? 602 HOH A O   1 
HETATM 2399 O  O   . HOH G 7 .   ? -4.804  5.676   33.853  1.00 47.83  ? 603 HOH A O   1 
HETATM 2400 O  O   . HOH G 7 .   ? 30.984  2.110   14.393  1.00 44.32  ? 604 HOH A O   1 
HETATM 2401 O  O   . HOH G 7 .   ? 28.745  7.962   22.015  1.00 20.01  ? 605 HOH A O   1 
HETATM 2402 O  O   . HOH G 7 .   ? 10.024  11.035  7.748   1.00 35.70  ? 606 HOH A O   1 
HETATM 2403 O  O   . HOH G 7 .   ? 14.739  -17.949 23.808  1.00 44.05  ? 607 HOH A O   1 
HETATM 2404 O  O   . HOH G 7 .   ? 22.651  -4.644  34.488  1.00 41.23  ? 608 HOH A O   1 
HETATM 2405 O  O   . HOH G 7 .   ? 24.016  -12.709 0.926   1.00 33.56  ? 609 HOH A O   1 
HETATM 2406 O  O   . HOH G 7 .   ? 6.644   8.065   32.861  1.00 43.81  ? 610 HOH A O   1 
HETATM 2407 O  O   . HOH G 7 .   ? -2.460  1.709   31.978  1.00 32.72  ? 611 HOH A O   1 
HETATM 2408 O  O   . HOH G 7 .   ? 11.560  -6.170  33.954  1.00 25.47  ? 612 HOH A O   1 
HETATM 2409 O  O   . HOH G 7 .   ? 6.173   -9.266  -3.830  1.00 44.36  ? 613 HOH A O   1 
HETATM 2410 O  O   . HOH G 7 .   ? 4.062   20.238  4.259   1.00 27.93  ? 614 HOH A O   1 
HETATM 2411 O  O   . HOH G 7 .   ? -9.555  -10.860 22.115  1.00 48.40  ? 615 HOH A O   1 
HETATM 2412 O  O   . HOH G 7 .   ? 16.088  -11.605 34.234  1.00 40.93  ? 616 HOH A O   1 
HETATM 2413 O  O   . HOH G 7 .   ? 2.110   5.222   -3.408  1.00 36.98  ? 617 HOH A O   1 
HETATM 2414 O  O   . HOH G 7 .   ? 14.153  3.333   35.210  1.00 30.36  ? 618 HOH A O   1 
HETATM 2415 O  O   . HOH G 7 .   ? 31.097  -11.745 9.520   1.00 52.79  ? 619 HOH A O   1 
HETATM 2416 O  O   . HOH G 7 .   ? 13.628  -6.842  -2.335  1.00 27.91  ? 620 HOH A O   1 
HETATM 2417 O  O   . HOH G 7 .   ? 5.724   -18.407 22.694  1.00 39.89  ? 621 HOH A O   1 
HETATM 2418 O  O   . HOH G 7 .   ? 15.482  5.352   -5.651  1.00 35.98  ? 622 HOH A O   1 
HETATM 2419 O  O   . HOH G 7 .   ? -3.561  7.060   35.581  1.00 47.92  ? 623 HOH A O   1 
HETATM 2420 O  O   . HOH G 7 .   ? -10.616 7.501   13.113  1.00 48.37  ? 624 HOH A O   1 
HETATM 2421 O  O   . HOH G 7 .   ? 15.400  -10.543 -5.273  1.00 39.35  ? 625 HOH A O   1 
HETATM 2422 O  O   . HOH G 7 .   ? 30.859  3.952   11.899  1.00 53.07  ? 626 HOH A O   1 
HETATM 2423 O  O   . HOH G 7 .   ? 34.162  -1.936  13.564  1.00 34.60  ? 627 HOH A O   1 
HETATM 2424 O  O   . HOH G 7 .   ? 29.522  5.509   28.096  1.00 46.04  ? 628 HOH A O   1 
HETATM 2425 O  O   . HOH G 7 .   ? 18.263  -13.000 32.706  1.00 36.43  ? 629 HOH A O   1 
HETATM 2426 O  O   . HOH G 7 .   ? 22.045  13.955  20.328  1.00 48.38  ? 630 HOH A O   1 
HETATM 2427 O  O   . HOH G 7 .   ? 30.225  3.920   30.279  1.00 45.72  ? 631 HOH A O   1 
HETATM 2428 O  O   . HOH G 7 .   ? -4.464  6.373   4.004   1.00 39.02  ? 632 HOH A O   1 
HETATM 2429 O  O   . HOH G 7 .   ? -4.199  13.050  19.742  1.00 34.77  ? 633 HOH A O   1 
HETATM 2430 O  O   . HOH G 7 .   ? 31.370  -0.620  14.147  1.00 28.92  ? 634 HOH A O   1 
HETATM 2431 O  O   . HOH G 7 .   ? 25.768  -7.946  8.229   1.00 41.85  ? 635 HOH A O   1 
HETATM 2432 O  O   . HOH G 7 .   ? 5.857   -14.342 25.397  1.00 39.72  ? 636 HOH A O   1 
HETATM 2433 O  O   . HOH G 7 .   ? 29.747  -2.848  23.836  1.00 30.24  ? 637 HOH A O   1 
HETATM 2434 O  O   . HOH G 7 .   ? 19.012  20.303  15.452  1.00 41.67  ? 638 HOH A O   1 
HETATM 2435 O  O   . HOH G 7 .   ? 35.726  2.038   15.032  1.00 50.20  ? 639 HOH A O   1 
HETATM 2436 O  O   . HOH G 7 .   ? 14.936  14.964  10.427  1.00 45.16  ? 640 HOH A O   1 
HETATM 2437 O  O   . HOH G 7 .   ? 8.259   -15.352 16.998  1.00 18.54  ? 641 HOH A O   1 
HETATM 2438 O  O   . HOH G 7 .   ? 31.528  -6.937  8.588   1.00 42.55  ? 642 HOH A O   1 
HETATM 2439 O  O   . HOH G 7 .   ? -7.104  12.645  19.715  1.00 49.92  ? 643 HOH A O   1 
HETATM 2440 O  O   . HOH G 7 .   ? 12.232  9.778   7.935   1.00 42.28  ? 644 HOH A O   1 
HETATM 2441 O  O   . HOH G 7 .   ? 8.133   20.784  12.057  1.00 35.38  ? 645 HOH A O   1 
HETATM 2442 O  O   . HOH G 7 .   ? 21.434  -0.552  39.293  1.00 47.10  ? 646 HOH A O   1 
HETATM 2443 O  O   . HOH G 7 .   ? 20.206  12.843  24.340  1.00 44.01  ? 647 HOH A O   1 
HETATM 2444 O  O   . HOH G 7 .   ? 8.717   8.438   31.074  1.00 37.79  ? 648 HOH A O   1 
HETATM 2445 O  O   . HOH G 7 .   ? 22.483  -8.051  28.960  1.00 48.28  ? 649 HOH A O   1 
HETATM 2446 O  O   . HOH G 7 .   ? -3.532  11.210  26.525  1.00 49.08  ? 650 HOH A O   1 
HETATM 2447 O  O   . HOH G 7 .   ? 22.117  5.155   2.044   1.00 34.18  ? 651 HOH A O   1 
HETATM 2448 O  O   . HOH G 7 .   ? -2.815  -1.554  4.024   1.00 41.40  ? 652 HOH A O   1 
HETATM 2449 O  O   . HOH G 7 .   ? 17.411  8.090   6.055   1.00 27.25  ? 653 HOH A O   1 
HETATM 2450 O  O   . HOH G 7 .   ? 26.060  -9.084  18.401  1.00 49.51  ? 654 HOH A O   1 
HETATM 2451 O  O   . HOH G 7 .   ? 30.229  -7.760  0.343   1.00 39.34  ? 655 HOH A O   1 
HETATM 2452 O  O   . HOH G 7 .   ? 3.177   -7.004  34.948  1.00 35.21  ? 656 HOH A O   1 
HETATM 2453 O  O   . HOH G 7 .   ? 19.787  -11.166 26.991  1.00 26.65  ? 657 HOH A O   1 
HETATM 2454 O  O   . HOH G 7 .   ? 19.141  -15.550 25.459  1.00 31.62  ? 658 HOH A O   1 
HETATM 2455 O  O   . HOH G 7 .   ? 27.475  -3.542  27.453  1.00 40.89  ? 659 HOH A O   1 
HETATM 2456 O  O   . HOH G 7 .   ? 10.698  6.824   30.673  1.00 29.35  ? 660 HOH A O   1 
HETATM 2457 O  O   . HOH G 7 .   ? 4.198   -16.108 20.316  1.00 28.88  ? 661 HOH A O   1 
HETATM 2458 O  O   . HOH G 7 .   ? 4.356   -12.519 37.234  1.00 36.36  ? 662 HOH A O   1 
HETATM 2459 O  O   . HOH G 7 .   ? 1.174   -0.038  42.874  1.00 43.26  ? 663 HOH A O   1 
HETATM 2460 O  O   . HOH G 7 .   ? 24.071  -11.958 8.027   1.00 30.74  ? 664 HOH A O   1 
HETATM 2461 O  O   . HOH G 7 .   ? 3.099   -10.251 31.413  1.00 33.59  ? 665 HOH A O   1 
HETATM 2462 O  O   . HOH G 7 .   ? 18.979  -10.026 31.553  1.00 34.62  ? 666 HOH A O   1 
HETATM 2463 O  O   . HOH G 7 .   ? 20.084  -11.365 32.966  1.00 36.95  ? 667 HOH A O   1 
HETATM 2464 O  O   . HOH G 7 .   ? 9.155   2.701   -7.587  1.00 39.88  ? 668 HOH A O   1 
HETATM 2465 O  O   . HOH G 7 .   ? 5.265   18.770  26.535  1.00 56.14  ? 669 HOH A O   1 
HETATM 2466 O  O   . HOH G 7 .   ? 23.032  -12.232 20.433  1.00 32.54  ? 670 HOH A O   1 
HETATM 2467 O  O   . HOH G 7 .   ? 9.884   -9.346  -2.794  1.00 37.30  ? 671 HOH A O   1 
HETATM 2468 O  O   . HOH G 7 .   ? -2.993  -5.469  0.325   1.00 32.81  ? 672 HOH A O   1 
HETATM 2469 O  O   . HOH G 7 .   ? 10.736  24.925  17.114  1.00 17.41  ? 673 HOH A O   1 
HETATM 2470 O  O   . HOH G 7 .   ? 9.498   12.604  0.936   1.00 25.69  ? 674 HOH A O   1 
HETATM 2471 O  O   . HOH G 7 .   ? 13.906  -8.301  -4.527  1.00 34.58  ? 675 HOH A O   1 
HETATM 2472 O  O   . HOH G 7 .   ? 27.226  7.096   29.784  1.00 38.27  ? 676 HOH A O   1 
HETATM 2473 O  O   . HOH G 7 .   ? 22.566  -15.798 7.169   1.00 30.57  ? 677 HOH A O   1 
HETATM 2474 O  O   . HOH G 7 .   ? 12.041  4.926   34.775  1.00 26.94  ? 678 HOH A O   1 
HETATM 2475 O  O   . HOH G 7 .   ? 15.973  -7.831  33.884  1.00 38.49  ? 679 HOH A O   1 
HETATM 2476 O  O   . HOH G 7 .   ? 16.890  -13.507 -2.495  1.00 34.41  ? 680 HOH A O   1 
HETATM 2477 O  O   . HOH G 7 .   ? 14.981  -19.026 26.395  1.00 46.92  ? 681 HOH A O   1 
HETATM 2478 O  O   . HOH G 7 .   ? 19.874  -9.315  28.954  1.00 18.62  ? 682 HOH A O   1 
HETATM 2479 O  O   . HOH G 7 .   ? 8.685   15.417  4.915   1.00 31.36  ? 683 HOH A O   1 
HETATM 2480 O  O   . HOH G 7 .   ? 20.813  -17.966 6.663   1.00 29.20  ? 684 HOH A O   1 
HETATM 2481 O  O   . HOH G 7 .   ? 23.819  8.081   32.535  1.00 43.51  ? 685 HOH A O   1 
HETATM 2482 O  O   . HOH G 7 .   ? 25.215  12.089  17.699  1.00 45.86  ? 686 HOH A O   1 
HETATM 2483 O  O   . HOH G 7 .   ? 8.127   23.649  26.043  1.00 29.91  ? 687 HOH A O   1 
HETATM 2484 O  O   . HOH G 7 .   ? -5.495  0.518   26.016  1.00 28.71  ? 688 HOH A O   1 
HETATM 2485 O  O   . HOH G 7 .   ? 3.444   -19.485 17.523  1.00 24.61  ? 689 HOH A O   1 
HETATM 2486 O  O   . HOH G 7 .   ? 27.722  10.309  18.535  1.00 36.14  ? 690 HOH A O   1 
HETATM 2487 O  O   . HOH G 7 .   ? 20.600  -5.117  -7.610  1.00 43.45  ? 691 HOH A O   1 
HETATM 2488 O  O   . HOH G 7 .   ? 19.444  -15.364 4.747   1.00 45.31  ? 692 HOH A O   1 
HETATM 2489 O  O   . HOH G 7 .   ? 18.195  -17.591 27.158  1.00 53.98  ? 693 HOH A O   1 
HETATM 2490 O  O   . HOH G 7 .   ? 6.998   5.478   33.240  1.00 43.90  ? 694 HOH A O   1 
HETATM 2491 O  O   . HOH G 7 .   ? 18.363  -7.511  34.418  1.00 36.74  ? 695 HOH A O   1 
HETATM 2492 O  O   . HOH G 7 .   ? 25.134  10.480  23.571  1.00 44.12  ? 696 HOH A O   1 
HETATM 2493 O  O   . HOH G 7 .   ? 24.482  4.897   0.153   1.00 37.91  ? 697 HOH A O   1 
HETATM 2494 O  O   . HOH G 7 .   ? 3.614   12.883  -2.055  1.00 27.34  ? 698 HOH A O   1 
HETATM 2495 O  O   . HOH G 7 .   ? 35.495  6.425   24.265  1.00 33.72  ? 699 HOH A O   1 
HETATM 2496 O  O   . HOH G 7 .   ? 9.008   15.192  2.082   1.00 29.87  ? 700 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   . HIS A 3   ? 0.3443 0.6011 0.4756 0.0449  -0.0391 0.0537  3   HIS A N   
2    C  CA  . HIS A 3   ? 0.4863 0.6853 0.6455 0.0864  0.0805  0.2006  3   HIS A CA  
3    C  C   . HIS A 3   ? 0.7121 0.7146 0.3754 -0.0552 -0.0557 -0.0509 3   HIS A C   
4    O  O   . HIS A 3   ? 0.8315 0.5809 0.4345 -0.2764 -0.2128 -0.0111 3   HIS A O   
5    C  CB  . HIS A 3   ? 0.5511 0.3978 0.6384 -0.0201 0.0211  0.1438  3   HIS A CB  
6    C  CG  . HIS A 3   ? 0.4426 0.4547 0.4255 -0.0835 -0.0035 0.0933  3   HIS A CG  
7    N  ND1 . HIS A 3   ? 0.4558 0.5535 0.3802 -0.2000 -0.0712 0.1338  3   HIS A ND1 
8    C  CD2 . HIS A 3   ? 0.4465 0.5074 0.4248 0.0058  -0.0331 -0.0328 3   HIS A CD2 
9    C  CE1 . HIS A 3   ? 0.3220 0.5687 0.4840 -0.2071 -0.0132 0.0800  3   HIS A CE1 
10   N  NE2 . HIS A 3   ? 0.4547 0.4438 0.6161 -0.1327 0.0384  0.0432  3   HIS A NE2 
11   N  N   . HIS A 4   ? 0.4123 1.0201 0.9943 -0.0256 0.1180  -0.0876 4   HIS A N   
12   C  CA  . HIS A 4   ? 0.4874 0.5373 0.7676 -0.0888 0.1241  -0.0569 4   HIS A CA  
13   C  C   . HIS A 4   ? 0.4526 0.6336 0.5011 0.1868  0.0823  -0.0952 4   HIS A C   
14   O  O   . HIS A 4   ? 0.3073 0.4796 0.3133 -0.0100 0.1309  0.0580  4   HIS A O   
15   C  CB  . HIS A 4   ? 0.4673 0.9793 0.7210 -0.1874 0.2013  0.3468  4   HIS A CB  
16   C  CG  . HIS A 4   ? 1.0956 0.8933 1.3049 -0.0908 0.3948  0.5281  4   HIS A CG  
17   N  ND1 . HIS A 4   ? 0.8418 1.8815 1.0073 -0.2985 0.0412  0.8574  4   HIS A ND1 
18   C  CD2 . HIS A 4   ? 0.6904 1.8370 1.1547 0.0407  0.2405  0.4163  4   HIS A CD2 
19   C  CE1 . HIS A 4   ? 1.1258 1.7986 1.5510 -0.4758 0.1852  0.3977  4   HIS A CE1 
20   N  NE2 . HIS A 4   ? 0.3856 1.9691 1.6381 -0.1022 0.2404  0.2387  4   HIS A NE2 
21   N  N   . TRP A 5   ? 0.2393 0.3064 0.2849 -0.0222 0.0282  0.0771  5   TRP A N   
22   C  CA  . TRP A 5   ? 0.2213 0.2107 0.2744 0.0309  0.0474  0.0491  5   TRP A CA  
23   C  C   . TRP A 5   ? 0.2214 0.2945 0.2911 0.0131  0.0376  0.0583  5   TRP A C   
24   O  O   . TRP A 5   ? 0.1957 0.2782 0.2601 -0.0223 0.0479  0.0499  5   TRP A O   
25   C  CB  . TRP A 5   ? 0.1497 0.1867 0.2899 -0.0238 0.0164  0.0104  5   TRP A CB  
26   C  CG  . TRP A 5   ? 0.1653 0.1984 0.2530 -0.0108 0.0293  0.0172  5   TRP A CG  
27   C  CD1 . TRP A 5   ? 0.2323 0.2292 0.3491 0.0091  0.0438  0.0684  5   TRP A CD1 
28   C  CD2 . TRP A 5   ? 0.1569 0.2251 0.1802 0.0003  0.0089  0.0163  5   TRP A CD2 
29   N  NE1 . TRP A 5   ? 0.2036 0.3043 0.2764 -0.0109 0.0641  0.1146  5   TRP A NE1 
30   C  CE2 . TRP A 5   ? 0.1881 0.2235 0.1899 0.0058  0.0332  0.0159  5   TRP A CE2 
31   C  CE3 . TRP A 5   ? 0.1761 0.2206 0.2002 -0.0299 0.0237  0.0076  5   TRP A CE3 
32   C  CZ2 . TRP A 5   ? 0.1845 0.3665 0.2371 -0.0261 0.0330  -0.0239 5   TRP A CZ2 
33   C  CZ3 . TRP A 5   ? 0.1854 0.3095 0.2248 -0.0314 0.0323  -0.0529 5   TRP A CZ3 
34   C  CH2 . TRP A 5   ? 0.1808 0.3185 0.1989 -0.0217 -0.0247 -0.0825 5   TRP A CH2 
35   N  N   . GLY A 6   ? 0.2127 0.1927 0.2815 0.0368  0.0741  -0.0223 6   GLY A N   
36   C  CA  . GLY A 6   ? 0.2470 0.2416 0.2347 -0.0195 0.0816  0.0036  6   GLY A CA  
37   C  C   . GLY A 6   ? 0.2283 0.2159 0.2900 0.0114  0.1335  -0.0003 6   GLY A C   
38   O  O   . GLY A 6   ? 0.2064 0.2335 0.2935 0.0154  0.0930  0.0016  6   GLY A O   
39   N  N   . TYR A 7   ? 0.2165 0.2501 0.3452 -0.0170 0.1465  -0.0472 7   TYR A N   
40   C  CA  . TYR A 7   ? 0.2413 0.2528 0.4342 -0.0792 0.1154  0.0035  7   TYR A CA  
41   C  C   . TYR A 7   ? 0.2971 0.2580 0.6412 -0.0326 0.1356  -0.0536 7   TYR A C   
42   O  O   . TYR A 7   ? 0.2091 0.3246 0.5299 -0.0227 0.0421  -0.1090 7   TYR A O   
43   C  CB  . TYR A 7   ? 0.2285 0.1831 0.3801 0.0162  0.0681  -0.0660 7   TYR A CB  
44   C  CG  . TYR A 7   ? 0.1729 0.1734 0.2113 -0.0135 0.0633  -0.0262 7   TYR A CG  
45   C  CD1 . TYR A 7   ? 0.1186 0.1917 0.2158 -0.0289 0.0584  -0.0494 7   TYR A CD1 
46   C  CD2 . TYR A 7   ? 0.1733 0.2085 0.2070 -0.0203 0.0332  -0.0389 7   TYR A CD2 
47   C  CE1 . TYR A 7   ? 0.1244 0.1791 0.2050 -0.0212 0.0298  -0.0149 7   TYR A CE1 
48   C  CE2 . TYR A 7   ? 0.1370 0.2020 0.1612 -0.0331 0.0282  -0.0145 7   TYR A CE2 
49   C  CZ  . TYR A 7   ? 0.1360 0.1460 0.1737 -0.0516 0.0286  -0.0261 7   TYR A CZ  
50   O  OH  . TYR A 7   ? 0.1689 0.1535 0.1824 -0.0234 0.0240  -0.0174 7   TYR A OH  
51   N  N   . GLY A 8   ? 0.3312 0.2931 0.6141 0.0762  0.1921  -0.0895 8   GLY A N   
52   C  CA  . GLY A 8   ? 0.2359 0.1565 0.6224 -0.0040 0.1338  -0.0912 8   GLY A CA  
53   C  C   . GLY A 8   ? 0.4898 0.2896 0.3083 0.0322  0.1923  -0.0229 8   GLY A C   
54   O  O   . GLY A 8   ? 0.3209 0.2827 0.5195 -0.0397 0.2110  -0.1092 8   GLY A O   
55   N  N   . LYS A 9   ? 0.2798 0.3268 0.5859 0.0055  0.0195  -0.0433 9   LYS A N   
56   C  CA  . LYS A 9   ? 0.4695 0.4526 0.5024 -0.0334 -0.1370 -0.1914 9   LYS A CA  
57   C  C   . LYS A 9   ? 0.3065 0.4845 0.4554 0.0276  -0.1220 -0.0173 9   LYS A C   
58   O  O   . LYS A 9   ? 0.2814 0.6474 0.3980 -0.1657 0.0710  -0.0596 9   LYS A O   
59   C  CB  . LYS A 9   ? 0.3515 0.7231 0.3601 0.0200  0.0648  -0.1764 9   LYS A CB  
60   N  N   . HIS A 10  ? 0.7882 0.3802 0.6501 -0.0181 -0.0221 0.1753  10  HIS A N   
61   C  CA  . HIS A 10  ? 0.6552 0.4197 0.8524 -0.0148 -0.1167 0.1161  10  HIS A CA  
62   C  C   . HIS A 10  ? 0.3499 0.5098 0.3483 0.0189  0.1394  0.1828  10  HIS A C   
63   O  O   . HIS A 10  ? 0.2975 0.3703 0.3516 0.1751  0.1506  0.1092  10  HIS A O   
64   C  CB  . HIS A 10  ? 0.6886 0.6828 0.6147 -0.1247 0.2317  0.0491  10  HIS A CB  
65   C  CG  . HIS A 10  ? 0.8647 1.0957 0.6738 -0.0294 0.2474  0.3404  10  HIS A CG  
66   N  ND1 . HIS A 10  ? 1.7644 1.5804 0.7570 -0.2336 0.8576  0.6020  10  HIS A ND1 
67   C  CD2 . HIS A 10  ? 1.3131 1.2612 1.6790 0.0923  0.3119  0.5389  10  HIS A CD2 
68   C  CE1 . HIS A 10  ? 0.7801 1.8757 0.8162 0.2211  -0.2675 -0.5822 10  HIS A CE1 
69   N  NE2 . HIS A 10  ? 1.1895 1.5209 1.4892 -0.3097 0.9790  0.7257  10  HIS A NE2 
70   N  N   . ASN A 11  ? 0.3435 0.2968 0.4131 0.0365  0.1844  0.0900  11  ASN A N   
71   C  CA  . ASN A 11  ? 0.2372 0.2491 0.2606 -0.0190 0.1173  0.0383  11  ASN A CA  
72   C  C   . ASN A 11  ? 0.2215 0.2513 0.3591 0.0205  0.1274  0.0216  11  ASN A C   
73   O  O   . ASN A 11  ? 0.2343 0.2913 0.2568 0.0557  0.1050  0.0789  11  ASN A O   
74   C  CB  . ASN A 11  ? 0.2246 0.2317 0.2237 -0.0060 0.1174  0.0096  11  ASN A CB  
75   C  CG  . ASN A 11  ? 0.2362 0.2483 0.3363 0.0222  0.0809  -0.0166 11  ASN A CG  
76   O  OD1 . ASN A 11  ? 0.2341 0.2901 0.4192 -0.0196 0.1139  -0.0668 11  ASN A OD1 
77   N  ND2 . ASN A 11  ? 0.3237 0.3656 0.2875 0.0480  0.0942  -0.0060 11  ASN A ND2 
78   N  N   . GLY A 12  ? 0.1966 0.2624 0.3168 0.0278  0.1237  0.0440  12  GLY A N   
79   C  CA  . GLY A 12  ? 0.1806 0.2568 0.2526 -0.0033 0.0839  0.0405  12  GLY A CA  
80   C  C   . GLY A 12  ? 0.1518 0.2298 0.2881 0.0340  0.0615  0.0465  12  GLY A C   
81   O  O   . GLY A 12  ? 0.1313 0.2244 0.3191 0.0286  0.0493  0.0502  12  GLY A O   
82   N  N   . PRO A 13  ? 0.1829 0.1653 0.2305 -0.0070 0.0769  -0.0067 13  PRO A N   
83   C  CA  . PRO A 13  ? 0.1575 0.1533 0.2584 -0.0005 0.0798  -0.0106 13  PRO A CA  
84   C  C   . PRO A 13  ? 0.1872 0.1441 0.2427 0.0051  0.0538  -0.0003 13  PRO A C   
85   O  O   . PRO A 13  ? 0.1542 0.1696 0.2781 0.0048  0.0763  -0.0227 13  PRO A O   
86   C  CB  . PRO A 13  ? 0.1845 0.1905 0.2551 -0.0396 0.0969  -0.0350 13  PRO A CB  
87   C  CG  . PRO A 13  ? 0.1939 0.2041 0.2274 -0.0369 0.0999  -0.0356 13  PRO A CG  
88   C  CD  . PRO A 13  ? 0.1698 0.2052 0.2411 -0.0049 0.0880  -0.0134 13  PRO A CD  
89   N  N   . GLU A 14  ? 0.1765 0.1632 0.2811 0.0113  0.0666  0.0506  14  GLU A N   
90   C  CA  . GLU A 14  ? 0.2372 0.1877 0.2777 0.0273  0.0521  0.0440  14  GLU A CA  
91   C  C   . GLU A 14  ? 0.1605 0.2060 0.2796 0.0716  0.0608  0.0379  14  GLU A C   
92   O  O   . GLU A 14  ? 0.1914 0.2113 0.3257 0.0686  0.0434  0.0696  14  GLU A O   
93   C  CB  . GLU A 14  ? 0.3484 0.2323 0.3644 0.1077  0.0386  0.0549  14  GLU A CB  
94   C  CG  . GLU A 14  ? 0.2732 0.3439 0.3988 0.0983  -0.0688 -0.0337 14  GLU A CG  
95   C  CD  . GLU A 14  ? 0.2977 0.3571 0.4936 0.0653  -0.0716 -0.1065 14  GLU A CD  
96   O  OE1 . GLU A 14  ? 0.3289 0.2620 0.3238 0.1141  -0.0592 -0.0850 14  GLU A OE1 
97   O  OE2 . GLU A 14  ? 0.5978 0.2237 0.3988 0.0554  -0.0138 -0.0840 14  GLU A OE2 
98   N  N   . HIS A 15  ? 0.1848 0.1661 0.2811 0.0157  0.0532  0.0640  15  HIS A N   
99   C  CA  . HIS A 15  ? 0.1754 0.1772 0.2770 0.0072  0.0675  0.0153  15  HIS A CA  
100  C  C   . HIS A 15  ? 0.1260 0.1938 0.2470 0.0329  0.0282  0.0252  15  HIS A C   
101  O  O   . HIS A 15  ? 0.1036 0.2185 0.3130 0.0321  0.0179  0.0507  15  HIS A O   
102  C  CB  . HIS A 15  ? 0.1463 0.2256 0.2409 0.0544  0.0171  0.0107  15  HIS A CB  
103  C  CG  . HIS A 15  ? 0.1971 0.2312 0.2572 0.0715  0.0436  0.0427  15  HIS A CG  
104  N  ND1 . HIS A 15  ? 0.2084 0.3269 0.3156 0.0998  0.0281  0.0396  15  HIS A ND1 
105  C  CD2 . HIS A 15  ? 0.2416 0.2159 0.2609 0.1009  0.0728  0.0216  15  HIS A CD2 
106  C  CE1 . HIS A 15  ? 0.3278 0.3631 0.2194 0.1638  0.0454  0.0493  15  HIS A CE1 
107  N  NE2 . HIS A 15  ? 0.3052 0.3062 0.3609 0.1840  0.0348  -0.0118 15  HIS A NE2 
108  N  N   . TRP A 16  ? 0.1259 0.1610 0.2819 0.0303  0.0303  0.0536  16  TRP A N   
109  C  CA  . TRP A 16  ? 0.0926 0.1547 0.2652 0.0301  0.0049  0.0245  16  TRP A CA  
110  C  C   . TRP A 16  ? 0.0953 0.1729 0.2699 0.0033  0.0290  0.0184  16  TRP A C   
111  O  O   . TRP A 16  ? 0.1079 0.1536 0.2997 -0.0032 -0.0057 0.0266  16  TRP A O   
112  C  CB  . TRP A 16  ? 0.0919 0.1831 0.2511 0.0020  0.0217  -0.0366 16  TRP A CB  
113  C  CG  . TRP A 16  ? 0.1288 0.1567 0.2246 -0.0207 0.0277  0.0011  16  TRP A CG  
114  C  CD1 . TRP A 16  ? 0.1504 0.1946 0.1996 0.0067  0.0315  0.0228  16  TRP A CD1 
115  C  CD2 . TRP A 16  ? 0.1147 0.1630 0.2213 -0.0168 0.0410  -0.0019 16  TRP A CD2 
116  N  NE1 . TRP A 16  ? 0.1310 0.1666 0.2251 0.0054  0.0466  0.0317  16  TRP A NE1 
117  C  CE2 . TRP A 16  ? 0.1120 0.1470 0.2377 -0.0076 0.0334  0.0109  16  TRP A CE2 
118  C  CE3 . TRP A 16  ? 0.1235 0.1504 0.2280 -0.0135 0.0441  0.0076  16  TRP A CE3 
119  C  CZ2 . TRP A 16  ? 0.1063 0.1658 0.2692 -0.0104 0.0570  0.0046  16  TRP A CZ2 
120  C  CZ3 . TRP A 16  ? 0.1091 0.1432 0.2229 -0.0237 0.0488  -0.0277 16  TRP A CZ3 
121  C  CH2 . TRP A 16  ? 0.1317 0.1653 0.2286 -0.0204 0.0608  -0.0440 16  TRP A CH2 
122  N  N   . HIS A 17  ? 0.0935 0.2110 0.2262 0.0247  0.0190  0.0094  17  HIS A N   
123  C  CA  . HIS A 17  ? 0.1292 0.2014 0.2461 -0.0142 0.0037  0.0348  17  HIS A CA  
124  C  C   . HIS A 17  ? 0.1399 0.2294 0.3014 -0.0269 0.0084  0.0321  17  HIS A C   
125  O  O   . HIS A 17  ? 0.0957 0.2530 0.3110 0.0003  -0.0108 0.0343  17  HIS A O   
126  C  CB  . HIS A 17  ? 0.1238 0.1935 0.2472 0.0192  0.0223  0.0310  17  HIS A CB  
127  C  CG  . HIS A 17  ? 0.1244 0.2050 0.3449 0.0198  0.0042  0.0614  17  HIS A CG  
128  N  ND1 . HIS A 17  ? 0.1489 0.2813 0.3536 0.0077  -0.0111 0.0832  17  HIS A ND1 
129  C  CD2 . HIS A 17  ? 0.1673 0.2165 0.2750 0.0680  0.0017  0.0436  17  HIS A CD2 
130  C  CE1 . HIS A 17  ? 0.1199 0.3312 0.3795 0.0268  0.0252  0.0469  17  HIS A CE1 
131  N  NE2 . HIS A 17  ? 0.1838 0.2376 0.3460 0.0726  -0.0361 0.1002  17  HIS A NE2 
132  N  N   . LYS A 18  ? 0.0919 0.2182 0.3188 0.0121  0.0083  0.0754  18  LYS A N   
133  C  CA  . LYS A 18  ? 0.0932 0.2567 0.3746 0.0029  0.0333  0.0905  18  LYS A CA  
134  C  C   . LYS A 18  ? 0.1413 0.2172 0.4578 0.0082  -0.0019 0.0913  18  LYS A C   
135  O  O   . LYS A 18  ? 0.2014 0.2670 0.5655 -0.0541 -0.0859 0.1184  18  LYS A O   
136  C  CB  . LYS A 18  ? 0.1374 0.2596 0.4209 0.0449  0.0484  0.1230  18  LYS A CB  
137  C  CG  . LYS A 18  ? 0.1411 0.1981 0.3939 0.0531  0.0087  0.0502  18  LYS A CG  
138  C  CD  . LYS A 18  ? 0.1249 0.2764 0.3630 0.0597  0.0569  0.0590  18  LYS A CD  
139  C  CE  . LYS A 18  ? 0.1678 0.2509 0.3419 0.0425  0.0518  0.0692  18  LYS A CE  
140  N  NZ  . LYS A 18  ? 0.1495 0.3031 0.2850 0.0915  0.0267  0.1077  18  LYS A NZ  
141  N  N   . ASP A 19  ? 0.1180 0.2205 0.3908 0.0074  0.0160  0.0751  19  ASP A N   
142  C  CA  . ASP A 19  ? 0.1497 0.2005 0.3693 -0.0337 0.0165  0.0663  19  ASP A CA  
143  C  C   . ASP A 19  ? 0.1016 0.1845 0.4028 -0.0430 -0.0109 0.0609  19  ASP A C   
144  O  O   . ASP A 19  ? 0.1650 0.1763 0.4470 -0.0170 0.0486  0.0622  19  ASP A O   
145  C  CB  . ASP A 19  ? 0.1794 0.3207 0.3157 0.0250  0.0193  0.0657  19  ASP A CB  
146  C  CG  . ASP A 19  ? 0.2283 0.3545 0.4589 -0.0396 0.1082  -0.0780 19  ASP A CG  
147  O  OD1 . ASP A 19  ? 0.2269 0.5231 0.4598 -0.0943 0.0199  0.0854  19  ASP A OD1 
148  O  OD2 . ASP A 19  ? 0.4231 0.6011 0.7629 -0.0592 0.1493  -0.3209 19  ASP A OD2 
149  N  N   . PHE A 20  ? 0.1089 0.1659 0.3484 -0.0250 0.0071  0.0378  20  PHE A N   
150  C  CA  . PHE A 20  ? 0.1152 0.2039 0.3236 0.0154  -0.0279 0.0186  20  PHE A CA  
151  C  C   . PHE A 20  ? 0.1113 0.2307 0.3292 -0.0113 -0.0150 0.0424  20  PHE A C   
152  O  O   . PHE A 20  ? 0.1108 0.1770 0.2886 -0.0047 0.0060  0.0091  20  PHE A O   
153  C  CB  . PHE A 20  ? 0.1076 0.2348 0.2891 -0.0304 -0.0095 0.0572  20  PHE A CB  
154  C  CG  . PHE A 20  ? 0.1174 0.2411 0.2691 -0.0170 0.0205  0.0354  20  PHE A CG  
155  C  CD1 . PHE A 20  ? 0.1226 0.2624 0.3698 -0.0251 0.0013  0.0834  20  PHE A CD1 
156  C  CD2 . PHE A 20  ? 0.1295 0.3001 0.2618 -0.0223 0.0317  0.0326  20  PHE A CD2 
157  C  CE1 . PHE A 20  ? 0.1256 0.3352 0.3594 -0.0334 0.0273  0.0616  20  PHE A CE1 
158  C  CE2 . PHE A 20  ? 0.1709 0.2602 0.2699 -0.0373 0.0414  0.0062  20  PHE A CE2 
159  C  CZ  . PHE A 20  ? 0.1352 0.2785 0.4112 -0.0369 0.0692  0.1037  20  PHE A CZ  
160  N  N   . PRO A 21  ? 0.1456 0.1917 0.3242 -0.0375 0.0000  0.0319  21  PRO A N   
161  C  CA  . PRO A 21  ? 0.1518 0.2100 0.2813 -0.0315 -0.0311 -0.0051 21  PRO A CA  
162  C  C   . PRO A 21  ? 0.1447 0.2243 0.2673 -0.0029 -0.0414 -0.0100 21  PRO A C   
163  O  O   . PRO A 21  ? 0.1323 0.2061 0.3006 -0.0205 -0.0315 0.0087  21  PRO A O   
164  C  CB  . PRO A 21  ? 0.1125 0.3169 0.4039 -0.0913 -0.0397 -0.0104 21  PRO A CB  
165  C  CG  . PRO A 21  ? 0.3433 0.3517 0.4484 -0.1110 -0.1451 0.0048  21  PRO A CG  
166  C  CD  . PRO A 21  ? 0.1592 0.2355 0.3770 -0.0679 -0.0447 0.1007  21  PRO A CD  
167  N  N   . ILE A 22  ? 0.1036 0.1745 0.3129 -0.0270 -0.0207 -0.0293 22  ILE A N   
168  C  CA  . ILE A 22  ? 0.1292 0.1676 0.2728 -0.0201 -0.0174 -0.0168 22  ILE A CA  
169  C  C   . ILE A 22  ? 0.1317 0.1608 0.2056 -0.0126 -0.0348 -0.0091 22  ILE A C   
170  O  O   . ILE A 22  ? 0.1364 0.1533 0.2552 -0.0128 0.0008  -0.0212 22  ILE A O   
171  C  CB  . ILE A 22  ? 0.1371 0.1507 0.2531 -0.0034 -0.0209 -0.0211 22  ILE A CB  
172  C  CG1 . ILE A 22  ? 0.1777 0.2228 0.2620 -0.0034 -0.0037 -0.0753 22  ILE A CG1 
173  C  CG2 . ILE A 22  ? 0.1405 0.1330 0.2933 -0.0483 -0.0354 -0.0214 22  ILE A CG2 
174  C  CD1 . ILE A 22  ? 0.2063 0.3389 0.2724 -0.0234 -0.0351 -0.0935 22  ILE A CD1 
175  N  N   . ALA A 23  ? 0.1403 0.1605 0.2329 -0.0197 -0.0222 -0.0204 23  ALA A N   
176  C  CA  . ALA A 23  ? 0.1447 0.1648 0.2300 -0.0322 -0.0050 -0.0116 23  ALA A CA  
177  C  C   . ALA A 23  ? 0.0969 0.1683 0.2316 0.0027  -0.0068 -0.0133 23  ALA A C   
178  O  O   . ALA A 23  ? 0.1371 0.1698 0.2307 0.0035  -0.0021 -0.0075 23  ALA A O   
179  C  CB  . ALA A 23  ? 0.1174 0.1891 0.2402 0.0032  -0.0059 0.0063  23  ALA A CB  
180  N  N   . LYS A 24  ? 0.1323 0.2034 0.2283 0.0262  -0.0303 -0.0031 24  LYS A N   
181  C  CA  . LYS A 24  ? 0.1428 0.2179 0.2189 0.0081  -0.0502 -0.0156 24  LYS A CA  
182  C  C   . LYS A 24  ? 0.1787 0.1960 0.2731 0.0277  -0.0234 -0.0326 24  LYS A C   
183  O  O   . LYS A 24  ? 0.1679 0.3006 0.2873 0.0122  -0.0359 -0.0425 24  LYS A O   
184  C  CB  . LYS A 24  ? 0.1442 0.2377 0.2449 0.0035  -0.0385 0.0251  24  LYS A CB  
185  C  CG  . LYS A 24  ? 0.1849 0.2533 0.2948 0.0399  -0.0138 0.0253  24  LYS A CG  
186  C  CD  . LYS A 24  ? 0.1784 0.3073 0.3723 0.0413  -0.0044 -0.0074 24  LYS A CD  
187  C  CE  . LYS A 24  ? 0.2884 0.3362 0.3365 0.1179  0.0098  0.0572  24  LYS A CE  
188  N  NZ  . LYS A 24  ? 0.3585 0.3041 0.4627 0.0768  0.0421  0.0359  24  LYS A NZ  
189  N  N   . GLY A 25  ? 0.1528 0.1759 0.2922 0.0159  -0.0032 -0.0589 25  GLY A N   
190  C  CA  . GLY A 25  ? 0.1393 0.2122 0.2499 0.0042  -0.0307 -0.0502 25  GLY A CA  
191  C  C   . GLY A 25  ? 0.1840 0.2061 0.2030 -0.0068 -0.0587 -0.0487 25  GLY A C   
192  O  O   . GLY A 25  ? 0.1557 0.2034 0.1917 0.0037  -0.0460 -0.0308 25  GLY A O   
193  N  N   . GLU A 26  ? 0.1672 0.2339 0.2117 0.0145  -0.0714 -0.0715 26  GLU A N   
194  C  CA  . GLU A 26  ? 0.1970 0.3152 0.1788 0.0311  -0.0427 -0.0894 26  GLU A CA  
195  C  C   . GLU A 26  ? 0.1816 0.2053 0.1490 0.0464  -0.0272 -0.0356 26  GLU A C   
196  O  O   . GLU A 26  ? 0.2143 0.2525 0.1421 -0.0058 -0.0353 -0.0463 26  GLU A O   
197  C  CB  . GLU A 26  ? 0.2373 0.3474 0.2448 0.0142  -0.0863 -0.1458 26  GLU A CB  
198  C  CG  . GLU A 26  ? 0.2377 0.4688 0.3923 -0.0036 -0.0892 -0.2112 26  GLU A CG  
199  C  CD  . GLU A 26  ? 0.4706 0.5746 0.2402 -0.0391 -0.1920 -0.0301 26  GLU A CD  
200  O  OE1 . GLU A 26  ? 0.4955 0.5328 0.3949 -0.1360 -0.1936 0.0478  26  GLU A OE1 
201  O  OE2 . GLU A 26  ? 0.4240 0.7536 0.4963 0.0234  -0.1664 0.0487  26  GLU A OE2 
202  N  N   . ARG A 27  ? 0.1518 0.1669 0.1542 0.0010  -0.0370 -0.0380 27  ARG A N   
203  C  CA  . ARG A 27  ? 0.1292 0.1694 0.1571 0.0070  -0.0359 -0.0627 27  ARG A CA  
204  C  C   . ARG A 27  ? 0.1234 0.1334 0.1400 0.0167  -0.0092 -0.0319 27  ARG A C   
205  O  O   . ARG A 27  ? 0.1291 0.1395 0.1583 0.0124  -0.0253 -0.0165 27  ARG A O   
206  C  CB  . ARG A 27  ? 0.2253 0.1795 0.1666 0.0423  0.0107  -0.0370 27  ARG A CB  
207  C  CG  . ARG A 27  ? 0.2020 0.2642 0.2495 -0.0039 -0.0672 -0.0121 27  ARG A CG  
208  C  CD  . ARG A 27  ? 0.2958 0.3065 0.3412 0.0751  -0.0722 0.0221  27  ARG A CD  
209  N  NE  . ARG A 27  ? 0.2610 0.1662 0.2762 0.0287  -0.0013 -0.0073 27  ARG A NE  
210  C  CZ  . ARG A 27  ? 0.2244 0.1413 0.1773 0.0378  0.0257  -0.0190 27  ARG A CZ  
211  N  NH1 . ARG A 27  ? 0.1436 0.2185 0.2353 0.0308  -0.0119 -0.1426 27  ARG A NH1 
212  N  NH2 . ARG A 27  ? 0.2093 0.2129 0.2702 -0.0215 -0.0043 -0.0980 27  ARG A NH2 
213  N  N   . GLN A 28  ? 0.1217 0.1187 0.1460 -0.0006 -0.0024 -0.0531 28  GLN A N   
214  C  CA  . GLN A 28  ? 0.0961 0.1269 0.1346 0.0114  -0.0184 -0.0501 28  GLN A CA  
215  C  C   . GLN A 28  ? 0.1038 0.0982 0.1382 0.0113  -0.0179 -0.0190 28  GLN A C   
216  O  O   . GLN A 28  ? 0.1319 0.1244 0.1310 0.0013  -0.0269 -0.0049 28  GLN A O   
217  C  CB  . GLN A 28  ? 0.0800 0.1298 0.1644 0.0060  0.0035  -0.0232 28  GLN A CB  
218  C  CG  . GLN A 28  ? 0.1269 0.1307 0.1653 -0.0196 -0.0217 -0.0128 28  GLN A CG  
219  C  CD  . GLN A 28  ? 0.1195 0.1298 0.1752 -0.0020 -0.0363 -0.0321 28  GLN A CD  
220  O  OE1 . GLN A 28  ? 0.1226 0.1403 0.1813 -0.0087 -0.0182 -0.0339 28  GLN A OE1 
221  N  NE2 . GLN A 28  ? 0.1181 0.1233 0.1903 -0.0041 -0.0217 -0.0190 28  GLN A NE2 
222  N  N   . SER A 29  ? 0.1003 0.1126 0.1339 0.0121  -0.0096 -0.0210 29  SER A N   
223  C  CA  . SER A 29  ? 0.1093 0.1003 0.1100 0.0051  -0.0241 -0.0181 29  SER A CA  
224  C  C   . SER A 29  ? 0.1129 0.0989 0.1158 0.0019  -0.0027 -0.0054 29  SER A C   
225  O  O   . SER A 29  ? 0.1104 0.1159 0.1439 0.0041  0.0070  -0.0179 29  SER A O   
226  C  CB  . SER A 29  ? 0.1052 0.1058 0.1229 0.0211  -0.0081 -0.0161 29  SER A CB  
227  O  OG  . SER A 29  ? 0.1120 0.0962 0.1405 0.0011  0.0002  -0.0274 29  SER A OG  
228  N  N   . PRO A 30  ? 0.1009 0.1044 0.1129 0.0025  -0.0015 -0.0103 30  PRO A N   
229  C  CA  . PRO A 30  ? 0.1219 0.1111 0.0989 -0.0174 0.0044  -0.0030 30  PRO A CA  
230  C  C   . PRO A 30  ? 0.1220 0.0698 0.1320 0.0027  -0.0031 0.0012  30  PRO A C   
231  O  O   . PRO A 30  ? 0.1305 0.1168 0.1208 0.0083  -0.0086 -0.0082 30  PRO A O   
232  C  CB  . PRO A 30  ? 0.0932 0.0957 0.1213 0.0069  0.0050  -0.0196 30  PRO A CB  
233  C  CG  . PRO A 30  ? 0.0925 0.1124 0.1208 0.0030  0.0152  0.0033  30  PRO A CG  
234  C  CD  . PRO A 30  ? 0.1156 0.1072 0.1036 -0.0084 0.0089  -0.0216 30  PRO A CD  
235  N  N   . VAL A 31  ? 0.1463 0.0831 0.1145 -0.0015 0.0051  0.0117  31  VAL A N   
236  C  CA  . VAL A 31  ? 0.1392 0.0917 0.1159 0.0183  0.0021  0.0173  31  VAL A CA  
237  C  C   . VAL A 31  ? 0.1368 0.1179 0.1031 0.0148  0.0003  0.0164  31  VAL A C   
238  O  O   . VAL A 31  ? 0.1356 0.1030 0.1382 0.0162  -0.0084 0.0240  31  VAL A O   
239  C  CB  . VAL A 31  ? 0.1159 0.1212 0.1384 0.0111  0.0027  -0.0077 31  VAL A CB  
240  C  CG1 . VAL A 31  ? 0.1587 0.1328 0.1474 -0.0216 -0.0053 0.0239  31  VAL A CG1 
241  C  CG2 . VAL A 31  ? 0.1298 0.1259 0.1467 0.0197  0.0211  -0.0095 31  VAL A CG2 
242  N  N   . ASP A 32  ? 0.1295 0.1220 0.1183 0.0201  0.0141  0.0362  32  ASP A N   
243  C  CA  . ASP A 32  ? 0.1497 0.0921 0.1363 0.0289  0.0244  0.0141  32  ASP A CA  
244  C  C   . ASP A 32  ? 0.1314 0.1025 0.1269 0.0190  0.0198  0.0247  32  ASP A C   
245  O  O   . ASP A 32  ? 0.1544 0.1561 0.1463 0.0188  -0.0013 0.0027  32  ASP A O   
246  C  CB  . ASP A 32  ? 0.1702 0.1045 0.1705 0.0301  -0.0225 0.0245  32  ASP A CB  
247  C  CG  . ASP A 32  ? 0.1978 0.1352 0.1226 -0.0114 0.0054  0.0075  32  ASP A CG  
248  O  OD1 . ASP A 32  ? 0.1842 0.1132 0.1352 0.0051  -0.0021 0.0252  32  ASP A OD1 
249  O  OD2 . ASP A 32  ? 0.2622 0.1571 0.1413 -0.0137 -0.0049 0.0372  32  ASP A OD2 
250  N  N   . ILE A 33  ? 0.1366 0.1023 0.1423 0.0194  -0.0034 0.0275  33  ILE A N   
251  C  CA  . ILE A 33  ? 0.1443 0.1265 0.1910 0.0477  0.0196  0.0397  33  ILE A CA  
252  C  C   . ILE A 33  ? 0.1783 0.1310 0.1600 0.0200  0.0099  0.0229  33  ILE A C   
253  O  O   . ILE A 33  ? 0.1901 0.1313 0.1791 0.0072  0.0324  0.0453  33  ILE A O   
254  C  CB  . ILE A 33  ? 0.1439 0.1240 0.1745 0.0264  0.0270  0.0374  33  ILE A CB  
255  C  CG1 . ILE A 33  ? 0.1574 0.1224 0.1597 0.0132  -0.0012 0.0388  33  ILE A CG1 
256  C  CG2 . ILE A 33  ? 0.1441 0.1400 0.1793 0.0290  0.0359  0.0424  33  ILE A CG2 
257  C  CD1 . ILE A 33  ? 0.1891 0.1905 0.1964 0.0392  -0.0334 0.0179  33  ILE A CD1 
258  N  N   . ASP A 34  ? 0.1865 0.1659 0.1382 0.0200  0.0251  0.0458  34  ASP A N   
259  C  CA  . ASP A 34  ? 0.1784 0.1816 0.2016 0.0132  0.0434  0.0732  34  ASP A CA  
260  C  C   . ASP A 34  ? 0.1991 0.1518 0.1583 0.0304  0.0399  0.0750  34  ASP A C   
261  O  O   . ASP A 34  ? 0.3164 0.1826 0.1781 0.0710  0.0620  0.0605  34  ASP A O   
262  C  CB  . ASP A 34  ? 0.2497 0.1794 0.2215 0.0074  -0.0177 0.0590  34  ASP A CB  
263  C  CG  . ASP A 34  ? 0.3252 0.2575 0.2575 -0.0640 -0.0249 0.1391  34  ASP A CG  
264  O  OD1 . ASP A 34  ? 0.3229 0.2523 0.2865 0.0616  0.0609  0.1518  34  ASP A OD1 
265  O  OD2 . ASP A 34  ? 0.5147 0.4263 0.3030 0.0164  -0.0710 0.0995  34  ASP A OD2 
266  N  N   . THR A 35  ? 0.2005 0.1917 0.2151 0.0297  0.0372  0.0976  35  THR A N   
267  C  CA  . THR A 35  ? 0.2201 0.2430 0.2396 0.0816  0.0853  0.0993  35  THR A CA  
268  C  C   . THR A 35  ? 0.2734 0.2427 0.2330 0.0656  0.0796  0.0469  35  THR A C   
269  O  O   . THR A 35  ? 0.3231 0.2373 0.2529 0.0665  0.1107  0.0317  35  THR A O   
270  C  CB  . THR A 35  ? 0.2465 0.2597 0.3204 0.0601  0.0785  0.1000  35  THR A CB  
271  O  OG1 . THR A 35  ? 0.2199 0.2588 0.3285 0.0239  0.0632  0.1316  35  THR A OG1 
272  C  CG2 . THR A 35  ? 0.2645 0.3545 0.3045 0.0983  0.0471  0.1047  35  THR A CG2 
273  N  N   . HIS A 36  ? 0.3758 0.2059 0.2294 0.0967  0.1490  0.0759  36  HIS A N   
274  C  CA  . HIS A 36  ? 0.4393 0.2215 0.1955 0.0796  0.1088  0.0829  36  HIS A CA  
275  C  C   . HIS A 36  ? 0.4862 0.3547 0.1996 0.0315  0.1190  0.0103  36  HIS A C   
276  O  O   . HIS A 36  ? 0.6463 0.4619 0.2735 0.1530  0.2037  0.0640  36  HIS A O   
277  C  CB  . HIS A 36  ? 0.5624 0.2009 0.2730 0.1033  0.1179  0.1015  36  HIS A CB  
278  C  CG  . HIS A 36  ? 0.5292 0.3423 0.2025 0.1119  -0.0013 0.1215  36  HIS A CG  
279  N  ND1 . HIS A 36  ? 0.7435 0.3929 0.1754 0.2381  -0.0341 0.1091  36  HIS A ND1 
280  C  CD2 . HIS A 36  ? 0.6585 0.2294 0.3125 -0.0891 -0.1379 0.0776  36  HIS A CD2 
281  C  CE1 . HIS A 36  ? 0.8405 0.2128 0.5636 0.1129  0.0143  0.0656  36  HIS A CE1 
282  N  NE2 . HIS A 36  ? 0.8856 0.4364 0.3229 0.1992  -0.0567 -0.0569 36  HIS A NE2 
283  N  N   . THR A 37  ? 0.4250 0.2041 0.2629 0.1129  0.1140  0.0649  37  THR A N   
284  C  CA  . THR A 37  ? 0.5796 0.2052 0.1747 0.1354  0.0959  0.0814  37  THR A CA  
285  C  C   . THR A 37  ? 0.3389 0.2452 0.1784 0.0995  0.0490  0.0465  37  THR A C   
286  O  O   . THR A 37  ? 0.6390 0.2777 0.2194 0.1016  0.0107  0.0402  37  THR A O   
287  C  CB  . THR A 37  ? 0.6725 0.3489 0.5856 0.1826  -0.0033 0.0305  37  THR A CB  
288  O  OG1 . THR A 37  ? 0.4927 0.8823 1.2473 0.2093  -0.0489 0.2886  37  THR A OG1 
289  C  CG2 . THR A 37  ? 0.3424 0.2685 0.5225 0.1296  0.0883  -0.0003 37  THR A CG2 
290  N  N   . ALA A 38  ? 0.3494 0.2125 0.1909 0.0701  0.0535  0.0747  38  ALA A N   
291  C  CA  . ALA A 38  ? 0.3716 0.2545 0.1465 0.1173  0.0801  0.0901  38  ALA A CA  
292  C  C   . ALA A 38  ? 0.3869 0.2348 0.2402 0.0820  0.1329  0.0919  38  ALA A C   
293  O  O   . ALA A 38  ? 0.4750 0.2616 0.3957 0.0864  0.2512  0.0871  38  ALA A O   
294  C  CB  . ALA A 38  ? 0.2454 0.1999 0.2152 0.0529  0.0365  0.0496  38  ALA A CB  
295  N  N   . LYS A 39  ? 0.3764 0.2423 0.2264 0.1401  0.0280  0.0775  39  LYS A N   
296  C  CA  . LYS A 39  ? 0.3483 0.3592 0.2327 0.1949  -0.0060 0.0120  39  LYS A CA  
297  C  C   . LYS A 39  ? 0.2232 0.2584 0.1657 0.0545  0.0358  0.0261  39  LYS A C   
298  O  O   . LYS A 39  ? 0.2372 0.2476 0.1423 0.0441  0.0367  0.0261  39  LYS A O   
299  C  CB  . LYS A 39  ? 0.4349 0.5243 0.2794 0.2285  -0.1177 -0.0522 39  LYS A CB  
300  C  CG  . LYS A 39  ? 0.6196 0.7858 0.2772 0.2613  -0.0164 -0.1267 39  LYS A CG  
301  C  CD  . LYS A 39  ? 0.2509 0.6113 0.3776 0.2246  0.0801  0.0718  39  LYS A CD  
302  C  CE  . LYS A 39  ? 0.6503 0.6077 0.2412 0.2133  0.0099  -0.0023 39  LYS A CE  
303  N  NZ  . LYS A 39  ? 0.3782 0.7952 0.3225 0.2570  0.0536  0.1437  39  LYS A NZ  
304  N  N   . TYR A 40  ? 0.3036 0.2803 0.1750 -0.0157 0.0479  0.0226  40  TYR A N   
305  C  CA  . TYR A 40  ? 0.2728 0.3012 0.1715 -0.0288 0.0773  -0.0138 40  TYR A CA  
306  C  C   . TYR A 40  ? 0.2253 0.2900 0.1496 -0.0476 0.0588  -0.0144 40  TYR A C   
307  O  O   . TYR A 40  ? 0.2567 0.4039 0.1384 0.0569  0.0364  -0.0016 40  TYR A O   
308  C  CB  . TYR A 40  ? 0.3352 0.3626 0.1666 -0.0875 0.0721  0.0431  40  TYR A CB  
309  C  CG  . TYR A 40  ? 0.2924 0.5392 0.2522 -0.0967 0.0995  -0.0116 40  TYR A CG  
310  C  CD1 . TYR A 40  ? 0.2808 0.4478 0.2084 -0.1226 0.0458  -0.0662 40  TYR A CD1 
311  C  CD2 . TYR A 40  ? 0.4225 0.7996 0.2450 -0.0003 0.1437  0.0013  40  TYR A CD2 
312  C  CE1 . TYR A 40  ? 0.2599 0.6922 0.2656 -0.0526 0.0344  -0.0286 40  TYR A CE1 
313  C  CE2 . TYR A 40  ? 0.4375 0.8872 0.3563 0.0324  0.0756  -0.0797 40  TYR A CE2 
314  C  CZ  . TYR A 40  ? 0.3301 0.8448 0.3370 -0.0988 0.1142  -0.0671 40  TYR A CZ  
315  O  OH  . TYR A 40  ? 0.3810 0.8040 0.5723 0.0990  -0.0399 -0.1463 40  TYR A OH  
316  N  N   . ASP A 41  ? 0.2189 0.2746 0.1644 0.0317  0.0510  -0.0247 41  ASP A N   
317  C  CA  . ASP A 41  ? 0.2370 0.2719 0.1632 0.0255  0.0388  -0.0330 41  ASP A CA  
318  C  C   . ASP A 41  ? 0.3062 0.4522 0.1851 0.1020  0.0004  -0.0395 41  ASP A C   
319  O  O   . ASP A 41  ? 0.2470 0.2909 0.2353 0.0497  0.0479  0.0220  41  ASP A O   
320  C  CB  . ASP A 41  ? 0.2673 0.2292 0.2609 -0.0026 -0.0055 0.0015  41  ASP A CB  
321  C  CG  . ASP A 41  ? 0.4160 0.3159 0.3160 -0.0214 -0.0205 -0.1161 41  ASP A CG  
322  O  OD1 . ASP A 41  ? 0.4259 0.2884 0.2928 0.0575  -0.0307 -0.0939 41  ASP A OD1 
323  O  OD2 . ASP A 41  ? 0.3996 0.2852 0.4513 -0.0389 -0.1113 -0.0209 41  ASP A OD2 
324  N  N   . PRO A 42  ? 0.2948 0.5457 0.1905 0.1659  0.0095  -0.0251 42  PRO A N   
325  C  CA  . PRO A 42  ? 0.2590 0.6014 0.2365 0.1207  0.0639  0.0827  42  PRO A CA  
326  C  C   . PRO A 42  ? 0.5231 0.5610 0.2579 0.1007  0.0476  -0.0351 42  PRO A C   
327  O  O   . PRO A 42  ? 0.4286 0.9526 0.3820 0.1791  0.0489  0.0129  42  PRO A O   
328  C  CB  . PRO A 42  ? 0.4131 0.7298 0.2384 0.2435  0.1508  0.0858  42  PRO A CB  
329  C  CG  . PRO A 42  ? 0.4130 0.5430 0.3216 0.2561  0.0824  -0.0313 42  PRO A CG  
330  C  CD  . PRO A 42  ? 0.4595 0.6293 0.1553 0.2567  0.1356  0.0232  42  PRO A CD  
331  N  N   . SER A 43  ? 0.3783 0.4218 0.2526 0.2191  0.0298  0.0096  43  SER A N   
332  C  CA  . SER A 43  ? 0.5969 0.3552 0.2720 0.2482  -0.0402 -0.0713 43  SER A CA  
333  C  C   . SER A 43  ? 0.4111 0.4553 0.2935 0.2229  0.0179  -0.0260 43  SER A C   
334  O  O   . SER A 43  ? 0.6645 0.4794 0.4563 0.2377  -0.1065 0.0019  43  SER A O   
335  C  CB  . SER A 43  ? 0.5898 0.4515 0.2592 0.2178  -0.1085 -0.0744 43  SER A CB  
336  O  OG  . SER A 43  ? 0.5158 0.3245 0.6940 0.0179  -0.1329 -0.2054 43  SER A OG  
337  N  N   . LEU A 44  ? 0.4173 0.4093 0.2420 0.1664  -0.0060 -0.0125 44  LEU A N   
338  C  CA  . LEU A 44  ? 0.2614 0.4081 0.2634 0.0411  0.0015  0.0784  44  LEU A CA  
339  C  C   . LEU A 44  ? 0.2272 0.7009 0.3721 -0.0059 0.0259  0.1521  44  LEU A C   
340  O  O   . LEU A 44  ? 0.2662 0.7910 0.2791 -0.0335 0.0106  0.1744  44  LEU A O   
341  C  CB  . LEU A 44  ? 0.2555 0.4484 0.2755 -0.0435 -0.0036 -0.0118 44  LEU A CB  
342  C  CG  . LEU A 44  ? 0.2716 0.2775 0.2232 0.0119  0.0195  0.0778  44  LEU A CG  
343  C  CD1 . LEU A 44  ? 0.2359 0.3075 0.2654 -0.0149 0.0352  0.0016  44  LEU A CD1 
344  C  CD2 . LEU A 44  ? 0.2120 0.2536 0.2420 -0.0221 0.0044  0.0302  44  LEU A CD2 
345  N  N   . LYS A 45  ? 0.2502 0.7995 0.3391 0.0511  -0.0310 0.1914  45  LYS A N   
346  C  CA  . LYS A 45  ? 0.3373 0.2785 0.5260 0.0149  -0.1278 -0.0701 45  LYS A CA  
347  C  C   . LYS A 45  ? 0.3030 0.5173 0.2889 0.1038  -0.1198 0.0292  45  LYS A C   
348  O  O   . LYS A 45  ? 0.2095 0.8090 0.3932 -0.0036 0.0234  -0.2474 45  LYS A O   
349  C  CB  . LYS A 45  ? 0.4670 0.3364 0.2278 0.1835  0.1278  -0.0365 45  LYS A CB  
350  C  CG  . LYS A 45  ? 0.2611 0.5044 0.3064 -0.0020 0.0107  -0.0574 45  LYS A CG  
351  C  CD  . LYS A 45  ? 0.3243 0.4811 0.5340 -0.1184 0.0177  -0.0702 45  LYS A CD  
352  C  CE  . LYS A 45  ? 0.5947 0.5432 0.5763 0.0011  -0.1612 -0.1254 45  LYS A CE  
353  N  N   . PRO A 46  ? 0.2492 0.3859 0.3754 -0.0156 -0.0321 -0.0154 46  PRO A N   
354  C  CA  . PRO A 46  ? 0.2434 0.6982 0.1952 -0.1351 0.0098  0.0643  46  PRO A CA  
355  C  C   . PRO A 46  ? 0.1772 0.5420 0.1791 -0.0077 0.0201  0.0163  46  PRO A C   
356  O  O   . PRO A 46  ? 0.1669 0.5359 0.3766 -0.0693 -0.0166 0.1050  46  PRO A O   
357  C  CB  . PRO A 46  ? 0.2402 0.4824 0.3209 -0.0083 0.0051  -0.0688 46  PRO A CB  
358  C  CG  . PRO A 46  ? 0.2154 0.6738 0.4057 -0.0453 0.0985  -0.1274 46  PRO A CG  
359  C  CD  . PRO A 46  ? 0.3540 0.5641 0.3842 0.1630  -0.0998 -0.2395 46  PRO A CD  
360  N  N   . LEU A 47  ? 0.2570 0.4957 0.2580 -0.0049 -0.0550 0.0333  47  LEU A N   
361  C  CA  . LEU A 47  ? 0.1841 0.3968 0.3676 -0.0353 -0.0057 0.0915  47  LEU A CA  
362  C  C   . LEU A 47  ? 0.1963 0.2663 0.5062 -0.0636 -0.0523 0.1425  47  LEU A C   
363  O  O   . LEU A 47  ? 0.1996 0.3360 0.4739 -0.0770 -0.0591 0.2293  47  LEU A O   
364  C  CB  . LEU A 47  ? 0.4527 0.3128 0.5441 0.0147  -0.0655 0.1680  47  LEU A CB  
365  C  CG  . LEU A 47  ? 0.3339 0.4715 0.5583 -0.0303 -0.1567 0.0070  47  LEU A CG  
366  C  CD1 . LEU A 47  ? 0.1648 0.2984 0.6092 -0.0675 -0.0809 0.0253  47  LEU A CD1 
367  C  CD2 . LEU A 47  ? 0.3150 0.2347 0.7846 -0.0553 -0.1811 0.0423  47  LEU A CD2 
368  N  N   . SER A 48  ? 0.1179 0.2444 0.2750 0.0079  -0.0016 0.0837  48  SER A N   
369  C  CA  . SER A 48  ? 0.1098 0.1996 0.2688 -0.0029 0.0088  0.0398  48  SER A CA  
370  C  C   . SER A 48  ? 0.1040 0.1880 0.2764 -0.0025 0.0277  0.0326  48  SER A C   
371  O  O   . SER A 48  ? 0.1367 0.2145 0.2663 -0.0475 0.0293  -0.0038 48  SER A O   
372  C  CB  . SER A 48  ? 0.1769 0.1877 0.2717 0.0282  0.0128  0.0623  48  SER A CB  
373  O  OG  . SER A 48  ? 0.2078 0.2870 0.3492 0.0398  -0.0199 0.0842  48  SER A OG  
374  N  N   . VAL A 49  ? 0.1802 0.2078 0.2545 -0.0522 0.0271  0.0414  49  VAL A N   
375  C  CA  . VAL A 49  ? 0.1772 0.1962 0.2420 -0.0882 0.0318  -0.0302 49  VAL A CA  
376  C  C   . VAL A 49  ? 0.2124 0.2830 0.2705 -0.1060 0.0293  0.0244  49  VAL A C   
377  O  O   . VAL A 49  ? 0.2376 0.4009 0.3523 -0.1574 0.0212  0.0133  49  VAL A O   
378  C  CB  . VAL A 49  ? 0.3176 0.2039 0.2936 -0.0474 0.0450  0.0002  49  VAL A CB  
379  C  CG1 . VAL A 49  ? 0.3625 0.2739 0.3245 -0.0779 0.0986  -0.0577 49  VAL A CG1 
380  C  CG2 . VAL A 49  ? 0.2539 0.2524 0.3456 -0.0331 0.0401  0.0025  49  VAL A CG2 
381  N  N   . SER A 50  ? 0.1711 0.2323 0.2804 -0.0308 0.0294  0.0215  50  SER A N   
382  C  CA  . SER A 50  ? 0.1540 0.2596 0.3261 -0.0016 -0.0039 -0.0186 50  SER A CA  
383  C  C   . SER A 50  ? 0.1122 0.1957 0.2914 -0.0118 -0.0137 -0.0127 50  SER A C   
384  O  O   . SER A 50  ? 0.1488 0.2297 0.2791 -0.0483 -0.0137 0.0229  50  SER A O   
385  C  CB  . SER A 50  ? 0.2461 0.2984 0.3409 -0.0134 0.0574  -0.0690 50  SER A CB  
386  O  OG  . SER A 50  ? 0.2764 0.5256 0.4161 -0.0289 0.0677  -0.0817 50  SER A OG  
387  N  N   . TYR A 51  ? 0.1820 0.2190 0.2645 -0.0231 -0.0080 -0.0089 51  TYR A N   
388  C  CA  . TYR A 51  ? 0.1855 0.1980 0.2187 0.0089  -0.0260 0.0388  51  TYR A CA  
389  C  C   . TYR A 51  ? 0.2110 0.2114 0.2414 0.0209  -0.0085 0.0927  51  TYR A C   
390  O  O   . TYR A 51  ? 0.1963 0.2820 0.2503 -0.0127 -0.0353 0.0706  51  TYR A O   
391  C  CB  . TYR A 51  ? 0.1691 0.2027 0.2194 0.0057  -0.0557 0.0296  51  TYR A CB  
392  C  CG  . TYR A 51  ? 0.1659 0.1421 0.2451 -0.0279 -0.0600 0.0488  51  TYR A CG  
393  C  CD1 . TYR A 51  ? 0.1497 0.1496 0.2965 -0.0287 -0.0314 0.0087  51  TYR A CD1 
394  C  CD2 . TYR A 51  ? 0.1356 0.1542 0.2045 0.0005  -0.0039 0.0201  51  TYR A CD2 
395  C  CE1 . TYR A 51  ? 0.1344 0.1398 0.2462 0.0018  -0.0068 0.0356  51  TYR A CE1 
396  C  CE2 . TYR A 51  ? 0.1524 0.1686 0.1984 -0.0604 -0.0445 0.0293  51  TYR A CE2 
397  C  CZ  . TYR A 51  ? 0.1233 0.1309 0.2114 -0.0319 -0.0194 0.0251  51  TYR A CZ  
398  O  OH  . TYR A 51  ? 0.1500 0.1447 0.2253 -0.0124 -0.0468 0.0121  51  TYR A OH  
399  N  N   A ASP A 52  ? 0.1729 0.2992 0.3657 -0.0025 -0.0176 0.0489  52  ASP A N   
400  N  N   B ASP A 52  ? 0.1783 0.3213 0.3423 0.0129  -0.0228 0.0826  52  ASP A N   
401  C  CA  A ASP A 52  ? 0.1788 0.3677 0.3301 -0.0267 0.0044  0.0495  52  ASP A CA  
402  C  CA  B ASP A 52  ? 0.2693 0.3414 0.3181 0.0681  -0.0328 0.1366  52  ASP A CA  
403  C  C   A ASP A 52  ? 0.1436 0.3991 0.2981 0.0065  0.0154  0.0234  52  ASP A C   
404  C  C   B ASP A 52  ? 0.1820 0.3637 0.3189 0.0113  -0.0015 0.0649  52  ASP A C   
405  O  O   A ASP A 52  ? 0.3133 0.2737 0.3326 0.0425  -0.0464 0.0012  52  ASP A O   
406  O  O   B ASP A 52  ? 0.3411 0.3262 0.3262 0.0051  -0.0377 0.1024  52  ASP A O   
407  C  CB  A ASP A 52  ? 0.1016 0.4012 0.3488 -0.0345 -0.0231 0.0134  52  ASP A CB  
408  C  CB  B ASP A 52  ? 0.2311 0.3927 0.3666 0.0434  0.0214  0.1538  52  ASP A CB  
409  C  CG  A ASP A 52  ? 0.1791 0.3646 0.4006 -0.0301 -0.0087 -0.0203 52  ASP A CG  
410  C  CG  B ASP A 52  ? 0.2579 0.4701 0.3743 0.0983  0.0260  0.1676  52  ASP A CG  
411  O  OD1 A ASP A 52  ? 0.1374 0.3912 0.4200 0.0201  0.0302  -0.0104 52  ASP A OD1 
412  O  OD1 B ASP A 52  ? 0.2795 0.4967 0.3838 0.1659  -0.0115 0.1316  52  ASP A OD1 
413  O  OD2 A ASP A 52  ? 0.3735 0.4645 0.4835 0.0350  -0.1399 0.0627  52  ASP A OD2 
414  O  OD2 B ASP A 52  ? 0.5687 0.5109 0.5820 0.2285  0.0653  0.1420  52  ASP A OD2 
415  N  N   . GLN A 53  ? 0.1619 0.3010 0.3878 0.0300  -0.0002 0.0790  53  GLN A N   
416  C  CA  . GLN A 53  ? 0.2229 0.3263 0.4193 0.0294  0.0561  0.0784  53  GLN A CA  
417  C  C   . GLN A 53  ? 0.2427 0.2669 0.3449 0.0930  0.0368  0.0658  53  GLN A C   
418  O  O   . GLN A 53  ? 0.2544 0.3449 0.2906 -0.0247 -0.0712 0.0731  53  GLN A O   
419  C  CB  . GLN A 53  ? 0.4207 0.3891 0.6792 0.1797  0.1430  -0.0040 53  GLN A CB  
420  C  CG  . GLN A 53  ? 0.4354 0.6321 0.9985 0.0659  0.3240  0.1676  53  GLN A CG  
421  C  CD  . GLN A 53  ? 0.4806 0.8810 1.0153 0.1805  0.1014  0.1634  53  GLN A CD  
422  O  OE1 . GLN A 53  ? 0.8374 1.0819 1.0300 0.3362  0.3050  0.3039  53  GLN A OE1 
423  N  NE2 . GLN A 53  ? 0.7590 1.1734 0.8556 -0.0055 0.0610  0.3319  53  GLN A NE2 
424  N  N   . ALA A 54  ? 0.1791 0.1751 0.3565 -0.0016 -0.0212 0.0144  54  ALA A N   
425  C  CA  . ALA A 54  ? 0.1851 0.1407 0.2995 0.0127  -0.0107 -0.0212 54  ALA A CA  
426  C  C   . ALA A 54  ? 0.2388 0.2043 0.2850 -0.0247 -0.0284 -0.0442 54  ALA A C   
427  O  O   . ALA A 54  ? 0.2316 0.3761 0.3364 -0.0653 -0.0485 -0.0974 54  ALA A O   
428  C  CB  . ALA A 54  ? 0.2556 0.1578 0.2812 0.0068  -0.0035 0.0197  54  ALA A CB  
429  N  N   . THR A 55  ? 0.1892 0.1701 0.2523 0.0048  -0.0414 0.0659  55  THR A N   
430  C  CA  . THR A 55  ? 0.1969 0.2181 0.2759 0.0139  -0.0675 0.1015  55  THR A CA  
431  C  C   . THR A 55  ? 0.2154 0.1571 0.1644 0.0004  -0.0705 0.0422  55  THR A C   
432  O  O   . THR A 55  ? 0.2214 0.1320 0.2103 -0.0087 -0.0639 0.0612  55  THR A O   
433  C  CB  . THR A 55  ? 0.2597 0.2097 0.3269 0.0061  -0.0339 0.0851  55  THR A CB  
434  O  OG1 . THR A 55  ? 0.3403 0.2365 0.5933 0.0512  -0.1891 0.0279  55  THR A OG1 
435  C  CG2 . THR A 55  ? 0.4750 0.3172 0.3360 0.1339  -0.0436 0.1549  55  THR A CG2 
436  N  N   . SER A 56  ? 0.2050 0.1558 0.2028 0.0141  -0.0473 0.0266  56  SER A N   
437  C  CA  . SER A 56  ? 0.2014 0.1226 0.1776 -0.0054 -0.0294 0.0250  56  SER A CA  
438  C  C   . SER A 56  ? 0.2437 0.1607 0.1826 0.0265  -0.0522 0.0387  56  SER A C   
439  O  O   . SER A 56  ? 0.2654 0.1640 0.2104 0.0008  -0.0850 0.0648  56  SER A O   
440  C  CB  . SER A 56  ? 0.2918 0.1380 0.1486 -0.0163 -0.0709 -0.0053 56  SER A CB  
441  O  OG  . SER A 56  ? 0.2820 0.1647 0.2025 -0.0288 -0.1037 0.0410  56  SER A OG  
442  N  N   . LEU A 57  ? 0.2220 0.1414 0.1754 0.0473  -0.0378 0.0611  57  LEU A N   
443  C  CA  . LEU A 57  ? 0.3418 0.1571 0.2179 0.0116  0.0227  0.0752  57  LEU A CA  
444  C  C   . LEU A 57  ? 0.2598 0.2304 0.1431 0.0435  -0.0160 0.0639  57  LEU A C   
445  O  O   . LEU A 57  ? 0.3094 0.1743 0.1590 0.0061  -0.0519 0.0424  57  LEU A O   
446  C  CB  . LEU A 57  ? 0.3185 0.1643 0.3296 -0.0234 0.0409  0.0737  57  LEU A CB  
447  C  CG  . LEU A 57  ? 0.4482 0.1799 0.2740 0.0239  -0.0240 0.0509  57  LEU A CG  
448  C  CD1 . LEU A 57  ? 0.6315 0.2005 0.3252 -0.1331 0.0573  0.0312  57  LEU A CD1 
449  C  CD2 . LEU A 57  ? 0.6595 0.1948 0.4006 0.0634  -0.2001 0.0132  57  LEU A CD2 
450  N  N   . ARG A 58  ? 0.2319 0.1684 0.1626 0.0144  -0.0406 0.0154  58  ARG A N   
451  C  CA  . ARG A 58  ? 0.2067 0.1465 0.1773 0.0203  -0.0278 0.0598  58  ARG A CA  
452  C  C   . ARG A 58  ? 0.2485 0.1174 0.1557 -0.0071 -0.0330 0.0238  58  ARG A C   
453  O  O   . ARG A 58  ? 0.3082 0.1777 0.1262 0.0288  -0.0263 0.0175  58  ARG A O   
454  C  CB  . ARG A 58  ? 0.2703 0.1793 0.2678 -0.0034 0.0030  0.1175  58  ARG A CB  
455  C  CG  . ARG A 58  ? 0.2914 0.2415 0.3195 -0.0621 0.0776  0.1008  58  ARG A CG  
456  C  CD  . ARG A 58  ? 0.2828 0.2734 0.2391 -0.0825 -0.0245 0.0414  58  ARG A CD  
457  N  NE  . ARG A 58  ? 0.2049 0.2020 0.2547 -0.0226 -0.0141 0.0304  58  ARG A NE  
458  C  CZ  . ARG A 58  ? 0.2016 0.2398 0.2179 -0.0751 0.0065  0.0446  58  ARG A CZ  
459  N  NH1 . ARG A 58  ? 0.2966 0.2211 0.2759 -0.0816 0.0631  0.0653  58  ARG A NH1 
460  N  NH2 . ARG A 58  ? 0.1988 0.2086 0.2409 -0.0282 0.0001  0.0247  58  ARG A NH2 
461  N  N   . ILE A 59  ? 0.2347 0.1152 0.1328 -0.0044 -0.0195 0.0198  59  ILE A N   
462  C  CA  . ILE A 59  ? 0.2139 0.1053 0.1569 0.0029  0.0031  0.0351  59  ILE A CA  
463  C  C   . ILE A 59  ? 0.2122 0.1495 0.1061 -0.0005 -0.0080 0.0277  59  ILE A C   
464  O  O   . ILE A 59  ? 0.2678 0.1848 0.1082 0.0029  0.0061  0.0399  59  ILE A O   
465  C  CB  . ILE A 59  ? 0.2280 0.1377 0.1183 -0.0233 -0.0331 0.0353  59  ILE A CB  
466  C  CG1 . ILE A 59  ? 0.2305 0.1529 0.1165 -0.0211 -0.0252 0.0436  59  ILE A CG1 
467  C  CG2 . ILE A 59  ? 0.2841 0.1723 0.1248 0.0116  -0.0529 0.0293  59  ILE A CG2 
468  C  CD1 . ILE A 59  ? 0.2808 0.1410 0.1920 -0.0311 -0.0747 0.0441  59  ILE A CD1 
469  N  N   . LEU A 60  ? 0.1923 0.1870 0.1342 -0.0319 -0.0212 0.0310  60  LEU A N   
470  C  CA  . LEU A 60  ? 0.1751 0.1479 0.1217 -0.0006 -0.0256 0.0187  60  LEU A CA  
471  C  C   . LEU A 60  ? 0.2077 0.1468 0.1083 -0.0032 -0.0218 0.0033  60  LEU A C   
472  O  O   . LEU A 60  ? 0.1641 0.1813 0.1199 -0.0148 -0.0072 0.0334  60  LEU A O   
473  C  CB  . LEU A 60  ? 0.2254 0.1110 0.2120 -0.0250 -0.0037 0.0282  60  LEU A CB  
474  C  CG  . LEU A 60  ? 0.2518 0.1701 0.1619 -0.0572 -0.0332 0.0219  60  LEU A CG  
475  C  CD1 . LEU A 60  ? 0.2964 0.1640 0.1694 -0.0558 -0.0060 0.0031  60  LEU A CD1 
476  C  CD2 . LEU A 60  ? 0.2357 0.1192 0.2116 -0.0335 -0.0201 0.0049  60  LEU A CD2 
477  N  N   . ASN A 61  ? 0.1964 0.1172 0.1345 -0.0136 -0.0072 -0.0032 61  ASN A N   
478  C  CA  . ASN A 61  ? 0.1659 0.1306 0.1284 -0.0179 0.0242  -0.0132 61  ASN A CA  
479  C  C   . ASN A 61  ? 0.1942 0.1309 0.1574 -0.0324 0.0182  0.0069  61  ASN A C   
480  O  O   . ASN A 61  ? 0.2059 0.1399 0.1380 -0.0399 0.0170  0.0170  61  ASN A O   
481  C  CB  . ASN A 61  ? 0.2161 0.1249 0.1181 -0.0002 0.0368  0.0030  61  ASN A CB  
482  C  CG  . ASN A 61  ? 0.1838 0.1292 0.1141 -0.0264 0.0024  0.0212  61  ASN A CG  
483  O  OD1 . ASN A 61  ? 0.2154 0.1532 0.1443 -0.0271 -0.0052 0.0179  61  ASN A OD1 
484  N  ND2 . ASN A 61  ? 0.2578 0.1316 0.1442 -0.0399 0.0264  0.0026  61  ASN A ND2 
485  N  N   . THR A 62  ? 0.2048 0.1499 0.1432 -0.0584 -0.0146 0.0250  62  THR A N   
486  C  CA  . THR A 62  ? 0.2045 0.1420 0.1328 -0.0359 -0.0149 0.0084  62  THR A CA  
487  C  C   . THR A 62  ? 0.2060 0.1346 0.1615 -0.0286 0.0232  0.0285  62  THR A C   
488  O  O   . THR A 62  ? 0.2301 0.1820 0.2056 -0.0584 0.0008  0.0237  62  THR A O   
489  C  CB  . THR A 62  ? 0.2325 0.1393 0.1335 -0.0278 -0.0058 0.0241  62  THR A CB  
490  O  OG1 . THR A 62  ? 0.1992 0.1324 0.1562 -0.0243 0.0057  0.0186  62  THR A OG1 
491  C  CG2 . THR A 62  ? 0.2657 0.1470 0.1682 0.0152  -0.0234 -0.0020 62  THR A CG2 
492  N  N   . GLY A 63  ? 0.1923 0.1434 0.1233 -0.0288 0.0339  0.0241  63  GLY A N   
493  C  CA  . GLY A 63  ? 0.1888 0.1629 0.1267 -0.0336 0.0351  0.0168  63  GLY A CA  
494  C  C   . GLY A 63  ? 0.1914 0.1524 0.1418 -0.0428 0.0368  0.0051  63  GLY A C   
495  O  O   . GLY A 63  ? 0.2053 0.1709 0.1628 -0.0297 0.0152  -0.0006 63  GLY A O   
496  N  N   A TYR A 64  ? 0.1773 0.1668 0.1076 -0.0274 0.0188  0.0231  64  TYR A N   
497  N  N   B TYR A 64  ? 0.1751 0.1903 0.1119 -0.0273 0.0199  0.0189  64  TYR A N   
498  C  CA  A TYR A 64  ? 0.1970 0.1502 0.1298 -0.0578 0.0043  0.0410  64  TYR A CA  
499  C  CA  B TYR A 64  ? 0.1941 0.1787 0.1079 -0.0534 0.0074  0.0113  64  TYR A CA  
500  C  C   A TYR A 64  ? 0.1726 0.1014 0.1459 -0.0237 0.0218  0.0384  64  TYR A C   
501  C  C   B TYR A 64  ? 0.1698 0.1237 0.1481 -0.0200 0.0122  0.0156  64  TYR A C   
502  O  O   A TYR A 64  ? 0.1302 0.1510 0.2722 -0.0256 0.0218  0.1197  64  TYR A O   
503  O  O   B TYR A 64  ? 0.1960 0.1805 0.1776 -0.0036 -0.0164 0.0643  64  TYR A O   
504  C  CB  A TYR A 64  ? 0.2183 0.1885 0.1446 -0.0075 0.0098  -0.0001 64  TYR A CB  
505  C  CB  B TYR A 64  ? 0.1659 0.1709 0.1486 -0.0279 -0.0011 -0.0216 64  TYR A CB  
506  C  CG  A TYR A 64  ? 0.2574 0.1745 0.1357 -0.0629 -0.0244 0.0006  64  TYR A CG  
507  C  CG  B TYR A 64  ? 0.1982 0.1951 0.2312 0.0192  0.0152  -0.0206 64  TYR A CG  
508  C  CD1 A TYR A 64  ? 0.2345 0.2493 0.2088 -0.0431 -0.0381 0.0031  64  TYR A CD1 
509  C  CD1 B TYR A 64  ? 0.0502 0.3040 0.2339 -0.0325 0.0341  -0.0735 64  TYR A CD1 
510  C  CD2 A TYR A 64  ? 0.1260 0.1698 0.2381 -0.0713 -0.0446 -0.0009 64  TYR A CD2 
511  C  CD2 B TYR A 64  ? 0.2934 0.2512 0.2138 0.0238  0.0870  -0.0691 64  TYR A CD2 
512  C  CE1 A TYR A 64  ? 0.2159 0.2613 0.1518 -0.0245 -0.0064 -0.0369 64  TYR A CE1 
513  C  CE1 B TYR A 64  ? 0.2412 0.3413 0.2170 0.0144  -0.0129 -0.0987 64  TYR A CE1 
514  C  CE2 A TYR A 64  ? 0.1492 0.2147 0.3284 -0.1057 0.0163  -0.0069 64  TYR A CE2 
515  C  CE2 B TYR A 64  ? 0.2467 0.1757 0.1898 -0.0365 0.1268  -0.0998 64  TYR A CE2 
516  C  CZ  A TYR A 64  ? 0.2611 0.2836 0.2438 -0.0165 0.0071  0.0197  64  TYR A CZ  
517  C  CZ  B TYR A 64  ? 0.3098 0.2088 0.1960 -0.0138 0.0765  0.0036  64  TYR A CZ  
518  O  OH  A TYR A 64  ? 0.2333 0.3869 0.3684 0.0162  0.0052  0.1082  64  TYR A OH  
519  O  OH  B TYR A 64  ? 0.3798 0.1745 0.2551 -0.0332 0.0087  -0.0293 64  TYR A OH  
520  N  N   . LEU A 65  ? 0.1740 0.1195 0.1461 -0.0243 0.0064  0.0043  65  LEU A N   
521  C  CA  . LEU A 65  ? 0.1669 0.1332 0.1307 -0.0135 0.0125  0.0151  65  LEU A CA  
522  C  C   . LEU A 65  ? 0.1890 0.1313 0.1018 -0.0267 0.0027  0.0051  65  LEU A C   
523  O  O   . LEU A 65  ? 0.1769 0.1335 0.1339 -0.0277 0.0167  0.0132  65  LEU A O   
524  C  CB  . LEU A 65  ? 0.1935 0.1691 0.1134 -0.0108 -0.0074 0.0190  65  LEU A CB  
525  C  CG  . LEU A 65  ? 0.1996 0.1845 0.1134 0.0021  0.0080  -0.0113 65  LEU A CG  
526  C  CD1 . LEU A 65  ? 0.2344 0.1342 0.1518 -0.0170 -0.0057 -0.0316 65  LEU A CD1 
527  C  CD2 . LEU A 65  ? 0.2452 0.3741 0.1185 0.0331  0.0282  -0.0100 65  LEU A CD2 
528  N  N   . PHE A 66  ? 0.1877 0.1037 0.1432 -0.0212 -0.0153 -0.0122 66  PHE A N   
529  C  CA  . PHE A 66  ? 0.1838 0.1348 0.0982 -0.0148 0.0051  0.0110  66  PHE A CA  
530  C  C   . PHE A 66  ? 0.1909 0.1208 0.0897 -0.0182 -0.0214 0.0065  66  PHE A C   
531  O  O   . PHE A 66  ? 0.1878 0.1525 0.1117 -0.0436 -0.0025 0.0147  66  PHE A O   
532  C  CB  . PHE A 66  ? 0.1899 0.1711 0.1192 -0.0583 0.0151  -0.0015 66  PHE A CB  
533  C  CG  . PHE A 66  ? 0.1908 0.1404 0.0935 -0.0435 0.0044  -0.0035 66  PHE A CG  
534  C  CD1 . PHE A 66  ? 0.1848 0.2016 0.1086 -0.0435 -0.0223 -0.0102 66  PHE A CD1 
535  C  CD2 . PHE A 66  ? 0.1937 0.1270 0.1592 -0.0363 -0.0209 -0.0190 66  PHE A CD2 
536  C  CE1 . PHE A 66  ? 0.1835 0.1346 0.1705 -0.0186 -0.0258 0.0125  66  PHE A CE1 
537  C  CE2 . PHE A 66  ? 0.1833 0.1206 0.1533 -0.0320 -0.0379 -0.0097 66  PHE A CE2 
538  C  CZ  . PHE A 66  ? 0.1729 0.1223 0.1499 -0.0229 -0.0337 -0.0044 66  PHE A CZ  
539  N  N   . GLN A 67  ? 0.1723 0.1447 0.1314 0.0002  0.0000  0.0515  67  GLN A N   
540  C  CA  . GLN A 67  ? 0.1806 0.1600 0.1565 0.0300  -0.0321 0.0026  67  GLN A CA  
541  C  C   . GLN A 67  ? 0.2014 0.1256 0.0982 0.0114  -0.0199 0.0247  67  GLN A C   
542  O  O   . GLN A 67  ? 0.2139 0.1953 0.1080 0.0114  0.0055  0.0280  67  GLN A O   
543  C  CB  . GLN A 67  ? 0.2266 0.1605 0.1987 -0.0174 -0.0444 0.0430  67  GLN A CB  
544  C  CG  . GLN A 67  ? 0.2305 0.1826 0.1795 -0.0458 -0.0301 0.0044  67  GLN A CG  
545  C  CD  . GLN A 67  ? 0.2546 0.2952 0.3062 -0.0856 -0.0621 -0.0291 67  GLN A CD  
546  O  OE1 . GLN A 67  ? 0.2976 0.3387 0.2928 -0.1131 -0.1014 -0.0005 67  GLN A OE1 
547  N  NE2 . GLN A 67  ? 0.3644 0.2110 0.3741 -0.0836 -0.0147 -0.0491 67  GLN A NE2 
548  N  N   . VAL A 68  ? 0.2053 0.1271 0.1375 0.0212  -0.0111 0.0214  68  VAL A N   
549  C  CA  . VAL A 68  ? 0.2495 0.1531 0.1176 0.0326  -0.0316 0.0334  68  VAL A CA  
550  C  C   . VAL A 68  ? 0.2117 0.1640 0.1425 -0.0077 -0.0134 0.0379  68  VAL A C   
551  O  O   . VAL A 68  ? 0.2268 0.1337 0.1362 0.0179  -0.0223 0.0364  68  VAL A O   
552  C  CB  . VAL A 68  ? 0.2197 0.1411 0.1650 0.0471  -0.0121 0.0190  68  VAL A CB  
553  C  CG1 . VAL A 68  ? 0.2207 0.1640 0.1562 0.0353  -0.0407 0.0141  68  VAL A CG1 
554  C  CG2 . VAL A 68  ? 0.2215 0.1507 0.1635 0.0381  0.0206  0.0133  68  VAL A CG2 
555  N  N   . GLU A 69  ? 0.2503 0.1244 0.1201 0.0227  -0.0265 0.0206  69  GLU A N   
556  C  CA  . GLU A 69  ? 0.1920 0.1255 0.1335 0.0079  -0.0053 0.0135  69  GLU A CA  
557  C  C   . GLU A 69  ? 0.2298 0.1291 0.1416 0.0403  -0.0370 0.0622  69  GLU A C   
558  O  O   . GLU A 69  ? 0.2582 0.1084 0.1903 0.0170  -0.0707 0.0369  69  GLU A O   
559  C  CB  . GLU A 69  ? 0.1909 0.1824 0.1690 -0.0063 0.0079  0.0255  69  GLU A CB  
560  C  CG  . GLU A 69  ? 0.1978 0.1993 0.2082 0.0018  0.0245  -0.0063 69  GLU A CG  
561  C  CD  . GLU A 69  ? 0.2345 0.1632 0.2398 -0.0267 0.0111  0.0163  69  GLU A CD  
562  O  OE1 . GLU A 69  ? 0.2300 0.2286 0.4722 -0.0255 0.0763  0.0310  69  GLU A OE1 
563  O  OE2 . GLU A 69  ? 0.2911 0.2427 0.2731 -0.0352 0.0216  0.0907  69  GLU A OE2 
564  N  N   . PHE A 70  ? 0.1758 0.1357 0.1719 -0.0163 0.0047  0.0397  70  PHE A N   
565  C  CA  . PHE A 70  ? 0.1630 0.1238 0.1966 -0.0096 -0.0352 0.0580  70  PHE A CA  
566  C  C   . PHE A 70  ? 0.1971 0.1319 0.1845 -0.0309 -0.0321 0.0277  70  PHE A C   
567  O  O   . PHE A 70  ? 0.2082 0.1276 0.2294 -0.0107 -0.0471 0.0465  70  PHE A O   
568  C  CB  . PHE A 70  ? 0.1860 0.1170 0.1776 -0.0044 -0.0209 0.0270  70  PHE A CB  
569  C  CG  . PHE A 70  ? 0.1783 0.1102 0.1863 -0.0018 -0.0266 0.0524  70  PHE A CG  
570  C  CD1 . PHE A 70  ? 0.1712 0.1367 0.1802 0.0108  -0.0211 0.0614  70  PHE A CD1 
571  C  CD2 . PHE A 70  ? 0.1946 0.1353 0.1727 -0.0300 -0.0472 0.0304  70  PHE A CD2 
572  C  CE1 . PHE A 70  ? 0.2224 0.1666 0.2165 -0.0389 -0.0268 0.0403  70  PHE A CE1 
573  C  CE2 . PHE A 70  ? 0.2093 0.1216 0.1949 -0.0150 -0.0231 0.0531  70  PHE A CE2 
574  C  CZ  . PHE A 70  ? 0.2230 0.1084 0.1845 -0.0052 -0.0004 0.0283  70  PHE A CZ  
575  N  N   . ASP A 71  ? 0.2593 0.1127 0.2485 -0.0210 -0.0833 0.0508  71  ASP A N   
576  C  CA  . ASP A 71  ? 0.2481 0.1185 0.2702 -0.0256 -0.0569 0.0523  71  ASP A CA  
577  C  C   . ASP A 71  ? 0.2020 0.1009 0.2706 -0.0365 -0.0150 0.0364  71  ASP A C   
578  O  O   . ASP A 71  ? 0.2152 0.1802 0.4423 -0.0588 0.0129  0.0064  71  ASP A O   
579  C  CB  . ASP A 71  ? 0.2843 0.1726 0.3511 -0.0124 -0.1189 0.0552  71  ASP A CB  
580  C  CG  . ASP A 71  ? 0.3338 0.1612 0.3856 0.0152  -0.1151 0.0480  71  ASP A CG  
581  O  OD1 . ASP A 71  ? 0.2824 0.1438 0.4507 0.0105  -0.0783 0.0899  71  ASP A OD1 
582  O  OD2 . ASP A 71  ? 0.3141 0.2124 0.4560 -0.0102 -0.1341 0.0195  71  ASP A OD2 
583  N  N   . ASP A 72  ? 0.2298 0.0901 0.2814 -0.0222 -0.0276 0.0359  72  ASP A N   
584  C  CA  . ASP A 72  ? 0.2215 0.1357 0.2615 -0.0270 -0.0111 0.0411  72  ASP A CA  
585  C  C   . ASP A 72  ? 0.2688 0.1459 0.2937 -0.0352 0.0079  0.0162  72  ASP A C   
586  O  O   . ASP A 72  ? 0.3467 0.1405 0.2740 -0.0566 -0.0115 0.0341  72  ASP A O   
587  C  CB  . ASP A 72  ? 0.2341 0.1578 0.2599 0.0100  0.0178  0.0425  72  ASP A CB  
588  C  CG  . ASP A 72  ? 0.2140 0.2725 0.2006 -0.0216 -0.0257 0.0378  72  ASP A CG  
589  O  OD1 . ASP A 72  ? 0.2774 0.3602 0.1859 -0.0724 -0.0381 0.0480  72  ASP A OD1 
590  O  OD2 . ASP A 72  ? 0.2761 0.2822 0.1945 -0.0153 -0.0457 0.0447  72  ASP A OD2 
591  N  N   . SER A 73  ? 0.3176 0.1273 0.3028 -0.0299 -0.0003 0.0374  73  SER A N   
592  C  CA  . SER A 73  ? 0.3075 0.1360 0.2964 -0.0251 -0.0340 0.0162  73  SER A CA  
593  C  C   . SER A 73  ? 0.4003 0.2203 0.3728 -0.0356 0.1062  0.0057  73  SER A C   
594  O  O   . SER A 73  ? 0.6747 0.1168 0.3837 -0.0183 0.0076  -0.0157 73  SER A O   
595  C  CB  . SER A 73  ? 0.3515 0.1822 0.2696 -0.0146 -0.0121 0.0029  73  SER A CB  
596  O  OG  . SER A 73  ? 0.3180 0.1445 0.2936 0.0208  0.0038  0.0519  73  SER A OG  
597  N  N   . GLN A 74  ? 0.3500 0.1755 0.3380 0.0248  0.0929  0.0034  74  GLN A N   
598  C  CA  . GLN A 74  ? 0.3668 0.2575 0.4060 0.0204  0.1178  -0.0185 74  GLN A CA  
599  C  C   . GLN A 74  ? 0.3503 0.2448 0.2784 -0.0620 0.0241  -0.1023 74  GLN A C   
600  O  O   . GLN A 74  ? 0.3252 0.1970 0.2523 -0.0457 -0.0499 0.0255  74  GLN A O   
601  C  CB  . GLN A 74  ? 0.4416 0.3552 0.4537 0.0763  0.0639  0.1241  74  GLN A CB  
602  C  CG  . GLN A 74  ? 0.6269 0.3462 0.6651 -0.0563 -0.0069 0.1261  74  GLN A CG  
603  C  CD  . GLN A 74  ? 0.5012 0.5270 0.6536 0.1124  -0.0152 0.1046  74  GLN A CD  
604  O  OE1 . GLN A 74  ? 0.5145 0.6657 0.7823 -0.0237 0.1830  0.1812  74  GLN A OE1 
605  N  NE2 . GLN A 74  ? 0.5267 0.3953 0.5242 0.1330  0.0582  0.1723  74  GLN A NE2 
606  N  N   A ASP A 75  ? 0.3778 0.3668 0.3200 -0.0615 0.0528  -0.0697 75  ASP A N   
607  N  N   B ASP A 75  ? 0.3846 0.3705 0.3510 -0.0779 0.1088  -0.0284 75  ASP A N   
608  C  CA  A ASP A 75  ? 0.3046 0.4263 0.3177 -0.1316 0.0345  -0.0570 75  ASP A CA  
609  C  CA  B ASP A 75  ? 0.2739 0.4202 0.4599 -0.1908 0.0423  0.0073  75  ASP A CA  
610  C  C   A ASP A 75  ? 0.2863 0.3326 0.4532 -0.0595 -0.0590 0.0284  75  ASP A C   
611  C  C   B ASP A 75  ? 0.3280 0.3590 0.4683 -0.0155 -0.1180 -0.0047 75  ASP A C   
612  O  O   A ASP A 75  ? 0.3438 0.7207 0.5119 -0.0661 0.0743  0.1208  75  ASP A O   
613  O  O   B ASP A 75  ? 0.4565 0.1812 0.4313 0.0488  -0.2104 0.0663  75  ASP A O   
614  C  CB  A ASP A 75  ? 0.2934 0.4973 0.3055 -0.0177 0.0236  -0.0257 75  ASP A CB  
615  C  CB  B ASP A 75  ? 0.3413 0.6582 0.5139 -0.1896 0.1169  -0.0408 75  ASP A CB  
616  C  CG  A ASP A 75  ? 0.1680 0.3787 0.3328 -0.1161 0.0364  -0.0848 75  ASP A CG  
617  C  CG  B ASP A 75  ? 0.2074 0.7374 0.6273 -0.1628 -0.1120 0.1869  75  ASP A CG  
618  O  OD1 A ASP A 75  ? 0.2371 0.7094 0.3431 0.0730  -0.0842 -0.1923 75  ASP A OD1 
619  O  OD1 B ASP A 75  ? 0.5144 0.8944 0.5784 -0.0710 -0.1129 0.0540  75  ASP A OD1 
620  O  OD2 A ASP A 75  ? 0.4087 0.4913 0.2468 0.1271  0.0484  0.0013  75  ASP A OD2 
621  O  OD2 B ASP A 75  ? 0.4395 0.7983 0.8098 -0.1109 -0.0916 -0.0077 75  ASP A OD2 
622  N  N   . LYS A 76  ? 0.3643 0.2511 0.2709 -0.0665 -0.0998 0.0941  76  LYS A N   
623  C  CA  . LYS A 76  ? 0.4141 0.2170 0.4466 -0.0754 -0.1284 0.0671  76  LYS A CA  
624  C  C   . LYS A 76  ? 0.4844 0.2552 0.5513 0.0347  -0.0108 0.1234  76  LYS A C   
625  O  O   . LYS A 76  ? 0.3529 0.3535 0.8223 0.0100  0.0144  0.1473  76  LYS A O   
626  C  CB  . LYS A 76  ? 0.3754 0.2109 0.4318 0.0154  -0.1280 0.0873  76  LYS A CB  
627  C  CG  . LYS A 76  ? 0.5144 0.2363 0.3512 -0.0417 -0.1205 0.0825  76  LYS A CG  
628  C  CD  . LYS A 76  ? 0.6553 0.1928 0.3442 -0.0532 -0.0323 0.0855  76  LYS A CD  
629  C  CE  . LYS A 76  ? 0.3473 0.2174 0.3716 -0.0041 -0.0374 0.0244  76  LYS A CE  
630  N  NZ  . LYS A 76  ? 0.4888 0.4400 0.3790 0.0569  0.0128  0.1712  76  LYS A NZ  
631  N  N   . ALA A 77  ? 0.3147 0.2904 0.4078 0.0107  -0.1342 0.0942  77  ALA A N   
632  C  CA  . ALA A 77  ? 0.2208 0.3582 0.3606 -0.0313 -0.0871 0.1450  77  ALA A CA  
633  C  C   . ALA A 77  ? 0.1346 0.3619 0.3332 0.0339  -0.0210 0.1086  77  ALA A C   
634  O  O   . ALA A 77  ? 0.1738 0.3838 0.3989 -0.0367 -0.0367 0.0408  77  ALA A O   
635  C  CB  . ALA A 77  ? 0.3385 0.2863 0.4302 0.0282  -0.1225 0.0894  77  ALA A CB  
636  N  N   . VAL A 78  ? 0.1914 0.1569 0.2711 -0.0042 -0.0687 0.0289  78  VAL A N   
637  C  CA  . VAL A 78  ? 0.2307 0.1486 0.2788 0.0071  -0.0796 0.0562  78  VAL A CA  
638  C  C   . VAL A 78  ? 0.1874 0.1446 0.2876 -0.0241 -0.0494 0.0430  78  VAL A C   
639  O  O   . VAL A 78  ? 0.2039 0.1488 0.3625 -0.0403 -0.0627 0.0638  78  VAL A O   
640  C  CB  . VAL A 78  ? 0.3000 0.1743 0.4488 0.0414  -0.0275 0.0176  78  VAL A CB  
641  C  CG1 . VAL A 78  ? 0.3554 0.1442 0.4002 0.0232  -0.1203 0.0029  78  VAL A CG1 
642  C  CG2 . VAL A 78  ? 0.3046 0.1973 0.3416 0.0482  0.0301  0.0484  78  VAL A CG2 
643  N  N   . LEU A 79  ? 0.1723 0.1342 0.2229 0.0179  -0.0054 0.0411  79  LEU A N   
644  C  CA  . LEU A 79  ? 0.1614 0.1533 0.2020 0.0001  0.0104  0.0344  79  LEU A CA  
645  C  C   . LEU A 79  ? 0.1679 0.1152 0.2395 -0.0066 0.0379  0.0134  79  LEU A C   
646  O  O   . LEU A 79  ? 0.1693 0.1522 0.2561 -0.0311 0.0239  -0.0072 79  LEU A O   
647  C  CB  . LEU A 79  ? 0.1180 0.1536 0.2814 -0.0204 -0.0206 0.0560  79  LEU A CB  
648  C  CG  . LEU A 79  ? 0.1492 0.1536 0.2365 0.0099  -0.0020 0.0279  79  LEU A CG  
649  C  CD1 . LEU A 79  ? 0.1578 0.1594 0.4086 -0.0008 0.0486  0.0770  79  LEU A CD1 
650  C  CD2 . LEU A 79  ? 0.1338 0.1917 0.2545 0.0231  0.0006  0.0010  79  LEU A CD2 
651  N  N   . LYS A 80  ? 0.1726 0.1773 0.2205 -0.0140 0.0136  0.0299  80  LYS A N   
652  C  CA  . LYS A 80  ? 0.1745 0.1465 0.2499 -0.0201 0.0347  -0.0050 80  LYS A CA  
653  C  C   . LYS A 80  ? 0.1292 0.1582 0.2373 -0.0084 0.0488  -0.0031 80  LYS A C   
654  O  O   . LYS A 80  ? 0.1515 0.1558 0.2907 -0.0241 0.0247  0.0063  80  LYS A O   
655  C  CB  . LYS A 80  ? 0.3219 0.1729 0.3430 0.0307  0.0331  0.0447  80  LYS A CB  
656  C  CG  . LYS A 80  ? 0.3238 0.2628 0.4737 0.0166  0.0290  0.1202  80  LYS A CG  
657  C  CD  . LYS A 80  ? 0.5312 0.2953 0.3841 0.1151  0.0165  0.0606  80  LYS A CD  
658  C  CE  . LYS A 80  ? 0.3952 0.3320 0.6761 0.0889  -0.0160 0.1444  80  LYS A CE  
659  N  N   . GLY A 81  ? 0.1995 0.1794 0.2397 0.0454  0.0608  0.0204  81  GLY A N   
660  C  CA  . GLY A 81  ? 0.1955 0.2093 0.2772 0.0640  0.0886  0.0430  81  GLY A CA  
661  C  C   . GLY A 81  ? 0.1885 0.1628 0.3358 0.0326  0.0772  0.0647  81  GLY A C   
662  O  O   . GLY A 81  ? 0.1845 0.1890 0.2947 0.0083  0.0521  0.0111  81  GLY A O   
663  N  N   . GLY A 82  ? 0.2229 0.2053 0.3956 0.0034  0.0581  0.1134  82  GLY A N   
664  C  CA  . GLY A 82  ? 0.2879 0.2196 0.5107 0.0347  0.0833  0.1674  82  GLY A CA  
665  C  C   . GLY A 82  ? 0.2954 0.2677 0.4209 0.0750  0.1291  0.0943  82  GLY A C   
666  O  O   . GLY A 82  ? 0.2562 0.3475 0.4051 0.1339  0.1454  0.0981  82  GLY A O   
667  N  N   . PRO A 83  ? 0.2351 0.1892 0.3052 0.0465  0.0526  0.0578  83  PRO A N   
668  C  CA  . PRO A 83  ? 0.2409 0.1937 0.3030 0.0762  0.0488  0.0412  83  PRO A CA  
669  C  C   . PRO A 83  ? 0.2208 0.1905 0.2391 0.0685  0.0301  -0.0044 83  PRO A C   
670  O  O   . PRO A 83  ? 0.2836 0.2924 0.2896 0.0656  -0.0026 -0.0281 83  PRO A O   
671  C  CB  . PRO A 83  ? 0.2398 0.2078 0.2470 0.0899  0.0325  0.0413  83  PRO A CB  
672  C  CG  . PRO A 83  ? 0.2090 0.2178 0.2337 0.0244  0.0194  0.0408  83  PRO A CG  
673  C  CD  . PRO A 83  ? 0.1881 0.1914 0.2813 0.0095  0.0700  0.0497  83  PRO A CD  
674  N  N   . LEU A 84  ? 0.1805 0.1747 0.2476 0.0397  0.0108  -0.0048 84  LEU A N   
675  C  CA  . LEU A 84  ? 0.2096 0.1403 0.2505 0.0414  0.0518  -0.0253 84  LEU A CA  
676  C  C   . LEU A 84  ? 0.1908 0.1977 0.3169 0.0534  0.0364  -0.0687 84  LEU A C   
677  O  O   . LEU A 84  ? 0.2056 0.2165 0.3752 0.0797  0.0484  -0.0568 84  LEU A O   
678  C  CB  . LEU A 84  ? 0.1942 0.0935 0.2518 0.0057  0.0815  -0.0077 84  LEU A CB  
679  C  CG  . LEU A 84  ? 0.1597 0.0885 0.2612 0.0324  0.0385  0.0032  84  LEU A CG  
680  C  CD1 . LEU A 84  ? 0.1705 0.1949 0.2430 0.0203  0.0387  0.0115  84  LEU A CD1 
681  C  CD2 . LEU A 84  ? 0.1540 0.1316 0.2507 0.0044  0.0278  -0.0318 84  LEU A CD2 
682  N  N   . ASP A 85  ? 0.2562 0.1808 0.3159 0.0299  0.0735  -0.0705 85  ASP A N   
683  C  CA  . ASP A 85  ? 0.3547 0.1852 0.3369 0.0240  0.0851  -0.0833 85  ASP A CA  
684  C  C   . ASP A 85  ? 0.2709 0.1845 0.3823 -0.0021 0.1119  -0.0400 85  ASP A C   
685  O  O   . ASP A 85  ? 0.3271 0.3283 0.4604 0.0026  0.1716  -0.0603 85  ASP A O   
686  C  CB  . ASP A 85  ? 0.4151 0.1971 0.3480 0.0588  0.0491  -0.0578 85  ASP A CB  
687  C  CG  . ASP A 85  ? 0.3333 0.3990 0.4398 0.0200  0.0010  0.0858  85  ASP A CG  
688  O  OD1 . ASP A 85  ? 0.3398 0.7084 0.4662 -0.0162 0.0725  0.1380  85  ASP A OD1 
689  O  OD2 . ASP A 85  ? 0.4071 0.4797 0.3955 -0.0466 -0.0441 -0.0410 85  ASP A OD2 
690  N  N   . GLY A 86  ? 0.3040 0.3063 0.5414 -0.0254 0.0353  0.0505  86  GLY A N   
691  C  CA  . GLY A 86  ? 0.3247 0.2567 0.3324 -0.0332 0.0449  -0.0542 86  GLY A CA  
692  C  C   . GLY A 86  ? 0.2836 0.2132 0.3308 -0.0446 -0.0614 0.0037  86  GLY A C   
693  O  O   . GLY A 86  ? 0.3278 0.2762 0.4443 -0.1121 -0.0555 0.0501  86  GLY A O   
694  N  N   . THR A 87  ? 0.2926 0.1784 0.3344 0.0552  0.0201  -0.0080 87  THR A N   
695  C  CA  . THR A 87  ? 0.2581 0.2690 0.3266 0.0536  0.0529  -0.0091 87  THR A CA  
696  C  C   . THR A 87  ? 0.1953 0.1229 0.3014 -0.0072 0.0111  -0.0253 87  THR A C   
697  O  O   . THR A 87  ? 0.2122 0.1031 0.3545 -0.0062 0.0396  -0.0268 87  THR A O   
698  C  CB  . THR A 87  ? 0.2379 0.5771 0.3602 0.2565  -0.0433 -0.0314 87  THR A CB  
699  O  OG1 . THR A 87  ? 0.2967 0.5401 0.4827 0.1755  -0.0071 -0.1488 87  THR A OG1 
700  C  CG2 . THR A 87  ? 0.3133 0.3897 0.4038 0.1205  -0.0172 0.0552  87  THR A CG2 
701  N  N   . TYR A 88  ? 0.1503 0.1041 0.2603 0.0065  0.0214  0.0087  88  TYR A N   
702  C  CA  . TYR A 88  ? 0.1399 0.1201 0.2636 0.0118  0.0122  0.0205  88  TYR A CA  
703  C  C   . TYR A 88  ? 0.1021 0.1203 0.2456 0.0067  -0.0154 0.0420  88  TYR A C   
704  O  O   . TYR A 88  ? 0.1393 0.1908 0.3044 -0.0497 -0.0174 0.0606  88  TYR A O   
705  C  CB  . TYR A 88  ? 0.1802 0.1041 0.2111 -0.0013 -0.0037 0.0155  88  TYR A CB  
706  C  CG  . TYR A 88  ? 0.1447 0.0779 0.2025 -0.0170 0.0133  -0.0143 88  TYR A CG  
707  C  CD1 . TYR A 88  ? 0.1862 0.1266 0.1966 0.0266  0.0156  -0.0171 88  TYR A CD1 
708  C  CD2 . TYR A 88  ? 0.1605 0.0829 0.2133 0.0179  -0.0100 0.0201  88  TYR A CD2 
709  C  CE1 . TYR A 88  ? 0.1393 0.1456 0.2039 -0.0057 0.0348  -0.0204 88  TYR A CE1 
710  C  CE2 . TYR A 88  ? 0.1388 0.1011 0.1835 0.0004  0.0124  0.0163  88  TYR A CE2 
711  C  CZ  . TYR A 88  ? 0.1335 0.0874 0.2054 0.0022  0.0233  -0.0147 88  TYR A CZ  
712  O  OH  . TYR A 88  ? 0.1743 0.1367 0.2018 0.0038  0.0277  -0.0281 88  TYR A OH  
713  N  N   . ARG A 89  ? 0.1382 0.1141 0.2141 -0.0059 0.0071  -0.0086 89  ARG A N   
714  C  CA  . ARG A 89  ? 0.1632 0.1084 0.2192 0.0139  -0.0080 0.0148  89  ARG A CA  
715  C  C   . ARG A 89  ? 0.1493 0.0919 0.1604 0.0066  -0.0205 0.0322  89  ARG A C   
716  O  O   . ARG A 89  ? 0.1447 0.0899 0.1775 -0.0046 -0.0061 0.0124  89  ARG A O   
717  C  CB  . ARG A 89  ? 0.2253 0.1041 0.2932 -0.0001 -0.0732 0.0402  89  ARG A CB  
718  C  CG  . ARG A 89  ? 0.3109 0.1988 0.2519 0.0061  -0.0432 0.0996  89  ARG A CG  
719  C  CD  . ARG A 89  ? 0.2890 0.1849 0.3022 0.0464  0.0141  0.0832  89  ARG A CD  
720  N  NE  . ARG A 89  ? 0.4258 0.2190 0.2404 0.0842  -0.0475 0.0527  89  ARG A NE  
721  C  CZ  . ARG A 89  ? 0.4609 0.2103 0.1877 0.0827  0.0105  0.0288  89  ARG A CZ  
722  N  NH1 . ARG A 89  ? 0.4494 0.2079 0.2778 0.0753  0.0285  0.0478  89  ARG A NH1 
723  N  NH2 . ARG A 89  ? 0.3243 0.2470 0.2756 0.0744  0.0092  0.0456  89  ARG A NH2 
724  N  N   . LEU A 90  ? 0.1867 0.0819 0.1795 -0.0111 -0.0276 0.0287  90  LEU A N   
725  C  CA  . LEU A 90  ? 0.1364 0.1079 0.1923 -0.0114 -0.0165 0.0164  90  LEU A CA  
726  C  C   . LEU A 90  ? 0.1517 0.1205 0.1539 -0.0122 -0.0396 0.0282  90  LEU A C   
727  O  O   . LEU A 90  ? 0.1727 0.1727 0.2046 -0.0037 -0.0522 0.0651  90  LEU A O   
728  C  CB  . LEU A 90  ? 0.1881 0.1285 0.1772 -0.0273 -0.0378 0.0124  90  LEU A CB  
729  C  CG  . LEU A 90  ? 0.2100 0.1240 0.1756 -0.0400 -0.0435 0.0149  90  LEU A CG  
730  C  CD1 . LEU A 90  ? 0.2488 0.1053 0.1967 -0.0288 -0.0241 0.0251  90  LEU A CD1 
731  C  CD2 . LEU A 90  ? 0.2590 0.1808 0.2282 -0.0923 -0.0724 0.0134  90  LEU A CD2 
732  N  N   . LYS A 91  ? 0.1582 0.0851 0.1709 -0.0023 0.0021  0.0263  91  LYS A N   
733  C  CA  . LYS A 91  ? 0.1684 0.0955 0.1701 -0.0130 -0.0079 0.0171  91  LYS A CA  
734  C  C   . LYS A 91  ? 0.1829 0.0873 0.1421 -0.0195 -0.0107 0.0318  91  LYS A C   
735  O  O   . LYS A 91  ? 0.1921 0.1056 0.1316 -0.0211 -0.0245 0.0320  91  LYS A O   
736  C  CB  . LYS A 91  ? 0.1816 0.1477 0.1841 -0.0403 -0.0108 -0.0403 91  LYS A CB  
737  C  CG  . LYS A 91  ? 0.1790 0.1603 0.2373 -0.0523 0.0190  -0.0020 91  LYS A CG  
738  C  CD  . LYS A 91  ? 0.2962 0.2568 0.2961 -0.1417 -0.0166 -0.0331 91  LYS A CD  
739  C  CE  . LYS A 91  ? 0.3741 0.3633 0.3556 -0.1955 0.0439  0.0373  91  LYS A CE  
740  N  NZ  . LYS A 91  ? 0.8215 0.3519 0.5266 -0.1254 -0.0886 0.0610  91  LYS A NZ  
741  N  N   . GLN A 92  ? 0.1773 0.0797 0.1443 -0.0097 -0.0105 0.0138  92  GLN A N   
742  C  CA  . GLN A 92  ? 0.1678 0.0871 0.1331 0.0095  -0.0065 0.0259  92  GLN A CA  
743  C  C   . GLN A 92  ? 0.1641 0.1122 0.1145 -0.0121 -0.0049 0.0296  92  GLN A C   
744  O  O   . GLN A 92  ? 0.1840 0.0948 0.1137 -0.0062 -0.0129 0.0264  92  GLN A O   
745  C  CB  . GLN A 92  ? 0.1528 0.1411 0.1538 0.0117  -0.0168 0.0387  92  GLN A CB  
746  C  CG  . GLN A 92  ? 0.1795 0.1359 0.1644 -0.0043 -0.0332 0.0355  92  GLN A CG  
747  C  CD  . GLN A 92  ? 0.2100 0.1183 0.1659 -0.0167 -0.0252 0.0517  92  GLN A CD  
748  O  OE1 . GLN A 92  ? 0.1914 0.1416 0.1646 -0.0075 -0.0242 0.0159  92  GLN A OE1 
749  N  NE2 . GLN A 92  ? 0.2196 0.2811 0.2738 -0.0435 -0.0245 0.1011  92  GLN A NE2 
750  N  N   . PHE A 93  ? 0.1702 0.0980 0.1163 -0.0075 -0.0288 0.0234  93  PHE A N   
751  C  CA  . PHE A 93  ? 0.1345 0.1016 0.1432 0.0012  -0.0110 0.0342  93  PHE A CA  
752  C  C   . PHE A 93  ? 0.1377 0.1071 0.1054 -0.0047 -0.0229 0.0244  93  PHE A C   
753  O  O   . PHE A 93  ? 0.1978 0.1057 0.1177 0.0043  -0.0190 0.0198  93  PHE A O   
754  C  CB  . PHE A 93  ? 0.1497 0.1183 0.1249 -0.0343 -0.0326 0.0336  93  PHE A CB  
755  C  CG  . PHE A 93  ? 0.1614 0.1049 0.1260 -0.0060 -0.0236 0.0190  93  PHE A CG  
756  C  CD1 . PHE A 93  ? 0.1765 0.1149 0.1319 0.0080  -0.0238 0.0026  93  PHE A CD1 
757  C  CD2 . PHE A 93  ? 0.1483 0.1781 0.1242 -0.0006 -0.0466 0.0380  93  PHE A CD2 
758  C  CE1 . PHE A 93  ? 0.1859 0.1416 0.1632 0.0075  -0.0617 -0.0006 93  PHE A CE1 
759  C  CE2 . PHE A 93  ? 0.1797 0.1460 0.1307 -0.0011 -0.0389 0.0222  93  PHE A CE2 
760  C  CZ  . PHE A 93  ? 0.1808 0.1468 0.1233 0.0000  -0.0346 0.0283  93  PHE A CZ  
761  N  N   . HIS A 94  ? 0.1306 0.0809 0.1285 0.0117  -0.0200 0.0068  94  HIS A N   
762  C  CA  . HIS A 94  ? 0.1312 0.0840 0.1188 0.0060  -0.0111 0.0245  94  HIS A CA  
763  C  C   . HIS A 94  ? 0.1339 0.0900 0.0876 0.0060  -0.0148 0.0142  94  HIS A C   
764  O  O   . HIS A 94  ? 0.1576 0.0973 0.1068 0.0020  0.0118  0.0153  94  HIS A O   
765  C  CB  . HIS A 94  ? 0.1556 0.1310 0.0917 -0.0317 -0.0208 0.0214  94  HIS A CB  
766  C  CG  . HIS A 94  ? 0.1540 0.0815 0.0882 -0.0100 -0.0081 0.0124  94  HIS A CG  
767  N  ND1 . HIS A 94  ? 0.1481 0.0842 0.1234 -0.0173 -0.0130 0.0105  94  HIS A ND1 
768  C  CD2 . HIS A 94  ? 0.1316 0.1228 0.0971 -0.0102 -0.0194 0.0164  94  HIS A CD2 
769  C  CE1 . HIS A 94  ? 0.1238 0.0973 0.1230 0.0005  -0.0080 0.0373  94  HIS A CE1 
770  N  NE2 . HIS A 94  ? 0.1208 0.0970 0.1050 -0.0064 -0.0203 0.0183  94  HIS A NE2 
771  N  N   . PHE A 95  ? 0.1406 0.0774 0.1216 0.0086  -0.0116 0.0070  95  PHE A N   
772  C  CA  . PHE A 95  ? 0.1364 0.0662 0.1174 0.0035  -0.0261 0.0009  95  PHE A CA  
773  C  C   . PHE A 95  ? 0.1335 0.0952 0.1285 0.0064  0.0050  -0.0076 95  PHE A C   
774  O  O   . PHE A 95  ? 0.1607 0.1117 0.1235 -0.0126 -0.0012 0.0017  95  PHE A O   
775  C  CB  . PHE A 95  ? 0.1463 0.1195 0.1134 0.0012  -0.0122 -0.0353 95  PHE A CB  
776  C  CG  . PHE A 95  ? 0.1468 0.0871 0.1356 -0.0133 -0.0184 -0.0015 95  PHE A CG  
777  C  CD1 . PHE A 95  ? 0.1456 0.1093 0.1251 -0.0121 -0.0243 -0.0002 95  PHE A CD1 
778  C  CD2 . PHE A 95  ? 0.1544 0.1040 0.1414 -0.0345 -0.0234 -0.0178 95  PHE A CD2 
779  C  CE1 . PHE A 95  ? 0.1583 0.1342 0.1256 0.0000  -0.0263 -0.0023 95  PHE A CE1 
780  C  CE2 . PHE A 95  ? 0.1686 0.1147 0.1438 -0.0370 -0.0395 -0.0179 95  PHE A CE2 
781  C  CZ  . PHE A 95  ? 0.1522 0.1145 0.1854 0.0029  -0.0100 -0.0035 95  PHE A CZ  
782  N  N   . HIS A 96  ? 0.1391 0.1068 0.1181 -0.0033 -0.0171 0.0000  96  HIS A N   
783  C  CA  . HIS A 96  ? 0.1287 0.0939 0.1269 -0.0031 -0.0055 -0.0156 96  HIS A CA  
784  C  C   . HIS A 96  ? 0.1259 0.1046 0.1222 -0.0086 -0.0084 -0.0113 96  HIS A C   
785  O  O   . HIS A 96  ? 0.1296 0.1113 0.1341 0.0002  0.0030  -0.0133 96  HIS A O   
786  C  CB  . HIS A 96  ? 0.1562 0.0707 0.1162 -0.0207 -0.0022 -0.0094 96  HIS A CB  
787  C  CG  . HIS A 96  ? 0.1398 0.0695 0.1106 -0.0130 0.0089  -0.0048 96  HIS A CG  
788  N  ND1 . HIS A 96  ? 0.1201 0.1122 0.1156 -0.0244 0.0019  -0.0111 96  HIS A ND1 
789  C  CD2 . HIS A 96  ? 0.1544 0.0657 0.1170 0.0099  -0.0222 -0.0075 96  HIS A CD2 
790  C  CE1 . HIS A 96  ? 0.1364 0.1104 0.1309 -0.0108 -0.0032 0.0021  96  HIS A CE1 
791  N  NE2 . HIS A 96  ? 0.1424 0.0829 0.1059 -0.0126 -0.0145 -0.0006 96  HIS A NE2 
792  N  N   . TRP A 97  ? 0.1583 0.0838 0.1183 -0.0034 0.0013  0.0018  97  TRP A N   
793  C  CA  . TRP A 97  ? 0.1450 0.0878 0.1220 -0.0006 -0.0051 -0.0113 97  TRP A CA  
794  C  C   . TRP A 97  ? 0.1370 0.1041 0.1018 -0.0062 0.0171  -0.0069 97  TRP A C   
795  O  O   . TRP A 97  ? 0.1489 0.0952 0.1267 -0.0099 0.0186  -0.0026 97  TRP A O   
796  C  CB  . TRP A 97  ? 0.1682 0.1204 0.1088 -0.0207 0.0032  -0.0087 97  TRP A CB  
797  C  CG  . TRP A 97  ? 0.1518 0.1045 0.0996 -0.0099 -0.0096 -0.0130 97  TRP A CG  
798  C  CD1 . TRP A 97  ? 0.1506 0.1314 0.1101 -0.0178 0.0177  -0.0175 97  TRP A CD1 
799  C  CD2 . TRP A 97  ? 0.1511 0.1145 0.1145 -0.0160 0.0016  -0.0072 97  TRP A CD2 
800  N  NE1 . TRP A 97  ? 0.2100 0.1414 0.1046 -0.0156 0.0104  -0.0207 97  TRP A NE1 
801  C  CE2 . TRP A 97  ? 0.1641 0.1244 0.1258 -0.0206 0.0230  -0.0161 97  TRP A CE2 
802  C  CE3 . TRP A 97  ? 0.1733 0.1041 0.1180 -0.0079 -0.0240 -0.0042 97  TRP A CE3 
803  C  CZ2 . TRP A 97  ? 0.1939 0.1240 0.1289 -0.0206 0.0067  -0.0047 97  TRP A CZ2 
804  C  CZ3 . TRP A 97  ? 0.1625 0.1332 0.1235 -0.0110 0.0037  0.0175  97  TRP A CZ3 
805  C  CH2 . TRP A 97  ? 0.2023 0.1384 0.1335 -0.0212 0.0174  -0.0344 97  TRP A CH2 
806  N  N   . GLY A 98  ? 0.1525 0.0889 0.1185 -0.0017 0.0107  -0.0102 98  GLY A N   
807  C  CA  . GLY A 98  ? 0.1557 0.1041 0.1093 0.0137  -0.0118 -0.0109 98  GLY A CA  
808  C  C   . GLY A 98  ? 0.1662 0.1172 0.1210 -0.0031 0.0067  -0.0163 98  GLY A C   
809  O  O   . GLY A 98  ? 0.1927 0.1131 0.1403 -0.0150 -0.0105 -0.0162 98  GLY A O   
810  N  N   . SER A 99  ? 0.1817 0.0932 0.1477 -0.0132 0.0206  -0.0347 99  SER A N   
811  C  CA  . SER A 99  ? 0.1953 0.0917 0.1659 0.0091  0.0331  -0.0493 99  SER A CA  
812  C  C   . SER A 99  ? 0.1923 0.0988 0.1648 0.0128  0.0305  -0.0406 99  SER A C   
813  O  O   . SER A 99  ? 0.2807 0.1152 0.2007 -0.0285 0.0227  -0.0582 99  SER A O   
814  C  CB  . SER A 99  ? 0.2122 0.1450 0.1707 0.0400  0.0219  -0.0542 99  SER A CB  
815  O  OG  . SER A 99  ? 0.2043 0.1334 0.2138 0.0238  0.0173  -0.0229 99  SER A OG  
816  N  N   . LEU A 100 ? 0.1402 0.0949 0.2011 -0.0098 0.0311  -0.0243 100 LEU A N   
817  C  CA  . LEU A 100 ? 0.1664 0.0812 0.2420 -0.0121 0.0299  -0.0036 100 LEU A CA  
818  C  C   . LEU A 100 ? 0.1808 0.0835 0.1862 -0.0025 0.0254  -0.0262 100 LEU A C   
819  O  O   . LEU A 100 ? 0.2093 0.0885 0.1826 -0.0122 0.0153  -0.0283 100 LEU A O   
820  C  CB  . LEU A 100 ? 0.2391 0.1587 0.2405 0.0502  0.0422  0.0248  100 LEU A CB  
821  C  CG  . LEU A 100 ? 0.2661 0.1806 0.2911 0.0697  0.0660  0.0055  100 LEU A CG  
822  C  CD1 . LEU A 100 ? 0.3700 0.4098 0.3037 0.2308  0.0691  -0.0234 100 LEU A CD1 
823  C  CD2 . LEU A 100 ? 0.3845 0.2593 0.2564 0.0500  0.1130  -0.0826 100 LEU A CD2 
824  N  N   . ASP A 101 ? 0.1632 0.1231 0.2486 -0.0095 0.0129  0.0100  101 ASP A N   
825  C  CA  . ASP A 101 ? 0.2005 0.1158 0.2116 0.0100  0.0183  0.0357  101 ASP A CA  
826  C  C   . ASP A 101 ? 0.2345 0.0962 0.1951 0.0027  0.0361  0.0183  101 ASP A C   
827  O  O   . ASP A 101 ? 0.2909 0.1234 0.2233 0.0034  0.0770  0.0244  101 ASP A O   
828  C  CB  . ASP A 101 ? 0.2250 0.1346 0.2582 -0.0407 0.0129  0.0622  101 ASP A CB  
829  C  CG  . ASP A 101 ? 0.1639 0.2024 0.2975 -0.0245 0.0194  0.0211  101 ASP A CG  
830  O  OD1 . ASP A 101 ? 0.2274 0.1482 0.2070 -0.0024 0.0159  -0.0225 101 ASP A OD1 
831  O  OD2 . ASP A 101 ? 0.2594 0.2272 0.3279 -0.0908 -0.0153 -0.0186 101 ASP A OD2 
832  N  N   . GLY A 102 ? 0.2556 0.1188 0.2208 -0.0489 -0.0051 0.0468  102 GLY A N   
833  C  CA  . GLY A 102 ? 0.3067 0.1364 0.2185 -0.0626 -0.0245 0.0366  102 GLY A CA  
834  C  C   . GLY A 102 ? 0.2348 0.1280 0.2256 -0.0356 0.0199  0.0260  102 GLY A C   
835  O  O   . GLY A 102 ? 0.2314 0.1421 0.2122 -0.0251 0.0365  0.0244  102 GLY A O   
836  N  N   . GLN A 103 ? 0.1777 0.1016 0.1892 -0.0148 0.0370  0.0034  103 GLN A N   
837  C  CA  . GLN A 103 ? 0.1623 0.1237 0.1357 0.0006  0.0084  -0.0100 103 GLN A CA  
838  C  C   . GLN A 103 ? 0.1479 0.1088 0.1222 -0.0136 0.0239  -0.0207 103 GLN A C   
839  O  O   . GLN A 103 ? 0.1823 0.1003 0.1464 -0.0156 0.0117  -0.0217 103 GLN A O   
840  C  CB  . GLN A 103 ? 0.1838 0.1152 0.1770 0.0319  0.0420  0.0068  103 GLN A CB  
841  C  CG  . GLN A 103 ? 0.1793 0.1350 0.1772 0.0301  0.0526  0.0126  103 GLN A CG  
842  C  CD  . GLN A 103 ? 0.2145 0.2204 0.1673 0.0886  0.0656  0.0710  103 GLN A CD  
843  O  OE1 . GLN A 103 ? 0.3707 0.2935 0.3051 0.1489  0.1268  0.1705  103 GLN A OE1 
844  N  NE2 . GLN A 103 ? 0.2071 0.1441 0.2341 0.0302  0.0567  0.0199  103 GLN A NE2 
845  N  N   . GLY A 104 ? 0.1432 0.0818 0.1285 0.0133  0.0277  -0.0068 104 GLY A N   
846  C  CA  . GLY A 104 ? 0.1407 0.0883 0.1292 -0.0040 0.0008  -0.0067 104 GLY A CA  
847  C  C   . GLY A 104 ? 0.1335 0.0950 0.0996 -0.0129 0.0065  -0.0089 104 GLY A C   
848  O  O   . GLY A 104 ? 0.1429 0.1137 0.1486 -0.0099 -0.0006 0.0179  104 GLY A O   
849  N  N   . SER A 105 ? 0.1314 0.1032 0.1046 0.0063  0.0116  -0.0048 105 SER A N   
850  C  CA  . SER A 105 ? 0.1126 0.0946 0.1180 -0.0027 0.0168  -0.0062 105 SER A CA  
851  C  C   . SER A 105 ? 0.1165 0.0801 0.1265 -0.0013 0.0108  -0.0139 105 SER A C   
852  O  O   . SER A 105 ? 0.1274 0.0935 0.1208 0.0022  0.0030  -0.0155 105 SER A O   
853  C  CB  . SER A 105 ? 0.1208 0.0971 0.1154 0.0092  0.0280  0.0140  105 SER A CB  
854  O  OG  . SER A 105 ? 0.1393 0.0664 0.1492 -0.0067 0.0080  0.0074  105 SER A OG  
855  N  N   . GLU A 106 ? 0.1395 0.0869 0.1012 -0.0061 0.0036  -0.0194 106 GLU A N   
856  C  CA  . GLU A 106 ? 0.1353 0.0718 0.0968 -0.0133 0.0013  -0.0029 106 GLU A CA  
857  C  C   . GLU A 106 ? 0.1099 0.0768 0.1009 -0.0032 0.0006  -0.0071 106 GLU A C   
858  O  O   . GLU A 106 ? 0.1163 0.0946 0.1163 0.0030  -0.0035 0.0130  106 GLU A O   
859  C  CB  . GLU A 106 ? 0.1447 0.0788 0.1120 0.0032  0.0043  0.0195  106 GLU A CB  
860  C  CG  . GLU A 106 ? 0.1686 0.0806 0.1142 -0.0228 0.0173  0.0083  106 GLU A CG  
861  C  CD  . GLU A 106 ? 0.1167 0.0890 0.0987 -0.0124 0.0220  0.0002  106 GLU A CD  
862  O  OE1 . GLU A 106 ? 0.1066 0.0982 0.1269 -0.0062 0.0044  -0.0114 106 GLU A OE1 
863  O  OE2 . GLU A 106 ? 0.1235 0.1012 0.1485 -0.0055 0.0231  -0.0047 106 GLU A OE2 
864  N  N   . HIS A 107 ? 0.1095 0.0873 0.1020 -0.0052 0.0159  0.0075  107 HIS A N   
865  C  CA  . HIS A 107 ? 0.1230 0.0842 0.1122 0.0044  0.0296  0.0193  107 HIS A CA  
866  C  C   . HIS A 107 ? 0.1117 0.0870 0.1174 0.0002  0.0024  0.0034  107 HIS A C   
867  O  O   . HIS A 107 ? 0.1247 0.1023 0.1271 -0.0017 -0.0111 0.0030  107 HIS A O   
868  C  CB  . HIS A 107 ? 0.1147 0.0892 0.1174 0.0013  0.0059  -0.0073 107 HIS A CB  
869  C  CG  . HIS A 107 ? 0.1134 0.0820 0.0923 0.0023  0.0137  -0.0012 107 HIS A CG  
870  N  ND1 . HIS A 107 ? 0.1062 0.0926 0.1000 0.0075  0.0030  0.0065  107 HIS A ND1 
871  C  CD2 . HIS A 107 ? 0.1089 0.0833 0.1086 0.0089  0.0035  -0.0175 107 HIS A CD2 
872  C  CE1 . HIS A 107 ? 0.1321 0.0993 0.1109 0.0116  -0.0183 -0.0139 107 HIS A CE1 
873  N  NE2 . HIS A 107 ? 0.1226 0.0906 0.1086 0.0042  -0.0044 -0.0054 107 HIS A NE2 
874  N  N   . THR A 108 ? 0.1456 0.0763 0.1246 -0.0048 -0.0011 0.0227  108 THR A N   
875  C  CA  . THR A 108 ? 0.1393 0.0688 0.1438 0.0091  0.0097  0.0201  108 THR A CA  
876  C  C   . THR A 108 ? 0.1141 0.0833 0.1356 0.0050  -0.0072 0.0117  108 THR A C   
877  O  O   . THR A 108 ? 0.1382 0.1066 0.1289 0.0108  0.0055  0.0078  108 THR A O   
878  C  CB  . THR A 108 ? 0.1384 0.1050 0.1241 0.0201  0.0008  -0.0006 108 THR A CB  
879  O  OG1 . THR A 108 ? 0.1622 0.0964 0.1364 0.0172  -0.0122 0.0143  108 THR A OG1 
880  C  CG2 . THR A 108 ? 0.1750 0.0864 0.1420 0.0170  0.0363  0.0111  108 THR A CG2 
881  N  N   . VAL A 109 ? 0.1605 0.0921 0.1384 -0.0165 0.0119  0.0457  109 VAL A N   
882  C  CA  . VAL A 109 ? 0.1608 0.1183 0.1630 -0.0103 0.0208  0.0497  109 VAL A CA  
883  C  C   . VAL A 109 ? 0.1751 0.1089 0.1580 -0.0207 0.0248  0.0408  109 VAL A C   
884  O  O   . VAL A 109 ? 0.1837 0.0960 0.2038 -0.0281 0.0150  0.0411  109 VAL A O   
885  C  CB  . VAL A 109 ? 0.1551 0.0994 0.1917 0.0110  0.0261  0.0283  109 VAL A CB  
886  C  CG1 . VAL A 109 ? 0.1493 0.1817 0.2195 0.0071  0.0384  0.0342  109 VAL A CG1 
887  C  CG2 . VAL A 109 ? 0.1926 0.0833 0.2082 0.0227  0.0192  0.0262  109 VAL A CG2 
888  N  N   . ASP A 110 ? 0.1996 0.1386 0.1410 0.0134  0.0209  0.0719  110 ASP A N   
889  C  CA  . ASP A 110 ? 0.2280 0.1195 0.1499 0.0117  0.0303  0.0699  110 ASP A CA  
890  C  C   . ASP A 110 ? 0.2619 0.1206 0.1348 -0.0042 0.0373  0.0227  110 ASP A C   
891  O  O   . ASP A 110 ? 0.3015 0.1014 0.2161 0.0252  0.0064  0.0488  110 ASP A O   
892  C  CB  . ASP A 110 ? 0.2968 0.1334 0.2178 0.0000  0.0759  0.1017  110 ASP A CB  
893  C  CG  . ASP A 110 ? 0.3101 0.1884 0.1887 0.0456  0.0489  0.1130  110 ASP A CG  
894  O  OD1 . ASP A 110 ? 0.2901 0.1813 0.2628 0.0312  0.1132  0.0884  110 ASP A OD1 
895  O  OD2 . ASP A 110 ? 0.3150 0.2900 0.2580 -0.0294 0.0668  0.0822  110 ASP A OD2 
896  N  N   . LYS A 111 ? 0.1758 0.1410 0.1644 0.0151  0.0078  0.0525  111 LYS A N   
897  C  CA  . LYS A 111 ? 0.2138 0.1249 0.1698 0.0313  0.0015  0.0368  111 LYS A CA  
898  C  C   . LYS A 111 ? 0.2129 0.0971 0.1808 -0.0013 -0.0113 0.0484  111 LYS A C   
899  O  O   . LYS A 111 ? 0.2394 0.1296 0.2280 0.0273  0.0207  0.0290  111 LYS A O   
900  C  CB  . LYS A 111 ? 0.2461 0.1490 0.2078 0.0595  -0.0321 0.0472  111 LYS A CB  
901  C  CG  . LYS A 111 ? 0.3175 0.2368 0.1903 0.0905  -0.0604 0.0455  111 LYS A CG  
902  C  CD  . LYS A 111 ? 0.2517 0.3210 0.2291 0.0283  -0.0331 -0.0285 111 LYS A CD  
903  C  CE  . LYS A 111 ? 0.3802 0.3618 0.1829 0.0789  -0.0833 0.0055  111 LYS A CE  
904  N  NZ  . LYS A 111 ? 0.4291 0.4646 0.3958 0.1207  -0.1604 0.0441  111 LYS A NZ  
905  N  N   . LYS A 112 ? 0.2007 0.0996 0.1729 -0.0096 -0.0122 0.0435  112 LYS A N   
906  C  CA  . LYS A 112 ? 0.2265 0.1429 0.1781 -0.0271 -0.0072 0.0529  112 LYS A CA  
907  C  C   . LYS A 112 ? 0.1942 0.1045 0.1676 0.0264  -0.0009 0.0287  112 LYS A C   
908  O  O   . LYS A 112 ? 0.1847 0.0885 0.1741 0.0035  0.0042  0.0003  112 LYS A O   
909  C  CB  . LYS A 112 ? 0.2415 0.1316 0.2296 -0.0577 -0.0201 0.0413  112 LYS A CB  
910  C  CG  . LYS A 112 ? 0.2111 0.1844 0.2208 -0.0500 0.0003  0.0020  112 LYS A CG  
911  C  CD  . LYS A 112 ? 0.2264 0.2682 0.3030 -0.0350 0.0347  0.0370  112 LYS A CD  
912  C  CE  . LYS A 112 ? 0.2614 0.2329 0.3545 -0.0044 0.0066  0.0241  112 LYS A CE  
913  N  NZ  . LYS A 112 ? 0.3058 0.1820 0.3126 -0.0195 -0.0684 0.0870  112 LYS A NZ  
914  N  N   A LYS A 113 ? 0.1999 0.1092 0.1597 0.0267  -0.0089 0.0168  113 LYS A N   
915  N  N   B LYS A 113 ? 0.2041 0.1084 0.1626 0.0278  -0.0055 0.0164  113 LYS A N   
916  C  CA  A LYS A 113 ? 0.1747 0.1170 0.1522 0.0006  0.0027  0.0098  113 LYS A CA  
917  C  CA  B LYS A 113 ? 0.1682 0.1199 0.1543 0.0009  0.0035  0.0092  113 LYS A CA  
918  C  C   A LYS A 113 ? 0.1705 0.1018 0.1549 -0.0127 -0.0006 0.0249  113 LYS A C   
919  C  C   B LYS A 113 ? 0.1705 0.0973 0.1529 -0.0151 -0.0008 0.0271  113 LYS A C   
920  O  O   A LYS A 113 ? 0.2113 0.0856 0.2591 0.0035  -0.0254 0.0117  113 LYS A O   
921  O  O   B LYS A 113 ? 0.2197 0.0973 0.2580 -0.0100 -0.0245 -0.0008 113 LYS A O   
922  C  CB  A LYS A 113 ? 0.1722 0.1459 0.1890 0.0027  0.0022  -0.0309 113 LYS A CB  
923  C  CB  B LYS A 113 ? 0.1691 0.1431 0.1956 0.0116  0.0063  -0.0249 113 LYS A CB  
924  C  CG  A LYS A 113 ? 0.1863 0.1327 0.1690 0.0154  -0.0003 0.0074  113 LYS A CG  
925  C  CG  B LYS A 113 ? 0.1937 0.1535 0.1694 0.0296  -0.0039 -0.0013 113 LYS A CG  
926  C  CD  A LYS A 113 ? 0.1544 0.1402 0.1890 0.0046  -0.0089 -0.0310 113 LYS A CD  
927  C  CD  B LYS A 113 ? 0.1745 0.1393 0.2160 0.0221  0.0059  -0.0201 113 LYS A CD  
928  C  CE  A LYS A 113 ? 0.2187 0.1395 0.2005 -0.0520 -0.0409 -0.0043 113 LYS A CE  
929  C  CE  B LYS A 113 ? 0.2081 0.1684 0.2225 -0.0265 -0.0040 0.0170  113 LYS A CE  
930  N  NZ  A LYS A 113 ? 0.2176 0.2584 0.2695 0.0133  -0.0702 0.0497  113 LYS A NZ  
931  N  NZ  B LYS A 113 ? 0.2806 0.1756 0.3219 0.0606  -0.0348 0.0337  113 LYS A NZ  
932  N  N   . TYR A 114 ? 0.1271 0.1159 0.1697 0.0066  0.0071  0.0212  114 TYR A N   
933  C  CA  . TYR A 114 ? 0.1346 0.1066 0.1612 0.0134  0.0077  -0.0035 114 TYR A CA  
934  C  C   . TYR A 114 ? 0.1612 0.0822 0.1704 -0.0063 0.0113  -0.0076 114 TYR A C   
935  O  O   . TYR A 114 ? 0.1389 0.1039 0.1802 -0.0070 0.0077  -0.0067 114 TYR A O   
936  C  CB  . TYR A 114 ? 0.1238 0.0876 0.1762 0.0147  0.0203  0.0072  114 TYR A CB  
937  C  CG  . TYR A 114 ? 0.1364 0.0889 0.1709 0.0152  -0.0059 0.0209  114 TYR A CG  
938  C  CD1 . TYR A 114 ? 0.1930 0.1176 0.1702 0.0024  0.0104  0.0042  114 TYR A CD1 
939  C  CD2 . TYR A 114 ? 0.1465 0.1204 0.1784 -0.0139 0.0139  0.0320  114 TYR A CD2 
940  C  CE1 . TYR A 114 ? 0.2440 0.1143 0.1697 0.0083  0.0044  0.0039  114 TYR A CE1 
941  C  CE2 . TYR A 114 ? 0.2161 0.1375 0.2068 -0.0075 0.0672  0.0308  114 TYR A CE2 
942  C  CZ  . TYR A 114 ? 0.2122 0.1662 0.2060 0.0055  0.0605  0.0435  114 TYR A CZ  
943  O  OH  . TYR A 114 ? 0.2649 0.2555 0.2271 0.0542  0.0881  0.0471  114 TYR A OH  
944  N  N   . ALA A 115 ? 0.1830 0.0763 0.1700 -0.0193 -0.0086 -0.0077 115 ALA A N   
945  C  CA  . ALA A 115 ? 0.1890 0.0743 0.1459 -0.0126 -0.0239 -0.0145 115 ALA A CA  
946  C  C   . ALA A 115 ? 0.1725 0.0844 0.1804 -0.0013 0.0029  0.0046  115 ALA A C   
947  O  O   . ALA A 115 ? 0.1546 0.1059 0.1881 -0.0168 0.0035  -0.0183 115 ALA A O   
948  C  CB  . ALA A 115 ? 0.1852 0.0894 0.1989 -0.0325 -0.0297 -0.0362 115 ALA A CB  
949  N  N   . ALA A 116 ? 0.1540 0.0903 0.1482 -0.0114 -0.0071 -0.0030 116 ALA A N   
950  C  CA  . ALA A 116 ? 0.1543 0.0955 0.1156 -0.0115 0.0032  -0.0044 116 ALA A CA  
951  C  C   . ALA A 116 ? 0.1385 0.0928 0.1159 -0.0187 -0.0010 -0.0048 116 ALA A C   
952  O  O   . ALA A 116 ? 0.1350 0.0802 0.1310 -0.0155 0.0017  0.0025  116 ALA A O   
953  C  CB  . ALA A 116 ? 0.1571 0.1432 0.1195 -0.0128 -0.0122 0.0168  116 ALA A CB  
954  N  N   . GLU A 117 ? 0.1337 0.0828 0.1280 -0.0150 -0.0114 -0.0069 117 GLU A N   
955  C  CA  . GLU A 117 ? 0.1417 0.0721 0.1089 0.0089  -0.0232 0.0168  117 GLU A CA  
956  C  C   . GLU A 117 ? 0.1314 0.0759 0.1000 0.0018  -0.0159 0.0176  117 GLU A C   
957  O  O   . GLU A 117 ? 0.1346 0.0986 0.1276 0.0006  0.0002  0.0238  117 GLU A O   
958  C  CB  . GLU A 117 ? 0.1400 0.1156 0.0932 0.0141  -0.0184 0.0073  117 GLU A CB  
959  C  CG  . GLU A 117 ? 0.1629 0.1049 0.1032 0.0177  -0.0192 -0.0059 117 GLU A CG  
960  C  CD  . GLU A 117 ? 0.1161 0.0915 0.1256 -0.0013 -0.0073 0.0000  117 GLU A CD  
961  O  OE1 . GLU A 117 ? 0.1213 0.1177 0.1147 0.0122  -0.0159 0.0094  117 GLU A OE1 
962  O  OE2 . GLU A 117 ? 0.1403 0.1041 0.1159 -0.0023 -0.0119 -0.0024 117 GLU A OE2 
963  N  N   . LEU A 118 ? 0.1353 0.0775 0.1145 0.0060  -0.0179 0.0105  118 LEU A N   
964  C  CA  . LEU A 118 ? 0.1324 0.0682 0.0976 -0.0026 -0.0271 0.0070  118 LEU A CA  
965  C  C   . LEU A 118 ? 0.1198 0.1120 0.0903 0.0057  -0.0020 0.0015  118 LEU A C   
966  O  O   . LEU A 118 ? 0.1420 0.0862 0.0908 0.0042  -0.0036 0.0109  118 LEU A O   
967  C  CB  . LEU A 118 ? 0.1321 0.0883 0.1410 0.0038  -0.0348 0.0070  118 LEU A CB  
968  C  CG  . LEU A 118 ? 0.1251 0.1027 0.1417 0.0052  -0.0215 0.0475  118 LEU A CG  
969  C  CD1 . LEU A 118 ? 0.1680 0.0948 0.1439 -0.0298 -0.0266 0.0271  118 LEU A CD1 
970  C  CD2 . LEU A 118 ? 0.1342 0.1339 0.1669 -0.0037 -0.0445 0.0403  118 LEU A CD2 
971  N  N   . HIS A 119 ? 0.1326 0.0709 0.1150 0.0002  -0.0057 0.0107  119 HIS A N   
972  C  CA  . HIS A 119 ? 0.1104 0.0894 0.1259 -0.0019 -0.0155 0.0122  119 HIS A CA  
973  C  C   . HIS A 119 ? 0.1141 0.0966 0.0926 -0.0074 -0.0287 0.0068  119 HIS A C   
974  O  O   . HIS A 119 ? 0.1348 0.1070 0.1111 -0.0078 -0.0071 0.0065  119 HIS A O   
975  C  CB  . HIS A 119 ? 0.1016 0.0933 0.1133 0.0048  -0.0206 0.0184  119 HIS A CB  
976  C  CG  . HIS A 119 ? 0.1159 0.0860 0.0935 0.0106  -0.0102 0.0071  119 HIS A CG  
977  N  ND1 . HIS A 119 ? 0.1224 0.1045 0.0961 -0.0018 0.0041  0.0111  119 HIS A ND1 
978  C  CD2 . HIS A 119 ? 0.1320 0.0863 0.0930 -0.0098 -0.0230 0.0168  119 HIS A CD2 
979  C  CE1 . HIS A 119 ? 0.1465 0.0846 0.0950 -0.0119 -0.0048 0.0059  119 HIS A CE1 
980  N  NE2 . HIS A 119 ? 0.1244 0.1007 0.1059 -0.0082 -0.0234 0.0095  119 HIS A NE2 
981  N  N   . LEU A 120 ? 0.1265 0.0673 0.1231 -0.0075 -0.0054 0.0022  120 LEU A N   
982  C  CA  . LEU A 120 ? 0.1296 0.0671 0.1332 -0.0111 -0.0174 0.0068  120 LEU A CA  
983  C  C   . LEU A 120 ? 0.1267 0.0680 0.1102 0.0086  -0.0068 0.0033  120 LEU A C   
984  O  O   . LEU A 120 ? 0.1263 0.0854 0.1090 0.0034  -0.0066 0.0234  120 LEU A O   
985  C  CB  . LEU A 120 ? 0.1224 0.0777 0.1543 -0.0111 -0.0211 0.0120  120 LEU A CB  
986  C  CG  . LEU A 120 ? 0.1364 0.0892 0.1617 -0.0271 -0.0479 0.0273  120 LEU A CG  
987  C  CD1 . LEU A 120 ? 0.2072 0.1346 0.2113 -0.0534 -0.0100 0.0354  120 LEU A CD1 
988  C  CD2 . LEU A 120 ? 0.1607 0.1398 0.1687 0.0060  -0.0687 -0.0086 120 LEU A CD2 
989  N  N   . VAL A 121 ? 0.1489 0.0820 0.1314 -0.0316 -0.0214 0.0187  121 VAL A N   
990  C  CA  . VAL A 121 ? 0.1271 0.0826 0.1274 -0.0211 -0.0175 0.0154  121 VAL A CA  
991  C  C   . VAL A 121 ? 0.1664 0.0856 0.1127 -0.0111 -0.0013 0.0244  121 VAL A C   
992  O  O   . VAL A 121 ? 0.1733 0.0933 0.1447 -0.0044 -0.0302 0.0239  121 VAL A O   
993  C  CB  . VAL A 121 ? 0.1256 0.0837 0.1425 -0.0093 -0.0128 0.0255  121 VAL A CB  
994  C  CG1 . VAL A 121 ? 0.1471 0.1134 0.1751 -0.0417 0.0216  -0.0060 121 VAL A CG1 
995  C  CG2 . VAL A 121 ? 0.1694 0.0960 0.1447 0.0086  -0.0232 0.0197  121 VAL A CG2 
996  N  N   . HIS A 122 ? 0.1303 0.0657 0.1324 -0.0086 -0.0035 0.0117  122 HIS A N   
997  C  CA  . HIS A 122 ? 0.1342 0.0585 0.1587 -0.0157 -0.0019 0.0068  122 HIS A CA  
998  C  C   . HIS A 122 ? 0.1517 0.0759 0.1432 -0.0077 -0.0096 0.0055  122 HIS A C   
999  O  O   . HIS A 122 ? 0.1901 0.0774 0.1583 -0.0140 -0.0399 0.0141  122 HIS A O   
1000 C  CB  . HIS A 122 ? 0.1391 0.1025 0.1646 -0.0147 0.0033  0.0157  122 HIS A CB  
1001 C  CG  . HIS A 122 ? 0.1356 0.0784 0.1544 -0.0048 -0.0143 0.0141  122 HIS A CG  
1002 N  ND1 . HIS A 122 ? 0.1251 0.0849 0.1759 0.0069  -0.0280 0.0193  122 HIS A ND1 
1003 C  CD2 . HIS A 122 ? 0.1280 0.1053 0.1711 -0.0178 -0.0122 0.0201  122 HIS A CD2 
1004 C  CE1 . HIS A 122 ? 0.1306 0.1244 0.1520 0.0011  -0.0167 -0.0062 122 HIS A CE1 
1005 N  NE2 . HIS A 122 ? 0.1316 0.1088 0.1604 -0.0256 -0.0208 0.0188  122 HIS A NE2 
1006 N  N   . TRP A 123 ? 0.1586 0.0671 0.1389 -0.0179 -0.0011 0.0089  123 TRP A N   
1007 C  CA  . TRP A 123 ? 0.1601 0.0648 0.1431 -0.0195 0.0044  -0.0061 123 TRP A CA  
1008 C  C   . TRP A 123 ? 0.1386 0.0819 0.1551 -0.0097 -0.0020 0.0111  123 TRP A C   
1009 O  O   . TRP A 123 ? 0.1410 0.0725 0.1863 -0.0076 -0.0218 0.0038  123 TRP A O   
1010 C  CB  . TRP A 123 ? 0.1629 0.1456 0.1425 -0.0328 -0.0054 0.0084  123 TRP A CB  
1011 C  CG  . TRP A 123 ? 0.1725 0.1012 0.1921 -0.0288 -0.0100 0.0168  123 TRP A CG  
1012 C  CD1 . TRP A 123 ? 0.1967 0.1296 0.1755 -0.0508 -0.0373 0.0167  123 TRP A CD1 
1013 C  CD2 . TRP A 123 ? 0.2534 0.0910 0.1655 -0.0276 0.0027  0.0190  123 TRP A CD2 
1014 N  NE1 . TRP A 123 ? 0.2513 0.1046 0.1872 -0.0425 -0.0262 0.0104  123 TRP A NE1 
1015 C  CE2 . TRP A 123 ? 0.2983 0.0855 0.1903 -0.0447 -0.0100 0.0284  123 TRP A CE2 
1016 C  CE3 . TRP A 123 ? 0.2945 0.0937 0.1813 -0.0368 0.0053  0.0166  123 TRP A CE3 
1017 C  CZ2 . TRP A 123 ? 0.3879 0.0817 0.1957 -0.0598 -0.0514 0.0389  123 TRP A CZ2 
1018 C  CZ3 . TRP A 123 ? 0.4215 0.0770 0.2171 -0.0453 -0.0312 0.0024  123 TRP A CZ3 
1019 C  CH2 . TRP A 123 ? 0.3665 0.0767 0.2447 -0.0678 -0.0533 0.0142  123 TRP A CH2 
1020 N  N   . ASN A 124 ? 0.1770 0.0786 0.1391 -0.0200 0.0125  -0.0204 124 ASN A N   
1021 C  CA  . ASN A 124 ? 0.1993 0.0666 0.1870 0.0127  -0.0048 -0.0392 124 ASN A CA  
1022 C  C   . ASN A 124 ? 0.1587 0.1093 0.1975 -0.0103 -0.0131 -0.0167 124 ASN A C   
1023 O  O   . ASN A 124 ? 0.1461 0.1102 0.1781 -0.0051 0.0079  -0.0168 124 ASN A O   
1024 C  CB  . ASN A 124 ? 0.2030 0.1213 0.1355 -0.0015 0.0308  -0.0135 124 ASN A CB  
1025 C  CG  . ASN A 124 ? 0.2685 0.1206 0.1672 -0.0065 0.0687  -0.0030 124 ASN A CG  
1026 O  OD1 . ASN A 124 ? 0.2429 0.1125 0.2143 -0.0073 0.0451  -0.0332 124 ASN A OD1 
1027 N  ND2 . ASN A 124 ? 0.3110 0.1249 0.1626 -0.0142 0.0405  -0.0060 124 ASN A ND2 
1028 N  N   . THR A 125 ? 0.1874 0.0955 0.2212 0.0232  -0.0184 -0.0121 125 THR A N   
1029 C  CA  . THR A 125 ? 0.2163 0.0891 0.2645 0.0345  -0.0370 -0.0023 125 THR A CA  
1030 C  C   . THR A 125 ? 0.2055 0.1056 0.2708 0.0455  0.0109  -0.0198 125 THR A C   
1031 O  O   . THR A 125 ? 0.2243 0.1104 0.2835 0.0323  0.0136  0.0073  125 THR A O   
1032 C  CB  . THR A 125 ? 0.2287 0.1714 0.3574 0.0473  -0.0675 -0.0124 125 THR A CB  
1033 O  OG1 . THR A 125 ? 0.2901 0.1817 0.4458 0.0905  -0.0209 0.0032  125 THR A OG1 
1034 C  CG2 . THR A 125 ? 0.3013 0.1284 0.3525 0.0050  -0.0562 0.0122  125 THR A CG2 
1035 N  N   . LYS A 126 ? 0.2584 0.0901 0.1856 0.0119  0.0282  -0.0158 126 LYS A N   
1036 C  CA  . LYS A 126 ? 0.2656 0.0979 0.2377 -0.0108 0.0831  -0.0561 126 LYS A CA  
1037 C  C   . LYS A 126 ? 0.2185 0.1115 0.2474 -0.0166 0.0102  -0.0042 126 LYS A C   
1038 O  O   . LYS A 126 ? 0.3201 0.1118 0.3054 -0.0249 0.0372  -0.0573 126 LYS A O   
1039 C  CB  . LYS A 126 ? 0.3373 0.1302 0.2377 0.0044  0.0351  -0.0671 126 LYS A CB  
1040 C  CG  . LYS A 126 ? 0.3739 0.1593 0.2477 0.0388  0.0495  -0.0196 126 LYS A CG  
1041 C  CD  . LYS A 126 ? 0.5061 0.2574 0.2583 -0.0617 0.1713  -0.0153 126 LYS A CD  
1042 C  CE  . LYS A 126 ? 0.6097 0.2348 0.3238 0.0460  0.0454  -0.0061 126 LYS A CE  
1043 N  NZ  . LYS A 126 ? 0.6433 0.3966 0.3818 -0.1360 -0.0825 0.2258  126 LYS A NZ  
1044 N  N   . TYR A 127 ? 0.2165 0.1267 0.1860 0.0000  0.0099  0.0009  127 TYR A N   
1045 C  CA  . TYR A 127 ? 0.2032 0.1149 0.1862 -0.0077 -0.0069 -0.0020 127 TYR A CA  
1046 C  C   . TYR A 127 ? 0.2423 0.1054 0.1927 0.0075  0.0243  -0.0244 127 TYR A C   
1047 O  O   . TYR A 127 ? 0.2438 0.1234 0.2084 -0.0077 0.0170  0.0227  127 TYR A O   
1048 C  CB  . TYR A 127 ? 0.1982 0.1283 0.2035 -0.0069 0.0231  -0.0037 127 TYR A CB  
1049 C  CG  . TYR A 127 ? 0.2605 0.0855 0.1952 -0.0050 -0.0068 -0.0241 127 TYR A CG  
1050 C  CD1 . TYR A 127 ? 0.2517 0.1339 0.2039 -0.0136 0.0147  -0.0631 127 TYR A CD1 
1051 C  CD2 . TYR A 127 ? 0.1989 0.1018 0.1998 -0.0096 -0.0063 0.0026  127 TYR A CD2 
1052 C  CE1 . TYR A 127 ? 0.3352 0.1312 0.2125 0.0005  -0.0047 -0.0117 127 TYR A CE1 
1053 C  CE2 . TYR A 127 ? 0.2238 0.1345 0.1788 0.0281  -0.0277 -0.0181 127 TYR A CE2 
1054 C  CZ  . TYR A 127 ? 0.3001 0.1280 0.1938 0.0208  -0.0157 -0.0218 127 TYR A CZ  
1055 O  OH  . TYR A 127 ? 0.3972 0.1707 0.1765 0.0166  -0.0063 -0.0452 127 TYR A OH  
1056 N  N   . GLY A 128 ? 0.2125 0.1097 0.1971 -0.0249 0.0136  0.0208  128 GLY A N   
1057 C  CA  . GLY A 128 ? 0.2534 0.0716 0.2028 -0.0143 0.0557  0.0270  128 GLY A CA  
1058 C  C   . GLY A 128 ? 0.2779 0.1310 0.1856 0.0186  0.0082  0.0184  128 GLY A C   
1059 O  O   . GLY A 128 ? 0.3066 0.1241 0.1863 0.0211  -0.0133 0.0234  128 GLY A O   
1060 N  N   A ASP A 129 ? 0.3082 0.1120 0.1733 0.0362  0.0439  0.0115  129 ASP A N   
1061 N  N   B ASP A 129 ? 0.2605 0.1393 0.2253 0.0078  -0.0051 -0.0044 129 ASP A N   
1062 C  CA  A ASP A 129 ? 0.3115 0.1016 0.1737 0.0381  0.0735  0.0154  129 ASP A CA  
1063 C  CA  B ASP A 129 ? 0.3110 0.1313 0.1788 0.0050  -0.0165 0.0151  129 ASP A CA  
1064 C  C   A ASP A 129 ? 0.3126 0.0950 0.1899 0.0100  0.0319  0.0144  129 ASP A C   
1065 C  C   B ASP A 129 ? 0.2985 0.1470 0.1978 0.0048  -0.0880 -0.0097 129 ASP A C   
1066 O  O   A ASP A 129 ? 0.3094 0.1185 0.2165 0.0366  0.0269  -0.0111 129 ASP A O   
1067 O  O   B ASP A 129 ? 0.3158 0.1050 0.1714 0.0124  -0.0480 -0.0016 129 ASP A O   
1068 C  CB  A ASP A 129 ? 0.2404 0.1373 0.2011 -0.0083 0.0452  0.0385  129 ASP A CB  
1069 C  CB  B ASP A 129 ? 0.2649 0.2177 0.1560 -0.0379 -0.0651 0.0032  129 ASP A CB  
1070 C  CG  A ASP A 129 ? 0.2097 0.0463 0.2129 0.0257  0.0721  0.0179  129 ASP A CG  
1071 C  CG  B ASP A 129 ? 0.2336 0.2303 0.2773 0.0234  -0.0383 -0.0594 129 ASP A CG  
1072 O  OD1 A ASP A 129 ? 0.3650 0.1102 0.2225 -0.0566 0.0077  -0.0013 129 ASP A OD1 
1073 O  OD1 B ASP A 129 ? 0.3794 0.2020 0.1547 0.0650  0.0389  -0.0086 129 ASP A OD1 
1074 O  OD2 A ASP A 129 ? 0.2521 0.1038 0.3057 -0.0238 0.1238  0.0403  129 ASP A OD2 
1075 O  OD2 B ASP A 129 ? 0.1597 0.2116 0.2756 0.0284  0.0019  0.0427  129 ASP A OD2 
1076 N  N   . TYR A 130 ? 0.3950 0.1270 0.1540 0.0370  0.0251  0.0179  130 TYR A N   
1077 C  CA  . TYR A 130 ? 0.2975 0.1067 0.1901 0.0124  0.0258  0.0173  130 TYR A CA  
1078 C  C   . TYR A 130 ? 0.2882 0.1479 0.2093 0.0296  0.0604  0.0314  130 TYR A C   
1079 O  O   . TYR A 130 ? 0.2396 0.1321 0.2020 -0.0057 0.0428  0.0256  130 TYR A O   
1080 C  CB  . TYR A 130 ? 0.3665 0.1201 0.1791 0.0143  0.0434  0.0050  130 TYR A CB  
1081 C  CG  . TYR A 130 ? 0.3015 0.1256 0.2088 0.0019  0.0758  0.0024  130 TYR A CG  
1082 C  CD1 . TYR A 130 ? 0.3535 0.2070 0.2282 0.0431  0.1033  -0.0310 130 TYR A CD1 
1083 C  CD2 . TYR A 130 ? 0.3721 0.1084 0.1702 -0.0022 0.0563  -0.0060 130 TYR A CD2 
1084 C  CE1 . TYR A 130 ? 0.4011 0.1813 0.2728 0.0440  0.1237  0.0248  130 TYR A CE1 
1085 C  CE2 . TYR A 130 ? 0.4061 0.0860 0.2742 0.0048  0.0847  -0.0326 130 TYR A CE2 
1086 C  CZ  . TYR A 130 ? 0.4043 0.1676 0.2979 0.0089  0.0759  0.0083  130 TYR A CZ  
1087 O  OH  . TYR A 130 ? 0.7942 0.1791 0.3725 0.1692  0.0247  0.0048  130 TYR A OH  
1088 N  N   . GLY A 131 ? 0.3189 0.1504 0.2326 -0.0284 0.0530  0.0308  131 GLY A N   
1089 C  CA  . GLY A 131 ? 0.2969 0.2135 0.2782 -0.0122 0.0876  0.0712  131 GLY A CA  
1090 C  C   . GLY A 131 ? 0.2174 0.2075 0.2581 -0.0336 0.0655  0.1092  131 GLY A C   
1091 O  O   . GLY A 131 ? 0.2275 0.2456 0.2861 -0.0519 0.0155  0.0679  131 GLY A O   
1092 N  N   . LYS A 132 ? 0.2412 0.1617 0.2671 -0.0712 0.0810  0.0380  132 LYS A N   
1093 C  CA  . LYS A 132 ? 0.2200 0.1435 0.2799 -0.0388 0.0734  0.0423  132 LYS A CA  
1094 C  C   . LYS A 132 ? 0.1702 0.1806 0.2224 -0.0594 0.0193  0.0395  132 LYS A C   
1095 O  O   . LYS A 132 ? 0.2520 0.1696 0.3014 -0.0636 -0.0486 0.0690  132 LYS A O   
1096 C  CB  . LYS A 132 ? 0.2419 0.1456 0.2916 -0.0128 -0.0111 0.0208  132 LYS A CB  
1097 C  CG  . LYS A 132 ? 0.3794 0.1885 0.4084 -0.0555 -0.0452 0.1653  132 LYS A CG  
1098 C  CD  . LYS A 132 ? 0.3212 0.3312 0.7390 -0.0955 -0.1738 0.0643  132 LYS A CD  
1099 C  CE  . LYS A 132 ? 0.7311 0.1644 1.0177 -0.0747 -0.1121 0.0120  132 LYS A CE  
1100 N  NZ  . LYS A 132 ? 0.8360 0.3525 1.0567 -0.1137 0.1586  0.2654  132 LYS A NZ  
1101 N  N   . ALA A 133 ? 0.1766 0.1234 0.2075 -0.0496 0.0296  0.0268  133 ALA A N   
1102 C  CA  . ALA A 133 ? 0.1734 0.1607 0.1601 -0.0568 0.0143  0.0319  133 ALA A CA  
1103 C  C   . ALA A 133 ? 0.1862 0.1558 0.2014 -0.0279 0.0333  0.0119  133 ALA A C   
1104 O  O   . ALA A 133 ? 0.1429 0.1876 0.2262 -0.0264 0.0166  0.0223  133 ALA A O   
1105 C  CB  . ALA A 133 ? 0.1686 0.1195 0.1702 -0.0212 -0.0042 0.0055  133 ALA A CB  
1106 N  N   . VAL A 134 ? 0.1975 0.1388 0.2513 0.0194  0.0669  0.0809  134 VAL A N   
1107 C  CA  . VAL A 134 ? 0.2537 0.2151 0.2958 0.0751  0.0666  0.1138  134 VAL A CA  
1108 C  C   . VAL A 134 ? 0.1855 0.3389 0.3199 0.0631  0.0835  0.1515  134 VAL A C   
1109 O  O   . VAL A 134 ? 0.1831 0.3685 0.5551 0.0795  0.0779  0.2614  134 VAL A O   
1110 C  CB  . VAL A 134 ? 0.3784 0.2493 0.3024 0.0274  0.1159  0.1271  134 VAL A CB  
1111 C  CG1 . VAL A 134 ? 0.3594 0.2136 0.1991 0.0412  0.1070  0.0274  134 VAL A CG1 
1112 C  CG2 . VAL A 134 ? 0.2473 0.3273 0.4034 0.0479  0.1222  0.1947  134 VAL A CG2 
1113 N  N   . GLN A 135 ? 0.1921 0.3393 0.3886 -0.0370 0.0530  0.2055  135 GLN A N   
1114 C  CA  . GLN A 135 ? 0.2242 0.4003 0.4918 -0.0232 -0.0407 0.1867  135 GLN A CA  
1115 C  C   . GLN A 135 ? 0.2082 0.3215 0.4096 -0.1008 -0.1140 0.1518  135 GLN A C   
1116 O  O   . GLN A 135 ? 0.1964 0.4607 0.3475 -0.1133 -0.0806 0.1405  135 GLN A O   
1117 C  CB  . GLN A 135 ? 0.2892 0.3899 0.5484 -0.0412 -0.1209 0.1218  135 GLN A CB  
1118 C  CG  . GLN A 135 ? 0.3349 0.7465 0.5308 0.0167  -0.0855 0.1799  135 GLN A CG  
1119 C  CD  . GLN A 135 ? 0.6664 0.9431 0.8207 0.0804  0.0073  0.4043  135 GLN A CD  
1120 O  OE1 . GLN A 135 ? 0.2764 0.5453 0.7318 -0.0423 0.0596  0.1701  135 GLN A OE1 
1121 N  NE2 . GLN A 135 ? 0.7939 0.7827 0.8103 -0.2002 -0.2693 0.1996  135 GLN A NE2 
1122 N  N   . GLN A 136 ? 0.1791 0.2377 0.2866 -0.0463 -0.0141 0.1182  136 GLN A N   
1123 C  CA  . GLN A 136 ? 0.2159 0.1443 0.2179 -0.0253 -0.0673 -0.0002 136 GLN A CA  
1124 C  C   . GLN A 136 ? 0.1568 0.1571 0.2081 0.0100  -0.0208 -0.0206 136 GLN A C   
1125 O  O   . GLN A 136 ? 0.2034 0.1571 0.1456 -0.0179 0.0036  0.0051  136 GLN A O   
1126 C  CB  . GLN A 136 ? 0.2434 0.1314 0.2654 -0.0109 -0.0638 0.0417  136 GLN A CB  
1127 C  CG  . GLN A 136 ? 0.3046 0.1363 0.2899 -0.0315 -0.0488 0.0462  136 GLN A CG  
1128 C  CD  . GLN A 136 ? 0.3085 0.2189 0.2943 -0.0642 -0.0945 0.0791  136 GLN A CD  
1129 O  OE1 . GLN A 136 ? 0.3168 0.3141 0.2893 -0.0255 -0.1054 -0.0794 136 GLN A OE1 
1130 N  NE2 . GLN A 136 ? 0.4259 0.3703 0.3163 -0.0991 -0.0117 0.0980  136 GLN A NE2 
1131 N  N   A PRO A 137 ? 0.1727 0.1982 0.2029 0.0156  -0.0234 -0.0406 137 PRO A N   
1132 N  N   B PRO A 137 ? 0.2167 0.1650 0.2002 0.0057  -0.0310 -0.0513 137 PRO A N   
1133 C  CA  A PRO A 137 ? 0.1863 0.2046 0.1517 0.0417  -0.0212 -0.0379 137 PRO A CA  
1134 C  CA  B PRO A 137 ? 0.2029 0.1870 0.1574 0.0365  -0.0176 -0.0317 137 PRO A CA  
1135 C  C   A PRO A 137 ? 0.2067 0.1930 0.1235 0.0149  0.0050  -0.0021 137 PRO A C   
1136 C  C   B PRO A 137 ? 0.2136 0.1858 0.1210 0.0179  0.0131  -0.0013 137 PRO A C   
1137 O  O   A PRO A 137 ? 0.1967 0.1761 0.2445 -0.0035 -0.0078 -0.0032 137 PRO A O   
1138 O  O   B PRO A 137 ? 0.2113 0.1644 0.2409 0.0165  0.0162  0.0017  137 PRO A O   
1139 C  CB  A PRO A 137 ? 0.2341 0.3190 0.1586 0.0237  -0.0567 -0.0447 137 PRO A CB  
1140 C  CB  B PRO A 137 ? 0.2664 0.2733 0.1597 0.0165  -0.0458 -0.0347 137 PRO A CB  
1141 C  CG  A PRO A 137 ? 0.2972 0.3379 0.1833 0.0076  -0.0802 -0.1218 137 PRO A CG  
1142 C  CG  B PRO A 137 ? 0.2761 0.3068 0.2034 -0.0142 -0.0484 -0.0451 137 PRO A CG  
1143 C  CD  A PRO A 137 ? 0.1536 0.2966 0.2545 -0.0029 -0.0563 -0.1018 137 PRO A CD  
1144 C  CD  B PRO A 137 ? 0.2528 0.2262 0.2208 -0.0239 -0.0662 -0.0666 137 PRO A CD  
1145 N  N   . ASP A 138 ? 0.1765 0.1967 0.1301 0.0107  0.0058  0.0003  138 ASP A N   
1146 C  CA  . ASP A 138 ? 0.1696 0.2132 0.1271 0.0111  0.0132  -0.0148 138 ASP A CA  
1147 C  C   . ASP A 138 ? 0.1808 0.1313 0.1395 -0.0086 0.0006  -0.0261 138 ASP A C   
1148 O  O   . ASP A 138 ? 0.1779 0.1622 0.1684 0.0139  0.0029  -0.0138 138 ASP A O   
1149 C  CB  . ASP A 138 ? 0.2636 0.2018 0.1368 0.0553  0.0342  -0.0034 138 ASP A CB  
1150 C  CG  . ASP A 138 ? 0.2262 0.2235 0.1583 0.0370  -0.0041 -0.0040 138 ASP A CG  
1151 O  OD1 . ASP A 138 ? 0.2595 0.1852 0.2057 0.0409  0.0020  -0.0408 138 ASP A OD1 
1152 O  OD2 . ASP A 138 ? 0.2517 0.2438 0.2161 0.0201  0.0272  -0.0537 138 ASP A OD2 
1153 N  N   . GLY A 139 ? 0.1892 0.1034 0.1149 -0.0126 0.0031  0.0020  139 GLY A N   
1154 C  CA  . GLY A 139 ? 0.1711 0.1098 0.1143 -0.0233 -0.0220 0.0004  139 GLY A CA  
1155 C  C   . GLY A 139 ? 0.1352 0.0986 0.1314 -0.0106 -0.0127 -0.0034 139 GLY A C   
1156 O  O   . GLY A 139 ? 0.1662 0.0955 0.1328 -0.0092 -0.0103 -0.0008 139 GLY A O   
1157 N  N   . LEU A 140 ? 0.1298 0.0874 0.1481 -0.0085 0.0010  -0.0320 140 LEU A N   
1158 C  CA  . LEU A 140 ? 0.1353 0.0748 0.1036 -0.0183 0.0248  -0.0161 140 LEU A CA  
1159 C  C   . LEU A 140 ? 0.1181 0.0810 0.1210 -0.0136 0.0081  -0.0046 140 LEU A C   
1160 O  O   . LEU A 140 ? 0.1389 0.0883 0.1190 -0.0181 0.0003  -0.0088 140 LEU A O   
1161 C  CB  . LEU A 140 ? 0.1213 0.1084 0.1453 0.0067  0.0287  -0.0100 140 LEU A CB  
1162 C  CG  . LEU A 140 ? 0.1650 0.1363 0.1817 0.0402  0.0584  0.0247  140 LEU A CG  
1163 C  CD1 . LEU A 140 ? 0.1866 0.1951 0.1658 0.0649  0.0491  -0.0149 140 LEU A CD1 
1164 C  CD2 . LEU A 140 ? 0.2613 0.1662 0.2215 0.0690  0.0527  0.0454  140 LEU A CD2 
1165 N  N   . ALA A 141 ? 0.1210 0.0860 0.1389 -0.0117 -0.0160 0.0086  141 ALA A N   
1166 C  CA  . ALA A 141 ? 0.1395 0.0806 0.1453 -0.0200 0.0216  0.0011  141 ALA A CA  
1167 C  C   . ALA A 141 ? 0.1012 0.0946 0.1280 0.0032  -0.0152 0.0089  141 ALA A C   
1168 O  O   . ALA A 141 ? 0.1307 0.0838 0.1507 0.0074  -0.0287 0.0236  141 ALA A O   
1169 C  CB  . ALA A 141 ? 0.1147 0.1260 0.1700 -0.0168 0.0171  0.0297  141 ALA A CB  
1170 N  N   . VAL A 142 ? 0.1165 0.0833 0.1380 0.0025  -0.0082 0.0012  142 VAL A N   
1171 C  CA  . VAL A 142 ? 0.1223 0.0915 0.1310 -0.0094 0.0143  -0.0008 142 VAL A CA  
1172 C  C   . VAL A 142 ? 0.1256 0.0967 0.0959 -0.0075 0.0145  0.0124  142 VAL A C   
1173 O  O   . VAL A 142 ? 0.1303 0.0995 0.0986 0.0006  -0.0044 0.0016  142 VAL A O   
1174 C  CB  . VAL A 142 ? 0.1134 0.0897 0.1005 0.0011  -0.0012 0.0006  142 VAL A CB  
1175 C  CG1 . VAL A 142 ? 0.1533 0.0891 0.1120 0.0036  -0.0091 -0.0106 142 VAL A CG1 
1176 C  CG2 . VAL A 142 ? 0.1319 0.1364 0.1270 -0.0391 -0.0009 0.0048  142 VAL A CG2 
1177 N  N   . LEU A 143 ? 0.1108 0.0716 0.1446 -0.0071 -0.0089 0.0118  143 LEU A N   
1178 C  CA  . LEU A 143 ? 0.1056 0.0736 0.1278 -0.0086 -0.0075 0.0125  143 LEU A CA  
1179 C  C   . LEU A 143 ? 0.1228 0.0885 0.1151 -0.0177 0.0017  0.0122  143 LEU A C   
1180 O  O   . LEU A 143 ? 0.1522 0.0898 0.1212 -0.0240 0.0044  0.0166  143 LEU A O   
1181 C  CB  . LEU A 143 ? 0.1059 0.1409 0.1744 -0.0186 -0.0280 0.0196  143 LEU A CB  
1182 C  CG  . LEU A 143 ? 0.1099 0.1544 0.1935 -0.0210 -0.0199 0.0554  143 LEU A CG  
1183 C  CD1 . LEU A 143 ? 0.1472 0.1819 0.1890 -0.0633 -0.0259 0.0396  143 LEU A CD1 
1184 C  CD2 . LEU A 143 ? 0.1267 0.1539 0.2363 0.0218  -0.0140 0.0245  143 LEU A CD2 
1185 N  N   . GLY A 144 ? 0.1176 0.0788 0.1195 -0.0037 -0.0083 0.0065  144 GLY A N   
1186 C  CA  . GLY A 144 ? 0.1212 0.0705 0.1288 -0.0210 0.0135  0.0003  144 GLY A CA  
1187 C  C   . GLY A 144 ? 0.0969 0.0732 0.1101 -0.0048 -0.0099 0.0066  144 GLY A C   
1188 O  O   . GLY A 144 ? 0.1456 0.0889 0.1386 -0.0100 0.0124  0.0163  144 GLY A O   
1189 N  N   . ILE A 145 ? 0.1181 0.0790 0.1220 -0.0076 -0.0098 -0.0088 145 ILE A N   
1190 C  CA  . ILE A 145 ? 0.1224 0.0729 0.1255 -0.0073 -0.0282 0.0026  145 ILE A CA  
1191 C  C   . ILE A 145 ? 0.1240 0.0869 0.1216 -0.0089 -0.0115 0.0062  145 ILE A C   
1192 O  O   . ILE A 145 ? 0.1328 0.0926 0.1317 -0.0133 0.0010  0.0038  145 ILE A O   
1193 C  CB  . ILE A 145 ? 0.1195 0.0891 0.1374 -0.0036 -0.0218 0.0035  145 ILE A CB  
1194 C  CG1 . ILE A 145 ? 0.1533 0.1030 0.1847 0.0268  -0.0263 0.0115  145 ILE A CG1 
1195 C  CG2 . ILE A 145 ? 0.1374 0.1248 0.1948 -0.0316 -0.0499 0.0051  145 ILE A CG2 
1196 C  CD1 . ILE A 145 ? 0.1400 0.1154 0.1830 0.0152  -0.0348 0.0146  145 ILE A CD1 
1197 N  N   . PHE A 146 ? 0.1317 0.0689 0.1205 -0.0105 -0.0133 -0.0033 146 PHE A N   
1198 C  CA  . PHE A 146 ? 0.1428 0.0725 0.1159 0.0039  0.0011  -0.0037 146 PHE A CA  
1199 C  C   . PHE A 146 ? 0.1320 0.0777 0.1414 -0.0240 -0.0025 0.0074  146 PHE A C   
1200 O  O   . PHE A 146 ? 0.1310 0.0971 0.1569 -0.0019 0.0009  -0.0055 146 PHE A O   
1201 C  CB  . PHE A 146 ? 0.1522 0.1046 0.1142 -0.0153 -0.0223 0.0105  146 PHE A CB  
1202 C  CG  . PHE A 146 ? 0.1210 0.0729 0.1155 0.0057  -0.0192 0.0140  146 PHE A CG  
1203 C  CD1 . PHE A 146 ? 0.1198 0.0934 0.1538 0.0041  -0.0122 -0.0003 146 PHE A CD1 
1204 C  CD2 . PHE A 146 ? 0.1339 0.0806 0.1284 -0.0133 -0.0018 0.0171  146 PHE A CD2 
1205 C  CE1 . PHE A 146 ? 0.1425 0.0907 0.1192 -0.0017 -0.0054 0.0039  146 PHE A CE1 
1206 C  CE2 . PHE A 146 ? 0.1277 0.0786 0.1341 -0.0186 -0.0013 0.0187  146 PHE A CE2 
1207 C  CZ  . PHE A 146 ? 0.1310 0.0861 0.1235 -0.0070 0.0134  0.0223  146 PHE A CZ  
1208 N  N   . LEU A 147 ? 0.1461 0.1068 0.1312 -0.0170 0.0033  -0.0137 147 LEU A N   
1209 C  CA  . LEU A 147 ? 0.1612 0.0786 0.1298 -0.0105 -0.0063 -0.0009 147 LEU A CA  
1210 C  C   . LEU A 147 ? 0.1429 0.0865 0.1219 -0.0068 -0.0248 -0.0017 147 LEU A C   
1211 O  O   . LEU A 147 ? 0.1416 0.1054 0.1666 -0.0195 -0.0086 0.0104  147 LEU A O   
1212 C  CB  . LEU A 147 ? 0.1590 0.1055 0.1231 -0.0029 -0.0088 0.0194  147 LEU A CB  
1213 C  CG  . LEU A 147 ? 0.1590 0.0797 0.1453 -0.0176 -0.0227 0.0003  147 LEU A CG  
1214 C  CD1 . LEU A 147 ? 0.2125 0.0856 0.1590 -0.0157 -0.0143 -0.0032 147 LEU A CD1 
1215 C  CD2 . LEU A 147 ? 0.2280 0.1137 0.1267 -0.0303 -0.0178 0.0085  147 LEU A CD2 
1216 N  N   . LYS A 148 ? 0.1700 0.0901 0.1449 -0.0233 -0.0189 -0.0161 148 LYS A N   
1217 C  CA  . LYS A 148 ? 0.1544 0.0820 0.1684 -0.0204 -0.0284 0.0212  148 LYS A CA  
1218 C  C   . LYS A 148 ? 0.1673 0.0946 0.2025 -0.0255 -0.0376 0.0000  148 LYS A C   
1219 O  O   . LYS A 148 ? 0.2093 0.1259 0.1863 0.0159  -0.0523 -0.0204 148 LYS A O   
1220 C  CB  . LYS A 148 ? 0.1684 0.1863 0.1919 -0.0203 -0.0071 0.0348  148 LYS A CB  
1221 C  CG  . LYS A 148 ? 0.1888 0.1759 0.2057 -0.0094 0.0358  0.0303  148 LYS A CG  
1222 C  CD  . LYS A 148 ? 0.3031 0.2174 0.2380 0.0134  0.0722  0.0652  148 LYS A CD  
1223 C  CE  . LYS A 148 ? 0.3163 0.4109 0.3590 0.0003  0.1690  0.0571  148 LYS A CE  
1224 N  NZ  . LYS A 148 ? 0.5585 0.5123 0.4521 -0.1770 0.1055  0.1885  148 LYS A NZ  
1225 N  N   . VAL A 149 ? 0.2128 0.0612 0.1956 -0.0336 -0.0354 0.0058  149 VAL A N   
1226 C  CA  . VAL A 149 ? 0.1841 0.0892 0.1892 -0.0322 -0.0274 -0.0034 149 VAL A CA  
1227 C  C   . VAL A 149 ? 0.2300 0.0871 0.1932 -0.0559 -0.0364 0.0138  149 VAL A C   
1228 O  O   . VAL A 149 ? 0.2486 0.1039 0.2085 -0.0376 -0.0454 0.0304  149 VAL A O   
1229 C  CB  . VAL A 149 ? 0.1880 0.1242 0.1957 -0.0126 -0.0220 0.0044  149 VAL A CB  
1230 C  CG1 . VAL A 149 ? 0.2424 0.1711 0.2174 -0.0475 -0.0710 0.0036  149 VAL A CG1 
1231 C  CG2 . VAL A 149 ? 0.2138 0.1391 0.2257 -0.0372 -0.0281 -0.0072 149 VAL A CG2 
1232 N  N   . GLY A 150 ? 0.1747 0.1230 0.2020 -0.0478 -0.0234 -0.0197 150 GLY A N   
1233 C  CA  . GLY A 150 ? 0.1959 0.1310 0.2495 -0.0625 -0.0443 0.0144  150 GLY A CA  
1234 C  C   . GLY A 150 ? 0.1826 0.1529 0.2077 -0.0549 -0.0262 -0.0194 150 GLY A C   
1235 O  O   . GLY A 150 ? 0.2255 0.1356 0.2020 -0.0356 -0.0245 -0.0059 150 GLY A O   
1236 N  N   A SER A 151 ? 0.2045 0.0934 0.2269 -0.0216 -0.0205 0.0043  151 SER A N   
1237 N  N   B SER A 151 ? 0.2068 0.1034 0.2359 -0.0194 -0.0245 0.0009  151 SER A N   
1238 C  CA  A SER A 151 ? 0.1592 0.1562 0.2555 -0.0268 -0.0358 0.0017  151 SER A CA  
1239 C  CA  B SER A 151 ? 0.2347 0.1500 0.2317 -0.0080 -0.0381 0.0061  151 SER A CA  
1240 C  C   A SER A 151 ? 0.1978 0.1262 0.1779 -0.0373 -0.0438 -0.0476 151 SER A C   
1241 C  C   B SER A 151 ? 0.2139 0.1410 0.1765 -0.0058 -0.0236 -0.0280 151 SER A C   
1242 O  O   A SER A 151 ? 0.1928 0.1449 0.1991 -0.0453 -0.0454 -0.0513 151 SER A O   
1243 O  O   B SER A 151 ? 0.2615 0.1190 0.1707 -0.0212 -0.0439 0.0072  151 SER A O   
1244 C  CB  A SER A 151 ? 0.1208 0.1716 0.3902 -0.0354 -0.0440 0.0022  151 SER A CB  
1245 C  CB  B SER A 151 ? 0.2215 0.1784 0.3759 -0.0484 -0.0104 -0.0080 151 SER A CB  
1246 O  OG  A SER A 151 ? 0.1991 0.3268 0.3335 -0.0095 -0.0306 -0.0787 151 SER A OG  
1247 O  OG  B SER A 151 ? 0.1815 0.2444 0.3891 -0.0709 0.0019  0.0295  151 SER A OG  
1248 N  N   . ALA A 152 ? 0.1917 0.1301 0.1799 -0.0339 -0.0366 -0.0145 152 ALA A N   
1249 C  CA  . ALA A 152 ? 0.1946 0.1289 0.1752 -0.0122 -0.0302 -0.0194 152 ALA A CA  
1250 C  C   . ALA A 152 ? 0.1859 0.1138 0.1993 -0.0069 -0.0315 -0.0057 152 ALA A C   
1251 O  O   . ALA A 152 ? 0.2340 0.1619 0.2172 -0.0115 -0.0097 -0.0168 152 ALA A O   
1252 C  CB  . ALA A 152 ? 0.2719 0.1766 0.1658 -0.0164 -0.0559 -0.0044 152 ALA A CB  
1253 N  N   . LYS A 153 ? 0.2377 0.0979 0.2244 -0.0058 -0.0456 0.0178  153 LYS A N   
1254 C  CA  . LYS A 153 ? 0.1862 0.1429 0.2452 0.0197  -0.0576 -0.0015 153 LYS A CA  
1255 C  C   . LYS A 153 ? 0.1980 0.1561 0.2539 0.0087  -0.0572 0.0027  153 LYS A C   
1256 O  O   . LYS A 153 ? 0.2116 0.1439 0.2142 -0.0122 -0.0754 0.0016  153 LYS A O   
1257 C  CB  . LYS A 153 ? 0.1812 0.1535 0.1909 0.0100  -0.0576 -0.0044 153 LYS A CB  
1258 C  CG  . LYS A 153 ? 0.2214 0.1647 0.2323 -0.0046 -0.0483 -0.0373 153 LYS A CG  
1259 C  CD  . LYS A 153 ? 0.3743 0.1386 0.1952 -0.0003 -0.0209 -0.0250 153 LYS A CD  
1260 C  CE  . LYS A 153 ? 0.5040 0.1540 0.2050 0.0110  -0.0243 -0.0200 153 LYS A CE  
1261 N  NZ  . LYS A 153 ? 0.5662 0.3242 0.2594 -0.0833 0.0231  0.0171  153 LYS A NZ  
1262 N  N   . PRO A 154 ? 0.1790 0.1576 0.2529 -0.0478 -0.0445 0.0306  154 PRO A N   
1263 C  CA  . PRO A 154 ? 0.1575 0.1913 0.2978 -0.0363 -0.0811 0.0553  154 PRO A CA  
1264 C  C   . PRO A 154 ? 0.1675 0.2009 0.2842 -0.0284 -0.0515 0.0411  154 PRO A C   
1265 O  O   . PRO A 154 ? 0.1939 0.2488 0.2588 -0.0063 -0.0585 0.0542  154 PRO A O   
1266 C  CB  . PRO A 154 ? 0.1529 0.1581 0.4686 -0.0447 -0.0480 0.0359  154 PRO A CB  
1267 C  CG  . PRO A 154 ? 0.1982 0.2023 0.3559 -0.0681 -0.0608 0.0402  154 PRO A CG  
1268 C  CD  . PRO A 154 ? 0.1654 0.2054 0.3118 -0.0414 -0.0357 0.0749  154 PRO A CD  
1269 N  N   . GLY A 155 ? 0.1612 0.1395 0.3021 0.0133  -0.0612 0.0369  155 GLY A N   
1270 C  CA  . GLY A 155 ? 0.1726 0.1446 0.3570 0.0114  -0.0368 0.0400  155 GLY A CA  
1271 C  C   . GLY A 155 ? 0.2013 0.1328 0.2647 -0.0177 -0.0171 0.0361  155 GLY A C   
1272 O  O   . GLY A 155 ? 0.2347 0.1332 0.3963 -0.0199 -0.0385 0.0588  155 GLY A O   
1273 N  N   . LEU A 156 ? 0.1784 0.1485 0.2258 0.0015  -0.0249 0.0108  156 LEU A N   
1274 C  CA  . LEU A 156 ? 0.1874 0.1334 0.1870 -0.0053 -0.0438 0.0128  156 LEU A CA  
1275 C  C   . LEU A 156 ? 0.2071 0.1258 0.1909 -0.0203 -0.0530 -0.0151 156 LEU A C   
1276 O  O   . LEU A 156 ? 0.1953 0.1411 0.1757 -0.0183 -0.0537 0.0147  156 LEU A O   
1277 C  CB  . LEU A 156 ? 0.1650 0.1313 0.2158 -0.0227 -0.0573 0.0223  156 LEU A CB  
1278 C  CG  . LEU A 156 ? 0.1694 0.1068 0.1729 -0.0340 -0.0447 0.0261  156 LEU A CG  
1279 C  CD1 . LEU A 156 ? 0.1865 0.1395 0.2117 -0.0597 -0.0536 0.0150  156 LEU A CD1 
1280 C  CD2 . LEU A 156 ? 0.2064 0.1235 0.1945 -0.0128 -0.0604 0.0321  156 LEU A CD2 
1281 N  N   . GLN A 157 ? 0.2043 0.1427 0.1928 -0.0461 -0.0539 0.0049  157 GLN A N   
1282 C  CA  . GLN A 157 ? 0.2305 0.1831 0.1874 -0.0646 -0.0630 -0.0194 157 GLN A CA  
1283 C  C   . GLN A 157 ? 0.2283 0.1671 0.2240 -0.0323 -0.0701 -0.0093 157 GLN A C   
1284 O  O   . GLN A 157 ? 0.2235 0.1608 0.2179 -0.0234 -0.0807 0.0079  157 GLN A O   
1285 C  CB  . GLN A 157 ? 0.2533 0.1576 0.2667 -0.0465 -0.1161 -0.0248 157 GLN A CB  
1286 C  CG  . GLN A 157 ? 0.3501 0.1289 0.2599 -0.0111 -0.0723 -0.0251 157 GLN A CG  
1287 C  CD  . GLN A 157 ? 0.3197 0.1195 0.1930 -0.0329 -0.0280 0.0005  157 GLN A CD  
1288 O  OE1 . GLN A 157 ? 0.3514 0.1366 0.2140 -0.0451 -0.0706 0.0116  157 GLN A OE1 
1289 N  NE2 . GLN A 157 ? 0.3401 0.1708 0.1949 -0.0643 -0.0751 -0.0212 157 GLN A NE2 
1290 N  N   . LYS A 158 ? 0.2165 0.1684 0.2219 -0.0329 -0.0632 -0.0106 158 LYS A N   
1291 C  CA  . LYS A 158 ? 0.2303 0.1756 0.2357 -0.0636 -0.0765 -0.0048 158 LYS A CA  
1292 C  C   . LYS A 158 ? 0.2183 0.1632 0.1691 -0.0071 -0.0509 -0.0067 158 LYS A C   
1293 O  O   . LYS A 158 ? 0.2670 0.1784 0.1630 -0.0556 -0.0535 0.0190  158 LYS A O   
1294 C  CB  . LYS A 158 ? 0.2948 0.2240 0.2273 -0.0055 -0.0747 -0.0098 158 LYS A CB  
1295 C  CG  . LYS A 158 ? 0.2906 0.3571 0.3378 -0.0618 -0.0641 -0.0389 158 LYS A CG  
1296 N  N   . VAL A 159 ? 0.1978 0.1262 0.1824 -0.0277 -0.0792 0.0006  159 VAL A N   
1297 C  CA  . VAL A 159 ? 0.1974 0.1244 0.1483 -0.0461 -0.0502 0.0138  159 VAL A CA  
1298 C  C   . VAL A 159 ? 0.2487 0.1472 0.1596 -0.0241 -0.0322 0.0200  159 VAL A C   
1299 O  O   . VAL A 159 ? 0.2262 0.1260 0.1901 -0.0247 -0.0491 -0.0094 159 VAL A O   
1300 C  CB  . VAL A 159 ? 0.2138 0.1256 0.1446 -0.0057 -0.0652 -0.0004 159 VAL A CB  
1301 C  CG1 . VAL A 159 ? 0.2034 0.1870 0.1747 -0.0550 -0.0518 0.0175  159 VAL A CG1 
1302 C  CG2 . VAL A 159 ? 0.2642 0.1368 0.1794 0.0116  -0.0528 -0.0275 159 VAL A CG2 
1303 N  N   . VAL A 160 ? 0.2308 0.1284 0.1431 -0.0168 -0.0363 0.0134  160 VAL A N   
1304 C  CA  . VAL A 160 ? 0.2662 0.1528 0.1812 -0.0111 0.0024  0.0093  160 VAL A CA  
1305 C  C   . VAL A 160 ? 0.2898 0.1465 0.1763 -0.0174 -0.0340 -0.0298 160 VAL A C   
1306 O  O   . VAL A 160 ? 0.2998 0.1526 0.1662 -0.0381 -0.0052 -0.0134 160 VAL A O   
1307 C  CB  . VAL A 160 ? 0.3791 0.1168 0.1815 -0.0083 -0.0228 0.0117  160 VAL A CB  
1308 C  CG1 . VAL A 160 ? 0.3327 0.1834 0.2400 -0.0367 -0.0271 -0.0256 160 VAL A CG1 
1309 C  CG2 . VAL A 160 ? 0.4102 0.1628 0.1899 0.0467  -0.0292 0.0055  160 VAL A CG2 
1310 N  N   . ASP A 161 ? 0.2758 0.1684 0.1571 -0.0502 -0.0509 -0.0155 161 ASP A N   
1311 C  CA  . ASP A 161 ? 0.3344 0.2350 0.1640 -0.0554 -0.0605 -0.0184 161 ASP A CA  
1312 C  C   . ASP A 161 ? 0.3464 0.2549 0.1686 -0.0730 -0.0734 -0.0034 161 ASP A C   
1313 O  O   . ASP A 161 ? 0.5144 0.3320 0.2000 -0.0915 -0.0012 -0.0153 161 ASP A O   
1314 C  CB  . ASP A 161 ? 0.3538 0.2575 0.2414 -0.1116 -0.0946 0.0533  161 ASP A CB  
1315 C  CG  . ASP A 161 ? 0.4307 0.2154 0.1874 -0.0844 0.0218  -0.0151 161 ASP A CG  
1316 O  OD1 . ASP A 161 ? 0.3958 0.3014 0.3596 -0.0691 -0.0565 -0.0987 161 ASP A OD1 
1317 O  OD2 . ASP A 161 ? 0.3616 0.3298 0.3570 -0.0269 -0.0829 -0.0386 161 ASP A OD2 
1318 N  N   . VAL A 162 ? 0.3341 0.2282 0.1353 -0.0479 -0.0873 0.0260  162 VAL A N   
1319 C  CA  . VAL A 162 ? 0.3044 0.2274 0.1486 -0.0257 -0.0369 0.0367  162 VAL A CA  
1320 C  C   . VAL A 162 ? 0.2963 0.1734 0.1585 -0.0104 -0.0420 0.0183  162 VAL A C   
1321 O  O   . VAL A 162 ? 0.3015 0.1822 0.1489 -0.0249 -0.0383 -0.0001 162 VAL A O   
1322 C  CB  . VAL A 162 ? 0.2798 0.2014 0.2451 0.0271  -0.0352 0.0526  162 VAL A CB  
1323 C  CG1 . VAL A 162 ? 0.4103 0.1671 0.2020 -0.0178 -0.0208 0.0072  162 VAL A CG1 
1324 C  CG2 . VAL A 162 ? 0.2994 0.2474 0.1973 0.0331  0.0114  0.0472  162 VAL A CG2 
1325 N  N   . LEU A 163 ? 0.2693 0.1406 0.1709 -0.0094 -0.0546 -0.0074 163 LEU A N   
1326 C  CA  . LEU A 163 ? 0.2256 0.1446 0.1597 0.0171  -0.0099 0.0034  163 LEU A CA  
1327 C  C   . LEU A 163 ? 0.3001 0.1780 0.1417 -0.0057 0.0004  -0.0055 163 LEU A C   
1328 O  O   . LEU A 163 ? 0.3017 0.2077 0.1388 -0.0279 0.0037  -0.0069 163 LEU A O   
1329 C  CB  . LEU A 163 ? 0.2920 0.1461 0.1310 -0.0100 -0.0369 -0.0107 163 LEU A CB  
1330 C  CG  . LEU A 163 ? 0.2775 0.1095 0.1323 -0.0163 0.0006  0.0326  163 LEU A CG  
1331 C  CD1 . LEU A 163 ? 0.2790 0.1644 0.1932 0.0157  -0.0054 0.0719  163 LEU A CD1 
1332 C  CD2 . LEU A 163 ? 0.2796 0.1353 0.1522 -0.0114 -0.0187 0.0210  163 LEU A CD2 
1333 N  N   . ASP A 164 ? 0.3903 0.1855 0.1429 -0.0375 -0.0026 -0.0059 164 ASP A N   
1334 C  CA  . ASP A 164 ? 0.4231 0.2512 0.1756 -0.0402 0.0168  -0.0185 164 ASP A CA  
1335 C  C   . ASP A 164 ? 0.4053 0.2694 0.1483 -0.0488 0.0336  -0.0309 164 ASP A C   
1336 O  O   . ASP A 164 ? 0.4251 0.3362 0.1898 -0.0095 0.0719  0.0132  164 ASP A O   
1337 C  CB  . ASP A 164 ? 0.5866 0.3810 0.2848 -0.0972 0.0185  -0.1632 164 ASP A CB  
1338 C  CG  . ASP A 164 ? 0.5292 0.6379 0.3907 -0.2006 -0.0644 -0.1062 164 ASP A CG  
1339 O  OD1 . ASP A 164 ? 0.6323 0.5578 0.3111 -0.2975 0.0027  -0.0205 164 ASP A OD1 
1340 O  OD2 . ASP A 164 ? 0.8089 0.9761 0.3691 -0.2366 0.1824  -0.2939 164 ASP A OD2 
1341 N  N   . SER A 165 ? 0.2926 0.2670 0.1353 -0.0715 -0.0234 0.0000  165 SER A N   
1342 C  CA  . SER A 165 ? 0.2759 0.2396 0.1531 -0.0172 -0.0255 0.0134  165 SER A CA  
1343 C  C   . SER A 165 ? 0.2395 0.2541 0.1461 -0.0089 -0.0069 0.0408  165 SER A C   
1344 O  O   . SER A 165 ? 0.2877 0.2411 0.1714 -0.0282 -0.0024 0.0284  165 SER A O   
1345 C  CB  . SER A 165 ? 0.3209 0.2817 0.2315 0.0247  0.0357  0.0592  165 SER A CB  
1346 O  OG  . SER A 165 ? 0.3353 0.2317 0.2381 -0.0297 -0.0587 0.0323  165 SER A OG  
1347 N  N   . ILE A 166 ? 0.2466 0.2104 0.1267 0.0078  -0.0325 0.0053  166 ILE A N   
1348 C  CA  . ILE A 166 ? 0.2158 0.1751 0.1716 -0.0103 0.0128  -0.0105 166 ILE A CA  
1349 C  C   . ILE A 166 ? 0.1920 0.2077 0.1334 -0.0142 0.0062  -0.0182 166 ILE A C   
1350 O  O   . ILE A 166 ? 0.2577 0.1860 0.1278 0.0004  -0.0046 0.0264  166 ILE A O   
1351 C  CB  . ILE A 166 ? 0.2293 0.1296 0.1425 -0.0284 0.0006  -0.0016 166 ILE A CB  
1352 C  CG1 . ILE A 166 ? 0.2364 0.1434 0.1267 -0.0489 -0.0018 -0.0026 166 ILE A CG1 
1353 C  CG2 . ILE A 166 ? 0.2473 0.1411 0.2133 -0.0120 -0.0228 0.0287  166 ILE A CG2 
1354 C  CD1 . ILE A 166 ? 0.2529 0.1741 0.1326 -0.0329 -0.0003 -0.0086 166 ILE A CD1 
1355 N  N   . LYS A 167 ? 0.2499 0.1741 0.1432 -0.0124 0.0188  -0.0022 167 LYS A N   
1356 C  CA  . LYS A 167 ? 0.2062 0.1835 0.1637 0.0095  -0.0245 -0.0443 167 LYS A CA  
1357 C  C   . LYS A 167 ? 0.1964 0.1635 0.1468 -0.0204 0.0293  0.0100  167 LYS A C   
1358 O  O   . LYS A 167 ? 0.2433 0.1672 0.1294 -0.0314 -0.0106 0.0013  167 LYS A O   
1359 C  CB  . LYS A 167 ? 0.2887 0.1676 0.1644 0.0006  -0.0061 -0.0522 167 LYS A CB  
1360 C  CG  . LYS A 167 ? 0.2971 0.2078 0.1777 0.0108  -0.0372 -0.0161 167 LYS A CG  
1361 C  CD  . LYS A 167 ? 0.4120 0.2323 0.2612 0.0769  -0.0922 -0.1136 167 LYS A CD  
1362 C  CE  . LYS A 167 ? 0.4718 0.2738 0.4412 0.0804  -0.0647 -0.0550 167 LYS A CE  
1363 N  NZ  . LYS A 167 ? 0.5439 0.7396 0.4456 -0.1582 -0.0606 -0.2656 167 LYS A NZ  
1364 N  N   . THR A 168 ? 0.2124 0.1533 0.1511 -0.0268 0.0306  0.0171  168 THR A N   
1365 C  CA  . THR A 168 ? 0.2179 0.1844 0.1395 -0.0227 0.0254  0.0160  168 THR A CA  
1366 C  C   . THR A 168 ? 0.1759 0.1526 0.1310 0.0149  0.0469  0.0108  168 THR A C   
1367 O  O   . THR A 168 ? 0.2179 0.1702 0.1725 0.0015  0.0204  0.0316  168 THR A O   
1368 C  CB  . THR A 168 ? 0.2512 0.1630 0.1547 -0.0063 0.0291  0.0092  168 THR A CB  
1369 O  OG1 . THR A 168 ? 0.2460 0.2297 0.1597 0.0128  0.0402  0.0337  168 THR A OG1 
1370 C  CG2 . THR A 168 ? 0.3096 0.1766 0.1618 0.0337  0.0639  -0.0159 168 THR A CG2 
1371 N  N   . LYS A 169 ? 0.2450 0.1532 0.1567 -0.0468 0.0220  0.0174  169 LYS A N   
1372 C  CA  . LYS A 169 ? 0.2312 0.1416 0.1562 -0.0293 0.0013  0.0208  169 LYS A CA  
1373 C  C   . LYS A 169 ? 0.1549 0.1575 0.2086 -0.0178 0.0618  0.0524  169 LYS A C   
1374 O  O   . LYS A 169 ? 0.2709 0.2096 0.1919 -0.0778 0.0725  0.0359  169 LYS A O   
1375 C  CB  . LYS A 169 ? 0.2073 0.1895 0.1619 -0.0258 0.0167  0.0178  169 LYS A CB  
1376 C  CG  . LYS A 169 ? 0.2606 0.2143 0.1985 -0.0964 0.0011  0.0444  169 LYS A CG  
1377 C  CD  . LYS A 169 ? 0.2488 0.2800 0.2035 -0.0683 0.0384  -0.0062 169 LYS A CD  
1378 C  CE  . LYS A 169 ? 0.5060 0.4463 0.5475 -0.1582 -0.1317 -0.1141 169 LYS A CE  
1379 N  N   . GLY A 170 ? 0.2314 0.1368 0.1992 -0.0076 0.0301  0.0244  170 GLY A N   
1380 C  CA  . GLY A 170 ? 0.2470 0.1712 0.2219 -0.0332 0.0129  0.0846  170 GLY A CA  
1381 C  C   . GLY A 170 ? 0.2861 0.1687 0.2509 0.0037  -0.0205 0.0499  170 GLY A C   
1382 O  O   . GLY A 170 ? 0.3132 0.1761 0.2922 -0.0038 0.0478  0.0891  170 GLY A O   
1383 N  N   . LYS A 171 ? 0.2456 0.1826 0.1718 -0.0472 0.0416  0.0513  171 LYS A N   
1384 C  CA  . LYS A 171 ? 0.2774 0.2177 0.1546 -0.0245 0.0228  0.0344  171 LYS A CA  
1385 C  C   . LYS A 171 ? 0.2291 0.1734 0.1453 0.0197  -0.0156 0.0362  171 LYS A C   
1386 O  O   . LYS A 171 ? 0.2531 0.1844 0.1460 0.0027  0.0150  0.0326  171 LYS A O   
1387 C  CB  . LYS A 171 ? 0.2225 0.1928 0.2096 -0.0059 0.0155  0.0295  171 LYS A CB  
1388 C  CG  . LYS A 171 ? 0.2225 0.3042 0.3040 0.0099  0.0314  -0.0971 171 LYS A CG  
1389 C  CD  . LYS A 171 ? 0.4871 0.3575 0.2986 -0.0545 0.0063  -0.0851 171 LYS A CD  
1390 C  CE  . LYS A 171 ? 0.9247 0.5504 0.4715 -0.0441 -0.3102 -0.0542 171 LYS A CE  
1391 N  NZ  . LYS A 171 ? 0.9606 0.3648 0.3523 -0.2039 0.0270  -0.0027 171 LYS A NZ  
1392 N  N   . SER A 172 ? 0.2222 0.2036 0.1443 0.0024  -0.0128 0.0671  172 SER A N   
1393 C  CA  . SER A 172 ? 0.2181 0.2377 0.1939 -0.0174 0.0135  0.0269  172 SER A CA  
1394 C  C   . SER A 172 ? 0.2621 0.1414 0.1474 0.0016  -0.0065 0.0357  172 SER A C   
1395 O  O   . SER A 172 ? 0.2873 0.2881 0.1535 0.0242  0.0091  0.0531  172 SER A O   
1396 C  CB  . SER A 172 ? 0.2501 0.2564 0.1465 -0.0655 -0.0375 0.0288  172 SER A CB  
1397 O  OG  . SER A 172 ? 0.2710 0.2570 0.2305 -0.0048 0.0051  0.0789  172 SER A OG  
1398 N  N   . ALA A 173 ? 0.2825 0.2258 0.1729 0.0420  0.0103  0.0370  173 ALA A N   
1399 C  CA  . ALA A 173 ? 0.3216 0.2075 0.1180 0.0431  -0.0124 0.0303  173 ALA A CA  
1400 C  C   . ALA A 173 ? 0.2361 0.2746 0.1647 0.0200  -0.0784 -0.0247 173 ALA A C   
1401 O  O   . ALA A 173 ? 0.2538 0.1794 0.1411 -0.0004 -0.0556 0.0188  173 ALA A O   
1402 C  CB  . ALA A 173 ? 0.4074 0.1939 0.1808 0.0637  -0.0662 0.0000  173 ALA A CB  
1403 N  N   . ASP A 174 ? 0.2256 0.3277 0.1727 0.0467  -0.0337 0.0394  174 ASP A N   
1404 C  CA  . ASP A 174 ? 0.2667 0.2779 0.1916 0.0502  -0.0298 0.0170  174 ASP A CA  
1405 C  C   . ASP A 174 ? 0.2713 0.2237 0.2575 0.0511  -0.0223 0.0127  174 ASP A C   
1406 O  O   . ASP A 174 ? 0.2800 0.2528 0.2682 0.0296  -0.0565 -0.0094 174 ASP A O   
1407 C  CB  . ASP A 174 ? 0.2673 0.4014 0.2649 0.0951  -0.0469 0.0644  174 ASP A CB  
1408 C  CG  . ASP A 174 ? 0.6628 0.5243 0.3353 -0.0662 -0.1155 0.1447  174 ASP A CG  
1409 O  OD1 . ASP A 174 ? 0.6289 0.6485 0.5466 -0.1824 -0.2369 0.1391  174 ASP A OD1 
1410 O  OD2 . ASP A 174 ? 0.5579 0.7871 0.3380 -0.0926 -0.0701 0.0884  174 ASP A OD2 
1411 N  N   . PHE A 175 ? 0.2293 0.1575 0.2279 -0.0256 -0.0438 -0.0023 175 PHE A N   
1412 C  CA  . PHE A 175 ? 0.2326 0.1553 0.2293 0.0109  -0.0439 0.0456  175 PHE A CA  
1413 C  C   . PHE A 175 ? 0.2586 0.1367 0.2432 -0.0149 -0.0458 0.0447  175 PHE A C   
1414 O  O   . PHE A 175 ? 0.2886 0.2108 0.2599 0.0784  -0.1227 -0.0163 175 PHE A O   
1415 C  CB  . PHE A 175 ? 0.2595 0.1615 0.2237 -0.0164 -0.0528 0.0610  175 PHE A CB  
1416 C  CG  . PHE A 175 ? 0.2452 0.1165 0.2080 0.0039  -0.0114 0.0102  175 PHE A CG  
1417 C  CD1 . PHE A 175 ? 0.2950 0.1428 0.1834 -0.0146 -0.0491 0.0129  175 PHE A CD1 
1418 C  CD2 . PHE A 175 ? 0.2559 0.1600 0.1867 0.0237  -0.0380 0.0265  175 PHE A CD2 
1419 C  CE1 . PHE A 175 ? 0.3523 0.1287 0.2345 0.0061  0.0340  0.0270  175 PHE A CE1 
1420 C  CE2 . PHE A 175 ? 0.2835 0.1461 0.2266 0.0325  -0.0455 0.0389  175 PHE A CE2 
1421 C  CZ  . PHE A 175 ? 0.2547 0.1866 0.1949 0.0200  -0.0274 0.0055  175 PHE A CZ  
1422 N  N   . THR A 176 ? 0.2578 0.1865 0.1877 0.0162  -0.0425 0.0397  176 THR A N   
1423 C  CA  . THR A 176 ? 0.2273 0.1829 0.1529 0.0084  -0.0322 0.0641  176 THR A CA  
1424 C  C   . THR A 176 ? 0.2020 0.1411 0.1604 0.0186  -0.0436 0.0438  176 THR A C   
1425 O  O   . THR A 176 ? 0.2495 0.1571 0.1694 -0.0006 -0.0595 0.0413  176 THR A O   
1426 C  CB  . THR A 176 ? 0.2233 0.2029 0.2237 0.0105  -0.0831 0.0809  176 THR A CB  
1427 O  OG1 . THR A 176 ? 0.4546 0.2543 0.1823 0.0731  -0.0781 0.0673  176 THR A OG1 
1428 C  CG2 . THR A 176 ? 0.2977 0.2960 0.3850 -0.0591 -0.0916 0.1820  176 THR A CG2 
1429 N  N   . ASN A 177 ? 0.2107 0.1820 0.1568 -0.0025 -0.0433 0.0328  177 ASN A N   
1430 C  CA  . ASN A 177 ? 0.2175 0.1665 0.1603 -0.0115 -0.0464 0.0507  177 ASN A CA  
1431 C  C   . ASN A 177 ? 0.2551 0.1346 0.1647 -0.0071 -0.0759 0.0184  177 ASN A C   
1432 O  O   . ASN A 177 ? 0.2875 0.1942 0.2776 -0.0429 -0.1082 0.0681  177 ASN A O   
1433 C  CB  . ASN A 177 ? 0.2585 0.1639 0.2136 0.0079  -0.1005 0.0423  177 ASN A CB  
1434 C  CG  . ASN A 177 ? 0.2806 0.1847 0.1993 0.0634  -0.0765 0.0425  177 ASN A CG  
1435 O  OD1 . ASN A 177 ? 0.2964 0.2020 0.2946 0.0390  -0.0218 0.0540  177 ASN A OD1 
1436 N  ND2 . ASN A 177 ? 0.2649 0.2081 0.1829 0.0194  -0.0778 0.0332  177 ASN A ND2 
1437 N  N   . PHE A 178 ? 0.2534 0.1456 0.1287 -0.0034 -0.0557 0.0369  178 PHE A N   
1438 C  CA  . PHE A 178 ? 0.2432 0.1562 0.1364 -0.0196 -0.0626 0.0505  178 PHE A CA  
1439 C  C   . PHE A 178 ? 0.2426 0.1758 0.1217 -0.0533 -0.0792 0.0354  178 PHE A C   
1440 O  O   . PHE A 178 ? 0.2842 0.1507 0.1463 -0.0620 -0.0723 0.0341  178 PHE A O   
1441 C  CB  . PHE A 178 ? 0.2503 0.1661 0.1314 -0.0036 -0.0403 0.0491  178 PHE A CB  
1442 C  CG  . PHE A 178 ? 0.2327 0.1727 0.1682 -0.0280 -0.0596 0.0613  178 PHE A CG  
1443 C  CD1 . PHE A 178 ? 0.2638 0.1658 0.1856 -0.0629 -0.0122 0.0555  178 PHE A CD1 
1444 C  CD2 . PHE A 178 ? 0.1752 0.2030 0.1428 0.0139  -0.0229 0.0659  178 PHE A CD2 
1445 C  CE1 . PHE A 178 ? 0.3579 0.1747 0.1549 -0.0352 -0.0335 0.0487  178 PHE A CE1 
1446 C  CE2 . PHE A 178 ? 0.2201 0.1768 0.1508 -0.0129 -0.0425 0.0484  178 PHE A CE2 
1447 C  CZ  . PHE A 178 ? 0.2142 0.1932 0.1511 -0.0269 -0.0148 0.0266  178 PHE A CZ  
1448 N  N   . ASP A 179 ? 0.2345 0.1770 0.1718 -0.0262 -0.0651 0.0516  179 ASP A N   
1449 C  CA  . ASP A 179 ? 0.1820 0.2136 0.1831 -0.0035 -0.0488 0.0823  179 ASP A CA  
1450 C  C   . ASP A 179 ? 0.1837 0.1497 0.1632 -0.0106 -0.0530 0.0436  179 ASP A C   
1451 O  O   . ASP A 179 ? 0.2118 0.1446 0.1909 -0.0203 -0.0273 0.0368  179 ASP A O   
1452 C  CB  . ASP A 179 ? 0.1765 0.2780 0.2122 -0.0042 -0.0642 0.0620  179 ASP A CB  
1453 C  CG  . ASP A 179 ? 0.1863 0.2289 0.2825 -0.0201 -0.0447 0.0358  179 ASP A CG  
1454 O  OD1 . ASP A 179 ? 0.1694 0.1826 0.2664 0.0113  -0.0535 0.0451  179 ASP A OD1 
1455 O  OD2 . ASP A 179 ? 0.1678 0.6347 0.3027 -0.0495 -0.0465 0.0223  179 ASP A OD2 
1456 N  N   . PRO A 180 ? 0.1524 0.1313 0.1659 -0.0133 -0.0414 0.0337  180 PRO A N   
1457 C  CA  . PRO A 180 ? 0.1511 0.1601 0.1514 -0.0187 -0.0286 0.0455  180 PRO A CA  
1458 C  C   . PRO A 180 ? 0.1574 0.1435 0.1716 -0.0236 -0.0234 0.0387  180 PRO A C   
1459 O  O   . PRO A 180 ? 0.2028 0.1452 0.1655 -0.0070 -0.0491 0.0325  180 PRO A O   
1460 C  CB  . PRO A 180 ? 0.1878 0.1470 0.2025 -0.0139 -0.0545 0.0194  180 PRO A CB  
1461 C  CG  . PRO A 180 ? 0.1966 0.1411 0.1766 -0.0183 -0.0501 0.0362  180 PRO A CG  
1462 C  CD  . PRO A 180 ? 0.1969 0.1253 0.1951 -0.0200 -0.0818 0.0099  180 PRO A CD  
1463 N  N   . ARG A 181 ? 0.1373 0.1726 0.1565 -0.0177 -0.0086 0.0198  181 ARG A N   
1464 C  CA  . ARG A 181 ? 0.1338 0.1860 0.2025 -0.0216 -0.0026 0.0152  181 ARG A CA  
1465 C  C   . ARG A 181 ? 0.1734 0.1860 0.1816 -0.0352 -0.0664 0.0396  181 ARG A C   
1466 O  O   . ARG A 181 ? 0.1610 0.1775 0.2341 -0.0102 -0.0373 0.0658  181 ARG A O   
1467 C  CB  . ARG A 181 ? 0.1305 0.1723 0.2904 -0.0158 -0.0251 0.0655  181 ARG A CB  
1468 C  CG  . ARG A 181 ? 0.1794 0.1830 0.2456 -0.0024 -0.0158 0.0458  181 ARG A CG  
1469 C  CD  . ARG A 181 ? 0.1758 0.1967 0.2722 -0.0078 0.0086  0.0683  181 ARG A CD  
1470 N  NE  . ARG A 181 ? 0.2104 0.1763 0.2883 -0.0073 -0.0016 0.0732  181 ARG A NE  
1471 C  CZ  . ARG A 181 ? 0.2205 0.2091 0.2675 0.0035  0.0372  0.0718  181 ARG A CZ  
1472 N  NH1 . ARG A 181 ? 0.1888 0.3055 0.3876 0.0458  0.0576  0.0554  181 ARG A NH1 
1473 N  NH2 . ARG A 181 ? 0.2132 0.3148 0.3287 0.0337  0.0044  0.1301  181 ARG A NH2 
1474 N  N   . GLY A 182 ? 0.1763 0.1388 0.1946 0.0185  -0.0538 0.0259  182 GLY A N   
1475 C  CA  . GLY A 182 ? 0.2197 0.1222 0.2490 0.0081  -0.0659 0.0155  182 GLY A CA  
1476 C  C   . GLY A 182 ? 0.1876 0.1303 0.2020 0.0041  -0.0416 0.0004  182 GLY A C   
1477 O  O   . GLY A 182 ? 0.2606 0.1259 0.2780 -0.0006 -0.1117 -0.0005 182 GLY A O   
1478 N  N   . LEU A 183 ? 0.2014 0.1386 0.1698 -0.0110 -0.0573 0.0328  183 LEU A N   
1479 C  CA  . LEU A 183 ? 0.1848 0.1549 0.1766 0.0013  -0.0401 0.0308  183 LEU A CA  
1480 C  C   . LEU A 183 ? 0.1761 0.1138 0.1558 -0.0140 -0.0396 0.0106  183 LEU A C   
1481 O  O   . LEU A 183 ? 0.1969 0.1608 0.1991 0.0047  -0.0305 0.0526  183 LEU A O   
1482 C  CB  . LEU A 183 ? 0.1605 0.1756 0.1733 0.0281  -0.0116 0.0680  183 LEU A CB  
1483 C  CG  . LEU A 183 ? 0.2096 0.1403 0.1550 0.0137  -0.0207 0.0268  183 LEU A CG  
1484 C  CD1 . LEU A 183 ? 0.1987 0.2316 0.2038 -0.0010 -0.0245 0.0895  183 LEU A CD1 
1485 C  CD2 . LEU A 183 ? 0.3033 0.1568 0.2298 0.0029  -0.0205 -0.0133 183 LEU A CD2 
1486 N  N   . LEU A 184 ? 0.1799 0.1508 0.1751 -0.0027 -0.0200 0.0344  184 LEU A N   
1487 C  CA  . LEU A 184 ? 0.1844 0.1233 0.1985 -0.0482 -0.0332 0.0254  184 LEU A CA  
1488 C  C   . LEU A 184 ? 0.2145 0.1770 0.2203 -0.0768 -0.0712 0.0697  184 LEU A C   
1489 O  O   . LEU A 184 ? 0.2968 0.2863 0.2979 -0.1556 -0.1594 0.1331  184 LEU A O   
1490 C  CB  . LEU A 184 ? 0.1826 0.1445 0.1888 -0.0308 -0.0265 0.0260  184 LEU A CB  
1491 C  CG  . LEU A 184 ? 0.1301 0.1556 0.2025 -0.0127 -0.0185 0.0414  184 LEU A CG  
1492 C  CD1 . LEU A 184 ? 0.1914 0.2011 0.2150 0.0267  -0.0230 0.0284  184 LEU A CD1 
1493 C  CD2 . LEU A 184 ? 0.1434 0.1867 0.2621 -0.0217 -0.0575 0.0443  184 LEU A CD2 
1494 N  N   . PRO A 185 ? 0.1445 0.1701 0.2213 -0.0302 -0.0498 0.0629  185 PRO A N   
1495 C  CA  . PRO A 185 ? 0.1348 0.1596 0.2238 -0.0396 -0.0403 0.0545  185 PRO A CA  
1496 C  C   . PRO A 185 ? 0.1223 0.1698 0.2570 -0.0198 -0.0535 0.1087  185 PRO A C   
1497 O  O   . PRO A 185 ? 0.1192 0.1515 0.3638 -0.0103 -0.0608 0.1069  185 PRO A O   
1498 C  CB  . PRO A 185 ? 0.1605 0.1604 0.2000 -0.0063 -0.0109 0.0523  185 PRO A CB  
1499 C  CG  . PRO A 185 ? 0.1377 0.1587 0.1565 0.0212  -0.0111 0.0083  185 PRO A CG  
1500 C  CD  . PRO A 185 ? 0.1098 0.1636 0.1632 0.0158  -0.0317 0.0199  185 PRO A CD  
1501 N  N   . GLU A 186 ? 0.1680 0.1424 0.2710 -0.0586 -0.0232 0.0502  186 GLU A N   
1502 C  CA  . GLU A 186 ? 0.1625 0.1993 0.2574 -0.0333 -0.0145 0.0773  186 GLU A CA  
1503 C  C   . GLU A 186 ? 0.1063 0.1617 0.2958 -0.0273 -0.0214 0.0715  186 GLU A C   
1504 O  O   . GLU A 186 ? 0.1068 0.2348 0.3555 0.0375  -0.0066 0.0831  186 GLU A O   
1505 C  CB  . GLU A 186 ? 0.3007 0.1673 0.4928 -0.0853 -0.0989 0.1074  186 GLU A CB  
1506 C  CG  . GLU A 186 ? 0.5183 0.3042 0.4963 -0.0915 -0.0825 0.0842  186 GLU A CG  
1507 C  CD  . GLU A 186 ? 0.4689 0.2551 0.4782 -0.0554 -0.0826 0.0900  186 GLU A CD  
1508 O  OE1 . GLU A 186 ? 0.6261 0.4754 0.5926 -0.1663 -0.2064 -0.0051 186 GLU A OE1 
1509 O  OE2 . GLU A 186 ? 0.2118 0.3100 0.4949 -0.1024 -0.0757 0.1319  186 GLU A OE2 
1510 N  N   . SER A 187 ? 0.1040 0.1948 0.2652 -0.0255 -0.0339 0.0405  187 SER A N   
1511 C  CA  . SER A 187 ? 0.1411 0.1427 0.2605 -0.0234 -0.0239 0.0550  187 SER A CA  
1512 C  C   . SER A 187 ? 0.1074 0.1610 0.2447 -0.0103 0.0006  0.0354  187 SER A C   
1513 O  O   . SER A 187 ? 0.1183 0.2187 0.2684 -0.0120 0.0058  0.0286  187 SER A O   
1514 C  CB  . SER A 187 ? 0.1576 0.1902 0.2391 0.0122  0.0145  0.0703  187 SER A CB  
1515 O  OG  . SER A 187 ? 0.1643 0.2104 0.2616 -0.0300 0.0203  0.0611  187 SER A OG  
1516 N  N   . LEU A 188 ? 0.1263 0.1536 0.2613 -0.0155 0.0026  0.0155  188 LEU A N   
1517 C  CA  . LEU A 188 ? 0.1228 0.1811 0.2872 -0.0155 -0.0344 0.0021  188 LEU A CA  
1518 C  C   . LEU A 188 ? 0.1034 0.1702 0.2366 -0.0040 0.0127  -0.0074 188 LEU A C   
1519 O  O   . LEU A 188 ? 0.1488 0.2220 0.2511 -0.0356 0.0111  -0.0206 188 LEU A O   
1520 C  CB  . LEU A 188 ? 0.1762 0.1693 0.3567 -0.0052 -0.0078 0.0244  188 LEU A CB  
1521 C  CG  . LEU A 188 ? 0.1709 0.2043 0.3811 0.0190  0.0031  0.0952  188 LEU A CG  
1522 C  CD1 . LEU A 188 ? 0.2007 0.1831 0.4594 -0.0046 -0.0923 0.0853  188 LEU A CD1 
1523 C  CD2 . LEU A 188 ? 0.1352 0.3690 0.3152 -0.0226 -0.0284 0.0785  188 LEU A CD2 
1524 N  N   . ASP A 189 ? 0.1156 0.1946 0.2165 0.0136  0.0205  0.0239  189 ASP A N   
1525 C  CA  . ASP A 189 ? 0.1158 0.2143 0.2197 -0.0266 0.0200  -0.0067 189 ASP A CA  
1526 C  C   . ASP A 189 ? 0.1176 0.1544 0.2107 0.0080  0.0276  -0.0141 189 ASP A C   
1527 O  O   . ASP A 189 ? 0.1248 0.1350 0.1880 0.0183  0.0018  -0.0037 189 ASP A O   
1528 C  CB  . ASP A 189 ? 0.1957 0.2586 0.2010 -0.0577 0.0122  0.0461  189 ASP A CB  
1529 C  CG  . ASP A 189 ? 0.2174 0.3607 0.2656 -0.1053 0.0483  0.0339  189 ASP A CG  
1530 O  OD1 . ASP A 189 ? 0.1946 0.4597 0.3736 -0.0581 0.0956  -0.0819 189 ASP A OD1 
1531 O  OD2 . ASP A 189 ? 0.3212 0.4355 0.3176 -0.1562 -0.0006 0.0915  189 ASP A OD2 
1532 N  N   . TYR A 190 ? 0.1106 0.1553 0.1777 0.0055  0.0231  0.0234  190 TYR A N   
1533 C  CA  . TYR A 190 ? 0.1086 0.1666 0.1497 -0.0144 0.0074  0.0427  190 TYR A CA  
1534 C  C   . TYR A 190 ? 0.1263 0.1399 0.1352 0.0019  0.0222  0.0158  190 TYR A C   
1535 O  O   . TYR A 190 ? 0.1381 0.1863 0.1404 0.0075  0.0278  0.0186  190 TYR A O   
1536 C  CB  . TYR A 190 ? 0.1587 0.1277 0.1617 0.0011  0.0264  0.0171  190 TYR A CB  
1537 C  CG  . TYR A 190 ? 0.1407 0.1373 0.1679 -0.0023 0.0077  0.0182  190 TYR A CG  
1538 C  CD1 . TYR A 190 ? 0.1579 0.1628 0.1468 -0.0068 0.0201  0.0086  190 TYR A CD1 
1539 C  CD2 . TYR A 190 ? 0.1474 0.1745 0.1546 0.0099  0.0334  0.0218  190 TYR A CD2 
1540 C  CE1 . TYR A 190 ? 0.1317 0.1389 0.1794 0.0100  0.0114  0.0158  190 TYR A CE1 
1541 C  CE2 . TYR A 190 ? 0.1382 0.1923 0.1715 0.0234  0.0005  -0.0078 190 TYR A CE2 
1542 C  CZ  . TYR A 190 ? 0.1425 0.1478 0.1605 -0.0013 0.0230  0.0190  190 TYR A CZ  
1543 O  OH  . TYR A 190 ? 0.1914 0.1562 0.1867 0.0172  0.0203  -0.0058 190 TYR A OH  
1544 N  N   . TRP A 191 ? 0.1140 0.1244 0.1389 -0.0023 0.0044  0.0143  191 TRP A N   
1545 C  CA  . TRP A 191 ? 0.1295 0.1305 0.1400 -0.0026 0.0189  -0.0035 191 TRP A CA  
1546 C  C   . TRP A 191 ? 0.1427 0.1465 0.1095 -0.0152 0.0060  0.0091  191 TRP A C   
1547 O  O   . TRP A 191 ? 0.1671 0.1346 0.1158 -0.0100 0.0115  0.0033  191 TRP A O   
1548 C  CB  . TRP A 191 ? 0.1701 0.1138 0.1355 0.0065  0.0416  0.0018  191 TRP A CB  
1549 C  CG  . TRP A 191 ? 0.1423 0.1231 0.1346 0.0034  0.0002  0.0139  191 TRP A CG  
1550 C  CD1 . TRP A 191 ? 0.1934 0.1514 0.1461 0.0192  0.0306  0.0154  191 TRP A CD1 
1551 C  CD2 . TRP A 191 ? 0.1217 0.1102 0.1459 0.0133  0.0096  0.0245  191 TRP A CD2 
1552 N  NE1 . TRP A 191 ? 0.2111 0.1521 0.1797 0.0151  0.0217  0.0317  191 TRP A NE1 
1553 C  CE2 . TRP A 191 ? 0.1691 0.0822 0.1729 0.0359  0.0104  0.0348  191 TRP A CE2 
1554 C  CE3 . TRP A 191 ? 0.1156 0.1459 0.1723 0.0179  -0.0119 -0.0080 191 TRP A CE3 
1555 C  CZ2 . TRP A 191 ? 0.1903 0.1041 0.2185 0.0144  -0.0017 0.0228  191 TRP A CZ2 
1556 C  CZ3 . TRP A 191 ? 0.1199 0.1317 0.1982 0.0147  0.0091  -0.0099 191 TRP A CZ3 
1557 C  CH2 . TRP A 191 ? 0.1601 0.1869 0.2140 0.0064  -0.0062 0.0376  191 TRP A CH2 
1558 N  N   . THR A 192 ? 0.1210 0.1406 0.1111 -0.0063 -0.0018 0.0027  192 THR A N   
1559 C  CA  . THR A 192 ? 0.1274 0.1269 0.1301 0.0089  -0.0001 0.0083  192 THR A CA  
1560 C  C   . THR A 192 ? 0.1206 0.1285 0.1079 0.0136  0.0086  0.0236  192 THR A C   
1561 O  O   . THR A 192 ? 0.1427 0.1500 0.1079 0.0095  -0.0039 0.0170  192 THR A O   
1562 C  CB  . THR A 192 ? 0.1604 0.1156 0.1100 0.0225  0.0203  0.0065  192 THR A CB  
1563 O  OG1 . THR A 192 ? 0.1420 0.1212 0.1388 0.0274  0.0163  0.0072  192 THR A OG1 
1564 C  CG2 . THR A 192 ? 0.1747 0.1470 0.1099 0.0276  0.0247  0.0017  192 THR A CG2 
1565 N  N   . TYR A 193 ? 0.1192 0.1319 0.1179 0.0081  0.0165  -0.0080 193 TYR A N   
1566 C  CA  . TYR A 193 ? 0.1271 0.1208 0.1468 0.0209  0.0021  -0.0120 193 TYR A CA  
1567 C  C   . TYR A 193 ? 0.1295 0.1163 0.1203 0.0289  -0.0190 -0.0233 193 TYR A C   
1568 O  O   . TYR A 193 ? 0.1375 0.1143 0.1106 0.0081  -0.0118 -0.0036 193 TYR A O   
1569 C  CB  . TYR A 193 ? 0.1592 0.1280 0.1115 0.0451  -0.0212 -0.0408 193 TYR A CB  
1570 C  CG  . TYR A 193 ? 0.1490 0.0639 0.1079 0.0097  -0.0085 0.0036  193 TYR A CG  
1571 C  CD1 . TYR A 193 ? 0.1614 0.0928 0.0986 0.0251  -0.0207 -0.0133 193 TYR A CD1 
1572 C  CD2 . TYR A 193 ? 0.1320 0.0973 0.1317 0.0326  -0.0032 -0.0063 193 TYR A CD2 
1573 C  CE1 . TYR A 193 ? 0.1145 0.1000 0.1213 0.0138  0.0070  0.0061  193 TYR A CE1 
1574 C  CE2 . TYR A 193 ? 0.1525 0.1045 0.1223 0.0226  -0.0067 -0.0188 193 TYR A CE2 
1575 C  CZ  . TYR A 193 ? 0.1210 0.0813 0.1353 0.0163  0.0084  -0.0223 193 TYR A CZ  
1576 O  OH  . TYR A 193 ? 0.1163 0.0948 0.1172 0.0005  -0.0034 -0.0143 193 TYR A OH  
1577 N  N   . PRO A 194 ? 0.1244 0.1464 0.1086 0.0095  -0.0070 -0.0319 194 PRO A N   
1578 C  CA  . PRO A 194 ? 0.1323 0.1288 0.1366 0.0118  0.0116  -0.0413 194 PRO A CA  
1579 C  C   . PRO A 194 ? 0.1055 0.1296 0.1288 0.0133  -0.0070 -0.0247 194 PRO A C   
1580 O  O   . PRO A 194 ? 0.1518 0.1382 0.1355 0.0348  -0.0207 -0.0196 194 PRO A O   
1581 C  CB  . PRO A 194 ? 0.2077 0.1411 0.1190 0.0356  -0.0058 -0.0518 194 PRO A CB  
1582 C  CG  . PRO A 194 ? 0.1831 0.1589 0.1267 -0.0027 -0.0031 -0.0450 194 PRO A CG  
1583 C  CD  . PRO A 194 ? 0.1923 0.1941 0.1007 -0.0210 -0.0196 -0.0216 194 PRO A CD  
1584 N  N   . GLY A 195 ? 0.1316 0.0994 0.1328 -0.0020 0.0158  -0.0358 195 GLY A N   
1585 C  CA  . GLY A 195 ? 0.1317 0.1386 0.1163 0.0013  0.0175  -0.0092 195 GLY A CA  
1586 C  C   . GLY A 195 ? 0.0943 0.0998 0.1240 0.0013  -0.0088 -0.0140 195 GLY A C   
1587 O  O   . GLY A 195 ? 0.1249 0.0900 0.1454 -0.0081 -0.0156 -0.0140 195 GLY A O   
1588 N  N   . SER A 196 ? 0.0948 0.1266 0.1122 -0.0012 -0.0016 -0.0257 196 SER A N   
1589 C  CA  . SER A 196 ? 0.1102 0.1289 0.1159 0.0135  0.0291  -0.0285 196 SER A CA  
1590 C  C   . SER A 196 ? 0.0930 0.1016 0.1337 0.0000  -0.0147 -0.0042 196 SER A C   
1591 O  O   . SER A 196 ? 0.0982 0.1039 0.1338 0.0036  0.0006  -0.0204 196 SER A O   
1592 C  CB  . SER A 196 ? 0.0989 0.1012 0.1720 0.0184  0.0040  -0.0330 196 SER A CB  
1593 O  OG  . SER A 196 ? 0.0901 0.1107 0.1689 0.0099  -0.0135 -0.0398 196 SER A OG  
1594 N  N   . LEU A 197 ? 0.1126 0.1084 0.1217 0.0205  0.0046  -0.0078 197 LEU A N   
1595 C  CA  . LEU A 197 ? 0.1305 0.0955 0.1206 -0.0055 0.0106  -0.0019 197 LEU A CA  
1596 C  C   . LEU A 197 ? 0.1023 0.0855 0.1449 -0.0173 -0.0046 0.0002  197 LEU A C   
1597 O  O   . LEU A 197 ? 0.1045 0.1127 0.1564 -0.0006 -0.0053 -0.0242 197 LEU A O   
1598 C  CB  . LEU A 197 ? 0.1049 0.0991 0.1786 -0.0076 0.0129  0.0215  197 LEU A CB  
1599 C  CG  . LEU A 197 ? 0.1553 0.0853 0.2416 -0.0133 0.0192  0.0227  197 LEU A CG  
1600 C  CD1 . LEU A 197 ? 0.1919 0.1436 0.2649 -0.0708 0.0089  0.0386  197 LEU A CD1 
1601 C  CD2 . LEU A 197 ? 0.1235 0.1635 0.3152 0.0016  0.0456  0.0417  197 LEU A CD2 
1602 N  N   . THR A 198 ? 0.1137 0.0851 0.1370 -0.0042 -0.0030 -0.0059 198 THR A N   
1603 C  CA  . THR A 198 ? 0.1113 0.0869 0.1420 -0.0058 0.0218  -0.0108 198 THR A CA  
1604 C  C   . THR A 198 ? 0.0923 0.1371 0.1335 -0.0041 0.0161  -0.0149 198 THR A C   
1605 O  O   . THR A 198 ? 0.0930 0.1395 0.1590 -0.0052 0.0059  -0.0192 198 THR A O   
1606 C  CB  . THR A 198 ? 0.0998 0.1120 0.1154 -0.0234 0.0052  0.0048  198 THR A CB  
1607 O  OG1 . THR A 198 ? 0.1049 0.1037 0.1134 -0.0073 -0.0021 0.0166  198 THR A OG1 
1608 C  CG2 . THR A 198 ? 0.0987 0.1197 0.1213 -0.0027 0.0188  -0.0068 198 THR A CG2 
1609 N  N   . THR A 199 ? 0.1156 0.1565 0.1658 -0.0177 0.0354  0.0018  199 THR A N   
1610 C  CA  . THR A 199 ? 0.1334 0.1726 0.1844 -0.0480 0.0518  -0.0134 199 THR A CA  
1611 C  C   . THR A 199 ? 0.1252 0.1597 0.2011 -0.0158 0.0247  -0.0196 199 THR A C   
1612 O  O   . THR A 199 ? 0.1583 0.1384 0.1967 -0.0164 0.0409  -0.0076 199 THR A O   
1613 C  CB  . THR A 199 ? 0.2438 0.1597 0.1601 -0.0761 0.0535  -0.0272 199 THR A CB  
1614 O  OG1 . THR A 199 ? 0.5078 0.1533 0.1644 -0.0475 -0.0238 0.0188  199 THR A OG1 
1615 C  CG2 . THR A 199 ? 0.1919 0.1456 0.1948 -0.0474 0.0055  -0.0206 199 THR A CG2 
1616 N  N   . PRO A 200 ? 0.1368 0.1474 0.2114 -0.0278 0.0527  -0.0049 200 PRO A N   
1617 C  CA  . PRO A 200 ? 0.1295 0.1472 0.2570 -0.0278 0.0586  0.0084  200 PRO A CA  
1618 C  C   . PRO A 200 ? 0.1428 0.1759 0.2139 -0.0258 0.0440  0.0158  200 PRO A C   
1619 O  O   . PRO A 200 ? 0.1504 0.2036 0.2466 -0.0411 0.0243  0.0003  200 PRO A O   
1620 C  CB  . PRO A 200 ? 0.1456 0.1676 0.2602 0.0066  0.0595  -0.0113 200 PRO A CB  
1621 C  CG  . PRO A 200 ? 0.1443 0.1899 0.2368 -0.0081 0.0935  -0.0129 200 PRO A CG  
1622 C  CD  . PRO A 200 ? 0.1496 0.2170 0.2175 -0.0100 0.0677  -0.0337 200 PRO A CD  
1623 N  N   . PRO A 201 ? 0.1309 0.1723 0.2002 -0.0315 0.0199  0.0270  201 PRO A N   
1624 C  CA  . PRO A 201 ? 0.1533 0.1357 0.2264 -0.0522 0.0139  0.0305  201 PRO A CA  
1625 C  C   . PRO A 201 ? 0.1263 0.1411 0.2154 -0.0160 0.0079  0.0220  201 PRO A C   
1626 O  O   . PRO A 201 ? 0.1474 0.1453 0.2273 -0.0220 0.0117  -0.0103 201 PRO A O   
1627 C  CB  . PRO A 201 ? 0.1941 0.1274 0.2596 -0.0237 -0.0043 0.0457  201 PRO A CB  
1628 C  CG  . PRO A 201 ? 0.1842 0.1744 0.2914 -0.0423 -0.0172 0.0005  201 PRO A CG  
1629 C  CD  . PRO A 201 ? 0.1938 0.1648 0.2046 -0.0249 -0.0077 0.0392  201 PRO A CD  
1630 N  N   . LEU A 202 ? 0.1163 0.1132 0.2133 -0.0116 0.0354  0.0041  202 LEU A N   
1631 C  CA  . LEU A 202 ? 0.1240 0.1477 0.1802 0.0038  0.0013  0.0043  202 LEU A CA  
1632 C  C   . LEU A 202 ? 0.0908 0.1386 0.1935 -0.0390 0.0151  0.0041  202 LEU A C   
1633 O  O   . LEU A 202 ? 0.1067 0.1292 0.1932 -0.0086 -0.0087 -0.0267 202 LEU A O   
1634 C  CB  . LEU A 202 ? 0.1234 0.1230 0.1891 -0.0040 -0.0100 -0.0010 202 LEU A CB  
1635 C  CG  . LEU A 202 ? 0.0883 0.1377 0.2086 -0.0034 0.0219  -0.0253 202 LEU A CG  
1636 C  CD1 . LEU A 202 ? 0.0932 0.1788 0.2345 -0.0025 0.0110  -0.0102 202 LEU A CD1 
1637 C  CD2 . LEU A 202 ? 0.1228 0.1536 0.2531 -0.0249 0.0000  -0.0291 202 LEU A CD2 
1638 N  N   . THR A 203 ? 0.1177 0.1097 0.2357 -0.0240 0.0157  -0.0088 203 THR A N   
1639 C  CA  . THR A 203 ? 0.1342 0.1213 0.2179 -0.0241 0.0109  -0.0161 203 THR A CA  
1640 C  C   . THR A 203 ? 0.1034 0.1181 0.2086 -0.0182 0.0022  -0.0237 203 THR A C   
1641 O  O   . THR A 203 ? 0.1152 0.1119 0.1974 -0.0190 -0.0071 -0.0397 203 THR A O   
1642 C  CB  . THR A 203 ? 0.2139 0.1106 0.2726 -0.0067 0.0334  0.0156  203 THR A CB  
1643 O  OG1 . THR A 203 ? 0.2261 0.1389 0.3423 -0.0030 0.0932  0.0234  203 THR A OG1 
1644 C  CG2 . THR A 203 ? 0.1860 0.1180 0.3640 0.0164  0.0071  -0.0228 203 THR A CG2 
1645 N  N   . GLU A 204 ? 0.1453 0.1349 0.2079 -0.0055 -0.0249 -0.0433 204 GLU A N   
1646 C  CA  . GLU A 204 ? 0.1346 0.1526 0.1841 0.0013  -0.0467 -0.0381 204 GLU A CA  
1647 C  C   . GLU A 204 ? 0.1357 0.1497 0.1712 -0.0051 -0.0161 -0.0357 204 GLU A C   
1648 O  O   . GLU A 204 ? 0.2129 0.1597 0.1729 0.0365  -0.0595 -0.0535 204 GLU A O   
1649 C  CB  . GLU A 204 ? 0.1521 0.1400 0.2150 0.0206  -0.0699 -0.0432 204 GLU A CB  
1650 C  CG  . GLU A 204 ? 0.1350 0.1407 0.2276 0.0203  -0.0392 -0.0345 204 GLU A CG  
1651 C  CD  . GLU A 204 ? 0.1644 0.1693 0.2438 0.0365  -0.0760 -0.0509 204 GLU A CD  
1652 O  OE1 . GLU A 204 ? 0.2075 0.1892 0.3317 0.0139  -0.1222 -0.0772 204 GLU A OE1 
1653 O  OE2 . GLU A 204 ? 0.1283 0.1539 0.2359 0.0107  -0.0626 -0.0354 204 GLU A OE2 
1654 N  N   . CYS A 205 ? 0.1215 0.0815 0.1720 -0.0110 -0.0126 -0.0210 205 CYS A N   
1655 C  CA  . CYS A 205 ? 0.1163 0.1183 0.1579 0.0077  0.0043  0.0072  205 CYS A CA  
1656 C  C   . CYS A 205 ? 0.1240 0.0928 0.1452 0.0103  -0.0188 -0.0367 205 CYS A C   
1657 O  O   . CYS A 205 ? 0.1294 0.1076 0.1583 -0.0003 -0.0161 -0.0096 205 CYS A O   
1658 C  CB  . CYS A 205 ? 0.1421 0.1345 0.1323 -0.0182 -0.0072 -0.0001 205 CYS A CB  
1659 S  SG  . CYS A 205 ? 0.1696 0.1562 0.1553 0.0105  0.0004  -0.0182 205 CYS A SG  
1660 N  N   . VAL A 206 ? 0.1117 0.1072 0.1607 -0.0047 -0.0146 -0.0048 206 VAL A N   
1661 C  CA  . VAL A 206 ? 0.1249 0.0932 0.1177 0.0020  -0.0143 -0.0130 206 VAL A CA  
1662 C  C   . VAL A 206 ? 0.0919 0.1071 0.1377 0.0051  -0.0025 -0.0076 206 VAL A C   
1663 O  O   . VAL A 206 ? 0.1231 0.1287 0.1571 0.0201  -0.0111 -0.0037 206 VAL A O   
1664 C  CB  . VAL A 206 ? 0.1086 0.0891 0.1381 -0.0036 0.0031  -0.0288 206 VAL A CB  
1665 C  CG1 . VAL A 206 ? 0.1088 0.1241 0.1465 -0.0059 -0.0307 -0.0186 206 VAL A CG1 
1666 C  CG2 . VAL A 206 ? 0.1265 0.1410 0.1759 -0.0030 0.0342  -0.0244 206 VAL A CG2 
1667 N  N   . THR A 207 ? 0.1047 0.0891 0.1267 0.0029  0.0051  -0.0136 207 THR A N   
1668 C  CA  . THR A 207 ? 0.1088 0.1080 0.1334 -0.0054 0.0174  -0.0218 207 THR A CA  
1669 C  C   . THR A 207 ? 0.1093 0.0908 0.1230 0.0080  -0.0044 0.0019  207 THR A C   
1670 O  O   . THR A 207 ? 0.1362 0.0977 0.1296 0.0013  -0.0165 0.0021  207 THR A O   
1671 C  CB  . THR A 207 ? 0.1230 0.1163 0.1203 -0.0030 0.0125  -0.0330 207 THR A CB  
1672 O  OG1 . THR A 207 ? 0.1581 0.1040 0.1601 -0.0074 -0.0012 -0.0376 207 THR A OG1 
1673 C  CG2 . THR A 207 ? 0.1514 0.1546 0.1291 0.0019  0.0195  0.0108  207 THR A CG2 
1674 N  N   . TRP A 208 ? 0.1062 0.0702 0.1456 0.0122  -0.0072 -0.0151 208 TRP A N   
1675 C  CA  . TRP A 208 ? 0.0976 0.0725 0.1382 0.0126  -0.0054 -0.0201 208 TRP A CA  
1676 C  C   . TRP A 208 ? 0.1034 0.0897 0.1104 0.0129  0.0023  -0.0035 208 TRP A C   
1677 O  O   . TRP A 208 ? 0.1246 0.1040 0.1144 0.0159  0.0044  0.0072  208 TRP A O   
1678 C  CB  . TRP A 208 ? 0.0996 0.0928 0.1149 0.0198  0.0151  0.0091  208 TRP A CB  
1679 C  CG  . TRP A 208 ? 0.0890 0.0727 0.1188 0.0137  0.0089  0.0016  208 TRP A CG  
1680 C  CD1 . TRP A 208 ? 0.0973 0.0831 0.1550 0.0142  0.0073  -0.0113 208 TRP A CD1 
1681 C  CD2 . TRP A 208 ? 0.1177 0.0707 0.1319 0.0024  0.0044  0.0004  208 TRP A CD2 
1682 N  NE1 . TRP A 208 ? 0.0998 0.1003 0.1529 0.0052  -0.0032 -0.0067 208 TRP A NE1 
1683 C  CE2 . TRP A 208 ? 0.1104 0.0774 0.1289 0.0241  -0.0057 0.0161  208 TRP A CE2 
1684 C  CE3 . TRP A 208 ? 0.1249 0.0840 0.1188 0.0286  -0.0118 0.0020  208 TRP A CE3 
1685 C  CZ2 . TRP A 208 ? 0.1215 0.0854 0.1312 0.0258  0.0002  0.0041  208 TRP A CZ2 
1686 C  CZ3 . TRP A 208 ? 0.1260 0.0908 0.1176 0.0071  -0.0023 -0.0011 208 TRP A CZ3 
1687 C  CH2 . TRP A 208 ? 0.1199 0.1053 0.1395 0.0063  -0.0081 0.0117  208 TRP A CH2 
1688 N  N   . ILE A 209 ? 0.1117 0.0646 0.1238 -0.0093 -0.0020 0.0126  209 ILE A N   
1689 C  CA  . ILE A 209 ? 0.0967 0.1014 0.1219 -0.0059 -0.0041 -0.0011 209 ILE A CA  
1690 C  C   . ILE A 209 ? 0.1065 0.1163 0.1084 -0.0131 -0.0008 0.0023  209 ILE A C   
1691 O  O   . ILE A 209 ? 0.1386 0.0919 0.1210 -0.0013 -0.0015 0.0005  209 ILE A O   
1692 C  CB  . ILE A 209 ? 0.1165 0.1108 0.1594 0.0006  -0.0027 -0.0040 209 ILE A CB  
1693 C  CG1 . ILE A 209 ? 0.1089 0.0982 0.2081 0.0175  -0.0087 -0.0168 209 ILE A CG1 
1694 C  CG2 . ILE A 209 ? 0.1080 0.1377 0.1917 0.0077  0.0068  0.0257  209 ILE A CG2 
1695 C  CD1 . ILE A 209 ? 0.1569 0.1210 0.2693 0.0256  -0.0236 0.0328  209 ILE A CD1 
1696 N  N   . VAL A 210 ? 0.1127 0.0946 0.1152 0.0059  0.0100  -0.0044 210 VAL A N   
1697 C  CA  . VAL A 210 ? 0.0870 0.1055 0.0986 -0.0006 0.0029  0.0000  210 VAL A CA  
1698 C  C   . VAL A 210 ? 0.0894 0.1052 0.1221 0.0019  0.0138  0.0108  210 VAL A C   
1699 O  O   . VAL A 210 ? 0.1310 0.1156 0.1206 -0.0196 0.0136  0.0049  210 VAL A O   
1700 C  CB  . VAL A 210 ? 0.1000 0.0779 0.1276 0.0066  0.0003  0.0067  210 VAL A CB  
1701 C  CG1 . VAL A 210 ? 0.1310 0.0806 0.1461 0.0041  0.0035  -0.0129 210 VAL A CG1 
1702 C  CG2 . VAL A 210 ? 0.1226 0.0944 0.1438 -0.0137 0.0150  0.0089  210 VAL A CG2 
1703 N  N   . LEU A 211 ? 0.0914 0.1000 0.1578 -0.0057 -0.0067 0.0023  211 LEU A N   
1704 C  CA  . LEU A 211 ? 0.0806 0.1215 0.1594 -0.0020 -0.0136 0.0086  211 LEU A CA  
1705 C  C   . LEU A 211 ? 0.1154 0.1242 0.1332 -0.0003 -0.0016 0.0193  211 LEU A C   
1706 O  O   . LEU A 211 ? 0.1395 0.1158 0.1334 -0.0069 0.0044  -0.0053 211 LEU A O   
1707 C  CB  . LEU A 211 ? 0.1107 0.1256 0.1558 -0.0186 -0.0173 0.0401  211 LEU A CB  
1708 C  CG  . LEU A 211 ? 0.1287 0.1269 0.1765 -0.0120 -0.0071 0.0329  211 LEU A CG  
1709 C  CD1 . LEU A 211 ? 0.1159 0.2217 0.2199 0.0266  -0.0348 0.0485  211 LEU A CD1 
1710 C  CD2 . LEU A 211 ? 0.1788 0.1474 0.1996 0.0106  0.0232  0.0111  211 LEU A CD2 
1711 N  N   . LYS A 212 ? 0.1102 0.1370 0.1608 -0.0117 -0.0017 0.0270  212 LYS A N   
1712 C  CA  . LYS A 212 ? 0.1700 0.1260 0.1439 -0.0069 -0.0215 0.0277  212 LYS A CA  
1713 C  C   . LYS A 212 ? 0.1298 0.1567 0.1569 -0.0179 -0.0129 0.0263  212 LYS A C   
1714 O  O   . LYS A 212 ? 0.1493 0.1452 0.2212 -0.0142 -0.0172 0.0227  212 LYS A O   
1715 C  CB  . LYS A 212 ? 0.2469 0.1528 0.1323 -0.0286 -0.0074 -0.0027 212 LYS A CB  
1716 C  CG  . LYS A 212 ? 0.3441 0.1737 0.2238 -0.0236 -0.0103 0.0309  212 LYS A CG  
1717 C  CD  . LYS A 212 ? 0.5894 0.3163 0.2746 -0.1892 0.0933  -0.0063 212 LYS A CD  
1718 C  CE  . LYS A 212 ? 0.6521 0.2491 0.5276 -0.0995 -0.1515 0.0221  212 LYS A CE  
1719 N  NZ  . LYS A 212 ? 1.0017 0.5486 0.5806 0.0370  -0.0391 -0.0430 212 LYS A NZ  
1720 N  N   A GLU A 213 ? 0.1131 0.1267 0.1421 -0.0283 -0.0024 0.0195  213 GLU A N   
1721 N  N   B GLU A 213 ? 0.1203 0.1220 0.1420 -0.0201 -0.0034 0.0178  213 GLU A N   
1722 C  CA  A GLU A 213 ? 0.1134 0.1500 0.1686 -0.0270 -0.0064 0.0044  213 GLU A CA  
1723 C  CA  B GLU A 213 ? 0.1235 0.1424 0.1684 -0.0323 -0.0065 0.0094  213 GLU A CA  
1724 C  C   A GLU A 213 ? 0.1210 0.1095 0.1650 -0.0438 0.0016  0.0140  213 GLU A C   
1725 C  C   B GLU A 213 ? 0.1206 0.1093 0.1661 -0.0438 0.0001  0.0143  213 GLU A C   
1726 O  O   A GLU A 213 ? 0.1244 0.1321 0.1650 -0.0236 -0.0047 0.0370  213 GLU A O   
1727 O  O   B GLU A 213 ? 0.1176 0.1324 0.1653 -0.0305 0.0032  0.0370  213 GLU A O   
1728 C  CB  A GLU A 213 ? 0.1163 0.1392 0.1867 -0.0139 -0.0025 0.0023  213 GLU A CB  
1729 C  CB  B GLU A 213 ? 0.1360 0.1054 0.2185 -0.0222 -0.0305 0.0251  213 GLU A CB  
1730 C  CG  A GLU A 213 ? 0.1360 0.2154 0.2143 -0.0297 -0.0496 -0.0003 213 GLU A CG  
1731 C  CG  B GLU A 213 ? 0.1504 0.1339 0.2301 -0.0137 -0.0586 0.0155  213 GLU A CG  
1732 C  CD  A GLU A 213 ? 0.1490 0.1795 0.2509 -0.0199 -0.0361 0.0059  213 GLU A CD  
1733 C  CD  B GLU A 213 ? 0.1447 0.1515 0.2803 -0.0228 -0.0347 -0.0019 213 GLU A CD  
1734 O  OE1 A GLU A 213 ? 0.1432 0.2114 0.2160 -0.0361 -0.0111 0.0308  213 GLU A OE1 
1735 O  OE1 B GLU A 213 ? 0.1111 0.1597 0.2284 -0.0218 -0.0052 -0.0006 213 GLU A OE1 
1736 O  OE2 A GLU A 213 ? 0.1811 0.1794 0.2669 -0.0124 -0.0668 0.0265  213 GLU A OE2 
1737 O  OE2 B GLU A 213 ? 0.1819 0.1680 0.3142 -0.0702 -0.0100 -0.0060 213 GLU A OE2 
1738 N  N   . PRO A 214 ? 0.1502 0.1199 0.1386 -0.0173 -0.0124 0.0210  214 PRO A N   
1739 C  CA  . PRO A 214 ? 0.1267 0.1359 0.1280 0.0046  -0.0049 -0.0005 214 PRO A CA  
1740 C  C   . PRO A 214 ? 0.1339 0.1393 0.1503 -0.0266 -0.0107 0.0060  214 PRO A C   
1741 O  O   . PRO A 214 ? 0.1526 0.1680 0.1909 -0.0491 -0.0095 0.0268  214 PRO A O   
1742 C  CB  . PRO A 214 ? 0.1851 0.1011 0.1757 0.0064  -0.0068 0.0139  214 PRO A CB  
1743 C  CG  . PRO A 214 ? 0.2918 0.1856 0.2685 0.0167  0.0798  0.0269  214 PRO A CG  
1744 C  CD  . PRO A 214 ? 0.1860 0.1093 0.2032 -0.0174 0.0388  0.0380  214 PRO A CD  
1745 N  N   . ILE A 215 ? 0.1615 0.1116 0.1338 -0.0163 -0.0166 0.0111  215 ILE A N   
1746 C  CA  . ILE A 215 ? 0.1860 0.1190 0.1278 -0.0161 -0.0270 -0.0022 215 ILE A CA  
1747 C  C   . ILE A 215 ? 0.1708 0.1127 0.1511 -0.0163 -0.0103 0.0132  215 ILE A C   
1748 O  O   . ILE A 215 ? 0.1696 0.1187 0.1905 -0.0157 -0.0111 -0.0074 215 ILE A O   
1749 C  CB  . ILE A 215 ? 0.1862 0.0991 0.1546 -0.0019 -0.0081 -0.0044 215 ILE A CB  
1750 C  CG1 . ILE A 215 ? 0.2068 0.1296 0.1341 -0.0335 -0.0106 0.0111  215 ILE A CG1 
1751 C  CG2 . ILE A 215 ? 0.1697 0.1292 0.1888 0.0066  -0.0227 -0.0367 215 ILE A CG2 
1752 C  CD1 . ILE A 215 ? 0.2511 0.1313 0.1478 -0.0124 -0.0412 0.0212  215 ILE A CD1 
1753 N  N   A SER A 216 ? 0.1944 0.0928 0.1837 0.0084  -0.0255 -0.0166 216 SER A N   
1754 N  N   B SER A 216 ? 0.1874 0.1213 0.1691 -0.0052 -0.0210 -0.0037 216 SER A N   
1755 C  CA  A SER A 216 ? 0.2165 0.0791 0.1581 -0.0156 -0.0231 -0.0037 216 SER A CA  
1756 C  CA  B SER A 216 ? 0.2150 0.1003 0.1705 -0.0341 -0.0109 0.0004  216 SER A CA  
1757 C  C   A SER A 216 ? 0.1903 0.0881 0.1575 -0.0089 -0.0192 -0.0033 216 SER A C   
1758 C  C   B SER A 216 ? 0.1585 0.0845 0.1729 -0.0346 -0.0209 0.0039  216 SER A C   
1759 O  O   A SER A 216 ? 0.2139 0.1271 0.1517 0.0049  -0.0203 0.0095  216 SER A O   
1760 O  O   B SER A 216 ? 0.1575 0.1337 0.1870 -0.0278 -0.0347 0.0053  216 SER A O   
1761 C  CB  A SER A 216 ? 0.2931 0.0527 0.1544 -0.0456 0.0208  -0.0251 216 SER A CB  
1762 C  CB  B SER A 216 ? 0.2829 0.1596 0.2279 -0.0840 0.0436  0.0500  216 SER A CB  
1763 O  OG  A SER A 216 ? 0.2215 0.1456 0.1849 -0.0815 -0.0279 0.0230  216 SER A OG  
1764 O  OG  B SER A 216 ? 0.3271 0.2383 0.2413 -0.1096 -0.0409 -0.0071 216 SER A OG  
1765 N  N   . VAL A 217 ? 0.1765 0.1256 0.1655 -0.0247 -0.0231 -0.0156 217 VAL A N   
1766 C  CA  . VAL A 217 ? 0.1784 0.0862 0.1666 -0.0196 -0.0236 -0.0044 217 VAL A CA  
1767 C  C   . VAL A 217 ? 0.1888 0.0930 0.1644 -0.0037 -0.0510 -0.0096 217 VAL A C   
1768 O  O   . VAL A 217 ? 0.1794 0.1125 0.1581 -0.0302 -0.0477 0.0055  217 VAL A O   
1769 C  CB  . VAL A 217 ? 0.1655 0.0873 0.2257 -0.0237 -0.0392 -0.0168 217 VAL A CB  
1770 C  CG1 . VAL A 217 ? 0.2323 0.0944 0.1673 -0.0291 -0.0458 -0.0125 217 VAL A CG1 
1771 C  CG2 . VAL A 217 ? 0.1626 0.1059 0.2525 -0.0411 -0.0436 -0.0145 217 VAL A CG2 
1772 N  N   . SER A 218 ? 0.1848 0.1014 0.1585 -0.0392 -0.0348 -0.0098 218 SER A N   
1773 C  CA  . SER A 218 ? 0.1991 0.0919 0.1560 -0.0348 -0.0418 0.0021  218 SER A CA  
1774 C  C   . SER A 218 ? 0.2074 0.1003 0.1517 -0.0256 -0.0070 0.0067  218 SER A C   
1775 O  O   . SER A 218 ? 0.2005 0.1027 0.1612 -0.0189 -0.0232 0.0151  218 SER A O   
1776 C  CB  . SER A 218 ? 0.2275 0.1439 0.1180 -0.0276 -0.0248 -0.0083 218 SER A CB  
1777 O  OG  . SER A 218 ? 0.2018 0.1324 0.1817 -0.0329 -0.0234 -0.0041 218 SER A OG  
1778 N  N   . SER A 219 ? 0.1887 0.1031 0.1661 -0.0173 -0.0232 -0.0161 219 SER A N   
1779 C  CA  . SER A 219 ? 0.1876 0.1021 0.2061 -0.0221 -0.0276 0.0198  219 SER A CA  
1780 C  C   . SER A 219 ? 0.2043 0.0822 0.1991 -0.0179 -0.0272 -0.0027 219 SER A C   
1781 O  O   . SER A 219 ? 0.2077 0.0959 0.2740 -0.0299 0.0048  -0.0060 219 SER A O   
1782 C  CB  . SER A 219 ? 0.3176 0.0950 0.2613 -0.0700 -0.0353 0.0018  219 SER A CB  
1783 O  OG  . SER A 219 ? 0.3345 0.1389 0.3439 -0.0039 -0.0615 0.0016  219 SER A OG  
1784 N  N   . GLU A 220 ? 0.2190 0.1156 0.1783 -0.0062 -0.0079 0.0054  220 GLU A N   
1785 C  CA  . GLU A 220 ? 0.2703 0.1246 0.1694 -0.0203 -0.0263 0.0082  220 GLU A CA  
1786 C  C   . GLU A 220 ? 0.2625 0.1226 0.1461 -0.0194 -0.0170 0.0151  220 GLU A C   
1787 O  O   . GLU A 220 ? 0.2610 0.1309 0.1884 -0.0192 0.0201  0.0049  220 GLU A O   
1788 C  CB  . GLU A 220 ? 0.3219 0.1517 0.1718 -0.0120 -0.0611 -0.0380 220 GLU A CB  
1789 C  CG  . GLU A 220 ? 0.3899 0.1608 0.2276 -0.0435 -0.0712 -0.0530 220 GLU A CG  
1790 C  CD  . GLU A 220 ? 0.3460 0.1903 0.3306 -0.0613 -0.0313 -0.0629 220 GLU A CD  
1791 O  OE1 . GLU A 220 ? 0.3055 0.1623 0.2546 -0.0732 -0.0407 -0.0016 220 GLU A OE1 
1792 O  OE2 . GLU A 220 ? 0.6028 0.2024 0.4488 -0.1311 0.0790  -0.1157 220 GLU A OE2 
1793 N  N   . GLN A 221 ? 0.2106 0.1068 0.1705 -0.0211 -0.0373 0.0146  221 GLN A N   
1794 C  CA  . GLN A 221 ? 0.1580 0.0989 0.1874 -0.0390 -0.0323 0.0258  221 GLN A CA  
1795 C  C   . GLN A 221 ? 0.1676 0.1052 0.1841 -0.0331 -0.0396 0.0184  221 GLN A C   
1796 O  O   . GLN A 221 ? 0.1750 0.1194 0.1532 -0.0194 -0.0095 0.0190  221 GLN A O   
1797 C  CB  . GLN A 221 ? 0.1533 0.1635 0.1815 -0.0155 -0.0277 0.0173  221 GLN A CB  
1798 C  CG  . GLN A 221 ? 0.1903 0.1465 0.1553 -0.0229 -0.0561 -0.0036 221 GLN A CG  
1799 C  CD  . GLN A 221 ? 0.2291 0.0939 0.1766 -0.0302 -0.0366 -0.0046 221 GLN A CD  
1800 O  OE1 . GLN A 221 ? 0.1860 0.1080 0.1769 -0.0085 -0.0407 0.0168  221 GLN A OE1 
1801 N  NE2 . GLN A 221 ? 0.2125 0.1174 0.1870 -0.0217 -0.0377 0.0022  221 GLN A NE2 
1802 N  N   . VAL A 222 ? 0.1952 0.1201 0.1605 -0.0151 -0.0376 0.0262  222 VAL A N   
1803 C  CA  . VAL A 222 ? 0.1982 0.1342 0.1580 -0.0032 -0.0354 0.0378  222 VAL A CA  
1804 C  C   . VAL A 222 ? 0.2031 0.1439 0.1747 -0.0300 -0.0259 0.0044  222 VAL A C   
1805 O  O   . VAL A 222 ? 0.2098 0.1418 0.1729 -0.0351 -0.0119 0.0265  222 VAL A O   
1806 C  CB  . VAL A 222 ? 0.2470 0.1650 0.1878 -0.0141 -0.0606 0.0669  222 VAL A CB  
1807 C  CG1 . VAL A 222 ? 0.2612 0.1650 0.2874 -0.0220 -0.0106 0.0585  222 VAL A CG1 
1808 C  CG2 . VAL A 222 ? 0.2543 0.2662 0.2082 -0.0363 -0.0747 0.0223  222 VAL A CG2 
1809 N  N   A LEU A 223 ? 0.2093 0.1083 0.1896 -0.0074 -0.0128 0.0106  223 LEU A N   
1810 N  N   B LEU A 223 ? 0.2116 0.1156 0.1711 0.0117  -0.0117 0.0025  223 LEU A N   
1811 C  CA  A LEU A 223 ? 0.2002 0.1529 0.2927 -0.0378 0.0416  -0.0111 223 LEU A CA  
1812 C  CA  B LEU A 223 ? 0.2219 0.1271 0.2529 -0.0208 0.0396  -0.0318 223 LEU A CA  
1813 C  C   A LEU A 223 ? 0.2116 0.1190 0.2145 -0.0196 0.0047  -0.0491 223 LEU A C   
1814 C  C   B LEU A 223 ? 0.2024 0.1328 0.1869 -0.0170 0.0046  -0.0436 223 LEU A C   
1815 O  O   A LEU A 223 ? 0.2036 0.1583 0.1975 -0.0058 0.0053  -0.0439 223 LEU A O   
1816 O  O   B LEU A 223 ? 0.1863 0.1683 0.2110 -0.0217 -0.0128 -0.0059 223 LEU A O   
1817 C  CB  A LEU A 223 ? 0.3077 0.1230 0.4677 -0.0860 0.0096  -0.0065 223 LEU A CB  
1818 C  CB  B LEU A 223 ? 0.2387 0.1561 0.2017 -0.0043 0.0657  -0.0679 223 LEU A CB  
1819 C  CG  A LEU A 223 ? 0.4800 0.2030 0.5266 -0.0956 -0.0336 0.0389  223 LEU A CG  
1820 C  CG  B LEU A 223 ? 0.3338 0.2113 0.2659 -0.0704 0.0347  -0.0098 223 LEU A CG  
1821 C  CD1 A LEU A 223 ? 0.2416 0.2102 0.5315 -0.0832 -0.0882 -0.1469 223 LEU A CD1 
1822 C  CD1 B LEU A 223 ? 0.3853 0.1788 0.3001 -0.0732 0.0209  -0.0252 223 LEU A CD1 
1823 C  CD2 A LEU A 223 ? 0.5110 0.3445 0.5220 -0.1397 -0.0988 -0.2178 223 LEU A CD2 
1824 C  CD2 B LEU A 223 ? 0.2958 0.1400 0.4694 -0.1236 0.0467  0.0129  223 LEU A CD2 
1825 N  N   . LYS A 224 ? 0.2127 0.1571 0.1429 -0.0198 -0.0044 -0.0190 224 LYS A N   
1826 C  CA  . LYS A 224 ? 0.2247 0.1707 0.1653 -0.0254 -0.0018 0.0016  224 LYS A CA  
1827 C  C   . LYS A 224 ? 0.2190 0.1432 0.1199 -0.0060 -0.0078 0.0269  224 LYS A C   
1828 O  O   . LYS A 224 ? 0.2328 0.1586 0.1267 -0.0215 -0.0016 0.0084  224 LYS A O   
1829 C  CB  . LYS A 224 ? 0.2507 0.2154 0.1860 -0.0051 -0.0145 0.0318  224 LYS A CB  
1830 C  CG  . LYS A 224 ? 0.2617 0.3213 0.1952 -0.0751 0.0048  0.0073  224 LYS A CG  
1831 C  CD  . LYS A 224 ? 0.2705 0.3534 0.3682 -0.0607 -0.0620 -0.0871 224 LYS A CD  
1832 C  CE  . LYS A 224 ? 0.4166 0.4480 0.3183 -0.0389 -0.0966 -0.1623 224 LYS A CE  
1833 N  NZ  . LYS A 224 ? 0.3680 0.3367 0.3953 0.0044  0.0284  -0.0474 224 LYS A NZ  
1834 N  N   . PHE A 225 ? 0.1847 0.1307 0.1156 -0.0057 -0.0203 -0.0003 225 PHE A N   
1835 C  CA  . PHE A 225 ? 0.1806 0.1285 0.1143 -0.0152 -0.0184 0.0175  225 PHE A CA  
1836 C  C   . PHE A 225 ? 0.1804 0.1222 0.1208 -0.0182 -0.0083 -0.0006 225 PHE A C   
1837 O  O   . PHE A 225 ? 0.2090 0.1294 0.1306 -0.0252 0.0142  -0.0065 225 PHE A O   
1838 C  CB  . PHE A 225 ? 0.2053 0.1186 0.1197 0.0000  0.0063  0.0110  225 PHE A CB  
1839 C  CG  . PHE A 225 ? 0.2017 0.0912 0.1625 0.0002  0.0044  0.0027  225 PHE A CG  
1840 C  CD1 . PHE A 225 ? 0.1917 0.1091 0.2039 0.0190  0.0077  0.0401  225 PHE A CD1 
1841 C  CD2 . PHE A 225 ? 0.1623 0.1517 0.1765 -0.0054 0.0128  -0.0233 225 PHE A CD2 
1842 C  CE1 . PHE A 225 ? 0.1982 0.1543 0.2089 -0.0157 0.0337  0.0125  225 PHE A CE1 
1843 C  CE2 . PHE A 225 ? 0.1736 0.1224 0.2425 0.0072  0.0179  -0.0251 225 PHE A CE2 
1844 C  CZ  . PHE A 225 ? 0.1673 0.1317 0.2196 -0.0083 0.0128  -0.0221 225 PHE A CZ  
1845 N  N   . ARG A 226 ? 0.1984 0.1231 0.1151 0.0032  -0.0034 -0.0150 226 ARG A N   
1846 C  CA  . ARG A 226 ? 0.2077 0.1195 0.1349 0.0105  0.0201  0.0137  226 ARG A CA  
1847 C  C   . ARG A 226 ? 0.1941 0.1248 0.1479 -0.0223 0.0124  -0.0151 226 ARG A C   
1848 O  O   . ARG A 226 ? 0.1953 0.2020 0.1666 0.0019  -0.0034 -0.0131 226 ARG A O   
1849 C  CB  . ARG A 226 ? 0.2620 0.1252 0.1330 0.0048  -0.0044 0.0171  226 ARG A CB  
1850 C  CG  . ARG A 226 ? 0.2362 0.1195 0.1405 -0.0204 -0.0030 0.0219  226 ARG A CG  
1851 C  CD  . ARG A 226 ? 0.3090 0.1159 0.1395 0.0140  -0.0110 0.0103  226 ARG A CD  
1852 N  NE  . ARG A 226 ? 0.2283 0.1418 0.1586 -0.0535 -0.0301 0.0105  226 ARG A NE  
1853 C  CZ  . ARG A 226 ? 0.1729 0.1403 0.1962 -0.0270 -0.0121 -0.0244 226 ARG A CZ  
1854 N  NH1 . ARG A 226 ? 0.2383 0.1743 0.2645 -0.0236 -0.0612 -0.0773 226 ARG A NH1 
1855 N  NH2 . ARG A 226 ? 0.2100 0.1210 0.2032 -0.0354 0.0189  0.0133  226 ARG A NH2 
1856 N  N   . LYS A 227 ? 0.2160 0.1603 0.1047 -0.0162 -0.0016 -0.0260 227 LYS A N   
1857 C  CA  . LYS A 227 ? 0.2587 0.1786 0.1081 -0.0477 0.0020  -0.0115 227 LYS A CA  
1858 C  C   . LYS A 227 ? 0.2505 0.1454 0.1296 -0.0046 0.0318  -0.0107 227 LYS A C   
1859 O  O   . LYS A 227 ? 0.3064 0.1869 0.1339 -0.0517 0.0267  -0.0067 227 LYS A O   
1860 C  CB  . LYS A 227 ? 0.2504 0.2337 0.1181 -0.0289 -0.0070 -0.0210 227 LYS A CB  
1861 C  CG  . LYS A 227 ? 0.3055 0.2653 0.1808 -0.0854 0.0184  -0.0593 227 LYS A CG  
1862 C  CD  . LYS A 227 ? 0.3457 0.5118 0.3296 -0.1306 -0.0406 -0.1973 227 LYS A CD  
1863 C  CE  . LYS A 227 ? 0.5323 0.6528 0.3826 -0.0435 0.0088  -0.0888 227 LYS A CE  
1864 N  NZ  . LYS A 227 ? 0.8206 0.9200 0.5644 -0.2736 -0.1875 -0.0585 227 LYS A NZ  
1865 N  N   . LEU A 228 ? 0.2473 0.1355 0.1298 -0.0304 0.0218  -0.0085 228 LEU A N   
1866 C  CA  . LEU A 228 ? 0.2264 0.1292 0.1296 -0.0226 0.0084  0.0000  228 LEU A CA  
1867 C  C   . LEU A 228 ? 0.2543 0.1804 0.0928 -0.0230 0.0289  0.0087  228 LEU A C   
1868 O  O   . LEU A 228 ? 0.2405 0.1442 0.1388 -0.0111 0.0195  -0.0113 228 LEU A O   
1869 C  CB  . LEU A 228 ? 0.2405 0.1655 0.0966 -0.0036 0.0009  0.0022  228 LEU A CB  
1870 C  CG  . LEU A 228 ? 0.2217 0.1820 0.1140 -0.0036 -0.0016 0.0108  228 LEU A CG  
1871 C  CD1 . LEU A 228 ? 0.2474 0.1594 0.1356 -0.0284 -0.0010 -0.0221 228 LEU A CD1 
1872 C  CD2 . LEU A 228 ? 0.2532 0.1848 0.1364 0.0091  0.0111  0.0332  228 LEU A CD2 
1873 N  N   . ASN A 229 ? 0.2140 0.1666 0.1273 -0.0221 0.0359  0.0116  229 ASN A N   
1874 C  CA  . ASN A 229 ? 0.1932 0.1847 0.1172 0.0160  0.0300  -0.0314 229 ASN A CA  
1875 C  C   . ASN A 229 ? 0.2566 0.1766 0.1147 0.0211  0.0201  -0.0047 229 ASN A C   
1876 O  O   . ASN A 229 ? 0.2327 0.1761 0.1531 0.0025  0.0216  0.0027  229 ASN A O   
1877 C  CB  . ASN A 229 ? 0.2764 0.2224 0.1147 -0.0373 0.0233  -0.0141 229 ASN A CB  
1878 C  CG  . ASN A 229 ? 0.2759 0.2164 0.1526 -0.0414 0.0318  -0.0208 229 ASN A CG  
1879 O  OD1 . ASN A 229 ? 0.3315 0.2781 0.1716 -0.0287 0.0665  -0.0394 229 ASN A OD1 
1880 N  ND2 . ASN A 229 ? 0.3128 0.1982 0.1404 -0.0380 0.0322  -0.0347 229 ASN A ND2 
1881 N  N   . PHE A 230 ? 0.2128 0.1374 0.1310 -0.0354 0.0423  -0.0162 230 PHE A N   
1882 C  CA  . PHE A 230 ? 0.2456 0.1443 0.0973 -0.0402 0.0096  0.0122  230 PHE A CA  
1883 C  C   . PHE A 230 ? 0.2979 0.1770 0.1091 0.0010  0.0526  0.0221  230 PHE A C   
1884 O  O   . PHE A 230 ? 0.2853 0.1842 0.1716 -0.0573 0.0429  0.0035  230 PHE A O   
1885 C  CB  . PHE A 230 ? 0.2258 0.1579 0.1382 -0.0256 0.0179  0.0008  230 PHE A CB  
1886 C  CG  . PHE A 230 ? 0.2363 0.1500 0.1445 -0.0469 0.0434  -0.0252 230 PHE A CG  
1887 C  CD1 . PHE A 230 ? 0.2395 0.1860 0.1099 -0.0270 0.0165  -0.0318 230 PHE A CD1 
1888 C  CD2 . PHE A 230 ? 0.2585 0.1367 0.1310 -0.0333 0.0072  -0.0329 230 PHE A CD2 
1889 C  CE1 . PHE A 230 ? 0.2627 0.1696 0.1373 -0.0502 0.0079  -0.0093 230 PHE A CE1 
1890 C  CE2 . PHE A 230 ? 0.2262 0.2154 0.1263 -0.0200 0.0174  -0.0216 230 PHE A CE2 
1891 C  CZ  . PHE A 230 ? 0.1949 0.1661 0.1553 0.0043  -0.0081 -0.0161 230 PHE A CZ  
1892 N  N   . ASN A 231 ? 0.2100 0.2048 0.1041 -0.0244 0.0441  -0.0030 231 ASN A N   
1893 C  CA  . ASN A 231 ? 0.2133 0.1776 0.1472 -0.0164 0.0633  0.0091  231 ASN A CA  
1894 C  C   . ASN A 231 ? 0.1917 0.2630 0.1113 -0.0073 0.0282  0.0088  231 ASN A C   
1895 O  O   . ASN A 231 ? 0.2323 0.1788 0.1873 -0.0053 0.0449  0.0037  231 ASN A O   
1896 C  CB  . ASN A 231 ? 0.1891 0.1905 0.1937 -0.0129 0.0668  -0.0055 231 ASN A CB  
1897 C  CG  . ASN A 231 ? 0.2064 0.1707 0.1676 -0.0029 0.0398  0.0177  231 ASN A CG  
1898 O  OD1 . ASN A 231 ? 0.2644 0.1719 0.1876 -0.0398 0.0636  -0.0221 231 ASN A OD1 
1899 N  ND2 . ASN A 231 ? 0.2473 0.2204 0.1675 0.0406  0.0256  -0.0099 231 ASN A ND2 
1900 N  N   . GLY A 232 ? 0.2537 0.1454 0.1775 0.0188  0.0502  0.0168  232 GLY A N   
1901 C  CA  . GLY A 232 ? 0.2067 0.1805 0.1773 0.0282  0.0347  0.0182  232 GLY A CA  
1902 C  C   . GLY A 232 ? 0.2143 0.1823 0.1838 0.0055  -0.0050 0.0236  232 GLY A C   
1903 O  O   . GLY A 232 ? 0.2384 0.2142 0.1557 0.0265  0.0659  0.0245  232 GLY A O   
1904 N  N   . GLU A 233 ? 0.2363 0.1996 0.1526 0.0222  0.0374  0.0116  233 GLU A N   
1905 C  CA  . GLU A 233 ? 0.2354 0.1619 0.1738 -0.0055 -0.0040 0.0017  233 GLU A CA  
1906 C  C   . GLU A 233 ? 0.2441 0.2170 0.1788 0.0025  0.0075  0.0044  233 GLU A C   
1907 O  O   . GLU A 233 ? 0.2426 0.2517 0.1939 0.0073  0.0290  0.0391  233 GLU A O   
1908 C  CB  . GLU A 233 ? 0.2610 0.2181 0.1438 0.0245  0.0370  0.0566  233 GLU A CB  
1909 C  CG  . GLU A 233 ? 0.2452 0.2919 0.1389 -0.0013 0.0447  0.0326  233 GLU A CG  
1910 C  CD  . GLU A 233 ? 0.3778 0.3430 0.2246 0.1119  0.0163  -0.0144 233 GLU A CD  
1911 O  OE1 . GLU A 233 ? 0.3666 0.2922 0.3307 0.0447  0.0463  0.0189  233 GLU A OE1 
1912 O  OE2 . GLU A 233 ? 0.4450 0.4153 0.2669 -0.0791 -0.0520 0.0013  233 GLU A OE2 
1913 N  N   . GLY A 234 ? 0.3832 0.2685 0.1949 0.0717  0.1105  -0.0025 234 GLY A N   
1914 C  CA  . GLY A 234 ? 0.3389 0.3335 0.1956 0.0961  0.0296  -0.0055 234 GLY A CA  
1915 C  C   . GLY A 234 ? 0.3838 0.2518 0.1687 0.1332  0.0186  -0.0190 234 GLY A C   
1916 O  O   . GLY A 234 ? 0.3763 0.5110 0.2749 0.1425  0.1300  0.0204  234 GLY A O   
1917 N  N   . GLU A 235 ? 0.3024 0.2606 0.1978 0.0996  0.0421  0.0250  235 GLU A N   
1918 C  CA  . GLU A 235 ? 0.2330 0.2682 0.2336 0.0954  0.0487  0.0616  235 GLU A CA  
1919 C  C   . GLU A 235 ? 0.2544 0.3108 0.2474 0.0566  0.0779  0.0233  235 GLU A C   
1920 O  O   . GLU A 235 ? 0.2976 0.3500 0.2265 0.0406  0.0822  -0.0159 235 GLU A O   
1921 C  CB  . GLU A 235 ? 0.2858 0.2134 0.2635 0.0566  0.0511  0.0601  235 GLU A CB  
1922 C  CG  . GLU A 235 ? 0.2390 0.2244 0.3092 0.0069  0.0798  0.0498  235 GLU A CG  
1923 C  CD  . GLU A 235 ? 0.5209 0.3579 0.3259 -0.1152 0.1136  -0.0441 235 GLU A CD  
1924 O  OE1 . GLU A 235 ? 0.2351 0.3338 0.4029 -0.0229 0.0450  0.0560  235 GLU A OE1 
1925 O  OE2 . GLU A 235 ? 0.6454 0.3321 0.5567 -0.1024 0.2624  0.0504  235 GLU A OE2 
1926 N  N   . PRO A 236 ? 0.2293 0.2559 0.2369 0.0311  0.0793  0.0464  236 PRO A N   
1927 C  CA  . PRO A 236 ? 0.2445 0.2584 0.2427 -0.0319 0.0952  0.0151  236 PRO A CA  
1928 C  C   . PRO A 236 ? 0.2201 0.2499 0.2002 -0.0136 0.0641  -0.0074 236 PRO A C   
1929 O  O   . PRO A 236 ? 0.2359 0.2153 0.1885 0.0051  0.0496  0.0086  236 PRO A O   
1930 C  CB  . PRO A 236 ? 0.1991 0.3405 0.2852 0.0203  0.0969  -0.0006 236 PRO A CB  
1931 C  CG  . PRO A 236 ? 0.2565 0.2735 0.3097 0.0702  0.1307  0.0893  236 PRO A CG  
1932 C  CD  . PRO A 236 ? 0.2205 0.3105 0.3153 0.0687  0.0471  0.0649  236 PRO A CD  
1933 N  N   A GLU A 237 ? 0.1964 0.2210 0.2580 0.0078  0.0652  -0.0247 237 GLU A N   
1934 N  N   B GLU A 237 ? 0.2128 0.3078 0.1984 -0.0558 0.0524  -0.0730 237 GLU A N   
1935 C  CA  A GLU A 237 ? 0.1874 0.2229 0.2158 -0.0013 0.0461  -0.0127 237 GLU A CA  
1936 C  CA  B GLU A 237 ? 0.2319 0.2831 0.1636 -0.0480 0.0606  -0.0355 237 GLU A CA  
1937 C  C   A GLU A 237 ? 0.1985 0.2231 0.2070 -0.0135 0.0505  -0.0262 237 GLU A C   
1938 C  C   B GLU A 237 ? 0.2244 0.2488 0.1845 -0.0089 0.0250  -0.0424 237 GLU A C   
1939 O  O   A GLU A 237 ? 0.1163 0.2296 0.2958 -0.0210 0.0388  -0.0469 237 GLU A O   
1940 O  O   B GLU A 237 ? 0.2809 0.2419 0.1798 0.0174  0.0324  -0.0615 237 GLU A O   
1941 C  CB  A GLU A 237 ? 0.1802 0.2305 0.3014 0.0168  -0.0089 -0.0399 237 GLU A CB  
1942 C  CB  B GLU A 237 ? 0.2608 0.2634 0.2124 -0.0283 0.0502  -0.0988 237 GLU A CB  
1943 C  CG  A GLU A 237 ? 0.2010 0.0964 0.3757 -0.0319 0.0380  -0.0443 237 GLU A CG  
1944 C  CG  B GLU A 237 ? 0.2470 0.2954 0.3496 -0.0704 0.0578  -0.0714 237 GLU A CG  
1945 C  CD  A GLU A 237 ? 0.3009 0.2395 0.2020 -0.0873 -0.0319 -0.0514 237 GLU A CD  
1946 C  CD  B GLU A 237 ? 0.3349 0.3782 0.2207 -0.0177 0.0274  -0.1018 237 GLU A CD  
1947 O  OE1 A GLU A 237 ? 0.2676 0.2860 0.3044 -0.0066 0.0527  -0.0770 237 GLU A OE1 
1948 O  OE1 B GLU A 237 ? 0.3757 0.4165 0.2175 -0.0908 0.0050  -0.1251 237 GLU A OE1 
1949 O  OE2 A GLU A 237 ? 0.3825 0.1702 0.2305 -0.0233 0.0036  -0.0621 237 GLU A OE2 
1950 O  OE2 B GLU A 237 ? 0.3468 0.4629 0.2748 -0.0855 0.0405  -0.1228 237 GLU A OE2 
1951 N  N   . GLU A 238 ? 0.2213 0.2438 0.1759 -0.0668 0.0690  -0.0413 238 GLU A N   
1952 C  CA  . GLU A 238 ? 0.2005 0.2776 0.1905 -0.0523 0.0496  -0.0145 238 GLU A CA  
1953 C  C   . GLU A 238 ? 0.1838 0.1747 0.1393 -0.0128 0.0559  -0.0316 238 GLU A C   
1954 O  O   . GLU A 238 ? 0.2420 0.1600 0.2208 -0.0239 0.0504  -0.0385 238 GLU A O   
1955 C  CB  . GLU A 238 ? 0.2863 0.3767 0.2857 -0.1489 0.0395  -0.0550 238 GLU A CB  
1956 C  CG  . GLU A 238 ? 0.3061 0.5092 0.1880 -0.0614 0.0392  -0.0190 238 GLU A CG  
1957 C  CD  . GLU A 238 ? 0.6316 0.6595 0.6705 -0.2728 -0.0872 -0.1059 238 GLU A CD  
1958 O  OE1 . GLU A 238 ? 0.7018 0.7144 0.4480 -0.2734 -0.0967 -0.1117 238 GLU A OE1 
1959 O  OE2 . GLU A 238 ? 0.7447 1.0479 0.7244 -0.2201 -0.2780 0.0912  238 GLU A OE2 
1960 N  N   . LEU A 239 ? 0.2118 0.2206 0.1612 -0.0545 0.0533  -0.0398 239 LEU A N   
1961 C  CA  . LEU A 239 ? 0.1946 0.1543 0.1568 -0.0476 0.0308  -0.0454 239 LEU A CA  
1962 C  C   . LEU A 239 ? 0.2048 0.1269 0.1447 -0.0168 0.0363  -0.0217 239 LEU A C   
1963 O  O   . LEU A 239 ? 0.1754 0.1483 0.1626 -0.0255 0.0333  -0.0272 239 LEU A O   
1964 C  CB  . LEU A 239 ? 0.1945 0.1169 0.1648 0.0139  0.0199  -0.0212 239 LEU A CB  
1965 C  CG  . LEU A 239 ? 0.1747 0.1718 0.2211 -0.0076 0.0089  -0.0908 239 LEU A CG  
1966 C  CD1 . LEU A 239 ? 0.2829 0.1617 0.3448 0.0060  -0.0289 -0.0706 239 LEU A CD1 
1967 C  CD2 . LEU A 239 ? 0.2717 0.1687 0.1684 -0.0182 0.0230  -0.0714 239 LEU A CD2 
1968 N  N   . MET A 240 ? 0.2082 0.1324 0.1238 0.0015  0.0359  -0.0073 240 MET A N   
1969 C  CA  . MET A 240 ? 0.2092 0.1127 0.1342 -0.0040 0.0602  -0.0076 240 MET A CA  
1970 C  C   . MET A 240 ? 0.1791 0.1320 0.1228 -0.0229 0.0286  -0.0217 240 MET A C   
1971 O  O   . MET A 240 ? 0.1723 0.1471 0.1425 -0.0192 0.0307  -0.0038 240 MET A O   
1972 C  CB  . MET A 240 ? 0.2521 0.1269 0.1210 0.0048  0.0457  -0.0175 240 MET A CB  
1973 C  CG  . MET A 240 ? 0.1869 0.1424 0.1174 -0.0077 0.0366  -0.0326 240 MET A CG  
1974 S  SD  . MET A 240 ? 0.2474 0.1177 0.1489 -0.0137 0.0304  -0.0075 240 MET A SD  
1975 C  CE  . MET A 240 ? 0.2604 0.1303 0.1321 -0.0390 0.0570  -0.0004 240 MET A CE  
1976 N  N   . VAL A 241 ? 0.1817 0.0921 0.1187 -0.0076 0.0300  -0.0027 241 VAL A N   
1977 C  CA  . VAL A 241 ? 0.1824 0.1127 0.1190 -0.0367 0.0313  -0.0128 241 VAL A CA  
1978 C  C   . VAL A 241 ? 0.1582 0.1198 0.1323 0.0068  0.0263  -0.0100 241 VAL A C   
1979 O  O   . VAL A 241 ? 0.1535 0.1364 0.1349 -0.0015 0.0370  -0.0057 241 VAL A O   
1980 C  CB  . VAL A 241 ? 0.1629 0.1163 0.1335 -0.0321 0.0200  -0.0165 241 VAL A CB  
1981 C  CG1 . VAL A 241 ? 0.1974 0.1129 0.1571 -0.0174 -0.0208 -0.0245 241 VAL A CG1 
1982 C  CG2 . VAL A 241 ? 0.1862 0.1303 0.1812 0.0100  0.0401  -0.0131 241 VAL A CG2 
1983 N  N   . ASP A 242 ? 0.1429 0.1154 0.1206 0.0016  0.0288  -0.0140 242 ASP A N   
1984 C  CA  . ASP A 242 ? 0.1453 0.1023 0.1454 0.0087  0.0064  -0.0141 242 ASP A CA  
1985 C  C   . ASP A 242 ? 0.1450 0.1111 0.1208 -0.0193 0.0353  -0.0030 242 ASP A C   
1986 O  O   . ASP A 242 ? 0.1578 0.1252 0.1547 -0.0179 0.0126  -0.0133 242 ASP A O   
1987 C  CB  . ASP A 242 ? 0.1371 0.0977 0.1720 0.0103  0.0299  -0.0020 242 ASP A CB  
1988 C  CG  . ASP A 242 ? 0.1949 0.1007 0.1244 -0.0020 0.0479  0.0021  242 ASP A CG  
1989 O  OD1 . ASP A 242 ? 0.1727 0.1111 0.1314 -0.0044 0.0243  -0.0068 242 ASP A OD1 
1990 O  OD2 . ASP A 242 ? 0.2036 0.0991 0.1831 0.0011  0.0474  -0.0171 242 ASP A OD2 
1991 N  N   . ASN A 243 ? 0.1436 0.0987 0.1238 -0.0091 0.0315  -0.0181 243 ASN A N   
1992 C  CA  . ASN A 243 ? 0.1790 0.0961 0.1076 -0.0081 0.0100  -0.0178 243 ASN A CA  
1993 C  C   . ASN A 243 ? 0.1071 0.1095 0.1162 -0.0033 0.0158  0.0011  243 ASN A C   
1994 O  O   . ASN A 243 ? 0.1597 0.1109 0.1303 0.0163  0.0234  0.0085  243 ASN A O   
1995 C  CB  . ASN A 243 ? 0.1492 0.1423 0.1117 -0.0083 0.0118  0.0048  243 ASN A CB  
1996 C  CG  . ASN A 243 ? 0.1418 0.0921 0.1382 0.0002  0.0309  -0.0083 243 ASN A CG  
1997 O  OD1 . ASN A 243 ? 0.1806 0.1159 0.1489 -0.0253 0.0156  0.0117  243 ASN A OD1 
1998 N  ND2 . ASN A 243 ? 0.1824 0.1644 0.1720 -0.0127 -0.0161 0.0463  243 ASN A ND2 
1999 N  N   . TRP A 244 ? 0.1442 0.0953 0.0950 -0.0037 0.0161  -0.0105 244 TRP A N   
2000 C  CA  . TRP A 244 ? 0.1266 0.1068 0.0986 -0.0055 0.0141  -0.0064 244 TRP A CA  
2001 C  C   . TRP A 244 ? 0.1210 0.1278 0.1274 -0.0040 0.0107  0.0146  244 TRP A C   
2002 O  O   . TRP A 244 ? 0.1342 0.1168 0.1320 0.0082  -0.0030 -0.0108 244 TRP A O   
2003 C  CB  . TRP A 244 ? 0.1493 0.0653 0.1142 0.0008  0.0100  -0.0031 244 TRP A CB  
2004 C  CG  . TRP A 244 ? 0.1388 0.0664 0.1301 -0.0070 0.0051  0.0054  244 TRP A CG  
2005 C  CD1 . TRP A 244 ? 0.1294 0.1110 0.1398 0.0166  0.0260  -0.0194 244 TRP A CD1 
2006 C  CD2 . TRP A 244 ? 0.1344 0.0924 0.1147 0.0043  0.0229  0.0075  244 TRP A CD2 
2007 N  NE1 . TRP A 244 ? 0.1389 0.1083 0.1137 0.0080  0.0184  0.0029  244 TRP A NE1 
2008 C  CE2 . TRP A 244 ? 0.1386 0.0989 0.1240 0.0260  0.0106  0.0065  244 TRP A CE2 
2009 C  CE3 . TRP A 244 ? 0.1443 0.1499 0.1221 -0.0077 0.0058  0.0358  244 TRP A CE3 
2010 C  CZ2 . TRP A 244 ? 0.1686 0.0949 0.1477 0.0136  -0.0111 0.0076  244 TRP A CZ2 
2011 C  CZ3 . TRP A 244 ? 0.1847 0.1335 0.1253 0.0039  0.0334  0.0231  244 TRP A CZ3 
2012 C  CH2 . TRP A 244 ? 0.1854 0.1413 0.1399 -0.0082 -0.0006 0.0095  244 TRP A CH2 
2013 N  N   . ARG A 245 ? 0.1278 0.1145 0.1180 -0.0234 -0.0039 -0.0079 245 ARG A N   
2014 C  CA  . ARG A 245 ? 0.1170 0.1045 0.1170 -0.0095 0.0081  -0.0119 245 ARG A CA  
2015 C  C   . ARG A 245 ? 0.1107 0.1162 0.1140 -0.0111 -0.0050 -0.0198 245 ARG A C   
2016 O  O   . ARG A 245 ? 0.1206 0.1190 0.1429 -0.0055 0.0176  -0.0160 245 ARG A O   
2017 C  CB  . ARG A 245 ? 0.1055 0.1205 0.1370 -0.0108 -0.0141 -0.0402 245 ARG A CB  
2018 C  CG  . ARG A 245 ? 0.0959 0.1081 0.1668 -0.0031 -0.0220 -0.0383 245 ARG A CG  
2019 C  CD  . ARG A 245 ? 0.1115 0.1247 0.1676 -0.0309 -0.0018 -0.0488 245 ARG A CD  
2020 N  NE  . ARG A 245 ? 0.0998 0.1324 0.1773 -0.0353 0.0103  -0.0331 245 ARG A NE  
2021 C  CZ  . ARG A 245 ? 0.0971 0.1156 0.1632 -0.0187 0.0150  -0.0386 245 ARG A CZ  
2022 N  NH1 . ARG A 245 ? 0.1212 0.1302 0.1896 0.0022  0.0145  -0.0254 245 ARG A NH1 
2023 N  NH2 . ARG A 245 ? 0.0987 0.1547 0.2017 -0.0098 -0.0032 -0.0207 245 ARG A NH2 
2024 N  N   . PRO A 246 ? 0.1344 0.1126 0.1488 0.0064  0.0170  -0.0078 246 PRO A N   
2025 C  CA  . PRO A 246 ? 0.1493 0.1310 0.1377 0.0124  0.0214  -0.0019 246 PRO A CA  
2026 C  C   . PRO A 246 ? 0.1222 0.1252 0.1241 0.0236  0.0102  0.0049  246 PRO A C   
2027 O  O   . PRO A 246 ? 0.1434 0.1319 0.1456 0.0025  -0.0099 -0.0002 246 PRO A O   
2028 C  CB  . PRO A 246 ? 0.1847 0.1831 0.2029 0.0787  0.0325  -0.0071 246 PRO A CB  
2029 C  CG  . PRO A 246 ? 0.1921 0.2315 0.2908 0.0652  0.0718  0.0854  246 PRO A CG  
2030 C  CD  . PRO A 246 ? 0.1208 0.1824 0.1932 0.0345  0.0195  0.0377  246 PRO A CD  
2031 N  N   . ALA A 247 ? 0.1596 0.1339 0.1089 0.0122  0.0065  0.0100  247 ALA A N   
2032 C  CA  . ALA A 247 ? 0.1492 0.1149 0.1012 0.0173  0.0018  0.0049  247 ALA A CA  
2033 C  C   . ALA A 247 ? 0.1432 0.1113 0.1302 0.0302  0.0074  0.0210  247 ALA A C   
2034 O  O   . ALA A 247 ? 0.1711 0.1199 0.1729 0.0493  -0.0226 -0.0168 247 ALA A O   
2035 C  CB  . ALA A 247 ? 0.1805 0.1493 0.1377 0.0098  0.0272  0.0295  247 ALA A CB  
2036 N  N   . GLN A 248 ? 0.1246 0.1188 0.1237 0.0183  -0.0075 -0.0025 248 GLN A N   
2037 C  CA  . GLN A 248 ? 0.1371 0.1100 0.1495 0.0273  -0.0175 0.0062  248 GLN A CA  
2038 C  C   . GLN A 248 ? 0.1460 0.1113 0.1477 0.0284  -0.0326 0.0107  248 GLN A C   
2039 O  O   . GLN A 248 ? 0.1463 0.1461 0.1529 0.0245  -0.0047 0.0019  248 GLN A O   
2040 C  CB  . GLN A 248 ? 0.1705 0.1138 0.1465 0.0252  0.0039  -0.0015 248 GLN A CB  
2041 C  CG  . GLN A 248 ? 0.1526 0.1277 0.1492 0.0013  0.0185  0.0011  248 GLN A CG  
2042 C  CD  . GLN A 248 ? 0.1113 0.2093 0.1560 -0.0095 0.0065  -0.0142 248 GLN A CD  
2043 O  OE1 . GLN A 248 ? 0.1429 0.2319 0.2085 -0.0292 -0.0284 -0.0225 248 GLN A OE1 
2044 N  NE2 . GLN A 248 ? 0.1643 0.1581 0.1908 0.0170  0.0128  -0.0051 248 GLN A NE2 
2045 N  N   . PRO A 249 ? 0.1709 0.1811 0.1691 0.0381  -0.0364 -0.0254 249 PRO A N   
2046 C  CA  . PRO A 249 ? 0.1856 0.2751 0.1550 0.1000  -0.0225 -0.0326 249 PRO A CA  
2047 C  C   . PRO A 249 ? 0.1708 0.1680 0.1486 0.0549  -0.0307 -0.0066 249 PRO A C   
2048 O  O   . PRO A 249 ? 0.1812 0.1860 0.1590 0.0398  -0.0317 0.0118  249 PRO A O   
2049 C  CB  . PRO A 249 ? 0.1905 0.3684 0.2059 0.1291  -0.0678 -0.0995 249 PRO A CB  
2050 C  CG  . PRO A 249 ? 0.2296 0.4067 0.1550 0.1016  -0.0633 -0.0732 249 PRO A CG  
2051 C  CD  . PRO A 249 ? 0.1558 0.2952 0.1808 0.0289  -0.0477 -0.0184 249 PRO A CD  
2052 N  N   . LEU A 250 ? 0.1920 0.2253 0.1370 0.0753  -0.0083 -0.0027 250 LEU A N   
2053 C  CA  . LEU A 250 ? 0.1648 0.1998 0.1450 0.0436  -0.0016 -0.0298 250 LEU A CA  
2054 C  C   . LEU A 250 ? 0.1770 0.2050 0.1736 0.0364  -0.0274 -0.0296 250 LEU A C   
2055 O  O   . LEU A 250 ? 0.2036 0.1798 0.1856 0.0344  -0.0439 -0.0017 250 LEU A O   
2056 C  CB  . LEU A 250 ? 0.2359 0.1913 0.1558 0.0223  0.0066  0.0029  250 LEU A CB  
2057 C  CG  . LEU A 250 ? 0.2476 0.2172 0.1526 0.0242  0.0260  0.0065  250 LEU A CG  
2058 C  CD1 . LEU A 250 ? 0.2286 0.2020 0.1447 0.0168  0.0114  -0.0013 250 LEU A CD1 
2059 C  CD2 . LEU A 250 ? 0.2978 0.2481 0.1842 -0.0651 0.0392  -0.0329 250 LEU A CD2 
2060 N  N   . LYS A 251 ? 0.2134 0.2670 0.1395 0.0561  -0.0516 -0.0539 251 LYS A N   
2061 C  CA  . LYS A 251 ? 0.2477 0.2347 0.1274 0.0712  -0.0710 -0.0359 251 LYS A CA  
2062 C  C   . LYS A 251 ? 0.2834 0.2743 0.2333 0.1120  -0.0274 -0.0243 251 LYS A C   
2063 O  O   . LYS A 251 ? 0.3726 0.4124 0.2018 -0.0029 0.0326  -0.0703 251 LYS A O   
2064 C  CB  . LYS A 251 ? 0.2597 0.2423 0.2139 0.0226  -0.0725 -0.0686 251 LYS A CB  
2065 C  CG  . LYS A 251 ? 0.2835 0.3718 0.2555 -0.0140 0.0115  -0.1082 251 LYS A CG  
2066 C  CD  . LYS A 251 ? 0.4047 0.3884 0.2849 -0.0665 0.0105  -0.1253 251 LYS A CD  
2067 C  CE  . LYS A 251 ? 0.3599 0.3977 0.3116 -0.0574 0.0170  -0.1291 251 LYS A CE  
2068 N  NZ  . LYS A 251 ? 0.3660 0.3579 0.3784 0.0139  -0.0196 -0.0053 251 LYS A NZ  
2069 N  N   . ASN A 252 ? 0.2312 0.3113 0.2301 0.1025  -0.1042 -0.0798 252 ASN A N   
2070 C  CA  . ASN A 252 ? 0.2944 0.5658 0.3962 0.1442  -0.0166 -0.1420 252 ASN A CA  
2071 C  C   . ASN A 252 ? 0.3419 0.4798 0.5273 0.1184  -0.1538 -0.2129 252 ASN A C   
2072 O  O   . ASN A 252 ? 0.4529 0.4834 0.5400 0.1623  -0.1720 -0.2053 252 ASN A O   
2073 C  CB  . ASN A 252 ? 0.3967 0.4967 0.5466 0.0746  -0.0276 -0.1865 252 ASN A CB  
2074 C  CG  . ASN A 252 ? 0.6757 0.4283 0.7677 0.1570  0.0979  -0.2252 252 ASN A CG  
2075 O  OD1 . ASN A 252 ? 0.7386 0.7689 0.6753 -0.1210 -0.2814 0.0049  252 ASN A OD1 
2076 N  ND2 . ASN A 252 ? 0.6351 0.3820 0.4858 0.1210  -0.1976 -0.1456 252 ASN A ND2 
2077 N  N   . ARG A 253 ? 0.1770 0.3216 0.1544 0.0372  0.0100  0.0020  253 ARG A N   
2078 C  CA  . ARG A 253 ? 0.1687 0.2400 0.1565 0.0252  0.0049  -0.0300 253 ARG A CA  
2079 C  C   . ARG A 253 ? 0.2310 0.1953 0.1495 0.0059  0.0055  -0.0454 253 ARG A C   
2080 O  O   . ARG A 253 ? 0.3045 0.1998 0.2588 0.0420  0.0683  0.0212  253 ARG A O   
2081 C  CB  . ARG A 253 ? 0.1989 0.1597 0.1389 -0.0010 -0.0076 -0.0252 253 ARG A CB  
2082 C  CG  . ARG A 253 ? 0.2197 0.1520 0.1183 0.0038  0.0005  -0.0206 253 ARG A CG  
2083 C  CD  . ARG A 253 ? 0.1891 0.1571 0.1170 0.0445  -0.0050 -0.0075 253 ARG A CD  
2084 N  NE  . ARG A 253 ? 0.1963 0.1407 0.1197 0.0430  -0.0068 -0.0105 253 ARG A NE  
2085 C  CZ  . ARG A 253 ? 0.1362 0.1161 0.1183 0.0252  0.0099  0.0039  253 ARG A CZ  
2086 N  NH1 . ARG A 253 ? 0.1367 0.1332 0.1324 0.0126  -0.0198 0.0034  253 ARG A NH1 
2087 N  NH2 . ARG A 253 ? 0.1436 0.1073 0.1611 0.0214  -0.0167 -0.0255 253 ARG A NH2 
2088 N  N   . GLN A 254 ? 0.2269 0.2036 0.1414 0.0073  -0.0310 -0.0365 254 GLN A N   
2089 C  CA  . GLN A 254 ? 0.2442 0.2955 0.1493 -0.0089 -0.0532 -0.0239 254 GLN A CA  
2090 C  C   . GLN A 254 ? 0.2192 0.2438 0.1382 -0.0071 -0.0443 0.0088  254 GLN A C   
2091 O  O   . GLN A 254 ? 0.2807 0.2236 0.2577 -0.0074 -0.0798 -0.0122 254 GLN A O   
2092 C  CB  . GLN A 254 ? 0.3370 0.3632 0.1571 -0.0126 -0.0144 -0.0644 254 GLN A CB  
2093 C  CG  . GLN A 254 ? 0.4948 0.4545 0.1756 0.1761  -0.0096 0.0283  254 GLN A CG  
2094 C  CD  . GLN A 254 ? 0.5689 0.8194 0.4347 0.2089  0.1419  0.0520  254 GLN A CD  
2095 O  OE1 . GLN A 254 ? 1.2361 0.9113 0.3946 0.3416  0.4390  0.3138  254 GLN A OE1 
2096 N  NE2 . GLN A 254 ? 0.7832 0.3461 0.6657 -0.1362 0.3158  -0.0179 254 GLN A NE2 
2097 N  N   . ILE A 255 ? 0.1903 0.2117 0.1228 0.0136  -0.0033 0.0003  255 ILE A N   
2098 C  CA  . ILE A 255 ? 0.1762 0.1757 0.1174 0.0328  0.0102  -0.0146 255 ILE A CA  
2099 C  C   . ILE A 255 ? 0.1826 0.1533 0.1508 0.0113  0.0307  0.0205  255 ILE A C   
2100 O  O   . ILE A 255 ? 0.2280 0.1576 0.2000 0.0182  0.0535  0.0480  255 ILE A O   
2101 C  CB  . ILE A 255 ? 0.1553 0.1368 0.1461 0.0290  -0.0069 0.0146  255 ILE A CB  
2102 C  CG1 . ILE A 255 ? 0.1646 0.1780 0.1777 0.0485  0.0006  -0.0080 255 ILE A CG1 
2103 C  CG2 . ILE A 255 ? 0.1720 0.2078 0.1553 0.0291  -0.0023 0.0211  255 ILE A CG2 
2104 C  CD1 . ILE A 255 ? 0.1896 0.1837 0.2036 0.0141  0.0239  -0.0378 255 ILE A CD1 
2105 N  N   . LYS A 256 ? 0.1575 0.1763 0.1429 0.0129  0.0073  0.0106  256 LYS A N   
2106 C  CA  . LYS A 256 ? 0.1686 0.1644 0.1410 0.0305  0.0212  0.0077  256 LYS A CA  
2107 C  C   . LYS A 256 ? 0.1510 0.1722 0.1321 0.0243  0.0277  0.0141  256 LYS A C   
2108 O  O   . LYS A 256 ? 0.1890 0.2275 0.1256 -0.0160 0.0347  0.0074  256 LYS A O   
2109 C  CB  . LYS A 256 ? 0.2389 0.1632 0.1920 -0.0038 0.0331  -0.0223 256 LYS A CB  
2110 C  CG  . LYS A 256 ? 0.2985 0.2757 0.2749 -0.0251 0.0153  -0.0945 256 LYS A CG  
2111 C  CD  . LYS A 256 ? 0.4695 0.2921 0.3446 0.0430  0.0384  -0.0197 256 LYS A CD  
2112 N  N   . ALA A 257 ? 0.1977 0.1831 0.1278 -0.0019 0.0414  0.0137  257 ALA A N   
2113 C  CA  . ALA A 257 ? 0.1610 0.1960 0.1486 0.0108  0.0358  0.0296  257 ALA A CA  
2114 C  C   . ALA A 257 ? 0.1630 0.1725 0.1125 0.0059  0.0498  0.0387  257 ALA A C   
2115 O  O   . ALA A 257 ? 0.1996 0.2433 0.1400 -0.0010 0.0444  -0.0119 257 ALA A O   
2116 C  CB  . ALA A 257 ? 0.2309 0.2060 0.1522 -0.0292 0.0249  0.0529  257 ALA A CB  
2117 N  N   . SER A 258 ? 0.1777 0.1669 0.1417 -0.0050 0.0233  0.0204  258 SER A N   
2118 C  CA  . SER A 258 ? 0.1709 0.2097 0.1708 0.0091  0.0298  0.0082  258 SER A CA  
2119 C  C   . SER A 258 ? 0.1604 0.2437 0.1982 0.0190  0.0508  0.0121  258 SER A C   
2120 O  O   . SER A 258 ? 0.1709 0.3723 0.2684 0.0431  0.0668  0.0194  258 SER A O   
2121 C  CB  . SER A 258 ? 0.2114 0.1590 0.1702 -0.0079 0.0046  0.0153  258 SER A CB  
2122 O  OG  . SER A 258 ? 0.1612 0.1980 0.1740 -0.0066 0.0275  0.0044  258 SER A OG  
2123 N  N   . PHE A 259 ? 0.1726 0.2701 0.1737 -0.0385 0.0624  0.0107  259 PHE A N   
2124 C  CA  . PHE A 259 ? 0.2272 0.2501 0.2509 -0.0611 0.0765  0.0145  259 PHE A CA  
2125 C  C   . PHE A 259 ? 0.3394 0.3788 0.2985 -0.0209 0.0326  0.0126  259 PHE A C   
2126 O  O   . PHE A 259 ? 0.3838 0.3284 0.2393 -0.0917 -0.0027 0.1180  259 PHE A O   
2127 C  CB  . PHE A 259 ? 0.2341 0.2282 0.2703 -0.0004 0.0435  0.0106  259 PHE A CB  
2128 C  CG  . PHE A 259 ? 0.2095 0.2456 0.2470 0.0172  0.0176  0.1037  259 PHE A CG  
2129 C  CD1 . PHE A 259 ? 0.2132 0.1944 0.1761 -0.0203 0.0155  -0.0085 259 PHE A CD1 
2130 C  CD2 . PHE A 259 ? 0.3168 0.2125 0.3780 -0.0447 0.0582  0.1004  259 PHE A CD2 
2131 C  CE1 . PHE A 259 ? 0.2731 0.2027 0.2129 0.0212  0.0027  -0.0261 259 PHE A CE1 
2132 C  CE2 . PHE A 259 ? 0.2654 0.3177 0.4375 -0.0389 -0.0361 0.1038  259 PHE A CE2 
2133 C  CZ  . PHE A 259 ? 0.2636 0.1672 0.3944 -0.0313 -0.0137 -0.0365 259 PHE A CZ  
2134 N  N   . LYS A 260 ? 0.3836 0.7616 0.4117 -0.1342 0.1288  -0.0258 260 LYS A N   
2135 C  CA  . LYS A 260 ? 1.0033 0.5119 0.5950 0.0120  -0.0054 0.0774  260 LYS A CA  
2136 C  C   . LYS A 260 ? 0.8543 0.9957 0.6794 0.0677  -0.1306 -0.0264 260 LYS A C   
2137 O  O   . LYS A 260 ? 1.1271 1.1264 0.7733 0.4283  -0.1370 -0.0380 260 LYS A O   
2138 C  CB  . LYS A 260 ? 1.1122 0.6051 1.1392 -0.2268 0.3684  0.2625  260 LYS A CB  
2139 O  OXT . LYS A 260 ? 0.9886 0.8741 0.6126 0.0016  0.1105  -0.0807 260 LYS A OXT 
2140 ZN ZN  . ZN  B .   ? 0.1317 0.1025 0.1080 -0.0016 -0.0075 0.0027  301 ZN  A ZN  
2141 O  O20 A V13 C .   ? 0.3276 0.4890 0.3215 0.0184  0.0029  0.1345  302 V13 A O20 
2142 O  O20 B V13 C .   ? 0.4636 0.4476 0.3658 0.0064  -0.1547 0.1107  302 V13 A O20 
2143 S  S15 A V13 C .   ? 0.3112 0.2487 0.3021 -0.0807 0.0067  0.0538  302 V13 A S15 
2144 S  S15 B V13 C .   ? 0.3292 0.5149 0.3366 -0.1425 -0.0453 0.1912  302 V13 A S15 
2145 O  O19 A V13 C .   ? 0.6682 0.3617 0.6184 0.1193  0.1324  -0.0207 302 V13 A O19 
2146 O  O19 B V13 C .   ? 0.5231 0.2972 0.4051 -0.0376 -0.0917 0.1234  302 V13 A O19 
2147 C  C16 A V13 C .   ? 0.4305 0.2855 0.3280 -0.1073 -0.0179 0.1491  302 V13 A C16 
2148 C  C16 B V13 C .   ? 0.9632 0.4398 0.6005 -0.0380 -0.2060 -0.0820 302 V13 A C16 
2149 C  C17 A V13 C .   ? 0.4258 0.1027 0.0933 0.0084  -0.0268 0.0140  302 V13 A C17 
2150 C  C17 B V13 C .   ? 0.8951 0.6384 0.8531 0.1404  -0.1755 0.0261  302 V13 A C17 
2151 O  O18 A V13 C .   ? 0.3675 0.3522 0.2640 -0.0842 0.0668  -0.0572 302 V13 A O18 
2152 O  O18 B V13 C .   ? 0.5223 0.8119 1.2881 -0.1311 0.3326  -0.0278 302 V13 A O18 
2153 C  C1  A V13 C .   ? 0.2055 0.2255 0.2255 -0.0034 -0.0015 0.0775  302 V13 A C1  
2154 C  C1  B V13 C .   ? 0.2845 0.2927 0.2057 -0.1294 -0.0533 0.0358  302 V13 A C1  
2155 C  C6  A V13 C .   ? 0.1985 0.1723 0.1382 -0.0078 0.0058  0.0142  302 V13 A C6  
2156 C  C6  B V13 C .   ? 0.2127 0.1978 0.2689 -0.1302 -0.0330 0.0359  302 V13 A C6  
2157 F  F11 A V13 C .   ? 0.2109 0.2445 0.2371 -0.0285 0.0082  -0.0325 302 V13 A F11 
2158 F  F11 B V13 C .   ? 0.4226 0.2445 0.4248 -0.0439 -0.0770 0.1080  302 V13 A F11 
2159 C  C5  A V13 C .   ? 0.2038 0.1428 0.1619 -0.0140 0.0113  -0.0161 302 V13 A C5  
2160 C  C5  B V13 C .   ? 0.1989 0.0822 0.1908 -0.0306 -0.0167 -0.0168 302 V13 A C5  
2161 F  F12 A V13 C .   ? 0.1502 0.1877 0.1867 0.0087  0.0126  -0.0153 302 V13 A F12 
2162 F  F12 B V13 C .   ? 0.1927 0.0357 0.2207 -0.0072 -0.0260 -0.0020 302 V13 A F12 
2163 C  C4  A V13 C .   ? 0.2064 0.1593 0.1745 -0.0034 0.0199  0.0178  302 V13 A C4  
2164 C  C4  B V13 C .   ? 0.1421 0.0991 0.1122 -0.0100 -0.0403 0.0148  302 V13 A C4  
2165 S  S7  A V13 C .   ? 0.1367 0.1048 0.1352 0.0132  -0.0092 -0.0058 302 V13 A S7  
2166 S  S7  B V13 C .   ? 0.1428 0.0986 0.1106 -0.0201 -0.0172 -0.0097 302 V13 A S7  
2167 O  O9  A V13 C .   ? 0.1253 0.1167 0.1195 0.0016  -0.0065 0.0013  302 V13 A O9  
2168 O  O9  B V13 C .   ? 0.1364 0.1090 0.1443 -0.0059 -0.0556 -0.0195 302 V13 A O9  
2169 N  N10 A V13 C .   ? 0.1562 0.1132 0.1526 0.0211  -0.0403 -0.0262 302 V13 A N10 
2170 N  N10 B V13 C .   ? 0.1967 0.1084 0.1957 -0.0346 -0.0318 -0.0603 302 V13 A N10 
2171 O  O8  A V13 C .   ? 0.1172 0.1580 0.1657 -0.0243 0.0093  -0.0168 302 V13 A O8  
2172 O  O8  B V13 C .   ? 0.1393 0.0542 0.1359 0.0034  -0.0194 -0.0151 302 V13 A O8  
2173 C  C3  A V13 C .   ? 0.2000 0.2013 0.2585 0.0387  0.0109  -0.0025 302 V13 A C3  
2174 C  C3  B V13 C .   ? 0.1568 0.2183 0.1230 -0.0816 0.0097  -0.0087 302 V13 A C3  
2175 F  F13 A V13 C .   ? 0.1993 0.1819 0.4572 0.0244  -0.1059 0.0359  302 V13 A F13 
2176 F  F13 B V13 C .   ? 0.0976 0.2786 0.2815 -0.0504 0.0359  -0.1038 302 V13 A F13 
2177 C  C2  A V13 C .   ? 0.1993 0.1794 0.3693 0.0163  -0.0370 -0.0124 302 V13 A C2  
2178 C  C2  B V13 C .   ? 0.2454 0.3303 0.1479 -0.1252 -0.0119 0.0324  302 V13 A C2  
2179 F  F14 A V13 C .   ? 0.2576 0.1779 0.3959 -0.0377 -0.0972 0.0910  302 V13 A F14 
2180 F  F14 B V13 C .   ? 0.3694 0.4467 0.1357 -0.2470 0.0544  0.0328  302 V13 A F14 
2181 N  N1  . BCN D .   ? 0.5787 0.5664 0.3570 -0.1093 -0.1003 0.2151  303 BCN A N1  
2182 C  C1  . BCN D .   ? 0.2981 0.5292 0.4219 -0.1256 -0.0879 0.0635  303 BCN A C1  
2183 C  C2  . BCN D .   ? 0.7123 0.7065 0.5758 -0.0253 -0.0859 0.2275  303 BCN A C2  
2184 O  O21 . BCN D .   ? 0.6745 0.6429 0.8938 -0.3244 -0.1127 0.0476  303 BCN A O21 
2185 O  O22 . BCN D .   ? 0.8246 0.4476 0.5507 0.0203  0.0139  0.0864  303 BCN A O22 
2186 C  C3  . BCN D .   ? 0.7523 0.6226 0.5153 -0.1713 -0.0659 -0.1347 303 BCN A C3  
2187 C  C4  . BCN D .   ? 0.2813 0.6393 0.6751 -0.1488 -0.0469 -0.0217 303 BCN A C4  
2188 O  O4  . BCN D .   ? 0.6383 0.4973 0.7616 -0.2094 -0.1249 0.1801  303 BCN A O4  
2189 C  C5  . BCN D .   ? 0.4106 0.3483 0.4716 -0.0639 0.0656  0.0754  303 BCN A C5  
2190 C  C6  . BCN D .   ? 0.8868 0.3630 0.5358 0.1052  0.1075  -0.2166 303 BCN A C6  
2191 O  O6  . BCN D .   ? 0.4474 0.3163 0.3687 -0.0718 0.0688  -0.0212 303 BCN A O6  
2192 S  S   . DMS E .   ? 0.3110 0.3656 0.3730 -0.0265 0.0215  -0.0397 304 DMS A S   
2193 O  O   . DMS E .   ? 0.4632 0.5001 0.4914 0.0409  0.1267  -0.3118 304 DMS A O   
2194 C  C1  . DMS E .   ? 0.3657 0.2962 0.6498 -0.0328 -0.0107 0.1728  304 DMS A C1  
2195 C  C2  . DMS E .   ? 0.2917 0.3066 0.3184 -0.0313 0.0644  -0.1531 304 DMS A C2  
2196 NA NA  . NA  F .   ? 0.4162 0.1863 0.3500 -0.0242 -0.0044 0.0013  305 NA  A NA  
2197 O  O   . HOH G .   ? 0.2946 0.3039 0.6456 -0.0361 -0.0003 0.1023  401 HOH A O   
2198 O  O   . HOH G .   ? 0.8033 0.4529 0.8544 0.0036  -0.4454 0.0048  402 HOH A O   
2199 O  O   . HOH G .   ? 0.3705 0.3437 0.3864 -0.0306 0.0775  0.1085  403 HOH A O   
2200 O  O   . HOH G .   ? 0.5497 0.5438 0.4186 0.0405  0.1342  0.0550  404 HOH A O   
2201 O  O   . HOH G .   ? 0.3114 0.3464 0.5612 0.1024  -0.0111 -0.0204 405 HOH A O   
2202 O  O   . HOH G .   ? 0.3908 0.7735 0.6276 -0.2257 0.3189  0.0567  406 HOH A O   
2203 O  O   . HOH G .   ? 0.4562 0.3999 0.8758 -0.0333 -0.1585 -0.0937 407 HOH A O   
2204 O  O   . HOH G .   ? 0.3078 0.2787 0.3430 -0.0156 0.0740  0.0709  408 HOH A O   
2205 O  O   . HOH G .   ? 0.4671 0.2991 0.6847 0.0662  -0.1159 0.0815  409 HOH A O   
2206 O  O   . HOH G .   ? 0.7893 0.4126 0.3697 -0.0752 0.0226  0.0597  410 HOH A O   
2207 O  O   . HOH G .   ? 0.5075 1.0382 0.4292 0.1610  -0.0738 -0.1735 411 HOH A O   
2208 O  O   . HOH G .   ? 0.1772 0.5158 0.4672 0.0001  0.0163  -0.1361 412 HOH A O   
2209 O  O   . HOH G .   ? 0.6549 0.4552 0.7260 -0.1838 0.2247  -0.0883 413 HOH A O   
2210 O  O   . HOH G .   ? 0.4813 0.4527 0.3030 0.0004  0.0373  0.0974  414 HOH A O   
2211 O  O   . HOH G .   ? 0.7440 0.2623 0.3443 0.1716  -0.0648 -0.0544 415 HOH A O   
2212 O  O   . HOH G .   ? 0.3590 0.2621 0.3226 -0.0472 0.0634  -0.0757 416 HOH A O   
2213 O  O   . HOH G .   ? 0.7503 0.4335 0.5278 0.0252  0.2094  0.1377  417 HOH A O   
2214 O  O   . HOH G .   ? 0.6147 0.3304 0.5168 -0.0886 -0.1669 0.1683  418 HOH A O   
2215 O  O   . HOH G .   ? 0.4786 0.3633 1.0172 0.0310  -0.2843 -0.0529 419 HOH A O   
2216 O  O   . HOH G .   ? 0.5551 0.3367 0.4746 -0.0395 -0.2900 -0.0965 420 HOH A O   
2217 O  O   . HOH G .   ? 0.2332 0.3999 0.5118 0.0351  0.0000  0.0524  421 HOH A O   
2218 O  O   . HOH G .   ? 0.8112 0.8488 0.3684 -0.1064 -0.0903 -0.0693 422 HOH A O   
2219 O  O   . HOH G .   ? 0.4325 0.7656 0.3494 -0.1002 0.0414  -0.0205 423 HOH A O   
2220 O  O   . HOH G .   ? 0.8402 0.3586 0.2893 -0.2559 0.1337  -0.1254 424 HOH A O   
2221 O  O   . HOH G .   ? 0.4263 0.4012 0.3130 0.1177  0.1312  -0.0366 425 HOH A O   
2222 O  O   . HOH G .   ? 0.5681 0.3994 0.4661 -0.2189 -0.2313 0.1732  426 HOH A O   
2223 O  O   . HOH G .   ? 0.5389 0.5678 0.3812 -0.0939 0.0878  -0.0264 427 HOH A O   
2224 O  O   . HOH G .   ? 0.5057 0.4398 0.3660 -0.1312 0.0129  -0.0351 428 HOH A O   
2225 O  O   . HOH G .   ? 0.3657 0.5159 0.4676 0.0826  -0.0692 -0.2595 429 HOH A O   
2226 O  O   . HOH G .   ? 0.4353 0.2602 0.5312 0.0072  -0.1790 0.1041  430 HOH A O   
2227 O  O   . HOH G .   ? 0.4410 0.3340 0.2696 -0.1571 0.0955  -0.1015 431 HOH A O   
2228 O  O   . HOH G .   ? 0.3963 0.6610 0.5499 -0.0093 0.0469  0.3315  432 HOH A O   
2229 O  O   . HOH G .   ? 0.3861 0.3193 0.3672 -0.0447 0.1365  -0.1159 433 HOH A O   
2230 O  O   . HOH G .   ? 0.3506 0.3752 0.3933 -0.1102 0.0449  0.1017  434 HOH A O   
2231 O  O   . HOH G .   ? 0.4234 0.3626 0.1600 0.0004  -0.0155 0.0087  435 HOH A O   
2232 O  O   . HOH G .   ? 0.1449 0.1256 0.1314 -0.0126 0.0263  -0.0033 436 HOH A O   
2233 O  O   . HOH G .   ? 0.3491 0.2176 0.4299 -0.0113 -0.1796 -0.0890 437 HOH A O   
2234 O  O   . HOH G .   ? 0.2835 0.2749 0.3680 0.0389  -0.0303 0.0289  438 HOH A O   
2235 O  O   . HOH G .   ? 0.4616 0.4283 0.4205 0.0108  -0.0115 0.0162  439 HOH A O   
2236 O  O   . HOH G .   ? 0.2869 0.5410 0.4769 -0.0927 0.0832  0.0434  440 HOH A O   
2237 O  O   . HOH G .   ? 0.6932 0.4034 1.2733 -0.1473 0.3362  0.1460  441 HOH A O   
2238 O  O   . HOH G .   ? 0.7224 0.3098 0.2078 0.0930  -0.0011 0.0322  442 HOH A O   
2239 O  O   . HOH G .   ? 0.3404 0.3864 0.2311 -0.1506 -0.1198 0.0306  443 HOH A O   
2240 O  O   . HOH G .   ? 0.3454 0.2807 0.2323 0.0177  -0.0454 0.0357  444 HOH A O   
2241 O  O   . HOH G .   ? 0.3963 0.8047 0.4002 0.2780  0.0685  0.1289  445 HOH A O   
2242 O  O   . HOH G .   ? 0.8861 0.9155 0.5108 0.0009  0.1708  -0.0638 446 HOH A O   
2243 O  O   . HOH G .   ? 0.6059 0.9247 0.6578 0.1956  0.1123  0.2443  447 HOH A O   
2244 O  O   . HOH G .   ? 0.1998 0.1162 0.1921 -0.0323 0.0452  -0.0037 448 HOH A O   
2245 O  O   . HOH G .   ? 0.3878 0.3600 0.8123 -0.0422 -0.2022 -0.0747 449 HOH A O   
2246 O  O   . HOH G .   ? 0.2722 0.4422 0.3248 0.0957  0.1246  0.0206  450 HOH A O   
2247 O  O   . HOH G .   ? 0.3707 1.0157 0.4971 -0.0386 -0.1477 -0.0502 451 HOH A O   
2248 O  O   . HOH G .   ? 0.5473 0.8931 0.4709 -0.2314 -0.1161 0.2816  452 HOH A O   
2249 O  O   . HOH G .   ? 0.3223 0.2594 0.3399 0.0674  -0.1286 -0.0737 453 HOH A O   
2250 O  O   . HOH G .   ? 0.2574 0.2314 0.3470 0.0127  -0.1441 -0.0649 454 HOH A O   
2251 O  O   . HOH G .   ? 0.2512 0.2081 0.1917 0.0167  0.0767  0.0407  455 HOH A O   
2252 O  O   . HOH G .   ? 0.4093 0.2825 0.7025 -0.0122 -0.0157 -0.1172 456 HOH A O   
2253 O  O   . HOH G .   ? 0.3031 0.2900 0.2412 0.0743  0.0306  -0.0155 457 HOH A O   
2254 O  O   . HOH G .   ? 0.2557 0.3450 0.5683 0.0738  0.0091  0.1384  458 HOH A O   
2255 O  O   . HOH G .   ? 0.3146 0.3444 0.4518 0.0138  0.0071  -0.1185 459 HOH A O   
2256 O  O   . HOH G .   ? 0.3444 0.5771 0.4595 0.0244  0.1723  0.0842  460 HOH A O   
2257 O  O   . HOH G .   ? 0.7605 0.3830 0.1982 -0.0188 -0.0219 -0.0662 461 HOH A O   
2258 O  O   . HOH G .   ? 0.3263 0.1912 0.2452 -0.0525 -0.0332 -0.0403 462 HOH A O   
2259 O  O   . HOH G .   ? 0.5059 0.3780 0.3183 0.0513  0.0983  0.0842  463 HOH A O   
2260 O  O   . HOH G .   ? 0.5375 0.5097 0.3971 -0.1703 -0.0840 0.0429  464 HOH A O   
2261 O  O   . HOH G .   ? 0.7177 0.3362 0.3262 0.0594  -0.1104 -0.1292 465 HOH A O   
2262 O  O   . HOH G .   ? 0.4768 0.3944 0.4801 -0.0018 -0.0254 -0.0236 466 HOH A O   
2263 O  O   . HOH G .   ? 0.2654 0.6815 0.6190 0.0682  -0.0220 0.1293  467 HOH A O   
2264 O  O   . HOH G .   ? 0.2685 0.4986 0.3145 -0.1459 0.0239  -0.0093 468 HOH A O   
2265 O  O   . HOH G .   ? 0.3708 0.1500 0.3815 -0.0353 0.0232  -0.0243 469 HOH A O   
2266 O  O   . HOH G .   ? 0.2600 0.2549 0.8191 0.0003  0.1178  -0.1064 470 HOH A O   
2267 O  O   . HOH G .   ? 0.3846 0.6169 0.2744 0.0741  0.0205  -0.0247 471 HOH A O   
2268 O  O   . HOH G .   ? 0.2247 0.3715 0.7360 0.0055  0.0179  0.0991  472 HOH A O   
2269 O  O   . HOH G .   ? 0.4046 0.3220 0.2772 -0.1083 -0.0822 -0.0413 473 HOH A O   
2270 O  O   . HOH G .   ? 0.1987 0.1339 0.1608 -0.0210 0.0116  -0.0206 474 HOH A O   
2271 O  O   . HOH G .   ? 0.2833 0.7235 0.4067 0.0990  0.0668  0.0419  475 HOH A O   
2272 O  O   . HOH G .   ? 0.5431 0.4220 0.3068 0.1203  0.1347  0.1493  476 HOH A O   
2273 O  O   . HOH G .   ? 0.2958 0.9363 0.3813 0.0238  -0.0276 0.2692  477 HOH A O   
2274 O  O   . HOH G .   ? 0.3025 0.2260 0.2572 -0.0189 -0.0147 -0.0022 478 HOH A O   
2275 O  O   . HOH G .   ? 0.2215 0.2790 0.3709 0.0002  0.0203  -0.0537 479 HOH A O   
2276 O  O   . HOH G .   ? 0.7357 0.5252 0.4075 -0.0681 -0.0351 0.0084  480 HOH A O   
2277 O  O   . HOH G .   ? 0.1459 0.1732 0.1776 0.0231  -0.0358 0.0331  481 HOH A O   
2278 O  O   . HOH G .   ? 0.1935 0.2049 0.2147 0.0378  -0.0026 0.0149  482 HOH A O   
2279 O  O   . HOH G .   ? 0.4112 0.3999 0.4466 0.0055  0.0207  0.0179  483 HOH A O   
2280 O  O   . HOH G .   ? 0.2919 0.2147 0.3928 0.0128  0.0515  -0.0729 484 HOH A O   
2281 O  O   . HOH G .   ? 0.6420 0.4262 0.5342 0.2525  -0.2612 -0.1996 485 HOH A O   
2282 O  O   . HOH G .   ? 0.3492 0.3028 0.3777 -0.0225 -0.0480 0.1465  486 HOH A O   
2283 O  O   . HOH G .   ? 0.1719 0.1759 0.3776 -0.0255 -0.0294 0.0116  487 HOH A O   
2284 O  O   . HOH G .   ? 0.3262 0.3754 0.5353 -0.0039 -0.1450 0.1268  488 HOH A O   
2285 O  O   . HOH G .   ? 0.3074 0.3209 0.2492 0.0873  -0.0610 -0.0232 489 HOH A O   
2286 O  O   . HOH G .   ? 0.4671 0.2584 0.4095 -0.0408 0.1344  0.1149  490 HOH A O   
2287 O  O   . HOH G .   ? 0.4736 0.4011 0.5226 0.1082  0.0498  0.1332  491 HOH A O   
2288 O  O   . HOH G .   ? 0.3956 0.5365 0.4933 0.1685  -0.0591 -0.0961 492 HOH A O   
2289 O  O   . HOH G .   ? 0.2766 0.2904 0.3643 -0.0838 -0.0254 0.0802  493 HOH A O   
2290 O  O   . HOH G .   ? 0.4923 0.2422 0.2420 -0.0447 0.0144  0.0924  494 HOH A O   
2291 O  O   . HOH G .   ? 0.2815 0.5503 0.3494 -0.0935 -0.0731 0.0064  495 HOH A O   
2292 O  O   . HOH G .   ? 0.1691 0.1357 0.1274 0.0263  0.0082  0.0117  496 HOH A O   
2293 O  O   . HOH G .   ? 0.3051 0.1720 0.2106 0.0218  -0.1096 0.0277  497 HOH A O   
2294 O  O   . HOH G .   ? 0.1417 0.1039 0.1521 -0.0024 0.0252  0.0025  498 HOH A O   
2295 O  O   . HOH G .   ? 0.3780 0.1533 0.3016 0.0355  -0.0796 -0.0017 499 HOH A O   
2296 O  O   . HOH G .   ? 0.1635 0.1014 0.1463 0.0234  -0.0041 -0.0187 500 HOH A O   
2297 O  O   . HOH G .   ? 0.2866 0.3974 0.2250 0.0220  0.0065  -0.0656 501 HOH A O   
2298 O  O   . HOH G .   ? 0.2502 0.2330 0.2161 0.0113  0.0804  -0.0239 502 HOH A O   
2299 O  O   . HOH G .   ? 0.1120 0.1819 0.2699 0.0075  0.0133  -0.0300 503 HOH A O   
2300 O  O   . HOH G .   ? 0.4894 0.4348 0.2498 -0.0083 0.0723  -0.1190 504 HOH A O   
2301 O  O   . HOH G .   ? 0.4308 0.3189 0.3975 0.1700  -0.1155 -0.0838 505 HOH A O   
2302 O  O   . HOH G .   ? 0.2497 0.2423 0.4648 -0.0956 -0.0066 0.0954  506 HOH A O   
2303 O  O   . HOH G .   ? 0.2811 0.4260 0.8325 -0.0484 -0.1990 0.1162  507 HOH A O   
2304 O  O   . HOH G .   ? 0.4992 0.4197 0.4810 0.0730  0.0776  0.0882  508 HOH A O   
2305 O  O   . HOH G .   ? 0.1414 0.1831 0.2838 -0.0278 0.0138  0.0385  509 HOH A O   
2306 O  O   . HOH G .   ? 0.1752 0.3320 0.4165 -0.0331 -0.0388 0.0615  510 HOH A O   
2307 O  O   . HOH G .   ? 0.2190 0.2353 0.2206 -0.0221 0.0001  0.0581  511 HOH A O   
2308 O  O   . HOH G .   ? 0.3055 0.3165 0.2074 0.0233  0.0132  0.0241  512 HOH A O   
2309 O  O   . HOH G .   ? 0.4737 0.2976 0.8203 -0.1254 -0.1696 0.1453  513 HOH A O   
2310 O  O   . HOH G .   ? 0.4798 0.6102 0.3096 -0.0262 0.1117  0.0230  514 HOH A O   
2311 O  O   . HOH G .   ? 0.2924 0.2670 0.3435 -0.0353 -0.0592 0.1005  515 HOH A O   
2312 O  O   . HOH G .   ? 0.3315 0.1788 0.3565 -0.0192 0.0487  -0.0578 516 HOH A O   
2313 O  O   . HOH G .   ? 0.3182 0.1890 0.3181 -0.0230 -0.1329 0.0107  517 HOH A O   
2314 O  O   . HOH G .   ? 0.3501 0.2122 0.4969 -0.0514 0.1529  -0.0939 518 HOH A O   
2315 O  O   . HOH G .   ? 0.2970 0.2874 0.3014 0.0315  0.0129  -0.0477 519 HOH A O   
2316 O  O   . HOH G .   ? 0.3677 0.2061 0.3309 -0.0155 -0.0611 0.0811  520 HOH A O   
2317 O  O   . HOH G .   ? 0.3450 0.7862 0.3878 0.0401  -0.0198 0.0775  521 HOH A O   
2318 O  O   . HOH G .   ? 0.4411 0.4384 0.2181 0.0412  -0.1115 0.0495  522 HOH A O   
2319 O  O   . HOH G .   ? 0.6241 0.4281 0.8272 0.1419  -0.0675 0.1564  523 HOH A O   
2320 O  O   . HOH G .   ? 0.2451 0.1454 0.1910 0.0400  0.0011  0.0137  524 HOH A O   
2321 O  O   . HOH G .   ? 0.4493 0.2768 0.5024 -0.1092 -0.1419 0.1453  525 HOH A O   
2322 O  O   . HOH G .   ? 0.3953 0.1905 0.3308 0.1093  -0.0557 -0.0458 526 HOH A O   
2323 O  O   . HOH G .   ? 0.3362 0.3718 0.3473 -0.1167 0.0030  -0.1120 527 HOH A O   
2324 O  O   . HOH G .   ? 0.5143 0.4894 0.4255 0.1492  0.0181  0.0436  528 HOH A O   
2325 O  O   . HOH G .   ? 0.6286 0.3177 0.3703 -0.2150 -0.2231 0.0153  529 HOH A O   
2326 O  O   . HOH G .   ? 0.3942 0.4275 0.5570 0.0662  0.0314  -0.1291 530 HOH A O   
2327 O  O   . HOH G .   ? 0.1874 0.5134 0.3029 0.0445  0.0333  0.1927  531 HOH A O   
2328 O  O   . HOH G .   ? 0.2869 0.2390 0.3036 0.0001  -0.0550 0.0440  532 HOH A O   
2329 O  O   . HOH G .   ? 0.2425 0.1561 0.3740 -0.0187 0.0582  -0.0152 533 HOH A O   
2330 O  O   . HOH G .   ? 0.2541 0.4116 0.7024 -0.1282 0.0576  -0.0254 534 HOH A O   
2331 O  O   . HOH G .   ? 0.3227 0.2951 0.7181 0.0490  0.1354  0.1931  535 HOH A O   
2332 O  O   . HOH G .   ? 0.2450 0.1673 0.2492 -0.0709 0.0162  -0.0447 536 HOH A O   
2333 O  O   . HOH G .   ? 0.2562 0.1869 0.2395 0.0077  -0.0036 -0.0588 537 HOH A O   
2334 O  O   . HOH G .   ? 0.2958 0.2423 0.3053 0.0174  -0.0806 -0.0092 538 HOH A O   
2335 O  O   . HOH G .   ? 0.3190 0.3781 0.5175 0.0793  -0.1165 0.0637  539 HOH A O   
2336 O  O   . HOH G .   ? 0.2325 0.3793 0.4566 -0.0179 -0.0276 0.0149  540 HOH A O   
2337 O  O   . HOH G .   ? 0.4411 0.2675 0.6664 0.0149  0.2222  0.0284  541 HOH A O   
2338 O  O   . HOH G .   ? 0.4730 0.4189 0.2481 -0.1254 -0.0150 -0.0302 542 HOH A O   
2339 O  O   . HOH G .   ? 0.2711 0.2454 0.2172 0.0008  0.0189  -0.0096 543 HOH A O   
2340 O  O   . HOH G .   ? 0.2794 0.2027 0.5898 -0.0082 0.0157  -0.0067 544 HOH A O   
2341 O  O   . HOH G .   ? 0.2445 0.1805 0.2723 -0.0414 -0.0759 0.0376  545 HOH A O   
2342 O  O   . HOH G .   ? 0.5445 0.3328 0.2565 -0.1531 0.0605  -0.0968 546 HOH A O   
2343 O  O   . HOH G .   ? 0.2916 0.3059 0.2786 -0.0688 0.0591  0.0664  547 HOH A O   
2344 O  O   . HOH G .   ? 0.2937 0.3193 0.2927 0.0228  -0.1370 -0.0117 548 HOH A O   
2345 O  O   . HOH G .   ? 0.4842 0.2276 0.2711 0.0166  0.0080  -0.0084 549 HOH A O   
2346 O  O   . HOH G .   ? 0.1611 0.1403 0.1772 0.0316  -0.0096 0.0284  550 HOH A O   
2347 O  O   . HOH G .   ? 0.3263 0.2543 0.2687 0.0217  0.0544  0.1264  551 HOH A O   
2348 O  O   . HOH G .   ? 0.4510 0.3967 0.4461 -0.0440 -0.0471 0.2552  552 HOH A O   
2349 O  O   . HOH G .   ? 0.4030 0.4011 0.6710 0.1073  0.0127  0.0480  553 HOH A O   
2350 O  O   . HOH G .   ? 0.1822 0.3322 0.5759 0.0337  -0.0312 0.1187  554 HOH A O   
2351 O  O   . HOH G .   ? 0.2828 0.3134 0.6391 -0.1199 0.1621  -0.1112 555 HOH A O   
2352 O  O   . HOH G .   ? 0.1802 0.1745 0.2678 -0.0326 -0.0306 0.0337  556 HOH A O   
2353 O  O   . HOH G .   ? 0.6210 0.2722 0.3366 0.0333  -0.0466 0.0139  557 HOH A O   
2354 O  O   . HOH G .   ? 0.2438 0.2547 0.4950 -0.0883 -0.1120 -0.0620 558 HOH A O   
2355 O  O   . HOH G .   ? 0.1170 0.2228 0.2655 0.0152  0.0059  -0.0432 559 HOH A O   
2356 O  O   . HOH G .   ? 0.4800 0.2916 0.3569 0.0283  -0.0233 -0.0433 560 HOH A O   
2357 O  O   . HOH G .   ? 0.5326 0.2925 0.2841 -0.1085 0.2054  -0.1024 561 HOH A O   
2358 O  O   . HOH G .   ? 0.2100 0.4353 0.3970 0.0261  0.0001  -0.1211 562 HOH A O   
2359 O  O   . HOH G .   ? 0.2096 0.3668 0.4481 -0.0251 -0.0122 0.0155  563 HOH A O   
2360 O  O   . HOH G .   ? 0.4733 0.5879 0.4830 0.0570  -0.0095 0.1227  564 HOH A O   
2361 O  O   . HOH G .   ? 0.4710 0.4198 0.5723 0.0687  -0.2005 0.0916  565 HOH A O   
2362 O  O   . HOH G .   ? 0.2420 0.2688 0.3083 0.0378  0.0274  0.0251  566 HOH A O   
2363 O  O   . HOH G .   ? 0.2909 0.6945 0.8446 -0.0102 0.0934  -0.1049 567 HOH A O   
2364 O  O   . HOH G .   ? 0.5381 0.2874 0.2096 0.1577  -0.0010 0.0407  568 HOH A O   
2365 O  O   . HOH G .   ? 0.2181 0.3625 0.4386 0.1127  0.0901  0.0653  569 HOH A O   
2366 O  O   . HOH G .   ? 0.3955 0.3753 0.1781 0.0776  -0.0154 0.0149  570 HOH A O   
2367 O  O   . HOH G .   ? 0.2908 0.1938 0.2667 0.0687  -0.0203 0.0278  571 HOH A O   
2368 O  O   . HOH G .   ? 0.6556 0.3313 0.3596 -0.0050 -0.1138 -0.0592 572 HOH A O   
2369 O  O   . HOH G .   ? 0.5690 0.3941 0.4613 0.0858  0.0320  0.0987  573 HOH A O   
2370 O  O   . HOH G .   ? 0.3045 0.3270 0.2208 0.0577  -0.0072 0.1110  574 HOH A O   
2371 O  O   . HOH G .   ? 0.4059 0.4253 0.5389 -0.0653 -0.0512 -0.0958 575 HOH A O   
2372 O  O   . HOH G .   ? 0.2490 0.2481 0.3405 0.0948  -0.0223 -0.0423 576 HOH A O   
2373 O  O   . HOH G .   ? 0.5675 0.1745 0.4631 -0.0161 -0.0498 -0.0388 577 HOH A O   
2374 O  O   . HOH G .   ? 0.1528 0.2420 0.1974 0.0095  -0.0498 0.0308  578 HOH A O   
2375 O  O   . HOH G .   ? 0.4282 0.2007 0.3266 0.0754  -0.0012 0.0525  579 HOH A O   
2376 O  O   . HOH G .   ? 0.5895 0.2685 0.1705 0.1320  -0.0170 -0.0057 580 HOH A O   
2377 O  O   . HOH G .   ? 0.3473 0.4743 0.3917 0.1708  0.0855  0.0018  581 HOH A O   
2378 O  O   . HOH G .   ? 0.4744 0.2655 0.7086 -0.0324 -0.2060 -0.0425 582 HOH A O   
2379 O  O   . HOH G .   ? 0.4577 0.3960 0.3222 -0.1014 0.0232  0.1374  583 HOH A O   
2380 O  O   . HOH G .   ? 0.2020 0.3386 0.3217 0.1049  -0.0556 -0.0282 584 HOH A O   
2381 O  O   . HOH G .   ? 0.3024 0.3023 0.4883 0.0479  0.0569  0.0616  585 HOH A O   
2382 O  O   . HOH G .   ? 0.7033 0.5401 0.2174 0.1277  0.1216  0.1112  586 HOH A O   
2383 O  O   . HOH G .   ? 0.6786 0.4243 0.2328 0.0963  -0.0754 0.0425  587 HOH A O   
2384 O  O   . HOH G .   ? 0.5040 0.2487 0.3586 0.0563  -0.0629 0.0046  588 HOH A O   
2385 O  O   . HOH G .   ? 0.1655 0.1162 0.1605 0.0079  0.0012  -0.0050 589 HOH A O   
2386 O  O   . HOH G .   ? 0.3713 0.7347 0.3886 -0.1682 -0.0903 0.0932  590 HOH A O   
2387 O  O   . HOH G .   ? 0.5992 0.3421 0.9082 0.0756  0.2386  0.1657  591 HOH A O   
2388 O  O   . HOH G .   ? 0.6287 0.2276 0.6380 -0.1381 0.0467  0.2084  592 HOH A O   
2389 O  O   . HOH G .   ? 0.4071 0.4675 0.4081 -0.0627 0.1705  -0.0697 593 HOH A O   
2390 O  O   . HOH G .   ? 0.3757 0.2201 0.2710 -0.0722 -0.1047 0.0025  594 HOH A O   
2391 O  O   . HOH G .   ? 0.4910 0.8154 0.2833 0.1289  0.0313  0.0623  595 HOH A O   
2392 O  O   . HOH G .   ? 0.3940 0.2549 0.5586 -0.0471 -0.0171 0.1297  596 HOH A O   
2393 O  O   . HOH G .   ? 0.2636 0.2420 0.6065 0.0210  -0.0330 0.0927  597 HOH A O   
2394 O  O   . HOH G .   ? 0.4519 0.3887 0.6584 -0.0973 -0.0155 0.0907  598 HOH A O   
2395 O  O   . HOH G .   ? 0.3699 0.2986 0.3274 0.0088  -0.1051 0.0190  599 HOH A O   
2396 O  O   . HOH G .   ? 0.4272 0.2756 0.4079 -0.0675 0.0705  -0.0315 600 HOH A O   
2397 O  O   . HOH G .   ? 0.4653 0.5912 0.6089 0.2329  0.0703  0.0653  601 HOH A O   
2398 O  O   . HOH G .   ? 0.4109 0.1129 0.2931 0.0233  -0.0003 0.0085  602 HOH A O   
2399 O  O   . HOH G .   ? 0.3758 0.5990 0.8426 0.0089  0.0530  0.1645  603 HOH A O   
2400 O  O   . HOH G .   ? 0.3156 0.5025 0.8658 0.1142  -0.1395 -0.2767 604 HOH A O   
2401 O  O   . HOH G .   ? 0.1508 0.2082 0.4014 -0.0095 -0.0170 0.0149  605 HOH A O   
2402 O  O   . HOH G .   ? 0.4673 0.5942 0.2951 -0.3017 0.0674  -0.0547 606 HOH A O   
2403 O  O   . HOH G .   ? 0.7536 0.4910 0.4291 0.0702  -0.1462 0.0215  607 HOH A O   
2404 O  O   . HOH G .   ? 0.6976 0.5464 0.3225 0.3106  -0.1529 -0.0412 608 HOH A O   
2405 O  O   . HOH G .   ? 0.2597 0.2164 0.7990 0.0410  0.1314  -0.0656 609 HOH A O   
2406 O  O   . HOH G .   ? 0.6759 0.4816 0.5070 0.1275  0.1254  -0.1543 610 HOH A O   
2407 O  O   . HOH G .   ? 0.4506 0.3281 0.4644 -0.0408 0.2150  -0.0644 611 HOH A O   
2408 O  O   . HOH G .   ? 0.3785 0.2315 0.3577 0.0798  0.1156  0.0616  612 HOH A O   
2409 O  O   . HOH G .   ? 0.4484 0.5558 0.6814 -0.1176 0.0506  -0.3134 613 HOH A O   
2410 O  O   . HOH G .   ? 0.4553 0.2796 0.3265 -0.0554 -0.0239 0.0245  614 HOH A O   
2411 O  O   . HOH G .   ? 0.5126 0.4837 0.8427 -0.0869 0.1141  0.0218  615 HOH A O   
2412 O  O   . HOH G .   ? 0.6493 0.6107 0.2951 0.0500  -0.0785 0.1996  616 HOH A O   
2413 O  O   . HOH G .   ? 0.6445 0.4358 0.3247 0.2220  -0.1808 -0.0829 617 HOH A O   
2414 O  O   . HOH G .   ? 0.4220 0.3009 0.4305 0.0823  0.1043  0.1026  618 HOH A O   
2415 O  O   . HOH G .   ? 0.4017 1.0524 0.5517 0.0200  0.0649  0.2220  619 HOH A O   
2416 O  O   . HOH G .   ? 0.3591 0.4639 0.2376 -0.0618 -0.0039 0.0166  620 HOH A O   
2417 O  O   . HOH G .   ? 0.4667 0.2958 0.7530 0.0871  0.1824  0.1362  621 HOH A O   
2418 O  O   . HOH G .   ? 0.3887 0.6579 0.3206 0.1417  0.0490  0.2802  622 HOH A O   
2419 O  O   . HOH G .   ? 0.5583 0.7245 0.5381 0.0809  -0.0507 0.0687  623 HOH A O   
2420 O  O   . HOH G .   ? 0.4104 0.7849 0.6424 -0.1517 -0.0245 0.3161  624 HOH A O   
2421 O  O   . HOH G .   ? 0.5673 0.3474 0.5806 -0.1110 -0.0314 0.0184  625 HOH A O   
2422 O  O   . HOH G .   ? 0.4579 0.4601 1.0984 -0.1141 -0.2254 0.0068  626 HOH A O   
2423 O  O   . HOH G .   ? 0.3134 0.5825 0.4188 -0.0783 0.0017  0.2002  627 HOH A O   
2424 O  O   . HOH G .   ? 0.5115 0.8221 0.4156 0.0001  -0.0587 0.0161  628 HOH A O   
2425 O  O   . HOH G .   ? 0.6788 0.3610 0.3442 -0.0406 0.0533  0.1002  629 HOH A O   
2426 O  O   . HOH G .   ? 0.3641 0.3772 1.0970 -0.0075 0.0049  0.1819  630 HOH A O   
2427 O  O   . HOH G .   ? 0.5210 0.6764 0.5398 -0.0563 0.0125  -0.1098 631 HOH A O   
2428 O  O   . HOH G .   ? 0.4221 0.4822 0.5781 0.0766  0.0208  0.0216  632 HOH A O   
2429 O  O   . HOH G .   ? 0.4288 0.4525 0.4397 0.0442  0.0494  0.1367  633 HOH A O   
2430 O  O   . HOH G .   ? 0.2825 0.4003 0.4160 0.0043  0.0130  0.1351  634 HOH A O   
2431 O  O   . HOH G .   ? 0.5145 0.6587 0.4170 -0.0578 -0.0534 -0.1011 635 HOH A O   
2432 O  O   . HOH G .   ? 0.4398 0.3987 0.6705 0.1102  -0.0989 -0.1615 636 HOH A O   
2433 O  O   . HOH G .   ? 0.3065 0.4767 0.3659 0.0814  -0.0536 -0.1170 637 HOH A O   
2434 O  O   . HOH G .   ? 0.5255 0.3833 0.6743 0.0477  0.1228  0.2714  638 HOH A O   
2435 O  O   . HOH G .   ? 0.7896 0.7407 0.3771 0.1489  0.4066  0.1534  639 HOH A O   
2436 O  O   . HOH G .   ? 0.8680 0.4789 0.3689 -0.0903 0.0649  0.1969  640 HOH A O   
2437 O  O   . HOH G .   ? 0.2438 0.1636 0.2972 -0.0174 -0.0485 0.0023  641 HOH A O   
2438 O  O   . HOH G .   ? 0.2398 0.5571 0.8198 -0.0422 0.1892  -0.2375 642 HOH A O   
2439 O  O   . HOH G .   ? 0.4084 0.9171 0.5713 -0.0145 -0.0844 0.1504  643 HOH A O   
2440 O  O   . HOH G .   ? 0.5536 0.5207 0.5323 -0.0100 -0.0067 0.0745  644 HOH A O   
2441 O  O   . HOH G .   ? 0.5406 0.2549 0.5486 -0.1065 0.1456  0.0198  645 HOH A O   
2442 O  O   . HOH G .   ? 0.4826 1.0092 0.2978 0.1144  -0.0666 -0.0491 646 HOH A O   
2443 O  O   . HOH G .   ? 0.4557 0.3901 0.8262 -0.0037 -0.1222 -0.1162 647 HOH A O   
2444 O  O   . HOH G .   ? 0.3653 0.7253 0.3453 0.1389  -0.0300 -0.0190 648 HOH A O   
2445 O  O   . HOH G .   ? 0.8970 0.3124 0.6249 0.1833  0.0167  -0.0156 649 HOH A O   
2446 O  O   . HOH G .   ? 0.4152 0.8541 0.5954 0.3856  0.0825  0.1367  650 HOH A O   
2447 O  O   . HOH G .   ? 0.5791 0.2966 0.4228 -0.0267 0.1374  0.0362  651 HOH A O   
2448 O  O   . HOH G .   ? 0.4286 0.3064 0.8381 -0.0146 -0.1004 0.1092  652 HOH A O   
2449 O  O   . HOH G .   ? 0.3999 0.3077 0.3278 -0.0068 -0.0510 -0.0179 653 HOH A O   
2450 O  O   . HOH G .   ? 0.6689 0.3539 0.8582 0.0308  0.4092  -0.0515 654 HOH A O   
2451 O  O   . HOH G .   ? 0.4533 0.4881 0.5534 -0.0839 0.2144  -0.0855 655 HOH A O   
2452 O  O   . HOH G .   ? 0.7126 0.2900 0.3353 0.1154  0.1385  0.0647  656 HOH A O   
2453 O  O   . HOH G .   ? 0.3393 0.3031 0.3702 0.1176  -0.1655 -0.0290 657 HOH A O   
2454 O  O   . HOH G .   ? 0.5057 0.3461 0.3495 0.1996  -0.1291 -0.0394 658 HOH A O   
2455 O  O   . HOH G .   ? 0.3134 0.8304 0.4099 0.0326  0.0005  0.0869  659 HOH A O   
2456 O  O   . HOH G .   ? 0.3644 0.3723 0.3784 -0.1022 -0.0585 -0.1188 660 HOH A O   
2457 O  O   . HOH G .   ? 0.3027 0.3937 0.4008 0.0088  0.0724  0.0195  661 HOH A O   
2458 O  O   . HOH G .   ? 0.5353 0.5359 0.3104 -0.1024 0.0013  0.0904  662 HOH A O   
2459 O  O   . HOH G .   ? 0.6697 0.6544 0.3194 0.2008  0.1386  -0.0577 663 HOH A O   
2460 O  O   . HOH G .   ? 0.3127 0.4042 0.4512 -0.0302 0.0190  -0.1100 664 HOH A O   
2461 O  O   . HOH G .   ? 0.3501 0.3150 0.6110 -0.0212 0.0959  0.0922  665 HOH A O   
2462 O  O   . HOH G .   ? 0.3421 0.6462 0.3272 0.0212  -0.0387 0.0850  666 HOH A O   
2463 O  O   . HOH G .   ? 0.6325 0.4256 0.3460 0.1186  -0.0222 0.0337  667 HOH A O   
2464 O  O   . HOH G .   ? 0.6667 0.4649 0.3836 0.0602  -0.0640 0.0306  668 HOH A O   
2465 O  O   . HOH G .   ? 0.8658 0.7506 0.5168 0.0046  0.1829  -0.3509 669 HOH A O   
2466 O  O   . HOH G .   ? 0.3643 0.4096 0.4625 0.1215  0.0528  -0.0075 670 HOH A O   
2467 O  O   . HOH G .   ? 0.6184 0.4027 0.3963 0.0836  -0.0912 -0.0012 671 HOH A O   
2468 O  O   . HOH G .   ? 0.4798 0.4179 0.3488 -0.0939 -0.1515 0.0559  672 HOH A O   
2469 O  O   . HOH G .   ? 0.2567 0.1535 0.2512 -0.0055 0.0161  0.0320  673 HOH A O   
2470 O  O   . HOH G .   ? 0.3346 0.2593 0.3822 -0.0027 0.0128  0.0422  674 HOH A O   
2471 O  O   . HOH G .   ? 0.4656 0.4856 0.3626 0.0342  -0.0113 -0.0540 675 HOH A O   
2472 O  O   . HOH G .   ? 0.3501 0.6165 0.4874 -0.0212 -0.0908 -0.0932 676 HOH A O   
2473 O  O   . HOH G .   ? 0.4512 0.2949 0.4154 0.0027  0.0785  -0.0659 677 HOH A O   
2474 O  O   . HOH G .   ? 0.4093 0.3197 0.2945 0.0731  0.0816  -0.0195 678 HOH A O   
2475 O  O   . HOH G .   ? 0.4589 0.3059 0.6977 -0.0348 -0.2046 0.1351  679 HOH A O   
2476 O  O   . HOH G .   ? 0.4471 0.4483 0.4121 -0.1498 0.0392  -0.0395 680 HOH A O   
2477 O  O   . HOH G .   ? 0.5873 0.3492 0.8461 -0.0155 -0.0308 -0.1671 681 HOH A O   
2478 O  O   . HOH G .   ? 0.2690 0.2063 0.2323 0.0552  -0.0547 0.0126  682 HOH A O   
2479 O  O   . HOH G .   ? 0.4136 0.2379 0.5402 -0.0342 0.1088  -0.0370 683 HOH A O   
2480 O  O   . HOH G .   ? 0.5036 0.3030 0.3029 -0.0405 0.1300  -0.1386 684 HOH A O   
2481 O  O   . HOH G .   ? 0.4960 0.4561 0.7011 0.1042  -0.1014 -0.2850 685 HOH A O   
2482 O  O   . HOH G .   ? 0.2499 0.4958 0.9967 -0.0674 0.1132  0.1574  686 HOH A O   
2483 O  O   . HOH G .   ? 0.4218 0.1826 0.5321 -0.0159 0.1599  -0.0003 687 HOH A O   
2484 O  O   . HOH G .   ? 0.4043 0.2940 0.3926 0.0581  -0.0077 0.0628  688 HOH A O   
2485 O  O   . HOH G .   ? 0.3152 0.2791 0.3407 0.0290  -0.0248 0.0431  689 HOH A O   
2486 O  O   . HOH G .   ? 0.4381 0.3036 0.6315 -0.1272 0.0095  0.1287  690 HOH A O   
2487 O  O   . HOH G .   ? 0.7491 0.4975 0.4042 -0.1032 0.1260  -0.1439 691 HOH A O   
2488 O  O   . HOH G .   ? 0.9175 0.3256 0.4785 0.1237  0.1564  -0.0765 692 HOH A O   
2489 O  O   . HOH G .   ? 0.5227 0.6436 0.8848 0.1310  -0.0452 -0.0013 693 HOH A O   
2490 O  O   . HOH G .   ? 0.7702 0.4965 0.4013 0.1778  -0.0900 -0.1817 694 HOH A O   
2491 O  O   . HOH G .   ? 0.6036 0.2872 0.5052 0.0489  0.2020  0.0800  695 HOH A O   
2492 O  O   . HOH G .   ? 0.3351 0.6735 0.6677 -0.1289 -0.1018 0.0397  696 HOH A O   
2493 O  O   . HOH G .   ? 0.3819 0.4603 0.5983 0.0924  0.0952  0.2651  697 HOH A O   
2494 O  O   . HOH G .   ? 0.3282 0.3960 0.3145 0.0033  -0.0427 0.0688  698 HOH A O   
2495 O  O   . HOH G .   ? 0.1781 0.4202 0.6830 -0.0763 -0.0469 0.1069  699 HOH A O   
2496 O  O   . HOH G .   ? 0.3083 0.3515 0.4753 -0.0132 0.0632  -0.0021 700 HOH A O   
# 
