data_7NZT
# 
_entry.id   7NZT 
# 
_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   7NZT         pdb_00007nzt 10.2210/pdb7nzt/pdb 
WWPDB D_1292114753 ?            ?                   
# 
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                        7NZT 
_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 
# 
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 'DIMETHYL SULFOXIDE'                                                                 78.133    2   ?       ? ? ? 
4 non-polymer syn '3-(cyclooctylamino)-2,5,6-trifluoro-4-[(2-hydroxyethyl)sulfonyl]benzenesulfonamide' 444.489   1   ?       ? ? ? 
5 water       nat water                                                                                18.015    295 ?       ? ? ? 
# 
_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 'DIMETHYL SULFOXIDE'                                                                 DMS 
4 '3-(cyclooctylamino)-2,5,6-trifluoro-4-[(2-hydroxyethyl)sulfonyl]benzenesulfonamide' V14 
5 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 
CYS 'L-peptide linking' y CYSTEINE                                                                             ? 'C3 H7 N O2 S' 
121.158 
DMS non-polymer         . 'DIMETHYL SULFOXIDE'                                                                 ? 'C2 H6 O S' 
78.133  
GLN 'L-peptide linking' y GLUTAMINE                                                                            ? 'C5 H10 N2 O3' 
146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                                                                      ? 'C5 H9 N O4' 
147.129 
GLY 'peptide linking'   y GLYCINE                                                                              ? 'C2 H5 N O2' 
75.067  
HIS 'L-peptide linking' y HISTIDINE                                                                            ? 'C6 H10 N3 O2 1' 
156.162 
HOH non-polymer         . WATER                                                                                ? 'H2 O' 18.015  
ILE 'L-peptide linking' y ISOLEUCINE                                                                           ? 'C6 H13 N O2' 
131.173 
LEU 'L-peptide linking' y LEUCINE                                                                              ? 'C6 H13 N O2' 
131.173 
LYS 'L-peptide linking' y LYSINE                                                                               ? 'C6 H15 N2 O2 1' 
147.195 
MET 'L-peptide linking' y METHIONINE                                                                           ? 'C5 H11 N O2 S' 
149.211 
PHE 'L-peptide linking' y PHENYLALANINE                                                                        ? 'C9 H11 N O2' 
165.189 
PRO 'L-peptide linking' y PROLINE                                                                              ? 'C5 H9 N O2' 
115.130 
SER 'L-peptide linking' y SERINE                                                                               ? 'C3 H7 N O3' 
105.093 
THR 'L-peptide linking' y THREONINE                                                                            ? 'C4 H9 N O3' 
119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                                                           ? 'C11 H12 N2 O2' 
204.225 
TYR 'L-peptide linking' y TYROSINE                                                                             ? 'C9 H11 N O3' 
181.189 
V14 non-polymer         . '3-(cyclooctylamino)-2,5,6-trifluoro-4-[(2-hydroxyethyl)sulfonyl]benzenesulfonamide' ? 
'C16 H23 F3 N2 O5 S2' 444.489 
VAL 'L-peptide linking' y VALINE                                                                               ? 'C5 H11 N O2' 
117.146 
ZN  non-polymer         . 'ZINC ION'                                                                           ? 'Zn 2' 65.409  
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   SER 2   2   ?   ?   ?   A . n 
A 1 3   HIS 3   3   ?   ?   ?   A . n 
A 1 4   HIS 4   4   4   HIS HIS A . n 
A 1 5   TRP 5   5   5   TRP TRP A . n 
A 1 6   GLY 6   6   6   GLY GLY A . n 
A 1 7   TYR 7   7   7   TYR TYR A . n 
A 1 8   GLY 8   8   8   GLY GLY A . n 
A 1 9   LYS 9   9   9   LYS LYS A . n 
A 1 10  HIS 10  10  10  HIS HIS A . n 
A 1 11  ASN 11  11  11  ASN ASN A . n 
A 1 12  GLY 12  12  12  GLY GLY A . n 
A 1 13  PRO 13  13  13  PRO PRO A . n 
A 1 14  GLU 14  14  14  GLU GLU A . n 
A 1 15  HIS 15  15  15  HIS HIS A . n 
A 1 16  TRP 16  16  16  TRP TRP A . n 
A 1 17  HIS 17  17  17  HIS HIS A . n 
A 1 18  LYS 18  18  18  LYS LYS A . n 
A 1 19  ASP 19  19  19  ASP ASP A . n 
A 1 20  PHE 20  20  20  PHE PHE A . n 
A 1 21  PRO 21  21  21  PRO PRO A . n 
A 1 22  ILE 22  22  22  ILE ILE A . n 
A 1 23  ALA 23  23  23  ALA ALA A . n 
A 1 24  LYS 24  24  24  LYS LYS A . n 
A 1 25  GLY 25  25  25  GLY GLY A . n 
A 1 26  GLU 26  26  26  GLU GLU A . n 
A 1 27  ARG 27  27  27  ARG ARG A . n 
A 1 28  GLN 28  28  28  GLN GLN A . n 
A 1 29  SER 29  29  29  SER SER A . n 
A 1 30  PRO 30  30  30  PRO PRO A . n 
A 1 31  VAL 31  31  31  VAL VAL A . n 
A 1 32  ASP 32  32  32  ASP ASP A . n 
A 1 33  ILE 33  33  33  ILE ILE A . n 
A 1 34  ASP 34  34  34  ASP ASP A . n 
A 1 35  THR 35  35  35  THR THR A . n 
A 1 36  HIS 36  36  36  HIS HIS A . n 
A 1 37  THR 37  37  37  THR THR A . n 
A 1 38  ALA 38  38  38  ALA ALA A . n 
A 1 39  LYS 39  39  39  LYS LYS A . n 
A 1 40  TYR 40  40  40  TYR TYR A . n 
A 1 41  ASP 41  41  41  ASP ASP A . n 
A 1 42  PRO 42  42  42  PRO PRO A . n 
A 1 43  SER 43  43  43  SER SER A . n 
A 1 44  LEU 44  44  44  LEU LEU A . n 
A 1 45  LYS 45  45  45  LYS LYS A . n 
A 1 46  PRO 46  46  46  PRO PRO A . n 
A 1 47  LEU 47  47  47  LEU LEU A . n 
A 1 48  SER 48  48  48  SER SER A . n 
A 1 49  VAL 49  49  49  VAL VAL A . n 
A 1 50  SER 50  50  50  SER SER A . n 
A 1 51  TYR 51  51  51  TYR TYR A . n 
A 1 52  ASP 52  52  52  ASP ASP A . n 
A 1 53  GLN 53  53  53  GLN GLN A . n 
A 1 54  ALA 54  54  54  ALA ALA A . n 
A 1 55  THR 55  55  55  THR THR A . n 
A 1 56  SER 56  56  56  SER SER A . n 
A 1 57  LEU 57  57  57  LEU LEU A . n 
A 1 58  ARG 58  58  58  ARG ARG A . n 
A 1 59  ILE 59  59  59  ILE ILE A . n 
A 1 60  LEU 60  60  60  LEU LEU A . n 
A 1 61  ASN 61  61  61  ASN ASN A . n 
A 1 62  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 DMS 1   302 1   DMS DMS A . 
D 3 DMS 1   303 2   DMS DMS A . 
E 4 V14 1   304 1   V14 V14 A . 
F 5 HOH 1   401 59  HOH HOH A . 
F 5 HOH 2   402 221 HOH HOH A . 
F 5 HOH 3   403 190 HOH HOH A . 
F 5 HOH 4   404 270 HOH HOH A . 
F 5 HOH 5   405 286 HOH HOH A . 
F 5 HOH 6   406 268 HOH HOH A . 
F 5 HOH 7   407 148 HOH HOH A . 
F 5 HOH 8   408 261 HOH HOH A . 
F 5 HOH 9   409 259 HOH HOH A . 
F 5 HOH 10  410 129 HOH HOH A . 
F 5 HOH 11  411 108 HOH HOH A . 
F 5 HOH 12  412 99  HOH HOH A . 
F 5 HOH 13  413 35  HOH HOH A . 
F 5 HOH 14  414 122 HOH HOH A . 
F 5 HOH 15  415 234 HOH HOH A . 
F 5 HOH 16  416 257 HOH HOH A . 
F 5 HOH 17  417 55  HOH HOH A . 
F 5 HOH 18  418 126 HOH HOH A . 
F 5 HOH 19  419 102 HOH HOH A . 
F 5 HOH 20  420 272 HOH HOH A . 
F 5 HOH 21  421 69  HOH HOH A . 
F 5 HOH 22  422 171 HOH HOH A . 
F 5 HOH 23  423 165 HOH HOH A . 
F 5 HOH 24  424 170 HOH HOH A . 
F 5 HOH 25  425 120 HOH HOH A . 
F 5 HOH 26  426 109 HOH HOH A . 
F 5 HOH 27  427 100 HOH HOH A . 
F 5 HOH 28  428 32  HOH HOH A . 
F 5 HOH 29  429 134 HOH HOH A . 
F 5 HOH 30  430 182 HOH HOH A . 
F 5 HOH 31  431 64  HOH HOH A . 
F 5 HOH 32  432 19  HOH HOH A . 
F 5 HOH 33  433 90  HOH HOH A . 
F 5 HOH 34  434 111 HOH HOH A . 
F 5 HOH 35  435 3   HOH HOH A . 
F 5 HOH 36  436 200 HOH HOH A . 
F 5 HOH 37  437 163 HOH HOH A . 
F 5 HOH 38  438 139 HOH HOH A . 
F 5 HOH 39  439 144 HOH HOH A . 
F 5 HOH 40  440 2   HOH HOH A . 
F 5 HOH 41  441 140 HOH HOH A . 
F 5 HOH 42  442 164 HOH HOH A . 
F 5 HOH 43  443 197 HOH HOH A . 
F 5 HOH 44  444 112 HOH HOH A . 
F 5 HOH 45  445 128 HOH HOH A . 
F 5 HOH 46  446 31  HOH HOH A . 
F 5 HOH 47  447 260 HOH HOH A . 
F 5 HOH 48  448 89  HOH HOH A . 
F 5 HOH 49  449 294 HOH HOH A . 
F 5 HOH 50  450 193 HOH HOH A . 
F 5 HOH 51  451 87  HOH HOH A . 
F 5 HOH 52  452 30  HOH HOH A . 
F 5 HOH 53  453 169 HOH HOH A . 
F 5 HOH 54  454 52  HOH HOH A . 
F 5 HOH 55  455 15  HOH HOH A . 
F 5 HOH 56  456 149 HOH HOH A . 
F 5 HOH 57  457 79  HOH HOH A . 
F 5 HOH 58  458 39  HOH HOH A . 
F 5 HOH 59  459 110 HOH HOH A . 
F 5 HOH 60  460 256 HOH HOH A . 
F 5 HOH 61  461 84  HOH HOH A . 
F 5 HOH 62  462 60  HOH HOH A . 
F 5 HOH 63  463 38  HOH HOH A . 
F 5 HOH 64  464 20  HOH HOH A . 
F 5 HOH 65  465 83  HOH HOH A . 
F 5 HOH 66  466 104 HOH HOH A . 
F 5 HOH 67  467 246 HOH HOH A . 
F 5 HOH 68  468 156 HOH HOH A . 
F 5 HOH 69  469 180 HOH HOH A . 
F 5 HOH 70  470 189 HOH HOH A . 
F 5 HOH 71  471 57  HOH HOH A . 
F 5 HOH 72  472 241 HOH HOH A . 
F 5 HOH 73  473 119 HOH HOH A . 
F 5 HOH 74  474 17  HOH HOH A . 
F 5 HOH 75  475 131 HOH HOH A . 
F 5 HOH 76  476 231 HOH HOH A . 
F 5 HOH 77  477 33  HOH HOH A . 
F 5 HOH 78  478 158 HOH HOH A . 
F 5 HOH 79  479 81  HOH HOH A . 
F 5 HOH 80  480 143 HOH HOH A . 
F 5 HOH 81  481 162 HOH HOH A . 
F 5 HOH 82  482 288 HOH HOH A . 
F 5 HOH 83  483 141 HOH HOH A . 
F 5 HOH 84  484 7   HOH HOH A . 
F 5 HOH 85  485 1   HOH HOH A . 
F 5 HOH 86  486 10  HOH HOH A . 
F 5 HOH 87  487 29  HOH HOH A . 
F 5 HOH 88  488 66  HOH HOH A . 
F 5 HOH 89  489 105 HOH HOH A . 
F 5 HOH 90  490 168 HOH HOH A . 
F 5 HOH 91  491 145 HOH HOH A . 
F 5 HOH 92  492 226 HOH HOH A . 
F 5 HOH 93  493 11  HOH HOH A . 
F 5 HOH 94  494 45  HOH HOH A . 
F 5 HOH 95  495 248 HOH HOH A . 
F 5 HOH 96  496 223 HOH HOH A . 
F 5 HOH 97  497 138 HOH HOH A . 
F 5 HOH 98  498 36  HOH HOH A . 
F 5 HOH 99  499 12  HOH HOH A . 
F 5 HOH 100 500 68  HOH HOH A . 
F 5 HOH 101 501 58  HOH HOH A . 
F 5 HOH 102 502 65  HOH HOH A . 
F 5 HOH 103 503 63  HOH HOH A . 
F 5 HOH 104 504 225 HOH HOH A . 
F 5 HOH 105 505 92  HOH HOH A . 
F 5 HOH 106 506 262 HOH HOH A . 
F 5 HOH 107 507 42  HOH HOH A . 
F 5 HOH 108 508 28  HOH HOH A . 
F 5 HOH 109 509 151 HOH HOH A . 
F 5 HOH 110 510 5   HOH HOH A . 
F 5 HOH 111 511 46  HOH HOH A . 
F 5 HOH 112 512 154 HOH HOH A . 
F 5 HOH 113 513 41  HOH HOH A . 
F 5 HOH 114 514 282 HOH HOH A . 
F 5 HOH 115 515 133 HOH HOH A . 
F 5 HOH 116 516 9   HOH HOH A . 
F 5 HOH 117 517 88  HOH HOH A . 
F 5 HOH 118 518 6   HOH HOH A . 
F 5 HOH 119 519 95  HOH HOH A . 
F 5 HOH 120 520 242 HOH HOH A . 
F 5 HOH 121 521 115 HOH HOH A . 
F 5 HOH 122 522 93  HOH HOH A . 
F 5 HOH 123 523 174 HOH HOH A . 
F 5 HOH 124 524 132 HOH HOH A . 
F 5 HOH 125 525 269 HOH HOH A . 
F 5 HOH 126 526 73  HOH HOH A . 
F 5 HOH 127 527 172 HOH HOH A . 
F 5 HOH 128 528 153 HOH HOH A . 
F 5 HOH 129 529 8   HOH HOH A . 
F 5 HOH 130 530 173 HOH HOH A . 
F 5 HOH 131 531 13  HOH HOH A . 
F 5 HOH 132 532 24  HOH HOH A . 
F 5 HOH 133 533 228 HOH HOH A . 
F 5 HOH 134 534 258 HOH HOH A . 
F 5 HOH 135 535 97  HOH HOH A . 
F 5 HOH 136 536 121 HOH HOH A . 
F 5 HOH 137 537 49  HOH HOH A . 
F 5 HOH 138 538 18  HOH HOH A . 
F 5 HOH 139 539 247 HOH HOH A . 
F 5 HOH 140 540 70  HOH HOH A . 
F 5 HOH 141 541 106 HOH HOH A . 
F 5 HOH 142 542 254 HOH HOH A . 
F 5 HOH 143 543 21  HOH HOH A . 
F 5 HOH 144 544 155 HOH HOH A . 
F 5 HOH 145 545 284 HOH HOH A . 
F 5 HOH 146 546 62  HOH HOH A . 
F 5 HOH 147 547 179 HOH HOH A . 
F 5 HOH 148 548 255 HOH HOH A . 
F 5 HOH 149 549 78  HOH HOH A . 
F 5 HOH 150 550 44  HOH HOH A . 
F 5 HOH 151 551 147 HOH HOH A . 
F 5 HOH 152 552 91  HOH HOH A . 
F 5 HOH 153 553 56  HOH HOH A . 
F 5 HOH 154 554 114 HOH HOH A . 
F 5 HOH 155 555 211 HOH HOH A . 
F 5 HOH 156 556 40  HOH HOH A . 
F 5 HOH 157 557 204 HOH HOH A . 
F 5 HOH 158 558 26  HOH HOH A . 
F 5 HOH 159 559 94  HOH HOH A . 
F 5 HOH 160 560 224 HOH HOH A . 
F 5 HOH 161 561 277 HOH HOH A . 
F 5 HOH 162 562 82  HOH HOH A . 
F 5 HOH 163 563 96  HOH HOH A . 
F 5 HOH 164 564 123 HOH HOH A . 
F 5 HOH 165 565 16  HOH HOH A . 
F 5 HOH 166 566 238 HOH HOH A . 
F 5 HOH 167 567 76  HOH HOH A . 
F 5 HOH 168 568 177 HOH HOH A . 
F 5 HOH 169 569 124 HOH HOH A . 
F 5 HOH 170 570 118 HOH HOH A . 
F 5 HOH 171 571 75  HOH HOH A . 
F 5 HOH 172 572 72  HOH HOH A . 
F 5 HOH 173 573 101 HOH HOH A . 
F 5 HOH 174 574 125 HOH HOH A . 
F 5 HOH 175 575 196 HOH HOH A . 
F 5 HOH 176 576 51  HOH HOH A . 
F 5 HOH 177 577 67  HOH HOH A . 
F 5 HOH 178 578 278 HOH HOH A . 
F 5 HOH 179 579 4   HOH HOH A . 
F 5 HOH 180 580 167 HOH HOH A . 
F 5 HOH 181 581 48  HOH HOH A . 
F 5 HOH 182 582 159 HOH HOH A . 
F 5 HOH 183 583 53  HOH HOH A . 
F 5 HOH 184 584 160 HOH HOH A . 
F 5 HOH 185 585 237 HOH HOH A . 
F 5 HOH 186 586 27  HOH HOH A . 
F 5 HOH 187 587 235 HOH HOH A . 
F 5 HOH 188 588 107 HOH HOH A . 
F 5 HOH 189 589 23  HOH HOH A . 
F 5 HOH 190 590 161 HOH HOH A . 
F 5 HOH 191 591 14  HOH HOH A . 
F 5 HOH 192 592 232 HOH HOH A . 
F 5 HOH 193 593 209 HOH HOH A . 
F 5 HOH 194 594 43  HOH HOH A . 
F 5 HOH 195 595 275 HOH HOH A . 
F 5 HOH 196 596 77  HOH HOH A . 
F 5 HOH 197 597 176 HOH HOH A . 
F 5 HOH 198 598 267 HOH HOH A . 
F 5 HOH 199 599 245 HOH HOH A . 
F 5 HOH 200 600 142 HOH HOH A . 
F 5 HOH 201 601 74  HOH HOH A . 
F 5 HOH 202 602 198 HOH HOH A . 
F 5 HOH 203 603 137 HOH HOH A . 
F 5 HOH 204 604 71  HOH HOH A . 
F 5 HOH 205 605 175 HOH HOH A . 
F 5 HOH 206 606 150 HOH HOH A . 
F 5 HOH 207 607 86  HOH HOH A . 
F 5 HOH 208 608 47  HOH HOH A . 
F 5 HOH 209 609 202 HOH HOH A . 
F 5 HOH 210 610 157 HOH HOH A . 
F 5 HOH 211 611 103 HOH HOH A . 
F 5 HOH 212 612 37  HOH HOH A . 
F 5 HOH 213 613 240 HOH HOH A . 
F 5 HOH 214 614 22  HOH HOH A . 
F 5 HOH 215 615 166 HOH HOH A . 
F 5 HOH 216 616 249 HOH HOH A . 
F 5 HOH 217 617 195 HOH HOH A . 
F 5 HOH 218 618 217 HOH HOH A . 
F 5 HOH 219 619 266 HOH HOH A . 
F 5 HOH 220 620 290 HOH HOH A . 
F 5 HOH 221 621 61  HOH HOH A . 
F 5 HOH 222 622 25  HOH HOH A . 
F 5 HOH 223 623 253 HOH HOH A . 
F 5 HOH 224 624 215 HOH HOH A . 
F 5 HOH 225 625 54  HOH HOH A . 
F 5 HOH 226 626 50  HOH HOH A . 
F 5 HOH 227 627 206 HOH HOH A . 
F 5 HOH 228 628 271 HOH HOH A . 
F 5 HOH 229 629 146 HOH HOH A . 
F 5 HOH 230 630 239 HOH HOH A . 
F 5 HOH 231 631 233 HOH HOH A . 
F 5 HOH 232 632 208 HOH HOH A . 
F 5 HOH 233 633 250 HOH HOH A . 
F 5 HOH 234 634 291 HOH HOH A . 
F 5 HOH 235 635 216 HOH HOH A . 
F 5 HOH 236 636 295 HOH HOH A . 
F 5 HOH 237 637 236 HOH HOH A . 
F 5 HOH 238 638 178 HOH HOH A . 
F 5 HOH 239 639 274 HOH HOH A . 
F 5 HOH 240 640 283 HOH HOH A . 
F 5 HOH 241 641 191 HOH HOH A . 
F 5 HOH 242 642 181 HOH HOH A . 
F 5 HOH 243 643 222 HOH HOH A . 
F 5 HOH 244 644 285 HOH HOH A . 
F 5 HOH 245 645 184 HOH HOH A . 
F 5 HOH 246 646 251 HOH HOH A . 
F 5 HOH 247 647 289 HOH HOH A . 
F 5 HOH 248 648 213 HOH HOH A . 
F 5 HOH 249 649 80  HOH HOH A . 
F 5 HOH 250 650 152 HOH HOH A . 
F 5 HOH 251 651 280 HOH HOH A . 
F 5 HOH 252 652 281 HOH HOH A . 
F 5 HOH 253 653 212 HOH HOH A . 
F 5 HOH 254 654 85  HOH HOH A . 
F 5 HOH 255 655 207 HOH HOH A . 
F 5 HOH 256 656 219 HOH HOH A . 
F 5 HOH 257 657 127 HOH HOH A . 
F 5 HOH 258 658 210 HOH HOH A . 
F 5 HOH 259 659 136 HOH HOH A . 
F 5 HOH 260 660 214 HOH HOH A . 
F 5 HOH 261 661 276 HOH HOH A . 
F 5 HOH 262 662 130 HOH HOH A . 
F 5 HOH 263 663 273 HOH HOH A . 
F 5 HOH 264 664 135 HOH HOH A . 
F 5 HOH 265 665 203 HOH HOH A . 
F 5 HOH 266 666 244 HOH HOH A . 
F 5 HOH 267 667 293 HOH HOH A . 
F 5 HOH 268 668 187 HOH HOH A . 
F 5 HOH 269 669 98  HOH HOH A . 
F 5 HOH 270 670 113 HOH HOH A . 
F 5 HOH 271 671 227 HOH HOH A . 
F 5 HOH 272 672 292 HOH HOH A . 
F 5 HOH 273 673 279 HOH HOH A . 
F 5 HOH 274 674 194 HOH HOH A . 
F 5 HOH 275 675 264 HOH HOH A . 
F 5 HOH 276 676 34  HOH HOH A . 
F 5 HOH 277 677 199 HOH HOH A . 
F 5 HOH 278 678 201 HOH HOH A . 
F 5 HOH 279 679 183 HOH HOH A . 
F 5 HOH 280 680 117 HOH HOH A . 
F 5 HOH 281 681 185 HOH HOH A . 
F 5 HOH 282 682 220 HOH HOH A . 
F 5 HOH 283 683 229 HOH HOH A . 
F 5 HOH 284 684 205 HOH HOH A . 
F 5 HOH 285 685 192 HOH HOH A . 
F 5 HOH 286 686 287 HOH HOH A . 
F 5 HOH 287 687 186 HOH HOH A . 
F 5 HOH 288 688 263 HOH HOH A . 
F 5 HOH 289 689 243 HOH HOH A . 
F 5 HOH 290 690 116 HOH HOH A . 
F 5 HOH 291 691 188 HOH HOH A . 
F 5 HOH 292 692 218 HOH HOH A . 
F 5 HOH 293 693 252 HOH HOH A . 
F 5 HOH 294 694 265 HOH HOH A . 
F 5 HOH 295 695 230 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 HIS 4   ? ND1 ? A HIS 4   ND1 
2  1 Y 1 A HIS 4   ? CD2 ? A HIS 4   CD2 
3  1 Y 1 A HIS 4   ? CE1 ? A HIS 4   CE1 
4  1 Y 1 A HIS 4   ? NE2 ? A HIS 4   NE2 
5  1 Y 1 A LYS 9   ? CG  ? A LYS 9   CG  
6  1 Y 1 A LYS 9   ? CD  ? A LYS 9   CD  
7  1 Y 1 A LYS 9   ? CE  ? A LYS 9   CE  
8  1 Y 1 A LYS 9   ? NZ  ? A LYS 9   NZ  
9  1 Y 1 A LYS 45  ? NZ  ? A LYS 45  NZ  
10 1 Y 1 A LYS 80  ? CE  ? A LYS 80  CE  
11 1 Y 1 A LYS 80  ? NZ  ? A LYS 80  NZ  
12 1 Y 1 A LYS 158 ? CD  ? A LYS 158 CD  
13 1 Y 1 A LYS 158 ? CE  ? A LYS 158 CE  
14 1 Y 1 A LYS 158 ? NZ  ? A LYS 158 NZ  
15 1 Y 1 A LYS 167 ? NZ  ? A LYS 167 NZ  
16 1 Y 1 A LYS 169 ? NZ  ? A LYS 169 NZ  
17 1 Y 1 A LYS 171 ? CE  ? A LYS 171 CE  
18 1 Y 1 A LYS 171 ? NZ  ? A LYS 171 NZ  
19 1 Y 1 A LYS 256 ? CD  ? A LYS 256 CD  
20 1 Y 1 A LYS 256 ? CE  ? A LYS 256 CE  
21 1 Y 1 A LYS 256 ? NZ  ? A LYS 256 NZ  
22 1 Y 1 A LYS 260 ? CD  ? A LYS 260 CD  
23 1 Y 1 A LYS 260 ? CE  ? A LYS 260 CE  
24 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       ? ? ? 3.3.20   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                   104.240 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     7NZT 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     42.224 
_cell.length_a_esd                 ? 
_cell.length_b                     41.335 
_cell.length_b_esd                 ? 
_cell.length_c                     71.742 
_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                         7NZT 
_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                   7NZT 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                      ? 
_exptl_crystal.density_diffrn              ? 
_exptl_crystal.density_Matthews            2.07 
_exptl_crystal.density_method              ? 
_exptl_crystal.density_percent_sol         40.45 
_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                         7NZT 
_reflns.data_reduction_details           ? 
_reflns.data_reduction_method            ? 
_reflns.d_resolution_high                1.350 
_reflns.d_resolution_low                 69.540 
_reflns.details                          ? 
_reflns.limit_h_max                      ? 
_reflns.limit_h_min                      ? 
_reflns.limit_k_max                      ? 
_reflns.limit_k_min                      ? 
_reflns.limit_l_max                      ? 
_reflns.limit_l_min                      ? 
_reflns.number_all                       ? 
_reflns.number_obs                       50279 
_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             95.300 
_reflns.R_free_details                   ? 
_reflns.Rmerge_F_all                     ? 
_reflns.Rmerge_F_obs                     ? 
_reflns.Friedel_coverage                 ? 
_reflns.number_gt                        ? 
_reflns.threshold_expression             ? 
_reflns.pdbx_redundancy                  7.000 
_reflns.pdbx_Rmerge_I_obs                ? 
_reflns.pdbx_Rmerge_I_all                ? 
_reflns.pdbx_Rsym_value                  0.050 
_reflns.pdbx_netI_over_av_sigmaI         8.700 
_reflns.pdbx_netI_over_sigmaI            21.600 
_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                  0.060 
_reflns.pdbx_Rpim_I_all                  0.023 
_reflns.pdbx_d_opt                       ? 
_reflns.pdbx_number_measured_all         ? 
_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 
1.350 1.420  ? 2.600  51329 ? ? ? 7217 94.100 ? ? ? ? 0.273 ? ? ? ? ? ? ? ? 7.100 0.273 ? ? 6.400  0.327 0.121 ? 1  1 ? ? ? 
1.420 1.510  ? 3.400  45839 ? ? ? 6739 93.100 ? ? ? ? 0.203 ? ? ? ? ? ? ? ? 6.800 0.203 ? ? 8.200  0.248 0.094 ? 2  1 ? ? ? 
1.510 1.610  ? 4.400  45561 ? ? ? 6421 94.500 ? ? ? ? 0.147 ? ? ? ? ? ? ? ? 7.100 0.147 ? ? 11.600 0.182 0.068 ? 3  1 ? ? ? 
1.610 1.740  ? 5.500  43433 ? ? ? 6100 95.900 ? ? ? ? 0.108 ? ? ? ? ? ? ? ? 7.100 0.108 ? ? 15.300 0.130 0.049 ? 4  1 ? ? ? 
1.740 1.910  ? 7.000  37476 ? ? ? 5507 94.000 ? ? ? ? 0.078 ? ? ? ? ? ? ? ? 6.800 0.078 ? ? 20.200 0.094 0.035 ? 5  1 ? ? ? 
1.910 2.130  ? 10.600 37657 ? ? ? 5146 97.200 ? ? ? ? 0.053 ? ? ? ? ? ? ? ? 7.300 0.053 ? ? 29.100 0.064 0.023 ? 6  1 ? ? ? 
2.130 2.460  ? 14.200 32582 ? ? ? 4596 97.700 ? ? ? ? 0.042 ? ? ? ? ? ? ? ? 7.100 0.042 ? ? 34.900 0.051 0.019 ? 7  1 ? ? ? 
2.460 3.020  ? 16.200 26149 ? ? ? 3798 95.800 ? ? ? ? 0.036 ? ? ? ? ? ? ? ? 6.900 0.036 ? ? 40.100 0.044 0.017 ? 8  1 ? ? ? 
3.020 4.270  ? 19.400 21723 ? ? ? 3071 98.800 ? ? ? ? 0.028 ? ? ? ? ? ? ? ? 7.100 0.028 ? ? 51.300 0.035 0.013 ? 9  1 ? ? ? 
4.270 69.539 ? 14.100 11499 ? ? ? 1684 96.000 ? ? ? ? 0.032 ? ? ? ? ? ? ? ? 6.800 0.032 ? ? 51.800 0.037 0.014 ? 10 1 ? ? ? 
# 
_refine.aniso_B[1][1]                            0.0200 
_refine.aniso_B[1][2]                            0.0000 
_refine.aniso_B[1][3]                            -0.0200 
_refine.aniso_B[2][2]                            0.1500 
_refine.aniso_B[2][3]                            0.0000 
_refine.aniso_B[3][3]                            -0.1400 
_refine.B_iso_max                                113.610 
_refine.B_iso_mean                               14.8460 
_refine.B_iso_min                                5.010 
_refine.correlation_coeff_Fo_to_Fc               0.9770 
_refine.correlation_coeff_Fo_to_Fc_free          0.9650 
_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                                 7NZT 
_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                            1.3500 
_refine.ls_d_res_low                             69.539 
_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                     45219 
_refine.ls_number_reflns_R_free                  5045 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    94.9400 
_refine.ls_percent_reflns_R_free                 10.0000 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1268 
_refine.ls_R_factor_R_free                       0.1657 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1225 
_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                       0.0570 
_refine.pdbx_overall_ESU_R_Free                  0.0550 
_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                       1.3500 
_refine_hist.d_res_low                        69.539 
_refine_hist.number_atoms_solvent             295 
_refine_hist.number_atoms_total               2363 
_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       257 
_refine_hist.pdbx_B_iso_mean_ligand           15.47 
_refine_hist.pdbx_B_iso_mean_solvent          27.83 
_refine_hist.pdbx_number_atoms_protein        2031 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         37 
_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' ? 0.015  0.012  2244 ? r_bond_refined_d       ? ? 
'X-RAY DIFFRACTION' ? 2.121  1.657  3073 ? r_angle_refined_deg    ? ? 
'X-RAY DIFFRACTION' ? 6.887  5.000  282  ? r_dihedral_angle_1_deg ? ? 
'X-RAY DIFFRACTION' ? 36.498 23.981 108  ? r_dihedral_angle_2_deg ? ? 
'X-RAY DIFFRACTION' ? 12.730 15.000 360  ? r_dihedral_angle_3_deg ? ? 
'X-RAY DIFFRACTION' ? 22.540 15.000 7    ? r_dihedral_angle_4_deg ? ? 
'X-RAY DIFFRACTION' ? 0.136  0.200  273  ? r_chiral_restr         ? ? 
'X-RAY DIFFRACTION' ? 0.016  0.020  1775 ? r_gen_planes_refined   ? ? 
'X-RAY DIFFRACTION' ? 4.642  3.000  2244 ? r_rigid_bond_restr     ? ? 
'X-RAY DIFFRACTION' ? 23.967 5.000  178  ? r_sphericity_free      ? ? 
'X-RAY DIFFRACTION' ? 12.170 5.000  2288 ? r_sphericity_bonded    ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.3500 
_refine_ls_shell.d_res_low                        1.3850 
_refine_ls_shell.number_reflns_all                3669 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             358 
_refine_ls_shell.number_reflns_R_work             3311 
_refine_ls_shell.percent_reflns_obs               93.6700 
_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                  0.1370 
_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   20 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
# 
_struct.entry_id                     7NZT 
_struct.title                        
;Crystal structure of chimeric carbonic anhydrase VA with 3-(cyclooctylamino)-2,5,6-trifluoro-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        7NZT 
_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 3 ? 
E N N 4 ? 
F N N 5 ? 
# 
_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              7NZT 
_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 7NZT THR A 62  ? UNP P00918 ASN 62  'engineered mutation' 62  1 
1 7NZT TYR A 64  ? UNP P00918 HIS 64  'engineered mutation' 64  2 
1 7NZT LEU A 65  ? UNP P00918 ALA 65  'engineered mutation' 65  3 
1 7NZT GLN A 67  ? UNP P00918 ASN 67  'engineered mutation' 67  4 
1 7NZT LYS A 91  ? UNP P00918 ILE 91  'engineered mutation' 91  5 
1 7NZT TYR A 130 ? UNP P00918 PHE 130 'engineered mutation' 130 6 
1 7NZT 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)' 400   ? 
1 MORE         3     ? 
1 'SSA (A^2)'  11180 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 GLY A 12  ? ASP A 19  ? GLY A 12  ASP A 19  5 ? 8 
HELX_P HELX_P2 AA2 PHE A 20  ? GLY A 25  ? PHE A 20  GLY A 25  5 ? 6 
HELX_P HELX_P3 AA3 LYS A 126 ? GLY A 128 ? LYS A 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 219 ? ARG A 226 ? SER A 219 ARG A 226 1 ? 8 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A HIS 94  NE2 ? ? ? 1_555 B ZN  . ZN  ? ? A HIS 94  A ZN  301 1_555 ? ? ? ? ? ? ? 1.965 ? ? 
metalc2 metalc ? ? A HIS 96  NE2 ? ? ? 1_555 B ZN  . ZN  ? ? A HIS 96  A ZN  301 1_555 ? ? ? ? ? ? ? 2.014 ? ? 
metalc3 metalc ? ? A HIS 119 ND1 ? ? ? 1_555 B ZN  . ZN  ? ? A HIS 119 A ZN  301 1_555 ? ? ? ? ? ? ? 2.032 ? ? 
metalc4 metalc ? ? B ZN  .   ZN  ? ? ? 1_555 E V14 . N10 ? ? A ZN  301 A V14 304 1_555 ? ? ? ? ? ? ? 1.926 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1 NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 104.1 ? 
2 NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 111.2 ? 
3 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 101.7 ? 
4 NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N10 ? E V14 .   ? A V14 304 ? 1_555 115.1 ? 
5 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N10 ? E V14 .   ? A V14 304 ? 1_555 115.5 ? 
6 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N10 ? E V14 .   ? A V14 304 ? 1_555 108.4 ? 
# 
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 -4.16 
2 PRO 200 A . ? PRO 200 A PRO 201 A ? PRO 201 A 1 7.57  
# 
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 ? GLY A 150 ? LEU A 140 GLY A 150 
AA2 6  ALA A 116 ? ASN A 124 ? ALA A 116 ASN A 124 
AA2 7  TYR A 88  ? TRP A 97  ? TYR A 88  TRP A 97  
AA2 8  PHE A 66  ? PHE A 70  ? PHE A 66  PHE A 70  
AA2 9  SER A 56  ? ASN A 61  ? SER A 56  ASN A 61  
AA2 10 SER A 172 ? ASP A 174 ? SER A 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 ? GLY A 150 ? LEU A 140 GLY A 150 
AA3 6  ILE A 215 ? SER A 218 ? ILE A 215 SER A 218 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2  N ILE A 33  ? N ILE A 33  O THR A 108 ? O THR A 108 
AA2 1 2  N LYS A 39  ? N LYS A 39  O ALA A 257 ? O ALA A 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 VAL A 121 ? O VAL A 121 N LYS A 91  ? N LYS A 91  
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 48  ? N SER A 48  O LYS A 80  ? O LYS A 80  
AA3 2 3  N LEU A 79  ? N LEU A 79  O TYR A 88  ? O TYR A 88  
AA3 3 4  N LYS A 91  ? N LYS A 91  O VAL A 121 ? O VAL A 121 
AA3 4 5  N LEU A 118 ? N LEU A 118 O ILE A 145 ? O ILE A 145 
AA3 5 6  N GLY A 150 ? N GLY A 150 O VAL A 217 ? O VAL A 217 
# 
_pdbx_validate_rmsd_bond.id                        1 
_pdbx_validate_rmsd_bond.PDB_model_num             1 
_pdbx_validate_rmsd_bond.auth_atom_id_1            CG 
_pdbx_validate_rmsd_bond.auth_asym_id_1            A 
_pdbx_validate_rmsd_bond.auth_comp_id_1            HIS 
_pdbx_validate_rmsd_bond.auth_seq_id_1             10 
_pdbx_validate_rmsd_bond.PDB_ins_code_1            ? 
_pdbx_validate_rmsd_bond.label_alt_id_1            ? 
_pdbx_validate_rmsd_bond.auth_atom_id_2            CD2 
_pdbx_validate_rmsd_bond.auth_asym_id_2            A 
_pdbx_validate_rmsd_bond.auth_comp_id_2            HIS 
_pdbx_validate_rmsd_bond.auth_seq_id_2             10 
_pdbx_validate_rmsd_bond.PDB_ins_code_2            ? 
_pdbx_validate_rmsd_bond.label_alt_id_2            ? 
_pdbx_validate_rmsd_bond.bond_value                1.436 
_pdbx_validate_rmsd_bond.bond_target_value         1.354 
_pdbx_validate_rmsd_bond.bond_deviation            0.082 
_pdbx_validate_rmsd_bond.bond_standard_deviation   0.009 
_pdbx_validate_rmsd_bond.linker_flag               N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASN A 11  ? ? -146.78 21.19   
2 1 LEU A 57  ? ? -123.04 -51.69  
3 1 GLU A 106 ? ? -90.36  -61.15  
4 1 LYS A 111 ? ? 72.87   -1.19   
5 1 PHE A 175 ? ? -151.07 61.40   
6 1 ASN A 243 ? ? -97.84  47.63   
7 1 LYS A 251 ? ? 54.10   -135.64 
# 
_pdbx_entry_details.entry_id                 7NZT 
_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         ? 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 694 ? 6.02 . 
2 1 O ? A HOH 695 ? 6.26 . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A MET 1 ? A MET 1 
2 1 Y 1 A SER 2 ? A SER 2 
3 1 Y 1 A HIS 3 ? A HIS 3 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
CYS N    N  N N 74  
CYS CA   C  N R 75  
CYS C    C  N N 76  
CYS O    O  N N 77  
CYS CB   C  N N 78  
CYS SG   S  N N 79  
CYS OXT  O  N N 80  
CYS H    H  N N 81  
CYS H2   H  N N 82  
CYS HA   H  N N 83  
CYS HB2  H  N N 84  
CYS HB3  H  N N 85  
CYS HG   H  N N 86  
CYS HXT  H  N N 87  
DMS S    S  N N 88  
DMS O    O  N N 89  
DMS C1   C  N N 90  
DMS C2   C  N N 91  
DMS H11  H  N N 92  
DMS H12  H  N N 93  
DMS H13  H  N N 94  
DMS H21  H  N N 95  
DMS H22  H  N N 96  
DMS H23  H  N N 97  
GLN N    N  N N 98  
GLN CA   C  N S 99  
GLN C    C  N N 100 
GLN O    O  N N 101 
GLN CB   C  N N 102 
GLN CG   C  N N 103 
GLN CD   C  N N 104 
GLN OE1  O  N N 105 
GLN NE2  N  N N 106 
GLN OXT  O  N N 107 
GLN H    H  N N 108 
GLN H2   H  N N 109 
GLN HA   H  N N 110 
GLN HB2  H  N N 111 
GLN HB3  H  N N 112 
GLN HG2  H  N N 113 
GLN HG3  H  N N 114 
GLN HE21 H  N N 115 
GLN HE22 H  N N 116 
GLN HXT  H  N N 117 
GLU N    N  N N 118 
GLU CA   C  N S 119 
GLU C    C  N N 120 
GLU O    O  N N 121 
GLU CB   C  N N 122 
GLU CG   C  N N 123 
GLU CD   C  N N 124 
GLU OE1  O  N N 125 
GLU OE2  O  N N 126 
GLU OXT  O  N N 127 
GLU H    H  N N 128 
GLU H2   H  N N 129 
GLU HA   H  N N 130 
GLU HB2  H  N N 131 
GLU HB3  H  N N 132 
GLU HG2  H  N N 133 
GLU HG3  H  N N 134 
GLU HE2  H  N N 135 
GLU HXT  H  N N 136 
GLY N    N  N N 137 
GLY CA   C  N N 138 
GLY C    C  N N 139 
GLY O    O  N N 140 
GLY OXT  O  N N 141 
GLY H    H  N N 142 
GLY H2   H  N N 143 
GLY HA2  H  N N 144 
GLY HA3  H  N N 145 
GLY HXT  H  N N 146 
HIS N    N  N N 147 
HIS CA   C  N S 148 
HIS C    C  N N 149 
HIS O    O  N N 150 
HIS CB   C  N N 151 
HIS CG   C  Y N 152 
HIS ND1  N  Y N 153 
HIS CD2  C  Y N 154 
HIS CE1  C  Y N 155 
HIS NE2  N  Y N 156 
HIS OXT  O  N N 157 
HIS H    H  N N 158 
HIS H2   H  N N 159 
HIS HA   H  N N 160 
HIS HB2  H  N N 161 
HIS HB3  H  N N 162 
HIS HD1  H  N N 163 
HIS HD2  H  N N 164 
HIS HE1  H  N N 165 
HIS HE2  H  N N 166 
HIS HXT  H  N N 167 
HOH O    O  N N 168 
HOH H1   H  N N 169 
HOH H2   H  N N 170 
ILE N    N  N N 171 
ILE CA   C  N S 172 
ILE C    C  N N 173 
ILE O    O  N N 174 
ILE CB   C  N S 175 
ILE CG1  C  N N 176 
ILE CG2  C  N N 177 
ILE CD1  C  N N 178 
ILE OXT  O  N N 179 
ILE H    H  N N 180 
ILE H2   H  N N 181 
ILE HA   H  N N 182 
ILE HB   H  N N 183 
ILE HG12 H  N N 184 
ILE HG13 H  N N 185 
ILE HG21 H  N N 186 
ILE HG22 H  N N 187 
ILE HG23 H  N N 188 
ILE HD11 H  N N 189 
ILE HD12 H  N N 190 
ILE HD13 H  N N 191 
ILE HXT  H  N N 192 
LEU N    N  N N 193 
LEU CA   C  N S 194 
LEU C    C  N N 195 
LEU O    O  N N 196 
LEU CB   C  N N 197 
LEU CG   C  N N 198 
LEU CD1  C  N N 199 
LEU CD2  C  N N 200 
LEU OXT  O  N N 201 
LEU H    H  N N 202 
LEU H2   H  N N 203 
LEU HA   H  N N 204 
LEU HB2  H  N N 205 
LEU HB3  H  N N 206 
LEU HG   H  N N 207 
LEU HD11 H  N N 208 
LEU HD12 H  N N 209 
LEU HD13 H  N N 210 
LEU HD21 H  N N 211 
LEU HD22 H  N N 212 
LEU HD23 H  N N 213 
LEU HXT  H  N N 214 
LYS N    N  N N 215 
LYS CA   C  N S 216 
LYS C    C  N N 217 
LYS O    O  N N 218 
LYS CB   C  N N 219 
LYS CG   C  N N 220 
LYS CD   C  N N 221 
LYS CE   C  N N 222 
LYS NZ   N  N N 223 
LYS OXT  O  N N 224 
LYS H    H  N N 225 
LYS H2   H  N N 226 
LYS HA   H  N N 227 
LYS HB2  H  N N 228 
LYS HB3  H  N N 229 
LYS HG2  H  N N 230 
LYS HG3  H  N N 231 
LYS HD2  H  N N 232 
LYS HD3  H  N N 233 
LYS HE2  H  N N 234 
LYS HE3  H  N N 235 
LYS HZ1  H  N N 236 
LYS HZ2  H  N N 237 
LYS HZ3  H  N N 238 
LYS HXT  H  N N 239 
MET N    N  N N 240 
MET CA   C  N S 241 
MET C    C  N N 242 
MET O    O  N N 243 
MET CB   C  N N 244 
MET CG   C  N N 245 
MET SD   S  N N 246 
MET CE   C  N N 247 
MET OXT  O  N N 248 
MET H    H  N N 249 
MET H2   H  N N 250 
MET HA   H  N N 251 
MET HB2  H  N N 252 
MET HB3  H  N N 253 
MET HG2  H  N N 254 
MET HG3  H  N N 255 
MET HE1  H  N N 256 
MET HE2  H  N N 257 
MET HE3  H  N N 258 
MET HXT  H  N N 259 
PHE N    N  N N 260 
PHE CA   C  N S 261 
PHE C    C  N N 262 
PHE O    O  N N 263 
PHE CB   C  N N 264 
PHE CG   C  Y N 265 
PHE CD1  C  Y N 266 
PHE CD2  C  Y N 267 
PHE CE1  C  Y N 268 
PHE CE2  C  Y N 269 
PHE CZ   C  Y N 270 
PHE OXT  O  N N 271 
PHE H    H  N N 272 
PHE H2   H  N N 273 
PHE HA   H  N N 274 
PHE HB2  H  N N 275 
PHE HB3  H  N N 276 
PHE HD1  H  N N 277 
PHE HD2  H  N N 278 
PHE HE1  H  N N 279 
PHE HE2  H  N N 280 
PHE HZ   H  N N 281 
PHE HXT  H  N N 282 
PRO N    N  N N 283 
PRO CA   C  N S 284 
PRO C    C  N N 285 
PRO O    O  N N 286 
PRO CB   C  N N 287 
PRO CG   C  N N 288 
PRO CD   C  N N 289 
PRO OXT  O  N N 290 
PRO H    H  N N 291 
PRO HA   H  N N 292 
PRO HB2  H  N N 293 
PRO HB3  H  N N 294 
PRO HG2  H  N N 295 
PRO HG3  H  N N 296 
PRO HD2  H  N N 297 
PRO HD3  H  N N 298 
PRO HXT  H  N N 299 
SER N    N  N N 300 
SER CA   C  N S 301 
SER C    C  N N 302 
SER O    O  N N 303 
SER CB   C  N N 304 
SER OG   O  N N 305 
SER OXT  O  N N 306 
SER H    H  N N 307 
SER H2   H  N N 308 
SER HA   H  N N 309 
SER HB2  H  N N 310 
SER HB3  H  N N 311 
SER HG   H  N N 312 
SER HXT  H  N N 313 
THR N    N  N N 314 
THR CA   C  N S 315 
THR C    C  N N 316 
THR O    O  N N 317 
THR CB   C  N R 318 
THR OG1  O  N N 319 
THR CG2  C  N N 320 
THR OXT  O  N N 321 
THR H    H  N N 322 
THR H2   H  N N 323 
THR HA   H  N N 324 
THR HB   H  N N 325 
THR HG1  H  N N 326 
THR HG21 H  N N 327 
THR HG22 H  N N 328 
THR HG23 H  N N 329 
THR HXT  H  N N 330 
TRP N    N  N N 331 
TRP CA   C  N S 332 
TRP C    C  N N 333 
TRP O    O  N N 334 
TRP CB   C  N N 335 
TRP CG   C  Y N 336 
TRP CD1  C  Y N 337 
TRP CD2  C  Y N 338 
TRP NE1  N  Y N 339 
TRP CE2  C  Y N 340 
TRP CE3  C  Y N 341 
TRP CZ2  C  Y N 342 
TRP CZ3  C  Y N 343 
TRP CH2  C  Y N 344 
TRP OXT  O  N N 345 
TRP H    H  N N 346 
TRP H2   H  N N 347 
TRP HA   H  N N 348 
TRP HB2  H  N N 349 
TRP HB3  H  N N 350 
TRP HD1  H  N N 351 
TRP HE1  H  N N 352 
TRP HE3  H  N N 353 
TRP HZ2  H  N N 354 
TRP HZ3  H  N N 355 
TRP HH2  H  N N 356 
TRP HXT  H  N N 357 
TYR N    N  N N 358 
TYR CA   C  N S 359 
TYR C    C  N N 360 
TYR O    O  N N 361 
TYR CB   C  N N 362 
TYR CG   C  Y N 363 
TYR CD1  C  Y N 364 
TYR CD2  C  Y N 365 
TYR CE1  C  Y N 366 
TYR CE2  C  Y N 367 
TYR CZ   C  Y N 368 
TYR OH   O  N N 369 
TYR OXT  O  N N 370 
TYR H    H  N N 371 
TYR H2   H  N N 372 
TYR HA   H  N N 373 
TYR HB2  H  N N 374 
TYR HB3  H  N N 375 
TYR HD1  H  N N 376 
TYR HD2  H  N N 377 
TYR HE1  H  N N 378 
TYR HE2  H  N N 379 
TYR HH   H  N N 380 
TYR HXT  H  N N 381 
V14 F20  F  N N 382 
V14 C5   C  Y N 383 
V14 C4   C  Y N 384 
V14 S7   S  N N 385 
V14 O9   O  N N 386 
V14 N10  N  N N 387 
V14 O8   O  N N 388 
V14 C3   C  Y N 389 
V14 F12  F  N N 390 
V14 C2   C  Y N 391 
V14 F13  F  N N 392 
V14 C6   C  Y N 393 
V14 C1   C  Y N 394 
V14 S11  S  N N 395 
V14 O16  O  N N 396 
V14 O17  O  N N 397 
V14 C15  C  N N 398 
V14 C18  C  N N 399 
V14 O21  O  N N 400 
V14 N19  N  N N 401 
V14 C14  C  N N 402 
V14 C28  C  N N 403 
V14 C27  C  N N 404 
V14 C26  C  N N 405 
V14 C25  C  N N 406 
V14 C24  C  N N 407 
V14 C23  C  N N 408 
V14 C22  C  N N 409 
V14 H1   H  N N 410 
V14 H2   H  N N 411 
V14 H3   H  N N 412 
V14 H4   H  N N 413 
V14 H5   H  N N 414 
V14 H6   H  N N 415 
V14 H7   H  N N 416 
V14 H8   H  N N 417 
V14 H9   H  N N 418 
V14 H10  H  N N 419 
V14 H11  H  N N 420 
V14 H12  H  N N 421 
V14 H13  H  N N 422 
V14 H14  H  N N 423 
V14 H15  H  N N 424 
V14 H16  H  N N 425 
V14 H17  H  N N 426 
V14 H18  H  N N 427 
V14 H19  H  N N 428 
V14 H20  H  N N 429 
V14 H21  H  N N 430 
V14 H22  H  N N 431 
V14 H23  H  N N 432 
VAL N    N  N N 433 
VAL CA   C  N S 434 
VAL C    C  N N 435 
VAL O    O  N N 436 
VAL CB   C  N N 437 
VAL CG1  C  N N 438 
VAL CG2  C  N N 439 
VAL OXT  O  N N 440 
VAL H    H  N N 441 
VAL H2   H  N N 442 
VAL HA   H  N N 443 
VAL HB   H  N N 444 
VAL HG11 H  N N 445 
VAL HG12 H  N N 446 
VAL HG13 H  N N 447 
VAL HG21 H  N N 448 
VAL HG22 H  N N 449 
VAL HG23 H  N N 450 
VAL HXT  H  N N 451 
ZN  ZN   ZN N N 452 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
DMS S   O    doub N N 83  
DMS S   C1   sing N N 84  
DMS S   C2   sing N N 85  
DMS C1  H11  sing N N 86  
DMS C1  H12  sing N N 87  
DMS C1  H13  sing N N 88  
DMS C2  H21  sing N N 89  
DMS C2  H22  sing N N 90  
DMS C2  H23  sing N N 91  
GLN N   CA   sing N N 92  
GLN N   H    sing N N 93  
GLN N   H2   sing N N 94  
GLN CA  C    sing N N 95  
GLN CA  CB   sing N N 96  
GLN CA  HA   sing N N 97  
GLN C   O    doub N N 98  
GLN C   OXT  sing N N 99  
GLN CB  CG   sing N N 100 
GLN CB  HB2  sing N N 101 
GLN CB  HB3  sing N N 102 
GLN CG  CD   sing N N 103 
GLN CG  HG2  sing N N 104 
GLN CG  HG3  sing N N 105 
GLN CD  OE1  doub N N 106 
GLN CD  NE2  sing N N 107 
GLN NE2 HE21 sing N N 108 
GLN NE2 HE22 sing N N 109 
GLN OXT HXT  sing N N 110 
GLU N   CA   sing N N 111 
GLU N   H    sing N N 112 
GLU N   H2   sing N N 113 
GLU CA  C    sing N N 114 
GLU CA  CB   sing N N 115 
GLU CA  HA   sing N N 116 
GLU C   O    doub N N 117 
GLU C   OXT  sing N N 118 
GLU CB  CG   sing N N 119 
GLU CB  HB2  sing N N 120 
GLU CB  HB3  sing N N 121 
GLU CG  CD   sing N N 122 
GLU CG  HG2  sing N N 123 
GLU CG  HG3  sing N N 124 
GLU CD  OE1  doub N N 125 
GLU CD  OE2  sing N N 126 
GLU OE2 HE2  sing N N 127 
GLU OXT HXT  sing N N 128 
GLY N   CA   sing N N 129 
GLY N   H    sing N N 130 
GLY N   H2   sing N N 131 
GLY CA  C    sing N N 132 
GLY CA  HA2  sing N N 133 
GLY CA  HA3  sing N N 134 
GLY C   O    doub N N 135 
GLY C   OXT  sing N N 136 
GLY OXT HXT  sing N N 137 
HIS N   CA   sing N N 138 
HIS N   H    sing N N 139 
HIS N   H2   sing N N 140 
HIS CA  C    sing N N 141 
HIS CA  CB   sing N N 142 
HIS CA  HA   sing N N 143 
HIS C   O    doub N N 144 
HIS C   OXT  sing N N 145 
HIS CB  CG   sing N N 146 
HIS CB  HB2  sing N N 147 
HIS CB  HB3  sing N N 148 
HIS CG  ND1  sing Y N 149 
HIS CG  CD2  doub Y N 150 
HIS ND1 CE1  doub Y N 151 
HIS ND1 HD1  sing N N 152 
HIS CD2 NE2  sing Y N 153 
HIS CD2 HD2  sing N N 154 
HIS CE1 NE2  sing Y N 155 
HIS CE1 HE1  sing N N 156 
HIS NE2 HE2  sing N N 157 
HIS OXT HXT  sing N N 158 
HOH O   H1   sing N N 159 
HOH O   H2   sing N N 160 
ILE N   CA   sing N N 161 
ILE N   H    sing N N 162 
ILE N   H2   sing N N 163 
ILE CA  C    sing N N 164 
ILE CA  CB   sing N N 165 
ILE CA  HA   sing N N 166 
ILE C   O    doub N N 167 
ILE C   OXT  sing N N 168 
ILE CB  CG1  sing N N 169 
ILE CB  CG2  sing N N 170 
ILE CB  HB   sing N N 171 
ILE CG1 CD1  sing N N 172 
ILE CG1 HG12 sing N N 173 
ILE CG1 HG13 sing N N 174 
ILE CG2 HG21 sing N N 175 
ILE CG2 HG22 sing N N 176 
ILE CG2 HG23 sing N N 177 
ILE CD1 HD11 sing N N 178 
ILE CD1 HD12 sing N N 179 
ILE CD1 HD13 sing N N 180 
ILE OXT HXT  sing N N 181 
LEU N   CA   sing N N 182 
LEU N   H    sing N N 183 
LEU N   H2   sing N N 184 
LEU CA  C    sing N N 185 
LEU CA  CB   sing N N 186 
LEU CA  HA   sing N N 187 
LEU C   O    doub N N 188 
LEU C   OXT  sing N N 189 
LEU CB  CG   sing N N 190 
LEU CB  HB2  sing N N 191 
LEU CB  HB3  sing N N 192 
LEU CG  CD1  sing N N 193 
LEU CG  CD2  sing N N 194 
LEU CG  HG   sing N N 195 
LEU CD1 HD11 sing N N 196 
LEU CD1 HD12 sing N N 197 
LEU CD1 HD13 sing N N 198 
LEU CD2 HD21 sing N N 199 
LEU CD2 HD22 sing N N 200 
LEU CD2 HD23 sing N N 201 
LEU OXT HXT  sing N N 202 
LYS N   CA   sing N N 203 
LYS N   H    sing N N 204 
LYS N   H2   sing N N 205 
LYS CA  C    sing N N 206 
LYS CA  CB   sing N N 207 
LYS CA  HA   sing N N 208 
LYS C   O    doub N N 209 
LYS C   OXT  sing N N 210 
LYS CB  CG   sing N N 211 
LYS CB  HB2  sing N N 212 
LYS CB  HB3  sing N N 213 
LYS CG  CD   sing N N 214 
LYS CG  HG2  sing N N 215 
LYS CG  HG3  sing N N 216 
LYS CD  CE   sing N N 217 
LYS CD  HD2  sing N N 218 
LYS CD  HD3  sing N N 219 
LYS CE  NZ   sing N N 220 
LYS CE  HE2  sing N N 221 
LYS CE  HE3  sing N N 222 
LYS NZ  HZ1  sing N N 223 
LYS NZ  HZ2  sing N N 224 
LYS NZ  HZ3  sing N N 225 
LYS OXT HXT  sing N N 226 
MET N   CA   sing N N 227 
MET N   H    sing N N 228 
MET N   H2   sing N N 229 
MET CA  C    sing N N 230 
MET CA  CB   sing N N 231 
MET CA  HA   sing N N 232 
MET C   O    doub N N 233 
MET C   OXT  sing N N 234 
MET CB  CG   sing N N 235 
MET CB  HB2  sing N N 236 
MET CB  HB3  sing N N 237 
MET CG  SD   sing N N 238 
MET CG  HG2  sing N N 239 
MET CG  HG3  sing N N 240 
MET SD  CE   sing N N 241 
MET CE  HE1  sing N N 242 
MET CE  HE2  sing N N 243 
MET CE  HE3  sing N N 244 
MET OXT HXT  sing N N 245 
PHE N   CA   sing N N 246 
PHE N   H    sing N N 247 
PHE N   H2   sing N N 248 
PHE CA  C    sing N N 249 
PHE CA  CB   sing N N 250 
PHE CA  HA   sing N N 251 
PHE C   O    doub N N 252 
PHE C   OXT  sing N N 253 
PHE CB  CG   sing N N 254 
PHE CB  HB2  sing N N 255 
PHE CB  HB3  sing N N 256 
PHE CG  CD1  doub Y N 257 
PHE CG  CD2  sing Y N 258 
PHE CD1 CE1  sing Y N 259 
PHE CD1 HD1  sing N N 260 
PHE CD2 CE2  doub Y N 261 
PHE CD2 HD2  sing N N 262 
PHE CE1 CZ   doub Y N 263 
PHE CE1 HE1  sing N N 264 
PHE CE2 CZ   sing Y N 265 
PHE CE2 HE2  sing N N 266 
PHE CZ  HZ   sing N N 267 
PHE OXT HXT  sing N N 268 
PRO N   CA   sing N N 269 
PRO N   CD   sing N N 270 
PRO N   H    sing N N 271 
PRO CA  C    sing N N 272 
PRO CA  CB   sing N N 273 
PRO CA  HA   sing N N 274 
PRO C   O    doub N N 275 
PRO C   OXT  sing N N 276 
PRO CB  CG   sing N N 277 
PRO CB  HB2  sing N N 278 
PRO CB  HB3  sing N N 279 
PRO CG  CD   sing N N 280 
PRO CG  HG2  sing N N 281 
PRO CG  HG3  sing N N 282 
PRO CD  HD2  sing N N 283 
PRO CD  HD3  sing N N 284 
PRO OXT HXT  sing N N 285 
SER N   CA   sing N N 286 
SER N   H    sing N N 287 
SER N   H2   sing N N 288 
SER CA  C    sing N N 289 
SER CA  CB   sing N N 290 
SER CA  HA   sing N N 291 
SER C   O    doub N N 292 
SER C   OXT  sing N N 293 
SER CB  OG   sing N N 294 
SER CB  HB2  sing N N 295 
SER CB  HB3  sing N N 296 
SER OG  HG   sing N N 297 
SER OXT HXT  sing N N 298 
THR N   CA   sing N N 299 
THR N   H    sing N N 300 
THR N   H2   sing N N 301 
THR CA  C    sing N N 302 
THR CA  CB   sing N N 303 
THR CA  HA   sing N N 304 
THR C   O    doub N N 305 
THR C   OXT  sing N N 306 
THR CB  OG1  sing N N 307 
THR CB  CG2  sing N N 308 
THR CB  HB   sing N N 309 
THR OG1 HG1  sing N N 310 
THR CG2 HG21 sing N N 311 
THR CG2 HG22 sing N N 312 
THR CG2 HG23 sing N N 313 
THR OXT HXT  sing N N 314 
TRP N   CA   sing N N 315 
TRP N   H    sing N N 316 
TRP N   H2   sing N N 317 
TRP CA  C    sing N N 318 
TRP CA  CB   sing N N 319 
TRP CA  HA   sing N N 320 
TRP C   O    doub N N 321 
TRP C   OXT  sing N N 322 
TRP CB  CG   sing N N 323 
TRP CB  HB2  sing N N 324 
TRP CB  HB3  sing N N 325 
TRP CG  CD1  doub Y N 326 
TRP CG  CD2  sing Y N 327 
TRP CD1 NE1  sing Y N 328 
TRP CD1 HD1  sing N N 329 
TRP CD2 CE2  doub Y N 330 
TRP CD2 CE3  sing Y N 331 
TRP NE1 CE2  sing Y N 332 
TRP NE1 HE1  sing N N 333 
TRP CE2 CZ2  sing Y N 334 
TRP CE3 CZ3  doub Y N 335 
TRP CE3 HE3  sing N N 336 
TRP CZ2 CH2  doub Y N 337 
TRP CZ2 HZ2  sing N N 338 
TRP CZ3 CH2  sing Y N 339 
TRP CZ3 HZ3  sing N N 340 
TRP CH2 HH2  sing N N 341 
TRP OXT HXT  sing N N 342 
TYR N   CA   sing N N 343 
TYR N   H    sing N N 344 
TYR N   H2   sing N N 345 
TYR CA  C    sing N N 346 
TYR CA  CB   sing N N 347 
TYR CA  HA   sing N N 348 
TYR C   O    doub N N 349 
TYR C   OXT  sing N N 350 
TYR CB  CG   sing N N 351 
TYR CB  HB2  sing N N 352 
TYR CB  HB3  sing N N 353 
TYR CG  CD1  doub Y N 354 
TYR CG  CD2  sing Y N 355 
TYR CD1 CE1  sing Y N 356 
TYR CD1 HD1  sing N N 357 
TYR CD2 CE2  doub Y N 358 
TYR CD2 HD2  sing N N 359 
TYR CE1 CZ   doub Y N 360 
TYR CE1 HE1  sing N N 361 
TYR CE2 CZ   sing Y N 362 
TYR CE2 HE2  sing N N 363 
TYR CZ  OH   sing N N 364 
TYR OH  HH   sing N N 365 
TYR OXT HXT  sing N N 366 
V14 C18 O21  sing N N 367 
V14 C18 C15  sing N N 368 
V14 C15 S11  sing N N 369 
V14 O17 S11  doub N N 370 
V14 C22 C23  sing N N 371 
V14 C22 C14  sing N N 372 
V14 C23 C24  sing N N 373 
V14 N19 C14  sing N N 374 
V14 N19 C6   sing N N 375 
V14 C24 C25  sing N N 376 
V14 S11 C1   sing N N 377 
V14 S11 O16  doub N N 378 
V14 C14 C28  sing N N 379 
V14 C6  C1   doub Y N 380 
V14 C6  C5   sing Y N 381 
V14 C1  C2   sing Y N 382 
V14 F20 C5   sing N N 383 
V14 C25 C26  sing N N 384 
V14 C5  C4   doub Y N 385 
V14 C26 C27  sing N N 386 
V14 C28 C27  sing N N 387 
V14 C2  F13  sing N N 388 
V14 C2  C3   doub Y N 389 
V14 C4  C3   sing Y N 390 
V14 C4  S7   sing N N 391 
V14 C3  F12  sing N N 392 
V14 N10 S7   sing N N 393 
V14 S7  O9   doub N N 394 
V14 S7  O8   doub N N 395 
V14 N10 H1   sing N N 396 
V14 N10 H2   sing N N 397 
V14 C15 H3   sing N N 398 
V14 C15 H4   sing N N 399 
V14 C18 H5   sing N N 400 
V14 C18 H6   sing N N 401 
V14 O21 H7   sing N N 402 
V14 N19 H8   sing N N 403 
V14 C14 H9   sing N N 404 
V14 C28 H10  sing N N 405 
V14 C28 H11  sing N N 406 
V14 C27 H12  sing N N 407 
V14 C27 H13  sing N N 408 
V14 C26 H14  sing N N 409 
V14 C26 H15  sing N N 410 
V14 C25 H16  sing N N 411 
V14 C25 H17  sing N N 412 
V14 C24 H18  sing N N 413 
V14 C24 H19  sing N N 414 
V14 C23 H20  sing N N 415 
V14 C23 H21  sing N N 416 
V14 C22 H22  sing N N 417 
V14 C22 H23  sing N N 418 
VAL N   CA   sing N N 419 
VAL N   H    sing N N 420 
VAL N   H2   sing N N 421 
VAL CA  C    sing N N 422 
VAL CA  CB   sing N N 423 
VAL CA  HA   sing N N 424 
VAL C   O    doub N N 425 
VAL C   OXT  sing N N 426 
VAL CB  CG1  sing N N 427 
VAL CB  CG2  sing N N 428 
VAL CB  HB   sing N N 429 
VAL CG1 HG11 sing N N 430 
VAL CG1 HG12 sing N N 431 
VAL CG1 HG13 sing N N 432 
VAL CG2 HG21 sing N N 433 
VAL CG2 HG22 sing N N 434 
VAL CG2 HG23 sing N N 435 
VAL OXT HXT  sing N N 436 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        V14 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   V14 
_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                    7NZT 
_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]   0.023683 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.006009 
_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]   0.014381 
_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  
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 4   ? 32.783 1.648   8.493   1.00 68.73  ? 4   HIS A N   1 
ATOM   2    C  CA  . HIS A 1 4   ? 31.460 2.160   8.942   1.00 56.90  ? 4   HIS A CA  1 
ATOM   3    C  C   . HIS A 1 4   ? 30.728 1.071   9.732   1.00 54.22  ? 4   HIS A C   1 
ATOM   4    O  O   . HIS A 1 4   ? 30.925 -0.150  9.523   1.00 32.02  ? 4   HIS A O   1 
ATOM   5    C  CB  . HIS A 1 4   ? 30.641 2.654   7.741   1.00 98.05  ? 4   HIS A CB  1 
ATOM   6    C  CG  . HIS A 1 4   ? 29.848 3.887   8.021   1.00 113.61 ? 4   HIS A CG  1 
ATOM   7    N  N   . TRP A 1 5   ? 29.753 1.392   10.624  1.00 25.82  ? 5   TRP A N   1 
ATOM   8    C  CA  . TRP A 1 5   ? 29.022 0.401   11.437  1.00 21.97  ? 5   TRP A CA  1 
ATOM   9    C  C   . TRP A 1 5   ? 28.063 -0.434  10.602  1.00 19.37  ? 5   TRP A C   1 
ATOM   10   O  O   . TRP A 1 5   ? 27.618 0.027   9.557   1.00 20.34  ? 5   TRP A O   1 
ATOM   11   C  CB  . TRP A 1 5   ? 28.191 1.027   12.587  1.00 19.16  ? 5   TRP A CB  1 
ATOM   12   C  CG  . TRP A 1 5   ? 27.036 1.905   12.157  1.00 19.71  ? 5   TRP A CG  1 
ATOM   13   C  CD1 . TRP A 1 5   ? 27.076 3.241   11.863  1.00 20.61  ? 5   TRP A CD1 1 
ATOM   14   C  CD2 . TRP A 1 5   ? 25.656 1.504   12.046  1.00 18.54  ? 5   TRP A CD2 1 
ATOM   15   N  NE1 . TRP A 1 5   ? 25.822 3.681   11.516  1.00 21.78  ? 5   TRP A NE1 1 
ATOM   16   C  CE2 . TRP A 1 5   ? 24.926 2.636   11.610  1.00 16.93  ? 5   TRP A CE2 1 
ATOM   17   C  CE3 . TRP A 1 5   ? 24.995 0.269   12.163  1.00 18.05  ? 5   TRP A CE3 1 
ATOM   18   C  CZ2 . TRP A 1 5   ? 23.535 2.603   11.454  1.00 20.28  ? 5   TRP A CZ2 1 
ATOM   19   C  CZ3 . TRP A 1 5   ? 23.616 0.224   11.979  1.00 21.04  ? 5   TRP A CZ3 1 
ATOM   20   C  CH2 . TRP A 1 5   ? 22.908 1.375   11.596  1.00 21.38  ? 5   TRP A CH2 1 
ATOM   21   N  N   . GLY A 1 6   ? 27.721 -1.638  11.095  1.00 18.42  ? 6   GLY A N   1 
ATOM   22   C  CA  . GLY A 1 6   ? 26.676 -2.441  10.469  1.00 16.90  ? 6   GLY A CA  1 
ATOM   23   C  C   . GLY A 1 6   ? 26.295 -3.611  11.374  1.00 21.02  ? 6   GLY A C   1 
ATOM   24   O  O   . GLY A 1 6   ? 26.313 -3.473  12.601  1.00 21.50  ? 6   GLY A O   1 
ATOM   25   N  N   . TYR A 1 7   ? 25.987 -4.743  10.759  1.00 18.82  ? 7   TYR A N   1 
ATOM   26   C  CA  . TYR A 1 7   ? 25.501 -5.838  11.598  1.00 22.43  ? 7   TYR A CA  1 
ATOM   27   C  C   . TYR A 1 7   ? 26.422 -7.058  11.529  1.00 24.70  ? 7   TYR A C   1 
ATOM   28   O  O   . TYR A 1 7   ? 26.116 -8.063  12.191  1.00 35.28  ? 7   TYR A O   1 
ATOM   29   C  CB  . TYR A 1 7   ? 24.004 -6.147  11.389  1.00 19.84  ? 7   TYR A CB  1 
ATOM   30   C  CG  . TYR A 1 7   ? 23.060 -5.062  11.888  1.00 16.48  ? 7   TYR A CG  1 
ATOM   31   C  CD1 . TYR A 1 7   ? 22.611 -5.021  13.232  1.00 18.55  ? 7   TYR A CD1 1 
ATOM   32   C  CD2 . TYR A 1 7   ? 22.592 -4.079  11.020  1.00 15.73  ? 7   TYR A CD2 1 
ATOM   33   C  CE1 . TYR A 1 7   ? 21.766 -3.982  13.658  1.00 14.65  ? 7   TYR A CE1 1 
ATOM   34   C  CE2 . TYR A 1 7   ? 21.732 -3.084  11.432  1.00 13.73  ? 7   TYR A CE2 1 
ATOM   35   C  CZ  . TYR A 1 7   ? 21.274 -3.080  12.752  1.00 13.75  ? 7   TYR A CZ  1 
ATOM   36   O  OH  . TYR A 1 7   ? 20.447 -2.129  13.101  1.00 21.23  ? 7   TYR A OH  1 
ATOM   37   N  N   . GLY A 1 8   ? 27.557 -6.963  10.790  1.00 25.22  ? 8   GLY A N   1 
ATOM   38   C  CA  . GLY A 1 8   ? 28.457 -8.100  10.544  1.00 29.34  ? 8   GLY A CA  1 
ATOM   39   C  C   . GLY A 1 8   ? 29.468 -8.408  11.670  1.00 27.73  ? 8   GLY A C   1 
ATOM   40   O  O   . GLY A 1 8   ? 29.561 -7.729  12.724  1.00 31.45  ? 8   GLY A O   1 
ATOM   41   N  N   . LYS A 1 9   ? 30.257 -9.466  11.440  1.00 40.00  ? 9   LYS A N   1 
ATOM   42   C  CA  . LYS A 1 9   ? 31.324 -9.914  12.336  1.00 44.41  ? 9   LYS A CA  1 
ATOM   43   C  C   . LYS A 1 9   ? 32.235 -8.732  12.619  1.00 40.51  ? 9   LYS A C   1 
ATOM   44   O  O   . LYS A 1 9   ? 32.637 -8.505  13.771  1.00 34.43  ? 9   LYS A O   1 
ATOM   45   C  CB  . LYS A 1 9   ? 32.197 -11.010 11.693  1.00 40.19  ? 9   LYS A CB  1 
ATOM   46   N  N   . HIS A 1 10  ? 32.531 -7.965  11.545  1.00 35.62  ? 10  HIS A N   1 
ATOM   47   C  CA  . HIS A 1 10  ? 33.608 -7.023  11.726  1.00 39.70  ? 10  HIS A CA  1 
ATOM   48   C  C   . HIS A 1 10  ? 33.093 -5.635  12.044  1.00 22.37  ? 10  HIS A C   1 
ATOM   49   O  O   . HIS A 1 10  ? 33.926 -4.847  12.451  1.00 22.33  ? 10  HIS A O   1 
ATOM   50   C  CB  . HIS A 1 10  ? 34.630 -7.090  10.580  1.00 39.45  ? 10  HIS A CB  1 
ATOM   51   C  CG  . HIS A 1 10  ? 35.511 -8.335  10.677  1.00 49.92  ? 10  HIS A CG  1 
ATOM   52   N  ND1 . HIS A 1 10  ? 36.692 -8.297  11.512  1.00 48.07  ? 10  HIS A ND1 1 
ATOM   53   C  CD2 . HIS A 1 10  ? 35.384 -9.663  10.146  1.00 45.44  ? 10  HIS A CD2 1 
ATOM   54   C  CE1 . HIS A 1 10  ? 37.213 -9.558  11.434  1.00 47.57  ? 10  HIS A CE1 1 
ATOM   55   N  NE2 . HIS A 1 10  ? 36.427 -10.411 10.615  1.00 47.91  ? 10  HIS A NE2 1 
ATOM   56   N  N   . ASN A 1 11  ? 31.761 -5.384  11.989  1.00 24.67  ? 11  ASN A N   1 
ATOM   57   C  CA  . ASN A 1 11  ? 31.298 -4.026  12.223  1.00 19.20  ? 11  ASN A CA  1 
ATOM   58   C  C   . ASN A 1 11  ? 29.919 -3.997  12.924  1.00 18.77  ? 11  ASN A C   1 
ATOM   59   O  O   . ASN A 1 11  ? 29.237 -2.951  12.995  1.00 19.38  ? 11  ASN A O   1 
ATOM   60   C  CB  . ASN A 1 11  ? 31.143 -3.234  10.927  1.00 19.83  ? 11  ASN A CB  1 
ATOM   61   C  CG  . ASN A 1 11  ? 30.067 -3.809  10.034  1.00 20.98  ? 11  ASN A CG  1 
ATOM   62   O  OD1 . ASN A 1 11  ? 29.471 -4.854  10.376  1.00 25.47  ? 11  ASN A OD1 1 
ATOM   63   N  ND2 . ASN A 1 11  ? 29.804 -3.160  8.900   1.00 27.20  ? 11  ASN A ND2 1 
ATOM   64   N  N   . GLY A 1 12  ? 29.584 -5.109  13.584  1.00 18.10  ? 12  GLY A N   1 
ATOM   65   C  CA  . GLY A 1 12  ? 28.307 -5.281  14.229  1.00 14.91  ? 12  GLY A CA  1 
ATOM   66   C  C   . GLY A 1 12  ? 28.245 -4.649  15.611  1.00 14.60  ? 12  GLY A C   1 
ATOM   67   O  O   . GLY A 1 12  ? 29.166 -3.978  16.093  1.00 14.38  ? 12  GLY A O   1 
ATOM   68   N  N   . PRO A 1 13  ? 27.155 -4.978  16.315  1.00 12.53  ? 13  PRO A N   1 
ATOM   69   C  CA  . PRO A 1 13  ? 26.908 -4.370  17.596  1.00 12.49  ? 13  PRO A CA  1 
ATOM   70   C  C   . PRO A 1 13  ? 28.056 -4.400  18.574  1.00 12.84  ? 13  PRO A C   1 
ATOM   71   O  O   . PRO A 1 13  ? 28.155 -3.469  19.376  1.00 13.16  ? 13  PRO A O   1 
ATOM   72   C  CB  . PRO A 1 13  ? 25.689 -5.127  18.132  1.00 14.03  ? 13  PRO A CB  1 
ATOM   73   C  CG  . PRO A 1 13  ? 24.953 -5.474  16.870  1.00 15.40  ? 13  PRO A CG  1 
ATOM   74   C  CD  . PRO A 1 13  ? 26.027 -5.789  15.824  1.00 12.68  ? 13  PRO A CD  1 
ATOM   75   N  N   . GLU A 1 14  ? 28.871 -5.440  18.559  1.00 13.01  ? 14  GLU A N   1 
ATOM   76   C  CA  . GLU A 1 14  ? 29.923 -5.538  19.547  1.00 14.17  ? 14  GLU A CA  1 
ATOM   77   C  C   . GLU A 1 14  ? 31.058 -4.548  19.248  1.00 12.75  ? 14  GLU A C   1 
ATOM   78   O  O   . GLU A 1 14  ? 31.948 -4.404  20.061  1.00 14.89  ? 14  GLU A O   1 
ATOM   79   C  CB  . GLU A 1 14  ? 30.433 -6.973  19.582  1.00 20.26  ? 14  GLU A CB  1 
ATOM   80   C  CG  . GLU A 1 14  ? 31.059 -7.457  18.264  1.00 27.92  ? 14  GLU A CG  1 
ATOM   81   C  CD  . GLU A 1 14  ? 30.302 -8.018  17.036  1.00 32.03  ? 14  GLU A CD  1 
ATOM   82   O  OE1 . GLU A 1 14  ? 29.161 -7.577  16.795  1.00 23.21  ? 14  GLU A OE1 1 
ATOM   83   O  OE2 . GLU A 1 14  ? 30.866 -8.887  16.342  1.00 28.91  ? 14  GLU A OE2 1 
ATOM   84   N  N   . HIS A 1 15  ? 31.041 -3.907  18.078  1.00 11.73  ? 15  HIS A N   1 
ATOM   85   C  CA  . HIS A 1 15  ? 32.097 -2.968  17.706  1.00 10.83  ? 15  HIS A CA  1 
ATOM   86   C  C   . HIS A 1 15  ? 31.647 -1.540  17.873  1.00 10.64  ? 15  HIS A C   1 
ATOM   87   O  O   . HIS A 1 15  ? 32.478 -0.622  17.876  1.00 11.03  ? 15  HIS A O   1 
ATOM   88   C  CB  . HIS A 1 15  ? 32.512 -3.128  16.252  1.00 11.89  ? 15  HIS A CB  1 
ATOM   89   C  CG  . HIS A 1 15  ? 33.177 -4.428  15.986  1.00 14.23  ? 15  HIS A CG  1 
ATOM   90   N  ND1 . HIS A 1 15  ? 34.535 -4.547  16.131  1.00 15.28  ? 15  HIS A ND1 1 
ATOM   91   C  CD2 . HIS A 1 15  ? 32.690 -5.641  15.629  1.00 16.34  ? 15  HIS A CD2 1 
ATOM   92   C  CE1 . HIS A 1 15  ? 34.866 -5.816  15.886  1.00 18.29  ? 15  HIS A CE1 1 
ATOM   93   N  NE2 . HIS A 1 15  ? 33.781 -6.478  15.554  1.00 23.08  ? 15  HIS A NE2 1 
ATOM   94   N  N   . TRP A 1 16  ? 30.336 -1.295  18.043  1.00 11.04  ? 16  TRP A N   1 
ATOM   95   C  CA  . TRP A 1 16  ? 29.830 0.066   17.963  1.00 9.44   ? 16  TRP A CA  1 
ATOM   96   C  C   . TRP A 1 16  ? 30.447 1.006   19.015  1.00 10.51  ? 16  TRP A C   1 
ATOM   97   O  O   . TRP A 1 16  ? 30.582 2.208   18.784  1.00 10.78  ? 16  TRP A O   1 
ATOM   98   C  CB  . TRP A 1 16  ? 28.301 0.046   18.079  1.00 9.63   ? 16  TRP A CB  1 
ATOM   99   C  CG  . TRP A 1 16  ? 27.642 -0.610  16.908  1.00 10.62  ? 16  TRP A CG  1 
ATOM   100  C  CD1 . TRP A 1 16  ? 28.186 -1.008  15.707  1.00 11.92  ? 16  TRP A CD1 1 
ATOM   101  C  CD2 . TRP A 1 16  ? 26.242 -0.962  16.838  1.00 9.73   ? 16  TRP A CD2 1 
ATOM   102  N  NE1 . TRP A 1 16  ? 27.230 -1.556  14.888  1.00 13.06  ? 16  TRP A NE1 1 
ATOM   103  C  CE2 . TRP A 1 16  ? 26.027 -1.496  15.554  1.00 11.39  ? 16  TRP A CE2 1 
ATOM   104  C  CE3 . TRP A 1 16  ? 25.170 -0.825  17.709  1.00 9.07   ? 16  TRP A CE3 1 
ATOM   105  C  CZ2 . TRP A 1 16  ? 24.774 -1.964  15.168  1.00 11.39  ? 16  TRP A CZ2 1 
ATOM   106  C  CZ3 . TRP A 1 16  ? 23.932 -1.269  17.317  1.00 9.80   ? 16  TRP A CZ3 1 
ATOM   107  C  CH2 . TRP A 1 16  ? 23.727 -1.831  16.075  1.00 11.29  ? 16  TRP A CH2 1 
ATOM   108  N  N   . HIS A 1 17  ? 30.806 0.464   20.173  1.00 9.97   ? 17  HIS A N   1 
ATOM   109  C  CA  . HIS A 1 17  ? 31.288 1.283   21.280  1.00 10.27  ? 17  HIS A CA  1 
ATOM   110  C  C   . HIS A 1 17  ? 32.537 2.089   20.885  1.00 11.37  ? 17  HIS A C   1 
ATOM   111  O  O   . HIS A 1 17  ? 32.835 3.109   21.514  1.00 13.43  ? 17  HIS A O   1 
ATOM   112  C  CB  . HIS A 1 17  ? 31.547 0.455   22.527  1.00 10.54  ? 17  HIS A CB  1 
ATOM   113  C  CG  . HIS A 1 17  ? 32.749 -0.409  22.398  1.00 12.17  ? 17  HIS A CG  1 
ATOM   114  N  ND1 . HIS A 1 17  ? 33.966 -0.059  22.938  1.00 14.09  ? 17  HIS A ND1 1 
ATOM   115  C  CD2 . HIS A 1 17  ? 32.907 -1.576  21.753  1.00 12.92  ? 17  HIS A CD2 1 
ATOM   116  C  CE1 . HIS A 1 17  ? 34.834 -0.999  22.611  1.00 13.49  ? 17  HIS A CE1 1 
ATOM   117  N  NE2 . HIS A 1 17  ? 34.232 -1.957  21.910  1.00 12.48  ? 17  HIS A NE2 1 
ATOM   118  N  N   . LYS A 1 18  ? 33.322 1.582   19.931  1.00 10.58  ? 18  LYS A N   1 
ATOM   119  C  CA  . LYS A 1 18  ? 34.559 2.298   19.579  1.00 11.65  ? 18  LYS A CA  1 
ATOM   120  C  C   . LYS A 1 18  ? 34.242 3.647   18.946  1.00 13.40  ? 18  LYS A C   1 
ATOM   121  O  O   . LYS A 1 18  ? 34.989 4.580   19.171  1.00 19.54  ? 18  LYS A O   1 
ATOM   122  C  CB  . LYS A 1 18  ? 35.384 1.406   18.651  1.00 12.64  ? 18  LYS A CB  1 
ATOM   123  C  CG  . LYS A 1 18  ? 35.977 0.172   19.326  1.00 13.65  ? 18  LYS A CG  1 
ATOM   124  C  CD  . LYS A 1 18  ? 36.717 -0.800  18.408  1.00 13.43  ? 18  LYS A CD  1 
ATOM   125  C  CE  . LYS A 1 18  ? 35.717 -1.711  17.736  1.00 11.75  ? 18  LYS A CE  1 
ATOM   126  N  NZ  . LYS A 1 18  ? 36.407 -2.505  16.685  1.00 12.91  ? 18  LYS A NZ  1 
ATOM   127  N  N   . ASP A 1 19  ? 33.190 3.761   18.117  1.00 12.44  ? 19  ASP A N   1 
ATOM   128  C  CA  . ASP A 1 19  ? 32.784 5.022   17.517  1.00 13.38  ? 19  ASP A CA  1 
ATOM   129  C  C   . ASP A 1 19  ? 31.755 5.737   18.387  1.00 12.73  ? 19  ASP A C   1 
ATOM   130  O  O   . ASP A 1 19  ? 31.659 6.958   18.299  1.00 15.38  ? 19  ASP A O   1 
ATOM   131  C  CB  . ASP A 1 19  ? 32.254 4.822   16.091  1.00 16.53  ? 19  ASP A CB  1 
ATOM   132  C  CG  . ASP A 1 19  ? 33.398 4.517   15.145  1.00 27.93  ? 19  ASP A CG  1 
ATOM   133  O  OD1 . ASP A 1 19  ? 34.333 5.351   15.050  1.00 27.30  ? 19  ASP A OD1 1 
ATOM   134  O  OD2 . ASP A 1 19  ? 33.381 3.411   14.527  1.00 45.93  ? 19  ASP A OD2 1 
ATOM   135  N  N   . PHE A 1 20  ? 30.981 4.980   19.184  1.00 10.27  ? 20  PHE A N   1 
ATOM   136  C  CA  . PHE A 1 20  ? 29.867 5.569   19.915  1.00 11.35  ? 20  PHE A CA  1 
ATOM   137  C  C   . PHE A 1 20  ? 29.980 5.039   21.324  1.00 11.19  ? 20  PHE A C   1 
ATOM   138  O  O   . PHE A 1 20  ? 29.322 4.019   21.672  1.00 11.78  ? 20  PHE A O   1 
ATOM   139  C  CB  . PHE A 1 20  ? 28.553 5.111   19.255  1.00 14.30  ? 20  PHE A CB  1 
ATOM   140  C  CG  . PHE A 1 20  ? 28.494 5.485   17.807  1.00 13.13  ? 20  PHE A CG  1 
ATOM   141  C  CD1 . PHE A 1 20  ? 28.150 6.780   17.421  1.00 15.67  ? 20  PHE A CD1 1 
ATOM   142  C  CD2 . PHE A 1 20  ? 28.869 4.560   16.839  1.00 15.06  ? 20  PHE A CD2 1 
ATOM   143  C  CE1 . PHE A 1 20  ? 28.172 7.130   16.074  1.00 18.15  ? 20  PHE A CE1 1 
ATOM   144  C  CE2 . PHE A 1 20  ? 28.858 4.890   15.494  1.00 15.77  ? 20  PHE A CE2 1 
ATOM   145  C  CZ  . PHE A 1 20  ? 28.555 6.186   15.128  1.00 16.10  ? 20  PHE A CZ  1 
ATOM   146  N  N   . PRO A 1 21  ? 30.809 5.671   22.197  1.00 11.98  ? 21  PRO A N   1 
ATOM   147  C  CA  . PRO A 1 21  ? 31.046 5.140   23.542  1.00 11.47  ? 21  PRO A CA  1 
ATOM   148  C  C   . PRO A 1 21  ? 29.814 5.012   24.415  1.00 11.06  ? 21  PRO A C   1 
ATOM   149  O  O   . PRO A 1 21  ? 29.812 4.222   25.359  1.00 11.93  ? 21  PRO A O   1 
ATOM   150  C  CB  . PRO A 1 21  ? 32.088 6.114   24.175  1.00 14.79  ? 21  PRO A CB  1 
ATOM   151  C  CG  . PRO A 1 21  ? 32.251 7.238   23.195  1.00 21.40  ? 21  PRO A CG  1 
ATOM   152  C  CD  . PRO A 1 21  ? 31.681 6.812   21.864  1.00 15.08  ? 21  PRO A CD  1 
ATOM   153  N  N   . ILE A 1 22  ? 28.758 5.769   24.050  1.00 10.98  ? 22  ILE A N   1 
ATOM   154  C  CA  . ILE A 1 22  ? 27.489 5.635   24.775  1.00 10.41  ? 22  ILE A CA  1 
ATOM   155  C  C   . ILE A 1 22  ? 26.902 4.228   24.628  1.00 9.24   ? 22  ILE A C   1 
ATOM   156  O  O   . ILE A 1 22  ? 25.981 3.855   25.373  1.00 9.80   ? 22  ILE A O   1 
ATOM   157  C  CB  . ILE A 1 22  ? 26.484 6.717   24.340  1.00 10.36  ? 22  ILE A CB  1 
ATOM   158  C  CG1 . ILE A 1 22  ? 25.412 6.975   25.393  1.00 12.16  ? 22  ILE A CG1 1 
ATOM   159  C  CG2 . ILE A 1 22  ? 25.879 6.381   22.973  1.00 11.83  ? 22  ILE A CG2 1 
ATOM   160  C  CD1 . ILE A 1 22  ? 25.962 7.466   26.703  1.00 16.85  ? 22  ILE A CD1 1 
ATOM   161  N  N   . ALA A 1 23  ? 27.465 3.407   23.699  1.00 9.58   ? 23  ALA A N   1 
ATOM   162  C  CA  . ALA A 1 23  ? 27.014 2.014   23.567  1.00 9.47   ? 23  ALA A CA  1 
ATOM   163  C  C   . ALA A 1 23  ? 27.107 1.280   24.898  1.00 9.76   ? 23  ALA A C   1 
ATOM   164  O  O   . ALA A 1 23  ? 26.387 0.311   25.107  1.00 10.17  ? 23  ALA A O   1 
ATOM   165  C  CB  . ALA A 1 23  ? 27.845 1.302   22.532  1.00 9.76   ? 23  ALA A CB  1 
ATOM   166  N  N   . LYS A 1 24  ? 28.005 1.733   25.804  1.00 11.10  ? 24  LYS A N   1 
ATOM   167  C  CA  . LYS A 1 24  ? 28.167 1.097   27.112  1.00 11.99  ? 24  LYS A CA  1 
ATOM   168  C  C   . LYS A 1 24  ? 27.544 1.959   28.198  1.00 12.64  ? 24  LYS A C   1 
ATOM   169  O  O   . LYS A 1 24  ? 27.963 1.878   29.366  1.00 14.33  ? 24  LYS A O   1 
ATOM   170  C  CB  . LYS A 1 24  ? 29.650 0.896   27.396  1.00 13.80  ? 24  LYS A CB  1 
ATOM   171  C  CG  . LYS A 1 24  ? 30.322 -0.084  26.439  1.00 15.19  ? 24  LYS A CG  1 
ATOM   172  C  CD  . LYS A 1 24  ? 31.742 -0.426  26.883  1.00 21.63  ? 24  LYS A CD  1 
ATOM   173  C  CE  . LYS A 1 24  ? 32.494 -1.313  25.933  1.00 21.82  ? 24  LYS A CE  1 
ATOM   174  N  NZ  . LYS A 1 24  ? 32.144 -2.716  26.156  1.00 27.65  ? 24  LYS A NZ  1 
ATOM   175  N  N   . GLY A 1 25  ? 26.556 2.784   27.799  1.00 12.09  ? 25  GLY A N   1 
ATOM   176  C  CA  . GLY A 1 25  ? 25.962 3.753   28.731  1.00 12.34  ? 25  GLY A CA  1 
ATOM   177  C  C   . GLY A 1 25  ? 24.970 3.113   29.708  1.00 11.05  ? 25  GLY A C   1 
ATOM   178  O  O   . GLY A 1 25  ? 24.802 1.888   29.790  1.00 12.17  ? 25  GLY A O   1 
ATOM   179  N  N   . GLU A 1 26  ? 24.288 3.977   30.476  1.00 11.57  ? 26  GLU A N   1 
ATOM   180  C  CA  . GLU A 1 26  ? 23.415 3.524   31.552  1.00 12.98  ? 26  GLU A CA  1 
ATOM   181  C  C   . GLU A 1 26  ? 21.972 3.289   31.153  1.00 10.57  ? 26  GLU A C   1 
ATOM   182  O  O   . GLU A 1 26  ? 21.194 2.776   31.950  1.00 13.06  ? 26  GLU A O   1 
ATOM   183  C  CB  . GLU A 1 26  ? 23.403 4.580   32.665  1.00 15.99  ? 26  GLU A CB  1 
ATOM   184  C  CG  . GLU A 1 26  ? 24.806 4.808   33.193  1.00 19.83  ? 26  GLU A CG  1 
ATOM   185  C  CD  . GLU A 1 26  ? 25.425 3.562   33.823  1.00 23.87  ? 26  GLU A CD  1 
ATOM   186  O  OE1 . GLU A 1 26  ? 24.730 2.902   34.653  1.00 29.56  ? 26  GLU A OE1 1 
ATOM   187  O  OE2 . GLU A 1 26  ? 26.597 3.239   33.465  1.00 31.19  ? 26  GLU A OE2 1 
ATOM   188  N  N   . ARG A 1 27  ? 21.596 3.673   29.935  1.00 8.84   ? 27  ARG A N   1 
ATOM   189  C  CA  . ARG A 1 27  ? 20.210 3.507   29.506  1.00 8.08   ? 27  ARG A CA  1 
ATOM   190  C  C   . ARG A 1 27  ? 20.150 3.031   28.052  1.00 7.97   ? 27  ARG A C   1 
ATOM   191  O  O   . ARG A 1 27  ? 19.433 3.610   27.216  1.00 8.28   ? 27  ARG A O   1 
ATOM   192  C  CB  . ARG A 1 27  ? 19.315 4.728   29.785  1.00 12.44  ? 27  ARG A CB  1 
ATOM   193  C  CG  . ARG A 1 27  ? 19.705 6.057   29.204  1.00 15.56  ? 27  ARG A CG  1 
ATOM   194  C  CD  . ARG A 1 27  ? 18.712 7.188   29.412  1.00 19.29  ? 27  ARG A CD  1 
ATOM   195  N  NE  . ARG A 1 27  ? 17.598 7.129   28.474  1.00 16.51  ? 27  ARG A NE  1 
ATOM   196  C  CZ  . ARG A 1 27  ? 16.704 8.097   28.305  1.00 12.22  ? 27  ARG A CZ  1 
ATOM   197  N  NH1 . ARG A 1 27  ? 16.791 9.208   29.015  1.00 13.01  ? 27  ARG A NH1 1 
ATOM   198  N  NH2 . ARG A 1 27  ? 15.729 7.949   27.426  1.00 14.99  ? 27  ARG A NH2 1 
ATOM   199  N  N   . GLN A 1 28  ? 20.857 1.941   27.728  1.00 6.99   ? 28  GLN A N   1 
ATOM   200  C  CA  . GLN A 1 28  ? 20.889 1.435   26.350  1.00 7.11   ? 28  GLN A CA  1 
ATOM   201  C  C   . GLN A 1 28  ? 19.727 0.488   26.095  1.00 6.43   ? 28  GLN A C   1 
ATOM   202  O  O   . GLN A 1 28  ? 19.228 -0.216  26.993  1.00 7.57   ? 28  GLN A O   1 
ATOM   203  C  CB  . GLN A 1 28  ? 22.253 0.748   26.170  1.00 7.39   ? 28  GLN A CB  1 
ATOM   204  C  CG  . GLN A 1 28  ? 23.408 1.789   26.092  1.00 7.38   ? 28  GLN A CG  1 
ATOM   205  C  CD  . GLN A 1 28  ? 23.309 2.585   24.805  1.00 7.79   ? 28  GLN A CD  1 
ATOM   206  O  OE1 . GLN A 1 28  ? 23.494 2.065   23.708  1.00 8.18   ? 28  GLN A OE1 1 
ATOM   207  N  NE2 . GLN A 1 28  ? 22.933 3.861   24.903  1.00 8.00   ? 28  GLN A NE2 1 
ATOM   208  N  N   . SER A 1 29  ? 19.355 0.451   24.808  1.00 6.21   ? 29  SER A N   1 
ATOM   209  C  CA  . SER A 1 29  ? 18.299 -0.417  24.345  1.00 5.58   ? 29  SER A CA  1 
ATOM   210  C  C   . SER A 1 29  ? 18.818 -1.288  23.239  1.00 6.59   ? 29  SER A C   1 
ATOM   211  O  O   . SER A 1 29  ? 19.768 -0.963  22.547  1.00 7.15   ? 29  SER A O   1 
ATOM   212  C  CB  . SER A 1 29  ? 17.120 0.427   23.811  1.00 6.43   ? 29  SER A CB  1 
ATOM   213  O  OG  . SER A 1 29  ? 16.538 1.177   24.862  1.00 6.39   ? 29  SER A OG  1 
ATOM   214  N  N   . PRO A 1 30  ? 18.162 -2.415  22.919  1.00 6.03   ? 30  PRO A N   1 
ATOM   215  C  CA  . PRO A 1 30  ? 16.985 -2.948  23.625  1.00 5.97   ? 30  PRO A CA  1 
ATOM   216  C  C   . PRO A 1 30  ? 17.401 -3.647  24.922  1.00 6.05   ? 30  PRO A C   1 
ATOM   217  O  O   . PRO A 1 30  ? 18.591 -3.671  25.276  1.00 7.50   ? 30  PRO A O   1 
ATOM   218  C  CB  . PRO A 1 30  ? 16.435 -3.949  22.603  1.00 6.23   ? 30  PRO A CB  1 
ATOM   219  C  CG  . PRO A 1 30  ? 17.734 -4.530  22.016  1.00 6.39   ? 30  PRO A CG  1 
ATOM   220  C  CD  . PRO A 1 30  ? 18.638 -3.321  21.835  1.00 6.08   ? 30  PRO A CD  1 
ATOM   221  N  N   . VAL A 1 31  ? 16.404 -4.184  25.608  1.00 6.64   ? 31  VAL A N   1 
ATOM   222  C  CA  . VAL A 1 31  ? 16.608 -4.960  26.824  1.00 6.89   ? 31  VAL A CA  1 
ATOM   223  C  C   . VAL A 1 31  ? 15.694 -6.164  26.783  1.00 6.45   ? 31  VAL A C   1 
ATOM   224  O  O   . VAL A 1 31  ? 14.733 -6.251  26.012  1.00 7.64   ? 31  VAL A O   1 
ATOM   225  C  CB  . VAL A 1 31  ? 16.282 -4.138  28.111  1.00 7.29   ? 31  VAL A CB  1 
ATOM   226  C  CG1 . VAL A 1 31  ? 17.197 -2.901  28.190  1.00 8.91   ? 31  VAL A CG1 1 
ATOM   227  C  CG2 . VAL A 1 31  ? 14.806 -3.712  28.139  1.00 8.28   ? 31  VAL A CG2 1 
ATOM   228  N  N   . ASP A 1 32  ? 16.052 -7.155  27.635  1.00 7.26   ? 32  ASP A N   1 
ATOM   229  C  CA  . ASP A 1 32  ? 15.136 -8.231  27.941  1.00 8.02   ? 32  ASP A CA  1 
ATOM   230  C  C   . ASP A 1 32  ? 14.061 -7.730  28.910  1.00 7.35   ? 32  ASP A C   1 
ATOM   231  O  O   . ASP A 1 32  ? 14.364 -7.047  29.898  1.00 9.63   ? 32  ASP A O   1 
ATOM   232  C  CB  . ASP A 1 32  ? 15.872 -9.415  28.526  1.00 8.64   ? 32  ASP A CB  1 
ATOM   233  C  CG  . ASP A 1 32  ? 14.910 -10.566 28.814  1.00 9.90   ? 32  ASP A CG  1 
ATOM   234  O  OD1 . ASP A 1 32  ? 14.215 -11.019 27.896  1.00 9.17   ? 32  ASP A OD1 1 
ATOM   235  O  OD2 . ASP A 1 32  ? 14.889 -11.013 29.991  1.00 12.35  ? 32  ASP A OD2 1 
ATOM   236  N  N   . ILE A 1 33  ? 12.797 -8.046  28.601  1.00 8.01   ? 33  ILE A N   1 
ATOM   237  C  CA  . ILE A 1 33  ? 11.670 -7.662  29.439  1.00 9.69   ? 33  ILE A CA  1 
ATOM   238  C  C   . ILE A 1 33  ? 11.371 -8.910  30.267  1.00 9.85   ? 33  ILE A C   1 
ATOM   239  O  O   . ILE A 1 33  ? 10.832 -9.911  29.769  1.00 11.43  ? 33  ILE A O   1 
ATOM   240  C  CB  . ILE A 1 33  ? 10.469 -7.190  28.613  1.00 8.88   ? 33  ILE A CB  1 
ATOM   241  C  CG1 . ILE A 1 33  ? 10.869 -5.991  27.751  1.00 9.83   ? 33  ILE A CG1 1 
ATOM   242  C  CG2 . ILE A 1 33  ? 9.245  -6.955  29.533  1.00 10.64  ? 33  ILE A CG2 1 
ATOM   243  C  CD1 . ILE A 1 33  ? 9.811  -5.649  26.728  1.00 11.19  ? 33  ILE A CD1 1 
ATOM   244  N  N   A ASP A 1 34  ? 11.772 -8.868  31.550  0.50 9.91   ? 34  ASP A N   1 
ATOM   245  N  N   B ASP A 1 34  ? 11.803 -8.895  31.519  0.50 9.74   ? 34  ASP A N   1 
ATOM   246  C  CA  A ASP A 1 34  ? 11.479 -9.915  32.538  0.50 12.14  ? 34  ASP A CA  1 
ATOM   247  C  CA  B ASP A 1 34  ? 11.512 -10.011 32.409  0.50 11.16  ? 34  ASP A CA  1 
ATOM   248  C  C   A ASP A 1 34  ? 10.051 -9.681  33.049  0.50 13.24  ? 34  ASP A C   1 
ATOM   249  C  C   B ASP A 1 34  ? 10.124 -9.732  33.007  0.50 12.69  ? 34  ASP A C   1 
ATOM   250  O  O   A ASP A 1 34  ? 9.798  -8.774  33.860  0.50 15.68  ? 34  ASP A O   1 
ATOM   251  O  O   B ASP A 1 34  ? 9.981  -8.818  33.836  0.50 14.30  ? 34  ASP A O   1 
ATOM   252  C  CB  A ASP A 1 34  ? 12.431 -9.849  33.743  0.50 13.34  ? 34  ASP A CB  1 
ATOM   253  C  CB  B ASP A 1 34  ? 12.621 -10.092 33.454  0.50 14.13  ? 34  ASP A CB  1 
ATOM   254  C  CG  A ASP A 1 34  ? 12.218 -10.943 34.789  0.50 15.23  ? 34  ASP A CG  1 
ATOM   255  C  CG  B ASP A 1 34  ? 12.468 -11.298 34.357  0.50 15.48  ? 34  ASP A CG  1 
ATOM   256  O  OD1 A ASP A 1 34  ? 11.100 -11.527 34.846  0.50 14.35  ? 34  ASP A OD1 1 
ATOM   257  O  OD1 B ASP A 1 34  ? 12.899 -12.411 33.966  0.50 17.49  ? 34  ASP A OD1 1 
ATOM   258  O  OD2 A ASP A 1 34  ? 13.175 -11.248 35.525  0.50 19.70  ? 34  ASP A OD2 1 
ATOM   259  O  OD2 B ASP A 1 34  ? 11.870 -11.143 35.456  0.50 16.48  ? 34  ASP A OD2 1 
ATOM   260  N  N   . THR A 1 35  ? 9.099  -10.478 32.549  1.00 13.76  ? 35  THR A N   1 
ATOM   261  C  CA  . THR A 1 35  ? 7.700  -10.158 32.764  1.00 14.50  ? 35  THR A CA  1 
ATOM   262  C  C   . THR A 1 35  ? 7.374  -10.280 34.233  1.00 14.50  ? 35  THR A C   1 
ATOM   263  O  O   . THR A 1 35  ? 6.425  -9.647  34.699  1.00 19.61  ? 35  THR A O   1 
ATOM   264  C  CB  . THR A 1 35  ? 6.776  -11.056 31.925  1.00 18.78  ? 35  THR A CB  1 
ATOM   265  O  OG1 . THR A 1 35  ? 6.918  -12.392 32.412  1.00 18.96  ? 35  THR A OG1 1 
ATOM   266  C  CG2 . THR A 1 35  ? 6.971  -10.938 30.420  1.00 20.87  ? 35  THR A CG2 1 
ATOM   267  N  N   . HIS A 1 36  ? 8.130  -11.125 34.952  1.00 17.72  ? 36  HIS A N   1 
ATOM   268  C  CA  . HIS A 1 36  ? 7.925  -11.296 36.365  1.00 19.50  ? 36  HIS A CA  1 
ATOM   269  C  C   . HIS A 1 36  ? 8.408  -10.131 37.189  1.00 21.91  ? 36  HIS A C   1 
ATOM   270  O  O   . HIS A 1 36  ? 7.830  -9.922  38.244  1.00 33.27  ? 36  HIS A O   1 
ATOM   271  C  CB  . HIS A 1 36  ? 8.565  -12.590 36.871  1.00 18.88  ? 36  HIS A CB  1 
ATOM   272  C  CG  . HIS A 1 36  ? 7.948  -13.702 36.139  1.00 23.26  ? 36  HIS A CG  1 
ATOM   273  N  ND1 . HIS A 1 36  ? 8.642  -14.390 35.126  1.00 27.80  ? 36  HIS A ND1 1 
ATOM   274  C  CD2 . HIS A 1 36  ? 6.690  -14.184 36.164  1.00 24.88  ? 36  HIS A CD2 1 
ATOM   275  C  CE1 . HIS A 1 36  ? 7.842  -15.308 34.632  1.00 25.18  ? 36  HIS A CE1 1 
ATOM   276  N  NE2 . HIS A 1 36  ? 6.663  -15.236 35.269  1.00 26.95  ? 36  HIS A NE2 1 
ATOM   277  N  N   . THR A 1 37  ? 9.447  -9.421  36.760  1.00 18.47  ? 37  THR A N   1 
ATOM   278  C  CA  . THR A 1 37  ? 9.958  -8.300  37.531  1.00 20.10  ? 37  THR A CA  1 
ATOM   279  C  C   . THR A 1 37  ? 9.476  -6.934  37.057  1.00 16.78  ? 37  THR A C   1 
ATOM   280  O  O   . THR A 1 37  ? 9.643  -5.947  37.772  1.00 23.65  ? 37  THR A O   1 
ATOM   281  C  CB  . THR A 1 37  ? 11.477 -8.270  37.611  1.00 25.57  ? 37  THR A CB  1 
ATOM   282  O  OG1 . THR A 1 37  ? 11.969 -8.297  36.293  1.00 32.41  ? 37  THR A OG1 1 
ATOM   283  C  CG2 . THR A 1 37  ? 11.981 -9.567  38.181  1.00 22.24  ? 37  THR A CG2 1 
ATOM   284  N  N   . ALA A 1 38  ? 8.752  -6.855  35.949  1.00 15.70  ? 38  ALA A N   1 
ATOM   285  C  CA  . ALA A 1 38  ? 8.176  -5.603  35.532  1.00 15.94  ? 38  ALA A CA  1 
ATOM   286  C  C   . ALA A 1 38  ? 7.071  -5.315  36.536  1.00 17.41  ? 38  ALA A C   1 
ATOM   287  O  O   . ALA A 1 38  ? 6.352  -6.190  36.995  1.00 24.72  ? 38  ALA A O   1 
ATOM   288  C  CB  . ALA A 1 38  ? 7.636  -5.747  34.137  1.00 15.27  ? 38  ALA A CB  1 
ATOM   289  N  N   A LYS A 1 39  ? 6.926  -4.057  36.887  0.50 18.22  ? 39  LYS A N   1 
ATOM   290  N  N   B LYS A 1 39  ? 6.996  -4.096  37.011  0.50 15.97  ? 39  LYS A N   1 
ATOM   291  C  CA  A LYS A 1 39  ? 6.027  -3.602  37.944  0.50 17.54  ? 39  LYS A CA  1 
ATOM   292  C  CA  B LYS A 1 39  ? 5.901  -3.838  37.933  0.50 16.92  ? 39  LYS A CA  1 
ATOM   293  C  C   A LYS A 1 39  ? 4.772  -2.997  37.303  0.50 13.93  ? 39  LYS A C   1 
ATOM   294  C  C   B LYS A 1 39  ? 4.766  -3.065  37.271  0.50 13.83  ? 39  LYS A C   1 
ATOM   295  O  O   A LYS A 1 39  ? 4.888  -2.045  36.531  0.50 12.65  ? 39  LYS A O   1 
ATOM   296  O  O   B LYS A 1 39  ? 4.932  -2.075  36.547  0.50 12.56  ? 39  LYS A O   1 
ATOM   297  C  CB  A LYS A 1 39  ? 6.813  -2.502  38.672  0.50 19.64  ? 39  LYS A CB  1 
ATOM   298  C  CB  B LYS A 1 39  ? 6.329  -3.114  39.198  0.50 19.03  ? 39  LYS A CB  1 
ATOM   299  C  CG  A LYS A 1 39  ? 6.025  -1.589  39.598  0.50 21.14  ? 39  LYS A CG  1 
ATOM   300  C  CG  B LYS A 1 39  ? 5.262  -3.138  40.270  0.50 17.00  ? 39  LYS A CG  1 
ATOM   301  C  CD  A LYS A 1 39  ? 6.008  -2.116  40.991  0.50 21.35  ? 39  LYS A CD  1 
ATOM   302  C  CD  B LYS A 1 39  ? 5.549  -2.167  41.394  0.50 19.32  ? 39  LYS A CD  1 
ATOM   303  C  CE  A LYS A 1 39  ? 5.363  -1.127  41.922  0.50 24.74  ? 39  LYS A CE  1 
ATOM   304  C  CE  B LYS A 1 39  ? 4.562  -2.344  42.527  0.50 19.77  ? 39  LYS A CE  1 
ATOM   305  N  NZ  A LYS A 1 39  ? 4.943  -1.859  43.134  0.50 25.51  ? 39  LYS A NZ  1 
ATOM   306  N  NZ  B LYS A 1 39  ? 4.914  -1.396  43.607  0.50 20.65  ? 39  LYS A NZ  1 
ATOM   307  N  N   . TYR A 1 40  ? 3.571  -3.531  37.584  1.00 15.57  ? 40  TYR A N   1 
ATOM   308  C  CA  . TYR A 1 40  ? 2.326  -2.862  37.218  1.00 15.12  ? 40  TYR A CA  1 
ATOM   309  C  C   . TYR A 1 40  ? 2.318  -1.477  37.856  1.00 13.98  ? 40  TYR A C   1 
ATOM   310  O  O   . TYR A 1 40  ? 2.508  -1.345  39.089  1.00 16.61  ? 40  TYR A O   1 
ATOM   311  C  CB  . TYR A 1 40  ? 1.083  -3.663  37.640  1.00 19.82  ? 40  TYR A CB  1 
ATOM   312  C  CG  . TYR A 1 40  ? -0.186 -2.869  37.527  1.00 22.42  ? 40  TYR A CG  1 
ATOM   313  C  CD1 . TYR A 1 40  ? -0.606 -2.386  36.304  1.00 21.69  ? 40  TYR A CD1 1 
ATOM   314  C  CD2 . TYR A 1 40  ? -0.990 -2.627  38.640  1.00 28.12  ? 40  TYR A CD2 1 
ATOM   315  C  CE1 . TYR A 1 40  ? -1.760 -1.648  36.160  1.00 25.82  ? 40  TYR A CE1 1 
ATOM   316  C  CE2 . TYR A 1 40  ? -2.154 -1.883  38.520  1.00 30.33  ? 40  TYR A CE2 1 
ATOM   317  C  CZ  . TYR A 1 40  ? -2.551 -1.414  37.273  1.00 27.88  ? 40  TYR A CZ  1 
ATOM   318  O  OH  . TYR A 1 40  ? -3.669 -0.667  37.130  1.00 35.33  ? 40  TYR A OH  1 
ATOM   319  N  N   . ASP A 1 41  ? 2.076  -0.473  37.013  1.00 13.95  ? 41  ASP A N   1 
ATOM   320  C  CA  . ASP A 1 41  ? 2.019  0.911   37.480  1.00 14.39  ? 41  ASP A CA  1 
ATOM   321  C  C   . ASP A 1 41  ? 0.612  1.431   37.256  1.00 20.80  ? 41  ASP A C   1 
ATOM   322  O  O   . ASP A 1 41  ? 0.303  1.840   36.136  1.00 20.50  ? 41  ASP A O   1 
ATOM   323  C  CB  . ASP A 1 41  ? 3.029  1.783   36.730  1.00 17.14  ? 41  ASP A CB  1 
ATOM   324  C  CG  . ASP A 1 41  ? 3.195  3.178   37.296  1.00 24.01  ? 41  ASP A CG  1 
ATOM   325  O  OD1 . ASP A 1 41  ? 2.337  3.617   38.055  1.00 24.97  ? 41  ASP A OD1 1 
ATOM   326  O  OD2 . ASP A 1 41  ? 4.214  3.823   36.963  1.00 27.31  ? 41  ASP A OD2 1 
ATOM   327  N  N   . PRO A 1 42  ? -0.241 1.492   38.323  1.00 24.22  ? 42  PRO A N   1 
ATOM   328  C  CA  . PRO A 1 42  ? -1.633 1.922   38.158  1.00 28.32  ? 42  PRO A CA  1 
ATOM   329  C  C   . PRO A 1 42  ? -1.712 3.380   37.739  1.00 29.12  ? 42  PRO A C   1 
ATOM   330  O  O   . PRO A 1 42  ? -2.763 3.835   37.248  1.00 36.53  ? 42  PRO A O   1 
ATOM   331  C  CB  . PRO A 1 42  ? -2.218 1.775   39.569  1.00 39.99  ? 42  PRO A CB  1 
ATOM   332  C  CG  . PRO A 1 42  ? -0.983 1.895   40.445  1.00 38.45  ? 42  PRO A CG  1 
ATOM   333  C  CD  . PRO A 1 42  ? 0.042  1.069   39.713  1.00 23.88  ? 42  PRO A CD  1 
ATOM   334  N  N   . SER A 1 43  ? -0.609 4.125   37.946  1.00 23.28  ? 43  SER A N   1 
ATOM   335  C  CA  . SER A 1 43  ? -0.687 5.521   37.530  1.00 29.89  ? 43  SER A CA  1 
ATOM   336  C  C   . SER A 1 43  ? -0.383 5.733   36.026  1.00 26.98  ? 43  SER A C   1 
ATOM   337  O  O   . SER A 1 43  ? -0.540 6.858   35.522  1.00 35.21  ? 43  SER A O   1 
ATOM   338  C  CB  . SER A 1 43  ? 0.194  6.350   38.377  1.00 34.03  ? 43  SER A CB  1 
ATOM   339  O  OG  . SER A 1 43  ? 1.508  6.206   37.903  1.00 31.47  ? 43  SER A OG  1 
ATOM   340  N  N   . LEU A 1 44  ? 0.075  4.706   35.282  1.00 23.38  ? 44  LEU A N   1 
ATOM   341  C  CA  . LEU A 1 44  ? 0.211  4.856   33.831  1.00 22.37  ? 44  LEU A CA  1 
ATOM   342  C  C   . LEU A 1 44  ? -1.147 5.025   33.161  1.00 26.12  ? 44  LEU A C   1 
ATOM   343  O  O   . LEU A 1 44  ? -2.111 4.375   33.525  1.00 32.24  ? 44  LEU A O   1 
ATOM   344  C  CB  . LEU A 1 44  ? 0.895  3.631   33.222  1.00 20.48  ? 44  LEU A CB  1 
ATOM   345  C  CG  . LEU A 1 44  ? 2.381  3.515   33.479  1.00 16.17  ? 44  LEU A CG  1 
ATOM   346  C  CD1 . LEU A 1 44  ? 2.783  2.136   32.959  1.00 17.78  ? 44  LEU A CD1 1 
ATOM   347  C  CD2 . LEU A 1 44  ? 3.109  4.603   32.670  1.00 16.45  ? 44  LEU A CD2 1 
ATOM   348  N  N   . LYS A 1 45  ? -1.190 5.796   32.083  1.00 23.92  ? 45  LYS A N   1 
ATOM   349  C  CA  . LYS A 1 45  ? -2.445 5.920   31.346  1.00 26.26  ? 45  LYS A CA  1 
ATOM   350  C  C   . LYS A 1 45  ? -2.511 5.035   30.110  1.00 21.07  ? 45  LYS A C   1 
ATOM   351  O  O   . LYS A 1 45  ? -1.534 4.415   29.680  1.00 22.15  ? 45  LYS A O   1 
ATOM   352  C  CB  . LYS A 1 45  ? -2.747 7.332   30.933  1.00 23.94  ? 45  LYS A CB  1 
ATOM   353  C  CG  . LYS A 1 45  ? -2.664 8.308   32.078  1.00 29.53  ? 45  LYS A CG  1 
ATOM   354  C  CD  . LYS A 1 45  ? -2.394 9.681   31.588  1.00 36.83  ? 45  LYS A CD  1 
ATOM   355  C  CE  . LYS A 1 45  ? -1.794 10.554  32.674  1.00 47.24  ? 45  LYS A CE  1 
ATOM   356  N  N   . PRO A 1 46  ? -3.720 4.799   29.536  1.00 21.02  ? 46  PRO A N   1 
ATOM   357  C  CA  . PRO A 1 46  ? -3.781 4.066   28.271  1.00 17.53  ? 46  PRO A CA  1 
ATOM   358  C  C   . PRO A 1 46  ? -3.009 4.919   27.301  1.00 15.60  ? 46  PRO A C   1 
ATOM   359  O  O   . PRO A 1 46  ? -2.997 6.127   27.422  1.00 17.99  ? 46  PRO A O   1 
ATOM   360  C  CB  . PRO A 1 46  ? -5.285 4.112   27.961  1.00 21.62  ? 46  PRO A CB  1 
ATOM   361  C  CG  . PRO A 1 46  ? -5.896 4.018   29.321  1.00 28.30  ? 46  PRO A CG  1 
ATOM   362  C  CD  . PRO A 1 46  ? -5.061 5.025   30.115  1.00 25.00  ? 46  PRO A CD  1 
ATOM   363  N  N   . LEU A 1 47  ? -2.363 4.232   26.368  1.00 18.82  ? 47  LEU A N   1 
ATOM   364  C  CA  . LEU A 1 47  ? -1.783 4.951   25.293  1.00 18.43  ? 47  LEU A CA  1 
ATOM   365  C  C   . LEU A 1 47  ? -2.923 5.607   24.518  1.00 15.56  ? 47  LEU A C   1 
ATOM   366  O  O   . LEU A 1 47  ? -3.984 5.023   24.333  1.00 18.75  ? 47  LEU A O   1 
ATOM   367  C  CB  . LEU A 1 47  ? -1.245 3.813   24.449  1.00 27.82  ? 47  LEU A CB  1 
ATOM   368  C  CG  . LEU A 1 47  ? 0.069  4.013   23.771  1.00 33.81  ? 47  LEU A CG  1 
ATOM   369  C  CD1 . LEU A 1 47  ? 0.965  4.824   24.684  1.00 29.58  ? 47  LEU A CD1 1 
ATOM   370  C  CD2 . LEU A 1 47  ? 0.536  2.615   23.395  1.00 37.24  ? 47  LEU A CD2 1 
ATOM   371  N  N   . SER A 1 48  ? -2.625 6.753   23.920  1.00 12.38  ? 48  SER A N   1 
ATOM   372  C  CA  . SER A 1 48  ? -3.478 7.373   22.905  1.00 11.30  ? 48  SER A CA  1 
ATOM   373  C  C   . SER A 1 48  ? -2.710 7.290   21.585  1.00 11.60  ? 48  SER A C   1 
ATOM   374  O  O   . SER A 1 48  ? -1.759 8.027   21.394  1.00 13.16  ? 48  SER A O   1 
ATOM   375  C  CB  . SER A 1 48  ? -3.783 8.815   23.267  1.00 13.48  ? 48  SER A CB  1 
ATOM   376  O  OG  . SER A 1 48  ? -4.520 9.438   22.251  1.00 19.12  ? 48  SER A OG  1 
ATOM   377  N  N   . VAL A 1 49  ? -3.120 6.417   20.693  1.00 13.24  ? 49  VAL A N   1 
ATOM   378  C  CA  . VAL A 1 49  ? -2.500 6.308   19.386  1.00 13.38  ? 49  VAL A CA  1 
ATOM   379  C  C   . VAL A 1 49  ? -3.476 6.951   18.400  1.00 15.74  ? 49  VAL A C   1 
ATOM   380  O  O   . VAL A 1 49  ? -4.542 6.414   18.175  1.00 20.48  ? 49  VAL A O   1 
ATOM   381  C  CB  . VAL A 1 49  ? -2.274 4.823   19.046  1.00 17.50  ? 49  VAL A CB  1 
ATOM   382  C  CG1 . VAL A 1 49  ? -1.596 4.698   17.694  1.00 25.01  ? 49  VAL A CG1 1 
ATOM   383  C  CG2 . VAL A 1 49  ? -1.509 4.132   20.175  1.00 17.33  ? 49  VAL A CG2 1 
ATOM   384  N  N   . SER A 1 50  ? -3.134 8.116   17.837  1.00 14.35  ? 50  SER A N   1 
ATOM   385  C  CA  . SER A 1 50  ? -4.082 8.870   17.015  1.00 14.32  ? 50  SER A CA  1 
ATOM   386  C  C   . SER A 1 50  ? -3.498 8.913   15.623  1.00 12.35  ? 50  SER A C   1 
ATOM   387  O  O   . SER A 1 50  ? -2.753 9.824   15.309  1.00 13.21  ? 50  SER A O   1 
ATOM   388  C  CB  . SER A 1 50  ? -4.328 10.321  17.496  1.00 19.52  ? 50  SER A CB  1 
ATOM   389  O  OG  . SER A 1 50  ? -5.077 10.292  18.678  1.00 25.49  ? 50  SER A OG  1 
ATOM   390  N  N   . TYR A 1 51  ? -3.794 7.910   14.826  1.00 13.53  ? 51  TYR A N   1 
ATOM   391  C  CA  . TYR A 1 51  ? -3.211 7.772   13.516  1.00 12.83  ? 51  TYR A CA  1 
ATOM   392  C  C   . TYR A 1 51  ? -4.180 7.985   12.333  1.00 14.71  ? 51  TYR A C   1 
ATOM   393  O  O   . TYR A 1 51  ? -3.775 7.805   11.181  1.00 16.75  ? 51  TYR A O   1 
ATOM   394  C  CB  . TYR A 1 51  ? -2.570 6.396   13.365  1.00 12.33  ? 51  TYR A CB  1 
ATOM   395  C  CG  . TYR A 1 51  ? -1.300 6.109   14.140  1.00 11.37  ? 51  TYR A CG  1 
ATOM   396  C  CD1 . TYR A 1 51  ? -0.581 7.088   14.835  1.00 11.95  ? 51  TYR A CD1 1 
ATOM   397  C  CD2 . TYR A 1 51  ? -0.769 4.815   14.101  1.00 10.57  ? 51  TYR A CD2 1 
ATOM   398  C  CE1 . TYR A 1 51  ? 0.628  6.773   15.453  1.00 11.19  ? 51  TYR A CE1 1 
ATOM   399  C  CE2 . TYR A 1 51  ? 0.398  4.491   14.780  1.00 10.93  ? 51  TYR A CE2 1 
ATOM   400  C  CZ  . TYR A 1 51  ? 1.136  5.477   15.418  1.00 9.11   ? 51  TYR A CZ  1 
ATOM   401  O  OH  . TYR A 1 51  ? 2.263  5.108   16.076  1.00 10.50  ? 51  TYR A OH  1 
ATOM   402  N  N   A ASP A 1 52  ? -5.400 8.466   12.605  0.50 16.45  ? 52  ASP A N   1 
ATOM   403  N  N   B ASP A 1 52  ? -5.427 8.440   12.592  0.50 16.71  ? 52  ASP A N   1 
ATOM   404  C  CA  A ASP A 1 52  ? -6.407 8.593   11.556  0.50 17.81  ? 52  ASP A CA  1 
ATOM   405  C  CA  B ASP A 1 52  ? -6.425 8.609   11.527  0.50 19.09  ? 52  ASP A CA  1 
ATOM   406  C  C   A ASP A 1 52  ? -5.978 9.570   10.459  0.50 17.38  ? 52  ASP A C   1 
ATOM   407  C  C   B ASP A 1 52  ? -5.921 9.540   10.426  0.50 18.04  ? 52  ASP A C   1 
ATOM   408  O  O   A ASP A 1 52  ? -6.359 9.371   9.310   0.50 22.54  ? 52  ASP A O   1 
ATOM   409  O  O   B ASP A 1 52  ? -6.185 9.278   9.256   0.50 22.96  ? 52  ASP A O   1 
ATOM   410  C  CB  A ASP A 1 52  ? -7.769 8.937   12.155  0.50 20.76  ? 52  ASP A CB  1 
ATOM   411  C  CB  B ASP A 1 52  ? -7.819 9.025   12.031  0.50 24.32  ? 52  ASP A CB  1 
ATOM   412  C  CG  A ASP A 1 52  ? -7.679 10.121  13.091  0.50 21.84  ? 52  ASP A CG  1 
ATOM   413  C  CG  B ASP A 1 52  ? -8.870 9.169   10.925  0.50 29.53  ? 52  ASP A CG  1 
ATOM   414  O  OD1 A ASP A 1 52  ? -7.037 9.971   14.164  0.50 25.06  ? 52  ASP A OD1 1 
ATOM   415  O  OD1 B ASP A 1 52  ? -9.343 8.115   10.404  0.50 33.01  ? 52  ASP A OD1 1 
ATOM   416  O  OD2 A ASP A 1 52  ? -8.290 11.173  12.753  0.50 29.17  ? 52  ASP A OD2 1 
ATOM   417  O  OD2 B ASP A 1 52  ? -9.213 10.335  10.578  0.50 37.03  ? 52  ASP A OD2 1 
ATOM   418  N  N   . GLN A 1 53  ? -5.160 10.579  10.784  1.00 18.47  ? 53  GLN A N   1 
ATOM   419  C  CA  . GLN A 1 53  ? -4.752 11.554  9.768   1.00 22.59  ? 53  GLN A CA  1 
ATOM   420  C  C   . GLN A 1 53  ? -3.331 11.314  9.286   1.00 18.20  ? 53  GLN A C   1 
ATOM   421  O  O   . GLN A 1 53  ? -2.732 12.177  8.682   1.00 18.58  ? 53  GLN A O   1 
ATOM   422  C  CB  . GLN A 1 53  ? -4.969 12.978  10.276  1.00 30.40  ? 53  GLN A CB  1 
ATOM   423  C  CG  . GLN A 1 53  ? -6.429 13.260  10.555  1.00 35.14  ? 53  GLN A CG  1 
ATOM   424  C  CD  . GLN A 1 53  ? -7.131 13.441  9.229   1.00 51.66  ? 53  GLN A CD  1 
ATOM   425  O  OE1 . GLN A 1 53  ? -7.059 14.507  8.615   1.00 64.33  ? 53  GLN A OE1 1 
ATOM   426  N  NE2 . GLN A 1 53  ? -7.763 12.375  8.747   1.00 57.01  ? 53  GLN A NE2 1 
ATOM   427  N  N   . ALA A 1 54  ? -2.753 10.141  9.552   1.00 16.41  ? 54  ALA A N   1 
ATOM   428  C  CA  . ALA A 1 54  ? -1.405 9.852   9.073   1.00 13.21  ? 54  ALA A CA  1 
ATOM   429  C  C   . ALA A 1 54  ? -1.287 10.008  7.563   1.00 15.31  ? 54  ALA A C   1 
ATOM   430  O  O   . ALA A 1 54  ? -2.150 9.571   6.792   1.00 19.62  ? 54  ALA A O   1 
ATOM   431  C  CB  . ALA A 1 54  ? -0.975 8.442   9.451   1.00 14.98  ? 54  ALA A CB  1 
ATOM   432  N  N   . THR A 1 55  ? -0.163 10.618  7.169   1.00 13.16  ? 55  THR A N   1 
ATOM   433  C  CA  . THR A 1 55  ? 0.157  10.863  5.766   1.00 13.49  ? 55  THR A CA  1 
ATOM   434  C  C   . THR A 1 55  ? 1.485  10.177  5.470   1.00 9.73   ? 55  THR A C   1 
ATOM   435  O  O   . THR A 1 55  ? 2.539  10.731  5.718   1.00 10.11  ? 55  THR A O   1 
ATOM   436  C  CB  . THR A 1 55  ? 0.294  12.378  5.461   1.00 17.78  ? 55  THR A CB  1 
ATOM   437  O  OG1 . THR A 1 55  ? -0.947 13.003  5.787   1.00 24.08  ? 55  THR A OG1 1 
ATOM   438  C  CG2 . THR A 1 55  ? 0.576  12.598  4.001   1.00 23.54  ? 55  THR A CG2 1 
ATOM   439  N  N   . SER A 1 56  ? 1.437  8.958   4.936   1.00 9.86   ? 56  SER A N   1 
ATOM   440  C  CA  . SER A 1 56  ? 2.678  8.304   4.534   1.00 8.73   ? 56  SER A CA  1 
ATOM   441  C  C   . SER A 1 56  ? 3.201  8.935   3.249   1.00 10.57  ? 56  SER A C   1 
ATOM   442  O  O   . SER A 1 56  ? 2.425  9.444   2.448   1.00 11.40  ? 56  SER A O   1 
ATOM   443  C  CB  . SER A 1 56  ? 2.517  6.775   4.408   1.00 10.75  ? 56  SER A CB  1 
ATOM   444  O  OG  . SER A 1 56  ? 1.615  6.490   3.334   1.00 11.33  ? 56  SER A OG  1 
ATOM   445  N  N   . LEU A 1 57  ? 4.513  8.897   3.048   1.00 9.31   ? 57  LEU A N   1 
ATOM   446  C  CA  . LEU A 1 57  ? 5.118  9.552   1.893   1.00 10.88  ? 57  LEU A CA  1 
ATOM   447  C  C   . LEU A 1 57  ? 5.924  8.574   1.047   1.00 10.89  ? 57  LEU A C   1 
ATOM   448  O  O   . LEU A 1 57  ? 5.822  8.567   -0.183  1.00 11.74  ? 57  LEU A O   1 
ATOM   449  C  CB  . LEU A 1 57  ? 5.947  10.756  2.324   1.00 12.78  ? 57  LEU A CB  1 
ATOM   450  C  CG  . LEU A 1 57  ? 5.134  11.906  2.955   1.00 13.88  ? 57  LEU A CG  1 
ATOM   451  C  CD1 . LEU A 1 57  ? 6.097  12.979  3.475   1.00 19.58  ? 57  LEU A CD1 1 
ATOM   452  C  CD2 . LEU A 1 57  ? 4.091  12.501  1.999   1.00 20.11  ? 57  LEU A CD2 1 
ATOM   453  N  N   . ARG A 1 58  ? 6.826  7.836   1.686   1.00 10.13  ? 58  ARG A N   1 
ATOM   454  C  CA  . ARG A 1 58  ? 7.923  7.249   0.952   1.00 9.97   ? 58  ARG A CA  1 
ATOM   455  C  C   . ARG A 1 58  ? 8.409  6.024   1.747   1.00 8.97   ? 58  ARG A C   1 
ATOM   456  O  O   . ARG A 1 58  ? 8.325  5.978   2.961   1.00 10.41  ? 58  ARG A O   1 
ATOM   457  C  CB  . ARG A 1 58  ? 9.098  8.240   0.801   1.00 11.61  ? 58  ARG A CB  1 
ATOM   458  C  CG  . ARG A 1 58  ? 10.166 7.758   -0.154  1.00 12.66  ? 58  ARG A CG  1 
ATOM   459  C  CD  . ARG A 1 58  ? 11.143 8.888   -0.368  1.00 15.28  ? 58  ARG A CD  1 
ATOM   460  N  NE  . ARG A 1 58  ? 11.985 9.075   0.819   1.00 12.56  ? 58  ARG A NE  1 
ATOM   461  C  CZ  . ARG A 1 58  ? 13.307 9.258   0.832   1.00 11.01  ? 58  ARG A CZ  1 
ATOM   462  N  NH1 . ARG A 1 58  ? 13.974 9.481   -0.300  1.00 14.30  ? 58  ARG A NH1 1 
ATOM   463  N  NH2 . ARG A 1 58  ? 13.936 9.314   1.970   1.00 11.18  ? 58  ARG A NH2 1 
ATOM   464  N  N   . ILE A 1 59  ? 8.945  5.021   1.052   1.00 7.84   ? 59  ILE A N   1 
ATOM   465  C  CA  . ILE A 1 59  ? 9.605  3.883   1.692   1.00 7.84   ? 59  ILE A CA  1 
ATOM   466  C  C   . ILE A 1 59  ? 11.040 3.889   1.184   1.00 8.30   ? 59  ILE A C   1 
ATOM   467  O  O   . ILE A 1 59  ? 11.295 4.141   -0.008  1.00 9.74   ? 59  ILE A O   1 
ATOM   468  C  CB  . ILE A 1 59  ? 8.860  2.579   1.392   1.00 7.85   ? 59  ILE A CB  1 
ATOM   469  C  CG1 . ILE A 1 59  ? 9.398  1.423   2.264   1.00 8.83   ? 59  ILE A CG1 1 
ATOM   470  C  CG2 . ILE A 1 59  ? 8.819  2.209   -0.089  1.00 10.36  ? 59  ILE A CG2 1 
ATOM   471  C  CD1 . ILE A 1 59  ? 8.486  0.197   2.167   1.00 11.10  ? 59  ILE A CD1 1 
ATOM   472  N  N   . LEU A 1 60  ? 11.986 3.580   2.075   1.00 8.31   ? 60  LEU A N   1 
ATOM   473  C  CA  . LEU A 1 60  ? 13.410 3.756   1.764   1.00 7.17   ? 60  LEU A CA  1 
ATOM   474  C  C   . LEU A 1 60  ? 14.234 2.601   2.347   1.00 7.59   ? 60  LEU A C   1 
ATOM   475  O  O   . LEU A 1 60  ? 14.032 2.210   3.490   1.00 8.39   ? 60  LEU A O   1 
ATOM   476  C  CB  . LEU A 1 60  ? 13.901 5.088   2.404   1.00 10.29  ? 60  LEU A CB  1 
ATOM   477  C  CG  . LEU A 1 60  ? 15.432 5.283   2.381   1.00 9.35   ? 60  LEU A CG  1 
ATOM   478  C  CD1 . LEU A 1 60  ? 15.955 5.539   0.971   1.00 10.99  ? 60  LEU A CD1 1 
ATOM   479  C  CD2 . LEU A 1 60  ? 15.850 6.468   3.317   1.00 10.90  ? 60  LEU A CD2 1 
ATOM   480  N  N   . ASN A 1 61  ? 15.125 2.038   1.500   1.00 7.57   ? 61  ASN A N   1 
ATOM   481  C  CA  . ASN A 1 61  ? 16.131 1.073   1.972   1.00 7.00   ? 61  ASN A CA  1 
ATOM   482  C  C   . ASN A 1 61  ? 17.340 1.873   2.468   1.00 8.16   ? 61  ASN A C   1 
ATOM   483  O  O   . ASN A 1 61  ? 17.972 2.556   1.635   1.00 8.55   ? 61  ASN A O   1 
ATOM   484  C  CB  . ASN A 1 61  ? 16.451 0.099   0.820   1.00 7.58   ? 61  ASN A CB  1 
ATOM   485  C  CG  . ASN A 1 61  ? 17.535 -0.882  1.241   1.00 7.37   ? 61  ASN A CG  1 
ATOM   486  O  OD1 . ASN A 1 61  ? 18.397 -0.636  2.095   1.00 9.36   ? 61  ASN A OD1 1 
ATOM   487  N  ND2 . ASN A 1 61  ? 17.490 -2.045  0.642   1.00 8.69   ? 61  ASN A ND2 1 
ATOM   488  N  N   . THR A 1 62  ? 17.615 1.893   3.782   1.00 8.42   ? 62  THR A N   1 
ATOM   489  C  CA  . THR A 1 62  ? 18.678 2.747   4.290   1.00 8.83   ? 62  THR A CA  1 
ATOM   490  C  C   . THR A 1 62  ? 20.035 2.075   4.164   1.00 9.59   ? 62  THR A C   1 
ATOM   491  O  O   . THR A 1 62  ? 21.072 2.694   4.517   1.00 12.54  ? 62  THR A O   1 
ATOM   492  C  CB  . THR A 1 62  ? 18.413 3.025   5.786   1.00 9.06   ? 62  THR A CB  1 
ATOM   493  O  OG1 . THR A 1 62  ? 18.617 1.784   6.462   1.00 8.92   ? 62  THR A OG1 1 
ATOM   494  C  CG2 . THR A 1 62  ? 17.034 3.607   6.020   1.00 10.82  ? 62  THR A CG2 1 
ATOM   495  N  N   . GLY A 1 63  ? 20.095 0.804   3.758   1.00 8.38   ? 63  GLY A N   1 
ATOM   496  C  CA  . GLY A 1 63  ? 21.325 0.029   3.806   1.00 9.04   ? 63  GLY A CA  1 
ATOM   497  C  C   . GLY A 1 63  ? 21.468 -0.788  5.095   1.00 8.56   ? 63  GLY A C   1 
ATOM   498  O  O   . GLY A 1 63  ? 22.354 -1.660  5.195   1.00 12.06  ? 63  GLY A O   1 
ATOM   499  N  N   . TYR A 1 64  ? 20.585 -0.535  6.068   1.00 7.79   ? 64  TYR A N   1 
ATOM   500  C  CA  . TYR A 1 64  ? 20.589 -1.316  7.314   1.00 8.54   ? 64  TYR A CA  1 
ATOM   501  C  C   . TYR A 1 64  ? 19.213 -1.942  7.543   1.00 7.68   ? 64  TYR A C   1 
ATOM   502  O  O   . TYR A 1 64  ? 19.148 -3.016  8.142   1.00 10.61  ? 64  TYR A O   1 
ATOM   503  C  CB  . TYR A 1 64  ? 21.000 -0.417  8.505   1.00 12.18  ? 64  TYR A CB  1 
ATOM   504  C  CG  . TYR A 1 64  ? 22.398 0.233   8.418   1.00 21.12  ? 64  TYR A CG  1 
ATOM   505  C  CD1 . TYR A 1 64  ? 23.555 -0.372  8.912   1.00 25.42  ? 64  TYR A CD1 1 
ATOM   506  C  CD2 . TYR A 1 64  ? 22.622 1.494   7.862   1.00 35.28  ? 64  TYR A CD2 1 
ATOM   507  C  CE1 . TYR A 1 64  ? 24.826 0.219   8.847   1.00 34.60  ? 64  TYR A CE1 1 
ATOM   508  C  CE2 . TYR A 1 64  ? 23.887 2.095   7.791   1.00 35.37  ? 64  TYR A CE2 1 
ATOM   509  C  CZ  . TYR A 1 64  ? 25.035 1.476   8.282   1.00 43.73  ? 64  TYR A CZ  1 
ATOM   510  O  OH  . TYR A 1 64  ? 26.315 2.079   8.215   1.00 24.44  ? 64  TYR A OH  1 
ATOM   511  N  N   . LEU A 1 65  ? 18.129 -1.288  7.093   1.00 8.39   ? 65  LEU A N   1 
ATOM   512  C  CA  . LEU A 1 65  ? 16.756 -1.726  7.294   1.00 7.58   ? 65  LEU A CA  1 
ATOM   513  C  C   . LEU A 1 65  ? 15.942 -0.993  6.234   1.00 6.65   ? 65  LEU A C   1 
ATOM   514  O  O   . LEU A 1 65  ? 16.520 -0.375  5.338   1.00 8.05   ? 65  LEU A O   1 
ATOM   515  C  CB  . LEU A 1 65  ? 16.259 -1.461  8.733   1.00 8.87   ? 65  LEU A CB  1 
ATOM   516  C  CG  . LEU A 1 65  ? 16.603 -0.135  9.357   1.00 9.81   ? 65  LEU A CG  1 
ATOM   517  C  CD1 . LEU A 1 65  ? 15.819 0.990   8.703   1.00 10.66  ? 65  LEU A CD1 1 
ATOM   518  C  CD2 . LEU A 1 65  ? 16.323 -0.238  10.856  1.00 12.71  ? 65  LEU A CD2 1 
ATOM   519  N  N   . PHE A 1 66  ? 14.615 -1.084  6.263   1.00 6.83   ? 66  PHE A N   1 
ATOM   520  C  CA  . PHE A 1 66  ? 13.799 -0.199  5.469   1.00 7.11   ? 66  PHE A CA  1 
ATOM   521  C  C   . PHE A 1 66  ? 12.871 0.553   6.401   1.00 6.70   ? 66  PHE A C   1 
ATOM   522  O  O   . PHE A 1 66  ? 12.505 0.087   7.496   1.00 7.30   ? 66  PHE A O   1 
ATOM   523  C  CB  . PHE A 1 66  ? 13.033 -0.946  4.355   1.00 8.46   ? 66  PHE A CB  1 
ATOM   524  C  CG  . PHE A 1 66  ? 11.888 -1.783  4.865   1.00 7.03   ? 66  PHE A CG  1 
ATOM   525  C  CD1 . PHE A 1 66  ? 10.617 -1.247  4.978   1.00 8.09   ? 66  PHE A CD1 1 
ATOM   526  C  CD2 . PHE A 1 66  ? 12.045 -3.128  5.211   1.00 9.00   ? 66  PHE A CD2 1 
ATOM   527  C  CE1 . PHE A 1 66  ? 9.560  -2.019  5.473   1.00 9.07   ? 66  PHE A CE1 1 
ATOM   528  C  CE2 . PHE A 1 66  ? 10.976 -3.913  5.648   1.00 8.72   ? 66  PHE A CE2 1 
ATOM   529  C  CZ  . PHE A 1 66  ? 9.730  -3.367  5.766   1.00 9.35   ? 66  PHE A CZ  1 
ATOM   530  N  N   . GLN A 1 67  ? 12.449 1.718   5.907   1.00 7.50   ? 67  GLN A N   1 
ATOM   531  C  CA  . GLN A 1 67  ? 11.587 2.579   6.716   1.00 7.88   ? 67  GLN A CA  1 
ATOM   532  C  C   . GLN A 1 67  ? 10.512 3.224   5.823   1.00 7.40   ? 67  GLN A C   1 
ATOM   533  O  O   . GLN A 1 67  ? 10.765 3.539   4.650   1.00 9.53   ? 67  GLN A O   1 
ATOM   534  C  CB  . GLN A 1 67  ? 12.368 3.675   7.464   1.00 9.02   ? 67  GLN A CB  1 
ATOM   535  C  CG  . GLN A 1 67  ? 13.139 4.590   6.521   1.00 9.60   ? 67  GLN A CG  1 
ATOM   536  C  CD  . GLN A 1 67  ? 14.066 5.539   7.224   1.00 13.10  ? 67  GLN A CD  1 
ATOM   537  O  OE1 . GLN A 1 67  ? 14.768 5.148   8.145   1.00 14.32  ? 67  GLN A OE1 1 
ATOM   538  N  NE2 . GLN A 1 67  ? 14.027 6.790   6.809   1.00 14.70  ? 67  GLN A NE2 1 
ATOM   539  N  N   . VAL A 1 68  ? 9.342  3.393   6.446   1.00 7.50   ? 68  VAL A N   1 
ATOM   540  C  CA  . VAL A 1 68  ? 8.240  4.103   5.826   1.00 7.53   ? 68  VAL A CA  1 
ATOM   541  C  C   . VAL A 1 68  ? 8.184  5.462   6.530   1.00 8.09   ? 68  VAL A C   1 
ATOM   542  O  O   . VAL A 1 68  ? 8.006  5.531   7.750   1.00 8.71   ? 68  VAL A O   1 
ATOM   543  C  CB  . VAL A 1 68  ? 6.918  3.306   5.944   1.00 8.33   ? 68  VAL A CB  1 
ATOM   544  C  CG1 . VAL A 1 68  ? 5.697  4.174   5.470   1.00 9.76   ? 68  VAL A CG1 1 
ATOM   545  C  CG2 . VAL A 1 68  ? 6.976  2.050   5.097   1.00 9.66   ? 68  VAL A CG2 1 
ATOM   546  N  N   . GLU A 1 69  ? 8.224  6.514   5.729   1.00 8.36   ? 69  GLU A N   1 
ATOM   547  C  CA  . GLU A 1 69  ? 8.315  7.878   6.256   1.00 7.72   ? 69  GLU A CA  1 
ATOM   548  C  C   . GLU A 1 69  ? 6.949  8.565   6.140   1.00 8.25   ? 69  GLU A C   1 
ATOM   549  O  O   . GLU A 1 69  ? 6.227  8.315   5.154   1.00 9.00   ? 69  GLU A O   1 
ATOM   550  C  CB  . GLU A 1 69  ? 9.305  8.712   5.437   1.00 9.36   ? 69  GLU A CB  1 
ATOM   551  C  CG  . GLU A 1 69  ? 10.678 8.050   5.503   1.00 9.74   ? 69  GLU A CG  1 
ATOM   552  C  CD  . GLU A 1 69  ? 11.635 8.575   4.447   1.00 10.87  ? 69  GLU A CD  1 
ATOM   553  O  OE1 . GLU A 1 69  ? 12.855 8.258   4.541   1.00 13.24  ? 69  GLU A OE1 1 
ATOM   554  O  OE2 . GLU A 1 69  ? 11.213 9.299   3.547   1.00 13.11  ? 69  GLU A OE2 1 
ATOM   555  N  N   . PHE A 1 70  ? 6.666  9.456   7.128   1.00 9.07   ? 70  PHE A N   1 
ATOM   556  C  CA  . PHE A 1 70  ? 5.376  10.154  7.168   1.00 8.40   ? 70  PHE A CA  1 
ATOM   557  C  C   . PHE A 1 70  ? 5.626  11.648  7.118   1.00 9.68   ? 70  PHE A C   1 
ATOM   558  O  O   . PHE A 1 70  ? 6.706  12.143  7.485   1.00 10.16  ? 70  PHE A O   1 
ATOM   559  C  CB  . PHE A 1 70  ? 4.633  9.821   8.485   1.00 8.72   ? 70  PHE A CB  1 
ATOM   560  C  CG  . PHE A 1 70  ? 4.103  8.421   8.443   1.00 8.86   ? 70  PHE A CG  1 
ATOM   561  C  CD1 . PHE A 1 70  ? 4.925  7.314   8.664   1.00 10.07  ? 70  PHE A CD1 1 
ATOM   562  C  CD2 . PHE A 1 70  ? 2.788  8.192   8.130   1.00 9.24   ? 70  PHE A CD2 1 
ATOM   563  C  CE1 . PHE A 1 70  ? 4.422  6.012   8.549   1.00 11.75  ? 70  PHE A CE1 1 
ATOM   564  C  CE2 . PHE A 1 70  ? 2.295  6.905   7.995   1.00 10.12  ? 70  PHE A CE2 1 
ATOM   565  C  CZ  . PHE A 1 70  ? 3.106  5.807   8.244   1.00 10.09  ? 70  PHE A CZ  1 
ATOM   566  N  N   . ASP A 1 71  ? 4.553  12.401  6.804   1.00 11.39  ? 71  ASP A N   1 
ATOM   567  C  CA  . ASP A 1 71  ? 4.641  13.852  6.931   1.00 11.39  ? 71  ASP A CA  1 
ATOM   568  C  C   . ASP A 1 71  ? 4.527  14.250  8.409   1.00 10.49  ? 71  ASP A C   1 
ATOM   569  O  O   . ASP A 1 71  ? 3.468  14.087  9.051   1.00 13.81  ? 71  ASP A O   1 
ATOM   570  C  CB  . ASP A 1 71  ? 3.473  14.473  6.176   1.00 14.35  ? 71  ASP A CB  1 
ATOM   571  C  CG  . ASP A 1 71  ? 3.406  15.996  6.312   1.00 14.66  ? 71  ASP A CG  1 
ATOM   572  O  OD1 . ASP A 1 71  ? 4.324  16.594  6.860   1.00 14.06  ? 71  ASP A OD1 1 
ATOM   573  O  OD2 . ASP A 1 71  ? 2.381  16.557  6.013   1.00 17.13  ? 71  ASP A OD2 1 
ATOM   574  N  N   . ASP A 1 72  ? 5.627  14.693  8.983   1.00 11.47  ? 72  ASP A N   1 
ATOM   575  C  CA  . ASP A 1 72  ? 5.686  15.095  10.377  1.00 11.95  ? 72  ASP A CA  1 
ATOM   576  C  C   . ASP A 1 72  ? 5.901  16.606  10.436  1.00 12.18  ? 72  ASP A C   1 
ATOM   577  O  O   . ASP A 1 72  ? 6.478  17.103  11.409  1.00 15.04  ? 72  ASP A O   1 
ATOM   578  C  CB  . ASP A 1 72  ? 6.780  14.343  11.124  1.00 12.60  ? 72  ASP A CB  1 
ATOM   579  C  CG  . ASP A 1 72  ? 8.158  14.610  10.573  1.00 11.87  ? 72  ASP A CG  1 
ATOM   580  O  OD1 . ASP A 1 72  ? 8.271  15.149  9.400   1.00 13.70  ? 72  ASP A OD1 1 
ATOM   581  O  OD2 . ASP A 1 72  ? 9.146  14.143  11.228  1.00 13.95  ? 72  ASP A OD2 1 
ATOM   582  N  N   . SER A 1 73  ? 5.407  17.331  9.419   1.00 11.57  ? 73  SER A N   1 
ATOM   583  C  CA  . SER A 1 73  ? 5.592  18.797  9.407   1.00 12.96  ? 73  SER A CA  1 
ATOM   584  C  C   . SER A 1 73  ? 4.416  19.454  10.122  1.00 13.91  ? 73  SER A C   1 
ATOM   585  O  O   . SER A 1 73  ? 4.414  20.685  10.278  1.00 18.62  ? 73  SER A O   1 
ATOM   586  C  CB  . SER A 1 73  ? 5.711  19.302  7.979   1.00 13.71  ? 73  SER A CB  1 
ATOM   587  O  OG  . SER A 1 73  ? 4.418  19.235  7.323   1.00 14.10  ? 73  SER A OG  1 
ATOM   588  N  N   . GLN A 1 74  ? 3.440  18.676  10.613  1.00 14.78  ? 74  GLN A N   1 
ATOM   589  C  CA  . GLN A 1 74  ? 2.221  19.101  11.337  1.00 17.78  ? 74  GLN A CA  1 
ATOM   590  C  C   . GLN A 1 74  ? 1.777  17.906  12.177  1.00 17.03  ? 74  GLN A C   1 
ATOM   591  O  O   . GLN A 1 74  ? 2.179  16.804  11.844  1.00 15.05  ? 74  GLN A O   1 
ATOM   592  C  CB  . GLN A 1 74  ? 1.094  19.253  10.329  1.00 26.64  ? 74  GLN A CB  1 
ATOM   593  C  CG  . GLN A 1 74  ? 1.086  20.573  9.591   1.00 28.27  ? 74  GLN A CG  1 
ATOM   594  C  CD  . GLN A 1 74  ? -0.305 20.663  9.026   1.00 27.46  ? 74  GLN A CD  1 
ATOM   595  O  OE1 . GLN A 1 74  ? -1.222 21.121  9.701   1.00 31.41  ? 74  GLN A OE1 1 
ATOM   596  N  NE2 . GLN A 1 74  ? -0.471 20.122  7.829   1.00 23.60  ? 74  GLN A NE2 1 
ATOM   597  N  N   . ASP A 1 75  ? 0.896  18.120  13.149  1.00 17.10  ? 75  ASP A N   1 
ATOM   598  C  CA  . ASP A 1 75  ? 0.424  17.057  14.020  1.00 19.96  ? 75  ASP A CA  1 
ATOM   599  C  C   . ASP A 1 75  ? -0.658 16.225  13.325  1.00 19.91  ? 75  ASP A C   1 
ATOM   600  O  O   . ASP A 1 75  ? -1.839 16.361  13.565  1.00 37.12  ? 75  ASP A O   1 
ATOM   601  C  CB  . ASP A 1 75  ? -0.168 17.626  15.305  1.00 18.59  ? 75  ASP A CB  1 
ATOM   602  C  CG  . ASP A 1 75  ? 0.864  18.053  16.326  1.00 23.26  ? 75  ASP A CG  1 
ATOM   603  O  OD1 . ASP A 1 75  ? 2.055  17.766  16.138  1.00 29.84  ? 75  ASP A OD1 1 
ATOM   604  O  OD2 . ASP A 1 75  ? 0.431  18.570  17.342  1.00 26.43  ? 75  ASP A OD2 1 
ATOM   605  N  N   . LYS A 1 76  ? -0.249 15.308  12.495  1.00 17.72  ? 76  LYS A N   1 
ATOM   606  C  CA  . LYS A 1 76  ? -1.190 14.497  11.742  1.00 16.97  ? 76  LYS A CA  1 
ATOM   607  C  C   . LYS A 1 76  ? -1.484 13.179  12.417  1.00 20.85  ? 76  LYS A C   1 
ATOM   608  O  O   . LYS A 1 76  ? -2.615 12.722  12.369  1.00 33.70  ? 76  LYS A O   1 
ATOM   609  C  CB  . LYS A 1 76  ? -0.543 14.259  10.392  1.00 19.26  ? 76  LYS A CB  1 
ATOM   610  C  CG  . LYS A 1 76  ? -0.707 15.509  9.560   1.00 21.50  ? 76  LYS A CG  1 
ATOM   611  C  CD  . LYS A 1 76  ? -0.285 15.245  8.174   1.00 21.77  ? 76  LYS A CD  1 
ATOM   612  C  CE  . LYS A 1 76  ? -0.735 16.296  7.179   1.00 19.12  ? 76  LYS A CE  1 
ATOM   613  N  NZ  . LYS A 1 76  ? -0.499 15.815  5.799   1.00 21.11  ? 76  LYS A NZ  1 
ATOM   614  N  N   . ALA A 1 77  ? -0.428 12.479  12.742  1.00 18.12  ? 77  ALA A N   1 
ATOM   615  C  CA  . ALA A 1 77  ? -0.516 11.237  13.495  1.00 16.17  ? 77  ALA A CA  1 
ATOM   616  C  C   . ALA A 1 77  ? 0.363  11.448  14.716  1.00 16.25  ? 77  ALA A C   1 
ATOM   617  O  O   . ALA A 1 77  ? 1.549  11.810  14.562  1.00 17.54  ? 77  ALA A O   1 
ATOM   618  C  CB  . ALA A 1 77  ? 0.084  10.148  12.618  1.00 20.86  ? 77  ALA A CB  1 
ATOM   619  N  N   . VAL A 1 78  ? -0.191 11.199  15.891  1.00 11.96  ? 78  VAL A N   1 
ATOM   620  C  CA  . VAL A 1 78  ? 0.537  11.484  17.120  1.00 11.69  ? 78  VAL A CA  1 
ATOM   621  C  C   . VAL A 1 78  ? 0.309  10.357  18.112  1.00 11.36  ? 78  VAL A C   1 
ATOM   622  O  O   . VAL A 1 78  ? -0.736 9.683   18.066  1.00 13.76  ? 78  VAL A O   1 
ATOM   623  C  CB  . VAL A 1 78  ? 0.128  12.819  17.747  1.00 15.05  ? 78  VAL A CB  1 
ATOM   624  C  CG1 . VAL A 1 78  ? 0.355  13.986  16.799  1.00 17.66  ? 78  VAL A CG1 1 
ATOM   625  C  CG2 . VAL A 1 78  ? -1.295 12.784  18.184  1.00 18.12  ? 78  VAL A CG2 1 
ATOM   626  N  N   . LEU A 1 79  ? 1.255  10.236  19.049  1.00 10.60  ? 79  LEU A N   1 
ATOM   627  C  CA  . LEU A 1 79  ? 1.217  9.353   20.188  1.00 9.70   ? 79  LEU A CA  1 
ATOM   628  C  C   . LEU A 1 79  ? 1.198  10.252  21.407  1.00 10.02  ? 79  LEU A C   1 
ATOM   629  O  O   . LEU A 1 79  ? 2.062  11.143  21.549  1.00 11.65  ? 79  LEU A O   1 
ATOM   630  C  CB  . LEU A 1 79  ? 2.446  8.441   20.160  1.00 10.64  ? 79  LEU A CB  1 
ATOM   631  C  CG  . LEU A 1 79  ? 2.516  7.383   21.241  1.00 12.08  ? 79  LEU A CG  1 
ATOM   632  C  CD1 . LEU A 1 79  ? 1.421  6.309   21.118  1.00 15.34  ? 79  LEU A CD1 1 
ATOM   633  C  CD2 . LEU A 1 79  ? 3.877  6.705   21.145  1.00 13.32  ? 79  LEU A CD2 1 
ATOM   634  N  N   . LYS A 1 80  ? 0.306  9.911   22.351  1.00 11.59  ? 80  LYS A N   1 
ATOM   635  C  CA  . LYS A 1 80  ? 0.202  10.669  23.584  1.00 12.32  ? 80  LYS A CA  1 
ATOM   636  C  C   . LYS A 1 80  ? -0.181 9.687   24.688  1.00 13.04  ? 80  LYS A C   1 
ATOM   637  O  O   . LYS A 1 80  ? -0.498 8.533   24.408  1.00 12.03  ? 80  LYS A O   1 
ATOM   638  C  CB  . LYS A 1 80  ? -0.878 11.764  23.486  1.00 18.45  ? 80  LYS A CB  1 
ATOM   639  C  CG  . LYS A 1 80  ? -0.757 12.826  22.411  1.00 19.37  ? 80  LYS A CG  1 
ATOM   640  C  CD  . LYS A 1 80  ? -2.046 13.684  22.383  1.00 29.36  ? 80  LYS A CD  1 
ATOM   641  N  N   . GLY A 1 81  ? -0.216 10.166  25.919  1.00 12.79  ? 81  GLY A N   1 
ATOM   642  C  CA  . GLY A 1 81  ? -0.687 9.341   27.015  1.00 14.39  ? 81  GLY A CA  1 
ATOM   643  C  C   . GLY A 1 81  ? 0.357  8.293   27.389  1.00 12.09  ? 81  GLY A C   1 
ATOM   644  O  O   . GLY A 1 81  ? 1.567  8.467   27.185  1.00 13.90  ? 81  GLY A O   1 
ATOM   645  N  N   . GLY A 1 82  ? -0.092 7.213   28.038  1.00 16.24  ? 82  GLY A N   1 
ATOM   646  C  CA  . GLY A 1 82  ? 0.866  6.270   28.569  1.00 18.60  ? 82  GLY A CA  1 
ATOM   647  C  C   . GLY A 1 82  ? 1.800  6.956   29.553  1.00 19.86  ? 82  GLY A C   1 
ATOM   648  O  O   . GLY A 1 82  ? 1.377  7.733   30.427  1.00 22.15  ? 82  GLY A O   1 
ATOM   649  N  N   . PRO A 1 83  ? 3.120  6.697   29.420  1.00 15.82  ? 83  PRO A N   1 
ATOM   650  C  CA  . PRO A 1 83  ? 4.111  7.323   30.289  1.00 16.43  ? 83  PRO A CA  1 
ATOM   651  C  C   . PRO A 1 83  ? 4.461  8.722   29.814  1.00 14.64  ? 83  PRO A C   1 
ATOM   652  O  O   . PRO A 1 83  ? 5.259  9.369   30.481  1.00 21.51  ? 83  PRO A O   1 
ATOM   653  C  CB  . PRO A 1 83  ? 5.289  6.351   30.131  1.00 14.29  ? 83  PRO A CB  1 
ATOM   654  C  CG  . PRO A 1 83  ? 5.220  5.977   28.677  1.00 12.75  ? 83  PRO A CG  1 
ATOM   655  C  CD  . PRO A 1 83  ? 3.727  5.807   28.395  1.00 13.50  ? 83  PRO A CD  1 
ATOM   656  N  N   . LEU A 1 84  ? 3.900  9.173   28.661  1.00 12.05  ? 84  LEU A N   1 
ATOM   657  C  CA  . LEU A 1 84  ? 4.406  10.371  27.966  1.00 12.23  ? 84  LEU A CA  1 
ATOM   658  C  C   . LEU A 1 84  ? 3.751  11.648  28.498  1.00 14.45  ? 84  LEU A C   1 
ATOM   659  O  O   . LEU A 1 84  ? 2.549  11.675  28.772  1.00 17.75  ? 84  LEU A O   1 
ATOM   660  C  CB  . LEU A 1 84  ? 4.131  10.291  26.462  1.00 11.50  ? 84  LEU A CB  1 
ATOM   661  C  CG  . LEU A 1 84  ? 4.694  9.044   25.783  1.00 10.20  ? 84  LEU A CG  1 
ATOM   662  C  CD1 . LEU A 1 84  ? 4.193  8.976   24.351  1.00 11.28  ? 84  LEU A CD1 1 
ATOM   663  C  CD2 . LEU A 1 84  ? 6.231  9.042   25.847  1.00 11.85  ? 84  LEU A CD2 1 
ATOM   664  N  N   . ASP A 1 85  ? 4.578  12.694  28.613  1.00 16.29  ? 85  ASP A N   1 
ATOM   665  C  CA  . ASP A 1 85  ? 4.107  14.048  28.864  1.00 17.85  ? 85  ASP A CA  1 
ATOM   666  C  C   . ASP A 1 85  ? 4.074  14.735  27.499  1.00 17.64  ? 85  ASP A C   1 
ATOM   667  O  O   . ASP A 1 85  ? 5.041  14.664  26.722  1.00 25.56  ? 85  ASP A O   1 
ATOM   668  C  CB  . ASP A 1 85  ? 5.040  14.701  29.909  1.00 23.36  ? 85  ASP A CB  1 
ATOM   669  C  CG  . ASP A 1 85  ? 4.938  14.113  31.332  1.00 29.88  ? 85  ASP A CG  1 
ATOM   670  O  OD1 . ASP A 1 85  ? 3.834  13.613  31.707  1.00 43.37  ? 85  ASP A OD1 1 
ATOM   671  O  OD2 . ASP A 1 85  ? 5.938  14.185  32.097  1.00 32.33  ? 85  ASP A OD2 1 
ATOM   672  N  N   . GLY A 1 86  ? 2.988  15.405  27.131  1.00 22.94  ? 86  GLY A N   1 
ATOM   673  C  CA  . GLY A 1 86  ? 3.061  16.046  25.824  1.00 18.94  ? 86  GLY A CA  1 
ATOM   674  C  C   . GLY A 1 86  ? 2.762  15.142  24.598  1.00 16.98  ? 86  GLY A C   1 
ATOM   675  O  O   . GLY A 1 86  ? 2.175  14.064  24.689  1.00 23.45  ? 86  GLY A O   1 
ATOM   676  N  N   . THR A 1 87  ? 3.073  15.654  23.388  1.00 16.29  ? 87  THR A N   1 
ATOM   677  C  CA  . THR A 1 87  ? 2.571  15.160  22.114  1.00 16.26  ? 87  THR A CA  1 
ATOM   678  C  C   . THR A 1 87  ? 3.771  14.721  21.296  1.00 14.01  ? 87  THR A C   1 
ATOM   679  O  O   . THR A 1 87  ? 4.752  15.450  21.161  1.00 12.34  ? 87  THR A O   1 
ATOM   680  C  CB  . THR A 1 87  ? 1.851  16.268  21.319  1.00 17.49  ? 87  THR A CB  1 
ATOM   681  O  OG1 . THR A 1 87  ? 0.681  16.560  22.070  1.00 25.46  ? 87  THR A OG1 1 
ATOM   682  C  CG2 . THR A 1 87  ? 1.462  15.786  19.941  1.00 19.71  ? 87  THR A CG2 1 
ATOM   683  N  N   . TYR A 1 88  ? 3.734  13.482  20.824  1.00 10.76  ? 88  TYR A N   1 
ATOM   684  C  CA  . TYR A 1 88  ? 4.821  12.957  20.030  1.00 10.07  ? 88  TYR A CA  1 
ATOM   685  C  C   . TYR A 1 88  ? 4.350  12.653  18.605  1.00 10.00  ? 88  TYR A C   1 
ATOM   686  O  O   . TYR A 1 88  ? 3.411  11.901  18.396  1.00 12.57  ? 88  TYR A O   1 
ATOM   687  C  CB  . TYR A 1 88  ? 5.432  11.704  20.666  1.00 10.39  ? 88  TYR A CB  1 
ATOM   688  C  CG  . TYR A 1 88  ? 6.226  11.941  21.926  1.00 8.18   ? 88  TYR A CG  1 
ATOM   689  C  CD1 . TYR A 1 88  ? 5.608  12.399  23.105  1.00 10.07  ? 88  TYR A CD1 1 
ATOM   690  C  CD2 . TYR A 1 88  ? 7.618  11.744  21.936  1.00 9.39   ? 88  TYR A CD2 1 
ATOM   691  C  CE1 . TYR A 1 88  ? 6.382  12.595  24.245  1.00 10.72  ? 88  TYR A CE1 1 
ATOM   692  C  CE2 . TYR A 1 88  ? 8.392  11.939  23.077  1.00 8.61   ? 88  TYR A CE2 1 
ATOM   693  C  CZ  . TYR A 1 88  ? 7.748  12.285  24.244  1.00 9.20   ? 88  TYR A CZ  1 
ATOM   694  O  OH  . TYR A 1 88  ? 8.479  12.435  25.381  1.00 11.68  ? 88  TYR A OH  1 
ATOM   695  N  N   . ARG A 1 89  ? 4.971  13.258  17.595  1.00 9.54   ? 89  ARG A N   1 
ATOM   696  C  CA  . ARG A 1 89  ? 4.550  13.123  16.226  1.00 10.76  ? 89  ARG A CA  1 
ATOM   697  C  C   . ARG A 1 89  ? 5.195  11.930  15.544  1.00 8.13   ? 89  ARG A C   1 
ATOM   698  O  O   . ARG A 1 89  ? 6.410  11.742  15.645  1.00 8.35   ? 89  ARG A O   1 
ATOM   699  C  CB  . ARG A 1 89  ? 5.004  14.386  15.485  1.00 14.35  ? 89  ARG A CB  1 
ATOM   700  C  CG  . ARG A 1 89  ? 4.068  14.835  14.404  1.00 26.89  ? 89  ARG A CG  1 
ATOM   701  C  CD  . ARG A 1 89  ? 4.673  16.128  13.902  1.00 18.97  ? 89  ARG A CD  1 
ATOM   702  N  NE  . ARG A 1 89  ? 4.101  17.304  14.543  1.00 18.06  ? 89  ARG A NE  1 
ATOM   703  C  CZ  . ARG A 1 89  ? 4.453  18.593  14.319  1.00 17.44  ? 89  ARG A CZ  1 
ATOM   704  N  NH1 . ARG A 1 89  ? 5.403  18.878  13.444  1.00 17.06  ? 89  ARG A NH1 1 
ATOM   705  N  NH2 . ARG A 1 89  ? 3.848  19.567  14.974  1.00 24.47  ? 89  ARG A NH2 1 
ATOM   706  N  N   . LEU A 1 90  ? 4.366  11.135  14.821  1.00 8.69   ? 90  LEU A N   1 
ATOM   707  C  CA  . LEU A 1 90  ? 4.887  9.990   14.084  1.00 8.60   ? 90  LEU A CA  1 
ATOM   708  C  C   . LEU A 1 90  ? 5.740  10.501  12.944  1.00 8.55   ? 90  LEU A C   1 
ATOM   709  O  O   . LEU A 1 90  ? 5.252  11.278  12.093  1.00 11.13  ? 90  LEU A O   1 
ATOM   710  C  CB  . LEU A 1 90  ? 3.741  9.130   13.570  1.00 9.71   ? 90  LEU A CB  1 
ATOM   711  C  CG  . LEU A 1 90  ? 4.170  7.987   12.641  1.00 9.55   ? 90  LEU A CG  1 
ATOM   712  C  CD1 . LEU A 1 90  ? 4.940  6.934   13.449  1.00 11.96  ? 90  LEU A CD1 1 
ATOM   713  C  CD2 . LEU A 1 90  ? 2.904  7.342   12.010  1.00 12.65  ? 90  LEU A CD2 1 
ATOM   714  N  N   . LYS A 1 91  ? 6.980  10.019  12.881  1.00 7.64   ? 91  LYS A N   1 
ATOM   715  C  CA  . LYS A 1 91  ? 7.880  10.368  11.796  1.00 8.34   ? 91  LYS A CA  1 
ATOM   716  C  C   . LYS A 1 91  ? 8.068  9.248   10.773  1.00 7.90   ? 91  LYS A C   1 
ATOM   717  O  O   . LYS A 1 91  ? 8.129  9.510   9.593   1.00 8.07   ? 91  LYS A O   1 
ATOM   718  C  CB  . LYS A 1 91  ? 9.215  10.839  12.372  1.00 9.21   ? 91  LYS A CB  1 
ATOM   719  C  CG  . LYS A 1 91  ? 10.340 11.030  11.344  1.00 10.87  ? 91  LYS A CG  1 
ATOM   720  C  CD  . LYS A 1 91  ? 11.541 11.740  11.889  1.00 11.80  ? 91  LYS A CD  1 
ATOM   721  C  CE  . LYS A 1 91  ? 12.524 12.008  10.745  1.00 15.04  ? 91  LYS A CE  1 
ATOM   722  N  NZ  . LYS A 1 91  ? 11.843 12.863  9.717   1.00 20.65  ? 91  LYS A NZ  1 
ATOM   723  N  N   . GLN A 1 92  ? 8.215  8.018   11.278  1.00 8.03   ? 92  GLN A N   1 
ATOM   724  C  CA  . GLN A 1 92  ? 8.517  6.888   10.405  1.00 7.63   ? 92  GLN A CA  1 
ATOM   725  C  C   . GLN A 1 92  ? 8.263  5.624   11.192  1.00 7.40   ? 92  GLN A C   1 
ATOM   726  O  O   . GLN A 1 92  ? 8.190  5.664   12.428  1.00 8.12   ? 92  GLN A O   1 
ATOM   727  C  CB  . GLN A 1 92  ? 9.999  6.928   9.933   1.00 8.41   ? 92  GLN A CB  1 
ATOM   728  C  CG  . GLN A 1 92  ? 11.027 6.993   11.089  1.00 10.42  ? 92  GLN A CG  1 
ATOM   729  C  CD  . GLN A 1 92  ? 11.888 5.757   11.098  1.00 10.05  ? 92  GLN A CD  1 
ATOM   730  O  OE1 . GLN A 1 92  ? 11.349 4.686   11.334  1.00 12.66  ? 92  GLN A OE1 1 
ATOM   731  N  NE2 . GLN A 1 92  ? 13.187 5.875   11.008  1.00 20.11  ? 92  GLN A NE2 1 
ATOM   732  N  N   . PHE A 1 93  ? 8.172  4.521   10.424  1.00 6.72   ? 93  PHE A N   1 
ATOM   733  C  CA  . PHE A 1 93  ? 8.275  3.240   11.073  1.00 6.04   ? 93  PHE A CA  1 
ATOM   734  C  C   . PHE A 1 93  ? 9.309  2.422   10.306  1.00 5.88   ? 93  PHE A C   1 
ATOM   735  O  O   . PHE A 1 93  ? 9.553  2.635   9.114   1.00 7.39   ? 93  PHE A O   1 
ATOM   736  C  CB  . PHE A 1 93  ? 6.935  2.505   11.271  1.00 7.70   ? 93  PHE A CB  1 
ATOM   737  C  CG  . PHE A 1 93  ? 6.239  2.020   10.028  1.00 6.57   ? 93  PHE A CG  1 
ATOM   738  C  CD1 . PHE A 1 93  ? 6.659  0.918   9.311   1.00 7.43   ? 93  PHE A CD1 1 
ATOM   739  C  CD2 . PHE A 1 93  ? 5.090  2.683   9.611   1.00 6.99   ? 93  PHE A CD2 1 
ATOM   740  C  CE1 . PHE A 1 93  ? 6.002  0.487   8.144   1.00 8.58   ? 93  PHE A CE1 1 
ATOM   741  C  CE2 . PHE A 1 93  ? 4.388  2.231   8.496   1.00 7.88   ? 93  PHE A CE2 1 
ATOM   742  C  CZ  . PHE A 1 93  ? 4.844  1.147   7.753   1.00 8.88   ? 93  PHE A CZ  1 
ATOM   743  N  N   . HIS A 1 94  ? 9.836  1.401   11.010  1.00 6.30   ? 94  HIS A N   1 
ATOM   744  C  CA  . HIS A 1 94  ? 10.783 0.493   10.383  1.00 6.43   ? 94  HIS A CA  1 
ATOM   745  C  C   . HIS A 1 94  ? 10.726 -0.833  11.093  1.00 5.25   ? 94  HIS A C   1 
ATOM   746  O  O   . HIS A 1 94  ? 10.031 -0.962  12.111  1.00 6.32   ? 94  HIS A O   1 
ATOM   747  C  CB  . HIS A 1 94  ? 12.225 1.104   10.418  1.00 7.28   ? 94  HIS A CB  1 
ATOM   748  C  CG  . HIS A 1 94  ? 12.737 1.307   11.802  1.00 5.77   ? 94  HIS A CG  1 
ATOM   749  N  ND1 . HIS A 1 94  ? 12.596 2.516   12.493  1.00 6.05   ? 94  HIS A ND1 1 
ATOM   750  C  CD2 . HIS A 1 94  ? 13.347 0.460   12.717  1.00 6.68   ? 94  HIS A CD2 1 
ATOM   751  C  CE1 . HIS A 1 94  ? 13.121 2.378   13.729  1.00 5.30   ? 94  HIS A CE1 1 
ATOM   752  N  NE2 . HIS A 1 94  ? 13.591 1.145   13.901  1.00 5.08   ? 94  HIS A NE2 1 
ATOM   753  N  N   . PHE A 1 95  ? 11.471 -1.806  10.536  1.00 6.47   ? 95  PHE A N   1 
ATOM   754  C  CA  . PHE A 1 95  ? 11.534 -3.105  11.162  1.00 5.22   ? 95  PHE A CA  1 
ATOM   755  C  C   . PHE A 1 95  ? 12.978 -3.535  11.336  1.00 5.53   ? 95  PHE A C   1 
ATOM   756  O  O   . PHE A 1 95  ? 13.885 -3.120  10.630  1.00 7.06   ? 95  PHE A O   1 
ATOM   757  C  CB  . PHE A 1 95  ? 10.838 -4.155  10.284  1.00 6.43   ? 95  PHE A CB  1 
ATOM   758  C  CG  . PHE A 1 95  ? 9.367  -3.906  10.007  1.00 6.35   ? 95  PHE A CG  1 
ATOM   759  C  CD1 . PHE A 1 95  ? 8.976  -3.015  9.004   1.00 8.09   ? 95  PHE A CD1 1 
ATOM   760  C  CD2 . PHE A 1 95  ? 8.373  -4.591  10.706  1.00 7.76   ? 95  PHE A CD2 1 
ATOM   761  C  CE1 . PHE A 1 95  ? 7.649  -2.822  8.718   1.00 8.03   ? 95  PHE A CE1 1 
ATOM   762  C  CE2 . PHE A 1 95  ? 7.028  -4.411  10.384  1.00 7.99   ? 95  PHE A CE2 1 
ATOM   763  C  CZ  . PHE A 1 95  ? 6.676  -3.520  9.378   1.00 8.79   ? 95  PHE A CZ  1 
ATOM   764  N  N   . HIS A 1 96  ? 13.128 -4.476  12.286  1.00 6.32   ? 96  HIS A N   1 
ATOM   765  C  CA  . HIS A 1 96  ? 14.340 -5.285  12.400  1.00 6.19   ? 96  HIS A CA  1 
ATOM   766  C  C   . HIS A 1 96  ? 13.875 -6.740  12.310  1.00 5.61   ? 96  HIS A C   1 
ATOM   767  O  O   . HIS A 1 96  ? 12.798 -7.069  12.787  1.00 6.66   ? 96  HIS A O   1 
ATOM   768  C  CB  . HIS A 1 96  ? 15.081 -5.098  13.768  1.00 6.78   ? 96  HIS A CB  1 
ATOM   769  C  CG  . HIS A 1 96  ? 15.275 -3.658  14.128  1.00 6.11   ? 96  HIS A CG  1 
ATOM   770  N  ND1 . HIS A 1 96  ? 16.511 -3.028  13.958  1.00 5.93   ? 96  HIS A ND1 1 
ATOM   771  C  CD2 . HIS A 1 96  ? 14.419 -2.702  14.510  1.00 6.55   ? 96  HIS A CD2 1 
ATOM   772  C  CE1 . HIS A 1 96  ? 16.419 -1.756  14.363  1.00 5.72   ? 96  HIS A CE1 1 
ATOM   773  N  NE2 . HIS A 1 96  ? 15.154 -1.471  14.645  1.00 6.34   ? 96  HIS A NE2 1 
ATOM   774  N  N   . TRP A 1 97  ? 14.699 -7.596  11.678  1.00 5.96   ? 97  TRP A N   1 
ATOM   775  C  CA  . TRP A 1 97  ? 14.280 -8.982  11.514  1.00 6.04   ? 97  TRP A CA  1 
ATOM   776  C  C   . TRP A 1 97  ? 15.478 -9.896  11.409  1.00 6.21   ? 97  TRP A C   1 
ATOM   777  O  O   . TRP A 1 97  ? 16.648 -9.499  11.324  1.00 6.59   ? 97  TRP A O   1 
ATOM   778  C  CB  . TRP A 1 97  ? 13.361 -9.136  10.279  1.00 6.58   ? 97  TRP A CB  1 
ATOM   779  C  CG  . TRP A 1 97  ? 14.002 -8.744  8.991   1.00 6.14   ? 97  TRP A CG  1 
ATOM   780  C  CD1 . TRP A 1 97  ? 14.700 -9.584  8.173   1.00 7.06   ? 97  TRP A CD1 1 
ATOM   781  C  CD2 . TRP A 1 97  ? 14.115 -7.441  8.420   1.00 6.53   ? 97  TRP A CD2 1 
ATOM   782  N  NE1 . TRP A 1 97  ? 15.198 -8.912  7.067   1.00 7.50   ? 97  TRP A NE1 1 
ATOM   783  C  CE2 . TRP A 1 97  ? 14.822 -7.574  7.203   1.00 6.96   ? 97  TRP A CE2 1 
ATOM   784  C  CE3 . TRP A 1 97  ? 13.661 -6.166  8.783   1.00 7.05   ? 97  TRP A CE3 1 
ATOM   785  C  CZ2 . TRP A 1 97  ? 15.068 -6.493  6.369   1.00 7.85   ? 97  TRP A CZ2 1 
ATOM   786  C  CZ3 . TRP A 1 97  ? 13.890 -5.089  7.980   1.00 7.34   ? 97  TRP A CZ3 1 
ATOM   787  C  CH2 . TRP A 1 97  ? 14.594 -5.282  6.771   1.00 8.19   ? 97  TRP A CH2 1 
ATOM   788  N  N   . GLY A 1 98  ? 15.150 -11.202 11.430  1.00 6.27   ? 98  GLY A N   1 
ATOM   789  C  CA  . GLY A 1 98  ? 16.189 -12.219 11.478  1.00 7.21   ? 98  GLY A CA  1 
ATOM   790  C  C   . GLY A 1 98  ? 16.386 -12.969 10.167  1.00 7.01   ? 98  GLY A C   1 
ATOM   791  O  O   . GLY A 1 98  ? 15.643 -12.790 9.197   1.00 7.91   ? 98  GLY A O   1 
ATOM   792  N  N   . SER A 1 99  ? 17.374 -13.900 10.241  1.00 7.75   ? 99  SER A N   1 
ATOM   793  C  CA  . SER A 1 99  ? 17.571 -14.870 9.147   1.00 8.45   ? 99  SER A CA  1 
ATOM   794  C  C   . SER A 1 99  ? 16.711 -16.121 9.325   1.00 8.59   ? 99  SER A C   1 
ATOM   795  O  O   . SER A 1 99  ? 16.556 -16.896 8.393   1.00 11.28  ? 99  SER A O   1 
ATOM   796  C  CB  . SER A 1 99  ? 19.025 -15.200 9.072   1.00 9.08   ? 99  SER A CB  1 
ATOM   797  O  OG  . SER A 1 99  ? 19.495 -15.670 10.340  1.00 9.85   ? 99  SER A OG  1 
ATOM   798  N  N   . LEU A 1 100 ? 16.181 -16.339 10.531  1.00 8.12   ? 100 LEU A N   1 
ATOM   799  C  CA  . LEU A 1 100 ? 15.369 -17.508 10.899  1.00 8.00   ? 100 LEU A CA  1 
ATOM   800  C  C   . LEU A 1 100 ? 14.183 -16.985 11.712  1.00 8.46   ? 100 LEU A C   1 
ATOM   801  O  O   . LEU A 1 100 ? 14.270 -15.942 12.370  1.00 8.68   ? 100 LEU A O   1 
ATOM   802  C  CB  . LEU A 1 100 ? 16.193 -18.422 11.812  1.00 9.80   ? 100 LEU A CB  1 
ATOM   803  C  CG  . LEU A 1 100 ? 17.488 -18.974 11.217  1.00 10.59  ? 100 LEU A CG  1 
ATOM   804  C  CD1 . LEU A 1 100 ? 18.305 -19.690 12.306  1.00 16.15  ? 100 LEU A CD1 1 
ATOM   805  C  CD2 . LEU A 1 100 ? 17.129 -19.944 10.091  1.00 13.02  ? 100 LEU A CD2 1 
ATOM   806  N  N   . ASP A 1 101 ? 13.105 -17.754 11.771  1.00 8.52   ? 101 ASP A N   1 
ATOM   807  C  CA  . ASP A 1 101 ? 11.871 -17.284 12.357  1.00 9.10   ? 101 ASP A CA  1 
ATOM   808  C  C   . ASP A 1 101 ? 11.966 -17.105 13.861  1.00 10.28  ? 101 ASP A C   1 
ATOM   809  O  O   . ASP A 1 101 ? 11.151 -16.361 14.416  1.00 12.90  ? 101 ASP A O   1 
ATOM   810  C  CB  . ASP A 1 101 ? 10.712 -18.245 12.088  1.00 10.47  ? 101 ASP A CB  1 
ATOM   811  C  CG  . ASP A 1 101 ? 10.264 -18.314 10.654  1.00 12.23  ? 101 ASP A CG  1 
ATOM   812  O  OD1 . ASP A 1 101 ? 10.571 -17.423 9.822   1.00 11.14  ? 101 ASP A OD1 1 
ATOM   813  O  OD2 . ASP A 1 101 ? 9.586  -19.263 10.340  1.00 17.03  ? 101 ASP A OD2 1 
ATOM   814  N  N   . GLY A 1 102 ? 12.970 -17.697 14.515  1.00 10.12  ? 102 GLY A N   1 
ATOM   815  C  CA  . GLY A 1 102 ? 13.093 -17.510 15.948  1.00 12.55  ? 102 GLY A CA  1 
ATOM   816  C  C   . GLY A 1 102 ? 14.128 -16.483 16.403  1.00 11.41  ? 102 GLY A C   1 
ATOM   817  O  O   . GLY A 1 102 ? 14.543 -16.476 17.558  1.00 12.23  ? 102 GLY A O   1 
ATOM   818  N  N   . GLN A 1 103 ? 14.492 -15.559 15.512  1.00 9.00   ? 103 GLN A N   1 
ATOM   819  C  CA  . GLN A 1 103 ? 15.331 -14.432 15.910  1.00 8.43   ? 103 GLN A CA  1 
ATOM   820  C  C   . GLN A 1 103 ? 14.962 -13.258 15.018  1.00 7.01   ? 103 GLN A C   1 
ATOM   821  O  O   . GLN A 1 103 ? 14.435 -13.466 13.940  1.00 7.86   ? 103 GLN A O   1 
ATOM   822  C  CB  . GLN A 1 103 ? 16.806 -14.769 15.866  1.00 9.11   ? 103 GLN A CB  1 
ATOM   823  C  CG  . GLN A 1 103 ? 17.260 -15.042 14.419  1.00 9.61   ? 103 GLN A CG  1 
ATOM   824  C  CD  . GLN A 1 103 ? 18.600 -15.732 14.396  1.00 10.00  ? 103 GLN A CD  1 
ATOM   825  O  OE1 . GLN A 1 103 ? 18.694 -16.850 14.898  1.00 12.84  ? 103 GLN A OE1 1 
ATOM   826  N  NE2 . GLN A 1 103 ? 19.634 -15.138 13.804  1.00 10.94  ? 103 GLN A NE2 1 
ATOM   827  N  N   . GLY A 1 104 ? 15.329 -12.038 15.489  1.00 6.47   ? 104 GLY A N   1 
ATOM   828  C  CA  . GLY A 1 104 ? 15.037 -10.869 14.672  1.00 6.71   ? 104 GLY A CA  1 
ATOM   829  C  C   . GLY A 1 104 ? 14.592 -9.714  15.543  1.00 6.35   ? 104 GLY A C   1 
ATOM   830  O  O   . GLY A 1 104 ? 14.805 -8.563  15.156  1.00 8.06   ? 104 GLY A O   1 
ATOM   831  N  N   . SER A 1 105 ? 13.901 -9.984  16.670  1.00 6.20   ? 105 SER A N   1 
ATOM   832  C  CA  . SER A 1 105 ? 13.476 -8.889  17.518  1.00 5.76   ? 105 SER A CA  1 
ATOM   833  C  C   . SER A 1 105 ? 14.672 -8.342  18.276  1.00 6.27   ? 105 SER A C   1 
ATOM   834  O  O   . SER A 1 105 ? 15.697 -8.995  18.468  1.00 7.03   ? 105 SER A O   1 
ATOM   835  C  CB  . SER A 1 105 ? 12.352 -9.253  18.462  1.00 6.73   ? 105 SER A CB  1 
ATOM   836  O  OG  . SER A 1 105 ? 12.731 -10.242 19.411  1.00 6.78   ? 105 SER A OG  1 
ATOM   837  N  N   . GLU A 1 106 ? 14.538 -7.105  18.688  1.00 6.02   ? 106 GLU A N   1 
ATOM   838  C  CA  . GLU A 1 106 ? 15.541 -6.393  19.508  1.00 5.71   ? 106 GLU A CA  1 
ATOM   839  C  C   . GLU A 1 106 ? 15.220 -6.620  20.977  1.00 5.46   ? 106 GLU A C   1 
ATOM   840  O  O   . GLU A 1 106 ? 15.984 -7.187  21.752  1.00 6.08   ? 106 GLU A O   1 
ATOM   841  C  CB  . GLU A 1 106 ? 15.586 -4.919  19.103  1.00 6.47   ? 106 GLU A CB  1 
ATOM   842  C  CG  . GLU A 1 106 ? 15.952 -4.771  17.624  1.00 6.87   ? 106 GLU A CG  1 
ATOM   843  C  CD  . GLU A 1 106 ? 16.670 -3.491  17.343  1.00 6.50   ? 106 GLU A CD  1 
ATOM   844  O  OE1 . GLU A 1 106 ? 16.069 -2.437  17.581  1.00 6.72   ? 106 GLU A OE1 1 
ATOM   845  O  OE2 . GLU A 1 106 ? 17.851 -3.576  16.934  1.00 6.83   ? 106 GLU A OE2 1 
ATOM   846  N  N   . HIS A 1 107 ? 14.032 -6.176  21.401  1.00 6.11   ? 107 HIS A N   1 
ATOM   847  C  CA  . HIS A 1 107 ? 13.582 -6.593  22.727  1.00 6.51   ? 107 HIS A CA  1 
ATOM   848  C  C   . HIS A 1 107 ? 13.303 -8.077  22.727  1.00 6.65   ? 107 HIS A C   1 
ATOM   849  O  O   . HIS A 1 107 ? 12.939 -8.694  21.689  1.00 6.48   ? 107 HIS A O   1 
ATOM   850  C  CB  . HIS A 1 107 ? 12.318 -5.795  23.104  1.00 6.36   ? 107 HIS A CB  1 
ATOM   851  C  CG  . HIS A 1 107 ? 12.633 -4.342  23.271  1.00 5.59   ? 107 HIS A CG  1 
ATOM   852  N  ND1 . HIS A 1 107 ? 12.577 -3.443  22.226  1.00 5.94   ? 107 HIS A ND1 1 
ATOM   853  C  CD2 . HIS A 1 107 ? 13.083 -3.629  24.367  1.00 5.82   ? 107 HIS A CD2 1 
ATOM   854  C  CE1 . HIS A 1 107 ? 12.976 -2.224  22.686  1.00 6.48   ? 107 HIS A CE1 1 
ATOM   855  N  NE2 . HIS A 1 107 ? 13.343 -2.320  23.936  1.00 6.40   ? 107 HIS A NE2 1 
ATOM   856  N  N   . THR A 1 108 ? 13.406 -8.630  23.939  1.00 7.29   ? 108 THR A N   1 
ATOM   857  C  CA  . THR A 1 108 ? 13.001 -10.020 24.138  1.00 7.90   ? 108 THR A CA  1 
ATOM   858  C  C   . THR A 1 108 ? 12.040 -10.010 25.329  1.00 6.77   ? 108 THR A C   1 
ATOM   859  O  O   . THR A 1 108 ? 12.022 -9.082  26.131  1.00 8.00   ? 108 THR A O   1 
ATOM   860  C  CB  . THR A 1 108 ? 14.228 -10.932 24.324  1.00 8.84   ? 108 THR A CB  1 
ATOM   861  O  OG1 . THR A 1 108 ? 15.013 -10.450 25.446  1.00 8.05   ? 108 THR A OG1 1 
ATOM   862  C  CG2 . THR A 1 108 ? 15.066 -10.992 23.082  1.00 9.40   ? 108 THR A CG2 1 
ATOM   863  N  N   . VAL A 1 109 ? 11.281 -11.095 25.490  1.00 9.37   ? 109 VAL A N   1 
ATOM   864  C  CA  . VAL A 1 109 ? 10.303 -11.212 26.565  1.00 10.08  ? 109 VAL A CA  1 
ATOM   865  C  C   . VAL A 1 109 ? 10.614 -12.520 27.299  1.00 9.80   ? 109 VAL A C   1 
ATOM   866  O  O   . VAL A 1 109 ? 10.464 -13.586 26.704  1.00 11.75  ? 109 VAL A O   1 
ATOM   867  C  CB  . VAL A 1 109 ? 8.846  -11.192 26.025  1.00 10.91  ? 109 VAL A CB  1 
ATOM   868  C  CG1 . VAL A 1 109 ? 7.822  -11.356 27.176  1.00 12.90  ? 109 VAL A CG1 1 
ATOM   869  C  CG2 . VAL A 1 109 ? 8.564  -9.939  25.240  1.00 11.47  ? 109 VAL A CG2 1 
ATOM   870  N  N   . ASP A 1 110 ? 11.124 -12.440 28.534  1.00 10.13  ? 110 ASP A N   1 
ATOM   871  C  CA  . ASP A 1 110 ? 11.545 -13.637 29.256  1.00 10.94  ? 110 ASP A CA  1 
ATOM   872  C  C   . ASP A 1 110 ? 12.502 -14.431 28.361  1.00 11.65  ? 110 ASP A C   1 
ATOM   873  O  O   . ASP A 1 110 ? 12.439 -15.679 28.299  1.00 12.83  ? 110 ASP A O   1 
ATOM   874  C  CB  . ASP A 1 110 ? 10.331 -14.471 29.721  1.00 14.26  ? 110 ASP A CB  1 
ATOM   875  C  CG  . ASP A 1 110 ? 9.516  -13.709 30.749  1.00 15.10  ? 110 ASP A CG  1 
ATOM   876  O  OD1 . ASP A 1 110 ? 10.098 -12.837 31.418  1.00 15.87  ? 110 ASP A OD1 1 
ATOM   877  O  OD2 . ASP A 1 110 ? 8.305  -13.976 30.839  1.00 18.70  ? 110 ASP A OD2 1 
ATOM   878  N  N   . LYS A 1 111 ? 13.420 -13.699 27.688  1.00 10.09  ? 111 LYS A N   1 
ATOM   879  C  CA  . LYS A 1 111 ? 14.467 -14.223 26.817  1.00 10.39  ? 111 LYS A CA  1 
ATOM   880  C  C   . LYS A 1 111 ? 13.911 -14.740 25.486  1.00 11.59  ? 111 LYS A C   1 
ATOM   881  O  O   . LYS A 1 111 ? 14.732 -15.031 24.618  1.00 13.00  ? 111 LYS A O   1 
ATOM   882  C  CB  . LYS A 1 111 ? 15.400 -15.232 27.500  1.00 12.67  ? 111 LYS A CB  1 
ATOM   883  C  CG  . LYS A 1 111 ? 16.062 -14.680 28.768  1.00 14.68  ? 111 LYS A CG  1 
ATOM   884  C  CD  . LYS A 1 111 ? 17.081 -13.561 28.482  1.00 18.90  ? 111 LYS A CD  1 
ATOM   885  C  CE  . LYS A 1 111 ? 17.777 -12.913 29.661  1.00 22.20  ? 111 LYS A CE  1 
ATOM   886  N  NZ  . LYS A 1 111 ? 18.945 -13.700 30.027  1.00 27.41  ? 111 LYS A NZ  1 
ATOM   887  N  N   . LYS A 1 112 ? 12.591 -14.685 25.279  1.00 10.56  ? 112 LYS A N   1 
ATOM   888  C  CA  . LYS A 1 112 ? 12.075 -15.099 23.980  1.00 13.26  ? 112 LYS A CA  1 
ATOM   889  C  C   . LYS A 1 112 ? 12.366 -14.023 22.928  1.00 10.26  ? 112 LYS A C   1 
ATOM   890  O  O   . LYS A 1 112 ? 12.045 -12.848 23.125  1.00 9.82   ? 112 LYS A O   1 
ATOM   891  C  CB  . LYS A 1 112 ? 10.555 -15.233 24.087  1.00 13.36  ? 112 LYS A CB  1 
ATOM   892  C  CG  . LYS A 1 112 ? 9.824  -15.702 22.855  1.00 14.31  ? 112 LYS A CG  1 
ATOM   893  C  CD  . LYS A 1 112 ? 8.283  -15.767 22.944  1.00 17.29  ? 112 LYS A CD  1 
ATOM   894  C  CE  . LYS A 1 112 ? 7.698  -15.886 21.549  1.00 22.57  ? 112 LYS A CE  1 
ATOM   895  N  NZ  . LYS A 1 112 ? 7.998  -17.169 20.895  1.00 29.32  ? 112 LYS A NZ  1 
ATOM   896  N  N   . LYS A 1 113 ? 12.843 -14.471 21.772  1.00 10.28  ? 113 LYS A N   1 
ATOM   897  C  CA  . LYS A 1 113 ? 13.030 -13.636 20.592  1.00 10.00  ? 113 LYS A CA  1 
ATOM   898  C  C   . LYS A 1 113 ? 11.890 -13.897 19.616  1.00 9.79   ? 113 LYS A C   1 
ATOM   899  O  O   . LYS A 1 113 ? 11.447 -15.040 19.429  1.00 12.76  ? 113 LYS A O   1 
ATOM   900  C  CB  . LYS A 1 113 ? 14.349 -13.972 19.883  1.00 10.51  ? 113 LYS A CB  1 
ATOM   901  C  CG  . LYS A 1 113 ? 15.586 -13.659 20.703  1.00 9.83   ? 113 LYS A CG  1 
ATOM   902  C  CD  . LYS A 1 113 ? 16.865 -14.276 20.064  1.00 12.15  ? 113 LYS A CD  1 
ATOM   903  C  CE  . LYS A 1 113 ? 18.059 -13.619 20.720  1.00 13.17  ? 113 LYS A CE  1 
ATOM   904  N  NZ  . LYS A 1 113 ? 19.255 -14.414 20.901  1.00 25.45  ? 113 LYS A NZ  1 
ATOM   905  N  N   . TYR A 1 114 ? 11.438 -12.809 18.995  1.00 8.17   ? 114 TYR A N   1 
ATOM   906  C  CA  . TYR A 1 114 ? 10.445 -12.896 17.923  1.00 7.66   ? 114 TYR A CA  1 
ATOM   907  C  C   . TYR A 1 114 ? 11.086 -12.790 16.538  1.00 7.28   ? 114 TYR A C   1 
ATOM   908  O  O   . TYR A 1 114 ? 12.305 -12.514 16.448  1.00 7.61   ? 114 TYR A O   1 
ATOM   909  C  CB  . TYR A 1 114 ? 9.370  -11.808 18.085  1.00 8.51   ? 114 TYR A CB  1 
ATOM   910  C  CG  . TYR A 1 114 ? 8.475  -12.031 19.255  1.00 8.09   ? 114 TYR A CG  1 
ATOM   911  C  CD1 . TYR A 1 114 ? 8.808  -11.624 20.545  1.00 10.40  ? 114 TYR A CD1 1 
ATOM   912  C  CD2 . TYR A 1 114 ? 7.289  -12.720 19.052  1.00 10.06  ? 114 TYR A CD2 1 
ATOM   913  C  CE1 . TYR A 1 114 ? 7.950  -11.840 21.617  1.00 11.81  ? 114 TYR A CE1 1 
ATOM   914  C  CE2 . TYR A 1 114 ? 6.414  -12.944 20.125  1.00 11.81  ? 114 TYR A CE2 1 
ATOM   915  C  CZ  . TYR A 1 114 ? 6.738  -12.476 21.386  1.00 13.07  ? 114 TYR A CZ  1 
ATOM   916  O  OH  . TYR A 1 114 ? 5.924  -12.680 22.467  1.00 20.69  ? 114 TYR A OH  1 
ATOM   917  N  N   . ALA A 1 115 ? 10.331 -13.065 15.471  1.00 7.47   ? 115 ALA A N   1 
ATOM   918  C  CA  . ALA A 1 115 ? 10.931 -13.097 14.130  1.00 7.43   ? 115 ALA A CA  1 
ATOM   919  C  C   . ALA A 1 115 ? 11.284 -11.694 13.666  1.00 7.49   ? 115 ALA A C   1 
ATOM   920  O  O   . ALA A 1 115 ? 12.121 -11.512 12.790  1.00 7.89   ? 115 ALA A O   1 
ATOM   921  C  CB  . ALA A 1 115 ? 9.882  -13.668 13.171  1.00 8.74   ? 115 ALA A CB  1 
ATOM   922  N  N   . ALA A 1 116 ? 10.631 -10.663 14.247  1.00 7.18   ? 116 ALA A N   1 
ATOM   923  C  CA  . ALA A 1 116 ? 10.900 -9.294  13.790  1.00 7.69   ? 116 ALA A CA  1 
ATOM   924  C  C   . ALA A 1 116 ? 10.307 -8.372  14.853  1.00 6.63   ? 116 ALA A C   1 
ATOM   925  O  O   . ALA A 1 116 ? 9.577  -8.802  15.730  1.00 7.02   ? 116 ALA A O   1 
ATOM   926  C  CB  . ALA A 1 116 ? 10.309 -9.024  12.381  1.00 7.89   ? 116 ALA A CB  1 
ATOM   927  N  N   . GLU A 1 117 ? 10.621 -7.077  14.687  1.00 6.28   ? 117 GLU A N   1 
ATOM   928  C  CA  . GLU A 1 117 ? 10.081 -6.064  15.606  1.00 6.68   ? 117 GLU A CA  1 
ATOM   929  C  C   . GLU A 1 117 ? 9.874  -4.814  14.766  1.00 5.79   ? 117 GLU A C   1 
ATOM   930  O  O   . GLU A 1 117 ? 10.768 -4.378  14.052  1.00 7.02   ? 117 GLU A O   1 
ATOM   931  C  CB  . GLU A 1 117 ? 11.028 -5.843  16.778  1.00 6.92   ? 117 GLU A CB  1 
ATOM   932  C  CG  . GLU A 1 117 ? 10.434 -4.998  17.910  1.00 6.73   ? 117 GLU A CG  1 
ATOM   933  C  CD  . GLU A 1 117 ? 11.355 -4.918  19.095  1.00 5.86   ? 117 GLU A CD  1 
ATOM   934  O  OE1 . GLU A 1 117 ? 12.072 -5.900  19.388  1.00 6.49   ? 117 GLU A OE1 1 
ATOM   935  O  OE2 . GLU A 1 117 ? 11.360 -3.871  19.804  1.00 6.64   ? 117 GLU A OE2 1 
ATOM   936  N  N   . LEU A 1 118 ? 8.662  -4.268  14.898  1.00 5.69   ? 118 LEU A N   1 
ATOM   937  C  CA  . LEU A 1 118 ? 8.228  -3.047  14.255  1.00 5.78   ? 118 LEU A CA  1 
ATOM   938  C  C   . LEU A 1 118 ? 8.448  -1.930  15.264  1.00 5.74   ? 118 LEU A C   1 
ATOM   939  O  O   . LEU A 1 118 ? 7.991  -1.995  16.396  1.00 5.83   ? 118 LEU A O   1 
ATOM   940  C  CB  . LEU A 1 118 ? 6.732  -3.212  13.923  1.00 6.83   ? 118 LEU A CB  1 
ATOM   941  C  CG  . LEU A 1 118 ? 5.939  -1.922  13.572  1.00 6.57   ? 118 LEU A CG  1 
ATOM   942  C  CD1 . LEU A 1 118 ? 6.499  -1.207  12.330  1.00 7.32   ? 118 LEU A CD1 1 
ATOM   943  C  CD2 . LEU A 1 118 ? 4.474  -2.334  13.370  1.00 8.41   ? 118 LEU A CD2 1 
ATOM   944  N  N   . HIS A 1 119 ? 9.060  -0.838  14.774  1.00 5.17   ? 119 HIS A N   1 
ATOM   945  C  CA  . HIS A 1 119 ? 9.284  0.369   15.558  1.00 5.39   ? 119 HIS A CA  1 
ATOM   946  C  C   . HIS A 1 119 ? 8.627  1.559   14.884  1.00 5.46   ? 119 HIS A C   1 
ATOM   947  O  O   . HIS A 1 119 ? 9.004  1.898   13.751  1.00 6.61   ? 119 HIS A O   1 
ATOM   948  C  CB  . HIS A 1 119 ? 10.807 0.603   15.651  1.00 5.36   ? 119 HIS A CB  1 
ATOM   949  C  CG  . HIS A 1 119 ? 11.440 -0.394  16.557  1.00 5.01   ? 119 HIS A CG  1 
ATOM   950  N  ND1 . HIS A 1 119 ? 12.815 -0.637  16.565  1.00 5.48   ? 119 HIS A ND1 1 
ATOM   951  C  CD2 . HIS A 1 119 ? 10.908 -1.180  17.545  1.00 5.51   ? 119 HIS A CD2 1 
ATOM   952  C  CE1 . HIS A 1 119 ? 13.080 -1.546  17.499  1.00 5.84   ? 119 HIS A CE1 1 
ATOM   953  N  NE2 . HIS A 1 119 ? 11.946 -1.889  18.100  1.00 5.92   ? 119 HIS A NE2 1 
ATOM   954  N  N   . LEU A 1 120 ? 7.650  2.180   15.605  1.00 5.59   ? 120 LEU A N   1 
ATOM   955  C  CA  . LEU A 1 120 ? 7.019  3.423   15.138  1.00 5.94   ? 120 LEU A CA  1 
ATOM   956  C  C   . LEU A 1 120 ? 7.677  4.560   15.916  1.00 5.84   ? 120 LEU A C   1 
ATOM   957  O  O   . LEU A 1 120 ? 7.598  4.592   17.138  1.00 5.76   ? 120 LEU A O   1 
ATOM   958  C  CB  . LEU A 1 120 ? 5.513  3.340   15.352  1.00 6.47   ? 120 LEU A CB  1 
ATOM   959  C  CG  . LEU A 1 120 ? 4.829  2.281   14.488  1.00 7.21   ? 120 LEU A CG  1 
ATOM   960  C  CD1 . LEU A 1 120 ? 4.116  1.290   15.394  1.00 11.97  ? 120 LEU A CD1 1 
ATOM   961  C  CD2 . LEU A 1 120 ? 3.874  2.931   13.493  1.00 10.24  ? 120 LEU A CD2 1 
ATOM   962  N  N   . VAL A 1 121 ? 8.439  5.404   15.216  1.00 5.81   ? 121 VAL A N   1 
ATOM   963  C  CA  . VAL A 1 121 ? 9.291  6.420   15.851  1.00 6.55   ? 121 VAL A CA  1 
ATOM   964  C  C   . VAL A 1 121 ? 8.526  7.754   15.846  1.00 6.97   ? 121 VAL A C   1 
ATOM   965  O  O   . VAL A 1 121 ? 8.151  8.279   14.795  1.00 7.83   ? 121 VAL A O   1 
ATOM   966  C  CB  . VAL A 1 121 ? 10.612 6.549   15.066  1.00 7.09   ? 121 VAL A CB  1 
ATOM   967  C  CG1 . VAL A 1 121 ? 11.506 7.633   15.669  1.00 9.64   ? 121 VAL A CG1 1 
ATOM   968  C  CG2 . VAL A 1 121 ? 11.372 5.218   14.943  1.00 7.35   ? 121 VAL A CG2 1 
ATOM   969  N  N   . HIS A 1 122 ? 8.482  8.369   17.048  1.00 6.18   ? 122 HIS A N   1 
ATOM   970  C  CA  . HIS A 1 122 ? 7.794  9.636   17.240  1.00 6.49   ? 122 HIS A CA  1 
ATOM   971  C  C   . HIS A 1 122 ? 8.732  10.601  17.948  1.00 6.66   ? 122 HIS A C   1 
ATOM   972  O  O   . HIS A 1 122 ? 9.516  10.194  18.795  1.00 8.11   ? 122 HIS A O   1 
ATOM   973  C  CB  . HIS A 1 122 ? 6.538  9.434   18.124  1.00 7.14   ? 122 HIS A CB  1 
ATOM   974  C  CG  . HIS A 1 122 ? 5.640  8.322   17.759  1.00 6.72   ? 122 HIS A CG  1 
ATOM   975  N  ND1 . HIS A 1 122 ? 5.979  6.991   17.992  1.00 6.97   ? 122 HIS A ND1 1 
ATOM   976  C  CD2 . HIS A 1 122 ? 4.422  8.323   17.133  1.00 7.86   ? 122 HIS A CD2 1 
ATOM   977  C  CE1 . HIS A 1 122 ? 4.960  6.234   17.562  1.00 7.76   ? 122 HIS A CE1 1 
ATOM   978  N  NE2 . HIS A 1 122 ? 3.971  6.993   17.038  1.00 8.01   ? 122 HIS A NE2 1 
ATOM   979  N  N   . TRP A 1 123 ? 8.604  11.900  17.674  1.00 7.04   ? 123 TRP A N   1 
ATOM   980  C  CA  . TRP A 1 123 ? 9.434  12.874  18.398  1.00 6.95   ? 123 TRP A CA  1 
ATOM   981  C  C   . TRP A 1 123 ? 8.550  13.912  19.091  1.00 6.91   ? 123 TRP A C   1 
ATOM   982  O  O   . TRP A 1 123 ? 7.432  14.251  18.626  1.00 7.60   ? 123 TRP A O   1 
ATOM   983  C  CB  . TRP A 1 123 ? 10.437 13.539  17.457  1.00 8.11   ? 123 TRP A CB  1 
ATOM   984  C  CG  . TRP A 1 123 ? 9.842  14.176  16.249  1.00 8.74   ? 123 TRP A CG  1 
ATOM   985  C  CD1 . TRP A 1 123 ? 9.637  13.567  15.021  1.00 8.48   ? 123 TRP A CD1 1 
ATOM   986  C  CD2 . TRP A 1 123 ? 9.476  15.555  16.061  1.00 9.19   ? 123 TRP A CD2 1 
ATOM   987  N  NE1 . TRP A 1 123 ? 9.133  14.443  14.103  1.00 9.62   ? 123 TRP A NE1 1 
ATOM   988  C  CE2 . TRP A 1 123 ? 9.042  15.682  14.708  1.00 9.64   ? 123 TRP A CE2 1 
ATOM   989  C  CE3 . TRP A 1 123 ? 9.487  16.713  16.874  1.00 9.43   ? 123 TRP A CE3 1 
ATOM   990  C  CZ2 . TRP A 1 123 ? 8.606  16.891  14.159  1.00 10.79  ? 123 TRP A CZ2 1 
ATOM   991  C  CZ3 . TRP A 1 123 ? 9.099  17.893  16.295  1.00 10.35  ? 123 TRP A CZ3 1 
ATOM   992  C  CH2 . TRP A 1 123 ? 8.609  17.988  14.995  1.00 11.12  ? 123 TRP A CH2 1 
ATOM   993  N  N   . ASN A 1 124 ? 9.041  14.393  20.243  1.00 7.91   ? 124 ASN A N   1 
ATOM   994  C  CA  . ASN A 1 124 ? 8.305  15.288  21.113  1.00 8.81   ? 124 ASN A CA  1 
ATOM   995  C  C   . ASN A 1 124 ? 8.230  16.660  20.464  1.00 9.30   ? 124 ASN A C   1 
ATOM   996  O  O   . ASN A 1 124 ? 9.250  17.339  20.229  1.00 8.95   ? 124 ASN A O   1 
ATOM   997  C  CB  . ASN A 1 124 ? 9.135  15.306  22.396  1.00 9.70   ? 124 ASN A CB  1 
ATOM   998  C  CG  . ASN A 1 124 ? 8.410  15.976  23.531  1.00 12.15  ? 124 ASN A CG  1 
ATOM   999  O  OD1 . ASN A 1 124 ? 7.573  16.852  23.261  1.00 13.13  ? 124 ASN A OD1 1 
ATOM   1000 N  ND2 . ASN A 1 124 ? 8.636  15.505  24.762  1.00 13.67  ? 124 ASN A ND2 1 
ATOM   1001 N  N   . THR A 1 125 ? 6.999  17.102  20.146  1.00 9.95   ? 125 THR A N   1 
ATOM   1002 C  CA  . THR A 1 125 ? 6.836  18.344  19.388  1.00 11.02  ? 125 THR A CA  1 
ATOM   1003 C  C   . THR A 1 125 ? 7.253  19.590  20.198  1.00 10.50  ? 125 THR A C   1 
ATOM   1004 O  O   . THR A 1 125 ? 7.529  20.599  19.573  1.00 12.08  ? 125 THR A O   1 
ATOM   1005 C  CB  . THR A 1 125 ? 5.399  18.483  18.917  1.00 12.43  ? 125 THR A CB  1 
ATOM   1006 O  OG1 . THR A 1 125 ? 4.569  18.608  20.066  1.00 15.90  ? 125 THR A OG1 1 
ATOM   1007 C  CG2 . THR A 1 125 ? 5.012  17.338  18.007  1.00 16.97  ? 125 THR A CG2 1 
ATOM   1008 N  N   . LYS A 1 126 ? 7.532  19.464  21.516  1.00 11.25  ? 126 LYS A N   1 
ATOM   1009 C  CA  . LYS A 1 126 ? 8.009  20.648  22.218  1.00 13.01  ? 126 LYS A CA  1 
ATOM   1010 C  C   . LYS A 1 126 ? 9.414  21.026  21.760  1.00 12.54  ? 126 LYS A C   1 
ATOM   1011 O  O   . LYS A 1 126 ? 9.820  22.169  21.990  1.00 15.27  ? 126 LYS A O   1 
ATOM   1012 C  CB  . LYS A 1 126 ? 7.925  20.412  23.716  1.00 16.00  ? 126 LYS A CB  1 
ATOM   1013 C  CG  . LYS A 1 126 ? 9.063  19.652  24.327  1.00 17.86  ? 126 LYS A CG  1 
ATOM   1014 C  CD  . LYS A 1 126 ? 8.546  19.282  25.701  1.00 23.92  ? 126 LYS A CD  1 
ATOM   1015 C  CE  . LYS A 1 126 ? 9.687  18.877  26.575  1.00 27.53  ? 126 LYS A CE  1 
ATOM   1016 N  NZ  . LYS A 1 126 ? 9.332  19.014  28.007  1.00 41.26  ? 126 LYS A NZ  1 
ATOM   1017 N  N   . TYR A 1 127 ? 10.142 20.106  21.102  1.00 11.20  ? 127 TYR A N   1 
ATOM   1018 C  CA  . TYR A 1 127 ? 11.474 20.400  20.635  1.00 10.12  ? 127 TYR A CA  1 
ATOM   1019 C  C   . TYR A 1 127 ? 11.522 20.851  19.163  1.00 10.10  ? 127 TYR A C   1 
ATOM   1020 O  O   . TYR A 1 127 ? 12.625 21.159  18.662  1.00 11.64  ? 127 TYR A O   1 
ATOM   1021 C  CB  . TYR A 1 127 ? 12.442 19.241  20.866  1.00 10.06  ? 127 TYR A CB  1 
ATOM   1022 C  CG  . TYR A 1 127 ? 12.497 18.883  22.324  1.00 11.01  ? 127 TYR A CG  1 
ATOM   1023 C  CD1 . TYR A 1 127 ? 12.855 19.869  23.247  1.00 13.51  ? 127 TYR A CD1 1 
ATOM   1024 C  CD2 . TYR A 1 127 ? 12.216 17.591  22.791  1.00 10.81  ? 127 TYR A CD2 1 
ATOM   1025 C  CE1 . TYR A 1 127 ? 12.899 19.565  24.610  1.00 13.30  ? 127 TYR A CE1 1 
ATOM   1026 C  CE2 . TYR A 1 127 ? 12.239 17.287  24.147  1.00 11.61  ? 127 TYR A CE2 1 
ATOM   1027 C  CZ  . TYR A 1 127 ? 12.605 18.294  25.043  1.00 13.37  ? 127 TYR A CZ  1 
ATOM   1028 O  OH  . TYR A 1 127 ? 12.674 18.033  26.371  1.00 16.91  ? 127 TYR A OH  1 
ATOM   1029 N  N   . GLY A 1 128 ? 10.375 20.953  18.490  1.00 9.49   ? 128 GLY A N   1 
ATOM   1030 C  CA  . GLY A 1 128 ? 10.331 21.682  17.223  1.00 9.41   ? 128 GLY A CA  1 
ATOM   1031 C  C   . GLY A 1 128 ? 10.750 20.905  15.985  1.00 9.38   ? 128 GLY A C   1 
ATOM   1032 O  O   . GLY A 1 128 ? 10.104 21.051  14.957  1.00 11.59  ? 128 GLY A O   1 
ATOM   1033 N  N   . ASP A 1 129 ? 11.861 20.149  16.087  1.00 10.31  ? 129 ASP A N   1 
ATOM   1034 C  CA  . ASP A 1 129 ? 12.255 19.300  14.972  1.00 10.41  ? 129 ASP A CA  1 
ATOM   1035 C  C   . ASP A 1 129 ? 12.886 18.071  15.589  1.00 9.81   ? 129 ASP A C   1 
ATOM   1036 O  O   . ASP A 1 129 ? 13.332 18.060  16.747  1.00 10.30  ? 129 ASP A O   1 
ATOM   1037 C  CB  . ASP A 1 129 ? 13.146 20.093  13.983  1.00 10.28  ? 129 ASP A CB  1 
ATOM   1038 C  CG  . ASP A 1 129 ? 14.534 20.494  14.473  1.00 10.54  ? 129 ASP A CG  1 
ATOM   1039 O  OD1 . ASP A 1 129 ? 15.432 19.600  14.646  1.00 13.02  ? 129 ASP A OD1 1 
ATOM   1040 O  OD2 . ASP A 1 129 ? 14.757 21.684  14.745  1.00 12.81  ? 129 ASP A OD2 1 
ATOM   1041 N  N   . TYR A 1 130 ? 12.966 17.024  14.802  1.00 9.27   ? 130 TYR A N   1 
ATOM   1042 C  CA  . TYR A 1 130 ? 13.420 15.744  15.325  1.00 9.51   ? 130 TYR A CA  1 
ATOM   1043 C  C   . TYR A 1 130 ? 14.901 15.809  15.676  1.00 9.14   ? 130 TYR A C   1 
ATOM   1044 O  O   . TYR A 1 130 ? 15.318 15.154  16.606  1.00 11.10  ? 130 TYR A O   1 
ATOM   1045 C  CB  . TYR A 1 130 ? 13.110 14.574  14.395  1.00 11.54  ? 130 TYR A CB  1 
ATOM   1046 C  CG  . TYR A 1 130 ? 13.842 14.617  13.075  1.00 12.51  ? 130 TYR A CG  1 
ATOM   1047 C  CD1 . TYR A 1 130 ? 15.149 14.106  12.978  1.00 14.29  ? 130 TYR A CD1 1 
ATOM   1048 C  CD2 . TYR A 1 130 ? 13.246 15.141  11.909  1.00 13.17  ? 130 TYR A CD2 1 
ATOM   1049 C  CE1 . TYR A 1 130 ? 15.822 14.124  11.761  1.00 17.08  ? 130 TYR A CE1 1 
ATOM   1050 C  CE2 . TYR A 1 130 ? 13.939 15.190  10.715  1.00 14.74  ? 130 TYR A CE2 1 
ATOM   1051 C  CZ  . TYR A 1 130 ? 15.213 14.677  10.640  1.00 14.38  ? 130 TYR A CZ  1 
ATOM   1052 O  OH  . TYR A 1 130 ? 15.828 14.686  9.397   1.00 19.22  ? 130 TYR A OH  1 
ATOM   1053 N  N   . GLY A 1 131 ? 15.653 16.608  14.907  1.00 10.68  ? 131 GLY A N   1 
ATOM   1054 C  CA  . GLY A 1 131 ? 17.064 16.700  15.224  1.00 12.72  ? 131 GLY A CA  1 
ATOM   1055 C  C   . GLY A 1 131 ? 17.349 17.328  16.591  1.00 13.09  ? 131 GLY A C   1 
ATOM   1056 O  O   . GLY A 1 131 ? 18.339 16.983  17.260  1.00 16.16  ? 131 GLY A O   1 
ATOM   1057 N  N   A LYS A 1 132 ? 16.504 18.276  17.009  0.50 11.73  ? 132 LYS A N   1 
ATOM   1058 N  N   B LYS A 1 132 ? 16.513 18.292  17.011  0.50 11.72  ? 132 LYS A N   1 
ATOM   1059 C  CA  A LYS A 1 132 ? 16.635 18.817  18.354  0.50 11.53  ? 132 LYS A CA  1 
ATOM   1060 C  CA  B LYS A 1 132 ? 16.581 18.868  18.353  0.50 11.85  ? 132 LYS A CA  1 
ATOM   1061 C  C   A LYS A 1 132 ? 16.142 17.813  19.396  0.50 10.94  ? 132 LYS A C   1 
ATOM   1062 C  C   B LYS A 1 132 ? 16.126 17.839  19.396  0.50 10.22  ? 132 LYS A C   1 
ATOM   1063 O  O   A LYS A 1 132 ? 16.702 17.709  20.480  0.50 13.58  ? 132 LYS A O   1 
ATOM   1064 O  O   B LYS A 1 132 ? 16.716 17.703  20.460  0.50 11.70  ? 132 LYS A O   1 
ATOM   1065 C  CB  A LYS A 1 132 ? 15.837 20.110  18.485  0.50 12.07  ? 132 LYS A CB  1 
ATOM   1066 C  CB  B LYS A 1 132 ? 15.731 20.147  18.380  0.50 14.22  ? 132 LYS A CB  1 
ATOM   1067 C  CG  A LYS A 1 132 ? 16.060 20.739  19.846  0.50 10.94  ? 132 LYS A CG  1 
ATOM   1068 C  CG  B LYS A 1 132 ? 16.453 21.429  17.967  0.50 15.33  ? 132 LYS A CG  1 
ATOM   1069 C  CD  A LYS A 1 132 ? 17.466 21.246  20.130  0.50 14.89  ? 132 LYS A CD  1 
ATOM   1070 C  CD  B LYS A 1 132 ? 17.418 21.850  19.067  0.50 25.29  ? 132 LYS A CD  1 
ATOM   1071 C  CE  A LYS A 1 132 ? 18.149 21.960  18.978  0.50 18.87  ? 132 LYS A CE  1 
ATOM   1072 C  CE  B LYS A 1 132 ? 17.935 23.240  18.798  0.50 24.14  ? 132 LYS A CE  1 
ATOM   1073 N  NZ  A LYS A 1 132 ? 17.798 23.394  18.831  0.50 22.10  ? 132 LYS A NZ  1 
ATOM   1074 N  NZ  B LYS A 1 132 ? 16.783 24.018  18.286  0.50 17.86  ? 132 LYS A NZ  1 
ATOM   1075 N  N   . ALA A 1 133 ? 15.065 17.086  19.063  1.00 9.19   ? 133 ALA A N   1 
ATOM   1076 C  CA  . ALA A 1 133 ? 14.490 16.139  20.017  1.00 9.28   ? 133 ALA A CA  1 
ATOM   1077 C  C   . ALA A 1 133 ? 15.507 15.054  20.359  1.00 9.76   ? 133 ALA A C   1 
ATOM   1078 O  O   . ALA A 1 133 ? 15.517 14.600  21.488  1.00 10.34  ? 133 ALA A O   1 
ATOM   1079 C  CB  . ALA A 1 133 ? 13.227 15.527  19.420  1.00 9.40   ? 133 ALA A CB  1 
ATOM   1080 N  N   . VAL A 1 134 ? 16.317 14.589  19.413  1.00 10.13  ? 134 VAL A N   1 
ATOM   1081 C  CA  . VAL A 1 134 ? 17.315 13.565  19.746  1.00 12.17  ? 134 VAL A CA  1 
ATOM   1082 C  C   . VAL A 1 134 ? 18.351 14.025  20.753  1.00 12.80  ? 134 VAL A C   1 
ATOM   1083 O  O   . VAL A 1 134 ? 18.998 13.164  21.354  1.00 18.24  ? 134 VAL A O   1 
ATOM   1084 C  CB  . VAL A 1 134 ? 17.980 13.003  18.492  1.00 14.90  ? 134 VAL A CB  1 
ATOM   1085 C  CG1 . VAL A 1 134 ? 16.898 12.421  17.680  1.00 14.10  ? 134 VAL A CG1 1 
ATOM   1086 C  CG2 . VAL A 1 134 ? 18.732 13.982  17.662  1.00 21.54  ? 134 VAL A CG2 1 
ATOM   1087 N  N   . GLN A 1 135 ? 18.504 15.327  20.946  1.00 13.39  ? 135 GLN A N   1 
ATOM   1088 C  CA  . GLN A 1 135 ? 19.457 15.828  21.910  1.00 17.10  ? 135 GLN A CA  1 
ATOM   1089 C  C   . GLN A 1 135 ? 18.854 15.859  23.308  1.00 15.17  ? 135 GLN A C   1 
ATOM   1090 O  O   . GLN A 1 135 ? 19.466 16.380  24.250  1.00 20.42  ? 135 GLN A O   1 
ATOM   1091 C  CB  . GLN A 1 135 ? 19.957 17.197  21.423  1.00 19.66  ? 135 GLN A CB  1 
ATOM   1092 C  CG  . GLN A 1 135 ? 20.580 17.162  20.030  1.00 26.30  ? 135 GLN A CG  1 
ATOM   1093 C  CD  . GLN A 1 135 ? 20.929 18.564  19.546  1.00 39.17  ? 135 GLN A CD  1 
ATOM   1094 O  OE1 . GLN A 1 135 ? 20.558 18.960  18.430  1.00 34.41  ? 135 GLN A OE1 1 
ATOM   1095 N  NE2 . GLN A 1 135 ? 21.565 19.334  20.416  1.00 42.43  ? 135 GLN A NE2 1 
ATOM   1096 N  N   . GLN A 1 136 ? 17.640 15.304  23.480  1.00 11.96  ? 136 GLN A N   1 
ATOM   1097 C  CA  . GLN A 1 136 ? 16.960 15.457  24.757  1.00 11.75  ? 136 GLN A CA  1 
ATOM   1098 C  C   . GLN A 1 136 ? 16.646 14.100  25.359  1.00 11.16  ? 136 GLN A C   1 
ATOM   1099 O  O   . GLN A 1 136 ? 16.345 13.154  24.616  1.00 10.15  ? 136 GLN A O   1 
ATOM   1100 C  CB  . GLN A 1 136 ? 15.675 16.236  24.578  1.00 13.21  ? 136 GLN A CB  1 
ATOM   1101 C  CG  . GLN A 1 136 ? 15.751 17.448  23.638  1.00 15.33  ? 136 GLN A CG  1 
ATOM   1102 C  CD  . GLN A 1 136 ? 16.802 18.447  24.023  1.00 14.69  ? 136 GLN A CD  1 
ATOM   1103 O  OE1 . GLN A 1 136 ? 16.979 18.722  25.214  1.00 16.24  ? 136 GLN A OE1 1 
ATOM   1104 N  NE2 . GLN A 1 136 ? 17.343 19.131  23.005  1.00 20.42  ? 136 GLN A NE2 1 
ATOM   1105 N  N   A PRO A 1 137 ? 16.600 13.981  26.698  0.50 10.66  ? 137 PRO A N   1 
ATOM   1106 N  N   B PRO A 1 137 ? 16.726 13.973  26.696  0.50 11.09  ? 137 PRO A N   1 
ATOM   1107 C  CA  A PRO A 1 137 ? 16.413 12.671  27.308  0.50 10.99  ? 137 PRO A CA  1 
ATOM   1108 C  CA  B PRO A 1 137 ? 16.426 12.703  27.346  0.50 11.63  ? 137 PRO A CA  1 
ATOM   1109 C  C   A PRO A 1 137 ? 15.004 12.159  27.062  0.50 10.96  ? 137 PRO A C   1 
ATOM   1110 C  C   B PRO A 1 137 ? 15.025 12.177  27.067  0.50 10.99  ? 137 PRO A C   1 
ATOM   1111 O  O   A PRO A 1 137 ? 14.768 10.962  27.123  0.50 13.72  ? 137 PRO A O   1 
ATOM   1112 O  O   B PRO A 1 137 ? 14.820 10.974  27.117  0.50 13.83  ? 137 PRO A O   1 
ATOM   1113 C  CB  A PRO A 1 137 ? 16.621 12.916  28.799  0.50 13.63  ? 137 PRO A CB  1 
ATOM   1114 C  CB  B PRO A 1 137 ? 16.589 12.990  28.838  0.50 15.39  ? 137 PRO A CB  1 
ATOM   1115 C  CG  A PRO A 1 137 ? 16.307 14.391  28.965  0.50 13.10  ? 137 PRO A CG  1 
ATOM   1116 C  CG  B PRO A 1 137 ? 17.532 14.176  28.889  0.50 16.97  ? 137 PRO A CG  1 
ATOM   1117 C  CD  A PRO A 1 137 ? 16.760 15.066  27.680  0.50 14.81  ? 137 PRO A CD  1 
ATOM   1118 C  CD  B PRO A 1 137 ? 17.273 14.978  27.625  0.50 13.44  ? 137 PRO A CD  1 
ATOM   1119 N  N   . ASP A 1 138 ? 14.089 13.065  26.717  1.00 10.87  ? 138 ASP A N   1 
ATOM   1120 C  CA  . ASP A 1 138 ? 12.685 12.695  26.490  1.00 11.54  ? 138 ASP A CA  1 
ATOM   1121 C  C   . ASP A 1 138 ? 12.298 13.114  25.066  1.00 9.39   ? 138 ASP A C   1 
ATOM   1122 O  O   . ASP A 1 138 ? 11.188 13.550  24.813  1.00 11.13  ? 138 ASP A O   1 
ATOM   1123 C  CB  . ASP A 1 138 ? 11.753 13.344  27.529  1.00 13.83  ? 138 ASP A CB  1 
ATOM   1124 C  CG  . ASP A 1 138 ? 11.752 14.831  27.490  1.00 14.70  ? 138 ASP A CG  1 
ATOM   1125 O  OD1 . ASP A 1 138 ? 12.706 15.410  26.929  1.00 12.75  ? 138 ASP A OD1 1 
ATOM   1126 O  OD2 . ASP A 1 138 ? 10.876 15.436  28.159  1.00 16.06  ? 138 ASP A OD2 1 
ATOM   1127 N  N   . GLY A 1 139 ? 13.248 13.008  24.131  1.00 7.69   ? 139 GLY A N   1 
ATOM   1128 C  CA  . GLY A 1 139 ? 12.974 13.529  22.805  1.00 7.92   ? 139 GLY A CA  1 
ATOM   1129 C  C   . GLY A 1 139 ? 12.148 12.618  21.910  1.00 7.60   ? 139 GLY A C   1 
ATOM   1130 O  O   . GLY A 1 139 ? 11.429 13.125  21.037  1.00 8.69   ? 139 GLY A O   1 
ATOM   1131 N  N   . LEU A 1 140 ? 12.333 11.288  22.066  1.00 6.49   ? 140 LEU A N   1 
ATOM   1132 C  CA  . LEU A 1 140 ? 11.637 10.352  21.185  1.00 6.17   ? 140 LEU A CA  1 
ATOM   1133 C  C   . LEU A 1 140 ? 10.779 9.416   22.017  1.00 5.98   ? 140 LEU A C   1 
ATOM   1134 O  O   . LEU A 1 140 ? 11.099 9.113   23.153  1.00 6.92   ? 140 LEU A O   1 
ATOM   1135 C  CB  . LEU A 1 140 ? 12.645 9.508   20.381  1.00 7.16   ? 140 LEU A CB  1 
ATOM   1136 C  CG  . LEU A 1 140 ? 13.562 10.228  19.409  1.00 8.79   ? 140 LEU A CG  1 
ATOM   1137 C  CD1 . LEU A 1 140 ? 14.322 9.203   18.588  1.00 10.43  ? 140 LEU A CD1 1 
ATOM   1138 C  CD2 . LEU A 1 140 ? 12.948 11.252  18.540  1.00 11.33  ? 140 LEU A CD2 1 
ATOM   1139 N  N   . ALA A 1 141 ? 9.720  8.899   21.342  1.00 6.52   ? 141 ALA A N   1 
ATOM   1140 C  CA  . ALA A 1 141 ? 8.981  7.778   21.900  1.00 6.86   ? 141 ALA A CA  1 
ATOM   1141 C  C   . ALA A 1 141 ? 8.881  6.762   20.757  1.00 6.02   ? 141 ALA A C   1 
ATOM   1142 O  O   . ALA A 1 141 ? 8.455  7.129   19.670  1.00 6.33   ? 141 ALA A O   1 
ATOM   1143 C  CB  . ALA A 1 141 ? 7.590  8.224   22.346  1.00 7.50   ? 141 ALA A CB  1 
ATOM   1144 N  N   . VAL A 1 142 ? 9.376  5.549   21.052  1.00 6.07   ? 142 VAL A N   1 
ATOM   1145 C  CA  . VAL A 1 142 ? 9.317  4.509   20.038  1.00 6.18   ? 142 VAL A CA  1 
ATOM   1146 C  C   . VAL A 1 142 ? 8.326  3.463   20.541  1.00 5.49   ? 142 VAL A C   1 
ATOM   1147 O  O   . VAL A 1 142 ? 8.461  2.927   21.646  1.00 6.17   ? 142 VAL A O   1 
ATOM   1148 C  CB  . VAL A 1 142 ? 10.686 3.926   19.658  1.00 6.10   ? 142 VAL A CB  1 
ATOM   1149 C  CG1 . VAL A 1 142 ? 10.525 2.891   18.517  1.00 7.27   ? 142 VAL A CG1 1 
ATOM   1150 C  CG2 . VAL A 1 142 ? 11.657 5.041   19.239  1.00 7.75   ? 142 VAL A CG2 1 
ATOM   1151 N  N   . LEU A 1 143 ? 7.326  3.191   19.685  1.00 5.90   ? 143 LEU A N   1 
ATOM   1152 C  CA  . LEU A 1 143 ? 6.343  2.158   19.969  1.00 6.26   ? 143 LEU A CA  1 
ATOM   1153 C  C   . LEU A 1 143 ? 6.822  0.905   19.259  1.00 6.24   ? 143 LEU A C   1 
ATOM   1154 O  O   . LEU A 1 143 ? 6.953  0.876   18.047  1.00 6.93   ? 143 LEU A O   1 
ATOM   1155 C  CB  . LEU A 1 143 ? 4.982  2.651   19.461  1.00 7.39   ? 143 LEU A CB  1 
ATOM   1156 C  CG  . LEU A 1 143 ? 3.809  1.684   19.612  1.00 7.98   ? 143 LEU A CG  1 
ATOM   1157 C  CD1 . LEU A 1 143 ? 3.558  1.376   21.054  1.00 10.22  ? 143 LEU A CD1 1 
ATOM   1158 C  CD2 . LEU A 1 143 ? 2.567  2.285   18.985  1.00 10.23  ? 143 LEU A CD2 1 
ATOM   1159 N  N   . GLY A 1 144 ? 7.086  -0.155  20.042  1.00 5.77   ? 144 GLY A N   1 
ATOM   1160 C  CA  . GLY A 1 144 ? 7.593  -1.412  19.513  1.00 5.86   ? 144 GLY A CA  1 
ATOM   1161 C  C   . GLY A 1 144 ? 6.530  -2.501  19.553  1.00 5.50   ? 144 GLY A C   1 
ATOM   1162 O  O   . GLY A 1 144 ? 5.808  -2.625  20.527  1.00 7.30   ? 144 GLY A O   1 
ATOM   1163 N  N   . ILE A 1 145 ? 6.488  -3.258  18.458  1.00 5.68   ? 145 ILE A N   1 
ATOM   1164 C  CA  . ILE A 1 145 ? 5.489  -4.316  18.304  1.00 6.03   ? 145 ILE A CA  1 
ATOM   1165 C  C   . ILE A 1 145 ? 6.239  -5.523  17.776  1.00 5.21   ? 145 ILE A C   1 
ATOM   1166 O  O   . ILE A 1 145 ? 6.919  -5.466  16.760  1.00 6.64   ? 145 ILE A O   1 
ATOM   1167 C  CB  . ILE A 1 145 ? 4.379  -3.837  17.322  1.00 6.43   ? 145 ILE A CB  1 
ATOM   1168 C  CG1 . ILE A 1 145 ? 3.735  -2.554  17.841  1.00 9.63   ? 145 ILE A CG1 1 
ATOM   1169 C  CG2 . ILE A 1 145 ? 3.375  -4.945  17.060  1.00 8.99   ? 145 ILE A CG2 1 
ATOM   1170 C  CD1 . ILE A 1 145 ? 2.681  -1.930  16.907  1.00 9.28   ? 145 ILE A CD1 1 
ATOM   1171 N  N   . PHE A 1 146 ? 6.053  -6.633  18.479  1.00 5.48   ? 146 PHE A N   1 
ATOM   1172 C  CA  . PHE A 1 146 ? 6.668  -7.880  18.028  1.00 5.73   ? 146 PHE A CA  1 
ATOM   1173 C  C   . PHE A 1 146 ? 5.917  -8.525  16.862  1.00 6.43   ? 146 PHE A C   1 
ATOM   1174 O  O   . PHE A 1 146 ? 4.710  -8.407  16.809  1.00 7.82   ? 146 PHE A O   1 
ATOM   1175 C  CB  . PHE A 1 146 ? 6.667  -8.869  19.197  1.00 6.66   ? 146 PHE A CB  1 
ATOM   1176 C  CG  . PHE A 1 146 ? 7.500  -8.362  20.347  1.00 5.90   ? 146 PHE A CG  1 
ATOM   1177 C  CD1 . PHE A 1 146 ? 8.868  -8.227  20.191  1.00 6.70   ? 146 PHE A CD1 1 
ATOM   1178 C  CD2 . PHE A 1 146 ? 6.943  -8.153  21.603  1.00 6.87   ? 146 PHE A CD2 1 
ATOM   1179 C  CE1 . PHE A 1 146 ? 9.685  -7.821  21.259  1.00 7.04   ? 146 PHE A CE1 1 
ATOM   1180 C  CE2 . PHE A 1 146 ? 7.764  -7.745  22.673  1.00 7.30   ? 146 PHE A CE2 1 
ATOM   1181 C  CZ  . PHE A 1 146 ? 9.130  -7.570  22.506  1.00 7.41   ? 146 PHE A CZ  1 
ATOM   1182 N  N   . LEU A 1 147 ? 6.679  -9.177  15.993  1.00 6.93   ? 147 LEU A N   1 
ATOM   1183 C  CA  . LEU A 1 147 ? 6.099  -9.970  14.915  1.00 7.20   ? 147 LEU A CA  1 
ATOM   1184 C  C   . LEU A 1 147 ? 6.430  -11.439 15.166  1.00 6.77   ? 147 LEU A C   1 
ATOM   1185 O  O   . LEU A 1 147 ? 7.584  -11.842 15.269  1.00 8.01   ? 147 LEU A O   1 
ATOM   1186 C  CB  . LEU A 1 147 ? 6.667  -9.552  13.547  1.00 7.27   ? 147 LEU A CB  1 
ATOM   1187 C  CG  . LEU A 1 147 ? 6.079  -8.318  12.882  1.00 7.18   ? 147 LEU A CG  1 
ATOM   1188 C  CD1 . LEU A 1 147 ? 6.275  -7.079  13.738  1.00 8.82   ? 147 LEU A CD1 1 
ATOM   1189 C  CD2 . LEU A 1 147 ? 6.679  -8.104  11.508  1.00 9.39   ? 147 LEU A CD2 1 
ATOM   1190 N  N   . LYS A 1 148 ? 5.364  -12.269 15.223  1.00 8.48   ? 148 LYS A N   1 
ATOM   1191 C  CA  . LYS A 1 148 ? 5.564  -13.716 15.259  1.00 8.65   ? 148 LYS A CA  1 
ATOM   1192 C  C   . LYS A 1 148 ? 5.040  -14.265 13.947  1.00 9.54   ? 148 LYS A C   1 
ATOM   1193 O  O   . LYS A 1 148 ? 4.194  -13.697 13.272  1.00 12.39  ? 148 LYS A O   1 
ATOM   1194 C  CB  . LYS A 1 148 ? 4.814  -14.346 16.432  1.00 12.98  ? 148 LYS A CB  1 
ATOM   1195 C  CG  . LYS A 1 148 ? 3.320  -14.287 16.357  1.00 13.17  ? 148 LYS A CG  1 
ATOM   1196 C  CD  . LYS A 1 148 ? 2.695  -15.030 17.565  1.00 18.92  ? 148 LYS A CD  1 
ATOM   1197 C  CE  . LYS A 1 148 ? 1.191  -15.165 17.487  1.00 28.09  ? 148 LYS A CE  1 
ATOM   1198 N  NZ  . LYS A 1 148 ? 0.681  -15.868 18.687  1.00 30.79  ? 148 LYS A NZ  1 
ATOM   1199 N  N   . VAL A 1 149 ? 5.593  -15.397 13.520  1.00 9.87   ? 149 VAL A N   1 
ATOM   1200 C  CA  . VAL A 1 149 ? 5.185  -16.055 12.279  1.00 9.87   ? 149 VAL A CA  1 
ATOM   1201 C  C   . VAL A 1 149 ? 3.973  -16.945 12.519  1.00 10.21  ? 149 VAL A C   1 
ATOM   1202 O  O   . VAL A 1 149 ? 3.991  -17.844 13.342  1.00 12.69  ? 149 VAL A O   1 
ATOM   1203 C  CB  . VAL A 1 149 ? 6.393  -16.799 11.710  1.00 9.69   ? 149 VAL A CB  1 
ATOM   1204 C  CG1 . VAL A 1 149 ? 6.011  -17.582 10.456  1.00 12.66  ? 149 VAL A CG1 1 
ATOM   1205 C  CG2 . VAL A 1 149 ? 7.495  -15.813 11.394  1.00 11.13  ? 149 VAL A CG2 1 
ATOM   1206 N  N   . GLY A 1 150 ? 2.936  -16.718 11.734  1.00 10.37  ? 150 GLY A N   1 
ATOM   1207 C  CA  . GLY A 1 150 ? 1.734  -17.526 11.802  1.00 11.73  ? 150 GLY A CA  1 
ATOM   1208 C  C   . GLY A 1 150 ? 0.871  -17.170 10.608  1.00 10.61  ? 150 GLY A C   1 
ATOM   1209 O  O   . GLY A 1 150 ? 1.315  -17.319 9.472   1.00 11.12  ? 150 GLY A O   1 
ATOM   1210 N  N   A SER A 1 151 ? -0.342 -16.645 10.866  0.50 11.49  ? 151 SER A N   1 
ATOM   1211 N  N   B SER A 1 151 ? -0.316 -16.607 10.902  0.50 12.03  ? 151 SER A N   1 
ATOM   1212 C  CA  A SER A 1 151 ? -1.179 -16.177 9.765   0.50 10.51  ? 151 SER A CA  1 
ATOM   1213 C  CA  B SER A 1 151 ? -1.179 -16.081 9.853   0.50 11.83  ? 151 SER A CA  1 
ATOM   1214 C  C   A SER A 1 151 ? -0.681 -14.828 9.263   0.50 9.03   ? 151 SER A C   1 
ATOM   1215 C  C   B SER A 1 151 ? -0.572 -14.825 9.236   0.50 9.23   ? 151 SER A C   1 
ATOM   1216 O  O   A SER A 1 151 ? -0.140 -14.042 10.038  0.50 10.12  ? 151 SER A O   1 
ATOM   1217 O  O   B SER A 1 151 ? 0.202  -14.122 9.880   0.50 10.21  ? 151 SER A O   1 
ATOM   1218 C  CB  A SER A 1 151 ? -2.584 -16.017 10.214  0.50 13.24  ? 151 SER A CB  1 
ATOM   1219 C  CB  B SER A 1 151 ? -2.548 -15.806 10.392  0.50 15.94  ? 151 SER A CB  1 
ATOM   1220 O  OG  A SER A 1 151 ? -2.647 -14.938 11.135  0.50 13.99  ? 151 SER A OG  1 
ATOM   1221 O  OG  B SER A 1 151 ? -3.190 -17.030 10.713  0.50 19.63  ? 151 SER A OG  1 
ATOM   1222 N  N   . ALA A 1 152 ? -0.921 -14.543 7.983   1.00 10.34  ? 152 ALA A N   1 
ATOM   1223 C  CA  . ALA A 1 152 ? -0.564 -13.252 7.361   1.00 9.32   ? 152 ALA A CA  1 
ATOM   1224 C  C   . ALA A 1 152 ? -1.174 -12.064 8.120   1.00 11.41  ? 152 ALA A C   1 
ATOM   1225 O  O   . ALA A 1 152 ? -2.300 -12.120 8.644   1.00 12.65  ? 152 ALA A O   1 
ATOM   1226 C  CB  . ALA A 1 152 ? -1.083 -13.221 5.930   1.00 12.08  ? 152 ALA A CB  1 
ATOM   1227 N  N   . LYS A 1 153 ? -0.478 -10.946 8.048   1.00 11.20  ? 153 LYS A N   1 
ATOM   1228 C  CA  . LYS A 1 153 ? -1.028 -9.671  8.481   1.00 11.09  ? 153 LYS A CA  1 
ATOM   1229 C  C   . LYS A 1 153 ? -1.469 -8.903  7.251   1.00 10.53  ? 153 LYS A C   1 
ATOM   1230 O  O   . LYS A 1 153 ? -0.632 -8.401  6.489   1.00 11.03  ? 153 LYS A O   1 
ATOM   1231 C  CB  . LYS A 1 153 ? 0.040  -8.890  9.236   1.00 10.93  ? 153 LYS A CB  1 
ATOM   1232 C  CG  . LYS A 1 153 ? -0.474 -7.657  9.977   1.00 12.72  ? 153 LYS A CG  1 
ATOM   1233 C  CD  . LYS A 1 153 ? -1.387 -7.994  11.209  1.00 14.88  ? 153 LYS A CD  1 
ATOM   1234 C  CE  . LYS A 1 153 ? -1.663 -6.828  12.128  1.00 16.41  ? 153 LYS A CE  1 
ATOM   1235 N  NZ  . LYS A 1 153 ? -2.737 -7.204  13.081  1.00 23.52  ? 153 LYS A NZ  1 
ATOM   1236 N  N   . PRO A 1 154 ? -2.789 -8.771  6.992   1.00 12.61  ? 154 PRO A N   1 
ATOM   1237 C  CA  . PRO A 1 154 ? -3.240 -8.135  5.750   1.00 13.98  ? 154 PRO A CA  1 
ATOM   1238 C  C   . PRO A 1 154 ? -2.705 -6.696  5.637   1.00 12.17  ? 154 PRO A C   1 
ATOM   1239 O  O   . PRO A 1 154 ? -2.363 -6.276  4.549   1.00 15.08  ? 154 PRO A O   1 
ATOM   1240 C  CB  . PRO A 1 154 ? -4.763 -8.170  5.928   1.00 16.70  ? 154 PRO A CB  1 
ATOM   1241 C  CG  . PRO A 1 154 ? -4.984 -9.361  6.798   1.00 21.27  ? 154 PRO A CG  1 
ATOM   1242 C  CD  . PRO A 1 154 ? -3.860 -9.339  7.815   1.00 13.48  ? 154 PRO A CD  1 
ATOM   1243 N  N   . GLY A 1 155 ? -2.631 -5.984  6.766   1.00 12.27  ? 155 GLY A N   1 
ATOM   1244 C  CA  . GLY A 1 155 ? -2.242 -4.593  6.757   1.00 13.09  ? 155 GLY A CA  1 
ATOM   1245 C  C   . GLY A 1 155 ? -0.770 -4.387  6.458   1.00 11.42  ? 155 GLY A C   1 
ATOM   1246 O  O   . GLY A 1 155 ? -0.346 -3.279  6.266   1.00 14.36  ? 155 GLY A O   1 
ATOM   1247 N  N   . LEU A 1 156 ? 0.008  -5.471  6.447   1.00 10.58  ? 156 LEU A N   1 
ATOM   1248 C  CA  . LEU A 1 156 ? 1.434  -5.441  6.129   1.00 10.04  ? 156 LEU A CA  1 
ATOM   1249 C  C   . LEU A 1 156 ? 1.673  -5.710  4.642   1.00 9.42   ? 156 LEU A C   1 
ATOM   1250 O  O   . LEU A 1 156 ? 2.763  -5.441  4.124   1.00 9.86   ? 156 LEU A O   1 
ATOM   1251 C  CB  . LEU A 1 156 ? 2.196  -6.468  6.971   1.00 10.87  ? 156 LEU A CB  1 
ATOM   1252 C  CG  . LEU A 1 156 ? 3.732  -6.588  6.817   1.00 9.45   ? 156 LEU A CG  1 
ATOM   1253 C  CD1 . LEU A 1 156 ? 4.506  -5.319  7.192   1.00 11.02  ? 156 LEU A CD1 1 
ATOM   1254 C  CD2 . LEU A 1 156 ? 4.277  -7.761  7.586   1.00 9.79   ? 156 LEU A CD2 1 
ATOM   1255 N  N   . GLN A 1 157 ? 0.672  -6.260  3.932   1.00 10.75  ? 157 GLN A N   1 
ATOM   1256 C  CA  . GLN A 1 157 ? 1.005  -6.759  2.607   1.00 12.09  ? 157 GLN A CA  1 
ATOM   1257 C  C   . GLN A 1 157 ? 1.365  -5.625  1.647   1.00 11.45  ? 157 GLN A C   1 
ATOM   1258 O  O   . GLN A 1 157 ? 2.239  -5.818  0.809   1.00 10.62  ? 157 GLN A O   1 
ATOM   1259 C  CB  . GLN A 1 157 ? -0.127 -7.651  2.076   1.00 14.43  ? 157 GLN A CB  1 
ATOM   1260 C  CG  . GLN A 1 157 ? 0.282  -8.397  0.778   1.00 15.26  ? 157 GLN A CG  1 
ATOM   1261 C  CD  . GLN A 1 157 ? 1.462  -9.328  0.975   1.00 13.14  ? 157 GLN A CD  1 
ATOM   1262 O  OE1 . GLN A 1 157 ? 1.625  -9.940  2.037   1.00 14.18  ? 157 GLN A OE1 1 
ATOM   1263 N  NE2 . GLN A 1 157 ? 2.254  -9.562  -0.070  1.00 14.74  ? 157 GLN A NE2 1 
ATOM   1264 N  N   . LYS A 1 158 ? 0.793  -4.416  1.782   1.00 12.40  ? 158 LYS A N   1 
ATOM   1265 C  CA  . LYS A 1 158 ? 1.217  -3.333  0.886   1.00 12.00  ? 158 LYS A CA  1 
ATOM   1266 C  C   . LYS A 1 158 ? 2.717  -3.009  1.033   1.00 10.44  ? 158 LYS A C   1 
ATOM   1267 O  O   . LYS A 1 158 ? 3.387  -2.636  0.068   1.00 11.61  ? 158 LYS A O   1 
ATOM   1268 C  CB  . LYS A 1 158 ? 0.319  -2.108  1.109   1.00 15.48  ? 158 LYS A CB  1 
ATOM   1269 C  CG  . LYS A 1 158 ? -0.920 -2.192  0.219   1.00 20.59  ? 158 LYS A CG  1 
ATOM   1270 N  N   . VAL A 1 159 ? 3.219  -3.162  2.256   1.00 9.44   ? 159 VAL A N   1 
ATOM   1271 C  CA  . VAL A 1 159 ? 4.618  -2.924  2.512   1.00 9.76   ? 159 VAL A CA  1 
ATOM   1272 C  C   . VAL A 1 159 ? 5.447  -4.036  1.838   1.00 10.29  ? 159 VAL A C   1 
ATOM   1273 O  O   . VAL A 1 159 ? 6.411  -3.795  1.121   1.00 10.76  ? 159 VAL A O   1 
ATOM   1274 C  CB  . VAL A 1 159 ? 4.902  -2.931  4.015   1.00 9.45   ? 159 VAL A CB  1 
ATOM   1275 C  CG1 . VAL A 1 159 ? 6.418  -2.880  4.254   1.00 11.11  ? 159 VAL A CG1 1 
ATOM   1276 C  CG2 . VAL A 1 159 ? 4.191  -1.793  4.719   1.00 12.04  ? 159 VAL A CG2 1 
ATOM   1277 N  N   . VAL A 1 160 ? 5.075  -5.306  2.087   1.00 9.26   ? 160 VAL A N   1 
ATOM   1278 C  CA  . VAL A 1 160 ? 5.834  -6.431  1.532   1.00 11.88  ? 160 VAL A CA  1 
ATOM   1279 C  C   . VAL A 1 160 ? 5.884  -6.313  0.001   1.00 11.01  ? 160 VAL A C   1 
ATOM   1280 O  O   . VAL A 1 160 ? 6.925  -6.592  -0.600  1.00 11.71  ? 160 VAL A O   1 
ATOM   1281 C  CB  . VAL A 1 160 ? 5.142  -7.774  1.943   1.00 13.87  ? 160 VAL A CB  1 
ATOM   1282 C  CG1 . VAL A 1 160 ? 5.587  -8.966  1.097   1.00 14.79  ? 160 VAL A CG1 1 
ATOM   1283 C  CG2 . VAL A 1 160 ? 5.335  -7.956  3.440   1.00 13.99  ? 160 VAL A CG2 1 
ATOM   1284 N  N   . ASP A 1 161 ? 4.756  -5.895  -0.634  1.00 12.09  ? 161 ASP A N   1 
ATOM   1285 C  CA  . ASP A 1 161 ? 4.697  -5.962  -2.079  1.00 14.90  ? 161 ASP A CA  1 
ATOM   1286 C  C   . ASP A 1 161 ? 5.570  -4.925  -2.761  1.00 14.19  ? 161 ASP A C   1 
ATOM   1287 O  O   . ASP A 1 161 ? 5.913  -5.153  -3.929  1.00 18.83  ? 161 ASP A O   1 
ATOM   1288 C  CB  . ASP A 1 161 ? 3.254  -5.905  -2.488  1.00 17.62  ? 161 ASP A CB  1 
ATOM   1289 C  CG  . ASP A 1 161 ? 2.655  -7.322  -2.482  1.00 20.35  ? 161 ASP A CG  1 
ATOM   1290 O  OD1 . ASP A 1 161 ? 3.420  -8.345  -2.556  1.00 27.54  ? 161 ASP A OD1 1 
ATOM   1291 O  OD2 . ASP A 1 161 ? 1.496  -7.379  -2.287  1.00 25.52  ? 161 ASP A OD2 1 
ATOM   1292 N  N   . VAL A 1 162 ? 5.958  -3.841  -2.048  1.00 11.44  ? 162 VAL A N   1 
ATOM   1293 C  CA  . VAL A 1 162 ? 6.765  -2.804  -2.681  1.00 13.01  ? 162 VAL A CA  1 
ATOM   1294 C  C   . VAL A 1 162 ? 8.254  -3.098  -2.484  1.00 11.18  ? 162 VAL A C   1 
ATOM   1295 O  O   . VAL A 1 162 ? 9.080  -2.414  -3.057  1.00 12.08  ? 162 VAL A O   1 
ATOM   1296 C  CB  . VAL A 1 162 ? 6.355  -1.417  -2.105  1.00 14.60  ? 162 VAL A CB  1 
ATOM   1297 C  CG1 . VAL A 1 162 ? 6.942  -1.189  -0.718  1.00 16.18  ? 162 VAL A CG1 1 
ATOM   1298 C  CG2 . VAL A 1 162 ? 6.769  -0.233  -2.974  1.00 17.89  ? 162 VAL A CG2 1 
ATOM   1299 N  N   . LEU A 1 163 ? 8.638  -4.082  -1.647  1.00 11.47  ? 163 LEU A N   1 
ATOM   1300 C  CA  . LEU A 1 163 ? 10.049 -4.237  -1.271  1.00 10.03  ? 163 LEU A CA  1 
ATOM   1301 C  C   . LEU A 1 163 ? 10.944 -4.561  -2.483  1.00 10.86  ? 163 LEU A C   1 
ATOM   1302 O  O   . LEU A 1 163 ? 12.114 -4.172  -2.507  1.00 11.96  ? 163 LEU A O   1 
ATOM   1303 C  CB  . LEU A 1 163 ? 10.233 -5.317  -0.191  1.00 10.60  ? 163 LEU A CB  1 
ATOM   1304 C  CG  . LEU A 1 163 ? 9.570  -4.943  1.131   1.00 10.74  ? 163 LEU A CG  1 
ATOM   1305 C  CD1 . LEU A 1 163 ? 9.864  -6.016  2.163   1.00 11.94  ? 163 LEU A CD1 1 
ATOM   1306 C  CD2 . LEU A 1 163 ? 10.105 -3.655  1.675   1.00 11.69  ? 163 LEU A CD2 1 
ATOM   1307 N  N   . ASP A 1 164 ? 10.424 -5.280  -3.484  1.00 14.33  ? 164 ASP A N   1 
ATOM   1308 C  CA  . ASP A 1 164 ? 11.263 -5.554  -4.658  1.00 15.99  ? 164 ASP A CA  1 
ATOM   1309 C  C   . ASP A 1 164 ? 11.645 -4.267  -5.398  1.00 16.24  ? 164 ASP A C   1 
ATOM   1310 O  O   . ASP A 1 164 ? 12.631 -4.286  -6.127  1.00 22.14  ? 164 ASP A O   1 
ATOM   1311 C  CB  . ASP A 1 164 ? 10.583 -6.540  -5.616  1.00 22.79  ? 164 ASP A CB  1 
ATOM   1312 C  CG  . ASP A 1 164 ? 9.577  -5.813  -6.475  1.00 32.74  ? 164 ASP A CG  1 
ATOM   1313 O  OD1 . ASP A 1 164 ? 8.640  -5.252  -5.889  1.00 31.24  ? 164 ASP A OD1 1 
ATOM   1314 O  OD2 . ASP A 1 164 ? 9.762  -5.781  -7.740  1.00 54.22  ? 164 ASP A OD2 1 
ATOM   1315 N  N   . SER A 1 165 ? 10.931 -3.144  -5.192  1.00 14.51  ? 165 SER A N   1 
ATOM   1316 C  CA  . SER A 1 165 ? 11.272 -1.879  -5.832  1.00 14.49  ? 165 SER A CA  1 
ATOM   1317 C  C   . SER A 1 165 ? 12.331 -1.100  -5.039  1.00 11.68  ? 165 SER A C   1 
ATOM   1318 O  O   . SER A 1 165 ? 12.866 -0.112  -5.550  1.00 14.21  ? 165 SER A O   1 
ATOM   1319 C  CB  . SER A 1 165 ? 10.025 -1.082  -6.066  1.00 18.88  ? 165 SER A CB  1 
ATOM   1320 O  OG  . SER A 1 165 ? 9.582  -0.473  -4.864  1.00 17.77  ? 165 SER A OG  1 
ATOM   1321 N  N   . ILE A 1 166 ? 12.664 -1.577  -3.823  1.00 10.74  ? 166 ILE A N   1 
ATOM   1322 C  CA  . ILE A 1 166 ? 13.674 -0.911  -3.009  1.00 10.15  ? 166 ILE A CA  1 
ATOM   1323 C  C   . ILE A 1 166 ? 14.704 -1.951  -2.514  1.00 10.12  ? 166 ILE A C   1 
ATOM   1324 O  O   . ILE A 1 166 ? 15.150 -1.940  -1.388  1.00 9.98   ? 166 ILE A O   1 
ATOM   1325 C  CB  . ILE A 1 166 ? 13.066 -0.091  -1.850  1.00 9.17   ? 166 ILE A CB  1 
ATOM   1326 C  CG1 . ILE A 1 166 ? 12.257 -0.947  -0.891  1.00 9.67   ? 166 ILE A CG1 1 
ATOM   1327 C  CG2 . ILE A 1 166 ? 12.257 1.084   -2.365  1.00 11.85  ? 166 ILE A CG2 1 
ATOM   1328 C  CD1 . ILE A 1 166 ? 12.298 -0.382  0.511   1.00 12.35  ? 166 ILE A CD1 1 
ATOM   1329 N  N   . LYS A 1 167 ? 15.101 -2.838  -3.440  1.00 10.25  ? 167 LYS A N   1 
ATOM   1330 C  CA  . LYS A 1 167 ? 15.929 -3.976  -3.048  1.00 9.56   ? 167 LYS A CA  1 
ATOM   1331 C  C   . LYS A 1 167 ? 17.245 -3.548  -2.403  1.00 8.86   ? 167 LYS A C   1 
ATOM   1332 O  O   . LYS A 1 167 ? 17.691 -4.185  -1.439  1.00 9.72   ? 167 LYS A O   1 
ATOM   1333 C  CB  . LYS A 1 167 ? 16.230 -4.882  -4.254  1.00 11.68  ? 167 LYS A CB  1 
ATOM   1334 C  CG  . LYS A 1 167 ? 16.982 -6.158  -3.857  1.00 13.82  ? 167 LYS A CG  1 
ATOM   1335 C  CD  . LYS A 1 167 ? 17.265 -7.082  -5.092  1.00 18.04  ? 167 LYS A CD  1 
ATOM   1336 C  CE  . LYS A 1 167 ? 18.146 -8.280  -4.828  1.00 27.40  ? 167 LYS A CE  1 
ATOM   1337 N  N   . THR A 1 168 ? 17.859 -2.489  -2.914  1.00 8.72   ? 168 THR A N   1 
ATOM   1338 C  CA  . THR A 1 168 ? 19.248 -2.158  -2.569  1.00 9.48   ? 168 THR A CA  1 
ATOM   1339 C  C   . THR A 1 168 ? 19.326 -0.799  -1.847  1.00 8.64   ? 168 THR A C   1 
ATOM   1340 O  O   . THR A 1 168 ? 18.413 0.056   -1.918  1.00 9.84   ? 168 THR A O   1 
ATOM   1341 C  CB  . THR A 1 168 ? 20.177 -2.174  -3.806  1.00 10.54  ? 168 THR A CB  1 
ATOM   1342 O  OG1 . THR A 1 168 ? 19.539 -1.372  -4.804  1.00 12.04  ? 168 THR A OG1 1 
ATOM   1343 C  CG2 . THR A 1 168 ? 20.312 -3.591  -4.301  1.00 11.82  ? 168 THR A CG2 1 
ATOM   1344 N  N   . LYS A 1 169 ? 20.405 -0.648  -1.093  1.00 9.76   ? 169 LYS A N   1 
ATOM   1345 C  CA  . LYS A 1 169 ? 20.717 0.540   -0.316  1.00 9.36   ? 169 LYS A CA  1 
ATOM   1346 C  C   . LYS A 1 169 ? 20.546 1.808   -1.120  1.00 9.93   ? 169 LYS A C   1 
ATOM   1347 O  O   . LYS A 1 169 ? 21.099 1.937   -2.206  1.00 12.61  ? 169 LYS A O   1 
ATOM   1348 C  CB  . LYS A 1 169 ? 22.160 0.450   0.208   1.00 10.96  ? 169 LYS A CB  1 
ATOM   1349 C  CG  . LYS A 1 169 ? 22.616 1.686   1.047   1.00 11.85  ? 169 LYS A CG  1 
ATOM   1350 C  CD  . LYS A 1 169 ? 24.001 1.533   1.599   1.00 15.01  ? 169 LYS A CD  1 
ATOM   1351 C  CE  . LYS A 1 169 ? 25.004 1.179   0.511   1.00 24.24  ? 169 LYS A CE  1 
ATOM   1352 N  N   . GLY A 1 170 ? 19.738 2.727   -0.575  1.00 9.93   ? 170 GLY A N   1 
ATOM   1353 C  CA  . GLY A 1 170 ? 19.561 4.028   -1.205  1.00 11.97  ? 170 GLY A CA  1 
ATOM   1354 C  C   . GLY A 1 170 ? 18.365 4.112   -2.161  1.00 11.56  ? 170 GLY A C   1 
ATOM   1355 O  O   . GLY A 1 170 ? 18.014 5.215   -2.643  1.00 14.34  ? 170 GLY A O   1 
ATOM   1356 N  N   A LYS A 1 171 ? 17.735 2.977   -2.465  0.50 11.16  ? 171 LYS A N   1 
ATOM   1357 N  N   B LYS A 1 171 ? 17.725 2.976   -2.451  0.50 11.35  ? 171 LYS A N   1 
ATOM   1358 C  CA  A LYS A 1 171 ? 16.506 3.025   -3.253  0.50 12.80  ? 171 LYS A CA  1 
ATOM   1359 C  CA  B LYS A 1 171 ? 16.488 3.002   -3.225  0.50 12.13  ? 171 LYS A CA  1 
ATOM   1360 C  C   A LYS A 1 171 ? 15.353 3.509   -2.378  0.50 9.50   ? 171 LYS A C   1 
ATOM   1361 C  C   B LYS A 1 171 ? 15.319 3.479   -2.365  0.50 10.01  ? 171 LYS A C   1 
ATOM   1362 O  O   A LYS A 1 171 ? 15.216 3.041   -1.249  0.50 10.05  ? 171 LYS A O   1 
ATOM   1363 O  O   B LYS A 1 171 ? 15.102 2.949   -1.274  0.50 10.14  ? 171 LYS A O   1 
ATOM   1364 C  CB  A LYS A 1 171 ? 16.228 1.687   -3.939  0.50 12.24  ? 171 LYS A CB  1 
ATOM   1365 C  CB  B LYS A 1 171 ? 16.269 1.666   -3.932  0.50 12.11  ? 171 LYS A CB  1 
ATOM   1366 C  CG  A LYS A 1 171 ? 17.277 1.274   -4.973  0.50 15.39  ? 171 LYS A CG  1 
ATOM   1367 C  CG  B LYS A 1 171 ? 17.379 1.323   -4.932  0.50 14.84  ? 171 LYS A CG  1 
ATOM   1368 C  CD  A LYS A 1 171 ? 16.798 0.176   -5.884  0.50 20.61  ? 171 LYS A CD  1 
ATOM   1369 C  CD  B LYS A 1 171 ? 17.455 2.298   -6.093  0.50 16.74  ? 171 LYS A CD  1 
ATOM   1370 N  N   . SER A 1 172 ? 14.455 4.291   -2.982  1.00 12.52  ? 172 SER A N   1 
ATOM   1371 C  CA  . SER A 1 172 ? 13.201 4.695   -2.391  1.00 13.19  ? 172 SER A CA  1 
ATOM   1372 C  C   . SER A 1 172 ? 12.066 4.526   -3.398  1.00 10.74  ? 172 SER A C   1 
ATOM   1373 O  O   . SER A 1 172 ? 12.264 4.477   -4.631  1.00 13.24  ? 172 SER A O   1 
ATOM   1374 C  CB  . SER A 1 172 ? 13.300 6.091   -1.807  1.00 12.57  ? 172 SER A CB  1 
ATOM   1375 O  OG  . SER A 1 172 ? 13.473 7.029   -2.824  1.00 16.10  ? 172 SER A OG  1 
ATOM   1376 N  N   . ALA A 1 173 ? 10.835 4.581   -2.892  1.00 12.13  ? 173 ALA A N   1 
ATOM   1377 C  CA  . ALA A 1 173 ? 9.653  4.513   -3.717  1.00 12.80  ? 173 ALA A CA  1 
ATOM   1378 C  C   . ALA A 1 173 ? 8.542  5.282   -3.034  1.00 13.58  ? 173 ALA A C   1 
ATOM   1379 O  O   . ALA A 1 173 ? 8.504  5.416   -1.791  1.00 9.91   ? 173 ALA A O   1 
ATOM   1380 C  CB  . ALA A 1 173 ? 9.250  3.069   -3.924  1.00 14.16  ? 173 ALA A CB  1 
ATOM   1381 N  N   . ASP A 1 174 ? 7.695  5.877   -3.870  1.00 14.05  ? 174 ASP A N   1 
ATOM   1382 C  CA  . ASP A 1 174 ? 6.518  6.507   -3.310  1.00 14.11  ? 174 ASP A CA  1 
ATOM   1383 C  C   . ASP A 1 174 ? 5.778  5.466   -2.477  1.00 12.88  ? 174 ASP A C   1 
ATOM   1384 O  O   . ASP A 1 174 ? 5.609  4.289   -2.820  1.00 15.43  ? 174 ASP A O   1 
ATOM   1385 C  CB  . ASP A 1 174 ? 5.695  7.190   -4.411  1.00 19.56  ? 174 ASP A CB  1 
ATOM   1386 C  CG  . ASP A 1 174 ? 6.343  8.407   -5.138  1.00 30.28  ? 174 ASP A CG  1 
ATOM   1387 O  OD1 . ASP A 1 174 ? 6.978  9.323   -4.467  1.00 36.47  ? 174 ASP A OD1 1 
ATOM   1388 O  OD2 . ASP A 1 174 ? 6.248  8.461   -6.412  1.00 39.00  ? 174 ASP A OD2 1 
ATOM   1389 N  N   . PHE A 1 175 ? 5.204  5.946   -1.372  1.00 11.18  ? 175 PHE A N   1 
ATOM   1390 C  CA  . PHE A 1 175 ? 4.464  5.072   -0.510  1.00 11.34  ? 175 PHE A CA  1 
ATOM   1391 C  C   . PHE A 1 175 ? 3.380  5.874   0.193   1.00 11.45  ? 175 PHE A C   1 
ATOM   1392 O  O   . PHE A 1 175 ? 3.330  5.938   1.413   1.00 15.52  ? 175 PHE A O   1 
ATOM   1393 C  CB  . PHE A 1 175 ? 5.391  4.288   0.432   1.00 11.56  ? 175 PHE A CB  1 
ATOM   1394 C  CG  . PHE A 1 175 ? 4.770  3.009   0.950   1.00 10.96  ? 175 PHE A CG  1 
ATOM   1395 C  CD1 . PHE A 1 175 ? 4.588  1.933   0.084   1.00 11.11  ? 175 PHE A CD1 1 
ATOM   1396 C  CD2 . PHE A 1 175 ? 4.330  2.870   2.259   1.00 10.83  ? 175 PHE A CD2 1 
ATOM   1397 C  CE1 . PHE A 1 175 ? 4.059  0.751   0.554   1.00 12.89  ? 175 PHE A CE1 1 
ATOM   1398 C  CE2 . PHE A 1 175 ? 3.776  1.671   2.738   1.00 11.62  ? 175 PHE A CE2 1 
ATOM   1399 C  CZ  . PHE A 1 175 ? 3.641  0.616   1.855   1.00 12.29  ? 175 PHE A CZ  1 
ATOM   1400 N  N   . THR A 1 176 ? 2.488  6.432   -0.595  1.00 11.63  ? 176 THR A N   1 
ATOM   1401 C  CA  . THR A 1 176 ? 1.407  7.267   -0.096  1.00 11.38  ? 176 THR A CA  1 
ATOM   1402 C  C   . THR A 1 176 ? 0.221  6.404   0.299   1.00 8.96   ? 176 THR A C   1 
ATOM   1403 O  O   . THR A 1 176 ? 0.048  5.286   -0.182  1.00 10.83  ? 176 THR A O   1 
ATOM   1404 C  CB  . THR A 1 176 ? 1.015  8.341   -1.118  1.00 11.90  ? 176 THR A CB  1 
ATOM   1405 O  OG1 . THR A 1 176 ? 0.711  7.717   -2.363  1.00 16.99  ? 176 THR A OG1 1 
ATOM   1406 C  CG2 . THR A 1 176 ? 2.107  9.374   -1.231  1.00 20.49  ? 176 THR A CG2 1 
ATOM   1407 N  N   . ASN A 1 177 ? -0.641 6.996   1.122   1.00 9.83   ? 177 ASN A N   1 
ATOM   1408 C  CA  . ASN A 1 177 ? -1.916 6.410   1.475   1.00 10.75  ? 177 ASN A CA  1 
ATOM   1409 C  C   . ASN A 1 177 ? -1.826 5.059   2.175   1.00 11.04  ? 177 ASN A C   1 
ATOM   1410 O  O   . ASN A 1 177 ? -2.756 4.252   2.056   1.00 14.87  ? 177 ASN A O   1 
ATOM   1411 C  CB  . ASN A 1 177 ? -2.860 6.347   0.277   1.00 11.68  ? 177 ASN A CB  1 
ATOM   1412 C  CG  . ASN A 1 177 ? -3.009 7.716   -0.338  1.00 12.24  ? 177 ASN A CG  1 
ATOM   1413 O  OD1 . ASN A 1 177 ? -3.664 8.588   0.217   1.00 15.84  ? 177 ASN A OD1 1 
ATOM   1414 N  ND2 . ASN A 1 177 ? -2.395 7.871   -1.500  1.00 12.20  ? 177 ASN A ND2 1 
ATOM   1415 N  N   . PHE A 1 178 ? -0.795 4.886   2.968   1.00 10.20  ? 178 PHE A N   1 
ATOM   1416 C  CA  . PHE A 1 178 ? -0.668 3.686   3.790   1.00 9.26   ? 178 PHE A CA  1 
ATOM   1417 C  C   . PHE A 1 178 ? -1.138 4.009   5.205   1.00 9.61   ? 178 PHE A C   1 
ATOM   1418 O  O   . PHE A 1 178 ? -0.693 4.994   5.794   1.00 11.25  ? 178 PHE A O   1 
ATOM   1419 C  CB  . PHE A 1 178 ? 0.797  3.259   3.853   1.00 10.43  ? 178 PHE A CB  1 
ATOM   1420 C  CG  . PHE A 1 178 ? 0.929  2.013   4.709   1.00 9.67   ? 178 PHE A CG  1 
ATOM   1421 C  CD1 . PHE A 1 178 ? 0.600  0.765   4.176   1.00 11.21  ? 178 PHE A CD1 1 
ATOM   1422 C  CD2 . PHE A 1 178 ? 1.365  2.071   6.021   1.00 9.58   ? 178 PHE A CD2 1 
ATOM   1423 C  CE1 . PHE A 1 178 ? 0.575  -0.397  4.950   1.00 11.98  ? 178 PHE A CE1 1 
ATOM   1424 C  CE2 . PHE A 1 178 ? 1.444  0.904   6.797   1.00 9.98   ? 178 PHE A CE2 1 
ATOM   1425 C  CZ  . PHE A 1 178 ? 1.050  -0.322  6.264   1.00 10.55  ? 178 PHE A CZ  1 
ATOM   1426 N  N   . ASP A 1 179 ? -1.949 3.135   5.789   1.00 10.43  ? 179 ASP A N   1 
ATOM   1427 C  CA  . ASP A 1 179 ? -2.568 3.388   7.064   1.00 10.89  ? 179 ASP A CA  1 
ATOM   1428 C  C   . ASP A 1 179 ? -1.845 2.521   8.082   1.00 10.09  ? 179 ASP A C   1 
ATOM   1429 O  O   . ASP A 1 179 ? -2.046 1.292   8.146   1.00 10.29  ? 179 ASP A O   1 
ATOM   1430 C  CB  . ASP A 1 179 ? -4.034 3.000   7.040   1.00 13.74  ? 179 ASP A CB  1 
ATOM   1431 C  CG  . ASP A 1 179 ? -4.795 3.377   8.291   1.00 15.13  ? 179 ASP A CG  1 
ATOM   1432 O  OD1 . ASP A 1 179 ? -4.134 3.642   9.335   1.00 12.86  ? 179 ASP A OD1 1 
ATOM   1433 O  OD2 . ASP A 1 179 ? -6.033 3.462   8.174   1.00 22.59  ? 179 ASP A OD2 1 
ATOM   1434 N  N   . PRO A 1 180 ? -1.044 3.098   9.004   1.00 8.81   ? 180 PRO A N   1 
ATOM   1435 C  CA  . PRO A 1 180 ? -0.274 2.271   9.950   1.00 8.22   ? 180 PRO A CA  1 
ATOM   1436 C  C   . PRO A 1 180 ? -1.141 1.597   10.982  1.00 8.87   ? 180 PRO A C   1 
ATOM   1437 O  O   . PRO A 1 180 ? -0.644 0.755   11.712  1.00 9.44   ? 180 PRO A O   1 
ATOM   1438 C  CB  . PRO A 1 180 ? 0.716  3.252   10.549  1.00 9.94   ? 180 PRO A CB  1 
ATOM   1439 C  CG  . PRO A 1 180 ? 0.009  4.608   10.423  1.00 9.74   ? 180 PRO A CG  1 
ATOM   1440 C  CD  . PRO A 1 180 ? -0.731 4.532   9.109   1.00 10.17  ? 180 PRO A CD  1 
ATOM   1441 N  N   . ARG A 1 181 ? -2.397 2.031   11.087  1.00 8.91   ? 181 ARG A N   1 
ATOM   1442 C  CA  . ARG A 1 181 ? -3.288 1.363   12.053  1.00 9.02   ? 181 ARG A CA  1 
ATOM   1443 C  C   . ARG A 1 181 ? -3.433 -0.120  11.709  1.00 9.96   ? 181 ARG A C   1 
ATOM   1444 O  O   . ARG A 1 181 ? -3.732 -0.920  12.607  1.00 11.49  ? 181 ARG A O   1 
ATOM   1445 C  CB  . ARG A 1 181 ? -4.666 2.002   12.086  1.00 10.02  ? 181 ARG A CB  1 
ATOM   1446 C  CG  . ARG A 1 181 ? -4.553 3.420   12.622  1.00 12.21  ? 181 ARG A CG  1 
ATOM   1447 C  CD  . ARG A 1 181 ? -5.876 4.134   12.634  1.00 14.18  ? 181 ARG A CD  1 
ATOM   1448 N  NE  . ARG A 1 181 ? -6.255 4.396   11.264  1.00 15.10  ? 181 ARG A NE  1 
ATOM   1449 C  CZ  . ARG A 1 181 ? -7.326 5.118   10.943  1.00 17.57  ? 181 ARG A CZ  1 
ATOM   1450 N  NH1 . ARG A 1 181 ? -8.116 5.595   11.908  1.00 18.68  ? 181 ARG A NH1 1 
ATOM   1451 N  NH2 . ARG A 1 181 ? -7.603 5.284   9.660   1.00 19.29  ? 181 ARG A NH2 1 
ATOM   1452 N  N   . GLY A 1 182 ? -3.264 -0.507  10.432  1.00 10.17  ? 182 GLY A N   1 
ATOM   1453 C  CA  . GLY A 1 182 ? -3.307 -1.913  10.059  1.00 10.73  ? 182 GLY A CA  1 
ATOM   1454 C  C   . GLY A 1 182 ? -2.201 -2.798  10.615  1.00 9.82   ? 182 GLY A C   1 
ATOM   1455 O  O   . GLY A 1 182 ? -2.198 -3.997  10.367  1.00 12.20  ? 182 GLY A O   1 
ATOM   1456 N  N   . LEU A 1 183 ? -1.192 -2.182  11.280  1.00 9.22   ? 183 LEU A N   1 
ATOM   1457 C  CA  . LEU A 1 183 ? -0.045 -2.915  11.820  1.00 9.61   ? 183 LEU A CA  1 
ATOM   1458 C  C   . LEU A 1 183 ? -0.179 -3.134  13.324  1.00 8.85   ? 183 LEU A C   1 
ATOM   1459 O  O   . LEU A 1 183 ? 0.702  -3.733  13.937  1.00 11.23  ? 183 LEU A O   1 
ATOM   1460 C  CB  . LEU A 1 183 ? 1.256  -2.169  11.501  1.00 9.71   ? 183 LEU A CB  1 
ATOM   1461 C  CG  . LEU A 1 183 ? 1.555  -2.071  10.010  1.00 11.41  ? 183 LEU A CG  1 
ATOM   1462 C  CD1 . LEU A 1 183 ? 2.781  -1.234  9.871   1.00 13.34  ? 183 LEU A CD1 1 
ATOM   1463 C  CD2 . LEU A 1 183 ? 1.678  -3.445  9.376   1.00 15.33  ? 183 LEU A CD2 1 
ATOM   1464 N  N   . LEU A 1 184 ? -1.258 -2.638  13.948  1.00 9.03   ? 184 LEU A N   1 
ATOM   1465 C  CA  . LEU A 1 184 ? -1.404 -2.680  15.412  1.00 9.94   ? 184 LEU A CA  1 
ATOM   1466 C  C   . LEU A 1 184 ? -2.141 -3.945  15.846  1.00 11.46  ? 184 LEU A C   1 
ATOM   1467 O  O   . LEU A 1 184 ? -3.057 -4.413  15.183  1.00 19.12  ? 184 LEU A O   1 
ATOM   1468 C  CB  . LEU A 1 184 ? -2.189 -1.450  15.932  1.00 10.74  ? 184 LEU A CB  1 
ATOM   1469 C  CG  . LEU A 1 184 ? -1.583 -0.105  15.535  1.00 10.12  ? 184 LEU A CG  1 
ATOM   1470 C  CD1 . LEU A 1 184 ? -2.472 1.015   15.999  1.00 12.04  ? 184 LEU A CD1 1 
ATOM   1471 C  CD2 . LEU A 1 184 ? -0.150 0.040   15.998  1.00 14.89  ? 184 LEU A CD2 1 
ATOM   1472 N  N   . PRO A 1 185 ? -1.747 -4.558  16.972  1.00 9.72   ? 185 PRO A N   1 
ATOM   1473 C  CA  . PRO A 1 185 ? -2.521 -5.666  17.512  1.00 9.91   ? 185 PRO A CA  1 
ATOM   1474 C  C   . PRO A 1 185 ? -3.784 -5.134  18.188  1.00 9.97   ? 185 PRO A C   1 
ATOM   1475 O  O   . PRO A 1 185 ? -4.027 -3.928  18.273  1.00 11.82  ? 185 PRO A O   1 
ATOM   1476 C  CB  . PRO A 1 185 ? -1.583 -6.230  18.567  1.00 10.06  ? 185 PRO A CB  1 
ATOM   1477 C  CG  . PRO A 1 185 ? -0.787 -5.000  19.041  1.00 8.74   ? 185 PRO A CG  1 
ATOM   1478 C  CD  . PRO A 1 185 ? -0.629 -4.112  17.807  1.00 8.66   ? 185 PRO A CD  1 
ATOM   1479 N  N   A GLU A 1 186 ? -4.642 -6.018  18.713  0.50 11.14  ? 186 GLU A N   1 
ATOM   1480 N  N   B GLU A 1 186 ? -4.590 -6.076  18.660  0.50 11.18  ? 186 GLU A N   1 
ATOM   1481 C  CA  A GLU A 1 186 ? -5.901 -5.587  19.322  0.50 10.94  ? 186 GLU A CA  1 
ATOM   1482 C  CA  B GLU A 1 186 ? -5.863 -5.731  19.259  0.50 10.34  ? 186 GLU A CA  1 
ATOM   1483 C  C   A GLU A 1 186 ? -5.644 -4.835  20.622  0.50 10.52  ? 186 GLU A C   1 
ATOM   1484 C  C   B GLU A 1 186 ? -5.631 -4.912  20.528  0.50 10.12  ? 186 GLU A C   1 
ATOM   1485 O  O   A GLU A 1 186 ? -6.303 -3.834  20.932  0.50 11.36  ? 186 GLU A O   1 
ATOM   1486 O  O   B GLU A 1 186 ? -6.235 -3.844  20.638  0.50 12.46  ? 186 GLU A O   1 
ATOM   1487 C  CB  A GLU A 1 186 ? -6.727 -6.796  19.763  0.50 12.76  ? 186 GLU A CB  1 
ATOM   1488 C  CB  B GLU A 1 186 ? -6.693 -7.001  19.430  0.50 11.50  ? 186 GLU A CB  1 
ATOM   1489 C  CG  A GLU A 1 186 ? -7.487 -7.441  18.646  0.50 16.92  ? 186 GLU A CG  1 
ATOM   1490 C  CG  B GLU A 1 186 ? -7.840 -6.848  20.395  0.50 14.28  ? 186 GLU A CG  1 
ATOM   1491 C  CD  A GLU A 1 186 ? -8.147 -8.752  19.071  0.50 20.11  ? 186 GLU A CD  1 
ATOM   1492 C  CD  B GLU A 1 186 ? -8.565 -8.154  20.662  0.50 15.03  ? 186 GLU A CD  1 
ATOM   1493 O  OE1 A GLU A 1 186 ? -8.599 -9.503  18.171  0.50 24.32  ? 186 GLU A OE1 1 
ATOM   1494 O  OE1 B GLU A 1 186 ? -8.429 -9.092  19.834  0.50 18.10  ? 186 GLU A OE1 1 
ATOM   1495 O  OE2 A GLU A 1 186 ? -8.200 -9.022  20.310  0.50 21.37  ? 186 GLU A OE2 1 
ATOM   1496 O  OE2 B GLU A 1 186 ? -9.295 -8.211  21.661  0.50 17.78  ? 186 GLU A OE2 1 
ATOM   1497 N  N   . SER A 1 187 ? -4.749 -5.382  21.438  1.00 10.06  ? 187 SER A N   1 
ATOM   1498 C  CA  . SER A 1 187 ? -4.540 -4.744  22.725  1.00 11.22  ? 187 SER A CA  1 
ATOM   1499 C  C   . SER A 1 187 ? -3.424 -3.721  22.653  1.00 10.40  ? 187 SER A C   1 
ATOM   1500 O  O   . SER A 1 187 ? -2.385 -3.970  22.033  1.00 11.85  ? 187 SER A O   1 
ATOM   1501 C  CB  . SER A 1 187 ? -4.153 -5.818  23.744  1.00 11.41  ? 187 SER A CB  1 
ATOM   1502 O  OG  . SER A 1 187 ? -3.929 -5.228  25.033  1.00 12.52  ? 187 SER A OG  1 
ATOM   1503 N  N   . LEU A 1 188 ? -3.582 -2.652  23.441  1.00 9.81   ? 188 LEU A N   1 
ATOM   1504 C  CA  . LEU A 1 188 ? -2.522 -1.661  23.647  1.00 11.08  ? 188 LEU A CA  1 
ATOM   1505 C  C   . LEU A 1 188 ? -1.866 -1.793  25.009  1.00 10.62  ? 188 LEU A C   1 
ATOM   1506 O  O   . LEU A 1 188 ? -1.237 -0.860  25.468  1.00 11.86  ? 188 LEU A O   1 
ATOM   1507 C  CB  . LEU A 1 188 ? -3.060 -0.244  23.440  1.00 11.94  ? 188 LEU A CB  1 
ATOM   1508 C  CG  . LEU A 1 188 ? -3.484 0.125   22.015  1.00 14.43  ? 188 LEU A CG  1 
ATOM   1509 C  CD1 . LEU A 1 188 ? -4.078 1.532   21.918  1.00 16.35  ? 188 LEU A CD1 1 
ATOM   1510 C  CD2 . LEU A 1 188 ? -2.364 -0.097  21.007  1.00 16.31  ? 188 LEU A CD2 1 
ATOM   1511 N  N   . ASP A 1 189 ? -2.001 -2.942  25.685  1.00 10.82  ? 189 ASP A N   1 
ATOM   1512 C  CA  . ASP A 1 189 ? -1.238 -3.206  26.900  1.00 10.23  ? 189 ASP A CA  1 
ATOM   1513 C  C   . ASP A 1 189 ? 0.269  -3.138  26.587  1.00 8.47   ? 189 ASP A C   1 
ATOM   1514 O  O   . ASP A 1 189 ? 0.684  -3.630  25.526  1.00 9.17   ? 189 ASP A O   1 
ATOM   1515 C  CB  . ASP A 1 189 ? -1.578 -4.562  27.509  1.00 12.80  ? 189 ASP A CB  1 
ATOM   1516 C  CG  . ASP A 1 189 ? -2.960 -4.703  28.094  1.00 16.78  ? 189 ASP A CG  1 
ATOM   1517 O  OD1 . ASP A 1 189 ? -3.601 -3.686  28.281  1.00 20.33  ? 189 ASP A OD1 1 
ATOM   1518 O  OD2 . ASP A 1 189 ? -3.329 -5.860  28.408  1.00 22.04  ? 189 ASP A OD2 1 
ATOM   1519 N  N   . TYR A 1 190 ? 1.052  -2.519  27.469  1.00 8.59   ? 190 TYR A N   1 
ATOM   1520 C  CA  . TYR A 1 190 ? 2.436  -2.255  27.123  1.00 7.33   ? 190 TYR A CA  1 
ATOM   1521 C  C   . TYR A 1 190 ? 3.338  -2.352  28.354  1.00 7.38   ? 190 TYR A C   1 
ATOM   1522 O  O   . TYR A 1 190 ? 2.894  -2.229  29.522  1.00 8.94   ? 190 TYR A O   1 
ATOM   1523 C  CB  . TYR A 1 190 ? 2.559  -0.890  26.439  1.00 8.02   ? 190 TYR A CB  1 
ATOM   1524 C  CG  . TYR A 1 190 ? 2.213  0.281   27.311  1.00 7.50   ? 190 TYR A CG  1 
ATOM   1525 C  CD1 . TYR A 1 190 ? 3.135  0.867   28.177  1.00 9.55   ? 190 TYR A CD1 1 
ATOM   1526 C  CD2 . TYR A 1 190 ? 0.909  0.773   27.303  1.00 9.44   ? 190 TYR A CD2 1 
ATOM   1527 C  CE1 . TYR A 1 190 ? 2.778  1.924   29.008  1.00 9.07   ? 190 TYR A CE1 1 
ATOM   1528 C  CE2 . TYR A 1 190 ? 0.543  1.846   28.116  1.00 9.00   ? 190 TYR A CE2 1 
ATOM   1529 C  CZ  . TYR A 1 190 ? 1.486  2.446   28.941  1.00 9.23   ? 190 TYR A CZ  1 
ATOM   1530 O  OH  . TYR A 1 190 ? 1.128  3.471   29.762  1.00 11.15  ? 190 TYR A OH  1 
ATOM   1531 N  N   . TRP A 1 191 ? 4.649  -2.470  28.039  1.00 7.05   ? 191 TRP A N   1 
ATOM   1532 C  CA  . TRP A 1 191 ? 5.704  -2.189  29.013  1.00 7.56   ? 191 TRP A CA  1 
ATOM   1533 C  C   . TRP A 1 191 ? 6.405  -0.912  28.568  1.00 7.14   ? 191 TRP A C   1 
ATOM   1534 O  O   . TRP A 1 191 ? 6.436  -0.587  27.378  1.00 8.69   ? 191 TRP A O   1 
ATOM   1535 C  CB  . TRP A 1 191 ? 6.726  -3.334  28.965  1.00 8.42   ? 191 TRP A CB  1 
ATOM   1536 C  CG  . TRP A 1 191 ? 6.187  -4.659  29.385  1.00 8.15   ? 191 TRP A CG  1 
ATOM   1537 C  CD1 . TRP A 1 191 ? 6.014  -5.088  30.671  1.00 9.01   ? 191 TRP A CD1 1 
ATOM   1538 C  CD2 . TRP A 1 191 ? 5.898  -5.802  28.524  1.00 8.18   ? 191 TRP A CD2 1 
ATOM   1539 N  NE1 . TRP A 1 191 ? 5.566  -6.391  30.667  1.00 10.32  ? 191 TRP A NE1 1 
ATOM   1540 C  CE2 . TRP A 1 191 ? 5.544  -6.861  29.382  1.00 8.44   ? 191 TRP A CE2 1 
ATOM   1541 C  CE3 . TRP A 1 191 ? 5.993  -6.006  27.132  1.00 9.66   ? 191 TRP A CE3 1 
ATOM   1542 C  CZ2 . TRP A 1 191 ? 5.219  -8.105  28.863  1.00 10.06  ? 191 TRP A CZ2 1 
ATOM   1543 C  CZ3 . TRP A 1 191 ? 5.723  -7.260  26.630  1.00 9.99   ? 191 TRP A CZ3 1 
ATOM   1544 C  CH2 . TRP A 1 191 ? 5.330  -8.274  27.508  1.00 11.28  ? 191 TRP A CH2 1 
ATOM   1545 N  N   . THR A 1 192 ? 6.988  -0.195  29.542  1.00 7.44   ? 192 THR A N   1 
ATOM   1546 C  CA  . THR A 1 192 ? 7.728  1.007   29.180  1.00 7.36   ? 192 THR A CA  1 
ATOM   1547 C  C   . THR A 1 192 ? 8.965  1.140   30.051  1.00 7.61   ? 192 THR A C   1 
ATOM   1548 O  O   . THR A 1 192 ? 8.969  0.735   31.239  1.00 8.37   ? 192 THR A O   1 
ATOM   1549 C  CB  . THR A 1 192 ? 6.790  2.214   29.297  1.00 7.14   ? 192 THR A CB  1 
ATOM   1550 O  OG1 . THR A 1 192 ? 7.501  3.377   28.851  1.00 7.90   ? 192 THR A OG1 1 
ATOM   1551 C  CG2 . THR A 1 192 ? 6.216  2.461   30.690  1.00 9.15   ? 192 THR A CG2 1 
ATOM   1552 N  N   . TYR A 1 193 ? 10.015 1.751   29.465  1.00 6.60   ? 193 TYR A N   1 
ATOM   1553 C  CA  . TYR A 1 193 ? 11.251 2.021   30.207  1.00 6.77   ? 193 TYR A CA  1 
ATOM   1554 C  C   . TYR A 1 193 ? 12.033 3.049   29.441  1.00 6.54   ? 193 TYR A C   1 
ATOM   1555 O  O   . TYR A 1 193 ? 11.795 3.255   28.249  1.00 7.20   ? 193 TYR A O   1 
ATOM   1556 C  CB  . TYR A 1 193 ? 12.089 0.734   30.388  1.00 8.37   ? 193 TYR A CB  1 
ATOM   1557 C  CG  . TYR A 1 193 ? 12.750 0.244   29.132  1.00 5.98   ? 193 TYR A CG  1 
ATOM   1558 C  CD1 . TYR A 1 193 ? 12.033 -0.467  28.155  1.00 6.25   ? 193 TYR A CD1 1 
ATOM   1559 C  CD2 . TYR A 1 193 ? 14.072 0.589   28.900  1.00 7.13   ? 193 TYR A CD2 1 
ATOM   1560 C  CE1 . TYR A 1 193 ? 12.640 -0.832  26.966  1.00 6.95   ? 193 TYR A CE1 1 
ATOM   1561 C  CE2 . TYR A 1 193 ? 14.716 0.270   27.718  1.00 6.96   ? 193 TYR A CE2 1 
ATOM   1562 C  CZ  . TYR A 1 193 ? 13.971 -0.401  26.739  1.00 5.86   ? 193 TYR A CZ  1 
ATOM   1563 O  OH  . TYR A 1 193 ? 14.632 -0.730  25.569  1.00 6.39   ? 193 TYR A OH  1 
ATOM   1564 N  N   . PRO A 1 194 ? 12.943 3.769   30.122  1.00 7.42   ? 194 PRO A N   1 
ATOM   1565 C  CA  . PRO A 1 194 ? 13.795 4.742   29.431  1.00 7.96   ? 194 PRO A CA  1 
ATOM   1566 C  C   . PRO A 1 194 ? 14.976 4.076   28.750  1.00 6.82   ? 194 PRO A C   1 
ATOM   1567 O  O   . PRO A 1 194 ? 15.663 3.320   29.415  1.00 7.98   ? 194 PRO A O   1 
ATOM   1568 C  CB  . PRO A 1 194 ? 14.255 5.679   30.592  1.00 8.30   ? 194 PRO A CB  1 
ATOM   1569 C  CG  . PRO A 1 194 ? 14.266 4.774   31.813  1.00 9.33   ? 194 PRO A CG  1 
ATOM   1570 C  CD  . PRO A 1 194 ? 13.124 3.793   31.581  1.00 9.55   ? 194 PRO A CD  1 
ATOM   1571 N  N   . GLY A 1 195 ? 15.228 4.441   27.503  1.00 7.04   ? 195 GLY A N   1 
ATOM   1572 C  CA  . GLY A 1 195 ? 16.308 3.791   26.797  1.00 6.55   ? 195 GLY A CA  1 
ATOM   1573 C  C   . GLY A 1 195 ? 16.871 4.677   25.712  1.00 5.77   ? 195 GLY A C   1 
ATOM   1574 O  O   . GLY A 1 195 ? 16.984 5.910   25.868  1.00 7.17   ? 195 GLY A O   1 
ATOM   1575 N  N   . SER A 1 196 ? 17.292 3.997   24.645  1.00 6.22   ? 196 SER A N   1 
ATOM   1576 C  CA  . SER A 1 196 ? 18.145 4.629   23.641  1.00 6.45   ? 196 SER A CA  1 
ATOM   1577 C  C   . SER A 1 196 ? 17.711 4.220   22.241  1.00 5.66   ? 196 SER A C   1 
ATOM   1578 O  O   . SER A 1 196 ? 16.932 3.300   22.038  1.00 6.19   ? 196 SER A O   1 
ATOM   1579 C  CB  . SER A 1 196 ? 19.610 4.221   23.837  1.00 7.07   ? 196 SER A CB  1 
ATOM   1580 O  OG  . SER A 1 196 ? 19.836 2.868   23.384  1.00 7.04   ? 196 SER A OG  1 
ATOM   1581 N  N   . LEU A 1 197 ? 18.258 4.903   21.220  1.00 6.12   ? 197 LEU A N   1 
ATOM   1582 C  CA  . LEU A 1 197 ? 18.287 4.333   19.874  1.00 6.56   ? 197 LEU A CA  1 
ATOM   1583 C  C   . LEU A 1 197 ? 18.957 2.988   19.933  1.00 6.17   ? 197 LEU A C   1 
ATOM   1584 O  O   . LEU A 1 197 ? 19.947 2.802   20.652  1.00 6.61   ? 197 LEU A O   1 
ATOM   1585 C  CB  . LEU A 1 197 ? 19.052 5.276   18.899  1.00 7.58   ? 197 LEU A CB  1 
ATOM   1586 C  CG  . LEU A 1 197 ? 18.509 6.713   18.863  1.00 8.87   ? 197 LEU A CG  1 
ATOM   1587 C  CD1 . LEU A 1 197 ? 19.385 7.530   17.934  1.00 12.25  ? 197 LEU A CD1 1 
ATOM   1588 C  CD2 . LEU A 1 197 ? 17.029 6.741   18.429  1.00 11.80  ? 197 LEU A CD2 1 
ATOM   1589 N  N   . THR A 1 198 ? 18.564 2.081   19.024  1.00 6.97   ? 198 THR A N   1 
ATOM   1590 C  CA  . THR A 1 198 ? 19.213 0.789   18.984  1.00 6.70   ? 198 THR A CA  1 
ATOM   1591 C  C   . THR A 1 198 ? 20.234 0.696   17.848  1.00 7.07   ? 198 THR A C   1 
ATOM   1592 O  O   . THR A 1 198 ? 20.803 -0.383  17.632  1.00 7.89   ? 198 THR A O   1 
ATOM   1593 C  CB  . THR A 1 198 ? 18.205 -0.375  18.892  1.00 6.72   ? 198 THR A CB  1 
ATOM   1594 O  OG1 . THR A 1 198 ? 17.592 -0.273  17.586  1.00 5.92   ? 198 THR A OG1 1 
ATOM   1595 C  CG2 . THR A 1 198 ? 17.180 -0.366  20.021  1.00 6.77   ? 198 THR A CG2 1 
ATOM   1596 N  N   . THR A 1 199 ? 20.412 1.798   17.100  1.00 7.65   ? 199 THR A N   1 
ATOM   1597 C  CA  . THR A 1 199 ? 21.496 1.869   16.136  1.00 8.75   ? 199 THR A CA  1 
ATOM   1598 C  C   . THR A 1 199 ? 22.329 3.096   16.480  1.00 9.48   ? 199 THR A C   1 
ATOM   1599 O  O   . THR A 1 199 ? 21.848 4.035   17.126  1.00 9.57   ? 199 THR A O   1 
ATOM   1600 C  CB  . THR A 1 199 ? 20.962 2.091   14.720  1.00 9.80   ? 199 THR A CB  1 
ATOM   1601 O  OG1 . THR A 1 199 ? 20.095 3.223   14.730  1.00 14.18  ? 199 THR A OG1 1 
ATOM   1602 C  CG2 . THR A 1 199 ? 20.174 0.894   14.267  1.00 9.92   ? 199 THR A CG2 1 
ATOM   1603 N  N   . PRO A 1 200 ? 23.599 3.157   16.007  1.00 9.97   ? 200 PRO A N   1 
ATOM   1604 C  CA  . PRO A 1 200 ? 24.378 4.397   16.103  1.00 10.36  ? 200 PRO A CA  1 
ATOM   1605 C  C   . PRO A 1 200 ? 23.445 5.518   15.659  1.00 9.42   ? 200 PRO A C   1 
ATOM   1606 O  O   . PRO A 1 200 ? 22.747 5.447   14.626  1.00 11.98  ? 200 PRO A O   1 
ATOM   1607 C  CB  . PRO A 1 200 ? 25.556 4.074   15.171  1.00 12.41  ? 200 PRO A CB  1 
ATOM   1608 C  CG  . PRO A 1 200 ? 25.781 2.583   15.403  1.00 12.28  ? 200 PRO A CG  1 
ATOM   1609 C  CD  . PRO A 1 200 ? 24.352 2.048   15.382  1.00 10.73  ? 200 PRO A CD  1 
ATOM   1610 N  N   . PRO A 1 201 ? 23.489 6.673   16.335  1.00 9.77   ? 201 PRO A N   1 
ATOM   1611 C  CA  . PRO A 1 201 ? 24.467 7.038   17.384  1.00 10.73  ? 201 PRO A CA  1 
ATOM   1612 C  C   . PRO A 1 201 ? 24.117 6.573   18.815  1.00 9.27   ? 201 PRO A C   1 
ATOM   1613 O  O   . PRO A 1 201 ? 24.823 6.896   19.769  1.00 10.26  ? 201 PRO A O   1 
ATOM   1614 C  CB  . PRO A 1 201 ? 24.458 8.572   17.294  1.00 13.08  ? 201 PRO A CB  1 
ATOM   1615 C  CG  . PRO A 1 201 ? 23.058 8.906   16.879  1.00 15.60  ? 201 PRO A CG  1 
ATOM   1616 C  CD  . PRO A 1 201 ? 22.674 7.814   15.899  1.00 13.74  ? 201 PRO A CD  1 
ATOM   1617 N  N   . LEU A 1 202 ? 23.076 5.750   18.979  1.00 8.58   ? 202 LEU A N   1 
ATOM   1618 C  CA  . LEU A 1 202 ? 22.787 5.084   20.258  1.00 7.79   ? 202 LEU A CA  1 
ATOM   1619 C  C   . LEU A 1 202 ? 22.422 6.078   21.362  1.00 7.21   ? 202 LEU A C   1 
ATOM   1620 O  O   . LEU A 1 202 ? 22.466 5.757   22.540  1.00 8.05   ? 202 LEU A O   1 
ATOM   1621 C  CB  . LEU A 1 202 ? 23.931 4.166   20.737  1.00 8.10   ? 202 LEU A CB  1 
ATOM   1622 C  CG  . LEU A 1 202 ? 24.263 3.055   19.711  1.00 8.31   ? 202 LEU A CG  1 
ATOM   1623 C  CD1 . LEU A 1 202 ? 25.529 2.346   20.137  1.00 10.48  ? 202 LEU A CD1 1 
ATOM   1624 C  CD2 . LEU A 1 202 ? 23.138 2.007   19.620  1.00 9.49   ? 202 LEU A CD2 1 
ATOM   1625 N  N   . THR A 1 203 ? 21.906 7.244   20.916  1.00 8.73   ? 203 THR A N   1 
ATOM   1626 C  CA  . THR A 1 203 ? 21.602 8.339   21.836  1.00 9.11   ? 203 THR A CA  1 
ATOM   1627 C  C   . THR A 1 203 ? 20.526 7.904   22.841  1.00 7.69   ? 203 THR A C   1 
ATOM   1628 O  O   . THR A 1 203 ? 19.504 7.269   22.495  1.00 8.21   ? 203 THR A O   1 
ATOM   1629 C  CB  . THR A 1 203 ? 21.138 9.537   21.018  1.00 11.79  ? 203 THR A CB  1 
ATOM   1630 O  OG1 . THR A 1 203 ? 22.117 9.719   19.982  1.00 13.87  ? 203 THR A OG1 1 
ATOM   1631 C  CG2 . THR A 1 203 ? 21.034 10.756  21.881  1.00 15.54  ? 203 THR A CG2 1 
ATOM   1632 N  N   . GLU A 1 204 ? 20.682 8.346   24.098  1.00 9.06   ? 204 GLU A N   1 
ATOM   1633 C  CA  . GLU A 1 204 ? 19.777 7.960   25.184  1.00 8.60   ? 204 GLU A CA  1 
ATOM   1634 C  C   . GLU A 1 204 ? 18.634 8.963   25.268  1.00 8.43   ? 204 GLU A C   1 
ATOM   1635 O  O   . GLU A 1 204 ? 18.495 9.713   26.256  1.00 11.43  ? 204 GLU A O   1 
ATOM   1636 C  CB  . GLU A 1 204 ? 20.584 7.799   26.478  1.00 9.55   ? 204 GLU A CB  1 
ATOM   1637 C  CG  . GLU A 1 204 ? 21.525 6.615   26.350  1.00 8.58   ? 204 GLU A CG  1 
ATOM   1638 C  CD  . GLU A 1 204 ? 22.389 6.346   27.574  1.00 10.51  ? 204 GLU A CD  1 
ATOM   1639 O  OE1 . GLU A 1 204 ? 22.642 7.258   28.398  1.00 13.50  ? 204 GLU A OE1 1 
ATOM   1640 O  OE2 . GLU A 1 204 ? 22.820 5.159   27.736  1.00 9.95   ? 204 GLU A OE2 1 
ATOM   1641 N  N   . CYS A 1 205 ? 17.759 8.927   24.277  1.00 6.93   ? 205 CYS A N   1 
ATOM   1642 C  CA  . CYS A 1 205 ? 16.753 9.969   24.075  1.00 6.57   ? 205 CYS A CA  1 
ATOM   1643 C  C   . CYS A 1 205 ? 15.378 9.328   23.918  1.00 7.67   ? 205 CYS A C   1 
ATOM   1644 O  O   . CYS A 1 205 ? 14.452 10.009  23.535  1.00 8.56   ? 205 CYS A O   1 
ATOM   1645 C  CB  . CYS A 1 205 ? 16.996 10.835  22.840  1.00 8.24   ? 205 CYS A CB  1 
ATOM   1646 S  SG  . CYS A 1 205 ? 17.121 9.883   21.311  1.00 10.73  ? 205 CYS A SG  1 
ATOM   1647 N  N   . VAL A 1 206 ? 15.207 8.018   24.240  1.00 6.95   ? 206 VAL A N   1 
ATOM   1648 C  CA  . VAL A 1 206 ? 13.982 7.325   23.857  1.00 6.24   ? 206 VAL A CA  1 
ATOM   1649 C  C   . VAL A 1 206 ? 13.198 6.868   25.075  1.00 6.39   ? 206 VAL A C   1 
ATOM   1650 O  O   . VAL A 1 206 ? 13.739 6.183   25.924  1.00 8.13   ? 206 VAL A O   1 
ATOM   1651 C  CB  . VAL A 1 206 ? 14.267 6.075   23.001  1.00 6.46   ? 206 VAL A CB  1 
ATOM   1652 C  CG1 . VAL A 1 206 ? 12.960 5.347   22.616  1.00 7.34   ? 206 VAL A CG1 1 
ATOM   1653 C  CG2 . VAL A 1 206 ? 15.062 6.453   21.729  1.00 8.83   ? 206 VAL A CG2 1 
ATOM   1654 N  N   . THR A 1 207 ? 11.892 7.195   25.124  1.00 5.92   ? 207 THR A N   1 
ATOM   1655 C  CA  . THR A 1 207 ? 10.962 6.444   25.963  1.00 6.40   ? 207 THR A CA  1 
ATOM   1656 C  C   . THR A 1 207 ? 10.426 5.281   25.120  1.00 6.18   ? 207 THR A C   1 
ATOM   1657 O  O   . THR A 1 207 ? 9.767  5.505   24.115  1.00 7.44   ? 207 THR A O   1 
ATOM   1658 C  CB  . THR A 1 207 ? 9.785  7.333   26.416  1.00 6.83   ? 207 THR A CB  1 
ATOM   1659 O  OG1 . THR A 1 207 ? 10.290 8.448   27.153  1.00 8.89   ? 207 THR A OG1 1 
ATOM   1660 C  CG2 . THR A 1 207 ? 8.845  6.528   27.309  1.00 8.86   ? 207 THR A CG2 1 
ATOM   1661 N  N   . TRP A 1 208 ? 10.757 4.068   25.567  1.00 6.44   ? 208 TRP A N   1 
ATOM   1662 C  CA  . TRP A 1 208 ? 10.291 2.870   24.891  1.00 5.52   ? 208 TRP A CA  1 
ATOM   1663 C  C   . TRP A 1 208 ? 8.920  2.446   25.385  1.00 5.83   ? 208 TRP A C   1 
ATOM   1664 O  O   . TRP A 1 208 ? 8.731  2.399   26.597  1.00 6.67   ? 208 TRP A O   1 
ATOM   1665 C  CB  . TRP A 1 208 ? 11.308 1.706   25.079  1.00 5.95   ? 208 TRP A CB  1 
ATOM   1666 C  CG  . TRP A 1 208 ? 12.441 1.861   24.113  1.00 5.34   ? 208 TRP A CG  1 
ATOM   1667 C  CD1 . TRP A 1 208 ? 13.670 2.461   24.304  1.00 6.06   ? 208 TRP A CD1 1 
ATOM   1668 C  CD2 . TRP A 1 208 ? 12.383 1.450   22.724  1.00 5.84   ? 208 TRP A CD2 1 
ATOM   1669 N  NE1 . TRP A 1 208 ? 14.366 2.423   23.116  1.00 6.71   ? 208 TRP A NE1 1 
ATOM   1670 C  CE2 . TRP A 1 208 ? 13.620 1.825   22.117  1.00 6.16   ? 208 TRP A CE2 1 
ATOM   1671 C  CE3 . TRP A 1 208 ? 11.419 0.810   21.914  1.00 6.55   ? 208 TRP A CE3 1 
ATOM   1672 C  CZ2 . TRP A 1 208 ? 13.904 1.565   20.779  1.00 6.46   ? 208 TRP A CZ2 1 
ATOM   1673 C  CZ3 . TRP A 1 208 ? 11.728 0.513   20.604  1.00 6.27   ? 208 TRP A CZ3 1 
ATOM   1674 C  CH2 . TRP A 1 208 ? 12.943 0.911   20.027  1.00 7.45   ? 208 TRP A CH2 1 
ATOM   1675 N  N   . ILE A 1 209 ? 8.033  2.121   24.437  1.00 5.56   ? 209 ILE A N   1 
ATOM   1676 C  CA  . ILE A 1 209 ? 6.719  1.589   24.793  1.00 5.47   ? 209 ILE A CA  1 
ATOM   1677 C  C   . ILE A 1 209 ? 6.587  0.333   23.941  1.00 5.73   ? 209 ILE A C   1 
ATOM   1678 O  O   . ILE A 1 209 ? 6.551  0.441   22.728  1.00 6.84   ? 209 ILE A O   1 
ATOM   1679 C  CB  . ILE A 1 209 ? 5.622  2.635   24.451  1.00 6.91   ? 209 ILE A CB  1 
ATOM   1680 C  CG1 . ILE A 1 209 ? 5.824  3.894   25.298  1.00 6.99   ? 209 ILE A CG1 1 
ATOM   1681 C  CG2 . ILE A 1 209 ? 4.229  2.014   24.741  1.00 8.76   ? 209 ILE A CG2 1 
ATOM   1682 C  CD1 . ILE A 1 209 ? 4.999  5.077   24.788  1.00 9.78   ? 209 ILE A CD1 1 
ATOM   1683 N  N   . VAL A 1 210 ? 6.624  -0.847  24.604  1.00 6.16   ? 210 VAL A N   1 
ATOM   1684 C  CA  . VAL A 1 210 ? 6.651  -2.104  23.861  1.00 6.21   ? 210 VAL A CA  1 
ATOM   1685 C  C   . VAL A 1 210 ? 5.322  -2.791  24.129  1.00 5.51   ? 210 VAL A C   1 
ATOM   1686 O  O   . VAL A 1 210 ? 5.006  -3.105  25.287  1.00 7.11   ? 210 VAL A O   1 
ATOM   1687 C  CB  . VAL A 1 210 ? 7.842  -2.983  24.305  1.00 5.78   ? 210 VAL A CB  1 
ATOM   1688 C  CG1 . VAL A 1 210 ? 7.777  -4.311  23.556  1.00 7.50   ? 210 VAL A CG1 1 
ATOM   1689 C  CG2 . VAL A 1 210 ? 9.145  -2.226  24.028  1.00 7.27   ? 210 VAL A CG2 1 
ATOM   1690 N  N   . LEU A 1 211 ? 4.553  -3.078  23.055  1.00 6.48   ? 211 LEU A N   1 
ATOM   1691 C  CA  . LEU A 1 211 ? 3.245  -3.728  23.253  1.00 6.89   ? 211 LEU A CA  1 
ATOM   1692 C  C   . LEU A 1 211 ? 3.428  -5.200  23.643  1.00 7.23   ? 211 LEU A C   1 
ATOM   1693 O  O   . LEU A 1 211 ? 4.307  -5.906  23.096  1.00 7.67   ? 211 LEU A O   1 
ATOM   1694 C  CB  . LEU A 1 211 ? 2.437  -3.602  21.930  1.00 7.82   ? 211 LEU A CB  1 
ATOM   1695 C  CG  . LEU A 1 211 ? 2.056  -2.176  21.531  1.00 8.56   ? 211 LEU A CG  1 
ATOM   1696 C  CD1 . LEU A 1 211 ? 1.012  -2.197  20.422  1.00 10.14  ? 211 LEU A CD1 1 
ATOM   1697 C  CD2 . LEU A 1 211 ? 1.553  -1.357  22.690  1.00 9.23   ? 211 LEU A CD2 1 
ATOM   1698 N  N   A LYS A 1 212 ? 2.576  -5.669  24.552  0.50 8.21   ? 212 LYS A N   1 
ATOM   1699 N  N   B LYS A 1 212 ? 2.574  -5.662  24.558  0.50 8.17   ? 212 LYS A N   1 
ATOM   1700 C  CA  A LYS A 1 212 ? 2.600  -7.059  25.000  0.50 10.20  ? 212 LYS A CA  1 
ATOM   1701 C  CA  B LYS A 1 212 ? 2.632  -7.058  24.981  0.50 10.10  ? 212 LYS A CA  1 
ATOM   1702 C  C   A LYS A 1 212 ? 2.152  -8.020  23.900  0.50 8.71   ? 212 LYS A C   1 
ATOM   1703 C  C   B LYS A 1 212 ? 2.163  -8.016  23.889  0.50 8.71   ? 212 LYS A C   1 
ATOM   1704 O  O   A LYS A 1 212 ? 2.714  -9.105  23.737  0.50 10.81  ? 212 LYS A O   1 
ATOM   1705 O  O   B LYS A 1 212 ? 2.715  -9.105  23.738  0.50 10.81  ? 212 LYS A O   1 
ATOM   1706 C  CB  A LYS A 1 212 ? 1.694  -7.118  26.228  0.50 15.67  ? 212 LYS A CB  1 
ATOM   1707 C  CB  B LYS A 1 212 ? 1.772  -7.282  26.219  0.50 15.15  ? 212 LYS A CB  1 
ATOM   1708 C  CG  A LYS A 1 212 ? 1.100  -8.459  26.645  0.50 21.11  ? 212 LYS A CG  1 
ATOM   1709 C  CG  B LYS A 1 212 ? 1.738  -8.736  26.691  0.50 17.20  ? 212 LYS A CG  1 
ATOM   1710 C  CD  A LYS A 1 212 ? -0.101 -8.209  27.596  0.50 22.62  ? 212 LYS A CD  1 
ATOM   1711 C  CD  B LYS A 1 212 ? 0.906  -8.919  27.956  0.50 23.14  ? 212 LYS A CD  1 
ATOM   1712 C  CE  A LYS A 1 212 ? -1.515 -8.214  27.021  0.50 23.55  ? 212 LYS A CE  1 
ATOM   1713 C  CE  B LYS A 1 212 ? 0.749  -10.368 28.370  0.50 25.03  ? 212 LYS A CE  1 
ATOM   1714 N  NZ  A LYS A 1 212 ? -1.633 -7.760  25.601  0.50 15.78  ? 212 LYS A NZ  1 
ATOM   1715 N  NZ  B LYS A 1 212 ? -0.380 -10.542 29.319  0.50 31.31  ? 212 LYS A NZ  1 
ATOM   1716 N  N   . GLU A 1 213 ? 1.159  -7.631  23.113  1.00 7.43   ? 213 GLU A N   1 
ATOM   1717 C  CA  . GLU A 1 213 ? 0.564  -8.544  22.140  1.00 8.36   ? 213 GLU A CA  1 
ATOM   1718 C  C   . GLU A 1 213 ? 1.343  -8.460  20.841  1.00 8.04   ? 213 GLU A C   1 
ATOM   1719 O  O   . GLU A 1 213 ? 1.393  -7.407  20.212  1.00 7.86   ? 213 GLU A O   1 
ATOM   1720 C  CB  . GLU A 1 213 ? -0.905 -8.184  21.886  1.00 9.37   ? 213 GLU A CB  1 
ATOM   1721 C  CG  . GLU A 1 213 ? -1.575 -9.202  20.983  1.00 11.28  ? 213 GLU A CG  1 
ATOM   1722 C  CD  . GLU A 1 213 ? -3.051 -8.996  20.747  1.00 16.63  ? 213 GLU A CD  1 
ATOM   1723 O  OE1 . GLU A 1 213 ? -3.646 -8.074  21.315  1.00 11.79  ? 213 GLU A OE1 1 
ATOM   1724 O  OE2 . GLU A 1 213 ? -3.613 -9.914  20.124  1.00 25.71  ? 213 GLU A OE2 1 
ATOM   1725 N  N   A PRO A 1 214 ? 1.935  -9.570  20.341  0.50 7.78   ? 214 PRO A N   1 
ATOM   1726 N  N   B PRO A 1 214 ? 1.960  -9.564  20.370  0.50 7.71   ? 214 PRO A N   1 
ATOM   1727 C  CA  A PRO A 1 214 ? 2.577  -9.500  19.035  0.50 8.36   ? 214 PRO A CA  1 
ATOM   1728 C  CA  B PRO A 1 214 ? 2.577  -9.525  19.047  0.50 8.35   ? 214 PRO A CA  1 
ATOM   1729 C  C   A PRO A 1 214 ? 1.508  -9.515  17.942  0.50 8.09   ? 214 PRO A C   1 
ATOM   1730 C  C   B PRO A 1 214 ? 1.512  -9.529  17.944  0.50 8.17   ? 214 PRO A C   1 
ATOM   1731 O  O   A PRO A 1 214 ? 0.354  -9.891  18.182  0.50 9.93   ? 214 PRO A O   1 
ATOM   1732 O  O   B PRO A 1 214 ? 0.360  -9.911  18.184  0.50 10.89  ? 214 PRO A O   1 
ATOM   1733 C  CB  A PRO A 1 214 ? 3.306  -10.850 18.942  0.50 9.95   ? 214 PRO A CB  1 
ATOM   1734 C  CB  B PRO A 1 214 ? 3.324  -10.868 18.985  0.50 9.51   ? 214 PRO A CB  1 
ATOM   1735 C  CG  A PRO A 1 214 ? 2.455  -11.788 19.771  0.50 10.77  ? 214 PRO A CG  1 
ATOM   1736 C  CG  B PRO A 1 214 ? 3.467  -11.310 20.438  0.50 8.41   ? 214 PRO A CG  1 
ATOM   1737 C  CD  A PRO A 1 214 ? 1.973  -10.923 20.923  0.50 10.78  ? 214 PRO A CD  1 
ATOM   1738 C  CD  B PRO A 1 214 ? 2.179  -10.837 21.080  0.50 9.56   ? 214 PRO A CD  1 
ATOM   1739 N  N   . ILE A 1 215 ? 1.910  -9.053  16.746  1.00 7.56   ? 215 ILE A N   1 
ATOM   1740 C  CA  . ILE A 1 215 ? 1.098  -9.317  15.563  1.00 8.42   ? 215 ILE A CA  1 
ATOM   1741 C  C   . ILE A 1 215 ? 1.648  -10.550 14.887  1.00 8.42   ? 215 ILE A C   1 
ATOM   1742 O  O   . ILE A 1 215 ? 2.848  -10.873 15.004  1.00 9.64   ? 215 ILE A O   1 
ATOM   1743 C  CB  . ILE A 1 215 ? 1.051  -8.097  14.604  1.00 7.99   ? 215 ILE A CB  1 
ATOM   1744 C  CG1 . ILE A 1 215 ? 2.442  -7.692  14.102  1.00 8.68   ? 215 ILE A CG1 1 
ATOM   1745 C  CG2 . ILE A 1 215 ? 0.356  -6.916  15.315  1.00 9.65   ? 215 ILE A CG2 1 
ATOM   1746 C  CD1 . ILE A 1 215 ? 2.403  -6.696  12.918  1.00 9.17   ? 215 ILE A CD1 1 
ATOM   1747 N  N   A SER A 1 216 ? 0.739  -11.205 14.149  0.50 10.29  ? 216 SER A N   1 
ATOM   1748 N  N   B SER A 1 216 ? 0.769  -11.300 14.218  0.50 10.49  ? 216 SER A N   1 
ATOM   1749 C  CA  A SER A 1 216 ? 1.050  -12.384 13.345  0.50 8.47   ? 216 SER A CA  1 
ATOM   1750 C  CA  B SER A 1 216 ? 1.304  -12.417 13.443  0.50 10.20  ? 216 SER A CA  1 
ATOM   1751 C  C   A SER A 1 216 ? 1.320  -11.972 11.907  0.50 9.16   ? 216 SER A C   1 
ATOM   1752 C  C   B SER A 1 216 ? 1.371  -11.995 11.989  0.50 9.00   ? 216 SER A C   1 
ATOM   1753 O  O   A SER A 1 216 ? 0.504  -11.262 11.328  0.50 11.41  ? 216 SER A O   1 
ATOM   1754 O  O   B SER A 1 216 ? 0.469  -11.333 11.486  0.50 9.85   ? 216 SER A O   1 
ATOM   1755 C  CB  A SER A 1 216 ? -0.076 -13.366 13.458  0.50 11.56  ? 216 SER A CB  1 
ATOM   1756 C  CB  B SER A 1 216 ? 0.505  -13.680 13.609  0.50 13.12  ? 216 SER A CB  1 
ATOM   1757 O  OG  A SER A 1 216 ? 0.086  -14.112 14.653  0.50 16.45  ? 216 SER A OG  1 
ATOM   1758 O  OG  B SER A 1 216 ? -0.810 -13.420 13.171  0.50 16.18  ? 216 SER A OG  1 
ATOM   1759 N  N   . VAL A 1 217 ? 2.456  -12.433 11.357  1.00 8.67   ? 217 VAL A N   1 
ATOM   1760 C  CA  . VAL A 1 217 ? 2.733  -12.267 9.936   1.00 8.72   ? 217 VAL A CA  1 
ATOM   1761 C  C   . VAL A 1 217 ? 2.991  -13.635 9.343   1.00 8.55   ? 217 VAL A C   1 
ATOM   1762 O  O   . VAL A 1 217 ? 3.352  -14.572 10.038  1.00 9.03   ? 217 VAL A O   1 
ATOM   1763 C  CB  . VAL A 1 217 ? 3.920  -11.317 9.685   1.00 9.70   ? 217 VAL A CB  1 
ATOM   1764 C  CG1 . VAL A 1 217 ? 3.659  -10.002 10.391  1.00 10.06  ? 217 VAL A CG1 1 
ATOM   1765 C  CG2 . VAL A 1 217 ? 5.186  -11.920 10.248  1.00 11.05  ? 217 VAL A CG2 1 
ATOM   1766 N  N   . SER A 1 218 ? 2.820  -13.763 8.049   1.00 9.23   ? 218 SER A N   1 
ATOM   1767 C  CA  . SER A 1 218 ? 3.051  -15.089 7.491   1.00 9.37   ? 218 SER A CA  1 
ATOM   1768 C  C   . SER A 1 218 ? 4.531  -15.351 7.277   1.00 9.26   ? 218 SER A C   1 
ATOM   1769 O  O   . SER A 1 218 ? 5.345  -14.427 7.124   1.00 9.01   ? 218 SER A O   1 
ATOM   1770 C  CB  . SER A 1 218 ? 2.269  -15.295 6.236   1.00 10.01  ? 218 SER A CB  1 
ATOM   1771 O  OG  . SER A 1 218 ? 2.728  -14.393 5.246   1.00 9.56   ? 218 SER A OG  1 
ATOM   1772 N  N   . SER A 1 219 ? 4.888  -16.633 7.116   1.00 9.72   ? 219 SER A N   1 
ATOM   1773 C  CA  . SER A 1 219 ? 6.256  -16.999 6.762   1.00 11.33  ? 219 SER A CA  1 
ATOM   1774 C  C   . SER A 1 219 ? 6.672  -16.307 5.459   1.00 10.14  ? 219 SER A C   1 
ATOM   1775 O  O   . SER A 1 219 ? 7.832  -15.836 5.343   1.00 12.43  ? 219 SER A O   1 
ATOM   1776 C  CB  . SER A 1 219 ? 6.408  -18.513 6.735   1.00 12.90  ? 219 SER A CB  1 
ATOM   1777 O  OG  . SER A 1 219 ? 5.526  -19.085 5.772   1.00 13.61  ? 219 SER A OG  1 
ATOM   1778 N  N   . GLU A 1 220 ? 5.714  -16.162 4.516   1.00 11.16  ? 220 GLU A N   1 
ATOM   1779 C  CA  . GLU A 1 220 ? 6.083  -15.539 3.238   1.00 11.66  ? 220 GLU A CA  1 
ATOM   1780 C  C   . GLU A 1 220 ? 6.315  -14.029 3.343   1.00 12.22  ? 220 GLU A C   1 
ATOM   1781 O  O   . GLU A 1 220 ? 7.219  -13.483 2.683   1.00 13.01  ? 220 GLU A O   1 
ATOM   1782 C  CB  . GLU A 1 220 ? 5.007  -15.713 2.170   1.00 14.17  ? 220 GLU A CB  1 
ATOM   1783 C  CG  . GLU A 1 220 ? 4.833  -17.195 1.764   1.00 14.29  ? 220 GLU A CG  1 
ATOM   1784 C  CD  . GLU A 1 220 ? 3.892  -17.977 2.677   1.00 15.00  ? 220 GLU A CD  1 
ATOM   1785 O  OE1 . GLU A 1 220 ? 3.281  -17.414 3.605   1.00 14.69  ? 220 GLU A OE1 1 
ATOM   1786 O  OE2 . GLU A 1 220 ? 3.776  -19.184 2.462   1.00 22.57  ? 220 GLU A OE2 1 
ATOM   1787 N  N   . GLN A 1 221 ? 5.582  -13.376 4.281   1.00 10.24  ? 221 GLN A N   1 
ATOM   1788 C  CA  . GLN A 1 221 ? 5.806  -11.934 4.458   1.00 8.99   ? 221 GLN A CA  1 
ATOM   1789 C  C   . GLN A 1 221 ? 7.224  -11.689 4.987   1.00 9.10   ? 221 GLN A C   1 
ATOM   1790 O  O   . GLN A 1 221 ? 7.946  -10.855 4.447   1.00 10.16  ? 221 GLN A O   1 
ATOM   1791 C  CB  . GLN A 1 221 ? 4.729  -11.388 5.365   1.00 10.27  ? 221 GLN A CB  1 
ATOM   1792 C  CG  . GLN A 1 221 ? 3.388  -11.263 4.656   1.00 9.78   ? 221 GLN A CG  1 
ATOM   1793 C  CD  . GLN A 1 221 ? 2.290  -10.749 5.547   1.00 10.38  ? 221 GLN A CD  1 
ATOM   1794 O  OE1 . GLN A 1 221 ? 2.152  -11.138 6.707   1.00 10.10  ? 221 GLN A OE1 1 
ATOM   1795 N  NE2 . GLN A 1 221 ? 1.421  -9.908  4.979   1.00 10.25  ? 221 GLN A NE2 1 
ATOM   1796 N  N   . VAL A 1 222 ? 7.674  -12.450 5.993   1.00 9.13   ? 222 VAL A N   1 
ATOM   1797 C  CA  . VAL A 1 222 ? 8.994  -12.230 6.563   1.00 10.12  ? 222 VAL A CA  1 
ATOM   1798 C  C   . VAL A 1 222 ? 10.065 -12.702 5.590   1.00 9.89   ? 222 VAL A C   1 
ATOM   1799 O  O   . VAL A 1 222 ? 11.138 -12.105 5.500   1.00 10.81  ? 222 VAL A O   1 
ATOM   1800 C  CB  . VAL A 1 222 ? 9.158  -12.778 8.006   1.00 13.12  ? 222 VAL A CB  1 
ATOM   1801 C  CG1 . VAL A 1 222 ? 9.026  -14.257 8.132   1.00 15.42  ? 222 VAL A CG1 1 
ATOM   1802 C  CG2 . VAL A 1 222 ? 10.487 -12.298 8.616   1.00 14.47  ? 222 VAL A CG2 1 
ATOM   1803 N  N   . LEU A 1 223 ? 9.767  -13.748 4.800   1.00 11.44  ? 223 LEU A N   1 
ATOM   1804 C  CA  . LEU A 1 223 ? 10.738 -14.190 3.824   1.00 13.30  ? 223 LEU A CA  1 
ATOM   1805 C  C   . LEU A 1 223 ? 11.071 -13.038 2.874   1.00 10.86  ? 223 LEU A C   1 
ATOM   1806 O  O   . LEU A 1 223 ? 12.220 -12.895 2.419   1.00 12.19  ? 223 LEU A O   1 
ATOM   1807 C  CB  . LEU A 1 223 ? 10.101 -15.412 3.114   1.00 17.78  ? 223 LEU A CB  1 
ATOM   1808 C  CG  . LEU A 1 223 ? 10.845 -16.092 2.004   1.00 21.13  ? 223 LEU A CG  1 
ATOM   1809 C  CD1 . LEU A 1 223 ? 10.126 -17.411 1.731   1.00 23.81  ? 223 LEU A CD1 1 
ATOM   1810 C  CD2 . LEU A 1 223 ? 10.739 -15.258 0.764   1.00 20.09  ? 223 LEU A CD2 1 
ATOM   1811 N  N   . LYS A 1 224 ? 10.045 -12.256 2.526   1.00 10.59  ? 224 LYS A N   1 
ATOM   1812 C  CA  . LYS A 1 224 ? 10.275 -11.142 1.612   1.00 10.32  ? 224 LYS A CA  1 
ATOM   1813 C  C   . LYS A 1 224 ? 11.135 -10.039 2.225   1.00 9.25   ? 224 LYS A C   1 
ATOM   1814 O  O   . LYS A 1 224 ? 11.954 -9.445  1.512   1.00 9.65   ? 224 LYS A O   1 
ATOM   1815 C  CB  . LYS A 1 224 ? 8.940  -10.683 1.034   1.00 13.11  ? 224 LYS A CB  1 
ATOM   1816 C  CG  . LYS A 1 224 ? 8.388  -11.755 0.062   1.00 15.98  ? 224 LYS A CG  1 
ATOM   1817 C  CD  . LYS A 1 224 ? 7.037  -11.580 -0.539  1.00 18.27  ? 224 LYS A CD  1 
ATOM   1818 C  CE  . LYS A 1 224 ? 6.614  -12.624 -1.583  1.00 22.26  ? 224 LYS A CE  1 
ATOM   1819 N  NZ  . LYS A 1 224 ? 5.342  -12.218 -2.258  1.00 24.05  ? 224 LYS A NZ  1 
ATOM   1820 N  N   . PHE A 1 225 ? 11.027 -9.785  3.552   1.00 8.46   ? 225 PHE A N   1 
ATOM   1821 C  CA  . PHE A 1 225 ? 11.949 -8.874  4.185   1.00 8.87   ? 225 PHE A CA  1 
ATOM   1822 C  C   . PHE A 1 225 ? 13.377 -9.331  3.940   1.00 8.09   ? 225 PHE A C   1 
ATOM   1823 O  O   . PHE A 1 225 ? 14.283 -8.520  3.694   1.00 9.31   ? 225 PHE A O   1 
ATOM   1824 C  CB  . PHE A 1 225 ? 11.761 -8.847  5.700   1.00 9.04   ? 225 PHE A CB  1 
ATOM   1825 C  CG  . PHE A 1 225 ? 10.533 -8.157  6.243   1.00 7.60   ? 225 PHE A CG  1 
ATOM   1826 C  CD1 . PHE A 1 225 ? 9.510  -7.759  5.398   1.00 9.54   ? 225 PHE A CD1 1 
ATOM   1827 C  CD2 . PHE A 1 225 ? 10.400 -7.906  7.599   1.00 9.62   ? 225 PHE A CD2 1 
ATOM   1828 C  CE1 . PHE A 1 225 ? 8.383  -7.125  5.897   1.00 11.18  ? 225 PHE A CE1 1 
ATOM   1829 C  CE2 . PHE A 1 225 ? 9.273  -7.272  8.097   1.00 11.19  ? 225 PHE A CE2 1 
ATOM   1830 C  CZ  . PHE A 1 225 ? 8.266  -6.883  7.245   1.00 10.18  ? 225 PHE A CZ  1 
ATOM   1831 N  N   . ARG A 1 226 ? 13.608 -10.671 4.009   1.00 7.80   ? 226 ARG A N   1 
ATOM   1832 C  CA  . ARG A 1 226 ? 14.957 -11.221 3.946   1.00 8.69   ? 226 ARG A CA  1 
ATOM   1833 C  C   . ARG A 1 226 ? 15.523 -11.249 2.529   1.00 8.44   ? 226 ARG A C   1 
ATOM   1834 O  O   . ARG A 1 226 ? 16.721 -11.602 2.383   1.00 10.48  ? 226 ARG A O   1 
ATOM   1835 C  CB  . ARG A 1 226 ? 14.946 -12.650 4.511   1.00 9.94   ? 226 ARG A CB  1 
ATOM   1836 C  CG  . ARG A 1 226 ? 14.420 -12.768 5.947   1.00 9.49   ? 226 ARG A CG  1 
ATOM   1837 C  CD  . ARG A 1 226 ? 14.496 -14.202 6.357   1.00 10.78  ? 226 ARG A CD  1 
ATOM   1838 N  NE  . ARG A 1 226 ? 13.934 -14.427 7.703   1.00 9.74   ? 226 ARG A NE  1 
ATOM   1839 C  CZ  . ARG A 1 226 ? 12.980 -15.306 7.963   1.00 9.27   ? 226 ARG A CZ  1 
ATOM   1840 N  NH1 . ARG A 1 226 ? 12.556 -16.142 7.018   1.00 11.68  ? 226 ARG A NH1 1 
ATOM   1841 N  NH2 . ARG A 1 226 ? 12.480 -15.356 9.164   1.00 9.74   ? 226 ARG A NH2 1 
ATOM   1842 N  N   . LYS A 1 227 ? 14.727 -10.832 1.527   1.00 8.74   ? 227 LYS A N   1 
ATOM   1843 C  CA  . LYS A 1 227 ? 15.230 -10.675 0.176   1.00 10.46  ? 227 LYS A CA  1 
ATOM   1844 C  C   . LYS A 1 227 ? 15.797 -9.278  -0.109  1.00 10.87  ? 227 LYS A C   1 
ATOM   1845 O  O   . LYS A 1 227 ? 16.456 -9.079  -1.132  1.00 11.88  ? 227 LYS A O   1 
ATOM   1846 C  CB  . LYS A 1 227 ? 14.134 -11.006 -0.825  1.00 11.56  ? 227 LYS A CB  1 
ATOM   1847 C  CG  . LYS A 1 227 ? 13.754 -12.473 -0.758  1.00 14.81  ? 227 LYS A CG  1 
ATOM   1848 C  CD  . LYS A 1 227 ? 12.644 -12.795 -1.748  1.00 21.53  ? 227 LYS A CD  1 
ATOM   1849 C  CE  . LYS A 1 227 ? 13.141 -12.943 -3.168  1.00 28.01  ? 227 LYS A CE  1 
ATOM   1850 N  NZ  . LYS A 1 227 ? 12.049 -13.313 -4.084  1.00 33.07  ? 227 LYS A NZ  1 
ATOM   1851 N  N   . LEU A 1 228 ? 15.595 -8.327  0.811   1.00 9.31   ? 228 LEU A N   1 
ATOM   1852 C  CA  . LEU A 1 228 ? 16.265 -7.053  0.698   1.00 8.27   ? 228 LEU A CA  1 
ATOM   1853 C  C   . LEU A 1 228 ? 17.773 -7.236  0.742   1.00 8.20   ? 228 LEU A C   1 
ATOM   1854 O  O   . LEU A 1 228 ? 18.277 -8.287  1.181   1.00 9.45   ? 228 LEU A O   1 
ATOM   1855 C  CB  . LEU A 1 228 ? 15.775 -6.110  1.784   1.00 8.92   ? 228 LEU A CB  1 
ATOM   1856 C  CG  . LEU A 1 228 ? 14.323 -5.671  1.634   1.00 8.11   ? 228 LEU A CG  1 
ATOM   1857 C  CD1 . LEU A 1 228 ? 13.915 -4.984  2.949   1.00 8.62   ? 228 LEU A CD1 1 
ATOM   1858 C  CD2 . LEU A 1 228 ? 14.198 -4.683  0.459   1.00 10.57  ? 228 LEU A CD2 1 
ATOM   1859 N  N   . ASN A 1 229 ? 18.483 -6.182  0.356   1.00 8.93   ? 229 ASN A N   1 
ATOM   1860 C  CA  . ASN A 1 229 ? 19.935 -6.230  0.374   1.00 9.47   ? 229 ASN A CA  1 
ATOM   1861 C  C   . ASN A 1 229 ? 20.492 -5.090  1.228   1.00 8.89   ? 229 ASN A C   1 
ATOM   1862 O  O   . ASN A 1 229 ? 20.039 -3.933  1.109   1.00 10.11  ? 229 ASN A O   1 
ATOM   1863 C  CB  . ASN A 1 229 ? 20.519 -5.998  -1.030  1.00 11.11  ? 229 ASN A CB  1 
ATOM   1864 C  CG  . ASN A 1 229 ? 20.383 -7.126  -2.026  1.00 12.58  ? 229 ASN A CG  1 
ATOM   1865 O  OD1 . ASN A 1 229 ? 20.885 -6.981  -3.149  1.00 13.85  ? 229 ASN A OD1 1 
ATOM   1866 N  ND2 . ASN A 1 229 ? 19.785 -8.231  -1.619  1.00 13.43  ? 229 ASN A ND2 1 
ATOM   1867 N  N   . PHE A 1 230 ? 21.592 -5.371  1.952   1.00 8.27   ? 230 PHE A N   1 
ATOM   1868 C  CA  . PHE A 1 230 ? 22.330 -4.301  2.611   1.00 8.52   ? 230 PHE A CA  1 
ATOM   1869 C  C   . PHE A 1 230 ? 23.148 -3.477  1.622   1.00 9.47   ? 230 PHE A C   1 
ATOM   1870 O  O   . PHE A 1 230 ? 23.396 -2.270  1.838   1.00 10.71  ? 230 PHE A O   1 
ATOM   1871 C  CB  . PHE A 1 230 ? 23.340 -4.896  3.595   1.00 9.31   ? 230 PHE A CB  1 
ATOM   1872 C  CG  . PHE A 1 230 ? 22.801 -5.532  4.866   1.00 9.34   ? 230 PHE A CG  1 
ATOM   1873 C  CD1 . PHE A 1 230 ? 22.104 -4.781  5.799   1.00 10.44  ? 230 PHE A CD1 1 
ATOM   1874 C  CD2 . PHE A 1 230 ? 23.133 -6.832  5.222   1.00 10.17  ? 230 PHE A CD2 1 
ATOM   1875 C  CE1 . PHE A 1 230 ? 21.702 -5.341  7.011   1.00 10.92  ? 230 PHE A CE1 1 
ATOM   1876 C  CE2 . PHE A 1 230 ? 22.735 -7.397  6.424   1.00 9.74   ? 230 PHE A CE2 1 
ATOM   1877 C  CZ  . PHE A 1 230 ? 22.029 -6.643  7.344   1.00 10.04  ? 230 PHE A CZ  1 
ATOM   1878 N  N   . ASN A 1 231 ? 23.643 -4.139  0.575   1.00 9.09   ? 231 ASN A N   1 
ATOM   1879 C  CA  . ASN A 1 231 ? 24.483 -3.476  -0.433  1.00 9.38   ? 231 ASN A CA  1 
ATOM   1880 C  C   . ASN A 1 231 ? 23.659 -2.585  -1.350  1.00 9.78   ? 231 ASN A C   1 
ATOM   1881 O  O   . ASN A 1 231 ? 22.438 -2.695  -1.487  1.00 10.34  ? 231 ASN A O   1 
ATOM   1882 C  CB  . ASN A 1 231 ? 25.148 -4.563  -1.287  1.00 10.07  ? 231 ASN A CB  1 
ATOM   1883 C  CG  . ASN A 1 231 ? 24.074 -5.476  -1.872  1.00 9.20   ? 231 ASN A CG  1 
ATOM   1884 O  OD1 . ASN A 1 231 ? 23.580 -6.379  -1.181  1.00 10.67  ? 231 ASN A OD1 1 
ATOM   1885 N  ND2 . ASN A 1 231 ? 23.677 -5.283  -3.138  1.00 10.96  ? 231 ASN A ND2 1 
ATOM   1886 N  N   . GLY A 1 232 ? 24.412 -1.689  -2.022  1.00 9.96   ? 232 GLY A N   1 
ATOM   1887 C  CA  . GLY A 1 232 ? 23.821 -0.874  -3.071  1.00 10.10  ? 232 GLY A CA  1 
ATOM   1888 C  C   . GLY A 1 232 ? 23.733 -1.653  -4.384  1.00 8.79   ? 232 GLY A C   1 
ATOM   1889 O  O   . GLY A 1 232 ? 24.366 -2.714  -4.565  1.00 10.80  ? 232 GLY A O   1 
ATOM   1890 N  N   . GLU A 1 233 ? 22.966 -1.120  -5.356  1.00 9.29   ? 233 GLU A N   1 
ATOM   1891 C  CA  . GLU A 1 233 ? 22.933 -1.684  -6.702  1.00 9.78   ? 233 GLU A CA  1 
ATOM   1892 C  C   . GLU A 1 233 ? 24.352 -1.770  -7.230  1.00 10.14  ? 233 GLU A C   1 
ATOM   1893 O  O   . GLU A 1 233 ? 25.174 -0.878  -7.064  1.00 9.76   ? 233 GLU A O   1 
ATOM   1894 C  CB  . GLU A 1 233 ? 22.054 -0.776  -7.579  1.00 11.53  ? 233 GLU A CB  1 
ATOM   1895 C  CG  . GLU A 1 233 ? 21.743 -1.306  -8.980  1.00 13.69  ? 233 GLU A CG  1 
ATOM   1896 C  CD  . GLU A 1 233 ? 20.942 -0.331  -9.823  1.00 18.40  ? 233 GLU A CD  1 
ATOM   1897 O  OE1 . GLU A 1 233 ? 20.746 0.814   -9.369  1.00 20.38  ? 233 GLU A OE1 1 
ATOM   1898 O  OE2 . GLU A 1 233 ? 20.577 -0.677  -10.958 1.00 23.94  ? 233 GLU A OE2 1 
ATOM   1899 N  N   . GLY A 1 234 ? 24.615 -2.808  -8.009  1.00 10.90  ? 234 GLY A N   1 
ATOM   1900 C  CA  . GLY A 1 234 ? 25.905 -2.876  -8.678  1.00 10.26  ? 234 GLY A CA  1 
ATOM   1901 C  C   . GLY A 1 234 ? 27.039 -3.290  -7.743  1.00 9.48   ? 234 GLY A C   1 
ATOM   1902 O  O   . GLY A 1 234 ? 28.192 -3.225  -8.156  1.00 11.86  ? 234 GLY A O   1 
ATOM   1903 N  N   . GLU A 1 235 ? 26.691 -3.791  -6.546  1.00 10.35  ? 235 GLU A N   1 
ATOM   1904 C  CA  . GLU A 1 235 ? 27.673 -4.295  -5.576  1.00 10.93  ? 235 GLU A CA  1 
ATOM   1905 C  C   . GLU A 1 235 ? 27.293 -5.726  -5.205  1.00 12.00  ? 235 GLU A C   1 
ATOM   1906 O  O   . GLU A 1 235 ? 26.151 -6.168  -5.437  1.00 11.76  ? 235 GLU A O   1 
ATOM   1907 C  CB  . GLU A 1 235 ? 27.635 -3.467  -4.257  1.00 12.80  ? 235 GLU A CB  1 
ATOM   1908 C  CG  . GLU A 1 235 ? 27.952 -2.007  -4.442  1.00 13.68  ? 235 GLU A CG  1 
ATOM   1909 C  CD  . GLU A 1 235 ? 27.776 -1.197  -3.165  1.00 19.92  ? 235 GLU A CD  1 
ATOM   1910 O  OE1 . GLU A 1 235 ? 28.388 -0.137  -3.079  1.00 30.46  ? 235 GLU A OE1 1 
ATOM   1911 O  OE2 . GLU A 1 235 ? 27.137 -1.661  -2.226  1.00 16.71  ? 235 GLU A OE2 1 
ATOM   1912 N  N   . PRO A 1 236 ? 28.262 -6.494  -4.674  1.00 10.88  ? 236 PRO A N   1 
ATOM   1913 C  CA  . PRO A 1 236 ? 27.963 -7.886  -4.350  1.00 11.26  ? 236 PRO A CA  1 
ATOM   1914 C  C   . PRO A 1 236 ? 26.827 -8.002  -3.354  1.00 9.69   ? 236 PRO A C   1 
ATOM   1915 O  O   . PRO A 1 236 ? 26.648 -7.164  -2.467  1.00 10.49  ? 236 PRO A O   1 
ATOM   1916 C  CB  . PRO A 1 236 ? 29.255 -8.330  -3.660  1.00 15.14  ? 236 PRO A CB  1 
ATOM   1917 C  CG  . PRO A 1 236 ? 30.325 -7.528  -4.437  1.00 16.15  ? 236 PRO A CG  1 
ATOM   1918 C  CD  . PRO A 1 236 ? 29.698 -6.145  -4.555  1.00 14.67  ? 236 PRO A CD  1 
ATOM   1919 N  N   A GLU A 1 237 ? 26.001 -9.037  -3.545  0.50 10.56  ? 237 GLU A N   1 
ATOM   1920 N  N   B GLU A 1 237 ? 26.037 -9.063  -3.524  0.50 10.88  ? 237 GLU A N   1 
ATOM   1921 C  CA  A GLU A 1 237 ? 24.762 -9.118  -2.777  0.50 9.07   ? 237 GLU A CA  1 
ATOM   1922 C  CA  B GLU A 1 237 ? 24.796 -9.185  -2.770  0.50 9.00   ? 237 GLU A CA  1 
ATOM   1923 C  C   A GLU A 1 237 ? 25.042 -9.619  -1.355  0.50 9.36   ? 237 GLU A C   1 
ATOM   1924 C  C   B GLU A 1 237 ? 25.097 -9.615  -1.331  0.50 10.01  ? 237 GLU A C   1 
ATOM   1925 O  O   A GLU A 1 237 ? 25.620 -10.679 -1.146  0.50 11.63  ? 237 GLU A O   1 
ATOM   1926 O  O   B GLU A 1 237 ? 25.756 -10.621 -1.088  0.50 12.13  ? 237 GLU A O   1 
ATOM   1927 C  CB  A GLU A 1 237 ? 23.762 -10.093 -3.423  0.50 12.95  ? 237 GLU A CB  1 
ATOM   1928 C  CB  B GLU A 1 237 ? 23.927 -10.281 -3.411  0.50 13.75  ? 237 GLU A CB  1 
ATOM   1929 C  CG  A GLU A 1 237 ? 22.431 -10.076 -2.675  0.50 14.24  ? 237 GLU A CG  1 
ATOM   1930 C  CG  B GLU A 1 237 ? 22.549 -10.340 -2.758  0.50 17.69  ? 237 GLU A CG  1 
ATOM   1931 C  CD  A GLU A 1 237 ? 21.305 -10.954 -3.213  0.50 17.83  ? 237 GLU A CD  1 
ATOM   1932 C  CD  B GLU A 1 237 ? 21.449 -10.966 -3.608  0.50 18.58  ? 237 GLU A CD  1 
ATOM   1933 O  OE1 A GLU A 1 237 ? 21.494 -12.215 -3.306  0.50 20.49  ? 237 GLU A OE1 1 
ATOM   1934 O  OE1 B GLU A 1 237 ? 21.754 -11.385 -4.727  0.50 22.09  ? 237 GLU A OE1 1 
ATOM   1935 O  OE2 A GLU A 1 237 ? 20.182 -10.389 -3.465  0.50 12.54  ? 237 GLU A OE2 1 
ATOM   1936 O  OE2 B GLU A 1 237 ? 20.263 -11.037 -3.135  0.50 29.54  ? 237 GLU A OE2 1 
ATOM   1937 N  N   . GLU A 1 238 ? 24.546 -8.860  -0.377  1.00 9.57   ? 238 GLU A N   1 
ATOM   1938 C  CA  . GLU A 1 238 ? 24.596 -9.225  1.036   1.00 10.90  ? 238 GLU A CA  1 
ATOM   1939 C  C   . GLU A 1 238 ? 23.150 -9.149  1.524   1.00 9.02   ? 238 GLU A C   1 
ATOM   1940 O  O   . GLU A 1 238 ? 22.584 -8.057  1.643   1.00 10.56  ? 238 GLU A O   1 
ATOM   1941 C  CB  . GLU A 1 238 ? 25.421 -8.170  1.811   1.00 14.69  ? 238 GLU A CB  1 
ATOM   1942 C  CG  . GLU A 1 238 ? 26.877 -7.893  1.447   1.00 17.91  ? 238 GLU A CG  1 
ATOM   1943 C  CD  . GLU A 1 238 ? 27.381 -6.599  2.145   1.00 30.15  ? 238 GLU A CD  1 
ATOM   1944 O  OE1 . GLU A 1 238 ? 27.321 -5.454  1.533   1.00 36.87  ? 238 GLU A OE1 1 
ATOM   1945 O  OE2 . GLU A 1 238 ? 27.756 -6.686  3.324   1.00 38.31  ? 238 GLU A OE2 1 
ATOM   1946 N  N   . LEU A 1 239 ? 22.504 -10.303 1.786   1.00 9.31   ? 239 LEU A N   1 
ATOM   1947 C  CA  . LEU A 1 239 ? 21.093 -10.249 2.158   1.00 8.29   ? 239 LEU A CA  1 
ATOM   1948 C  C   . LEU A 1 239 ? 20.915 -9.480  3.476   1.00 7.93   ? 239 LEU A C   1 
ATOM   1949 O  O   . LEU A 1 239 ? 21.649 -9.651  4.442   1.00 8.80   ? 239 LEU A O   1 
ATOM   1950 C  CB  . LEU A 1 239 ? 20.568 -11.682 2.315   1.00 8.90   ? 239 LEU A CB  1 
ATOM   1951 C  CG  . LEU A 1 239 ? 20.554 -12.489 1.029   1.00 11.28  ? 239 LEU A CG  1 
ATOM   1952 C  CD1 . LEU A 1 239 ? 20.203 -13.902 1.372   1.00 14.94  ? 239 LEU A CD1 1 
ATOM   1953 C  CD2 . LEU A 1 239 ? 19.561 -11.883 0.032   1.00 13.54  ? 239 LEU A CD2 1 
ATOM   1954 N  N   . MET A 1 240 ? 19.849 -8.697  3.513   1.00 7.72   ? 240 MET A N   1 
ATOM   1955 C  CA  . MET A 1 240 ? 19.553 -7.871  4.681   1.00 8.14   ? 240 MET A CA  1 
ATOM   1956 C  C   . MET A 1 240 ? 18.763 -8.758  5.657   1.00 7.01   ? 240 MET A C   1 
ATOM   1957 O  O   . MET A 1 240 ? 17.551 -8.968  5.548   1.00 7.46   ? 240 MET A O   1 
ATOM   1958 C  CB  . MET A 1 240 ? 18.700 -6.676  4.242   1.00 8.53   ? 240 MET A CB  1 
ATOM   1959 C  CG  . MET A 1 240 ? 18.395 -5.706  5.449   1.00 8.41   ? 240 MET A CG  1 
ATOM   1960 S  SD  . MET A 1 240 ? 17.462 -4.288  4.944   1.00 9.41   ? 240 MET A SD  1 
ATOM   1961 C  CE  . MET A 1 240 ? 18.736 -3.277  4.185   1.00 9.87   ? 240 MET A CE  1 
ATOM   1962 N  N   . VAL A 1 241 ? 19.515 -9.340  6.598   1.00 6.46   ? 241 VAL A N   1 
ATOM   1963 C  CA  . VAL A 1 241 ? 18.952 -10.212 7.643   1.00 7.54   ? 241 VAL A CA  1 
ATOM   1964 C  C   . VAL A 1 241 ? 19.738 -9.942  8.920   1.00 7.68   ? 241 VAL A C   1 
ATOM   1965 O  O   . VAL A 1 241 ? 20.914 -9.527  8.843   1.00 7.72   ? 241 VAL A O   1 
ATOM   1966 C  CB  . VAL A 1 241 ? 19.080 -11.736 7.305   1.00 8.24   ? 241 VAL A CB  1 
ATOM   1967 C  CG1 . VAL A 1 241 ? 18.193 -12.093 6.081   1.00 10.65  ? 241 VAL A CG1 1 
ATOM   1968 C  CG2 . VAL A 1 241 ? 20.542 -12.167 7.089   1.00 9.16   ? 241 VAL A CG2 1 
ATOM   1969 N  N   . ASP A 1 242 ? 19.087 -10.212 10.086  1.00 6.75   ? 242 ASP A N   1 
ATOM   1970 C  CA  . ASP A 1 242 ? 19.828 -10.070 11.326  1.00 6.81   ? 242 ASP A CA  1 
ATOM   1971 C  C   . ASP A 1 242 ? 20.312 -8.658  11.593  1.00 6.72   ? 242 ASP A C   1 
ATOM   1972 O  O   . ASP A 1 242 ? 21.429 -8.424  12.045  1.00 8.39   ? 242 ASP A O   1 
ATOM   1973 C  CB  . ASP A 1 242 ? 20.883 -11.130 11.558  1.00 7.50   ? 242 ASP A CB  1 
ATOM   1974 C  CG  . ASP A 1 242 ? 20.283 -12.518 11.662  1.00 7.39   ? 242 ASP A CG  1 
ATOM   1975 O  OD1 . ASP A 1 242 ? 19.201 -12.678 12.304  1.00 7.63   ? 242 ASP A OD1 1 
ATOM   1976 O  OD2 . ASP A 1 242 ? 20.856 -13.445 11.019  1.00 9.64   ? 242 ASP A OD2 1 
ATOM   1977 N  N   . ASN A 1 243 ? 19.404 -7.705  11.325  1.00 6.56   ? 243 ASN A N   1 
ATOM   1978 C  CA  . ASN A 1 243 ? 19.714 -6.283  11.564  1.00 6.81   ? 243 ASN A CA  1 
ATOM   1979 C  C   . ASN A 1 243 ? 19.144 -5.833  12.901  1.00 6.30   ? 243 ASN A C   1 
ATOM   1980 O  O   . ASN A 1 243 ? 18.437 -4.828  12.990  1.00 7.05   ? 243 ASN A O   1 
ATOM   1981 C  CB  . ASN A 1 243 ? 19.186 -5.434  10.390  1.00 7.44   ? 243 ASN A CB  1 
ATOM   1982 C  CG  . ASN A 1 243 ? 17.740 -5.673  10.075  1.00 7.04   ? 243 ASN A CG  1 
ATOM   1983 O  OD1 . ASN A 1 243 ? 17.037 -6.452  10.717  1.00 7.64   ? 243 ASN A OD1 1 
ATOM   1984 N  ND2 . ASN A 1 243 ? 17.284 -4.979  9.047   1.00 8.96   ? 243 ASN A ND2 1 
ATOM   1985 N  N   . TRP A 1 244 ? 19.363 -6.604  13.964  1.00 5.21   ? 244 TRP A N   1 
ATOM   1986 C  CA  . TRP A 1 244 ? 18.914 -6.343  15.323  1.00 5.71   ? 244 TRP A CA  1 
ATOM   1987 C  C   . TRP A 1 244 ? 20.111 -6.232  16.252  1.00 5.96   ? 244 TRP A C   1 
ATOM   1988 O  O   . TRP A 1 244 ? 21.115 -6.923  16.090  1.00 7.02   ? 244 TRP A O   1 
ATOM   1989 C  CB  . TRP A 1 244 ? 17.955 -7.460  15.818  1.00 5.95   ? 244 TRP A CB  1 
ATOM   1990 C  CG  . TRP A 1 244 ? 18.454 -8.867  15.585  1.00 6.01   ? 244 TRP A CG  1 
ATOM   1991 C  CD1 . TRP A 1 244 ? 18.344 -9.596  14.425  1.00 6.82   ? 244 TRP A CD1 1 
ATOM   1992 C  CD2 . TRP A 1 244 ? 19.006 -9.738  16.578  1.00 6.25   ? 244 TRP A CD2 1 
ATOM   1993 N  NE1 . TRP A 1 244 ? 18.836 -10.866 14.621  1.00 7.13   ? 244 TRP A NE1 1 
ATOM   1994 C  CE2 . TRP A 1 244 ? 19.250 -10.983 15.928  1.00 7.26   ? 244 TRP A CE2 1 
ATOM   1995 C  CE3 . TRP A 1 244 ? 19.297 -9.584  17.962  1.00 7.61   ? 244 TRP A CE3 1 
ATOM   1996 C  CZ2 . TRP A 1 244 ? 19.795 -12.084 16.603  1.00 8.94   ? 244 TRP A CZ2 1 
ATOM   1997 C  CZ3 . TRP A 1 244 ? 19.823 -10.674 18.624  1.00 7.81   ? 244 TRP A CZ3 1 
ATOM   1998 C  CH2 . TRP A 1 244 ? 20.078 -11.891 17.941  1.00 8.48   ? 244 TRP A CH2 1 
ATOM   1999 N  N   . ARG A 1 245 ? 19.968 -5.344  17.217  1.00 6.31   ? 245 ARG A N   1 
ATOM   2000 C  CA  . ARG A 1 245 ? 20.917 -5.260  18.324  1.00 6.28   ? 245 ARG A CA  1 
ATOM   2001 C  C   . ARG A 1 245 ? 20.464 -6.203  19.433  1.00 6.13   ? 245 ARG A C   1 
ATOM   2002 O  O   . ARG A 1 245 ? 19.279 -6.202  19.788  1.00 7.61   ? 245 ARG A O   1 
ATOM   2003 C  CB  . ARG A 1 245 ? 20.969 -3.817  18.841  1.00 6.62   ? 245 ARG A CB  1 
ATOM   2004 C  CG  . ARG A 1 245 ? 22.141 -3.624  19.800  1.00 6.74   ? 245 ARG A CG  1 
ATOM   2005 C  CD  . ARG A 1 245 ? 22.059 -2.255  20.437  1.00 7.49   ? 245 ARG A CD  1 
ATOM   2006 N  NE  . ARG A 1 245 ? 23.303 -1.960  21.175  1.00 7.84   ? 245 ARG A NE  1 
ATOM   2007 C  CZ  . ARG A 1 245 ? 23.488 -0.948  22.035  1.00 7.37   ? 245 ARG A CZ  1 
ATOM   2008 N  NH1 . ARG A 1 245 ? 22.472 -0.160  22.398  1.00 8.51   ? 245 ARG A NH1 1 
ATOM   2009 N  NH2 . ARG A 1 245 ? 24.744 -0.715  22.494  1.00 8.94   ? 245 ARG A NH2 1 
ATOM   2010 N  N   . PRO A 1 246 ? 21.368 -6.999  20.051  1.00 7.26   ? 246 PRO A N   1 
ATOM   2011 C  CA  . PRO A 1 246 ? 20.962 -7.826  21.191  1.00 7.16   ? 246 PRO A CA  1 
ATOM   2012 C  C   . PRO A 1 246 ? 20.598 -7.007  22.436  1.00 7.60   ? 246 PRO A C   1 
ATOM   2013 O  O   . PRO A 1 246 ? 20.946 -5.825  22.551  1.00 8.59   ? 246 PRO A O   1 
ATOM   2014 C  CB  . PRO A 1 246 ? 22.192 -8.689  21.483  1.00 11.39  ? 246 PRO A CB  1 
ATOM   2015 C  CG  . PRO A 1 246 ? 23.060 -8.604  20.257  1.00 14.85  ? 246 PRO A CG  1 
ATOM   2016 C  CD  . PRO A 1 246 ? 22.789 -7.223  19.682  1.00 9.88   ? 246 PRO A CD  1 
ATOM   2017 N  N   . ALA A 1 247 ? 19.964 -7.684  23.397  1.00 7.80   ? 247 ALA A N   1 
ATOM   2018 C  CA  . ALA A 1 247 ? 19.580 -7.068  24.658  1.00 7.87   ? 247 ALA A CA  1 
ATOM   2019 C  C   . ALA A 1 247 ? 20.829 -6.541  25.345  1.00 7.79   ? 247 ALA A C   1 
ATOM   2020 O  O   . ALA A 1 247 ? 21.897 -7.229  25.379  1.00 9.75   ? 247 ALA A O   1 
ATOM   2021 C  CB  . ALA A 1 247 ? 18.813 -8.075  25.521  1.00 9.95   ? 247 ALA A CB  1 
ATOM   2022 N  N   . GLN A 1 248 ? 20.676 -5.377  26.000  1.00 7.16   ? 248 GLN A N   1 
ATOM   2023 C  CA  . GLN A 1 248 ? 21.729 -4.681  26.695  1.00 8.23   ? 248 GLN A CA  1 
ATOM   2024 C  C   . GLN A 1 248 ? 21.418 -4.716  28.180  1.00 8.52   ? 248 GLN A C   1 
ATOM   2025 O  O   . GLN A 1 248 ? 20.274 -4.923  28.571  1.00 9.53   ? 248 GLN A O   1 
ATOM   2026 C  CB  . GLN A 1 248 ? 21.827 -3.235  26.220  1.00 9.38   ? 248 GLN A CB  1 
ATOM   2027 C  CG  . GLN A 1 248 ? 22.121 -3.162  24.692  1.00 9.58   ? 248 GLN A CG  1 
ATOM   2028 C  CD  . GLN A 1 248 ? 23.435 -3.836  24.339  1.00 10.50  ? 248 GLN A CD  1 
ATOM   2029 O  OE1 . GLN A 1 248 ? 24.480 -3.536  24.942  1.00 13.07  ? 248 GLN A OE1 1 
ATOM   2030 N  NE2 . GLN A 1 248 ? 23.431 -4.747  23.361  1.00 9.76   ? 248 GLN A NE2 1 
ATOM   2031 N  N   . PRO A 1 249 ? 22.427 -4.439  29.033  1.00 10.38  ? 249 PRO A N   1 
ATOM   2032 C  CA  . PRO A 1 249 ? 22.210 -4.480  30.459  1.00 11.06  ? 249 PRO A CA  1 
ATOM   2033 C  C   . PRO A 1 249 ? 21.153 -3.486  30.925  1.00 10.10  ? 249 PRO A C   1 
ATOM   2034 O  O   . PRO A 1 249 ? 21.169 -2.289  30.566  1.00 10.47  ? 249 PRO A O   1 
ATOM   2035 C  CB  . PRO A 1 249 ? 23.599 -4.081  31.011  1.00 15.12  ? 249 PRO A CB  1 
ATOM   2036 C  CG  . PRO A 1 249 ? 24.577 -4.512  29.984  1.00 14.50  ? 249 PRO A CG  1 
ATOM   2037 C  CD  . PRO A 1 249 ? 23.833 -4.195  28.685  1.00 13.24  ? 249 PRO A CD  1 
ATOM   2038 N  N   . LEU A 1 250 ? 20.258 -3.958  31.790  1.00 10.73  ? 250 LEU A N   1 
ATOM   2039 C  CA  . LEU A 1 250 ? 19.188 -3.091  32.254  1.00 9.86   ? 250 LEU A CA  1 
ATOM   2040 C  C   . LEU A 1 250 ? 19.732 -2.026  33.205  1.00 10.30  ? 250 LEU A C   1 
ATOM   2041 O  O   . LEU A 1 250 ? 19.191 -0.912  33.301  1.00 10.79  ? 250 LEU A O   1 
ATOM   2042 C  CB  . LEU A 1 250 ? 18.153 -3.945  33.002  1.00 12.18  ? 250 LEU A CB  1 
ATOM   2043 C  CG  . LEU A 1 250 ? 16.862 -3.244  33.408  1.00 13.15  ? 250 LEU A CG  1 
ATOM   2044 C  CD1 . LEU A 1 250 ? 16.138 -2.674  32.185  1.00 11.83  ? 250 LEU A CD1 1 
ATOM   2045 C  CD2 . LEU A 1 250 ? 15.988 -4.242  34.216  1.00 15.35  ? 250 LEU A CD2 1 
ATOM   2046 N  N   . LYS A 1 251 ? 20.808 -2.342  33.907  1.00 11.98  ? 251 LYS A N   1 
ATOM   2047 C  CA  . LYS A 1 251 ? 21.445 -1.378  34.827  1.00 11.45  ? 251 LYS A CA  1 
ATOM   2048 C  C   . LYS A 1 251 ? 20.418 -0.835  35.823  1.00 13.50  ? 251 LYS A C   1 
ATOM   2049 O  O   . LYS A 1 251 ? 19.668 -1.632  36.366  1.00 17.52  ? 251 LYS A O   1 
ATOM   2050 C  CB  . LYS A 1 251 ? 22.243 -0.311  34.066  1.00 12.37  ? 251 LYS A CB  1 
ATOM   2051 C  CG  . LYS A 1 251 ? 23.365 -0.984  33.302  1.00 17.64  ? 251 LYS A CG  1 
ATOM   2052 C  CD  . LYS A 1 251 ? 24.319 -0.049  32.699  1.00 20.47  ? 251 LYS A CD  1 
ATOM   2053 C  CE  . LYS A 1 251 ? 25.583 -0.757  32.271  1.00 21.39  ? 251 LYS A CE  1 
ATOM   2054 N  NZ  . LYS A 1 251 ? 26.332 0.143   31.347  1.00 23.83  ? 251 LYS A NZ  1 
ATOM   2055 N  N   . ASN A 1 252 ? 20.412 0.472   36.070  1.00 12.24  ? 252 ASN A N   1 
ATOM   2056 C  CA  . ASN A 1 252 ? 19.550 0.966   37.099  1.00 15.35  ? 252 ASN A CA  1 
ATOM   2057 C  C   . ASN A 1 252 ? 18.272 1.448   36.454  1.00 15.84  ? 252 ASN A C   1 
ATOM   2058 O  O   . ASN A 1 252 ? 18.033 2.690   36.439  1.00 20.17  ? 252 ASN A O   1 
ATOM   2059 C  CB  . ASN A 1 252 ? 20.253 2.066   37.902  1.00 17.88  ? 252 ASN A CB  1 
ATOM   2060 C  CG  . ASN A 1 252 ? 19.726 2.164   39.321  1.00 22.16  ? 252 ASN A CG  1 
ATOM   2061 O  OD1 . ASN A 1 252 ? 18.606 1.746   39.574  1.00 28.79  ? 252 ASN A OD1 1 
ATOM   2062 N  ND2 . ASN A 1 252 ? 20.576 2.528   40.285  1.00 36.17  ? 252 ASN A ND2 1 
ATOM   2063 N  N   . ARG A 1 253 ? 17.484 0.447   35.942  1.00 11.87  ? 253 ARG A N   1 
ATOM   2064 C  CA  . ARG A 1 253 ? 16.199 0.823   35.380  1.00 11.67  ? 253 ARG A CA  1 
ATOM   2065 C  C   . ARG A 1 253 ? 15.130 -0.150  35.824  1.00 12.50  ? 253 ARG A C   1 
ATOM   2066 O  O   . ARG A 1 253 ? 15.419 -1.314  36.054  1.00 16.04  ? 253 ARG A O   1 
ATOM   2067 C  CB  . ARG A 1 253 ? 16.260 0.843   33.843  1.00 10.07  ? 253 ARG A CB  1 
ATOM   2068 C  CG  . ARG A 1 253 ? 17.116 2.008   33.349  1.00 9.81   ? 253 ARG A CG  1 
ATOM   2069 C  CD  . ARG A 1 253 ? 17.200 1.961   31.831  1.00 9.86   ? 253 ARG A CD  1 
ATOM   2070 N  NE  . ARG A 1 253 ? 18.060 0.848   31.387  1.00 8.84   ? 253 ARG A NE  1 
ATOM   2071 C  CZ  . ARG A 1 253 ? 18.310 0.574   30.109  1.00 6.73   ? 253 ARG A CZ  1 
ATOM   2072 N  NH1 . ARG A 1 253 ? 17.719 1.273   29.135  1.00 7.19   ? 253 ARG A NH1 1 
ATOM   2073 N  NH2 . ARG A 1 253 ? 19.146 -0.398  29.778  1.00 7.22   ? 253 ARG A NH2 1 
ATOM   2074 N  N   A GLN A 1 254 ? 13.895 0.338   35.990  0.50 13.91  ? 254 GLN A N   1 
ATOM   2075 N  N   B GLN A 1 254 ? 13.906 0.346   35.876  0.50 12.17  ? 254 GLN A N   1 
ATOM   2076 C  CA  A GLN A 1 254 ? 12.710 -0.490  36.215  0.50 14.94  ? 254 GLN A CA  1 
ATOM   2077 C  CA  B GLN A 1 254 ? 12.758 -0.502  36.142  0.50 13.19  ? 254 GLN A CA  1 
ATOM   2078 C  C   A GLN A 1 254 ? 11.822 -0.444  34.978  0.50 14.21  ? 254 GLN A C   1 
ATOM   2079 C  C   B GLN A 1 254 ? 11.848 -0.446  34.935  0.50 13.21  ? 254 GLN A C   1 
ATOM   2080 O  O   A GLN A 1 254 ? 11.515 0.635   34.458  0.50 18.14  ? 254 GLN A O   1 
ATOM   2081 O  O   B GLN A 1 254 ? 11.598 0.630   34.381  0.50 16.19  ? 254 GLN A O   1 
ATOM   2082 C  CB  A GLN A 1 254 ? 11.887 0.063   37.388  0.50 22.80  ? 254 GLN A CB  1 
ATOM   2083 C  CB  B GLN A 1 254 ? 11.954 0.056   37.313  0.50 14.87  ? 254 GLN A CB  1 
ATOM   2084 C  CG  A GLN A 1 254 ? 12.040 1.570   37.555  0.50 28.75  ? 254 GLN A CG  1 
ATOM   2085 C  CG  B GLN A 1 254 ? 12.604 -0.221  38.662  0.50 17.28  ? 254 GLN A CG  1 
ATOM   2086 C  CD  A GLN A 1 254 ? 11.588 2.119   38.887  0.50 25.63  ? 254 GLN A CD  1 
ATOM   2087 C  CD  B GLN A 1 254 ? 11.535 -0.704  39.629  0.50 21.53  ? 254 GLN A CD  1 
ATOM   2088 O  OE1 A GLN A 1 254 ? 11.423 3.335   39.060  0.50 17.37  ? 254 GLN A OE1 1 
ATOM   2089 O  OE1 B GLN A 1 254 ? 10.361 -0.868  39.269  0.50 33.70  ? 254 GLN A OE1 1 
ATOM   2090 N  NE2 A GLN A 1 254 ? 11.378 1.207   39.841  0.50 22.73  ? 254 GLN A NE2 1 
ATOM   2091 N  NE2 B GLN A 1 254 ? 11.926 -1.007  40.850  0.50 20.58  ? 254 GLN A NE2 1 
ATOM   2092 N  N   . ILE A 1 255 ? 11.413 -1.617  34.483  1.00 10.60  ? 255 ILE A N   1 
ATOM   2093 C  CA  . ILE A 1 255 ? 10.403 -1.681  33.436  1.00 10.63  ? 255 ILE A CA  1 
ATOM   2094 C  C   . ILE A 1 255 ? 9.044  -1.663  34.108  1.00 10.96  ? 255 ILE A C   1 
ATOM   2095 O  O   . ILE A 1 255 ? 8.798  -2.425  35.044  1.00 11.62  ? 255 ILE A O   1 
ATOM   2096 C  CB  . ILE A 1 255 ? 10.592 -2.952  32.590  1.00 10.31  ? 255 ILE A CB  1 
ATOM   2097 C  CG1 . ILE A 1 255 ? 12.042 -2.976  32.032  1.00 12.19  ? 255 ILE A CG1 1 
ATOM   2098 C  CG2 . ILE A 1 255 ? 9.515  -3.001  31.485  1.00 12.41  ? 255 ILE A CG2 1 
ATOM   2099 C  CD1 . ILE A 1 255 ? 12.352 -4.230  31.183  1.00 15.44  ? 255 ILE A CD1 1 
ATOM   2100 N  N   . LYS A 1 256 ? 8.150  -0.820  33.629  1.00 9.58   ? 256 LYS A N   1 
ATOM   2101 C  CA  . LYS A 1 256 ? 6.800  -0.699  34.155  1.00 9.46   ? 256 LYS A CA  1 
ATOM   2102 C  C   . LYS A 1 256 ? 5.826  -1.350  33.182  1.00 8.70   ? 256 LYS A C   1 
ATOM   2103 O  O   . LYS A 1 256 ? 5.997  -1.243  31.970  1.00 11.08  ? 256 LYS A O   1 
ATOM   2104 C  CB  . LYS A 1 256 ? 6.471  0.782   34.441  1.00 12.44  ? 256 LYS A CB  1 
ATOM   2105 C  CG  . LYS A 1 256 ? 7.421  1.412   35.489  1.00 16.49  ? 256 LYS A CG  1 
ATOM   2106 N  N   . ALA A 1 257 ? 4.799  -1.960  33.734  1.00 10.06  ? 257 ALA A N   1 
ATOM   2107 C  CA  . ALA A 1 257 ? 3.700  -2.551  32.976  1.00 9.90   ? 257 ALA A CA  1 
ATOM   2108 C  C   . ALA A 1 257 ? 2.424  -1.742  33.120  1.00 9.11   ? 257 ALA A C   1 
ATOM   2109 O  O   . ALA A 1 257 ? 2.108  -1.241  34.227  1.00 11.23  ? 257 ALA A O   1 
ATOM   2110 C  CB  . ALA A 1 257 ? 3.444  -3.981  33.385  1.00 11.58  ? 257 ALA A CB  1 
ATOM   2111 N  N   . SER A 1 258 ? 1.687  -1.603  32.017  1.00 8.99   ? 258 SER A N   1 
ATOM   2112 C  CA  . SER A 1 258 ? 0.432  -0.859  32.027  1.00 11.15  ? 258 SER A CA  1 
ATOM   2113 C  C   . SER A 1 258 ? -0.734 -1.744  32.469  1.00 11.16  ? 258 SER A C   1 
ATOM   2114 O  O   . SER A 1 258 ? -1.874 -1.224  32.625  1.00 17.16  ? 258 SER A O   1 
ATOM   2115 C  CB  . SER A 1 258 ? 0.087  -0.320  30.671  1.00 11.66  ? 258 SER A CB  1 
ATOM   2116 O  OG  . SER A 1 258 ? -0.314 -1.384  29.791  1.00 10.38  ? 258 SER A OG  1 
ATOM   2117 N  N   . PHE A 1 259 ? -0.440 -3.025  32.737  1.00 12.44  ? 259 PHE A N   1 
ATOM   2118 C  CA  . PHE A 1 259 ? -1.442 -4.070  32.930  1.00 15.21  ? 259 PHE A CA  1 
ATOM   2119 C  C   . PHE A 1 259 ? -1.101 -5.004  34.109  1.00 19.28  ? 259 PHE A C   1 
ATOM   2120 O  O   . PHE A 1 259 ? -0.017 -4.840  34.709  1.00 20.77  ? 259 PHE A O   1 
ATOM   2121 C  CB  . PHE A 1 259 ? -1.667 -4.887  31.637  1.00 14.44  ? 259 PHE A CB  1 
ATOM   2122 C  CG  . PHE A 1 259 ? -0.398 -5.577  31.184  1.00 13.51  ? 259 PHE A CG  1 
ATOM   2123 C  CD1 . PHE A 1 259 ? 0.572  -4.923  30.449  1.00 11.79  ? 259 PHE A CD1 1 
ATOM   2124 C  CD2 . PHE A 1 259 ? -0.193 -6.918  31.521  1.00 17.56  ? 259 PHE A CD2 1 
ATOM   2125 C  CE1 . PHE A 1 259 ? 1.748  -5.564  30.108  1.00 14.61  ? 259 PHE A CE1 1 
ATOM   2126 C  CE2 . PHE A 1 259 ? 0.983  -7.559  31.156  1.00 20.23  ? 259 PHE A CE2 1 
ATOM   2127 C  CZ  . PHE A 1 259 ? 1.962  -6.872  30.468  1.00 21.59  ? 259 PHE A CZ  1 
ATOM   2128 N  N   . LYS A 1 260 ? -2.050 -5.905  34.436  1.00 25.82  ? 260 LYS A N   1 
ATOM   2129 C  CA  . LYS A 1 260 ? -2.001 -7.008  35.455  1.00 38.09  ? 260 LYS A CA  1 
ATOM   2130 C  C   . LYS A 1 260 ? -2.195 -6.561  36.918  1.00 48.38  ? 260 LYS A C   1 
ATOM   2131 O  O   . LYS A 1 260 ? -1.435 -6.987  37.757  1.00 64.75  ? 260 LYS A O   1 
ATOM   2132 C  CB  . LYS A 1 260 ? -0.770 -7.906  35.275  1.00 42.84  ? 260 LYS A CB  1 
ATOM   2133 C  CG  . LYS A 1 260 ? -0.918 -9.013  34.240  1.00 54.73  ? 260 LYS A CG  1 
ATOM   2134 O  OXT . LYS A 1 260 ? -3.149 -5.838  37.205  1.00 57.23  ? 260 LYS A OXT 1 
HETATM 2135 ZN ZN  . ZN  B 2 .   ? 14.309 0.171   15.449  1.00 6.01   ? 301 ZN  A ZN  1 
HETATM 2136 S  S   . DMS C 3 .   ? 22.425 -9.777  14.956  1.00 17.11  ? 302 DMS A S   1 
HETATM 2137 O  O   . DMS C 3 .   ? 23.013 -11.091 14.522  1.00 22.91  ? 302 DMS A O   1 
HETATM 2138 C  C1  . DMS C 3 .   ? 22.682 -9.688  16.710  1.00 15.20  ? 302 DMS A C1  1 
HETATM 2139 C  C2  . DMS C 3 .   ? 23.637 -8.568  14.557  1.00 20.75  ? 302 DMS A C2  1 
HETATM 2140 S  S   . DMS D 3 .   ? 12.831 -19.550 8.430   1.00 14.39  ? 303 DMS A S   1 
HETATM 2141 O  O   . DMS D 3 .   ? 13.218 -19.968 9.919   1.00 13.20  ? 303 DMS A O   1 
HETATM 2142 C  C1  . DMS D 3 .   ? 14.307 -19.693 7.421   1.00 16.72  ? 303 DMS A C1  1 
HETATM 2143 C  C2  . DMS D 3 .   ? 11.945 -20.908 7.786   1.00 16.77  ? 303 DMS A C2  1 
HETATM 2144 F  F20 . V14 E 4 .   ? 14.977 5.521   15.854  1.00 15.61  ? 304 V14 A F20 1 
HETATM 2145 C  C5  . V14 E 4 .   ? 15.714 4.798   14.950  1.00 12.61  ? 304 V14 A C5  1 
HETATM 2146 C  C4  . V14 E 4 .   ? 15.952 3.475   15.290  1.00 8.26   ? 304 V14 A C4  1 
HETATM 2147 S  S7  . V14 E 4 .   ? 15.300 2.752   16.775  1.00 6.96   ? 304 V14 A S7  1 
HETATM 2148 O  O9  . V14 E 4 .   ? 13.922 3.140   16.716  1.00 7.15   ? 304 V14 A O9  1 
HETATM 2149 N  N10 . V14 E 4 .   ? 15.446 1.204   16.610  1.00 7.16   ? 304 V14 A N10 1 
HETATM 2150 O  O8  . V14 E 4 .   ? 16.073 3.263   17.854  1.00 7.33   ? 304 V14 A O8  1 
HETATM 2151 C  C3  . V14 E 4 .   ? 16.666 2.740   14.315  1.00 8.45   ? 304 V14 A C3  1 
HETATM 2152 F  F12 . V14 E 4 .   ? 17.002 1.431   14.421  1.00 11.77  ? 304 V14 A F12 1 
HETATM 2153 C  C2  . V14 E 4 .   ? 17.192 3.282   13.233  1.00 11.85  ? 304 V14 A C2  1 
HETATM 2154 F  F13 . V14 E 4 .   ? 17.919 2.520   12.365  1.00 13.44  ? 304 V14 A F13 1 
HETATM 2155 C  C6  . V14 E 4 .   ? 16.135 5.342   13.750  1.00 13.44  ? 304 V14 A C6  1 
HETATM 2156 C  C1  . V14 E 4 .   ? 16.958 4.602   12.882  1.00 13.68  ? 304 V14 A C1  1 
HETATM 2157 S  S11 . V14 E 4 .   ? 17.802 5.203   11.444  1.00 16.58  ? 304 V14 A S11 1 
HETATM 2158 O  O16 . V14 E 4 .   ? 17.477 6.627   11.237  1.00 21.60  ? 304 V14 A O16 1 
HETATM 2159 O  O17 . V14 E 4 .   ? 17.489 4.254   10.337  1.00 17.16  ? 304 V14 A O17 1 
HETATM 2160 C  C15 . V14 E 4 .   ? 19.594 5.055   11.665  1.00 19.32  ? 304 V14 A C15 1 
HETATM 2161 C  C18 . V14 E 4 .   ? 20.260 6.038   12.614  1.00 22.17  ? 304 V14 A C18 1 
HETATM 2162 O  O21 . V14 E 4 .   ? 20.112 5.743   14.023  1.00 25.01  ? 304 V14 A O21 1 
HETATM 2163 N  N19 . V14 E 4 .   ? 15.727 6.655   13.435  1.00 15.43  ? 304 V14 A N19 1 
HETATM 2164 C  C14 . V14 E 4 .   ? 15.503 7.779   14.350  1.00 14.36  ? 304 V14 A C14 1 
HETATM 2165 C  C28 . V14 E 4 .   ? 16.898 7.966   14.988  1.00 19.96  ? 304 V14 A C28 1 
HETATM 2166 C  C27 . V14 E 4 .   ? 17.942 8.774   14.147  1.00 19.08  ? 304 V14 A C27 1 
HETATM 2167 C  C26 . V14 E 4 .   ? 18.212 10.273  14.471  1.00 21.53  ? 304 V14 A C26 1 
HETATM 2168 C  C25 . V14 E 4 .   ? 17.052 11.283  14.230  1.00 22.90  ? 304 V14 A C25 1 
HETATM 2169 C  C24 . V14 E 4 .   ? 15.793 11.010  15.056  1.00 19.61  ? 304 V14 A C24 1 
HETATM 2170 C  C23 . V14 E 4 .   ? 14.602 10.313  14.346  1.00 20.05  ? 304 V14 A C23 1 
HETATM 2171 C  C22 . V14 E 4 .   ? 14.900 8.979   13.579  1.00 16.99  ? 304 V14 A C22 1 
HETATM 2172 O  O   . HOH F 5 .   ? 3.494  20.933  6.225   1.00 10.93  ? 401 HOH A O   1 
HETATM 2173 O  O   . HOH F 5 .   ? 10.537 -3.964  38.293  1.00 35.50  ? 402 HOH A O   1 
HETATM 2174 O  O   . HOH F 5 .   ? 10.113 -13.262 33.761  1.00 28.58  ? 403 HOH A O   1 
HETATM 2175 O  O   . HOH F 5 .   ? 22.565 -13.367 14.349  1.00 35.06  ? 404 HOH A O   1 
HETATM 2176 O  O   . HOH F 5 .   ? 17.854 13.558  9.018   1.00 31.11  ? 405 HOH A O   1 
HETATM 2177 O  O   . HOH F 5 .   ? 29.971 -9.846  9.097   1.00 40.32  ? 406 HOH A O   1 
HETATM 2178 O  O   . HOH F 5 .   ? 29.702 1.499   -4.259  1.00 25.92  ? 407 HOH A O   1 
HETATM 2179 O  O   . HOH F 5 .   ? 0.089  -5.493  -1.739  1.00 40.01  ? 408 HOH A O   1 
HETATM 2180 O  O   . HOH F 5 .   ? -5.858 -10.850 20.178  1.00 43.20  ? 409 HOH A O   1 
HETATM 2181 O  O   . HOH F 5 .   ? 5.785  -8.495  37.556  1.00 27.00  ? 410 HOH A O   1 
HETATM 2182 O  O   . HOH F 5 .   ? 7.025  -7.018  -5.114  1.00 27.16  ? 411 HOH A O   1 
HETATM 2183 O  O   . HOH F 5 .   ? 2.198  19.500  18.849  1.00 23.12  ? 412 HOH A O   1 
HETATM 2184 O  O   . HOH F 5 .   ? 25.594 -0.710  29.095  1.00 24.99  ? 413 HOH A O   1 
HETATM 2185 O  O   . HOH F 5 .   ? -0.486 -12.216 18.772  1.00 31.18  ? 414 HOH A O   1 
HETATM 2186 O  O   . HOH F 5 .   ? -1.355 21.742  12.173  1.00 30.90  ? 415 HOH A O   1 
HETATM 2187 O  O   . HOH F 5 .   ? -1.679 -13.132 16.227  1.00 30.82  ? 416 HOH A O   1 
HETATM 2188 O  O   . HOH F 5 .   ? -4.516 11.461  13.566  1.00 27.21  ? 417 HOH A O   1 
HETATM 2189 O  O   . HOH F 5 .   ? -2.938 -1.530  29.530  1.00 26.43  ? 418 HOH A O   1 
HETATM 2190 O  O   . HOH F 5 .   ? 20.795 2.887   34.498  1.00 24.63  ? 419 HOH A O   1 
HETATM 2191 O  O   . HOH F 5 .   ? 22.678 3.706   36.003  1.00 42.82  ? 420 HOH A O   1 
HETATM 2192 O  O   . HOH F 5 .   ? 14.719 -2.776  -6.373  1.00 21.73  ? 421 HOH A O   1 
HETATM 2193 O  O   . HOH F 5 .   ? 4.568  -20.179 0.179   1.00 29.49  ? 422 HOH A O   1 
HETATM 2194 O  O   . HOH F 5 .   ? 8.771  14.355  29.273  1.00 24.54  ? 423 HOH A O   1 
HETATM 2195 O  O   . HOH F 5 .   ? 6.440  -16.857 18.809  1.00 27.78  ? 424 HOH A O   1 
HETATM 2196 O  O   . HOH F 5 .   ? 5.814  21.475  13.414  1.00 25.41  ? 425 HOH A O   1 
HETATM 2197 O  O   . HOH F 5 .   ? 30.670 -3.922  -7.607  1.00 18.57  ? 426 HOH A O   1 
HETATM 2198 O  O   . HOH F 5 .   ? 12.655 -13.632 36.516  1.00 23.33  ? 427 HOH A O   1 
HETATM 2199 O  O   . HOH F 5 .   ? 16.311 -10.182 32.048  1.00 18.94  ? 428 HOH A O   1 
HETATM 2200 O  O   . HOH F 5 .   ? 0.610  10.456  30.082  1.00 26.45  ? 429 HOH A O   1 
HETATM 2201 O  O   . HOH F 5 .   ? 7.053  -3.213  -6.424  1.00 37.25  ? 430 HOH A O   1 
HETATM 2202 O  O   . HOH F 5 .   ? 14.066 -17.980 19.676  1.00 25.75  ? 431 HOH A O   1 
HETATM 2203 O  O   . HOH F 5 .   ? 10.588 10.537  25.563  1.00 11.63  ? 432 HOH A O   1 
HETATM 2204 O  O   . HOH F 5 .   ? 23.148 9.795   27.845  1.00 20.83  ? 433 HOH A O   1 
HETATM 2205 O  O   . HOH F 5 .   ? -2.974 10.717  20.523  1.00 23.29  ? 434 HOH A O   1 
HETATM 2206 O  O   . HOH F 5 .   ? 24.501 6.739   30.211  1.00 17.15  ? 435 HOH A O   1 
HETATM 2207 O  O   . HOH F 5 .   ? 4.020  -14.459 21.993  1.00 30.60  ? 436 HOH A O   1 
HETATM 2208 O  O   . HOH F 5 .   ? 12.120 7.876   28.981  1.00 22.08  ? 437 HOH A O   1 
HETATM 2209 O  O   . HOH F 5 .   ? 25.016 -1.307  3.704   1.00 24.64  ? 438 HOH A O   1 
HETATM 2210 O  O   . HOH F 5 .   ? 24.167 -7.624  -6.427  1.00 24.88  ? 439 HOH A O   1 
HETATM 2211 O  O   . HOH F 5 .   ? 19.764 -2.192  15.664  1.00 10.30  ? 440 HOH A O   1 
HETATM 2212 O  O   . HOH F 5 .   ? 32.380 -5.252  22.538  1.00 28.70  ? 441 HOH A O   1 
HETATM 2213 O  O   . HOH F 5 .   ? -1.911 1.844   34.672  1.00 39.54  ? 442 HOH A O   1 
HETATM 2214 O  O   . HOH F 5 .   ? 32.669 1.484   16.208  1.00 26.77  ? 443 HOH A O   1 
HETATM 2215 O  O   . HOH F 5 .   ? 22.960 -13.713 9.413   1.00 22.72  ? 444 HOH A O   1 
HETATM 2216 O  O   . HOH F 5 .   ? 16.756 -14.213 1.833   1.00 23.41  ? 445 HOH A O   1 
HETATM 2217 O  O   . HOH F 5 .   ? 25.393 -1.676  26.628  1.00 16.79  ? 446 HOH A O   1 
HETATM 2218 O  O   . HOH F 5 .   ? -6.352 -5.578  26.103  1.00 37.50  ? 447 HOH A O   1 
HETATM 2219 O  O   . HOH F 5 .   ? 14.139 -13.043 31.559  1.00 19.89  ? 448 HOH A O   1 
HETATM 2220 O  O   . HOH F 5 .   ? 5.366  2.378   -4.676  1.00 30.50  ? 449 HOH A O   1 
HETATM 2221 O  O   . HOH F 5 .   ? 10.556 -16.322 17.255  1.00 29.03  ? 450 HOH A O   1 
HETATM 2222 O  O   . HOH F 5 .   ? 34.581 1.953   24.597  1.00 18.75  ? 451 HOH A O   1 
HETATM 2223 O  O   . HOH F 5 .   ? 15.814 18.185  12.400  1.00 14.42  ? 452 HOH A O   1 
HETATM 2224 O  O   . HOH F 5 .   ? -4.746 8.144   27.164  1.00 28.55  ? 453 HOH A O   1 
HETATM 2225 O  O   . HOH F 5 .   ? 4.142  -21.195 4.205   1.00 19.84  ? 454 HOH A O   1 
HETATM 2226 O  O   . HOH F 5 .   ? 20.983 0.940   -4.698  1.00 13.11  ? 455 HOH A O   1 
HETATM 2227 O  O   . HOH F 5 .   ? 4.492  7.094   -7.923  1.00 26.98  ? 456 HOH A O   1 
HETATM 2228 O  O   . HOH F 5 .   ? 8.494  15.028  31.939  1.00 26.98  ? 457 HOH A O   1 
HETATM 2229 O  O   . HOH F 5 .   ? 1.879  -19.064 5.212   1.00 17.14  ? 458 HOH A O   1 
HETATM 2230 O  O   . HOH F 5 .   ? -4.844 -3.712  13.279  1.00 32.61  ? 459 HOH A O   1 
HETATM 2231 O  O   . HOH F 5 .   ? 17.109 22.494  15.805  1.00 21.09  ? 460 HOH A O   1 
HETATM 2232 O  O   . HOH F 5 .   ? 6.679  -14.812 28.841  1.00 27.15  ? 461 HOH A O   1 
HETATM 2233 O  O   . HOH F 5 .   ? 2.281  -18.908 15.153  1.00 24.12  ? 462 HOH A O   1 
HETATM 2234 O  O   . HOH F 5 .   ? 28.515 -5.858  -1.001  1.00 17.73  ? 463 HOH A O   1 
HETATM 2235 O  O   . HOH F 5 .   ? 19.176 2.557   9.003   1.00 15.12  ? 464 HOH A O   1 
HETATM 2236 O  O   . HOH F 5 .   ? 5.392  10.720  -1.781  1.00 39.59  ? 465 HOH A O   1 
HETATM 2237 O  O   . HOH F 5 .   ? 14.650 3.647   10.488  1.00 22.90  ? 466 HOH A O   1 
HETATM 2238 O  O   . HOH F 5 .   ? -3.999 6.556   8.779   1.00 35.22  ? 467 HOH A O   1 
HETATM 2239 O  O   . HOH F 5 .   ? 18.865 -2.676  -7.092  1.00 26.20  ? 468 HOH A O   1 
HETATM 2240 O  O   . HOH F 5 .   ? -4.497 -8.779  17.817  1.00 24.20  ? 469 HOH A O   1 
HETATM 2241 O  O   . HOH F 5 .   ? 2.679  -10.746 -3.595  1.00 24.92  ? 470 HOH A O   1 
HETATM 2242 O  O   . HOH F 5 .   ? 0.923  12.721  26.696  1.00 17.60  ? 471 HOH A O   1 
HETATM 2243 O  O   . HOH F 5 .   ? -2.955 1.614   1.413   1.00 28.92  ? 472 HOH A O   1 
HETATM 2244 O  O   . HOH F 5 .   ? 20.807 3.060   -10.907 1.00 24.34  ? 473 HOH A O   1 
HETATM 2245 O  O   . HOH F 5 .   ? 18.529 -6.936  29.141  1.00 10.66  ? 474 HOH A O   1 
HETATM 2246 O  O   . HOH F 5 .   ? 20.728 -18.669 14.984  1.00 40.67  ? 475 HOH A O   1 
HETATM 2247 O  O   . HOH F 5 .   ? 11.214 7.968   -4.040  1.00 30.08  ? 476 HOH A O   1 
HETATM 2248 O  O   . HOH F 5 .   ? -0.266 9.609   2.000   1.00 13.76  ? 477 HOH A O   1 
HETATM 2249 O  O   . HOH F 5 .   ? 32.439 -1.822  7.979   1.00 41.71  ? 478 HOH A O   1 
HETATM 2250 O  O   . HOH F 5 .   ? 23.547 -11.490 5.142   1.00 15.22  ? 479 HOH A O   1 
HETATM 2251 O  O   . HOH F 5 .   ? 1.652  19.187  6.210   1.00 18.97  ? 480 HOH A O   1 
HETATM 2252 O  O   . HOH F 5 .   ? 13.459 -3.098  39.969  1.00 29.49  ? 481 HOH A O   1 
HETATM 2253 O  O   . HOH F 5 .   ? 13.805 -6.544  -7.140  1.00 36.83  ? 482 HOH A O   1 
HETATM 2254 O  O   . HOH F 5 .   ? -4.813 10.119  6.458   1.00 36.27  ? 483 HOH A O   1 
HETATM 2255 O  O   . HOH F 5 .   ? 13.139 -13.582 11.312  1.00 8.44   ? 484 HOH A O   1 
HETATM 2256 O  O   . HOH F 5 .   ? 4.036  -6.549  20.443  1.00 7.57   ? 485 HOH A O   1 
HETATM 2257 O  O   . HOH F 5 .   ? 7.357  12.343  27.883  1.00 15.44  ? 486 HOH A O   1 
HETATM 2258 O  O   . HOH F 5 .   ? 17.243 -11.024 -2.901  1.00 22.18  ? 487 HOH A O   1 
HETATM 2259 O  O   . HOH F 5 .   ? 11.969 2.334   -6.414  1.00 25.39  ? 488 HOH A O   1 
HETATM 2260 O  O   . HOH F 5 .   ? 14.411 -3.495  37.383  1.00 18.72  ? 489 HOH A O   1 
HETATM 2261 O  O   . HOH F 5 .   ? 35.005 3.950   22.982  1.00 20.26  ? 490 HOH A O   1 
HETATM 2262 O  O   . HOH F 5 .   ? 7.280  -18.885 3.661   1.00 22.84  ? 491 HOH A O   1 
HETATM 2263 O  O   . HOH F 5 .   ? 9.226  11.198  3.398   1.00 16.26  ? 492 HOH A O   1 
HETATM 2264 O  O   . HOH F 5 .   ? 16.532 -11.577 18.000  1.00 8.41   ? 493 HOH A O   1 
HETATM 2265 O  O   . HOH F 5 .   ? 26.573 8.894   20.498  1.00 16.49  ? 494 HOH A O   1 
HETATM 2266 O  O   . HOH F 5 .   ? 24.338 -2.449  6.935   1.00 33.14  ? 495 HOH A O   1 
HETATM 2267 O  O   . HOH F 5 .   ? 2.989  8.371   38.754  1.00 42.25  ? 496 HOH A O   1 
HETATM 2268 O  O   . HOH F 5 .   ? -3.362 22.458  8.581   1.00 29.46  ? 497 HOH A O   1 
HETATM 2269 O  O   . HOH F 5 .   ? 2.817  12.448  11.521  1.00 19.64  ? 498 HOH A O   1 
HETATM 2270 O  O   . HOH F 5 .   ? 17.546 -9.282  20.856  1.00 8.69   ? 499 HOH A O   1 
HETATM 2271 O  O   . HOH F 5 .   ? -1.708 -4.073  3.011   1.00 22.77  ? 500 HOH A O   1 
HETATM 2272 O  O   . HOH F 5 .   ? 13.691 -6.890  32.577  1.00 16.08  ? 501 HOH A O   1 
HETATM 2273 O  O   . HOH F 5 .   ? -5.189 4.644   21.177  1.00 19.06  ? 502 HOH A O   1 
HETATM 2274 O  O   . HOH F 5 .   ? 2.629  -2.032  -2.525  1.00 24.34  ? 503 HOH A O   1 
HETATM 2275 O  O   . HOH F 5 .   ? -6.456 6.270   24.342  1.00 35.12  ? 504 HOH A O   1 
HETATM 2276 O  O   . HOH F 5 .   ? -5.463 5.615   15.689  1.00 23.47  ? 505 HOH A O   1 
HETATM 2277 O  O   . HOH F 5 .   ? 10.130 2.947   33.821  1.00 37.61  ? 506 HOH A O   1 
HETATM 2278 O  O   . HOH F 5 .   ? 9.001  12.449  5.965   1.00 20.88  ? 507 HOH A O   1 
HETATM 2279 O  O   . HOH F 5 .   ? 9.940  -17.353 7.124   1.00 15.60  ? 508 HOH A O   1 
HETATM 2280 O  O   . HOH F 5 .   ? 8.103  -7.181  -3.039  1.00 20.61  ? 509 HOH A O   1 
HETATM 2281 O  O   . HOH F 5 .   ? -0.515 -5.277  23.643  1.00 10.98  ? 510 HOH A O   1 
HETATM 2282 O  O   . HOH F 5 .   ? -3.857 -5.969  9.334   1.00 18.06  ? 511 HOH A O   1 
HETATM 2283 O  O   . HOH F 5 .   ? 19.805 10.842  28.428  1.00 36.94  ? 512 HOH A O   1 
HETATM 2284 O  O   . HOH F 5 .   ? 5.025  -10.479 24.435  1.00 14.66  ? 513 HOH A O   1 
HETATM 2285 O  O   . HOH F 5 .   ? 24.480 10.565  21.170  1.00 25.84  ? 514 HOH A O   1 
HETATM 2286 O  O   . HOH F 5 .   ? 25.543 1.159   -5.213  1.00 24.17  ? 515 HOH A O   1 
HETATM 2287 O  O   . HOH F 5 .   ? 17.300 -13.992 24.349  1.00 14.28  ? 516 HOH A O   1 
HETATM 2288 O  O   . HOH F 5 .   ? 16.786 -6.832  31.253  1.00 19.53  ? 517 HOH A O   1 
HETATM 2289 O  O   . HOH F 5 .   ? -1.105 7.610   4.933   1.00 13.58  ? 518 HOH A O   1 
HETATM 2290 O  O   . HOH F 5 .   ? 22.211 -9.981  25.091  1.00 23.76  ? 519 HOH A O   1 
HETATM 2291 O  O   . HOH F 5 .   ? -2.216 -9.550  17.160  1.00 32.49  ? 520 HOH A O   1 
HETATM 2292 O  O   . HOH F 5 .   ? 13.971 -15.017 1.957   1.00 17.50  ? 521 HOH A O   1 
HETATM 2293 O  O   . HOH F 5 .   ? -2.161 -1.303  7.032   1.00 20.45  ? 522 HOH A O   1 
HETATM 2294 O  O   . HOH F 5 .   ? 16.348 -16.975 5.611   1.00 24.31  ? 523 HOH A O   1 
HETATM 2295 O  O   . HOH F 5 .   ? 21.694 -7.868  -5.671  1.00 36.39  ? 524 HOH A O   1 
HETATM 2296 O  O   . HOH F 5 .   ? 24.492 -11.227 12.156  1.00 40.52  ? 525 HOH A O   1 
HETATM 2297 O  O   . HOH F 5 .   ? 1.411  -2.374  41.444  1.00 37.47  ? 526 HOH A O   1 
HETATM 2298 O  O   . HOH F 5 .   ? 0.912  15.669  28.983  1.00 39.95  ? 527 HOH A O   1 
HETATM 2299 O  O   . HOH F 5 .   ? 17.090 6.698   8.295   1.00 25.53  ? 528 HOH A O   1 
HETATM 2300 O  O   . HOH F 5 .   ? 17.650 -11.347 25.204  1.00 11.08  ? 529 HOH A O   1 
HETATM 2301 O  O   . HOH F 5 .   ? 7.531  22.148  14.993  1.00 22.23  ? 530 HOH A O   1 
HETATM 2302 O  O   . HOH F 5 .   ? 25.961 -3.004  21.058  1.00 12.35  ? 531 HOH A O   1 
HETATM 2303 O  O   . HOH F 5 .   ? 3.291  -18.896 8.236   1.00 12.54  ? 532 HOH A O   1 
HETATM 2304 O  O   . HOH F 5 .   ? 10.244 14.367  7.552   1.00 27.57  ? 533 HOH A O   1 
HETATM 2305 O  O   . HOH F 5 .   ? -2.914 -12.627 19.837  1.00 37.86  ? 534 HOH A O   1 
HETATM 2306 O  O   . HOH F 5 .   ? -2.808 1.208   26.559  1.00 19.71  ? 535 HOH A O   1 
HETATM 2307 O  O   . HOH F 5 .   ? -5.629 -0.587  14.665  1.00 19.61  ? 536 HOH A O   1 
HETATM 2308 O  O   . HOH F 5 .   ? 8.002  -14.952 26.558  1.00 21.11  ? 537 HOH A O   1 
HETATM 2309 O  O   . HOH F 5 .   ? 29.686 -1.957  21.208  1.00 12.96  ? 538 HOH A O   1 
HETATM 2310 O  O   . HOH F 5 .   ? 21.188 5.266   5.698   1.00 27.60  ? 539 HOH A O   1 
HETATM 2311 O  O   . HOH F 5 .   ? 23.752 2.931   -2.216  1.00 27.06  ? 540 HOH A O   1 
HETATM 2312 O  O   . HOH F 5 .   ? 19.505 6.407   -4.738  1.00 21.33  ? 541 HOH A O   1 
HETATM 2313 O  O   . HOH F 5 .   ? 18.618 -16.895 22.115  1.00 36.30  ? 542 HOH A O   1 
HETATM 2314 O  O   . HOH F 5 .   ? 9.168  4.643   30.764  1.00 17.13  ? 543 HOH A O   1 
HETATM 2315 O  O   . HOH F 5 .   ? 23.121 -13.647 -1.475  1.00 51.65  ? 544 HOH A O   1 
HETATM 2316 O  O   . HOH F 5 .   ? 21.292 9.063   30.123  1.00 31.36  ? 545 HOH A O   1 
HETATM 2317 O  O   . HOH F 5 .   ? 23.672 -9.443  9.510   1.00 18.57  ? 546 HOH A O   1 
HETATM 2318 O  O   . HOH F 5 .   ? 22.770 -4.851  -8.706  1.00 33.89  ? 547 HOH A O   1 
HETATM 2319 O  O   . HOH F 5 .   ? 18.523 19.934  15.858  1.00 43.39  ? 548 HOH A O   1 
HETATM 2320 O  O   . HOH F 5 .   ? 20.839 -12.407 22.144  1.00 19.04  ? 549 HOH A O   1 
HETATM 2321 O  O   . HOH F 5 .   ? 34.140 -4.022  24.609  1.00 26.44  ? 550 HOH A O   1 
HETATM 2322 O  O   . HOH F 5 .   ? 0.459  20.800  13.994  1.00 23.54  ? 551 HOH A O   1 
HETATM 2323 O  O   . HOH F 5 .   ? 7.415  16.132  27.278  1.00 27.36  ? 552 HOH A O   1 
HETATM 2324 O  O   . HOH F 5 .   ? 6.089  22.101  17.628  1.00 21.04  ? 553 HOH A O   1 
HETATM 2325 O  O   . HOH F 5 .   ? 22.879 9.927   24.985  1.00 18.38  ? 554 HOH A O   1 
HETATM 2326 O  O   . HOH F 5 .   ? 35.655 1.811   15.152  1.00 32.30  ? 555 HOH A O   1 
HETATM 2327 O  O   . HOH F 5 .   ? 27.020 -11.088 -5.281  1.00 15.13  ? 556 HOH A O   1 
HETATM 2328 O  O   . HOH F 5 .   ? 8.508  -21.055 8.389   1.00 29.03  ? 557 HOH A O   1 
HETATM 2329 O  O   . HOH F 5 .   ? 4.828  -8.046  32.942  1.00 21.02  ? 558 HOH A O   1 
HETATM 2330 O  O   . HOH F 5 .   ? -5.775 -2.142  25.215  1.00 20.58  ? 559 HOH A O   1 
HETATM 2331 O  O   . HOH F 5 .   ? -6.925 7.977   21.692  1.00 33.08  ? 560 HOH A O   1 
HETATM 2332 O  O   . HOH F 5 .   ? -5.816 -9.117  22.881  1.00 44.87  ? 561 HOH A O   1 
HETATM 2333 O  O   . HOH F 5 .   ? 4.928  17.904  23.647  1.00 23.91  ? 562 HOH A O   1 
HETATM 2334 O  O   . HOH F 5 .   ? -5.168 -5.641  30.604  1.00 33.10  ? 563 HOH A O   1 
HETATM 2335 O  O   . HOH F 5 .   ? 6.319  16.251  4.821   1.00 35.66  ? 564 HOH A O   1 
HETATM 2336 O  O   . HOH F 5 .   ? 1.682  11.833  9.036   1.00 12.76  ? 565 HOH A O   1 
HETATM 2337 O  O   . HOH F 5 .   ? -2.390 -16.450 6.409   1.00 27.37  ? 566 HOH A O   1 
HETATM 2338 O  O   . HOH F 5 .   ? 11.964 -4.016  35.972  1.00 19.22  ? 567 HOH A O   1 
HETATM 2339 O  O   . HOH F 5 .   ? 19.512 20.963  23.490  1.00 37.75  ? 568 HOH A O   1 
HETATM 2340 O  O   . HOH F 5 .   ? 8.451  9.768   28.935  1.00 27.35  ? 569 HOH A O   1 
HETATM 2341 O  O   . HOH F 5 .   ? -2.431 -11.484 11.452  1.00 27.40  ? 570 HOH A O   1 
HETATM 2342 O  O   . HOH F 5 .   ? -1.877 -9.986  14.203  1.00 17.63  ? 571 HOH A O   1 
HETATM 2343 O  O   . HOH F 5 .   ? 32.342 3.060   26.125  1.00 22.76  ? 572 HOH A O   1 
HETATM 2344 O  O   . HOH F 5 .   ? 3.320  7.134   -3.458  1.00 21.80  ? 573 HOH A O   1 
HETATM 2345 O  O   . HOH F 5 .   ? 9.697  19.810  12.376  1.00 23.44  ? 574 HOH A O   1 
HETATM 2346 O  O   . HOH F 5 .   ? 22.234 -4.783  34.540  1.00 33.25  ? 575 HOH A O   1 
HETATM 2347 O  O   . HOH F 5 .   ? -1.159 -16.622 13.683  1.00 22.76  ? 576 HOH A O   1 
HETATM 2348 O  O   . HOH F 5 .   ? 20.472 -6.761  32.535  1.00 24.32  ? 577 HOH A O   1 
HETATM 2349 O  O   . HOH F 5 .   ? -1.400 -10.554 24.817  1.00 32.02  ? 578 HOH A O   1 
HETATM 2350 O  O   . HOH F 5 .   ? 22.347 0.180   29.534  1.00 12.13  ? 579 HOH A O   1 
HETATM 2351 O  O   . HOH F 5 .   ? 7.330  0.914   -6.115  1.00 28.19  ? 580 HOH A O   1 
HETATM 2352 O  O   . HOH F 5 .   ? 8.184  5.399   -6.720  1.00 22.34  ? 581 HOH A O   1 
HETATM 2353 O  O   . HOH F 5 .   ? 13.878 3.162   35.051  1.00 25.42  ? 582 HOH A O   1 
HETATM 2354 O  O   . HOH F 5 .   ? 10.129 10.960  8.004   1.00 19.86  ? 583 HOH A O   1 
HETATM 2355 O  O   . HOH F 5 .   ? 10.394 23.848  19.645  1.00 39.73  ? 584 HOH A O   1 
HETATM 2356 O  O   . HOH F 5 .   ? 10.304 -17.546 27.428  1.00 50.43  ? 585 HOH A O   1 
HETATM 2357 O  O   . HOH F 5 .   ? 18.968 -10.425 22.839  1.00 9.15   ? 586 HOH A O   1 
HETATM 2358 O  O   . HOH F 5 .   ? -0.692 21.316  17.485  1.00 44.61  ? 587 HOH A O   1 
HETATM 2359 O  O   . HOH F 5 .   ? 7.973  -16.456 14.950  1.00 20.10  ? 588 HOH A O   1 
HETATM 2360 O  O   . HOH F 5 .   ? -3.139 1.019   4.075   1.00 17.91  ? 589 HOH A O   1 
HETATM 2361 O  O   . HOH F 5 .   ? 13.917 -16.801 4.429   1.00 18.67  ? 590 HOH A O   1 
HETATM 2362 O  O   . HOH F 5 .   ? -1.352 5.566   -3.112  1.00 19.09  ? 591 HOH A O   1 
HETATM 2363 O  O   . HOH F 5 .   ? 15.322 5.139   -5.728  1.00 28.20  ? 592 HOH A O   1 
HETATM 2364 O  O   . HOH F 5 .   ? 28.087 -1.967  30.127  1.00 36.75  ? 593 HOH A O   1 
HETATM 2365 O  O   . HOH F 5 .   ? 28.714 8.065   22.112  1.00 15.35  ? 594 HOH A O   1 
HETATM 2366 O  O   . HOH F 5 .   ? 12.527 -18.111 26.532  1.00 35.99  ? 595 HOH A O   1 
HETATM 2367 O  O   . HOH F 5 .   ? 13.971 8.554   9.861   1.00 26.82  ? 596 HOH A O   1 
HETATM 2368 O  O   . HOH F 5 .   ? 18.481 -12.917 32.905  1.00 30.21  ? 597 HOH A O   1 
HETATM 2369 O  O   . HOH F 5 .   ? 27.221 -9.677  14.494  1.00 55.92  ? 598 HOH A O   1 
HETATM 2370 O  O   . HOH F 5 .   ? -7.157 7.362   19.361  1.00 34.53  ? 599 HOH A O   1 
HETATM 2371 O  O   . HOH F 5 .   ? 26.198 -5.413  22.330  1.00 26.45  ? 600 HOH A O   1 
HETATM 2372 O  O   . HOH F 5 .   ? 12.942 -17.498 21.765  1.00 23.88  ? 601 HOH A O   1 
HETATM 2373 O  O   . HOH F 5 .   ? 14.914 -18.053 24.240  1.00 41.70  ? 602 HOH A O   1 
HETATM 2374 O  O   . HOH F 5 .   ? 25.624 -4.960  7.721   1.00 33.17  ? 603 HOH A O   1 
HETATM 2375 O  O   . HOH F 5 .   ? 18.184 8.038   -1.343  1.00 24.87  ? 604 HOH A O   1 
HETATM 2376 O  O   . HOH F 5 .   ? -2.550 1.763   31.863  1.00 34.39  ? 605 HOH A O   1 
HETATM 2377 O  O   . HOH F 5 .   ? 9.257  -1.891  42.225  1.00 35.81  ? 606 HOH A O   1 
HETATM 2378 O  O   . HOH F 5 .   ? 11.570 -6.125  34.073  1.00 22.40  ? 607 HOH A O   1 
HETATM 2379 O  O   . HOH F 5 .   ? 11.543 17.747  12.108  1.00 13.95  ? 608 HOH A O   1 
HETATM 2380 O  O   . HOH F 5 .   ? 6.036  -9.555  -3.780  1.00 41.94  ? 609 HOH A O   1 
HETATM 2381 O  O   . HOH F 5 .   ? 33.876 -1.919  13.612  1.00 37.65  ? 610 HOH A O   1 
HETATM 2382 O  O   . HOH F 5 .   ? 19.649 -15.740 18.070  1.00 29.50  ? 611 HOH A O   1 
HETATM 2383 O  O   . HOH F 5 .   ? 29.478 5.201   28.337  1.00 35.31  ? 612 HOH A O   1 
HETATM 2384 O  O   . HOH F 5 .   ? 14.843 -0.457  -8.005  1.00 34.52  ? 613 HOH A O   1 
HETATM 2385 O  O   . HOH F 5 .   ? 28.415 -7.249  -7.751  1.00 23.38  ? 614 HOH A O   1 
HETATM 2386 O  O   . HOH F 5 .   ? 2.044  5.075   -3.566  1.00 34.26  ? 615 HOH A O   1 
HETATM 2387 O  O   . HOH F 5 .   ? 25.692 -7.792  8.302   1.00 38.41  ? 616 HOH A O   1 
HETATM 2388 O  O   . HOH F 5 .   ? 8.487  -16.890 32.236  1.00 40.04  ? 617 HOH A O   1 
HETATM 2389 O  O   . HOH F 5 .   ? 30.595 4.006   12.355  1.00 35.41  ? 618 HOH A O   1 
HETATM 2390 O  O   . HOH F 5 .   ? 3.351  -5.943  39.761  1.00 46.07  ? 619 HOH A O   1 
HETATM 2391 O  O   . HOH F 5 .   ? -3.704 -7.949  2.068   1.00 27.79  ? 620 HOH A O   1 
HETATM 2392 O  O   . HOH F 5 .   ? 7.431  20.880  11.611  1.00 29.13  ? 621 HOH A O   1 
HETATM 2393 O  O   . HOH F 5 .   ? 29.725 -2.783  23.874  1.00 27.75  ? 622 HOH A O   1 
HETATM 2394 O  O   . HOH F 5 .   ? 5.704  -14.453 25.279  1.00 46.92  ? 623 HOH A O   1 
HETATM 2395 O  O   . HOH F 5 .   ? 12.630 -15.667 34.649  1.00 28.88  ? 624 HOH A O   1 
HETATM 2396 O  O   . HOH F 5 .   ? 3.372  21.656  17.549  1.00 24.10  ? 625 HOH A O   1 
HETATM 2397 O  O   . HOH F 5 .   ? 21.506 2.733   -6.620  1.00 22.98  ? 626 HOH A O   1 
HETATM 2398 O  O   . HOH F 5 .   ? 16.599 9.561   9.615   1.00 36.73  ? 627 HOH A O   1 
HETATM 2399 O  O   . HOH F 5 .   ? 22.306 -14.612 19.252  1.00 44.55  ? 628 HOH A O   1 
HETATM 2400 O  O   . HOH F 5 .   ? 0.125  23.456  6.878   1.00 22.02  ? 629 HOH A O   1 
HETATM 2401 O  O   . HOH F 5 .   ? -2.809 -1.721  4.291   1.00 36.42  ? 630 HOH A O   1 
HETATM 2402 O  O   . HOH F 5 .   ? 16.100 9.368   -3.171  1.00 40.91  ? 631 HOH A O   1 
HETATM 2403 O  O   . HOH F 5 .   ? 31.320 -0.432  14.341  1.00 37.03  ? 632 HOH A O   1 
HETATM 2404 O  O   . HOH F 5 .   ? -4.254 13.631  19.507  1.00 43.66  ? 633 HOH A O   1 
HETATM 2405 O  O   . HOH F 5 .   ? -2.432 12.698  27.061  1.00 36.70  ? 634 HOH A O   1 
HETATM 2406 O  O   . HOH F 5 .   ? 31.624 8.632   15.161  1.00 39.47  ? 635 HOH A O   1 
HETATM 2407 O  O   . HOH F 5 .   ? 23.051 -7.897  29.622  1.00 39.86  ? 636 HOH A O   1 
HETATM 2408 O  O   . HOH F 5 .   ? 12.249 9.554   8.205   1.00 29.13  ? 637 HOH A O   1 
HETATM 2409 O  O   . HOH F 5 .   ? 8.285  -15.470 17.160  1.00 31.49  ? 638 HOH A O   1 
HETATM 2410 O  O   . HOH F 5 .   ? 8.738  8.710   31.115  1.00 36.39  ? 639 HOH A O   1 
HETATM 2411 O  O   . HOH F 5 .   ? 22.449 14.215  21.483  1.00 46.30  ? 640 HOH A O   1 
HETATM 2412 O  O   . HOH F 5 .   ? 6.678  -22.163 4.252   1.00 25.14  ? 641 HOH A O   1 
HETATM 2413 O  O   . HOH F 5 .   ? 18.960 -10.396 31.607  1.00 36.10  ? 642 HOH A O   1 
HETATM 2414 O  O   . HOH F 5 .   ? 2.909  -7.076  34.834  1.00 30.99  ? 643 HOH A O   1 
HETATM 2415 O  O   . HOH F 5 .   ? 19.658 9.539   10.570  1.00 39.06  ? 644 HOH A O   1 
HETATM 2416 O  O   . HOH F 5 .   ? 17.425 8.048   6.012   1.00 20.80  ? 645 HOH A O   1 
HETATM 2417 O  O   . HOH F 5 .   ? -3.802 11.049  26.295  1.00 41.27  ? 646 HOH A O   1 
HETATM 2418 O  O   . HOH F 5 .   ? 14.224 10.786  7.663   1.00 37.61  ? 647 HOH A O   1 
HETATM 2419 O  O   . HOH F 5 .   ? 7.259  -19.817 1.107   1.00 40.07  ? 648 HOH A O   1 
HETATM 2420 O  O   . HOH F 5 .   ? 19.684 -11.318 27.166  1.00 26.30  ? 649 HOH A O   1 
HETATM 2421 O  O   . HOH F 5 .   ? 24.063 -11.577 8.086   1.00 25.87  ? 650 HOH A O   1 
HETATM 2422 O  O   . HOH F 5 .   ? 4.276  -16.286 20.454  1.00 42.18  ? 651 HOH A O   1 
HETATM 2423 O  O   . HOH F 5 .   ? 0.901  -13.761 21.906  1.00 44.70  ? 652 HOH A O   1 
HETATM 2424 O  O   . HOH F 5 .   ? 20.859 4.773   8.529   1.00 37.07  ? 653 HOH A O   1 
HETATM 2425 O  O   . HOH F 5 .   ? 10.674 6.907   30.685  1.00 23.56  ? 654 HOH A O   1 
HETATM 2426 O  O   . HOH F 5 .   ? 27.476 -3.607  27.406  1.00 33.25  ? 655 HOH A O   1 
HETATM 2427 O  O   . HOH F 5 .   ? 30.179 -7.785  0.175   1.00 31.91  ? 656 HOH A O   1 
HETATM 2428 O  O   . HOH F 5 .   ? 9.863  -19.222 5.168   1.00 21.13  ? 657 HOH A O   1 
HETATM 2429 O  O   . HOH F 5 .   ? 20.027 -15.690 -2.072  1.00 33.01  ? 658 HOH A O   1 
HETATM 2430 O  O   . HOH F 5 .   ? 3.051  -10.330 31.339  1.00 28.95  ? 659 HOH A O   1 
HETATM 2431 O  O   . HOH F 5 .   ? 22.190 -15.128 16.944  1.00 54.93  ? 660 HOH A O   1 
HETATM 2432 O  O   . HOH F 5 .   ? 4.895  18.912  26.379  1.00 44.98  ? 661 HOH A O   1 
HETATM 2433 O  O   . HOH F 5 .   ? 8.781  -21.563 5.995   1.00 24.36  ? 662 HOH A O   1 
HETATM 2434 O  O   . HOH F 5 .   ? 1.038  -0.190  43.029  1.00 34.09  ? 663 HOH A O   1 
HETATM 2435 O  O   . HOH F 5 .   ? 18.276 17.198  11.793  1.00 23.70  ? 664 HOH A O   1 
HETATM 2436 O  O   . HOH F 5 .   ? 36.545 0.489   26.141  1.00 25.28  ? 665 HOH A O   1 
HETATM 2437 O  O   . HOH F 5 .   ? 4.243  -12.489 37.300  1.00 26.19  ? 666 HOH A O   1 
HETATM 2438 O  O   . HOH F 5 .   ? 9.028  2.629   -7.634  1.00 33.52  ? 667 HOH A O   1 
HETATM 2439 O  O   . HOH F 5 .   ? 19.367 6.528   4.552   1.00 27.57  ? 668 HOH A O   1 
HETATM 2440 O  O   . HOH F 5 .   ? 4.067  -12.172 26.297  1.00 23.86  ? 669 HOH A O   1 
HETATM 2441 O  O   . HOH F 5 .   ? 16.917 -13.586 -2.695  1.00 31.01  ? 670 HOH A O   1 
HETATM 2442 O  O   . HOH F 5 .   ? 9.554  12.561  0.987   1.00 22.29  ? 671 HOH A O   1 
HETATM 2443 O  O   . HOH F 5 .   ? 14.725 -18.929 26.347  1.00 36.36  ? 672 HOH A O   1 
HETATM 2444 O  O   . HOH F 5 .   ? -0.333 -12.187 23.237  1.00 36.38  ? 673 HOH A O   1 
HETATM 2445 O  O   . HOH F 5 .   ? 27.181 7.220   29.953  1.00 35.56  ? 674 HOH A O   1 
HETATM 2446 O  O   . HOH F 5 .   ? 23.074 -12.269 20.701  1.00 30.93  ? 675 HOH A O   1 
HETATM 2447 O  O   . HOH F 5 .   ? 19.918 -9.278  28.987  1.00 18.93  ? 676 HOH A O   1 
HETATM 2448 O  O   . HOH F 5 .   ? 19.023 -15.493 25.501  1.00 32.41  ? 677 HOH A O   1 
HETATM 2449 O  O   . HOH F 5 .   ? 15.829 -7.993  34.190  1.00 46.06  ? 678 HOH A O   1 
HETATM 2450 O  O   . HOH F 5 .   ? 13.716 18.743  10.606  1.00 12.21  ? 679 HOH A O   1 
HETATM 2451 O  O   . HOH F 5 .   ? 22.643 -15.696 7.158   1.00 30.13  ? 680 HOH A O   1 
HETATM 2452 O  O   . HOH F 5 .   ? 17.980 -15.636 4.004   1.00 23.68  ? 681 HOH A O   1 
HETATM 2453 O  O   . HOH F 5 .   ? 9.328  -9.658  -2.927  1.00 33.08  ? 682 HOH A O   1 
HETATM 2454 O  O   . HOH F 5 .   ? 8.718  15.367  4.860   1.00 28.21  ? 683 HOH A O   1 
HETATM 2455 O  O   . HOH F 5 .   ? 21.219 -19.680 17.455  1.00 37.99  ? 684 HOH A O   1 
HETATM 2456 O  O   . HOH F 5 .   ? 9.624  -23.782 9.547   1.00 25.90  ? 685 HOH A O   1 
HETATM 2457 O  O   . HOH F 5 .   ? 23.345 6.402   5.986   1.00 30.67  ? 686 HOH A O   1 
HETATM 2458 O  O   . HOH F 5 .   ? 20.332 -4.915  -7.835  1.00 36.24  ? 687 HOH A O   1 
HETATM 2459 O  O   . HOH F 5 .   ? 25.155 -9.944  23.196  1.00 40.05  ? 688 HOH A O   1 
HETATM 2460 O  O   . HOH F 5 .   ? 27.784 10.412  18.462  1.00 31.34  ? 689 HOH A O   1 
HETATM 2461 O  O   . HOH F 5 .   ? 18.300 -7.654  34.366  1.00 35.71  ? 690 HOH A O   1 
HETATM 2462 O  O   . HOH F 5 .   ? 8.106  23.761  26.355  1.00 29.56  ? 691 HOH A O   1 
HETATM 2463 O  O   . HOH F 5 .   ? 35.387 0.164   28.680  1.00 40.29  ? 692 HOH A O   1 
HETATM 2464 O  O   . HOH F 5 .   ? 20.217 -15.431 5.147   1.00 31.48  ? 693 HOH A O   1 
HETATM 2465 O  O   . HOH F 5 .   ? 25.228 -11.464 21.252  1.00 37.08  ? 694 HOH A O   1 
HETATM 2466 O  O   . HOH F 5 .   ? 9.124  15.010  2.049   1.00 31.78  ? 695 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 4   ? 1.2557 0.2669 1.0890 -0.0979 0.0318  0.2001  4   HIS A N   
2    C  CA  . HIS A 4   ? 1.2798 0.4399 0.4421 0.2111  0.2459  0.0697  4   HIS A CA  
3    C  C   . HIS A 4   ? 0.4300 0.6201 1.0099 0.2500  0.2936  -0.0701 4   HIS A C   
4    O  O   . HIS A 4   ? 0.3737 0.4936 0.3495 -0.1193 0.0936  0.0467  4   HIS A O   
5    C  CB  . HIS A 4   ? 0.3340 1.0886 2.3030 0.4727  0.5404  1.0124  4   HIS A CB  
6    C  CG  . HIS A 4   ? 1.1521 0.9667 2.1978 0.1163  0.7558  0.2945  4   HIS A CG  
7    N  N   . TRP A 5   ? 0.1961 0.3831 0.4016 0.0135  0.0077  0.0756  5   TRP A N   
8    C  CA  . TRP A 5   ? 0.3150 0.2022 0.3176 0.0514  0.0552  -0.0104 5   TRP A CA  
9    C  C   . TRP A 5   ? 0.2178 0.2548 0.2634 0.0323  0.0660  0.0221  5   TRP A C   
10   O  O   . TRP A 5   ? 0.2392 0.2755 0.2583 -0.0585 0.0198  0.0421  5   TRP A O   
11   C  CB  . TRP A 5   ? 0.2040 0.2221 0.3017 0.0236  0.0222  -0.0372 5   TRP A CB  
12   C  CG  . TRP A 5   ? 0.2371 0.2241 0.2875 0.0418  0.0822  0.0526  5   TRP A CG  
13   C  CD1 . TRP A 5   ? 0.2989 0.2540 0.2302 0.0289  0.0745  0.0797  5   TRP A CD1 
14   C  CD2 . TRP A 5   ? 0.2924 0.2309 0.1813 -0.0377 0.0488  -0.0460 5   TRP A CD2 
15   N  NE1 . TRP A 5   ? 0.2799 0.2597 0.2878 -0.0335 0.0604  0.0913  5   TRP A NE1 
16   C  CE2 . TRP A 5   ? 0.2295 0.2958 0.1181 -0.0637 0.0219  0.0149  5   TRP A CE2 
17   C  CE3 . TRP A 5   ? 0.1476 0.2619 0.2763 -0.0581 0.0348  -0.0765 5   TRP A CE3 
18   C  CZ2 . TRP A 5   ? 0.2421 0.3660 0.1624 -0.0560 0.0303  -0.0458 5   TRP A CZ2 
19   C  CZ3 . TRP A 5   ? 0.1404 0.3559 0.3033 -0.0335 0.0771  -0.1195 5   TRP A CZ3 
20   C  CH2 . TRP A 5   ? 0.2058 0.3637 0.2425 -0.0511 0.0316  -0.0424 5   TRP A CH2 
21   N  N   . GLY A 6   ? 0.1688 0.2191 0.3118 0.0042  0.0330  -0.0335 6   GLY A N   
22   C  CA  . GLY A 6   ? 0.1929 0.2143 0.2349 -0.0232 0.0385  -0.0064 6   GLY A CA  
23   C  C   . GLY A 6   ? 0.2637 0.2259 0.3089 0.0000  0.0763  0.0156  6   GLY A C   
24   O  O   . GLY A 6   ? 0.1968 0.3247 0.2952 -0.0223 0.0418  -0.0201 6   GLY A O   
25   N  N   . TYR A 7   ? 0.2033 0.2558 0.2558 0.0143  0.0658  -0.0432 7   TYR A N   
26   C  CA  . TYR A 7   ? 0.2223 0.2241 0.4055 -0.0122 0.0586  -0.0018 7   TYR A CA  
27   C  C   . TYR A 7   ? 0.1756 0.2820 0.4808 0.0190  0.0649  -0.1320 7   TYR A C   
28   O  O   . TYR A 7   ? 0.2917 0.4104 0.6381 -0.0925 0.1317  -0.0675 7   TYR A O   
29   C  CB  . TYR A 7   ? 0.2001 0.1979 0.3556 0.0389  0.0373  -0.0250 7   TYR A CB  
30   C  CG  . TYR A 7   ? 0.1879 0.1745 0.2636 0.0174  0.0336  -0.0175 7   TYR A CG  
31   C  CD1 . TYR A 7   ? 0.0988 0.3166 0.2895 -0.0599 0.0598  -0.0862 7   TYR A CD1 
32   C  CD2 . TYR A 7   ? 0.1896 0.1767 0.2312 -0.0656 -0.0114 -0.0057 7   TYR A CD2 
33   C  CE1 . TYR A 7   ? 0.1850 0.1911 0.1803 -0.0979 -0.0016 -0.0205 7   TYR A CE1 
34   C  CE2 . TYR A 7   ? 0.2233 0.1336 0.1645 -0.0523 -0.0137 0.0151  7   TYR A CE2 
35   C  CZ  . TYR A 7   ? 0.1677 0.1221 0.2324 -0.0844 0.0219  -0.0611 7   TYR A CZ  
36   O  OH  . TYR A 7   ? 0.2032 0.2026 0.4005 -0.0824 0.0597  -0.1246 7   TYR A OH  
37   N  N   . GLY A 8   ? 0.2033 0.2813 0.4734 0.0368  0.0757  -0.0231 8   GLY A N   
38   C  CA  . GLY A 8   ? 0.2424 0.3125 0.5597 0.0335  0.1489  -0.1419 8   GLY A CA  
39   C  C   . GLY A 8   ? 0.4591 0.3395 0.2551 0.0773  0.2601  -0.0148 8   GLY A C   
40   O  O   . GLY A 8   ? 0.3860 0.3887 0.4203 0.0000  0.1738  -0.1335 8   GLY A O   
41   N  N   . LYS A 9   ? 0.5064 0.3065 0.7070 0.1170  0.0891  -0.0630 9   LYS A N   
42   C  CA  . LYS A 9   ? 0.5753 0.4605 0.6516 -0.0087 0.0047  -0.0616 9   LYS A CA  
43   C  C   . LYS A 9   ? 0.4017 0.6203 0.5172 -0.0864 -0.0260 0.1267  9   LYS A C   
44   O  O   . LYS A 9   ? 0.3703 0.4379 0.4997 -0.1026 0.1370  -0.0543 9   LYS A O   
45   C  CB  . LYS A 9   ? 0.2734 0.4844 0.7689 0.0548  0.1749  0.2554  9   LYS A CB  
46   N  N   . HIS A 10  ? 0.5267 0.1857 0.6409 0.1577  0.1742  0.0341  10  HIS A N   
47   C  CA  . HIS A 10  ? 0.5289 0.3377 0.6417 0.0989  0.1143  -0.0242 10  HIS A CA  
48   C  C   . HIS A 10  ? 0.2180 0.2910 0.3409 0.0523  0.1026  0.0771  10  HIS A C   
49   O  O   . HIS A 10  ? 0.1953 0.3687 0.2845 0.0460  0.0580  0.0618  10  HIS A O   
50   C  CB  . HIS A 10  ? 0.4902 0.3856 0.6229 0.0346  0.1132  0.0504  10  HIS A CB  
51   C  CG  . HIS A 10  ? 0.6583 0.6020 0.6365 0.1665  0.1167  0.0082  10  HIS A CG  
52   N  ND1 . HIS A 10  ? 0.5272 0.6842 0.6150 0.3424  0.1342  0.0185  10  HIS A ND1 
53   C  CD2 . HIS A 10  ? 0.5500 0.5539 0.6227 0.0859  0.0239  -0.0358 10  HIS A CD2 
54   C  CE1 . HIS A 10  ? 0.6735 0.5390 0.5945 0.1767  0.1656  -0.0098 10  HIS A CE1 
55   N  NE2 . HIS A 10  ? 0.7674 0.3788 0.6739 0.2426  0.1758  -0.0397 10  HIS A NE2 
56   N  N   . ASN A 11  ? 0.2276 0.3707 0.3391 0.0842  0.1458  0.0593  11  ASN A N   
57   C  CA  . ASN A 11  ? 0.1957 0.3039 0.2301 0.0399  0.1100  0.0088  11  ASN A CA  
58   C  C   . ASN A 11  ? 0.1717 0.2788 0.2626 -0.0317 0.0983  -0.0294 11  ASN A C   
59   O  O   . ASN A 11  ? 0.2359 0.3032 0.1972 -0.0139 0.0945  0.0009  11  ASN A O   
60   C  CB  . ASN A 11  ? 0.2266 0.2672 0.2597 -0.0215 0.1280  0.0299  11  ASN A CB  
61   C  CG  . ASN A 11  ? 0.2953 0.1505 0.3513 0.0563  0.0397  -0.0044 11  ASN A CG  
62   O  OD1 . ASN A 11  ? 0.3037 0.2820 0.3818 -0.0067 0.0882  0.0394  11  ASN A OD1 
63   N  ND2 . ASN A 11  ? 0.3453 0.4074 0.2806 0.0981  -0.0425 -0.0195 11  ASN A ND2 
64   N  N   . GLY A 12  ? 0.1627 0.3104 0.2144 -0.0640 0.0880  -0.0472 12  GLY A N   
65   C  CA  . GLY A 12  ? 0.1214 0.2748 0.1705 -0.0107 0.0468  -0.0109 12  GLY A CA  
66   C  C   . GLY A 12  ? 0.1390 0.2069 0.2089 -0.0099 0.0332  -0.0128 12  GLY A C   
67   O  O   . GLY A 12  ? 0.0918 0.2122 0.2421 -0.0013 0.0234  0.0004  12  GLY A O   
68   N  N   . PRO A 13  ? 0.1537 0.1663 0.1559 -0.0300 0.0342  -0.0361 13  PRO A N   
69   C  CA  . PRO A 13  ? 0.1343 0.1587 0.1814 -0.0304 0.0597  -0.0408 13  PRO A CA  
70   C  C   . PRO A 13  ? 0.1439 0.1573 0.1864 -0.0003 0.0306  -0.0297 13  PRO A C   
71   O  O   . PRO A 13  ? 0.1390 0.1641 0.1968 -0.0214 0.0315  -0.0410 13  PRO A O   
72   C  CB  . PRO A 13  ? 0.1390 0.2090 0.1849 -0.0779 0.0517  -0.0646 13  PRO A CB  
73   C  CG  . PRO A 13  ? 0.1954 0.2446 0.1450 -0.0527 0.0518  -0.0714 13  PRO A CG  
74   C  CD  . PRO A 13  ? 0.1267 0.2134 0.1418 -0.0081 0.0095  -0.0409 13  PRO A CD  
75   N  N   . GLU A 14  ? 0.1354 0.1296 0.2293 -0.0221 0.0293  0.0067  14  GLU A N   
76   C  CA  . GLU A 14  ? 0.1659 0.1591 0.2133 0.0134  0.0248  0.0440  14  GLU A CA  
77   C  C   . GLU A 14  ? 0.1365 0.1670 0.1807 0.0290  0.0316  0.0034  14  GLU A C   
78   O  O   . GLU A 14  ? 0.1709 0.1771 0.2176 0.0595  -0.0027 0.0165  14  GLU A O   
79   C  CB  . GLU A 14  ? 0.3043 0.1548 0.3105 0.0192  -0.0178 0.0829  14  GLU A CB  
80   C  CG  . GLU A 14  ? 0.4010 0.2957 0.3642 0.0107  -0.0200 -0.0553 14  GLU A CG  
81   C  CD  . GLU A 14  ? 0.3367 0.3492 0.5310 0.0629  -0.0482 -0.1645 14  GLU A CD  
82   O  OE1 . GLU A 14  ? 0.3226 0.2168 0.3424 0.0568  -0.0657 -0.1066 14  GLU A OE1 
83   O  OE2 . GLU A 14  ? 0.5303 0.2450 0.3231 0.0386  -0.0009 -0.1029 14  GLU A OE2 
84   N  N   . HIS A 15  ? 0.1153 0.1462 0.1838 -0.0010 0.0270  0.0059  15  HIS A N   
85   C  CA  . HIS A 15  ? 0.1006 0.1336 0.1771 -0.0013 0.0188  0.0040  15  HIS A CA  
86   C  C   . HIS A 15  ? 0.0866 0.1400 0.1774 0.0102  -0.0023 0.0022  15  HIS A C   
87   O  O   . HIS A 15  ? 0.0498 0.1555 0.2136 0.0107  -0.0013 0.0065  15  HIS A O   
88   C  CB  . HIS A 15  ? 0.0879 0.1710 0.1929 0.0321  0.0080  -0.0046 15  HIS A CB  
89   C  CG  . HIS A 15  ? 0.1253 0.1746 0.2405 0.0476  0.0015  0.0212  15  HIS A CG  
90   N  ND1 . HIS A 15  ? 0.1230 0.2187 0.2385 0.0838  -0.0081 -0.0440 15  HIS A ND1 
91   C  CD2 . HIS A 15  ? 0.1509 0.1929 0.2770 0.0476  0.0340  -0.0346 15  HIS A CD2 
92   C  CE1 . HIS A 15  ? 0.2392 0.2108 0.2449 0.0615  0.0118  -0.0384 15  HIS A CE1 
93   N  NE2 . HIS A 15  ? 0.2201 0.2604 0.3966 0.1020  0.0392  -0.1162 15  HIS A NE2 
94   N  N   . TRP A 16  ? 0.0916 0.1501 0.1774 0.0277  -0.0053 0.0214  16  TRP A N   
95   C  CA  . TRP A 16  ? 0.0372 0.1372 0.1839 0.0058  -0.0030 0.0212  16  TRP A CA  
96   C  C   . TRP A 16  ? 0.0697 0.1498 0.1796 -0.0053 0.0061  0.0114  16  TRP A C   
97   O  O   . TRP A 16  ? 0.0884 0.1414 0.1796 -0.0037 0.0013  0.0052  16  TRP A O   
98   C  CB  . TRP A 16  ? 0.0384 0.1634 0.1638 -0.0055 0.0104  -0.0147 16  TRP A CB  
99   C  CG  . TRP A 16  ? 0.0848 0.1634 0.1552 -0.0116 0.0088  -0.0061 16  TRP A CG  
100  C  CD1 . TRP A 16  ? 0.1032 0.2065 0.1430 -0.0015 0.0184  0.0115  16  TRP A CD1 
101  C  CD2 . TRP A 16  ? 0.0775 0.1333 0.1590 -0.0032 0.0332  -0.0234 16  TRP A CD2 
102  N  NE1 . TRP A 16  ? 0.0960 0.2220 0.1782 0.0132  0.0187  -0.0119 16  TRP A NE1 
103  C  CE2 . TRP A 16  ? 0.0947 0.1717 0.1662 -0.0055 0.0107  -0.0274 16  TRP A CE2 
104  C  CE3 . TRP A 16  ? 0.0733 0.0902 0.1807 0.0011  0.0372  -0.0159 16  TRP A CE3 
105  C  CZ2 . TRP A 16  ? 0.0909 0.1591 0.1825 -0.0229 0.0208  -0.0012 16  TRP A CZ2 
106  C  CZ3 . TRP A 16  ? 0.0856 0.1048 0.1821 -0.0157 0.0274  -0.0317 16  TRP A CZ3 
107  C  CH2 . TRP A 16  ? 0.1196 0.1376 0.1717 -0.0109 0.0295  -0.0286 16  TRP A CH2 
108  N  N   . HIS A 17  ? 0.0671 0.1667 0.1451 0.0024  0.0119  -0.0051 17  HIS A N   
109  C  CA  . HIS A 17  ? 0.0898 0.1437 0.1566 -0.0084 0.0020  0.0048  17  HIS A CA  
110  C  C   . HIS A 17  ? 0.0722 0.1807 0.1789 -0.0048 0.0122  -0.0040 17  HIS A C   
111  O  O   . HIS A 17  ? 0.1130 0.1940 0.2029 -0.0030 -0.0058 -0.0114 17  HIS A O   
112  C  CB  . HIS A 17  ? 0.0773 0.1868 0.1361 0.0230  -0.0035 0.0022  17  HIS A CB  
113  C  CG  . HIS A 17  ? 0.0848 0.1864 0.1911 0.0217  0.0006  0.0192  17  HIS A CG  
114  N  ND1 . HIS A 17  ? 0.1032 0.2026 0.2294 0.0057  -0.0221 0.0409  17  HIS A ND1 
115  C  CD2 . HIS A 17  ? 0.1448 0.1663 0.1796 0.0657  0.0032  0.0534  17  HIS A CD2 
116  C  CE1 . HIS A 17  ? 0.0917 0.2338 0.1868 0.0097  -0.0168 0.0057  17  HIS A CE1 
117  N  NE2 . HIS A 17  ? 0.1365 0.1807 0.1566 0.0348  -0.0166 0.0633  17  HIS A NE2 
118  N  N   . LYS A 18  ? 0.0598 0.1440 0.1982 0.0094  0.0133  0.0075  18  LYS A N   
119  C  CA  . LYS A 18  ? 0.0681 0.1728 0.2015 -0.0006 0.0277  0.0341  18  LYS A CA  
120  C  C   . LYS A 18  ? 0.0778 0.1947 0.2366 -0.0290 -0.0089 0.0454  18  LYS A C   
121  O  O   . LYS A 18  ? 0.1163 0.2187 0.4075 -0.0543 -0.0469 0.0558  18  LYS A O   
122  C  CB  . LYS A 18  ? 0.0817 0.1638 0.2348 0.0206  -0.0003 0.0248  18  LYS A CB  
123  C  CG  . LYS A 18  ? 0.1238 0.1720 0.2227 0.0499  0.0040  0.0102  18  LYS A CG  
124  C  CD  . LYS A 18  ? 0.0938 0.1810 0.2355 0.0496  -0.0050 0.0031  18  LYS A CD  
125  C  CE  . LYS A 18  ? 0.1051 0.1756 0.1655 0.0233  -0.0080 0.0330  18  LYS A CE  
126  N  NZ  . LYS A 18  ? 0.1040 0.1958 0.1907 0.0565  0.0200  0.0465  18  LYS A NZ  
127  N  N   . ASP A 19  ? 0.0782 0.1911 0.2033 0.0085  0.0044  0.0553  19  ASP A N   
128  C  CA  . ASP A 19  ? 0.1181 0.1688 0.2212 -0.0098 0.0245  0.0498  19  ASP A CA  
129  C  C   . ASP A 19  ? 0.0866 0.1656 0.2313 -0.0196 0.0096  0.0331  19  ASP A C   
130  O  O   . ASP A 19  ? 0.1462 0.1516 0.2866 -0.0277 0.0354  0.0196  19  ASP A O   
131  C  CB  . ASP A 19  ? 0.1274 0.2802 0.2205 0.0081  0.0302  -0.0015 19  ASP A CB  
132  C  CG  . ASP A 19  ? 0.2755 0.4578 0.3279 -0.0612 0.1761  -0.0758 19  ASP A CG  
133  O  OD1 . ASP A 19  ? 0.3112 0.3888 0.3373 -0.0620 0.1372  0.0270  19  ASP A OD1 
134  O  OD2 . ASP A 19  ? 0.5830 0.5233 0.6387 -0.0581 0.0935  -0.1694 19  ASP A OD2 
135  N  N   . PHE A 20  ? 0.0733 0.1454 0.1713 -0.0188 0.0069  -0.0154 20  PHE A N   
136  C  CA  . PHE A 20  ? 0.0872 0.1559 0.1882 0.0047  0.0049  -0.0201 20  PHE A CA  
137  C  C   . PHE A 20  ? 0.0798 0.1620 0.1832 -0.0156 0.0215  -0.0060 20  PHE A C   
138  O  O   . PHE A 20  ? 0.0954 0.1225 0.2294 -0.0149 0.0286  -0.0286 20  PHE A O   
139  C  CB  . PHE A 20  ? 0.1005 0.2313 0.2116 -0.0374 -0.0013 0.0018  20  PHE A CB  
140  C  CG  . PHE A 20  ? 0.0714 0.2065 0.2209 -0.0322 0.0081  0.0153  20  PHE A CG  
141  C  CD1 . PHE A 20  ? 0.1044 0.2324 0.2584 -0.0342 0.0002  0.0365  20  PHE A CD1 
142  C  CD2 . PHE A 20  ? 0.1304 0.2511 0.1907 -0.0421 0.0185  0.0154  20  PHE A CD2 
143  C  CE1 . PHE A 20  ? 0.1177 0.3189 0.2529 -0.0879 0.0385  0.0291  20  PHE A CE1 
144  C  CE2 . PHE A 20  ? 0.1186 0.2799 0.2008 -0.0326 0.0143  0.0144  20  PHE A CE2 
145  C  CZ  . PHE A 20  ? 0.1134 0.2755 0.2226 -0.0636 0.0334  0.0578  20  PHE A CZ  
146  N  N   . PRO A 21  ? 0.0974 0.1641 0.1936 -0.0291 0.0006  0.0108  21  PRO A N   
147  C  CA  . PRO A 21  ? 0.0793 0.1680 0.1886 -0.0293 -0.0228 -0.0041 21  PRO A CA  
148  C  C   . PRO A 21  ? 0.0908 0.1358 0.1936 -0.0304 -0.0203 -0.0117 21  PRO A C   
149  O  O   . PRO A 21  ? 0.1039 0.1476 0.2015 -0.0227 -0.0182 -0.0146 21  PRO A O   
150  C  CB  . PRO A 21  ? 0.0814 0.2341 0.2464 -0.0768 -0.0204 -0.0062 21  PRO A CB  
151  C  CG  . PRO A 21  ? 0.2759 0.2284 0.3086 -0.1108 -0.0873 0.0013  21  PRO A CG  
152  C  CD  . PRO A 21  ? 0.1182 0.2081 0.2464 -0.0656 -0.0055 0.0107  21  PRO A CD  
153  N  N   . ILE A 22  ? 0.0717 0.1336 0.2118 -0.0268 -0.0081 -0.0236 22  ILE A N   
154  C  CA  . ILE A 22  ? 0.0771 0.1160 0.2022 -0.0136 -0.0013 -0.0416 22  ILE A CA  
155  C  C   . ILE A 22  ? 0.0997 0.1160 0.1351 -0.0166 -0.0120 -0.0198 22  ILE A C   
156  O  O   . ILE A 22  ? 0.0900 0.1128 0.1695 0.0000  0.0089  -0.0194 22  ILE A O   
157  C  CB  . ILE A 22  ? 0.1063 0.1116 0.1759 -0.0115 0.0041  -0.0141 22  ILE A CB  
158  C  CG1 . ILE A 22  ? 0.1261 0.1641 0.1717 -0.0103 0.0134  -0.0510 22  ILE A CG1 
159  C  CG2 . ILE A 22  ? 0.0927 0.1631 0.1935 -0.0253 -0.0151 -0.0284 22  ILE A CG2 
160  C  CD1 . ILE A 22  ? 0.1724 0.2694 0.1983 -0.0129 -0.0083 -0.0794 22  ILE A CD1 
161  N  N   . ALA A 23  ? 0.0972 0.1142 0.1523 -0.0147 -0.0255 -0.0438 23  ALA A N   
162  C  CA  . ALA A 23  ? 0.1084 0.0951 0.1562 0.0022  0.0040  -0.0296 23  ALA A CA  
163  C  C   . ALA A 23  ? 0.0909 0.1196 0.1602 0.0053  -0.0040 -0.0215 23  ALA A C   
164  O  O   . ALA A 23  ? 0.1017 0.1137 0.1710 0.0071  0.0113  -0.0080 23  ALA A O   
165  C  CB  . ALA A 23  ? 0.0943 0.1289 0.1476 0.0229  0.0038  -0.0223 23  ALA A CB  
166  N  N   . LYS A 24  ? 0.1045 0.1497 0.1676 0.0256  -0.0252 -0.0207 24  LYS A N   
167  C  CA  . LYS A 24  ? 0.1097 0.1667 0.1789 0.0121  -0.0350 -0.0194 24  LYS A CA  
168  C  C   . LYS A 24  ? 0.1120 0.1749 0.1932 0.0105  -0.0269 -0.0369 24  LYS A C   
169  O  O   . LYS A 24  ? 0.1347 0.2169 0.1928 0.0027  -0.0068 -0.0100 24  LYS A O   
170  C  CB  . LYS A 24  ? 0.1074 0.2320 0.1850 0.0306  -0.0127 0.0110  24  LYS A CB  
171  C  CG  . LYS A 24  ? 0.1153 0.2330 0.2287 0.0308  0.0006  -0.0151 24  LYS A CG  
172  C  CD  . LYS A 24  ? 0.1199 0.3467 0.3553 0.0682  0.0094  0.0048  24  LYS A CD  
173  C  CE  . LYS A 24  ? 0.2634 0.3043 0.2612 0.0594  0.0268  0.0633  24  LYS A CE  
174  N  NZ  . LYS A 24  ? 0.3956 0.3010 0.3538 0.0609  0.0718  0.0413  24  LYS A NZ  
175  N  N   . GLY A 25  ? 0.1017 0.1534 0.2043 0.0157  0.0096  -0.0242 25  GLY A N   
176  C  CA  . GLY A 25  ? 0.0819 0.1907 0.1961 -0.0075 0.0063  -0.0444 25  GLY A CA  
177  C  C   . GLY A 25  ? 0.1268 0.1677 0.1250 -0.0021 -0.0282 -0.0080 25  GLY A C   
178  O  O   . GLY A 25  ? 0.1336 0.1685 0.1602 -0.0066 -0.0397 -0.0105 25  GLY A O   
179  N  N   . GLU A 26  ? 0.1080 0.2008 0.1307 -0.0219 -0.0347 -0.0494 26  GLU A N   
180  C  CA  . GLU A 26  ? 0.1155 0.2361 0.1415 -0.0293 -0.0139 -0.0587 26  GLU A CA  
181  C  C   . GLU A 26  ? 0.0976 0.1645 0.1394 0.0388  -0.0165 -0.0299 26  GLU A C   
182  O  O   . GLU A 26  ? 0.1487 0.2354 0.1119 0.0011  -0.0306 -0.0139 26  GLU A O   
183  C  CB  . GLU A 26  ? 0.1358 0.2755 0.1961 -0.0194 -0.0491 -0.1028 26  GLU A CB  
184  C  CG  . GLU A 26  ? 0.1322 0.3893 0.2319 0.0055  -0.0670 -0.0817 26  GLU A CG  
185  C  CD  . GLU A 26  ? 0.2294 0.4562 0.2213 0.0370  -0.0580 -0.0394 26  GLU A CD  
186  O  OE1 . GLU A 26  ? 0.3789 0.4166 0.3276 -0.0950 -0.0818 -0.0043 26  GLU A OE1 
187  O  OE2 . GLU A 26  ? 0.1886 0.5361 0.4600 0.0838  -0.0871 -0.0242 26  GLU A OE2 
188  N  N   . ARG A 27  ? 0.0934 0.1090 0.1333 0.0027  -0.0175 -0.0168 27  ARG A N   
189  C  CA  . ARG A 27  ? 0.0807 0.1443 0.0820 0.0114  -0.0029 -0.0006 27  ARG A CA  
190  C  C   . ARG A 27  ? 0.0917 0.1200 0.0909 0.0279  -0.0031 -0.0127 27  ARG A C   
191  O  O   . ARG A 27  ? 0.1003 0.0979 0.1163 0.0013  -0.0255 0.0000  27  ARG A O   
192  C  CB  . ARG A 27  ? 0.1638 0.1602 0.1487 0.0455  -0.0284 -0.0300 27  ARG A CB  
193  C  CG  . ARG A 27  ? 0.2162 0.2258 0.1491 0.0369  -0.0270 -0.0055 27  ARG A CG  
194  C  CD  . ARG A 27  ? 0.1580 0.2565 0.3183 0.0408  -0.0144 -0.0190 27  ARG A CD  
195  N  NE  . ARG A 27  ? 0.2159 0.1832 0.2281 0.0116  0.0095  0.0179  27  ARG A NE  
196  C  CZ  . ARG A 27  ? 0.1976 0.1121 0.1544 0.0079  0.0133  -0.0316 27  ARG A CZ  
197  N  NH1 . ARG A 27  ? 0.1100 0.1879 0.1964 0.0236  -0.0049 -0.1372 27  ARG A NH1 
198  N  NH2 . ARG A 27  ? 0.1351 0.1681 0.2661 -0.0540 0.0157  -0.0878 27  ARG A NH2 
199  N  N   . GLN A 28  ? 0.0729 0.0920 0.1005 -0.0049 -0.0065 -0.0253 28  GLN A N   
200  C  CA  . GLN A 28  ? 0.0557 0.1097 0.1047 0.0065  -0.0135 -0.0299 28  GLN A CA  
201  C  C   . GLN A 28  ? 0.0900 0.0539 0.1002 0.0071  -0.0173 -0.0097 28  GLN A C   
202  O  O   . GLN A 28  ? 0.1133 0.0911 0.0832 0.0027  -0.0096 -0.0081 28  GLN A O   
203  C  CB  . GLN A 28  ? 0.0480 0.1011 0.1317 -0.0033 -0.0091 -0.0297 28  GLN A CB  
204  C  CG  . GLN A 28  ? 0.0863 0.0708 0.1232 -0.0082 -0.0250 -0.0197 28  GLN A CG  
205  C  CD  . GLN A 28  ? 0.0827 0.0947 0.1182 0.0053  -0.0017 -0.0162 28  GLN A CD  
206  O  OE1 . GLN A 28  ? 0.0902 0.1046 0.1160 -0.0073 0.0011  -0.0149 28  GLN A OE1 
207  N  NE2 . GLN A 28  ? 0.0747 0.0847 0.1444 -0.0047 -0.0136 -0.0291 28  GLN A NE2 
208  N  N   . SER A 29  ? 0.0593 0.0857 0.0908 0.0005  -0.0055 0.0027  29  SER A N   
209  C  CA  . SER A 29  ? 0.0600 0.0641 0.0881 0.0111  -0.0061 -0.0053 29  SER A CA  
210  C  C   . SER A 29  ? 0.0726 0.0662 0.1116 0.0127  0.0076  -0.0150 29  SER A C   
211  O  O   . SER A 29  ? 0.0741 0.0807 0.1168 0.0099  0.0039  0.0012  29  SER A O   
212  C  CB  . SER A 29  ? 0.0699 0.0671 0.1073 0.0214  -0.0128 -0.0122 29  SER A CB  
213  O  OG  . SER A 29  ? 0.0817 0.0540 0.1072 0.0105  -0.0097 -0.0212 29  SER A OG  
214  N  N   . PRO A 30  ? 0.0662 0.0595 0.1033 0.0107  0.0122  -0.0070 30  PRO A N   
215  C  CA  . PRO A 30  ? 0.0868 0.0717 0.0681 -0.0116 0.0032  -0.0061 30  PRO A CA  
216  C  C   . PRO A 30  ? 0.0762 0.0607 0.0927 0.0165  -0.0057 -0.0072 30  PRO A C   
217  O  O   . PRO A 30  ? 0.0845 0.0981 0.1023 0.0166  -0.0207 0.0046  30  PRO A O   
218  C  CB  . PRO A 30  ? 0.0765 0.0617 0.0985 0.0024  0.0033  -0.0253 30  PRO A CB  
219  C  CG  . PRO A 30  ? 0.0606 0.0730 0.1093 -0.0083 0.0032  -0.0073 30  PRO A CG  
220  C  CD  . PRO A 30  ? 0.0920 0.0559 0.0830 -0.0095 0.0155  -0.0085 30  PRO A CD  
221  N  N   . VAL A 31  ? 0.1072 0.0643 0.0807 0.0122  0.0091  0.0013  31  VAL A N   
222  C  CA  . VAL A 31  ? 0.1002 0.0690 0.0926 -0.0076 -0.0060 0.0159  31  VAL A CA  
223  C  C   . VAL A 31  ? 0.0929 0.0627 0.0891 0.0033  0.0062  0.0105  31  VAL A C   
224  O  O   . VAL A 31  ? 0.0934 0.0891 0.1076 -0.0068 0.0032  0.0348  31  VAL A O   
225  C  CB  . VAL A 31  ? 0.0944 0.0864 0.0961 -0.0039 -0.0107 0.0070  31  VAL A CB  
226  C  CG1 . VAL A 31  ? 0.1185 0.1058 0.1142 -0.0317 -0.0023 -0.0005 31  VAL A CG1 
227  C  CG2 . VAL A 31  ? 0.1117 0.0893 0.1134 0.0321  -0.0023 -0.0033 31  VAL A CG2 
228  N  N   . ASP A 32  ? 0.0952 0.0663 0.1142 0.0157  0.0036  0.0263  32  ASP A N   
229  C  CA  . ASP A 32  ? 0.0932 0.0814 0.1300 0.0217  0.0137  0.0306  32  ASP A CA  
230  C  C   . ASP A 32  ? 0.1054 0.0557 0.1182 0.0157  0.0096  0.0086  32  ASP A C   
231  O  O   . ASP A 32  ? 0.1120 0.1101 0.1437 -0.0047 -0.0031 -0.0085 32  ASP A O   
232  C  CB  . ASP A 32  ? 0.1109 0.0838 0.1336 0.0223  -0.0135 0.0279  32  ASP A CB  
233  C  CG  . ASP A 32  ? 0.1271 0.1048 0.1440 0.0015  -0.0245 0.0133  32  ASP A CG  
234  O  OD1 . ASP A 32  ? 0.1451 0.0817 0.1216 -0.0039 -0.0238 0.0223  32  ASP A OD1 
235  O  OD2 . ASP A 32  ? 0.1749 0.1527 0.1415 -0.0015 -0.0083 0.0336  32  ASP A OD2 
236  N  N   . ILE A 33  ? 0.1073 0.0918 0.1051 0.0128  0.0000  0.0055  33  ILE A N   
237  C  CA  . ILE A 33  ? 0.1081 0.1232 0.1365 0.0321  0.0154  0.0447  33  ILE A CA  
238  C  C   . ILE A 33  ? 0.1346 0.1146 0.1250 0.0212  0.0005  0.0376  33  ILE A C   
239  O  O   . ILE A 33  ? 0.1516 0.1171 0.1652 0.0016  -0.0054 0.0509  33  ILE A O   
240  C  CB  . ILE A 33  ? 0.1142 0.1051 0.1178 0.0216  0.0231  0.0456  33  ILE A CB  
241  C  CG1 . ILE A 33  ? 0.1523 0.0935 0.1275 0.0000  -0.0073 0.0452  33  ILE A CG1 
242  C  CG2 . ILE A 33  ? 0.1286 0.1346 0.1408 0.0356  0.0447  0.0476  33  ILE A CG2 
243  C  CD1 . ILE A 33  ? 0.1357 0.1415 0.1480 0.0022  -0.0204 0.0313  33  ILE A CD1 
244  N  N   A ASP A 34  ? 0.1469 0.1239 0.1054 0.0122  0.0155  0.0730  34  ASP A N   
245  N  N   B ASP A 34  ? 0.1505 0.1111 0.1084 0.0130  0.0114  0.0571  34  ASP A N   
246  C  CA  A ASP A 34  ? 0.1882 0.1404 0.1325 0.0505  0.0167  0.1112  34  ASP A CA  
247  C  CA  B ASP A 34  ? 0.1738 0.1289 0.1209 0.0650  0.0100  0.0965  34  ASP A CA  
248  C  C   A ASP A 34  ? 0.1917 0.1473 0.1638 0.0469  0.0185  0.0912  34  ASP A C   
249  C  C   B ASP A 34  ? 0.1759 0.1487 0.1573 0.0497  0.0187  0.0890  34  ASP A C   
250  O  O   A ASP A 34  ? 0.2305 0.2015 0.1638 0.0625  0.0486  0.0649  34  ASP A O   
251  O  O   B ASP A 34  ? 0.2177 0.1983 0.1275 0.0306  0.0274  0.0655  34  ASP A O   
252  C  CB  A ASP A 34  ? 0.1264 0.1907 0.1893 0.0399  0.0240  0.0309  34  ASP A CB  
253  C  CB  B ASP A 34  ? 0.1767 0.2004 0.1595 0.0564  -0.0054 0.0170  34  ASP A CB  
254  C  CG  A ASP A 34  ? 0.1861 0.2277 0.1645 0.0093  -0.0066 0.0495  34  ASP A CG  
255  C  CG  B ASP A 34  ? 0.1623 0.2302 0.1954 0.0746  0.0456  0.0477  34  ASP A CG  
256  O  OD1 A ASP A 34  ? 0.1832 0.1997 0.1623 0.0204  0.0120  0.1175  34  ASP A OD1 
257  O  OD1 B ASP A 34  ? 0.2377 0.1828 0.2442 0.1011  0.0669  0.1066  34  ASP A OD1 
258  O  OD2 A ASP A 34  ? 0.2910 0.3013 0.1563 0.0154  -0.0230 0.2074  34  ASP A OD2 
259  O  OD2 B ASP A 34  ? 0.2687 0.2173 0.1400 0.0148  0.0607  0.0709  34  ASP A OD2 
260  N  N   . THR A 35  ? 0.1491 0.1904 0.1832 0.0435  0.0463  0.1004  35  THR A N   
261  C  CA  . THR A 35  ? 0.1516 0.2300 0.1692 0.0652  0.0551  0.0702  35  THR A CA  
262  C  C   . THR A 35  ? 0.2058 0.1846 0.1605 0.0381  0.0543  0.0602  35  THR A C   
263  O  O   . THR A 35  ? 0.2266 0.2463 0.2722 0.0634  0.0724  0.0329  35  THR A O   
264  C  CB  . THR A 35  ? 0.2259 0.2658 0.2216 0.0271  0.0016  0.1062  35  THR A CB  
265  O  OG1 . THR A 35  ? 0.1904 0.2759 0.2541 -0.0127 0.0388  0.1384  35  THR A OG1 
266  C  CG2 . THR A 35  ? 0.1846 0.3774 0.2306 0.0950  0.0023  0.0985  35  THR A CG2 
267  N  N   . HIS A 36  ? 0.2613 0.2015 0.2101 0.0630  0.0702  0.0870  36  HIS A N   
268  C  CA  . HIS A 36  ? 0.3528 0.1742 0.2137 0.0804  0.0597  0.1166  36  HIS A CA  
269  C  C   . HIS A 36  ? 0.3272 0.3398 0.1652 0.0348  0.0763  0.0456  36  HIS A C   
270  O  O   . HIS A 36  ? 0.6706 0.4001 0.1932 0.0021  0.2112  0.0390  36  HIS A O   
271  C  CB  . HIS A 36  ? 0.3685 0.2042 0.1447 0.0809  0.0743  0.1653  36  HIS A CB  
272  C  CG  . HIS A 36  ? 0.4765 0.2921 0.1148 0.1302  -0.0203 0.1110  36  HIS A CG  
273  N  ND1 . HIS A 36  ? 0.5001 0.3208 0.2352 0.1483  -0.0114 0.0636  36  HIS A ND1 
274  C  CD2 . HIS A 36  ? 0.5777 0.2392 0.1286 -0.0211 -0.1210 0.1155  36  HIS A CD2 
275  C  CE1 . HIS A 36  ? 0.4670 0.2626 0.2273 0.1177  -0.0738 0.0457  36  HIS A CE1 
276  N  NE2 . HIS A 36  ? 0.5469 0.3017 0.1753 0.1155  -0.0106 0.0396  36  HIS A NE2 
277  N  N   . THR A 37  ? 0.2623 0.1879 0.2514 0.1271  0.0956  0.0715  37  THR A N   
278  C  CA  . THR A 37  ? 0.3445 0.2026 0.2166 0.0779  -0.0052 0.1059  37  THR A CA  
279  C  C   . THR A 37  ? 0.2716 0.1806 0.1853 0.0567  -0.0008 0.0809  37  THR A C   
280  O  O   . THR A 37  ? 0.4116 0.2605 0.2265 0.0728  -0.0625 0.0304  37  THR A O   
281  C  CB  . THR A 37  ? 0.3628 0.3510 0.2577 0.1309  -0.0138 0.1508  37  THR A CB  
282  O  OG1 . THR A 37  ? 0.4234 0.4618 0.3462 0.0891  0.0729  0.1315  37  THR A OG1 
283  C  CG2 . THR A 37  ? 0.2895 0.2212 0.3345 0.1345  0.0485  0.0458  37  THR A CG2 
284  N  N   . ALA A 38  ? 0.2691 0.1856 0.1419 0.0725  0.0495  0.0664  38  ALA A N   
285  C  CA  . ALA A 38  ? 0.2663 0.2087 0.1304 0.1163  0.0486  0.0497  38  ALA A CA  
286  C  C   . ALA A 38  ? 0.2554 0.1875 0.2187 0.0790  0.0844  0.0521  38  ALA A C   
287  O  O   . ALA A 38  ? 0.3331 0.2337 0.3724 0.0632  0.1928  0.0456  38  ALA A O   
288  C  CB  . ALA A 38  ? 0.2356 0.1997 0.1448 0.0987  0.0348  0.0395  38  ALA A CB  
289  N  N   A LYS A 39  ? 0.2965 0.2324 0.1631 0.1168  0.0052  -0.0278 39  LYS A N   
290  N  N   B LYS A 39  ? 0.2903 0.1850 0.1314 0.1054  -0.0044 0.0656  39  LYS A N   
291  C  CA  A LYS A 39  ? 0.2669 0.2564 0.1432 0.1298  -0.0177 -0.0171 39  LYS A CA  
292  C  CA  B LYS A 39  ? 0.2651 0.2421 0.1357 0.1126  -0.0319 0.0228  39  LYS A CA  
293  C  C   A LYS A 39  ? 0.2230 0.2073 0.0988 0.0619  -0.0087 0.0185  39  LYS A C   
294  C  C   B LYS A 39  ? 0.2090 0.2051 0.1111 0.0568  -0.0307 0.0251  39  LYS A C   
295  O  O   A LYS A 39  ? 0.1724 0.2180 0.0900 0.0544  0.0027  0.0192  39  LYS A O   
296  O  O   B LYS A 39  ? 0.1555 0.2159 0.1056 0.0491  0.0048  0.0199  39  LYS A O   
297  C  CB  A LYS A 39  ? 0.3237 0.3082 0.1142 0.1144  -0.0430 -0.0173 39  LYS A CB  
298  C  CB  B LYS A 39  ? 0.2681 0.3141 0.1408 0.1274  -0.0483 -0.0018 39  LYS A CB  
299  C  CG  A LYS A 39  ? 0.3327 0.3516 0.1189 0.0822  0.0190  -0.0249 39  LYS A CG  
300  C  CG  B LYS A 39  ? 0.2069 0.2446 0.1943 0.1620  -0.0550 -0.0345 39  LYS A CG  
301  C  CD  A LYS A 39  ? 0.3371 0.2956 0.1784 -0.0002 0.0061  0.0305  39  LYS A CD  
302  C  CD  B LYS A 39  ? 0.2072 0.2900 0.2367 0.1184  -0.0670 -0.0587 39  LYS A CD  
303  C  CE  A LYS A 39  ? 0.4343 0.3980 0.1076 -0.0077 -0.0106 -0.0430 39  LYS A CE  
304  C  CE  B LYS A 39  ? 0.2450 0.3365 0.1695 0.1405  -0.0776 -0.1101 39  LYS A CE  
305  N  NZ  A LYS A 39  ? 0.2662 0.4892 0.2137 0.0858  0.0905  0.0198  39  LYS A NZ  
306  N  NZ  B LYS A 39  ? 0.2248 0.3190 0.2407 0.0403  -0.1147 -0.0921 39  LYS A NZ  
307  N  N   . TYR A 40  ? 0.2691 0.2122 0.1101 0.0309  0.0310  0.0060  40  TYR A N   
308  C  CA  . TYR A 40  ? 0.2270 0.2044 0.1429 -0.0222 0.0206  -0.0192 40  TYR A CA  
309  C  C   . TYR A 40  ? 0.1874 0.2162 0.1275 -0.0160 0.0399  -0.0238 40  TYR A C   
310  O  O   . TYR A 40  ? 0.2198 0.2978 0.1135 0.0702  0.0386  -0.0044 40  TYR A O   
311  C  CB  . TYR A 40  ? 0.2838 0.2867 0.1825 -0.0556 0.0583  0.0406  40  TYR A CB  
312  C  CG  . TYR A 40  ? 0.2431 0.4295 0.1792 -0.0925 0.0757  0.0316  40  TYR A CG  
313  C  CD1 . TYR A 40  ? 0.2816 0.3894 0.1530 -0.0037 0.0656  -0.0130 40  TYR A CD1 
314  C  CD2 . TYR A 40  ? 0.3212 0.5412 0.2061 0.0226  0.1013  0.0102  40  TYR A CD2 
315  C  CE1 . TYR A 40  ? 0.1911 0.6429 0.1469 -0.0330 0.0381  0.0115  40  TYR A CE1 
316  C  CE2 . TYR A 40  ? 0.3590 0.5722 0.2212 0.0534  0.0357  0.0011  40  TYR A CE2 
317  C  CZ  . TYR A 40  ? 0.2088 0.6415 0.2090 0.0131  0.0746  -0.0058 40  TYR A CZ  
318  O  OH  . TYR A 40  ? 0.2432 0.7712 0.3280 0.0685  0.0230  -0.0607 40  TYR A OH  
319  N  N   . ASP A 41  ? 0.1674 0.2144 0.1479 0.0362  0.0353  -0.0329 41  ASP A N   
320  C  CA  . ASP A 41  ? 0.2241 0.2063 0.1160 0.0491  -0.0032 -0.0117 41  ASP A CA  
321  C  C   . ASP A 41  ? 0.2709 0.3470 0.1723 0.1113  0.0055  -0.0073 41  ASP A C   
322  O  O   . ASP A 41  ? 0.2356 0.3388 0.2043 0.1035  -0.0070 0.0263  41  ASP A O   
323  C  CB  . ASP A 41  ? 0.2166 0.2396 0.1947 0.0411  -0.0086 0.0474  41  ASP A CB  
324  C  CG  . ASP A 41  ? 0.3290 0.3079 0.2753 0.0446  -0.0297 -0.0337 41  ASP A CG  
325  O  OD1 . ASP A 41  ? 0.4112 0.2856 0.2518 0.1456  -0.0618 -0.0741 41  ASP A OD1 
326  O  OD2 . ASP A 41  ? 0.4392 0.2870 0.3111 -0.0221 -0.1039 0.0153  41  ASP A OD2 
327  N  N   . PRO A 42  ? 0.3015 0.4801 0.1386 0.1962  0.0159  0.0120  42  PRO A N   
328  C  CA  . PRO A 42  ? 0.2975 0.5643 0.2142 0.2249  0.0911  -0.0048 42  PRO A CA  
329  C  C   . PRO A 42  ? 0.3534 0.5778 0.1749 0.1593  0.1154  0.0357  42  PRO A C   
330  O  O   . PRO A 42  ? 0.3987 0.6712 0.3180 0.1899  0.0405  0.1178  42  PRO A O   
331  C  CB  . PRO A 42  ? 0.4756 0.8499 0.1940 0.1882  0.0959  0.0793  42  PRO A CB  
332  C  CG  . PRO A 42  ? 0.4002 0.6501 0.4104 0.2702  0.0523  -0.0787 42  PRO A CG  
333  C  CD  . PRO A 42  ? 0.3753 0.3930 0.1390 0.1515  0.0482  0.0453  42  PRO A CD  
334  N  N   . SER A 43  ? 0.3879 0.3359 0.1606 0.1988  0.0259  -0.0521 43  SER A N   
335  C  CA  . SER A 43  ? 0.5593 0.3237 0.2526 0.1570  -0.0408 -0.0592 43  SER A CA  
336  C  C   . SER A 43  ? 0.3324 0.3930 0.2997 0.3012  0.0583  0.0044  43  SER A C   
337  O  O   . SER A 43  ? 0.6225 0.4091 0.3061 0.2482  -0.0565 -0.0446 43  SER A O   
338  C  CB  . SER A 43  ? 0.4952 0.4031 0.3944 0.1361  -0.0974 -0.0513 43  SER A CB  
339  O  OG  . SER A 43  ? 0.5554 0.3882 0.2522 -0.0065 -0.0099 -0.0427 43  SER A OG  
340  N  N   . LEU A 44  ? 0.3130 0.3753 0.1997 0.1682  -0.0071 -0.0226 44  LEU A N   
341  C  CA  . LEU A 44  ? 0.2335 0.4138 0.2026 0.0712  -0.0261 -0.0022 44  LEU A CA  
342  C  C   . LEU A 44  ? 0.2557 0.5377 0.1990 0.0355  -0.0370 0.0894  44  LEU A C   
343  O  O   . LEU A 44  ? 0.2234 0.7271 0.2742 0.0146  0.0207  0.1659  44  LEU A O   
344  C  CB  . LEU A 44  ? 0.2100 0.4081 0.1598 -0.0231 -0.0275 -0.0410 44  LEU A CB  
345  C  CG  . LEU A 44  ? 0.1989 0.2428 0.1728 -0.0274 0.0189  -0.0030 44  LEU A CG  
346  C  CD1 . LEU A 44  ? 0.2482 0.2579 0.1694 -0.0521 0.0259  -0.0212 44  LEU A CD1 
347  C  CD2 . LEU A 44  ? 0.2410 0.1889 0.1950 -0.0254 -0.0140 0.0124  44  LEU A CD2 
348  N  N   . LYS A 45  ? 0.2554 0.4652 0.1882 0.0751  -0.0376 0.0577  45  LYS A N   
349  C  CA  . LYS A 45  ? 0.2595 0.3032 0.4349 0.0423  -0.1384 -0.0782 45  LYS A CA  
350  C  C   . LYS A 45  ? 0.2496 0.2986 0.2522 0.1090  -0.0416 0.0617  45  LYS A C   
351  O  O   . LYS A 45  ? 0.2148 0.3189 0.3080 -0.0392 0.0739  -0.0592 45  LYS A O   
352  C  CB  . LYS A 45  ? 0.2910 0.3567 0.2620 0.1720  0.1411  0.0008  45  LYS A CB  
353  C  CG  . LYS A 45  ? 0.3180 0.4701 0.3337 -0.0181 0.0087  -0.0688 45  LYS A CG  
354  C  CD  . LYS A 45  ? 0.3445 0.4929 0.5618 -0.0971 -0.0890 -0.0303 45  LYS A CD  
355  C  CE  . LYS A 45  ? 0.4801 0.4972 0.8177 -0.0351 -0.2540 -0.1473 45  LYS A CE  
356  N  N   . PRO A 46  ? 0.2460 0.3140 0.2384 -0.0502 -0.0092 -0.0089 46  PRO A N   
357  C  CA  . PRO A 46  ? 0.1548 0.3132 0.1979 -0.0204 0.0232  0.0255  46  PRO A CA  
358  C  C   . PRO A 46  ? 0.1282 0.2692 0.1950 0.0218  0.0270  0.0290  46  PRO A C   
359  O  O   . PRO A 46  ? 0.1340 0.3028 0.2468 -0.0374 -0.0085 0.0673  46  PRO A O   
360  C  CB  . PRO A 46  ? 0.1444 0.4040 0.2730 0.0022  0.0333  0.0034  46  PRO A CB  
361  C  CG  . PRO A 46  ? 0.2201 0.5434 0.3118 -0.0670 0.0913  -0.0834 46  PRO A CG  
362  C  CD  . PRO A 46  ? 0.2431 0.3662 0.3406 0.1000  -0.0464 -0.0890 46  PRO A CD  
363  N  N   . LEU A 47  ? 0.2191 0.2338 0.2620 0.0233  -0.0154 0.0009  47  LEU A N   
364  C  CA  . LEU A 47  ? 0.0908 0.2960 0.3136 -0.0564 -0.0677 0.0749  47  LEU A CA  
365  C  C   . LEU A 47  ? 0.1455 0.1789 0.2665 -0.0723 -0.0851 0.0670  47  LEU A C   
366  O  O   . LEU A 47  ? 0.1164 0.2511 0.3449 -0.0759 -0.0644 0.1240  47  LEU A O   
367  C  CB  . LEU A 47  ? 0.3310 0.2852 0.4410 0.0166  -0.0549 0.1035  47  LEU A CB  
368  C  CG  . LEU A 47  ? 0.3233 0.3959 0.5655 0.0873  -0.0592 0.0294  47  LEU A CG  
369  C  CD1 . LEU A 47  ? 0.2180 0.3028 0.6030 0.0531  -0.0287 0.0189  47  LEU A CD1 
370  C  CD2 . LEU A 47  ? 0.4715 0.2248 0.7185 0.0374  -0.0952 0.1119  47  LEU A CD2 
371  N  N   . SER A 48  ? 0.0821 0.1527 0.2356 -0.0096 -0.0174 0.0488  48  SER A N   
372  C  CA  . SER A 48  ? 0.0791 0.1656 0.1843 -0.0018 -0.0043 -0.0018 48  SER A CA  
373  C  C   . SER A 48  ? 0.1073 0.1469 0.1864 -0.0381 0.0117  0.0164  48  SER A C   
374  O  O   . SER A 48  ? 0.1253 0.1685 0.2063 -0.0596 0.0354  -0.0103 48  SER A O   
375  C  CB  . SER A 48  ? 0.1119 0.1634 0.2367 0.0217  -0.0054 0.0118  48  SER A CB  
376  O  OG  . SER A 48  ? 0.1882 0.2226 0.3154 0.0341  -0.0316 0.0487  48  SER A OG  
377  N  N   . VAL A 49  ? 0.1680 0.1677 0.1670 -0.0147 0.0209  0.0018  49  VAL A N   
378  C  CA  . VAL A 49  ? 0.1494 0.1807 0.1781 -0.0640 0.0165  -0.0472 49  VAL A CA  
379  C  C   . VAL A 49  ? 0.1620 0.2037 0.2324 -0.0869 -0.0119 -0.0082 49  VAL A C   
380  O  O   . VAL A 49  ? 0.2111 0.3161 0.2511 -0.1668 -0.0076 -0.0030 49  VAL A O   
381  C  CB  . VAL A 49  ? 0.2561 0.1879 0.2208 -0.0526 0.0239  -0.0590 49  VAL A CB  
382  C  CG1 . VAL A 49  ? 0.3901 0.2878 0.2724 -0.1009 0.1139  -0.0583 49  VAL A CG1 
383  C  CG2 . VAL A 49  ? 0.1530 0.1796 0.3256 -0.0514 0.0452  -0.0029 49  VAL A CG2 
384  N  N   . SER A 50  ? 0.1433 0.1882 0.2136 -0.0425 0.0006  0.0030  50  SER A N   
385  C  CA  . SER A 50  ? 0.1242 0.1918 0.2281 -0.0103 0.0145  -0.0296 50  SER A CA  
386  C  C   . SER A 50  ? 0.1060 0.1419 0.2213 -0.0144 0.0016  -0.0078 50  SER A C   
387  O  O   . SER A 50  ? 0.1159 0.1741 0.2119 -0.0359 -0.0001 0.0219  50  SER A O   
388  C  CB  . SER A 50  ? 0.2274 0.2112 0.3028 -0.0274 0.0754  -0.0563 50  SER A CB  
389  O  OG  . SER A 50  ? 0.2590 0.3908 0.3186 0.0151  0.0717  -0.0115 50  SER A OG  
390  N  N   . TYR A 51  ? 0.1580 0.1527 0.2032 0.0034  -0.0060 -0.0305 51  TYR A N   
391  C  CA  . TYR A 51  ? 0.1021 0.1791 0.2061 0.0109  -0.0100 0.0279  51  TYR A CA  
392  C  C   . TYR A 51  ? 0.1368 0.2001 0.2216 0.0083  -0.0293 0.0617  51  TYR A C   
393  O  O   . TYR A 51  ? 0.1889 0.2213 0.2259 0.0077  -0.0383 0.0277  51  TYR A O   
394  C  CB  . TYR A 51  ? 0.1207 0.1637 0.1839 0.0113  -0.0282 -0.0079 51  TYR A CB  
395  C  CG  . TYR A 51  ? 0.0990 0.1333 0.1997 -0.0062 -0.0139 0.0030  51  TYR A CG  
396  C  CD1 . TYR A 51  ? 0.1311 0.1218 0.2011 -0.0050 -0.0053 0.0020  51  TYR A CD1 
397  C  CD2 . TYR A 51  ? 0.1112 0.1386 0.1516 0.0039  0.0144  -0.0052 51  TYR A CD2 
398  C  CE1 . TYR A 51  ? 0.1234 0.1092 0.1925 0.0128  0.0148  0.0074  51  TYR A CE1 
399  C  CE2 . TYR A 51  ? 0.1433 0.1157 0.1562 -0.0502 -0.0272 0.0254  51  TYR A CE2 
400  C  CZ  . TYR A 51  ? 0.1103 0.0961 0.1394 -0.0117 -0.0095 0.0051  51  TYR A CZ  
401  O  OH  . TYR A 51  ? 0.1164 0.1110 0.1713 -0.0042 -0.0211 -0.0055 51  TYR A OH  
402  N  N   A ASP A 52  ? 0.1433 0.2595 0.2222 0.0055  0.0108  0.0273  52  ASP A N   
403  N  N   B ASP A 52  ? 0.1322 0.2684 0.2342 0.0050  -0.0067 0.0416  52  ASP A N   
404  C  CA  A ASP A 52  ? 0.1343 0.2903 0.2521 0.0143  0.0160  0.0559  52  ASP A CA  
405  C  CA  B ASP A 52  ? 0.1759 0.2913 0.2579 0.0129  -0.0220 0.0892  52  ASP A CA  
406  C  C   A ASP A 52  ? 0.1666 0.2301 0.2637 0.0286  0.0145  0.0358  52  ASP A C   
407  C  C   B ASP A 52  ? 0.1706 0.2373 0.2773 0.0199  -0.0058 0.0604  52  ASP A C   
408  O  O   A ASP A 52  ? 0.2848 0.3061 0.2655 0.0845  0.0008  0.0328  52  ASP A O   
409  O  O   B ASP A 52  ? 0.2239 0.3516 0.2967 0.0686  -0.0427 0.0585  52  ASP A O   
410  C  CB  A ASP A 52  ? 0.1552 0.3347 0.2989 0.0528  0.0151  -0.0105 52  ASP A CB  
411  C  CB  B ASP A 52  ? 0.1870 0.3825 0.3545 0.0449  -0.0230 0.0615  52  ASP A CB  
412  C  CG  A ASP A 52  ? 0.0996 0.3107 0.4196 0.0336  0.1277  -0.0607 52  ASP A CG  
413  C  CG  B ASP A 52  ? 0.2435 0.4734 0.4051 -0.0187 -0.0824 0.0979  52  ASP A CG  
414  O  OD1 A ASP A 52  ? 0.1850 0.2884 0.4787 -0.0023 0.1370  -0.0306 52  ASP A OD1 
415  O  OD1 B ASP A 52  ? 0.3726 0.4588 0.4227 0.0741  0.0129  0.0251  52  ASP A OD1 
416  O  OD2 A ASP A 52  ? 0.2216 0.3521 0.5345 -0.0061 -0.0249 0.0219  52  ASP A OD2 
417  O  OD2 B ASP A 52  ? 0.4144 0.4577 0.5349 0.0310  0.0500  0.0921  52  ASP A OD2 
418  N  N   . GLN A 53  ? 0.1230 0.2564 0.3222 0.0223  0.0234  0.0523  53  GLN A N   
419  C  CA  . GLN A 53  ? 0.1932 0.2547 0.4106 -0.0119 0.0502  0.0675  53  GLN A CA  
420  C  C   . GLN A 53  ? 0.1990 0.1825 0.3098 0.0331  0.0297  0.0201  53  GLN A C   
421  O  O   . GLN A 53  ? 0.1982 0.2047 0.3031 0.0049  0.0184  0.0244  53  GLN A O   
422  C  CB  . GLN A 53  ? 0.2877 0.2522 0.6151 0.0857  0.0765  0.1037  53  GLN A CB  
423  C  CG  . GLN A 53  ? 0.3079 0.4306 0.5966 0.0950  0.1798  0.1634  53  GLN A CG  
424  C  CD  . GLN A 53  ? 0.6812 0.7185 0.5632 -0.0049 0.0591  0.1021  53  GLN A CD  
425  O  OE1 . GLN A 53  ? 0.7940 0.9190 0.7310 -0.0596 -0.3190 0.3244  53  GLN A OE1 
426  N  NE2 . GLN A 53  ? 0.5856 0.6968 0.8838 -0.0353 0.1125  0.1815  53  GLN A NE2 
427  N  N   . ALA A 54  ? 0.1433 0.1462 0.3337 -0.0069 0.0247  -0.0164 54  ALA A N   
428  C  CA  . ALA A 54  ? 0.1358 0.1432 0.2230 -0.0023 0.0109  -0.0211 54  ALA A CA  
429  C  C   . ALA A 54  ? 0.1753 0.1921 0.2142 -0.0048 0.0195  -0.0690 54  ALA A C   
430  O  O   . ALA A 54  ? 0.1911 0.2727 0.2814 -0.0391 -0.0027 -0.1126 54  ALA A O   
431  C  CB  . ALA A 54  ? 0.1591 0.1247 0.2852 -0.0027 0.0364  -0.0080 54  ALA A CB  
432  N  N   . THR A 55  ? 0.1347 0.1329 0.2324 0.0345  0.0179  0.0160  55  THR A N   
433  C  CA  . THR A 55  ? 0.1433 0.1329 0.2360 0.0093  -0.0076 0.0433  55  THR A CA  
434  C  C   . THR A 55  ? 0.1232 0.1146 0.1317 -0.0105 -0.0269 0.0161  55  THR A C   
435  O  O   . THR A 55  ? 0.1232 0.0935 0.1674 -0.0049 -0.0168 0.0309  55  THR A O   
436  C  CB  . THR A 55  ? 0.2284 0.1164 0.3304 0.0374  -0.0051 0.0132  55  THR A CB  
437  O  OG1 . THR A 55  ? 0.2446 0.1990 0.4713 0.0829  -0.0836 -0.0218 55  THR A OG1 
438  C  CG2 . THR A 55  ? 0.3182 0.2306 0.3456 0.0358  -0.0872 0.1276  55  THR A CG2 
439  N  N   . SER A 56  ? 0.1297 0.1030 0.1419 0.0271  -0.0229 0.0298  56  SER A N   
440  C  CA  . SER A 56  ? 0.1289 0.0853 0.1173 -0.0044 0.0084  0.0086  56  SER A CA  
441  C  C   . SER A 56  ? 0.1566 0.0986 0.1462 0.0025  -0.0026 0.0394  56  SER A C   
442  O  O   . SER A 56  ? 0.1785 0.0983 0.1562 0.0084  -0.0275 0.0509  56  SER A O   
443  C  CB  . SER A 56  ? 0.1795 0.0886 0.1404 -0.0203 -0.0514 0.0086  56  SER A CB  
444  O  OG  . SER A 56  ? 0.1573 0.1279 0.1450 -0.0177 -0.0514 0.0392  56  SER A OG  
445  N  N   . LEU A 57  ? 0.1404 0.0782 0.1351 0.0046  0.0019  0.0206  57  LEU A N   
446  C  CA  . LEU A 57  ? 0.1613 0.0900 0.1620 -0.0135 0.0151  0.0252  57  LEU A CA  
447  C  C   . LEU A 57  ? 0.1315 0.1407 0.1415 0.0238  0.0009  0.0348  57  LEU A C   
448  O  O   . LEU A 57  ? 0.1731 0.1253 0.1476 0.0248  -0.0249 0.0185  57  LEU A O   
449  C  CB  . LEU A 57  ? 0.1767 0.0881 0.2205 -0.0161 0.0232  0.0013  57  LEU A CB  
450  C  CG  . LEU A 57  ? 0.1958 0.1150 0.2166 0.0204  0.0154  0.0086  57  LEU A CG  
451  C  CD1 . LEU A 57  ? 0.2904 0.1408 0.3128 -0.0567 0.0177  0.0061  57  LEU A CD1 
452  C  CD2 . LEU A 57  ? 0.2860 0.1784 0.2996 0.0462  -0.0460 0.0230  57  LEU A CD2 
453  N  N   . ARG A 58  ? 0.1168 0.1196 0.1483 0.0044  -0.0243 0.0184  58  ARG A N   
454  C  CA  . ARG A 58  ? 0.1372 0.0970 0.1448 0.0221  -0.0026 0.0384  58  ARG A CA  
455  C  C   . ARG A 58  ? 0.1340 0.0979 0.1085 0.0226  -0.0144 0.0146  58  ARG A C   
456  O  O   . ARG A 58  ? 0.1759 0.1168 0.1028 0.0325  -0.0078 0.0001  58  ARG A O   
457  C  CB  . ARG A 58  ? 0.1608 0.0796 0.2007 0.0458  0.0268  0.0311  58  ARG A CB  
458  C  CG  . ARG A 58  ? 0.1742 0.1292 0.1777 -0.0205 0.0498  0.0345  58  ARG A CG  
459  C  CD  . ARG A 58  ? 0.1698 0.2000 0.2108 -0.0730 -0.0075 0.0420  58  ARG A CD  
460  N  NE  . ARG A 58  ? 0.1343 0.1523 0.1904 -0.0537 0.0122  0.0111  58  ARG A NE  
461  C  CZ  . ARG A 58  ? 0.1234 0.1376 0.1570 -0.0398 0.0010  0.0249  58  ARG A CZ  
462  N  NH1 . ARG A 58  ? 0.2075 0.1577 0.1782 -0.0844 0.0451  0.0072  58  ARG A NH1 
463  N  NH2 . ARG A 58  ? 0.1397 0.1311 0.1537 -0.0011 0.0097  0.0027  58  ARG A NH2 
464  N  N   . ILE A 59  ? 0.1293 0.0775 0.0911 0.0190  -0.0108 0.0168  59  ILE A N   
465  C  CA  . ILE A 59  ? 0.1332 0.0527 0.1118 0.0055  -0.0016 0.0217  59  ILE A CA  
466  C  C   . ILE A 59  ? 0.1275 0.1006 0.0871 0.0017  -0.0024 0.0095  59  ILE A C   
467  O  O   . ILE A 59  ? 0.1537 0.1304 0.0859 0.0193  -0.0109 0.0223  59  ILE A O   
468  C  CB  . ILE A 59  ? 0.1272 0.0783 0.0927 -0.0069 -0.0253 0.0154  59  ILE A CB  
469  C  CG1 . ILE A 59  ? 0.1540 0.0751 0.1064 -0.0117 -0.0162 0.0332  59  ILE A CG1 
470  C  CG2 . ILE A 59  ? 0.1921 0.1135 0.0880 0.0003  -0.0216 0.0122  59  ILE A CG2 
471  C  CD1 . ILE A 59  ? 0.1825 0.0889 0.1501 -0.0290 -0.0313 0.0248  59  ILE A CD1 
472  N  N   . LEU A 60  ? 0.1097 0.1042 0.1017 0.0118  0.0038  0.0198  60  LEU A N   
473  C  CA  . LEU A 60  ? 0.1031 0.0981 0.0713 0.0100  -0.0134 0.0121  60  LEU A CA  
474  C  C   . LEU A 60  ? 0.1124 0.0990 0.0768 0.0132  -0.0097 0.0084  60  LEU A C   
475  O  O   . LEU A 60  ? 0.1293 0.1049 0.0844 -0.0013 0.0102  0.0042  60  LEU A O   
476  C  CB  . LEU A 60  ? 0.1451 0.0985 0.1473 -0.0146 -0.0075 0.0021  60  LEU A CB  
477  C  CG  . LEU A 60  ? 0.1490 0.0861 0.1203 -0.0217 0.0152  0.0088  60  LEU A CG  
478  C  CD1 . LEU A 60  ? 0.1914 0.0996 0.1264 -0.0536 0.0286  0.0133  60  LEU A CD1 
479  C  CD2 . LEU A 60  ? 0.1634 0.0859 0.1648 -0.0011 -0.0006 -0.0211 60  LEU A CD2 
480  N  N   . ASN A 61  ? 0.1091 0.0563 0.1221 -0.0043 0.0111  -0.0038 61  ASN A N   
481  C  CA  . ASN A 61  ? 0.1030 0.0803 0.0827 -0.0048 0.0150  0.0044  61  ASN A CA  
482  C  C   . ASN A 61  ? 0.1257 0.0674 0.1168 -0.0158 0.0142  0.0079  61  ASN A C   
483  O  O   . ASN A 61  ? 0.1247 0.0905 0.1094 -0.0131 0.0260  0.0061  61  ASN A O   
484  C  CB  . ASN A 61  ? 0.1292 0.0722 0.0864 -0.0034 0.0035  0.0036  61  ASN A CB  
485  C  CG  . ASN A 61  ? 0.1166 0.0584 0.1049 -0.0138 0.0103  0.0115  61  ASN A CG  
486  O  OD1 . ASN A 61  ? 0.1455 0.1023 0.1080 -0.0041 0.0098  0.0205  61  ASN A OD1 
487  N  ND2 . ASN A 61  ? 0.1537 0.0690 0.1071 -0.0073 0.0356  -0.0013 61  ASN A ND2 
488  N  N   . THR A 62  ? 0.1171 0.0769 0.1260 -0.0188 0.0081  0.0054  62  THR A N   
489  C  CA  . THR A 62  ? 0.1063 0.0970 0.1322 -0.0151 -0.0033 0.0153  62  THR A CA  
490  C  C   . THR A 62  ? 0.1268 0.1024 0.1350 -0.0039 0.0073  0.0176  62  THR A C   
491  O  O   . THR A 62  ? 0.1576 0.1325 0.1863 -0.0397 0.0078  -0.0094 62  THR A O   
492  C  CB  . THR A 62  ? 0.1268 0.0888 0.1286 0.0088  0.0130  0.0242  62  THR A CB  
493  O  OG1 . THR A 62  ? 0.1379 0.0638 0.1372 -0.0179 0.0173  0.0048  62  THR A OG1 
494  C  CG2 . THR A 62  ? 0.1451 0.1191 0.1469 0.0357  -0.0095 -0.0092 62  THR A CG2 
495  N  N   . GLY A 63  ? 0.1189 0.1013 0.0981 -0.0038 0.0155  0.0222  63  GLY A N   
496  C  CA  . GLY A 63  ? 0.1088 0.1053 0.1293 -0.0107 0.0313  0.0421  63  GLY A CA  
497  C  C   . GLY A 63  ? 0.1382 0.0853 0.1015 -0.0052 0.0242  0.0081  63  GLY A C   
498  O  O   . GLY A 63  ? 0.1613 0.1238 0.1728 0.0284  0.0469  0.0374  63  GLY A O   
499  N  N   . TYR A 64  ? 0.0990 0.1109 0.0857 -0.0126 0.0096  0.0120  64  TYR A N   
500  C  CA  . TYR A 64  ? 0.1173 0.1124 0.0945 -0.0286 0.0228  0.0189  64  TYR A CA  
501  C  C   . TYR A 64  ? 0.1176 0.0674 0.1067 -0.0182 0.0126  0.0128  64  TYR A C   
502  O  O   . TYR A 64  ? 0.1231 0.1188 0.1613 -0.0006 0.0226  0.0735  64  TYR A O   
503  C  CB  . TYR A 64  ? 0.1645 0.1723 0.1260 -0.0259 -0.0345 -0.0086 64  TYR A CB  
504  C  CG  . TYR A 64  ? 0.2309 0.3489 0.2227 -0.1001 -0.0266 -0.0162 64  TYR A CG  
505  C  CD1 . TYR A 64  ? 0.2308 0.3810 0.3541 -0.0517 -0.0626 -0.0807 64  TYR A CD1 
506  C  CD2 . TYR A 64  ? 0.4767 0.4124 0.4512 -0.0794 -0.0173 0.0615  64  TYR A CD2 
507  C  CE1 . TYR A 64  ? 0.2459 0.6481 0.4207 -0.1406 0.0510  -0.1367 64  TYR A CE1 
508  C  CE2 . TYR A 64  ? 0.4205 0.4835 0.4399 -0.0403 0.0876  -0.0495 64  TYR A CE2 
509  C  CZ  . TYR A 64  ? 0.3868 0.6668 0.6079 -0.1627 -0.0541 -0.0232 64  TYR A CZ  
510  O  OH  . TYR A 64  ? 0.3635 0.3606 0.2044 -0.0851 0.0016  -0.0024 64  TYR A OH  
511  N  N   . LEU A 65  ? 0.1108 0.0723 0.1354 -0.0033 0.0301  0.0008  65  LEU A N   
512  C  CA  . LEU A 65  ? 0.0981 0.0839 0.1058 0.0144  0.0088  0.0103  65  LEU A CA  
513  C  C   . LEU A 65  ? 0.0952 0.0733 0.0839 -0.0142 -0.0078 -0.0013 65  LEU A C   
514  O  O   . LEU A 65  ? 0.1206 0.0775 0.1076 -0.0193 0.0179  -0.0012 65  LEU A O   
515  C  CB  . LEU A 65  ? 0.1483 0.0958 0.0927 -0.0104 0.0103  -0.0055 65  LEU A CB  
516  C  CG  . LEU A 65  ? 0.1559 0.1116 0.1053 -0.0078 0.0150  -0.0223 65  LEU A CG  
517  C  CD1 . LEU A 65  ? 0.1577 0.0944 0.1529 -0.0074 0.0233  -0.0223 65  LEU A CD1 
518  C  CD2 . LEU A 65  ? 0.1676 0.1997 0.1153 -0.0232 0.0296  -0.0138 65  LEU A CD2 
519  N  N   . PHE A 66  ? 0.0994 0.0519 0.1083 -0.0084 -0.0092 -0.0058 66  PHE A N   
520  C  CA  . PHE A 66  ? 0.1340 0.0719 0.0643 0.0039  -0.0027 -0.0017 66  PHE A CA  
521  C  C   . PHE A 66  ? 0.1135 0.0841 0.0566 0.0097  -0.0207 -0.0016 66  PHE A C   
522  O  O   . PHE A 66  ? 0.0941 0.0941 0.0891 -0.0172 0.0059  0.0002  66  PHE A O   
523  C  CB  . PHE A 66  ? 0.1322 0.1008 0.0882 -0.0347 -0.0136 0.0128  66  PHE A CB  
524  C  CG  . PHE A 66  ? 0.1177 0.0644 0.0848 -0.0157 -0.0037 -0.0095 66  PHE A CG  
525  C  CD1 . PHE A 66  ? 0.1055 0.1091 0.0927 -0.0142 -0.0272 0.0080  66  PHE A CD1 
526  C  CD2 . PHE A 66  ? 0.1282 0.0759 0.1376 -0.0163 -0.0311 0.0093  66  PHE A CD2 
527  C  CE1 . PHE A 66  ? 0.1415 0.0875 0.1155 -0.0111 0.0021  0.0065  66  PHE A CE1 
528  C  CE2 . PHE A 66  ? 0.1376 0.0662 0.1275 -0.0177 -0.0034 -0.0161 66  PHE A CE2 
529  C  CZ  . PHE A 66  ? 0.1490 0.0911 0.1150 -0.0066 -0.0135 0.0088  66  PHE A CZ  
530  N  N   . GLN A 67  ? 0.1060 0.0814 0.0974 0.0231  0.0000  0.0033  67  GLN A N   
531  C  CA  . GLN A 67  ? 0.1200 0.0742 0.1049 0.0287  -0.0030 -0.0044 67  GLN A CA  
532  C  C   . GLN A 67  ? 0.1153 0.0820 0.0838 0.0068  -0.0062 0.0074  67  GLN A C   
533  O  O   . GLN A 67  ? 0.1261 0.1346 0.1014 0.0115  0.0215  0.0234  67  GLN A O   
534  C  CB  . GLN A 67  ? 0.1297 0.0988 0.1142 -0.0120 -0.0099 0.0258  67  GLN A CB  
535  C  CG  . GLN A 67  ? 0.1272 0.0926 0.1448 -0.0237 0.0047  0.0096  67  GLN A CG  
536  C  CD  . GLN A 67  ? 0.1667 0.1358 0.1950 -0.0274 -0.0236 -0.0155 67  GLN A CD  
537  O  OE1 . GLN A 67  ? 0.1800 0.1990 0.1649 -0.0374 -0.0316 -0.0084 67  GLN A OE1 
538  N  NE2 . GLN A 67  ? 0.2209 0.1186 0.2191 -0.0211 0.0049  -0.0219 67  GLN A NE2 
539  N  N   . VAL A 68  ? 0.1060 0.0798 0.0988 0.0146  -0.0127 0.0255  68  VAL A N   
540  C  CA  . VAL A 68  ? 0.1153 0.0801 0.0906 0.0127  -0.0324 0.0143  68  VAL A CA  
541  C  C   . VAL A 68  ? 0.1311 0.0819 0.0944 0.0137  -0.0233 0.0198  68  VAL A C   
542  O  O   . VAL A 68  ? 0.1321 0.1048 0.0938 0.0201  -0.0124 0.0160  68  VAL A O   
543  C  CB  . VAL A 68  ? 0.0963 0.0802 0.1400 0.0223  -0.0233 -0.0086 68  VAL A CB  
544  C  CG1 . VAL A 68  ? 0.1076 0.1289 0.1342 0.0268  -0.0421 0.0160  68  VAL A CG1 
545  C  CG2 . VAL A 68  ? 0.1494 0.0986 0.1189 0.0323  -0.0150 -0.0153 68  VAL A CG2 
546  N  N   . GLU A 69  ? 0.1376 0.0522 0.1279 0.0226  -0.0100 0.0185  69  GLU A N   
547  C  CA  . GLU A 69  ? 0.1209 0.0625 0.1097 0.0016  -0.0001 0.0172  69  GLU A CA  
548  C  C   . GLU A 69  ? 0.1227 0.0839 0.1066 -0.0011 -0.0160 0.0378  69  GLU A C   
549  O  O   . GLU A 69  ? 0.1343 0.0748 0.1325 0.0106  -0.0379 0.0171  69  GLU A O   
550  C  CB  . GLU A 69  ? 0.1121 0.0873 0.1562 -0.0006 0.0140  0.0227  69  GLU A CB  
551  C  CG  . GLU A 69  ? 0.1200 0.0977 0.1523 -0.0012 0.0048  -0.0012 69  GLU A CG  
552  C  CD  . GLU A 69  ? 0.1329 0.1243 0.1555 -0.0413 -0.0027 0.0002  69  GLU A CD  
553  O  OE1 . GLU A 69  ? 0.1523 0.1318 0.2187 -0.0105 0.0324  0.0093  69  GLU A OE1 
554  O  OE2 . GLU A 69  ? 0.2007 0.1212 0.1764 -0.0140 0.0478  0.0336  69  GLU A OE2 
555  N  N   . PHE A 70  ? 0.1137 0.0891 0.1415 0.0035  0.0196  0.0258  70  PHE A N   
556  C  CA  . PHE A 70  ? 0.0974 0.0836 0.1379 0.0005  0.0006  0.0176  70  PHE A CA  
557  C  C   . PHE A 70  ? 0.1451 0.0864 0.1361 -0.0068 -0.0008 -0.0105 70  PHE A C   
558  O  O   . PHE A 70  ? 0.1232 0.0880 0.1746 0.0027  0.0006  0.0282  70  PHE A O   
559  C  CB  . PHE A 70  ? 0.1289 0.0979 0.1042 -0.0081 -0.0109 -0.0012 70  PHE A CB  
560  C  CG  . PHE A 70  ? 0.1272 0.0875 0.1216 0.0051  -0.0153 0.0245  70  PHE A CG  
561  C  CD1 . PHE A 70  ? 0.1216 0.1058 0.1552 0.0190  -0.0146 0.0304  70  PHE A CD1 
562  C  CD2 . PHE A 70  ? 0.1447 0.0812 0.1249 -0.0250 -0.0190 0.0100  70  PHE A CD2 
563  C  CE1 . PHE A 70  ? 0.1433 0.1343 0.1688 -0.0114 0.0261  0.0262  70  PHE A CE1 
564  C  CE2 . PHE A 70  ? 0.1606 0.0679 0.1559 -0.0161 -0.0116 0.0140  70  PHE A CE2 
565  C  CZ  . PHE A 70  ? 0.1523 0.0961 0.1347 0.0058  0.0452  0.0278  70  PHE A CZ  
566  N  N   . ASP A 71  ? 0.1849 0.0615 0.1863 -0.0039 -0.0155 0.0242  71  ASP A N   
567  C  CA  . ASP A 71  ? 0.1666 0.0656 0.2004 0.0068  -0.0091 -0.0078 71  ASP A CA  
568  C  C   . ASP A 71  ? 0.1534 0.0688 0.1760 -0.0018 -0.0043 0.0336  71  ASP A C   
569  O  O   . ASP A 71  ? 0.1602 0.1602 0.2044 -0.0416 0.0075  -0.0063 71  ASP A O   
570  C  CB  . ASP A 71  ? 0.1813 0.1053 0.2588 0.0115  -0.0400 0.0135  71  ASP A CB  
571  C  CG  . ASP A 71  ? 0.2040 0.1017 0.2512 0.0088  -0.0738 0.0299  71  ASP A CG  
572  O  OD1 . ASP A 71  ? 0.1789 0.1264 0.2287 0.0055  -0.0466 0.0544  71  ASP A OD1 
573  O  OD2 . ASP A 71  ? 0.1789 0.1465 0.3256 0.0096  -0.0669 0.0204  71  ASP A OD2 
574  N  N   . ASP A 72  ? 0.1843 0.0696 0.1817 -0.0083 -0.0083 0.0225  72  ASP A N   
575  C  CA  . ASP A 72  ? 0.1929 0.0832 0.1777 -0.0110 -0.0027 0.0044  72  ASP A CA  
576  C  C   . ASP A 72  ? 0.1965 0.0893 0.1767 -0.0356 -0.0179 0.0164  72  ASP A C   
577  O  O   . ASP A 72  ? 0.2539 0.1234 0.1939 -0.0381 -0.0347 0.0237  72  ASP A O   
578  C  CB  . ASP A 72  ? 0.2004 0.0863 0.1918 -0.0172 0.0070  0.0421  72  ASP A CB  
579  C  CG  . ASP A 72  ? 0.1867 0.1213 0.1430 -0.0094 -0.0089 0.0146  72  ASP A CG  
580  O  OD1 . ASP A 72  ? 0.2251 0.1458 0.1494 -0.0209 -0.0044 0.0356  72  ASP A OD1 
581  O  OD2 . ASP A 72  ? 0.2606 0.1421 0.1272 0.0148  -0.0282 0.0197  72  ASP A OD2 
582  N  N   . SER A 73  ? 0.1616 0.0812 0.1965 -0.0098 0.0006  0.0150  73  SER A N   
583  C  CA  . SER A 73  ? 0.2068 0.0836 0.2019 -0.0116 -0.0141 0.0027  73  SER A CA  
584  C  C   . SER A 73  ? 0.2406 0.0715 0.2162 -0.0059 0.0228  -0.0062 73  SER A C   
585  O  O   . SER A 73  ? 0.4019 0.0688 0.2363 -0.0137 -0.0073 0.0071  73  SER A O   
586  C  CB  . SER A 73  ? 0.1699 0.1473 0.2037 -0.0049 -0.0122 0.0469  73  SER A CB  
587  O  OG  . SER A 73  ? 0.2019 0.1253 0.2083 0.0284  -0.0288 0.0280  73  SER A OG  
588  N  N   . GLN A 74  ? 0.2152 0.1231 0.2231 0.0004  0.0365  0.0011  74  GLN A N   
589  C  CA  . GLN A 74  ? 0.2155 0.1753 0.2845 0.0106  0.0671  0.0089  74  GLN A CA  
590  C  C   . GLN A 74  ? 0.2213 0.1746 0.2509 -0.0282 0.0114  -0.0238 74  GLN A C   
591  O  O   . GLN A 74  ? 0.2299 0.1361 0.2057 -0.0244 -0.0015 -0.0089 74  GLN A O   
592  C  CB  . GLN A 74  ? 0.2530 0.3652 0.3939 0.0895  0.0771  0.0594  74  GLN A CB  
593  C  CG  . GLN A 74  ? 0.2965 0.3608 0.4169 0.0871  0.0380  -0.0098 74  GLN A CG  
594  C  CD  . GLN A 74  ? 0.3437 0.3786 0.3212 0.0489  -0.0236 0.0359  74  GLN A CD  
595  O  OE1 . GLN A 74  ? 0.3705 0.3890 0.4339 -0.0783 0.1213  0.0586  74  GLN A OE1 
596  N  NE2 . GLN A 74  ? 0.2875 0.3010 0.3082 0.0791  -0.0475 0.0561  74  GLN A NE2 
597  N  N   . ASP A 75  ? 0.2471 0.2076 0.1947 0.0264  -0.0146 0.0113  75  ASP A N   
598  C  CA  . ASP A 75  ? 0.2590 0.3022 0.1972 -0.0471 0.0258  0.0160  75  ASP A CA  
599  C  C   . ASP A 75  ? 0.2312 0.2424 0.2828 0.0807  -0.1011 0.0245  75  ASP A C   
600  O  O   . ASP A 75  ? 0.2363 0.7007 0.4733 0.0798  -0.1231 -0.2095 75  ASP A O   
601  C  CB  . ASP A 75  ? 0.2209 0.2784 0.2069 0.0367  0.0017  0.0367  75  ASP A CB  
602  C  CG  . ASP A 75  ? 0.1868 0.4002 0.2965 0.0064  0.0193  -0.0724 75  ASP A CG  
603  O  OD1 . ASP A 75  ? 0.1943 0.5978 0.3416 0.0159  0.0062  -0.0137 75  ASP A OD1 
604  O  OD2 . ASP A 75  ? 0.3903 0.3467 0.2673 0.0429  0.0706  -0.0176 75  ASP A OD2 
605  N  N   . LYS A 76  ? 0.2212 0.1731 0.2788 0.0049  -0.0746 0.0322  76  LYS A N   
606  C  CA  . LYS A 76  ? 0.2647 0.1433 0.2367 0.0203  -0.0907 0.0384  76  LYS A CA  
607  C  C   . LYS A 76  ? 0.2342 0.1515 0.4064 0.0505  0.0057  0.0598  76  LYS A C   
608  O  O   . LYS A 76  ? 0.3204 0.4345 0.5255 -0.0678 -0.0480 0.1458  76  LYS A O   
609  C  CB  . LYS A 76  ? 0.3194 0.1669 0.2453 -0.0355 -0.0759 0.0376  76  LYS A CB  
610  C  CG  . LYS A 76  ? 0.3459 0.1900 0.2809 -0.0738 -0.1151 0.0687  76  LYS A CG  
611  C  CD  . LYS A 76  ? 0.3452 0.1875 0.2945 -0.0310 -0.0644 0.0496  76  LYS A CD  
612  C  CE  . LYS A 76  ? 0.2134 0.2548 0.2582 0.0783  -0.0857 0.0125  76  LYS A CE  
613  N  NZ  . LYS A 76  ? 0.2403 0.3130 0.2486 0.0284  -0.0384 0.0201  76  LYS A NZ  
614  N  N   . ALA A 77  ? 0.2150 0.2176 0.2559 0.0353  -0.0203 0.0847  77  ALA A N   
615  C  CA  . ALA A 77  ? 0.1462 0.2608 0.2072 -0.0388 -0.0037 0.0819  77  ALA A CA  
616  C  C   . ALA A 77  ? 0.1117 0.2713 0.2342 -0.0079 -0.0290 0.0929  77  ALA A C   
617  O  O   . ALA A 77  ? 0.1203 0.2496 0.2964 -0.0096 -0.0136 0.0831  77  ALA A O   
618  C  CB  . ALA A 77  ? 0.2277 0.2963 0.2684 0.0075  -0.0482 0.0318  77  ALA A CB  
619  N  N   . VAL A 78  ? 0.1425 0.1134 0.1983 -0.0083 -0.0122 0.0176  78  VAL A N   
620  C  CA  . VAL A 78  ? 0.1232 0.1292 0.1918 0.0195  -0.0148 0.0370  78  VAL A CA  
621  C  C   . VAL A 78  ? 0.1155 0.1168 0.1990 -0.0054 0.0071  0.0212  78  VAL A C   
622  O  O   . VAL A 78  ? 0.1394 0.1322 0.2514 -0.0232 -0.0248 0.0439  78  VAL A O   
623  C  CB  . VAL A 78  ? 0.1667 0.1121 0.2931 0.0171  -0.0044 0.0348  78  VAL A CB  
624  C  CG1 . VAL A 78  ? 0.1864 0.1100 0.3745 0.0089  -0.0073 0.0665  78  VAL A CG1 
625  C  CG2 . VAL A 78  ? 0.2098 0.1993 0.2794 0.0121  0.0785  0.0359  78  VAL A CG2 
626  N  N   . LEU A 79  ? 0.1462 0.0965 0.1601 0.0111  0.0174  0.0129  79  LEU A N   
627  C  CA  . LEU A 79  ? 0.1189 0.0855 0.1641 0.0055  0.0215  0.0044  79  LEU A CA  
628  C  C   . LEU A 79  ? 0.1322 0.0997 0.1487 -0.0259 0.0072  0.0022  79  LEU A C   
629  O  O   . LEU A 79  ? 0.1303 0.1132 0.1990 -0.0291 0.0272  -0.0258 79  LEU A O   
630  C  CB  . LEU A 79  ? 0.0810 0.1092 0.2141 -0.0095 -0.0019 0.0148  79  LEU A CB  
631  C  CG  . LEU A 79  ? 0.1437 0.1243 0.1907 0.0049  -0.0207 0.0118  79  LEU A CG  
632  C  CD1 . LEU A 79  ? 0.1752 0.1494 0.2582 -0.0201 0.0156  0.0254  79  LEU A CD1 
633  C  CD2 . LEU A 79  ? 0.1483 0.1529 0.2047 0.0273  0.0013  0.0154  79  LEU A CD2 
634  N  N   . LYS A 80  ? 0.1652 0.1182 0.1566 0.0015  0.0276  0.0153  80  LYS A N   
635  C  CA  . LYS A 80  ? 0.1573 0.1212 0.1896 -0.0122 0.0368  -0.0119 80  LYS A CA  
636  C  C   . LYS A 80  ? 0.1465 0.1455 0.2033 -0.0212 0.0362  -0.0026 80  LYS A C   
637  O  O   . LYS A 80  ? 0.0949 0.1364 0.2259 -0.0154 0.0115  0.0106  80  LYS A O   
638  C  CB  . LYS A 80  ? 0.3153 0.1322 0.2536 0.0680  0.0960  0.0226  80  LYS A CB  
639  C  CG  . LYS A 80  ? 0.2931 0.1796 0.2633 0.0352  0.0518  0.0421  80  LYS A CG  
640  C  CD  . LYS A 80  ? 0.3536 0.2348 0.5270 0.0996  -0.1035 0.0247  80  LYS A CD  
641  N  N   . GLY A 81  ? 0.1641 0.1486 0.1731 0.0031  0.0414  0.0253  81  GLY A N   
642  C  CA  . GLY A 81  ? 0.1863 0.1239 0.2366 0.0634  0.0952  0.0406  81  GLY A CA  
643  C  C   . GLY A 81  ? 0.1343 0.0893 0.2356 0.0222  0.0598  0.0188  81  GLY A C   
644  O  O   . GLY A 81  ? 0.1333 0.1681 0.2266 -0.0267 0.0298  -0.0006 81  GLY A O   
645  N  N   . GLY A 82  ? 0.1602 0.1587 0.2982 0.0161  0.0680  0.0881  82  GLY A N   
646  C  CA  . GLY A 82  ? 0.2073 0.1437 0.3556 0.0388  0.0607  0.0889  82  GLY A CA  
647  C  C   . GLY A 82  ? 0.2374 0.1814 0.3355 0.0447  0.0867  0.0149  82  GLY A C   
648  O  O   . GLY A 82  ? 0.2372 0.2694 0.3349 0.1273  0.1254  0.0515  82  GLY A O   
649  N  N   . PRO A 83  ? 0.2094 0.1559 0.2355 0.0513  0.0429  0.0161  83  PRO A N   
650  C  CA  . PRO A 83  ? 0.1882 0.1885 0.2475 0.0411  0.0564  0.0082  83  PRO A CA  
651  C  C   . PRO A 83  ? 0.1774 0.1882 0.1904 0.0716  0.0428  0.0018  83  PRO A C   
652  O  O   . PRO A 83  ? 0.2605 0.2952 0.2615 0.0308  -0.0026 -0.0124 83  PRO A O   
653  C  CB  . PRO A 83  ? 0.1641 0.1907 0.1879 0.0269  0.0094  0.0004  83  PRO A CB  
654  C  CG  . PRO A 83  ? 0.1548 0.1641 0.1652 0.0265  -0.0021 0.0193  83  PRO A CG  
655  C  CD  . PRO A 83  ? 0.1544 0.1534 0.2047 -0.0111 0.0128  -0.0288 83  PRO A CD  
656  N  N   . LEU A 84  ? 0.1512 0.1243 0.1821 0.0272  0.0238  0.0099  84  LEU A N   
657  C  CA  . LEU A 84  ? 0.1760 0.0882 0.2004 0.0237  0.0174  -0.0144 84  LEU A CA  
658  C  C   . LEU A 84  ? 0.1967 0.1225 0.2295 0.0220  0.0308  -0.0634 84  LEU A C   
659  O  O   . LEU A 84  ? 0.2213 0.1555 0.2978 0.0299  0.0335  -0.0898 84  LEU A O   
660  C  CB  . LEU A 84  ? 0.1497 0.1049 0.1821 0.0126  0.0410  -0.0260 84  LEU A CB  
661  C  CG  . LEU A 84  ? 0.1058 0.1037 0.1778 0.0131  0.0240  -0.0145 84  LEU A CG  
662  C  CD1 . LEU A 84  ? 0.1412 0.1275 0.1598 -0.0082 0.0263  -0.0162 84  LEU A CD1 
663  C  CD2 . LEU A 84  ? 0.1056 0.1351 0.2094 0.0087  0.0305  -0.0650 84  LEU A CD2 
664  N  N   . ASP A 85  ? 0.2457 0.1243 0.2489 0.0086  0.0361  -0.0785 85  ASP A N   
665  C  CA  . ASP A 85  ? 0.2759 0.1214 0.2807 -0.0063 0.0531  -0.0922 85  ASP A CA  
666  C  C   . ASP A 85  ? 0.2215 0.1078 0.3410 0.0362  0.0738  -0.0603 85  ASP A C   
667  O  O   . ASP A 85  ? 0.3022 0.2788 0.3902 -0.0168 0.1288  -0.1390 85  ASP A O   
668  C  CB  . ASP A 85  ? 0.3899 0.1372 0.3603 0.0639  -0.0691 -0.1293 85  ASP A CB  
669  C  CG  . ASP A 85  ? 0.2903 0.3843 0.4606 0.0889  -0.1403 -0.0142 85  ASP A CG  
670  O  OD1 . ASP A 85  ? 0.4701 0.6869 0.4906 -0.0851 0.1035  -0.1293 85  ASP A OD1 
671  O  OD2 . ASP A 85  ? 0.2069 0.4758 0.5455 -0.0120 -0.0834 -0.1073 85  ASP A OD2 
672  N  N   . GLY A 86  ? 0.2345 0.1821 0.4550 -0.0095 0.0635  0.0495  86  GLY A N   
673  C  CA  . GLY A 86  ? 0.2481 0.1624 0.3093 -0.0245 0.0085  -0.0423 86  GLY A CA  
674  C  C   . GLY A 86  ? 0.2349 0.1278 0.2825 0.0080  0.0140  -0.0326 86  GLY A C   
675  O  O   . GLY A 86  ? 0.3514 0.2277 0.3118 -0.1044 -0.0249 0.0385  86  GLY A O   
676  N  N   . THR A 87  ? 0.1773 0.1706 0.2709 -0.0115 0.0552  -0.0423 87  THR A N   
677  C  CA  . THR A 87  ? 0.1465 0.2143 0.2568 0.0489  0.0392  0.0015  87  THR A CA  
678  C  C   . THR A 87  ? 0.1487 0.0994 0.2842 -0.0381 0.0759  -0.0292 87  THR A C   
679  O  O   . THR A 87  ? 0.1354 0.0801 0.2533 -0.0217 0.0650  -0.0238 87  THR A O   
680  C  CB  . THR A 87  ? 0.1469 0.2180 0.2996 0.0789  0.0225  -0.0077 87  THR A CB  
681  O  OG1 . THR A 87  ? 0.2227 0.3438 0.4009 0.1003  0.0782  -0.0798 87  THR A OG1 
682  C  CG2 . THR A 87  ? 0.2417 0.2112 0.2958 0.0168  -0.0013 0.0162  87  THR A CG2 
683  N  N   . TYR A 88  ? 0.1150 0.0920 0.2015 -0.0214 0.0499  -0.0085 88  TYR A N   
684  C  CA  . TYR A 88  ? 0.1046 0.0870 0.1910 -0.0012 0.0358  0.0030  88  TYR A CA  
685  C  C   . TYR A 88  ? 0.1106 0.0753 0.1940 -0.0085 0.0059  0.0103  88  TYR A C   
686  O  O   . TYR A 88  ? 0.1102 0.1375 0.2299 -0.0372 -0.0078 0.0442  88  TYR A O   
687  C  CB  . TYR A 88  ? 0.1260 0.0749 0.1939 -0.0114 -0.0077 -0.0133 88  TYR A CB  
688  C  CG  . TYR A 88  ? 0.1128 0.0393 0.1584 0.0080  0.0132  -0.0329 88  TYR A CG  
689  C  CD1 . TYR A 88  ? 0.1304 0.0873 0.1649 0.0032  0.0263  -0.0366 88  TYR A CD1 
690  C  CD2 . TYR A 88  ? 0.1115 0.0641 0.1810 0.0108  0.0038  -0.0072 88  TYR A CD2 
691  C  CE1 . TYR A 88  ? 0.0920 0.1400 0.1753 -0.0067 0.0323  -0.0394 88  TYR A CE1 
692  C  CE2 . TYR A 88  ? 0.1194 0.0557 0.1519 -0.0157 0.0285  -0.0212 88  TYR A CE2 
693  C  CZ  . TYR A 88  ? 0.1021 0.0789 0.1685 -0.0088 0.0181  -0.0455 88  TYR A CZ  
694  O  OH  . TYR A 88  ? 0.1519 0.1353 0.1565 -0.0256 0.0249  -0.0563 88  TYR A OH  
695  N  N   . ARG A 89  ? 0.1214 0.0663 0.1746 -0.0034 0.0215  -0.0144 89  ARG A N   
696  C  CA  . ARG A 89  ? 0.1448 0.0812 0.1828 0.0041  0.0147  0.0105  89  ARG A CA  
697  C  C   . ARG A 89  ? 0.0891 0.0699 0.1498 -0.0031 -0.0055 0.0219  89  ARG A C   
698  O  O   . ARG A 89  ? 0.0911 0.0812 0.1450 0.0047  0.0029  0.0118  89  ARG A O   
699  C  CB  . ARG A 89  ? 0.1358 0.0672 0.3421 -0.0083 0.0283  0.0421  89  ARG A CB  
700  C  CG  . ARG A 89  ? 0.2795 0.3176 0.4246 -0.0521 -0.0217 0.2359  89  ARG A CG  
701  C  CD  . ARG A 89  ? 0.2796 0.1091 0.3319 0.0199  -0.0209 0.0985  89  ARG A CD  
702  N  NE  . ARG A 89  ? 0.3010 0.1663 0.2187 0.0432  -0.0278 0.0438  89  ARG A NE  
703  C  CZ  . ARG A 89  ? 0.2763 0.1383 0.2478 0.0588  -0.0341 0.0197  89  ARG A CZ  
704  N  NH1 . ARG A 89  ? 0.2760 0.1652 0.2069 0.0160  -0.0539 -0.0051 89  ARG A NH1 
705  N  NH2 . ARG A 89  ? 0.3046 0.3258 0.2992 0.0379  -0.0400 -0.1542 89  ARG A NH2 
706  N  N   . LEU A 90  ? 0.1232 0.0577 0.1493 -0.0143 -0.0013 0.0187  90  LEU A N   
707  C  CA  . LEU A 90  ? 0.1322 0.0838 0.1108 -0.0193 -0.0140 0.0077  90  LEU A CA  
708  C  C   . LEU A 90  ? 0.1017 0.0944 0.1286 -0.0022 -0.0192 0.0240  90  LEU A C   
709  O  O   . LEU A 90  ? 0.1389 0.1264 0.1576 0.0147  -0.0374 0.0399  90  LEU A O   
710  C  CB  . LEU A 90  ? 0.1562 0.1029 0.1099 -0.0269 -0.0421 0.0051  90  LEU A CB  
711  C  CG  . LEU A 90  ? 0.1613 0.0875 0.1137 -0.0411 -0.0325 0.0085  90  LEU A CG  
712  C  CD1 . LEU A 90  ? 0.2288 0.0959 0.1296 -0.0149 -0.0255 0.0265  90  LEU A CD1 
713  C  CD2 . LEU A 90  ? 0.1806 0.1343 0.1655 -0.0717 -0.0435 0.0100  90  LEU A CD2 
714  N  N   . LYS A 91  ? 0.0970 0.0722 0.1207 -0.0024 -0.0035 -0.0052 91  LYS A N   
715  C  CA  . LYS A 91  ? 0.1286 0.0732 0.1150 -0.0171 -0.0066 -0.0050 91  LYS A CA  
716  C  C   . LYS A 91  ? 0.1372 0.0575 0.1051 0.0263  -0.0091 0.0149  91  LYS A C   
717  O  O   . LYS A 91  ? 0.1401 0.0616 0.1049 -0.0027 -0.0178 0.0167  91  LYS A O   
718  C  CB  . LYS A 91  ? 0.1221 0.0864 0.1414 -0.0306 -0.0079 0.0102  91  LYS A CB  
719  C  CG  . LYS A 91  ? 0.1365 0.1207 0.1559 -0.0494 0.0115  0.0034  91  LYS A CG  
720  C  CD  . LYS A 91  ? 0.1523 0.1200 0.1760 -0.0407 0.0077  -0.0334 91  LYS A CD  
721  C  CE  . LYS A 91  ? 0.1961 0.1372 0.2380 -0.0644 0.0379  0.0141  91  LYS A CE  
722  N  NZ  . LYS A 91  ? 0.3471 0.2215 0.2161 -0.0705 -0.0317 -0.0129 91  LYS A NZ  
723  N  N   . GLN A 92  ? 0.1504 0.0419 0.1128 -0.0015 -0.0164 0.0044  92  GLN A N   
724  C  CA  . GLN A 92  ? 0.1351 0.0408 0.1141 0.0157  0.0017  0.0138  92  GLN A CA  
725  C  C   . GLN A 92  ? 0.1404 0.0553 0.0855 -0.0042 -0.0076 0.0102  92  GLN A C   
726  O  O   . GLN A 92  ? 0.1544 0.0647 0.0893 0.0143  -0.0153 -0.0081 92  GLN A O   
727  C  CB  . GLN A 92  ? 0.1333 0.0723 0.1141 0.0171  -0.0089 0.0323  92  GLN A CB  
728  C  CG  . GLN A 92  ? 0.1537 0.1196 0.1224 0.0172  -0.0251 0.0280  92  GLN A CG  
729  C  CD  . GLN A 92  ? 0.1692 0.0923 0.1200 -0.0128 -0.0177 0.0052  92  GLN A CD  
730  O  OE1 . GLN A 92  ? 0.2040 0.0873 0.1893 -0.0032 -0.0381 0.0365  92  GLN A OE1 
731  N  NE2 . GLN A 92  ? 0.1764 0.2107 0.3771 0.0177  0.0027  -0.0447 92  GLN A NE2 
732  N  N   . PHE A 93  ? 0.1145 0.0481 0.0926 0.0146  -0.0109 0.0058  93  PHE A N   
733  C  CA  . PHE A 93  ? 0.0900 0.0434 0.0961 0.0095  0.0037  0.0069  93  PHE A CA  
734  C  C   . PHE A 93  ? 0.0952 0.0565 0.0715 0.0049  -0.0086 -0.0049 93  PHE A C   
735  O  O   . PHE A 93  ? 0.1232 0.0782 0.0791 0.0081  -0.0152 0.0000  93  PHE A O   
736  C  CB  . PHE A 93  ? 0.1146 0.0785 0.0995 -0.0263 -0.0168 0.0071  93  PHE A CB  
737  C  CG  . PHE A 93  ? 0.0895 0.0627 0.0972 -0.0126 -0.0170 0.0088  93  PHE A CG  
738  C  CD1 . PHE A 93  ? 0.1268 0.0619 0.0935 -0.0175 0.0025  0.0115  93  PHE A CD1 
739  C  CD2 . PHE A 93  ? 0.0820 0.0983 0.0853 -0.0039 -0.0073 0.0157  93  PHE A CD2 
740  C  CE1 . PHE A 93  ? 0.1145 0.1051 0.1063 -0.0064 -0.0203 -0.0002 93  PHE A CE1 
741  C  CE2 . PHE A 93  ? 0.0996 0.0954 0.1044 -0.0088 -0.0172 0.0011  93  PHE A CE2 
742  C  CZ  . PHE A 93  ? 0.1421 0.0935 0.1017 -0.0003 -0.0312 0.0013  93  PHE A CZ  
743  N  N   . HIS A 94  ? 0.0898 0.0489 0.1005 0.0059  -0.0088 0.0029  94  HIS A N   
744  C  CA  . HIS A 94  ? 0.0945 0.0546 0.0952 0.0072  0.0096  0.0128  94  HIS A CA  
745  C  C   . HIS A 94  ? 0.0830 0.0634 0.0529 0.0033  -0.0027 0.0072  94  HIS A C   
746  O  O   . HIS A 94  ? 0.1093 0.0654 0.0652 -0.0017 0.0083  0.0029  94  HIS A O   
747  C  CB  . HIS A 94  ? 0.1017 0.0996 0.0751 -0.0108 -0.0023 0.0094  94  HIS A CB  
748  C  CG  . HIS A 94  ? 0.1032 0.0416 0.0744 -0.0076 0.0011  -0.0035 94  HIS A CG  
749  N  ND1 . HIS A 94  ? 0.0952 0.0463 0.0881 -0.0072 -0.0080 -0.0108 94  HIS A ND1 
750  C  CD2 . HIS A 94  ? 0.1185 0.0505 0.0847 -0.0141 -0.0026 0.0086  94  HIS A CD2 
751  C  CE1 . HIS A 94  ? 0.0794 0.0347 0.0872 0.0194  0.0017  0.0241  94  HIS A CE1 
752  N  NE2 . HIS A 94  ? 0.0839 0.0268 0.0820 0.0165  -0.0063 0.0047  94  HIS A NE2 
753  N  N   . PHE A 95  ? 0.1071 0.0476 0.0909 0.0075  0.0006  0.0076  95  PHE A N   
754  C  CA  . PHE A 95  ? 0.0837 0.0316 0.0830 -0.0059 -0.0023 -0.0095 95  PHE A CA  
755  C  C   . PHE A 95  ? 0.0854 0.0463 0.0783 -0.0041 -0.0126 -0.0158 95  PHE A C   
756  O  O   . PHE A 95  ? 0.1020 0.0601 0.1062 -0.0159 -0.0088 0.0017  95  PHE A O   
757  C  CB  . PHE A 95  ? 0.0942 0.0461 0.1040 0.0033  -0.0201 -0.0230 95  PHE A CB  
758  C  CG  . PHE A 95  ? 0.0954 0.0528 0.0927 0.0160  -0.0089 -0.0212 95  PHE A CG  
759  C  CD1 . PHE A 95  ? 0.1325 0.0677 0.1071 0.0104  -0.0297 -0.0162 95  PHE A CD1 
760  C  CD2 . PHE A 95  ? 0.1089 0.0909 0.0950 -0.0082 -0.0152 -0.0251 95  PHE A CD2 
761  C  CE1 . PHE A 95  ? 0.1304 0.0830 0.0915 0.0182  -0.0172 -0.0144 95  PHE A CE1 
762  C  CE2 . PHE A 95  ? 0.1196 0.0891 0.0950 -0.0185 -0.0299 -0.0184 95  PHE A CE2 
763  C  CZ  . PHE A 95  ? 0.1358 0.0932 0.1049 0.0118  -0.0062 -0.0160 95  PHE A CZ  
764  N  N   . HIS A 96  ? 0.1020 0.0553 0.0829 0.0065  -0.0243 -0.0070 96  HIS A N   
765  C  CA  . HIS A 96  ? 0.0819 0.0559 0.0972 -0.0021 -0.0026 0.0051  96  HIS A CA  
766  C  C   . HIS A 96  ? 0.0796 0.0602 0.0732 -0.0030 -0.0047 -0.0110 96  HIS A C   
767  O  O   . HIS A 96  ? 0.0871 0.0616 0.1045 0.0024  0.0088  -0.0102 96  HIS A O   
768  C  CB  . HIS A 96  ? 0.0986 0.0463 0.1124 -0.0142 -0.0116 -0.0146 96  HIS A CB  
769  C  CG  . HIS A 96  ? 0.0990 0.0338 0.0993 -0.0011 -0.0098 0.0055  96  HIS A CG  
770  N  ND1 . HIS A 96  ? 0.0963 0.0355 0.0933 -0.0067 0.0015  0.0005  96  HIS A ND1 
771  C  CD2 . HIS A 96  ? 0.1256 0.0188 0.1046 0.0000  -0.0227 -0.0223 96  HIS A CD2 
772  C  CE1 . HIS A 96  ? 0.0970 0.0445 0.0758 0.0055  0.0076  -0.0049 96  HIS A CE1 
773  N  NE2 . HIS A 96  ? 0.0857 0.0481 0.1069 -0.0174 -0.0057 -0.0141 96  HIS A NE2 
774  N  N   . TRP A 97  ? 0.1040 0.0446 0.0776 -0.0061 0.0088  -0.0107 97  TRP A N   
775  C  CA  . TRP A 97  ? 0.0997 0.0381 0.0915 0.0122  -0.0086 -0.0215 97  TRP A CA  
776  C  C   . TRP A 97  ? 0.0918 0.0487 0.0952 0.0068  0.0103  -0.0196 97  TRP A C   
777  O  O   . TRP A 97  ? 0.0911 0.0575 0.1015 0.0031  0.0134  -0.0032 97  TRP A O   
778  C  CB  . TRP A 97  ? 0.1072 0.0706 0.0721 -0.0168 0.0043  -0.0131 97  TRP A CB  
779  C  CG  . TRP A 97  ? 0.0827 0.0656 0.0848 0.0006  0.0055  -0.0017 97  TRP A CG  
780  C  CD1 . TRP A 97  ? 0.1150 0.0767 0.0767 -0.0124 0.0150  -0.0207 97  TRP A CD1 
781  C  CD2 . TRP A 97  ? 0.0952 0.0633 0.0897 -0.0093 0.0062  -0.0066 97  TRP A CD2 
782  N  NE1 . TRP A 97  ? 0.1353 0.0566 0.0932 -0.0054 0.0142  -0.0102 97  TRP A NE1 
783  C  CE2 . TRP A 97  ? 0.1139 0.0573 0.0932 -0.0075 0.0120  -0.0107 97  TRP A CE2 
784  C  CE3 . TRP A 97  ? 0.1168 0.0571 0.0941 0.0001  -0.0185 0.0041  97  TRP A CE3 
785  C  CZ2 . TRP A 97  ? 0.1199 0.0757 0.1024 0.0048  -0.0002 0.0089  97  TRP A CZ2 
786  C  CZ3 . TRP A 97  ? 0.1058 0.0803 0.0926 -0.0079 0.0006  0.0100  97  TRP A CZ3 
787  C  CH2 . TRP A 97  ? 0.1159 0.0886 0.1066 0.0033  0.0098  -0.0108 97  TRP A CH2 
788  N  N   . GLY A 98  ? 0.1032 0.0467 0.0882 -0.0018 0.0064  -0.0098 98  GLY A N   
789  C  CA  . GLY A 98  ? 0.1250 0.0523 0.0963 0.0144  -0.0067 -0.0038 98  GLY A CA  
790  C  C   . GLY A 98  ? 0.1150 0.0478 0.1033 -0.0030 -0.0023 -0.0037 98  GLY A C   
791  O  O   . GLY A 98  ? 0.1094 0.0659 0.1250 -0.0117 -0.0076 -0.0041 98  GLY A O   
792  N  N   . SER A 99  ? 0.1199 0.0475 0.1268 -0.0002 0.0129  -0.0100 99  SER A N   
793  C  CA  . SER A 99  ? 0.1383 0.0530 0.1297 0.0044  0.0381  -0.0131 99  SER A CA  
794  C  C   . SER A 99  ? 0.1505 0.0568 0.1189 -0.0020 0.0166  -0.0066 99  SER A C   
795  O  O   . SER A 99  ? 0.2076 0.0792 0.1415 -0.0257 0.0184  -0.0306 99  SER A O   
796  C  CB  . SER A 99  ? 0.1469 0.0678 0.1303 0.0270  0.0287  -0.0367 99  SER A CB  
797  O  OG  . SER A 99  ? 0.1292 0.0665 0.1784 0.0016  0.0081  0.0081  99  SER A OG  
798  N  N   . LEU A 100 ? 0.1148 0.0644 0.1293 -0.0201 0.0285  0.0048  100 LEU A N   
799  C  CA  . LEU A 100 ? 0.1124 0.0372 0.1544 -0.0093 0.0260  -0.0116 100 LEU A CA  
800  C  C   . LEU A 100 ? 0.1440 0.0612 0.1160 -0.0093 0.0392  -0.0248 100 LEU A C   
801  O  O   . LEU A 100 ? 0.1742 0.0532 0.1023 -0.0021 0.0154  -0.0111 100 LEU A O   
802  C  CB  . LEU A 100 ? 0.1508 0.0741 0.1476 0.0130  0.0203  -0.0027 100 LEU A CB  
803  C  CG  . LEU A 100 ? 0.1649 0.0864 0.1509 0.0234  0.0201  -0.0203 100 LEU A CG  
804  C  CD1 . LEU A 100 ? 0.1983 0.1886 0.2266 0.0822  -0.0348 -0.0168 100 LEU A CD1 
805  C  CD2 . LEU A 100 ? 0.2090 0.1386 0.1469 -0.0032 0.0559  -0.0567 100 LEU A CD2 
806  N  N   . ASP A 101 ? 0.1214 0.0523 0.1497 0.0061  0.0322  -0.0132 101 ASP A N   
807  C  CA  . ASP A 101 ? 0.1264 0.0644 0.1548 0.0108  0.0309  0.0089  101 ASP A CA  
808  C  C   . ASP A 101 ? 0.1727 0.0696 0.1483 0.0087  0.0518  0.0024  101 ASP A C   
809  O  O   . ASP A 101 ? 0.2263 0.0847 0.1789 0.0176  0.0838  0.0047  101 ASP A O   
810  C  CB  . ASP A 101 ? 0.1465 0.0670 0.1843 -0.0102 0.0321  0.0201  101 ASP A CB  
811  C  CG  . ASP A 101 ? 0.1655 0.0944 0.2047 -0.0136 0.0063  -0.0142 101 ASP A CG  
812  O  OD1 . ASP A 101 ? 0.1698 0.0893 0.1641 0.0002  0.0058  -0.0186 101 ASP A OD1 
813  O  OD2 . ASP A 101 ? 0.2532 0.1580 0.2359 -0.0810 0.0074  -0.0677 101 ASP A OD2 
814  N  N   . GLY A 102 ? 0.1724 0.0847 0.1272 -0.0526 0.0154  -0.0030 102 GLY A N   
815  C  CA  . GLY A 102 ? 0.2191 0.1267 0.1311 -0.0498 0.0122  -0.0227 102 GLY A CA  
816  C  C   . GLY A 102 ? 0.2126 0.1005 0.1203 -0.0450 0.0106  0.0089  102 GLY A C   
817  O  O   . GLY A 102 ? 0.2055 0.1268 0.1322 -0.0463 0.0114  0.0156  102 GLY A O   
818  N  N   . GLN A 103 ? 0.1418 0.0563 0.1437 -0.0179 0.0260  -0.0042 103 GLN A N   
819  C  CA  . GLN A 103 ? 0.1336 0.0685 0.1182 -0.0190 0.0164  -0.0100 103 GLN A CA  
820  C  C   . GLN A 103 ? 0.0850 0.0821 0.0988 -0.0182 0.0055  -0.0258 103 GLN A C   
821  O  O   . GLN A 103 ? 0.1285 0.0699 0.0999 -0.0154 -0.0035 -0.0234 103 GLN A O   
822  C  CB  . GLN A 103 ? 0.1565 0.0741 0.1153 -0.0044 0.0068  -0.0054 103 GLN A CB  
823  C  CG  . GLN A 103 ? 0.1595 0.0823 0.1230 0.0238  0.0136  -0.0106 103 GLN A CG  
824  C  CD  . GLN A 103 ? 0.1250 0.0967 0.1580 -0.0098 -0.0069 0.0027  103 GLN A CD  
825  O  OE1 . GLN A 103 ? 0.1713 0.1011 0.2152 0.0168  0.0171  0.0179  103 GLN A OE1 
826  N  NE2 . GLN A 103 ? 0.1347 0.0819 0.1990 0.0222  0.0384  0.0134  103 GLN A NE2 
827  N  N   . GLY A 104 ? 0.1177 0.0449 0.0830 0.0122  0.0264  -0.0124 104 GLY A N   
828  C  CA  . GLY A 104 ? 0.0967 0.0653 0.0927 0.0122  0.0155  0.0044  104 GLY A CA  
829  C  C   . GLY A 104 ? 0.0932 0.0726 0.0753 0.0071  0.0029  0.0031  104 GLY A C   
830  O  O   . GLY A 104 ? 0.1142 0.0811 0.1109 -0.0041 0.0061  0.0122  104 GLY A O   
831  N  N   . SER A 105 ? 0.0918 0.0636 0.0802 0.0093  0.0109  -0.0150 105 SER A N   
832  C  CA  . SER A 105 ? 0.0735 0.0588 0.0864 0.0000  0.0081  -0.0233 105 SER A CA  
833  C  C   . SER A 105 ? 0.0722 0.0677 0.0983 0.0004  0.0002  -0.0086 105 SER A C   
834  O  O   . SER A 105 ? 0.0837 0.0679 0.1153 0.0055  0.0008  0.0001  105 SER A O   
835  C  CB  . SER A 105 ? 0.0870 0.0724 0.0961 -0.0037 0.0095  0.0151  105 SER A CB  
836  O  OG  . SER A 105 ? 0.0974 0.0476 0.1124 -0.0006 0.0006  -0.0017 105 SER A OG  
837  N  N   . GLU A 106 ? 0.0864 0.0624 0.0798 -0.0012 0.0034  -0.0050 106 GLU A N   
838  C  CA  . GLU A 106 ? 0.0838 0.0549 0.0784 -0.0046 0.0000  0.0074  106 GLU A CA  
839  C  C   . GLU A 106 ? 0.0766 0.0496 0.0811 0.0026  0.0058  0.0006  106 GLU A C   
840  O  O   . GLU A 106 ? 0.0988 0.0487 0.0832 0.0009  0.0006  0.0131  106 GLU A O   
841  C  CB  . GLU A 106 ? 0.0994 0.0505 0.0956 -0.0016 0.0183  0.0044  106 GLU A CB  
842  C  CG  . GLU A 106 ? 0.0977 0.0729 0.0902 -0.0137 0.0098  0.0081  106 GLU A CG  
843  C  CD  . GLU A 106 ? 0.0771 0.0610 0.1088 0.0053  0.0055  0.0156  106 GLU A CD  
844  O  OE1 . GLU A 106 ? 0.0633 0.0656 0.1264 -0.0041 0.0052  -0.0134 106 GLU A OE1 
845  O  OE2 . GLU A 106 ? 0.0760 0.0681 0.1152 0.0034  0.0052  -0.0024 106 GLU A OE2 
846  N  N   . HIS A 107 ? 0.0794 0.0627 0.0897 0.0037  0.0174  -0.0035 107 HIS A N   
847  C  CA  . HIS A 107 ? 0.0807 0.0712 0.0952 0.0070  0.0144  0.0048  107 HIS A CA  
848  C  C   . HIS A 107 ? 0.0814 0.0784 0.0926 -0.0046 -0.0017 0.0032  107 HIS A C   
849  O  O   . HIS A 107 ? 0.0778 0.0697 0.0986 -0.0068 0.0022  0.0037  107 HIS A O   
850  C  CB  . HIS A 107 ? 0.0802 0.0559 0.1055 0.0099  -0.0047 -0.0083 107 HIS A CB  
851  C  CG  . HIS A 107 ? 0.0625 0.0593 0.0906 0.0008  0.0049  0.0019  107 HIS A CG  
852  N  ND1 . HIS A 107 ? 0.0870 0.0507 0.0880 0.0072  0.0165  0.0010  107 HIS A ND1 
853  C  CD2 . HIS A 107 ? 0.0602 0.0566 0.1044 0.0043  0.0055  -0.0140 107 HIS A CD2 
854  C  CE1 . HIS A 107 ? 0.0751 0.0738 0.0972 0.0070  -0.0131 -0.0231 107 HIS A CE1 
855  N  NE2 . HIS A 107 ? 0.0839 0.0680 0.0909 -0.0009 0.0012  0.0044  107 HIS A NE2 
856  N  N   . THR A 108 ? 0.1157 0.0633 0.0979 -0.0076 0.0161  0.0119  108 THR A N   
857  C  CA  . THR A 108 ? 0.1196 0.0626 0.1177 -0.0074 0.0157  0.0167  108 THR A CA  
858  C  C   . THR A 108 ? 0.1152 0.0496 0.0925 0.0057  -0.0008 0.0236  108 THR A C   
859  O  O   . THR A 108 ? 0.1133 0.0884 0.1023 -0.0050 0.0061  0.0043  108 THR A O   
860  C  CB  . THR A 108 ? 0.1239 0.1021 0.1099 0.0067  -0.0075 0.0103  108 THR A CB  
861  O  OG1 . THR A 108 ? 0.1164 0.0656 0.1234 0.0068  -0.0049 0.0115  108 THR A OG1 
862  C  CG2 . THR A 108 ? 0.1358 0.1039 0.1176 0.0162  0.0003  -0.0063 108 THR A CG2 
863  N  N   . VAL A 109 ? 0.1358 0.0823 0.1376 -0.0200 0.0081  0.0530  109 VAL A N   
864  C  CA  . VAL A 109 ? 0.1243 0.1243 0.1343 -0.0361 -0.0050 0.0578  109 VAL A CA  
865  C  C   . VAL A 109 ? 0.1329 0.1058 0.1335 -0.0329 0.0077  0.0390  109 VAL A C   
866  O  O   . VAL A 109 ? 0.1742 0.1027 0.1692 -0.0436 0.0053  0.0389  109 VAL A O   
867  C  CB  . VAL A 109 ? 0.1314 0.1297 0.1534 0.0055  -0.0055 0.0639  109 VAL A CB  
868  C  CG1 . VAL A 109 ? 0.1257 0.1598 0.2044 -0.0047 0.0214  0.0640  109 VAL A CG1 
869  C  CG2 . VAL A 109 ? 0.1439 0.0996 0.1921 0.0065  0.0294  0.0623  109 VAL A CG2 
870  N  N   . ASP A 110 ? 0.1674 0.0990 0.1182 -0.0165 0.0047  0.0596  110 ASP A N   
871  C  CA  . ASP A 110 ? 0.1440 0.1245 0.1468 0.0122  0.0218  0.0784  110 ASP A CA  
872  C  C   . ASP A 110 ? 0.1918 0.1164 0.1340 -0.0061 0.0298  0.0498  110 ASP A C   
873  O  O   . ASP A 110 ? 0.2022 0.1094 0.1759 0.0064  -0.0136 0.0533  110 ASP A O   
874  C  CB  . ASP A 110 ? 0.2089 0.1328 0.2000 -0.0050 0.0343  0.1402  110 ASP A CB  
875  C  CG  . ASP A 110 ? 0.2015 0.1738 0.1983 -0.0068 0.0117  0.1342  110 ASP A CG  
876  O  OD1 . ASP A 110 ? 0.1831 0.1749 0.2450 0.0058  0.0403  0.0811  110 ASP A OD1 
877  O  OD2 . ASP A 110 ? 0.1911 0.2975 0.2216 -0.0564 0.0292  0.0734  110 ASP A OD2 
878  N  N   . LYS A 111 ? 0.1278 0.1078 0.1476 -0.0048 0.0012  0.0318  111 LYS A N   
879  C  CA  . LYS A 111 ? 0.1480 0.0906 0.1559 0.0249  -0.0008 0.0303  111 LYS A CA  
880  C  C   . LYS A 111 ? 0.1688 0.0794 0.1918 -0.0063 -0.0111 0.0442  111 LYS A C   
881  O  O   . LYS A 111 ? 0.1777 0.1264 0.1897 -0.0063 -0.0141 0.0392  111 LYS A O   
882  C  CB  . LYS A 111 ? 0.2129 0.1221 0.1462 0.0446  -0.0322 0.0390  111 LYS A CB  
883  C  CG  . LYS A 111 ? 0.2312 0.1505 0.1760 0.0523  -0.0714 0.0242  111 LYS A CG  
884  C  CD  . LYS A 111 ? 0.2180 0.2248 0.2752 0.0152  -0.0499 -0.0260 111 LYS A CD  
885  C  CE  . LYS A 111 ? 0.3395 0.3139 0.1900 0.0670  -0.0701 0.0063  111 LYS A CE  
886  N  NZ  . LYS A 111 ? 0.3726 0.3240 0.3448 0.0879  -0.1316 -0.0122 111 LYS A NZ  
887  N  N   . LYS A 112 ? 0.1573 0.0961 0.1476 -0.0103 -0.0142 0.0575  112 LYS A N   
888  C  CA  . LYS A 112 ? 0.2152 0.1232 0.1652 -0.0629 -0.0089 0.0502  112 LYS A CA  
889  C  C   . LYS A 112 ? 0.1710 0.0802 0.1386 -0.0079 0.0068  0.0238  112 LYS A C   
890  O  O   . LYS A 112 ? 0.1422 0.0911 0.1394 -0.0050 0.0120  -0.0088 112 LYS A O   
891  C  CB  . LYS A 112 ? 0.2014 0.1249 0.1814 -0.0854 -0.0311 0.0256  112 LYS A CB  
892  C  CG  . LYS A 112 ? 0.2295 0.1436 0.1705 -0.0901 0.0157  -0.0317 112 LYS A CG  
893  C  CD  . LYS A 112 ? 0.2323 0.2033 0.2213 -0.0893 0.0072  0.0329  112 LYS A CD  
894  C  CE  . LYS A 112 ? 0.2684 0.3567 0.2326 -0.0551 0.0134  -0.0410 112 LYS A CE  
895  N  NZ  . LYS A 112 ? 0.5136 0.2424 0.3579 -0.0293 -0.1071 0.0464  112 LYS A NZ  
896  N  N   . LYS A 113 ? 0.1688 0.0674 0.1541 -0.0027 0.0137  0.0140  113 LYS A N   
897  C  CA  . LYS A 113 ? 0.1408 0.1088 0.1304 -0.0013 0.0089  0.0144  113 LYS A CA  
898  C  C   . LYS A 113 ? 0.1247 0.0882 0.1588 -0.0114 -0.0020 0.0230  113 LYS A C   
899  O  O   . LYS A 113 ? 0.1965 0.0762 0.2119 -0.0140 -0.0288 0.0343  113 LYS A O   
900  C  CB  . LYS A 113 ? 0.1448 0.0983 0.1562 0.0063  0.0142  -0.0332 113 LYS A CB  
901  C  CG  . LYS A 113 ? 0.1350 0.0884 0.1498 0.0030  0.0099  0.0151  113 LYS A CG  
902  C  CD  . LYS A 113 ? 0.1534 0.1221 0.1860 0.0292  0.0031  -0.0145 113 LYS A CD  
903  C  CE  . LYS A 113 ? 0.1871 0.1128 0.2001 -0.0167 -0.0228 0.0458  113 LYS A CE  
904  N  NZ  . LYS A 113 ? 0.3234 0.1544 0.4891 0.0665  -0.1439 -0.0096 113 LYS A NZ  
905  N  N   . TYR A 114 ? 0.1106 0.0935 0.1062 0.0069  0.0146  0.0033  114 TYR A N   
906  C  CA  . TYR A 114 ? 0.0986 0.0769 0.1155 0.0148  0.0135  0.0072  114 TYR A CA  
907  C  C   . TYR A 114 ? 0.1084 0.0618 0.1065 0.0080  0.0029  0.0011  114 TYR A C   
908  O  O   . TYR A 114 ? 0.1012 0.0663 0.1216 -0.0044 0.0119  -0.0122 114 TYR A O   
909  C  CB  . TYR A 114 ? 0.0785 0.0900 0.1548 0.0150  0.0206  0.0059  114 TYR A CB  
910  C  CG  . TYR A 114 ? 0.1072 0.0685 0.1315 0.0108  0.0082  -0.0085 114 TYR A CG  
911  C  CD1 . TYR A 114 ? 0.1868 0.0943 0.1139 0.0128  0.0033  0.0268  114 TYR A CD1 
912  C  CD2 . TYR A 114 ? 0.1256 0.0918 0.1645 -0.0189 0.0223  0.0314  114 TYR A CD2 
913  C  CE1 . TYR A 114 ? 0.1800 0.1195 0.1493 0.0365  0.0070  0.0207  114 TYR A CE1 
914  C  CE2 . TYR A 114 ? 0.1393 0.1322 0.1771 -0.0021 0.0383  0.0395  114 TYR A CE2 
915  C  CZ  . TYR A 114 ? 0.1724 0.1655 0.1588 0.0121  0.0507  0.0638  114 TYR A CZ  
916  O  OH  . TYR A 114 ? 0.2788 0.2852 0.2223 0.0792  0.1307  0.1005  114 TYR A OH  
917  N  N   . ALA A 115 ? 0.1315 0.0602 0.0918 -0.0087 0.0100  -0.0069 115 ALA A N   
918  C  CA  . ALA A 115 ? 0.1261 0.0591 0.0970 -0.0040 0.0088  -0.0135 115 ALA A CA  
919  C  C   . ALA A 115 ? 0.0905 0.0659 0.1279 -0.0068 -0.0009 -0.0026 115 ALA A C   
920  O  O   . ALA A 115 ? 0.0906 0.0722 0.1368 -0.0127 0.0089  -0.0221 115 ALA A O   
921  C  CB  . ALA A 115 ? 0.1389 0.0443 0.1487 -0.0173 -0.0062 -0.0290 115 ALA A CB  
922  N  N   . ALA A 116 ? 0.0959 0.0598 0.1171 -0.0138 0.0026  0.0006  116 ALA A N   
923  C  CA  . ALA A 116 ? 0.1297 0.0549 0.1074 0.0047  0.0197  0.0040  116 ALA A CA  
924  C  C   . ALA A 116 ? 0.0926 0.0645 0.0945 0.0016  0.0006  0.0038  116 ALA A C   
925  O  O   . ALA A 116 ? 0.0961 0.0690 0.1015 -0.0082 0.0119  -0.0228 116 ALA A O   
926  C  CB  . ALA A 116 ? 0.1164 0.0776 0.1058 0.0091  0.0100  0.0032  116 ALA A CB  
927  N  N   . GLU A 117 ? 0.0794 0.0583 0.1008 0.0066  0.0066  -0.0026 117 GLU A N   
928  C  CA  . GLU A 117 ? 0.1177 0.0489 0.0871 0.0187  -0.0122 -0.0027 117 GLU A CA  
929  C  C   . GLU A 117 ? 0.0757 0.0540 0.0902 -0.0013 -0.0062 0.0027  117 GLU A C   
930  O  O   . GLU A 117 ? 0.0943 0.0705 0.1017 -0.0013 0.0134  -0.0077 117 GLU A O   
931  C  CB  . GLU A 117 ? 0.0927 0.0854 0.0848 0.0010  0.0060  -0.0124 117 GLU A CB  
932  C  CG  . GLU A 117 ? 0.1008 0.0724 0.0823 0.0017  -0.0041 -0.0164 117 GLU A CG  
933  C  CD  . GLU A 117 ? 0.0820 0.0522 0.0884 -0.0031 0.0047  -0.0041 117 GLU A CD  
934  O  OE1 . GLU A 117 ? 0.0708 0.0717 0.1039 0.0013  -0.0049 0.0023  117 GLU A OE1 
935  O  OE2 . GLU A 117 ? 0.1058 0.0632 0.0830 -0.0044 -0.0174 -0.0095 117 GLU A OE2 
936  N  N   . LEU A 118 ? 0.0784 0.0460 0.0918 0.0009  -0.0049 0.0036  118 LEU A N   
937  C  CA  . LEU A 118 ? 0.0805 0.0417 0.0972 0.0050  -0.0116 -0.0024 118 LEU A CA  
938  C  C   . LEU A 118 ? 0.0906 0.0462 0.0812 0.0041  0.0031  0.0030  118 LEU A C   
939  O  O   . LEU A 118 ? 0.0828 0.0513 0.0873 0.0069  0.0122  -0.0022 118 LEU A O   
940  C  CB  . LEU A 118 ? 0.0820 0.0577 0.1196 0.0070  -0.0234 0.0118  118 LEU A CB  
941  C  CG  . LEU A 118 ? 0.0836 0.0661 0.0997 0.0149  -0.0066 0.0167  118 LEU A CG  
942  C  CD1 . LEU A 118 ? 0.1124 0.0677 0.0979 -0.0043 -0.0204 0.0168  118 LEU A CD1 
943  C  CD2 . LEU A 118 ? 0.0902 0.0986 0.1307 0.0024  -0.0238 0.0040  118 LEU A CD2 
944  N  N   . HIS A 119 ? 0.0853 0.0432 0.0678 0.0008  -0.0016 -0.0005 119 HIS A N   
945  C  CA  . HIS A 119 ? 0.0704 0.0602 0.0741 0.0004  -0.0119 -0.0109 119 HIS A CA  
946  C  C   . HIS A 119 ? 0.0759 0.0699 0.0617 -0.0051 -0.0111 0.0011  119 HIS A C   
947  O  O   . HIS A 119 ? 0.1069 0.0669 0.0771 0.0000  0.0089  -0.0001 119 HIS A O   
948  C  CB  . HIS A 119 ? 0.0712 0.0443 0.0882 -0.0010 -0.0088 0.0059  119 HIS A CB  
949  C  CG  . HIS A 119 ? 0.0805 0.0556 0.0540 0.0027  -0.0105 -0.0046 119 HIS A CG  
950  N  ND1 . HIS A 119 ? 0.0793 0.0476 0.0812 -0.0085 -0.0044 0.0019  119 HIS A ND1 
951  C  CD2 . HIS A 119 ? 0.0785 0.0690 0.0615 -0.0100 -0.0126 0.0002  119 HIS A CD2 
952  C  CE1 . HIS A 119 ? 0.0880 0.0426 0.0911 -0.0162 -0.0116 0.0046  119 HIS A CE1 
953  N  NE2 . HIS A 119 ? 0.0724 0.0701 0.0823 -0.0004 -0.0089 -0.0166 119 HIS A NE2 
954  N  N   . LEU A 120 ? 0.0926 0.0393 0.0803 0.0017  -0.0033 0.0019  120 LEU A N   
955  C  CA  . LEU A 120 ? 0.0818 0.0478 0.0961 0.0057  -0.0050 0.0048  120 LEU A CA  
956  C  C   . LEU A 120 ? 0.0961 0.0503 0.0753 0.0055  0.0009  0.0080  120 LEU A C   
957  O  O   . LEU A 120 ? 0.0830 0.0571 0.0785 0.0043  -0.0015 0.0089  120 LEU A O   
958  C  CB  . LEU A 120 ? 0.0829 0.0505 0.1124 0.0017  -0.0107 -0.0151 120 LEU A CB  
959  C  CG  . LEU A 120 ? 0.1017 0.0593 0.1127 -0.0179 -0.0397 0.0055  120 LEU A CG  
960  C  CD1 . LEU A 120 ? 0.2076 0.0945 0.1523 -0.0491 -0.0245 0.0378  120 LEU A CD1 
961  C  CD2 . LEU A 120 ? 0.1134 0.1332 0.1422 0.0392  -0.0457 -0.0078 120 LEU A CD2 
962  N  N   . VAL A 121 ? 0.0685 0.0617 0.0906 -0.0059 -0.0038 -0.0006 121 VAL A N   
963  C  CA  . VAL A 121 ? 0.1073 0.0417 0.0999 -0.0118 0.0022  -0.0031 121 VAL A CA  
964  C  C   . VAL A 121 ? 0.1297 0.0472 0.0875 -0.0008 0.0087  0.0129  121 VAL A C   
965  O  O   . VAL A 121 ? 0.1311 0.0636 0.1028 0.0021  -0.0049 0.0135  121 VAL A O   
966  C  CB  . VAL A 121 ? 0.0963 0.0593 0.1137 -0.0053 -0.0031 0.0073  121 VAL A CB  
967  C  CG1 . VAL A 121 ? 0.1049 0.1056 0.1555 -0.0304 -0.0018 -0.0156 121 VAL A CG1 
968  C  CG2 . VAL A 121 ? 0.0807 0.0672 0.1311 0.0005  -0.0118 0.0102  121 VAL A CG2 
969  N  N   . HIS A 122 ? 0.0899 0.0364 0.1084 -0.0050 0.0038  -0.0044 122 HIS A N   
970  C  CA  . HIS A 122 ? 0.0935 0.0276 0.1254 -0.0121 0.0192  -0.0077 122 HIS A CA  
971  C  C   . HIS A 122 ? 0.1132 0.0490 0.0908 -0.0124 0.0026  0.0051  122 HIS A C   
972  O  O   . HIS A 122 ? 0.1120 0.0650 0.1311 -0.0108 -0.0201 0.0068  122 HIS A O   
973  C  CB  . HIS A 122 ? 0.0850 0.0674 0.1186 -0.0103 0.0097  0.0061  122 HIS A CB  
974  C  CG  . HIS A 122 ? 0.1163 0.0401 0.0987 -0.0012 0.0044  0.0030  122 HIS A CG  
975  N  ND1 . HIS A 122 ? 0.0812 0.0520 0.1317 0.0059  0.0000  0.0240  122 HIS A ND1 
976  C  CD2 . HIS A 122 ? 0.1074 0.0864 0.1047 -0.0098 0.0082  -0.0009 122 HIS A CD2 
977  C  CE1 . HIS A 122 ? 0.0714 0.0954 0.1278 -0.0021 0.0015  -0.0017 122 HIS A CE1 
978  N  NE2 . HIS A 122 ? 0.0873 0.0899 0.1272 -0.0062 -0.0079 0.0054  122 HIS A NE2 
979  N  N   . TRP A 123 ? 0.1115 0.0401 0.1159 -0.0099 0.0044  -0.0082 123 TRP A N   
980  C  CA  . TRP A 123 ? 0.1049 0.0434 0.1155 -0.0178 0.0154  -0.0172 123 TRP A CA  
981  C  C   . TRP A 123 ? 0.0997 0.0507 0.1120 0.0033  0.0046  0.0102  123 TRP A C   
982  O  O   . TRP A 123 ? 0.1074 0.0532 0.1279 0.0122  -0.0070 0.0013  123 TRP A O   
983  C  CB  . TRP A 123 ? 0.1083 0.0924 0.1073 -0.0082 0.0053  0.0163  123 TRP A CB  
984  C  CG  . TRP A 123 ? 0.1357 0.0773 0.1189 -0.0176 -0.0071 0.0177  123 TRP A CG  
985  C  CD1 . TRP A 123 ? 0.1225 0.0968 0.1030 -0.0237 -0.0038 0.0197  123 TRP A CD1 
986  C  CD2 . TRP A 123 ? 0.1293 0.0731 0.1468 -0.0173 0.0062  0.0118  123 TRP A CD2 
987  N  NE1 . TRP A 123 ? 0.1760 0.0742 0.1150 -0.0185 -0.0248 -0.0011 123 TRP A NE1 
988  C  CE2 . TRP A 123 ? 0.1713 0.0539 0.1408 -0.0400 0.0009  0.0088  123 TRP A CE2 
989  C  CE3 . TRP A 123 ? 0.1253 0.0532 0.1796 -0.0337 0.0077  0.0174  123 TRP A CE3 
990  C  CZ2 . TRP A 123 ? 0.2137 0.0584 0.1376 -0.0345 0.0171  0.0193  123 TRP A CZ2 
991  C  CZ3 . TRP A 123 ? 0.1990 0.0557 0.1382 -0.0445 -0.0124 0.0186  123 TRP A CZ3 
992  C  CH2 . TRP A 123 ? 0.2155 0.0798 0.1272 -0.0156 0.0030  0.0074  123 TRP A CH2 
993  N  N   . ASN A 124 ? 0.1207 0.0724 0.1073 -0.0138 0.0158  -0.0081 124 ASN A N   
994  C  CA  . ASN A 124 ? 0.1168 0.0627 0.1552 0.0199  0.0066  -0.0113 124 ASN A CA  
995  C  C   . ASN A 124 ? 0.1354 0.0669 0.1509 -0.0136 -0.0004 -0.0103 124 ASN A C   
996  O  O   . ASN A 124 ? 0.1188 0.0730 0.1483 -0.0125 0.0054  -0.0181 124 ASN A O   
997  C  CB  . ASN A 124 ? 0.1529 0.1128 0.1027 -0.0354 0.0251  -0.0148 124 ASN A CB  
998  C  CG  . ASN A 124 ? 0.1874 0.1207 0.1534 -0.0229 0.0429  -0.0329 124 ASN A CG  
999  O  OD1 . ASN A 124 ? 0.1839 0.1214 0.1936 -0.0212 0.0403  -0.0291 124 ASN A OD1 
1000 N  ND2 . ASN A 124 ? 0.2573 0.1250 0.1368 -0.0198 0.0326  -0.0282 124 ASN A ND2 
1001 N  N   . THR A 125 ? 0.1512 0.0672 0.1595 0.0138  -0.0052 -0.0149 125 THR A N   
1002 C  CA  . THR A 125 ? 0.1688 0.0794 0.1706 0.0099  0.0095  -0.0019 125 THR A CA  
1003 C  C   . THR A 125 ? 0.1346 0.1015 0.1627 -0.0121 0.0357  -0.0091 125 THR A C   
1004 O  O   . THR A 125 ? 0.1365 0.1074 0.2150 -0.0088 0.0332  0.0126  125 THR A O   
1005 C  CB  . THR A 125 ? 0.1602 0.1089 0.2029 0.0218  -0.0047 -0.0219 125 THR A CB  
1006 O  OG1 . THR A 125 ? 0.1940 0.1310 0.2791 0.0368  0.0348  -0.0154 125 THR A OG1 
1007 C  CG2 . THR A 125 ? 0.2716 0.1227 0.2505 0.0027  -0.0035 -0.0509 125 THR A CG2 
1008 N  N   . LYS A 126 ? 0.1907 0.0629 0.1735 0.0173  0.0342  -0.0494 126 LYS A N   
1009 C  CA  . LYS A 126 ? 0.1900 0.1039 0.2004 -0.0326 0.0604  -0.0695 126 LYS A CA  
1010 C  C   . LYS A 126 ? 0.1498 0.0899 0.2367 -0.0243 0.0206  -0.0395 126 LYS A C   
1011 O  O   . LYS A 126 ? 0.2008 0.1014 0.2780 -0.0335 0.0449  -0.0829 126 LYS A O   
1012 C  CB  . LYS A 126 ? 0.2726 0.1412 0.1942 -0.0440 0.0328  -0.0974 126 LYS A CB  
1013 C  CG  . LYS A 126 ? 0.2647 0.2161 0.1978 -0.0223 0.0499  -0.0804 126 LYS A CG  
1014 C  CD  . LYS A 126 ? 0.4062 0.2921 0.2104 -0.0280 0.0875  -0.0475 126 LYS A CD  
1015 C  CE  . LYS A 126 ? 0.3731 0.4031 0.2698 0.0044  0.0977  -0.0029 126 LYS A CE  
1016 N  NZ  . LYS A 126 ? 0.6849 0.6862 0.1965 -0.1283 0.1151  0.1608  126 LYS A NZ  
1017 N  N   . TYR A 127 ? 0.1620 0.0954 0.1680 -0.0092 0.0110  -0.0161 127 TYR A N   
1018 C  CA  . TYR A 127 ? 0.1419 0.0909 0.1515 -0.0099 -0.0076 -0.0177 127 TYR A CA  
1019 C  C   . TYR A 127 ? 0.1576 0.0671 0.1591 -0.0008 0.0120  -0.0099 127 TYR A C   
1020 O  O   . TYR A 127 ? 0.1559 0.0970 0.1893 -0.0292 0.0236  -0.0162 127 TYR A O   
1021 C  CB  . TYR A 127 ? 0.1523 0.0942 0.1354 -0.0005 0.0128  -0.0047 127 TYR A CB  
1022 C  CG  . TYR A 127 ? 0.1990 0.0839 0.1354 -0.0092 0.0019  -0.0095 127 TYR A CG  
1023 C  CD1 . TYR A 127 ? 0.2234 0.1368 0.1530 -0.0124 -0.0193 -0.0370 127 TYR A CD1 
1024 C  CD2 . TYR A 127 ? 0.1577 0.0988 0.1541 -0.0343 0.0184  -0.0025 127 TYR A CD2 
1025 C  CE1 . TYR A 127 ? 0.2640 0.0961 0.1451 -0.0205 0.0150  -0.0287 127 TYR A CE1 
1026 C  CE2 . TYR A 127 ? 0.1892 0.1044 0.1476 -0.0019 -0.0003 -0.0227 127 TYR A CE2 
1027 C  CZ  . TYR A 127 ? 0.2655 0.1093 0.1332 -0.0147 0.0029  -0.0188 127 TYR A CZ  
1028 O  OH  . TYR A 127 ? 0.3574 0.1534 0.1315 0.0071  0.0218  -0.0162 127 TYR A OH  
1029 N  N   . GLY A 128 ? 0.1469 0.0829 0.1304 -0.0173 0.0173  0.0013  128 GLY A N   
1030 C  CA  . GLY A 128 ? 0.1595 0.0518 0.1461 -0.0009 0.0362  0.0032  128 GLY A CA  
1031 C  C   . GLY A 128 ? 0.1703 0.0469 0.1390 -0.0069 0.0033  -0.0026 128 GLY A C   
1032 O  O   . GLY A 128 ? 0.1558 0.1124 0.1720 0.0195  -0.0161 0.0168  128 GLY A O   
1033 N  N   . ASP A 129 ? 0.1631 0.0694 0.1591 -0.0010 0.0248  0.0067  129 ASP A N   
1034 C  CA  . ASP A 129 ? 0.1580 0.0908 0.1465 0.0124  0.0006  -0.0022 129 ASP A CA  
1035 C  C   . ASP A 129 ? 0.1534 0.0864 0.1329 -0.0040 -0.0108 -0.0146 129 ASP A C   
1036 O  O   . ASP A 129 ? 0.1680 0.0776 0.1455 -0.0071 -0.0303 -0.0254 129 ASP A O   
1037 C  CB  . ASP A 129 ? 0.1353 0.1491 0.1060 0.0032  -0.0066 0.0055  129 ASP A CB  
1038 C  CG  . ASP A 129 ? 0.1394 0.1082 0.1527 0.0145  -0.0184 -0.0625 129 ASP A CG  
1039 O  OD1 . ASP A 129 ? 0.1685 0.1440 0.1820 -0.0046 -0.0151 0.0316  129 ASP A OD1 
1040 O  OD2 . ASP A 129 ? 0.2033 0.1003 0.1832 -0.0136 -0.0050 0.0031  129 ASP A OD2 
1041 N  N   . TYR A 130 ? 0.1469 0.0679 0.1372 -0.0189 0.0146  -0.0071 130 TYR A N   
1042 C  CA  . TYR A 130 ? 0.1591 0.0641 0.1379 -0.0278 0.0165  0.0015  130 TYR A CA  
1043 C  C   . TYR A 130 ? 0.1425 0.0864 0.1182 -0.0008 0.0364  0.0167  130 TYR A C   
1044 O  O   . TYR A 130 ? 0.1756 0.1120 0.1339 0.0074  0.0147  0.0253  130 TYR A O   
1045 C  CB  . TYR A 130 ? 0.2335 0.0647 0.1401 -0.0248 0.0534  -0.0242 130 TYR A CB  
1046 C  CG  . TYR A 130 ? 0.2177 0.0900 0.1677 -0.0387 0.0602  0.0061  130 TYR A CG  
1047 C  CD1 . TYR A 130 ? 0.2209 0.1178 0.2040 -0.0509 0.1000  0.0139  130 TYR A CD1 
1048 C  CD2 . TYR A 130 ? 0.2676 0.0994 0.1333 -0.0287 0.0688  -0.0176 130 TYR A CD2 
1049 C  CE1 . TYR A 130 ? 0.3459 0.1336 0.1695 -0.0666 0.1086  -0.0097 130 TYR A CE1 
1050 C  CE2 . TYR A 130 ? 0.2561 0.1053 0.1986 -0.0547 0.1178  -0.0167 130 TYR A CE2 
1051 C  CZ  . TYR A 130 ? 0.2575 0.1101 0.1785 -0.0141 0.0905  -0.0512 130 TYR A CZ  
1052 O  OH  . TYR A 130 ? 0.3556 0.1491 0.2252 -0.0159 0.1582  -0.0297 130 TYR A OH  
1053 N  N   . GLY A 131 ? 0.1188 0.1196 0.1674 -0.0218 0.0331  0.0264  131 GLY A N   
1054 C  CA  . GLY A 131 ? 0.1115 0.1889 0.1828 -0.0274 0.0294  0.0526  131 GLY A CA  
1055 C  C   . GLY A 131 ? 0.1491 0.1419 0.2064 -0.0343 0.0074  0.0462  131 GLY A C   
1056 O  O   . GLY A 131 ? 0.1868 0.1914 0.2356 0.0099  -0.0332 0.0321  131 GLY A O   
1057 N  N   A LYS A 132 ? 0.1498 0.1005 0.1953 -0.0484 -0.0120 0.0416  132 LYS A N   
1058 N  N   B LYS A 132 ? 0.1516 0.1137 0.1799 -0.0491 -0.0178 0.0228  132 LYS A N   
1059 C  CA  A LYS A 132 ? 0.1645 0.0837 0.1896 -0.0297 -0.0027 0.0483  132 LYS A CA  
1060 C  CA  B LYS A 132 ? 0.1706 0.1094 0.1699 -0.0389 0.0002  0.0319  132 LYS A CA  
1061 C  C   A LYS A 132 ? 0.1171 0.1221 0.1760 -0.0630 -0.0132 0.0377  132 LYS A C   
1062 C  C   B LYS A 132 ? 0.1112 0.1271 0.1498 -0.0495 -0.0309 0.0286  132 LYS A C   
1063 O  O   A LYS A 132 ? 0.1800 0.1448 0.1910 -0.0471 -0.0374 0.0325  132 LYS A O   
1064 O  O   B LYS A 132 ? 0.1433 0.1473 0.1537 -0.0491 -0.0467 0.0127  132 LYS A O   
1065 C  CB  A LYS A 132 ? 0.1666 0.0999 0.1918 -0.0087 -0.0302 0.0497  132 LYS A CB  
1066 C  CB  B LYS A 132 ? 0.2036 0.1358 0.2008 -0.0047 -0.0283 0.0153  132 LYS A CB  
1067 C  CG  A LYS A 132 ? 0.1709 0.0575 0.1874 -0.0077 0.0132  0.0410  132 LYS A CG  
1068 C  CG  B LYS A 132 ? 0.3201 0.1232 0.1390 0.0376  0.0008  0.0901  132 LYS A CG  
1069 C  CD  A LYS A 132 ? 0.1875 0.1462 0.2320 -0.0292 -0.0468 0.1333  132 LYS A CD  
1070 C  CD  B LYS A 132 ? 0.3186 0.2827 0.3596 -0.0611 -0.0621 0.0634  132 LYS A CD  
1071 C  CE  A LYS A 132 ? 0.2712 0.1882 0.2576 -0.0267 -0.0085 0.1456  132 LYS A CE  
1072 C  CE  B LYS A 132 ? 0.3251 0.1857 0.4062 0.0615  -0.0974 -0.0078 132 LYS A CE  
1073 N  NZ  A LYS A 132 ? 0.2828 0.1652 0.3917 -0.0131 -0.0644 0.0126  132 LYS A NZ  
1074 N  NZ  B LYS A 132 ? 0.2734 0.2486 0.1566 0.0702  -0.0298 -0.0239 132 LYS A NZ  
1075 N  N   . ALA A 133 ? 0.1221 0.0739 0.1530 -0.0434 0.0083  -0.0146 133 ALA A N   
1076 C  CA  . ALA A 133 ? 0.1029 0.1056 0.1439 -0.0370 0.0004  0.0087  133 ALA A CA  
1077 C  C   . ALA A 133 ? 0.1132 0.1048 0.1529 -0.0299 0.0240  0.0301  133 ALA A C   
1078 O  O   . ALA A 133 ? 0.1224 0.1124 0.1580 0.0044  0.0055  0.0271  133 ALA A O   
1079 C  CB  . ALA A 133 ? 0.1250 0.0893 0.1426 -0.0464 -0.0050 -0.0069 133 ALA A CB  
1080 N  N   . VAL A 134 ? 0.1376 0.0952 0.1522 -0.0118 0.0251  0.0398  134 VAL A N   
1081 C  CA  . VAL A 134 ? 0.1706 0.1275 0.1641 0.0302  0.0287  0.0450  134 VAL A CA  
1082 C  C   . VAL A 134 ? 0.1021 0.1656 0.2187 0.0347  0.0310  0.0547  134 VAL A C   
1083 O  O   . VAL A 134 ? 0.1394 0.2338 0.3197 0.0743  0.0407  0.1241  134 VAL A O   
1084 C  CB  . VAL A 134 ? 0.1932 0.1473 0.2257 0.0453  0.0326  0.0071  134 VAL A CB  
1085 C  CG1 . VAL A 134 ? 0.2577 0.1243 0.1534 -0.0076 0.0268  0.0089  134 VAL A CG1 
1086 C  CG2 . VAL A 134 ? 0.2712 0.2427 0.3046 0.0588  0.1080  0.0828  134 VAL A CG2 
1087 N  N   . GLN A 135 ? 0.1221 0.1846 0.2019 -0.0258 0.0036  0.0898  135 GLN A N   
1088 C  CA  . GLN A 135 ? 0.1595 0.2440 0.2460 -0.0397 -0.0260 0.0664  135 GLN A CA  
1089 C  C   . GLN A 135 ? 0.1523 0.1947 0.2292 -0.0703 -0.0403 0.0477  135 GLN A C   
1090 O  O   . GLN A 135 ? 0.2118 0.3219 0.2423 -0.0917 -0.0807 0.0365  135 GLN A O   
1091 C  CB  . GLN A 135 ? 0.1879 0.2760 0.2830 -0.0919 -0.0687 0.0895  135 GLN A CB  
1092 C  CG  . GLN A 135 ? 0.2421 0.4284 0.3287 -0.1392 -0.0367 0.1284  135 GLN A CG  
1093 C  CD  . GLN A 135 ? 0.5942 0.4225 0.4715 -0.2052 -0.0313 0.1151  135 GLN A CD  
1094 O  OE1 . GLN A 135 ? 0.2583 0.5447 0.5045 -0.1170 0.0171  0.1062  135 GLN A OE1 
1095 N  NE2 . GLN A 135 ? 0.6728 0.4708 0.4684 -0.3285 -0.0095 0.2087  135 GLN A NE2 
1096 N  N   . GLN A 136 ? 0.1329 0.1685 0.1530 -0.0377 -0.0171 0.0700  136 GLN A N   
1097 C  CA  . GLN A 136 ? 0.1763 0.1181 0.1519 -0.0217 -0.0287 0.0024  136 GLN A CA  
1098 C  C   . GLN A 136 ? 0.1838 0.1247 0.1155 0.0000  -0.0245 -0.0026 136 GLN A C   
1099 O  O   . GLN A 136 ? 0.1645 0.1218 0.0993 0.0042  0.0003  -0.0098 136 GLN A O   
1100 C  CB  . GLN A 136 ? 0.1940 0.1261 0.1817 0.0015  -0.0287 0.0189  136 GLN A CB  
1101 C  CG  . GLN A 136 ? 0.2421 0.0949 0.2453 -0.0468 0.0085  0.0160  136 GLN A CG  
1102 C  CD  . GLN A 136 ? 0.1763 0.1911 0.1904 -0.0303 0.0049  -0.0122 136 GLN A CD  
1103 O  OE1 . GLN A 136 ? 0.2533 0.1753 0.1886 -0.0207 -0.0453 -0.0305 136 GLN A OE1 
1104 N  NE2 . GLN A 136 ? 0.2597 0.3003 0.2155 -0.0917 0.0345  0.0166  136 GLN A NE2 
1105 N  N   A PRO A 137 ? 0.1677 0.1264 0.1107 0.0092  -0.0192 -0.0344 137 PRO A N   
1106 N  N   B PRO A 137 ? 0.1853 0.1257 0.1102 0.0214  -0.0186 -0.0340 137 PRO A N   
1107 C  CA  A PRO A 137 ? 0.1656 0.1529 0.0990 0.0140  -0.0077 -0.0009 137 PRO A CA  
1108 C  CA  B PRO A 137 ? 0.1806 0.1558 0.1054 0.0185  -0.0065 0.0001  137 PRO A CA  
1109 C  C   A PRO A 137 ? 0.1731 0.1419 0.1014 -0.0006 0.0083  0.0076  137 PRO A C   
1110 C  C   B PRO A 137 ? 0.1882 0.1354 0.0938 0.0030  0.0098  0.0106  137 PRO A C   
1111 O  O   A PRO A 137 ? 0.1799 0.1336 0.2076 0.0026  -0.0010 0.0183  137 PRO A O   
1112 O  O   B PRO A 137 ? 0.1954 0.1300 0.2000 -0.0021 0.0146  0.0242  137 PRO A O   
1113 C  CB  A PRO A 137 ? 0.2026 0.2132 0.1017 0.0131  -0.0239 0.0016  137 PRO A CB  
1114 C  CB  B PRO A 137 ? 0.2407 0.2417 0.1023 0.0092  -0.0208 0.0134  137 PRO A CB  
1115 C  CG  A PRO A 137 ? 0.1627 0.2241 0.1107 0.0210  -0.0367 -0.0533 137 PRO A CG  
1116 C  CG  B PRO A 137 ? 0.2366 0.2697 0.1386 -0.0024 -0.0160 -0.0131 137 PRO A CG  
1117 C  CD  A PRO A 137 ? 0.2282 0.2197 0.1146 -0.0179 -0.0196 -0.0819 137 PRO A CD  
1118 C  CD  B PRO A 137 ? 0.1943 0.1695 0.1468 0.0214  -0.0451 -0.0581 137 PRO A CD  
1119 N  N   . ASP A 138 ? 0.1688 0.1491 0.0950 -0.0031 -0.0149 0.0050  138 ASP A N   
1120 C  CA  . ASP A 138 ? 0.1376 0.1852 0.1153 0.0102  0.0359  0.0359  138 ASP A CA  
1121 C  C   . ASP A 138 ? 0.1220 0.1282 0.1066 -0.0037 0.0143  -0.0079 138 ASP A C   
1122 O  O   . ASP A 138 ? 0.1354 0.1566 0.1307 0.0236  0.0102  -0.0117 138 ASP A O   
1123 C  CB  . ASP A 138 ? 0.2161 0.1824 0.1271 0.0317  0.0309  -0.0004 138 ASP A CB  
1124 C  CG  . ASP A 138 ? 0.2288 0.1932 0.1364 0.0031  0.0514  0.0088  138 ASP A CG  
1125 O  OD1 . ASP A 138 ? 0.1964 0.1494 0.1386 0.0222  0.0341  -0.0260 138 ASP A OD1 
1126 O  OD2 . ASP A 138 ? 0.2044 0.1949 0.2107 -0.0199 0.0443  -0.0565 138 ASP A OD2 
1127 N  N   . GLY A 139 ? 0.1397 0.0758 0.0767 -0.0042 0.0127  -0.0122 139 GLY A N   
1128 C  CA  . GLY A 139 ? 0.1225 0.0805 0.0977 -0.0289 -0.0100 0.0124  139 GLY A CA  
1129 C  C   . GLY A 139 ? 0.1083 0.0762 0.1040 -0.0075 -0.0051 -0.0047 139 GLY A C   
1130 O  O   . GLY A 139 ? 0.1523 0.0632 0.1146 0.0132  -0.0181 -0.0107 139 GLY A O   
1131 N  N   . LEU A 140 ? 0.0787 0.0681 0.0996 -0.0086 0.0170  -0.0214 140 LEU A N   
1132 C  CA  . LEU A 140 ? 0.0821 0.0636 0.0884 -0.0150 0.0190  -0.0200 140 LEU A CA  
1133 C  C   . LEU A 140 ? 0.0800 0.0616 0.0856 -0.0059 0.0034  -0.0132 140 LEU A C   
1134 O  O   . LEU A 140 ? 0.0972 0.0672 0.0985 -0.0120 -0.0080 -0.0107 140 LEU A O   
1135 C  CB  . LEU A 140 ? 0.0976 0.0938 0.0803 0.0039  0.0290  -0.0071 140 LEU A CB  
1136 C  CG  . LEU A 140 ? 0.1278 0.1005 0.1055 0.0222  0.0416  0.0150  140 LEU A CG  
1137 C  CD1 . LEU A 140 ? 0.1465 0.1024 0.1472 0.0485  0.0528  0.0182  140 LEU A CD1 
1138 C  CD2 . LEU A 140 ? 0.1839 0.0954 0.1511 0.0505  0.0342  0.0231  140 LEU A CD2 
1139 N  N   . ALA A 141 ? 0.0949 0.0481 0.1045 -0.0118 -0.0168 0.0025  141 ALA A N   
1140 C  CA  . ALA A 141 ? 0.0760 0.0540 0.1307 -0.0111 0.0159  -0.0063 141 ALA A CA  
1141 C  C   . ALA A 141 ? 0.0692 0.0573 0.1023 -0.0004 -0.0088 0.0176  141 ALA A C   
1142 O  O   . ALA A 141 ? 0.0961 0.0485 0.0961 0.0023  -0.0122 0.0157  141 ALA A O   
1143 C  CB  . ALA A 141 ? 0.0692 0.0647 0.1508 -0.0094 0.0164  0.0049  141 ALA A CB  
1144 N  N   . VAL A 142 ? 0.0780 0.0463 0.1062 0.0023  -0.0091 -0.0031 142 VAL A N   
1145 C  CA  . VAL A 142 ? 0.1022 0.0408 0.0918 0.0032  0.0248  -0.0020 142 VAL A CA  
1146 C  C   . VAL A 142 ? 0.0944 0.0443 0.0697 0.0011  0.0011  0.0033  142 VAL A C   
1147 O  O   . VAL A 142 ? 0.1008 0.0608 0.0726 0.0159  -0.0153 0.0009  142 VAL A O   
1148 C  CB  . VAL A 142 ? 0.0794 0.0549 0.0972 0.0013  -0.0046 -0.0072 142 VAL A CB  
1149 C  CG1 . VAL A 142 ? 0.1230 0.0435 0.1098 0.0194  -0.0022 -0.0122 142 VAL A CG1 
1150 C  CG2 . VAL A 142 ? 0.0877 0.1029 0.1037 -0.0138 0.0134  0.0057  142 VAL A CG2 
1151 N  N   . LEU A 143 ? 0.0821 0.0507 0.0911 -0.0013 -0.0096 0.0022  143 LEU A N   
1152 C  CA  . LEU A 143 ? 0.0717 0.0582 0.1080 -0.0048 -0.0156 -0.0097 143 LEU A CA  
1153 C  C   . LEU A 143 ? 0.0915 0.0619 0.0837 -0.0098 -0.0033 -0.0033 143 LEU A C   
1154 O  O   . LEU A 143 ? 0.1054 0.0715 0.0862 -0.0086 -0.0021 0.0055  143 LEU A O   
1155 C  CB  . LEU A 143 ? 0.0647 0.1004 0.1155 -0.0120 -0.0135 0.0151  143 LEU A CB  
1156 C  CG  . LEU A 143 ? 0.0820 0.0864 0.1347 -0.0175 -0.0189 0.0110  143 LEU A CG  
1157 C  CD1 . LEU A 143 ? 0.0983 0.1368 0.1533 -0.0275 -0.0171 0.0490  143 LEU A CD1 
1158 C  CD2 . LEU A 143 ? 0.1164 0.1278 0.1444 0.0228  -0.0212 0.0218  143 LEU A CD2 
1159 N  N   . GLY A 144 ? 0.0796 0.0398 0.0996 -0.0098 0.0029  -0.0069 144 GLY A N   
1160 C  CA  . GLY A 144 ? 0.0972 0.0364 0.0888 -0.0124 0.0095  -0.0066 144 GLY A CA  
1161 C  C   . GLY A 144 ? 0.0681 0.0568 0.0839 -0.0048 0.0002  0.0037  144 GLY A C   
1162 O  O   . GLY A 144 ? 0.1062 0.0708 0.1002 -0.0159 0.0179  0.0038  144 GLY A O   
1163 N  N   . ILE A 145 ? 0.0811 0.0443 0.0902 0.0050  0.0003  -0.0023 145 ILE A N   
1164 C  CA  . ILE A 145 ? 0.0890 0.0582 0.0818 -0.0100 -0.0041 -0.0035 145 ILE A CA  
1165 C  C   . ILE A 145 ? 0.0452 0.0577 0.0949 -0.0168 -0.0020 0.0122  145 ILE A C   
1166 O  O   . ILE A 145 ? 0.1045 0.0487 0.0988 -0.0100 0.0165  -0.0048 145 ILE A O   
1167 C  CB  . ILE A 145 ? 0.0866 0.0593 0.0981 -0.0086 0.0004  -0.0092 145 ILE A CB  
1168 C  CG1 . ILE A 145 ? 0.1433 0.0759 0.1465 0.0355  -0.0111 -0.0063 145 ILE A CG1 
1169 C  CG2 . ILE A 145 ? 0.0846 0.0943 0.1626 -0.0197 -0.0243 -0.0201 145 ILE A CG2 
1170 C  CD1 . ILE A 145 ? 0.1400 0.1042 0.1084 -0.0005 -0.0164 0.0173  145 ILE A CD1 
1171 N  N   . PHE A 146 ? 0.0681 0.0399 0.1002 -0.0019 0.0019  0.0047  146 PHE A N   
1172 C  CA  . PHE A 146 ? 0.0830 0.0443 0.0902 0.0032  -0.0013 -0.0037 146 PHE A CA  
1173 C  C   . PHE A 146 ? 0.0974 0.0662 0.0805 -0.0136 -0.0111 0.0243  146 PHE A C   
1174 O  O   . PHE A 146 ? 0.0879 0.0857 0.1234 -0.0006 0.0053  -0.0188 146 PHE A O   
1175 C  CB  . PHE A 146 ? 0.1209 0.0431 0.0890 -0.0086 -0.0022 -0.0044 146 PHE A CB  
1176 C  CG  . PHE A 146 ? 0.0859 0.0435 0.0944 0.0036  -0.0103 0.0085  146 PHE A CG  
1177 C  CD1 . PHE A 146 ? 0.0899 0.0590 0.1056 -0.0004 -0.0050 0.0143  146 PHE A CD1 
1178 C  CD2 . PHE A 146 ? 0.0952 0.0647 0.1008 -0.0245 -0.0005 0.0051  146 PHE A CD2 
1179 C  CE1 . PHE A 146 ? 0.0805 0.0759 0.1110 0.0020  -0.0053 0.0047  146 PHE A CE1 
1180 C  CE2 . PHE A 146 ? 0.0996 0.0733 0.1042 -0.0287 -0.0079 0.0092  146 PHE A CE2 
1181 C  CZ  . PHE A 146 ? 0.0983 0.0723 0.1108 -0.0005 -0.0005 0.0119  146 PHE A CZ  
1182 N  N   . LEU A 147 ? 0.0748 0.0748 0.1137 -0.0143 -0.0064 -0.0089 147 LEU A N   
1183 C  CA  . LEU A 147 ? 0.1322 0.0577 0.0835 -0.0158 -0.0176 0.0100  147 LEU A CA  
1184 C  C   . LEU A 147 ? 0.0963 0.0645 0.0961 0.0004  -0.0009 -0.0012 147 LEU A C   
1185 O  O   . LEU A 147 ? 0.0963 0.0643 0.1437 -0.0080 -0.0010 -0.0060 147 LEU A O   
1186 C  CB  . LEU A 147 ? 0.1067 0.0677 0.1017 -0.0128 0.0017  0.0057  147 LEU A CB  
1187 C  CG  . LEU A 147 ? 0.1225 0.0512 0.0988 -0.0234 -0.0059 0.0027  147 LEU A CG  
1188 C  CD1 . LEU A 147 ? 0.1608 0.0620 0.1124 -0.0271 -0.0022 -0.0102 147 LEU A CD1 
1189 C  CD2 . LEU A 147 ? 0.1606 0.0974 0.0986 -0.0105 0.0032  -0.0038 147 LEU A CD2 
1190 N  N   . LYS A 148 ? 0.1267 0.0651 0.1304 -0.0188 -0.0270 -0.0140 148 LYS A N   
1191 C  CA  . LYS A 148 ? 0.1598 0.0651 0.1038 0.0089  -0.0170 0.0012  148 LYS A CA  
1192 C  C   . LYS A 148 ? 0.1656 0.0680 0.1286 -0.0041 -0.0334 -0.0040 148 LYS A C   
1193 O  O   . LYS A 148 ? 0.1792 0.1098 0.1817 0.0397  -0.0690 -0.0364 148 LYS A O   
1194 C  CB  . LYS A 148 ? 0.1878 0.1925 0.1128 -0.0188 0.0027  0.0088  148 LYS A CB  
1195 C  CG  . LYS A 148 ? 0.1997 0.1533 0.1473 -0.0084 0.0152  0.0020  148 LYS A CG  
1196 C  CD  . LYS A 148 ? 0.2928 0.1846 0.2415 -0.0631 0.0460  0.0496  148 LYS A CD  
1197 C  CE  . LYS A 148 ? 0.3014 0.4363 0.3295 -0.0594 0.0818  0.0677  148 LYS A CE  
1198 N  NZ  . LYS A 148 ? 0.3294 0.4731 0.3674 -0.1921 0.0535  0.0661  148 LYS A NZ  
1199 N  N   . VAL A 149 ? 0.1530 0.0687 0.1534 0.0027  -0.0158 -0.0100 149 VAL A N   
1200 C  CA  . VAL A 149 ? 0.1372 0.0723 0.1652 -0.0069 -0.0205 -0.0077 149 VAL A CA  
1201 C  C   . VAL A 149 ? 0.1480 0.0893 0.1505 -0.0133 -0.0093 0.0027  149 VAL A C   
1202 O  O   . VAL A 149 ? 0.1972 0.1160 0.1687 -0.0379 -0.0267 0.0299  149 VAL A O   
1203 C  CB  . VAL A 149 ? 0.1245 0.0681 0.1753 -0.0222 -0.0147 -0.0197 149 VAL A CB  
1204 C  CG1 . VAL A 149 ? 0.1921 0.1318 0.1570 -0.0436 -0.0298 -0.0147 149 VAL A CG1 
1205 C  CG2 . VAL A 149 ? 0.1282 0.0841 0.2104 -0.0121 0.0155  -0.0033 149 VAL A CG2 
1206 N  N   . GLY A 150 ? 0.1498 0.0844 0.1595 -0.0253 -0.0228 -0.0122 150 GLY A N   
1207 C  CA  . GLY A 150 ? 0.1627 0.0969 0.1861 -0.0361 -0.0337 0.0192  150 GLY A CA  
1208 C  C   . GLY A 150 ? 0.1684 0.0794 0.1552 -0.0241 -0.0159 -0.0122 150 GLY A C   
1209 O  O   . GLY A 150 ? 0.1606 0.1092 0.1527 -0.0164 -0.0181 -0.0162 150 GLY A O   
1210 N  N   A SER A 151 ? 0.1483 0.1048 0.1832 -0.0333 -0.0192 0.0040  151 SER A N   
1211 N  N   B SER A 151 ? 0.1493 0.1084 0.1993 -0.0300 -0.0182 0.0041  151 SER A N   
1212 C  CA  A SER A 151 ? 0.1347 0.0891 0.1756 -0.0190 -0.0054 -0.0044 151 SER A CA  
1213 C  CA  B SER A 151 ? 0.1670 0.0902 0.1921 -0.0279 -0.0301 -0.0200 151 SER A CA  
1214 C  C   A SER A 151 ? 0.1358 0.0668 0.1404 -0.0185 -0.0292 -0.0293 151 SER A C   
1215 C  C   B SER A 151 ? 0.1289 0.0762 0.1454 0.0000  -0.0298 -0.0249 151 SER A C   
1216 O  O   A SER A 151 ? 0.1153 0.1048 0.1645 -0.0396 -0.0312 -0.0414 151 SER A O   
1217 O  O   B SER A 151 ? 0.1311 0.1137 0.1430 -0.0011 -0.0401 -0.0359 151 SER A O   
1218 C  CB  A SER A 151 ? 0.1523 0.1134 0.2374 -0.0152 0.0315  -0.0071 151 SER A CB  
1219 C  CB  B SER A 151 ? 0.1821 0.1268 0.2967 -0.0179 0.0019  -0.0073 151 SER A CB  
1220 O  OG  A SER A 151 ? 0.1534 0.1986 0.1791 -0.0129 -0.0037 -0.0376 151 SER A OG  
1221 O  OG  B SER A 151 ? 0.2071 0.1631 0.3753 -0.0467 -0.0193 0.0388  151 SER A OG  
1222 N  N   . ALA A 152 ? 0.1401 0.0996 0.1530 -0.0188 -0.0341 0.0061  152 ALA A N   
1223 C  CA  . ALA A 152 ? 0.1111 0.0909 0.1519 -0.0277 -0.0286 -0.0111 152 ALA A CA  
1224 C  C   . ALA A 152 ? 0.1590 0.1247 0.1498 -0.0443 -0.0047 -0.0362 152 ALA A C   
1225 O  O   . ALA A 152 ? 0.1558 0.1199 0.2050 -0.0253 0.0013  -0.0139 152 ALA A O   
1226 C  CB  . ALA A 152 ? 0.2117 0.1173 0.1297 -0.0129 -0.0326 -0.0298 152 ALA A CB  
1227 N  N   . LYS A 153 ? 0.1476 0.0908 0.1870 -0.0082 -0.0110 0.0033  153 LYS A N   
1228 C  CA  . LYS A 153 ? 0.1527 0.1024 0.1663 0.0108  -0.0438 0.0043  153 LYS A CA  
1229 C  C   . LYS A 153 ? 0.1249 0.0915 0.1838 -0.0043 -0.0408 0.0168  153 LYS A C   
1230 O  O   . LYS A 153 ? 0.1386 0.1033 0.1771 -0.0212 -0.0301 -0.0041 153 LYS A O   
1231 C  CB  . LYS A 153 ? 0.1483 0.1102 0.1569 -0.0065 -0.0400 0.0197  153 LYS A CB  
1232 C  CG  . LYS A 153 ? 0.1699 0.1038 0.2094 -0.0205 -0.0366 -0.0055 153 LYS A CG  
1233 C  CD  . LYS A 153 ? 0.2334 0.1350 0.1967 -0.0441 -0.0251 -0.0179 153 LYS A CD  
1234 C  CE  . LYS A 153 ? 0.2640 0.1627 0.1965 0.0029  -0.0075 0.0070  153 LYS A CE  
1235 N  NZ  . LYS A 153 ? 0.3441 0.2781 0.2713 -0.0457 0.0431  0.0581  153 LYS A NZ  
1236 N  N   . PRO A 154 ? 0.1194 0.1541 0.2054 -0.0494 -0.0452 0.0366  154 PRO A N   
1237 C  CA  . PRO A 154 ? 0.0952 0.1724 0.2633 -0.0323 -0.0836 0.0588  154 PRO A CA  
1238 C  C   . PRO A 154 ? 0.1083 0.1425 0.2116 0.0201  -0.0501 0.0439  154 PRO A C   
1239 O  O   . PRO A 154 ? 0.1663 0.2001 0.2065 -0.0161 -0.0525 0.0485  154 PRO A O   
1240 C  CB  . PRO A 154 ? 0.1031 0.1828 0.3486 -0.0149 -0.0409 0.0302  154 PRO A CB  
1241 C  CG  . PRO A 154 ? 0.1918 0.2673 0.3488 -0.0333 -0.1307 0.1093  154 PRO A CG  
1242 C  CD  . PRO A 154 ? 0.0956 0.1710 0.2456 -0.0223 -0.0339 0.0644  154 PRO A CD  
1243 N  N   . GLY A 155 ? 0.1153 0.1200 0.2306 -0.0044 -0.0248 0.0287  155 GLY A N   
1244 C  CA  . GLY A 155 ? 0.1033 0.1181 0.2758 0.0003  -0.0225 0.0018  155 GLY A CA  
1245 C  C   . GLY A 155 ? 0.1146 0.0856 0.2337 -0.0105 -0.0226 0.0348  155 GLY A C   
1246 O  O   . GLY A 155 ? 0.1498 0.0873 0.3085 -0.0185 -0.0025 0.0248  155 GLY A O   
1247 N  N   . LEU A 156 ? 0.1214 0.0997 0.1807 0.0083  -0.0076 0.0136  156 LEU A N   
1248 C  CA  . LEU A 156 ? 0.1093 0.1124 0.1598 0.0079  -0.0223 0.0023  156 LEU A CA  
1249 C  C   . LEU A 156 ? 0.1207 0.0841 0.1530 -0.0162 -0.0243 -0.0105 156 LEU A C   
1250 O  O   . LEU A 156 ? 0.1257 0.0978 0.1512 -0.0223 -0.0277 0.0190  156 LEU A O   
1251 C  CB  . LEU A 156 ? 0.1462 0.0909 0.1759 -0.0114 -0.0306 0.0151  156 LEU A CB  
1252 C  CG  . LEU A 156 ? 0.1444 0.0717 0.1426 -0.0271 -0.0247 0.0131  156 LEU A CG  
1253 C  CD1 . LEU A 156 ? 0.1469 0.1171 0.1544 -0.0585 -0.0429 0.0081  156 LEU A CD1 
1254 C  CD2 . LEU A 156 ? 0.1412 0.0925 0.1383 0.0079  -0.0255 0.0044  156 LEU A CD2 
1255 N  N   . GLN A 157 ? 0.1397 0.1128 0.1559 -0.0287 -0.0407 0.0021  157 GLN A N   
1256 C  CA  . GLN A 157 ? 0.1645 0.1214 0.1731 -0.0541 -0.0293 -0.0158 157 GLN A CA  
1257 C  C   . GLN A 157 ? 0.1490 0.1411 0.1448 -0.0274 -0.0447 -0.0057 157 GLN A C   
1258 O  O   . GLN A 157 ? 0.1576 0.1065 0.1393 -0.0095 -0.0461 0.0025  157 GLN A O   
1259 C  CB  . GLN A 157 ? 0.1850 0.1512 0.2118 -0.0685 -0.0795 0.0055  157 GLN A CB  
1260 C  CG  . GLN A 157 ? 0.2324 0.1285 0.2187 -0.0126 -0.0862 -0.0054 157 GLN A CG  
1261 C  CD  . GLN A 157 ? 0.2205 0.1203 0.1584 -0.0232 -0.0443 -0.0334 157 GLN A CD  
1262 O  OE1 . GLN A 157 ? 0.2173 0.1587 0.1627 -0.0103 -0.0363 -0.0022 157 GLN A OE1 
1263 N  NE2 . GLN A 157 ? 0.2618 0.1548 0.1433 -0.0423 -0.0363 -0.0237 157 GLN A NE2 
1264 N  N   . LYS A 158 ? 0.1566 0.1408 0.1735 -0.0337 -0.0531 -0.0047 158 LYS A N   
1265 C  CA  . LYS A 158 ? 0.1455 0.1220 0.1882 -0.0162 -0.0449 0.0000  158 LYS A CA  
1266 C  C   . LYS A 158 ? 0.1512 0.0997 0.1455 0.0034  -0.0265 0.0065  158 LYS A C   
1267 O  O   . LYS A 158 ? 0.1832 0.1365 0.1212 -0.0294 -0.0408 -0.0089 158 LYS A O   
1268 C  CB  . LYS A 158 ? 0.2094 0.1394 0.2391 0.0378  -0.0559 -0.0012 158 LYS A CB  
1269 C  CG  . LYS A 158 ? 0.2377 0.1932 0.3513 0.0167  -0.0969 0.0197  158 LYS A CG  
1270 N  N   . VAL A 159 ? 0.1293 0.0832 0.1461 -0.0264 -0.0425 -0.0127 159 VAL A N   
1271 C  CA  . VAL A 159 ? 0.1304 0.1072 0.1329 -0.0190 -0.0467 0.0201  159 VAL A CA  
1272 C  C   . VAL A 159 ? 0.1454 0.1040 0.1415 -0.0324 -0.0114 0.0062  159 VAL A C   
1273 O  O   . VAL A 159 ? 0.1533 0.1056 0.1498 -0.0430 -0.0217 0.0186  159 VAL A O   
1274 C  CB  . VAL A 159 ? 0.1268 0.1005 0.1318 -0.0054 -0.0395 0.0059  159 VAL A CB  
1275 C  CG1 . VAL A 159 ? 0.1257 0.1272 0.1692 -0.0483 -0.0323 0.0444  159 VAL A CG1 
1276 C  CG2 . VAL A 159 ? 0.1852 0.0835 0.1886 -0.0073 -0.0196 -0.0237 159 VAL A CG2 
1277 N  N   . VAL A 160 ? 0.1569 0.0888 0.1060 -0.0189 -0.0309 0.0035  160 VAL A N   
1278 C  CA  . VAL A 160 ? 0.1821 0.1188 0.1505 -0.0120 -0.0030 -0.0038 160 VAL A CA  
1279 C  C   . VAL A 160 ? 0.1728 0.0890 0.1565 -0.0257 -0.0138 -0.0270 160 VAL A C   
1280 O  O   . VAL A 160 ? 0.1842 0.1055 0.1552 -0.0167 -0.0111 -0.0192 160 VAL A O   
1281 C  CB  . VAL A 160 ? 0.2767 0.0805 0.1698 -0.0021 0.0002  0.0259  160 VAL A CB  
1282 C  CG1 . VAL A 160 ? 0.2187 0.1239 0.2191 -0.0012 0.0082  0.0134  160 VAL A CG1 
1283 C  CG2 . VAL A 160 ? 0.2493 0.0976 0.1846 0.0008  -0.0037 0.0236  160 VAL A CG2 
1284 N  N   . ASP A 161 ? 0.2094 0.1214 0.1285 -0.0362 -0.0334 -0.0223 161 ASP A N   
1285 C  CA  . ASP A 161 ? 0.2647 0.1710 0.1304 -0.0500 -0.0581 -0.0015 161 ASP A CA  
1286 C  C   . ASP A 161 ? 0.2292 0.1624 0.1476 -0.0258 -0.0264 -0.0111 161 ASP A C   
1287 O  O   . ASP A 161 ? 0.3590 0.2122 0.1440 -0.0739 -0.0069 -0.0160 161 ASP A O   
1288 C  CB  . ASP A 161 ? 0.2843 0.2572 0.1279 -0.1005 -0.0696 -0.0366 161 ASP A CB  
1289 C  CG  . ASP A 161 ? 0.2965 0.2227 0.2540 -0.0702 -0.0642 -0.0870 161 ASP A CG  
1290 O  OD1 . ASP A 161 ? 0.4073 0.2913 0.3477 -0.0111 -0.0384 -0.0526 161 ASP A OD1 
1291 O  OD2 . ASP A 161 ? 0.3236 0.3650 0.2809 -0.0094 -0.0329 -0.0540 161 ASP A OD2 
1292 N  N   . VAL A 162 ? 0.1825 0.1282 0.1239 -0.0052 -0.0398 0.0248  162 VAL A N   
1293 C  CA  . VAL A 162 ? 0.2015 0.1612 0.1315 -0.0130 -0.0229 0.0384  162 VAL A CA  
1294 C  C   . VAL A 162 ? 0.2008 0.1268 0.0968 0.0102  0.0079  0.0044  162 VAL A C   
1295 O  O   . VAL A 162 ? 0.1904 0.1547 0.1137 -0.0055 -0.0009 0.0084  162 VAL A O   
1296 C  CB  . VAL A 162 ? 0.2117 0.1451 0.1979 0.0040  0.0015  0.0561  162 VAL A CB  
1297 C  CG1 . VAL A 162 ? 0.3367 0.1024 0.1756 0.0168  0.0227  -0.0344 162 VAL A CG1 
1298 C  CG2 . VAL A 162 ? 0.2190 0.2166 0.2441 0.0119  0.0575  0.1034  162 VAL A CG2 
1299 N  N   . LEU A 163 ? 0.1868 0.1297 0.1191 0.0047  -0.0289 -0.0010 163 LEU A N   
1300 C  CA  . LEU A 163 ? 0.1573 0.1027 0.1209 -0.0027 -0.0027 -0.0032 163 LEU A CA  
1301 C  C   . LEU A 163 ? 0.1624 0.1166 0.1336 0.0120  -0.0082 -0.0187 163 LEU A C   
1302 O  O   . LEU A 163 ? 0.1774 0.1382 0.1386 -0.0038 0.0044  0.0068  163 LEU A O   
1303 C  CB  . LEU A 163 ? 0.1677 0.0979 0.1368 0.0096  0.0110  -0.0032 163 LEU A CB  
1304 C  CG  . LEU A 163 ? 0.2165 0.0872 0.1045 -0.0033 -0.0009 0.0131  163 LEU A CG  
1305 C  CD1 . LEU A 163 ? 0.1839 0.1264 0.1433 0.0026  -0.0234 0.0424  163 LEU A CD1 
1306 C  CD2 . LEU A 163 ? 0.1785 0.1336 0.1321 -0.0199 -0.0277 -0.0078 163 LEU A CD2 
1307 N  N   . ASP A 164 ? 0.2922 0.1322 0.1199 -0.0247 0.0316  -0.0396 164 ASP A N   
1308 C  CA  . ASP A 164 ? 0.2986 0.1760 0.1328 -0.0354 0.0510  -0.0286 164 ASP A CA  
1309 C  C   . ASP A 164 ? 0.2690 0.2172 0.1307 -0.0075 0.0244  0.0223  164 ASP A C   
1310 O  O   . ASP A 164 ? 0.3326 0.2970 0.2118 0.0186  0.0964  0.0326  164 ASP A O   
1311 C  CB  . ASP A 164 ? 0.4306 0.2730 0.1624 -0.0745 0.0204  -0.0703 164 ASP A CB  
1312 C  CG  . ASP A 164 ? 0.4266 0.4384 0.3789 -0.0687 -0.1161 -0.1523 164 ASP A CG  
1313 O  OD1 . ASP A 164 ? 0.4487 0.4455 0.2929 -0.1718 -0.0115 -0.0237 164 ASP A OD1 
1314 O  OD2 . ASP A 164 ? 0.5140 1.0029 0.5431 -0.0616 0.1606  -0.1045 164 ASP A OD2 
1315 N  N   . SER A 165 ? 0.2227 0.1950 0.1336 -0.0313 -0.0326 0.0035  165 SER A N   
1316 C  CA  . SER A 165 ? 0.2152 0.2187 0.1164 -0.0140 -0.0298 0.0281  165 SER A CA  
1317 C  C   . SER A 165 ? 0.2116 0.1425 0.0895 -0.0179 0.0107  0.0214  165 SER A C   
1318 O  O   . SER A 165 ? 0.2328 0.1695 0.1375 -0.0199 0.0083  0.0545  165 SER A O   
1319 C  CB  . SER A 165 ? 0.3118 0.2213 0.1842 0.0642  0.0163  0.0329  165 SER A CB  
1320 O  OG  . SER A 165 ? 0.2918 0.1831 0.2001 0.0047  -0.0324 0.0057  165 SER A OG  
1321 N  N   . ILE A 166 ? 0.1753 0.1365 0.0961 -0.0011 -0.0030 0.0205  166 ILE A N   
1322 C  CA  . ILE A 166 ? 0.1594 0.0976 0.1286 0.0027  0.0193  0.0150  166 ILE A CA  
1323 C  C   . ILE A 166 ? 0.1426 0.1153 0.1264 0.0027  0.0048  -0.0037 166 ILE A C   
1324 O  O   . ILE A 166 ? 0.1486 0.1072 0.1232 0.0079  0.0188  -0.0058 166 ILE A O   
1325 C  CB  . ILE A 166 ? 0.1293 0.0979 0.1212 0.0030  0.0082  0.0133  166 ILE A CB  
1326 C  CG1 . ILE A 166 ? 0.1756 0.0978 0.0941 -0.0196 0.0208  -0.0081 166 ILE A CG1 
1327 C  CG2 . ILE A 166 ? 0.1784 0.1093 0.1624 0.0159  0.0069  0.0535  166 ILE A CG2 
1328 C  CD1 . ILE A 166 ? 0.2270 0.1300 0.1124 0.0076  0.0186  -0.0276 166 ILE A CD1 
1329 N  N   . LYS A 167 ? 0.1688 0.0900 0.1304 0.0096  0.0078  -0.0065 167 LYS A N   
1330 C  CA  . LYS A 167 ? 0.1527 0.1065 0.1040 0.0151  -0.0016 -0.0121 167 LYS A CA  
1331 C  C   . LYS A 167 ? 0.1358 0.0873 0.1135 -0.0061 0.0193  0.0105  167 LYS A C   
1332 O  O   . LYS A 167 ? 0.1455 0.1075 0.1164 0.0044  -0.0087 0.0080  167 LYS A O   
1333 C  CB  . LYS A 167 ? 0.2172 0.0932 0.1333 0.0243  0.0283  -0.0228 167 LYS A CB  
1334 C  CG  . LYS A 167 ? 0.2065 0.1120 0.2064 0.0342  -0.0745 -0.0635 167 LYS A CG  
1335 C  CD  . LYS A 167 ? 0.3198 0.1185 0.2471 0.0501  -0.1090 -0.1047 167 LYS A CD  
1336 C  CE  . LYS A 167 ? 0.3884 0.1953 0.4575 0.0760  -0.0642 0.0691  167 LYS A CE  
1337 N  N   . THR A 168 ? 0.1289 0.0757 0.1268 0.0031  0.0234  0.0133  168 THR A N   
1338 C  CA  . THR A 168 ? 0.1458 0.0945 0.1199 -0.0105 0.0165  -0.0013 168 THR A CA  
1339 C  C   . THR A 168 ? 0.1397 0.0872 0.1014 0.0042  0.0380  0.0043  168 THR A C   
1340 O  O   . THR A 168 ? 0.1566 0.0844 0.1325 0.0048  0.0181  0.0254  168 THR A O   
1341 C  CB  . THR A 168 ? 0.1735 0.0932 0.1335 0.0222  0.0317  -0.0068 168 THR A CB  
1342 O  OG1 . THR A 168 ? 0.1949 0.1437 0.1186 0.0261  0.0276  0.0154  168 THR A OG1 
1343 C  CG2 . THR A 168 ? 0.1874 0.1073 0.1544 0.0247  0.0309  -0.0333 168 THR A CG2 
1344 N  N   . LYS A 169 ? 0.1562 0.0846 0.1300 -0.0279 0.0298  -0.0026 169 LYS A N   
1345 C  CA  . LYS A 169 ? 0.1648 0.0767 0.1141 -0.0082 0.0308  0.0039  169 LYS A CA  
1346 C  C   . LYS A 169 ? 0.1627 0.0785 0.1358 -0.0016 0.0479  0.0111  169 LYS A C   
1347 O  O   . LYS A 169 ? 0.1979 0.1311 0.1498 -0.0239 0.0618  0.0156  169 LYS A O   
1348 C  CB  . LYS A 169 ? 0.1670 0.1199 0.1293 -0.0298 0.0212  0.0030  169 LYS A CB  
1349 C  CG  . LYS A 169 ? 0.1552 0.1141 0.1807 -0.0465 0.0334  -0.0019 169 LYS A CG  
1350 C  CD  . LYS A 169 ? 0.1343 0.1936 0.2423 -0.0621 0.0425  -0.0396 169 LYS A CD  
1351 C  CE  . LYS A 169 ? 0.2469 0.4097 0.2644 0.0163  0.0644  -0.0873 169 LYS A CE  
1352 N  N   . GLY A 170 ? 0.1461 0.0741 0.1570 0.0052  0.0276  0.0098  170 GLY A N   
1353 C  CA  . GLY A 170 ? 0.1476 0.1049 0.2022 -0.0094 0.0221  0.0620  170 GLY A CA  
1354 C  C   . GLY A 170 ? 0.1458 0.1057 0.1878 0.0143  0.0367  0.0316  170 GLY A C   
1355 O  O   . GLY A 170 ? 0.2137 0.1093 0.2219 0.0178  0.0292  0.0461  170 GLY A O   
1356 N  N   A LYS A 171 ? 0.1764 0.1066 0.1411 -0.0080 0.0536  0.0521  171 LYS A N   
1357 N  N   B LYS A 171 ? 0.1892 0.1092 0.1328 -0.0055 0.0425  0.0400  171 LYS A N   
1358 C  CA  A LYS A 171 ? 0.1917 0.1523 0.1421 0.0049  0.0469  0.0367  171 LYS A CA  
1359 C  CA  B LYS A 171 ? 0.1918 0.1304 0.1383 0.0001  0.0430  0.0268  171 LYS A CA  
1360 C  C   A LYS A 171 ? 0.1588 0.0789 0.1232 -0.0048 0.0207  0.0354  171 LYS A C   
1361 C  C   B LYS A 171 ? 0.1728 0.0988 0.1085 0.0097  0.0179  0.0312  171 LYS A C   
1362 O  O   A LYS A 171 ? 0.1598 0.1032 0.1186 -0.0105 0.0330  0.0267  171 LYS A O   
1363 O  O   B LYS A 171 ? 0.1624 0.0978 0.1249 0.0122  0.0211  0.0446  171 LYS A O   
1364 C  CB  A LYS A 171 ? 0.1749 0.1515 0.1386 0.0228  0.0634  0.0256  171 LYS A CB  
1365 C  CB  B LYS A 171 ? 0.1746 0.1534 0.1321 0.0143  0.0352  -0.0029 171 LYS A CB  
1366 C  CG  A LYS A 171 ? 0.1792 0.2148 0.1904 0.1021  0.0769  0.0626  171 LYS A CG  
1367 C  CG  B LYS A 171 ? 0.2169 0.1879 0.1588 0.0361  0.0447  -0.0623 171 LYS A CG  
1368 C  CD  A LYS A 171 ? 0.2745 0.2745 0.2338 0.0705  0.0463  0.0332  171 LYS A CD  
1369 C  CD  B LYS A 171 ? 0.2662 0.1746 0.1950 0.0248  -0.0068 -0.0450 171 LYS A CD  
1370 N  N   . SER A 172 ? 0.1929 0.1602 0.1225 0.0323  0.0156  0.0571  172 SER A N   
1371 C  CA  . SER A 172 ? 0.1821 0.1914 0.1275 0.0219  0.0081  0.0084  172 SER A CA  
1372 C  C   . SER A 172 ? 0.1548 0.1311 0.1218 0.0279  0.0127  0.0236  172 SER A C   
1373 O  O   . SER A 172 ? 0.1756 0.2029 0.1243 0.0163  0.0111  0.0303  172 SER A O   
1374 C  CB  . SER A 172 ? 0.1753 0.1853 0.1168 0.0100  -0.0290 0.0159  172 SER A CB  
1375 O  OG  . SER A 172 ? 0.2536 0.1566 0.2015 0.0320  0.0368  0.0472  172 SER A OG  
1376 N  N   . ALA A 173 ? 0.1667 0.1624 0.1317 0.0548  0.0134  0.0015  173 ALA A N   
1377 C  CA  . ALA A 173 ? 0.2150 0.1583 0.1128 0.0087  -0.0188 -0.0026 173 ALA A CA  
1378 C  C   . ALA A 173 ? 0.2249 0.1720 0.1191 0.0402  -0.0264 0.0211  173 ALA A C   
1379 O  O   . ALA A 173 ? 0.1494 0.1135 0.1135 0.0171  -0.0236 0.0197  173 ALA A O   
1380 C  CB  . ALA A 173 ? 0.2428 0.1523 0.1426 0.0051  -0.0212 0.0035  173 ALA A CB  
1381 N  N   . ASP A 174 ? 0.2331 0.1674 0.1333 0.0539  -0.0284 0.0162  174 ASP A N   
1382 C  CA  . ASP A 174 ? 0.1932 0.2233 0.1195 0.0251  -0.0547 0.0332  174 ASP A CA  
1383 C  C   . ASP A 174 ? 0.1771 0.1498 0.1624 0.0407  -0.0116 -0.0008 174 ASP A C   
1384 O  O   . ASP A 174 ? 0.1954 0.1710 0.2196 0.0252  -0.0138 -0.0475 174 ASP A O   
1385 C  CB  . ASP A 174 ? 0.2745 0.3164 0.1523 0.1420  -0.0106 0.0946  174 ASP A CB  
1386 C  CG  . ASP A 174 ? 0.4855 0.3990 0.2658 0.0231  -0.1272 0.1556  174 ASP A CG  
1387 O  OD1 . ASP A 174 ? 0.3699 0.5014 0.5144 -0.0236 -0.1939 0.1085  174 ASP A OD1 
1388 O  OD2 . ASP A 174 ? 0.6627 0.5528 0.2663 -0.1962 -0.0746 0.1144  174 ASP A OD2 
1389 N  N   . PHE A 175 ? 0.1627 0.1415 0.1203 -0.0087 -0.0198 0.0058  175 PHE A N   
1390 C  CA  . PHE A 175 ? 0.1645 0.1227 0.1436 0.0046  -0.0194 0.0312  175 PHE A CA  
1391 C  C   . PHE A 175 ? 0.1318 0.1225 0.1807 -0.0085 -0.0203 0.0432  175 PHE A C   
1392 O  O   . PHE A 175 ? 0.2445 0.1505 0.1947 0.0723  -0.0741 -0.0354 175 PHE A O   
1393 C  CB  . PHE A 175 ? 0.1584 0.0936 0.1871 -0.0124 -0.0350 0.0367  175 PHE A CB  
1394 C  CG  . PHE A 175 ? 0.1425 0.0929 0.1807 -0.0242 0.0053  -0.0053 175 PHE A CG  
1395 C  CD1 . PHE A 175 ? 0.1882 0.0996 0.1342 -0.0149 -0.0069 -0.0008 175 PHE A CD1 
1396 C  CD2 . PHE A 175 ? 0.1318 0.1055 0.1742 0.0205  -0.0245 0.0160  175 PHE A CD2 
1397 C  CE1 . PHE A 175 ? 0.2227 0.0994 0.1674 -0.0003 0.0003  0.0212  175 PHE A CE1 
1398 C  CE2 . PHE A 175 ? 0.1595 0.1137 0.1681 -0.0019 -0.0477 0.0245  175 PHE A CE2 
1399 C  CZ  . PHE A 175 ? 0.1631 0.1505 0.1530 -0.0242 -0.0130 -0.0033 175 PHE A CZ  
1400 N  N   . THR A 176 ? 0.1731 0.1335 0.1351 0.0446  -0.0095 0.0276  176 THR A N   
1401 C  CA  . THR A 176 ? 0.1253 0.1529 0.1540 0.0521  -0.0182 0.0585  176 THR A CA  
1402 C  C   . THR A 176 ? 0.1325 0.1017 0.1060 0.0323  -0.0362 0.0136  176 THR A C   
1403 O  O   . THR A 176 ? 0.1656 0.1015 0.1440 0.0133  -0.0251 0.0059  176 THR A O   
1404 C  CB  . THR A 176 ? 0.1487 0.1346 0.1688 0.0373  -0.0274 0.0587  176 THR A CB  
1405 O  OG1 . THR A 176 ? 0.3301 0.1777 0.1376 0.0756  -0.0212 0.0629  176 THR A OG1 
1406 C  CG2 . THR A 176 ? 0.2133 0.2137 0.3513 -0.0195 0.0263  0.1174  176 THR A CG2 
1407 N  N   . ASN A 177 ? 0.1383 0.1108 0.1242 0.0043  0.0026  0.0145  177 ASN A N   
1408 C  CA  . ASN A 177 ? 0.1336 0.1315 0.1433 -0.0021 -0.0271 0.0582  177 ASN A CA  
1409 C  C   . ASN A 177 ? 0.1500 0.1121 0.1570 0.0168  -0.0310 0.0440  177 ASN A C   
1410 O  O   . ASN A 177 ? 0.1803 0.1516 0.2328 -0.0119 -0.0747 0.0634  177 ASN A O   
1411 C  CB  . ASN A 177 ? 0.1426 0.1347 0.1663 0.0208  -0.0477 0.0475  177 ASN A CB  
1412 C  CG  . ASN A 177 ? 0.1728 0.1351 0.1569 0.0307  -0.0187 0.0421  177 ASN A CG  
1413 O  OD1 . ASN A 177 ? 0.2108 0.1624 0.2284 0.0532  -0.0022 0.0227  177 ASN A OD1 
1414 N  ND2 . ASN A 177 ? 0.1774 0.1480 0.1379 0.0097  -0.0269 0.0166  177 ASN A ND2 
1415 N  N   . PHE A 178 ? 0.1638 0.1146 0.1092 -0.0057 -0.0262 0.0446  178 PHE A N   
1416 C  CA  . PHE A 178 ? 0.1357 0.1135 0.1027 -0.0144 -0.0158 0.0429  178 PHE A CA  
1417 C  C   . PHE A 178 ? 0.1404 0.1142 0.1102 -0.0199 -0.0267 0.0004  178 PHE A C   
1418 O  O   . PHE A 178 ? 0.2141 0.1005 0.1128 -0.0364 -0.0361 0.0219  178 PHE A O   
1419 C  CB  . PHE A 178 ? 0.1493 0.1121 0.1347 0.0110  0.0009  0.0318  178 PHE A CB  
1420 C  CG  . PHE A 178 ? 0.1286 0.1128 0.1257 0.0004  -0.0173 0.0286  178 PHE A CG  
1421 C  CD1 . PHE A 178 ? 0.1623 0.1080 0.1555 -0.0055 -0.0251 0.0225  178 PHE A CD1 
1422 C  CD2 . PHE A 178 ? 0.1004 0.1379 0.1257 0.0020  -0.0035 0.0247  178 PHE A CD2 
1423 C  CE1 . PHE A 178 ? 0.1846 0.1317 0.1386 -0.0161 -0.0346 0.0212  178 PHE A CE1 
1424 C  CE2 . PHE A 178 ? 0.1115 0.1314 0.1361 0.0066  -0.0364 0.0227  178 PHE A CE2 
1425 C  CZ  . PHE A 178 ? 0.1317 0.1383 0.1310 -0.0107 -0.0264 0.0210  178 PHE A CZ  
1426 N  N   . ASP A 179 ? 0.1620 0.1268 0.1073 -0.0021 -0.0175 0.0356  179 ASP A N   
1427 C  CA  . ASP A 179 ? 0.1534 0.1473 0.1127 -0.0039 -0.0206 0.0318  179 ASP A CA  
1428 C  C   . ASP A 179 ? 0.1461 0.1178 0.1195 -0.0068 -0.0206 0.0245  179 ASP A C   
1429 O  O   . ASP A 179 ? 0.1408 0.1189 0.1311 -0.0006 -0.0192 0.0384  179 ASP A O   
1430 C  CB  . ASP A 179 ? 0.1626 0.2137 0.1455 -0.0066 -0.0269 0.0685  179 ASP A CB  
1431 C  CG  . ASP A 179 ? 0.1293 0.2416 0.2037 -0.0107 -0.0103 0.0143  179 ASP A CG  
1432 O  OD1 . ASP A 179 ? 0.1796 0.1293 0.1796 0.0086  -0.0223 0.0424  179 ASP A OD1 
1433 O  OD2 . ASP A 179 ? 0.1358 0.4512 0.2715 0.0073  -0.0079 -0.0515 179 ASP A OD2 
1434 N  N   . PRO A 180 ? 0.1182 0.0952 0.1212 -0.0064 -0.0145 0.0204  180 PRO A N   
1435 C  CA  . PRO A 180 ? 0.1053 0.1119 0.0950 -0.0124 -0.0106 0.0162  180 PRO A CA  
1436 C  C   . PRO A 180 ? 0.0838 0.1253 0.1278 -0.0034 -0.0075 0.0355  180 PRO A C   
1437 O  O   . PRO A 180 ? 0.1468 0.0987 0.1132 -0.0070 -0.0323 0.0220  180 PRO A O   
1438 C  CB  . PRO A 180 ? 0.1076 0.1293 0.1407 -0.0144 -0.0341 0.0188  180 PRO A CB  
1439 C  CG  . PRO A 180 ? 0.1397 0.1065 0.1236 -0.0194 -0.0200 0.0236  180 PRO A CG  
1440 C  CD  . PRO A 180 ? 0.1455 0.1100 0.1307 -0.0271 -0.0258 -0.0227 180 PRO A CD  
1441 N  N   . ARG A 181 ? 0.0888 0.1234 0.1261 -0.0013 0.0110  0.0071  181 ARG A N   
1442 C  CA  . ARG A 181 ? 0.0832 0.1324 0.1268 -0.0201 0.0040  0.0089  181 ARG A CA  
1443 C  C   . ARG A 181 ? 0.1191 0.1275 0.1318 0.0063  -0.0380 0.0127  181 ARG A C   
1444 O  O   . ARG A 181 ? 0.1336 0.1476 0.1555 -0.0058 -0.0098 0.0244  181 ARG A O   
1445 C  CB  . ARG A 181 ? 0.0943 0.0935 0.1929 -0.0156 0.0069  0.0262  181 ARG A CB  
1446 C  CG  . ARG A 181 ? 0.1741 0.1100 0.1796 0.0044  -0.0230 0.0026  181 ARG A CG  
1447 C  CD  . ARG A 181 ? 0.1892 0.1361 0.2134 0.0267  0.0244  0.0266  181 ARG A CD  
1448 N  NE  . ARG A 181 ? 0.1483 0.1831 0.2425 0.0184  0.0211  0.0298  181 ARG A NE  
1449 C  CZ  . ARG A 181 ? 0.1562 0.2684 0.2428 0.0525  0.0307  0.0212  181 ARG A CZ  
1450 N  NH1 . ARG A 181 ? 0.1469 0.2647 0.2982 0.0326  0.0468  -0.0004 181 ARG A NH1 
1451 N  NH2 . ARG A 181 ? 0.2083 0.2425 0.2821 0.0322  0.0188  0.0803  181 ARG A NH2 
1452 N  N   . GLY A 182 ? 0.1160 0.1182 0.1518 -0.0103 -0.0209 -0.0020 182 GLY A N   
1453 C  CA  . GLY A 182 ? 0.1351 0.1157 0.1566 0.0074  -0.0485 -0.0132 182 GLY A CA  
1454 C  C   . GLY A 182 ? 0.1321 0.1146 0.1264 0.0049  -0.0337 -0.0080 182 GLY A C   
1455 O  O   . GLY A 182 ? 0.1534 0.1058 0.2040 -0.0155 -0.0413 -0.0016 182 GLY A O   
1456 N  N   . LEU A 183 ? 0.0981 0.1303 0.1216 0.0083  -0.0293 0.0064  183 LEU A N   
1457 C  CA  . LEU A 183 ? 0.0990 0.1221 0.1439 0.0082  -0.0220 0.0304  183 LEU A CA  
1458 C  C   . LEU A 183 ? 0.1150 0.0899 0.1311 -0.0001 -0.0098 0.0016  183 LEU A C   
1459 O  O   . LEU A 183 ? 0.1500 0.1153 0.1613 0.0117  -0.0257 0.0319  183 LEU A O   
1460 C  CB  . LEU A 183 ? 0.0988 0.1397 0.1304 0.0146  -0.0105 0.0465  183 LEU A CB  
1461 C  CG  . LEU A 183 ? 0.1555 0.1512 0.1267 0.0108  0.0001  0.0347  183 LEU A CG  
1462 C  CD1 . LEU A 183 ? 0.1229 0.2144 0.1694 0.0060  0.0061  0.0685  183 LEU A CD1 
1463 C  CD2 . LEU A 183 ? 0.2341 0.1515 0.1967 0.0287  -0.0248 0.0054  183 LEU A CD2 
1464 N  N   . LEU A 184 ? 0.1063 0.1124 0.1243 0.0086  -0.0186 0.0087  184 LEU A N   
1465 C  CA  . LEU A 184 ? 0.1254 0.1282 0.1239 -0.0275 0.0073  0.0212  184 LEU A CA  
1466 C  C   . LEU A 184 ? 0.1735 0.1116 0.1504 -0.0267 -0.0414 0.0542  184 LEU A C   
1467 O  O   . LEU A 184 ? 0.2612 0.2344 0.2310 -0.1095 -0.1401 0.1257  184 LEU A O   
1468 C  CB  . LEU A 184 ? 0.1171 0.1353 0.1555 -0.0251 -0.0025 0.0150  184 LEU A CB  
1469 C  CG  . LEU A 184 ? 0.1168 0.1282 0.1394 -0.0167 0.0027  0.0046  184 LEU A CG  
1470 C  CD1 . LEU A 184 ? 0.1191 0.1720 0.1663 -0.0040 0.0226  -0.0079 184 LEU A CD1 
1471 C  CD2 . LEU A 184 ? 0.1447 0.1856 0.2354 -0.0521 -0.0547 0.0183  184 LEU A CD2 
1472 N  N   . PRO A 185 ? 0.1206 0.1108 0.1379 -0.0257 -0.0381 0.0337  185 PRO A N   
1473 C  CA  . PRO A 185 ? 0.1148 0.1178 0.1437 -0.0133 0.0015  0.0458  185 PRO A CA  
1474 C  C   . PRO A 185 ? 0.1011 0.1207 0.1569 -0.0208 -0.0252 0.0193  185 PRO A C   
1475 O  O   . PRO A 185 ? 0.1060 0.1186 0.2245 -0.0106 -0.0271 0.0340  185 PRO A O   
1476 C  CB  . PRO A 185 ? 0.1318 0.1195 0.1310 -0.0122 -0.0104 0.0181  185 PRO A CB  
1477 C  CG  . PRO A 185 ? 0.1234 0.0844 0.1239 0.0163  -0.0229 0.0147  185 PRO A CG  
1478 C  CD  . PRO A 185 ? 0.1058 0.1171 0.1058 -0.0013 -0.0245 0.0128  185 PRO A CD  
1479 N  N   A GLU A 186 ? 0.1118 0.1234 0.1879 -0.0337 -0.0242 0.0292  186 GLU A N   
1480 N  N   B GLU A 186 ? 0.0932 0.1421 0.1893 -0.0347 -0.0264 0.0335  186 GLU A N   
1481 C  CA  A GLU A 186 ? 0.1058 0.1401 0.1695 -0.0423 -0.0234 0.0280  186 GLU A CA  
1482 C  CA  B GLU A 186 ? 0.0949 0.1267 0.1710 -0.0380 -0.0226 0.0443  186 GLU A CA  
1483 C  C   A GLU A 186 ? 0.1015 0.1186 0.1796 -0.0260 -0.0280 0.0245  186 GLU A C   
1484 C  C   B GLU A 186 ? 0.0907 0.1089 0.1850 -0.0111 -0.0158 0.0308  186 GLU A C   
1485 O  O   A GLU A 186 ? 0.1182 0.1655 0.1476 -0.0085 -0.0069 0.0149  186 GLU A O   
1486 O  O   B GLU A 186 ? 0.0863 0.1333 0.2539 0.0057  -0.0251 0.0389  186 GLU A O   
1487 C  CB  A GLU A 186 ? 0.1458 0.1271 0.2119 -0.0675 -0.0163 -0.0155 186 GLU A CB  
1488 C  CB  B GLU A 186 ? 0.1036 0.1033 0.2299 -0.0306 -0.0214 0.0054  186 GLU A CB  
1489 C  CG  A GLU A 186 ? 0.2234 0.1792 0.2399 -0.0893 -0.0473 -0.0342 186 GLU A CG  
1490 C  CG  B GLU A 186 ? 0.1008 0.1825 0.2590 -0.0384 -0.0027 0.0155  186 GLU A CG  
1491 C  CD  A GLU A 186 ? 0.2173 0.2477 0.2992 -0.0849 0.0524  0.0312  186 GLU A CD  
1492 C  CD  B GLU A 186 ? 0.1364 0.1936 0.2410 -0.0392 -0.0069 0.0469  186 GLU A CD  
1493 O  OE1 A GLU A 186 ? 0.2710 0.2565 0.3965 0.0030  -0.0036 -0.0342 186 GLU A OE1 
1494 O  OE1 B GLU A 186 ? 0.1296 0.2140 0.3441 -0.0212 -0.0192 0.0041  186 GLU A OE1 
1495 O  OE2 A GLU A 186 ? 0.2798 0.2489 0.2830 -0.0602 0.0024  -0.0192 186 GLU A OE2 
1496 O  OE2 B GLU A 186 ? 0.1644 0.2463 0.2648 0.0297  0.0281  0.0875  186 GLU A OE2 
1497 N  N   . SER A 187 ? 0.0918 0.1415 0.1486 -0.0227 -0.0156 0.0163  187 SER A N   
1498 C  CA  . SER A 187 ? 0.1300 0.1286 0.1674 -0.0288 -0.0198 0.0082  187 SER A CA  
1499 C  C   . SER A 187 ? 0.0884 0.1394 0.1673 -0.0084 -0.0117 -0.0075 187 SER A C   
1500 O  O   . SER A 187 ? 0.1040 0.1735 0.1724 -0.0060 -0.0052 -0.0016 187 SER A O   
1501 C  CB  . SER A 187 ? 0.1264 0.1537 0.1534 -0.0035 -0.0020 0.0201  187 SER A CB  
1502 O  OG  . SER A 187 ? 0.1501 0.1516 0.1738 -0.0190 -0.0003 0.0172  187 SER A OG  
1503 N  N   . LEU A 188 ? 0.1100 0.1076 0.1552 -0.0232 -0.0027 0.0075  188 LEU A N   
1504 C  CA  . LEU A 188 ? 0.1196 0.1091 0.1922 -0.0268 -0.0121 0.0011  188 LEU A CA  
1505 C  C   . LEU A 188 ? 0.0853 0.1207 0.1976 -0.0006 -0.0218 -0.0261 188 LEU A C   
1506 O  O   . LEU A 188 ? 0.1220 0.1649 0.1634 -0.0441 -0.0072 -0.0343 188 LEU A O   
1507 C  CB  . LEU A 188 ? 0.1177 0.1245 0.2112 -0.0081 -0.0161 0.0092  188 LEU A CB  
1508 C  CG  . LEU A 188 ? 0.1530 0.1767 0.2186 0.0172  -0.0319 0.0117  188 LEU A CG  
1509 C  CD1 . LEU A 188 ? 0.1433 0.1476 0.3301 -0.0284 -0.0517 0.0829  188 LEU A CD1 
1510 C  CD2 . LEU A 188 ? 0.1329 0.2752 0.2116 -0.0184 -0.0326 0.0596  188 LEU A CD2 
1511 N  N   . ASP A 189 ? 0.0979 0.1688 0.1440 0.0193  0.0199  0.0079  189 ASP A N   
1512 C  CA  . ASP A 189 ? 0.0924 0.1613 0.1350 -0.0175 0.0160  -0.0044 189 ASP A CA  
1513 C  C   . ASP A 189 ? 0.0959 0.0943 0.1315 -0.0027 0.0095  0.0023  189 ASP A C   
1514 O  O   . ASP A 189 ? 0.0932 0.1340 0.1209 -0.0016 0.0018  -0.0034 189 ASP A O   
1515 C  CB  . ASP A 189 ? 0.1390 0.2022 0.1448 -0.0539 0.0234  0.0225  189 ASP A CB  
1516 C  CG  . ASP A 189 ? 0.1368 0.3042 0.1965 -0.0692 0.0201  -0.0159 189 ASP A CG  
1517 O  OD1 . ASP A 189 ? 0.1397 0.3879 0.2446 -0.0428 0.0591  -0.0642 189 ASP A OD1 
1518 O  OD2 . ASP A 189 ? 0.2090 0.3710 0.2573 -0.1241 0.0016  0.0621  189 ASP A OD2 
1519 N  N   . TYR A 190 ? 0.0680 0.1354 0.1229 -0.0053 0.0111  0.0040  190 TYR A N   
1520 C  CA  . TYR A 190 ? 0.0706 0.1094 0.0985 -0.0122 0.0070  0.0126  190 TYR A CA  
1521 C  C   . TYR A 190 ? 0.0862 0.1054 0.0888 0.0140  0.0135  0.0122  190 TYR A C   
1522 O  O   . TYR A 190 ? 0.0944 0.1394 0.1058 0.0055  0.0336  0.0185  190 TYR A O   
1523 C  CB  . TYR A 190 ? 0.1243 0.0933 0.0870 0.0133  0.0054  0.0104  190 TYR A CB  
1524 C  CG  . TYR A 190 ? 0.0884 0.1036 0.0927 -0.0092 0.0168  0.0100  190 TYR A CG  
1525 C  CD1 . TYR A 190 ? 0.1390 0.1243 0.0995 -0.0290 0.0018  0.0089  190 TYR A CD1 
1526 C  CD2 . TYR A 190 ? 0.0934 0.1310 0.1343 0.0085  0.0411  0.0126  190 TYR A CD2 
1527 C  CE1 . TYR A 190 ? 0.1044 0.1067 0.1335 0.0111  0.0119  0.0221  190 TYR A CE1 
1528 C  CE2 . TYR A 190 ? 0.0960 0.1173 0.1285 -0.0049 -0.0042 0.0041  190 TYR A CE2 
1529 C  CZ  . TYR A 190 ? 0.0999 0.1200 0.1307 -0.0016 -0.0110 0.0108  190 TYR A CZ  
1530 O  OH  . TYR A 190 ? 0.1372 0.1178 0.1684 0.0175  0.0034  0.0071  190 TYR A OH  
1531 N  N   . TRP A 191 ? 0.0699 0.0902 0.1075 -0.0089 0.0015  -0.0032 191 TRP A N   
1532 C  CA  . TRP A 191 ? 0.0719 0.0952 0.1200 -0.0203 0.0057  -0.0121 191 TRP A CA  
1533 C  C   . TRP A 191 ? 0.0929 0.1023 0.0759 -0.0149 0.0258  -0.0067 191 TRP A C   
1534 O  O   . TRP A 191 ? 0.1296 0.1282 0.0723 -0.0197 0.0147  -0.0148 191 TRP A O   
1535 C  CB  . TRP A 191 ? 0.1135 0.1021 0.1044 0.0018  0.0301  0.0044  191 TRP A CB  
1536 C  CG  . TRP A 191 ? 0.0978 0.1005 0.1112 0.0095  0.0075  0.0115  191 TRP A CG  
1537 C  CD1 . TRP A 191 ? 0.1155 0.1142 0.1127 0.0031  0.0163  0.0168  191 TRP A CD1 
1538 C  CD2 . TRP A 191 ? 0.0907 0.1058 0.1142 0.0097  0.0013  0.0143  191 TRP A CD2 
1539 N  NE1 . TRP A 191 ? 0.1386 0.1088 0.1448 0.0143  0.0177  0.0173  191 TRP A NE1 
1540 C  CE2 . TRP A 191 ? 0.1006 0.0827 0.1372 0.0254  -0.0034 0.0155  191 TRP A CE2 
1541 C  CE3 . TRP A 191 ? 0.0750 0.1529 0.1393 0.0088  -0.0208 -0.0326 191 TRP A CE3 
1542 C  CZ2 . TRP A 191 ? 0.1444 0.0889 0.1487 -0.0011 -0.0058 0.0182  191 TRP A CZ2 
1543 C  CZ3 . TRP A 191 ? 0.1014 0.1372 0.1407 -0.0121 -0.0145 -0.0200 191 TRP A CZ3 
1544 C  CH2 . TRP A 191 ? 0.1346 0.1473 0.1465 0.0219  -0.0240 0.0033  191 TRP A CH2 
1545 N  N   . THR A 192 ? 0.0880 0.1163 0.0785 -0.0096 0.0018  0.0017  192 THR A N   
1546 C  CA  . THR A 192 ? 0.0715 0.1120 0.0960 -0.0017 0.0067  -0.0004 192 THR A CA  
1547 C  C   . THR A 192 ? 0.0756 0.1278 0.0857 0.0005  0.0064  0.0078  192 THR A C   
1548 O  O   . THR A 192 ? 0.1047 0.1214 0.0918 -0.0061 -0.0067 0.0084  192 THR A O   
1549 C  CB  . THR A 192 ? 0.0891 0.1032 0.0787 0.0104  0.0171  -0.0004 192 THR A CB  
1550 O  OG1 . THR A 192 ? 0.0762 0.1024 0.1214 0.0127  0.0029  -0.0055 192 THR A OG1 
1551 C  CG2 . THR A 192 ? 0.1272 0.1404 0.0801 0.0366  0.0233  0.0055  192 THR A CG2 
1552 N  N   . TYR A 193 ? 0.0654 0.0936 0.0915 0.0035  0.0025  -0.0168 193 TYR A N   
1553 C  CA  . TYR A 193 ? 0.0674 0.0918 0.0979 0.0155  -0.0067 -0.0084 193 TYR A CA  
1554 C  C   . TYR A 193 ? 0.0741 0.0908 0.0837 0.0125  -0.0132 -0.0194 193 TYR A C   
1555 O  O   . TYR A 193 ? 0.0952 0.0936 0.0847 0.0000  -0.0186 -0.0080 193 TYR A O   
1556 C  CB  . TYR A 193 ? 0.1006 0.1040 0.1134 0.0434  0.0044  -0.0268 193 TYR A CB  
1557 C  CG  . TYR A 193 ? 0.0771 0.0582 0.0918 0.0168  -0.0051 -0.0030 193 TYR A CG  
1558 C  CD1 . TYR A 193 ? 0.0947 0.0617 0.0811 0.0072  -0.0086 -0.0004 193 TYR A CD1 
1559 C  CD2 . TYR A 193 ? 0.0803 0.0830 0.1074 0.0159  0.0075  -0.0229 193 TYR A CD2 
1560 C  CE1 . TYR A 193 ? 0.0970 0.0680 0.0990 -0.0054 0.0211  0.0141  193 TYR A CE1 
1561 C  CE2 . TYR A 193 ? 0.1249 0.0679 0.0717 0.0183  -0.0046 -0.0108 193 TYR A CE2 
1562 C  CZ  . TYR A 193 ? 0.0708 0.0545 0.0972 0.0201  0.0005  -0.0134 193 TYR A CZ  
1563 O  OH  . TYR A 193 ? 0.0882 0.0523 0.1021 0.0154  0.0104  -0.0036 193 TYR A OH  
1564 N  N   . PRO A 194 ? 0.0898 0.1002 0.0920 -0.0030 0.0001  -0.0397 194 PRO A N   
1565 C  CA  . PRO A 194 ? 0.0873 0.0800 0.1351 -0.0030 0.0197  -0.0522 194 PRO A CA  
1566 C  C   . PRO A 194 ? 0.0730 0.0812 0.1049 0.0220  -0.0078 -0.0223 194 PRO A C   
1567 O  O   . PRO A 194 ? 0.0890 0.0961 0.1181 0.0212  -0.0122 -0.0077 194 PRO A O   
1568 C  CB  . PRO A 194 ? 0.1314 0.0952 0.0888 0.0086  0.0219  -0.0370 194 PRO A CB  
1569 C  CG  . PRO A 194 ? 0.1476 0.1142 0.0926 -0.0284 0.0010  -0.0285 194 PRO A CG  
1570 C  CD  . PRO A 194 ? 0.1347 0.1426 0.0854 -0.0230 -0.0005 -0.0435 194 PRO A CD  
1571 N  N   . GLY A 195 ? 0.0918 0.0597 0.1160 -0.0025 0.0234  -0.0368 195 GLY A N   
1572 C  CA  . GLY A 195 ? 0.0846 0.0830 0.0810 0.0057  0.0163  -0.0118 195 GLY A CA  
1573 C  C   . GLY A 195 ? 0.0714 0.0593 0.0884 -0.0115 -0.0076 -0.0111 195 GLY A C   
1574 O  O   . GLY A 195 ? 0.0911 0.0559 0.1254 -0.0073 -0.0039 -0.0129 195 GLY A O   
1575 N  N   . SER A 196 ? 0.0778 0.0814 0.0769 0.0042  0.0015  0.0013  196 SER A N   
1576 C  CA  . SER A 196 ? 0.0617 0.1074 0.0758 0.0227  0.0172  -0.0018 196 SER A CA  
1577 C  C   . SER A 196 ? 0.0589 0.0536 0.1024 -0.0042 -0.0039 -0.0068 196 SER A C   
1578 O  O   . SER A 196 ? 0.0625 0.0600 0.1127 -0.0074 -0.0055 -0.0117 196 SER A O   
1579 C  CB  . SER A 196 ? 0.0636 0.1011 0.1040 0.0263  -0.0040 -0.0518 196 SER A CB  
1580 O  OG  . SER A 196 ? 0.0751 0.0780 0.1141 0.0004  -0.0013 -0.0266 196 SER A OG  
1581 N  N   . LEU A 197 ? 0.0726 0.0663 0.0935 0.0175  0.0023  0.0052  197 LEU A N   
1582 C  CA  . LEU A 197 ? 0.0952 0.0559 0.0979 -0.0098 0.0073  0.0008  197 LEU A CA  
1583 C  C   . LEU A 197 ? 0.0753 0.0656 0.0932 -0.0057 -0.0067 0.0106  197 LEU A C   
1584 O  O   . LEU A 197 ? 0.0758 0.0714 0.1040 -0.0093 -0.0080 -0.0244 197 LEU A O   
1585 C  CB  . LEU A 197 ? 0.0886 0.0559 0.1433 -0.0067 0.0120  0.0226  197 LEU A CB  
1586 C  CG  . LEU A 197 ? 0.1278 0.0399 0.1692 -0.0188 -0.0095 0.0288  197 LEU A CG  
1587 C  CD1 . LEU A 197 ? 0.1918 0.0742 0.1990 -0.0650 -0.0081 0.0401  197 LEU A CD1 
1588 C  CD2 . LEU A 197 ? 0.1047 0.1286 0.2151 0.0388  0.0269  0.0630  197 LEU A CD2 
1589 N  N   . THR A 198 ? 0.0857 0.0662 0.1128 0.0201  -0.0047 -0.0136 198 THR A N   
1590 C  CA  . THR A 198 ? 0.0635 0.0549 0.1361 0.0051  -0.0052 0.0108  198 THR A CA  
1591 C  C   . THR A 198 ? 0.0607 0.0748 0.1333 -0.0094 -0.0061 0.0000  198 THR A C   
1592 O  O   . THR A 198 ? 0.0741 0.0812 0.1443 -0.0138 0.0114  -0.0099 198 THR A O   
1593 C  CB  . THR A 198 ? 0.0663 0.0950 0.0938 -0.0184 -0.0025 0.0027  198 THR A CB  
1594 O  OG1 . THR A 198 ? 0.0724 0.0584 0.0938 0.0010  -0.0055 0.0119  198 THR A OG1 
1595 C  CG2 . THR A 198 ? 0.0753 0.0872 0.0947 0.0108  0.0048  -0.0011 198 THR A CG2 
1596 N  N   . THR A 199 ? 0.0769 0.0965 0.1171 -0.0244 0.0135  0.0040  199 THR A N   
1597 C  CA  . THR A 199 ? 0.0987 0.1279 0.1058 -0.0483 0.0184  0.0059  199 THR A CA  
1598 C  C   . THR A 199 ? 0.1090 0.1146 0.1365 -0.0311 -0.0118 0.0100  199 THR A C   
1599 O  O   . THR A 199 ? 0.1017 0.1089 0.1529 -0.0359 0.0077  0.0132  199 THR A O   
1600 C  CB  . THR A 199 ? 0.1552 0.0923 0.1249 -0.0321 -0.0168 -0.0070 199 THR A CB  
1601 O  OG1 . THR A 199 ? 0.2371 0.1234 0.1782 0.0190  -0.0792 -0.0390 199 THR A OG1 
1602 C  CG2 . THR A 199 ? 0.1480 0.0823 0.1462 -0.0300 -0.0245 -0.0057 199 THR A CG2 
1603 N  N   . PRO A 200 ? 0.1268 0.1182 0.1336 -0.0381 0.0188  -0.0110 200 PRO A N   
1604 C  CA  . PRO A 200 ? 0.0810 0.1415 0.1709 -0.0450 0.0060  0.0100  200 PRO A CA  
1605 C  C   . PRO A 200 ? 0.0990 0.1422 0.1164 -0.0296 0.0307  -0.0061 200 PRO A C   
1606 O  O   . PRO A 200 ? 0.1544 0.1580 0.1426 -0.0381 -0.0072 -0.0047 200 PRO A O   
1607 C  CB  . PRO A 200 ? 0.1135 0.1699 0.1882 -0.0283 0.0300  -0.0033 200 PRO A CB  
1608 C  CG  . PRO A 200 ? 0.0944 0.1978 0.1742 -0.0200 0.0147  -0.0263 200 PRO A CG  
1609 C  CD  . PRO A 200 ? 0.1005 0.1594 0.1479 -0.0184 0.0122  -0.0176 200 PRO A CD  
1610 N  N   . PRO A 201 ? 0.1119 0.1340 0.1250 -0.0388 0.0025  0.0098  201 PRO A N   
1611 C  CA  . PRO A 201 ? 0.1397 0.1354 0.1324 -0.0738 -0.0015 0.0036  201 PRO A CA  
1612 C  C   . PRO A 201 ? 0.0970 0.1166 0.1386 -0.0176 -0.0031 0.0208  201 PRO A C   
1613 O  O   . PRO A 201 ? 0.1057 0.1282 0.1559 -0.0128 -0.0138 -0.0105 201 PRO A O   
1614 C  CB  . PRO A 201 ? 0.1767 0.1397 0.1803 -0.0458 0.0032  0.0267  201 PRO A CB  
1615 C  CG  . PRO A 201 ? 0.2136 0.1181 0.2612 -0.0417 -0.0598 0.0067  201 PRO A CG  
1616 C  CD  . PRO A 201 ? 0.1899 0.1214 0.2105 -0.0189 -0.0185 0.0070  201 PRO A CD  
1617 N  N   . LEU A 202 ? 0.0986 0.0787 0.1486 -0.0115 0.0153  -0.0006 202 LEU A N   
1618 C  CA  . LEU A 202 ? 0.0819 0.0836 0.1304 0.0063  -0.0080 0.0027  202 LEU A CA  
1619 C  C   . LEU A 202 ? 0.0454 0.0945 0.1336 -0.0183 -0.0198 -0.0037 202 LEU A C   
1620 O  O   . LEU A 202 ? 0.0713 0.0961 0.1383 0.0050  -0.0163 -0.0200 202 LEU A O   
1621 C  CB  . LEU A 202 ? 0.0685 0.1038 0.1353 0.0120  -0.0221 -0.0230 202 LEU A CB  
1622 C  CG  . LEU A 202 ? 0.0671 0.0789 0.1695 0.0125  0.0145  -0.0173 202 LEU A CG  
1623 C  CD1 . LEU A 202 ? 0.0593 0.1512 0.1874 0.0111  0.0016  -0.0070 202 LEU A CD1 
1624 C  CD2 . LEU A 202 ? 0.1110 0.0974 0.1523 -0.0150 0.0033  -0.0171 202 LEU A CD2 
1625 N  N   . THR A 203 ? 0.0826 0.0884 0.1606 0.0077  -0.0282 -0.0127 203 THR A N   
1626 C  CA  . THR A 203 ? 0.0905 0.0907 0.1648 -0.0027 -0.0006 -0.0058 203 THR A CA  
1627 C  C   . THR A 203 ? 0.0884 0.0668 0.1368 0.0041  -0.0064 -0.0127 203 THR A C   
1628 O  O   . THR A 203 ? 0.1045 0.0624 0.1451 -0.0046 -0.0140 -0.0115 203 THR A O   
1629 C  CB  . THR A 203 ? 0.1527 0.0803 0.2151 -0.0049 0.0116  0.0122  203 THR A CB  
1630 O  OG1 . THR A 203 ? 0.1580 0.1196 0.2493 0.0005  0.0381  0.0218  203 THR A OG1 
1631 C  CG2 . THR A 203 ? 0.1867 0.1254 0.2784 0.0315  0.0165  -0.0482 203 THR A CG2 
1632 N  N   . GLU A 204 ? 0.1178 0.0900 0.1364 0.0021  -0.0121 -0.0269 204 GLU A N   
1633 C  CA  . GLU A 204 ? 0.0783 0.1153 0.1332 0.0065  -0.0303 -0.0312 204 GLU A CA  
1634 C  C   . GLU A 204 ? 0.1046 0.0952 0.1203 0.0137  -0.0204 -0.0228 204 GLU A C   
1635 O  O   . GLU A 204 ? 0.1613 0.1271 0.1458 0.0406  -0.0451 -0.0594 204 GLU A O   
1636 C  CB  . GLU A 204 ? 0.1093 0.1182 0.1351 0.0374  -0.0422 -0.0428 204 GLU A CB  
1637 C  CG  . GLU A 204 ? 0.0665 0.1102 0.1491 0.0178  -0.0190 -0.0221 204 GLU A CG  
1638 C  CD  . GLU A 204 ? 0.0933 0.1375 0.1687 0.0175  -0.0465 -0.0402 204 GLU A CD  
1639 O  OE1 . GLU A 204 ? 0.1311 0.1494 0.2320 0.0170  -0.0885 -0.0627 204 GLU A OE1 
1640 O  OE2 . GLU A 204 ? 0.0936 0.1238 0.1606 -0.0003 -0.0308 -0.0135 204 GLU A OE2 
1641 N  N   . CYS A 205 ? 0.0785 0.0601 0.1247 0.0042  -0.0145 -0.0166 205 CYS A N   
1642 C  CA  . CYS A 205 ? 0.0688 0.0553 0.1254 0.0027  0.0020  -0.0012 205 CYS A CA  
1643 C  C   . CYS A 205 ? 0.0809 0.0656 0.1450 -0.0069 -0.0110 -0.0082 205 CYS A C   
1644 O  O   . CYS A 205 ? 0.0951 0.0789 0.1512 0.0038  -0.0226 -0.0086 205 CYS A O   
1645 C  CB  . CYS A 205 ? 0.1220 0.0653 0.1256 -0.0271 -0.0001 0.0034  205 CYS A CB  
1646 S  SG  . CYS A 205 ? 0.1491 0.1186 0.1397 0.0216  -0.0042 -0.0147 205 CYS A SG  
1647 N  N   . VAL A 206 ? 0.0741 0.0687 0.1213 -0.0107 -0.0087 -0.0023 206 VAL A N   
1648 C  CA  . VAL A 206 ? 0.0762 0.0602 0.1005 -0.0005 -0.0156 -0.0268 206 VAL A CA  
1649 C  C   . VAL A 206 ? 0.0814 0.0487 0.1124 0.0113  -0.0065 -0.0159 206 VAL A C   
1650 O  O   . VAL A 206 ? 0.0961 0.0920 0.1207 0.0111  -0.0116 0.0034  206 VAL A O   
1651 C  CB  . VAL A 206 ? 0.0882 0.0522 0.1049 -0.0097 -0.0107 -0.0248 206 VAL A CB  
1652 C  CG1 . VAL A 206 ? 0.0952 0.0453 0.1382 0.0000  -0.0469 -0.0128 206 VAL A CG1 
1653 C  CG2 . VAL A 206 ? 0.0968 0.1090 0.1296 0.0181  0.0033  0.0113  206 VAL A CG2 
1654 N  N   . THR A 207 ? 0.0697 0.0507 0.1042 -0.0100 0.0038  -0.0161 207 THR A N   
1655 C  CA  . THR A 207 ? 0.0759 0.0714 0.0960 -0.0057 0.0190  -0.0256 207 THR A CA  
1656 C  C   . THR A 207 ? 0.0724 0.0586 0.1038 -0.0175 -0.0002 -0.0024 207 THR A C   
1657 O  O   . THR A 207 ? 0.0864 0.0812 0.1146 -0.0066 -0.0157 -0.0073 207 THR A O   
1658 C  CB  . THR A 207 ? 0.0679 0.0880 0.1037 -0.0034 0.0133  -0.0296 207 THR A CB  
1659 O  OG1 . THR A 207 ? 0.1225 0.0888 0.1261 -0.0174 0.0097  -0.0337 207 THR A OG1 
1660 C  CG2 . THR A 207 ? 0.0979 0.1171 0.1214 0.0044  0.0242  0.0064  207 THR A CG2 
1661 N  N   . TRP A 208 ? 0.0812 0.0563 0.1072 -0.0051 -0.0082 -0.0164 208 TRP A N   
1662 C  CA  . TRP A 208 ? 0.0654 0.0541 0.0900 0.0021  -0.0051 -0.0192 208 TRP A CA  
1663 C  C   . TRP A 208 ? 0.0717 0.0674 0.0821 0.0069  -0.0033 0.0036  208 TRP A C   
1664 O  O   . TRP A 208 ? 0.0873 0.0759 0.0900 -0.0032 -0.0047 -0.0030 208 TRP A O   
1665 C  CB  . TRP A 208 ? 0.0687 0.0706 0.0864 0.0091  0.0022  0.0057  208 TRP A CB  
1666 C  CG  . TRP A 208 ? 0.0645 0.0399 0.0983 -0.0043 0.0055  -0.0002 208 TRP A CG  
1667 C  CD1 . TRP A 208 ? 0.0635 0.0564 0.1102 0.0027  -0.0012 -0.0068 208 TRP A CD1 
1668 C  CD2 . TRP A 208 ? 0.0757 0.0355 0.1107 0.0077  0.0054  -0.0212 208 TRP A CD2 
1669 N  NE1 . TRP A 208 ? 0.0837 0.0697 0.1014 0.0082  -0.0040 -0.0127 208 TRP A NE1 
1670 C  CE2 . TRP A 208 ? 0.0794 0.0626 0.0918 0.0122  -0.0038 0.0023  208 TRP A CE2 
1671 C  CE3 . TRP A 208 ? 0.0911 0.0610 0.0968 0.0206  -0.0138 -0.0189 208 TRP A CE3 
1672 C  CZ2 . TRP A 208 ? 0.1032 0.0396 0.1028 0.0260  0.0050  -0.0046 208 TRP A CZ2 
1673 C  CZ3 . TRP A 208 ? 0.0793 0.0660 0.0929 0.0126  0.0011  -0.0054 208 TRP A CZ3 
1674 C  CH2 . TRP A 208 ? 0.0785 0.0701 0.1343 0.0230  0.0077  -0.0024 208 TRP A CH2 
1675 N  N   . ILE A 209 ? 0.0791 0.0451 0.0872 -0.0061 0.0010  -0.0012 209 ILE A N   
1676 C  CA  . ILE A 209 ? 0.0600 0.0496 0.0983 -0.0006 -0.0113 0.0012  209 ILE A CA  
1677 C  C   . ILE A 209 ? 0.0601 0.0723 0.0854 -0.0013 -0.0036 -0.0051 209 ILE A C   
1678 O  O   . ILE A 209 ? 0.0997 0.0708 0.0890 0.0000  0.0068  0.0059  209 ILE A O   
1679 C  CB  . ILE A 209 ? 0.0782 0.0507 0.1336 0.0142  -0.0058 -0.0106 209 ILE A CB  
1680 C  CG1 . ILE A 209 ? 0.0854 0.0494 0.1307 0.0172  -0.0173 -0.0081 209 ILE A CG1 
1681 C  CG2 . ILE A 209 ? 0.0862 0.1075 0.1393 -0.0038 -0.0003 0.0141  209 ILE A CG2 
1682 C  CD1 . ILE A 209 ? 0.1142 0.0880 0.1692 0.0379  -0.0201 0.0257  209 ILE A CD1 
1683 N  N   . VAL A 210 ? 0.0724 0.0599 0.1017 0.0061  -0.0047 -0.0087 210 VAL A N   
1684 C  CA  . VAL A 210 ? 0.0629 0.0665 0.1063 0.0061  0.0113  -0.0135 210 VAL A CA  
1685 C  C   . VAL A 210 ? 0.0662 0.0663 0.0768 0.0023  0.0055  0.0115  210 VAL A C   
1686 O  O   . VAL A 210 ? 0.1078 0.0863 0.0760 -0.0124 0.0039  0.0136  210 VAL A O   
1687 C  CB  . VAL A 210 ? 0.0721 0.0505 0.0970 -0.0081 -0.0052 0.0030  210 VAL A CB  
1688 C  CG1 . VAL A 210 ? 0.0950 0.0546 0.1353 0.0088  -0.0174 -0.0158 210 VAL A CG1 
1689 C  CG2 . VAL A 210 ? 0.0882 0.0706 0.1173 -0.0193 0.0138  0.0171  210 VAL A CG2 
1690 N  N   . LEU A 211 ? 0.0776 0.0690 0.0995 -0.0131 -0.0034 0.0055  211 LEU A N   
1691 C  CA  . LEU A 211 ? 0.0701 0.0941 0.0972 -0.0100 -0.0024 0.0211  211 LEU A CA  
1692 C  C   . LEU A 211 ? 0.0909 0.0888 0.0950 -0.0139 -0.0006 0.0155  211 LEU A C   
1693 O  O   . LEU A 211 ? 0.1062 0.0856 0.0995 -0.0080 -0.0053 0.0062  211 LEU A O   
1694 C  CB  . LEU A 211 ? 0.1103 0.0941 0.0926 -0.0254 -0.0068 0.0374  211 LEU A CB  
1695 C  CG  . LEU A 211 ? 0.1093 0.1005 0.1153 0.0049  -0.0099 0.0211  211 LEU A CG  
1696 C  CD1 . LEU A 211 ? 0.1044 0.1598 0.1207 0.0102  -0.0125 0.0148  211 LEU A CD1 
1697 C  CD2 . LEU A 211 ? 0.0864 0.1015 0.1627 0.0034  0.0222  0.0084  211 LEU A CD2 
1698 N  N   A LYS A 212 ? 0.0969 0.0979 0.1170 -0.0370 0.0027  0.0105  212 LYS A N   
1699 N  N   B LYS A 212 ? 0.0961 0.0976 0.1168 -0.0374 0.0022  0.0105  212 LYS A N   
1700 C  CA  A LYS A 212 ? 0.1491 0.0985 0.1397 -0.0079 -0.0211 0.0192  212 LYS A CA  
1701 C  CA  B LYS A 212 ? 0.1462 0.0988 0.1386 -0.0063 -0.0195 0.0183  212 LYS A CA  
1702 C  C   A LYS A 212 ? 0.0994 0.1029 0.1286 -0.0247 0.0024  0.0311  212 LYS A C   
1703 C  C   B LYS A 212 ? 0.0995 0.1024 0.1289 -0.0248 0.0021  0.0310  212 LYS A C   
1704 O  O   A LYS A 212 ? 0.1116 0.1227 0.1763 -0.0047 -0.0140 0.0099  212 LYS A O   
1705 O  O   B LYS A 212 ? 0.1115 0.1227 0.1764 -0.0044 -0.0138 0.0100  212 LYS A O   
1706 C  CB  A LYS A 212 ? 0.2708 0.1850 0.1393 -0.0653 0.0008  0.0421  212 LYS A CB  
1707 C  CB  B LYS A 212 ? 0.2544 0.1681 0.1533 -0.0845 -0.0009 0.0311  212 LYS A CB  
1708 C  CG  A LYS A 212 ? 0.3699 0.2372 0.1949 -0.1233 -0.0132 0.0717  212 LYS A CG  
1709 C  CG  B LYS A 212 ? 0.2904 0.1911 0.1720 -0.0084 -0.0543 0.0779  212 LYS A CG  
1710 C  CD  A LYS A 212 ? 0.4171 0.2363 0.2061 -0.1335 0.0256  0.0207  212 LYS A CD  
1711 C  CD  B LYS A 212 ? 0.3380 0.2544 0.2870 -0.0734 0.0331  0.0746  212 LYS A CD  
1712 C  CE  A LYS A 212 ? 0.4250 0.1983 0.2716 -0.0320 0.0227  0.0950  212 LYS A CE  
1713 C  CE  B LYS A 212 ? 0.3808 0.2705 0.2997 -0.0376 0.0348  0.1081  212 LYS A CE  
1714 N  NZ  A LYS A 212 ? 0.1839 0.1620 0.2537 -0.0381 -0.0566 0.0144  212 LYS A NZ  
1715 N  NZ  B LYS A 212 ? 0.3853 0.3775 0.4268 0.0175  0.0758  0.1872  212 LYS A NZ  
1716 N  N   . GLU A 213 ? 0.0873 0.0805 0.1145 -0.0219 0.0047  0.0122  213 GLU A N   
1717 C  CA  . GLU A 213 ? 0.0952 0.0908 0.1314 -0.0229 0.0002  0.0023  213 GLU A CA  
1718 C  C   . GLU A 213 ? 0.1088 0.0593 0.1372 -0.0321 0.0077  -0.0023 213 GLU A C   
1719 O  O   . GLU A 213 ? 0.0944 0.0809 0.1234 -0.0215 0.0030  0.0136  213 GLU A O   
1720 C  CB  . GLU A 213 ? 0.1049 0.1013 0.1498 -0.0114 -0.0117 0.0013  213 GLU A CB  
1721 C  CG  . GLU A 213 ? 0.1146 0.1293 0.1846 -0.0109 -0.0120 -0.0308 213 GLU A CG  
1722 C  CD  . GLU A 213 ? 0.1032 0.2124 0.3162 -0.0046 0.0203  -0.0638 213 GLU A CD  
1723 O  OE1 . GLU A 213 ? 0.1124 0.1118 0.2237 -0.0142 -0.0200 0.0034  213 GLU A OE1 
1724 O  OE2 . GLU A 213 ? 0.1882 0.3660 0.4224 -0.0421 -0.0044 -0.1434 213 GLU A OE2 
1725 N  N   A PRO A 214 ? 0.1178 0.0616 0.1163 -0.0160 0.0026  0.0119  214 PRO A N   
1726 N  N   B PRO A 214 ? 0.1100 0.0688 0.1142 -0.0139 0.0030  0.0098  214 PRO A N   
1727 C  CA  A PRO A 214 ? 0.1214 0.0872 0.1089 0.0129  0.0023  -0.0136 214 PRO A CA  
1728 C  CA  B PRO A 214 ? 0.1135 0.0952 0.1084 0.0166  0.0026  -0.0136 214 PRO A CA  
1729 C  C   A PRO A 214 ? 0.1014 0.1085 0.0972 -0.0226 0.0173  -0.0116 214 PRO A C   
1730 C  C   B PRO A 214 ? 0.1006 0.1152 0.0945 -0.0215 0.0159  -0.0122 214 PRO A C   
1731 O  O   A PRO A 214 ? 0.1032 0.1465 0.1275 -0.0438 -0.0103 0.0015  214 PRO A O   
1732 O  O   B PRO A 214 ? 0.1053 0.1674 0.1408 -0.0484 -0.0104 0.0039  214 PRO A O   
1733 C  CB  A PRO A 214 ? 0.1469 0.0416 0.1893 -0.0127 0.0031  0.0179  214 PRO A CB  
1734 C  CB  B PRO A 214 ? 0.1292 0.0597 0.1723 -0.0024 0.0037  0.0192  214 PRO A CB  
1735 C  CG  A PRO A 214 ? 0.1656 0.0399 0.2037 -0.0208 0.0194  0.0080  214 PRO A CG  
1736 C  CG  B PRO A 214 ? 0.0917 0.0798 0.1480 -0.0064 0.0019  -0.0115 214 PRO A CG  
1737 C  CD  A PRO A 214 ? 0.1624 0.0638 0.1832 -0.0095 0.0434  0.0288  214 PRO A CD  
1738 C  CD  B PRO A 214 ? 0.1267 0.0604 0.1763 0.0063  0.0367  0.0171  214 PRO A CD  
1739 N  N   . ILE A 215 ? 0.0942 0.0952 0.0977 -0.0132 0.0067  -0.0022 215 ILE A N   
1740 C  CA  . ILE A 215 ? 0.1483 0.0796 0.0920 -0.0182 -0.0061 -0.0110 215 ILE A CA  
1741 C  C   . ILE A 215 ? 0.1267 0.0859 0.1073 -0.0098 0.0057  0.0062  215 ILE A C   
1742 O  O   . ILE A 215 ? 0.1297 0.0936 0.1430 -0.0190 -0.0115 -0.0288 215 ILE A O   
1743 C  CB  . ILE A 215 ? 0.1153 0.0769 0.1112 0.0037  0.0065  -0.0035 215 ILE A CB  
1744 C  CG1 . ILE A 215 ? 0.1279 0.0830 0.1188 -0.0134 0.0087  0.0048  215 ILE A CG1 
1745 C  CG2 . ILE A 215 ? 0.1286 0.0780 0.1598 0.0127  0.0135  -0.0128 215 ILE A CG2 
1746 C  CD1 . ILE A 215 ? 0.1286 0.0862 0.1336 -0.0029 -0.0278 0.0130  215 ILE A CD1 
1747 N  N   A SER A 216 ? 0.1602 0.0853 0.1451 -0.0006 -0.0133 -0.0273 216 SER A N   
1748 N  N   B SER A 216 ? 0.1613 0.0944 0.1426 -0.0063 -0.0079 -0.0222 216 SER A N   
1749 C  CA  A SER A 216 ? 0.1324 0.0805 0.1088 -0.0279 -0.0227 -0.0251 216 SER A CA  
1750 C  CA  B SER A 216 ? 0.1627 0.1062 0.1186 -0.0185 0.0379  -0.0119 216 SER A CA  
1751 C  C   A SER A 216 ? 0.1383 0.0791 0.1307 -0.0189 -0.0052 -0.0055 216 SER A C   
1752 C  C   B SER A 216 ? 0.1365 0.0751 0.1300 -0.0132 -0.0058 0.0046  216 SER A C   
1753 O  O   A SER A 216 ? 0.1796 0.1072 0.1468 -0.0044 -0.0245 -0.0054 216 SER A O   
1754 O  O   B SER A 216 ? 0.1559 0.0963 0.1220 -0.0133 -0.0296 -0.0050 216 SER A O   
1755 C  CB  A SER A 216 ? 0.1304 0.1249 0.1839 -0.0488 -0.0291 -0.0386 216 SER A CB  
1756 C  CB  B SER A 216 ? 0.1766 0.1426 0.1792 -0.0320 0.0245  0.0862  216 SER A CB  
1757 O  OG  A SER A 216 ? 0.2669 0.2044 0.1534 -0.0834 -0.0120 -0.0362 216 SER A OG  
1758 O  OG  B SER A 216 ? 0.1698 0.2482 0.1965 -0.0974 -0.0445 0.0013  216 SER A OG  
1759 N  N   . VAL A 217 ? 0.1253 0.0778 0.1261 -0.0286 -0.0155 -0.0237 217 VAL A N   
1760 C  CA  . VAL A 217 ? 0.1315 0.0782 0.1214 -0.0141 -0.0043 -0.0132 217 VAL A CA  
1761 C  C   . VAL A 217 ? 0.1186 0.0692 0.1368 -0.0108 -0.0402 0.0020  217 VAL A C   
1762 O  O   . VAL A 217 ? 0.1343 0.0642 0.1444 -0.0099 -0.0293 0.0125  217 VAL A O   
1763 C  CB  . VAL A 217 ? 0.1209 0.0592 0.1885 -0.0046 -0.0196 -0.0168 217 VAL A CB  
1764 C  CG1 . VAL A 217 ? 0.1591 0.0634 0.1595 -0.0048 -0.0148 -0.0082 217 VAL A CG1 
1765 C  CG2 . VAL A 217 ? 0.1279 0.0729 0.2187 -0.0154 -0.0422 -0.0216 217 VAL A CG2 
1766 N  N   . SER A 218 ? 0.1602 0.0706 0.1196 -0.0167 -0.0094 -0.0120 218 SER A N   
1767 C  CA  . SER A 218 ? 0.1419 0.0580 0.1562 -0.0230 -0.0148 -0.0134 218 SER A CA  
1768 C  C   . SER A 218 ? 0.1458 0.0565 0.1494 -0.0185 0.0054  -0.0130 218 SER A C   
1769 O  O   . SER A 218 ? 0.1462 0.0511 0.1451 -0.0158 -0.0118 0.0091  218 SER A O   
1770 C  CB  . SER A 218 ? 0.1958 0.0741 0.1103 -0.0288 -0.0012 -0.0026 218 SER A CB  
1771 O  OG  . SER A 218 ? 0.1606 0.0544 0.1483 -0.0239 -0.0140 0.0058  218 SER A OG  
1772 N  N   . SER A 219 ? 0.1580 0.0656 0.1455 0.0013  0.0221  -0.0151 219 SER A N   
1773 C  CA  . SER A 219 ? 0.1547 0.0714 0.2044 -0.0133 0.0253  0.0267  219 SER A CA  
1774 C  C   . SER A 219 ? 0.1468 0.0559 0.1824 -0.0108 0.0151  -0.0038 219 SER A C   
1775 O  O   . SER A 219 ? 0.1419 0.0881 0.2423 -0.0268 0.0111  0.0021  219 SER A O   
1776 C  CB  . SER A 219 ? 0.2162 0.0738 0.2000 -0.0159 -0.0004 0.0134  219 SER A CB  
1777 O  OG  . SER A 219 ? 0.2011 0.0882 0.2277 -0.0104 0.0030  0.0029  219 SER A OG  
1778 N  N   . GLU A 220 ? 0.1763 0.0778 0.1699 0.0069  0.0065  0.0027  220 GLU A N   
1779 C  CA  . GLU A 220 ? 0.1821 0.0810 0.1799 -0.0065 -0.0118 0.0193  220 GLU A CA  
1780 C  C   . GLU A 220 ? 0.2015 0.0875 0.1752 -0.0249 0.0092  -0.0057 220 GLU A C   
1781 O  O   . GLU A 220 ? 0.1886 0.1121 0.1935 -0.0249 0.0128  0.0015  220 GLU A O   
1782 C  CB  . GLU A 220 ? 0.2460 0.1083 0.1839 -0.0222 -0.0326 -0.0292 220 GLU A CB  
1783 C  CG  . GLU A 220 ? 0.2788 0.0993 0.1648 -0.0220 0.0035  -0.0108 220 GLU A CG  
1784 C  CD  . GLU A 220 ? 0.2190 0.1221 0.2288 -0.0531 -0.0102 -0.0274 220 GLU A CD  
1785 O  OE1 . GLU A 220 ? 0.2094 0.1537 0.1949 -0.0424 -0.0044 -0.0330 220 GLU A OE1 
1786 O  OE2 . GLU A 220 ? 0.3738 0.1247 0.3590 -0.0836 -0.0232 -0.0422 220 GLU A OE2 
1787 N  N   . GLN A 221 ? 0.1734 0.0462 0.1692 -0.0098 -0.0122 0.0033  221 GLN A N   
1788 C  CA  . GLN A 221 ? 0.1372 0.0507 0.1534 -0.0256 -0.0065 0.0103  221 GLN A CA  
1789 C  C   . GLN A 221 ? 0.1268 0.0784 0.1404 -0.0118 -0.0047 0.0093  221 GLN A C   
1790 O  O   . GLN A 221 ? 0.1408 0.0944 0.1508 -0.0166 0.0052  0.0293  221 GLN A O   
1791 C  CB  . GLN A 221 ? 0.1358 0.1093 0.1451 -0.0204 -0.0055 0.0068  221 GLN A CB  
1792 C  CG  . GLN A 221 ? 0.1702 0.0943 0.1072 -0.0017 -0.0221 -0.0058 221 GLN A CG  
1793 C  CD  . GLN A 221 ? 0.1450 0.0977 0.1516 -0.0071 -0.0206 -0.0062 221 GLN A CD  
1794 O  OE1 . GLN A 221 ? 0.1523 0.0742 0.1569 -0.0115 -0.0114 0.0048  221 GLN A OE1 
1795 N  NE2 . GLN A 221 ? 0.1505 0.0811 0.1576 -0.0204 -0.0439 -0.0022 221 GLN A NE2 
1796 N  N   . VAL A 222 ? 0.1279 0.0672 0.1516 -0.0153 -0.0164 0.0138  222 VAL A N   
1797 C  CA  . VAL A 222 ? 0.1199 0.1150 0.1494 0.0059  -0.0130 0.0263  222 VAL A CA  
1798 C  C   . VAL A 222 ? 0.1254 0.0961 0.1541 -0.0050 -0.0085 0.0111  222 VAL A C   
1799 O  O   . VAL A 222 ? 0.1498 0.1022 0.1588 -0.0324 0.0054  0.0238  222 VAL A O   
1800 C  CB  . VAL A 222 ? 0.1749 0.1437 0.1796 -0.0076 -0.0372 0.0628  222 VAL A CB  
1801 C  CG1 . VAL A 222 ? 0.2209 0.1375 0.2274 0.0185  0.0094  0.0451  222 VAL A CG1 
1802 C  CG2 . VAL A 222 ? 0.1864 0.2141 0.1493 -0.0295 -0.0496 0.0616  222 VAL A CG2 
1803 N  N   . LEU A 223 ? 0.1624 0.0841 0.1879 -0.0011 0.0042  0.0052  223 LEU A N   
1804 C  CA  . LEU A 223 ? 0.2227 0.0961 0.1864 -0.0167 0.0475  -0.0035 223 LEU A CA  
1805 C  C   . LEU A 223 ? 0.1541 0.0891 0.1692 -0.0163 0.0104  -0.0115 223 LEU A C   
1806 O  O   . LEU A 223 ? 0.1321 0.1227 0.2083 -0.0105 0.0150  -0.0234 223 LEU A O   
1807 C  CB  . LEU A 223 ? 0.2213 0.1425 0.3116 -0.0506 0.0650  -0.0516 223 LEU A CB  
1808 C  CG  . LEU A 223 ? 0.3811 0.1766 0.2451 -0.1023 0.0462  -0.0476 223 LEU A CG  
1809 C  CD1 . LEU A 223 ? 0.4753 0.1379 0.2913 -0.0766 0.0030  -0.1159 223 LEU A CD1 
1810 C  CD2 . LEU A 223 ? 0.2852 0.2026 0.2752 -0.0859 0.0163  0.0116  223 LEU A CD2 
1811 N  N   . LYS A 224 ? 0.1577 0.0850 0.1595 -0.0278 0.0006  -0.0236 224 LYS A N   
1812 C  CA  . LYS A 224 ? 0.1570 0.1232 0.1120 -0.0314 -0.0060 -0.0100 224 LYS A CA  
1813 C  C   . LYS A 224 ? 0.1231 0.1207 0.1076 -0.0199 0.0040  -0.0042 224 LYS A C   
1814 O  O   . LYS A 224 ? 0.1483 0.1008 0.1173 -0.0064 0.0223  -0.0018 224 LYS A O   
1815 C  CB  . LYS A 224 ? 0.1828 0.1882 0.1268 -0.0198 -0.0155 0.0157  224 LYS A CB  
1816 C  CG  . LYS A 224 ? 0.2223 0.2046 0.1799 -0.0871 0.0068  0.0037  224 LYS A CG  
1817 C  CD  . LYS A 224 ? 0.2442 0.1853 0.2644 -0.0596 -0.0276 -0.0691 224 LYS A CD  
1818 C  CE  . LYS A 224 ? 0.3341 0.2137 0.2981 -0.0929 -0.0683 -0.0791 224 LYS A CE  
1819 N  NZ  . LYS A 224 ? 0.2460 0.2784 0.3894 0.0506  0.0702  -0.0575 224 LYS A NZ  
1820 N  N   . PHE A 225 ? 0.1347 0.0796 0.1067 0.0010  -0.0204 0.0065  225 PHE A N   
1821 C  CA  . PHE A 225 ? 0.1336 0.0909 0.1124 -0.0212 0.0171  -0.0151 225 PHE A CA  
1822 C  C   . PHE A 225 ? 0.1397 0.0665 0.1012 -0.0156 0.0060  -0.0060 225 PHE A C   
1823 O  O   . PHE A 225 ? 0.1562 0.0828 0.1146 -0.0245 0.0125  -0.0033 225 PHE A O   
1824 C  CB  . PHE A 225 ? 0.1351 0.0926 0.1159 0.0119  0.0124  0.0158  225 PHE A CB  
1825 C  CG  . PHE A 225 ? 0.1111 0.0528 0.1250 -0.0064 -0.0024 0.0068  225 PHE A CG  
1826 C  CD1 . PHE A 225 ? 0.1171 0.0972 0.1480 0.0108  0.0034  0.0238  225 PHE A CD1 
1827 C  CD2 . PHE A 225 ? 0.1155 0.1150 0.1350 -0.0107 0.0091  -0.0295 225 PHE A CD2 
1828 C  CE1 . PHE A 225 ? 0.1394 0.1254 0.1597 -0.0089 0.0266  -0.0001 225 PHE A CE1 
1829 C  CE2 . PHE A 225 ? 0.1394 0.1257 0.1598 0.0146  -0.0113 -0.0550 225 PHE A CE2 
1830 C  CZ  . PHE A 225 ? 0.0997 0.1214 0.1655 -0.0179 0.0109  -0.0208 225 PHE A CZ  
1831 N  N   . ARG A 226 ? 0.1322 0.0726 0.0911 0.0110  -0.0013 -0.0111 226 ARG A N   
1832 C  CA  . ARG A 226 ? 0.1254 0.0881 0.1168 0.0027  0.0044  0.0095  226 ARG A CA  
1833 C  C   . ARG A 226 ? 0.1049 0.0935 0.1220 0.0015  0.0013  -0.0029 226 ARG A C   
1834 O  O   . ARG A 226 ? 0.1214 0.1414 0.1353 0.0198  0.0114  -0.0013 226 ARG A O   
1835 C  CB  . ARG A 226 ? 0.1523 0.0977 0.1274 0.0284  0.0231  0.0249  226 ARG A CB  
1836 C  CG  . ARG A 226 ? 0.1491 0.0958 0.1155 0.0204  0.0103  0.0311  226 ARG A CG  
1837 C  CD  . ARG A 226 ? 0.2039 0.0835 0.1221 0.0093  0.0080  0.0134  226 ARG A CD  
1838 N  NE  . ARG A 226 ? 0.1518 0.0836 0.1347 -0.0328 -0.0005 0.0131  226 ARG A NE  
1839 C  CZ  . ARG A 226 ? 0.1142 0.1142 0.1238 -0.0387 -0.0263 -0.0190 226 ARG A CZ  
1840 N  NH1 . ARG A 226 ? 0.1680 0.1006 0.1749 -0.0365 -0.0321 -0.0479 226 ARG A NH1 
1841 N  NH2 . ARG A 226 ? 0.1400 0.0796 0.1505 -0.0155 0.0226  0.0164  226 ARG A NH2 
1842 N  N   . LYS A 227 ? 0.1455 0.1033 0.0830 -0.0055 0.0100  -0.0023 227 LYS A N   
1843 C  CA  . LYS A 227 ? 0.1566 0.1455 0.0954 -0.0302 0.0153  0.0177  227 LYS A CA  
1844 C  C   . LYS A 227 ? 0.1673 0.1058 0.1397 -0.0106 0.0462  -0.0212 227 LYS A C   
1845 O  O   . LYS A 227 ? 0.1954 0.1419 0.1142 -0.0083 0.0312  -0.0151 227 LYS A O   
1846 C  CB  . LYS A 227 ? 0.1620 0.1645 0.1124 -0.0336 0.0075  -0.0110 227 LYS A CB  
1847 C  CG  . LYS A 227 ? 0.2558 0.1803 0.1264 -0.0839 0.0162  -0.0546 227 LYS A CG  
1848 C  CD  . LYS A 227 ? 0.2820 0.3076 0.2284 -0.0565 -0.0401 -0.0939 227 LYS A CD  
1849 C  CE  . LYS A 227 ? 0.4390 0.3779 0.2471 -0.1444 0.0139  -0.0908 227 LYS A CE  
1850 N  NZ  . LYS A 227 ? 0.3980 0.4456 0.4128 -0.0171 -0.0603 -0.1456 227 LYS A NZ  
1851 N  N   . LEU A 228 ? 0.1437 0.0807 0.1293 -0.0102 0.0001  -0.0079 228 LEU A N   
1852 C  CA  . LEU A 228 ? 0.1159 0.0943 0.1040 -0.0201 0.0260  -0.0021 228 LEU A CA  
1853 C  C   . LEU A 228 ? 0.1328 0.0996 0.0792 -0.0074 0.0239  0.0152  228 LEU A C   
1854 O  O   . LEU A 228 ? 0.1529 0.1066 0.0995 0.0106  0.0057  0.0063  228 LEU A O   
1855 C  CB  . LEU A 228 ? 0.1145 0.0942 0.1300 0.0094  0.0219  -0.0073 228 LEU A CB  
1856 C  CG  . LEU A 228 ? 0.1218 0.0893 0.0969 0.0138  0.0134  0.0107  228 LEU A CG  
1857 C  CD1 . LEU A 228 ? 0.1386 0.0958 0.0932 0.0181  0.0053  0.0021  228 LEU A CD1 
1858 C  CD2 . LEU A 228 ? 0.1720 0.1185 0.1111 0.0085  0.0066  0.0326  228 LEU A CD2 
1859 N  N   . ASN A 229 ? 0.1318 0.1134 0.0941 -0.0229 0.0259  0.0119  229 ASN A N   
1860 C  CA  . ASN A 229 ? 0.1307 0.1256 0.1033 0.0061  0.0152  0.0022  229 ASN A CA  
1861 C  C   . ASN A 229 ? 0.1279 0.1049 0.1049 0.0070  0.0186  0.0114  229 ASN A C   
1862 O  O   . ASN A 229 ? 0.1450 0.0965 0.1426 0.0054  0.0160  0.0153  229 ASN A O   
1863 C  CB  . ASN A 229 ? 0.1494 0.1501 0.1225 0.0008  0.0346  0.0100  229 ASN A CB  
1864 C  CG  . ASN A 229 ? 0.1922 0.1469 0.1386 0.0099  0.0325  0.0100  229 ASN A CG  
1865 O  OD1 . ASN A 229 ? 0.2234 0.1616 0.1412 0.0129  0.0390  -0.0009 229 ASN A OD1 
1866 N  ND2 . ASN A 229 ? 0.1925 0.1638 0.1537 -0.0168 0.0445  -0.0193 229 ASN A ND2 
1867 N  N   . PHE A 230 ? 0.1346 0.1063 0.0732 -0.0160 0.0158  -0.0086 230 PHE A N   
1868 C  CA  . PHE A 230 ? 0.1178 0.0960 0.1098 -0.0233 0.0121  -0.0008 230 PHE A CA  
1869 C  C   . PHE A 230 ? 0.1523 0.1191 0.0882 -0.0093 0.0348  -0.0055 230 PHE A C   
1870 O  O   . PHE A 230 ? 0.1638 0.1108 0.1324 -0.0209 0.0300  -0.0067 230 PHE A O   
1871 C  CB  . PHE A 230 ? 0.1317 0.1261 0.0956 -0.0286 0.0058  -0.0027 230 PHE A CB  
1872 C  CG  . PHE A 230 ? 0.1386 0.0999 0.1160 -0.0288 0.0342  -0.0122 230 PHE A CG  
1873 C  CD1 . PHE A 230 ? 0.1272 0.1544 0.1148 -0.0128 0.0331  -0.0161 230 PHE A CD1 
1874 C  CD2 . PHE A 230 ? 0.1857 0.0927 0.1078 -0.0190 0.0319  -0.0262 230 PHE A CD2 
1875 C  CE1 . PHE A 230 ? 0.1781 0.1216 0.1153 -0.0170 0.0173  -0.0084 230 PHE A CE1 
1876 C  CE2 . PHE A 230 ? 0.1713 0.1137 0.0850 -0.0326 0.0055  -0.0211 230 PHE A CE2 
1877 C  CZ  . PHE A 230 ? 0.1164 0.1214 0.1436 0.0157  -0.0005 -0.0128 230 PHE A CZ  
1878 N  N   . ASN A 231 ? 0.1433 0.1146 0.0872 -0.0023 0.0400  0.0040  231 ASN A N   
1879 C  CA  . ASN A 231 ? 0.1516 0.0864 0.1185 -0.0039 0.0474  0.0187  231 ASN A CA  
1880 C  C   . ASN A 231 ? 0.1351 0.1397 0.0968 -0.0126 0.0280  0.0046  231 ASN A C   
1881 O  O   . ASN A 231 ? 0.1490 0.1109 0.1328 0.0066  0.0376  0.0122  231 ASN A O   
1882 C  CB  . ASN A 231 ? 0.1397 0.1049 0.1379 -0.0078 0.0541  -0.0029 231 ASN A CB  
1883 C  CG  . ASN A 231 ? 0.1461 0.0695 0.1340 0.0063  0.0156  0.0210  231 ASN A CG  
1884 O  OD1 . ASN A 231 ? 0.1947 0.0791 0.1315 -0.0039 0.0357  0.0166  231 ASN A OD1 
1885 N  ND2 . ASN A 231 ? 0.1875 0.1090 0.1199 0.0311  0.0229  0.0152  231 ASN A ND2 
1886 N  N   . GLY A 232 ? 0.1939 0.1014 0.0832 -0.0031 0.0215  0.0144  232 GLY A N   
1887 C  CA  . GLY A 232 ? 0.1983 0.1027 0.0826 0.0010  0.0340  0.0318  232 GLY A CA  
1888 C  C   . GLY A 232 ? 0.1282 0.0954 0.1102 0.0057  0.0189  0.0166  232 GLY A C   
1889 O  O   . GLY A 232 ? 0.1473 0.1182 0.1447 0.0198  0.0398  0.0164  232 GLY A O   
1890 N  N   . GLU A 233 ? 0.1214 0.1389 0.0925 0.0119  0.0261  0.0231  233 GLU A N   
1891 C  CA  . GLU A 233 ? 0.1493 0.1031 0.1191 0.0121  0.0158  0.0087  233 GLU A CA  
1892 C  C   . GLU A 233 ? 0.1461 0.1124 0.1268 -0.0192 0.0250  -0.0087 233 GLU A C   
1893 O  O   . GLU A 233 ? 0.1340 0.1062 0.1307 -0.0055 0.0229  0.0066  233 GLU A O   
1894 C  CB  . GLU A 233 ? 0.1766 0.1285 0.1329 0.0114  0.0125  0.0398  233 GLU A CB  
1895 C  CG  . GLU A 233 ? 0.1702 0.2209 0.1289 0.0108  0.0055  0.0351  233 GLU A CG  
1896 C  CD  . GLU A 233 ? 0.2740 0.2029 0.2223 0.0396  -0.0140 0.0447  233 GLU A CD  
1897 O  OE1 . GLU A 233 ? 0.3064 0.1868 0.2809 0.0403  0.0575  0.0535  233 GLU A OE1 
1898 O  OE2 . GLU A 233 ? 0.3129 0.3545 0.2423 0.0669  -0.0453 -0.0109 233 GLU A OE2 
1899 N  N   . GLY A 234 ? 0.1598 0.1317 0.1225 0.0242  0.0400  0.0011  234 GLY A N   
1900 C  CA  . GLY A 234 ? 0.1397 0.1304 0.1196 0.0283  0.0226  0.0141  234 GLY A CA  
1901 C  C   . GLY A 234 ? 0.1609 0.0844 0.1150 0.0311  0.0275  0.0047  234 GLY A C   
1902 O  O   . GLY A 234 ? 0.1656 0.1322 0.1526 -0.0027 0.0211  0.0074  234 GLY A O   
1903 N  N   . GLU A 235 ? 0.1591 0.1098 0.1242 0.0164  0.0225  0.0240  235 GLU A N   
1904 C  CA  . GLU A 235 ? 0.1315 0.1282 0.1555 0.0068  0.0083  0.0248  235 GLU A CA  
1905 C  C   . GLU A 235 ? 0.1656 0.1437 0.1465 0.0181  0.0535  0.0407  235 GLU A C   
1906 O  O   . GLU A 235 ? 0.1767 0.1221 0.1480 0.0176  0.0250  0.0075  235 GLU A O   
1907 C  CB  . GLU A 235 ? 0.2247 0.1058 0.1558 -0.0031 0.0102  0.0307  235 GLU A CB  
1908 C  CG  . GLU A 235 ? 0.2486 0.1133 0.1577 -0.0114 0.0553  0.0473  235 GLU A CG  
1909 C  CD  . GLU A 235 ? 0.3248 0.2337 0.1982 -0.0883 0.0704  -0.0294 235 GLU A CD  
1910 O  OE1 . GLU A 235 ? 0.5389 0.2834 0.3348 -0.1679 0.1720  -0.0575 235 GLU A OE1 
1911 O  OE2 . GLU A 235 ? 0.1968 0.2198 0.2180 -0.0463 0.0482  -0.0269 235 GLU A OE2 
1912 N  N   . PRO A 236 ? 0.1498 0.1085 0.1548 -0.0017 0.0337  0.0350  236 PRO A N   
1913 C  CA  . PRO A 236 ? 0.1425 0.1293 0.1559 -0.0066 0.0561  0.0723  236 PRO A CA  
1914 C  C   . PRO A 236 ? 0.1203 0.1458 0.1020 0.0059  0.0252  0.0042  236 PRO A C   
1915 O  O   . PRO A 236 ? 0.1537 0.1173 0.1274 0.0168  0.0413  0.0086  236 PRO A O   
1916 C  CB  . PRO A 236 ? 0.1289 0.2367 0.2094 0.0273  0.0591  0.0613  236 PRO A CB  
1917 C  CG  . PRO A 236 ? 0.1670 0.1831 0.2633 0.0324  0.0719  0.0897  236 PRO A CG  
1918 C  CD  . PRO A 236 ? 0.1562 0.1609 0.2399 0.0092  0.0578  0.0500  236 PRO A CD  
1919 N  N   A GLU A 237 ? 0.1311 0.1216 0.1483 0.0060  0.0357  0.0168  237 GLU A N   
1920 N  N   B GLU A 237 ? 0.1365 0.1199 0.1570 0.0073  0.0412  0.0034  237 GLU A N   
1921 C  CA  A GLU A 237 ? 0.1440 0.0929 0.1074 -0.0001 0.0357  -0.0013 237 GLU A CA  
1922 C  CA  B GLU A 237 ? 0.1476 0.0871 0.1072 -0.0172 0.0337  -0.0221 237 GLU A CA  
1923 C  C   A GLU A 237 ? 0.1631 0.0706 0.1218 -0.0077 0.0525  0.0284  237 GLU A C   
1924 C  C   B GLU A 237 ? 0.1723 0.0850 0.1229 -0.0115 0.0522  0.0184  237 GLU A C   
1925 O  O   A GLU A 237 ? 0.1807 0.0943 0.1667 0.0192  0.0238  0.0170  237 GLU A O   
1926 O  O   B GLU A 237 ? 0.1875 0.1150 0.1584 0.0151  0.0432  0.0174  237 GLU A O   
1927 C  CB  A GLU A 237 ? 0.1832 0.1209 0.1879 -0.0336 0.0148  -0.0096 237 GLU A CB  
1928 C  CB  B GLU A 237 ? 0.2566 0.0945 0.1713 -0.0556 0.0271  -0.0563 237 GLU A CB  
1929 C  CG  A GLU A 237 ? 0.1814 0.1469 0.2126 0.0084  0.0176  0.0166  237 GLU A CG  
1930 C  CG  B GLU A 237 ? 0.2277 0.1613 0.2831 -0.0472 0.0115  -0.0335 237 GLU A CG  
1931 C  CD  A GLU A 237 ? 0.2051 0.2132 0.2593 -0.0281 0.0294  -0.0276 237 GLU A CD  
1932 C  CD  B GLU A 237 ? 0.3080 0.1749 0.2227 -0.0474 -0.0020 -0.0693 237 GLU A CD  
1933 O  OE1 A GLU A 237 ? 0.2409 0.2324 0.3051 -0.0097 0.1297  -0.0778 237 GLU A OE1 
1934 O  OE1 B GLU A 237 ? 0.4046 0.2090 0.2256 -0.0439 0.0019  -0.0974 237 GLU A OE1 
1935 O  OE2 A GLU A 237 ? 0.2712 0.0537 0.1515 -0.0272 0.0392  -0.0001 237 GLU A OE2 
1936 O  OE2 B GLU A 237 ? 0.4217 0.4088 0.2920 -0.1035 0.1108  -0.1219 237 GLU A OE2 
1937 N  N   . GLU A 238 ? 0.1468 0.1101 0.1067 -0.0263 0.0452  0.0091  238 GLU A N   
1938 C  CA  . GLU A 238 ? 0.1314 0.1663 0.1163 -0.0206 0.0416  0.0299  238 GLU A CA  
1939 C  C   . GLU A 238 ? 0.1207 0.0850 0.1368 0.0076  0.0355  0.0165  238 GLU A C   
1940 O  O   . GLU A 238 ? 0.1609 0.0827 0.1577 0.0071  0.0160  0.0117  238 GLU A O   
1941 C  CB  . GLU A 238 ? 0.1562 0.2223 0.1792 -0.0548 -0.0179 0.0506  238 GLU A CB  
1942 C  CG  . GLU A 238 ? 0.1659 0.3069 0.2076 -0.0271 0.0370  0.0053  238 GLU A CG  
1943 C  CD  . GLU A 238 ? 0.4685 0.3802 0.2967 -0.1368 -0.0614 -0.0152 238 GLU A CD  
1944 O  OE1 . GLU A 238 ? 0.5090 0.3929 0.4990 -0.0946 0.0452  0.0044  238 GLU A OE1 
1945 O  OE2 . GLU A 238 ? 0.5431 0.5934 0.3191 -0.1590 -0.0642 0.0269  238 GLU A OE2 
1946 N  N   . LEU A 239 ? 0.1272 0.1153 0.1112 -0.0283 0.0380  -0.0023 239 LEU A N   
1947 C  CA  . LEU A 239 ? 0.1221 0.0800 0.1128 -0.0292 0.0214  -0.0121 239 LEU A CA  
1948 C  C   . LEU A 239 ? 0.1239 0.0740 0.1033 0.0060  0.0201  0.0002  239 LEU A C   
1949 O  O   . LEU A 239 ? 0.1271 0.1014 0.1058 0.0018  0.0223  0.0119  239 LEU A O   
1950 C  CB  . LEU A 239 ? 0.1390 0.0618 0.1371 -0.0058 0.0119  -0.0049 239 LEU A CB  
1951 C  CG  . LEU A 239 ? 0.1728 0.0872 0.1684 0.0019  0.0212  -0.0456 239 LEU A CG  
1952 C  CD1 . LEU A 239 ? 0.2183 0.0801 0.2691 -0.0160 -0.0159 -0.0514 239 LEU A CD1 
1953 C  CD2 . LEU A 239 ? 0.2467 0.1329 0.1347 0.0089  0.0016  -0.0321 239 LEU A CD2 
1954 N  N   . MET A 240 ? 0.1155 0.0785 0.0990 -0.0003 0.0352  0.0035  240 MET A N   
1955 C  CA  . MET A 240 ? 0.1619 0.0523 0.0951 0.0029  0.0285  0.0084  240 MET A CA  
1956 C  C   . MET A 240 ? 0.1049 0.0692 0.0920 -0.0110 0.0187  -0.0167 240 MET A C   
1957 O  O   . MET A 240 ? 0.1064 0.0935 0.0836 -0.0114 0.0100  -0.0117 240 MET A O   
1958 C  CB  . MET A 240 ? 0.1454 0.0841 0.0944 0.0217  0.0336  0.0038  240 MET A CB  
1959 C  CG  . MET A 240 ? 0.1376 0.0699 0.1118 0.0000  0.0409  -0.0107 240 MET A CG  
1960 S  SD  . MET A 240 ? 0.1590 0.0759 0.1227 -0.0010 0.0346  -0.0027 240 MET A SD  
1961 C  CE  . MET A 240 ? 0.2001 0.0706 0.1042 -0.0179 0.0583  0.0053  240 MET A CE  
1962 N  N   . VAL A 241 ? 0.1130 0.0563 0.0760 -0.0069 0.0234  0.0032  241 VAL A N   
1963 C  CA  . VAL A 241 ? 0.1347 0.0750 0.0765 -0.0190 0.0295  0.0055  241 VAL A CA  
1964 C  C   . VAL A 241 ? 0.1139 0.0873 0.0906 -0.0044 0.0228  0.0041  241 VAL A C   
1965 O  O   . VAL A 241 ? 0.1182 0.0753 0.0997 -0.0037 0.0217  0.0037  241 VAL A O   
1966 C  CB  . VAL A 241 ? 0.1181 0.0832 0.1115 -0.0025 0.0134  -0.0140 241 VAL A CB  
1967 C  CG1 . VAL A 241 ? 0.1422 0.1185 0.1439 -0.0106 -0.0236 -0.0043 241 VAL A CG1 
1968 C  CG2 . VAL A 241 ? 0.1304 0.0856 0.1321 0.0011  0.0414  0.0047  241 VAL A CG2 
1969 N  N   . ASP A 242 ? 0.1141 0.0654 0.0768 -0.0043 0.0199  -0.0084 242 ASP A N   
1970 C  CA  . ASP A 242 ? 0.0920 0.0618 0.1049 0.0000  0.0059  -0.0131 242 ASP A CA  
1971 C  C   . ASP A 242 ? 0.0841 0.0680 0.1030 -0.0170 0.0109  0.0038  242 ASP A C   
1972 O  O   . ASP A 242 ? 0.1005 0.0841 0.1340 -0.0155 -0.0059 -0.0133 242 ASP A O   
1973 C  CB  . ASP A 242 ? 0.0818 0.0607 0.1422 0.0000  0.0232  -0.0070 242 ASP A CB  
1974 C  CG  . ASP A 242 ? 0.1225 0.0610 0.0970 -0.0076 0.0257  -0.0079 242 ASP A CG  
1975 O  OD1 . ASP A 242 ? 0.1121 0.0601 0.1176 -0.0025 0.0143  0.0076  242 ASP A OD1 
1976 O  OD2 . ASP A 242 ? 0.1562 0.0559 0.1540 -0.0089 0.0354  -0.0286 242 ASP A OD2 
1977 N  N   . ASN A 243 ? 0.1062 0.0513 0.0916 -0.0091 0.0134  -0.0016 243 ASN A N   
1978 C  CA  . ASN A 243 ? 0.1347 0.0540 0.0699 -0.0150 0.0105  -0.0043 243 ASN A CA  
1979 C  C   . ASN A 243 ? 0.1066 0.0559 0.0767 0.0121  -0.0060 -0.0150 243 ASN A C   
1980 O  O   . ASN A 243 ? 0.0965 0.0730 0.0981 0.0199  0.0226  0.0055  243 ASN A O   
1981 C  CB  . ASN A 243 ? 0.0995 0.0857 0.0972 -0.0097 0.0042  0.0122  243 ASN A CB  
1982 C  CG  . ASN A 243 ? 0.0942 0.0751 0.0979 -0.0046 0.0238  -0.0088 243 ASN A CG  
1983 O  OD1 . ASN A 243 ? 0.1056 0.0643 0.1203 -0.0087 0.0052  0.0124  243 ASN A OD1 
1984 N  ND2 . ASN A 243 ? 0.1242 0.1150 0.1012 -0.0087 -0.0054 -0.0002 243 ASN A ND2 
1985 N  N   . TRP A 244 ? 0.0662 0.0617 0.0699 -0.0025 -0.0041 -0.0104 244 TRP A N   
1986 C  CA  . TRP A 244 ? 0.0688 0.0715 0.0767 -0.0030 0.0106  -0.0041 244 TRP A CA  
1987 C  C   . TRP A 244 ? 0.0593 0.0590 0.1082 -0.0088 0.0097  -0.0040 244 TRP A C   
1988 O  O   . TRP A 244 ? 0.0848 0.0769 0.1049 0.0186  -0.0025 -0.0196 244 TRP A O   
1989 C  CB  . TRP A 244 ? 0.0748 0.0538 0.0974 0.0020  0.0211  -0.0020 244 TRP A CB  
1990 C  CG  . TRP A 244 ? 0.0832 0.0555 0.0893 0.0035  0.0076  0.0036  244 TRP A CG  
1991 C  CD1 . TRP A 244 ? 0.1146 0.0523 0.0923 0.0010  0.0255  0.0013  244 TRP A CD1 
1992 C  CD2 . TRP A 244 ? 0.0884 0.0586 0.0902 -0.0018 0.0011  0.0002  244 TRP A CD2 
1993 N  NE1 . TRP A 244 ? 0.1124 0.0636 0.0947 0.0022  0.0107  0.0061  244 TRP A NE1 
1994 C  CE2 . TRP A 244 ? 0.1074 0.0644 0.1040 -0.0033 0.0034  -0.0047 244 TRP A CE2 
1995 C  CE3 . TRP A 244 ? 0.1003 0.0954 0.0933 -0.0013 -0.0162 0.0240  244 TRP A CE3 
1996 C  CZ2 . TRP A 244 ? 0.1260 0.0956 0.1178 0.0023  -0.0044 0.0192  244 TRP A CZ2 
1997 C  CZ3 . TRP A 244 ? 0.1200 0.0871 0.0895 0.0195  0.0024  0.0115  244 TRP A CZ3 
1998 C  CH2 . TRP A 244 ? 0.1279 0.0762 0.1181 0.0107  -0.0072 0.0103  244 TRP A CH2 
1999 N  N   . ARG A 245 ? 0.0929 0.0699 0.0767 -0.0187 -0.0030 -0.0018 245 ARG A N   
2000 C  CA  . ARG A 245 ? 0.0857 0.0656 0.0870 -0.0117 -0.0019 -0.0167 245 ARG A CA  
2001 C  C   . ARG A 245 ? 0.0695 0.0776 0.0856 -0.0107 -0.0146 -0.0133 245 ARG A C   
2002 O  O   . ARG A 245 ? 0.0879 0.0911 0.1101 -0.0038 0.0047  -0.0144 245 ARG A O   
2003 C  CB  . ARG A 245 ? 0.0810 0.0767 0.0936 -0.0081 -0.0023 -0.0374 245 ARG A CB  
2004 C  CG  . ARG A 245 ? 0.0662 0.0741 0.1155 0.0143  -0.0107 -0.0339 245 ARG A CG  
2005 C  CD  . ARG A 245 ? 0.0783 0.0802 0.1261 -0.0122 -0.0018 -0.0397 245 ARG A CD  
2006 N  NE  . ARG A 245 ? 0.0722 0.1049 0.1207 -0.0273 0.0093  -0.0278 245 ARG A NE  
2007 C  CZ  . ARG A 245 ? 0.0671 0.0943 0.1185 -0.0273 0.0074  -0.0197 245 ARG A CZ  
2008 N  NH1 . ARG A 245 ? 0.0832 0.1200 0.1199 -0.0119 0.0231  0.0064  245 ARG A NH1 
2009 N  NH2 . ARG A 245 ? 0.0607 0.1368 0.1419 -0.0131 -0.0015 -0.0253 245 ARG A NH2 
2010 N  N   . PRO A 246 ? 0.1089 0.0753 0.0916 0.0188  0.0029  -0.0095 246 PRO A N   
2011 C  CA  . PRO A 246 ? 0.1017 0.0713 0.0988 0.0168  0.0069  -0.0111 246 PRO A CA  
2012 C  C   . PRO A 246 ? 0.1214 0.0856 0.0818 0.0189  0.0160  0.0017  246 PRO A C   
2013 O  O   . PRO A 246 ? 0.1084 0.0857 0.1322 0.0124  -0.0221 -0.0021 246 PRO A O   
2014 C  CB  . PRO A 246 ? 0.1379 0.1401 0.1548 0.0659  0.0013  0.0079  246 PRO A CB  
2015 C  CG  . PRO A 246 ? 0.1616 0.1942 0.2082 0.0571  0.0225  0.1079  246 PRO A CG  
2016 C  CD  . PRO A 246 ? 0.1085 0.1354 0.1314 0.0750  0.0089  0.0196  246 PRO A CD  
2017 N  N   . ALA A 247 ? 0.1289 0.0742 0.0932 0.0092  0.0154  0.0063  247 ALA A N   
2018 C  CA  . ALA A 247 ? 0.1275 0.0680 0.1033 0.0129  -0.0044 -0.0200 247 ALA A CA  
2019 C  C   . ALA A 247 ? 0.1057 0.0926 0.0978 0.0190  0.0005  -0.0078 247 ALA A C   
2020 O  O   . ALA A 247 ? 0.1340 0.1150 0.1214 0.0419  -0.0177 -0.0087 247 ALA A O   
2021 C  CB  . ALA A 247 ? 0.1634 0.0866 0.1279 0.0206  0.0030  0.0055  247 ALA A CB  
2022 N  N   . GLN A 248 ? 0.0873 0.0794 0.1053 0.0141  -0.0024 -0.0020 248 GLN A N   
2023 C  CA  . GLN A 248 ? 0.1015 0.0979 0.1130 0.0152  -0.0242 -0.0023 248 GLN A CA  
2024 C  C   . GLN A 248 ? 0.1075 0.0944 0.1218 0.0122  -0.0168 -0.0122 248 GLN A C   
2025 O  O   . GLN A 248 ? 0.1203 0.1322 0.1094 0.0201  0.0004  0.0079  248 GLN A O   
2026 C  CB  . GLN A 248 ? 0.1699 0.0820 0.1042 0.0389  -0.0025 -0.0179 248 GLN A CB  
2027 C  CG  . GLN A 248 ? 0.1209 0.1304 0.1124 0.0041  0.0098  -0.0053 248 GLN A CG  
2028 C  CD  . GLN A 248 ? 0.1102 0.1529 0.1357 -0.0002 0.0020  -0.0256 248 GLN A CD  
2029 O  OE1 . GLN A 248 ? 0.1214 0.1997 0.1753 -0.0259 -0.0042 -0.0282 248 GLN A OE1 
2030 N  NE2 . GLN A 248 ? 0.1286 0.1212 0.1209 0.0149  0.0017  0.0019  248 GLN A NE2 
2031 N  N   . PRO A 249 ? 0.1168 0.1562 0.1214 0.0023  -0.0168 -0.0220 249 PRO A N   
2032 C  CA  . PRO A 249 ? 0.0934 0.2047 0.1218 0.0662  -0.0067 0.0182  249 PRO A CA  
2033 C  C   . PRO A 249 ? 0.1057 0.1462 0.1318 0.0406  -0.0041 0.0114  249 PRO A C   
2034 O  O   . PRO A 249 ? 0.1188 0.1501 0.1286 0.0469  -0.0009 0.0072  249 PRO A O   
2035 C  CB  . PRO A 249 ? 0.1022 0.2949 0.1771 0.1005  -0.0498 -0.0536 249 PRO A CB  
2036 C  CG  . PRO A 249 ? 0.1782 0.2555 0.1171 0.0335  -0.0318 -0.0385 249 PRO A CG  
2037 C  CD  . PRO A 249 ? 0.0959 0.2521 0.1551 0.0221  -0.0326 -0.0150 249 PRO A CD  
2038 N  N   . LEU A 250 ? 0.1293 0.1735 0.1047 0.0436  0.0060  0.0046  250 LEU A N   
2039 C  CA  . LEU A 250 ? 0.1353 0.1325 0.1067 0.0201  0.0179  -0.0048 250 LEU A CA  
2040 C  C   . LEU A 250 ? 0.1419 0.1203 0.1292 0.0164  -0.0172 0.0067  250 LEU A C   
2041 O  O   . LEU A 250 ? 0.1343 0.1250 0.1504 0.0292  -0.0209 0.0145  250 LEU A O   
2042 C  CB  . LEU A 250 ? 0.1450 0.1724 0.1451 0.0054  0.0210  0.0157  250 LEU A CB  
2043 C  CG  . LEU A 250 ? 0.1749 0.1782 0.1465 0.0166  0.0430  0.0210  250 LEU A CG  
2044 C  CD1 . LEU A 250 ? 0.1638 0.1430 0.1425 0.0006  0.0039  -0.0096 250 LEU A CD1 
2045 C  CD2 . LEU A 250 ? 0.2087 0.1993 0.1752 -0.0323 0.0262  0.0228  250 LEU A CD2 
2046 N  N   . LYS A 251 ? 0.1419 0.1843 0.1286 0.0289  -0.0316 -0.0279 251 LYS A N   
2047 C  CA  . LYS A 251 ? 0.1518 0.1587 0.1243 0.0423  -0.0288 -0.0315 251 LYS A CA  
2048 C  C   . LYS A 251 ? 0.1511 0.1518 0.2100 0.0664  -0.0048 -0.0196 251 LYS A C   
2049 O  O   . LYS A 251 ? 0.2112 0.2586 0.1958 -0.0168 0.0096  -0.0321 251 LYS A O   
2050 C  CB  . LYS A 251 ? 0.1353 0.1390 0.1958 0.0353  -0.0585 -0.0439 251 LYS A CB  
2051 C  CG  . LYS A 251 ? 0.1881 0.2241 0.2582 0.0174  0.0183  -0.0916 251 LYS A CG  
2052 C  CD  . LYS A 251 ? 0.2263 0.2575 0.2939 0.0468  0.0326  0.0030  251 LYS A CD  
2053 C  CE  . LYS A 251 ? 0.2112 0.2644 0.3373 0.0271  0.0372  -0.0258 251 LYS A CE  
2054 N  NZ  . LYS A 251 ? 0.3072 0.2252 0.3730 0.0265  0.0184  0.0254  251 LYS A NZ  
2055 N  N   . ASN A 252 ? 0.1548 0.1756 0.1346 0.0368  -0.0333 -0.0164 252 ASN A N   
2056 C  CA  . ASN A 252 ? 0.1728 0.2123 0.1982 0.0190  -0.0230 -0.0443 252 ASN A CA  
2057 C  C   . ASN A 252 ? 0.2076 0.1641 0.2301 0.0205  -0.0438 0.0016  252 ASN A C   
2058 O  O   . ASN A 252 ? 0.2874 0.2152 0.2637 0.0425  -0.0290 -0.0324 252 ASN A O   
2059 C  CB  . ASN A 252 ? 0.2137 0.2399 0.2257 0.0335  -0.0516 -0.0763 252 ASN A CB  
2060 C  CG  . ASN A 252 ? 0.2331 0.3211 0.2877 0.0337  0.0292  -0.0825 252 ASN A CG  
2061 O  OD1 . ASN A 252 ? 0.2788 0.4613 0.3538 -0.0081 0.0269  -0.0832 252 ASN A OD1 
2062 N  ND2 . ASN A 252 ? 0.5224 0.4595 0.3923 -0.0422 -0.0857 -0.1099 252 ASN A ND2 
2063 N  N   . ARG A 253 ? 0.1293 0.2036 0.1178 0.0144  0.0011  -0.0061 253 ARG A N   
2064 C  CA  . ARG A 253 ? 0.1415 0.1695 0.1322 0.0324  -0.0121 -0.0161 253 ARG A CA  
2065 C  C   . ARG A 253 ? 0.1935 0.1728 0.1084 0.0077  0.0084  -0.0165 253 ARG A C   
2066 O  O   . ARG A 253 ? 0.1922 0.1904 0.2266 0.0110  0.0725  0.0473  253 ARG A O   
2067 C  CB  . ARG A 253 ? 0.1505 0.1088 0.1231 0.0008  -0.0292 -0.0006 253 ARG A CB  
2068 C  CG  . ARG A 253 ? 0.1706 0.0958 0.1063 0.0110  0.0005  -0.0136 253 ARG A CG  
2069 C  CD  . ARG A 253 ? 0.1580 0.1056 0.1108 0.0245  0.0080  -0.0367 253 ARG A CD  
2070 N  NE  . ARG A 253 ? 0.1329 0.1036 0.0990 0.0374  -0.0042 -0.0092 253 ARG A NE  
2071 C  CZ  . ARG A 253 ? 0.0900 0.0787 0.0866 0.0267  -0.0034 0.0032  253 ARG A CZ  
2072 N  NH1 . ARG A 253 ? 0.0812 0.0830 0.1088 0.0059  -0.0267 0.0131  253 ARG A NH1 
2073 N  NH2 . ARG A 253 ? 0.0934 0.0769 0.1040 0.0130  -0.0013 -0.0286 253 ARG A NH2 
2074 N  N   A GLN A 254 ? 0.1624 0.1860 0.1803 -0.0248 -0.0122 -0.0566 254 GLN A N   
2075 N  N   B GLN A 254 ? 0.1461 0.1907 0.1254 -0.0184 -0.0179 -0.0675 254 GLN A N   
2076 C  CA  A GLN A 254 ? 0.1652 0.2356 0.1667 -0.0380 -0.0311 -0.0406 254 GLN A CA  
2077 C  CA  B GLN A 254 ? 0.1383 0.2392 0.1234 -0.0208 -0.0306 -0.0267 254 GLN A CA  
2078 C  C   A GLN A 254 ? 0.2406 0.1749 0.1243 -0.0030 -0.0281 -0.0080 254 GLN A C   
2079 C  C   B GLN A 254 ? 0.2108 0.1796 0.1112 -0.0016 -0.0480 -0.0002 254 GLN A C   
2080 O  O   A GLN A 254 ? 0.2458 0.1907 0.2528 0.0071  -0.1129 0.0119  254 GLN A O   
2081 O  O   B GLN A 254 ? 0.2234 0.1595 0.2320 -0.0272 -0.0741 0.0184  254 GLN A O   
2082 C  CB  A GLN A 254 ? 0.3492 0.3258 0.1914 -0.0310 0.0104  -0.1314 254 GLN A CB  
2083 C  CB  B GLN A 254 ? 0.1756 0.2889 0.1003 -0.0409 -0.0201 -0.0380 254 GLN A CB  
2084 C  CG  A GLN A 254 ? 0.4241 0.3334 0.3348 -0.0778 0.1374  -0.0473 254 GLN A CG  
2085 C  CG  B GLN A 254 ? 0.1379 0.3803 0.1383 -0.0334 -0.0485 -0.0104 254 GLN A CG  
2086 C  CD  A GLN A 254 ? 0.4737 0.2065 0.2934 -0.0230 0.1456  0.0428  254 GLN A CD  
2087 C  CD  B GLN A 254 ? 0.1940 0.4677 0.1562 0.0722  0.0423  -0.0075 254 GLN A CD  
2088 O  OE1 A GLN A 254 ? 0.3183 0.1929 0.1487 -0.0325 0.0145  -0.0165 254 GLN A OE1 
2089 O  OE1 B GLN A 254 ? 0.3571 0.5339 0.3894 -0.1606 -0.0990 -0.1333 254 GLN A OE1 
2090 N  NE2 A GLN A 254 ? 0.4214 0.2992 0.1429 -0.0538 0.0425  0.0363  254 GLN A NE2 
2091 N  NE2 B GLN A 254 ? 0.2852 0.2697 0.2270 -0.0785 -0.0647 0.0417  254 GLN A NE2 
2092 N  N   . ILE A 255 ? 0.1153 0.1570 0.1300 0.0084  -0.0145 0.0001  255 ILE A N   
2093 C  CA  . ILE A 255 ? 0.1117 0.1687 0.1234 0.0273  -0.0073 -0.0076 255 ILE A CA  
2094 C  C   . ILE A 255 ? 0.1199 0.1404 0.1562 -0.0013 0.0094  0.0358  255 ILE A C   
2095 O  O   . ILE A 255 ? 0.1494 0.1365 0.1552 0.0051  0.0203  0.0288  255 ILE A O   
2096 C  CB  . ILE A 255 ? 0.1207 0.1375 0.1333 0.0417  -0.0193 0.0173  255 ILE A CB  
2097 C  CG1 . ILE A 255 ? 0.1451 0.1577 0.1602 0.0285  0.0215  0.0173  255 ILE A CG1 
2098 C  CG2 . ILE A 255 ? 0.1386 0.1850 0.1480 0.0220  -0.0259 -0.0116 255 ILE A CG2 
2099 C  CD1 . ILE A 255 ? 0.2055 0.2029 0.1782 0.0079  0.0138  -0.0376 255 ILE A CD1 
2100 N  N   . LYS A 256 ? 0.0997 0.1645 0.0995 -0.0017 -0.0074 0.0059  256 LYS A N   
2101 C  CA  . LYS A 256 ? 0.1142 0.1429 0.1021 0.0060  0.0051  -0.0144 256 LYS A CA  
2102 C  C   . LYS A 256 ? 0.1049 0.1415 0.0838 -0.0062 0.0016  0.0120  256 LYS A C   
2103 O  O   . LYS A 256 ? 0.1347 0.1990 0.0870 -0.0232 0.0038  0.0118  256 LYS A O   
2104 C  CB  . LYS A 256 ? 0.1573 0.1412 0.1742 0.0113  -0.0130 -0.0153 256 LYS A CB  
2105 C  CG  . LYS A 256 ? 0.2148 0.1717 0.2398 -0.0161 -0.0192 -0.0774 256 LYS A CG  
2106 N  N   . ALA A 257 ? 0.1354 0.1448 0.1017 -0.0190 0.0190  0.0102  257 ALA A N   
2107 C  CA  . ALA A 257 ? 0.1304 0.1171 0.1282 -0.0015 -0.0021 0.0003  257 ALA A CA  
2108 C  C   . ALA A 257 ? 0.1058 0.1619 0.0785 -0.0089 0.0100  -0.0055 257 ALA A C   
2109 O  O   . ALA A 257 ? 0.1368 0.1971 0.0926 -0.0060 0.0222  -0.0243 257 ALA A O   
2110 C  CB  . ALA A 257 ? 0.1615 0.1372 0.1408 -0.0399 0.0061  0.0362  257 ALA A CB  
2111 N  N   . SER A 258 ? 0.1209 0.1300 0.0905 -0.0077 0.0005  -0.0065 258 SER A N   
2112 C  CA  . SER A 258 ? 0.1112 0.1705 0.1419 0.0041  -0.0042 -0.0004 258 SER A CA  
2113 C  C   . SER A 258 ? 0.1206 0.1857 0.1176 0.0089  0.0274  -0.0005 258 SER A C   
2114 O  O   . SER A 258 ? 0.1397 0.3208 0.1914 0.0504  0.0573  0.0073  258 SER A O   
2115 C  CB  . SER A 258 ? 0.1641 0.1168 0.1620 -0.0143 -0.0179 0.0259  258 SER A CB  
2116 O  OG  . SER A 258 ? 0.1164 0.1595 0.1185 -0.0059 0.0088  -0.0055 258 SER A OG  
2117 N  N   . PHE A 259 ? 0.1296 0.1993 0.1437 -0.0292 0.0077  0.0146  259 PHE A N   
2118 C  CA  . PHE A 259 ? 0.1591 0.2148 0.2040 -0.0542 0.0239  0.0283  259 PHE A CA  
2119 C  C   . PHE A 259 ? 0.2572 0.2451 0.2302 -0.0534 0.0370  0.0666  259 PHE A C   
2120 O  O   . PHE A 259 ? 0.3324 0.2832 0.1735 -0.0762 -0.0103 0.0845  259 PHE A O   
2121 C  CB  . PHE A 259 ? 0.1494 0.2076 0.1914 -0.0245 0.0148  0.0230  259 PHE A CB  
2122 C  CG  . PHE A 259 ? 0.1498 0.1626 0.2008 -0.0161 -0.0333 0.0579  259 PHE A CG  
2123 C  CD1 . PHE A 259 ? 0.1631 0.1415 0.1432 -0.0196 -0.0177 -0.0137 259 PHE A CD1 
2124 C  CD2 . PHE A 259 ? 0.2231 0.1656 0.2785 -0.0143 0.0152  0.0762  259 PHE A CD2 
2125 C  CE1 . PHE A 259 ? 0.1832 0.1504 0.2216 -0.0140 -0.0381 -0.0368 259 PHE A CE1 
2126 C  CE2 . PHE A 259 ? 0.2108 0.2069 0.3510 -0.0044 -0.0256 0.0376  259 PHE A CE2 
2127 C  CZ  . PHE A 259 ? 0.2806 0.1336 0.4059 -0.0413 0.0087  -0.0088 259 PHE A CZ  
2128 N  N   . LYS A 260 ? 0.4041 0.3410 0.2356 -0.1885 0.0544  0.0222  260 LYS A N   
2129 C  CA  . LYS A 260 ? 0.5166 0.5540 0.3765 -0.0214 0.0900  0.2273  260 LYS A CA  
2130 C  C   . LYS A 260 ? 0.6431 0.7235 0.4717 -0.0824 0.1085  0.0900  260 LYS A C   
2131 O  O   . LYS A 260 ? 0.3219 1.0108 1.1276 -0.0060 -0.1703 0.1493  260 LYS A O   
2132 C  CB  . LYS A 260 ? 0.4412 0.6957 0.4907 -0.0681 0.2675  0.1495  260 LYS A CB  
2133 C  CG  . LYS A 260 ? 0.8895 0.7601 0.4298 -0.4913 0.1057  0.3855  260 LYS A CG  
2134 O  OXT . LYS A 260 ? 0.6150 0.8564 0.7029 0.1052  -0.1328 0.0980  260 LYS A OXT 
2135 ZN ZN  . ZN  B .   ? 0.0828 0.0496 0.0958 -0.0013 -0.0069 -0.0067 301 ZN  A ZN  
2136 S  S   . DMS C .   ? 0.2177 0.2108 0.2216 -0.0113 0.0047  -0.0272 302 DMS A S   
2137 O  O   . DMS C .   ? 0.3111 0.2288 0.3306 0.0092  0.0674  -0.0714 302 DMS A O   
2138 C  C1  . DMS C .   ? 0.1534 0.2147 0.2093 0.0151  -0.0220 -0.0348 302 DMS A C1  
2139 C  C2  . DMS C .   ? 0.1821 0.1893 0.4169 -0.0326 0.0128  -0.0300 302 DMS A C2  
2140 S  S   . DMS D .   ? 0.1882 0.1340 0.2244 0.0260  0.0104  -0.0439 303 DMS A S   
2141 O  O   . DMS D .   ? 0.1993 0.1089 0.1932 0.0179  0.0013  -0.0566 303 DMS A O   
2142 C  C1  . DMS D .   ? 0.2143 0.2274 0.1935 0.0242  0.0502  -0.0633 303 DMS A C1  
2143 C  C2  . DMS D .   ? 0.2160 0.1523 0.2688 -0.0115 -0.0627 -0.0414 303 DMS A C2  
2144 F  F20 . V14 E .   ? 0.2755 0.0632 0.2544 0.0177  0.0348  0.0058  304 V14 A F20 
2145 C  C5  . V14 E .   ? 0.2363 0.0705 0.1724 -0.0263 0.0201  0.0054  304 V14 A C5  
2146 C  C4  . V14 E .   ? 0.1256 0.0699 0.1181 -0.0239 -0.0208 -0.0221 304 V14 A C4  
2147 S  S7  . V14 E .   ? 0.0996 0.0553 0.1094 -0.0013 -0.0243 -0.0146 304 V14 A S7  
2148 O  O9  . V14 E .   ? 0.0999 0.0653 0.1062 0.0168  -0.0083 -0.0163 304 V14 A O9  
2149 N  N10 . V14 E .   ? 0.1278 0.0436 0.1005 -0.0051 -0.0214 -0.0151 304 V14 A N10 
2150 O  O8  . V14 E .   ? 0.1047 0.0547 0.1189 0.0058  -0.0373 -0.0176 304 V14 A O8  
2151 C  C3  . V14 E .   ? 0.1321 0.0880 0.1011 -0.0046 -0.0155 -0.0114 304 V14 A C3  
2152 F  F12 . V14 E .   ? 0.1243 0.1058 0.2169 0.0079  0.0336  -0.0189 304 V14 A F12 
2153 C  C2  . V14 E .   ? 0.1800 0.1491 0.1209 0.0217  0.0034  0.0095  304 V14 A C2  
2154 F  F13 . V14 E .   ? 0.1904 0.1458 0.1742 -0.0018 0.0312  -0.0077 304 V14 A F13 
2155 C  C6  . V14 E .   ? 0.1892 0.1343 0.1870 -0.0218 0.0337  0.0217  304 V14 A C6  
2156 C  C1  . V14 E .   ? 0.2413 0.1230 0.1555 -0.0065 0.0292  0.0292  304 V14 A C1  
2157 S  S11 . V14 E .   ? 0.3130 0.1451 0.1717 0.0055  0.0441  0.0307  304 V14 A S11 
2158 O  O16 . V14 E .   ? 0.4045 0.1634 0.2529 0.0651  0.0719  0.0669  304 V14 A O16 
2159 O  O17 . V14 E .   ? 0.2906 0.1874 0.1741 -0.0119 0.0067  0.0122  304 V14 A O17 
2160 C  C15 . V14 E .   ? 0.2727 0.1875 0.2737 -0.0901 0.0316  0.0200  304 V14 A C15 
2161 C  C18 . V14 E .   ? 0.3851 0.1710 0.2861 -0.0524 -0.1018 0.0976  304 V14 A C18 
2162 O  O21 . V14 E .   ? 0.3659 0.2749 0.3093 -0.0068 0.0323  0.0212  304 V14 A O21 
2163 N  N19 . V14 E .   ? 0.2205 0.1274 0.2381 0.0030  -0.0114 -0.0386 304 V14 A N19 
2164 C  C14 . V14 E .   ? 0.3043 0.0581 0.1832 -0.0249 -0.0141 0.0050  304 V14 A C14 
2165 C  C28 . V14 E .   ? 0.2688 0.2439 0.2457 -0.0589 0.0239  0.0427  304 V14 A C28 
2166 C  C27 . V14 E .   ? 0.3250 0.1534 0.2464 -0.0851 0.0039  0.0160  304 V14 A C27 
2167 C  C26 . V14 E .   ? 0.3151 0.1480 0.3549 -0.0469 0.0548  -0.0140 304 V14 A C26 
2168 C  C25 . V14 E .   ? 0.3438 0.1637 0.3624 -0.0204 0.1364  0.0516  304 V14 A C25 
2169 C  C24 . V14 E .   ? 0.3218 0.1972 0.2259 -0.0871 0.0850  -0.0305 304 V14 A C24 
2170 C  C23 . V14 E .   ? 0.2209 0.2108 0.3301 0.0204  0.0488  -0.0486 304 V14 A C23 
2171 C  C22 . V14 E .   ? 0.3154 0.1340 0.1961 0.0100  -0.0120 0.0436  304 V14 A C22 
2172 O  O   . HOH F .   ? 0.2018 0.0559 0.1573 -0.0201 -0.0143 -0.0006 401 HOH A O   
2173 O  O   . HOH F .   ? 0.5648 0.4866 0.2972 -0.1936 0.0976  -0.0937 402 HOH A O   
2174 O  O   . HOH F .   ? 0.4887 0.3299 0.2673 0.0334  -0.0647 0.0280  403 HOH A O   
2175 O  O   . HOH F .   ? 0.4236 0.3850 0.5236 0.0343  0.0357  -0.1107 404 HOH A O   
2176 O  O   . HOH F .   ? 0.4041 0.4643 0.3136 -0.0174 0.0216  0.0454  405 HOH A O   
2177 O  O   . HOH F .   ? 0.4142 0.5211 0.5964 -0.1058 -0.1702 0.3550  406 HOH A O   
2178 O  O   . HOH F .   ? 0.3570 0.2065 0.4214 0.0319  0.0147  0.0500  407 HOH A O   
2179 O  O   . HOH F .   ? 0.6599 0.3600 0.5001 0.0577  -0.2138 -0.0466 408 HOH A O   
2180 O  O   . HOH F .   ? 0.3032 0.4288 0.9095 -0.1687 -0.0657 -0.2173 409 HOH A O   
2181 O  O   . HOH F .   ? 0.3829 0.2123 0.4305 0.0084  0.0041  0.0264  410 HOH A O   
2182 O  O   . HOH F .   ? 0.5273 0.2576 0.2469 -0.1498 0.0195  -0.0558 411 HOH A O   
2183 O  O   . HOH F .   ? 0.2550 0.2288 0.3946 0.0041  0.0370  -0.0367 412 HOH A O   
2184 O  O   . HOH F .   ? 0.3997 0.2320 0.3176 -0.0849 0.0376  -0.0752 413 HOH A O   
2185 O  O   . HOH F .   ? 0.4891 0.1336 0.5620 -0.1311 0.0352  0.0726  414 HOH A O   
2186 O  O   . HOH F .   ? 0.5280 0.2526 0.3935 -0.0758 0.0095  0.0584  415 HOH A O   
2187 O  O   . HOH F .   ? 0.4461 0.3053 0.4196 -0.0871 0.0837  -0.0491 416 HOH A O   
2188 O  O   . HOH F .   ? 0.2964 0.2410 0.4965 -0.0190 -0.1339 0.1097  417 HOH A O   
2189 O  O   . HOH F .   ? 0.1875 0.4583 0.3583 0.0067  0.0125  -0.1588 418 HOH A O   
2190 O  O   . HOH F .   ? 0.4677 0.3140 0.1541 -0.1118 -0.0037 -0.0723 419 HOH A O   
2191 O  O   . HOH F .   ? 0.4516 0.7213 0.4539 -0.1136 0.1506  0.0599  420 HOH A O   
2192 O  O   . HOH F .   ? 0.3495 0.3173 0.1587 0.0130  0.0212  0.0210  421 HOH A O   
2193 O  O   . HOH F .   ? 0.5180 0.3334 0.2690 0.0620  -0.0267 -0.0249 422 HOH A O   
2194 O  O   . HOH F .   ? 0.3019 0.3140 0.3166 -0.0869 0.1448  -0.1553 423 HOH A O   
2195 O  O   . HOH F .   ? 0.3696 0.3345 0.3514 0.0043  0.0266  0.1562  424 HOH A O   
2196 O  O   . HOH F .   ? 0.3538 0.1907 0.4209 -0.0256 -0.0509 0.0886  425 HOH A O   
2197 O  O   . HOH F .   ? 0.2257 0.2076 0.2723 0.0194  0.0339  0.0469  426 HOH A O   
2198 O  O   . HOH F .   ? 0.2863 0.2723 0.3277 -0.0250 -0.0387 0.1252  427 HOH A O   
2199 O  O   . HOH F .   ? 0.2922 0.2379 0.1896 -0.0065 -0.0398 0.0226  428 HOH A O   
2200 O  O   . HOH F .   ? 0.3527 0.3362 0.3161 0.0479  0.1133  -0.0447 429 HOH A O   
2201 O  O   . HOH F .   ? 0.3510 0.6876 0.3766 -0.1333 0.0025  0.0644  430 HOH A O   
2202 O  O   . HOH F .   ? 0.4051 0.2971 0.2763 -0.0749 -0.0439 0.1262  431 HOH A O   
2203 O  O   . HOH F .   ? 0.1832 0.0875 0.1710 -0.0552 0.0416  -0.0142 432 HOH A O   
2204 O  O   . HOH F .   ? 0.2922 0.1846 0.3146 -0.0122 -0.1305 -0.0419 433 HOH A O   
2205 O  O   . HOH F .   ? 0.2655 0.2745 0.3450 0.0397  0.0114  0.0644  434 HOH A O   
2206 O  O   . HOH F .   ? 0.1800 0.2137 0.2579 0.0252  -0.1180 -0.0771 435 HOH A O   
2207 O  O   . HOH F .   ? 0.4700 0.2209 0.4717 0.0197  0.2166  0.0556  436 HOH A O   
2208 O  O   . HOH F .   ? 0.2658 0.2100 0.3631 0.0776  -0.1161 -0.0754 437 HOH A O   
2209 O  O   . HOH F .   ? 0.3434 0.2891 0.3037 -0.0822 -0.0913 -0.0267 438 HOH A O   
2210 O  O   . HOH F .   ? 0.2770 0.3511 0.3172 -0.0485 0.0063  -0.0575 439 HOH A O   
2211 O  O   . HOH F .   ? 0.1401 0.1067 0.1444 -0.0104 0.0417  -0.0170 440 HOH A O   
2212 O  O   . HOH F .   ? 0.4942 0.3657 0.2306 -0.0092 0.0022  0.0472  441 HOH A O   
2213 O  O   . HOH F .   ? 0.2238 0.9408 0.3376 0.0257  -0.1119 0.2458  442 HOH A O   
2214 O  O   . HOH F .   ? 0.2870 0.3456 0.3846 0.0625  0.0128  0.0797  443 HOH A O   
2215 O  O   . HOH F .   ? 0.1979 0.3359 0.3295 0.0430  0.1152  -0.0109 444 HOH A O   
2216 O  O   . HOH F .   ? 0.2213 0.2033 0.4648 -0.0627 0.0666  -0.0484 445 HOH A O   
2217 O  O   . HOH F .   ? 0.2623 0.1738 0.2019 -0.0374 -0.0161 -0.0418 446 HOH A O   
2218 O  O   . HOH F .   ? 0.2842 0.6458 0.4947 -0.1003 0.1009  -0.1107 447 HOH A O   
2219 O  O   . HOH F .   ? 0.3789 0.1864 0.1904 -0.0199 0.0170  0.0501  448 HOH A O   
2220 O  O   . HOH F .   ? 0.4248 0.3204 0.4137 0.0726  -0.1277 -0.0972 449 HOH A O   
2221 O  O   . HOH F .   ? 0.5197 0.2062 0.3768 -0.0493 0.1653  -0.0702 450 HOH A O   
2222 O  O   . HOH F .   ? 0.1541 0.2935 0.2649 -0.0270 -0.0186 0.0033  451 HOH A O   
2223 O  O   . HOH F .   ? 0.1814 0.1850 0.1814 -0.0085 0.0107  0.0394  452 HOH A O   
2224 O  O   . HOH F .   ? 0.1918 0.4060 0.4868 0.0249  -0.0192 0.0323  453 HOH A O   
2225 O  O   . HOH F .   ? 0.3546 0.1814 0.2179 -0.0577 -0.0179 -0.0363 454 HOH A O   
2226 O  O   . HOH F .   ? 0.1989 0.1480 0.1511 0.0307  0.0745  0.0368  455 HOH A O   
2227 O  O   . HOH F .   ? 0.2388 0.2995 0.4866 0.0776  -0.0903 0.0248  456 HOH A O   
2228 O  O   . HOH F .   ? 0.2975 0.3834 0.3444 -0.1409 0.0625  -0.1228 457 HOH A O   
2229 O  O   . HOH F .   ? 0.2597 0.1450 0.2467 -0.0093 0.0418  -0.0060 458 HOH A O   
2230 O  O   . HOH F .   ? 0.3586 0.5512 0.3291 0.0222  -0.0457 0.1860  459 HOH A O   
2231 O  O   . HOH F .   ? 0.2083 0.2500 0.3430 -0.0842 -0.0569 0.1618  460 HOH A O   
2232 O  O   . HOH F .   ? 0.2764 0.4463 0.3086 -0.1603 0.0000  0.1035  461 HOH A O   
2233 O  O   . HOH F .   ? 0.3169 0.3254 0.2741 -0.0313 -0.0389 0.1247  462 HOH A O   
2234 O  O   . HOH F .   ? 0.1771 0.2238 0.2727 0.0078  -0.0315 -0.0354 463 HOH A O   
2235 O  O   . HOH F .   ? 0.2348 0.1577 0.1820 -0.0190 0.0008  -0.0250 464 HOH A O   
2236 O  O   . HOH F .   ? 0.2749 0.6467 0.5827 -0.1641 0.1423  0.0126  465 HOH A O   
2237 O  O   . HOH F .   ? 0.2500 0.3033 0.3168 -0.0091 -0.0230 0.0129  466 HOH A O   
2238 O  O   . HOH F .   ? 0.5317 0.2470 0.5595 -0.0071 -0.1711 -0.0653 467 HOH A O   
2239 O  O   . HOH F .   ? 0.4078 0.3082 0.2794 -0.0751 -0.0876 -0.0089 468 HOH A O   
2240 O  O   . HOH F .   ? 0.2745 0.2600 0.3850 -0.0241 -0.0670 -0.0146 469 HOH A O   
2241 O  O   . HOH F .   ? 0.3319 0.3471 0.2680 -0.1381 -0.0549 0.0256  470 HOH A O   
2242 O  O   . HOH F .   ? 0.2064 0.1735 0.2888 -0.0131 0.0395  -0.0576 471 HOH A O   
2243 O  O   . HOH F .   ? 0.5560 0.2205 0.3222 0.0021  -0.0110 0.0420  472 HOH A O   
2244 O  O   . HOH F .   ? 0.2758 0.2504 0.3987 -0.0948 -0.0888 0.0607  473 HOH A O   
2245 O  O   . HOH F .   ? 0.1160 0.1458 0.1430 0.0127  -0.0390 0.0138  474 HOH A O   
2246 O  O   . HOH F .   ? 0.4358 0.4577 0.6517 0.0011  -0.0917 -0.1087 475 HOH A O   
2247 O  O   . HOH F .   ? 0.5631 0.2485 0.3312 0.1726  -0.0356 0.0586  476 HOH A O   
2248 O  O   . HOH F .   ? 0.1746 0.1404 0.2079 0.0089  -0.0738 0.0254  477 HOH A O   
2249 O  O   . HOH F .   ? 0.4947 0.3489 0.7413 -0.1054 -0.0695 -0.0414 478 HOH A O   
2250 O  O   . HOH F .   ? 0.2087 0.1752 0.1943 0.0303  0.0171  0.0295  479 HOH A O   
2251 O  O   . HOH F .   ? 0.2288 0.1716 0.3201 0.0159  -0.0473 0.0675  480 HOH A O   
2252 O  O   . HOH F .   ? 0.4957 0.3506 0.2740 0.1897  0.1232  0.1323  481 HOH A O   
2253 O  O   . HOH F .   ? 0.6431 0.3437 0.4126 0.0328  -0.0429 -0.1018 482 HOH A O   
2254 O  O   . HOH F .   ? 0.3608 0.4248 0.5923 0.0165  -0.2679 0.0924  483 HOH A O   
2255 O  O   . HOH F .   ? 0.1191 0.0832 0.1181 -0.0042 0.0086  -0.0243 484 HOH A O   
2256 O  O   . HOH F .   ? 0.0911 0.0856 0.1109 -0.0006 0.0162  -0.0003 485 HOH A O   
2257 O  O   . HOH F .   ? 0.1953 0.2112 0.1799 -0.0214 0.0650  -0.0476 486 HOH A O   
2258 O  O   . HOH F .   ? 0.4121 0.2209 0.2094 -0.0027 0.0860  -0.0552 487 HOH A O   
2259 O  O   . HOH F .   ? 0.5090 0.2288 0.2269 0.0633  -0.0044 0.0309  488 HOH A O   
2260 O  O   . HOH F .   ? 0.2547 0.2587 0.1979 0.0491  0.0447  0.0114  489 HOH A O   
2261 O  O   . HOH F .   ? 0.1735 0.2965 0.2997 0.0120  0.0015  -0.0553 490 HOH A O   
2262 O  O   . HOH F .   ? 0.2787 0.2532 0.3359 0.0040  0.0476  -0.0079 491 HOH A O   
2263 O  O   . HOH F .   ? 0.1857 0.1835 0.2485 -0.0335 0.0109  0.0352  492 HOH A O   
2264 O  O   . HOH F .   ? 0.1311 0.0810 0.1074 0.0179  -0.0125 -0.0222 493 HOH A O   
2265 O  O   . HOH F .   ? 0.1594 0.1566 0.3104 -0.0520 -0.0591 0.0070  494 HOH A O   
2266 O  O   . HOH F .   ? 0.4764 0.3010 0.4816 -0.0146 -0.2042 -0.0329 495 HOH A O   
2267 O  O   . HOH F .   ? 0.4715 0.3389 0.7949 -0.0801 -0.0783 -0.1377 496 HOH A O   
2268 O  O   . HOH F .   ? 0.2986 0.3854 0.4354 -0.0288 -0.0719 0.0221  497 HOH A O   
2269 O  O   . HOH F .   ? 0.2037 0.3204 0.2223 0.0538  -0.0570 -0.0110 498 HOH A O   
2270 O  O   . HOH F .   ? 0.1146 0.0979 0.1173 0.0161  -0.0010 0.0092  499 HOH A O   
2271 O  O   . HOH F .   ? 0.2428 0.3049 0.3175 0.0487  0.0222  0.1351  500 HOH A O   
2272 O  O   . HOH F .   ? 0.2274 0.2000 0.1835 -0.0290 -0.0102 -0.0352 501 HOH A O   
2273 O  O   . HOH F .   ? 0.1695 0.2287 0.3259 -0.0771 -0.0348 0.0633  502 HOH A O   
2274 O  O   . HOH F .   ? 0.3650 0.3808 0.1789 0.0386  -0.0983 0.0236  503 HOH A O   
2275 O  O   . HOH F .   ? 0.1559 0.5138 0.6646 -0.0622 -0.0672 0.0656  504 HOH A O   
2276 O  O   . HOH F .   ? 0.2910 0.3732 0.2273 -0.1069 -0.0166 -0.0264 505 HOH A O   
2277 O  O   . HOH F .   ? 0.5100 0.2416 0.6774 0.0622  0.2420  0.0706  506 HOH A O   
2278 O  O   . HOH F .   ? 0.1731 0.3234 0.2967 -0.0076 0.0634  0.0044  507 HOH A O   
2279 O  O   . HOH F .   ? 0.1753 0.1710 0.2464 -0.0188 0.0060  -0.0248 508 HOH A O   
2280 O  O   . HOH F .   ? 0.3486 0.2162 0.2180 -0.0747 0.0336  -0.0759 509 HOH A O   
2281 O  O   . HOH F .   ? 0.1186 0.1249 0.1735 0.0137  -0.0097 -0.0536 510 HOH A O   
2282 O  O   . HOH F .   ? 0.2399 0.1986 0.2477 -0.0329 -0.0381 0.0141  511 HOH A O   
2283 O  O   . HOH F .   ? 0.4281 0.4464 0.5290 0.1758  -0.1905 -0.0877 512 HOH A O   
2284 O  O   . HOH F .   ? 0.1588 0.1821 0.2160 0.0244  -0.0002 0.0113  513 HOH A O   
2285 O  O   . HOH F .   ? 0.1580 0.2374 0.5864 -0.0612 0.1421  -0.0092 514 HOH A O   
2286 O  O   . HOH F .   ? 0.5024 0.1807 0.2352 -0.0863 0.0340  0.0116  515 HOH A O   
2287 O  O   . HOH F .   ? 0.2241 0.1247 0.1936 -0.0055 -0.0031 0.0015  516 HOH A O   
2288 O  O   . HOH F .   ? 0.1904 0.3477 0.2037 -0.0097 0.0204  -0.0816 517 HOH A O   
2289 O  O   . HOH F .   ? 0.1742 0.1365 0.2050 -0.0164 -0.0421 0.0217  518 HOH A O   
2290 O  O   . HOH F .   ? 0.4140 0.1694 0.3190 0.0879  -0.0754 0.0041  519 HOH A O   
2291 O  O   . HOH F .   ? 0.2618 0.7242 0.2486 -0.0390 -0.0420 0.0619  520 HOH A O   
2292 O  O   . HOH F .   ? 0.1814 0.1584 0.3251 -0.0021 0.0054  -0.0643 521 HOH A O   
2293 O  O   . HOH F .   ? 0.1753 0.1943 0.4073 -0.0053 0.0491  -0.0512 522 HOH A O   
2294 O  O   . HOH F .   ? 0.4343 0.2099 0.2795 0.0850  0.0166  -0.0150 523 HOH A O   
2295 O  O   . HOH F .   ? 0.4126 0.6375 0.3324 -0.0372 0.0493  -0.0147 524 HOH A O   
2296 O  O   . HOH F .   ? 0.1444 0.8397 0.5552 0.0095  0.0536  -0.0359 525 HOH A O   
2297 O  O   . HOH F .   ? 0.4363 0.7998 0.1871 -0.1591 0.0262  0.0310  526 HOH A O   
2298 O  O   . HOH F .   ? 0.2927 0.5483 0.6768 -0.0128 -0.0075 -0.0776 527 HOH A O   
2299 O  O   . HOH F .   ? 0.3667 0.2921 0.3111 -0.1469 -0.1346 0.0630  528 HOH A O   
2300 O  O   . HOH F .   ? 0.1569 0.1078 0.1562 0.0176  0.0016  0.0365  529 HOH A O   
2301 O  O   . HOH F .   ? 0.2142 0.1875 0.4428 0.0302  -0.0559 0.0029  530 HOH A O   
2302 O  O   . HOH F .   ? 0.0914 0.1896 0.1882 0.0108  0.0065  -0.0313 531 HOH A O   
2303 O  O   . HOH F .   ? 0.1634 0.1207 0.1921 -0.0455 -0.0005 -0.0128 532 HOH A O   
2304 O  O   . HOH F .   ? 0.3312 0.3701 0.3464 0.0669  0.0697  -0.0681 533 HOH A O   
2305 O  O   . HOH F .   ? 0.5567 0.3787 0.5030 -0.2416 0.1697  -0.1176 534 HOH A O   
2306 O  O   . HOH F .   ? 0.1742 0.2874 0.2873 0.0332  0.0006  -0.0728 535 HOH A O   
2307 O  O   . HOH F .   ? 0.2073 0.3305 0.2072 0.0659  0.0566  0.1035  536 HOH A O   
2308 O  O   . HOH F .   ? 0.2746 0.2226 0.3050 -0.0807 0.0337  -0.0522 537 HOH A O   
2309 O  O   . HOH F .   ? 0.1340 0.1594 0.1990 -0.0190 0.0084  -0.0193 538 HOH A O   
2310 O  O   . HOH F .   ? 0.4148 0.2979 0.3360 -0.0831 0.0553  -0.0901 539 HOH A O   
2311 O  O   . HOH F .   ? 0.2842 0.3924 0.3517 -0.0773 0.0721  -0.0198 540 HOH A O   
2312 O  O   . HOH F .   ? 0.2931 0.2533 0.2640 -0.0511 0.0182  0.0837  541 HOH A O   
2313 O  O   . HOH F .   ? 0.4057 0.3299 0.6437 0.0179  -0.0824 0.2100  542 HOH A O   
2314 O  O   . HOH F .   ? 0.2266 0.1983 0.2259 0.0158  -0.0013 -0.0692 543 HOH A O   
2315 O  O   . HOH F .   ? 0.6510 0.6321 0.6795 0.2030  0.0365  -0.0287 544 HOH A O   
2316 O  O   . HOH F .   ? 0.3741 0.3485 0.4691 0.0320  -0.0084 -0.1852 545 HOH A O   
2317 O  O   . HOH F .   ? 0.2055 0.2029 0.2970 0.0229  0.0243  0.0444  546 HOH A O   
2318 O  O   . HOH F .   ? 0.2885 0.2733 0.7257 -0.0734 -0.1509 -0.1150 547 HOH A O   
2319 O  O   . HOH F .   ? 0.2065 0.6300 0.8122 0.2824  -0.0178 0.1946  548 HOH A O   
2320 O  O   . HOH F .   ? 0.2264 0.2194 0.2776 0.0811  -0.0258 -0.0278 549 HOH A O   
2321 O  O   . HOH F .   ? 0.2672 0.3491 0.3882 0.0670  0.0743  0.0085  550 HOH A O   
2322 O  O   . HOH F .   ? 0.3579 0.1760 0.3603 -0.0031 -0.0650 -0.0069 551 HOH A O   
2323 O  O   . HOH F .   ? 0.4938 0.2861 0.2594 -0.1632 0.1938  -0.1426 552 HOH A O   
2324 O  O   . HOH F .   ? 0.2698 0.2669 0.2627 -0.0066 -0.0402 0.0172  553 HOH A O   
2325 O  O   . HOH F .   ? 0.1782 0.2065 0.3136 -0.0866 -0.0795 -0.0529 554 HOH A O   
2326 O  O   . HOH F .   ? 0.4950 0.4444 0.2878 0.1496  0.0723  0.1729  555 HOH A O   
2327 O  O   . HOH F .   ? 0.2344 0.1448 0.1957 0.0411  0.0597  -0.0376 556 HOH A O   
2328 O  O   . HOH F .   ? 0.3258 0.3693 0.4078 -0.0853 0.0399  -0.0708 557 HOH A O   
2329 O  O   . HOH F .   ? 0.2380 0.3116 0.2489 0.0250  0.0439  0.1587  558 HOH A O   
2330 O  O   . HOH F .   ? 0.1760 0.2870 0.3191 0.0800  0.0379  0.0534  559 HOH A O   
2331 O  O   . HOH F .   ? 0.1850 0.4297 0.6421 -0.0013 0.0184  -0.0675 560 HOH A O   
2332 O  O   . HOH F .   ? 0.8220 0.4516 0.4313 0.0020  0.1756  -0.1620 561 HOH A O   
2333 O  O   . HOH F .   ? 0.3215 0.1473 0.4397 -0.0680 0.1676  -0.0819 562 HOH A O   
2334 O  O   . HOH F .   ? 0.1943 0.7358 0.3276 -0.0126 0.1148  0.1463  563 HOH A O   
2335 O  O   . HOH F .   ? 0.7190 0.2198 0.4160 -0.0564 0.0573  -0.0234 564 HOH A O   
2336 O  O   . HOH F .   ? 0.1526 0.1109 0.2212 -0.0190 -0.0195 0.0013  565 HOH A O   
2337 O  O   . HOH F .   ? 0.4891 0.2316 0.3194 -0.1659 -0.1353 -0.0069 566 HOH A O   
2338 O  O   . HOH F .   ? 0.2409 0.2810 0.2082 0.0195  -0.0480 0.0947  567 HOH A O   
2339 O  O   . HOH F .   ? 0.4676 0.4731 0.4935 -0.2851 -0.2430 0.2249  568 HOH A O   
2340 O  O   . HOH F .   ? 0.2640 0.2219 0.5533 0.0588  0.0115  0.0568  569 HOH A O   
2341 O  O   . HOH F .   ? 0.3365 0.3310 0.3736 -0.0844 -0.1111 0.1036  570 HOH A O   
2342 O  O   . HOH F .   ? 0.1440 0.2893 0.2366 0.0446  -0.0211 0.0087  571 HOH A O   
2343 O  O   . HOH F .   ? 0.1404 0.3299 0.3944 0.0165  0.0111  0.1089  572 HOH A O   
2344 O  O   . HOH F .   ? 0.2324 0.3506 0.2453 0.0663  -0.0497 0.0080  573 HOH A O   
2345 O  O   . HOH F .   ? 0.2977 0.2305 0.3624 -0.0486 0.0500  0.0434  574 HOH A O   
2346 O  O   . HOH F .   ? 0.5568 0.4074 0.2992 0.1198  -0.0192 -0.0696 575 HOH A O   
2347 O  O   . HOH F .   ? 0.4383 0.1932 0.2331 -0.0301 0.0628  -0.0062 576 HOH A O   
2348 O  O   . HOH F .   ? 0.4060 0.2026 0.3154 0.0835  0.0120  0.1066  577 HOH A O   
2349 O  O   . HOH F .   ? 0.3779 0.4504 0.3882 -0.1138 0.0144  0.1151  578 HOH A O   
2350 O  O   . HOH F .   ? 0.1220 0.1921 0.1465 0.0075  -0.0229 0.0450  579 HOH A O   
2351 O  O   . HOH F .   ? 0.3538 0.3025 0.4148 0.0812  -0.0685 -0.0078 580 HOH A O   
2352 O  O   . HOH F .   ? 0.3481 0.3614 0.1393 0.0414  -0.0044 0.0320  581 HOH A O   
2353 O  O   . HOH F .   ? 0.3416 0.3809 0.2431 0.0829  0.0917  0.0536  582 HOH A O   
2354 O  O   . HOH F .   ? 0.2997 0.2456 0.2093 -0.1040 0.0032  -0.0060 583 HOH A O   
2355 O  O   . HOH F .   ? 0.4469 0.4181 0.6445 -0.0521 0.1221  -0.0853 584 HOH A O   
2356 O  O   . HOH F .   ? 0.7048 0.2706 0.9408 -0.1066 -0.0730 0.1358  585 HOH A O   
2357 O  O   . HOH F .   ? 0.1383 0.0724 0.1368 0.0141  -0.0008 -0.0041 586 HOH A O   
2358 O  O   . HOH F .   ? 0.5133 0.8715 0.3100 -0.0380 -0.0049 0.0570  587 HOH A O   
2359 O  O   . HOH F .   ? 0.2264 0.2771 0.2601 0.0562  0.0017  0.0987  588 HOH A O   
2360 O  O   . HOH F .   ? 0.2633 0.2040 0.2132 -0.0697 -0.0724 -0.0115 589 HOH A O   
2361 O  O   . HOH F .   ? 0.2590 0.2310 0.2191 0.0151  0.0190  -0.0436 590 HOH A O   
2362 O  O   . HOH F .   ? 0.2425 0.3317 0.1512 0.1197  -0.0418 -0.0345 591 HOH A O   
2363 O  O   . HOH F .   ? 0.2986 0.5316 0.2414 0.0691  0.0168  0.1602  592 HOH A O   
2364 O  O   . HOH F .   ? 0.3939 0.4706 0.5317 0.1821  -0.0219 0.0784  593 HOH A O   
2365 O  O   . HOH F .   ? 0.1137 0.1929 0.2763 -0.0128 0.0122  0.0269  594 HOH A O   
2366 O  O   . HOH F .   ? 0.4415 0.4038 0.5219 0.0566  0.0340  -0.1402 595 HOH A O   
2367 O  O   . HOH F .   ? 0.4528 0.2281 0.3380 -0.1211 0.0510  0.0047  596 HOH A O   
2368 O  O   . HOH F .   ? 0.4413 0.3838 0.3227 0.0498  -0.0527 -0.0561 597 HOH A O   
2369 O  O   . HOH F .   ? 0.5360 0.5031 1.0856 0.0339  0.0182  0.1919  598 HOH A O   
2370 O  O   . HOH F .   ? 0.2251 0.3370 0.7500 -0.1097 0.0937  -0.1518 599 HOH A O   
2371 O  O   . HOH F .   ? 0.3208 0.3748 0.3093 0.1456  0.0399  0.0091  600 HOH A O   
2372 O  O   . HOH F .   ? 0.4787 0.1450 0.2834 0.1008  0.0605  -0.0125 601 HOH A O   
2373 O  O   . HOH F .   ? 0.7516 0.3768 0.4557 -0.0119 0.0027  0.0215  602 HOH A O   
2374 O  O   . HOH F .   ? 0.5187 0.4012 0.3402 -0.1018 0.0924  -0.0168 603 HOH A O   
2375 O  O   . HOH F .   ? 0.1681 0.1142 0.6623 -0.0648 0.0662  0.1173  604 HOH A O   
2376 O  O   . HOH F .   ? 0.5088 0.2730 0.5248 0.0468  0.2547  0.0066  605 HOH A O   
2377 O  O   . HOH F .   ? 0.3061 0.7459 0.3086 0.0815  -0.0867 -0.0732 606 HOH A O   
2378 O  O   . HOH F .   ? 0.3050 0.2391 0.3069 0.0817  0.0848  0.1018  607 HOH A O   
2379 O  O   . HOH F .   ? 0.1922 0.1713 0.1663 -0.0427 0.0253  -0.0353 608 HOH A O   
2380 O  O   . HOH F .   ? 0.3671 0.6379 0.5885 -0.2085 0.1203  -0.1585 609 HOH A O   
2381 O  O   . HOH F .   ? 0.4961 0.6244 0.3101 0.0632  0.0812  0.0354  610 HOH A O   
2382 O  O   . HOH F .   ? 0.3774 0.3251 0.4181 0.1583  -0.1078 -0.0862 611 HOH A O   
2383 O  O   . HOH F .   ? 0.3456 0.7098 0.2863 -0.0785 0.0075  0.0143  612 HOH A O   
2384 O  O   . HOH F .   ? 0.7913 0.2949 0.2252 -0.0455 0.1115  0.0491  613 HOH A O   
2385 O  O   . HOH F .   ? 0.4607 0.2622 0.1652 0.1173  0.0840  0.0142  614 HOH A O   
2386 O  O   . HOH F .   ? 0.6906 0.3506 0.2605 0.0886  -0.2062 -0.0075 615 HOH A O   
2387 O  O   . HOH F .   ? 0.4062 0.5263 0.5267 -0.0751 -0.1231 -0.0838 616 HOH A O   
2388 O  O   . HOH F .   ? 0.4914 0.4214 0.6086 -0.0475 0.0089  0.1193  617 HOH A O   
2389 O  O   . HOH F .   ? 0.2460 0.4602 0.6393 -0.0585 0.0629  -0.1689 618 HOH A O   
2390 O  O   . HOH F .   ? 0.6287 0.5166 0.6050 0.2480  0.1953  0.1895  619 HOH A O   
2391 O  O   . HOH F .   ? 0.3614 0.3054 0.3889 0.0118  -0.1136 -0.1207 620 HOH A O   
2392 O  O   . HOH F .   ? 0.5570 0.1537 0.3958 -0.1485 -0.1015 -0.0148 621 HOH A O   
2393 O  O   . HOH F .   ? 0.4217 0.3758 0.2569 0.0678  -0.0857 -0.0666 622 HOH A O   
2394 O  O   . HOH F .   ? 0.5922 0.5612 0.6294 0.1988  -0.0930 -0.0810 623 HOH A O   
2395 O  O   . HOH F .   ? 0.3227 0.3629 0.4117 -0.0891 0.0309  0.1652  624 HOH A O   
2396 O  O   . HOH F .   ? 0.3445 0.3150 0.2561 0.0369  -0.0341 -0.0004 625 HOH A O   
2397 O  O   . HOH F .   ? 0.4382 0.2043 0.2306 0.0551  0.0665  0.1242  626 HOH A O   
2398 O  O   . HOH F .   ? 0.5499 0.4054 0.4401 -0.1285 0.1423  0.0172  627 HOH A O   
2399 O  O   . HOH F .   ? 0.6962 0.5490 0.4476 0.3793  0.0054  0.1179  628 HOH A O   
2400 O  O   . HOH F .   ? 0.2612 0.2752 0.3003 0.0162  -0.0266 -0.0049 629 HOH A O   
2401 O  O   . HOH F .   ? 0.4665 0.2529 0.6641 -0.0557 -0.0311 0.0466  630 HOH A O   
2402 O  O   . HOH F .   ? 0.3353 0.3493 0.8699 0.0294  -0.1190 -0.2008 631 HOH A O   
2403 O  O   . HOH F .   ? 0.2262 0.6645 0.5160 0.0103  0.0132  0.2717  632 HOH A O   
2404 O  O   . HOH F .   ? 0.1329 0.7645 0.7615 0.0227  0.0119  -0.2891 633 HOH A O   
2405 O  O   . HOH F .   ? 0.4291 0.4652 0.5000 0.0348  -0.0044 -0.0292 634 HOH A O   
2406 O  O   . HOH F .   ? 0.3358 0.4275 0.7364 -0.0501 0.0583  0.0861  635 HOH A O   
2407 O  O   . HOH F .   ? 0.5893 0.4018 0.5231 0.0135  0.0053  0.0059  636 HOH A O   
2408 O  O   . HOH F .   ? 0.4048 0.2740 0.4277 -0.0135 -0.0344 -0.1719 637 HOH A O   
2409 O  O   . HOH F .   ? 0.3499 0.2812 0.5653 -0.0091 -0.0943 -0.1234 638 HOH A O   
2410 O  O   . HOH F .   ? 0.3080 0.7310 0.3434 0.0895  -0.0137 0.1326  639 HOH A O   
2411 O  O   . HOH F .   ? 0.4485 0.5309 0.7797 -0.0064 0.2579  -0.0491 640 HOH A O   
2412 O  O   . HOH F .   ? 0.4101 0.2626 0.2824 -0.0271 0.0281  -0.0220 641 HOH A O   
2413 O  O   . HOH F .   ? 0.2489 0.7402 0.3824 -0.0379 0.0201  -0.0485 642 HOH A O   
2414 O  O   . HOH F .   ? 0.5669 0.2330 0.3774 0.0712  0.1834  0.0622  643 HOH A O   
2415 O  O   . HOH F .   ? 0.4557 0.4782 0.5503 0.0363  -0.0861 0.1246  644 HOH A O   
2416 O  O   . HOH F .   ? 0.2705 0.2421 0.2777 -0.0612 -0.0039 0.0406  645 HOH A O   
2417 O  O   . HOH F .   ? 0.3043 0.7707 0.4931 0.1224  0.0884  -0.0364 646 HOH A O   
2418 O  O   . HOH F .   ? 0.6678 0.4469 0.3141 0.0881  0.1543  0.0177  647 HOH A O   
2419 O  O   . HOH F .   ? 0.5921 0.4616 0.4686 -0.0315 0.0030  -0.1781 648 HOH A O   
2420 O  O   . HOH F .   ? 0.3402 0.2816 0.3774 0.1049  -0.2010 -0.0341 649 HOH A O   
2421 O  O   . HOH F .   ? 0.2478 0.4349 0.3003 -0.1152 0.0514  -0.0155 650 HOH A O   
2422 O  O   . HOH F .   ? 0.3822 0.6694 0.5511 -0.0662 0.0882  0.1401  651 HOH A O   
2423 O  O   . HOH F .   ? 0.4198 0.6108 0.6678 -0.0882 0.1595  -0.0514 652 HOH A O   
2424 O  O   . HOH F .   ? 0.6102 0.3873 0.4110 -0.2304 0.0429  -0.1392 653 HOH A O   
2425 O  O   . HOH F .   ? 0.3213 0.3133 0.2604 -0.0842 -0.0710 -0.0539 654 HOH A O   
2426 O  O   . HOH F .   ? 0.3143 0.6236 0.3256 0.0889  -0.0368 0.0803  655 HOH A O   
2427 O  O   . HOH F .   ? 0.3412 0.4225 0.4485 0.0001  0.0805  -0.0244 656 HOH A O   
2428 O  O   . HOH F .   ? 0.3031 0.2496 0.2500 0.0276  0.0467  -0.0069 657 HOH A O   
2429 O  O   . HOH F .   ? 0.6216 0.3069 0.3255 -0.0013 0.0288  0.0203  658 HOH A O   
2430 O  O   . HOH F .   ? 0.3182 0.2338 0.5477 -0.0162 0.0644  0.1080  659 HOH A O   
2431 O  O   . HOH F .   ? 0.6697 0.7352 0.6819 0.0501  -0.2167 -0.2193 660 HOH A O   
2432 O  O   . HOH F .   ? 0.5464 0.6225 0.5398 0.0359  -0.0116 -0.0908 661 HOH A O   
2433 O  O   . HOH F .   ? 0.3708 0.2227 0.3319 -0.0505 -0.0827 0.0024  662 HOH A O   
2434 O  O   . HOH F .   ? 0.4963 0.5263 0.2724 0.1371  -0.0208 -0.0644 663 HOH A O   
2435 O  O   . HOH F .   ? 0.2318 0.4358 0.2328 0.1122  0.0966  0.0612  664 HOH A O   
2436 O  O   . HOH F .   ? 0.3829 0.3080 0.2698 0.1104  -0.0601 0.0082  665 HOH A O   
2437 O  O   . HOH F .   ? 0.3933 0.3858 0.2158 -0.0333 0.0616  0.0773  666 HOH A O   
2438 O  O   . HOH F .   ? 0.4997 0.4453 0.3287 0.0271  -0.0287 -0.0085 667 HOH A O   
2439 O  O   . HOH F .   ? 0.3290 0.3039 0.4146 0.0309  0.0436  0.0728  668 HOH A O   
2440 O  O   . HOH F .   ? 0.2687 0.3523 0.2856 0.0410  0.0569  0.0623  669 HOH A O   
2441 O  O   . HOH F .   ? 0.3177 0.3157 0.5449 -0.0817 -0.0407 -0.0644 670 HOH A O   
2442 O  O   . HOH F .   ? 0.3069 0.2298 0.3104 -0.0517 0.0243  0.0526  671 HOH A O   
2443 O  O   . HOH F .   ? 0.4922 0.3254 0.5641 -0.0384 -0.0401 -0.0556 672 HOH A O   
2444 O  O   . HOH F .   ? 0.5327 0.4691 0.3803 -0.1982 0.0568  0.0463  673 HOH A O   
2445 O  O   . HOH F .   ? 0.3104 0.5313 0.5092 -0.0084 -0.0424 -0.0460 674 HOH A O   
2446 O  O   . HOH F .   ? 0.3419 0.3846 0.4485 0.0612  0.1108  0.0010  675 HOH A O   
2447 O  O   . HOH F .   ? 0.2856 0.1825 0.2511 0.0466  -0.0582 0.0239  676 HOH A O   
2448 O  O   . HOH F .   ? 0.3767 0.4261 0.4286 0.1443  -0.0912 0.0225  677 HOH A O   
2449 O  O   . HOH F .   ? 0.4807 0.3739 0.8953 -0.0148 -0.2804 0.1035  678 HOH A O   
2450 O  O   . HOH F .   ? 0.1595 0.1537 0.1505 -0.0153 0.0262  -0.0087 679 HOH A O   
2451 O  O   . HOH F .   ? 0.5169 0.2558 0.3721 0.0192  0.0129  0.0000  680 HOH A O   
2452 O  O   . HOH F .   ? 0.3600 0.2428 0.2967 0.0724  0.0277  -0.0210 681 HOH A O   
2453 O  O   . HOH F .   ? 0.5628 0.2046 0.4893 0.0566  0.1097  0.0756  682 HOH A O   
2454 O  O   . HOH F .   ? 0.3839 0.3295 0.3583 -0.0939 0.0851  -0.1093 683 HOH A O   
2455 O  O   . HOH F .   ? 0.3538 0.3611 0.7286 0.0026  -0.0857 0.0798  684 HOH A O   
2456 O  O   . HOH F .   ? 0.3571 0.3722 0.2546 -0.1427 0.0555  0.0522  685 HOH A O   
2457 O  O   . HOH F .   ? 0.4083 0.4169 0.3402 -0.0261 0.0343  -0.1161 686 HOH A O   
2458 O  O   . HOH F .   ? 0.5352 0.4641 0.3775 -0.0683 0.1034  -0.1278 687 HOH A O   
2459 O  O   . HOH F .   ? 0.5397 0.5880 0.3937 0.2846  -0.0170 0.1367  688 HOH A O   
2460 O  O   . HOH F .   ? 0.4189 0.2634 0.5083 -0.1180 0.0367  0.0704  689 HOH A O   
2461 O  O   . HOH F .   ? 0.5411 0.2176 0.5980 0.0417  0.1382  0.1414  690 HOH A O   
2462 O  O   . HOH F .   ? 0.4121 0.2198 0.4909 -0.0197 0.1326  0.0807  691 HOH A O   
2463 O  O   . HOH F .   ? 0.4547 0.8033 0.2727 0.0430  -0.0365 0.1144  692 HOH A O   
2464 O  O   . HOH F .   ? 0.5252 0.2586 0.4124 0.1385  0.0757  -0.0168 693 HOH A O   
2465 O  O   . HOH F .   ? 0.4823 0.3681 0.5581 0.1052  0.0704  0.0894  694 HOH A O   
2466 O  O   . HOH F .   ? 0.3416 0.4097 0.4562 -0.1145 0.0963  0.0313  695 HOH A O   
# 
