data_7NZR
# 
_entry.id   7NZR 
# 
_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   7NZR         pdb_00007nzr 10.2210/pdb7nzr/pdb 
WWPDB D_1292114703 ?            ?                   
# 
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                        7NZR 
_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_
_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    1   ?       ? ? ? 
4 non-polymer syn '2-(cyclooctylamino)-3,5,6-trifluoro-4-[(2-hydroxyethyl)sulfanyl]benzenesulfonamide' 412.491   1   ?       ? ? ? 
5 water       nat water                                                                                18.015    288 ?       ? ? ? 
# 
_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 '2-(cyclooctylamino)-3,5,6-trifluoro-4-[(2-hydroxyethyl)sulfanyl]benzenesulfonamide' V90 
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 
V90 non-polymer         . '2-(cyclooctylamino)-3,5,6-trifluoro-4-[(2-hydroxyethyl)sulfanyl]benzenesulfonamide' ? 
'C16 H23 F3 N2 O3 S2' 412.491 
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   ?   ?   ?   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   ?   ?   ?   A . n 
A 1 8   GLY 8   8   ?   ?   ?   A . n 
A 1 9   LYS 9   9   ?   ?   ?   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 4 V90 1   303 1   V90 V10 A . 
E 5 HOH 1   401 288 HOH HOH A . 
E 5 HOH 2   402 243 HOH HOH A . 
E 5 HOH 3   403 102 HOH HOH A . 
E 5 HOH 4   404 55  HOH HOH A . 
E 5 HOH 5   405 169 HOH HOH A . 
E 5 HOH 6   406 122 HOH HOH A . 
E 5 HOH 7   407 152 HOH HOH A . 
E 5 HOH 8   408 232 HOH HOH A . 
E 5 HOH 9   409 40  HOH HOH A . 
E 5 HOH 10  410 219 HOH HOH A . 
E 5 HOH 11  411 76  HOH HOH A . 
E 5 HOH 12  412 258 HOH HOH A . 
E 5 HOH 13  413 150 HOH HOH A . 
E 5 HOH 14  414 134 HOH HOH A . 
E 5 HOH 15  415 80  HOH HOH A . 
E 5 HOH 16  416 144 HOH HOH A . 
E 5 HOH 17  417 99  HOH HOH A . 
E 5 HOH 18  418 125 HOH HOH A . 
E 5 HOH 19  419 37  HOH HOH A . 
E 5 HOH 20  420 249 HOH HOH A . 
E 5 HOH 21  421 197 HOH HOH A . 
E 5 HOH 22  422 92  HOH HOH A . 
E 5 HOH 23  423 124 HOH HOH A . 
E 5 HOH 24  424 120 HOH HOH A . 
E 5 HOH 25  425 155 HOH HOH A . 
E 5 HOH 26  426 174 HOH HOH A . 
E 5 HOH 27  427 200 HOH HOH A . 
E 5 HOH 28  428 143 HOH HOH A . 
E 5 HOH 29  429 50  HOH HOH A . 
E 5 HOH 30  430 109 HOH HOH A . 
E 5 HOH 31  431 273 HOH HOH A . 
E 5 HOH 32  432 77  HOH HOH A . 
E 5 HOH 33  433 31  HOH HOH A . 
E 5 HOH 34  434 81  HOH HOH A . 
E 5 HOH 35  435 103 HOH HOH A . 
E 5 HOH 36  436 97  HOH HOH A . 
E 5 HOH 37  437 145 HOH HOH A . 
E 5 HOH 38  438 287 HOH HOH A . 
E 5 HOH 39  439 53  HOH HOH A . 
E 5 HOH 40  440 32  HOH HOH A . 
E 5 HOH 41  441 256 HOH HOH A . 
E 5 HOH 42  442 36  HOH HOH A . 
E 5 HOH 43  443 116 HOH HOH A . 
E 5 HOH 44  444 259 HOH HOH A . 
E 5 HOH 45  445 226 HOH HOH A . 
E 5 HOH 46  446 113 HOH HOH A . 
E 5 HOH 47  447 15  HOH HOH A . 
E 5 HOH 48  448 11  HOH HOH A . 
E 5 HOH 49  449 108 HOH HOH A . 
E 5 HOH 50  450 107 HOH HOH A . 
E 5 HOH 51  451 12  HOH HOH A . 
E 5 HOH 52  452 88  HOH HOH A . 
E 5 HOH 53  453 69  HOH HOH A . 
E 5 HOH 54  454 56  HOH HOH A . 
E 5 HOH 55  455 111 HOH HOH A . 
E 5 HOH 56  456 257 HOH HOH A . 
E 5 HOH 57  457 3   HOH HOH A . 
E 5 HOH 58  458 246 HOH HOH A . 
E 5 HOH 59  459 4   HOH HOH A . 
E 5 HOH 60  460 112 HOH HOH A . 
E 5 HOH 61  461 68  HOH HOH A . 
E 5 HOH 62  462 110 HOH HOH A . 
E 5 HOH 63  463 25  HOH HOH A . 
E 5 HOH 64  464 5   HOH HOH A . 
E 5 HOH 65  465 75  HOH HOH A . 
E 5 HOH 66  466 186 HOH HOH A . 
E 5 HOH 67  467 139 HOH HOH A . 
E 5 HOH 68  468 86  HOH HOH A . 
E 5 HOH 69  469 70  HOH HOH A . 
E 5 HOH 70  470 30  HOH HOH A . 
E 5 HOH 71  471 130 HOH HOH A . 
E 5 HOH 72  472 44  HOH HOH A . 
E 5 HOH 73  473 274 HOH HOH A . 
E 5 HOH 74  474 126 HOH HOH A . 
E 5 HOH 75  475 14  HOH HOH A . 
E 5 HOH 76  476 181 HOH HOH A . 
E 5 HOH 77  477 84  HOH HOH A . 
E 5 HOH 78  478 277 HOH HOH A . 
E 5 HOH 79  479 106 HOH HOH A . 
E 5 HOH 80  480 159 HOH HOH A . 
E 5 HOH 81  481 49  HOH HOH A . 
E 5 HOH 82  482 185 HOH HOH A . 
E 5 HOH 83  483 7   HOH HOH A . 
E 5 HOH 84  484 94  HOH HOH A . 
E 5 HOH 85  485 16  HOH HOH A . 
E 5 HOH 86  486 244 HOH HOH A . 
E 5 HOH 87  487 9   HOH HOH A . 
E 5 HOH 88  488 121 HOH HOH A . 
E 5 HOH 89  489 1   HOH HOH A . 
E 5 HOH 90  490 62  HOH HOH A . 
E 5 HOH 91  491 199 HOH HOH A . 
E 5 HOH 92  492 42  HOH HOH A . 
E 5 HOH 93  493 265 HOH HOH A . 
E 5 HOH 94  494 276 HOH HOH A . 
E 5 HOH 95  495 93  HOH HOH A . 
E 5 HOH 96  496 104 HOH HOH A . 
E 5 HOH 97  497 83  HOH HOH A . 
E 5 HOH 98  498 35  HOH HOH A . 
E 5 HOH 99  499 189 HOH HOH A . 
E 5 HOH 100 500 254 HOH HOH A . 
E 5 HOH 101 501 72  HOH HOH A . 
E 5 HOH 102 502 204 HOH HOH A . 
E 5 HOH 103 503 22  HOH HOH A . 
E 5 HOH 104 504 187 HOH HOH A . 
E 5 HOH 105 505 61  HOH HOH A . 
E 5 HOH 106 506 65  HOH HOH A . 
E 5 HOH 107 507 17  HOH HOH A . 
E 5 HOH 108 508 119 HOH HOH A . 
E 5 HOH 109 509 284 HOH HOH A . 
E 5 HOH 110 510 2   HOH HOH A . 
E 5 HOH 111 511 198 HOH HOH A . 
E 5 HOH 112 512 183 HOH HOH A . 
E 5 HOH 113 513 231 HOH HOH A . 
E 5 HOH 114 514 160 HOH HOH A . 
E 5 HOH 115 515 175 HOH HOH A . 
E 5 HOH 116 516 178 HOH HOH A . 
E 5 HOH 117 517 98  HOH HOH A . 
E 5 HOH 118 518 227 HOH HOH A . 
E 5 HOH 119 519 127 HOH HOH A . 
E 5 HOH 120 520 46  HOH HOH A . 
E 5 HOH 121 521 188 HOH HOH A . 
E 5 HOH 122 522 52  HOH HOH A . 
E 5 HOH 123 523 85  HOH HOH A . 
E 5 HOH 124 524 229 HOH HOH A . 
E 5 HOH 125 525 138 HOH HOH A . 
E 5 HOH 126 526 179 HOH HOH A . 
E 5 HOH 127 527 6   HOH HOH A . 
E 5 HOH 128 528 58  HOH HOH A . 
E 5 HOH 129 529 27  HOH HOH A . 
E 5 HOH 130 530 39  HOH HOH A . 
E 5 HOH 131 531 91  HOH HOH A . 
E 5 HOH 132 532 48  HOH HOH A . 
E 5 HOH 133 533 222 HOH HOH A . 
E 5 HOH 134 534 74  HOH HOH A . 
E 5 HOH 135 535 190 HOH HOH A . 
E 5 HOH 136 536 23  HOH HOH A . 
E 5 HOH 137 537 28  HOH HOH A . 
E 5 HOH 138 538 261 HOH HOH A . 
E 5 HOH 139 539 151 HOH HOH A . 
E 5 HOH 140 540 10  HOH HOH A . 
E 5 HOH 141 541 18  HOH HOH A . 
E 5 HOH 142 542 211 HOH HOH A . 
E 5 HOH 143 543 96  HOH HOH A . 
E 5 HOH 144 544 233 HOH HOH A . 
E 5 HOH 145 545 146 HOH HOH A . 
E 5 HOH 146 546 286 HOH HOH A . 
E 5 HOH 147 547 66  HOH HOH A . 
E 5 HOH 148 548 225 HOH HOH A . 
E 5 HOH 149 549 20  HOH HOH A . 
E 5 HOH 150 550 33  HOH HOH A . 
E 5 HOH 151 551 263 HOH HOH A . 
E 5 HOH 152 552 67  HOH HOH A . 
E 5 HOH 153 553 54  HOH HOH A . 
E 5 HOH 154 554 64  HOH HOH A . 
E 5 HOH 155 555 194 HOH HOH A . 
E 5 HOH 156 556 29  HOH HOH A . 
E 5 HOH 157 557 19  HOH HOH A . 
E 5 HOH 158 558 176 HOH HOH A . 
E 5 HOH 159 559 24  HOH HOH A . 
E 5 HOH 160 560 214 HOH HOH A . 
E 5 HOH 161 561 51  HOH HOH A . 
E 5 HOH 162 562 161 HOH HOH A . 
E 5 HOH 163 563 45  HOH HOH A . 
E 5 HOH 164 564 177 HOH HOH A . 
E 5 HOH 165 565 13  HOH HOH A . 
E 5 HOH 166 566 115 HOH HOH A . 
E 5 HOH 167 567 182 HOH HOH A . 
E 5 HOH 168 568 230 HOH HOH A . 
E 5 HOH 169 569 136 HOH HOH A . 
E 5 HOH 170 570 235 HOH HOH A . 
E 5 HOH 171 571 114 HOH HOH A . 
E 5 HOH 172 572 73  HOH HOH A . 
E 5 HOH 173 573 60  HOH HOH A . 
E 5 HOH 174 574 38  HOH HOH A . 
E 5 HOH 175 575 221 HOH HOH A . 
E 5 HOH 176 576 8   HOH HOH A . 
E 5 HOH 177 577 79  HOH HOH A . 
E 5 HOH 178 578 26  HOH HOH A . 
E 5 HOH 179 579 34  HOH HOH A . 
E 5 HOH 180 580 217 HOH HOH A . 
E 5 HOH 181 581 215 HOH HOH A . 
E 5 HOH 182 582 131 HOH HOH A . 
E 5 HOH 183 583 21  HOH HOH A . 
E 5 HOH 184 584 280 HOH HOH A . 
E 5 HOH 185 585 129 HOH HOH A . 
E 5 HOH 186 586 135 HOH HOH A . 
E 5 HOH 187 587 172 HOH HOH A . 
E 5 HOH 188 588 59  HOH HOH A . 
E 5 HOH 189 589 180 HOH HOH A . 
E 5 HOH 190 590 212 HOH HOH A . 
E 5 HOH 191 591 271 HOH HOH A . 
E 5 HOH 192 592 267 HOH HOH A . 
E 5 HOH 193 593 101 HOH HOH A . 
E 5 HOH 194 594 223 HOH HOH A . 
E 5 HOH 195 595 278 HOH HOH A . 
E 5 HOH 196 596 43  HOH HOH A . 
E 5 HOH 197 597 268 HOH HOH A . 
E 5 HOH 198 598 117 HOH HOH A . 
E 5 HOH 199 599 157 HOH HOH A . 
E 5 HOH 200 600 269 HOH HOH A . 
E 5 HOH 201 601 82  HOH HOH A . 
E 5 HOH 202 602 184 HOH HOH A . 
E 5 HOH 203 603 57  HOH HOH A . 
E 5 HOH 204 604 281 HOH HOH A . 
E 5 HOH 205 605 148 HOH HOH A . 
E 5 HOH 206 606 250 HOH HOH A . 
E 5 HOH 207 607 279 HOH HOH A . 
E 5 HOH 208 608 237 HOH HOH A . 
E 5 HOH 209 609 202 HOH HOH A . 
E 5 HOH 210 610 207 HOH HOH A . 
E 5 HOH 211 611 165 HOH HOH A . 
E 5 HOH 212 612 47  HOH HOH A . 
E 5 HOH 213 613 239 HOH HOH A . 
E 5 HOH 214 614 156 HOH HOH A . 
E 5 HOH 215 615 209 HOH HOH A . 
E 5 HOH 216 616 260 HOH HOH A . 
E 5 HOH 217 617 193 HOH HOH A . 
E 5 HOH 218 618 275 HOH HOH A . 
E 5 HOH 219 619 213 HOH HOH A . 
E 5 HOH 220 620 132 HOH HOH A . 
E 5 HOH 221 621 262 HOH HOH A . 
E 5 HOH 222 622 241 HOH HOH A . 
E 5 HOH 223 623 78  HOH HOH A . 
E 5 HOH 224 624 245 HOH HOH A . 
E 5 HOH 225 625 158 HOH HOH A . 
E 5 HOH 226 626 71  HOH HOH A . 
E 5 HOH 227 627 240 HOH HOH A . 
E 5 HOH 228 628 236 HOH HOH A . 
E 5 HOH 229 629 173 HOH HOH A . 
E 5 HOH 230 630 251 HOH HOH A . 
E 5 HOH 231 631 208 HOH HOH A . 
E 5 HOH 232 632 234 HOH HOH A . 
E 5 HOH 233 633 123 HOH HOH A . 
E 5 HOH 234 634 248 HOH HOH A . 
E 5 HOH 235 635 252 HOH HOH A . 
E 5 HOH 236 636 266 HOH HOH A . 
E 5 HOH 237 637 133 HOH HOH A . 
E 5 HOH 238 638 100 HOH HOH A . 
E 5 HOH 239 639 247 HOH HOH A . 
E 5 HOH 240 640 264 HOH HOH A . 
E 5 HOH 241 641 141 HOH HOH A . 
E 5 HOH 242 642 224 HOH HOH A . 
E 5 HOH 243 643 228 HOH HOH A . 
E 5 HOH 244 644 210 HOH HOH A . 
E 5 HOH 245 645 191 HOH HOH A . 
E 5 HOH 246 646 285 HOH HOH A . 
E 5 HOH 247 647 283 HOH HOH A . 
E 5 HOH 248 648 63  HOH HOH A . 
E 5 HOH 249 649 168 HOH HOH A . 
E 5 HOH 250 650 149 HOH HOH A . 
E 5 HOH 251 651 255 HOH HOH A . 
E 5 HOH 252 652 137 HOH HOH A . 
E 5 HOH 253 653 154 HOH HOH A . 
E 5 HOH 254 654 105 HOH HOH A . 
E 5 HOH 255 655 87  HOH HOH A . 
E 5 HOH 256 656 238 HOH HOH A . 
E 5 HOH 257 657 89  HOH HOH A . 
E 5 HOH 258 658 118 HOH HOH A . 
E 5 HOH 259 659 220 HOH HOH A . 
E 5 HOH 260 660 164 HOH HOH A . 
E 5 HOH 261 661 216 HOH HOH A . 
E 5 HOH 262 662 41  HOH HOH A . 
E 5 HOH 263 663 171 HOH HOH A . 
E 5 HOH 264 664 140 HOH HOH A . 
E 5 HOH 265 665 195 HOH HOH A . 
E 5 HOH 266 666 147 HOH HOH A . 
E 5 HOH 267 667 95  HOH HOH A . 
E 5 HOH 268 668 282 HOH HOH A . 
E 5 HOH 269 669 242 HOH HOH A . 
E 5 HOH 270 670 196 HOH HOH A . 
E 5 HOH 271 671 128 HOH HOH A . 
E 5 HOH 272 672 167 HOH HOH A . 
E 5 HOH 273 673 162 HOH HOH A . 
E 5 HOH 274 674 153 HOH HOH A . 
E 5 HOH 275 675 218 HOH HOH A . 
E 5 HOH 276 676 203 HOH HOH A . 
E 5 HOH 277 677 166 HOH HOH A . 
E 5 HOH 278 678 205 HOH HOH A . 
E 5 HOH 279 679 163 HOH HOH A . 
E 5 HOH 280 680 90  HOH HOH A . 
E 5 HOH 281 681 253 HOH HOH A . 
E 5 HOH 282 682 142 HOH HOH A . 
E 5 HOH 283 683 270 HOH HOH A . 
E 5 HOH 284 684 206 HOH HOH A . 
E 5 HOH 285 685 272 HOH HOH A . 
E 5 HOH 286 686 201 HOH HOH A . 
E 5 HOH 287 687 192 HOH HOH A . 
E 5 HOH 288 688 170 HOH HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A LYS 45  ? CE  ? A LYS 45  CE  
2  1 Y 1 A LYS 45  ? NZ  ? A LYS 45  NZ  
3  1 Y 1 A LYS 80  ? CE  ? A LYS 80  CE  
4  1 Y 1 A LYS 80  ? NZ  ? A LYS 80  NZ  
5  1 Y 1 A LYS 167 ? NZ  ? A LYS 167 NZ  
6  1 Y 1 A LYS 212 ? CE  ? A LYS 212 CE  
7  1 Y 1 A LYS 212 ? NZ  ? A LYS 212 NZ  
8  1 Y 1 A GLN 254 ? CD  ? A GLN 254 CD  
9  1 Y 1 A GLN 254 ? OE1 ? A GLN 254 OE1 
10 1 Y 1 A GLN 254 ? NE2 ? A GLN 254 NE2 
11 1 Y 1 A LYS 256 ? CD  ? A LYS 256 CD  
12 1 Y 1 A LYS 256 ? CE  ? A LYS 256 CE  
13 1 Y 1 A LYS 256 ? NZ  ? A LYS 256 NZ  
14 1 Y 1 A LYS 260 ? CG  ? A LYS 260 CG  
15 1 Y 1 A LYS 260 ? CD  ? A LYS 260 CD  
16 1 Y 1 A LYS 260 ? CE  ? A LYS 260 CE  
17 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                   104.080 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     7NZR 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     42.324 
_cell.length_a_esd                 ? 
_cell.length_b                     41.160 
_cell.length_b_esd                 ? 
_cell.length_c                     71.681 
_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                         7NZR 
_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                   7NZR 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                      ? 
_exptl_crystal.density_diffrn              ? 
_exptl_crystal.density_Matthews            2.06 
_exptl_crystal.density_method              ? 
_exptl_crystal.density_percent_sol         40.33 
_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                         7NZR 
_reflns.data_reduction_details           ? 
_reflns.data_reduction_method            ? 
_reflns.d_resolution_high                1.280 
_reflns.d_resolution_low                 69.528 
_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                       58838 
_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             96.300 
_reflns.R_free_details                   ? 
_reflns.Rmerge_F_all                     ? 
_reflns.Rmerge_F_obs                     ? 
_reflns.Friedel_coverage                 ? 
_reflns.number_gt                        ? 
_reflns.threshold_expression             ? 
_reflns.pdbx_redundancy                  6.700 
_reflns.pdbx_Rmerge_I_obs                ? 
_reflns.pdbx_Rmerge_I_all                ? 
_reflns.pdbx_Rsym_value                  0.040 
_reflns.pdbx_netI_over_av_sigmaI         9.700 
_reflns.pdbx_netI_over_sigmaI            20.500 
_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                  0.049 
_reflns.pdbx_Rpim_I_all                  0.019 
_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 
1.284 1.350  ? 2.900  ? ? ? ? 7326 83.400 ? ? ? ? 0.258 ? ? ? ? ? ? ? ? 6.000 0.258 ? ? ? 0.320 0.128 ? 1  1 ? ? ? 
1.350 1.440  ? 3.900  ? ? ? ? 8209 97.600 ? ? ? ? 0.192 ? ? ? ? ? ? ? ? 6.800 0.192 ? ? ? 0.234 0.088 ? 2  1 ? ? ? 
1.440 1.530  ? 5.800  ? ? ? ? 7681 97.400 ? ? ? ? 0.129 ? ? ? ? ? ? ? ? 6.600 0.129 ? ? ? 0.158 0.060 ? 3  1 ? ? ? 
1.530 1.660  ? 8.300  ? ? ? ? 7242 98.500 ? ? ? ? 0.089 ? ? ? ? ? ? ? ? 6.900 0.089 ? ? ? 0.111 0.042 ? 4  1 ? ? ? 
1.660 1.820  ? 11.200 ? ? ? ? 6654 98.200 ? ? ? ? 0.064 ? ? ? ? ? ? ? ? 6.600 0.064 ? ? ? 0.082 0.031 ? 5  1 ? ? ? 
1.820 2.030  ? 14.600 ? ? ? ? 6107 99.200 ? ? ? ? 0.047 ? ? ? ? ? ? ? ? 7.000 0.047 ? ? ? 0.059 0.022 ? 6  1 ? ? ? 
2.030 2.340  ? 17.800 ? ? ? ? 5409 99.100 ? ? ? ? 0.038 ? ? ? ? ? ? ? ? 6.700 0.038 ? ? ? 0.048 0.018 ? 7  1 ? ? ? 
2.340 2.870  ? 18.200 ? ? ? ? 4603 99.800 ? ? ? ? 0.035 ? ? ? ? ? ? ? ? 7.000 0.035 ? ? ? 0.044 0.016 ? 8  1 ? ? ? 
2.870 4.060  ? 20.100 ? ? ? ? 3575 99.200 ? ? ? ? 0.030 ? ? ? ? ? ? ? ? 6.700 0.030 ? ? ? 0.036 0.014 ? 9  1 ? ? ? 
4.060 69.528 ? 19.900 ? ? ? ? 2032 99.600 ? ? ? ? 0.028 ? ? ? ? ? ? ? ? 6.600 0.028 ? ? ? 0.034 0.013 ? 10 1 ? ? ? 
# 
_refine.aniso_B[1][1]                            -0.0900 
_refine.aniso_B[1][2]                            -0.0000 
_refine.aniso_B[1][3]                            -0.1300 
_refine.aniso_B[2][2]                            0.2700 
_refine.aniso_B[2][3]                            -0.0000 
_refine.aniso_B[3][3]                            -0.1100 
_refine.B_iso_max                                100.050 
_refine.B_iso_mean                               18.3620 
_refine.B_iso_min                                7.260 
_refine.correlation_coeff_Fo_to_Fc               0.9810 
_refine.correlation_coeff_Fo_to_Fc_free          0.9730 
_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                                 7NZR 
_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                            1.2840 
_refine.ls_d_res_low                             41.0500 
_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                     52861 
_refine.ls_number_reflns_R_free                  5960 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    96.0000 
_refine.ls_percent_reflns_R_free                 10.1000 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1274 
_refine.ls_R_factor_R_free                       0.1586 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1239 
_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                       0.0470 
_refine.pdbx_overall_ESU_R_Free                  0.0460 
_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                       1.2840 
_refine_hist.d_res_low                        41.0500 
_refine_hist.number_atoms_solvent             288 
_refine_hist.number_atoms_total               2322 
_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       253 
_refine_hist.pdbx_B_iso_mean_ligand           18.62 
_refine_hist.pdbx_B_iso_mean_solvent          31.50 
_refine_hist.pdbx_number_atoms_protein        2003 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         31 
_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' ? 0.016  0.012  2246 ? r_bond_refined_d       ? ? 
'X-RAY DIFFRACTION' ? 2.143  1.657  3075 ? r_angle_refined_deg    ? ? 
'X-RAY DIFFRACTION' ? 6.878  5.000  283  ? r_dihedral_angle_1_deg ? ? 
'X-RAY DIFFRACTION' ? 35.655 23.394 109  ? r_dihedral_angle_2_deg ? ? 
'X-RAY DIFFRACTION' ? 12.437 15.000 369  ? r_dihedral_angle_3_deg ? ? 
'X-RAY DIFFRACTION' ? 22.088 15.000 9    ? r_dihedral_angle_4_deg ? ? 
'X-RAY DIFFRACTION' ? 0.143  0.200  275  ? r_chiral_restr         ? ? 
'X-RAY DIFFRACTION' ? 0.014  0.020  1775 ? r_gen_planes_refined   ? ? 
'X-RAY DIFFRACTION' ? 11.937 3.000  2246 ? r_rigid_bond_restr     ? ? 
'X-RAY DIFFRACTION' ? 23.322 5.000  152  ? r_sphericity_free      ? ? 
'X-RAY DIFFRACTION' ? 15.341 5.000  2309 ? r_sphericity_bonded    ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.2840 
_refine_ls_shell.d_res_low                        1.3170 
_refine_ls_shell.number_reflns_all                3133 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             316 
_refine_ls_shell.number_reflns_R_work             2817 
_refine_ls_shell.percent_reflns_obs               70.4200 
_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                  0.1960 
_refine_ls_shell.R_factor_R_free_error            0.0000 
_refine_ls_shell.R_factor_R_work                  0.1550 
_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                     7NZR 
_struct.title                        
;Crystal structure of chimeric carbonic anhydrase VA with 2-(cyclooctylamino)-3,5,6-trifluoro-4-[(2-hydroxyethyl)sulfanyl]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        7NZR 
_struct_keywords.text            
'drug design, carbonic anhydrase, benzenesulfonamide, metal-binding, lyase-lyase inhibitor complex, LYASE' 
_struct_keywords.pdbx_keywords   LYASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 5 ? 
# 
_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              7NZR 
_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 7NZR THR A 62  ? UNP P00918 ASN 62  'engineered mutation' 62  1 
1 7NZR TYR A 64  ? UNP P00918 HIS 64  'engineered mutation' 64  2 
1 7NZR LEU A 65  ? UNP P00918 ALA 65  'engineered mutation' 65  3 
1 7NZR GLN A 67  ? UNP P00918 ASN 67  'engineered mutation' 67  4 
1 7NZR LYS A 91  ? UNP P00918 ILE 91  'engineered mutation' 91  5 
1 7NZR TYR A 130 ? UNP P00918 PHE 130 'engineered mutation' 130 6 
1 7NZR 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)' 220   ? 
1 MORE         2     ? 
1 'SSA (A^2)'  11250 ? 
# 
_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 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 GLY A 12  ? ASP A 19  ? GLY A 12  ASP A 19  5 ? 8 
HELX_P HELX_P2 AA2 PHE A 20  ? GLY A 25  ? PHE A 20  GLY A 25  5 ? 6 
HELX_P HELX_P3 AA3 LYS A 126 ? GLY A 128 ? LYS A 126 GLY A 128 5 ? 3 
HELX_P HELX_P4 AA4 ASP A 129 ? VAL A 134 ? ASP A 129 VAL A 134 1 ? 6 
HELX_P HELX_P5 AA5 LYS A 153 ? GLY A 155 ? LYS A 153 GLY A 155 5 ? 3 
HELX_P HELX_P6 AA6 LEU A 156 ? LEU A 163 ? LEU A 156 LEU A 163 1 ? 8 
HELX_P HELX_P7 AA7 ASP A 164 ? LYS A 167 ? ASP A 164 LYS A 167 5 ? 4 
HELX_P HELX_P8 AA8 ASP A 179 ? LEU A 184 ? ASP A 179 LEU A 184 5 ? 6 
HELX_P HELX_P9 AA9 SER A 218 ? ARG A 226 ? SER A 218 ARG A 226 1 ? 9 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A HIS 94  NE2 ? ? ? 1_555 B ZN  . ZN  ? ? A HIS 94  A ZN  301 1_555 ? ? ? ? ? ? ? 1.984 ? ? 
metalc2 metalc ? ? A HIS 96  NE2 ? ? ? 1_555 B ZN  . ZN  ? ? A HIS 96  A ZN  301 1_555 ? ? ? ? ? ? ? 1.999 ? ? 
metalc3 metalc ? ? A HIS 119 ND1 ? ? ? 1_555 B ZN  . ZN  ? ? A HIS 119 A ZN  301 1_555 ? ? ? ? ? ? ? 2.031 ? ? 
metalc4 metalc ? ? B ZN  .   ZN  ? ? ? 1_555 D V90 . N11 ? ? A ZN  301 A V90 303 1_555 ? ? ? ? ? ? ? 1.934 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1 NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 103.9 ? 
2 NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 109.0 ? 
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 99.5  ? 
4 NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N11 ? D V90 .   ? A V90 303 ? 1_555 113.7 ? 
5 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N11 ? D V90 .   ? A V90 303 ? 1_555 114.7 ? 
6 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N11 ? D V90 .   ? A V90 303 ? 1_555 114.6 ? 
# 
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 -4.78 
2 PRO 200 A . ? PRO 200 A PRO 201 A ? PRO 201 A 1 10.21 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2  ? 
AA2 ? 10 ? 
AA3 ? 6  ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2  ? parallel      
AA2 1 2  ? parallel      
AA2 2 3  ? anti-parallel 
AA2 3 4  ? anti-parallel 
AA2 4 5  ? parallel      
AA2 5 6  ? anti-parallel 
AA2 6 7  ? anti-parallel 
AA2 7 8  ? anti-parallel 
AA2 8 9  ? anti-parallel 
AA2 9 10 ? anti-parallel 
AA3 1 2  ? anti-parallel 
AA3 2 3  ? anti-parallel 
AA3 3 4  ? anti-parallel 
AA3 4 5  ? anti-parallel 
AA3 5 6  ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1  ASP A 32  ? ILE A 33  ? ASP A 32  ILE A 33  
AA1 2  THR A 108 ? VAL A 109 ? THR A 108 VAL A 109 
AA2 1  LYS A 39  ? TYR A 40  ? LYS A 39  TYR A 40  
AA2 2  LYS A 256 ? ALA A 257 ? LYS A 256 ALA A 257 
AA2 3  TYR A 190 ? GLY A 195 ? TYR A 190 GLY A 195 
AA2 4  VAL A 206 ? LEU A 211 ? VAL A 206 LEU A 211 
AA2 5  LEU A 140 ? VAL A 149 ? LEU A 140 VAL A 149 
AA2 6  ALA A 116 ? ASN A 124 ? ALA A 116 ASN A 124 
AA2 7  TYR A 88  ? TRP A 97  ? TYR A 88  TRP A 97  
AA2 8  PHE A 66  ? PHE A 70  ? PHE A 66  PHE A 70  
AA2 9  SER A 56  ? ASN A 61  ? SER A 56  ASN A 61  
AA2 10 SER A 172 ? ASP A 174 ? SER A 172 ASP A 174 
AA3 1  LYS A 45  ? SER A 50  ? LYS A 45  SER A 50  
AA3 2  VAL A 78  ? GLY A 82  ? VAL A 78  GLY A 82  
AA3 3  TYR A 88  ? TRP A 97  ? TYR A 88  TRP A 97  
AA3 4  ALA A 116 ? ASN A 124 ? ALA A 116 ASN A 124 
AA3 5  LEU A 140 ? VAL A 149 ? LEU A 140 VAL A 149 
AA3 6  ILE A 215 ? VAL A 217 ? ILE A 215 VAL A 217 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2  N ILE A 33  ? N ILE A 33  O THR A 108 ? O THR A 108 
AA2 1 2  N LYS A 39  ? N LYS A 39  O ALA A 257 ? O ALA A 257 
AA2 2 3  O LYS A 256 ? O LYS A 256 N THR A 192 ? N THR A 192 
AA2 3 4  N GLY A 195 ? N GLY A 195 O VAL A 206 ? O VAL A 206 
AA2 4 5  O LEU A 211 ? O LEU A 211 N GLY A 144 ? N GLY A 144 
AA2 5 6  O ILE A 145 ? O ILE A 145 N LEU A 118 ? N LEU A 118 
AA2 6 7  O HIS A 119 ? O HIS A 119 N HIS A 94  ? N HIS A 94  
AA2 7 8  O PHE A 93  ? O PHE A 93  N VAL A 68  ? N VAL A 68  
AA2 8 9  O GLU A 69  ? O GLU A 69  N LEU A 57  ? N LEU A 57  
AA2 9 10 N ILE A 59  ? N ILE A 59  O ALA A 173 ? O ALA A 173 
AA3 1 2  N SER A 50  ? N SER A 50  O VAL A 78  ? O VAL A 78  
AA3 2 3  N LEU A 79  ? N LEU A 79  O TYR A 88  ? O TYR A 88  
AA3 3 4  N HIS A 94  ? N HIS A 94  O HIS A 119 ? O HIS A 119 
AA3 4 5  N LEU A 118 ? N LEU A 118 O ILE A 145 ? O ILE A 145 
AA3 5 6  N PHE A 146 ? N PHE A 146 O ILE A 215 ? O ILE A 215 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   OG1 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   THR 
_pdbx_validate_close_contact.auth_seq_id_1    199 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   A 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    401 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             1.77 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 O A HOH 406 ? ? 1_555 O A HOH 478 ? ? 1_565 2.06 
2 1 O A HOH 406 ? ? 1_555 O A HOH 535 ? ? 1_565 2.15 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 CG A ARG 89 ? ? CD A ARG 89 ? ? NE  A ARG 89 ? ? 93.24  111.80 -18.56 2.10 N 
2 1 NE A ARG 89 ? ? CZ A ARG 89 ? ? NH2 A ARG 89 ? ? 115.28 120.30 -5.02  0.50 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASN A 11  ? ? -142.93 23.95   
2 1 ARG A 27  ? B -141.79 46.33   
3 1 LYS A 76  ? ? -91.56  -77.37  
4 1 LYS A 111 ? ? 74.67   -0.15   
5 1 ASN A 243 ? ? -99.79  46.57   
6 1 LYS A 251 ? ? 57.58   -137.92 
7 1 LYS A 251 ? ? 57.58   -130.85 
8 1 ASN A 252 ? B -101.00 59.54   
# 
_pdbx_entry_details.entry_id                 7NZR 
_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 687 ? 6.30 . 
2 1 O ? A HOH 688 ? 6.30 . 
# 
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 
4 1 Y 1 A HIS 4 ? A HIS 4 
5 1 Y 1 A TYR 7 ? A TYR 7 
6 1 Y 1 A GLY 8 ? A GLY 8 
7 1 Y 1 A LYS 9 ? A LYS 9 
# 
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 
V90 F18  F  N N 382 
V90 C5   C  Y N 383 
V90 C6   C  Y N 384 
V90 S12  S  N N 385 
V90 C13  C  N N 386 
V90 C14  C  N N 387 
V90 O15  O  N N 388 
V90 C1   C  Y N 389 
V90 F17  F  N N 390 
V90 C4   C  Y N 391 
V90 C3   C  Y N 392 
V90 S8   S  N N 393 
V90 O10  O  N N 394 
V90 N11  N  N N 395 
V90 O9   O  N N 396 
V90 C2   C  Y N 397 
V90 F16  F  N N 398 
V90 N7   N  N N 399 
V90 C19  C  N N 400 
V90 C26  C  N N 401 
V90 C25  C  N N 402 
V90 C24  C  N N 403 
V90 C23  C  N N 404 
V90 C22  C  N N 405 
V90 C21  C  N N 406 
V90 C20  C  N N 407 
V90 H1   H  N N 408 
V90 H2   H  N N 409 
V90 H3   H  N N 410 
V90 H4   H  N N 411 
V90 H5   H  N N 412 
V90 H6   H  N N 413 
V90 H7   H  N N 414 
V90 H8   H  N N 415 
V90 H9   H  N N 416 
V90 H10  H  N N 417 
V90 H11  H  N N 418 
V90 H12  H  N N 419 
V90 H13  H  N N 420 
V90 H14  H  N N 421 
V90 H15  H  N N 422 
V90 H16  H  N N 423 
V90 H17  H  N N 424 
V90 H18  H  N N 425 
V90 H19  H  N N 426 
V90 H20  H  N N 427 
V90 H21  H  N N 428 
V90 H22  H  N N 429 
V90 H23  H  N N 430 
VAL N    N  N N 431 
VAL CA   C  N S 432 
VAL C    C  N N 433 
VAL O    O  N N 434 
VAL CB   C  N N 435 
VAL CG1  C  N N 436 
VAL CG2  C  N N 437 
VAL OXT  O  N N 438 
VAL H    H  N N 439 
VAL H2   H  N N 440 
VAL HA   H  N N 441 
VAL HB   H  N N 442 
VAL HG11 H  N N 443 
VAL HG12 H  N N 444 
VAL HG13 H  N N 445 
VAL HG21 H  N N 446 
VAL HG22 H  N N 447 
VAL HG23 H  N N 448 
VAL HXT  H  N N 449 
ZN  ZN   ZN N N 450 
# 
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 
V90 C22 C23  sing N N 367 
V90 C22 C21  sing N N 368 
V90 C23 C24  sing N N 369 
V90 C24 C25  sing N N 370 
V90 O15 C14  sing N N 371 
V90 C21 C20  sing N N 372 
V90 C14 C13  sing N N 373 
V90 C25 C26  sing N N 374 
V90 C20 C19  sing N N 375 
V90 C13 S12  sing N N 376 
V90 C26 C19  sing N N 377 
V90 C19 N7   sing N N 378 
V90 F18 C5   sing N N 379 
V90 S12 C6   sing N N 380 
V90 C5  C6   doub Y N 381 
V90 C5  C4   sing Y N 382 
V90 N7  C4   sing N N 383 
V90 C6  C1   sing Y N 384 
V90 C4  C3   doub Y N 385 
V90 C1  F17  sing N N 386 
V90 C1  C2   doub Y N 387 
V90 C3  C2   sing Y N 388 
V90 C3  S8   sing N N 389 
V90 N11 S8   sing N N 390 
V90 C2  F16  sing N N 391 
V90 O10 S8   doub N N 392 
V90 S8  O9   doub N N 393 
V90 C13 H1   sing N N 394 
V90 C13 H2   sing N N 395 
V90 C14 H3   sing N N 396 
V90 C14 H4   sing N N 397 
V90 O15 H5   sing N N 398 
V90 N11 H6   sing N N 399 
V90 N11 H7   sing N N 400 
V90 N7  H8   sing N N 401 
V90 C19 H9   sing N N 402 
V90 C26 H10  sing N N 403 
V90 C26 H11  sing N N 404 
V90 C25 H12  sing N N 405 
V90 C25 H13  sing N N 406 
V90 C24 H14  sing N N 407 
V90 C24 H15  sing N N 408 
V90 C23 H16  sing N N 409 
V90 C23 H17  sing N N 410 
V90 C22 H18  sing N N 411 
V90 C22 H19  sing N N 412 
V90 C21 H20  sing N N 413 
V90 C21 H21  sing N N 414 
V90 C20 H22  sing N N 415 
V90 C20 H23  sing N N 416 
VAL N   CA   sing N N 417 
VAL N   H    sing N N 418 
VAL N   H2   sing N N 419 
VAL CA  C    sing N N 420 
VAL CA  CB   sing N N 421 
VAL CA  HA   sing N N 422 
VAL C   O    doub N N 423 
VAL C   OXT  sing N N 424 
VAL CB  CG1  sing N N 425 
VAL CB  CG2  sing N N 426 
VAL CB  HB   sing N N 427 
VAL CG1 HG11 sing N N 428 
VAL CG1 HG12 sing N N 429 
VAL CG1 HG13 sing N N 430 
VAL CG2 HG21 sing N N 431 
VAL CG2 HG22 sing N N 432 
VAL CG2 HG23 sing N N 433 
VAL OXT HXT  sing N N 434 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        V90 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   V90 
_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                    7NZR 
_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]   0.023627 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.005925 
_atom_sites.fract_transf_matrix[2][1]   -0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.024295 
_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]   0.014383 
_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   . TRP A 1 5   ? 30.285 1.077   10.446  1.00 55.61  ? 5   TRP A N   1 
ATOM   2    C  CA  . TRP A 1 5   ? 29.400 0.202   11.353  1.00 41.97  ? 5   TRP A CA  1 
ATOM   3    C  C   . TRP A 1 5   ? 28.348 -0.554  10.520  1.00 42.52  ? 5   TRP A C   1 
ATOM   4    O  O   . TRP A 1 5   ? 27.906 -0.037  9.507   1.00 32.77  ? 5   TRP A O   1 
ATOM   5    C  CB  . TRP A 1 5   ? 28.761 1.034   12.491  1.00 41.83  ? 5   TRP A CB  1 
ATOM   6    C  CG  . TRP A 1 5   ? 27.566 1.873   12.102  1.00 38.87  ? 5   TRP A CG  1 
ATOM   7    C  CD1 . TRP A 1 5   ? 27.539 3.223   11.861  1.00 47.36  ? 5   TRP A CD1 1 
ATOM   8    C  CD2 . TRP A 1 5   ? 26.183 1.441   12.027  1.00 34.09  ? 5   TRP A CD2 1 
ATOM   9    N  NE1 . TRP A 1 5   ? 26.253 3.639   11.579  1.00 36.78  ? 5   TRP A NE1 1 
ATOM   10   C  CE2 . TRP A 1 5   ? 25.399 2.563   11.657  1.00 30.80  ? 5   TRP A CE2 1 
ATOM   11   C  CE3 . TRP A 1 5   ? 25.540 0.187   12.097  1.00 29.61  ? 5   TRP A CE3 1 
ATOM   12   C  CZ2 . TRP A 1 5   ? 24.008 2.486   11.480  1.00 36.71  ? 5   TRP A CZ2 1 
ATOM   13   C  CZ3 . TRP A 1 5   ? 24.166 0.115   11.933  1.00 45.51  ? 5   TRP A CZ3 1 
ATOM   14   C  CH2 . TRP A 1 5   ? 23.409 1.241   11.600  1.00 46.19  ? 5   TRP A CH2 1 
ATOM   15   N  N   . GLY A 1 6   ? 27.879 -1.740  10.967  1.00 35.15  ? 6   GLY A N   1 
ATOM   16   C  CA  . GLY A 1 6   ? 26.738 -2.472  10.368  1.00 36.53  ? 6   GLY A CA  1 
ATOM   17   C  C   . GLY A 1 6   ? 26.433 -3.767  11.151  1.00 46.83  ? 6   GLY A C   1 
ATOM   18   O  O   . GLY A 1 6   ? 26.170 -3.648  12.364  1.00 38.76  ? 6   GLY A O   1 
ATOM   19   N  N   . HIS A 1 10  ? 32.651 -7.718  10.875  1.00 81.90  ? 10  HIS A N   1 
ATOM   20   C  CA  . HIS A 1 10  ? 33.790 -6.892  11.445  1.00 77.86  ? 10  HIS A CA  1 
ATOM   21   C  C   . HIS A 1 10  ? 33.310 -5.557  11.977  1.00 46.30  ? 10  HIS A C   1 
ATOM   22   O  O   . HIS A 1 10  ? 34.141 -4.852  12.577  1.00 37.06  ? 10  HIS A O   1 
ATOM   23   C  CB  . HIS A 1 10  ? 35.050 -6.890  10.547  1.00 100.05 ? 10  HIS A CB  1 
ATOM   24   C  CG  . HIS A 1 10  ? 35.694 -8.222  10.523  1.00 84.05  ? 10  HIS A CG  1 
ATOM   25   N  ND1 . HIS A 1 10  ? 36.782 -8.612  11.429  1.00 72.68  ? 10  HIS A ND1 1 
ATOM   26   C  CD2 . HIS A 1 10  ? 35.349 -9.383  9.868   1.00 86.01  ? 10  HIS A CD2 1 
ATOM   27   C  CE1 . HIS A 1 10  ? 37.040 -9.952  11.221  1.00 87.57  ? 10  HIS A CE1 1 
ATOM   28   N  NE2 . HIS A 1 10  ? 36.167 -10.408 10.284  1.00 69.60  ? 10  HIS A NE2 1 
ATOM   29   N  N   . ASN A 1 11  ? 31.984 -5.235  11.853  1.00 59.32  ? 11  ASN A N   1 
ATOM   30   C  CA  . ASN A 1 11  ? 31.453 -3.881  12.096  1.00 51.11  ? 11  ASN A CA  1 
ATOM   31   C  C   . ASN A 1 11  ? 30.069 -3.933  12.773  1.00 39.82  ? 11  ASN A C   1 
ATOM   32   O  O   . ASN A 1 11  ? 29.278 -2.977  12.790  1.00 30.45  ? 11  ASN A O   1 
ATOM   33   C  CB  . ASN A 1 11  ? 31.378 -3.051  10.816  1.00 54.67  ? 11  ASN A CB  1 
ATOM   34   C  CG  . ASN A 1 11  ? 30.278 -3.526  9.897   1.00 70.16  ? 11  ASN A CG  1 
ATOM   35   O  OD1 . ASN A 1 11  ? 29.519 -4.433  10.264  1.00 60.05  ? 11  ASN A OD1 1 
ATOM   36   N  ND2 . ASN A 1 11  ? 30.175 -2.920  8.720   1.00 56.73  ? 11  ASN A ND2 1 
ATOM   37   N  N   . GLY A 1 12  ? 29.847 -5.053  13.443  1.00 32.05  ? 12  GLY A N   1 
ATOM   38   C  CA  . GLY A 1 12  ? 28.594 -5.377  14.114  1.00 22.37  ? 12  GLY A CA  1 
ATOM   39   C  C   . GLY A 1 12  ? 28.470 -4.639  15.441  1.00 20.52  ? 12  GLY A C   1 
ATOM   40   O  O   . GLY A 1 12  ? 29.360 -3.912  15.868  1.00 18.63  ? 12  GLY A O   1 
ATOM   41   N  N   . PRO A 1 13  ? 27.383 -4.922  16.194  1.00 16.91  ? 13  PRO A N   1 
ATOM   42   C  CA  . PRO A 1 13  ? 27.098 -4.170  17.417  1.00 17.45  ? 13  PRO A CA  1 
ATOM   43   C  C   . PRO A 1 13  ? 28.185 -4.253  18.466  1.00 15.78  ? 13  PRO A C   1 
ATOM   44   O  O   . PRO A 1 13  ? 28.293 -3.322  19.229  1.00 16.26  ? 13  PRO A O   1 
ATOM   45   C  CB  . PRO A 1 13  ? 25.844 -4.896  17.962  1.00 22.23  ? 13  PRO A CB  1 
ATOM   46   C  CG  . PRO A 1 13  ? 25.133 -5.421  16.778  1.00 19.57  ? 13  PRO A CG  1 
ATOM   47   C  CD  . PRO A 1 13  ? 26.242 -5.728  15.799  1.00 16.12  ? 13  PRO A CD  1 
ATOM   48   N  N   . GLU A 1 14  ? 28.964 -5.341  18.477  1.00 16.97  ? 14  GLU A N   1 
ATOM   49   C  CA  . GLU A 1 14  ? 30.037 -5.458  19.449  1.00 19.10  ? 14  GLU A CA  1 
ATOM   50   C  C   . GLU A 1 14  ? 31.193 -4.474  19.199  1.00 17.17  ? 14  GLU A C   1 
ATOM   51   O  O   . GLU A 1 14  ? 32.064 -4.297  20.070  1.00 19.34  ? 14  GLU A O   1 
ATOM   52   C  CB  . GLU A 1 14  ? 30.508 -6.904  19.517  1.00 23.06  ? 14  GLU A CB  1 
ATOM   53   C  CG  . GLU A 1 14  ? 31.186 -7.343  18.200  1.00 26.96  ? 14  GLU A CG  1 
ATOM   54   C  CD  . GLU A 1 14  ? 30.410 -7.831  16.957  1.00 32.36  ? 14  GLU A CD  1 
ATOM   55   O  OE1 . GLU A 1 14  ? 29.213 -7.478  16.772  1.00 25.33  ? 14  GLU A OE1 1 
ATOM   56   O  OE2 . GLU A 1 14  ? 31.006 -8.559  16.143  1.00 49.66  ? 14  GLU A OE2 1 
ATOM   57   N  N   . HIS A 1 15  ? 31.186 -3.808  18.033  1.00 15.76  ? 15  HIS A N   1 
ATOM   58   C  CA  . HIS A 1 15  ? 32.250 -2.880  17.715  1.00 15.04  ? 15  HIS A CA  1 
ATOM   59   C  C   . HIS A 1 15  ? 31.846 -1.440  17.896  1.00 12.70  ? 15  HIS A C   1 
ATOM   60   O  O   . HIS A 1 15  ? 32.714 -0.570  17.922  1.00 14.54  ? 15  HIS A O   1 
ATOM   61   C  CB  . HIS A 1 15  ? 32.703 -3.068  16.271  1.00 15.48  ? 15  HIS A CB  1 
ATOM   62   C  CG  . HIS A 1 15  ? 33.372 -4.381  16.065  1.00 18.05  ? 15  HIS A CG  1 
ATOM   63   N  ND1 . HIS A 1 15  ? 34.709 -4.507  16.201  1.00 18.38  ? 15  HIS A ND1 1 
ATOM   64   C  CD2 . HIS A 1 15  ? 32.854 -5.604  15.715  1.00 20.23  ? 15  HIS A CD2 1 
ATOM   65   C  CE1 . HIS A 1 15  ? 35.021 -5.786  15.971  1.00 20.78  ? 15  HIS A CE1 1 
ATOM   66   N  NE2 . HIS A 1 15  ? 33.916 -6.486  15.701  1.00 23.83  ? 15  HIS A NE2 1 
ATOM   67   N  N   . TRP A 1 16  ? 30.546 -1.170  18.054  1.00 13.59  ? 16  TRP A N   1 
ATOM   68   C  CA  . TRP A 1 16  ? 30.084 0.204   17.989  1.00 13.18  ? 16  TRP A CA  1 
ATOM   69   C  C   . TRP A 1 16  ? 30.633 1.096   19.092  1.00 13.20  ? 16  TRP A C   1 
ATOM   70   O  O   . TRP A 1 16  ? 30.792 2.300   18.865  1.00 14.16  ? 16  TRP A O   1 
ATOM   71   C  CB  . TRP A 1 16  ? 28.535 0.192   18.079  1.00 14.94  ? 16  TRP A CB  1 
ATOM   72   C  CG  . TRP A 1 16  ? 27.880 -0.484  16.918  1.00 15.31  ? 16  TRP A CG  1 
ATOM   73   C  CD1 . TRP A 1 16  ? 28.439 -0.887  15.735  1.00 16.69  ? 16  TRP A CD1 1 
ATOM   74   C  CD2 . TRP A 1 16  ? 26.465 -0.810  16.817  1.00 13.26  ? 16  TRP A CD2 1 
ATOM   75   N  NE1 . TRP A 1 16  ? 27.467 -1.391  14.905  1.00 20.81  ? 16  TRP A NE1 1 
ATOM   76   C  CE2 . TRP A 1 16  ? 26.251 -1.338  15.520  1.00 16.52  ? 16  TRP A CE2 1 
ATOM   77   C  CE3 . TRP A 1 16  ? 25.372 -0.667  17.678  1.00 13.70  ? 16  TRP A CE3 1 
ATOM   78   C  CZ2 . TRP A 1 16  ? 24.996 -1.739  15.059  1.00 16.97  ? 16  TRP A CZ2 1 
ATOM   79   C  CZ3 . TRP A 1 16  ? 24.143 -1.090  17.238  1.00 13.95  ? 16  TRP A CZ3 1 
ATOM   80   C  CH2 . TRP A 1 16  ? 23.942 -1.603  15.953  1.00 16.44  ? 16  TRP A CH2 1 
ATOM   81   N  N   . HIS A 1 17  ? 30.968 0.522   20.263  1.00 12.92  ? 17  HIS A N   1 
ATOM   82   C  CA  . HIS A 1 17  ? 31.466 1.320   21.371  1.00 14.09  ? 17  HIS A CA  1 
ATOM   83   C  C   . HIS A 1 17  ? 32.741 2.075   20.977  1.00 14.75  ? 17  HIS A C   1 
ATOM   84   O  O   . HIS A 1 17  ? 33.022 3.094   21.604  1.00 16.26  ? 17  HIS A O   1 
ATOM   85   C  CB  . HIS A 1 17  ? 31.732 0.472   22.601  1.00 14.07  ? 17  HIS A CB  1 
ATOM   86   C  CG  . HIS A 1 17  ? 32.882 -0.425  22.436  1.00 15.08  ? 17  HIS A CG  1 
ATOM   87   N  ND1 . HIS A 1 17  ? 34.128 -0.121  22.980  1.00 16.94  ? 17  HIS A ND1 1 
ATOM   88   C  CD2 . HIS A 1 17  ? 33.007 -1.574  21.734  1.00 17.06  ? 17  HIS A CD2 1 
ATOM   89   C  CE1 . HIS A 1 17  ? 34.976 -1.079  22.693  1.00 19.82  ? 17  HIS A CE1 1 
ATOM   90   N  NE2 . HIS A 1 17  ? 34.328 -2.003  21.927  1.00 16.55  ? 17  HIS A NE2 1 
ATOM   91   N  N   . LYS A 1 18  ? 33.487 1.578   19.978  1.00 14.69  ? 18  LYS A N   1 
ATOM   92   C  CA  . LYS A 1 18  ? 34.740 2.277   19.671  1.00 16.44  ? 18  LYS A CA  1 
ATOM   93   C  C   . LYS A 1 18  ? 34.493 3.638   19.013  1.00 16.58  ? 18  LYS A C   1 
ATOM   94   O  O   . LYS A 1 18  ? 35.318 4.523   19.135  1.00 23.29  ? 18  LYS A O   1 
ATOM   95   C  CB  . LYS A 1 18  ? 35.578 1.373   18.767  1.00 16.24  ? 18  LYS A CB  1 
ATOM   96   C  CG  . LYS A 1 18  ? 36.212 0.166   19.477  1.00 18.39  ? 18  LYS A CG  1 
ATOM   97   C  CD  . LYS A 1 18  ? 36.920 -0.778  18.534  1.00 17.28  ? 18  LYS A CD  1 
ATOM   98   C  CE  . LYS A 1 18  ? 35.925 -1.701  17.842  1.00 15.43  ? 18  LYS A CE  1 
ATOM   99   N  NZ  . LYS A 1 18  ? 36.580 -2.509  16.798  1.00 15.71  ? 18  LYS A NZ  1 
ATOM   100  N  N   . ASP A 1 19  ? 33.398 3.777   18.289  1.00 16.79  ? 19  ASP A N   1 
ATOM   101  C  CA  . ASP A 1 19  ? 33.041 5.053   17.691  1.00 16.18  ? 19  ASP A CA  1 
ATOM   102  C  C   . ASP A 1 19  ? 32.048 5.815   18.537  1.00 16.42  ? 19  ASP A C   1 
ATOM   103  O  O   . ASP A 1 19  ? 31.989 7.031   18.413  1.00 18.97  ? 19  ASP A O   1 
ATOM   104  C  CB  . ASP A 1 19  ? 32.501 4.864   16.276  1.00 20.49  ? 19  ASP A CB  1 
ATOM   105  C  CG  . ASP A 1 19  ? 33.624 4.482   15.336  1.00 28.61  ? 19  ASP A CG  1 
ATOM   106  O  OD1 . ASP A 1 19  ? 34.487 5.320   15.082  1.00 31.21  ? 19  ASP A OD1 1 
ATOM   107  O  OD2 . ASP A 1 19  ? 33.722 3.283   15.005  1.00 37.91  ? 19  ASP A OD2 1 
ATOM   108  N  N   . PHE A 1 20  ? 31.237 5.086   19.325  1.00 13.56  ? 20  PHE A N   1 
ATOM   109  C  CA  . PHE A 1 20  ? 30.144 5.689   20.073  1.00 14.96  ? 20  PHE A CA  1 
ATOM   110  C  C   . PHE A 1 20  ? 30.237 5.134   21.490  1.00 14.75  ? 20  PHE A C   1 
ATOM   111  O  O   . PHE A 1 20  ? 29.573 4.119   21.798  1.00 15.49  ? 20  PHE A O   1 
ATOM   112  C  CB  . PHE A 1 20  ? 28.783 5.309   19.441  1.00 17.48  ? 20  PHE A CB  1 
ATOM   113  C  CG  . PHE A 1 20  ? 28.725 5.800   18.019  1.00 20.78  ? 20  PHE A CG  1 
ATOM   114  C  CD1 . PHE A 1 20  ? 28.416 7.114   17.749  1.00 25.73  ? 20  PHE A CD1 1 
ATOM   115  C  CD2 . PHE A 1 20  ? 29.133 4.975   16.976  1.00 20.40  ? 20  PHE A CD2 1 
ATOM   116  C  CE1 . PHE A 1 20  ? 28.485 7.579   16.448  1.00 25.65  ? 20  PHE A CE1 1 
ATOM   117  C  CE2 . PHE A 1 20  ? 29.136 5.419   15.671  1.00 25.81  ? 20  PHE A CE2 1 
ATOM   118  C  CZ  . PHE A 1 20  ? 28.766 6.707   15.427  1.00 24.03  ? 20  PHE A CZ  1 
ATOM   119  N  N   . PRO A 1 21  ? 31.040 5.736   22.392  1.00 14.20  ? 21  PRO A N   1 
ATOM   120  C  CA  . PRO A 1 21  ? 31.256 5.161   23.720  1.00 15.38  ? 21  PRO A CA  1 
ATOM   121  C  C   . PRO A 1 21  ? 29.995 5.030   24.555  1.00 13.99  ? 21  PRO A C   1 
ATOM   122  O  O   . PRO A 1 21  ? 29.947 4.206   25.474  1.00 14.64  ? 21  PRO A O   1 
ATOM   123  C  CB  . PRO A 1 21  ? 32.235 6.150   24.416  1.00 17.46  ? 21  PRO A CB  1 
ATOM   124  C  CG  . PRO A 1 21  ? 32.628 7.132   23.390  1.00 24.66  ? 21  PRO A CG  1 
ATOM   125  C  CD  . PRO A 1 21  ? 31.928 6.872   22.087  1.00 17.55  ? 21  PRO A CD  1 
ATOM   126  N  N   . ILE A 1 22  ? 28.934 5.772   24.203  1.00 13.92  ? 22  ILE A N   1 
ATOM   127  C  CA  . ILE A 1 22  ? 27.651 5.630   24.893  1.00 13.18  ? 22  ILE A CA  1 
ATOM   128  C  C   . ILE A 1 22  ? 27.083 4.229   24.698  1.00 11.89  ? 22  ILE A C   1 
ATOM   129  O  O   . ILE A 1 22  ? 26.171 3.847   25.432  1.00 12.60  ? 22  ILE A O   1 
ATOM   130  C  CB  . ILE A 1 22  ? 26.658 6.707   24.470  1.00 12.71  ? 22  ILE A CB  1 
ATOM   131  C  CG1 . ILE A 1 22  ? 25.576 6.926   25.507  1.00 15.35  ? 22  ILE A CG1 1 
ATOM   132  C  CG2 . ILE A 1 22  ? 26.125 6.404   23.083  1.00 14.07  ? 22  ILE A CG2 1 
ATOM   133  C  CD1 . ILE A 1 22  ? 26.055 7.476   26.846  1.00 20.93  ? 22  ILE A CD1 1 
ATOM   134  N  N   . ALA A 1 23  ? 27.627 3.428   23.781  1.00 12.54  ? 23  ALA A N   1 
ATOM   135  C  CA  . ALA A 1 23  ? 27.196 2.040   23.616  1.00 12.48  ? 23  ALA A CA  1 
ATOM   136  C  C   . ALA A 1 23  ? 27.288 1.276   24.930  1.00 12.29  ? 23  ALA A C   1 
ATOM   137  O  O   . ALA A 1 23  ? 26.578 0.262   25.076  1.00 13.39  ? 23  ALA A O   1 
ATOM   138  C  CB  . ALA A 1 23  ? 27.985 1.344   22.530  1.00 12.69  ? 23  ALA A CB  1 
ATOM   139  N  N   . LYS A 1 24  ? 28.177 1.682   25.851  1.00 12.44  ? 24  LYS A N   1 
ATOM   140  C  CA  . LYS A 1 24  ? 28.349 1.046   27.159  1.00 14.69  ? 24  LYS A CA  1 
ATOM   141  C  C   . LYS A 1 24  ? 27.756 1.915   28.252  1.00 15.26  ? 24  LYS A C   1 
ATOM   142  O  O   . LYS A 1 24  ? 28.181 1.791   29.422  1.00 19.00  ? 24  LYS A O   1 
ATOM   143  C  CB  . LYS A 1 24  ? 29.837 0.806   27.404  1.00 16.98  ? 24  LYS A CB  1 
ATOM   144  C  CG  . LYS A 1 24  ? 30.436 -0.185  26.433  1.00 19.43  ? 24  LYS A CG  1 
ATOM   145  C  CD  . LYS A 1 24  ? 31.862 -0.428  26.736  1.00 26.28  ? 24  LYS A CD  1 
ATOM   146  C  CE  . LYS A 1 24  ? 32.570 -1.406  25.810  1.00 27.45  ? 24  LYS A CE  1 
ATOM   147  N  NZ  . LYS A 1 24  ? 32.244 -2.810  26.111  1.00 35.56  ? 24  LYS A NZ  1 
ATOM   148  N  N   . GLY A 1 25  ? 26.751 2.723   27.882  1.00 14.23  ? 25  GLY A N   1 
ATOM   149  C  CA  . GLY A 1 25  ? 26.135 3.682   28.805  1.00 14.77  ? 25  GLY A CA  1 
ATOM   150  C  C   . GLY A 1 25  ? 25.125 3.030   29.732  1.00 12.62  ? 25  GLY A C   1 
ATOM   151  O  O   . GLY A 1 25  ? 24.961 1.821   29.803  1.00 14.16  ? 25  GLY A O   1 
ATOM   152  N  N   . GLU A 1 26  ? 24.439 3.882   30.491  1.00 14.04  ? 26  GLU A N   1 
ATOM   153  C  CA  . GLU A 1 26  ? 23.558 3.423   31.561  1.00 15.36  ? 26  GLU A CA  1 
ATOM   154  C  C   . GLU A 1 26  ? 22.092 3.262   31.137  1.00 12.16  ? 26  GLU A C   1 
ATOM   155  O  O   . GLU A 1 26  ? 21.279 2.728   31.923  1.00 14.89  ? 26  GLU A O   1 
ATOM   156  C  CB  . GLU A 1 26  ? 23.560 4.433   32.726  1.00 19.57  ? 26  GLU A CB  1 
ATOM   157  C  CG  . GLU A 1 26  ? 24.972 4.671   33.325  1.00 27.41  ? 26  GLU A CG  1 
ATOM   158  C  CD  . GLU A 1 26  ? 25.657 3.389   33.813  1.00 31.06  ? 26  GLU A CD  1 
ATOM   159  O  OE1 . GLU A 1 26  ? 25.039 2.670   34.649  1.00 33.67  ? 26  GLU A OE1 1 
ATOM   160  O  OE2 . GLU A 1 26  ? 26.815 3.093   33.341  1.00 38.85  ? 26  GLU A OE2 1 
ATOM   161  N  N   A ARG A 1 27  ? 21.717 3.684   29.918  0.50 11.27  ? 27  ARG A N   1 
ATOM   162  N  N   B ARG A 1 27  ? 21.778 3.609   29.885  0.50 11.78  ? 27  ARG A N   1 
ATOM   163  C  CA  A ARG A 1 27  ? 20.323 3.516   29.480  0.50 10.28  ? 27  ARG A CA  1 
ATOM   164  C  CA  B ARG A 1 27  ? 20.383 3.577   29.443  0.50 10.52  ? 27  ARG A CA  1 
ATOM   165  C  C   A ARG A 1 27  ? 20.257 3.027   28.031  0.50 9.43   ? 27  ARG A C   1 
ATOM   166  C  C   B ARG A 1 27  ? 20.315 3.072   27.997  0.50 10.42  ? 27  ARG A C   1 
ATOM   167  O  O   A ARG A 1 27  ? 19.758 3.802   27.191  0.50 10.11  ? 27  ARG A O   1 
ATOM   168  O  O   B ARG A 1 27  ? 19.670 3.661   27.132  0.50 11.06  ? 27  ARG A O   1 
ATOM   169  C  CB  A ARG A 1 27  ? 19.430 4.734   29.785  0.50 11.43  ? 27  ARG A CB  1 
ATOM   170  C  CB  B ARG A 1 27  ? 19.765 4.971   29.595  0.50 12.30  ? 27  ARG A CB  1 
ATOM   171  C  CG  A ARG A 1 27  ? 19.817 6.068   29.153  0.50 12.76  ? 27  ARG A CG  1 
ATOM   172  C  CG  B ARG A 1 27  ? 19.995 5.695   30.926  0.50 14.72  ? 27  ARG A CG  1 
ATOM   173  C  CD  A ARG A 1 27  ? 18.846 7.271   29.322  0.50 15.94  ? 27  ARG A CD  1 
ATOM   174  C  CD  B ARG A 1 27  ? 19.344 7.081   30.907  0.50 15.68  ? 27  ARG A CD  1 
ATOM   175  N  NE  A ARG A 1 27  ? 17.661 7.145   28.449  0.50 13.46  ? 27  ARG A NE  1 
ATOM   176  N  NE  B ARG A 1 27  ? 19.775 7.865   32.073  0.50 18.17  ? 27  ARG A NE  1 
ATOM   177  C  CZ  A ARG A 1 27  ? 16.767 8.107   28.250  0.50 11.77  ? 27  ARG A CZ  1 
ATOM   178  C  CZ  B ARG A 1 27  ? 20.855 8.637   32.103  0.50 15.93  ? 27  ARG A CZ  1 
ATOM   179  N  NH1 A ARG A 1 27  ? 16.907 9.274   28.854  0.50 8.49   ? 27  ARG A NH1 1 
ATOM   180  N  NH1 B ARG A 1 27  ? 21.627 8.737   31.033  0.50 23.85  ? 27  ARG A NH1 1 
ATOM   181  N  NH2 A ARG A 1 27  ? 15.739 7.899   27.447  0.50 13.18  ? 27  ARG A NH2 1 
ATOM   182  N  NH2 B ARG A 1 27  ? 21.162 9.305   33.200  0.50 23.33  ? 27  ARG A NH2 1 
ATOM   183  N  N   . GLN A 1 28  ? 21.036 1.987   27.706  1.00 8.95   ? 28  GLN A N   1 
ATOM   184  C  CA  . GLN A 1 28  ? 21.074 1.441   26.347  1.00 9.02   ? 28  GLN A CA  1 
ATOM   185  C  C   . GLN A 1 28  ? 19.928 0.466   26.068  1.00 8.27   ? 28  GLN A C   1 
ATOM   186  O  O   . GLN A 1 28  ? 19.442 -0.218  26.974  1.00 10.14  ? 28  GLN A O   1 
ATOM   187  C  CB  . GLN A 1 28  ? 22.431 0.767   26.102  1.00 9.79   ? 28  GLN A CB  1 
ATOM   188  C  CG  . GLN A 1 28  ? 23.554 1.826   26.073  1.00 9.77   ? 28  GLN A CG  1 
ATOM   189  C  CD  . GLN A 1 28  ? 23.477 2.623   24.784  1.00 9.42   ? 28  GLN A CD  1 
ATOM   190  O  OE1 . GLN A 1 28  ? 23.676 2.106   23.691  1.00 9.88   ? 28  GLN A OE1 1 
ATOM   191  N  NE2 . GLN A 1 28  ? 23.104 3.896   24.880  1.00 10.40  ? 28  GLN A NE2 1 
ATOM   192  N  N   . SER A 1 29  ? 19.536 0.425   24.785  1.00 8.28   ? 29  SER A N   1 
ATOM   193  C  CA  . SER A 1 29  ? 18.481 -0.445  24.310  1.00 8.01   ? 29  SER A CA  1 
ATOM   194  C  C   . SER A 1 29  ? 19.015 -1.296  23.200  1.00 7.72   ? 29  SER A C   1 
ATOM   195  O  O   . SER A 1 29  ? 19.995 -0.992  22.544  1.00 9.25   ? 29  SER A O   1 
ATOM   196  C  CB  . SER A 1 29  ? 17.327 0.437   23.757  1.00 8.27   ? 29  SER A CB  1 
ATOM   197  O  OG  . SER A 1 29  ? 16.719 1.159   24.834  1.00 8.75   ? 29  SER A OG  1 
ATOM   198  N  N   . PRO A 1 30  ? 18.343 -2.416  22.888  1.00 7.93   ? 30  PRO A N   1 
ATOM   199  C  CA  . PRO A 1 30  ? 17.161 -2.960  23.603  1.00 8.40   ? 30  PRO A CA  1 
ATOM   200  C  C   . PRO A 1 30  ? 17.572 -3.649  24.890  1.00 8.01   ? 30  PRO A C   1 
ATOM   201  O  O   . PRO A 1 30  ? 18.760 -3.673  25.243  1.00 8.93   ? 30  PRO A O   1 
ATOM   202  C  CB  . PRO A 1 30  ? 16.626 -3.947  22.568  1.00 8.35   ? 30  PRO A CB  1 
ATOM   203  C  CG  . PRO A 1 30  ? 17.895 -4.550  21.986  1.00 8.84   ? 30  PRO A CG  1 
ATOM   204  C  CD  . PRO A 1 30  ? 18.825 -3.351  21.839  1.00 8.52   ? 30  PRO A CD  1 
ATOM   205  N  N   . VAL A 1 31  ? 16.563 -4.174  25.597  1.00 9.05   ? 31  VAL A N   1 
ATOM   206  C  CA  . VAL A 1 31  ? 16.788 -4.895  26.809  1.00 9.20   ? 31  VAL A CA  1 
ATOM   207  C  C   . VAL A 1 31  ? 15.915 -6.144  26.750  1.00 9.19   ? 31  VAL A C   1 
ATOM   208  O  O   . VAL A 1 31  ? 14.933 -6.212  26.022  1.00 9.73   ? 31  VAL A O   1 
ATOM   209  C  CB  . VAL A 1 31  ? 16.451 -4.105  28.100  1.00 9.04   ? 31  VAL A CB  1 
ATOM   210  C  CG1 . VAL A 1 31  ? 17.381 -2.862  28.193  1.00 11.12  ? 31  VAL A CG1 1 
ATOM   211  C  CG2 . VAL A 1 31  ? 14.967 -3.734  28.120  1.00 10.85  ? 31  VAL A CG2 1 
ATOM   212  N  N   . ASP A 1 32  ? 16.244 -7.109  27.625  1.00 9.68   ? 32  ASP A N   1 
ATOM   213  C  CA  . ASP A 1 32  ? 15.343 -8.218  27.920  1.00 10.13  ? 32  ASP A CA  1 
ATOM   214  C  C   . ASP A 1 32  ? 14.277 -7.735  28.896  1.00 10.02  ? 32  ASP A C   1 
ATOM   215  O  O   . ASP A 1 32  ? 14.583 -7.049  29.906  1.00 12.15  ? 32  ASP A O   1 
ATOM   216  C  CB  . ASP A 1 32  ? 16.088 -9.423  28.531  1.00 11.11  ? 32  ASP A CB  1 
ATOM   217  C  CG  . ASP A 1 32  ? 15.106 -10.563 28.799  1.00 12.77  ? 32  ASP A CG  1 
ATOM   218  O  OD1 . ASP A 1 32  ? 14.419 -10.997 27.868  1.00 12.24  ? 32  ASP A OD1 1 
ATOM   219  O  OD2 . ASP A 1 32  ? 15.075 -10.998 29.969  1.00 14.83  ? 32  ASP A OD2 1 
ATOM   220  N  N   . ILE A 1 33  ? 13.019 -8.016  28.566  1.00 9.68   ? 33  ILE A N   1 
ATOM   221  C  CA  . ILE A 1 33  ? 11.916 -7.616  29.460  1.00 11.12  ? 33  ILE A CA  1 
ATOM   222  C  C   . ILE A 1 33  ? 11.614 -8.885  30.288  1.00 11.49  ? 33  ILE A C   1 
ATOM   223  O  O   . ILE A 1 33  ? 11.027 -9.856  29.808  1.00 13.22  ? 33  ILE A O   1 
ATOM   224  C  CB  . ILE A 1 33  ? 10.708 -7.185  28.634  1.00 11.58  ? 33  ILE A CB  1 
ATOM   225  C  CG1 . ILE A 1 33  ? 11.060 -5.968  27.790  1.00 11.61  ? 33  ILE A CG1 1 
ATOM   226  C  CG2 . ILE A 1 33  ? 9.506  -6.928  29.571  1.00 12.96  ? 33  ILE A CG2 1 
ATOM   227  C  CD1 . ILE A 1 33  ? 10.016 -5.690  26.710  1.00 13.43  ? 33  ILE A CD1 1 
ATOM   228  N  N   . ASP A 1 34  ? 11.985 -8.812  31.565  1.00 13.17  ? 34  ASP A N   1 
ATOM   229  C  CA  . ASP A 1 34  ? 11.701 -9.893  32.513  1.00 13.65  ? 34  ASP A CA  1 
ATOM   230  C  C   . ASP A 1 34  ? 10.294 -9.612  33.044  1.00 14.89  ? 34  ASP A C   1 
ATOM   231  O  O   . ASP A 1 34  ? 10.074 -8.658  33.823  1.00 16.98  ? 34  ASP A O   1 
ATOM   232  C  CB  . ASP A 1 34  ? 12.737 -9.871  33.652  1.00 16.57  ? 34  ASP A CB  1 
ATOM   233  C  CG  . ASP A 1 34  ? 12.509 -10.921 34.781  1.00 21.22  ? 34  ASP A CG  1 
ATOM   234  O  OD1 . ASP A 1 34  ? 11.416 -11.393 34.930  1.00 20.89  ? 34  ASP A OD1 1 
ATOM   235  O  OD2 . ASP A 1 34  ? 13.449 -11.163 35.576  1.00 35.61  ? 34  ASP A OD2 1 
ATOM   236  N  N   . THR A 1 35  ? 9.326  -10.378 32.526  1.00 16.61  ? 35  THR A N   1 
ATOM   237  C  CA  . THR A 1 35  ? 7.947  -10.105 32.838  1.00 18.47  ? 35  THR A CA  1 
ATOM   238  C  C   . THR A 1 35  ? 7.607  -10.221 34.312  1.00 19.07  ? 35  THR A C   1 
ATOM   239  O  O   . THR A 1 35  ? 6.624  -9.652  34.752  1.00 20.99  ? 35  THR A O   1 
ATOM   240  C  CB  . THR A 1 35  ? 7.027  -10.978 31.992  1.00 20.48  ? 35  THR A CB  1 
ATOM   241  O  OG1 . THR A 1 35  ? 7.161  -12.314 32.457  1.00 21.32  ? 35  THR A OG1 1 
ATOM   242  C  CG2 . THR A 1 35  ? 7.252  -10.876 30.501  1.00 22.40  ? 35  THR A CG2 1 
ATOM   243  N  N   . HIS A 1 36  ? 8.418  -11.011 35.057  1.00 18.69  ? 36  HIS A N   1 
ATOM   244  C  CA  . HIS A 1 36  ? 8.185  -11.284 36.505  1.00 21.19  ? 36  HIS A CA  1 
ATOM   245  C  C   . HIS A 1 36  ? 8.705  -10.177 37.390  1.00 31.37  ? 36  HIS A C   1 
ATOM   246  O  O   . HIS A 1 36  ? 8.177  -10.025 38.499  1.00 50.49  ? 36  HIS A O   1 
ATOM   247  C  CB  . HIS A 1 36  ? 8.901  -12.601 36.909  1.00 22.11  ? 36  HIS A CB  1 
ATOM   248  C  CG  . HIS A 1 36  ? 8.361  -13.670 36.059  1.00 25.10  ? 36  HIS A CG  1 
ATOM   249  N  ND1 . HIS A 1 36  ? 9.049  -14.281 34.962  1.00 35.80  ? 36  HIS A ND1 1 
ATOM   250  C  CD2 . HIS A 1 36  ? 7.109  -14.142 36.070  1.00 23.41  ? 36  HIS A CD2 1 
ATOM   251  C  CE1 . HIS A 1 36  ? 8.246  -15.196 34.449  1.00 23.97  ? 36  HIS A CE1 1 
ATOM   252  N  NE2 . HIS A 1 36  ? 7.042  -15.139 35.141  1.00 28.05  ? 36  HIS A NE2 1 
ATOM   253  N  N   . THR A 1 37  ? 9.654  -9.396  36.902  1.00 20.06  ? 37  THR A N   1 
ATOM   254  C  CA  . THR A 1 37  ? 10.174 -8.236  37.634  1.00 23.47  ? 37  THR A CA  1 
ATOM   255  C  C   . THR A 1 37  ? 9.681  -6.872  37.153  1.00 21.83  ? 37  THR A C   1 
ATOM   256  O  O   . THR A 1 37  ? 9.841  -5.860  37.870  1.00 27.61  ? 37  THR A O   1 
ATOM   257  C  CB  . THR A 1 37  ? 11.689 -8.309  37.807  1.00 31.91  ? 37  THR A CB  1 
ATOM   258  O  OG1 . THR A 1 37  ? 12.280 -8.268  36.542  1.00 33.43  ? 37  THR A OG1 1 
ATOM   259  C  CG2 . THR A 1 37  ? 12.119 -9.670  38.300  1.00 33.69  ? 37  THR A CG2 1 
ATOM   260  N  N   . ALA A 1 38  ? 8.957  -6.819  36.031  1.00 17.14  ? 38  ALA A N   1 
ATOM   261  C  CA  . ALA A 1 38  ? 8.341  -5.568  35.592  1.00 18.54  ? 38  ALA A CA  1 
ATOM   262  C  C   . ALA A 1 38  ? 7.217  -5.288  36.563  1.00 22.37  ? 38  ALA A C   1 
ATOM   263  O  O   . ALA A 1 38  ? 6.469  -6.160  36.943  1.00 30.80  ? 38  ALA A O   1 
ATOM   264  C  CB  . ALA A 1 38  ? 7.770  -5.687  34.204  1.00 17.89  ? 38  ALA A CB  1 
ATOM   265  N  N   . LYS A 1 39  ? 7.083  -4.046  36.965  1.00 21.42  ? 39  LYS A N   1 
ATOM   266  C  CA  . LYS A 1 39  ? 6.128  -3.616  37.989  1.00 24.78  ? 39  LYS A CA  1 
ATOM   267  C  C   . LYS A 1 39  ? 4.906  -3.006  37.318  1.00 15.68  ? 39  LYS A C   1 
ATOM   268  O  O   . LYS A 1 39  ? 5.040  -2.009  36.583  1.00 16.13  ? 39  LYS A O   1 
ATOM   269  C  CB  . LYS A 1 39  ? 6.834  -2.495  38.752  1.00 36.64  ? 39  LYS A CB  1 
ATOM   270  C  CG  . LYS A 1 39  ? 5.939  -1.645  39.629  1.00 53.09  ? 39  LYS A CG  1 
ATOM   271  C  CD  . LYS A 1 39  ? 5.749  -2.337  40.935  1.00 51.23  ? 39  LYS A CD  1 
ATOM   272  C  CE  . LYS A 1 39  ? 5.504  -1.386  42.076  1.00 59.03  ? 39  LYS A CE  1 
ATOM   273  N  NZ  . LYS A 1 39  ? 4.681  -2.120  43.123  1.00 42.40  ? 39  LYS A NZ  1 
ATOM   274  N  N   . TYR A 1 40  ? 3.690  -3.497  37.641  1.00 18.60  ? 40  TYR A N   1 
ATOM   275  C  CA  . TYR A 1 40  ? 2.442  -2.862  37.243  1.00 17.63  ? 40  TYR A CA  1 
ATOM   276  C  C   . TYR A 1 40  ? 2.519  -1.485  37.874  1.00 16.07  ? 40  TYR A C   1 
ATOM   277  O  O   . TYR A 1 40  ? 2.664  -1.350  39.109  1.00 18.50  ? 40  TYR A O   1 
ATOM   278  C  CB  . TYR A 1 40  ? 1.160  -3.607  37.684  1.00 23.19  ? 40  TYR A CB  1 
ATOM   279  C  CG  . TYR A 1 40  ? -0.101 -2.808  37.544  1.00 36.68  ? 40  TYR A CG  1 
ATOM   280  C  CD1 . TYR A 1 40  ? -0.555 -2.407  36.299  1.00 29.95  ? 40  TYR A CD1 1 
ATOM   281  C  CD2 . TYR A 1 40  ? -0.898 -2.511  38.650  1.00 41.63  ? 40  TYR A CD2 1 
ATOM   282  C  CE1 . TYR A 1 40  ? -1.725 -1.704  36.114  1.00 51.85  ? 40  TYR A CE1 1 
ATOM   283  C  CE2 . TYR A 1 40  ? -2.053 -1.775  38.475  1.00 73.44  ? 40  TYR A CE2 1 
ATOM   284  C  CZ  . TYR A 1 40  ? -2.469 -1.373  37.220  1.00 67.20  ? 40  TYR A CZ  1 
ATOM   285  O  OH  . TYR A 1 40  ? -3.588 -0.649  36.986  1.00 52.11  ? 40  TYR A OH  1 
ATOM   286  N  N   . ASP A 1 41  ? 2.237  -0.499  37.053  1.00 16.01  ? 41  ASP A N   1 
ATOM   287  C  CA  . ASP A 1 41  ? 2.191  0.875   37.536  1.00 17.62  ? 41  ASP A CA  1 
ATOM   288  C  C   . ASP A 1 41  ? 0.785  1.438   37.368  1.00 22.68  ? 41  ASP A C   1 
ATOM   289  O  O   . ASP A 1 41  ? 0.491  1.819   36.228  1.00 22.64  ? 41  ASP A O   1 
ATOM   290  C  CB  . ASP A 1 41  ? 3.204  1.737   36.768  1.00 20.24  ? 41  ASP A CB  1 
ATOM   291  C  CG  . ASP A 1 41  ? 3.322  3.141   37.300  1.00 26.50  ? 41  ASP A CG  1 
ATOM   292  O  OD1 . ASP A 1 41  ? 2.478  3.522   38.126  1.00 29.13  ? 41  ASP A OD1 1 
ATOM   293  O  OD2 . ASP A 1 41  ? 4.283  3.816   36.921  1.00 31.18  ? 41  ASP A OD2 1 
ATOM   294  N  N   . PRO A 1 42  ? -0.075 1.515   38.465  1.00 37.76  ? 42  PRO A N   1 
ATOM   295  C  CA  . PRO A 1 42  ? -1.460 1.808   38.180  1.00 33.23  ? 42  PRO A CA  1 
ATOM   296  C  C   . PRO A 1 42  ? -1.585 3.277   37.786  1.00 35.96  ? 42  PRO A C   1 
ATOM   297  O  O   . PRO A 1 42  ? -2.643 3.724   37.275  1.00 55.09  ? 42  PRO A O   1 
ATOM   298  C  CB  . PRO A 1 42  ? -2.094 1.488   39.542  1.00 43.35  ? 42  PRO A CB  1 
ATOM   299  C  CG  . PRO A 1 42  ? -0.980 1.676   40.568  1.00 52.46  ? 42  PRO A CG  1 
ATOM   300  C  CD  . PRO A 1 42  ? 0.262  1.139   39.891  1.00 42.54  ? 42  PRO A CD  1 
ATOM   301  N  N   . SER A 1 43  ? -0.510 4.046   38.040  1.00 28.59  ? 43  SER A N   1 
ATOM   302  C  CA  . SER A 1 43  ? -0.565 5.452   37.651  1.00 33.16  ? 43  SER A CA  1 
ATOM   303  C  C   . SER A 1 43  ? -0.331 5.735   36.149  1.00 38.87  ? 43  SER A C   1 
ATOM   304  O  O   . SER A 1 43  ? -0.566 6.870   35.685  1.00 47.21  ? 43  SER A O   1 
ATOM   305  C  CB  . SER A 1 43  ? 0.415  6.220   38.463  1.00 45.93  ? 43  SER A CB  1 
ATOM   306  O  OG  . SER A 1 43  ? 1.627  6.362   37.753  1.00 37.81  ? 43  SER A OG  1 
ATOM   307  N  N   . LEU A 1 44  ? 0.183  4.774   35.361  1.00 33.02  ? 44  LEU A N   1 
ATOM   308  C  CA  . LEU A 1 44  ? 0.360  5.063   33.939  1.00 30.74  ? 44  LEU A CA  1 
ATOM   309  C  C   . LEU A 1 44  ? -0.989 5.494   33.368  1.00 39.01  ? 44  LEU A C   1 
ATOM   310  O  O   . LEU A 1 44  ? -1.974 4.759   33.562  1.00 40.26  ? 44  LEU A O   1 
ATOM   311  C  CB  . LEU A 1 44  ? 0.953  3.828   33.242  1.00 26.08  ? 44  LEU A CB  1 
ATOM   312  C  CG  . LEU A 1 44  ? 2.445  3.563   33.469  1.00 19.90  ? 44  LEU A CG  1 
ATOM   313  C  CD1 . LEU A 1 44  ? 2.789  2.142   33.028  1.00 22.41  ? 44  LEU A CD1 1 
ATOM   314  C  CD2 . LEU A 1 44  ? 3.235  4.563   32.666  1.00 19.84  ? 44  LEU A CD2 1 
ATOM   315  N  N   . LYS A 1 45  ? -1.003 6.697   32.722  1.00 34.70  ? 45  LYS A N   1 
ATOM   316  C  CA  . LYS A 1 45  ? -2.207 7.373   32.229  1.00 31.32  ? 45  LYS A CA  1 
ATOM   317  C  C   . LYS A 1 45  ? -2.565 6.627   30.971  1.00 26.78  ? 45  LYS A C   1 
ATOM   318  O  O   . LYS A 1 45  ? -1.783 5.905   30.406  1.00 27.53  ? 45  LYS A O   1 
ATOM   319  C  CB  . LYS A 1 45  ? -2.042 8.854   31.842  1.00 29.15  ? 45  LYS A CB  1 
ATOM   320  C  CG  . LYS A 1 45  ? -1.692 9.857   32.946  1.00 40.16  ? 45  LYS A CG  1 
ATOM   321  C  CD  . LYS A 1 45  ? -1.885 11.293  32.493  1.00 50.21  ? 45  LYS A CD  1 
ATOM   322  N  N   . PRO A 1 46  ? -3.781 6.643   30.444  1.00 23.97  ? 46  PRO A N   1 
ATOM   323  C  CA  . PRO A 1 46  ? -4.047 5.787   29.258  1.00 29.52  ? 46  PRO A CA  1 
ATOM   324  C  C   . PRO A 1 46  ? -3.175 6.224   28.051  1.00 27.49  ? 46  PRO A C   1 
ATOM   325  O  O   . PRO A 1 46  ? -2.920 7.426   27.837  1.00 26.35  ? 46  PRO A O   1 
ATOM   326  C  CB  . PRO A 1 46  ? -5.549 6.078   28.992  1.00 36.03  ? 46  PRO A CB  1 
ATOM   327  C  CG  . PRO A 1 46  ? -6.083 6.513   30.388  1.00 40.00  ? 46  PRO A CG  1 
ATOM   328  C  CD  . PRO A 1 46  ? -4.960 7.297   31.049  1.00 31.46  ? 46  PRO A CD  1 
ATOM   329  N  N   . LEU A 1 47  ? -2.767 5.252   27.247  1.00 21.65  ? 47  LEU A N   1 
ATOM   330  C  CA  . LEU A 1 47  ? -2.003 5.458   25.995  1.00 22.28  ? 47  LEU A CA  1 
ATOM   331  C  C   . LEU A 1 47  ? -2.956 5.792   24.839  1.00 18.65  ? 47  LEU A C   1 
ATOM   332  O  O   . LEU A 1 47  ? -3.956 5.111   24.579  1.00 22.58  ? 47  LEU A O   1 
ATOM   333  C  CB  . LEU A 1 47  ? -1.274 4.176   25.643  1.00 26.27  ? 47  LEU A CB  1 
ATOM   334  C  CG  . LEU A 1 47  ? -0.184 4.283   24.568  1.00 25.88  ? 47  LEU A CG  1 
ATOM   335  C  CD1 . LEU A 1 47  ? 1.020  5.058   25.081  1.00 25.43  ? 47  LEU A CD1 1 
ATOM   336  C  CD2 . LEU A 1 47  ? 0.331  2.923   24.149  1.00 25.96  ? 47  LEU A CD2 1 
ATOM   337  N  N   . SER A 1 48  ? -2.534 6.799   24.066  1.00 14.78  ? 48  SER A N   1 
ATOM   338  C  CA  . SER A 1 48  ? -3.349 7.386   23.023  1.00 14.01  ? 48  SER A CA  1 
ATOM   339  C  C   . SER A 1 48  ? -2.566 7.294   21.719  1.00 14.26  ? 48  SER A C   1 
ATOM   340  O  O   . SER A 1 48  ? -1.599 8.015   21.562  1.00 16.29  ? 48  SER A O   1 
ATOM   341  C  CB  . SER A 1 48  ? -3.729 8.818   23.383  1.00 16.98  ? 48  SER A CB  1 
ATOM   342  O  OG  . SER A 1 48  ? -4.401 9.418   22.337  1.00 21.67  ? 48  SER A OG  1 
ATOM   343  N  N   . VAL A 1 49  ? -2.974 6.441   20.811  1.00 15.23  ? 49  VAL A N   1 
ATOM   344  C  CA  . VAL A 1 49  ? -2.353 6.329   19.500  1.00 16.69  ? 49  VAL A CA  1 
ATOM   345  C  C   . VAL A 1 49  ? -3.341 6.879   18.493  1.00 18.43  ? 49  VAL A C   1 
ATOM   346  O  O   . VAL A 1 49  ? -4.404 6.293   18.288  1.00 22.89  ? 49  VAL A O   1 
ATOM   347  C  CB  . VAL A 1 49  ? -2.139 4.828   19.197  1.00 19.96  ? 49  VAL A CB  1 
ATOM   348  C  CG1 . VAL A 1 49  ? -1.418 4.668   17.902  1.00 27.69  ? 49  VAL A CG1 1 
ATOM   349  C  CG2 . VAL A 1 49  ? -1.335 4.117   20.289  1.00 20.97  ? 49  VAL A CG2 1 
ATOM   350  N  N   A SER A 1 50  ? -3.077 8.090   17.978  0.50 15.54  ? 50  SER A N   1 
ATOM   351  N  N   B SER A 1 50  ? -2.971 7.989   17.856  0.50 15.71  ? 50  SER A N   1 
ATOM   352  C  CA  A SER A 1 50  ? -4.030 8.736   17.082  0.50 16.19  ? 50  SER A CA  1 
ATOM   353  C  CA  B SER A 1 50  ? -3.963 8.728   17.098  0.50 16.69  ? 50  SER A CA  1 
ATOM   354  C  C   A SER A 1 50  ? -3.432 8.817   15.683  0.50 15.54  ? 50  SER A C   1 
ATOM   355  C  C   B SER A 1 50  ? -3.455 8.846   15.665  0.50 16.18  ? 50  SER A C   1 
ATOM   356  O  O   A SER A 1 50  ? -2.685 9.740   15.384  0.50 17.27  ? 50  SER A O   1 
ATOM   357  O  O   B SER A 1 50  ? -2.744 9.788   15.340  0.50 17.43  ? 50  SER A O   1 
ATOM   358  C  CB  A SER A 1 50  ? -4.415 10.123  17.546  0.50 17.56  ? 50  SER A CB  1 
ATOM   359  C  CB  B SER A 1 50  ? -4.213 10.081  17.733  0.50 23.73  ? 50  SER A CB  1 
ATOM   360  O  OG  A SER A 1 50  ? -5.032 10.070  18.807  0.50 19.57  ? 50  SER A OG  1 
ATOM   361  O  OG  B SER A 1 50  ? -5.002 10.888  16.877  0.50 24.99  ? 50  SER A OG  1 
ATOM   362  N  N   . TYR A 1 51  ? -3.753 7.849   14.837  1.00 16.67  ? 51  TYR A N   1 
ATOM   363  C  CA  . TYR A 1 51  ? -3.159 7.730   13.525  1.00 14.73  ? 51  TYR A CA  1 
ATOM   364  C  C   . TYR A 1 51  ? -4.139 7.987   12.372  1.00 15.78  ? 51  TYR A C   1 
ATOM   365  O  O   . TYR A 1 51  ? -3.777 7.770   11.218  1.00 19.10  ? 51  TYR A O   1 
ATOM   366  C  CB  . TYR A 1 51  ? -2.502 6.341   13.346  1.00 15.96  ? 51  TYR A CB  1 
ATOM   367  C  CG  . TYR A 1 51  ? -1.244 6.070   14.138  1.00 13.35  ? 51  TYR A CG  1 
ATOM   368  C  CD1 . TYR A 1 51  ? -0.566 7.058   14.848  1.00 14.45  ? 51  TYR A CD1 1 
ATOM   369  C  CD2 . TYR A 1 51  ? -0.742 4.766   14.181  1.00 12.41  ? 51  TYR A CD2 1 
ATOM   370  C  CE1 . TYR A 1 51  ? 0.652  6.755   15.470  1.00 13.16  ? 51  TYR A CE1 1 
ATOM   371  C  CE2 . TYR A 1 51  ? 0.452  4.445   14.827  1.00 12.74  ? 51  TYR A CE2 1 
ATOM   372  C  CZ  . TYR A 1 51  ? 1.153  5.453   15.478  1.00 12.34  ? 51  TYR A CZ  1 
ATOM   373  O  OH  . TYR A 1 51  ? 2.304  5.107   16.128  1.00 13.17  ? 51  TYR A OH  1 
ATOM   374  N  N   A ASP A 1 52  ? -5.347 8.480   12.662  0.50 19.17  ? 52  ASP A N   1 
ATOM   375  N  N   B ASP A 1 52  ? -5.397 8.394   12.653  0.50 19.50  ? 52  ASP A N   1 
ATOM   376  C  CA  A ASP A 1 52  ? -6.391 8.629   11.661  0.50 19.35  ? 52  ASP A CA  1 
ATOM   377  C  CA  B ASP A 1 52  ? -6.386 8.624   11.597  0.50 21.43  ? 52  ASP A CA  1 
ATOM   378  C  C   A ASP A 1 52  ? -6.016 9.601   10.544  0.50 21.02  ? 52  ASP A C   1 
ATOM   379  C  C   B ASP A 1 52  ? -5.816 9.482   10.469  0.50 18.65  ? 52  ASP A C   1 
ATOM   380  O  O   A ASP A 1 52  ? -6.508 9.447   9.430   0.50 23.76  ? 52  ASP A O   1 
ATOM   381  O  O   B ASP A 1 52  ? -5.999 9.154   9.300   0.50 25.17  ? 52  ASP A O   1 
ATOM   382  C  CB  A ASP A 1 52  ? -7.733 8.988   12.320  0.50 20.48  ? 52  ASP A CB  1 
ATOM   383  C  CB  B ASP A 1 52  ? -7.757 9.155   12.086  0.50 26.77  ? 52  ASP A CB  1 
ATOM   384  C  CG  A ASP A 1 52  ? -7.534 10.138  13.277  0.50 27.51  ? 52  ASP A CG  1 
ATOM   385  C  CG  B ASP A 1 52  ? -8.821 9.197   10.983  0.50 28.94  ? 52  ASP A CG  1 
ATOM   386  O  OD1 A ASP A 1 52  ? -6.720 9.988   14.252  0.50 36.19  ? 52  ASP A OD1 1 
ATOM   387  O  OD1 B ASP A 1 52  ? -9.139 8.105   10.428  0.50 35.65  ? 52  ASP A OD1 1 
ATOM   388  O  OD2 A ASP A 1 52  ? -8.226 11.185  13.060  0.50 36.64  ? 52  ASP A OD2 1 
ATOM   389  O  OD2 B ASP A 1 52  ? -9.306 10.314  10.668  0.50 37.64  ? 52  ASP A OD2 1 
ATOM   390  N  N   . GLN A 1 53  ? -5.147 10.580  10.819  1.00 21.74  ? 53  GLN A N   1 
ATOM   391  C  CA  . GLN A 1 53  ? -4.725 11.492  9.763   1.00 24.07  ? 53  GLN A CA  1 
ATOM   392  C  C   . GLN A 1 53  ? -3.319 11.243  9.252   1.00 18.68  ? 53  GLN A C   1 
ATOM   393  O  O   . GLN A 1 53  ? -2.704 12.125  8.653   1.00 20.68  ? 53  GLN A O   1 
ATOM   394  C  CB  . GLN A 1 53  ? -4.906 12.938  10.257  1.00 30.06  ? 53  GLN A CB  1 
ATOM   395  C  CG  . GLN A 1 53  ? -6.371 13.284  10.550  1.00 40.82  ? 53  GLN A CG  1 
ATOM   396  C  CD  . GLN A 1 53  ? -7.000 13.600  9.210   1.00 61.50  ? 53  GLN A CD  1 
ATOM   397  O  OE1 . GLN A 1 53  ? -6.807 14.735  8.671   1.00 70.01  ? 53  GLN A OE1 1 
ATOM   398  N  NE2 . GLN A 1 53  ? -7.691 12.562  8.633   1.00 64.32  ? 53  GLN A NE2 1 
ATOM   399  N  N   . ALA A 1 54  ? -2.745 10.075  9.571   1.00 17.82  ? 54  ALA A N   1 
ATOM   400  C  CA  . ALA A 1 54  ? -1.368 9.860   9.156   1.00 15.16  ? 54  ALA A CA  1 
ATOM   401  C  C   . ALA A 1 54  ? -1.249 9.947   7.645   1.00 17.44  ? 54  ALA A C   1 
ATOM   402  O  O   . ALA A 1 54  ? -2.121 9.470   6.903   1.00 21.81  ? 54  ALA A O   1 
ATOM   403  C  CB  . ALA A 1 54  ? -0.912 8.479   9.608   1.00 17.80  ? 54  ALA A CB  1 
ATOM   404  N  N   . THR A 1 55  ? -0.152 10.581  7.217   1.00 14.47  ? 55  THR A N   1 
ATOM   405  C  CA  . THR A 1 55  ? 0.147  10.779  5.805   1.00 15.14  ? 55  THR A CA  1 
ATOM   406  C  C   . THR A 1 55  ? 1.488  10.129  5.477   1.00 12.45  ? 55  THR A C   1 
ATOM   407  O  O   . THR A 1 55  ? 2.513  10.713  5.765   1.00 13.01  ? 55  THR A O   1 
ATOM   408  C  CB  . THR A 1 55  ? 0.201  12.316  5.461   1.00 20.38  ? 55  THR A CB  1 
ATOM   409  O  OG1 . THR A 1 55  ? -1.058 12.861  5.861   1.00 30.07  ? 55  THR A OG1 1 
ATOM   410  C  CG2 . THR A 1 55  ? 0.476  12.441  3.975   1.00 27.07  ? 55  THR A CG2 1 
ATOM   411  N  N   . SER A 1 56  ? 1.487  8.929   4.933   1.00 11.81  ? 56  SER A N   1 
ATOM   412  C  CA  . SER A 1 56  ? 2.741  8.320   4.549   1.00 10.61  ? 56  SER A CA  1 
ATOM   413  C  C   . SER A 1 56  ? 3.266  8.949   3.283   1.00 13.21  ? 56  SER A C   1 
ATOM   414  O  O   . SER A 1 56  ? 2.503  9.456   2.444   1.00 14.25  ? 56  SER A O   1 
ATOM   415  C  CB  . SER A 1 56  ? 2.551  6.788   4.434   1.00 12.63  ? 56  SER A CB  1 
ATOM   416  O  OG  . SER A 1 56  ? 1.715  6.492   3.331   1.00 13.92  ? 56  SER A OG  1 
ATOM   417  N  N   . LEU A 1 57  ? 4.591  8.946   3.144   1.00 11.43  ? 57  LEU A N   1 
ATOM   418  C  CA  . LEU A 1 57  ? 5.221  9.571   1.973   1.00 14.11  ? 57  LEU A CA  1 
ATOM   419  C  C   . LEU A 1 57  ? 6.016  8.581   1.133   1.00 13.43  ? 57  LEU A C   1 
ATOM   420  O  O   . LEU A 1 57  ? 5.933  8.595   -0.097  1.00 13.78  ? 57  LEU A O   1 
ATOM   421  C  CB  . LEU A 1 57  ? 6.091  10.746  2.409   1.00 16.18  ? 57  LEU A CB  1 
ATOM   422  C  CG  . LEU A 1 57  ? 5.296  11.922  3.044   1.00 19.35  ? 57  LEU A CG  1 
ATOM   423  C  CD1 . LEU A 1 57  ? 6.294  12.950  3.572   1.00 21.87  ? 57  LEU A CD1 1 
ATOM   424  C  CD2 . LEU A 1 57  ? 4.252  12.577  2.075   1.00 26.55  ? 57  LEU A CD2 1 
ATOM   425  N  N   . ARG A 1 58  ? 6.929  7.836   1.737   1.00 13.87  ? 58  ARG A N   1 
ATOM   426  C  CA  . ARG A 1 58  ? 8.012  7.230   0.972   1.00 11.65  ? 58  ARG A CA  1 
ATOM   427  C  C   . ARG A 1 58  ? 8.476  6.014   1.760   1.00 12.04  ? 58  ARG A C   1 
ATOM   428  O  O   . ARG A 1 58  ? 8.380  5.965   2.983   1.00 14.06  ? 58  ARG A O   1 
ATOM   429  C  CB  . ARG A 1 58  ? 9.162  8.231   0.838   1.00 15.70  ? 58  ARG A CB  1 
ATOM   430  C  CG  . ARG A 1 58  ? 10.270 7.793   -0.021  1.00 17.68  ? 58  ARG A CG  1 
ATOM   431  C  CD  . ARG A 1 58  ? 11.220 8.949   -0.158  1.00 21.12  ? 58  ARG A CD  1 
ATOM   432  N  NE  . ARG A 1 58  ? 12.107 9.007   0.986   1.00 16.53  ? 58  ARG A NE  1 
ATOM   433  C  CZ  . ARG A 1 58  ? 13.432 9.093   0.964   1.00 15.44  ? 58  ARG A CZ  1 
ATOM   434  N  NH1 . ARG A 1 58  ? 14.074 9.135   -0.191  1.00 19.03  ? 58  ARG A NH1 1 
ATOM   435  N  NH2 . ARG A 1 58  ? 14.111 9.138   2.096   1.00 15.69  ? 58  ARG A NH2 1 
ATOM   436  N  N   . ILE A 1 59  ? 9.030  5.050   1.068   1.00 10.75  ? 59  ILE A N   1 
ATOM   437  C  CA  . ILE A 1 59  ? 9.679  3.908   1.694   1.00 10.37  ? 59  ILE A CA  1 
ATOM   438  C  C   . ILE A 1 59  ? 11.121 3.892   1.193   1.00 10.44  ? 59  ILE A C   1 
ATOM   439  O  O   . ILE A 1 59  ? 11.392 4.188   0.029   1.00 12.31  ? 59  ILE A O   1 
ATOM   440  C  CB  . ILE A 1 59  ? 8.904  2.596   1.424   1.00 10.78  ? 59  ILE A CB  1 
ATOM   441  C  CG1 . ILE A 1 59  ? 9.453  1.443   2.292   1.00 10.85  ? 59  ILE A CG1 1 
ATOM   442  C  CG2 . ILE A 1 59  ? 8.891  2.276   -0.081  1.00 12.22  ? 59  ILE A CG2 1 
ATOM   443  C  CD1 . ILE A 1 59  ? 8.621  0.146   2.137   1.00 13.18  ? 59  ILE A CD1 1 
ATOM   444  N  N   . LEU A 1 60  ? 12.078 3.599   2.068   1.00 10.65  ? 60  LEU A N   1 
ATOM   445  C  CA  . LEU A 1 60  ? 13.488 3.737   1.786   1.00 9.64   ? 60  LEU A CA  1 
ATOM   446  C  C   . LEU A 1 60  ? 14.276 2.545   2.350   1.00 9.94   ? 60  LEU A C   1 
ATOM   447  O  O   . LEU A 1 60  ? 14.068 2.149   3.489   1.00 10.95  ? 60  LEU A O   1 
ATOM   448  C  CB  . LEU A 1 60  ? 14.013 5.024   2.507   1.00 12.24  ? 60  LEU A CB  1 
ATOM   449  C  CG  . LEU A 1 60  ? 15.534 5.174   2.477   1.00 12.53  ? 60  LEU A CG  1 
ATOM   450  C  CD1 . LEU A 1 60  ? 16.026 5.485   1.075   1.00 13.66  ? 60  LEU A CD1 1 
ATOM   451  C  CD2 . LEU A 1 60  ? 15.927 6.335   3.419   1.00 13.28  ? 60  LEU A CD2 1 
ATOM   452  N  N   . ASN A 1 61  ? 15.187 2.029   1.545   1.00 10.07  ? 61  ASN A N   1 
ATOM   453  C  CA  . ASN A 1 61  ? 16.183 1.046   1.992   1.00 10.53  ? 61  ASN A CA  1 
ATOM   454  C  C   . ASN A 1 61  ? 17.393 1.843   2.452   1.00 10.38  ? 61  ASN A C   1 
ATOM   455  O  O   . ASN A 1 61  ? 18.033 2.526   1.639   1.00 11.36  ? 61  ASN A O   1 
ATOM   456  C  CB  . ASN A 1 61  ? 16.532 0.091   0.839   1.00 10.87  ? 61  ASN A CB  1 
ATOM   457  C  CG  . ASN A 1 61  ? 17.593 -0.913  1.199   1.00 9.99   ? 61  ASN A CG  1 
ATOM   458  O  OD1 . ASN A 1 61  ? 18.455 -0.670  2.050   1.00 11.44  ? 61  ASN A OD1 1 
ATOM   459  N  ND2 . ASN A 1 61  ? 17.525 -2.081  0.591   1.00 11.51  ? 61  ASN A ND2 1 
ATOM   460  N  N   . THR A 1 62  ? 17.661 1.857   3.743   1.00 10.11  ? 62  THR A N   1 
ATOM   461  C  CA  . THR A 1 62  ? 18.729 2.674   4.282   1.00 10.60  ? 62  THR A CA  1 
ATOM   462  C  C   . THR A 1 62  ? 20.091 2.002   4.179   1.00 11.85  ? 62  THR A C   1 
ATOM   463  O  O   . THR A 1 62  ? 21.140 2.631   4.516   1.00 15.95  ? 62  THR A O   1 
ATOM   464  C  CB  . THR A 1 62  ? 18.512 2.964   5.788   1.00 11.61  ? 62  THR A CB  1 
ATOM   465  O  OG1 . THR A 1 62  ? 18.769 1.738   6.511   1.00 12.10  ? 62  THR A OG1 1 
ATOM   466  C  CG2 . THR A 1 62  ? 17.112 3.463   6.090   1.00 12.82  ? 62  THR A CG2 1 
ATOM   467  N  N   . GLY A 1 63  ? 20.174 0.750   3.738   1.00 11.25  ? 63  GLY A N   1 
ATOM   468  C  CA  . GLY A 1 63  ? 21.419 -0.042  3.782   1.00 10.89  ? 63  GLY A CA  1 
ATOM   469  C  C   . GLY A 1 63  ? 21.538 -0.860  5.062   1.00 10.78  ? 63  GLY A C   1 
ATOM   470  O  O   . GLY A 1 63  ? 22.450 -1.715  5.133   1.00 13.79  ? 63  GLY A O   1 
ATOM   471  N  N   . TYR A 1 64  ? 20.661 -0.628  6.028   1.00 10.22  ? 64  TYR A N   1 
ATOM   472  C  CA  . TYR A 1 64  ? 20.638 -1.453  7.240   1.00 10.64  ? 64  TYR A CA  1 
ATOM   473  C  C   . TYR A 1 64  ? 19.264 -2.030  7.439   1.00 9.54   ? 64  TYR A C   1 
ATOM   474  O  O   . TYR A 1 64  ? 19.151 -3.188  7.884   1.00 11.97  ? 64  TYR A O   1 
ATOM   475  C  CB  . TYR A 1 64  ? 21.032 -0.623  8.475   1.00 12.03  ? 64  TYR A CB  1 
ATOM   476  C  CG  . TYR A 1 64  ? 21.103 -1.430  9.769   1.00 14.21  ? 64  TYR A CG  1 
ATOM   477  C  CD1 . TYR A 1 64  ? 22.104 -2.350  10.033  1.00 15.27  ? 64  TYR A CD1 1 
ATOM   478  C  CD2 . TYR A 1 64  ? 20.234 -1.104  10.796  1.00 13.52  ? 64  TYR A CD2 1 
ATOM   479  C  CE1 . TYR A 1 64  ? 22.170 -2.998  11.257  1.00 14.32  ? 64  TYR A CE1 1 
ATOM   480  C  CE2 . TYR A 1 64  ? 20.285 -1.737  12.021  1.00 14.43  ? 64  TYR A CE2 1 
ATOM   481  C  CZ  . TYR A 1 64  ? 21.257 -2.688  12.252  1.00 14.03  ? 64  TYR A CZ  1 
ATOM   482  O  OH  . TYR A 1 64  ? 21.287 -3.285  13.475  1.00 16.09  ? 64  TYR A OH  1 
ATOM   483  N  N   . LEU A 1 65  ? 18.194 -1.290  7.111   1.00 9.92   ? 65  LEU A N   1 
ATOM   484  C  CA  . LEU A 1 65  ? 16.828 -1.756  7.266   1.00 9.33   ? 65  LEU A CA  1 
ATOM   485  C  C   . LEU A 1 65  ? 16.016 -1.017  6.215   1.00 9.39   ? 65  LEU A C   1 
ATOM   486  O  O   . LEU A 1 65  ? 16.570 -0.306  5.373   1.00 9.84   ? 65  LEU A O   1 
ATOM   487  C  CB  . LEU A 1 65  ? 16.342 -1.637  8.714   1.00 9.94   ? 65  LEU A CB  1 
ATOM   488  C  CG  . LEU A 1 65  ? 16.525 -0.282  9.388   1.00 9.16   ? 65  LEU A CG  1 
ATOM   489  C  CD1 . LEU A 1 65  ? 15.702 0.837   8.781   1.00 11.29  ? 65  LEU A CD1 1 
ATOM   490  C  CD2 . LEU A 1 65  ? 16.229 -0.467  10.854  1.00 11.52  ? 65  LEU A CD2 1 
ATOM   491  N  N   . PHE A 1 66  ? 14.672 -1.172  6.226   1.00 9.09   ? 66  PHE A N   1 
ATOM   492  C  CA  . PHE A 1 66  ? 13.802 -0.273  5.457   1.00 9.44   ? 66  PHE A CA  1 
ATOM   493  C  C   . PHE A 1 66  ? 12.899 0.477   6.397   1.00 9.55   ? 66  PHE A C   1 
ATOM   494  O  O   . PHE A 1 66  ? 12.532 -0.014  7.470   1.00 9.72   ? 66  PHE A O   1 
ATOM   495  C  CB  . PHE A 1 66  ? 13.082 -1.013  4.330   1.00 10.45  ? 66  PHE A CB  1 
ATOM   496  C  CG  . PHE A 1 66  ? 11.922 -1.814  4.834   1.00 10.49  ? 66  PHE A CG  1 
ATOM   497  C  CD1 . PHE A 1 66  ? 10.642 -1.271  4.990   1.00 11.77  ? 66  PHE A CD1 1 
ATOM   498  C  CD2 . PHE A 1 66  ? 12.100 -3.186  5.159   1.00 11.31  ? 66  PHE A CD2 1 
ATOM   499  C  CE1 . PHE A 1 66  ? 9.564  -2.026  5.439   1.00 12.06  ? 66  PHE A CE1 1 
ATOM   500  C  CE2 . PHE A 1 66  ? 11.017 -3.912  5.598   1.00 10.77  ? 66  PHE A CE2 1 
ATOM   501  C  CZ  . PHE A 1 66  ? 9.763  -3.377  5.709   1.00 12.09  ? 66  PHE A CZ  1 
ATOM   502  N  N   . GLN A 1 67  ? 12.492 1.651   5.926   1.00 10.54  ? 67  GLN A N   1 
ATOM   503  C  CA  . GLN A 1 67  ? 11.630 2.509   6.725   1.00 10.14  ? 67  GLN A CA  1 
ATOM   504  C  C   . GLN A 1 67  ? 10.587 3.185   5.846   1.00 9.14   ? 67  GLN A C   1 
ATOM   505  O  O   . GLN A 1 67  ? 10.848 3.474   4.666   1.00 12.24  ? 67  GLN A O   1 
ATOM   506  C  CB  . GLN A 1 67  ? 12.461 3.547   7.473   1.00 11.46  ? 67  GLN A CB  1 
ATOM   507  C  CG  . GLN A 1 67  ? 13.223 4.504   6.579   1.00 11.66  ? 67  GLN A CG  1 
ATOM   508  C  CD  . GLN A 1 67  ? 14.164 5.370   7.362   1.00 13.11  ? 67  GLN A CD  1 
ATOM   509  O  OE1 . GLN A 1 67  ? 14.840 4.903   8.279   1.00 14.64  ? 67  GLN A OE1 1 
ATOM   510  N  NE2 . GLN A 1 67  ? 14.251 6.623   6.965   1.00 16.52  ? 67  GLN A NE2 1 
ATOM   511  N  N   . VAL A 1 68  ? 9.445  3.425   6.445   1.00 10.46  ? 68  VAL A N   1 
ATOM   512  C  CA  . VAL A 1 68  ? 8.340  4.142   5.835   1.00 11.00  ? 68  VAL A CA  1 
ATOM   513  C  C   . VAL A 1 68  ? 8.247  5.477   6.558   1.00 10.67  ? 68  VAL A C   1 
ATOM   514  O  O   . VAL A 1 68  ? 8.098  5.517   7.787   1.00 10.97  ? 68  VAL A O   1 
ATOM   515  C  CB  . VAL A 1 68  ? 7.012  3.367   5.940   1.00 11.36  ? 68  VAL A CB  1 
ATOM   516  C  CG1 . VAL A 1 68  ? 5.818  4.254   5.485   1.00 13.08  ? 68  VAL A CG1 1 
ATOM   517  C  CG2 . VAL A 1 68  ? 7.084  2.098   5.108   1.00 12.61  ? 68  VAL A CG2 1 
ATOM   518  N  N   . GLU A 1 69  ? 8.326  6.533   5.769   1.00 11.40  ? 69  GLU A N   1 
ATOM   519  C  CA  . GLU A 1 69  ? 8.363  7.872   6.324   1.00 10.61  ? 69  GLU A CA  1 
ATOM   520  C  C   . GLU A 1 69  ? 6.995  8.569   6.197   1.00 12.09  ? 69  GLU A C   1 
ATOM   521  O  O   . GLU A 1 69  ? 6.278  8.314   5.229   1.00 12.76  ? 69  GLU A O   1 
ATOM   522  C  CB  . GLU A 1 69  ? 9.410  8.712   5.593   1.00 12.54  ? 69  GLU A CB  1 
ATOM   523  C  CG  . GLU A 1 69  ? 10.767 7.993   5.632   1.00 14.88  ? 69  GLU A CG  1 
ATOM   524  C  CD  . GLU A 1 69  ? 11.736 8.491   4.607   1.00 14.90  ? 69  GLU A CD  1 
ATOM   525  O  OE1 . GLU A 1 69  ? 12.980 8.203   4.778   1.00 17.75  ? 69  GLU A OE1 1 
ATOM   526  O  OE2 . GLU A 1 69  ? 11.302 9.165   3.611   1.00 17.66  ? 69  GLU A OE2 1 
ATOM   527  N  N   . PHE A 1 70  ? 6.687  9.451   7.169   1.00 11.51  ? 70  PHE A N   1 
ATOM   528  C  CA  . PHE A 1 70  ? 5.414  10.172  7.211   1.00 11.97  ? 70  PHE A CA  1 
ATOM   529  C  C   . PHE A 1 70  ? 5.674  11.666  7.128   1.00 13.01  ? 70  PHE A C   1 
ATOM   530  O  O   . PHE A 1 70  ? 6.749  12.144  7.472   1.00 14.67  ? 70  PHE A O   1 
ATOM   531  C  CB  . PHE A 1 70  ? 4.688  9.830   8.507   1.00 11.47  ? 70  PHE A CB  1 
ATOM   532  C  CG  . PHE A 1 70  ? 4.135  8.449   8.470   1.00 11.58  ? 70  PHE A CG  1 
ATOM   533  C  CD1 . PHE A 1 70  ? 4.968  7.353   8.689   1.00 12.20  ? 70  PHE A CD1 1 
ATOM   534  C  CD2 . PHE A 1 70  ? 2.782  8.234   8.186   1.00 12.00  ? 70  PHE A CD2 1 
ATOM   535  C  CE1 . PHE A 1 70  ? 4.494  6.057   8.567   1.00 12.77  ? 70  PHE A CE1 1 
ATOM   536  C  CE2 . PHE A 1 70  ? 2.315  6.932   8.047   1.00 11.40  ? 70  PHE A CE2 1 
ATOM   537  C  CZ  . PHE A 1 70  ? 3.164  5.859   8.253   1.00 12.92  ? 70  PHE A CZ  1 
ATOM   538  N  N   . ASP A 1 71  ? 4.611  12.406  6.753   1.00 14.06  ? 71  ASP A N   1 
ATOM   539  C  CA  . ASP A 1 71  ? 4.677  13.857  6.821   1.00 15.19  ? 71  ASP A CA  1 
ATOM   540  C  C   . ASP A 1 71  ? 4.447  14.225  8.277   1.00 13.75  ? 71  ASP A C   1 
ATOM   541  O  O   . ASP A 1 71  ? 3.335  14.067  8.826   1.00 19.71  ? 71  ASP A O   1 
ATOM   542  C  CB  . ASP A 1 71  ? 3.499  14.422  6.013   1.00 19.31  ? 71  ASP A CB  1 
ATOM   543  C  CG  . ASP A 1 71  ? 3.396  15.938  6.216   1.00 21.07  ? 71  ASP A CG  1 
ATOM   544  O  OD1 . ASP A 1 71  ? 4.319  16.569  6.765   1.00 20.57  ? 71  ASP A OD1 1 
ATOM   545  O  OD2 . ASP A 1 71  ? 2.380  16.505  5.864   1.00 23.28  ? 71  ASP A OD2 1 
ATOM   546  N  N   . ASP A 1 72  ? 5.507  14.668  8.931   1.00 15.44  ? 72  ASP A N   1 
ATOM   547  C  CA  . ASP A 1 72  ? 5.521  15.096  10.326  1.00 14.72  ? 72  ASP A CA  1 
ATOM   548  C  C   . ASP A 1 72  ? 5.687  16.622  10.418  1.00 16.70  ? 72  ASP A C   1 
ATOM   549  O  O   . ASP A 1 72  ? 6.270  17.085  11.382  1.00 18.18  ? 72  ASP A O   1 
ATOM   550  C  CB  . ASP A 1 72  ? 6.555  14.341  11.158  1.00 16.08  ? 72  ASP A CB  1 
ATOM   551  C  CG  . ASP A 1 72  ? 7.945  14.499  10.621  1.00 14.66  ? 72  ASP A CG  1 
ATOM   552  O  OD1 . ASP A 1 72  ? 8.140  15.074  9.466   1.00 17.61  ? 72  ASP A OD1 1 
ATOM   553  O  OD2 . ASP A 1 72  ? 8.867  14.084  11.333  1.00 15.89  ? 72  ASP A OD2 1 
ATOM   554  N  N   . SER A 1 73  ? 5.245  17.297  9.377   1.00 18.03  ? 73  SER A N   1 
ATOM   555  C  CA  . SER A 1 73  ? 5.396  18.728  9.424   1.00 18.03  ? 73  SER A CA  1 
ATOM   556  C  C   . SER A 1 73  ? 4.191  19.390  10.085  1.00 20.47  ? 73  SER A C   1 
ATOM   557  O  O   . SER A 1 73  ? 4.114  20.534  10.226  1.00 23.38  ? 73  SER A O   1 
ATOM   558  C  CB  . SER A 1 73  ? 5.633  19.261  8.002   1.00 19.76  ? 73  SER A CB  1 
ATOM   559  O  OG  . SER A 1 73  ? 4.394  19.183  7.281   1.00 19.48  ? 73  SER A OG  1 
ATOM   560  N  N   . GLN A 1 74  ? 3.191  18.622  10.550  1.00 18.77  ? 74  GLN A N   1 
ATOM   561  C  CA  . GLN A 1 74  ? 2.010  19.086  11.325  1.00 20.45  ? 74  GLN A CA  1 
ATOM   562  C  C   . GLN A 1 74  ? 1.618  17.937  12.258  1.00 21.54  ? 74  GLN A C   1 
ATOM   563  O  O   . GLN A 1 74  ? 2.012  16.837  11.936  1.00 20.39  ? 74  GLN A O   1 
ATOM   564  C  CB  . GLN A 1 74  ? 0.805  19.235  10.408  1.00 27.24  ? 74  GLN A CB  1 
ATOM   565  C  CG  . GLN A 1 74  ? 0.948  20.294  9.336   1.00 35.58  ? 74  GLN A CG  1 
ATOM   566  C  CD  . GLN A 1 74  ? -0.428 20.471  8.755   1.00 30.23  ? 74  GLN A CD  1 
ATOM   567  O  OE1 . GLN A 1 74  ? -1.331 20.971  9.434   1.00 32.28  ? 74  GLN A OE1 1 
ATOM   568  N  NE2 . GLN A 1 74  ? -0.598 19.987  7.529   1.00 32.05  ? 74  GLN A NE2 1 
ATOM   569  N  N   . ASP A 1 75  ? 0.732  18.188  13.257  1.00 23.80  ? 75  ASP A N   1 
ATOM   570  C  CA  . ASP A 1 75  ? 0.316  17.104  14.149  1.00 28.45  ? 75  ASP A CA  1 
ATOM   571  C  C   . ASP A 1 75  ? -0.767 16.247  13.507  1.00 25.64  ? 75  ASP A C   1 
ATOM   572  O  O   . ASP A 1 75  ? -1.958 16.549  13.627  1.00 47.89  ? 75  ASP A O   1 
ATOM   573  C  CB  . ASP A 1 75  ? -0.273 17.543  15.497  1.00 30.42  ? 75  ASP A CB  1 
ATOM   574  C  CG  . ASP A 1 75  ? 0.779  18.032  16.450  1.00 31.21  ? 75  ASP A CG  1 
ATOM   575  O  OD1 . ASP A 1 75  ? 1.953  17.710  16.259  1.00 39.71  ? 75  ASP A OD1 1 
ATOM   576  O  OD2 . ASP A 1 75  ? 0.407  18.685  17.387  1.00 42.07  ? 75  ASP A OD2 1 
ATOM   577  N  N   . LYS A 1 76  ? -0.356 15.312  12.691  1.00 21.97  ? 76  LYS A N   1 
ATOM   578  C  CA  . LYS A 1 76  ? -1.280 14.444  11.993  1.00 26.68  ? 76  LYS A CA  1 
ATOM   579  C  C   . LYS A 1 76  ? -1.428 13.249  12.927  1.00 29.62  ? 76  LYS A C   1 
ATOM   580  O  O   . LYS A 1 76  ? -2.305 13.176  13.777  1.00 49.39  ? 76  LYS A O   1 
ATOM   581  C  CB  . LYS A 1 76  ? -0.671 14.215  10.596  1.00 24.59  ? 76  LYS A CB  1 
ATOM   582  C  CG  . LYS A 1 76  ? -0.897 15.430  9.664   1.00 28.74  ? 76  LYS A CG  1 
ATOM   583  C  CD  . LYS A 1 76  ? -0.353 15.161  8.294   1.00 26.36  ? 76  LYS A CD  1 
ATOM   584  C  CE  . LYS A 1 76  ? -0.729 16.264  7.313   1.00 27.36  ? 76  LYS A CE  1 
ATOM   585  N  NZ  . LYS A 1 76  ? -0.481 15.937  5.897   1.00 28.95  ? 76  LYS A NZ  1 
ATOM   586  N  N   . ALA A 1 77  ? -0.435 12.434  12.889  1.00 23.37  ? 77  ALA A N   1 
ATOM   587  C  CA  . ALA A 1 77  ? -0.445 11.169  13.595  1.00 18.64  ? 77  ALA A CA  1 
ATOM   588  C  C   . ALA A 1 77  ? 0.401  11.367  14.819  1.00 19.08  ? 77  ALA A C   1 
ATOM   589  O  O   . ALA A 1 77  ? 1.566  11.776  14.670  1.00 20.34  ? 77  ALA A O   1 
ATOM   590  C  CB  . ALA A 1 77  ? 0.171  10.176  12.648  1.00 20.48  ? 77  ALA A CB  1 
ATOM   591  N  N   . VAL A 1 78  ? -0.172 11.162  16.004  1.00 15.55  ? 78  VAL A N   1 
ATOM   592  C  CA  . VAL A 1 78  ? 0.564  11.430  17.218  1.00 15.76  ? 78  VAL A CA  1 
ATOM   593  C  C   . VAL A 1 78  ? 0.326  10.322  18.241  1.00 13.48  ? 78  VAL A C   1 
ATOM   594  O  O   . VAL A 1 78  ? -0.702 9.614   18.235  1.00 17.79  ? 78  VAL A O   1 
ATOM   595  C  CB  . VAL A 1 78  ? 0.148  12.784  17.807  1.00 20.33  ? 78  VAL A CB  1 
ATOM   596  C  CG1 . VAL A 1 78  ? 0.405  13.971  16.871  1.00 20.74  ? 78  VAL A CG1 1 
ATOM   597  C  CG2 . VAL A 1 78  ? -1.276 12.747  18.171  1.00 23.46  ? 78  VAL A CG2 1 
ATOM   598  N  N   . LEU A 1 79  ? 1.300  10.235  19.161  1.00 13.29  ? 79  LEU A N   1 
ATOM   599  C  CA  . LEU A 1 79  ? 1.281  9.370   20.310  1.00 13.76  ? 79  LEU A CA  1 
ATOM   600  C  C   . LEU A 1 79  ? 1.303  10.250  21.548  1.00 13.37  ? 79  LEU A C   1 
ATOM   601  O  O   . LEU A 1 79  ? 2.140  11.164  21.649  1.00 15.20  ? 79  LEU A O   1 
ATOM   602  C  CB  . LEU A 1 79  ? 2.491  8.457   20.212  1.00 13.70  ? 79  LEU A CB  1 
ATOM   603  C  CG  . LEU A 1 79  ? 2.631  7.425   21.316  1.00 14.58  ? 79  LEU A CG  1 
ATOM   604  C  CD1 . LEU A 1 79  ? 1.495  6.420   21.208  1.00 17.44  ? 79  LEU A CD1 1 
ATOM   605  C  CD2 . LEU A 1 79  ? 3.992  6.725   21.181  1.00 16.23  ? 79  LEU A CD2 1 
ATOM   606  N  N   . LYS A 1 80  ? 0.449  9.926   22.503  1.00 14.23  ? 80  LYS A N   1 
ATOM   607  C  CA  . LYS A 1 80  ? 0.318  10.696  23.729  1.00 16.02  ? 80  LYS A CA  1 
ATOM   608  C  C   . LYS A 1 80  ? -0.039 9.718   24.854  1.00 15.32  ? 80  LYS A C   1 
ATOM   609  O  O   . LYS A 1 80  ? -0.408 8.581   24.565  1.00 15.55  ? 80  LYS A O   1 
ATOM   610  C  CB  . LYS A 1 80  ? -0.772 11.814  23.671  1.00 24.26  ? 80  LYS A CB  1 
ATOM   611  C  CG  . LYS A 1 80  ? -0.803 12.851  22.559  1.00 26.65  ? 80  LYS A CG  1 
ATOM   612  C  CD  . LYS A 1 80  ? -1.996 13.812  22.831  1.00 36.17  ? 80  LYS A CD  1 
ATOM   613  N  N   . GLY A 1 81  ? -0.023 10.183  26.094  1.00 15.84  ? 81  GLY A N   1 
ATOM   614  C  CA  . GLY A 1 81  ? -0.510 9.397   27.207  1.00 16.33  ? 81  GLY A CA  1 
ATOM   615  C  C   . GLY A 1 81  ? 0.504  8.322   27.587  1.00 15.47  ? 81  GLY A C   1 
ATOM   616  O  O   . GLY A 1 81  ? 1.698  8.455   27.325  1.00 15.29  ? 81  GLY A O   1 
ATOM   617  N  N   . GLY A 1 82  ? 0.040  7.349   28.350  1.00 18.63  ? 82  GLY A N   1 
ATOM   618  C  CA  . GLY A 1 82  ? 0.970  6.370   28.880  1.00 19.93  ? 82  GLY A CA  1 
ATOM   619  C  C   . GLY A 1 82  ? 1.980  7.045   29.782  1.00 19.63  ? 82  GLY A C   1 
ATOM   620  O  O   . GLY A 1 82  ? 1.614  7.877   30.627  1.00 21.32  ? 82  GLY A O   1 
ATOM   621  N  N   . PRO A 1 83  ? 3.288  6.765   29.572  1.00 16.50  ? 83  PRO A N   1 
ATOM   622  C  CA  . PRO A 1 83  ? 4.309  7.392   30.421  1.00 19.24  ? 83  PRO A CA  1 
ATOM   623  C  C   . PRO A 1 83  ? 4.662  8.773   29.898  1.00 16.80  ? 83  PRO A C   1 
ATOM   624  O  O   . PRO A 1 83  ? 5.486  9.423   30.555  1.00 23.03  ? 83  PRO A O   1 
ATOM   625  C  CB  . PRO A 1 83  ? 5.508  6.459   30.208  1.00 18.29  ? 83  PRO A CB  1 
ATOM   626  C  CG  . PRO A 1 83  ? 5.321  5.993   28.760  1.00 15.59  ? 83  PRO A CG  1 
ATOM   627  C  CD  . PRO A 1 83  ? 3.830  5.884   28.525  1.00 15.43  ? 83  PRO A CD  1 
ATOM   628  N  N   . LEU A 1 84  ? 4.043  9.196   28.760  1.00 16.49  ? 84  LEU A N   1 
ATOM   629  C  CA  . LEU A 1 84  ? 4.574  10.363  28.062  1.00 15.09  ? 84  LEU A CA  1 
ATOM   630  C  C   . LEU A 1 84  ? 3.946  11.637  28.622  1.00 16.01  ? 84  LEU A C   1 
ATOM   631  O  O   . LEU A 1 84  ? 2.746  11.700  28.938  1.00 21.07  ? 84  LEU A O   1 
ATOM   632  C  CB  . LEU A 1 84  ? 4.263  10.289  26.555  1.00 13.85  ? 84  LEU A CB  1 
ATOM   633  C  CG  . LEU A 1 84  ? 4.763  9.023   25.878  1.00 13.05  ? 84  LEU A CG  1 
ATOM   634  C  CD1 . LEU A 1 84  ? 4.252  8.990   24.420  1.00 15.87  ? 84  LEU A CD1 1 
ATOM   635  C  CD2 . LEU A 1 84  ? 6.302  8.984   25.931  1.00 14.15  ? 84  LEU A CD2 1 
ATOM   636  N  N   . ASP A 1 85  ? 4.773  12.682  28.657  1.00 18.36  ? 85  ASP A N   1 
ATOM   637  C  CA  . ASP A 1 85  ? 4.284  14.026  28.922  1.00 22.79  ? 85  ASP A CA  1 
ATOM   638  C  C   . ASP A 1 85  ? 4.257  14.694  27.565  1.00 21.57  ? 85  ASP A C   1 
ATOM   639  O  O   . ASP A 1 85  ? 5.257  14.699  26.827  1.00 26.78  ? 85  ASP A O   1 
ATOM   640  C  CB  . ASP A 1 85  ? 5.219  14.750  29.920  1.00 31.57  ? 85  ASP A CB  1 
ATOM   641  C  CG  . ASP A 1 85  ? 5.101  14.236  31.366  1.00 39.22  ? 85  ASP A CG  1 
ATOM   642  O  OD1 . ASP A 1 85  ? 3.998  13.782  31.730  1.00 54.23  ? 85  ASP A OD1 1 
ATOM   643  O  OD2 . ASP A 1 85  ? 6.114  14.337  32.174  1.00 38.25  ? 85  ASP A OD2 1 
ATOM   644  N  N   . GLY A 1 86  ? 3.180  15.385  27.251  1.00 26.35  ? 86  GLY A N   1 
ATOM   645  C  CA  . GLY A 1 86  ? 3.170  16.063  25.953  1.00 21.95  ? 86  GLY A CA  1 
ATOM   646  C  C   . GLY A 1 86  ? 2.831  15.188  24.718  1.00 24.63  ? 86  GLY A C   1 
ATOM   647  O  O   . GLY A 1 86  ? 2.254  14.108  24.805  1.00 26.74  ? 86  GLY A O   1 
ATOM   648  N  N   . THR A 1 87  ? 3.143  15.694  23.521  1.00 19.10  ? 87  THR A N   1 
ATOM   649  C  CA  . THR A 1 87  ? 2.658  15.222  22.230  1.00 18.88  ? 87  THR A CA  1 
ATOM   650  C  C   . THR A 1 87  ? 3.877  14.743  21.417  1.00 16.60  ? 87  THR A C   1 
ATOM   651  O  O   . THR A 1 87  ? 4.852  15.453  21.225  1.00 18.32  ? 87  THR A O   1 
ATOM   652  C  CB  . THR A 1 87  ? 1.847  16.340  21.487  1.00 31.74  ? 87  THR A CB  1 
ATOM   653  O  OG1 . THR A 1 87  ? 0.647  16.645  22.191  1.00 45.11  ? 87  THR A OG1 1 
ATOM   654  C  CG2 . THR A 1 87  ? 1.488  15.875  20.079  1.00 26.65  ? 87  THR A CG2 1 
ATOM   655  N  N   . TYR A 1 88  ? 3.799  13.519  20.910  1.00 13.23  ? 88  TYR A N   1 
ATOM   656  C  CA  . TYR A 1 88  ? 4.895  12.987  20.113  1.00 13.14  ? 88  TYR A CA  1 
ATOM   657  C  C   . TYR A 1 88  ? 4.400  12.692  18.686  1.00 13.21  ? 88  TYR A C   1 
ATOM   658  O  O   . TYR A 1 88  ? 3.441  11.931  18.511  1.00 17.08  ? 88  TYR A O   1 
ATOM   659  C  CB  . TYR A 1 88  ? 5.521  11.736  20.727  1.00 13.81  ? 88  TYR A CB  1 
ATOM   660  C  CG  . TYR A 1 88  ? 6.303  11.959  21.979  1.00 10.94  ? 88  TYR A CG  1 
ATOM   661  C  CD1 . TYR A 1 88  ? 5.692  12.368  23.170  1.00 13.09  ? 88  TYR A CD1 1 
ATOM   662  C  CD2 . TYR A 1 88  ? 7.674  11.729  21.963  1.00 11.65  ? 88  TYR A CD2 1 
ATOM   663  C  CE1 . TYR A 1 88  ? 6.452  12.572  24.321  1.00 14.34  ? 88  TYR A CE1 1 
ATOM   664  C  CE2 . TYR A 1 88  ? 8.451  11.918  23.090  1.00 11.41  ? 88  TYR A CE2 1 
ATOM   665  C  CZ  . TYR A 1 88  ? 7.832  12.273  24.290  1.00 12.12  ? 88  TYR A CZ  1 
ATOM   666  O  OH  . TYR A 1 88  ? 8.598  12.396  25.432  1.00 14.39  ? 88  TYR A OH  1 
ATOM   667  N  N   . ARG A 1 89  ? 5.050  13.275  17.686  1.00 12.65  ? 89  ARG A N   1 
ATOM   668  C  CA  . ARG A 1 89  ? 4.565  13.103  16.296  1.00 13.05  ? 89  ARG A CA  1 
ATOM   669  C  C   . ARG A 1 89  ? 5.236  11.913  15.610  1.00 10.54  ? 89  ARG A C   1 
ATOM   670  O  O   . ARG A 1 89  ? 6.463  11.763  15.655  1.00 10.42  ? 89  ARG A O   1 
ATOM   671  C  CB  . ARG A 1 89  ? 4.983  14.367  15.490  1.00 18.20  ? 89  ARG A CB  1 
ATOM   672  C  CG  . ARG A 1 89  ? 3.981  15.440  15.262  1.00 29.51  ? 89  ARG A CG  1 
ATOM   673  C  CD  . ARG A 1 89  ? 4.279  16.185  13.981  1.00 23.47  ? 89  ARG A CD  1 
ATOM   674  N  NE  . ARG A 1 89  ? 3.829  17.443  14.512  1.00 26.35  ? 89  ARG A NE  1 
ATOM   675  C  CZ  . ARG A 1 89  ? 4.305  18.646  14.266  1.00 24.84  ? 89  ARG A CZ  1 
ATOM   676  N  NH1 . ARG A 1 89  ? 5.282  18.859  13.382  1.00 28.16  ? 89  ARG A NH1 1 
ATOM   677  N  NH2 . ARG A 1 89  ? 3.730  19.627  14.935  1.00 37.38  ? 89  ARG A NH2 1 
ATOM   678  N  N   . LEU A 1 90  ? 4.418  11.124  14.899  1.00 10.80  ? 90  LEU A N   1 
ATOM   679  C  CA  . LEU A 1 90  ? 4.957  9.997   14.152  1.00 10.09  ? 90  LEU A CA  1 
ATOM   680  C  C   . LEU A 1 90  ? 5.795  10.496  12.984  1.00 10.17  ? 90  LEU A C   1 
ATOM   681  O  O   . LEU A 1 90  ? 5.318  11.234  12.126  1.00 13.17  ? 90  LEU A O   1 
ATOM   682  C  CB  . LEU A 1 90  ? 3.827  9.130   13.602  1.00 10.71  ? 90  LEU A CB  1 
ATOM   683  C  CG  . LEU A 1 90  ? 4.243  7.960   12.704  1.00 12.16  ? 90  LEU A CG  1 
ATOM   684  C  CD1 . LEU A 1 90  ? 5.029  6.899   13.504  1.00 12.62  ? 90  LEU A CD1 1 
ATOM   685  C  CD2 . LEU A 1 90  ? 3.019  7.312   12.075  1.00 13.65  ? 90  LEU A CD2 1 
ATOM   686  N  N   . LYS A 1 91  ? 7.040  10.061  12.929  1.00 9.98   ? 91  LYS A N   1 
ATOM   687  C  CA  . LYS A 1 91  ? 7.977  10.410  11.879  1.00 10.75  ? 91  LYS A CA  1 
ATOM   688  C  C   . LYS A 1 91  ? 8.162  9.297   10.849  1.00 9.99   ? 91  LYS A C   1 
ATOM   689  O  O   . LYS A 1 91  ? 8.172  9.538   9.652   1.00 10.69  ? 91  LYS A O   1 
ATOM   690  C  CB  . LYS A 1 91  ? 9.332  10.806  12.463  1.00 11.51  ? 91  LYS A CB  1 
ATOM   691  C  CG  . LYS A 1 91  ? 10.422 11.058  11.463  1.00 11.48  ? 91  LYS A CG  1 
ATOM   692  C  CD  . LYS A 1 91  ? 11.708 11.613  12.000  1.00 12.85  ? 91  LYS A CD  1 
ATOM   693  C  CE  . LYS A 1 91  ? 12.833 11.737  10.969  1.00 14.46  ? 91  LYS A CE  1 
ATOM   694  N  NZ  . LYS A 1 91  ? 12.457 12.631  9.837   1.00 20.05  ? 91  LYS A NZ  1 
ATOM   695  N  N   . GLN A 1 92  ? 8.300  8.046   11.333  1.00 10.12  ? 92  GLN A N   1 
ATOM   696  C  CA  . GLN A 1 92  ? 8.593  6.938   10.448  1.00 10.39  ? 92  GLN A CA  1 
ATOM   697  C  C   . GLN A 1 92  ? 8.362  5.667   11.228  1.00 9.54   ? 92  GLN A C   1 
ATOM   698  O  O   . GLN A 1 92  ? 8.335  5.692   12.449  1.00 9.79   ? 92  GLN A O   1 
ATOM   699  C  CB  . GLN A 1 92  ? 10.035 6.964   9.924   1.00 10.76  ? 92  GLN A CB  1 
ATOM   700  C  CG  . GLN A 1 92  ? 11.097 7.075   11.017  1.00 12.46  ? 92  GLN A CG  1 
ATOM   701  C  CD  . GLN A 1 92  ? 11.991 5.874   10.959  1.00 12.50  ? 92  GLN A CD  1 
ATOM   702  O  OE1 . GLN A 1 92  ? 11.535 4.759   11.282  1.00 12.76  ? 92  GLN A OE1 1 
ATOM   703  N  NE2 . GLN A 1 92  ? 13.156 6.061   10.345  1.00 18.35  ? 92  GLN A NE2 1 
ATOM   704  N  N   . PHE A 1 93  ? 8.203  4.553   10.488  1.00 8.78   ? 93  PHE A N   1 
ATOM   705  C  CA  . PHE A 1 93  ? 8.321  3.254   11.120  1.00 9.07   ? 93  PHE A CA  1 
ATOM   706  C  C   . PHE A 1 93  ? 9.323  2.428   10.347  1.00 8.74   ? 93  PHE A C   1 
ATOM   707  O  O   . PHE A 1 93  ? 9.561  2.637   9.162   1.00 9.14   ? 93  PHE A O   1 
ATOM   708  C  CB  . PHE A 1 93  ? 6.989  2.530   11.329  1.00 8.87   ? 93  PHE A CB  1 
ATOM   709  C  CG  . PHE A 1 93  ? 6.280  2.061   10.082  1.00 8.87   ? 93  PHE A CG  1 
ATOM   710  C  CD1 . PHE A 1 93  ? 6.703  0.932   9.372   1.00 9.90   ? 93  PHE A CD1 1 
ATOM   711  C  CD2 . PHE A 1 93  ? 5.134  2.713   9.633   1.00 9.66   ? 93  PHE A CD2 1 
ATOM   712  C  CE1 . PHE A 1 93  ? 6.021  0.512   8.237   1.00 10.97  ? 93  PHE A CE1 1 
ATOM   713  C  CE2 . PHE A 1 93  ? 4.473  2.314   8.477   1.00 10.54  ? 93  PHE A CE2 1 
ATOM   714  C  CZ  . PHE A 1 93  ? 4.906  1.183   7.790   1.00 10.86  ? 93  PHE A CZ  1 
ATOM   715  N  N   . HIS A 1 94  ? 9.866  1.394   11.026  1.00 8.31   ? 94  HIS A N   1 
ATOM   716  C  CA  . HIS A 1 94  ? 10.798 0.477   10.358  1.00 7.90   ? 94  HIS A CA  1 
ATOM   717  C  C   . HIS A 1 94  ? 10.758 -0.842  11.083  1.00 7.52   ? 94  HIS A C   1 
ATOM   718  O  O   . HIS A 1 94  ? 10.108 -0.977  12.133  1.00 8.51   ? 94  HIS A O   1 
ATOM   719  C  CB  . HIS A 1 94  ? 12.234 1.085   10.360  1.00 8.70   ? 94  HIS A CB  1 
ATOM   720  C  CG  . HIS A 1 94  ? 12.747 1.310   11.718  1.00 7.95   ? 94  HIS A CG  1 
ATOM   721  N  ND1 . HIS A 1 94  ? 12.678 2.529   12.370  1.00 8.82   ? 94  HIS A ND1 1 
ATOM   722  C  CD2 . HIS A 1 94  ? 13.356 0.475   12.628  1.00 8.32   ? 94  HIS A CD2 1 
ATOM   723  C  CE1 . HIS A 1 94  ? 13.202 2.419   13.584  1.00 7.83   ? 94  HIS A CE1 1 
ATOM   724  N  NE2 . HIS A 1 94  ? 13.644 1.161   13.797  1.00 7.61   ? 94  HIS A NE2 1 
ATOM   725  N  N   . PHE A 1 95  ? 11.485 -1.833  10.535  1.00 8.09   ? 95  PHE A N   1 
ATOM   726  C  CA  . PHE A 1 95  ? 11.532 -3.156  11.118  1.00 8.13   ? 95  PHE A CA  1 
ATOM   727  C  C   . PHE A 1 95  ? 12.976 -3.568  11.289  1.00 7.70   ? 95  PHE A C   1 
ATOM   728  O  O   . PHE A 1 95  ? 13.865 -3.148  10.558  1.00 8.89   ? 95  PHE A O   1 
ATOM   729  C  CB  . PHE A 1 95  ? 10.857 -4.214  10.231  1.00 9.39   ? 95  PHE A CB  1 
ATOM   730  C  CG  . PHE A 1 95  ? 9.387  -3.937  9.986   1.00 9.17   ? 95  PHE A CG  1 
ATOM   731  C  CD1 . PHE A 1 95  ? 8.992  -3.041  8.976   1.00 10.56  ? 95  PHE A CD1 1 
ATOM   732  C  CD2 . PHE A 1 95  ? 8.409  -4.612  10.714  1.00 9.81   ? 95  PHE A CD2 1 
ATOM   733  C  CE1 . PHE A 1 95  ? 7.632  -2.871  8.686   1.00 12.03  ? 95  PHE A CE1 1 
ATOM   734  C  CE2 . PHE A 1 95  ? 7.045  -4.418  10.447  1.00 10.72  ? 95  PHE A CE2 1 
ATOM   735  C  CZ  . PHE A 1 95  ? 6.675  -3.554  9.417   1.00 12.38  ? 95  PHE A CZ  1 
ATOM   736  N  N   . HIS A 1 96  ? 13.174 -4.447  12.281  1.00 8.32   ? 96  HIS A N   1 
ATOM   737  C  CA  . HIS A 1 96  ? 14.377 -5.250  12.404  1.00 8.03   ? 96  HIS A CA  1 
ATOM   738  C  C   . HIS A 1 96  ? 13.949 -6.714  12.317  1.00 8.17   ? 96  HIS A C   1 
ATOM   739  O  O   . HIS A 1 96  ? 12.866 -7.063  12.795  1.00 8.99   ? 96  HIS A O   1 
ATOM   740  C  CB  . HIS A 1 96  ? 15.031 -5.034  13.786  1.00 8.56   ? 96  HIS A CB  1 
ATOM   741  C  CG  . HIS A 1 96  ? 15.299 -3.605  14.122  1.00 7.52   ? 96  HIS A CG  1 
ATOM   742  N  ND1 . HIS A 1 96  ? 16.555 -3.028  13.984  1.00 7.72   ? 96  HIS A ND1 1 
ATOM   743  C  CD2 . HIS A 1 96  ? 14.491 -2.604  14.536  1.00 7.60   ? 96  HIS A CD2 1 
ATOM   744  C  CE1 . HIS A 1 96  ? 16.476 -1.728  14.346  1.00 8.67   ? 96  HIS A CE1 1 
ATOM   745  N  NE2 . HIS A 1 96  ? 15.197 -1.421  14.672  1.00 8.26   ? 96  HIS A NE2 1 
ATOM   746  N  N   . TRP A 1 97  ? 14.771 -7.564  11.683  1.00 8.07   ? 97  TRP A N   1 
ATOM   747  C  CA  . TRP A 1 97  ? 14.348 -8.962  11.506  1.00 8.59   ? 97  TRP A CA  1 
ATOM   748  C  C   . TRP A 1 97  ? 15.545 -9.856  11.386  1.00 8.68   ? 97  TRP A C   1 
ATOM   749  O  O   . TRP A 1 97  ? 16.711 -9.454  11.290  1.00 8.94   ? 97  TRP A O   1 
ATOM   750  C  CB  . TRP A 1 97  ? 13.431 -9.096  10.294  1.00 9.05   ? 97  TRP A CB  1 
ATOM   751  C  CG  . TRP A 1 97  ? 14.106 -8.750  8.991   1.00 8.99   ? 97  TRP A CG  1 
ATOM   752  C  CD1 . TRP A 1 97  ? 14.779 -9.612  8.172   1.00 9.51   ? 97  TRP A CD1 1 
ATOM   753  C  CD2 . TRP A 1 97  ? 14.173 -7.447  8.383   1.00 8.10   ? 97  TRP A CD2 1 
ATOM   754  N  NE1 . TRP A 1 97  ? 15.265 -8.938  7.056   1.00 10.05  ? 97  TRP A NE1 1 
ATOM   755  C  CE2 . TRP A 1 97  ? 14.865 -7.609  7.171   1.00 8.73   ? 97  TRP A CE2 1 
ATOM   756  C  CE3 . TRP A 1 97  ? 13.662 -6.178  8.725   1.00 8.99   ? 97  TRP A CE3 1 
ATOM   757  C  CZ2 . TRP A 1 97  ? 15.111 -6.536  6.311   1.00 10.13  ? 97  TRP A CZ2 1 
ATOM   758  C  CZ3 . TRP A 1 97  ? 13.940 -5.107  7.907   1.00 9.83   ? 97  TRP A CZ3 1 
ATOM   759  C  CH2 . TRP A 1 97  ? 14.612 -5.294  6.687   1.00 9.75   ? 97  TRP A CH2 1 
ATOM   760  N  N   . GLY A 1 98  ? 15.246 -11.171 11.425  1.00 9.07   ? 98  GLY A N   1 
ATOM   761  C  CA  . GLY A 1 98  ? 16.271 -12.197 11.466  1.00 9.69   ? 98  GLY A CA  1 
ATOM   762  C  C   . GLY A 1 98  ? 16.468 -12.963 10.174  1.00 9.19   ? 98  GLY A C   1 
ATOM   763  O  O   . GLY A 1 98  ? 15.728 -12.830 9.228   1.00 10.53  ? 98  GLY A O   1 
ATOM   764  N  N   . SER A 1 99  ? 17.460 -13.877 10.226  1.00 10.34  ? 99  SER A N   1 
ATOM   765  C  CA  . SER A 1 99  ? 17.647 -14.857 9.151   1.00 11.40  ? 99  SER A CA  1 
ATOM   766  C  C   . SER A 1 99  ? 16.795 -16.112 9.353   1.00 11.01  ? 99  SER A C   1 
ATOM   767  O  O   . SER A 1 99  ? 16.680 -16.911 8.423   1.00 14.18  ? 99  SER A O   1 
ATOM   768  C  CB  . SER A 1 99  ? 19.123 -15.180 9.063   1.00 12.95  ? 99  SER A CB  1 
ATOM   769  O  OG  . SER A 1 99  ? 19.605 -15.611 10.313  1.00 13.30  ? 99  SER A OG  1 
ATOM   770  N  N   . LEU A 1 100 ? 16.251 -16.317 10.570  1.00 11.16  ? 100 LEU A N   1 
ATOM   771  C  CA  . LEU A 1 100 ? 15.474 -17.481 10.964  1.00 11.27  ? 100 LEU A CA  1 
ATOM   772  C  C   . LEU A 1 100 ? 14.314 -16.976 11.757  1.00 12.48  ? 100 LEU A C   1 
ATOM   773  O  O   . LEU A 1 100 ? 14.415 -15.929 12.423  1.00 12.15  ? 100 LEU A O   1 
ATOM   774  C  CB  . LEU A 1 100 ? 16.341 -18.392 11.839  1.00 13.25  ? 100 LEU A CB  1 
ATOM   775  C  CG  . LEU A 1 100 ? 17.623 -18.947 11.219  1.00 14.25  ? 100 LEU A CG  1 
ATOM   776  C  CD1 . LEU A 1 100 ? 18.485 -19.624 12.294  1.00 17.13  ? 100 LEU A CD1 1 
ATOM   777  C  CD2 . LEU A 1 100 ? 17.240 -19.971 10.132  1.00 17.09  ? 100 LEU A CD2 1 
ATOM   778  N  N   . ASP A 1 101 ? 13.247 -17.751 11.839  1.00 12.23  ? 101 ASP A N   1 
ATOM   779  C  CA  . ASP A 1 101 ? 12.021 -17.271 12.471  1.00 12.89  ? 101 ASP A CA  1 
ATOM   780  C  C   . ASP A 1 101 ? 12.173 -17.101 13.972  1.00 13.48  ? 101 ASP A C   1 
ATOM   781  O  O   . ASP A 1 101 ? 11.357 -16.363 14.548  1.00 17.30  ? 101 ASP A O   1 
ATOM   782  C  CB  . ASP A 1 101 ? 10.847 -18.221 12.202  1.00 13.62  ? 101 ASP A CB  1 
ATOM   783  C  CG  . ASP A 1 101 ? 10.398 -18.302 10.736  1.00 16.05  ? 101 ASP A CG  1 
ATOM   784  O  OD1 . ASP A 1 101 ? 10.748 -17.444 9.908   1.00 15.27  ? 101 ASP A OD1 1 
ATOM   785  O  OD2 . ASP A 1 101 ? 9.740  -19.286 10.392  1.00 21.77  ? 101 ASP A OD2 1 
ATOM   786  N  N   . GLY A 1 102 ? 13.172 -17.722 14.603  1.00 13.99  ? 102 GLY A N   1 
ATOM   787  C  CA  . GLY A 1 102 ? 13.371 -17.567 16.051  1.00 16.70  ? 102 GLY A CA  1 
ATOM   788  C  C   . GLY A 1 102 ? 14.349 -16.465 16.478  1.00 14.11  ? 102 GLY A C   1 
ATOM   789  O  O   . GLY A 1 102 ? 14.786 -16.461 17.634  1.00 15.01  ? 102 GLY A O   1 
ATOM   790  N  N   . GLN A 1 103 ? 14.691 -15.549 15.550  1.00 12.05  ? 103 GLN A N   1 
ATOM   791  C  CA  . GLN A 1 103 ? 15.489 -14.418 15.973  1.00 11.53  ? 103 GLN A CA  1 
ATOM   792  C  C   . GLN A 1 103 ? 15.082 -13.255 15.058  1.00 9.98   ? 103 GLN A C   1 
ATOM   793  O  O   . GLN A 1 103 ? 14.564 -13.459 13.970  1.00 10.46  ? 103 GLN A O   1 
ATOM   794  C  CB  . GLN A 1 103 ? 16.975 -14.713 15.863  1.00 11.15  ? 103 GLN A CB  1 
ATOM   795  C  CG  . GLN A 1 103 ? 17.421 -14.982 14.425  1.00 11.28  ? 103 GLN A CG  1 
ATOM   796  C  CD  . GLN A 1 103 ? 18.752 -15.650 14.395  1.00 12.76  ? 103 GLN A CD  1 
ATOM   797  O  OE1 . GLN A 1 103 ? 18.858 -16.773 14.882  1.00 15.57  ? 103 GLN A OE1 1 
ATOM   798  N  NE2 . GLN A 1 103 ? 19.764 -15.080 13.769  1.00 13.08  ? 103 GLN A NE2 1 
ATOM   799  N  N   . GLY A 1 104 ? 15.455 -12.034 15.491  1.00 10.16  ? 104 GLY A N   1 
ATOM   800  C  CA  . GLY A 1 104 ? 15.133 -10.844 14.675  1.00 8.90   ? 104 GLY A CA  1 
ATOM   801  C  C   . GLY A 1 104 ? 14.692 -9.683  15.523  1.00 8.50   ? 104 GLY A C   1 
ATOM   802  O  O   . GLY A 1 104 ? 14.926 -8.526  15.146  1.00 9.85   ? 104 GLY A O   1 
ATOM   803  N  N   . SER A 1 105 ? 13.990 -9.935  16.646  1.00 8.20   ? 105 SER A N   1 
ATOM   804  C  CA  . SER A 1 105 ? 13.583 -8.836  17.484  1.00 8.45   ? 105 SER A CA  1 
ATOM   805  C  C   . SER A 1 105 ? 14.790 -8.294  18.215  1.00 8.34   ? 105 SER A C   1 
ATOM   806  O  O   . SER A 1 105 ? 15.821 -8.948  18.411  1.00 9.38   ? 105 SER A O   1 
ATOM   807  C  CB  . SER A 1 105 ? 12.501 -9.225  18.463  1.00 8.93   ? 105 SER A CB  1 
ATOM   808  O  OG  . SER A 1 105 ? 12.880 -10.201 19.389  1.00 9.16   ? 105 SER A OG  1 
ATOM   809  N  N   . GLU A 1 106 ? 14.650 -7.043  18.656  1.00 8.58   ? 106 GLU A N   1 
ATOM   810  C  CA  . GLU A 1 106 ? 15.671 -6.352  19.460  1.00 8.20   ? 106 GLU A CA  1 
ATOM   811  C  C   . GLU A 1 106 ? 15.367 -6.568  20.937  1.00 8.07   ? 106 GLU A C   1 
ATOM   812  O  O   . GLU A 1 106 ? 16.153 -7.152  21.676  1.00 8.62   ? 106 GLU A O   1 
ATOM   813  C  CB  . GLU A 1 106 ? 15.737 -4.867  19.092  1.00 9.05   ? 106 GLU A CB  1 
ATOM   814  C  CG  . GLU A 1 106 ? 16.097 -4.704  17.592  1.00 10.33  ? 106 GLU A CG  1 
ATOM   815  C  CD  . GLU A 1 106 ? 16.839 -3.417  17.350  1.00 9.13   ? 106 GLU A CD  1 
ATOM   816  O  OE1 . GLU A 1 106 ? 16.254 -2.368  17.634  1.00 9.57   ? 106 GLU A OE1 1 
ATOM   817  O  OE2 . GLU A 1 106 ? 18.009 -3.488  16.954  1.00 10.00  ? 106 GLU A OE2 1 
ATOM   818  N  N   . HIS A 1 107 ? 14.168 -6.140  21.363  1.00 8.57   ? 107 HIS A N   1 
ATOM   819  C  CA  . HIS A 1 107 ? 13.742 -6.550  22.705  1.00 8.35   ? 107 HIS A CA  1 
ATOM   820  C  C   . HIS A 1 107 ? 13.463 -8.049  22.738  1.00 7.87   ? 107 HIS A C   1 
ATOM   821  O  O   . HIS A 1 107 ? 13.121 -8.660  21.702  1.00 8.97   ? 107 HIS A O   1 
ATOM   822  C  CB  . HIS A 1 107 ? 12.482 -5.776  23.125  1.00 8.42   ? 107 HIS A CB  1 
ATOM   823  C  CG  . HIS A 1 107 ? 12.775 -4.310  23.255  1.00 7.87   ? 107 HIS A CG  1 
ATOM   824  N  ND1 . HIS A 1 107 ? 12.746 -3.417  22.208  1.00 8.53   ? 107 HIS A ND1 1 
ATOM   825  C  CD2 . HIS A 1 107 ? 13.269 -3.623  24.330  1.00 8.51   ? 107 HIS A CD2 1 
ATOM   826  C  CE1 . HIS A 1 107 ? 13.149 -2.224  22.672  1.00 9.43   ? 107 HIS A CE1 1 
ATOM   827  N  NE2 . HIS A 1 107 ? 13.507 -2.317  23.970  1.00 8.65   ? 107 HIS A NE2 1 
ATOM   828  N  N   . THR A 1 108 ? 13.581 -8.606  23.932  1.00 8.95   ? 108 THR A N   1 
ATOM   829  C  CA  . THR A 1 108 ? 13.192 -9.996  24.151  1.00 9.10   ? 108 THR A CA  1 
ATOM   830  C  C   . THR A 1 108 ? 12.241 -10.004 25.338  1.00 9.46   ? 108 THR A C   1 
ATOM   831  O  O   . THR A 1 108 ? 12.224 -9.049  26.144  1.00 10.37  ? 108 THR A O   1 
ATOM   832  C  CB  . THR A 1 108 ? 14.425 -10.877 24.361  1.00 11.06  ? 108 THR A CB  1 
ATOM   833  O  OG1 . THR A 1 108 ? 15.227 -10.392 25.455  1.00 11.12  ? 108 THR A OG1 1 
ATOM   834  C  CG2 . THR A 1 108 ? 15.253 -10.961 23.114  1.00 11.92  ? 108 THR A CG2 1 
ATOM   835  N  N   . VAL A 1 109 ? 11.483 -11.105 25.465  1.00 10.78  ? 109 VAL A N   1 
ATOM   836  C  CA  . VAL A 1 109 ? 10.540 -11.172 26.574  1.00 12.67  ? 109 VAL A CA  1 
ATOM   837  C  C   . VAL A 1 109 ? 10.855 -12.479 27.309  1.00 12.82  ? 109 VAL A C   1 
ATOM   838  O  O   . VAL A 1 109 ? 10.694 -13.571 26.762  1.00 13.86  ? 109 VAL A O   1 
ATOM   839  C  CB  . VAL A 1 109 ? 9.074  -11.181 26.040  1.00 12.40  ? 109 VAL A CB  1 
ATOM   840  C  CG1 . VAL A 1 109 ? 8.039  -11.289 27.161  1.00 15.30  ? 109 VAL A CG1 1 
ATOM   841  C  CG2 . VAL A 1 109 ? 8.768  -9.906  25.245  1.00 13.57  ? 109 VAL A CG2 1 
ATOM   842  N  N   . ASP A 1 110 ? 11.352 -12.377 28.551  1.00 12.30  ? 110 ASP A N   1 
ATOM   843  C  CA  . ASP A 1 110 ? 11.773 -13.598 29.257  1.00 14.57  ? 110 ASP A CA  1 
ATOM   844  C  C   . ASP A 1 110 ? 12.748 -14.386 28.369  1.00 14.18  ? 110 ASP A C   1 
ATOM   845  O  O   . ASP A 1 110 ? 12.689 -15.606 28.314  1.00 15.71  ? 110 ASP A O   1 
ATOM   846  C  CB  . ASP A 1 110 ? 10.574 -14.433 29.743  1.00 17.81  ? 110 ASP A CB  1 
ATOM   847  C  CG  . ASP A 1 110 ? 9.756  -13.673 30.767  1.00 18.45  ? 110 ASP A CG  1 
ATOM   848  O  OD1 . ASP A 1 110 ? 10.319 -12.808 31.467  1.00 18.58  ? 110 ASP A OD1 1 
ATOM   849  O  OD2 . ASP A 1 110 ? 8.577  -13.923 30.843  1.00 23.06  ? 110 ASP A OD2 1 
ATOM   850  N  N   . LYS A 1 111 ? 13.639 -13.671 27.687  1.00 12.77  ? 111 LYS A N   1 
ATOM   851  C  CA  . LYS A 1 111 ? 14.692 -14.163 26.835  1.00 13.06  ? 111 LYS A CA  1 
ATOM   852  C  C   . LYS A 1 111 ? 14.144 -14.674 25.494  1.00 13.34  ? 111 LYS A C   1 
ATOM   853  O  O   . LYS A 1 111 ? 14.929 -14.992 24.597  1.00 14.92  ? 111 LYS A O   1 
ATOM   854  C  CB  . LYS A 1 111 ? 15.643 -15.167 27.521  1.00 15.49  ? 111 LYS A CB  1 
ATOM   855  C  CG  . LYS A 1 111 ? 16.336 -14.624 28.778  1.00 21.02  ? 111 LYS A CG  1 
ATOM   856  C  CD  . LYS A 1 111 ? 17.262 -13.505 28.377  1.00 22.29  ? 111 LYS A CD  1 
ATOM   857  C  CE  . LYS A 1 111 ? 17.997 -12.845 29.518  1.00 29.34  ? 111 LYS A CE  1 
ATOM   858  N  NZ  . LYS A 1 111 ? 19.065 -13.738 29.921  1.00 35.32  ? 111 LYS A NZ  1 
ATOM   859  N  N   A LYS A 1 112 ? 12.816 -14.578 25.247  0.50 13.17  ? 112 LYS A N   1 
ATOM   860  N  N   B LYS A 1 112 ? 12.812 -14.615 25.269  0.50 13.36  ? 112 LYS A N   1 
ATOM   861  C  CA  A LYS A 1 112 ? 12.307 -15.068 23.978  0.50 13.25  ? 112 LYS A CA  1 
ATOM   862  C  CA  B LYS A 1 112 ? 12.281 -15.045 23.987  0.50 13.60  ? 112 LYS A CA  1 
ATOM   863  C  C   A LYS A 1 112 ? 12.512 -13.993 22.915  0.50 11.75  ? 112 LYS A C   1 
ATOM   864  C  C   B LYS A 1 112 ? 12.573 -13.977 22.937  0.50 12.36  ? 112 LYS A C   1 
ATOM   865  O  O   A LYS A 1 112 ? 12.144 -12.834 23.128  0.50 10.28  ? 112 LYS A O   1 
ATOM   866  O  O   B LYS A 1 112 ? 12.303 -12.801 23.174  0.50 12.63  ? 112 LYS A O   1 
ATOM   867  C  CB  A LYS A 1 112 ? 10.776 -15.199 24.056  0.50 15.67  ? 112 LYS A CB  1 
ATOM   868  C  CB  B LYS A 1 112 ? 10.748 -15.116 24.052  0.50 16.42  ? 112 LYS A CB  1 
ATOM   869  C  CG  A LYS A 1 112 ? 10.079 -15.740 22.810  0.50 17.74  ? 112 LYS A CG  1 
ATOM   870  C  CG  B LYS A 1 112 ? 10.009 -15.337 22.733  0.50 17.11  ? 112 LYS A CG  1 
ATOM   871  C  CD  A LYS A 1 112 ? 8.567  -15.606 22.846  0.50 19.92  ? 112 LYS A CD  1 
ATOM   872  C  CD  B LYS A 1 112 ? 8.558  -15.778 22.913  0.50 20.25  ? 112 LYS A CD  1 
ATOM   873  C  CE  A LYS A 1 112 ? 7.976  -15.767 21.462  0.50 20.79  ? 112 LYS A CE  1 
ATOM   874  C  CE  B LYS A 1 112 ? 7.971  -16.276 21.601  0.50 18.83  ? 112 LYS A CE  1 
ATOM   875  N  NZ  A LYS A 1 112 ? 8.100  -17.154 20.964  0.50 22.55  ? 112 LYS A NZ  1 
ATOM   876  N  NZ  B LYS A 1 112 ? 6.512  -16.529 21.677  0.50 19.75  ? 112 LYS A NZ  1 
ATOM   877  N  N   . LYS A 1 113 ? 13.053 -14.418 21.767  1.00 12.33  ? 113 LYS A N   1 
ATOM   878  C  CA  . LYS A 1 113 ? 13.218 -13.592 20.594  1.00 11.78  ? 113 LYS A CA  1 
ATOM   879  C  C   . LYS A 1 113 ? 12.080 -13.854 19.636  1.00 10.87  ? 113 LYS A C   1 
ATOM   880  O  O   . LYS A 1 113 ? 11.663 -14.982 19.463  1.00 16.40  ? 113 LYS A O   1 
ATOM   881  C  CB  . LYS A 1 113 ? 14.544 -13.901 19.910  1.00 13.22  ? 113 LYS A CB  1 
ATOM   882  C  CG  . LYS A 1 113 ? 15.784 -13.576 20.715  1.00 12.71  ? 113 LYS A CG  1 
ATOM   883  C  CD  . LYS A 1 113 ? 17.046 -14.197 20.054  1.00 14.30  ? 113 LYS A CD  1 
ATOM   884  C  CE  . LYS A 1 113 ? 18.223 -13.587 20.762  1.00 16.76  ? 113 LYS A CE  1 
ATOM   885  N  NZ  . LYS A 1 113 ? 19.359 -14.449 20.934  1.00 31.00  ? 113 LYS A NZ  1 
ATOM   886  N  N   . TYR A 1 114 ? 11.586 -12.793 19.020  1.00 10.97  ? 114 TYR A N   1 
ATOM   887  C  CA  . TYR A 1 114 ? 10.578 -12.896 17.981  1.00 10.21  ? 114 TYR A CA  1 
ATOM   888  C  C   . TYR A 1 114 ? 11.224 -12.790 16.605  1.00 9.62   ? 114 TYR A C   1 
ATOM   889  O  O   . TYR A 1 114 ? 12.442 -12.477 16.470  1.00 10.60  ? 114 TYR A O   1 
ATOM   890  C  CB  . TYR A 1 114 ? 9.505  -11.815 18.137  1.00 10.04  ? 114 TYR A CB  1 
ATOM   891  C  CG  . TYR A 1 114 ? 8.641  -12.037 19.341  1.00 10.22  ? 114 TYR A CG  1 
ATOM   892  C  CD1 . TYR A 1 114 ? 8.978  -11.590 20.594  1.00 12.47  ? 114 TYR A CD1 1 
ATOM   893  C  CD2 . TYR A 1 114 ? 7.438  -12.703 19.172  1.00 11.88  ? 114 TYR A CD2 1 
ATOM   894  C  CE1 . TYR A 1 114 ? 8.153  -11.819 21.674  1.00 15.80  ? 114 TYR A CE1 1 
ATOM   895  C  CE2 . TYR A 1 114 ? 6.568  -12.886 20.231  1.00 16.53  ? 114 TYR A CE2 1 
ATOM   896  C  CZ  . TYR A 1 114 ? 6.937  -12.445 21.487  1.00 16.87  ? 114 TYR A CZ  1 
ATOM   897  O  OH  . TYR A 1 114 ? 6.081  -12.585 22.583  1.00 24.91  ? 114 TYR A OH  1 
ATOM   898  N  N   . ALA A 1 115 ? 10.457 -13.071 15.541  1.00 9.82   ? 115 ALA A N   1 
ATOM   899  C  CA  . ALA A 1 115 ? 11.019 -13.080 14.187  1.00 9.89   ? 115 ALA A CA  1 
ATOM   900  C  C   . ALA A 1 115 ? 11.402 -11.686 13.728  1.00 9.54   ? 115 ALA A C   1 
ATOM   901  O  O   . ALA A 1 115 ? 12.218 -11.533 12.824  1.00 10.11  ? 115 ALA A O   1 
ATOM   902  C  CB  . ALA A 1 115 ? 10.016 -13.674 13.237  1.00 11.28  ? 115 ALA A CB  1 
ATOM   903  N  N   . ALA A 1 116 ? 10.741 -10.670 14.268  1.00 9.07   ? 116 ALA A N   1 
ATOM   904  C  CA  . ALA A 1 116 ? 10.988 -9.286  13.810  1.00 8.93   ? 116 ALA A CA  1 
ATOM   905  C  C   . ALA A 1 116 ? 10.416 -8.364  14.877  1.00 8.28   ? 116 ALA A C   1 
ATOM   906  O  O   . ALA A 1 116 ? 9.673  -8.793  15.749  1.00 8.66   ? 116 ALA A O   1 
ATOM   907  C  CB  . ALA A 1 116 ? 10.395 -9.008  12.434  1.00 10.43  ? 116 ALA A CB  1 
ATOM   908  N  N   . GLU A 1 117 ? 10.741 -7.075  14.731  1.00 8.27   ? 117 GLU A N   1 
ATOM   909  C  CA  . GLU A 1 117 ? 10.176 -6.050  15.612  1.00 8.50   ? 117 GLU A CA  1 
ATOM   910  C  C   . GLU A 1 117 ? 9.968  -4.815  14.787  1.00 7.87   ? 117 GLU A C   1 
ATOM   911  O  O   . GLU A 1 117 ? 10.864 -4.385  14.051  1.00 9.50   ? 117 GLU A O   1 
ATOM   912  C  CB  . GLU A 1 117 ? 11.162 -5.829  16.761  1.00 8.26   ? 117 GLU A CB  1 
ATOM   913  C  CG  . GLU A 1 117 ? 10.615 -4.922  17.862  1.00 8.80   ? 117 GLU A CG  1 
ATOM   914  C  CD  . GLU A 1 117 ? 11.539 -4.864  19.056  1.00 8.83   ? 117 GLU A CD  1 
ATOM   915  O  OE1 . GLU A 1 117 ? 12.199 -5.875  19.374  1.00 9.59   ? 117 GLU A OE1 1 
ATOM   916  O  OE2 . GLU A 1 117 ? 11.596 -3.806  19.736  1.00 9.94   ? 117 GLU A OE2 1 
ATOM   917  N  N   . LEU A 1 118 ? 8.757  -4.270  14.923  1.00 8.14   ? 118 LEU A N   1 
ATOM   918  C  CA  . LEU A 1 118 ? 8.335  -3.020  14.296  1.00 7.76   ? 118 LEU A CA  1 
ATOM   919  C  C   . LEU A 1 118 ? 8.560  -1.885  15.313  1.00 7.74   ? 118 LEU A C   1 
ATOM   920  O  O   . LEU A 1 118 ? 8.144  -1.982  16.450  1.00 7.97   ? 118 LEU A O   1 
ATOM   921  C  CB  . LEU A 1 118 ? 6.843  -3.179  13.925  1.00 8.97   ? 118 LEU A CB  1 
ATOM   922  C  CG  . LEU A 1 118 ? 6.058  -1.875  13.637  1.00 8.69   ? 118 LEU A CG  1 
ATOM   923  C  CD1 . LEU A 1 118 ? 6.618  -1.170  12.392  1.00 9.84   ? 118 LEU A CD1 1 
ATOM   924  C  CD2 . LEU A 1 118 ? 4.605  -2.283  13.399  1.00 10.82  ? 118 LEU A CD2 1 
ATOM   925  N  N   . HIS A 1 119 ? 9.185  -0.811  14.794  1.00 7.51   ? 119 HIS A N   1 
ATOM   926  C  CA  . HIS A 1 119 ? 9.405  0.400   15.597  1.00 7.94   ? 119 HIS A CA  1 
ATOM   927  C  C   . HIS A 1 119 ? 8.699  1.581   14.929  1.00 7.30   ? 119 HIS A C   1 
ATOM   928  O  O   . HIS A 1 119 ? 9.062  1.907   13.771  1.00 8.82   ? 119 HIS A O   1 
ATOM   929  C  CB  . HIS A 1 119 ? 10.913 0.683   15.661  1.00 8.04   ? 119 HIS A CB  1 
ATOM   930  C  CG  . HIS A 1 119 ? 11.601 -0.288  16.577  1.00 7.26   ? 119 HIS A CG  1 
ATOM   931  N  ND1 . HIS A 1 119 ? 12.968 -0.454  16.559  1.00 7.43   ? 119 HIS A ND1 1 
ATOM   932  C  CD2 . HIS A 1 119 ? 11.080 -1.156  17.503  1.00 7.67   ? 119 HIS A CD2 1 
ATOM   933  C  CE1 . HIS A 1 119 ? 13.269 -1.412  17.450  1.00 7.82   ? 119 HIS A CE1 1 
ATOM   934  N  NE2 . HIS A 1 119 ? 12.116 -1.833  18.041  1.00 7.96   ? 119 HIS A NE2 1 
ATOM   935  N  N   . LEU A 1 120 ? 7.720  2.164   15.630  1.00 7.71   ? 120 LEU A N   1 
ATOM   936  C  CA  . LEU A 1 120 ? 7.067  3.406   15.187  1.00 8.05   ? 120 LEU A CA  1 
ATOM   937  C  C   . LEU A 1 120 ? 7.700  4.530   15.987  1.00 8.00   ? 120 LEU A C   1 
ATOM   938  O  O   . LEU A 1 120 ? 7.588  4.565   17.204  1.00 8.39   ? 120 LEU A O   1 
ATOM   939  C  CB  . LEU A 1 120 ? 5.578  3.315   15.383  1.00 8.96   ? 120 LEU A CB  1 
ATOM   940  C  CG  . LEU A 1 120 ? 4.888  2.231   14.541  1.00 9.88   ? 120 LEU A CG  1 
ATOM   941  C  CD1 . LEU A 1 120 ? 4.138  1.253   15.458  1.00 14.14  ? 120 LEU A CD1 1 
ATOM   942  C  CD2 . LEU A 1 120 ? 3.943  2.871   13.554  1.00 12.91  ? 120 LEU A CD2 1 
ATOM   943  N  N   . VAL A 1 121 ? 8.432  5.384   15.264  1.00 9.09   ? 121 VAL A N   1 
ATOM   944  C  CA  . VAL A 1 121 ? 9.262  6.412   15.931  1.00 8.44   ? 121 VAL A CA  1 
ATOM   945  C  C   . VAL A 1 121 ? 8.561  7.770   15.919  1.00 8.50   ? 121 VAL A C   1 
ATOM   946  O  O   . VAL A 1 121 ? 8.156  8.266   14.863  1.00 9.69   ? 121 VAL A O   1 
ATOM   947  C  CB  . VAL A 1 121 ? 10.606 6.544   15.197  1.00 9.24   ? 121 VAL A CB  1 
ATOM   948  C  CG1 . VAL A 1 121 ? 11.510 7.584   15.874  1.00 11.98  ? 121 VAL A CG1 1 
ATOM   949  C  CG2 . VAL A 1 121 ? 11.340 5.191   15.103  1.00 10.32  ? 121 VAL A CG2 1 
ATOM   950  N  N   . HIS A 1 122 ? 8.482  8.369   17.124  1.00 8.50   ? 122 HIS A N   1 
ATOM   951  C  CA  . HIS A 1 122 ? 7.764  9.633   17.306  1.00 8.67   ? 122 HIS A CA  1 
ATOM   952  C  C   . HIS A 1 122 ? 8.707  10.590  18.018  1.00 8.34   ? 122 HIS A C   1 
ATOM   953  O  O   . HIS A 1 122 ? 9.494  10.160  18.861  1.00 10.42  ? 122 HIS A O   1 
ATOM   954  C  CB  . HIS A 1 122 ? 6.518  9.468   18.184  1.00 9.33   ? 122 HIS A CB  1 
ATOM   955  C  CG  . HIS A 1 122 ? 5.625  8.327   17.790  1.00 9.00   ? 122 HIS A CG  1 
ATOM   956  N  ND1 . HIS A 1 122 ? 5.979  7.003   18.040  1.00 9.29   ? 122 HIS A ND1 1 
ATOM   957  C  CD2 . HIS A 1 122 ? 4.400  8.285   17.211  1.00 9.98   ? 122 HIS A CD2 1 
ATOM   958  C  CE1 . HIS A 1 122 ? 4.962  6.234   17.627  1.00 10.16  ? 122 HIS A CE1 1 
ATOM   959  N  NE2 . HIS A 1 122 ? 3.996  6.976   17.095  1.00 10.02  ? 122 HIS A NE2 1 
ATOM   960  N  N   . TRP A 1 123 ? 8.618  11.887  17.704  1.00 8.81   ? 123 TRP A N   1 
ATOM   961  C  CA  . TRP A 1 123 ? 9.462  12.885  18.379  1.00 9.10   ? 123 TRP A CA  1 
ATOM   962  C  C   . TRP A 1 123 ? 8.601  13.893  19.122  1.00 10.06  ? 123 TRP A C   1 
ATOM   963  O  O   . TRP A 1 123 ? 7.475  14.254  18.707  1.00 10.77  ? 123 TRP A O   1 
ATOM   964  C  CB  . TRP A 1 123 ? 10.457 13.558  17.466  1.00 10.89  ? 123 TRP A CB  1 
ATOM   965  C  CG  . TRP A 1 123 ? 9.818  14.180  16.260  1.00 10.75  ? 123 TRP A CG  1 
ATOM   966  C  CD1 . TRP A 1 123 ? 9.584  13.546  15.053  1.00 11.96  ? 123 TRP A CD1 1 
ATOM   967  C  CD2 . TRP A 1 123 ? 9.440  15.547  16.056  1.00 11.03  ? 123 TRP A CD2 1 
ATOM   968  N  NE1 . TRP A 1 123 ? 9.065  14.401  14.137  1.00 12.39  ? 123 TRP A NE1 1 
ATOM   969  C  CE2 . TRP A 1 123 ? 8.982  15.666  14.728  1.00 12.75  ? 123 TRP A CE2 1 
ATOM   970  C  CE3 . TRP A 1 123 ? 9.481  16.703  16.874  1.00 12.19  ? 123 TRP A CE3 1 
ATOM   971  C  CZ2 . TRP A 1 123 ? 8.510  16.872  14.199  1.00 15.62  ? 123 TRP A CZ2 1 
ATOM   972  C  CZ3 . TRP A 1 123 ? 9.029  17.876  16.315  1.00 15.22  ? 123 TRP A CZ3 1 
ATOM   973  C  CH2 . TRP A 1 123 ? 8.490  17.955  15.046  1.00 15.45  ? 123 TRP A CH2 1 
ATOM   974  N  N   . ASN A 1 124 ? 9.132  14.354  20.261  1.00 9.87   ? 124 ASN A N   1 
ATOM   975  C  CA  . ASN A 1 124 ? 8.424  15.279  21.147  1.00 12.15  ? 124 ASN A CA  1 
ATOM   976  C  C   . ASN A 1 124 ? 8.321  16.662  20.505  1.00 12.15  ? 124 ASN A C   1 
ATOM   977  O  O   . ASN A 1 124 ? 9.331  17.310  20.255  1.00 11.27  ? 124 ASN A O   1 
ATOM   978  C  CB  . ASN A 1 124 ? 9.262  15.294  22.450  1.00 13.28  ? 124 ASN A CB  1 
ATOM   979  C  CG  . ASN A 1 124 ? 8.540  15.986  23.557  1.00 16.16  ? 124 ASN A CG  1 
ATOM   980  O  OD1 . ASN A 1 124 ? 7.678  16.851  23.291  1.00 16.54  ? 124 ASN A OD1 1 
ATOM   981  N  ND2 . ASN A 1 124 ? 8.821  15.480  24.766  1.00 16.90  ? 124 ASN A ND2 1 
ATOM   982  N  N   . THR A 1 125 ? 7.085  17.099  20.234  1.00 12.66  ? 125 THR A N   1 
ATOM   983  C  CA  . THR A 1 125 ? 6.912  18.318  19.443  1.00 14.74  ? 125 THR A CA  1 
ATOM   984  C  C   . THR A 1 125 ? 7.403  19.525  20.209  1.00 14.79  ? 125 THR A C   1 
ATOM   985  O  O   . THR A 1 125 ? 7.623  20.545  19.606  1.00 16.65  ? 125 THR A O   1 
ATOM   986  C  CB  . THR A 1 125 ? 5.446  18.452  19.059  1.00 17.95  ? 125 THR A CB  1 
ATOM   987  O  OG1 . THR A 1 125 ? 4.657  18.601  20.248  1.00 22.73  ? 125 THR A OG1 1 
ATOM   988  C  CG2 . THR A 1 125 ? 4.998  17.339  18.139  1.00 22.07  ? 125 THR A CG2 1 
ATOM   989  N  N   . LYS A 1 126 ? 7.612  19.456  21.536  1.00 15.03  ? 126 LYS A N   1 
ATOM   990  C  CA  . LYS A 1 126 ? 8.165  20.604  22.233  1.00 16.55  ? 126 LYS A CA  1 
ATOM   991  C  C   . LYS A 1 126 ? 9.567  20.996  21.740  1.00 15.99  ? 126 LYS A C   1 
ATOM   992  O  O   . LYS A 1 126 ? 10.005 22.056  21.935  1.00 22.37  ? 126 LYS A O   1 
ATOM   993  C  CB  . LYS A 1 126 ? 8.103  20.422  23.728  1.00 19.12  ? 126 LYS A CB  1 
ATOM   994  C  CG  . LYS A 1 126 ? 9.165  19.595  24.378  1.00 23.28  ? 126 LYS A CG  1 
ATOM   995  C  CD  . LYS A 1 126 ? 8.758  19.476  25.851  1.00 25.86  ? 126 LYS A CD  1 
ATOM   996  C  CE  . LYS A 1 126 ? 9.915  18.797  26.522  1.00 33.45  ? 126 LYS A CE  1 
ATOM   997  N  NZ  . LYS A 1 126 ? 9.869  18.896  27.995  1.00 49.01  ? 126 LYS A NZ  1 
ATOM   998  N  N   . TYR A 1 127 ? 10.286 20.064  21.104  1.00 13.23  ? 127 TYR A N   1 
ATOM   999  C  CA  . TYR A 1 127 ? 11.638 20.279  20.606  1.00 12.18  ? 127 TYR A CA  1 
ATOM   1000 C  C   . TYR A 1 127 ? 11.680 20.740  19.145  1.00 13.05  ? 127 TYR A C   1 
ATOM   1001 O  O   . TYR A 1 127 ? 12.768 21.014  18.606  1.00 13.81  ? 127 TYR A O   1 
ATOM   1002 C  CB  . TYR A 1 127 ? 12.573 19.091  20.869  1.00 13.20  ? 127 TYR A CB  1 
ATOM   1003 C  CG  . TYR A 1 127 ? 12.636 18.756  22.328  1.00 14.53  ? 127 TYR A CG  1 
ATOM   1004 C  CD1 . TYR A 1 127 ? 13.073 19.738  23.218  1.00 16.11  ? 127 TYR A CD1 1 
ATOM   1005 C  CD2 . TYR A 1 127 ? 12.349 17.471  22.788  1.00 14.56  ? 127 TYR A CD2 1 
ATOM   1006 C  CE1 . TYR A 1 127 ? 13.136 19.457  24.577  1.00 18.18  ? 127 TYR A CE1 1 
ATOM   1007 C  CE2 . TYR A 1 127 ? 12.435 17.171  24.141  1.00 14.70  ? 127 TYR A CE2 1 
ATOM   1008 C  CZ  . TYR A 1 127 ? 12.845 18.186  25.030  1.00 17.07  ? 127 TYR A CZ  1 
ATOM   1009 O  OH  . TYR A 1 127 ? 12.957 17.930  26.342  1.00 20.58  ? 127 TYR A OH  1 
ATOM   1010 N  N   . GLY A 1 128 ? 10.520 20.842  18.474  1.00 12.46  ? 128 GLY A N   1 
ATOM   1011 C  CA  . GLY A 1 128 ? 10.425 21.555  17.197  1.00 12.84  ? 128 GLY A CA  1 
ATOM   1012 C  C   . GLY A 1 128 ? 10.853 20.716  15.989  1.00 13.62  ? 128 GLY A C   1 
ATOM   1013 O  O   . GLY A 1 128 ? 10.227 20.828  14.943  1.00 15.41  ? 128 GLY A O   1 
ATOM   1014 N  N   . ASP A 1 129 ? 11.971 19.971  16.109  1.00 13.26  ? 129 ASP A N   1 
ATOM   1015 C  CA  . ASP A 1 129 ? 12.404 19.112  15.011  1.00 12.96  ? 129 ASP A CA  1 
ATOM   1016 C  C   . ASP A 1 129 ? 13.031 17.870  15.604  1.00 12.33  ? 129 ASP A C   1 
ATOM   1017 O  O   . ASP A 1 129 ? 13.520 17.881  16.756  1.00 13.74  ? 129 ASP A O   1 
ATOM   1018 C  CB  . ASP A 1 129 ? 13.326 19.844  13.982  1.00 13.83  ? 129 ASP A CB  1 
ATOM   1019 C  CG  . ASP A 1 129 ? 14.681 20.283  14.505  1.00 14.96  ? 129 ASP A CG  1 
ATOM   1020 O  OD1 . ASP A 1 129 ? 15.633 19.423  14.697  1.00 16.20  ? 129 ASP A OD1 1 
ATOM   1021 O  OD2 . ASP A 1 129 ? 14.882 21.496  14.788  1.00 17.17  ? 129 ASP A OD2 1 
ATOM   1022 N  N   . TYR A 1 130 ? 13.079 16.777  14.801  1.00 12.24  ? 130 TYR A N   1 
ATOM   1023 C  CA  . TYR A 1 130 ? 13.531 15.537  15.391  1.00 12.30  ? 130 TYR A CA  1 
ATOM   1024 C  C   . TYR A 1 130 ? 15.009 15.615  15.735  1.00 12.65  ? 130 TYR A C   1 
ATOM   1025 O  O   . TYR A 1 130 ? 15.441 14.940  16.666  1.00 12.89  ? 130 TYR A O   1 
ATOM   1026 C  CB  . TYR A 1 130 ? 13.265 14.324  14.506  1.00 12.77  ? 130 TYR A CB  1 
ATOM   1027 C  CG  . TYR A 1 130 ? 14.223 14.227  13.367  1.00 12.95  ? 130 TYR A CG  1 
ATOM   1028 C  CD1 . TYR A 1 130 ? 13.906 14.874  12.165  1.00 15.85  ? 130 TYR A CD1 1 
ATOM   1029 C  CD2 . TYR A 1 130 ? 15.382 13.474  13.447  1.00 17.08  ? 130 TYR A CD2 1 
ATOM   1030 C  CE1 . TYR A 1 130 ? 14.734 14.795  11.063  1.00 18.35  ? 130 TYR A CE1 1 
ATOM   1031 C  CE2 . TYR A 1 130 ? 16.228 13.375  12.332  1.00 20.22  ? 130 TYR A CE2 1 
ATOM   1032 C  CZ  . TYR A 1 130 ? 15.889 14.050  11.164  1.00 19.27  ? 130 TYR A CZ  1 
ATOM   1033 O  OH  . TYR A 1 130 ? 16.683 13.986  10.032  1.00 25.53  ? 130 TYR A OH  1 
ATOM   1034 N  N   . GLY A 1 131 ? 15.809 16.396  14.962  1.00 13.69  ? 131 GLY A N   1 
ATOM   1035 C  CA  . GLY A 1 131 ? 17.234 16.448  15.258  1.00 15.56  ? 131 GLY A CA  1 
ATOM   1036 C  C   . GLY A 1 131 ? 17.524 17.101  16.619  1.00 16.16  ? 131 GLY A C   1 
ATOM   1037 O  O   . GLY A 1 131 ? 18.450 16.669  17.330  1.00 20.66  ? 131 GLY A O   1 
ATOM   1038 N  N   A LYS A 1 132 ? 16.732 18.120  17.022  0.50 14.96  ? 132 LYS A N   1 
ATOM   1039 N  N   B LYS A 1 132 ? 16.702 18.089  17.009  0.50 14.78  ? 132 LYS A N   1 
ATOM   1040 C  CA  A LYS A 1 132 ? 16.800 18.688  18.367  0.50 16.40  ? 132 LYS A CA  1 
ATOM   1041 C  CA  B LYS A 1 132 ? 16.816 18.666  18.337  0.50 15.84  ? 132 LYS A CA  1 
ATOM   1042 C  C   A LYS A 1 132 ? 16.350 17.659  19.410  0.50 17.93  ? 132 LYS A C   1 
ATOM   1043 C  C   B LYS A 1 132 ? 16.350 17.672  19.400  0.50 18.39  ? 132 LYS A C   1 
ATOM   1044 O  O   A LYS A 1 132 ? 17.004 17.563  20.478  0.50 22.02  ? 132 LYS A O   1 
ATOM   1045 O  O   B LYS A 1 132 ? 17.014 17.589  20.457  0.50 24.32  ? 132 LYS A O   1 
ATOM   1046 C  CB  A LYS A 1 132 ? 15.936 19.954  18.472  0.50 20.97  ? 132 LYS A CB  1 
ATOM   1047 C  CB  B LYS A 1 132 ? 15.956 19.920  18.451  0.50 18.72  ? 132 LYS A CB  1 
ATOM   1048 C  CG  A LYS A 1 132 ? 16.515 21.213  17.826  0.50 26.34  ? 132 LYS A CG  1 
ATOM   1049 C  CG  B LYS A 1 132 ? 16.172 20.603  19.787  0.50 16.68  ? 132 LYS A CG  1 
ATOM   1050 C  CD  A LYS A 1 132 ? 17.886 21.592  18.388  0.50 27.21  ? 132 LYS A CD  1 
ATOM   1051 C  CD  B LYS A 1 132 ? 17.573 21.242  19.911  0.50 24.74  ? 132 LYS A CD  1 
ATOM   1052 C  CE  A LYS A 1 132 ? 17.842 22.884  19.182  0.50 32.47  ? 132 LYS A CE  1 
ATOM   1053 C  CE  B LYS A 1 132 ? 17.621 22.758  19.619  0.50 32.95  ? 132 LYS A CE  1 
ATOM   1054 N  NZ  A LYS A 1 132 ? 17.128 23.897  18.364  0.50 25.09  ? 132 LYS A NZ  1 
ATOM   1055 N  NZ  B LYS A 1 132 ? 17.920 23.189  18.208  0.50 34.24  ? 132 LYS A NZ  1 
ATOM   1056 N  N   . ALA A 1 133 ? 15.240 16.917  19.093  1.00 15.10  ? 133 ALA A N   1 
ATOM   1057 C  CA  . ALA A 1 133 ? 14.646 15.901  19.996  1.00 12.44  ? 133 ALA A CA  1 
ATOM   1058 C  C   . ALA A 1 133 ? 15.640 14.779  20.343  1.00 12.83  ? 133 ALA A C   1 
ATOM   1059 O  O   . ALA A 1 133 ? 15.701 14.356  21.500  1.00 16.15  ? 133 ALA A O   1 
ATOM   1060 C  CB  . ALA A 1 133 ? 13.356 15.309  19.407  1.00 12.80  ? 133 ALA A CB  1 
ATOM   1061 N  N   A VAL A 1 134 ? 16.488 14.368  19.395  0.50 12.77  ? 134 VAL A N   1 
ATOM   1062 N  N   B VAL A 1 134 ? 16.478 14.391  19.384  0.50 13.05  ? 134 VAL A N   1 
ATOM   1063 C  CA  A VAL A 1 134 ? 17.397 13.237  19.615  0.50 14.03  ? 134 VAL A CA  1 
ATOM   1064 C  CA  B VAL A 1 134 ? 17.531 13.417  19.659  0.50 14.03  ? 134 VAL A CA  1 
ATOM   1065 C  C   A VAL A 1 134 ? 18.522 13.531  20.596  0.50 15.57  ? 134 VAL A C   1 
ATOM   1066 C  C   B VAL A 1 134 ? 18.517 13.968  20.697  0.50 16.75  ? 134 VAL A C   1 
ATOM   1067 O  O   A VAL A 1 134 ? 19.161 12.580  21.061  0.50 16.85  ? 134 VAL A O   1 
ATOM   1068 O  O   B VAL A 1 134 ? 19.227 13.201  21.326  0.50 19.57  ? 134 VAL A O   1 
ATOM   1069 C  CB  A VAL A 1 134 ? 18.029 12.668  18.345  0.50 13.28  ? 134 VAL A CB  1 
ATOM   1070 C  CB  B VAL A 1 134 ? 18.212 12.900  18.374  0.50 17.18  ? 134 VAL A CB  1 
ATOM   1071 C  CG1 A VAL A 1 134 ? 16.947 12.138  17.471  0.50 11.55  ? 134 VAL A CG1 1 
ATOM   1072 C  CG1 B VAL A 1 134 ? 18.588 13.994  17.408  0.50 27.89  ? 134 VAL A CG1 1 
ATOM   1073 C  CG2 A VAL A 1 134 ? 18.903 13.656  17.612  0.50 20.06  ? 134 VAL A CG2 1 
ATOM   1074 C  CG2 B VAL A 1 134 ? 19.332 11.886  18.522  0.50 17.87  ? 134 VAL A CG2 1 
ATOM   1075 N  N   A GLN A 1 135 ? 18.756 14.811  20.853  0.50 15.42  ? 135 GLN A N   1 
ATOM   1076 N  N   B GLN A 1 135 ? 18.517 15.281  20.921  0.50 16.09  ? 135 GLN A N   1 
ATOM   1077 C  CA  A GLN A 1 135 ? 19.739 15.218  21.833  0.50 18.05  ? 135 GLN A CA  1 
ATOM   1078 C  CA  B GLN A 1 135 ? 19.476 15.841  21.854  0.50 17.81  ? 135 GLN A CA  1 
ATOM   1079 C  C   A GLN A 1 135 ? 19.095 15.500  23.196  0.50 17.70  ? 135 GLN A C   1 
ATOM   1080 C  C   B GLN A 1 135 ? 18.959 15.764  23.283  0.50 16.72  ? 135 GLN A C   1 
ATOM   1081 O  O   A GLN A 1 135 ? 19.780 16.053  24.045  0.50 21.86  ? 135 GLN A O   1 
ATOM   1082 O  O   B GLN A 1 135 ? 19.545 16.262  24.244  0.50 24.29  ? 135 GLN A O   1 
ATOM   1083 C  CB  A GLN A 1 135 ? 20.569 16.406  21.308  0.50 18.99  ? 135 GLN A CB  1 
ATOM   1084 C  CB  B GLN A 1 135 ? 19.887 17.235  21.392  0.50 18.25  ? 135 GLN A CB  1 
ATOM   1085 C  CG  A GLN A 1 135 ? 21.303 16.153  19.991  0.50 27.20  ? 135 GLN A CG  1 
ATOM   1086 C  CG  B GLN A 1 135 ? 20.544 17.136  20.025  0.50 22.31  ? 135 GLN A CG  1 
ATOM   1087 C  CD  A GLN A 1 135 ? 22.246 14.963  20.005  0.50 24.23  ? 135 GLN A CD  1 
ATOM   1088 C  CD  B GLN A 1 135 ? 21.020 18.457  19.484  0.50 28.35  ? 135 GLN A CD  1 
ATOM   1089 O  OE1 A GLN A 1 135 ? 22.649 14.452  21.060  0.50 37.26  ? 135 GLN A OE1 1 
ATOM   1090 O  OE1 B GLN A 1 135 ? 20.527 18.917  18.453  0.50 23.29  ? 135 GLN A OE1 1 
ATOM   1091 N  NE2 A GLN A 1 135 ? 22.513 14.429  18.816  0.50 30.19  ? 135 GLN A NE2 1 
ATOM   1092 N  NE2 B GLN A 1 135 ? 21.965 19.052  20.187  0.50 25.77  ? 135 GLN A NE2 1 
ATOM   1093 N  N   . GLN A 1 136 ? 17.809 15.123  23.420  1.00 14.84  ? 136 GLN A N   1 
ATOM   1094 C  CA  . GLN A 1 136 ? 17.143 15.312  24.686  1.00 13.71  ? 136 GLN A CA  1 
ATOM   1095 C  C   . GLN A 1 136 ? 16.831 13.969  25.303  1.00 13.73  ? 136 GLN A C   1 
ATOM   1096 O  O   . GLN A 1 136 ? 16.478 13.020  24.598  1.00 13.44  ? 136 GLN A O   1 
ATOM   1097 C  CB  . GLN A 1 136 ? 15.851 16.097  24.499  1.00 15.57  ? 136 GLN A CB  1 
ATOM   1098 C  CG  . GLN A 1 136 ? 15.976 17.320  23.564  1.00 16.52  ? 136 GLN A CG  1 
ATOM   1099 C  CD  . GLN A 1 136 ? 17.002 18.321  23.987  1.00 18.59  ? 136 GLN A CD  1 
ATOM   1100 O  OE1 . GLN A 1 136 ? 17.193 18.520  25.184  1.00 19.54  ? 136 GLN A OE1 1 
ATOM   1101 N  NE2 . GLN A 1 136 ? 17.594 19.011  23.009  1.00 26.50  ? 136 GLN A NE2 1 
ATOM   1102 N  N   . PRO A 1 137 ? 16.832 13.900  26.644  1.00 14.59  ? 137 PRO A N   1 
ATOM   1103 C  CA  . PRO A 1 137 ? 16.593 12.630  27.286  1.00 15.85  ? 137 PRO A CA  1 
ATOM   1104 C  C   . PRO A 1 137 ? 15.195 12.112  27.027  1.00 15.35  ? 137 PRO A C   1 
ATOM   1105 O  O   . PRO A 1 137 ? 14.968 10.905  27.151  1.00 18.63  ? 137 PRO A O   1 
ATOM   1106 C  CB  . PRO A 1 137 ? 16.767 12.883  28.784  1.00 20.76  ? 137 PRO A CB  1 
ATOM   1107 C  CG  . PRO A 1 137 ? 16.825 14.377  28.910  1.00 28.59  ? 137 PRO A CG  1 
ATOM   1108 C  CD  . PRO A 1 137 ? 17.229 14.974  27.589  1.00 21.26  ? 137 PRO A CD  1 
ATOM   1109 N  N   . ASP A 1 138 ? 14.236 13.007  26.731  1.00 14.40  ? 138 ASP A N   1 
ATOM   1110 C  CA  . ASP A 1 138 ? 12.843 12.607  26.469  1.00 14.25  ? 138 ASP A CA  1 
ATOM   1111 C  C   . ASP A 1 138 ? 12.457 13.083  25.071  1.00 11.86  ? 138 ASP A C   1 
ATOM   1112 O  O   . ASP A 1 138 ? 11.343 13.503  24.808  1.00 14.42  ? 138 ASP A O   1 
ATOM   1113 C  CB  . ASP A 1 138 ? 11.940 13.288  27.523  1.00 16.24  ? 138 ASP A CB  1 
ATOM   1114 C  CG  . ASP A 1 138 ? 11.973 14.778  27.512  1.00 17.05  ? 138 ASP A CG  1 
ATOM   1115 O  OD1 . ASP A 1 138 ? 12.926 15.383  26.909  1.00 17.31  ? 138 ASP A OD1 1 
ATOM   1116 O  OD2 . ASP A 1 138 ? 11.125 15.392  28.203  1.00 20.31  ? 138 ASP A OD2 1 
ATOM   1117 N  N   . GLY A 1 139 ? 13.361 12.926  24.122  1.00 11.04  ? 139 GLY A N   1 
ATOM   1118 C  CA  . GLY A 1 139 ? 13.121 13.471  22.796  1.00 11.26  ? 139 GLY A CA  1 
ATOM   1119 C  C   . GLY A 1 139 ? 12.241 12.551  21.953  1.00 9.64   ? 139 GLY A C   1 
ATOM   1120 O  O   . GLY A 1 139 ? 11.484 13.049  21.112  1.00 10.44  ? 139 GLY A O   1 
ATOM   1121 N  N   . LEU A 1 140 ? 12.383 11.217  22.086  1.00 8.97   ? 140 LEU A N   1 
ATOM   1122 C  CA  . LEU A 1 140 ? 11.671 10.299  21.212  1.00 8.23   ? 140 LEU A CA  1 
ATOM   1123 C  C   . LEU A 1 140 ? 10.832 9.374   22.052  1.00 8.76   ? 140 LEU A C   1 
ATOM   1124 O  O   . LEU A 1 140 ? 11.147 9.073   23.193  1.00 9.24   ? 140 LEU A O   1 
ATOM   1125 C  CB  . LEU A 1 140 ? 12.666 9.459   20.413  1.00 9.19   ? 140 LEU A CB  1 
ATOM   1126 C  CG  . LEU A 1 140 ? 13.579 10.172  19.420  1.00 11.36  ? 140 LEU A CG  1 
ATOM   1127 C  CD1 . LEU A 1 140 ? 14.304 9.157   18.583  1.00 12.36  ? 140 LEU A CD1 1 
ATOM   1128 C  CD2 . LEU A 1 140 ? 12.909 11.167  18.539  1.00 12.99  ? 140 LEU A CD2 1 
ATOM   1129 N  N   . ALA A 1 141 ? 9.754  8.859   21.409  1.00 9.01   ? 141 ALA A N   1 
ATOM   1130 C  CA  . ALA A 1 141 ? 8.969  7.749   21.972  1.00 8.95   ? 141 ALA A CA  1 
ATOM   1131 C  C   . ALA A 1 141 ? 8.870  6.756   20.838  1.00 8.28   ? 141 ALA A C   1 
ATOM   1132 O  O   . ALA A 1 141 ? 8.452  7.084   19.748  1.00 9.11   ? 141 ALA A O   1 
ATOM   1133 C  CB  . ALA A 1 141 ? 7.588  8.241   22.400  1.00 11.06  ? 141 ALA A CB  1 
ATOM   1134 N  N   . VAL A 1 142 ? 9.350  5.525   21.129  1.00 9.15   ? 142 VAL A N   1 
ATOM   1135 C  CA  . VAL A 1 142 ? 9.290  4.499   20.098  1.00 9.16   ? 142 VAL A CA  1 
ATOM   1136 C  C   . VAL A 1 142 ? 8.321  3.430   20.593  1.00 7.97   ? 142 VAL A C   1 
ATOM   1137 O  O   . VAL A 1 142 ? 8.496  2.906   21.698  1.00 9.00   ? 142 VAL A O   1 
ATOM   1138 C  CB  . VAL A 1 142 ? 10.679 3.916   19.768  1.00 8.94   ? 142 VAL A CB  1 
ATOM   1139 C  CG1 . VAL A 1 142 ? 10.504 2.863   18.664  1.00 10.40  ? 142 VAL A CG1 1 
ATOM   1140 C  CG2 . VAL A 1 142 ? 11.607 5.018   19.290  1.00 10.23  ? 142 VAL A CG2 1 
ATOM   1141 N  N   . LEU A 1 143 ? 7.316  3.166   19.753  1.00 8.26   ? 143 LEU A N   1 
ATOM   1142 C  CA  . LEU A 1 143 ? 6.344  2.104   20.012  1.00 8.73   ? 143 LEU A CA  1 
ATOM   1143 C  C   . LEU A 1 143 ? 6.908  0.868   19.307  1.00 8.74   ? 143 LEU A C   1 
ATOM   1144 O  O   . LEU A 1 143 ? 7.070  0.853   18.104  1.00 9.93   ? 143 LEU A O   1 
ATOM   1145 C  CB  . LEU A 1 143 ? 4.975  2.558   19.464  1.00 10.68  ? 143 LEU A CB  1 
ATOM   1146 C  CG  . LEU A 1 143 ? 3.826  1.627   19.630  1.00 11.88  ? 143 LEU A CG  1 
ATOM   1147 C  CD1 . LEU A 1 143 ? 3.593  1.357   21.110  1.00 14.24  ? 143 LEU A CD1 1 
ATOM   1148 C  CD2 . LEU A 1 143 ? 2.585  2.266   18.993  1.00 14.71  ? 143 LEU A CD2 1 
ATOM   1149 N  N   . GLY A 1 144 ? 7.176  -0.168  20.107  1.00 8.49   ? 144 GLY A N   1 
ATOM   1150 C  CA  . GLY A 1 144 ? 7.725  -1.425  19.578  1.00 8.31   ? 144 GLY A CA  1 
ATOM   1151 C  C   . GLY A 1 144 ? 6.689  -2.527  19.602  1.00 7.49   ? 144 GLY A C   1 
ATOM   1152 O  O   . GLY A 1 144 ? 5.962  -2.663  20.582  1.00 9.46   ? 144 GLY A O   1 
ATOM   1153 N  N   . ILE A 1 145 ? 6.616  -3.263  18.492  1.00 8.12   ? 145 ILE A N   1 
ATOM   1154 C  CA  . ILE A 1 145 ? 5.588  -4.321  18.318  1.00 7.97   ? 145 ILE A CA  1 
ATOM   1155 C  C   . ILE A 1 145 ? 6.359  -5.540  17.808  1.00 7.85   ? 145 ILE A C   1 
ATOM   1156 O  O   . ILE A 1 145 ? 7.069  -5.460  16.802  1.00 9.16   ? 145 ILE A O   1 
ATOM   1157 C  CB  . ILE A 1 145 ? 4.530  -3.856  17.327  1.00 9.32   ? 145 ILE A CB  1 
ATOM   1158 C  CG1 . ILE A 1 145 ? 3.856  -2.579  17.884  1.00 12.33  ? 145 ILE A CG1 1 
ATOM   1159 C  CG2 . ILE A 1 145 ? 3.524  -4.977  17.101  1.00 11.66  ? 145 ILE A CG2 1 
ATOM   1160 C  CD1 . ILE A 1 145 ? 2.783  -1.957  16.985  1.00 11.19  ? 145 ILE A CD1 1 
ATOM   1161 N  N   . PHE A 1 146 ? 6.169  -6.666  18.473  1.00 7.99   ? 146 PHE A N   1 
ATOM   1162 C  CA  . PHE A 1 146 ? 6.813  -7.889  18.054  1.00 8.01   ? 146 PHE A CA  1 
ATOM   1163 C  C   . PHE A 1 146 ? 6.041  -8.518  16.878  1.00 8.45   ? 146 PHE A C   1 
ATOM   1164 O  O   . PHE A 1 146 ? 4.808  -8.443  16.865  1.00 10.17  ? 146 PHE A O   1 
ATOM   1165 C  CB  . PHE A 1 146 ? 6.828  -8.866  19.237  1.00 9.65   ? 146 PHE A CB  1 
ATOM   1166 C  CG  . PHE A 1 146 ? 7.683  -8.392  20.386  1.00 8.07   ? 146 PHE A CG  1 
ATOM   1167 C  CD1 . PHE A 1 146 ? 9.056  -8.199  20.210  1.00 9.67   ? 146 PHE A CD1 1 
ATOM   1168 C  CD2 . PHE A 1 146 ? 7.123  -8.129  21.635  1.00 9.64   ? 146 PHE A CD2 1 
ATOM   1169 C  CE1 . PHE A 1 146 ? 9.867  -7.808  21.256  1.00 10.23  ? 146 PHE A CE1 1 
ATOM   1170 C  CE2 . PHE A 1 146 ? 7.914  -7.702  22.690  1.00 9.60   ? 146 PHE A CE2 1 
ATOM   1171 C  CZ  . PHE A 1 146 ? 9.293  -7.567  22.492  1.00 9.03   ? 146 PHE A CZ  1 
ATOM   1172 N  N   . LEU A 1 147 ? 6.784  -9.188  16.010  1.00 9.12   ? 147 LEU A N   1 
ATOM   1173 C  CA  . LEU A 1 147 ? 6.169  -9.984  14.940  1.00 9.31   ? 147 LEU A CA  1 
ATOM   1174 C  C   . LEU A 1 147 ? 6.532  -11.449 15.176  1.00 9.71   ? 147 LEU A C   1 
ATOM   1175 O  O   . LEU A 1 147 ? 7.698  -11.819 15.298  1.00 10.29  ? 147 LEU A O   1 
ATOM   1176 C  CB  . LEU A 1 147 ? 6.756  -9.570  13.585  1.00 10.08  ? 147 LEU A CB  1 
ATOM   1177 C  CG  . LEU A 1 147 ? 6.175  -8.333  12.924  1.00 9.55   ? 147 LEU A CG  1 
ATOM   1178 C  CD1 . LEU A 1 147 ? 6.346  -7.052  13.799  1.00 12.17  ? 147 LEU A CD1 1 
ATOM   1179 C  CD2 . LEU A 1 147 ? 6.769  -8.131  11.528  1.00 11.36  ? 147 LEU A CD2 1 
ATOM   1180 N  N   . LYS A 1 148 ? 5.503  -12.309 15.195  1.00 10.59  ? 148 LYS A N   1 
ATOM   1181 C  CA  . LYS A 1 148 ? 5.709  -13.746 15.192  1.00 11.05  ? 148 LYS A CA  1 
ATOM   1182 C  C   . LYS A 1 148 ? 5.200  -14.247 13.870  1.00 12.21  ? 148 LYS A C   1 
ATOM   1183 O  O   . LYS A 1 148 ? 4.376  -13.649 13.191  1.00 14.40  ? 148 LYS A O   1 
ATOM   1184 C  CB  . LYS A 1 148 ? 4.957  -14.412 16.342  1.00 13.76  ? 148 LYS A CB  1 
ATOM   1185 C  CG  . LYS A 1 148 ? 3.472  -14.301 16.279  1.00 14.76  ? 148 LYS A CG  1 
ATOM   1186 C  CD  . LYS A 1 148 ? 2.878  -15.045 17.486  1.00 21.27  ? 148 LYS A CD  1 
ATOM   1187 C  CE  . LYS A 1 148 ? 1.383  -15.173 17.422  1.00 31.32  ? 148 LYS A CE  1 
ATOM   1188 N  NZ  . LYS A 1 148 ? 0.891  -15.772 18.687  1.00 37.48  ? 148 LYS A NZ  1 
ATOM   1189 N  N   . VAL A 1 149 ? 5.687  -15.418 13.473  1.00 13.41  ? 149 VAL A N   1 
ATOM   1190 C  CA  . VAL A 1 149 ? 5.331  -16.045 12.208  1.00 12.86  ? 149 VAL A CA  1 
ATOM   1191 C  C   . VAL A 1 149 ? 4.125  -16.943 12.421  1.00 12.23  ? 149 VAL A C   1 
ATOM   1192 O  O   . VAL A 1 149 ? 4.135  -17.869 13.244  1.00 15.74  ? 149 VAL A O   1 
ATOM   1193 C  CB  . VAL A 1 149 ? 6.531  -16.791 11.609  1.00 13.11  ? 149 VAL A CB  1 
ATOM   1194 C  CG1 . VAL A 1 149 ? 6.050  -17.568 10.390  1.00 15.94  ? 149 VAL A CG1 1 
ATOM   1195 C  CG2 . VAL A 1 149 ? 7.614  -15.809 11.250  1.00 14.06  ? 149 VAL A CG2 1 
ATOM   1196 N  N   . GLY A 1 150 ? 3.051  -16.704 11.676  1.00 13.37  ? 150 GLY A N   1 
ATOM   1197 C  CA  . GLY A 1 150 ? 1.855  -17.520 11.737  1.00 13.71  ? 150 GLY A CA  1 
ATOM   1198 C  C   . GLY A 1 150 ? 0.959  -17.113 10.590  1.00 12.67  ? 150 GLY A C   1 
ATOM   1199 O  O   . GLY A 1 150 ? 1.364  -17.228 9.437   1.00 13.29  ? 150 GLY A O   1 
ATOM   1200 N  N   . SER A 1 151 ? -0.264 -16.621 10.878  1.00 14.25  ? 151 SER A N   1 
ATOM   1201 C  CA  . SER A 1 151 ? -1.131 -16.148 9.802   1.00 14.20  ? 151 SER A CA  1 
ATOM   1202 C  C   . SER A 1 151 ? -0.549 -14.859 9.211   1.00 13.45  ? 151 SER A C   1 
ATOM   1203 O  O   . SER A 1 151 ? 0.117  -14.096 9.910   1.00 14.04  ? 151 SER A O   1 
ATOM   1204 C  CB  . SER A 1 151 ? -2.509 -15.943 10.279  1.00 18.56  ? 151 SER A CB  1 
ATOM   1205 O  OG  . SER A 1 151 ? -2.571 -14.908 11.197  1.00 23.27  ? 151 SER A OG  1 
ATOM   1206 N  N   . ALA A 1 152 ? -0.855 -14.523 7.953   1.00 14.18  ? 152 ALA A N   1 
ATOM   1207 C  CA  . ALA A 1 152 ? -0.494 -13.243 7.343   1.00 13.55  ? 152 ALA A CA  1 
ATOM   1208 C  C   . ALA A 1 152 ? -1.127 -12.077 8.082   1.00 13.67  ? 152 ALA A C   1 
ATOM   1209 O  O   . ALA A 1 152 ? -2.209 -12.144 8.664   1.00 16.61  ? 152 ALA A O   1 
ATOM   1210 C  CB  . ALA A 1 152 ? -0.910 -13.215 5.862   1.00 16.57  ? 152 ALA A CB  1 
ATOM   1211 N  N   . LYS A 1 153 ? -0.419 -10.961 7.997   1.00 13.15  ? 153 LYS A N   1 
ATOM   1212 C  CA  . LYS A 1 153 ? -0.947 -9.664  8.473   1.00 12.99  ? 153 LYS A CA  1 
ATOM   1213 C  C   . LYS A 1 153 ? -1.424 -8.884  7.253   1.00 14.94  ? 153 LYS A C   1 
ATOM   1214 O  O   . LYS A 1 153 ? -0.589 -8.388  6.480   1.00 13.68  ? 153 LYS A O   1 
ATOM   1215 C  CB  . LYS A 1 153 ? 0.175  -8.905  9.193   1.00 13.03  ? 153 LYS A CB  1 
ATOM   1216 C  CG  . LYS A 1 153 ? -0.343 -7.666  9.948   1.00 14.96  ? 153 LYS A CG  1 
ATOM   1217 C  CD  . LYS A 1 153 ? -1.244 -8.044  11.191  1.00 17.15  ? 153 LYS A CD  1 
ATOM   1218 C  CE  . LYS A 1 153 ? -1.469 -6.842  12.090  1.00 19.39  ? 153 LYS A CE  1 
ATOM   1219 N  NZ  . LYS A 1 153 ? -2.447 -7.230  13.130  1.00 24.97  ? 153 LYS A NZ  1 
ATOM   1220 N  N   . PRO A 1 154 ? -2.736 -8.782  7.017   1.00 14.54  ? 154 PRO A N   1 
ATOM   1221 C  CA  . PRO A 1 154 ? -3.217 -8.091  5.813   1.00 17.87  ? 154 PRO A CA  1 
ATOM   1222 C  C   . PRO A 1 154 ? -2.659 -6.676  5.702   1.00 16.78  ? 154 PRO A C   1 
ATOM   1223 O  O   . PRO A 1 154 ? -2.294 -6.272  4.606   1.00 18.91  ? 154 PRO A O   1 
ATOM   1224 C  CB  . PRO A 1 154 ? -4.755 -8.147  5.986   1.00 19.67  ? 154 PRO A CB  1 
ATOM   1225 C  CG  . PRO A 1 154 ? -4.981 -9.342  6.864   1.00 21.04  ? 154 PRO A CG  1 
ATOM   1226 C  CD  . PRO A 1 154 ? -3.838 -9.346  7.851   1.00 17.33  ? 154 PRO A CD  1 
ATOM   1227 N  N   . GLY A 1 155 ? -2.599 -5.954  6.832   1.00 15.93  ? 155 GLY A N   1 
ATOM   1228 C  CA  . GLY A 1 155 ? -2.173 -4.572  6.859   1.00 17.50  ? 155 GLY A CA  1 
ATOM   1229 C  C   . GLY A 1 155 ? -0.707 -4.399  6.534   1.00 14.49  ? 155 GLY A C   1 
ATOM   1230 O  O   . GLY A 1 155 ? -0.276 -3.286  6.337   1.00 18.97  ? 155 GLY A O   1 
ATOM   1231 N  N   . LEU A 1 156 ? 0.073  -5.469  6.483   1.00 13.93  ? 156 LEU A N   1 
ATOM   1232 C  CA  . LEU A 1 156 ? 1.487  -5.430  6.118   1.00 12.51  ? 156 LEU A CA  1 
ATOM   1233 C  C   . LEU A 1 156 ? 1.708  -5.643  4.631   1.00 12.98  ? 156 LEU A C   1 
ATOM   1234 O  O   . LEU A 1 156 ? 2.790  -5.376  4.126   1.00 13.48  ? 156 LEU A O   1 
ATOM   1235 C  CB  . LEU A 1 156 ? 2.245  -6.454  6.947   1.00 12.82  ? 156 LEU A CB  1 
ATOM   1236 C  CG  . LEU A 1 156 ? 3.755  -6.554  6.763   1.00 11.37  ? 156 LEU A CG  1 
ATOM   1237 C  CD1 . LEU A 1 156 ? 4.507  -5.245  7.164   1.00 12.98  ? 156 LEU A CD1 1 
ATOM   1238 C  CD2 . LEU A 1 156 ? 4.357  -7.732  7.560   1.00 13.26  ? 156 LEU A CD2 1 
ATOM   1239 N  N   . GLN A 1 157 ? 0.742  -6.236  3.924   1.00 14.13  ? 157 GLN A N   1 
ATOM   1240 C  CA  . GLN A 1 157 ? 1.026  -6.737  2.571   1.00 16.36  ? 157 GLN A CA  1 
ATOM   1241 C  C   . GLN A 1 157 ? 1.402  -5.603  1.626   1.00 14.96  ? 157 GLN A C   1 
ATOM   1242 O  O   . GLN A 1 157 ? 2.254  -5.819  0.800   1.00 14.43  ? 157 GLN A O   1 
ATOM   1243 C  CB  . GLN A 1 157 ? -0.126 -7.584  2.009   1.00 18.07  ? 157 GLN A CB  1 
ATOM   1244 C  CG  . GLN A 1 157 ? 0.282  -8.313  0.726   1.00 20.15  ? 157 GLN A CG  1 
ATOM   1245 C  CD  . GLN A 1 157 ? 1.443  -9.278  0.898   1.00 16.85  ? 157 GLN A CD  1 
ATOM   1246 O  OE1 . GLN A 1 157 ? 1.671  -9.905  1.965   1.00 16.49  ? 157 GLN A OE1 1 
ATOM   1247 N  NE2 . GLN A 1 157 ? 2.236  -9.441  -0.153  1.00 19.84  ? 157 GLN A NE2 1 
ATOM   1248 N  N   . LYS A 1 158 ? 0.832  -4.387  1.777   1.00 14.65  ? 158 LYS A N   1 
ATOM   1249 C  CA  . LYS A 1 158 ? 1.219  -3.296  0.881   1.00 15.33  ? 158 LYS A CA  1 
ATOM   1250 C  C   . LYS A 1 158 ? 2.719  -2.961  0.999   1.00 14.37  ? 158 LYS A C   1 
ATOM   1251 O  O   . LYS A 1 158 ? 3.383  -2.589  0.022   1.00 15.83  ? 158 LYS A O   1 
ATOM   1252 C  CB  . LYS A 1 158 ? 0.315  -2.069  1.103   1.00 19.85  ? 158 LYS A CB  1 
ATOM   1253 C  CG  . LYS A 1 158 ? -1.026 -2.128  0.349   1.00 27.23  ? 158 LYS A CG  1 
ATOM   1254 C  CD  . LYS A 1 158 ? -1.834 -0.849  0.136   1.00 48.21  ? 158 LYS A CD  1 
ATOM   1255 C  CE  . LYS A 1 158 ? -3.304 -1.095  -0.343  1.00 75.60  ? 158 LYS A CE  1 
ATOM   1256 N  NZ  . LYS A 1 158 ? -4.223 0.093   -0.026  1.00 54.95  ? 158 LYS A NZ  1 
ATOM   1257 N  N   . VAL A 1 159 ? 3.251  -3.109  2.227   1.00 12.61  ? 159 VAL A N   1 
ATOM   1258 C  CA  . VAL A 1 159 ? 4.643  -2.862  2.448   1.00 12.73  ? 159 VAL A CA  1 
ATOM   1259 C  C   . VAL A 1 159 ? 5.465  -3.961  1.805   1.00 12.94  ? 159 VAL A C   1 
ATOM   1260 O  O   . VAL A 1 159 ? 6.395  -3.713  1.039   1.00 13.71  ? 159 VAL A O   1 
ATOM   1261 C  CB  . VAL A 1 159 ? 4.922  -2.890  3.951   1.00 12.49  ? 159 VAL A CB  1 
ATOM   1262 C  CG1 . VAL A 1 159 ? 6.470  -2.857  4.198   1.00 15.35  ? 159 VAL A CG1 1 
ATOM   1263 C  CG2 . VAL A 1 159 ? 4.200  -1.755  4.678   1.00 14.76  ? 159 VAL A CG2 1 
ATOM   1264 N  N   . VAL A 1 160 ? 5.093  -5.223  2.020   1.00 13.17  ? 160 VAL A N   1 
ATOM   1265 C  CA  . VAL A 1 160 ? 5.833  -6.345  1.442   1.00 15.63  ? 160 VAL A CA  1 
ATOM   1266 C  C   . VAL A 1 160 ? 5.858  -6.258  -0.074  1.00 15.87  ? 160 VAL A C   1 
ATOM   1267 O  O   . VAL A 1 160 ? 6.915  -6.509  -0.676  1.00 15.86  ? 160 VAL A O   1 
ATOM   1268 C  CB  . VAL A 1 160 ? 5.151  -7.689  1.886   1.00 17.23  ? 160 VAL A CB  1 
ATOM   1269 C  CG1 . VAL A 1 160 ? 5.534  -8.880  1.038   1.00 21.18  ? 160 VAL A CG1 1 
ATOM   1270 C  CG2 . VAL A 1 160 ? 5.338  -7.913  3.385   1.00 18.12  ? 160 VAL A CG2 1 
ATOM   1271 N  N   . ASP A 1 161 ? 4.702  -5.846  -0.662  1.00 15.19  ? 161 ASP A N   1 
ATOM   1272 C  CA  . ASP A 1 161 ? 4.643  -5.864  -2.127  1.00 17.69  ? 161 ASP A CA  1 
ATOM   1273 C  C   . ASP A 1 161 ? 5.520  -4.802  -2.810  1.00 17.82  ? 161 ASP A C   1 
ATOM   1274 O  O   . ASP A 1 161 ? 5.829  -4.969  -3.980  1.00 26.38  ? 161 ASP A O   1 
ATOM   1275 C  CB  . ASP A 1 161 ? 3.221  -5.778  -2.576  1.00 24.02  ? 161 ASP A CB  1 
ATOM   1276 C  CG  . ASP A 1 161 ? 2.667  -7.228  -2.482  1.00 25.05  ? 161 ASP A CG  1 
ATOM   1277 O  OD1 . ASP A 1 161 ? 3.475  -8.261  -2.669  1.00 31.19  ? 161 ASP A OD1 1 
ATOM   1278 O  OD2 . ASP A 1 161 ? 1.542  -7.325  -2.067  1.00 36.12  ? 161 ASP A OD2 1 
ATOM   1279 N  N   A VAL A 1 162 ? 5.944  -3.768  -2.061  0.50 15.06  ? 162 VAL A N   1 
ATOM   1280 N  N   B VAL A 1 162 ? 5.989  -3.767  -2.104  0.50 15.94  ? 162 VAL A N   1 
ATOM   1281 C  CA  A VAL A 1 162 ? 6.774  -2.710  -2.589  0.50 12.94  ? 162 VAL A CA  1 
ATOM   1282 C  CA  B VAL A 1 162 ? 6.846  -2.829  -2.792  0.50 16.94  ? 162 VAL A CA  1 
ATOM   1283 C  C   A VAL A 1 162 ? 8.260  -3.033  -2.430  0.50 13.88  ? 162 VAL A C   1 
ATOM   1284 C  C   B VAL A 1 162 ? 8.318  -3.072  -2.492  0.50 15.45  ? 162 VAL A C   1 
ATOM   1285 O  O   A VAL A 1 162 ? 9.061  -2.315  -3.008  0.50 13.69  ? 162 VAL A O   1 
ATOM   1286 O  O   B VAL A 1 162 ? 9.156  -2.336  -2.997  0.50 16.67  ? 162 VAL A O   1 
ATOM   1287 C  CB  A VAL A 1 162 ? 6.402  -1.324  -2.008  0.50 14.07  ? 162 VAL A CB  1 
ATOM   1288 C  CB  B VAL A 1 162 ? 6.420  -1.372  -2.537  0.50 19.64  ? 162 VAL A CB  1 
ATOM   1289 C  CG1 A VAL A 1 162 ? 7.060  -1.131  -0.647  0.50 14.30  ? 162 VAL A CG1 1 
ATOM   1290 C  CG1 B VAL A 1 162 ? 4.977  -1.150  -2.966  0.50 20.24  ? 162 VAL A CG1 1 
ATOM   1291 C  CG2 A VAL A 1 162 ? 6.721  -0.153  -2.955  0.50 13.98  ? 162 VAL A CG2 1 
ATOM   1292 C  CG2 B VAL A 1 162 ? 6.643  -0.948  -1.080  0.50 18.91  ? 162 VAL A CG2 1 
ATOM   1293 N  N   . LEU A 1 163 ? 8.658  -4.065  -1.652  1.00 15.00  ? 163 LEU A N   1 
ATOM   1294 C  CA  . LEU A 1 163 ? 10.061 -4.230  -1.304  1.00 13.10  ? 163 LEU A CA  1 
ATOM   1295 C  C   . LEU A 1 163 ? 10.927 -4.554  -2.519  1.00 14.36  ? 163 LEU A C   1 
ATOM   1296 O  O   . LEU A 1 163 ? 12.083 -4.146  -2.556  1.00 15.47  ? 163 LEU A O   1 
ATOM   1297 C  CB  . LEU A 1 163 ? 10.246 -5.287  -0.216  1.00 14.33  ? 163 LEU A CB  1 
ATOM   1298 C  CG  . LEU A 1 163 ? 9.557  -4.914  1.112   1.00 13.33  ? 163 LEU A CG  1 
ATOM   1299 C  CD1 . LEU A 1 163 ? 9.827  -6.003  2.132   1.00 16.87  ? 163 LEU A CD1 1 
ATOM   1300 C  CD2 . LEU A 1 163 ? 10.115 -3.636  1.671   1.00 14.08  ? 163 LEU A CD2 1 
ATOM   1301 N  N   . ASP A 1 164 ? 10.360 -5.236  -3.519  1.00 18.79  ? 164 ASP A N   1 
ATOM   1302 C  CA  . ASP A 1 164 ? 11.135 -5.511  -4.728  1.00 22.72  ? 164 ASP A CA  1 
ATOM   1303 C  C   . ASP A 1 164 ? 11.609 -4.221  -5.415  1.00 21.00  ? 164 ASP A C   1 
ATOM   1304 O  O   . ASP A 1 164 ? 12.597 -4.272  -6.151  1.00 26.03  ? 164 ASP A O   1 
ATOM   1305 C  CB  . ASP A 1 164 ? 10.380 -6.442  -5.701  1.00 35.69  ? 164 ASP A CB  1 
ATOM   1306 C  CG  . ASP A 1 164 ? 9.472  -5.698  -6.675  1.00 74.88  ? 164 ASP A CG  1 
ATOM   1307 O  OD1 . ASP A 1 164 ? 8.421  -5.189  -6.230  1.00 65.76  ? 164 ASP A OD1 1 
ATOM   1308 O  OD2 . ASP A 1 164 ? 9.828  -5.635  -7.895  1.00 87.84  ? 164 ASP A OD2 1 
ATOM   1309 N  N   . SER A 1 165 ? 10.939 -3.079  -5.205  1.00 17.08  ? 165 SER A N   1 
ATOM   1310 C  CA  . SER A 1 165 ? 11.323 -1.821  -5.839  1.00 17.73  ? 165 SER A CA  1 
ATOM   1311 C  C   . SER A 1 165 ? 12.378 -1.052  -5.036  1.00 14.75  ? 165 SER A C   1 
ATOM   1312 O  O   . SER A 1 165 ? 12.902 -0.045  -5.542  1.00 17.61  ? 165 SER A O   1 
ATOM   1313 C  CB  . SER A 1 165 ? 10.119 -0.996  -6.137  1.00 23.52  ? 165 SER A CB  1 
ATOM   1314 O  OG  . SER A 1 165 ? 9.663  -0.424  -4.934  1.00 20.57  ? 165 SER A OG  1 
ATOM   1315 N  N   . ILE A 1 166 ? 12.684 -1.532  -3.814  1.00 13.08  ? 166 ILE A N   1 
ATOM   1316 C  CA  . ILE A 1 166 ? 13.733 -0.896  -3.016  1.00 13.26  ? 166 ILE A CA  1 
ATOM   1317 C  C   . ILE A 1 166 ? 14.733 -1.963  -2.555  1.00 12.34  ? 166 ILE A C   1 
ATOM   1318 O  O   . ILE A 1 166 ? 15.156 -1.957  -1.417  1.00 12.13  ? 166 ILE A O   1 
ATOM   1319 C  CB  . ILE A 1 166 ? 13.149 -0.075  -1.836  1.00 12.28  ? 166 ILE A CB  1 
ATOM   1320 C  CG1 . ILE A 1 166 ? 12.293 -0.922  -0.905  1.00 12.87  ? 166 ILE A CG1 1 
ATOM   1321 C  CG2 . ILE A 1 166 ? 12.399 1.150   -2.416  1.00 15.35  ? 166 ILE A CG2 1 
ATOM   1322 C  CD1 . ILE A 1 166 ? 12.330 -0.429  0.540   1.00 15.43  ? 166 ILE A CD1 1 
ATOM   1323 N  N   . LYS A 1 167 ? 15.141 -2.834  -3.481  1.00 14.44  ? 167 LYS A N   1 
ATOM   1324 C  CA  . LYS A 1 167 ? 15.909 -4.014  -3.085  1.00 13.53  ? 167 LYS A CA  1 
ATOM   1325 C  C   . LYS A 1 167 ? 17.231 -3.588  -2.426  1.00 12.15  ? 167 LYS A C   1 
ATOM   1326 O  O   . LYS A 1 167 ? 17.715 -4.230  -1.481  1.00 12.42  ? 167 LYS A O   1 
ATOM   1327 C  CB  . LYS A 1 167 ? 16.163 -4.913  -4.286  1.00 14.74  ? 167 LYS A CB  1 
ATOM   1328 C  CG  . LYS A 1 167 ? 16.919 -6.181  -3.885  1.00 16.23  ? 167 LYS A CG  1 
ATOM   1329 C  CD  . LYS A 1 167 ? 17.223 -7.095  -5.098  1.00 21.36  ? 167 LYS A CD  1 
ATOM   1330 C  CE  . LYS A 1 167 ? 18.031 -8.342  -4.732  1.00 32.88  ? 167 LYS A CE  1 
ATOM   1331 N  N   . THR A 1 168 ? 17.880 -2.535  -2.944  1.00 11.25  ? 168 THR A N   1 
ATOM   1332 C  CA  . THR A 1 168 ? 19.245 -2.223  -2.571  1.00 12.48  ? 168 THR A CA  1 
ATOM   1333 C  C   . THR A 1 168 ? 19.364 -0.837  -1.882  1.00 11.45  ? 168 THR A C   1 
ATOM   1334 O  O   . THR A 1 168 ? 18.466 0.012   -1.925  1.00 12.82  ? 168 THR A O   1 
ATOM   1335 C  CB  . THR A 1 168 ? 20.153 -2.228  -3.815  1.00 12.64  ? 168 THR A CB  1 
ATOM   1336 O  OG1 . THR A 1 168 ? 19.569 -1.405  -4.835  1.00 14.30  ? 168 THR A OG1 1 
ATOM   1337 C  CG2 . THR A 1 168 ? 20.331 -3.652  -4.332  1.00 14.59  ? 168 THR A CG2 1 
ATOM   1338 N  N   A LYS A 1 169 ? 20.455 -0.688  -1.145  0.50 11.97  ? 169 LYS A N   1 
ATOM   1339 N  N   B LYS A 1 169 ? 20.480 -0.668  -1.205  0.50 12.06  ? 169 LYS A N   1 
ATOM   1340 C  CA  A LYS A 1 169 ? 20.781 0.462   -0.323  0.50 11.97  ? 169 LYS A CA  1 
ATOM   1341 C  CA  B LYS A 1 169 ? 20.766 0.474   -0.366  0.50 11.72  ? 169 LYS A CA  1 
ATOM   1342 C  C   A LYS A 1 169 ? 20.565 1.741   -1.116  0.50 12.36  ? 169 LYS A C   1 
ATOM   1343 C  C   B LYS A 1 169 ? 20.583 1.778   -1.123  0.50 12.18  ? 169 LYS A C   1 
ATOM   1344 O  O   A LYS A 1 169 ? 21.059 1.861   -2.234  0.50 13.48  ? 169 LYS A O   1 
ATOM   1345 O  O   B LYS A 1 169 ? 21.138 1.993   -2.196  0.50 15.00  ? 169 LYS A O   1 
ATOM   1346 C  CB  A LYS A 1 169 ? 22.262 0.381   0.100   0.50 13.34  ? 169 LYS A CB  1 
ATOM   1347 C  CB  B LYS A 1 169 ? 22.218 0.383   0.114   0.50 13.22  ? 169 LYS A CB  1 
ATOM   1348 C  CG  A LYS A 1 169 ? 22.723 1.527   1.020   0.50 15.75  ? 169 LYS A CG  1 
ATOM   1349 C  CG  B LYS A 1 169 ? 22.642 1.580   0.953   0.50 14.62  ? 169 LYS A CG  1 
ATOM   1350 C  CD  A LYS A 1 169 ? 24.209 1.485   1.479   0.50 18.99  ? 169 LYS A CD  1 
ATOM   1351 C  CD  B LYS A 1 169 ? 24.009 1.425   1.568   0.50 17.04  ? 169 LYS A CD  1 
ATOM   1352 C  CE  A LYS A 1 169 ? 24.621 2.674   2.342   0.50 26.11  ? 169 LYS A CE  1 
ATOM   1353 C  CE  B LYS A 1 169 ? 25.068 0.930   0.599   0.50 17.30  ? 169 LYS A CE  1 
ATOM   1354 N  NZ  A LYS A 1 169 ? 26.053 2.682   2.752   0.50 33.07  ? 169 LYS A NZ  1 
ATOM   1355 N  NZ  B LYS A 1 169 ? 26.373 0.832   1.291   0.50 24.17  ? 169 LYS A NZ  1 
ATOM   1356 N  N   . GLY A 1 170 ? 19.789 2.661   -0.551  1.00 12.63  ? 170 GLY A N   1 
ATOM   1357 C  CA  . GLY A 1 170 ? 19.598 3.983   -1.117  1.00 15.21  ? 170 GLY A CA  1 
ATOM   1358 C  C   . GLY A 1 170 ? 18.434 4.101   -2.096  1.00 14.44  ? 170 GLY A C   1 
ATOM   1359 O  O   . GLY A 1 170 ? 18.121 5.206   -2.547  1.00 18.50  ? 170 GLY A O   1 
ATOM   1360 N  N   A LYS A 1 171 ? 17.804 2.976   -2.483  0.50 13.95  ? 171 LYS A N   1 
ATOM   1361 N  N   B LYS A 1 171 ? 17.756 2.981   -2.398  0.50 13.56  ? 171 LYS A N   1 
ATOM   1362 C  CA  A LYS A 1 171 ? 16.570 3.063   -3.260  0.50 14.17  ? 171 LYS A CA  1 
ATOM   1363 C  CA  B LYS A 1 171 ? 16.533 3.006   -3.197  0.50 13.08  ? 171 LYS A CA  1 
ATOM   1364 C  C   A LYS A 1 171 ? 15.441 3.538   -2.348  0.50 12.79  ? 171 LYS A C   1 
ATOM   1365 C  C   B LYS A 1 171 ? 15.342 3.447   -2.350  0.50 11.93  ? 171 LYS A C   1 
ATOM   1366 O  O   A LYS A 1 171 ? 15.374 3.121   -1.202  0.50 12.87  ? 171 LYS A O   1 
ATOM   1367 O  O   B LYS A 1 171 ? 15.090 2.896   -1.290  0.50 10.19  ? 171 LYS A O   1 
ATOM   1368 C  CB  A LYS A 1 171 ? 16.200 1.749   -3.964  0.50 14.49  ? 171 LYS A CB  1 
ATOM   1369 C  CB  B LYS A 1 171 ? 16.251 1.663   -3.878  0.50 13.82  ? 171 LYS A CB  1 
ATOM   1370 C  CG  A LYS A 1 171 ? 17.285 1.233   -4.909  0.50 18.12  ? 171 LYS A CG  1 
ATOM   1371 C  CG  B LYS A 1 171 ? 17.352 1.262   -4.860  0.50 15.59  ? 171 LYS A CG  1 
ATOM   1372 C  CD  A LYS A 1 171 ? 16.771 0.220   -5.940  0.50 20.52  ? 171 LYS A CD  1 
ATOM   1373 C  CD  B LYS A 1 171 ? 17.372 2.131   -6.117  0.50 17.62  ? 171 LYS A CD  1 
ATOM   1374 C  CE  A LYS A 1 171 ? 17.489 0.235   -7.278  0.50 23.57  ? 171 LYS A CE  1 
ATOM   1375 C  CE  B LYS A 1 171 ? 18.320 1.685   -7.223  0.50 22.98  ? 171 LYS A CE  1 
ATOM   1376 N  NZ  A LYS A 1 171 ? 17.110 1.396   -8.117  0.50 38.47  ? 171 LYS A NZ  1 
ATOM   1377 N  NZ  B LYS A 1 171 ? 18.267 2.578   -8.414  0.50 27.66  ? 171 LYS A NZ  1 
ATOM   1378 N  N   . SER A 1 172 ? 14.555 4.349   -2.934  1.00 13.85  ? 172 SER A N   1 
ATOM   1379 C  CA  . SER A 1 172 ? 13.314 4.767   -2.320  1.00 14.28  ? 172 SER A CA  1 
ATOM   1380 C  C   . SER A 1 172 ? 12.188 4.601   -3.351  1.00 12.44  ? 172 SER A C   1 
ATOM   1381 O  O   . SER A 1 172 ? 12.393 4.587   -4.604  1.00 16.13  ? 172 SER A O   1 
ATOM   1382 C  CB  . SER A 1 172 ? 13.409 6.192   -1.729  1.00 15.38  ? 172 SER A CB  1 
ATOM   1383 O  OG  . SER A 1 172 ? 13.544 7.143   -2.773  1.00 17.89  ? 172 SER A OG  1 
ATOM   1384 N  N   . ALA A 1 173 ? 10.961 4.639   -2.816  1.00 15.04  ? 173 ALA A N   1 
ATOM   1385 C  CA  . ALA A 1 173 ? 9.779  4.609   -3.665  1.00 15.25  ? 173 ALA A CA  1 
ATOM   1386 C  C   . ALA A 1 173 ? 8.654  5.387   -2.998  1.00 13.59  ? 173 ALA A C   1 
ATOM   1387 O  O   . ALA A 1 173 ? 8.589  5.489   -1.769  1.00 12.91  ? 173 ALA A O   1 
ATOM   1388 C  CB  . ALA A 1 173 ? 9.330  3.175   -3.937  1.00 18.08  ? 173 ALA A CB  1 
ATOM   1389 N  N   . ASP A 1 174 ? 7.745  5.959   -3.800  1.00 15.02  ? 174 ASP A N   1 
ATOM   1390 C  CA  . ASP A 1 174 ? 6.571  6.601   -3.269  1.00 17.28  ? 174 ASP A CA  1 
ATOM   1391 C  C   . ASP A 1 174 ? 5.817  5.555   -2.448  1.00 15.95  ? 174 ASP A C   1 
ATOM   1392 O  O   . ASP A 1 174 ? 5.659  4.359   -2.791  1.00 18.79  ? 174 ASP A O   1 
ATOM   1393 C  CB  . ASP A 1 174 ? 5.691  7.149   -4.408  1.00 24.13  ? 174 ASP A CB  1 
ATOM   1394 C  CG  . ASP A 1 174 ? 6.198  8.445   -5.070  1.00 47.44  ? 174 ASP A CG  1 
ATOM   1395 O  OD1 . ASP A 1 174 ? 6.650  9.392   -4.355  1.00 51.35  ? 174 ASP A OD1 1 
ATOM   1396 O  OD2 . ASP A 1 174 ? 6.121  8.546   -6.355  1.00 47.22  ? 174 ASP A OD2 1 
ATOM   1397 N  N   . PHE A 1 175 ? 5.279  6.027   -1.332  1.00 13.57  ? 175 PHE A N   1 
ATOM   1398 C  CA  . PHE A 1 175 ? 4.531  5.130   -0.475  1.00 12.42  ? 175 PHE A CA  1 
ATOM   1399 C  C   . PHE A 1 175 ? 3.446  5.885   0.225   1.00 13.02  ? 175 PHE A C   1 
ATOM   1400 O  O   . PHE A 1 175 ? 3.429  6.003   1.424   1.00 18.56  ? 175 PHE A O   1 
ATOM   1401 C  CB  . PHE A 1 175 ? 5.467  4.334   0.434   1.00 14.16  ? 175 PHE A CB  1 
ATOM   1402 C  CG  . PHE A 1 175 ? 4.852  3.052   0.954   1.00 13.20  ? 175 PHE A CG  1 
ATOM   1403 C  CD1 . PHE A 1 175 ? 4.606  1.972   0.102   1.00 14.16  ? 175 PHE A CD1 1 
ATOM   1404 C  CD2 . PHE A 1 175 ? 4.445  2.934   2.277   1.00 13.99  ? 175 PHE A CD2 1 
ATOM   1405 C  CE1 . PHE A 1 175 ? 4.013  0.800   0.588   1.00 15.87  ? 175 PHE A CE1 1 
ATOM   1406 C  CE2 . PHE A 1 175 ? 3.861  1.751   2.765   1.00 13.86  ? 175 PHE A CE2 1 
ATOM   1407 C  CZ  . PHE A 1 175 ? 3.617  0.703   1.896   1.00 16.28  ? 175 PHE A CZ  1 
ATOM   1408 N  N   . THR A 1 176 ? 2.494  6.392   -0.546  1.00 13.38  ? 176 THR A N   1 
ATOM   1409 C  CA  . THR A 1 176 ? 1.451  7.263   -0.031  1.00 12.99  ? 176 THR A CA  1 
ATOM   1410 C  C   . THR A 1 176 ? 0.244  6.424   0.337   1.00 11.30  ? 176 THR A C   1 
ATOM   1411 O  O   . THR A 1 176 ? 0.067  5.267   -0.125  1.00 13.85  ? 176 THR A O   1 
ATOM   1412 C  CB  . THR A 1 176 ? 1.102  8.323   -1.071  1.00 16.39  ? 176 THR A CB  1 
ATOM   1413 O  OG1 . THR A 1 176 ? 0.814  7.724   -2.339  1.00 21.21  ? 176 THR A OG1 1 
ATOM   1414 C  CG2 . THR A 1 176 ? 2.208  9.345   -1.238  1.00 21.01  ? 176 THR A CG2 1 
ATOM   1415 N  N   . ASN A 1 177 ? -0.614 6.980   1.197   1.00 13.07  ? 177 ASN A N   1 
ATOM   1416 C  CA  . ASN A 1 177 ? -1.896 6.417   1.565   1.00 13.15  ? 177 ASN A CA  1 
ATOM   1417 C  C   . ASN A 1 177 ? -1.791 5.103   2.318   1.00 13.55  ? 177 ASN A C   1 
ATOM   1418 O  O   . ASN A 1 177 ? -2.668 4.252   2.183   1.00 19.24  ? 177 ASN A O   1 
ATOM   1419 C  CB  . ASN A 1 177 ? -2.827 6.314   0.368   1.00 15.09  ? 177 ASN A CB  1 
ATOM   1420 C  CG  . ASN A 1 177 ? -3.010 7.694   -0.236  1.00 14.78  ? 177 ASN A CG  1 
ATOM   1421 O  OD1 . ASN A 1 177 ? -3.570 8.612   0.385   1.00 19.83  ? 177 ASN A OD1 1 
ATOM   1422 N  ND2 . ASN A 1 177 ? -2.441 7.890   -1.419  1.00 15.69  ? 177 ASN A ND2 1 
ATOM   1423 N  N   . PHE A 1 178 ? -0.708 4.912   3.054   1.00 12.64  ? 178 PHE A N   1 
ATOM   1424 C  CA  . PHE A 1 178 ? -0.588 3.681   3.846   1.00 12.35  ? 178 PHE A CA  1 
ATOM   1425 C  C   . PHE A 1 178 ? -1.081 3.981   5.252   1.00 11.97  ? 178 PHE A C   1 
ATOM   1426 O  O   . PHE A 1 178 ? -0.655 4.974   5.844   1.00 13.43  ? 178 PHE A O   1 
ATOM   1427 C  CB  . PHE A 1 178 ? 0.855  3.196   3.881   1.00 12.94  ? 178 PHE A CB  1 
ATOM   1428 C  CG  . PHE A 1 178 ? 1.015  1.988   4.786   1.00 12.72  ? 178 PHE A CG  1 
ATOM   1429 C  CD1 . PHE A 1 178 ? 0.657  0.722   4.351   1.00 14.01  ? 178 PHE A CD1 1 
ATOM   1430 C  CD2 . PHE A 1 178 ? 1.522  2.123   6.068   1.00 12.50  ? 178 PHE A CD2 1 
ATOM   1431 C  CE1 . PHE A 1 178 ? 0.803  -0.381  5.177   1.00 14.07  ? 178 PHE A CE1 1 
ATOM   1432 C  CE2 . PHE A 1 178 ? 1.668  1.019   6.894   1.00 12.31  ? 178 PHE A CE2 1 
ATOM   1433 C  CZ  . PHE A 1 178 ? 1.309  -0.230  6.447   1.00 13.71  ? 178 PHE A CZ  1 
ATOM   1434 N  N   . ASP A 1 179 ? -1.906 3.122   5.818   1.00 13.53  ? 179 ASP A N   1 
ATOM   1435 C  CA  . ASP A 1 179 ? -2.484 3.356   7.128   1.00 13.81  ? 179 ASP A CA  1 
ATOM   1436 C  C   . ASP A 1 179 ? -1.772 2.489   8.154   1.00 11.56  ? 179 ASP A C   1 
ATOM   1437 O  O   . ASP A 1 179 ? -1.956 1.244   8.174   1.00 13.46  ? 179 ASP A O   1 
ATOM   1438 C  CB  . ASP A 1 179 ? -3.959 2.954   7.097   1.00 16.85  ? 179 ASP A CB  1 
ATOM   1439 C  CG  . ASP A 1 179 ? -4.709 3.345   8.358   1.00 18.12  ? 179 ASP A CG  1 
ATOM   1440 O  OD1 . ASP A 1 179 ? -4.081 3.609   9.409   1.00 15.61  ? 179 ASP A OD1 1 
ATOM   1441 O  OD2 . ASP A 1 179 ? -5.928 3.266   8.305   1.00 25.98  ? 179 ASP A OD2 1 
ATOM   1442 N  N   . PRO A 1 180 ? -0.958 3.057   9.068   1.00 11.21  ? 180 PRO A N   1 
ATOM   1443 C  CA  . PRO A 1 180 ? -0.187 2.249   10.021  1.00 11.39  ? 180 PRO A CA  1 
ATOM   1444 C  C   . PRO A 1 180 ? -1.080 1.604   11.065  1.00 11.73  ? 180 PRO A C   1 
ATOM   1445 O  O   . PRO A 1 180 ? -0.601 0.724   11.789  1.00 12.07  ? 180 PRO A O   1 
ATOM   1446 C  CB  . PRO A 1 180 ? 0.809  3.250   10.585  1.00 13.43  ? 180 PRO A CB  1 
ATOM   1447 C  CG  . PRO A 1 180 ? 0.089  4.606   10.474  1.00 13.41  ? 180 PRO A CG  1 
ATOM   1448 C  CD  . PRO A 1 180 ? -0.672 4.507   9.159   1.00 12.80  ? 180 PRO A CD  1 
ATOM   1449 N  N   . ARG A 1 181 ? -2.365 2.004   11.152  1.00 11.25  ? 181 ARG A N   1 
ATOM   1450 C  CA  . ARG A 1 181 ? -3.243 1.330   12.113  1.00 12.51  ? 181 ARG A CA  1 
ATOM   1451 C  C   . ARG A 1 181 ? -3.340 -0.156  11.805  1.00 12.90  ? 181 ARG A C   1 
ATOM   1452 O  O   . ARG A 1 181 ? -3.676 -0.932  12.706  1.00 13.79  ? 181 ARG A O   1 
ATOM   1453 C  CB  . ARG A 1 181 ? -4.615 1.988   12.123  1.00 13.35  ? 181 ARG A CB  1 
ATOM   1454 C  CG  . ARG A 1 181 ? -4.540 3.390   12.716  1.00 15.34  ? 181 ARG A CG  1 
ATOM   1455 C  CD  . ARG A 1 181 ? -5.830 4.108   12.672  1.00 17.65  ? 181 ARG A CD  1 
ATOM   1456 N  NE  . ARG A 1 181 ? -6.206 4.339   11.294  1.00 18.77  ? 181 ARG A NE  1 
ATOM   1457 C  CZ  . ARG A 1 181 ? -7.255 5.115   10.966  1.00 20.34  ? 181 ARG A CZ  1 
ATOM   1458 N  NH1 . ARG A 1 181 ? -8.065 5.526   11.943  1.00 24.56  ? 181 ARG A NH1 1 
ATOM   1459 N  NH2 . ARG A 1 181 ? -7.576 5.267   9.696   1.00 24.27  ? 181 ARG A NH2 1 
ATOM   1460 N  N   . GLY A 1 182 ? -3.149 -0.529  10.538  1.00 13.16  ? 182 GLY A N   1 
ATOM   1461 C  CA  . GLY A 1 182 ? -3.252 -1.921  10.135  1.00 13.70  ? 182 GLY A CA  1 
ATOM   1462 C  C   . GLY A 1 182 ? -2.113 -2.797  10.687  1.00 13.06  ? 182 GLY A C   1 
ATOM   1463 O  O   . GLY A 1 182 ? -2.119 -4.011  10.445  1.00 16.45  ? 182 GLY A O   1 
ATOM   1464 N  N   . LEU A 1 183 ? -1.104 -2.197  11.353  1.00 11.88  ? 183 LEU A N   1 
ATOM   1465 C  CA  . LEU A 1 183 ? 0.032  -2.930  11.881  1.00 11.65  ? 183 LEU A CA  1 
ATOM   1466 C  C   . LEU A 1 183 ? -0.090 -3.143  13.396  1.00 11.64  ? 183 LEU A C   1 
ATOM   1467 O  O   . LEU A 1 183 ? 0.805  -3.729  14.016  1.00 13.32  ? 183 LEU A O   1 
ATOM   1468 C  CB  . LEU A 1 183 ? 1.349  -2.230  11.559  1.00 12.62  ? 183 LEU A CB  1 
ATOM   1469 C  CG  . LEU A 1 183 ? 1.641  -2.105  10.057  1.00 13.62  ? 183 LEU A CG  1 
ATOM   1470 C  CD1 . LEU A 1 183 ? 2.868  -1.236  9.891   1.00 16.65  ? 183 LEU A CD1 1 
ATOM   1471 C  CD2 . LEU A 1 183 ? 1.749  -3.447  9.381   1.00 17.34  ? 183 LEU A CD2 1 
ATOM   1472 N  N   . LEU A 1 184 ? -1.182 -2.629  14.027  1.00 11.96  ? 184 LEU A N   1 
ATOM   1473 C  CA  . LEU A 1 184 ? -1.271 -2.697  15.477  1.00 12.46  ? 184 LEU A CA  1 
ATOM   1474 C  C   . LEU A 1 184 ? -2.009 -3.965  15.898  1.00 13.90  ? 184 LEU A C   1 
ATOM   1475 O  O   . LEU A 1 184 ? -2.919 -4.425  15.236  1.00 19.81  ? 184 LEU A O   1 
ATOM   1476 C  CB  . LEU A 1 184 ? -2.033 -1.471  16.002  1.00 14.26  ? 184 LEU A CB  1 
ATOM   1477 C  CG  . LEU A 1 184 ? -1.467 -0.115  15.578  1.00 14.49  ? 184 LEU A CG  1 
ATOM   1478 C  CD1 . LEU A 1 184 ? -2.375 1.004   16.093  1.00 17.36  ? 184 LEU A CD1 1 
ATOM   1479 C  CD2 . LEU A 1 184 ? -0.053 0.022   16.064  1.00 18.58  ? 184 LEU A CD2 1 
ATOM   1480 N  N   . PRO A 1 185 ? -1.625 -4.523  17.055  1.00 11.98  ? 185 PRO A N   1 
ATOM   1481 C  CA  . PRO A 1 185 ? -2.379 -5.677  17.614  1.00 12.96  ? 185 PRO A CA  1 
ATOM   1482 C  C   . PRO A 1 185 ? -3.657 -5.143  18.263  1.00 13.14  ? 185 PRO A C   1 
ATOM   1483 O  O   . PRO A 1 185 ? -3.883 -3.935  18.358  1.00 14.57  ? 185 PRO A O   1 
ATOM   1484 C  CB  . PRO A 1 185 ? -1.439 -6.268  18.666  1.00 13.41  ? 185 PRO A CB  1 
ATOM   1485 C  CG  . PRO A 1 185 ? -0.685 -5.036  19.133  1.00 12.06  ? 185 PRO A CG  1 
ATOM   1486 C  CD  . PRO A 1 185 ? -0.488 -4.115  17.887  1.00 10.49  ? 185 PRO A CD  1 
ATOM   1487 N  N   A GLU A 1 186 ? -4.517 -6.037  18.732  0.50 14.14  ? 186 GLU A N   1 
ATOM   1488 N  N   B GLU A 1 186 ? -4.481 -6.042  18.760  0.50 13.63  ? 186 GLU A N   1 
ATOM   1489 C  CA  A GLU A 1 186 ? -5.781 -5.638  19.359  0.50 15.22  ? 186 GLU A CA  1 
ATOM   1490 C  CA  B GLU A 1 186 ? -5.763 -5.659  19.348  0.50 13.21  ? 186 GLU A CA  1 
ATOM   1491 C  C   A GLU A 1 186 ? -5.526 -4.858  20.640  0.50 13.90  ? 186 GLU A C   1 
ATOM   1492 C  C   B GLU A 1 186 ? -5.557 -4.897  20.652  0.50 13.02  ? 186 GLU A C   1 
ATOM   1493 O  O   A GLU A 1 186 ? -6.168 -3.828  20.871  0.50 15.86  ? 186 GLU A O   1 
ATOM   1494 O  O   B GLU A 1 186 ? -6.237 -3.894  20.903  0.50 15.01  ? 186 GLU A O   1 
ATOM   1495 C  CB  A GLU A 1 186 ? -6.640 -6.864  19.677  0.50 18.29  ? 186 GLU A CB  1 
ATOM   1496 C  CB  B GLU A 1 186 ? -6.576 -6.936  19.523  0.50 12.78  ? 186 GLU A CB  1 
ATOM   1497 C  CG  A GLU A 1 186 ? -7.197 -7.546  18.435  0.50 25.32  ? 186 GLU A CG  1 
ATOM   1498 C  CG  B GLU A 1 186 ? -7.781 -6.766  20.424  0.50 14.42  ? 186 GLU A CG  1 
ATOM   1499 C  CD  A GLU A 1 186 ? -8.105 -8.746  18.678  0.50 34.10  ? 186 GLU A CD  1 
ATOM   1500 C  CD  B GLU A 1 186 ? -8.463 -8.075  20.808  0.50 17.40  ? 186 GLU A CD  1 
ATOM   1501 O  OE1 A GLU A 1 186 ? -8.519 -9.428  17.690  0.50 35.35  ? 186 GLU A OE1 1 
ATOM   1502 O  OE1 B GLU A 1 186 ? -8.085 -9.112  20.247  0.50 21.55  ? 186 GLU A OE1 1 
ATOM   1503 O  OE2 A GLU A 1 186 ? -8.408 -8.955  19.879  0.50 30.08  ? 186 GLU A OE2 1 
ATOM   1504 O  OE2 B GLU A 1 186 ? -9.327 -8.010  21.681  0.50 21.52  ? 186 GLU A OE2 1 
ATOM   1505 N  N   . SER A 1 187 ? -4.657 -5.412  21.485  1.00 12.18  ? 187 SER A N   1 
ATOM   1506 C  CA  . SER A 1 187 ? -4.427 -4.811  22.781  1.00 12.72  ? 187 SER A CA  1 
ATOM   1507 C  C   . SER A 1 187 ? -3.276 -3.812  22.749  1.00 11.84  ? 187 SER A C   1 
ATOM   1508 O  O   . SER A 1 187 ? -2.236 -4.055  22.153  1.00 14.73  ? 187 SER A O   1 
ATOM   1509 C  CB  . SER A 1 187 ? -4.067 -5.907  23.778  1.00 15.27  ? 187 SER A CB  1 
ATOM   1510 O  OG  . SER A 1 187 ? -3.744 -5.326  25.077  1.00 15.08  ? 187 SER A OG  1 
ATOM   1511 N  N   . LEU A 1 188 ? -3.442 -2.714  23.530  1.00 13.10  ? 188 LEU A N   1 
ATOM   1512 C  CA  . LEU A 1 188 ? -2.371 -1.744  23.716  1.00 14.05  ? 188 LEU A CA  1 
ATOM   1513 C  C   . LEU A 1 188 ? -1.687 -1.911  25.071  1.00 13.10  ? 188 LEU A C   1 
ATOM   1514 O  O   . LEU A 1 188 ? -1.007 -1.006  25.521  1.00 15.58  ? 188 LEU A O   1 
ATOM   1515 C  CB  . LEU A 1 188 ? -2.883 -0.305  23.535  1.00 17.04  ? 188 LEU A CB  1 
ATOM   1516 C  CG  . LEU A 1 188 ? -3.360 0.047   22.137  1.00 19.26  ? 188 LEU A CG  1 
ATOM   1517 C  CD1 . LEU A 1 188 ? -3.885 1.514   22.012  1.00 24.95  ? 188 LEU A CD1 1 
ATOM   1518 C  CD2 . LEU A 1 188 ? -2.275 -0.262  21.097  1.00 23.83  ? 188 LEU A CD2 1 
ATOM   1519 N  N   . ASP A 1 189 ? -1.842 -3.053  25.755  1.00 13.00  ? 189 ASP A N   1 
ATOM   1520 C  CA  . ASP A 1 189 ? -1.079 -3.292  26.959  1.00 12.69  ? 189 ASP A CA  1 
ATOM   1521 C  C   . ASP A 1 189 ? 0.418  -3.231  26.630  1.00 11.12  ? 189 ASP A C   1 
ATOM   1522 O  O   . ASP A 1 189 ? 0.842  -3.706  25.584  1.00 11.37  ? 189 ASP A O   1 
ATOM   1523 C  CB  . ASP A 1 189 ? -1.420 -4.667  27.555  1.00 14.80  ? 189 ASP A CB  1 
ATOM   1524 C  CG  . ASP A 1 189 ? -2.789 -4.830  28.188  1.00 19.57  ? 189 ASP A CG  1 
ATOM   1525 O  OD1 . ASP A 1 189 ? -3.412 -3.790  28.478  1.00 23.89  ? 189 ASP A OD1 1 
ATOM   1526 O  OD2 . ASP A 1 189 ? -3.118 -5.958  28.486  1.00 25.12  ? 189 ASP A OD2 1 
ATOM   1527 N  N   . TYR A 1 190 ? 1.217  -2.629  27.523  1.00 10.52  ? 190 TYR A N   1 
ATOM   1528 C  CA  . TYR A 1 190 ? 2.612  -2.349  27.179  1.00 9.81   ? 190 TYR A CA  1 
ATOM   1529 C  C   . TYR A 1 190 ? 3.512  -2.408  28.406  1.00 9.30   ? 190 TYR A C   1 
ATOM   1530 O  O   . TYR A 1 190 ? 3.049  -2.299  29.550  1.00 11.02  ? 190 TYR A O   1 
ATOM   1531 C  CB  . TYR A 1 190 ? 2.751  -0.994  26.480  1.00 10.21  ? 190 TYR A CB  1 
ATOM   1532 C  CG  . TYR A 1 190 ? 2.370  0.179   27.358  1.00 10.68  ? 190 TYR A CG  1 
ATOM   1533 C  CD1 . TYR A 1 190 ? 3.310  0.791   28.188  1.00 11.27  ? 190 TYR A CD1 1 
ATOM   1534 C  CD2 . TYR A 1 190 ? 1.097  0.703   27.295  1.00 12.38  ? 190 TYR A CD2 1 
ATOM   1535 C  CE1 . TYR A 1 190 ? 2.954  1.883   28.995  1.00 12.26  ? 190 TYR A CE1 1 
ATOM   1536 C  CE2 . TYR A 1 190 ? 0.730  1.777   28.084  1.00 12.16  ? 190 TYR A CE2 1 
ATOM   1537 C  CZ  . TYR A 1 190 ? 1.640  2.352   28.958  1.00 12.45  ? 190 TYR A CZ  1 
ATOM   1538 O  OH  . TYR A 1 190 ? 1.294  3.404   29.770  1.00 13.73  ? 190 TYR A OH  1 
ATOM   1539 N  N   . TRP A 1 191 ? 4.801  -2.531  28.086  1.00 9.86   ? 191 TRP A N   1 
ATOM   1540 C  CA  . TRP A 1 191 ? 5.871  -2.245  29.039  1.00 9.69   ? 191 TRP A CA  1 
ATOM   1541 C  C   . TRP A 1 191 ? 6.552  -0.940  28.614  1.00 9.30   ? 191 TRP A C   1 
ATOM   1542 O  O   . TRP A 1 191 ? 6.618  -0.648  27.424  1.00 10.85  ? 191 TRP A O   1 
ATOM   1543 C  CB  . TRP A 1 191 ? 6.917  -3.376  29.014  1.00 10.73  ? 191 TRP A CB  1 
ATOM   1544 C  CG  . TRP A 1 191 ? 6.375  -4.709  29.461  1.00 10.54  ? 191 TRP A CG  1 
ATOM   1545 C  CD1 . TRP A 1 191 ? 6.159  -5.118  30.747  1.00 11.97  ? 191 TRP A CD1 1 
ATOM   1546 C  CD2 . TRP A 1 191 ? 6.091  -5.818  28.593  1.00 10.55  ? 191 TRP A CD2 1 
ATOM   1547 N  NE1 . TRP A 1 191 ? 5.728  -6.428  30.726  1.00 12.41  ? 191 TRP A NE1 1 
ATOM   1548 C  CE2 . TRP A 1 191 ? 5.697  -6.881  29.433  1.00 11.68  ? 191 TRP A CE2 1 
ATOM   1549 C  CE3 . TRP A 1 191 ? 6.206  -6.024  27.198  1.00 11.55  ? 191 TRP A CE3 1 
ATOM   1550 C  CZ2 . TRP A 1 191 ? 5.392  -8.143  28.918  1.00 13.17  ? 191 TRP A CZ2 1 
ATOM   1551 C  CZ3 . TRP A 1 191 ? 5.916  -7.278  26.692  1.00 11.99  ? 191 TRP A CZ3 1 
ATOM   1552 C  CH2 . TRP A 1 191 ? 5.536  -8.321  27.553  1.00 13.55  ? 191 TRP A CH2 1 
ATOM   1553 N  N   . THR A 1 192 ? 7.135  -0.239  29.579  1.00 9.26   ? 192 THR A N   1 
ATOM   1554 C  CA  . THR A 1 192 ? 7.852  0.983   29.206  1.00 8.92   ? 192 THR A CA  1 
ATOM   1555 C  C   . THR A 1 192 ? 9.112  1.140   30.070  1.00 9.31   ? 192 THR A C   1 
ATOM   1556 O  O   . THR A 1 192 ? 9.147  0.756   31.258  1.00 10.16  ? 192 THR A O   1 
ATOM   1557 C  CB  . THR A 1 192 ? 6.917  2.197   29.323  1.00 9.70   ? 192 THR A CB  1 
ATOM   1558 O  OG1 . THR A 1 192 ? 7.615  3.379   28.904  1.00 10.88  ? 192 THR A OG1 1 
ATOM   1559 C  CG2 . THR A 1 192 ? 6.401  2.449   30.723  1.00 12.02  ? 192 THR A CG2 1 
ATOM   1560 N  N   . TYR A 1 193 ? 10.148 1.725   29.457  1.00 9.54   ? 193 TYR A N   1 
ATOM   1561 C  CA  . TYR A 1 193 ? 11.390 1.984   30.190  1.00 8.97   ? 193 TYR A CA  1 
ATOM   1562 C  C   . TYR A 1 193 ? 12.163 3.029   29.405  1.00 9.01   ? 193 TYR A C   1 
ATOM   1563 O  O   . TYR A 1 193 ? 11.922 3.227   28.215  1.00 9.25   ? 193 TYR A O   1 
ATOM   1564 C  CB  . TYR A 1 193 ? 12.206 0.678   30.398  1.00 9.94   ? 193 TYR A CB  1 
ATOM   1565 C  CG  . TYR A 1 193 ? 12.879 0.235   29.120  1.00 8.57   ? 193 TYR A CG  1 
ATOM   1566 C  CD1 . TYR A 1 193 ? 12.195 -0.475  28.133  1.00 9.12   ? 193 TYR A CD1 1 
ATOM   1567 C  CD2 . TYR A 1 193 ? 14.227 0.588   28.907  1.00 9.49   ? 193 TYR A CD2 1 
ATOM   1568 C  CE1 . TYR A 1 193 ? 12.833 -0.821  26.948  1.00 8.75   ? 193 TYR A CE1 1 
ATOM   1569 C  CE2 . TYR A 1 193 ? 14.854 0.249   27.723  1.00 9.28   ? 193 TYR A CE2 1 
ATOM   1570 C  CZ  . TYR A 1 193 ? 14.148 -0.426  26.749  1.00 7.93   ? 193 TYR A CZ  1 
ATOM   1571 O  OH  . TYR A 1 193 ? 14.798 -0.731  25.586  1.00 8.91   ? 193 TYR A OH  1 
ATOM   1572 N  N   . PRO A 1 194 ? 13.089 3.725   30.083  1.00 9.48   ? 194 PRO A N   1 
ATOM   1573 C  CA  . PRO A 1 194 ? 13.920 4.716   29.388  1.00 9.51   ? 194 PRO A CA  1 
ATOM   1574 C  C   . PRO A 1 194 ? 15.137 4.045   28.738  1.00 8.97   ? 194 PRO A C   1 
ATOM   1575 O  O   . PRO A 1 194 ? 15.849 3.263   29.375  1.00 9.96   ? 194 PRO A O   1 
ATOM   1576 C  CB  . PRO A 1 194 ? 14.389 5.648   30.517  1.00 12.20  ? 194 PRO A CB  1 
ATOM   1577 C  CG  . PRO A 1 194 ? 14.442 4.729   31.719  1.00 12.14  ? 194 PRO A CG  1 
ATOM   1578 C  CD  . PRO A 1 194 ? 13.281 3.747   31.535  1.00 12.60  ? 194 PRO A CD  1 
ATOM   1579 N  N   . GLY A 1 195 ? 15.365 4.383   27.473  1.00 8.81   ? 195 GLY A N   1 
ATOM   1580 C  CA  . GLY A 1 195 ? 16.504 3.766   26.775  1.00 9.27   ? 195 GLY A CA  1 
ATOM   1581 C  C   . GLY A 1 195 ? 17.024 4.649   25.666  1.00 8.54   ? 195 GLY A C   1 
ATOM   1582 O  O   . GLY A 1 195 ? 17.099 5.892   25.792  1.00 9.41   ? 195 GLY A O   1 
ATOM   1583 N  N   . SER A 1 196 ? 17.423 3.987   24.582  1.00 8.50   ? 196 SER A N   1 
ATOM   1584 C  CA  . SER A 1 196 ? 18.270 4.597   23.570  1.00 8.65   ? 196 SER A CA  1 
ATOM   1585 C  C   . SER A 1 196 ? 17.845 4.208   22.187  1.00 8.00   ? 196 SER A C   1 
ATOM   1586 O  O   . SER A 1 196 ? 17.067 3.264   21.971  1.00 8.40   ? 196 SER A O   1 
ATOM   1587 C  CB  . SER A 1 196 ? 19.725 4.223   23.778  1.00 9.11   ? 196 SER A CB  1 
ATOM   1588 O  OG  . SER A 1 196 ? 20.000 2.865   23.346  1.00 8.91   ? 196 SER A OG  1 
ATOM   1589 N  N   . LEU A 1 197 ? 18.418 4.897   21.180  1.00 8.36   ? 197 LEU A N   1 
ATOM   1590 C  CA  . LEU A 1 197 ? 18.454 4.358   19.832  1.00 8.49   ? 197 LEU A CA  1 
ATOM   1591 C  C   . LEU A 1 197 ? 19.173 3.019   19.831  1.00 8.89   ? 197 LEU A C   1 
ATOM   1592 O  O   . LEU A 1 197 ? 20.073 2.783   20.638  1.00 9.16   ? 197 LEU A O   1 
ATOM   1593 C  CB  . LEU A 1 197 ? 19.208 5.334   18.926  1.00 9.63   ? 197 LEU A CB  1 
ATOM   1594 C  CG  . LEU A 1 197 ? 18.656 6.754   18.848  1.00 10.79  ? 197 LEU A CG  1 
ATOM   1595 C  CD1 . LEU A 1 197 ? 19.548 7.595   17.913  1.00 13.86  ? 197 LEU A CD1 1 
ATOM   1596 C  CD2 . LEU A 1 197 ? 17.172 6.725   18.361  1.00 13.08  ? 197 LEU A CD2 1 
ATOM   1597 N  N   . THR A 1 198 ? 18.849 2.171   18.826  1.00 8.79   ? 198 THR A N   1 
ATOM   1598 C  CA  . THR A 1 198 ? 19.494 0.876   18.746  1.00 8.90   ? 198 THR A CA  1 
ATOM   1599 C  C   . THR A 1 198 ? 20.472 0.812   17.580  1.00 10.06  ? 198 THR A C   1 
ATOM   1600 O  O   . THR A 1 198 ? 20.958 -0.272  17.219  1.00 12.28  ? 198 THR A O   1 
ATOM   1601 C  CB  . THR A 1 198 ? 18.488 -0.265  18.720  1.00 8.99   ? 198 THR A CB  1 
ATOM   1602 O  OG1 . THR A 1 198 ? 17.749 -0.190  17.498  1.00 8.67   ? 198 THR A OG1 1 
ATOM   1603 C  CG2 . THR A 1 198 ? 17.594 -0.237  19.936  1.00 10.70  ? 198 THR A CG2 1 
ATOM   1604 N  N   A THR A 1 199 ? 20.746 1.963   16.928  0.50 11.76  ? 199 THR A N   1 
ATOM   1605 N  N   B THR A 1 199 ? 20.784 1.994   17.008  0.50 11.84  ? 199 THR A N   1 
ATOM   1606 C  CA  A THR A 1 199 ? 21.924 1.996   16.085  0.50 15.03  ? 199 THR A CA  1 
ATOM   1607 C  CA  B THR A 1 199 ? 21.764 2.120   15.962  0.50 13.88  ? 199 THR A CA  1 
ATOM   1608 C  C   A THR A 1 199 ? 22.665 3.267   16.402  0.50 14.59  ? 199 THR A C   1 
ATOM   1609 C  C   B THR A 1 199 ? 22.629 3.306   16.332  0.50 13.85  ? 199 THR A C   1 
ATOM   1610 O  O   A THR A 1 199 ? 22.141 4.189   17.035  0.50 12.69  ? 199 THR A O   1 
ATOM   1611 O  O   B THR A 1 199 ? 22.156 4.204   17.032  0.50 12.66  ? 199 THR A O   1 
ATOM   1612 C  CB  A THR A 1 199 ? 21.683 1.943   14.577  0.50 19.21  ? 199 THR A CB  1 
ATOM   1613 C  CB  B THR A 1 199 ? 20.996 2.229   14.657  0.50 17.07  ? 199 THR A CB  1 
ATOM   1614 O  OG1 A THR A 1 199 ? 20.806 3.046   14.391  0.50 17.38  ? 199 THR A OG1 1 
ATOM   1615 O  OG1 B THR A 1 199 ? 20.687 0.849   14.348  0.50 29.36  ? 199 THR A OG1 1 
ATOM   1616 C  CG2 A THR A 1 199 ? 21.083 0.612   14.119  0.50 17.66  ? 199 THR A CG2 1 
ATOM   1617 C  CG2 B THR A 1 199 ? 21.817 2.818   13.555  0.50 11.95  ? 199 THR A CG2 1 
ATOM   1618 N  N   . PRO A 1 200 ? 23.937 3.342   15.949  1.00 15.24  ? 200 PRO A N   1 
ATOM   1619 C  CA  . PRO A 1 200 ? 24.699 4.569   16.146  1.00 15.64  ? 200 PRO A CA  1 
ATOM   1620 C  C   . PRO A 1 200 ? 23.845 5.731   15.662  1.00 16.24  ? 200 PRO A C   1 
ATOM   1621 O  O   . PRO A 1 200 ? 23.196 5.671   14.587  1.00 20.01  ? 200 PRO A O   1 
ATOM   1622 C  CB  . PRO A 1 200 ? 25.888 4.285   15.197  1.00 17.73  ? 200 PRO A CB  1 
ATOM   1623 C  CG  . PRO A 1 200 ? 26.158 2.793   15.319  1.00 19.17  ? 200 PRO A CG  1 
ATOM   1624 C  CD  . PRO A 1 200 ? 24.741 2.254   15.311  1.00 17.63  ? 200 PRO A CD  1 
ATOM   1625 N  N   . PRO A 1 201 ? 23.850 6.868   16.380  1.00 16.13  ? 201 PRO A N   1 
ATOM   1626 C  CA  . PRO A 1 201 ? 24.778 7.171   17.490  1.00 16.70  ? 201 PRO A CA  1 
ATOM   1627 C  C   . PRO A 1 201 ? 24.359 6.703   18.892  1.00 13.25  ? 201 PRO A C   1 
ATOM   1628 O  O   . PRO A 1 201 ? 25.015 7.050   19.877  1.00 14.21  ? 201 PRO A O   1 
ATOM   1629 C  CB  . PRO A 1 201 ? 24.802 8.703   17.515  1.00 19.43  ? 201 PRO A CB  1 
ATOM   1630 C  CG  . PRO A 1 201 ? 23.396 9.104   17.052  1.00 24.07  ? 201 PRO A CG  1 
ATOM   1631 C  CD  . PRO A 1 201 ? 23.027 8.046   16.026  1.00 20.01  ? 201 PRO A CD  1 
ATOM   1632 N  N   . LEU A 1 202 ? 23.318 5.859   18.972  1.00 11.19  ? 202 LEU A N   1 
ATOM   1633 C  CA  . LEU A 1 202 ? 22.976 5.168   20.248  1.00 10.87  ? 202 LEU A CA  1 
ATOM   1634 C  C   . LEU A 1 202 ? 22.564 6.131   21.370  1.00 9.60   ? 202 LEU A C   1 
ATOM   1635 O  O   . LEU A 1 202 ? 22.669 5.825   22.548  1.00 10.82  ? 202 LEU A O   1 
ATOM   1636 C  CB  . LEU A 1 202 ? 24.112 4.253   20.727  1.00 10.63  ? 202 LEU A CB  1 
ATOM   1637 C  CG  . LEU A 1 202 ? 24.452 3.151   19.689  1.00 11.76  ? 202 LEU A CG  1 
ATOM   1638 C  CD1 . LEU A 1 202 ? 25.731 2.430   20.130  1.00 14.14  ? 202 LEU A CD1 1 
ATOM   1639 C  CD2 . LEU A 1 202 ? 23.337 2.127   19.581  1.00 11.83  ? 202 LEU A CD2 1 
ATOM   1640 N  N   A THR A 1 203 ? 22.073 7.312   20.999  0.50 12.38  ? 203 THR A N   1 
ATOM   1641 N  N   B THR A 1 203 ? 22.078 7.308   20.971  0.50 11.96  ? 203 THR A N   1 
ATOM   1642 C  CA  A THR A 1 203 ? 21.833 8.343   21.989  0.50 13.55  ? 203 THR A CA  1 
ATOM   1643 C  CA  B THR A 1 203 ? 21.670 8.412   21.819  0.50 13.41  ? 203 THR A CA  1 
ATOM   1644 C  C   A THR A 1 203 ? 20.657 7.920   22.884  0.50 11.54  ? 203 THR A C   1 
ATOM   1645 C  C   B THR A 1 203 ? 20.621 7.941   22.854  0.50 11.37  ? 203 THR A C   1 
ATOM   1646 O  O   A THR A 1 203 ? 19.688 7.244   22.471  0.50 10.83  ? 203 THR A O   1 
ATOM   1647 O  O   B THR A 1 203 ? 19.665 7.232   22.488  0.50 10.81  ? 203 THR A O   1 
ATOM   1648 C  CB  A THR A 1 203 ? 21.487 9.653   21.300  0.50 23.18  ? 203 THR A CB  1 
ATOM   1649 C  CB  B THR A 1 203 ? 21.117 9.489   20.876  0.50 13.81  ? 203 THR A CB  1 
ATOM   1650 O  OG1 A THR A 1 203 ? 21.323 10.708  22.233  0.50 32.95  ? 203 THR A OG1 1 
ATOM   1651 O  OG1 B THR A 1 203 ? 22.155 9.707   19.888  0.50 15.10  ? 203 THR A OG1 1 
ATOM   1652 C  CG2 A THR A 1 203 ? 20.158 9.518   20.637  0.50 16.85  ? 203 THR A CG2 1 
ATOM   1653 C  CG2 B THR A 1 203 ? 20.980 10.792  21.617  0.50 15.08  ? 203 THR A CG2 1 
ATOM   1654 N  N   . GLU A 1 204 ? 20.749 8.354   24.139  1.00 12.81  ? 204 GLU A N   1 
ATOM   1655 C  CA  . GLU A 1 204 ? 19.859 7.910   25.199  1.00 12.45  ? 204 GLU A CA  1 
ATOM   1656 C  C   . GLU A 1 204 ? 18.687 8.893   25.279  1.00 12.43  ? 204 GLU A C   1 
ATOM   1657 O  O   . GLU A 1 204 ? 18.490 9.604   26.279  1.00 15.85  ? 204 GLU A O   1 
ATOM   1658 C  CB  . GLU A 1 204 ? 20.630 7.758   26.513  1.00 12.71  ? 204 GLU A CB  1 
ATOM   1659 C  CG  . GLU A 1 204 ? 21.612 6.622   26.350  1.00 13.61  ? 204 GLU A CG  1 
ATOM   1660 C  CD  . GLU A 1 204 ? 22.508 6.345   27.549  1.00 14.14  ? 204 GLU A CD  1 
ATOM   1661 O  OE1 . GLU A 1 204 ? 22.733 7.253   28.397  1.00 17.65  ? 204 GLU A OE1 1 
ATOM   1662 O  OE2 . GLU A 1 204 ? 22.951 5.179   27.706  1.00 12.90  ? 204 GLU A OE2 1 
ATOM   1663 N  N   . CYS A 1 205 ? 17.858 8.886   24.248  1.00 10.37  ? 205 CYS A N   1 
ATOM   1664 C  CA  . CYS A 1 205 ? 16.799 9.872   24.051  1.00 9.57   ? 205 CYS A CA  1 
ATOM   1665 C  C   . CYS A 1 205 ? 15.418 9.263   23.915  1.00 9.49   ? 205 CYS A C   1 
ATOM   1666 O  O   . CYS A 1 205 ? 14.502 9.960   23.541  1.00 10.51  ? 205 CYS A O   1 
ATOM   1667 C  CB  . CYS A 1 205 ? 17.093 10.679  22.790  1.00 10.33  ? 205 CYS A CB  1 
ATOM   1668 S  SG  . CYS A 1 205 ? 17.139 9.706   21.265  1.00 12.34  ? 205 CYS A SG  1 
ATOM   1669 N  N   . VAL A 1 206 ? 15.279 7.958   24.202  1.00 9.17   ? 206 VAL A N   1 
ATOM   1670 C  CA  . VAL A 1 206 ? 14.042 7.254   23.870  1.00 8.69   ? 206 VAL A CA  1 
ATOM   1671 C  C   . VAL A 1 206 ? 13.290 6.818   25.098  1.00 8.99   ? 206 VAL A C   1 
ATOM   1672 O  O   . VAL A 1 206 ? 13.816 6.138   25.965  1.00 10.66  ? 206 VAL A O   1 
ATOM   1673 C  CB  . VAL A 1 206 ? 14.312 6.002   23.029  1.00 8.92   ? 206 VAL A CB  1 
ATOM   1674 C  CG1 . VAL A 1 206 ? 13.026 5.302   22.639  1.00 9.38   ? 206 VAL A CG1 1 
ATOM   1675 C  CG2 . VAL A 1 206 ? 15.092 6.361   21.737  1.00 10.77  ? 206 VAL A CG2 1 
ATOM   1676 N  N   . THR A 1 207 ? 11.964 7.132   25.105  1.00 8.37   ? 207 THR A N   1 
ATOM   1677 C  CA  . THR A 1 207 ? 11.034 6.426   25.986  1.00 9.29   ? 207 THR A CA  1 
ATOM   1678 C  C   . THR A 1 207 ? 10.465 5.249   25.166  1.00 8.35   ? 207 THR A C   1 
ATOM   1679 O  O   . THR A 1 207 ? 9.799  5.459   24.163  1.00 8.92   ? 207 THR A O   1 
ATOM   1680 C  CB  . THR A 1 207 ? 9.841  7.316   26.442  1.00 9.81   ? 207 THR A CB  1 
ATOM   1681 O  OG1 . THR A 1 207 ? 10.399 8.433   27.147  1.00 11.54  ? 207 THR A OG1 1 
ATOM   1682 C  CG2 . THR A 1 207 ? 8.935  6.533   27.334  1.00 12.23  ? 207 THR A CG2 1 
ATOM   1683 N  N   . TRP A 1 208 ? 10.859 4.029   25.579  1.00 8.72   ? 208 TRP A N   1 
ATOM   1684 C  CA  . TRP A 1 208 ? 10.371 2.852   24.859  1.00 7.83   ? 208 TRP A CA  1 
ATOM   1685 C  C   . TRP A 1 208 ? 9.019  2.421   25.414  1.00 7.93   ? 208 TRP A C   1 
ATOM   1686 O  O   . TRP A 1 208 ? 8.833  2.379   26.638  1.00 8.88   ? 208 TRP A O   1 
ATOM   1687 C  CB  . TRP A 1 208 ? 11.389 1.708   25.078  1.00 8.49   ? 208 TRP A CB  1 
ATOM   1688 C  CG  . TRP A 1 208 ? 12.563 1.816   24.139  1.00 7.91   ? 208 TRP A CG  1 
ATOM   1689 C  CD1 . TRP A 1 208 ? 13.789 2.418   24.345  1.00 9.16   ? 208 TRP A CD1 1 
ATOM   1690 C  CD2 . TRP A 1 208 ? 12.519 1.437   22.763  1.00 8.40   ? 208 TRP A CD2 1 
ATOM   1691 N  NE1 . TRP A 1 208 ? 14.491 2.379   23.184  1.00 9.16   ? 208 TRP A NE1 1 
ATOM   1692 C  CE2 . TRP A 1 208 ? 13.754 1.786   22.205  1.00 8.68   ? 208 TRP A CE2 1 
ATOM   1693 C  CE3 . TRP A 1 208 ? 11.562 0.790   21.942  1.00 8.23   ? 208 TRP A CE3 1 
ATOM   1694 C  CZ2 . TRP A 1 208 ? 14.070 1.529   20.876  1.00 9.71   ? 208 TRP A CZ2 1 
ATOM   1695 C  CZ3 . TRP A 1 208 ? 11.876 0.548   20.625  1.00 9.18   ? 208 TRP A CZ3 1 
ATOM   1696 C  CH2 . TRP A 1 208 ? 13.130 0.903   20.078  1.00 10.65  ? 208 TRP A CH2 1 
ATOM   1697 N  N   . ILE A 1 209 ? 8.118  2.103   24.491  1.00 8.30   ? 209 ILE A N   1 
ATOM   1698 C  CA  . ILE A 1 209 ? 6.784  1.576   24.838  1.00 7.95   ? 209 ILE A CA  1 
ATOM   1699 C  C   . ILE A 1 209 ? 6.660  0.316   23.993  1.00 8.55   ? 209 ILE A C   1 
ATOM   1700 O  O   . ILE A 1 209 ? 6.556  0.400   22.786  1.00 9.25   ? 209 ILE A O   1 
ATOM   1701 C  CB  . ILE A 1 209 ? 5.690  2.618   24.492  1.00 9.32   ? 209 ILE A CB  1 
ATOM   1702 C  CG1 . ILE A 1 209 ? 5.919  3.891   25.318  1.00 11.15  ? 209 ILE A CG1 1 
ATOM   1703 C  CG2 . ILE A 1 209 ? 4.315  2.000   24.773  1.00 11.76  ? 209 ILE A CG2 1 
ATOM   1704 C  CD1 . ILE A 1 209 ? 5.079  5.069   24.873  1.00 13.34  ? 209 ILE A CD1 1 
ATOM   1705 N  N   . VAL A 1 210 ? 6.757  -0.868  24.661  1.00 8.43   ? 210 VAL A N   1 
ATOM   1706 C  CA  . VAL A 1 210 ? 6.768  -2.138  23.909  1.00 8.29   ? 210 VAL A CA  1 
ATOM   1707 C  C   . VAL A 1 210 ? 5.463  -2.862  24.173  1.00 7.93   ? 210 VAL A C   1 
ATOM   1708 O  O   . VAL A 1 210 ? 5.146  -3.136  25.324  1.00 9.54   ? 210 VAL A O   1 
ATOM   1709 C  CB  . VAL A 1 210 ? 7.989  -2.981  24.355  1.00 8.21   ? 210 VAL A CB  1 
ATOM   1710 C  CG1 . VAL A 1 210 ? 7.973  -4.324  23.631  1.00 10.44  ? 210 VAL A CG1 1 
ATOM   1711 C  CG2 . VAL A 1 210 ? 9.300  -2.219  24.058  1.00 10.00  ? 210 VAL A CG2 1 
ATOM   1712 N  N   . LEU A 1 211 ? 4.693  -3.093  23.120  1.00 9.26   ? 211 LEU A N   1 
ATOM   1713 C  CA  . LEU A 1 211 ? 3.388  -3.773  23.300  1.00 9.78   ? 211 LEU A CA  1 
ATOM   1714 C  C   . LEU A 1 211 ? 3.592  -5.242  23.661  1.00 9.61   ? 211 LEU A C   1 
ATOM   1715 O  O   . LEU A 1 211 ? 4.481  -5.933  23.111  1.00 10.20  ? 211 LEU A O   1 
ATOM   1716 C  CB  . LEU A 1 211 ? 2.562  -3.642  22.008  1.00 10.21  ? 211 LEU A CB  1 
ATOM   1717 C  CG  . LEU A 1 211 ? 2.176  -2.204  21.624  1.00 10.95  ? 211 LEU A CG  1 
ATOM   1718 C  CD1 . LEU A 1 211 ? 1.148  -2.252  20.469  1.00 14.34  ? 211 LEU A CD1 1 
ATOM   1719 C  CD2 . LEU A 1 211 ? 1.681  -1.389  22.768  1.00 12.24  ? 211 LEU A CD2 1 
ATOM   1720 N  N   . LYS A 1 212 ? 2.745  -5.687  24.593  1.00 10.46  ? 212 LYS A N   1 
ATOM   1721 C  CA  . LYS A 1 212 ? 2.803  -7.110  24.979  1.00 12.26  ? 212 LYS A CA  1 
ATOM   1722 C  C   . LYS A 1 212 ? 2.320  -8.071  23.889  1.00 11.56  ? 212 LYS A C   1 
ATOM   1723 O  O   . LYS A 1 212 ? 2.893  -9.164  23.747  1.00 13.52  ? 212 LYS A O   1 
ATOM   1724 C  CB  . LYS A 1 212 ? 1.971  -7.320  26.229  1.00 14.56  ? 212 LYS A CB  1 
ATOM   1725 C  CG  . LYS A 1 212 ? 1.854  -8.760  26.722  1.00 18.54  ? 212 LYS A CG  1 
ATOM   1726 C  CD  . LYS A 1 212 ? 1.049  -8.819  28.018  1.00 29.43  ? 212 LYS A CD  1 
ATOM   1727 N  N   . GLU A 1 213 ? 1.310  -7.693  23.143  1.00 9.99   ? 213 GLU A N   1 
ATOM   1728 C  CA  . GLU A 1 213 ? 0.679  -8.600  22.183  1.00 10.52  ? 213 GLU A CA  1 
ATOM   1729 C  C   . GLU A 1 213 ? 1.450  -8.496  20.875  1.00 10.82  ? 213 GLU A C   1 
ATOM   1730 O  O   . GLU A 1 213 ? 1.505  -7.428  20.273  1.00 10.53  ? 213 GLU A O   1 
ATOM   1731 C  CB  . GLU A 1 213 ? -0.783 -8.240  21.958  1.00 11.54  ? 213 GLU A CB  1 
ATOM   1732 C  CG  . GLU A 1 213 ? -1.444 -9.206  20.999  1.00 14.24  ? 213 GLU A CG  1 
ATOM   1733 C  CD  . GLU A 1 213 ? -2.925 -9.001  20.804  1.00 19.59  ? 213 GLU A CD  1 
ATOM   1734 O  OE1 . GLU A 1 213 ? -3.522 -8.093  21.316  1.00 15.77  ? 213 GLU A OE1 1 
ATOM   1735 O  OE2 . GLU A 1 213 ? -3.494 -9.942  20.189  1.00 26.80  ? 213 GLU A OE2 1 
ATOM   1736 N  N   A PRO A 1 214 ? 2.018  -9.601  20.358  0.50 9.90   ? 214 PRO A N   1 
ATOM   1737 N  N   B PRO A 1 214 ? 2.122  -9.564  20.416  0.50 10.34  ? 214 PRO A N   1 
ATOM   1738 C  CA  A PRO A 1 214 ? 2.656  -9.542  19.063  0.50 10.08  ? 214 PRO A CA  1 
ATOM   1739 C  CA  B PRO A 1 214 ? 2.700  -9.537  19.084  0.50 10.59  ? 214 PRO A CA  1 
ATOM   1740 C  C   A PRO A 1 214 ? 1.616  -9.513  17.959  0.50 10.90  ? 214 PRO A C   1 
ATOM   1741 C  C   B PRO A 1 214 ? 1.655  -9.537  17.975  0.50 10.97  ? 214 PRO A C   1 
ATOM   1742 O  O   A PRO A 1 214 ? 0.451  -9.928  18.173  0.50 13.07  ? 214 PRO A O   1 
ATOM   1743 O  O   B PRO A 1 214 ? 0.505  -9.988  18.199  0.50 13.27  ? 214 PRO A O   1 
ATOM   1744 C  CB  A PRO A 1 214 ? 3.393  -10.864 18.965  0.50 11.31  ? 214 PRO A CB  1 
ATOM   1745 C  CB  B PRO A 1 214 ? 3.471  -10.844 19.024  0.50 11.45  ? 214 PRO A CB  1 
ATOM   1746 C  CG  A PRO A 1 214 ? 2.589  -11.824 19.830  0.50 12.13  ? 214 PRO A CG  1 
ATOM   1747 C  CG  B PRO A 1 214 ? 3.643  -11.263 20.481  0.50 12.77  ? 214 PRO A CG  1 
ATOM   1748 C  CD  A PRO A 1 214 ? 2.015  -10.968 20.947  0.50 10.98  ? 214 PRO A CD  1 
ATOM   1749 C  CD  B PRO A 1 214 ? 2.362  -10.834 21.159  0.50 11.54  ? 214 PRO A CD  1 
ATOM   1750 N  N   . ILE A 1 215 ? 2.063  -9.087  16.771  1.00 10.40  ? 215 ILE A N   1 
ATOM   1751 C  CA  . ILE A 1 215 ? 1.263  -9.349  15.574  1.00 10.64  ? 215 ILE A CA  1 
ATOM   1752 C  C   . ILE A 1 215 ? 1.816  -10.570 14.892  1.00 10.20  ? 215 ILE A C   1 
ATOM   1753 O  O   . ILE A 1 215 ? 2.989  -10.935 15.061  1.00 11.95  ? 215 ILE A O   1 
ATOM   1754 C  CB  . ILE A 1 215 ? 1.188  -8.111  14.644  1.00 11.01  ? 215 ILE A CB  1 
ATOM   1755 C  CG1 . ILE A 1 215 ? 2.594  -7.718  14.126  1.00 11.05  ? 215 ILE A CG1 1 
ATOM   1756 C  CG2 . ILE A 1 215 ? 0.456  -6.935  15.356  1.00 12.98  ? 215 ILE A CG2 1 
ATOM   1757 C  CD1 . ILE A 1 215 ? 2.526  -6.735  12.988  1.00 12.87  ? 215 ILE A CD1 1 
ATOM   1758 N  N   A SER A 1 216 ? 0.915  -11.185 14.137  0.50 11.69  ? 216 SER A N   1 
ATOM   1759 N  N   B SER A 1 216 ? 0.938  -11.276 14.200  0.50 11.74  ? 216 SER A N   1 
ATOM   1760 C  CA  A SER A 1 216 ? 1.245  -12.366 13.347  0.50 12.05  ? 216 SER A CA  1 
ATOM   1761 C  CA  B SER A 1 216 ? 1.451  -12.404 13.434  0.50 13.35  ? 216 SER A CA  1 
ATOM   1762 C  C   A SER A 1 216 ? 1.476  -11.968 11.902  0.50 12.71  ? 216 SER A C   1 
ATOM   1763 C  C   B SER A 1 216 ? 1.509  -12.001 11.972  0.50 10.18  ? 216 SER A C   1 
ATOM   1764 O  O   A SER A 1 216 ? 0.612  -11.303 11.322  0.50 14.82  ? 216 SER A O   1 
ATOM   1765 O  O   B SER A 1 216 ? 0.601  -11.329 11.463  0.50 12.20  ? 216 SER A O   1 
ATOM   1766 C  CB  A SER A 1 216 ? 0.136  -13.389 13.424  0.50 14.27  ? 216 SER A CB  1 
ATOM   1767 C  CB  B SER A 1 216 ? 0.640  -13.670 13.602  0.50 14.74  ? 216 SER A CB  1 
ATOM   1768 O  OG  A SER A 1 216 ? 0.151  -14.004 14.685  0.50 19.95  ? 216 SER A OG  1 
ATOM   1769 O  OG  B SER A 1 216 ? -0.702 -13.415 13.248  0.50 14.65  ? 216 SER A OG  1 
ATOM   1770 N  N   . VAL A 1 217 ? 2.588  -12.440 11.312  1.00 11.41  ? 217 VAL A N   1 
ATOM   1771 C  CA  . VAL A 1 217 ? 2.832  -12.219 9.903   1.00 11.49  ? 217 VAL A CA  1 
ATOM   1772 C  C   . VAL A 1 217 ? 3.115  -13.597 9.300   1.00 11.53  ? 217 VAL A C   1 
ATOM   1773 O  O   . VAL A 1 217 ? 3.472  -14.539 10.000  1.00 12.60  ? 217 VAL A O   1 
ATOM   1774 C  CB  . VAL A 1 217 ? 4.040  -11.307 9.671   1.00 12.08  ? 217 VAL A CB  1 
ATOM   1775 C  CG1 . VAL A 1 217 ? 3.795  -9.971  10.397  1.00 13.47  ? 217 VAL A CG1 1 
ATOM   1776 C  CG2 . VAL A 1 217 ? 5.350  -11.923 10.150  1.00 14.19  ? 217 VAL A CG2 1 
ATOM   1777 N  N   . SER A 1 218 ? 2.933  -13.748 7.985   1.00 11.39  ? 218 SER A N   1 
ATOM   1778 C  CA  . SER A 1 218 ? 3.140  -15.075 7.391   1.00 11.50  ? 218 SER A CA  1 
ATOM   1779 C  C   . SER A 1 218 ? 4.600  -15.319 7.121   1.00 11.66  ? 218 SER A C   1 
ATOM   1780 O  O   . SER A 1 218 ? 5.414  -14.406 6.990   1.00 12.14  ? 218 SER A O   1 
ATOM   1781 C  CB  . SER A 1 218 ? 2.349  -15.271 6.187   1.00 12.58  ? 218 SER A CB  1 
ATOM   1782 O  OG  . SER A 1 218 ? 2.796  -14.353 5.197   1.00 13.30  ? 218 SER A OG  1 
ATOM   1783 N  N   . SER A 1 219 ? 4.948  -16.591 6.986   1.00 13.01  ? 219 SER A N   1 
ATOM   1784 C  CA  . SER A 1 219 ? 6.284  -16.985 6.564   1.00 14.87  ? 219 SER A CA  1 
ATOM   1785 C  C   . SER A 1 219 ? 6.656  -16.251 5.248   1.00 13.67  ? 219 SER A C   1 
ATOM   1786 O  O   . SER A 1 219 ? 7.800  -15.817 5.082   1.00 15.18  ? 219 SER A O   1 
ATOM   1787 C  CB  . SER A 1 219 ? 6.462  -18.518 6.549   1.00 18.44  ? 219 SER A CB  1 
ATOM   1788 O  OG  . SER A 1 219 ? 5.524  -19.091 5.606   1.00 21.05  ? 219 SER A OG  1 
ATOM   1789 N  N   . GLU A 1 220 ? 5.683  -16.145 4.348   1.00 13.45  ? 220 GLU A N   1 
ATOM   1790 C  CA  . GLU A 1 220 ? 5.976  -15.522 3.064   1.00 15.21  ? 220 GLU A CA  1 
ATOM   1791 C  C   . GLU A 1 220 ? 6.262  -14.028 3.183   1.00 14.20  ? 220 GLU A C   1 
ATOM   1792 O  O   . GLU A 1 220 ? 7.174  -13.498 2.515   1.00 15.19  ? 220 GLU A O   1 
ATOM   1793 C  CB  . GLU A 1 220 ? 4.846  -15.659 2.064   1.00 17.61  ? 220 GLU A CB  1 
ATOM   1794 C  CG  . GLU A 1 220 ? 4.635  -17.116 1.583   1.00 23.05  ? 220 GLU A CG  1 
ATOM   1795 C  CD  . GLU A 1 220 ? 3.751  -17.886 2.525   1.00 29.35  ? 220 GLU A CD  1 
ATOM   1796 O  OE1 . GLU A 1 220 ? 3.236  -17.381 3.510   1.00 22.27  ? 220 GLU A OE1 1 
ATOM   1797 O  OE2 . GLU A 1 220 ? 3.610  -19.107 2.261   1.00 35.95  ? 220 GLU A OE2 1 
ATOM   1798 N  N   . GLN A 1 221 ? 5.603  -13.377 4.133   1.00 12.66  ? 221 GLN A N   1 
ATOM   1799 C  CA  . GLN A 1 221 ? 5.857  -11.944 4.334   1.00 11.38  ? 221 GLN A CA  1 
ATOM   1800 C  C   . GLN A 1 221 ? 7.268  -11.724 4.868   1.00 11.89  ? 221 GLN A C   1 
ATOM   1801 O  O   . GLN A 1 221 ? 8.005  -10.864 4.352   1.00 12.74  ? 221 GLN A O   1 
ATOM   1802 C  CB  . GLN A 1 221 ? 4.795  -11.378 5.245   1.00 12.46  ? 221 GLN A CB  1 
ATOM   1803 C  CG  . GLN A 1 221 ? 3.443  -11.266 4.561   1.00 12.91  ? 221 GLN A CG  1 
ATOM   1804 C  CD  . GLN A 1 221 ? 2.329  -10.768 5.465   1.00 11.72  ? 221 GLN A CD  1 
ATOM   1805 O  OE1 . GLN A 1 221 ? 2.225  -11.121 6.632   1.00 12.06  ? 221 GLN A OE1 1 
ATOM   1806 N  NE2 . GLN A 1 221 ? 1.488  -9.900  4.897   1.00 13.38  ? 221 GLN A NE2 1 
ATOM   1807 N  N   . VAL A 1 222 ? 7.682  -12.491 5.885   1.00 12.08  ? 222 VAL A N   1 
ATOM   1808 C  CA  . VAL A 1 222 ? 9.006  -12.256 6.432   1.00 12.53  ? 222 VAL A CA  1 
ATOM   1809 C  C   . VAL A 1 222 ? 10.071 -12.729 5.413   1.00 13.04  ? 222 VAL A C   1 
ATOM   1810 O  O   . VAL A 1 222 ? 11.167 -12.159 5.336   1.00 13.03  ? 222 VAL A O   1 
ATOM   1811 C  CB  . VAL A 1 222 ? 9.164  -12.807 7.871   1.00 17.05  ? 222 VAL A CB  1 
ATOM   1812 C  CG1 . VAL A 1 222 ? 9.137  -14.310 7.915   1.00 17.92  ? 222 VAL A CG1 1 
ATOM   1813 C  CG2 . VAL A 1 222 ? 10.486 -12.374 8.510   1.00 18.34  ? 222 VAL A CG2 1 
ATOM   1814 N  N   . LEU A 1 223 ? 9.770  -13.785 4.600   1.00 13.95  ? 223 LEU A N   1 
ATOM   1815 C  CA  . LEU A 1 223 ? 10.733 -14.194 3.588   1.00 17.39  ? 223 LEU A CA  1 
ATOM   1816 C  C   . LEU A 1 223 ? 11.077 -13.022 2.722   1.00 13.75  ? 223 LEU A C   1 
ATOM   1817 O  O   . LEU A 1 223 ? 12.230 -12.879 2.272   1.00 15.43  ? 223 LEU A O   1 
ATOM   1818 C  CB  . LEU A 1 223 ? 10.070 -15.357 2.777   1.00 20.04  ? 223 LEU A CB  1 
ATOM   1819 C  CG  . LEU A 1 223 ? 10.950 -16.319 2.016   1.00 41.69  ? 223 LEU A CG  1 
ATOM   1820 C  CD1 . LEU A 1 223 ? 11.922 -16.937 3.011   1.00 39.94  ? 223 LEU A CD1 1 
ATOM   1821 C  CD2 . LEU A 1 223 ? 9.996  -17.385 1.509   1.00 54.31  ? 223 LEU A CD2 1 
ATOM   1822 N  N   . LYS A 1 224 ? 10.066 -12.229 2.404   1.00 13.66  ? 224 LYS A N   1 
ATOM   1823 C  CA  . LYS A 1 224 ? 10.305 -11.105 1.496   1.00 13.94  ? 224 LYS A CA  1 
ATOM   1824 C  C   . LYS A 1 224 ? 11.141 -10.000 2.148   1.00 11.22  ? 224 LYS A C   1 
ATOM   1825 O  O   . LYS A 1 224 ? 11.936 -9.389  1.467   1.00 12.84  ? 224 LYS A O   1 
ATOM   1826 C  CB  . LYS A 1 224 ? 8.970  -10.599 0.905   1.00 16.65  ? 224 LYS A CB  1 
ATOM   1827 C  CG  . LYS A 1 224 ? 8.412  -11.618 -0.130  1.00 22.28  ? 224 LYS A CG  1 
ATOM   1828 C  CD  . LYS A 1 224 ? 7.078  -11.361 -0.730  1.00 23.52  ? 224 LYS A CD  1 
ATOM   1829 C  CE  . LYS A 1 224 ? 6.560  -12.461 -1.648  1.00 32.67  ? 224 LYS A CE  1 
ATOM   1830 N  NZ  . LYS A 1 224 ? 5.434  -11.978 -2.492  1.00 28.11  ? 224 LYS A NZ  1 
ATOM   1831 N  N   . PHE A 1 225 ? 11.016 -9.786  3.472   1.00 10.90  ? 225 PHE A N   1 
ATOM   1832 C  CA  . PHE A 1 225 ? 11.994 -8.921  4.157   1.00 10.74  ? 225 PHE A CA  1 
ATOM   1833 C  C   . PHE A 1 225 ? 13.403 -9.380  3.907   1.00 11.60  ? 225 PHE A C   1 
ATOM   1834 O  O   . PHE A 1 225 ? 14.283 -8.584  3.660   1.00 11.77  ? 225 PHE A O   1 
ATOM   1835 C  CB  . PHE A 1 225 ? 11.781 -8.903  5.667   1.00 11.03  ? 225 PHE A CB  1 
ATOM   1836 C  CG  . PHE A 1 225 ? 10.583 -8.160  6.208   1.00 10.81  ? 225 PHE A CG  1 
ATOM   1837 C  CD1 . PHE A 1 225 ? 9.563  -7.748  5.366   1.00 12.23  ? 225 PHE A CD1 1 
ATOM   1838 C  CD2 . PHE A 1 225 ? 10.476 -7.872  7.559   1.00 12.02  ? 225 PHE A CD2 1 
ATOM   1839 C  CE1 . PHE A 1 225 ? 8.463  -7.066  5.862   1.00 14.37  ? 225 PHE A CE1 1 
ATOM   1840 C  CE2 . PHE A 1 225 ? 9.376  -7.189  8.055   1.00 15.03  ? 225 PHE A CE2 1 
ATOM   1841 C  CZ  . PHE A 1 225 ? 8.372  -6.788  7.206   1.00 12.71  ? 225 PHE A CZ  1 
ATOM   1842 N  N   . ARG A 1 226 ? 13.639 -10.689 3.978   1.00 11.22  ? 226 ARG A N   1 
ATOM   1843 C  CA  . ARG A 1 226 ? 14.976 -11.288 3.887   1.00 11.48  ? 226 ARG A CA  1 
ATOM   1844 C  C   . ARG A 1 226 ? 15.536 -11.291 2.458   1.00 11.15  ? 226 ARG A C   1 
ATOM   1845 O  O   . ARG A 1 226 ? 16.705 -11.655 2.309   1.00 13.98  ? 226 ARG A O   1 
ATOM   1846 C  CB  . ARG A 1 226 ? 14.884 -12.720 4.433   1.00 12.80  ? 226 ARG A CB  1 
ATOM   1847 C  CG  . ARG A 1 226 ? 14.456 -12.828 5.902   1.00 12.03  ? 226 ARG A CG  1 
ATOM   1848 C  CD  . ARG A 1 226 ? 14.522 -14.263 6.323   1.00 14.75  ? 226 ARG A CD  1 
ATOM   1849 N  NE  . ARG A 1 226 ? 14.018 -14.422 7.696   1.00 12.69  ? 226 ARG A NE  1 
ATOM   1850 C  CZ  . ARG A 1 226 ? 13.047 -15.306 8.019   1.00 12.88  ? 226 ARG A CZ  1 
ATOM   1851 N  NH1 . ARG A 1 226 ? 12.611 -16.169 7.091   1.00 16.95  ? 226 ARG A NH1 1 
ATOM   1852 N  NH2 . ARG A 1 226 ? 12.647 -15.343 9.255   1.00 13.83  ? 226 ARG A NH2 1 
ATOM   1853 N  N   . LYS A 1 227 ? 14.750 -10.848 1.456   1.00 12.56  ? 227 LYS A N   1 
ATOM   1854 C  CA  . LYS A 1 227 ? 15.284 -10.746 0.101   1.00 13.02  ? 227 LYS A CA  1 
ATOM   1855 C  C   . LYS A 1 227 ? 15.803 -9.340  -0.160  1.00 13.01  ? 227 LYS A C   1 
ATOM   1856 O  O   . LYS A 1 227 ? 16.420 -9.103  -1.193  1.00 14.07  ? 227 LYS A O   1 
ATOM   1857 C  CB  . LYS A 1 227 ? 14.141 -11.086 -0.864  1.00 16.07  ? 227 LYS A CB  1 
ATOM   1858 C  CG  . LYS A 1 227 ? 13.776 -12.549 -0.843  1.00 18.65  ? 227 LYS A CG  1 
ATOM   1859 C  CD  . LYS A 1 227 ? 12.679 -12.891 -1.896  1.00 28.96  ? 227 LYS A CD  1 
ATOM   1860 C  CE  . LYS A 1 227 ? 13.053 -12.659 -3.349  1.00 33.79  ? 227 LYS A CE  1 
ATOM   1861 N  NZ  . LYS A 1 227 ? 12.244 -13.448 -4.306  1.00 50.87  ? 227 LYS A NZ  1 
ATOM   1862 N  N   . LEU A 1 228 ? 15.610 -8.395  0.798   1.00 12.09  ? 228 LEU A N   1 
ATOM   1863 C  CA  . LEU A 1 228 ? 16.267 -7.112  0.662   1.00 10.58  ? 228 LEU A CA  1 
ATOM   1864 C  C   . LEU A 1 228 ? 17.765 -7.276  0.735   1.00 11.53  ? 228 LEU A C   1 
ATOM   1865 O  O   . LEU A 1 228 ? 18.304 -8.322  1.147   1.00 11.65  ? 228 LEU A O   1 
ATOM   1866 C  CB  . LEU A 1 228 ? 15.762 -6.165  1.753   1.00 11.21  ? 228 LEU A CB  1 
ATOM   1867 C  CG  . LEU A 1 228 ? 14.307 -5.716  1.598   1.00 11.56  ? 228 LEU A CG  1 
ATOM   1868 C  CD1 . LEU A 1 228 ? 13.896 -5.053  2.883   1.00 12.34  ? 228 LEU A CD1 1 
ATOM   1869 C  CD2 . LEU A 1 228 ? 14.196 -4.695  0.436   1.00 14.70  ? 228 LEU A CD2 1 
ATOM   1870 N  N   . ASN A 1 229 ? 18.479 -6.218  0.307   1.00 11.94  ? 229 ASN A N   1 
ATOM   1871 C  CA  . ASN A 1 229 ? 19.942 -6.276  0.289   1.00 11.12  ? 229 ASN A CA  1 
ATOM   1872 C  C   . ASN A 1 229 ? 20.528 -5.143  1.140   1.00 11.55  ? 229 ASN A C   1 
ATOM   1873 O  O   . ASN A 1 229 ? 20.059 -3.991  1.052   1.00 12.46  ? 229 ASN A O   1 
ATOM   1874 C  CB  . ASN A 1 229 ? 20.519 -6.062  -1.122  1.00 13.25  ? 229 ASN A CB  1 
ATOM   1875 C  CG  . ASN A 1 229 ? 20.371 -7.212  -2.078  1.00 15.03  ? 229 ASN A CG  1 
ATOM   1876 O  OD1 . ASN A 1 229 ? 20.888 -7.094  -3.200  1.00 17.08  ? 229 ASN A OD1 1 
ATOM   1877 N  ND2 . ASN A 1 229 ? 19.760 -8.323  -1.687  1.00 15.04  ? 229 ASN A ND2 1 
ATOM   1878 N  N   . PHE A 1 230 ? 21.623 -5.429  1.882   1.00 10.84  ? 230 PHE A N   1 
ATOM   1879 C  CA  . PHE A 1 230 ? 22.391 -4.376  2.545   1.00 10.49  ? 230 PHE A CA  1 
ATOM   1880 C  C   . PHE A 1 230 ? 23.181 -3.561  1.537   1.00 11.65  ? 230 PHE A C   1 
ATOM   1881 O  O   . PHE A 1 230 ? 23.436 -2.363  1.742   1.00 13.26  ? 230 PHE A O   1 
ATOM   1882 C  CB  . PHE A 1 230 ? 23.403 -4.985  3.508   1.00 11.37  ? 230 PHE A CB  1 
ATOM   1883 C  CG  . PHE A 1 230 ? 22.895 -5.600  4.789   1.00 10.97  ? 230 PHE A CG  1 
ATOM   1884 C  CD1 . PHE A 1 230 ? 22.169 -4.841  5.701   1.00 11.38  ? 230 PHE A CD1 1 
ATOM   1885 C  CD2 . PHE A 1 230 ? 23.235 -6.896  5.157   1.00 12.39  ? 230 PHE A CD2 1 
ATOM   1886 C  CE1 . PHE A 1 230 ? 21.745 -5.384  6.905   1.00 12.28  ? 230 PHE A CE1 1 
ATOM   1887 C  CE2 . PHE A 1 230 ? 22.835 -7.427  6.382   1.00 13.11  ? 230 PHE A CE2 1 
ATOM   1888 C  CZ  . PHE A 1 230 ? 22.077 -6.674  7.257   1.00 12.20  ? 230 PHE A CZ  1 
ATOM   1889 N  N   . ASN A 1 231 ? 23.651 -4.216  0.465   1.00 12.49  ? 231 ASN A N   1 
ATOM   1890 C  CA  . ASN A 1 231 ? 24.503 -3.582  -0.544  1.00 12.60  ? 231 ASN A CA  1 
ATOM   1891 C  C   . ASN A 1 231 ? 23.675 -2.684  -1.440  1.00 12.05  ? 231 ASN A C   1 
ATOM   1892 O  O   . ASN A 1 231 ? 22.472 -2.772  -1.580  1.00 12.66  ? 231 ASN A O   1 
ATOM   1893 C  CB  . ASN A 1 231 ? 25.148 -4.691  -1.403  1.00 13.70  ? 231 ASN A CB  1 
ATOM   1894 C  CG  . ASN A 1 231 ? 24.090 -5.600  -1.988  1.00 12.44  ? 231 ASN A CG  1 
ATOM   1895 O  OD1 . ASN A 1 231 ? 23.583 -6.478  -1.257  1.00 13.50  ? 231 ASN A OD1 1 
ATOM   1896 N  ND2 . ASN A 1 231 ? 23.656 -5.396  -3.240  1.00 14.20  ? 231 ASN A ND2 1 
ATOM   1897 N  N   . GLY A 1 232 ? 24.424 -1.748  -2.088  1.00 12.94  ? 232 GLY A N   1 
ATOM   1898 C  CA  . GLY A 1 232 ? 23.853 -0.979  -3.181  1.00 13.37  ? 232 GLY A CA  1 
ATOM   1899 C  C   . GLY A 1 232 ? 23.761 -1.753  -4.488  1.00 13.59  ? 232 GLY A C   1 
ATOM   1900 O  O   . GLY A 1 232 ? 24.373 -2.822  -4.647  1.00 14.75  ? 232 GLY A O   1 
ATOM   1901 N  N   . GLU A 1 233 ? 23.020 -1.178  -5.446  1.00 13.50  ? 233 GLU A N   1 
ATOM   1902 C  CA  . GLU A 1 233 ? 22.943 -1.752  -6.773  1.00 13.96  ? 233 GLU A CA  1 
ATOM   1903 C  C   . GLU A 1 233 ? 24.327 -1.855  -7.379  1.00 14.51  ? 233 GLU A C   1 
ATOM   1904 O  O   . GLU A 1 233 ? 25.160 -0.996  -7.186  1.00 14.25  ? 233 GLU A O   1 
ATOM   1905 C  CB  . GLU A 1 233 ? 22.068 -0.811  -7.617  1.00 15.73  ? 233 GLU A CB  1 
ATOM   1906 C  CG  . GLU A 1 233 ? 21.735 -1.394  -9.030  1.00 17.61  ? 233 GLU A CG  1 
ATOM   1907 C  CD  . GLU A 1 233 ? 20.902 -0.465  -9.866  1.00 24.91  ? 233 GLU A CD  1 
ATOM   1908 O  OE1 . GLU A 1 233 ? 20.718 0.719   -9.424  1.00 24.48  ? 233 GLU A OE1 1 
ATOM   1909 O  OE2 . GLU A 1 233 ? 20.516 -0.872  -10.981 1.00 27.17  ? 233 GLU A OE2 1 
ATOM   1910 N  N   . GLY A 1 234 ? 24.541 -2.967  -8.122  1.00 15.38  ? 234 GLY A N   1 
ATOM   1911 C  CA  . GLY A 1 234 ? 25.800 -3.153  -8.815  1.00 14.96  ? 234 GLY A CA  1 
ATOM   1912 C  C   . GLY A 1 234 ? 26.938 -3.506  -7.858  1.00 12.82  ? 234 GLY A C   1 
ATOM   1913 O  O   . GLY A 1 234 ? 28.090 -3.513  -8.325  1.00 14.74  ? 234 GLY A O   1 
ATOM   1914 N  N   . GLU A 1 235 ? 26.643 -3.919  -6.628  1.00 13.91  ? 235 GLU A N   1 
ATOM   1915 C  CA  . GLU A 1 235 ? 27.641 -4.408  -5.689  1.00 14.28  ? 235 GLU A CA  1 
ATOM   1916 C  C   . GLU A 1 235 ? 27.274 -5.860  -5.327  1.00 15.63  ? 235 GLU A C   1 
ATOM   1917 O  O   . GLU A 1 235 ? 26.120 -6.287  -5.508  1.00 14.54  ? 235 GLU A O   1 
ATOM   1918 C  CB  . GLU A 1 235 ? 27.576 -3.577  -4.378  1.00 15.77  ? 235 GLU A CB  1 
ATOM   1919 C  CG  . GLU A 1 235 ? 27.966 -2.090  -4.540  1.00 18.80  ? 235 GLU A CG  1 
ATOM   1920 C  CD  . GLU A 1 235 ? 27.770 -1.275  -3.270  1.00 27.97  ? 235 GLU A CD  1 
ATOM   1921 O  OE1 . GLU A 1 235 ? 27.210 -1.777  -2.234  1.00 21.74  ? 235 GLU A OE1 1 
ATOM   1922 O  OE2 . GLU A 1 235 ? 28.168 -0.131  -3.302  1.00 38.51  ? 235 GLU A OE2 1 
ATOM   1923 N  N   . PRO A 1 236 ? 28.233 -6.633  -4.778  1.00 14.04  ? 236 PRO A N   1 
ATOM   1924 C  CA  . PRO A 1 236 ? 27.963 -8.028  -4.420  1.00 15.28  ? 236 PRO A CA  1 
ATOM   1925 C  C   . PRO A 1 236 ? 26.819 -8.126  -3.428  1.00 12.68  ? 236 PRO A C   1 
ATOM   1926 O  O   . PRO A 1 236 ? 26.639 -7.292  -2.516  1.00 13.70  ? 236 PRO A O   1 
ATOM   1927 C  CB  . PRO A 1 236 ? 29.301 -8.523  -3.860  1.00 17.93  ? 236 PRO A CB  1 
ATOM   1928 C  CG  . PRO A 1 236 ? 30.327 -7.621  -4.498  1.00 19.47  ? 236 PRO A CG  1 
ATOM   1929 C  CD  . PRO A 1 236 ? 29.645 -6.284  -4.620  1.00 17.75  ? 236 PRO A CD  1 
ATOM   1930 N  N   . GLU A 1 237 ? 25.961 -9.129  -3.640  1.00 13.81  ? 237 GLU A N   1 
ATOM   1931 C  CA  . GLU A 1 237 ? 24.742 -9.236  -2.868  1.00 13.11  ? 237 GLU A CA  1 
ATOM   1932 C  C   . GLU A 1 237 ? 25.049 -9.685  -1.440  1.00 13.32  ? 237 GLU A C   1 
ATOM   1933 O  O   . GLU A 1 237 ? 25.629 -10.759 -1.218  1.00 15.09  ? 237 GLU A O   1 
ATOM   1934 C  CB  . GLU A 1 237 ? 23.801 -10.240 -3.544  1.00 16.92  ? 237 GLU A CB  1 
ATOM   1935 C  CG  . GLU A 1 237 ? 22.449 -10.277 -2.802  1.00 20.11  ? 237 GLU A CG  1 
ATOM   1936 C  CD  . GLU A 1 237 ? 21.287 -10.977 -3.494  1.00 21.69  ? 237 GLU A CD  1 
ATOM   1937 O  OE1 . GLU A 1 237 ? 21.535 -11.976 -4.198  1.00 43.84  ? 237 GLU A OE1 1 
ATOM   1938 O  OE2 . GLU A 1 237 ? 20.139 -10.520 -3.326  1.00 21.83  ? 237 GLU A OE2 1 
ATOM   1939 N  N   . GLU A 1 238 ? 24.526 -8.924  -0.461  1.00 12.90  ? 238 GLU A N   1 
ATOM   1940 C  CA  . GLU A 1 238 ? 24.580 -9.294  0.952   1.00 13.58  ? 238 GLU A CA  1 
ATOM   1941 C  C   . GLU A 1 238 ? 23.149 -9.214  1.456   1.00 11.75  ? 238 GLU A C   1 
ATOM   1942 O  O   . GLU A 1 238 ? 22.616 -8.117  1.535   1.00 13.75  ? 238 GLU A O   1 
ATOM   1943 C  CB  . GLU A 1 238 ? 25.322 -8.225  1.778   1.00 17.90  ? 238 GLU A CB  1 
ATOM   1944 C  CG  . GLU A 1 238 ? 26.770 -7.916  1.390   1.00 27.78  ? 238 GLU A CG  1 
ATOM   1945 C  CD  . GLU A 1 238 ? 27.429 -6.702  2.056   1.00 44.98  ? 238 GLU A CD  1 
ATOM   1946 O  OE1 . GLU A 1 238 ? 27.938 -6.835  3.217   1.00 55.65  ? 238 GLU A OE1 1 
ATOM   1947 O  OE2 . GLU A 1 238 ? 27.463 -5.611  1.410   1.00 55.07  ? 238 GLU A OE2 1 
ATOM   1948 N  N   . LEU A 1 239 ? 22.484 -10.365 1.758   1.00 11.78  ? 239 LEU A N   1 
ATOM   1949 C  CA  . LEU A 1 239 ? 21.080 -10.288 2.108   1.00 11.36  ? 239 LEU A CA  1 
ATOM   1950 C  C   . LEU A 1 239 ? 20.935 -9.518  3.416   1.00 10.16  ? 239 LEU A C   1 
ATOM   1951 O  O   . LEU A 1 239 ? 21.689 -9.676  4.365   1.00 11.28  ? 239 LEU A O   1 
ATOM   1952 C  CB  . LEU A 1 239 ? 20.557 -11.707 2.293   1.00 12.39  ? 239 LEU A CB  1 
ATOM   1953 C  CG  . LEU A 1 239 ? 20.551 -12.532 1.019   1.00 14.08  ? 239 LEU A CG  1 
ATOM   1954 C  CD1 . LEU A 1 239 ? 20.111 -13.923 1.384   1.00 19.33  ? 239 LEU A CD1 1 
ATOM   1955 C  CD2 . LEU A 1 239 ? 19.647 -11.911 -0.028  1.00 16.29  ? 239 LEU A CD2 1 
ATOM   1956 N  N   . MET A 1 240 ? 19.877 -8.709  3.453   1.00 9.91   ? 240 MET A N   1 
ATOM   1957 C  CA  . MET A 1 240 ? 19.566 -7.877  4.604   1.00 10.16  ? 240 MET A CA  1 
ATOM   1958 C  C   . MET A 1 240 ? 18.810 -8.757  5.602   1.00 9.84   ? 240 MET A C   1 
ATOM   1959 O  O   . MET A 1 240 ? 17.584 -8.942  5.496   1.00 10.23  ? 240 MET A O   1 
ATOM   1960 C  CB  . MET A 1 240 ? 18.688 -6.691  4.153   1.00 10.77  ? 240 MET A CB  1 
ATOM   1961 C  CG  . MET A 1 240 ? 18.416 -5.699  5.334   1.00 10.67  ? 240 MET A CG  1 
ATOM   1962 S  SD  . MET A 1 240 ? 17.462 -4.302  4.829   1.00 11.48  ? 240 MET A SD  1 
ATOM   1963 C  CE  . MET A 1 240 ? 18.765 -3.279  4.139   1.00 11.83  ? 240 MET A CE  1 
ATOM   1964 N  N   . VAL A 1 241 ? 19.569 -9.341  6.547   1.00 9.41   ? 241 VAL A N   1 
ATOM   1965 C  CA  . VAL A 1 241 ? 18.995 -10.188 7.615   1.00 9.69   ? 241 VAL A CA  1 
ATOM   1966 C  C   . VAL A 1 241 ? 19.794 -9.902  8.859   1.00 8.98   ? 241 VAL A C   1 
ATOM   1967 O  O   . VAL A 1 241 ? 20.971 -9.498  8.781   1.00 10.42  ? 241 VAL A O   1 
ATOM   1968 C  CB  . VAL A 1 241 ? 19.095 -11.691 7.275   1.00 10.33  ? 241 VAL A CB  1 
ATOM   1969 C  CG1 . VAL A 1 241 ? 18.176 -12.058 6.092   1.00 13.19  ? 241 VAL A CG1 1 
ATOM   1970 C  CG2 . VAL A 1 241 ? 20.553 -12.176 7.030   1.00 12.06  ? 241 VAL A CG2 1 
ATOM   1971 N  N   . ASP A 1 242 ? 19.183 -10.134 10.038  1.00 9.37   ? 242 ASP A N   1 
ATOM   1972 C  CA  . ASP A 1 242 ? 19.899 -9.992  11.305  1.00 9.14   ? 242 ASP A CA  1 
ATOM   1973 C  C   . ASP A 1 242 ? 20.400 -8.577  11.533  1.00 8.53   ? 242 ASP A C   1 
ATOM   1974 O  O   . ASP A 1 242 ? 21.520 -8.385  11.946  1.00 11.45  ? 242 ASP A O   1 
ATOM   1975 C  CB  . ASP A 1 242 ? 20.979 -11.089 11.526  1.00 11.14  ? 242 ASP A CB  1 
ATOM   1976 C  CG  . ASP A 1 242 ? 20.377 -12.473 11.618  1.00 10.09  ? 242 ASP A CG  1 
ATOM   1977 O  OD1 . ASP A 1 242 ? 19.338 -12.618 12.302  1.00 10.11  ? 242 ASP A OD1 1 
ATOM   1978 O  OD2 . ASP A 1 242 ? 20.933 -13.389 10.985  1.00 13.27  ? 242 ASP A OD2 1 
ATOM   1979 N  N   . ASN A 1 243 ? 19.472 -7.639  11.316  1.00 8.55   ? 243 ASN A N   1 
ATOM   1980 C  CA  . ASN A 1 243 ? 19.757 -6.204  11.535  1.00 8.16   ? 243 ASN A CA  1 
ATOM   1981 C  C   . ASN A 1 243 ? 19.203 -5.757  12.874  1.00 7.82   ? 243 ASN A C   1 
ATOM   1982 O  O   . ASN A 1 243 ? 18.527 -4.722  12.998  1.00 10.21  ? 243 ASN A O   1 
ATOM   1983 C  CB  . ASN A 1 243 ? 19.235 -5.385  10.352  1.00 9.35   ? 243 ASN A CB  1 
ATOM   1984 C  CG  . ASN A 1 243 ? 17.778 -5.671  10.045  1.00 8.48   ? 243 ASN A CG  1 
ATOM   1985 O  OD1 . ASN A 1 243 ? 17.110 -6.375  10.786  1.00 9.92   ? 243 ASN A OD1 1 
ATOM   1986 N  ND2 . ASN A 1 243 ? 17.297 -5.081  8.969   1.00 9.90   ? 243 ASN A ND2 1 
ATOM   1987 N  N   . TRP A 1 244 ? 19.451 -6.541  13.928  1.00 8.27   ? 244 TRP A N   1 
ATOM   1988 C  CA  . TRP A 1 244 ? 19.012 -6.292  15.273  1.00 7.84   ? 244 TRP A CA  1 
ATOM   1989 C  C   . TRP A 1 244 ? 20.217 -6.173  16.184  1.00 8.30   ? 244 TRP A C   1 
ATOM   1990 O  O   . TRP A 1 244 ? 21.207 -6.865  16.016  1.00 9.72   ? 244 TRP A O   1 
ATOM   1991 C  CB  . TRP A 1 244 ? 18.060 -7.392  15.780  1.00 8.51   ? 244 TRP A CB  1 
ATOM   1992 C  CG  . TRP A 1 244 ? 18.537 -8.809  15.569  1.00 8.32   ? 244 TRP A CG  1 
ATOM   1993 C  CD1 . TRP A 1 244 ? 18.424 -9.539  14.407  1.00 8.36   ? 244 TRP A CD1 1 
ATOM   1994 C  CD2 . TRP A 1 244 ? 19.147 -9.668  16.546  1.00 9.19   ? 244 TRP A CD2 1 
ATOM   1995 N  NE1 . TRP A 1 244 ? 18.946 -10.809 14.602  1.00 8.99   ? 244 TRP A NE1 1 
ATOM   1996 C  CE2 . TRP A 1 244 ? 19.402 -10.912 15.893  1.00 9.34   ? 244 TRP A CE2 1 
ATOM   1997 C  CE3 . TRP A 1 244 ? 19.470 -9.517  17.912  1.00 10.01  ? 244 TRP A CE3 1 
ATOM   1998 C  CZ2 . TRP A 1 244 ? 19.995 -11.978 16.559  1.00 10.46  ? 244 TRP A CZ2 1 
ATOM   1999 C  CZ3 . TRP A 1 244 ? 20.024 -10.609 18.586  1.00 11.99  ? 244 TRP A CZ3 1 
ATOM   2000 C  CH2 . TRP A 1 244 ? 20.257 -11.815 17.896  1.00 10.87  ? 244 TRP A CH2 1 
ATOM   2001 N  N   . ARG A 1 245 ? 20.095 -5.292  17.160  1.00 8.43   ? 245 ARG A N   1 
ATOM   2002 C  CA  . ARG A 1 245 ? 21.062 -5.176  18.240  1.00 8.79   ? 245 ARG A CA  1 
ATOM   2003 C  C   . ARG A 1 245 ? 20.648 -6.107  19.367  1.00 9.21   ? 245 ARG A C   1 
ATOM   2004 O  O   . ARG A 1 245 ? 19.492 -6.135  19.729  1.00 10.34  ? 245 ARG A O   1 
ATOM   2005 C  CB  . ARG A 1 245 ? 21.152 -3.722  18.733  1.00 8.95   ? 245 ARG A CB  1 
ATOM   2006 C  CG  . ARG A 1 245 ? 22.263 -3.520  19.761  1.00 9.46   ? 245 ARG A CG  1 
ATOM   2007 C  CD  . ARG A 1 245 ? 22.229 -2.134  20.382  1.00 9.90   ? 245 ARG A CD  1 
ATOM   2008 N  NE  . ARG A 1 245 ? 23.435 -1.862  21.112  1.00 10.33  ? 245 ARG A NE  1 
ATOM   2009 C  CZ  . ARG A 1 245 ? 23.647 -0.832  21.936  1.00 10.57  ? 245 ARG A CZ  1 
ATOM   2010 N  NH1 . ARG A 1 245 ? 22.627 -0.062  22.299  1.00 12.39  ? 245 ARG A NH1 1 
ATOM   2011 N  NH2 . ARG A 1 245 ? 24.871 -0.612  22.430  1.00 12.04  ? 245 ARG A NH2 1 
ATOM   2012 N  N   . PRO A 1 246 ? 21.556 -6.889  19.956  1.00 9.87   ? 246 PRO A N   1 
ATOM   2013 C  CA  . PRO A 1 246 ? 21.173 -7.746  21.074  1.00 10.33  ? 246 PRO A CA  1 
ATOM   2014 C  C   . PRO A 1 246 ? 20.820 -6.940  22.333  1.00 10.28  ? 246 PRO A C   1 
ATOM   2015 O  O   . PRO A 1 246 ? 21.173 -5.744  22.480  1.00 10.69  ? 246 PRO A O   1 
ATOM   2016 C  CB  . PRO A 1 246 ? 22.389 -8.626  21.340  1.00 13.80  ? 246 PRO A CB  1 
ATOM   2017 C  CG  . PRO A 1 246 ? 23.321 -8.398  20.210  1.00 20.31  ? 246 PRO A CG  1 
ATOM   2018 C  CD  . PRO A 1 246 ? 22.954 -7.115  19.509  1.00 12.80  ? 246 PRO A CD  1 
ATOM   2019 N  N   . ALA A 1 247 ? 20.171 -7.619  23.300  1.00 10.24  ? 247 ALA A N   1 
ATOM   2020 C  CA  . ALA A 1 247 ? 19.823 -6.998  24.558  1.00 10.41  ? 247 ALA A CA  1 
ATOM   2021 C  C   . ALA A 1 247 ? 21.043 -6.482  25.275  1.00 10.00  ? 247 ALA A C   1 
ATOM   2022 O  O   . ALA A 1 247 ? 22.091 -7.176  25.333  1.00 12.04  ? 247 ALA A O   1 
ATOM   2023 C  CB  . ALA A 1 247 ? 19.058 -8.007  25.396  1.00 13.41  ? 247 ALA A CB  1 
ATOM   2024 N  N   . GLN A 1 248 ? 20.879 -5.326  25.919  1.00 10.00  ? 248 GLN A N   1 
ATOM   2025 C  CA  . GLN A 1 248 ? 21.935 -4.612  26.636  1.00 9.80   ? 248 GLN A CA  1 
ATOM   2026 C  C   . GLN A 1 248 ? 21.635 -4.675  28.121  1.00 10.39  ? 248 GLN A C   1 
ATOM   2027 O  O   . GLN A 1 248 ? 20.461 -4.870  28.515  1.00 11.75  ? 248 GLN A O   1 
ATOM   2028 C  CB  . GLN A 1 248 ? 21.984 -3.182  26.142  1.00 11.62  ? 248 GLN A CB  1 
ATOM   2029 C  CG  . GLN A 1 248 ? 22.307 -3.094  24.638  1.00 10.91  ? 248 GLN A CG  1 
ATOM   2030 C  CD  . GLN A 1 248 ? 23.648 -3.750  24.317  1.00 11.82  ? 248 GLN A CD  1 
ATOM   2031 O  OE1 . GLN A 1 248 ? 24.671 -3.492  24.953  1.00 15.34  ? 248 GLN A OE1 1 
ATOM   2032 N  NE2 . GLN A 1 248 ? 23.627 -4.667  23.364  1.00 13.05  ? 248 GLN A NE2 1 
ATOM   2033 N  N   . PRO A 1 249 ? 22.623 -4.420  28.985  1.00 13.07  ? 249 PRO A N   1 
ATOM   2034 C  CA  . PRO A 1 249 ? 22.372 -4.486  30.425  1.00 14.50  ? 249 PRO A CA  1 
ATOM   2035 C  C   . PRO A 1 249 ? 21.309 -3.495  30.877  1.00 12.70  ? 249 PRO A C   1 
ATOM   2036 O  O   . PRO A 1 249 ? 21.379 -2.284  30.560  1.00 12.82  ? 249 PRO A O   1 
ATOM   2037 C  CB  . PRO A 1 249 ? 23.777 -4.087  30.969  1.00 18.76  ? 249 PRO A CB  1 
ATOM   2038 C  CG  . PRO A 1 249 ? 24.780 -4.463  29.950  1.00 19.08  ? 249 PRO A CG  1 
ATOM   2039 C  CD  . PRO A 1 249 ? 24.044 -4.171  28.638  1.00 15.27  ? 249 PRO A CD  1 
ATOM   2040 N  N   . LEU A 1 250 ? 20.421 -3.922  31.756  1.00 13.22  ? 250 LEU A N   1 
ATOM   2041 C  CA  . LEU A 1 250 ? 19.379 -3.041  32.232  1.00 12.35  ? 250 LEU A CA  1 
ATOM   2042 C  C   . LEU A 1 250 ? 19.918 -2.000  33.230  1.00 11.80  ? 250 LEU A C   1 
ATOM   2043 O  O   . LEU A 1 250 ? 19.390 -0.887  33.319  1.00 12.64  ? 250 LEU A O   1 
ATOM   2044 C  CB  . LEU A 1 250 ? 18.321 -3.916  32.937  1.00 15.30  ? 250 LEU A CB  1 
ATOM   2045 C  CG  . LEU A 1 250 ? 17.041 -3.206  33.377  1.00 15.01  ? 250 LEU A CG  1 
ATOM   2046 C  CD1 . LEU A 1 250 ? 16.320 -2.625  32.147  1.00 15.14  ? 250 LEU A CD1 1 
ATOM   2047 C  CD2 . LEU A 1 250 ? 16.108 -4.160  34.159  1.00 17.91  ? 250 LEU A CD2 1 
ATOM   2048 N  N   . LYS A 1 251 ? 21.008 -2.308  33.918  1.00 14.10  ? 251 LYS A N   1 
ATOM   2049 C  CA  . LYS A 1 251 ? 21.647 -1.348  34.833  1.00 16.81  ? 251 LYS A CA  1 
ATOM   2050 C  C   . LYS A 1 251 ? 20.611 -0.925  35.870  1.00 18.45  ? 251 LYS A C   1 
ATOM   2051 O  O   . LYS A 1 251 ? 19.907 -1.768  36.408  1.00 24.07  ? 251 LYS A O   1 
ATOM   2052 C  CB  . LYS A 1 251 ? 22.432 -0.272  34.064  1.00 17.47  ? 251 LYS A CB  1 
ATOM   2053 C  CG  . LYS A 1 251 ? 23.571 -0.950  33.303  1.00 25.12  ? 251 LYS A CG  1 
ATOM   2054 C  CD  . LYS A 1 251 ? 24.630 -0.079  32.784  1.00 27.93  ? 251 LYS A CD  1 
ATOM   2055 C  CE  . LYS A 1 251 ? 25.905 -0.826  32.519  1.00 29.05  ? 251 LYS A CE  1 
ATOM   2056 N  NZ  . LYS A 1 251 ? 26.619 -0.053  31.466  1.00 31.80  ? 251 LYS A NZ  1 
ATOM   2057 N  N   A ASN A 1 252 ? 20.467 0.316   36.274  0.50 20.23  ? 252 ASN A N   1 
ATOM   2058 N  N   B ASN A 1 252 ? 20.547 0.396   36.011  0.50 14.94  ? 252 ASN A N   1 
ATOM   2059 C  CA  A ASN A 1 252 ? 19.577 0.357   37.447  0.50 25.79  ? 252 ASN A CA  1 
ATOM   2060 C  CA  B ASN A 1 252 ? 19.745 1.026   37.040  0.50 16.61  ? 252 ASN A CA  1 
ATOM   2061 C  C   A ASN A 1 252 ? 18.093 0.557   37.060  0.50 22.33  ? 252 ASN A C   1 
ATOM   2062 C  C   B ASN A 1 252 ? 18.446 1.537   36.445  0.50 15.90  ? 252 ASN A C   1 
ATOM   2063 O  O   A ASN A 1 252 ? 17.297 1.053   37.854  0.50 25.58  ? 252 ASN A O   1 
ATOM   2064 O  O   B ASN A 1 252 ? 18.165 2.736   36.525  0.50 20.98  ? 252 ASN A O   1 
ATOM   2065 C  CB  A ASN A 1 252 ? 20.163 1.195   38.608  0.50 33.52  ? 252 ASN A CB  1 
ATOM   2066 C  CB  B ASN A 1 252 ? 20.484 2.182   37.714  0.50 17.31  ? 252 ASN A CB  1 
ATOM   2067 C  CG  A ASN A 1 252 ? 21.236 0.541   39.478  0.50 35.22  ? 252 ASN A CG  1 
ATOM   2068 C  CG  B ASN A 1 252 ? 19.728 2.636   38.944  0.50 22.92  ? 252 ASN A CG  1 
ATOM   2069 O  OD1 A ASN A 1 252 ? 21.827 1.209   40.336  0.50 48.90  ? 252 ASN A OD1 1 
ATOM   2070 O  OD1 B ASN A 1 252 ? 19.279 1.805   39.734  0.50 26.89  ? 252 ASN A OD1 1 
ATOM   2071 N  ND2 A ASN A 1 252 ? 21.466 -0.761  39.333  0.50 35.95  ? 252 ASN A ND2 1 
ATOM   2072 N  ND2 B ASN A 1 252 ? 19.530 3.939   39.070  0.50 21.78  ? 252 ASN A ND2 1 
ATOM   2073 N  N   A ARG A 1 253 ? 17.707 0.183   35.825  0.50 14.00  ? 253 ARG A N   1 
ATOM   2074 N  N   B ARG A 1 253 ? 17.683 0.589   35.879  0.50 13.48  ? 253 ARG A N   1 
ATOM   2075 C  CA  A ARG A 1 253 ? 16.429 0.683   35.335  0.50 12.95  ? 253 ARG A CA  1 
ATOM   2076 C  CA  B ARG A 1 253 ? 16.365 0.903   35.367  0.50 12.28  ? 253 ARG A CA  1 
ATOM   2077 C  C   A ARG A 1 253 ? 15.280 -0.211  35.768  0.50 14.83  ? 253 ARG A C   1 
ATOM   2078 C  C   B ARG A 1 253 ? 15.339 -0.114  35.838  0.50 14.33  ? 253 ARG A C   1 
ATOM   2079 O  O   A ARG A 1 253 ? 15.431 -1.403  35.949  0.50 18.57  ? 253 ARG A O   1 
ATOM   2080 O  O   B ARG A 1 253 ? 15.659 -1.276  36.106  0.50 17.16  ? 253 ARG A O   1 
ATOM   2081 C  CB  A ARG A 1 253 ? 16.429 0.832   33.807  0.50 11.95  ? 253 ARG A CB  1 
ATOM   2082 C  CB  B ARG A 1 253 ? 16.424 0.918   33.835  0.50 11.17  ? 253 ARG A CB  1 
ATOM   2083 C  CG  A ARG A 1 253 ? 17.309 1.983   33.317  0.50 12.57  ? 253 ARG A CG  1 
ATOM   2084 C  CG  B ARG A 1 253 ? 17.366 2.003   33.306  0.50 11.04  ? 253 ARG A CG  1 
ATOM   2085 C  CD  A ARG A 1 253 ? 17.401 1.968   31.816  0.50 12.20  ? 253 ARG A CD  1 
ATOM   2086 C  CD  B ARG A 1 253 ? 17.435 1.995   31.808  0.50 10.49  ? 253 ARG A CD  1 
ATOM   2087 N  NE  A ARG A 1 253 ? 18.239 0.858   31.352  0.50 10.70  ? 253 ARG A NE  1 
ATOM   2088 N  NE  B ARG A 1 253 ? 18.253 0.869   31.349  0.50 9.95   ? 253 ARG A NE  1 
ATOM   2089 C  CZ  A ARG A 1 253 ? 18.492 0.594   30.069  0.50 8.82   ? 253 ARG A CZ  1 
ATOM   2090 C  CZ  B ARG A 1 253 ? 18.493 0.595   30.067  0.50 8.45   ? 253 ARG A CZ  1 
ATOM   2091 N  NH1 A ARG A 1 253 ? 17.884 1.297   29.102  0.50 9.06   ? 253 ARG A NH1 1 
ATOM   2092 N  NH1 B ARG A 1 253 ? 17.887 1.299   29.100  0.50 8.87   ? 253 ARG A NH1 1 
ATOM   2093 N  NH2 A ARG A 1 253 ? 19.343 -0.381  29.748  0.50 10.04  ? 253 ARG A NH2 1 
ATOM   2094 N  NH2 B ARG A 1 253 ? 19.333 -0.390  29.746  0.50 9.68   ? 253 ARG A NH2 1 
ATOM   2095 N  N   . GLN A 1 254 ? 14.085 0.353   35.860  1.00 14.43  ? 254 GLN A N   1 
ATOM   2096 C  CA  . GLN A 1 254 ? 12.909 -0.442  36.150  1.00 17.00  ? 254 GLN A CA  1 
ATOM   2097 C  C   . GLN A 1 254 ? 12.029 -0.423  34.929  1.00 15.06  ? 254 GLN A C   1 
ATOM   2098 O  O   . GLN A 1 254 ? 11.845 0.642   34.297  1.00 19.56  ? 254 GLN A O   1 
ATOM   2099 C  CB  . GLN A 1 254 ? 12.147 0.211   37.297  1.00 20.77  ? 254 GLN A CB  1 
ATOM   2100 C  CG  . GLN A 1 254 ? 12.846 -0.092  38.591  1.00 28.26  ? 254 GLN A CG  1 
ATOM   2101 N  N   . ILE A 1 255 ? 11.548 -1.583  34.514  1.00 13.31  ? 255 ILE A N   1 
ATOM   2102 C  CA  . ILE A 1 255 ? 10.555 -1.657  33.455  1.00 12.65  ? 255 ILE A CA  1 
ATOM   2103 C  C   . ILE A 1 255 ? 9.196  -1.643  34.133  1.00 11.61  ? 255 ILE A C   1 
ATOM   2104 O  O   . ILE A 1 255 ? 8.959  -2.389  35.088  1.00 14.08  ? 255 ILE A O   1 
ATOM   2105 C  CB  . ILE A 1 255 ? 10.770 -2.943  32.642  1.00 12.31  ? 255 ILE A CB  1 
ATOM   2106 C  CG1 . ILE A 1 255 ? 12.210 -2.925  32.063  1.00 13.53  ? 255 ILE A CG1 1 
ATOM   2107 C  CG2 . ILE A 1 255 ? 9.664  -2.995  31.566  1.00 13.72  ? 255 ILE A CG2 1 
ATOM   2108 C  CD1 . ILE A 1 255 ? 12.482 -4.095  31.148  1.00 16.42  ? 255 ILE A CD1 1 
ATOM   2109 N  N   . LYS A 1 256 ? 8.288  -0.785  33.649  1.00 12.12  ? 256 LYS A N   1 
ATOM   2110 C  CA  . LYS A 1 256 ? 6.944  -0.703  34.201  1.00 11.72  ? 256 LYS A CA  1 
ATOM   2111 C  C   . LYS A 1 256 ? 5.975  -1.324  33.228  1.00 11.15  ? 256 LYS A C   1 
ATOM   2112 O  O   . LYS A 1 256 ? 6.142  -1.273  32.011  1.00 13.23  ? 256 LYS A O   1 
ATOM   2113 C  CB  . LYS A 1 256 ? 6.602  0.787   34.426  1.00 14.69  ? 256 LYS A CB  1 
ATOM   2114 C  CG  . LYS A 1 256 ? 7.503  1.487   35.471  1.00 19.60  ? 256 LYS A CG  1 
ATOM   2115 N  N   . ALA A 1 257 ? 4.958  -1.964  33.779  1.00 12.19  ? 257 ALA A N   1 
ATOM   2116 C  CA  . ALA A 1 257 ? 3.881  -2.560  32.990  1.00 12.47  ? 257 ALA A CA  1 
ATOM   2117 C  C   . ALA A 1 257 ? 2.599  -1.765  33.130  1.00 11.18  ? 257 ALA A C   1 
ATOM   2118 O  O   . ALA A 1 257 ? 2.293  -1.274  34.233  1.00 13.57  ? 257 ALA A O   1 
ATOM   2119 C  CB  . ALA A 1 257 ? 3.644  -4.001  33.432  1.00 14.08  ? 257 ALA A CB  1 
ATOM   2120 N  N   . SER A 1 258 ? 1.871  -1.638  32.048  1.00 11.86  ? 258 SER A N   1 
ATOM   2121 C  CA  . SER A 1 258 ? 0.600  -0.899  32.049  1.00 14.31  ? 258 SER A CA  1 
ATOM   2122 C  C   . SER A 1 258 ? -0.580 -1.755  32.520  1.00 14.32  ? 258 SER A C   1 
ATOM   2123 O  O   . SER A 1 258 ? -1.685 -1.225  32.638  1.00 19.31  ? 258 SER A O   1 
ATOM   2124 C  CB  . SER A 1 258 ? 0.290  -0.352  30.660  1.00 14.29  ? 258 SER A CB  1 
ATOM   2125 O  OG  . SER A 1 258 ? -0.146 -1.446  29.837  1.00 13.10  ? 258 SER A OG  1 
ATOM   2126 N  N   . PHE A 1 259 ? -0.319 -3.064  32.784  1.00 15.59  ? 259 PHE A N   1 
ATOM   2127 C  CA  . PHE A 1 259 ? -1.358 -4.075  33.011  1.00 18.88  ? 259 PHE A CA  1 
ATOM   2128 C  C   . PHE A 1 259 ? -0.969 -4.997  34.189  1.00 28.77  ? 259 PHE A C   1 
ATOM   2129 O  O   . PHE A 1 259 ? 0.093  -4.740  34.797  1.00 30.20  ? 259 PHE A O   1 
ATOM   2130 C  CB  . PHE A 1 259 ? -1.554 -4.891  31.727  1.00 19.05  ? 259 PHE A CB  1 
ATOM   2131 C  CG  . PHE A 1 259 ? -0.258 -5.575  31.312  1.00 17.10  ? 259 PHE A CG  1 
ATOM   2132 C  CD1 . PHE A 1 259 ? 0.705  -4.958  30.543  1.00 13.97  ? 259 PHE A CD1 1 
ATOM   2133 C  CD2 . PHE A 1 259 ? 0.018  -6.884  31.737  1.00 20.80  ? 259 PHE A CD2 1 
ATOM   2134 C  CE1 . PHE A 1 259 ? 1.897  -5.591  30.245  1.00 17.03  ? 259 PHE A CE1 1 
ATOM   2135 C  CE2 . PHE A 1 259 ? 1.188  -7.552  31.392  1.00 22.41  ? 259 PHE A CE2 1 
ATOM   2136 C  CZ  . PHE A 1 259 ? 2.146  -6.894  30.648  1.00 20.67  ? 259 PHE A CZ  1 
ATOM   2137 N  N   . LYS A 1 260 ? -1.842 -5.973  34.520  1.00 64.21  ? 260 LYS A N   1 
ATOM   2138 C  CA  . LYS A 1 260 ? -1.697 -7.078  35.534  1.00 56.66  ? 260 LYS A CA  1 
ATOM   2139 C  C   . LYS A 1 260 ? -1.997 -6.705  37.003  1.00 77.48  ? 260 LYS A C   1 
ATOM   2140 O  O   . LYS A 1 260 ? -1.475 -7.417  37.900  1.00 87.15  ? 260 LYS A O   1 
ATOM   2141 C  CB  . LYS A 1 260 ? -0.383 -7.855  35.374  1.00 77.93  ? 260 LYS A CB  1 
ATOM   2142 O  OXT . LYS A 1 260 ? -2.771 -5.759  37.240  1.00 62.07  ? 260 LYS A OXT 1 
HETATM 2143 ZN ZN  . ZN  B 2 .   ? 14.451 0.290   15.387  1.00 8.02   ? 301 ZN  A ZN  1 
HETATM 2144 S  S   . DMS C 3 .   ? 22.552 -9.704  14.891  1.00 21.95  ? 302 DMS A S   1 
HETATM 2145 O  O   . DMS C 3 .   ? 23.188 -10.994 14.463  1.00 28.50  ? 302 DMS A O   1 
HETATM 2146 C  C1  . DMS C 3 .   ? 22.787 -9.542  16.612  1.00 18.61  ? 302 DMS A C1  1 
HETATM 2147 C  C2  . DMS C 3 .   ? 23.731 -8.464  14.543  1.00 27.30  ? 302 DMS A C2  1 
HETATM 2148 F  F18 . V90 D 4 .   ? 16.328 4.856   11.177  1.00 15.60  ? 303 V90 A F18 1 
HETATM 2149 C  C5  . V90 D 4 .   ? 16.765 3.966   12.109  1.00 12.49  ? 303 V90 A C5  1 
HETATM 2150 C  C6  . V90 D 4 .   ? 17.640 3.012   11.675  1.00 12.22  ? 303 V90 A C6  1 
HETATM 2151 S  S12 . V90 D 4 .   ? 18.356 3.015   10.033  1.00 15.70  ? 303 V90 A S12 1 
HETATM 2152 C  C13 . V90 D 4 .   ? 19.974 3.642   10.458  1.00 20.58  ? 303 V90 A C13 1 
HETATM 2153 C  C14 . V90 D 4 .   ? 19.917 5.122   10.927  1.00 33.35  ? 303 V90 A C14 1 
HETATM 2154 O  O15 . V90 D 4 .   ? 19.661 5.972   9.852   1.00 46.27  ? 303 V90 A O15 1 
HETATM 2155 C  C1  . V90 D 4 .   ? 18.013 2.082   12.584  1.00 11.91  ? 303 V90 A C1  1 
HETATM 2156 F  F17 . V90 D 4 .   ? 18.912 1.116   12.279  1.00 13.88  ? 303 V90 A F17 1 
HETATM 2157 C  C4  . V90 D 4 .   ? 16.230 4.043   13.393  1.00 11.61  ? 303 V90 A C4  1 
HETATM 2158 C  C3  . V90 D 4 .   ? 16.602 3.013   14.308  1.00 10.69  ? 303 V90 A C3  1 
HETATM 2159 S  S8  . V90 D 4 .   ? 16.010 2.932   15.999  1.00 9.89   ? 303 V90 A S8  1 
HETATM 2160 O  O10 . V90 D 4 .   ? 14.804 3.709   16.017  1.00 9.63   ? 303 V90 A O10 1 
HETATM 2161 N  N11 . V90 D 4 .   ? 15.731 1.402   16.317  1.00 8.17   ? 303 V90 A N11 1 
HETATM 2162 O  O9  . V90 D 4 .   ? 17.122 3.425   16.812  1.00 10.15  ? 303 V90 A O9  1 
HETATM 2163 C  C2  . V90 D 4 .   ? 17.486 2.113   13.849  1.00 10.74  ? 303 V90 A C2  1 
HETATM 2164 F  F16 . V90 D 4 .   ? 17.917 1.124   14.714  1.00 12.44  ? 303 V90 A F16 1 
HETATM 2165 N  N7  . V90 D 4 .   ? 15.328 5.099   13.732  1.00 13.11  ? 303 V90 A N7  1 
HETATM 2166 C  C19 . V90 D 4 .   ? 15.586 6.420   13.283  1.00 15.65  ? 303 V90 A C19 1 
HETATM 2167 C  C26 . V90 D 4 .   ? 14.366 7.230   13.784  1.00 19.01  ? 303 V90 A C26 1 
HETATM 2168 C  C25 . V90 D 4 .   ? 14.173 8.654   13.133  1.00 21.68  ? 303 V90 A C25 1 
HETATM 2169 C  C24 . V90 D 4 .   ? 14.957 9.766   13.731  1.00 30.72  ? 303 V90 A C24 1 
HETATM 2170 C  C23 . V90 D 4 .   ? 15.667 9.485   15.012  1.00 27.77  ? 303 V90 A C23 1 
HETATM 2171 C  C22 . V90 D 4 .   ? 17.094 9.007   14.773  1.00 28.69  ? 303 V90 A C22 1 
HETATM 2172 C  C21 . V90 D 4 .   ? 17.270 7.444   14.871  1.00 30.09  ? 303 V90 A C21 1 
HETATM 2173 C  C20 . V90 D 4 .   ? 16.949 6.831   13.572  1.00 20.76  ? 303 V90 A C20 1 
HETATM 2174 O  O   . HOH E 5 .   ? 19.743 4.359   14.910  1.00 30.25  ? 401 HOH A O   1 
HETATM 2175 O  O   . HOH E 5 .   ? 8.755  20.356  29.232  1.00 42.03  ? 402 HOH A O   1 
HETATM 2176 O  O   . HOH E 5 .   ? -4.838 8.372   27.254  1.00 49.16  ? 403 HOH A O   1 
HETATM 2177 O  O   . HOH E 5 .   ? -1.181 3.789   30.011  1.00 34.10  ? 404 HOH A O   1 
HETATM 2178 O  O   . HOH E 5 .   ? 7.299  -3.242  -6.192  1.00 38.98  ? 405 HOH A O   1 
HETATM 2179 O  O   . HOH E 5 .   ? 3.440  20.877  6.121   1.00 17.43  ? 406 HOH A O   1 
HETATM 2180 O  O   . HOH E 5 .   ? 0.247  -5.402  -1.832  1.00 38.34  ? 407 HOH A O   1 
HETATM 2181 O  O   . HOH E 5 .   ? -4.207 0.747   35.222  1.00 44.72  ? 408 HOH A O   1 
HETATM 2182 O  O   . HOH E 5 .   ? -1.427 -12.675 11.136  1.00 18.51  ? 409 HOH A O   1 
HETATM 2183 O  O   . HOH E 5 .   ? -6.965 8.070   15.633  1.00 45.10  ? 410 HOH A O   1 
HETATM 2184 O  O   . HOH E 5 .   ? 16.391 3.928   37.565  1.00 31.97  ? 411 HOH A O   1 
HETATM 2185 O  O   . HOH E 5 .   ? -5.789 -10.694 20.003  1.00 50.25  ? 412 HOH A O   1 
HETATM 2186 O  O   . HOH E 5 .   ? 22.888 4.821   12.307  1.00 35.10  ? 413 HOH A O   1 
HETATM 2187 O  O   . HOH E 5 .   ? 6.000  21.203  13.248  1.00 26.03  ? 414 HOH A O   1 
HETATM 2188 O  O   . HOH E 5 .   ? 19.027 10.407  29.371  1.00 33.41  ? 415 HOH A O   1 
HETATM 2189 O  O   . HOH E 5 .   ? 1.007  10.458  30.169  1.00 32.72  ? 416 HOH A O   1 
HETATM 2190 O  O   . HOH E 5 .   ? 5.945  -8.493  37.578  1.00 24.95  ? 417 HOH A O   1 
HETATM 2191 O  O   . HOH E 5 .   ? -2.995 1.654   1.462   1.00 34.80  ? 418 HOH A O   1 
HETATM 2192 O  O   . HOH E 5 .   ? 25.941 -0.802  29.197  1.00 23.80  ? 419 HOH A O   1 
HETATM 2193 O  O   . HOH E 5 .   ? 32.850 1.055   16.034  1.00 48.83  ? 420 HOH A O   1 
HETATM 2194 O  O   . HOH E 5 .   ? 4.310  -16.079 20.590  1.00 47.30  ? 421 HOH A O   1 
HETATM 2195 O  O   . HOH E 5 .   ? 11.105 15.002  10.714  1.00 21.06  ? 422 HOH A O   1 
HETATM 2196 O  O   . HOH E 5 .   ? -2.909 -1.566  29.545  1.00 29.91  ? 423 HOH A O   1 
HETATM 2197 O  O   . HOH E 5 .   ? -4.520 -3.778  13.404  1.00 43.17  ? 424 HOH A O   1 
HETATM 2198 O  O   . HOH E 5 .   ? 15.239 -9.541  36.328  1.00 45.09  ? 425 HOH A O   1 
HETATM 2199 O  O   . HOH E 5 .   ? 17.238 22.318  15.897  1.00 23.56  ? 426 HOH A O   1 
HETATM 2200 O  O   . HOH E 5 .   ? 2.342  19.462  18.901  1.00 30.90  ? 427 HOH A O   1 
HETATM 2201 O  O   . HOH E 5 .   ? 2.167  -17.863 19.514  1.00 46.97  ? 428 HOH A O   1 
HETATM 2202 O  O   . HOH E 5 .   ? 20.881 2.875   34.492  1.00 24.26  ? 429 HOH A O   1 
HETATM 2203 O  O   . HOH E 5 .   ? 8.651  14.870  31.922  1.00 29.71  ? 430 HOH A O   1 
HETATM 2204 O  O   . HOH E 5 .   ? 21.459 -8.023  -5.569  1.00 33.97  ? 431 HOH A O   1 
HETATM 2205 O  O   . HOH E 5 .   ? 14.646 -2.670  -6.377  1.00 24.41  ? 432 HOH A O   1 
HETATM 2206 O  O   . HOH E 5 .   ? 10.741 10.499  25.587  1.00 15.71  ? 433 HOH A O   1 
HETATM 2207 O  O   . HOH E 5 .   ? 23.227 9.753   27.799  1.00 22.44  ? 434 HOH A O   1 
HETATM 2208 O  O   . HOH E 5 .   ? 24.031 -7.428  -6.597  1.00 25.74  ? 435 HOH A O   1 
HETATM 2209 O  O   . HOH E 5 .   ? -2.923 10.639  20.549  1.00 22.34  ? 436 HOH A O   1 
HETATM 2210 O  O   . HOH E 5 .   ? -1.679 -12.936 16.232  1.00 44.56  ? 437 HOH A O   1 
HETATM 2211 O  O   . HOH E 5 .   ? 27.593 -9.079  15.465  1.00 38.47  ? 438 HOH A O   1 
HETATM 2212 O  O   . HOH E 5 .   ? -4.393 11.613  13.469  1.00 35.44  ? 439 HOH A O   1 
HETATM 2213 O  O   . HOH E 5 .   ? 28.487 -5.980  -0.981  1.00 20.45  ? 440 HOH A O   1 
HETATM 2214 O  O   . HOH E 5 .   ? 5.327  2.448   -4.571  1.00 35.84  ? 441 HOH A O   1 
HETATM 2215 O  O   . HOH E 5 .   ? 16.515 -10.158 32.007  1.00 22.19  ? 442 HOH A O   1 
HETATM 2216 O  O   . HOH E 5 .   ? 12.348 7.905   28.847  1.00 27.41  ? 443 HOH A O   1 
HETATM 2217 O  O   . HOH E 5 .   ? -2.689 -12.435 19.828  1.00 45.63  ? 444 HOH A O   1 
HETATM 2218 O  O   . HOH E 5 .   ? 22.956 -5.265  14.026  1.00 23.19  ? 445 HOH A O   1 
HETATM 2219 O  O   . HOH E 5 .   ? 6.840  -19.184 3.305   1.00 40.39  ? 446 HOH A O   1 
HETATM 2220 O  O   . HOH E 5 .   ? 25.586 -1.625  26.656  1.00 20.81  ? 447 HOH A O   1 
HETATM 2221 O  O   . HOH E 5 .   ? 1.261  -14.808 3.078   1.00 23.04  ? 448 HOH A O   1 
HETATM 2222 O  O   . HOH E 5 .   ? -3.453 22.378  8.675   1.00 38.81  ? 449 HOH A O   1 
HETATM 2223 O  O   . HOH E 5 .   ? 8.941  14.403  29.350  1.00 34.20  ? 450 HOH A O   1 
HETATM 2224 O  O   . HOH E 5 .   ? 15.945 17.953  12.495  1.00 16.50  ? 451 HOH A O   1 
HETATM 2225 O  O   . HOH E 5 .   ? 5.528  10.616  -1.792  1.00 43.96  ? 452 HOH A O   1 
HETATM 2226 O  O   . HOH E 5 .   ? 7.707  -20.502 11.625  1.00 33.35  ? 453 HOH A O   1 
HETATM 2227 O  O   . HOH E 5 .   ? 23.025 -13.645 9.335   1.00 22.49  ? 454 HOH A O   1 
HETATM 2228 O  O   . HOH E 5 .   ? 32.398 -5.258  22.548  1.00 35.63  ? 455 HOH A O   1 
HETATM 2229 O  O   . HOH E 5 .   ? -5.543 -8.888  22.885  1.00 59.21  ? 456 HOH A O   1 
HETATM 2230 O  O   . HOH E 5 .   ? 21.035 0.864   -4.726  1.00 15.04  ? 457 HOH A O   1 
HETATM 2231 O  O   . HOH E 5 .   ? 20.517 15.427  16.139  1.00 39.04  ? 458 HOH A O   1 
HETATM 2232 O  O   . HOH E 5 .   ? 19.739 -2.125  15.405  1.00 11.69  ? 459 HOH A O   1 
HETATM 2233 O  O   . HOH E 5 .   ? -0.397 -12.441 18.850  1.00 34.66  ? 460 HOH A O   1 
HETATM 2234 O  O   . HOH E 5 .   ? 1.452  -2.381  41.284  1.00 35.90  ? 461 HOH A O   1 
HETATM 2235 O  O   . HOH E 5 .   ? 13.755 -6.523  -7.082  1.00 34.06  ? 462 HOH A O   1 
HETATM 2236 O  O   . HOH E 5 .   ? -0.156 9.595   1.996   1.00 16.82  ? 463 HOH A O   1 
HETATM 2237 O  O   . HOH E 5 .   ? 24.635 6.715   30.240  1.00 20.51  ? 464 HOH A O   1 
HETATM 2238 O  O   . HOH E 5 .   ? 9.429  11.110  3.460   1.00 21.15  ? 465 HOH A O   1 
HETATM 2239 O  O   . HOH E 5 .   ? 30.663 -4.210  -7.853  1.00 26.70  ? 466 HOH A O   1 
HETATM 2240 O  O   . HOH E 5 .   ? 14.568 -3.516  37.413  1.00 22.71  ? 467 HOH A O   1 
HETATM 2241 O  O   . HOH E 5 .   ? 2.574  -1.937  -2.483  1.00 32.07  ? 468 HOH A O   1 
HETATM 2242 O  O   . HOH E 5 .   ? 23.588 -11.462 5.123   1.00 18.42  ? 469 HOH A O   1 
HETATM 2243 O  O   . HOH E 5 .   ? 1.132  12.725  26.855  1.00 21.28  ? 470 HOH A O   1 
HETATM 2244 O  O   . HOH E 5 .   ? 34.772 1.850   24.735  1.00 26.04  ? 471 HOH A O   1 
HETATM 2245 O  O   . HOH E 5 .   ? 5.187  -10.424 24.476  1.00 17.32  ? 472 HOH A O   1 
HETATM 2246 O  O   . HOH E 5 .   ? 18.601 -16.790 22.091  1.00 36.61  ? 473 HOH A O   1 
HETATM 2247 O  O   . HOH E 5 .   ? -4.797 9.822   6.551   1.00 36.09  ? 474 HOH A O   1 
HETATM 2248 O  O   . HOH E 5 .   ? 13.244 -13.563 11.327  1.00 11.51  ? 475 HOH A O   1 
HETATM 2249 O  O   . HOH E 5 .   ? 10.756 -16.329 17.277  1.00 25.81  ? 476 HOH A O   1 
HETATM 2250 O  O   . HOH E 5 .   ? 18.792 -2.691  -7.108  1.00 30.12  ? 477 HOH A O   1 
HETATM 2251 O  O   . HOH E 5 .   ? 2.015  -19.064 5.277   1.00 28.02  ? 478 HOH A O   1 
HETATM 2252 O  O   . HOH E 5 .   ? 25.072 -1.363  3.690   1.00 25.17  ? 479 HOH A O   1 
HETATM 2253 O  O   . HOH E 5 .   ? 35.191 3.930   23.044  1.00 24.93  ? 480 HOH A O   1 
HETATM 2254 O  O   . HOH E 5 .   ? 14.385 -13.053 31.638  1.00 26.03  ? 481 HOH A O   1 
HETATM 2255 O  O   . HOH E 5 .   ? -4.425 -13.541 7.874   1.00 31.16  ? 482 HOH A O   1 
HETATM 2256 O  O   . HOH E 5 .   ? -0.397 -5.332  23.727  1.00 13.72  ? 483 HOH A O   1 
HETATM 2257 O  O   . HOH E 5 .   ? 7.690  21.858  14.915  1.00 25.62  ? 484 HOH A O   1 
HETATM 2258 O  O   . HOH E 5 .   ? 18.714 -6.896  29.100  1.00 13.52  ? 485 HOH A O   1 
HETATM 2259 O  O   . HOH E 5 .   ? 15.621 18.703  27.419  1.00 41.38  ? 486 HOH A O   1 
HETATM 2260 O  O   . HOH E 5 .   ? 16.671 -11.521 17.986  1.00 10.87  ? 487 HOH A O   1 
HETATM 2261 O  O   . HOH E 5 .   ? 12.861 -13.655 36.560  1.00 26.33  ? 488 HOH A O   1 
HETATM 2262 O  O   . HOH E 5 .   ? 4.199  -6.584  20.457  1.00 10.04  ? 489 HOH A O   1 
HETATM 2263 O  O   . HOH E 5 .   ? 26.673 9.013   20.856  1.00 22.51  ? 490 HOH A O   1 
HETATM 2264 O  O   . HOH E 5 .   ? -6.774 8.104   21.886  1.00 34.34  ? 491 HOH A O   1 
HETATM 2265 O  O   . HOH E 5 .   ? 17.276 -11.019 -2.970  1.00 23.41  ? 492 HOH A O   1 
HETATM 2266 O  O   . HOH E 5 .   ? 36.180 2.122   15.424  1.00 36.07  ? 493 HOH A O   1 
HETATM 2267 O  O   . HOH E 5 .   ? 3.288  -18.739 8.179   1.00 17.73  ? 494 HOH A O   1 
HETATM 2268 O  O   . HOH E 5 .   ? 13.995 -14.912 1.704   1.00 23.48  ? 495 HOH A O   1 
HETATM 2269 O  O   . HOH E 5 .   ? 9.112  12.294  6.068   1.00 23.80  ? 496 HOH A O   1 
HETATM 2270 O  O   . HOH E 5 .   ? -2.108 -1.298  7.128   1.00 21.37  ? 497 HOH A O   1 
HETATM 2271 O  O   . HOH E 5 .   ? 2.904  12.409  11.513  1.00 19.67  ? 498 HOH A O   1 
HETATM 2272 O  O   . HOH E 5 .   ? 14.021 8.581   9.648   1.00 28.80  ? 499 HOH A O   1 
HETATM 2273 O  O   . HOH E 5 .   ? 9.930  14.086  7.620   1.00 37.44  ? 500 HOH A O   1 
HETATM 2274 O  O   . HOH E 5 .   ? 12.166 2.475   -6.380  1.00 27.38  ? 501 HOH A O   1 
HETATM 2275 O  O   . HOH E 5 .   ? 2.610  -10.722 -3.559  1.00 28.89  ? 502 HOH A O   1 
HETATM 2276 O  O   . HOH E 5 .   ? 17.716 -9.260  20.831  1.00 11.69  ? 503 HOH A O   1 
HETATM 2277 O  O   . HOH E 5 .   ? -4.293 -8.736  17.842  1.00 23.70  ? 504 HOH A O   1 
HETATM 2278 O  O   . HOH E 5 .   ? 16.999 -6.758  31.203  1.00 22.81  ? 505 HOH A O   1 
HETATM 2279 O  O   . HOH E 5 .   ? -5.255 5.495   15.789  1.00 26.99  ? 506 HOH A O   1 
HETATM 2280 O  O   . HOH E 5 .   ? 7.551  12.315  27.983  1.00 18.15  ? 507 HOH A O   1 
HETATM 2281 O  O   . HOH E 5 .   ? 20.914 -18.605 15.085  1.00 34.21  ? 508 HOH A O   1 
HETATM 2282 O  O   . HOH E 5 .   ? 12.482 6.398   -6.687  1.00 40.14  ? 509 HOH A O   1 
HETATM 2283 O  O   . HOH E 5 .   ? -1.065 7.565   4.978   1.00 16.27  ? 510 HOH A O   1 
HETATM 2284 O  O   . HOH E 5 .   ? -2.085 -9.722  17.097  1.00 33.61  ? 511 HOH A O   1 
HETATM 2285 O  O   . HOH E 5 .   ? 8.071  -7.191  -3.092  1.00 28.25  ? 512 HOH A O   1 
HETATM 2286 O  O   . HOH E 5 .   ? 3.544  -5.708  39.296  1.00 50.96  ? 513 HOH A O   1 
HETATM 2287 O  O   . HOH E 5 .   ? 22.396 -4.673  34.351  1.00 40.05  ? 514 HOH A O   1 
HETATM 2288 O  O   . HOH E 5 .   ? 17.059 6.505   8.745   1.00 22.47  ? 515 HOH A O   1 
HETATM 2289 O  O   . HOH E 5 .   ? 12.602 -13.104 33.092  1.00 66.47  ? 516 HOH A O   1 
HETATM 2290 O  O   . HOH E 5 .   ? 22.539 -9.896  24.966  1.00 27.66  ? 517 HOH A O   1 
HETATM 2291 O  O   . HOH E 5 .   ? 24.279 -2.682  6.995   1.00 29.20  ? 518 HOH A O   1 
HETATM 2292 O  O   . HOH E 5 .   ? -3.776 6.711   8.643   1.00 41.45  ? 519 HOH A O   1 
HETATM 2293 O  O   . HOH E 5 .   ? 36.853 -0.569  14.814  1.00 22.32  ? 520 HOH A O   1 
HETATM 2294 O  O   . HOH E 5 .   ? 0.308  20.859  13.937  1.00 30.39  ? 521 HOH A O   1 
HETATM 2295 O  O   . HOH E 5 .   ? 13.853 -6.869  32.596  1.00 18.82  ? 522 HOH A O   1 
HETATM 2296 O  O   . HOH E 5 .   ? 21.541 -17.530 10.924  1.00 29.69  ? 523 HOH A O   1 
HETATM 2297 O  O   . HOH E 5 .   ? 28.344 -1.768  30.086  1.00 34.87  ? 524 HOH A O   1 
HETATM 2298 O  O   . HOH E 5 .   ? 7.524  16.130  27.626  1.00 33.66  ? 525 HOH A O   1 
HETATM 2299 O  O   . HOH E 5 .   ? 1.667  19.209  5.952   1.00 29.10  ? 526 HOH A O   1 
HETATM 2300 O  O   . HOH E 5 .   ? 17.517 -13.963 24.329  1.00 16.36  ? 527 HOH A O   1 
HETATM 2301 O  O   . HOH E 5 .   ? -5.072 4.642   21.250  1.00 22.65  ? 528 HOH A O   1 
HETATM 2302 O  O   . HOH E 5 .   ? 1.654  11.843  9.086   1.00 15.29  ? 529 HOH A O   1 
HETATM 2303 O  O   . HOH E 5 .   ? 5.136  17.946  23.729  1.00 24.52  ? 530 HOH A O   1 
HETATM 2304 O  O   . HOH E 5 .   ? 4.013  -14.476 22.508  1.00 48.98  ? 531 HOH A O   1 
HETATM 2305 O  O   . HOH E 5 .   ? -3.756 -6.073  9.386   1.00 21.62  ? 532 HOH A O   1 
HETATM 2306 O  O   . HOH E 5 .   ? 17.643 -2.673  37.798  1.00 39.13  ? 533 HOH A O   1 
HETATM 2307 O  O   . HOH E 5 .   ? 6.745  -14.822 28.910  1.00 31.41  ? 534 HOH A O   1 
HETATM 2308 O  O   . HOH E 5 .   ? 4.051  -21.081 4.215   1.00 32.07  ? 535 HOH A O   1 
HETATM 2309 O  O   . HOH E 5 .   ? 29.814 -1.917  21.134  1.00 16.94  ? 536 HOH A O   1 
HETATM 2310 O  O   . HOH E 5 .   ? -1.683 -3.942  3.148   1.00 27.00  ? 537 HOH A O   1 
HETATM 2311 O  O   . HOH E 5 .   ? 22.659 -5.058  -8.346  1.00 38.11  ? 538 HOH A O   1 
HETATM 2312 O  O   . HOH E 5 .   ? -5.055 -5.707  30.524  1.00 37.04  ? 539 HOH A O   1 
HETATM 2313 O  O   . HOH E 5 .   ? 26.060 -2.928  20.916  1.00 16.83  ? 540 HOH A O   1 
HETATM 2314 O  O   . HOH E 5 .   ? 17.886 -11.310 25.139  1.00 12.96  ? 541 HOH A O   1 
HETATM 2315 O  O   . HOH E 5 .   ? 23.422 10.816  31.719  1.00 43.25  ? 542 HOH A O   1 
HETATM 2316 O  O   . HOH E 5 .   ? 22.973 9.950   24.871  1.00 20.81  ? 543 HOH A O   1 
HETATM 2317 O  O   . HOH E 5 .   ? -2.676 0.909   26.789  1.00 32.40  ? 544 HOH A O   1 
HETATM 2318 O  O   . HOH E 5 .   ? 25.507 1.085   -5.280  1.00 27.28  ? 545 HOH A O   1 
HETATM 2319 O  O   . HOH E 5 .   ? 15.473 9.362   5.514   1.00 20.25  ? 546 HOH A O   1 
HETATM 2320 O  O   . HOH E 5 .   ? 8.508  9.781   28.793  1.00 25.16  ? 547 HOH A O   1 
HETATM 2321 O  O   . HOH E 5 .   ? 26.614 2.109   8.150   1.00 22.05  ? 548 HOH A O   1 
HETATM 2322 O  O   . HOH E 5 .   ? 4.956  -8.077  33.060  1.00 21.94  ? 549 HOH A O   1 
HETATM 2323 O  O   . HOH E 5 .   ? 9.355  4.641   30.778  1.00 20.80  ? 550 HOH A O   1 
HETATM 2324 O  O   . HOH E 5 .   ? 20.953 2.700   8.089   1.00 29.76  ? 551 HOH A O   1 
HETATM 2325 O  O   . HOH E 5 .   ? 32.426 2.990   26.231  1.00 25.25  ? 552 HOH A O   1 
HETATM 2326 O  O   . HOH E 5 .   ? 23.744 -9.431  9.503   1.00 22.03  ? 553 HOH A O   1 
HETATM 2327 O  O   . HOH E 5 .   ? 10.028 -17.406 6.964   1.00 32.89  ? 554 HOH A O   1 
HETATM 2328 O  O   . HOH E 5 .   ? -6.639 6.096   24.314  1.00 37.29  ? 555 HOH A O   1 
HETATM 2329 O  O   . HOH E 5 .   ? 6.209  22.073  17.629  1.00 24.18  ? 556 HOH A O   1 
HETATM 2330 O  O   . HOH E 5 .   ? 11.602 -8.344  -1.188  1.00 26.63  ? 557 HOH A O   1 
HETATM 2331 O  O   . HOH E 5 .   ? 14.663 12.937  8.019   1.00 27.69  ? 558 HOH A O   1 
HETATM 2332 O  O   . HOH E 5 .   ? -1.051 -16.548 13.645  1.00 26.04  ? 559 HOH A O   1 
HETATM 2333 O  O   . HOH E 5 .   ? 32.102 8.456   15.909  1.00 51.32  ? 560 HOH A O   1 
HETATM 2334 O  O   . HOH E 5 .   ? 12.099 -4.017  35.973  1.00 19.99  ? 561 HOH A O   1 
HETATM 2335 O  O   . HOH E 5 .   ? -2.106 2.163   34.840  1.00 53.78  ? 562 HOH A O   1 
HETATM 2336 O  O   . HOH E 5 .   ? 8.165  -14.980 26.633  1.00 22.33  ? 563 HOH A O   1 
HETATM 2337 O  O   . HOH E 5 .   ? 14.313 23.237  19.641  1.00 33.59  ? 564 HOH A O   1 
HETATM 2338 O  O   . HOH E 5 .   ? -3.049 1.025   4.174   1.00 19.18  ? 565 HOH A O   1 
HETATM 2339 O  O   . HOH E 5 .   ? 16.810 -14.402 1.386   1.00 39.27  ? 566 HOH A O   1 
HETATM 2340 O  O   . HOH E 5 .   ? 11.116 7.963   -4.134  1.00 31.45  ? 567 HOH A O   1 
HETATM 2341 O  O   . HOH E 5 .   ? 13.538 -17.286 30.523  1.00 28.74  ? 568 HOH A O   1 
HETATM 2342 O  O   . HOH E 5 .   ? 7.388  1.093   -5.919  1.00 31.62  ? 569 HOH A O   1 
HETATM 2343 O  O   . HOH E 5 .   ? 3.432  7.091   -3.437  1.00 24.43  ? 570 HOH A O   1 
HETATM 2344 O  O   . HOH E 5 .   ? -5.745 -2.213  25.238  1.00 22.66  ? 571 HOH A O   1 
HETATM 2345 O  O   . HOH E 5 .   ? 20.511 -6.738  32.499  1.00 25.92  ? 572 HOH A O   1 
HETATM 2346 O  O   . HOH E 5 .   ? 34.301 -4.123  24.511  1.00 27.60  ? 573 HOH A O   1 
HETATM 2347 O  O   . HOH E 5 .   ? 11.620 -6.186  34.020  1.00 25.18  ? 574 HOH A O   1 
HETATM 2348 O  O   . HOH E 5 .   ? 0.972  15.850  29.114  1.00 36.82  ? 575 HOH A O   1 
HETATM 2349 O  O   . HOH E 5 .   ? 22.522 0.207   29.511  1.00 13.98  ? 576 HOH A O   1 
HETATM 2350 O  O   . HOH E 5 .   ? 24.074 -12.702 0.965   1.00 35.26  ? 577 HOH A O   1 
HETATM 2351 O  O   . HOH E 5 .   ? -1.775 -10.000 14.273  1.00 20.88  ? 578 HOH A O   1 
HETATM 2352 O  O   . HOH E 5 .   ? 8.138  5.495   -6.682  1.00 25.44  ? 579 HOH A O   1 
HETATM 2353 O  O   . HOH E 5 .   ? 20.817 5.433   7.189   1.00 36.92  ? 580 HOH A O   1 
HETATM 2354 O  O   . HOH E 5 .   ? -0.364 21.538  17.311  1.00 44.80  ? 581 HOH A O   1 
HETATM 2355 O  O   . HOH E 5 .   ? 8.072  -16.541 14.820  1.00 21.45  ? 582 HOH A O   1 
HETATM 2356 O  O   . HOH E 5 .   ? 19.176 -10.364 22.789  1.00 11.89  ? 583 HOH A O   1 
HETATM 2357 O  O   . HOH E 5 .   ? 9.988  19.465  12.320  1.00 23.37  ? 584 HOH A O   1 
HETATM 2358 O  O   . HOH E 5 .   ? 35.308 7.490   19.328  1.00 35.27  ? 585 HOH A O   1 
HETATM 2359 O  O   . HOH E 5 .   ? -2.068 1.708   32.319  1.00 33.13  ? 586 HOH A O   1 
HETATM 2360 O  O   . HOH E 5 .   ? 11.715 17.328  12.207  1.00 15.52  ? 587 HOH A O   1 
HETATM 2361 O  O   . HOH E 5 .   ? 21.106 -12.303 22.059  1.00 22.32  ? 588 HOH A O   1 
HETATM 2362 O  O   . HOH E 5 .   ? 15.486 5.336   -5.606  1.00 32.28  ? 589 HOH A O   1 
HETATM 2363 O  O   . HOH E 5 .   ? 13.222 -17.411 21.774  1.00 32.71  ? 590 HOH A O   1 
HETATM 2364 O  O   . HOH E 5 .   ? 14.004 -16.859 4.526   1.00 31.33  ? 591 HOH A O   1 
HETATM 2365 O  O   . HOH E 5 .   ? 28.340 5.450   32.208  1.00 37.20  ? 592 HOH A O   1 
HETATM 2366 O  O   . HOH E 5 .   ? 14.139 3.313   35.221  1.00 30.31  ? 593 HOH A O   1 
HETATM 2367 O  O   . HOH E 5 .   ? -4.420 -4.575  33.751  1.00 43.07  ? 594 HOH A O   1 
HETATM 2368 O  O   . HOH E 5 .   ? 0.084  -17.805 6.744   1.00 30.30  ? 595 HOH A O   1 
HETATM 2369 O  O   . HOH E 5 .   ? 28.910 8.064   22.209  1.00 18.06  ? 596 HOH A O   1 
HETATM 2370 O  O   . HOH E 5 .   ? 16.105 -11.754 34.202  1.00 38.90  ? 597 HOH A O   1 
HETATM 2371 O  O   . HOH E 5 .   ? 26.395 -5.322  22.253  1.00 32.71  ? 598 HOH A O   1 
HETATM 2372 O  O   . HOH E 5 .   ? 2.341  22.348  15.009  1.00 34.03  ? 599 HOH A O   1 
HETATM 2373 O  O   . HOH E 5 .   ? 7.397  16.359  6.774   1.00 37.41  ? 600 HOH A O   1 
HETATM 2374 O  O   . HOH E 5 .   ? 6.440  13.159  35.002  1.00 35.66  ? 601 HOH A O   1 
HETATM 2375 O  O   . HOH E 5 .   ? 15.834 -17.802 23.554  1.00 48.39  ? 602 HOH A O   1 
HETATM 2376 O  O   . HOH E 5 .   ? 10.480 10.940  8.050   1.00 24.95  ? 603 HOH A O   1 
HETATM 2377 O  O   . HOH E 5 .   ? 19.772 -15.711 18.082  1.00 29.43  ? 604 HOH A O   1 
HETATM 2378 O  O   . HOH E 5 .   ? 13.506 -6.954  -2.392  1.00 31.39  ? 605 HOH A O   1 
HETATM 2379 O  O   . HOH E 5 .   ? 18.549 -12.871 32.910  1.00 40.37  ? 606 HOH A O   1 
HETATM 2380 O  O   . HOH E 5 .   ? -2.356 -16.713 6.233   1.00 32.51  ? 607 HOH A O   1 
HETATM 2381 O  O   . HOH E 5 .   ? 13.886 10.212  7.091   1.00 47.87  ? 608 HOH A O   1 
HETATM 2382 O  O   . HOH E 5 .   ? 2.254  4.996   -3.413  1.00 34.38  ? 609 HOH A O   1 
HETATM 2383 O  O   . HOH E 5 .   ? 20.110 12.305  24.747  1.00 42.32  ? 610 HOH A O   1 
HETATM 2384 O  O   . HOH E 5 .   ? 29.510 5.975   28.134  1.00 40.98  ? 611 HOH A O   1 
HETATM 2385 O  O   . HOH E 5 .   ? 29.808 -2.959  23.972  1.00 32.77  ? 612 HOH A O   1 
HETATM 2386 O  O   . HOH E 5 .   ? 18.900 11.703  10.735  1.00 38.72  ? 613 HOH A O   1 
HETATM 2387 O  O   . HOH E 5 .   ? 23.326 -13.072 -1.283  1.00 41.41  ? 614 HOH A O   1 
HETATM 2388 O  O   . HOH E 5 .   ? 6.005  -14.309 25.385  1.00 42.22  ? 615 HOH A O   1 
HETATM 2389 O  O   . HOH E 5 .   ? -1.497 -7.738  25.543  1.00 24.16  ? 616 HOH A O   1 
HETATM 2390 O  O   . HOH E 5 .   ? 10.291 24.200  19.401  1.00 45.01  ? 617 HOH A O   1 
HETATM 2391 O  O   . HOH E 5 .   ? 21.176 -13.593 27.310  1.00 37.05  ? 618 HOH A O   1 
HETATM 2392 O  O   . HOH E 5 .   ? -1.393 -19.435 12.336  1.00 44.31  ? 619 HOH A O   1 
HETATM 2393 O  O   . HOH E 5 .   ? 8.396  -15.389 16.880  1.00 27.58  ? 620 HOH A O   1 
HETATM 2394 O  O   . HOH E 5 .   ? 22.763 -7.817  28.786  1.00 45.13  ? 621 HOH A O   1 
HETATM 2395 O  O   . HOH E 5 .   ? 8.738  8.485   31.025  1.00 38.83  ? 622 HOH A O   1 
HETATM 2396 O  O   . HOH E 5 .   ? -4.774 6.117   4.133   1.00 52.10  ? 623 HOH A O   1 
HETATM 2397 O  O   . HOH E 5 .   ? 21.824 18.816  24.150  1.00 48.80  ? 624 HOH A O   1 
HETATM 2398 O  O   . HOH E 5 .   ? -4.234 13.262  19.761  1.00 36.42  ? 625 HOH A O   1 
HETATM 2399 O  O   . HOH E 5 .   ? 3.439  21.782  17.599  1.00 30.18  ? 626 HOH A O   1 
HETATM 2400 O  O   . HOH E 5 .   ? 18.973 20.248  15.476  1.00 35.69  ? 627 HOH A O   1 
HETATM 2401 O  O   . HOH E 5 .   ? 22.344 4.851   2.110   1.00 30.92  ? 628 HOH A O   1 
HETATM 2402 O  O   . HOH E 5 .   ? 17.556 7.772   6.314   1.00 21.64  ? 629 HOH A O   1 
HETATM 2403 O  O   . HOH E 5 .   ? 3.336  -7.893  37.463  1.00 55.18  ? 630 HOH A O   1 
HETATM 2404 O  O   . HOH E 5 .   ? -2.812 -1.728  4.269   1.00 38.48  ? 631 HOH A O   1 
HETATM 2405 O  O   . HOH E 5 .   ? -3.474 11.215  26.683  1.00 46.38  ? 632 HOH A O   1 
HETATM 2406 O  O   . HOH E 5 .   ? 24.044 -11.428 7.956   1.00 31.22  ? 633 HOH A O   1 
HETATM 2407 O  O   . HOH E 5 .   ? 26.571 -9.032  18.901  1.00 45.68  ? 634 HOH A O   1 
HETATM 2408 O  O   . HOH E 5 .   ? 10.499 9.607   -2.345  1.00 48.76  ? 635 HOH A O   1 
HETATM 2409 O  O   . HOH E 5 .   ? 27.571 -3.547  27.379  1.00 36.10  ? 636 HOH A O   1 
HETATM 2410 O  O   . HOH E 5 .   ? 30.096 -7.955  0.004   1.00 29.48  ? 637 HOH A O   1 
HETATM 2411 O  O   . HOH E 5 .   ? 10.836 6.927   30.613  1.00 29.23  ? 638 HOH A O   1 
HETATM 2412 O  O   . HOH E 5 .   ? 26.920 -7.407  20.959  1.00 38.86  ? 639 HOH A O   1 
HETATM 2413 O  O   . HOH E 5 .   ? 23.548 1.902   7.489   1.00 43.43  ? 640 HOH A O   1 
HETATM 2414 O  O   . HOH E 5 .   ? 3.099  -7.270  34.889  1.00 34.78  ? 641 HOH A O   1 
HETATM 2415 O  O   . HOH E 5 .   ? 12.744 -15.634 34.745  1.00 32.96  ? 642 HOH A O   1 
HETATM 2416 O  O   . HOH E 5 .   ? 31.579 7.253   13.186  1.00 51.77  ? 643 HOH A O   1 
HETATM 2417 O  O   . HOH E 5 .   ? 5.620  22.516  23.104  1.00 46.46  ? 644 HOH A O   1 
HETATM 2418 O  O   . HOH E 5 .   ? 19.169 -10.029 31.454  1.00 36.72  ? 645 HOH A O   1 
HETATM 2419 O  O   . HOH E 5 .   ? 26.464 -5.596  7.912   1.00 39.45  ? 646 HOH A O   1 
HETATM 2420 O  O   . HOH E 5 .   ? -2.802 -5.479  0.390   1.00 36.60  ? 647 HOH A O   1 
HETATM 2421 O  O   . HOH E 5 .   ? 19.853 -11.091 26.972  1.00 29.44  ? 648 HOH A O   1 
HETATM 2422 O  O   . HOH E 5 .   ? 6.057  -1.093  -6.685  1.00 46.67  ? 649 HOH A O   1 
HETATM 2423 O  O   . HOH E 5 .   ? 15.766 -7.768  34.476  1.00 54.70  ? 650 HOH A O   1 
HETATM 2424 O  O   . HOH E 5 .   ? 8.908  2.573   -7.610  1.00 41.58  ? 651 HOH A O   1 
HETATM 2425 O  O   . HOH E 5 .   ? 18.522 17.198  11.811  1.00 31.38  ? 652 HOH A O   1 
HETATM 2426 O  O   . HOH E 5 .   ? 25.317 10.484  23.282  1.00 33.66  ? 653 HOH A O   1 
HETATM 2427 O  O   . HOH E 5 .   ? 6.500  24.464  18.827  1.00 28.13  ? 654 HOH A O   1 
HETATM 2428 O  O   . HOH E 5 .   ? -1.264 -10.394 24.993  1.00 37.28  ? 655 HOH A O   1 
HETATM 2429 O  O   . HOH E 5 .   ? 16.209 10.435  7.874   1.00 42.58  ? 656 HOH A O   1 
HETATM 2430 O  O   . HOH E 5 .   ? 4.342  -12.094 26.360  1.00 25.42  ? 657 HOH A O   1 
HETATM 2431 O  O   . HOH E 5 .   ? 19.353 6.434   4.755   1.00 25.42  ? 658 HOH A O   1 
HETATM 2432 O  O   . HOH E 5 .   ? 9.721  -9.406  -2.776  1.00 37.08  ? 659 HOH A O   1 
HETATM 2433 O  O   . HOH E 5 .   ? 9.675  12.578  1.120   1.00 22.33  ? 660 HOH A O   1 
HETATM 2434 O  O   . HOH E 5 .   ? 13.742 -8.278  -4.505  1.00 38.95  ? 661 HOH A O   1 
HETATM 2435 O  O   . HOH E 5 .   ? 20.112 -9.247  28.918  1.00 20.82  ? 662 HOH A O   1 
HETATM 2436 O  O   . HOH E 5 .   ? 13.849 18.406  10.741  1.00 16.13  ? 663 HOH A O   1 
HETATM 2437 O  O   . HOH E 5 .   ? 27.459 7.098   29.943  1.00 35.73  ? 664 HOH A O   1 
HETATM 2438 O  O   . HOH E 5 .   ? 8.859  15.318  5.069   1.00 33.39  ? 665 HOH A O   1 
HETATM 2439 O  O   . HOH E 5 .   ? 22.754 -15.572 7.148   1.00 32.73  ? 666 HOH A O   1 
HETATM 2440 O  O   . HOH E 5 .   ? 3.303  -10.187 31.725  1.00 32.99  ? 667 HOH A O   1 
HETATM 2441 O  O   . HOH E 5 .   ? 16.763 9.374   9.877   1.00 36.65  ? 668 HOH A O   1 
HETATM 2442 O  O   . HOH E 5 .   ? 8.902  -18.280 29.844  1.00 55.03  ? 669 HOH A O   1 
HETATM 2443 O  O   . HOH E 5 .   ? 19.345 -15.692 25.344  1.00 32.86  ? 670 HOH A O   1 
HETATM 2444 O  O   . HOH E 5 .   ? 16.869 -13.560 -2.379  1.00 34.51  ? 671 HOH A O   1 
HETATM 2445 O  O   . HOH E 5 .   ? 17.925 -15.736 4.009   1.00 32.35  ? 672 HOH A O   1 
HETATM 2446 O  O   . HOH E 5 .   ? 23.303 -12.090 20.572  1.00 33.34  ? 673 HOH A O   1 
HETATM 2447 O  O   . HOH E 5 .   ? 8.438  -17.580 26.354  1.00 32.02  ? 674 HOH A O   1 
HETATM 2448 O  O   . HOH E 5 .   ? -5.613 0.284   26.327  1.00 33.91  ? 675 HOH A O   1 
HETATM 2449 O  O   . HOH E 5 .   ? 25.344 -9.825  23.225  1.00 41.80  ? 676 HOH A O   1 
HETATM 2450 O  O   . HOH E 5 .   ? 20.296 -5.039  -7.823  1.00 35.19  ? 677 HOH A O   1 
HETATM 2451 O  O   . HOH E 5 .   ? 13.512 -3.076  39.970  1.00 28.01  ? 678 HOH A O   1 
HETATM 2452 O  O   . HOH E 5 .   ? 20.938 -18.200 6.515   1.00 29.67  ? 679 HOH A O   1 
HETATM 2453 O  O   . HOH E 5 .   ? 22.898 -14.289 4.778   1.00 25.20  ? 680 HOH A O   1 
HETATM 2454 O  O   . HOH E 5 .   ? 7.816  12.983  -0.583  1.00 48.42  ? 681 HOH A O   1 
HETATM 2455 O  O   . HOH E 5 .   ? 22.099 -20.154 13.283  1.00 44.96  ? 682 HOH A O   1 
HETATM 2456 O  O   . HOH E 5 .   ? 25.695 -7.849  8.217   1.00 34.96  ? 683 HOH A O   1 
HETATM 2457 O  O   . HOH E 5 .   ? 3.672  12.757  -2.079  1.00 31.30  ? 684 HOH A O   1 
HETATM 2458 O  O   . HOH E 5 .   ? 17.670 -15.967 -0.213  1.00 39.62  ? 685 HOH A O   1 
HETATM 2459 O  O   . HOH E 5 .   ? 20.224 -15.384 5.100   1.00 32.06  ? 686 HOH A O   1 
HETATM 2460 O  O   . HOH E 5 .   ? 9.334  14.997  2.263   1.00 34.30  ? 687 HOH A O   1 
HETATM 2461 O  O   . HOH E 5 .   ? 18.524 -17.688 2.332   1.00 32.32  ? 688 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   . TRP A 5   ? 0.5728 0.7490 0.7910 -0.0880 -0.0401 0.2137  5   TRP A N   
2    C  CA  . TRP A 5   ? 0.4975 0.4809 0.6164 -0.0616 0.0302  -0.0541 5   TRP A CA  
3    C  C   . TRP A 5   ? 0.5776 0.4410 0.5968 -0.1590 -0.0681 0.1218  5   TRP A C   
4    O  O   . TRP A 5   ? 0.4081 0.3600 0.4771 -0.0701 0.0908  0.0559  5   TRP A O   
5    C  CB  . TRP A 5   ? 0.6427 0.4882 0.4583 0.1397  0.0895  0.1504  5   TRP A CB  
6    C  CG  . TRP A 5   ? 0.5044 0.6639 0.3086 0.1016  0.0754  0.0908  5   TRP A CG  
7    C  CD1 . TRP A 5   ? 0.5808 0.7204 0.4984 0.1905  0.1900  0.1179  5   TRP A CD1 
8    C  CD2 . TRP A 5   ? 0.6130 0.2532 0.4289 -0.0557 0.1010  -0.0017 5   TRP A CD2 
9    N  NE1 . TRP A 5   ? 0.4716 0.5529 0.3729 -0.1417 0.0466  0.1385  5   TRP A NE1 
10   C  CE2 . TRP A 5   ? 0.4243 0.4354 0.3107 -0.0687 -0.0037 0.0023  5   TRP A CE2 
11   C  CE3 . TRP A 5   ? 0.6021 0.2830 0.2398 -0.0978 0.0069  -0.0121 5   TRP A CE3 
12   C  CZ2 . TRP A 5   ? 0.4324 0.6016 0.3608 0.0837  -0.0623 -0.1251 5   TRP A CZ2 
13   C  CZ3 . TRP A 5   ? 0.6521 0.4281 0.6490 -0.0464 -0.0697 -0.1676 5   TRP A CZ3 
14   C  CH2 . TRP A 5   ? 0.5926 0.6031 0.5594 0.0631  -0.0716 -0.1913 5   TRP A CH2 
15   N  N   . GLY A 6   ? 0.4192 0.1450 0.7713 0.0345  -0.0287 -0.0451 6   GLY A N   
16   C  CA  . GLY A 6   ? 0.2856 0.5836 0.5188 0.0196  0.0797  -0.3273 6   GLY A CA  
17   C  C   . GLY A 6   ? 0.4660 0.5205 0.7929 0.1923  0.0413  -0.0228 6   GLY A C   
18   O  O   . GLY A 6   ? 0.3751 0.4571 0.6404 -0.0124 0.2371  -0.0482 6   GLY A O   
19   N  N   . HIS A 10  ? 0.3254 0.8538 1.9328 0.1579  0.4184  -0.6278 10  HIS A N   
20   C  CA  . HIS A 10  ? 0.8901 0.6316 1.4368 0.2130  0.0275  0.0222  10  HIS A CA  
21   C  C   . HIS A 10  ? 0.5525 0.8844 0.3223 0.1196  0.0310  -0.0614 10  HIS A C   
22   O  O   . HIS A 10  ? 0.3749 0.6266 0.4065 0.1468  0.0924  0.0905  10  HIS A O   
23   C  CB  . HIS A 10  ? 1.2737 0.9741 1.5535 0.0037  0.3277  0.2605  10  HIS A CB  
24   C  CG  . HIS A 10  ? 0.8800 1.3960 0.9174 0.2165  0.5302  0.3008  10  HIS A CG  
25   N  ND1 . HIS A 10  ? 0.8548 1.2659 0.6409 0.0342  0.3146  0.1479  10  HIS A ND1 
26   C  CD2 . HIS A 10  ? 1.0385 1.3394 0.8899 0.2134  0.6997  0.2026  10  HIS A CD2 
27   C  CE1 . HIS A 10  ? 1.3213 1.3415 0.6643 0.2133  0.4950  0.1908  10  HIS A CE1 
28   N  NE2 . HIS A 10  ? 0.9229 0.8483 0.8731 0.1384  0.6330  0.2675  10  HIS A NE2 
29   N  N   . ASN A 11  ? 0.4744 0.9792 0.8003 0.0140  0.2399  -0.0255 11  ASN A N   
30   C  CA  . ASN A 11  ? 0.5441 0.7340 0.6638 -0.1198 0.0395  0.0570  11  ASN A CA  
31   C  C   . ASN A 11  ? 0.5817 0.5037 0.4274 -0.0314 -0.0537 -0.0679 11  ASN A C   
32   O  O   . ASN A 11  ? 0.5049 0.4300 0.2222 -0.1424 0.1344  0.0018  11  ASN A O   
33   C  CB  . ASN A 11  ? 0.7621 0.5071 0.8080 -0.0963 -0.0140 0.1016  11  ASN A CB  
34   C  CG  . ASN A 11  ? 0.9382 0.8924 0.8353 -0.0054 -0.1257 0.0580  11  ASN A CG  
35   O  OD1 . ASN A 11  ? 1.1883 0.7752 0.3182 0.1453  0.0861  0.0303  11  ASN A OD1 
36   N  ND2 . ASN A 11  ? 0.7143 0.5801 0.8609 0.2582  0.1584  0.0966  11  ASN A ND2 
37   N  N   . GLY A 12  ? 0.2479 0.5246 0.4451 -0.0200 0.1401  -0.0823 12  GLY A N   
38   C  CA  . GLY A 12  ? 0.1985 0.3480 0.3034 -0.0223 0.0031  -0.0267 12  GLY A CA  
39   C  C   . GLY A 12  ? 0.1592 0.2927 0.3277 -0.0323 0.0240  -0.0374 12  GLY A C   
40   O  O   . GLY A 12  ? 0.1310 0.2644 0.3126 -0.0031 0.0271  -0.0223 12  GLY A O   
41   N  N   . PRO A 13  ? 0.1531 0.2495 0.2398 -0.0307 0.0205  -0.0497 13  PRO A N   
42   C  CA  . PRO A 13  ? 0.1752 0.2099 0.2781 -0.0335 0.0190  -0.0570 13  PRO A CA  
43   C  C   . PRO A 13  ? 0.1489 0.2188 0.2319 -0.0141 0.0410  -0.0462 13  PRO A C   
44   O  O   . PRO A 13  ? 0.1493 0.2219 0.2465 -0.0024 0.0411  -0.0410 13  PRO A O   
45   C  CB  . PRO A 13  ? 0.1593 0.3802 0.3053 -0.0840 0.0648  -0.1500 13  PRO A CB  
46   C  CG  . PRO A 13  ? 0.2039 0.2899 0.2499 -0.0876 0.0800  -0.0769 13  PRO A CG  
47   C  CD  . PRO A 13  ? 0.1576 0.2495 0.2055 -0.0156 0.0150  -0.0419 13  PRO A CD  
48   N  N   . GLU A 14  ? 0.1558 0.2215 0.2674 -0.0216 0.0514  -0.0188 14  GLU A N   
49   C  CA  . GLU A 14  ? 0.2425 0.1496 0.3337 -0.0018 -0.0127 0.0309  14  GLU A CA  
50   C  C   . GLU A 14  ? 0.1949 0.2229 0.2347 0.0261  0.0401  -0.0245 14  GLU A C   
51   O  O   . GLU A 14  ? 0.2262 0.2269 0.2818 0.0351  0.0255  0.0036  14  GLU A O   
52   C  CB  . GLU A 14  ? 0.2850 0.1763 0.4149 0.0156  -0.0200 0.0618  14  GLU A CB  
53   C  CG  . GLU A 14  ? 0.2955 0.2319 0.4970 0.0715  -0.0092 -0.0753 14  GLU A CG  
54   C  CD  . GLU A 14  ? 0.2526 0.3861 0.5909 0.0558  -0.0416 -0.1485 14  GLU A CD  
55   O  OE1 . GLU A 14  ? 0.2794 0.2393 0.4438 0.0751  -0.0524 -0.1129 14  GLU A OE1 
56   O  OE2 . GLU A 14  ? 0.5661 0.6035 0.7172 0.0723  0.1018  -0.3208 14  GLU A OE2 
57   N  N   . HIS A 15  ? 0.1410 0.2264 0.2315 0.0006  0.0272  -0.0256 15  HIS A N   
58   C  CA  . HIS A 15  ? 0.1360 0.2122 0.2233 0.0086  0.0376  -0.0342 15  HIS A CA  
59   C  C   . HIS A 15  ? 0.0794 0.2082 0.1949 0.0048  -0.0089 -0.0096 15  HIS A C   
60   O  O   . HIS A 15  ? 0.0865 0.2159 0.2499 -0.0124 0.0294  -0.0055 15  HIS A O   
61   C  CB  . HIS A 15  ? 0.1151 0.2507 0.2222 0.0475  0.0208  -0.0104 15  HIS A CB  
62   C  CG  . HIS A 15  ? 0.1553 0.2043 0.3263 0.0129  0.0612  0.0223  15  HIS A CG  
63   N  ND1 . HIS A 15  ? 0.1712 0.2468 0.2804 0.0555  0.0179  0.0436  15  HIS A ND1 
64   C  CD2 . HIS A 15  ? 0.1723 0.2296 0.3669 0.0337  0.0669  -0.0408 15  HIS A CD2 
65   C  CE1 . HIS A 15  ? 0.2513 0.2696 0.2685 0.0496  0.0542  0.0170  15  HIS A CE1 
66   N  NE2 . HIS A 15  ? 0.2145 0.2724 0.4185 0.0886  0.0127  -0.0494 15  HIS A NE2 
67   N  N   . TRP A 16  ? 0.0829 0.1991 0.2344 -0.0033 0.0174  0.0122  16  TRP A N   
68   C  CA  . TRP A 16  ? 0.0894 0.1923 0.2190 -0.0006 -0.0013 -0.0205 16  TRP A CA  
69   C  C   . TRP A 16  ? 0.0976 0.1955 0.2085 -0.0310 0.0077  0.0012  16  TRP A C   
70   O  O   . TRP A 16  ? 0.1041 0.1835 0.2504 -0.0336 0.0204  -0.0103 16  TRP A O   
71   C  CB  . TRP A 16  ? 0.0925 0.2426 0.2326 -0.0132 0.0075  -0.0194 16  TRP A CB  
72   C  CG  . TRP A 16  ? 0.1154 0.2483 0.2182 -0.0161 0.0392  -0.0184 16  TRP A CG  
73   C  CD1 . TRP A 16  ? 0.0967 0.3159 0.2214 -0.0030 0.0461  -0.0171 16  TRP A CD1 
74   C  CD2 . TRP A 16  ? 0.1122 0.2206 0.1712 -0.0089 0.0280  -0.0185 16  TRP A CD2 
75   N  NE1 . TRP A 16  ? 0.1144 0.4121 0.2641 0.0105  0.0368  -0.0543 16  TRP A NE1 
76   C  CE2 . TRP A 16  ? 0.1189 0.3162 0.1927 -0.0283 0.0212  -0.0289 16  TRP A CE2 
77   C  CE3 . TRP A 16  ? 0.1065 0.2018 0.2124 -0.0199 0.0417  -0.0326 16  TRP A CE3 
78   C  CZ2 . TRP A 16  ? 0.1098 0.3087 0.2261 -0.0138 0.0314  -0.0665 16  TRP A CZ2 
79   C  CZ3 . TRP A 16  ? 0.1207 0.2038 0.2057 -0.0418 0.0160  -0.0107 16  TRP A CZ3 
80   C  CH2 . TRP A 16  ? 0.1306 0.2831 0.2111 -0.0098 0.0533  -0.0528 16  TRP A CH2 
81   N  N   . HIS A 17  ? 0.1007 0.1870 0.2032 0.0152  0.0156  0.0000  17  HIS A N   
82   C  CA  . HIS A 17  ? 0.1296 0.2045 0.2014 -0.0270 0.0129  0.0128  17  HIS A CA  
83   C  C   . HIS A 17  ? 0.1312 0.2393 0.1901 -0.0377 0.0094  -0.0058 17  HIS A C   
84   O  O   . HIS A 17  ? 0.1117 0.2420 0.2640 -0.0140 0.0005  -0.0355 17  HIS A O   
85   C  CB  . HIS A 17  ? 0.1204 0.2236 0.1905 0.0148  0.0190  0.0086  17  HIS A CB  
86   C  CG  . HIS A 17  ? 0.1058 0.2307 0.2366 0.0042  0.0154  0.0420  17  HIS A CG  
87   N  ND1 . HIS A 17  ? 0.1312 0.2626 0.2498 0.0082  0.0110  0.0261  17  HIS A ND1 
88   C  CD2 . HIS A 17  ? 0.1680 0.2540 0.2261 0.0721  0.0186  0.0303  17  HIS A CD2 
89   C  CE1 . HIS A 17  ? 0.1357 0.3319 0.2855 0.0508  0.0033  0.0035  17  HIS A CE1 
90   N  NE2 . HIS A 17  ? 0.1454 0.2391 0.2444 0.0358  0.0142  0.0776  17  HIS A NE2 
91   N  N   . LYS A 18  ? 0.0901 0.2217 0.2463 -0.0039 0.0200  0.0289  18  LYS A N   
92   C  CA  . LYS A 18  ? 0.1159 0.2504 0.2583 -0.0168 0.0709  0.0451  18  LYS A CA  
93   C  C   . LYS A 18  ? 0.0883 0.2735 0.2681 -0.0611 0.0326  0.0311  18  LYS A C   
94   O  O   . LYS A 18  ? 0.1747 0.2967 0.4133 -0.1072 -0.0310 0.0904  18  LYS A O   
95   C  CB  . LYS A 18  ? 0.1235 0.2328 0.2608 -0.0085 0.0434  0.0475  18  LYS A CB  
96   C  CG  . LYS A 18  ? 0.1216 0.2853 0.2919 0.0831  0.0179  0.0352  18  LYS A CG  
97   C  CD  . LYS A 18  ? 0.1201 0.2592 0.2771 0.0227  0.0017  0.0172  18  LYS A CD  
98   C  CE  . LYS A 18  ? 0.1569 0.2041 0.2251 0.0317  0.0083  0.0121  18  LYS A CE  
99   N  NZ  . LYS A 18  ? 0.1490 0.2178 0.2301 0.0472  0.0252  0.0502  18  LYS A NZ  
100  N  N   . ASP A 19  ? 0.1147 0.2523 0.2709 -0.0118 0.0137  0.0414  19  ASP A N   
101  C  CA  . ASP A 19  ? 0.1314 0.2215 0.2618 -0.0425 0.0324  0.0211  19  ASP A CA  
102  C  C   . ASP A 19  ? 0.1198 0.2433 0.2606 -0.0385 0.0293  0.0290  19  ASP A C   
103  O  O   . ASP A 19  ? 0.1791 0.2143 0.3272 -0.0439 0.0353  0.0243  19  ASP A O   
104  C  CB  . ASP A 19  ? 0.2272 0.3118 0.2395 -0.0374 0.0227  0.0054  19  ASP A CB  
105  C  CG  . ASP A 19  ? 0.2799 0.4012 0.4060 -0.0636 0.1256  -0.1011 19  ASP A CG  
106  O  OD1 . ASP A 19  ? 0.3082 0.4675 0.4100 -0.0651 0.0883  0.1135  19  ASP A OD1 
107  O  OD2 . ASP A 19  ? 0.5448 0.4436 0.4520 -0.0435 0.2129  -0.0623 19  ASP A OD2 
108  N  N   . PHE A 20  ? 0.1052 0.1708 0.2393 -0.0441 0.0138  0.0046  20  PHE A N   
109  C  CA  . PHE A 20  ? 0.1013 0.2351 0.2319 -0.0018 -0.0043 0.0036  20  PHE A CA  
110  C  C   . PHE A 20  ? 0.1086 0.2039 0.2481 -0.0321 -0.0069 0.0252  20  PHE A C   
111  O  O   . PHE A 20  ? 0.1263 0.1927 0.2697 -0.0366 0.0430  0.0034  20  PHE A O   
112  C  CB  . PHE A 20  ? 0.1066 0.3161 0.2416 -0.0318 0.0037  0.0143  20  PHE A CB  
113  C  CG  . PHE A 20  ? 0.1452 0.3539 0.2906 -0.0545 0.0019  0.0875  20  PHE A CG  
114  C  CD1 . PHE A 20  ? 0.2189 0.3805 0.3782 -0.0809 -0.0344 0.1415  20  PHE A CD1 
115  C  CD2 . PHE A 20  ? 0.1339 0.3908 0.2505 -0.0486 -0.0174 0.1011  20  PHE A CD2 
116  C  CE1 . PHE A 20  ? 0.1626 0.4928 0.3190 -0.1305 -0.0372 0.0998  20  PHE A CE1 
117  C  CE2 . PHE A 20  ? 0.1490 0.5396 0.2921 -0.0518 0.0156  0.1685  20  PHE A CE2 
118  C  CZ  . PHE A 20  ? 0.1611 0.4935 0.2586 -0.0825 -0.0118 0.1625  20  PHE A CZ  
119  N  N   . PRO A 21  ? 0.1009 0.1975 0.2413 -0.0277 -0.0043 0.0231  21  PRO A N   
120  C  CA  . PRO A 21  ? 0.1092 0.2361 0.2391 -0.0613 -0.0228 0.0192  21  PRO A CA  
121  C  C   . PRO A 21  ? 0.1199 0.1540 0.2576 -0.0452 -0.0160 -0.0020 21  PRO A C   
122  O  O   . PRO A 21  ? 0.1196 0.1910 0.2456 -0.0271 -0.0051 -0.0082 21  PRO A O   
123  C  CB  . PRO A 21  ? 0.1122 0.2522 0.2991 -0.0621 -0.0061 -0.0245 21  PRO A CB  
124  C  CG  . PRO A 21  ? 0.3194 0.2409 0.3765 -0.1068 -0.1147 0.0753  21  PRO A CG  
125  C  CD  . PRO A 21  ? 0.1416 0.2222 0.3029 -0.0499 -0.0064 0.0528  21  PRO A CD  
126  N  N   . ILE A 22  ? 0.1063 0.1755 0.2470 -0.0240 0.0001  -0.0245 22  ILE A N   
127  C  CA  . ILE A 22  ? 0.1043 0.1327 0.2638 -0.0146 -0.0038 -0.0145 22  ILE A CA  
128  C  C   . ILE A 22  ? 0.1100 0.1345 0.2072 -0.0085 -0.0043 -0.0173 22  ILE A C   
129  O  O   . ILE A 22  ? 0.1153 0.1514 0.2121 -0.0220 0.0125  -0.0029 22  ILE A O   
130  C  CB  . ILE A 22  ? 0.1136 0.1406 0.2289 -0.0154 0.0046  -0.0023 22  ILE A CB  
131  C  CG1 . ILE A 22  ? 0.1174 0.1783 0.2877 -0.0157 0.0273  -0.0686 22  ILE A CG1 
132  C  CG2 . ILE A 22  ? 0.1504 0.1392 0.2449 -0.0468 -0.0288 -0.0084 22  ILE A CG2 
133  C  CD1 . ILE A 22  ? 0.2377 0.2427 0.3147 -0.0304 -0.0292 -0.0776 22  ILE A CD1 
134  N  N   . ALA A 23  ? 0.1190 0.1580 0.1996 -0.0019 -0.0061 -0.0352 23  ALA A N   
135  C  CA  . ALA A 23  ? 0.1306 0.1540 0.1895 -0.0203 0.0168  -0.0298 23  ALA A CA  
136  C  C   . ALA A 23  ? 0.1138 0.1571 0.1960 -0.0025 0.0006  -0.0153 23  ALA A C   
137  O  O   . ALA A 23  ? 0.1447 0.1368 0.2273 -0.0054 0.0108  -0.0149 23  ALA A O   
138  C  CB  . ALA A 23  ? 0.1145 0.1727 0.1949 0.0239  0.0175  -0.0206 23  ALA A CB  
139  N  N   . LYS A 24  ? 0.1305 0.1381 0.2042 0.0154  -0.0044 -0.0250 24  LYS A N   
140  C  CA  . LYS A 24  ? 0.1321 0.2362 0.1899 0.0239  -0.0291 -0.0298 24  LYS A CA  
141  C  C   . LYS A 24  ? 0.1385 0.2032 0.2383 0.0076  -0.0071 -0.0486 24  LYS A C   
142  O  O   . LYS A 24  ? 0.2036 0.2792 0.2390 -0.0172 -0.0147 -0.0144 24  LYS A O   
143  C  CB  . LYS A 24  ? 0.1393 0.2651 0.2406 0.0582  -0.0020 0.0220  24  LYS A CB  
144  C  CG  . LYS A 24  ? 0.1738 0.3114 0.2529 0.0772  0.0170  0.0162  24  LYS A CG  
145  C  CD  . LYS A 24  ? 0.1777 0.4126 0.4084 0.0996  0.0227  0.0530  24  LYS A CD  
146  C  CE  . LYS A 24  ? 0.3365 0.3120 0.3944 0.0816  0.0410  0.1096  24  LYS A CE  
147  N  NZ  . LYS A 24  ? 0.4870 0.3037 0.5605 0.1307  0.1437  0.1102  24  LYS A NZ  
148  N  N   . GLY A 25  ? 0.1472 0.1650 0.2284 0.0002  0.0197  -0.0270 25  GLY A N   
149  C  CA  . GLY A 25  ? 0.1204 0.2102 0.2305 -0.0113 0.0189  -0.0642 25  GLY A CA  
150  C  C   . GLY A 25  ? 0.1284 0.1754 0.1758 -0.0210 -0.0276 -0.0315 25  GLY A C   
151  O  O   . GLY A 25  ? 0.1414 0.1928 0.2039 -0.0316 -0.0084 -0.0189 25  GLY A O   
152  N  N   . GLU A 26  ? 0.1406 0.2163 0.1766 -0.0077 -0.0044 -0.0434 26  GLU A N   
153  C  CA  . GLU A 26  ? 0.1421 0.2851 0.1565 -0.0162 -0.0069 -0.0540 26  GLU A CA  
154  C  C   . GLU A 26  ? 0.1342 0.1672 0.1608 0.0036  -0.0142 -0.0479 26  GLU A C   
155  O  O   . GLU A 26  ? 0.1628 0.2448 0.1583 -0.0109 0.0017  -0.0250 26  GLU A O   
156  C  CB  . GLU A 26  ? 0.1802 0.3276 0.2358 -0.0367 -0.0314 -0.1324 26  GLU A CB  
157  C  CG  . GLU A 26  ? 0.2125 0.4799 0.3491 -0.0027 -0.1029 -0.1676 26  GLU A CG  
158  C  CD  . GLU A 26  ? 0.3996 0.5222 0.2583 -0.0078 -0.0479 -0.0620 26  GLU A CD  
159  O  OE1 . GLU A 26  ? 0.3728 0.5122 0.3942 -0.1223 -0.1120 -0.0107 26  GLU A OE1 
160  O  OE2 . GLU A 26  ? 0.3682 0.6328 0.4752 0.0853  -0.0980 -0.1030 26  GLU A OE2 
161  N  N   A ARG A 27  ? 0.1468 0.1221 0.1593 -0.0257 -0.0153 -0.0466 27  ARG A N   
162  N  N   B ARG A 27  ? 0.1314 0.1562 0.1600 -0.0015 -0.0023 -0.0397 27  ARG A N   
163  C  CA  A ARG A 27  ? 0.1224 0.1292 0.1389 0.0009  -0.0044 -0.0408 27  ARG A CA  
164  C  CA  B ARG A 27  ? 0.1196 0.1328 0.1474 0.0146  0.0018  -0.0271 27  ARG A CA  
165  C  C   A ARG A 27  ? 0.1098 0.1125 0.1359 -0.0018 0.0076  -0.0179 27  ARG A C   
166  C  C   B ARG A 27  ? 0.1280 0.1155 0.1522 0.0177  -0.0113 -0.0136 27  ARG A C   
167  O  O   A ARG A 27  ? 0.0928 0.1395 0.1520 -0.0031 0.0073  -0.0064 27  ARG A O   
168  O  O   B ARG A 27  ? 0.1467 0.0966 0.1770 0.0146  -0.0264 -0.0050 27  ARG A O   
169  C  CB  A ARG A 27  ? 0.2036 0.0847 0.1459 -0.0006 -0.0040 -0.0355 27  ARG A CB  
170  C  CB  B ARG A 27  ? 0.1500 0.1258 0.1914 0.0129  0.0205  -0.0116 27  ARG A CB  
171  C  CG  A ARG A 27  ? 0.1991 0.1338 0.1518 -0.0006 -0.0435 0.0275  27  ARG A CG  
172  C  CG  B ARG A 27  ? 0.1835 0.1515 0.2244 0.0329  0.0249  -0.0410 27  ARG A CG  
173  C  CD  A ARG A 27  ? 0.2474 0.1571 0.2011 0.0313  -0.0468 0.0158  27  ARG A CD  
174  C  CD  B ARG A 27  ? 0.2830 0.1093 0.2034 0.0078  0.0139  -0.0189 27  ARG A CD  
175  N  NE  A ARG A 27  ? 0.2429 0.0824 0.1860 -0.0044 0.0029  -0.0148 27  ARG A NE  
176  N  NE  B ARG A 27  ? 0.3195 0.1799 0.1910 0.0290  0.0355  -0.0543 27  ARG A NE  
177  C  CZ  A ARG A 27  ? 0.2434 0.0472 0.1567 0.0125  0.0207  -0.0195 27  ARG A CZ  
178  C  CZ  B ARG A 27  ? 0.2569 0.1285 0.2197 0.0414  0.0172  -0.0708 27  ARG A CZ  
179  N  NH1 A ARG A 27  ? 0.0632 0.1312 0.1280 0.0318  -0.0198 -0.1219 27  ARG A NH1 
180  N  NH1 B ARG A 27  ? 0.2512 0.2808 0.3741 0.0135  0.1056  -0.0973 27  ARG A NH1 
181  N  NH2 A ARG A 27  ? 0.1766 0.0806 0.2434 -0.0291 0.0431  -0.0723 27  ARG A NH2 
182  N  NH2 B ARG A 27  ? 0.3218 0.2840 0.2805 -0.0606 -0.0127 -0.1198 27  ARG A NH2 
183  N  N   . GLN A 28  ? 0.0969 0.1055 0.1377 -0.0060 0.0040  -0.0333 28  GLN A N   
184  C  CA  . GLN A 28  ? 0.1000 0.0982 0.1447 -0.0065 -0.0070 -0.0295 28  GLN A CA  
185  C  C   . GLN A 28  ? 0.1091 0.0657 0.1393 -0.0025 -0.0067 -0.0210 28  GLN A C   
186  O  O   . GLN A 28  ? 0.1247 0.1186 0.1420 -0.0166 -0.0008 0.0036  28  GLN A O   
187  C  CB  . GLN A 28  ? 0.0955 0.1181 0.1583 -0.0013 0.0120  -0.0156 28  GLN A CB  
188  C  CG  . GLN A 28  ? 0.1174 0.1101 0.1439 -0.0018 -0.0044 -0.0158 28  GLN A CG  
189  C  CD  . GLN A 28  ? 0.1083 0.1032 0.1464 0.0073  -0.0066 -0.0272 28  GLN A CD  
190  O  OE1 . GLN A 28  ? 0.1280 0.1053 0.1421 -0.0098 -0.0001 -0.0249 28  GLN A OE1 
191  N  NE2 . GLN A 28  ? 0.0998 0.0982 0.1970 -0.0042 0.0049  -0.0267 28  GLN A NE2 
192  N  N   . SER A 29  ? 0.0914 0.0803 0.1428 0.0023  0.0047  -0.0060 29  SER A N   
193  C  CA  . SER A 29  ? 0.0849 0.0754 0.1441 0.0064  0.0071  -0.0199 29  SER A CA  
194  C  C   . SER A 29  ? 0.0885 0.0680 0.1368 0.0116  0.0120  -0.0027 29  SER A C   
195  O  O   . SER A 29  ? 0.1210 0.0906 0.1398 -0.0074 0.0291  -0.0008 29  SER A O   
196  C  CB  . SER A 29  ? 0.1014 0.0736 0.1391 0.0189  0.0044  -0.0021 29  SER A CB  
197  O  OG  . SER A 29  ? 0.1116 0.0684 0.1526 -0.0012 0.0165  -0.0130 29  SER A OG  
198  N  N   . PRO A 30  ? 0.1059 0.0756 0.1198 -0.0055 0.0063  0.0000  30  PRO A N   
199  C  CA  . PRO A 30  ? 0.1081 0.0881 0.1230 -0.0187 0.0095  0.0093  30  PRO A CA  
200  C  C   . PRO A 30  ? 0.0970 0.0725 0.1349 -0.0001 0.0115  0.0011  30  PRO A C   
201  O  O   . PRO A 30  ? 0.1040 0.1120 0.1233 0.0040  0.0017  0.0055  30  PRO A O   
202  C  CB  . PRO A 30  ? 0.1009 0.0806 0.1355 -0.0034 0.0150  -0.0042 30  PRO A CB  
203  C  CG  . PRO A 30  ? 0.0948 0.0930 0.1479 -0.0147 0.0220  -0.0139 30  PRO A CG  
204  C  CD  . PRO A 30  ? 0.1136 0.0779 0.1324 -0.0076 0.0269  -0.0081 30  PRO A CD  
205  N  N   . VAL A 31  ? 0.1153 0.0921 0.1363 0.0026  0.0229  0.0139  31  VAL A N   
206  C  CA  . VAL A 31  ? 0.1252 0.0944 0.1298 -0.0038 0.0170  0.0161  31  VAL A CA  
207  C  C   . VAL A 31  ? 0.1117 0.1044 0.1330 0.0069  0.0121  0.0018  31  VAL A C   
208  O  O   . VAL A 31  ? 0.1183 0.0973 0.1540 -0.0053 0.0110  0.0122  31  VAL A O   
209  C  CB  . VAL A 31  ? 0.1194 0.0790 0.1452 0.0019  0.0081  -0.0031 31  VAL A CB  
210  C  CG1 . VAL A 31  ? 0.1702 0.1061 0.1461 -0.0294 0.0211  0.0074  31  VAL A CG1 
211  C  CG2 . VAL A 31  ? 0.1267 0.1223 0.1632 -0.0006 0.0177  -0.0019 31  VAL A CG2 
212  N  N   . ASP A 32  ? 0.1072 0.1054 0.1553 0.0080  0.0167  0.0226  32  ASP A N   
213  C  CA  . ASP A 32  ? 0.1460 0.0854 0.1536 0.0070  0.0305  0.0265  32  ASP A CA  
214  C  C   . ASP A 32  ? 0.1367 0.1045 0.1395 0.0026  0.0089  0.0154  32  ASP A C   
215  O  O   . ASP A 32  ? 0.1490 0.1400 0.1726 0.0176  -0.0019 0.0011  32  ASP A O   
216  C  CB  . ASP A 32  ? 0.1533 0.1037 0.1650 0.0106  0.0011  0.0351  32  ASP A CB  
217  C  CG  . ASP A 32  ? 0.1802 0.1389 0.1662 -0.0011 0.0200  0.0469  32  ASP A CG  
218  O  OD1 . ASP A 32  ? 0.1928 0.1050 0.1673 -0.0001 0.0023  0.0407  32  ASP A OD1 
219  O  OD2 . ASP A 32  ? 0.2483 0.1474 0.1679 -0.0144 0.0272  0.0429  32  ASP A OD2 
220  N  N   . ILE A 33  ? 0.1285 0.0900 0.1493 0.0120  0.0214  0.0240  33  ILE A N   
221  C  CA  . ILE A 33  ? 0.1362 0.1046 0.1817 0.0229  0.0323  0.0432  33  ILE A CA  
222  C  C   . ILE A 33  ? 0.1474 0.0980 0.1910 -0.0006 0.0359  0.0289  33  ILE A C   
223  O  O   . ILE A 33  ? 0.1676 0.1353 0.1995 -0.0168 0.0199  0.0485  33  ILE A O   
224  C  CB  . ILE A 33  ? 0.1423 0.1111 0.1865 0.0133  0.0333  0.0441  33  ILE A CB  
225  C  CG1 . ILE A 33  ? 0.1684 0.1151 0.1576 0.0075  0.0005  0.0569  33  ILE A CG1 
226  C  CG2 . ILE A 33  ? 0.1526 0.1326 0.2072 0.0350  0.0511  0.0414  33  ILE A CG2 
227  C  CD1 . ILE A 33  ? 0.1593 0.1492 0.2018 0.0407  -0.0088 0.0489  33  ILE A CD1 
228  N  N   . ASP A 34  ? 0.1662 0.1691 0.1650 0.0211  0.0355  0.0630  34  ASP A N   
229  C  CA  . ASP A 34  ? 0.1553 0.1752 0.1883 0.0099  0.0447  0.0759  34  ASP A CA  
230  C  C   . ASP A 34  ? 0.1822 0.1802 0.2032 0.0178  0.0665  0.0902  34  ASP A C   
231  O  O   . ASP A 34  ? 0.2393 0.1808 0.2250 0.0310  0.0622  0.0663  34  ASP A O   
232  C  CB  . ASP A 34  ? 0.2117 0.1949 0.2228 0.0323  0.0148  0.0533  34  ASP A CB  
233  C  CG  . ASP A 34  ? 0.3069 0.2118 0.2876 -0.0479 0.0072  0.0658  34  ASP A CG  
234  O  OD1 . ASP A 34  ? 0.3004 0.2075 0.2858 0.0518  0.0561  0.1243  34  ASP A OD1 
235  O  OD2 . ASP A 34  ? 0.5186 0.4415 0.3929 0.0019  -0.0798 0.2416  34  ASP A OD2 
236  N  N   . THR A 35  ? 0.1860 0.2093 0.2358 0.0582  0.0440  0.1195  35  THR A N   
237  C  CA  . THR A 35  ? 0.1761 0.2310 0.2947 0.0709  0.0650  0.1050  35  THR A CA  
238  C  C   . THR A 35  ? 0.2246 0.1790 0.3208 0.0345  0.0899  0.0629  35  THR A C   
239  O  O   . THR A 35  ? 0.2692 0.2633 0.2649 0.0904  0.0834  0.0531  35  THR A O   
240  C  CB  . THR A 35  ? 0.2025 0.3045 0.2713 0.0347  0.0552  0.1184  35  THR A CB  
241  O  OG1 . THR A 35  ? 0.2219 0.2955 0.2925 0.0078  0.0615  0.1439  35  THR A OG1 
242  C  CG2 . THR A 35  ? 0.2330 0.3471 0.2709 0.0999  0.0547  0.1588  35  THR A CG2 
243  N  N   . HIS A 36  ? 0.2776 0.1848 0.2477 0.0797  0.1326  0.1038  36  HIS A N   
244  C  CA  . HIS A 36  ? 0.3165 0.2343 0.2544 0.0687  0.1433  0.1216  36  HIS A CA  
245  C  C   . HIS A 36  ? 0.4082 0.3462 0.4375 0.0194  0.1561  -0.0391 36  HIS A C   
246  O  O   . HIS A 36  ? 0.9987 0.5439 0.3757 0.0245  0.2425  -0.0467 36  HIS A O   
247  C  CB  . HIS A 36  ? 0.3784 0.2373 0.2244 0.0908  0.1286  0.0922  36  HIS A CB  
248  C  CG  . HIS A 36  ? 0.4753 0.1928 0.2857 0.0917  -0.0282 0.0949  36  HIS A CG  
249  N  ND1 . HIS A 36  ? 0.5635 0.4451 0.3517 0.2092  -0.0958 -0.0461 36  HIS A ND1 
250  C  CD2 . HIS A 36  ? 0.4185 0.2131 0.2578 -0.0044 -0.0600 0.0798  36  HIS A CD2 
251  C  CE1 . HIS A 36  ? 0.3977 0.2557 0.2573 0.1421  0.0027  0.0578  36  HIS A CE1 
252  N  NE2 . HIS A 36  ? 0.5041 0.3168 0.2450 0.1404  0.0098  0.0380  36  HIS A NE2 
253  N  N   . THR A 37  ? 0.2902 0.1928 0.2792 0.1047  0.0907  0.0682  37  THR A N   
254  C  CA  . THR A 37  ? 0.3622 0.2604 0.2692 0.0886  0.1024  0.0537  37  THR A CA  
255  C  C   . THR A 37  ? 0.2994 0.3202 0.2099 0.0831  0.0326  0.0501  37  THR A C   
256  O  O   . THR A 37  ? 0.4406 0.2888 0.3195 0.0812  0.0084  0.0300  37  THR A O   
257  C  CB  . THR A 37  ? 0.3562 0.5590 0.2974 0.2127  0.0111  0.0815  37  THR A CB  
258  O  OG1 . THR A 37  ? 0.4475 0.4200 0.4026 0.1209  0.0593  0.1336  37  THR A OG1 
259  C  CG2 . THR A 37  ? 0.3474 0.4448 0.4880 0.1911  0.0353  0.0326  37  THR A CG2 
260  N  N   . ALA A 38  ? 0.2305 0.2068 0.2141 0.0534  0.0551  0.0691  38  ALA A N   
261  C  CA  . ALA A 38  ? 0.2968 0.2093 0.1985 0.1094  0.0642  0.0712  38  ALA A CA  
262  C  C   . ALA A 38  ? 0.2993 0.2205 0.3302 0.0741  0.0965  0.0915  38  ALA A C   
263  O  O   . ALA A 38  ? 0.4180 0.2708 0.4814 0.0578  0.2956  0.0785  38  ALA A O   
264  C  CB  . ALA A 38  ? 0.2103 0.2336 0.2359 0.0717  0.0657  0.0436  38  ALA A CB  
265  N  N   . LYS A 39  ? 0.3517 0.2578 0.2043 0.1110  0.0568  0.0762  39  LYS A N   
266  C  CA  . LYS A 39  ? 0.3887 0.3532 0.1996 0.1979  0.0204  0.0223  39  LYS A CA  
267  C  C   . LYS A 39  ? 0.2043 0.2238 0.1676 0.0549  0.0399  -0.0145 39  LYS A C   
268  O  O   . LYS A 39  ? 0.2045 0.2598 0.1486 0.0454  0.0290  0.0290  39  LYS A O   
269  C  CB  . LYS A 39  ? 0.5875 0.5276 0.2772 0.1535  -0.0716 -0.1406 39  LYS A CB  
270  C  CG  . LYS A 39  ? 0.8522 0.7991 0.3659 0.1870  -0.1628 0.1361  39  LYS A CG  
271  C  CD  . LYS A 39  ? 0.4201 0.7850 0.7413 0.3480  0.1599  -0.1065 39  LYS A CD  
272  C  CE  . LYS A 39  ? 0.6102 0.8646 0.7682 0.2283  -0.3981 0.4703  39  LYS A CE  
273  N  NZ  . LYS A 39  ? 0.4324 0.6724 0.5062 0.1592  0.0473  0.1259  39  LYS A NZ  
274  N  N   . TYR A 40  ? 0.2817 0.2555 0.1696 0.0155  0.0417  0.0071  40  TYR A N   
275  C  CA  . TYR A 40  ? 0.2581 0.2355 0.1762 -0.0097 0.0601  -0.0127 40  TYR A CA  
276  C  C   . TYR A 40  ? 0.2107 0.2380 0.1619 -0.0447 0.0543  -0.0134 40  TYR A C   
277  O  O   . TYR A 40  ? 0.2525 0.3025 0.1481 0.0458  0.0425  -0.0044 40  TYR A O   
278  C  CB  . TYR A 40  ? 0.3807 0.3201 0.1802 -0.1259 0.0572  0.0259  40  TYR A CB  
279  C  CG  . TYR A 40  ? 0.3227 0.6818 0.3890 -0.0925 0.0961  0.0574  40  TYR A CG  
280  C  CD1 . TYR A 40  ? 0.4237 0.4585 0.2557 -0.2306 0.1043  -0.0610 40  TYR A CD1 
281  C  CD2 . TYR A 40  ? 0.4787 0.6386 0.4644 0.0079  0.1486  -0.0302 40  TYR A CD2 
282  C  CE1 . TYR A 40  ? 0.5138 0.8305 0.6258 -0.0264 0.0219  -0.0031 40  TYR A CE1 
283  C  CE2 . TYR A 40  ? 1.3401 0.7217 0.7287 -0.3443 0.2928  -0.2615 40  TYR A CE2 
284  C  CZ  . TYR A 40  ? 0.4471 1.2692 0.8370 0.0058  0.1841  -0.2345 40  TYR A CZ  
285  O  OH  . TYR A 40  ? 0.3881 1.1961 0.3957 0.1747  0.1758  -0.1966 40  TYR A OH  
286  N  N   . ASP A 41  ? 0.1917 0.2274 0.1891 0.0055  0.0577  -0.0159 41  ASP A N   
287  C  CA  . ASP A 41  ? 0.2197 0.2115 0.2384 0.0267  -0.0380 -0.0054 41  ASP A CA  
288  C  C   . ASP A 41  ? 0.2709 0.3257 0.2653 0.1100  -0.0712 -0.0253 41  ASP A C   
289  O  O   . ASP A 41  ? 0.2806 0.3543 0.2253 0.0957  0.0241  0.0223  41  ASP A O   
290  C  CB  . ASP A 41  ? 0.2817 0.2103 0.2771 -0.0152 -0.0354 0.0132  41  ASP A CB  
291  C  CG  . ASP A 41  ? 0.3926 0.2634 0.3508 -0.0502 -0.0971 -0.0556 41  ASP A CG  
292  O  OD1 . ASP A 41  ? 0.4539 0.3450 0.3079 0.0447  -0.0815 -0.0813 41  ASP A OD1 
293  O  OD2 . ASP A 41  ? 0.3341 0.3565 0.4940 -0.0917 -0.1333 0.0456  41  ASP A OD2 
294  N  N   . PRO A 42  ? 0.4569 0.6967 0.2811 -0.0278 -0.0993 0.1673  42  PRO A N   
295  C  CA  . PRO A 42  ? 0.5059 0.5590 0.1978 -0.0421 0.1118  0.0307  42  PRO A CA  
296  C  C   . PRO A 42  ? 0.4923 0.6028 0.2713 0.0978  0.1408  0.0273  42  PRO A C   
297  O  O   . PRO A 42  ? 0.6352 0.9741 0.4838 0.0985  -0.1415 0.2444  42  PRO A O   
298  C  CB  . PRO A 42  ? 0.5067 0.8681 0.2724 0.0380  0.1316  0.0945  42  PRO A CB  
299  C  CG  . PRO A 42  ? 0.7853 0.8235 0.3844 0.0607  -0.1802 0.0944  42  PRO A CG  
300  C  CD  . PRO A 42  ? 0.6062 0.6418 0.3682 0.3571  -0.0747 0.2378  42  PRO A CD  
301  N  N   . SER A 43  ? 0.5192 0.3182 0.2488 0.2046  0.0443  -0.0298 43  SER A N   
302  C  CA  . SER A 43  ? 0.7289 0.2512 0.2800 0.0949  0.0167  -0.0823 43  SER A CA  
303  C  C   . SER A 43  ? 0.6322 0.5835 0.2612 0.2610  0.0114  -0.0170 43  SER A C   
304  O  O   . SER A 43  ? 0.7364 0.5704 0.4871 0.2996  -0.0671 -0.0359 43  SER A O   
305  C  CB  . SER A 43  ? 0.6849 0.6010 0.4592 0.0639  -0.0383 -0.1682 43  SER A CB  
306  O  OG  . SER A 43  ? 0.6613 0.3328 0.4424 0.0356  -0.0690 -0.1007 43  SER A OG  
307  N  N   . LEU A 44  ? 0.4290 0.5662 0.2595 0.1858  -0.0217 -0.0133 44  LEU A N   
308  C  CA  . LEU A 44  ? 0.3380 0.5427 0.2874 0.0443  0.0055  0.0721  44  LEU A CA  
309  C  C   . LEU A 44  ? 0.2892 0.5879 0.6052 0.0708  -0.0018 0.1381  44  LEU A C   
310  O  O   . LEU A 44  ? 0.2588 0.8971 0.3738 -0.0229 0.0580  0.1828  44  LEU A O   
311  C  CB  . LEU A 44  ? 0.1887 0.5774 0.2247 -0.0391 -0.0094 0.0458  44  LEU A CB  
312  C  CG  . LEU A 44  ? 0.2011 0.3271 0.2280 -0.0488 -0.0023 0.0486  44  LEU A CG  
313  C  CD1 . LEU A 44  ? 0.3420 0.3310 0.1784 -0.1162 0.0374  0.0040  44  LEU A CD1 
314  C  CD2 . LEU A 44  ? 0.2793 0.2298 0.2447 -0.0535 0.0152  0.0128  44  LEU A CD2 
315  N  N   . LYS A 45  ? 0.3044 0.6433 0.3709 0.1227  0.0168  0.1298  45  LYS A N   
316  C  CA  . LYS A 45  ? 0.3037 0.4501 0.4361 0.0690  -0.0422 -0.0320 45  LYS A CA  
317  C  C   . LYS A 45  ? 0.2427 0.5305 0.2444 0.0902  0.0651  -0.0467 45  LYS A C   
318  O  O   . LYS A 45  ? 0.2643 0.5094 0.2722 0.1143  0.0210  0.0105  45  LYS A O   
319  C  CB  . LYS A 45  ? 0.2754 0.4323 0.3998 0.1393  -0.0848 -0.0674 45  LYS A CB  
320  C  CG  . LYS A 45  ? 0.5550 0.4459 0.5249 -0.0080 -0.0601 -0.1052 45  LYS A CG  
321  C  CD  . LYS A 45  ? 0.6671 0.5460 0.6945 0.1904  -0.2013 -0.1577 45  LYS A CD  
322  N  N   . PRO A 46  ? 0.2922 0.2841 0.3344 0.1091  0.0704  -0.0080 46  PRO A N   
323  C  CA  . PRO A 46  ? 0.2125 0.5401 0.3691 -0.1324 0.0665  -0.0133 46  PRO A CA  
324  C  C   . PRO A 46  ? 0.3217 0.2948 0.4280 -0.0270 -0.0907 0.1164  46  PRO A C   
325  O  O   . PRO A 46  ? 0.2167 0.4343 0.3501 -0.0020 0.0263  0.0842  46  PRO A O   
326  C  CB  . PRO A 46  ? 0.1007 0.7747 0.4936 -0.0958 0.1876  0.0857  46  PRO A CB  
327  C  CG  . PRO A 46  ? 0.3800 0.6016 0.5383 -0.1161 0.0164  0.2184  46  PRO A CG  
328  C  CD  . PRO A 46  ? 0.2808 0.5077 0.4070 0.1658  0.0913  -0.0906 46  PRO A CD  
329  N  N   . LEU A 47  ? 0.1092 0.4593 0.2541 -0.0429 0.0200  0.0872  47  LEU A N   
330  C  CA  . LEU A 47  ? 0.1959 0.3695 0.2810 -0.0060 0.0116  0.0981  47  LEU A CA  
331  C  C   . LEU A 47  ? 0.1630 0.1971 0.3485 -0.0026 -0.0170 0.0844  47  LEU A C   
332  O  O   . LEU A 47  ? 0.1895 0.2738 0.3945 -0.0490 -0.0482 0.1326  47  LEU A O   
333  C  CB  . LEU A 47  ? 0.3037 0.2669 0.4276 -0.0791 0.0444  -0.0425 47  LEU A CB  
334  C  CG  . LEU A 47  ? 0.2889 0.3750 0.3193 -0.0515 0.0162  0.0269  47  LEU A CG  
335  C  CD1 . LEU A 47  ? 0.2251 0.3269 0.4141 -0.0075 -0.0097 -0.0369 47  LEU A CD1 
336  C  CD2 . LEU A 47  ? 0.2194 0.2406 0.5265 -0.1152 -0.1170 0.0851  47  LEU A CD2 
337  N  N   . SER A 48  ? 0.1330 0.1817 0.2468 0.0059  0.0102  0.0419  48  SER A N   
338  C  CA  . SER A 48  ? 0.1280 0.1902 0.2140 0.0033  0.0151  0.0243  48  SER A CA  
339  C  C   . SER A 48  ? 0.1342 0.2063 0.2014 -0.0171 0.0016  0.0322  48  SER A C   
340  O  O   . SER A 48  ? 0.1464 0.2138 0.2588 -0.0429 0.0526  -0.0079 48  SER A O   
341  C  CB  . SER A 48  ? 0.1813 0.1747 0.2893 0.0527  0.0513  0.0502  48  SER A CB  
342  O  OG  . SER A 48  ? 0.2120 0.2319 0.3793 0.0496  0.0114  0.0664  48  SER A OG  
343  N  N   . VAL A 49  ? 0.1544 0.2251 0.1993 -0.0353 0.0198  0.0260  49  VAL A N   
344  C  CA  . VAL A 49  ? 0.2219 0.2024 0.2097 -0.0723 0.0528  -0.0231 49  VAL A CA  
345  C  C   . VAL A 49  ? 0.2050 0.2284 0.2670 -0.0939 0.0452  -0.0004 49  VAL A C   
346  O  O   . VAL A 49  ? 0.2654 0.3379 0.2665 -0.1590 0.0335  -0.0271 49  VAL A O   
347  C  CB  . VAL A 49  ? 0.2951 0.1975 0.2659 -0.0449 0.0655  -0.0468 49  VAL A CB  
348  C  CG1 . VAL A 49  ? 0.4338 0.3181 0.3001 -0.1057 0.1511  -0.0467 49  VAL A CG1 
349  C  CG2 . VAL A 49  ? 0.2714 0.2029 0.3225 -0.0324 0.0540  -0.0096 49  VAL A CG2 
350  N  N   A SER A 50  ? 0.2292 0.1806 0.1806 0.0062  0.0550  -0.0192 50  SER A N   
351  N  N   B SER A 50  ? 0.1478 0.1891 0.2601 -0.0342 0.0480  -0.0106 50  SER A N   
352  C  CA  A SER A 50  ? 0.1765 0.2034 0.2354 -0.0159 0.0245  -0.0234 50  SER A CA  
353  C  CA  B SER A 50  ? 0.1716 0.1960 0.2666 -0.0347 0.0152  -0.0278 50  SER A CA  
354  C  C   A SER A 50  ? 0.1374 0.2177 0.2352 -0.0141 0.0053  -0.0013 50  SER A C   
355  C  C   B SER A 50  ? 0.1307 0.2201 0.2639 -0.0184 -0.0004 -0.0113 50  SER A C   
356  O  O   A SER A 50  ? 0.1625 0.2233 0.2703 -0.0435 0.0138  0.0006  50  SER A O   
357  O  O   B SER A 50  ? 0.1682 0.2278 0.2661 -0.0423 0.0175  0.0049  50  SER A O   
358  C  CB  A SER A 50  ? 0.2400 0.1896 0.2377 0.0151  0.0190  0.0149  50  SER A CB  
359  C  CB  B SER A 50  ? 0.2868 0.2418 0.3729 0.0168  0.0623  -0.0741 50  SER A CB  
360  O  OG  A SER A 50  ? 0.2206 0.2611 0.2617 0.0450  0.0425  -0.0266 50  SER A OG  
361  O  OG  B SER A 50  ? 0.2996 0.1935 0.4565 0.0182  0.0588  -0.0707 50  SER A OG  
362  N  N   . TYR A 51  ? 0.1571 0.2312 0.2448 -0.0201 0.0125  -0.0306 51  TYR A N   
363  C  CA  . TYR A 51  ? 0.1535 0.1775 0.2286 -0.0039 0.0111  0.0201  51  TYR A CA  
364  C  C   . TYR A 51  ? 0.1474 0.1845 0.2675 -0.0050 -0.0043 0.0463  51  TYR A C   
365  O  O   . TYR A 51  ? 0.2043 0.2690 0.2523 -0.0146 0.0044  0.0287  51  TYR A O   
366  C  CB  . TYR A 51  ? 0.1585 0.1860 0.2618 0.0189  -0.0186 0.0063  51  TYR A CB  
367  C  CG  . TYR A 51  ? 0.1544 0.1543 0.1984 -0.0118 -0.0016 0.0240  51  TYR A CG  
368  C  CD1 . TYR A 51  ? 0.1441 0.1740 0.2311 -0.0139 0.0287  -0.0153 51  TYR A CD1 
369  C  CD2 . TYR A 51  ? 0.1271 0.1405 0.2038 -0.0209 0.0407  0.0085  51  TYR A CD2 
370  C  CE1 . TYR A 51  ? 0.1587 0.1216 0.2199 -0.0032 0.0266  0.0150  51  TYR A CE1 
371  C  CE2 . TYR A 51  ? 0.1579 0.1319 0.1942 -0.0309 0.0061  -0.0141 51  TYR A CE2 
372  C  CZ  . TYR A 51  ? 0.1450 0.1142 0.2096 -0.0346 0.0078  0.0038  51  TYR A CZ  
373  O  OH  . TYR A 51  ? 0.1460 0.1331 0.2212 -0.0130 -0.0012 -0.0102 51  TYR A OH  
374  N  N   A ASP A 52  ? 0.1737 0.2568 0.2978 0.0080  0.0322  0.0279  52  ASP A N   
375  N  N   B ASP A 52  ? 0.1561 0.2427 0.3423 0.0127  -0.0017 0.0428  52  ASP A N   
376  C  CA  A ASP A 52  ? 0.1486 0.2485 0.3382 0.0053  0.0366  0.0765  52  ASP A CA  
377  C  CA  B ASP A 52  ? 0.1919 0.2429 0.3794 0.0212  -0.0162 0.1218  52  ASP A CA  
378  C  C   A ASP A 52  ? 0.2746 0.2160 0.3080 0.0013  -0.0035 0.0533  52  ASP A C   
379  C  C   B ASP A 52  ? 0.1382 0.2066 0.3637 0.0710  0.0171  0.0555  52  ASP A C   
380  O  O   A ASP A 52  ? 0.2147 0.3569 0.3312 0.0571  -0.0322 0.0612  52  ASP A O   
381  O  O   B ASP A 52  ? 0.1837 0.4202 0.3523 0.0395  -0.0181 0.0507  52  ASP A O   
382  C  CB  A ASP A 52  ? 0.1610 0.3531 0.2639 0.0390  0.0172  0.0212  52  ASP A CB  
383  C  CB  B ASP A 52  ? 0.1939 0.4176 0.4058 0.0697  -0.0052 0.0869  52  ASP A CB  
384  C  CG  A ASP A 52  ? 0.2867 0.2814 0.4772 -0.0015 0.1050  -0.0507 52  ASP A CG  
385  C  CG  B ASP A 52  ? 0.2791 0.4411 0.3792 0.0381  -0.0452 0.0666  52  ASP A CG  
386  O  OD1 A ASP A 52  ? 0.4088 0.4517 0.5147 0.0410  0.0900  -0.0275 52  ASP A OD1 
387  O  OD1 B ASP A 52  ? 0.4354 0.5174 0.4017 0.1215  0.0262  0.0005  52  ASP A OD1 
388  O  OD2 A ASP A 52  ? 0.3855 0.4288 0.5777 0.0696  -0.0729 0.0715  52  ASP A OD2 
389  O  OD2 B ASP A 52  ? 0.4559 0.4875 0.4866 0.2913  0.1218  -0.0894 52  ASP A OD2 
390  N  N   . GLN A 53  ? 0.1637 0.2391 0.4231 0.0258  0.0440  0.0665  53  GLN A N   
391  C  CA  . GLN A 53  ? 0.1974 0.2170 0.5001 0.0197  0.0864  0.0647  53  GLN A CA  
392  C  C   . GLN A 53  ? 0.1921 0.1626 0.3551 0.0085  0.0538  0.0243  53  GLN A C   
393  O  O   . GLN A 53  ? 0.2401 0.1722 0.3736 0.0031  0.0234  0.0420  53  GLN A O   
394  C  CB  . GLN A 53  ? 0.3571 0.1993 0.5859 0.1123  0.1320  0.0422  53  GLN A CB  
395  C  CG  . GLN A 53  ? 0.3444 0.4569 0.7497 0.0976  0.1727  0.0387  53  GLN A CG  
396  C  CD  . GLN A 53  ? 0.6107 0.6753 1.0508 0.2888  -0.0346 0.2058  53  GLN A CD  
397  O  OE1 . GLN A 53  ? 0.7291 0.9368 0.9943 0.0317  -0.1404 0.3926  53  GLN A OE1 
398  N  NE2 . GLN A 53  ? 0.5422 0.4390 1.4627 0.1556  0.0803  0.2460  53  GLN A NE2 
399  N  N   . ALA A 54  ? 0.1607 0.1565 0.3599 0.0199  0.0269  0.0060  54  ALA A N   
400  C  CA  . ALA A 54  ? 0.1629 0.1538 0.2593 0.0312  0.0471  0.0038  54  ALA A CA  
401  C  C   . ALA A 54  ? 0.2157 0.1747 0.2722 0.0024  0.0218  -0.0189 54  ALA A C   
402  O  O   . ALA A 54  ? 0.1833 0.3000 0.3454 -0.0185 -0.0047 -0.0746 54  ALA A O   
403  C  CB  . ALA A 54  ? 0.2011 0.1386 0.3368 0.0111  0.0177  0.0277  54  ALA A CB  
404  N  N   . THR A 55  ? 0.1759 0.1278 0.2462 0.0378  0.0164  0.0552  55  THR A N   
405  C  CA  . THR A 55  ? 0.1776 0.1625 0.2351 0.0464  -0.0106 0.0579  55  THR A CA  
406  C  C   . THR A 55  ? 0.1568 0.1353 0.1808 0.0126  -0.0211 0.0107  55  THR A C   
407  O  O   . THR A 55  ? 0.1729 0.1141 0.2071 0.0050  -0.0282 0.0358  55  THR A O   
408  C  CB  . THR A 55  ? 0.2598 0.1468 0.3676 0.0699  -0.0069 0.0506  55  THR A CB  
409  O  OG1 . THR A 55  ? 0.2940 0.2682 0.5805 0.0702  -0.0825 -0.0770 55  THR A OG1 
410  C  CG2 . THR A 55  ? 0.3754 0.2546 0.3987 0.0705  -0.0322 0.1137  55  THR A CG2 
411  N  N   . SER A 56  ? 0.1533 0.1137 0.1816 0.0125  -0.0189 0.0251  56  SER A N   
412  C  CA  . SER A 56  ? 0.1328 0.1077 0.1626 -0.0053 -0.0058 0.0189  56  SER A CA  
413  C  C   . SER A 56  ? 0.1808 0.1307 0.1905 0.0062  0.0061  0.0248  56  SER A C   
414  O  O   . SER A 56  ? 0.2085 0.1298 0.2030 0.0158  -0.0221 0.0423  56  SER A O   
415  C  CB  . SER A 56  ? 0.1901 0.1156 0.1740 -0.0097 -0.0387 -0.0104 56  SER A CB  
416  O  OG  . SER A 56  ? 0.1949 0.1341 0.1999 -0.0329 -0.0432 0.0359  56  SER A OG  
417  N  N   . LEU A 57  ? 0.1672 0.1020 0.1650 0.0065  0.0087  0.0282  57  LEU A N   
418  C  CA  . LEU A 57  ? 0.2301 0.1013 0.2048 0.0080  0.0556  0.0249  57  LEU A CA  
419  C  C   . LEU A 57  ? 0.1808 0.1585 0.1708 0.0402  0.0300  0.0325  57  LEU A C   
420  O  O   . LEU A 57  ? 0.2093 0.1385 0.1759 0.0286  -0.0130 0.0060  57  LEU A O   
421  C  CB  . LEU A 57  ? 0.2213 0.1178 0.2755 0.0103  0.0416  0.0111  57  LEU A CB  
422  C  CG  . LEU A 57  ? 0.2968 0.1335 0.3049 0.0138  0.0873  -0.0042 57  LEU A CG  
423  C  CD1 . LEU A 57  ? 0.2990 0.1465 0.3856 -0.0620 0.1003  -0.0238 57  LEU A CD1 
424  C  CD2 . LEU A 57  ? 0.3439 0.2032 0.4615 0.1121  0.0993  0.0547  57  LEU A CD2 
425  N  N   . ARG A 58  ? 0.2089 0.1562 0.1619 0.0430  -0.0163 -0.0013 58  ARG A N   
426  C  CA  . ARG A 58  ? 0.1694 0.0988 0.1744 0.0189  0.0048  0.0423  58  ARG A CA  
427  C  C   . ARG A 58  ? 0.1949 0.1068 0.1558 0.0139  -0.0113 0.0214  58  ARG A C   
428  O  O   . ARG A 58  ? 0.2365 0.1623 0.1355 0.0489  -0.0030 -0.0019 58  ARG A O   
429  C  CB  . ARG A 58  ? 0.2463 0.1012 0.2490 0.0071  0.0374  0.0407  58  ARG A CB  
430  C  CG  . ARG A 58  ? 0.2718 0.1822 0.2179 -0.0065 0.0599  0.0463  58  ARG A CG  
431  C  CD  . ARG A 58  ? 0.2795 0.2296 0.2933 -0.0261 -0.0436 0.0836  58  ARG A CD  
432  N  NE  . ARG A 58  ? 0.1991 0.1723 0.2567 -0.0281 0.0131  0.0157  58  ARG A NE  
433  C  CZ  . ARG A 58  ? 0.1837 0.1797 0.2233 -0.0555 0.0387  0.0131  58  ARG A CZ  
434  N  NH1 . ARG A 58  ? 0.2881 0.1806 0.2545 -0.0569 0.0715  0.0328  58  ARG A NH1 
435  N  NH2 . ARG A 58  ? 0.2307 0.1285 0.2370 -0.0234 0.0608  -0.0100 58  ARG A NH2 
436  N  N   . ILE A 59  ? 0.1813 0.0882 0.1389 0.0135  0.0087  0.0204  59  ILE A N   
437  C  CA  . ILE A 59  ? 0.1659 0.0818 0.1465 0.0095  0.0032  0.0244  59  ILE A CA  
438  C  C   . ILE A 59  ? 0.1604 0.1178 0.1183 0.0181  0.0008  0.0042  59  ILE A C   
439  O  O   . ILE A 59  ? 0.1905 0.1506 0.1265 0.0286  0.0087  0.0206  59  ILE A O   
440  C  CB  . ILE A 59  ? 0.1845 0.0882 0.1368 0.0035  -0.0132 0.0271  59  ILE A CB  
441  C  CG1 . ILE A 59  ? 0.1878 0.0776 0.1468 0.0031  0.0039  0.0381  59  ILE A CG1 
442  C  CG2 . ILE A 59  ? 0.2082 0.1109 0.1453 -0.0069 -0.0174 0.0310  59  ILE A CG2 
443  C  CD1 . ILE A 59  ? 0.2289 0.0838 0.1881 -0.0146 0.0023  0.0084  59  ILE A CD1 
444  N  N   . LEU A 60  ? 0.1486 0.1058 0.1503 -0.0046 -0.0024 0.0188  60  LEU A N   
445  C  CA  . LEU A 60  ? 0.1289 0.0971 0.1402 0.0027  0.0035  0.0198  60  LEU A CA  
446  C  C   . LEU A 60  ? 0.1436 0.0873 0.1468 -0.0086 0.0170  0.0178  60  LEU A C   
447  O  O   . LEU A 60  ? 0.1671 0.1122 0.1367 -0.0076 0.0190  0.0216  60  LEU A O   
448  C  CB  . LEU A 60  ? 0.1583 0.1077 0.1989 -0.0166 -0.0009 0.0094  60  LEU A CB  
449  C  CG  . LEU A 60  ? 0.1680 0.1465 0.1615 -0.0429 0.0144  -0.0134 60  LEU A CG  
450  C  CD1 . LEU A 60  ? 0.2011 0.1357 0.1823 -0.0291 0.0401  0.0136  60  LEU A CD1 
451  C  CD2 . LEU A 60  ? 0.1745 0.1170 0.2131 -0.0108 -0.0190 -0.0149 60  LEU A CD2 
452  N  N   . ASN A 61  ? 0.1400 0.0889 0.1538 0.0013  0.0146  0.0044  61  ASN A N   
453  C  CA  . ASN A 61  ? 0.1612 0.1164 0.1226 0.0051  0.0049  -0.0006 61  ASN A CA  
454  C  C   . ASN A 61  ? 0.1425 0.1021 0.1497 -0.0127 0.0329  0.0193  61  ASN A C   
455  O  O   . ASN A 61  ? 0.1640 0.1043 0.1632 -0.0136 0.0430  0.0170  61  ASN A O   
456  C  CB  . ASN A 61  ? 0.1806 0.0917 0.1409 0.0164  0.0223  0.0051  61  ASN A CB  
457  C  CG  . ASN A 61  ? 0.1635 0.0791 0.1371 0.0035  0.0197  0.0098  61  ASN A CG  
458  O  OD1 . ASN A 61  ? 0.1783 0.1037 0.1528 -0.0020 0.0254  0.0215  61  ASN A OD1 
459  N  ND2 . ASN A 61  ? 0.2050 0.0908 0.1414 -0.0195 0.0425  0.0036  61  ASN A ND2 
460  N  N   . THR A 62  ? 0.1418 0.0876 0.1546 -0.0066 0.0106  0.0066  62  THR A N   
461  C  CA  . THR A 62  ? 0.1535 0.0838 0.1655 -0.0086 0.0108  0.0046  62  THR A CA  
462  C  C   . THR A 62  ? 0.1521 0.1102 0.1880 -0.0294 0.0414  0.0072  62  THR A C   
463  O  O   . THR A 62  ? 0.1790 0.1380 0.2892 -0.0409 0.0212  0.0189  62  THR A O   
464  C  CB  . THR A 62  ? 0.1817 0.0942 0.1650 -0.0129 0.0184  0.0140  62  THR A CB  
465  O  OG1 . THR A 62  ? 0.2009 0.0867 0.1720 -0.0040 0.0234  0.0023  62  THR A OG1 
466  C  CG2 . THR A 62  ? 0.1885 0.1327 0.1658 -0.0013 0.0230  0.0006  62  THR A CG2 
467  N  N   . GLY A 63  ? 0.1650 0.1204 0.1421 0.0096  0.0428  0.0091  63  GLY A N   
468  C  CA  . GLY A 63  ? 0.1445 0.1317 0.1374 -0.0049 0.0274  0.0212  63  GLY A CA  
469  C  C   . GLY A 63  ? 0.1579 0.0953 0.1565 -0.0181 0.0500  0.0148  63  GLY A C   
470  O  O   . GLY A 63  ? 0.1852 0.1393 0.1993 0.0247  0.0533  0.0273  63  GLY A O   
471  N  N   . TYR A 64  ? 0.1558 0.1176 0.1150 -0.0211 0.0339  0.0089  64  TYR A N   
472  C  CA  . TYR A 64  ? 0.1368 0.1492 0.1181 -0.0266 0.0193  0.0198  64  TYR A CA  
473  C  C   . TYR A 64  ? 0.1328 0.0973 0.1324 -0.0114 0.0253  0.0193  64  TYR A C   
474  O  O   . TYR A 64  ? 0.1492 0.1095 0.1960 0.0020  0.0451  0.0407  64  TYR A O   
475  C  CB  . TYR A 64  ? 0.1701 0.1382 0.1489 -0.0324 -0.0017 0.0066  64  TYR A CB  
476  C  CG  . TYR A 64  ? 0.2118 0.1707 0.1576 0.0025  0.0158  0.0136  64  TYR A CG  
477  C  CD1 . TYR A 64  ? 0.2341 0.1307 0.2154 -0.0020 -0.0013 0.0306  64  TYR A CD1 
478  C  CD2 . TYR A 64  ? 0.1719 0.1467 0.1951 -0.0289 0.0325  -0.0136 64  TYR A CD2 
479  C  CE1 . TYR A 64  ? 0.1637 0.1747 0.2055 -0.0105 0.0166  0.0398  64  TYR A CE1 
480  C  CE2 . TYR A 64  ? 0.2100 0.1196 0.2186 -0.0279 0.0216  -0.0227 64  TYR A CE2 
481  C  CZ  . TYR A 64  ? 0.1661 0.1482 0.2188 -0.0664 0.0093  0.0255  64  TYR A CZ  
482  O  OH  . TYR A 64  ? 0.2151 0.1955 0.2009 -0.0732 0.0139  0.0011  64  TYR A OH  
483  N  N   . LEU A 65  ? 0.1353 0.0818 0.1599 -0.0156 0.0256  0.0116  65  LEU A N   
484  C  CA  . LEU A 65  ? 0.1332 0.0874 0.1339 -0.0030 0.0217  0.0070  65  LEU A CA  
485  C  C   . LEU A 65  ? 0.1561 0.0889 0.1117 -0.0034 0.0159  0.0062  65  LEU A C   
486  O  O   . LEU A 65  ? 0.1418 0.0944 0.1375 -0.0073 0.0193  0.0151  65  LEU A O   
487  C  CB  . LEU A 65  ? 0.1673 0.0892 0.1210 -0.0196 0.0207  -0.0051 65  LEU A CB  
488  C  CG  . LEU A 65  ? 0.1102 0.1117 0.1262 0.0051  0.0081  -0.0189 65  LEU A CG  
489  C  CD1 . LEU A 65  ? 0.1464 0.0958 0.1866 0.0144  -0.0042 -0.0400 65  LEU A CD1 
490  C  CD2 . LEU A 65  ? 0.1346 0.1560 0.1472 -0.0326 0.0282  -0.0089 65  LEU A CD2 
491  N  N   . PHE A 66  ? 0.1402 0.0644 0.1409 -0.0095 0.0097  -0.0033 66  PHE A N   
492  C  CA  . PHE A 66  ? 0.1374 0.1101 0.1110 0.0027  0.0142  0.0037  66  PHE A CA  
493  C  C   . PHE A 66  ? 0.1490 0.0993 0.1146 0.0048  0.0003  0.0004  66  PHE A C   
494  O  O   . PHE A 66  ? 0.1310 0.1095 0.1288 -0.0078 0.0048  0.0023  66  PHE A O   
495  C  CB  . PHE A 66  ? 0.1508 0.1188 0.1274 -0.0239 0.0047  -0.0025 66  PHE A CB  
496  C  CG  . PHE A 66  ? 0.1763 0.0944 0.1278 -0.0199 0.0148  -0.0105 66  PHE A CG  
497  C  CD1 . PHE A 66  ? 0.1474 0.1558 0.1439 -0.0301 0.0001  -0.0089 66  PHE A CD1 
498  C  CD2 . PHE A 66  ? 0.1791 0.1025 0.1483 -0.0267 -0.0097 0.0116  66  PHE A CD2 
499  C  CE1 . PHE A 66  ? 0.1727 0.0944 0.1913 -0.0175 -0.0209 0.0172  66  PHE A CE1 
500  C  CE2 . PHE A 66  ? 0.1793 0.0725 0.1574 -0.0134 -0.0078 -0.0111 66  PHE A CE2 
501  C  CZ  . PHE A 66  ? 0.2007 0.1109 0.1479 0.0089  -0.0245 0.0182  66  PHE A CZ  
502  N  N   . GLN A 67  ? 0.1482 0.1032 0.1490 0.0218  -0.0019 0.0091  67  GLN A N   
503  C  CA  . GLN A 67  ? 0.1321 0.0815 0.1715 0.0282  -0.0114 -0.0075 67  GLN A CA  
504  C  C   . GLN A 67  ? 0.1274 0.1028 0.1172 0.0027  0.0103  0.0063  67  GLN A C   
505  O  O   . GLN A 67  ? 0.1729 0.1628 0.1292 0.0190  0.0290  0.0157  67  GLN A O   
506  C  CB  . GLN A 67  ? 0.1414 0.1082 0.1860 -0.0287 0.0121  0.0083  67  GLN A CB  
507  C  CG  . GLN A 67  ? 0.1848 0.0943 0.1641 -0.0337 0.0052  0.0076  67  GLN A CG  
508  C  CD  . GLN A 67  ? 0.1626 0.1068 0.2289 -0.0217 0.0284  -0.0105 67  GLN A CD  
509  O  OE1 . GLN A 67  ? 0.1769 0.1623 0.2170 -0.0015 0.0134  -0.0118 67  GLN A OE1 
510  N  NE2 . GLN A 67  ? 0.2863 0.1005 0.2409 -0.0564 0.0330  0.0002  67  GLN A NE2 
511  N  N   . VAL A 68  ? 0.1316 0.1314 0.1345 0.0330  0.0168  0.0207  68  VAL A N   
512  C  CA  . VAL A 68  ? 0.1635 0.1140 0.1403 0.0334  -0.0149 0.0176  68  VAL A CA  
513  C  C   . VAL A 68  ? 0.1502 0.1208 0.1345 0.0113  -0.0003 0.0254  68  VAL A C   
514  O  O   . VAL A 68  ? 0.1738 0.1080 0.1349 0.0130  -0.0086 0.0162  68  VAL A O   
515  C  CB  . VAL A 68  ? 0.1569 0.1280 0.1468 0.0164  -0.0157 0.0031  68  VAL A CB  
516  C  CG1 . VAL A 68  ? 0.1675 0.1610 0.1684 0.0170  -0.0362 0.0188  68  VAL A CG1 
517  C  CG2 . VAL A 68  ? 0.1804 0.1471 0.1515 -0.0080 0.0027  -0.0102 68  VAL A CG2 
518  N  N   . GLU A 69  ? 0.1790 0.0949 0.1594 0.0253  0.0062  0.0289  69  GLU A N   
519  C  CA  . GLU A 69  ? 0.1330 0.1076 0.1626 0.0033  0.0110  0.0240  69  GLU A CA  
520  C  C   . GLU A 69  ? 0.1547 0.1398 0.1650 0.0227  -0.0075 0.0420  69  GLU A C   
521  O  O   . GLU A 69  ? 0.1903 0.1002 0.1944 0.0174  -0.0296 0.0273  69  GLU A O   
522  C  CB  . GLU A 69  ? 0.1436 0.1447 0.1881 -0.0120 0.0073  0.0425  69  GLU A CB  
523  C  CG  . GLU A 69  ? 0.1610 0.1770 0.2274 -0.0083 0.0190  0.0041  69  GLU A CG  
524  C  CD  . GLU A 69  ? 0.2085 0.1623 0.1955 -0.0384 0.0080  0.0004  69  GLU A CD  
525  O  OE1 . GLU A 69  ? 0.2328 0.1461 0.2954 0.0197  0.0605  0.0245  69  GLU A OE1 
526  O  OE2 . GLU A 69  ? 0.2420 0.1975 0.2316 -0.0293 0.0182  0.0546  69  GLU A OE2 
527  N  N   . PHE A 70  ? 0.1463 0.1143 0.1766 0.0038  0.0102  0.0330  70  PHE A N   
528  C  CA  . PHE A 70  ? 0.1316 0.0985 0.2246 0.0034  0.0223  0.0504  70  PHE A CA  
529  C  C   . PHE A 70  ? 0.1823 0.1086 0.2035 -0.0068 -0.0089 0.0181  70  PHE A C   
530  O  O   . PHE A 70  ? 0.1776 0.1152 0.2647 -0.0177 -0.0082 0.0450  70  PHE A O   
531  C  CB  . PHE A 70  ? 0.1671 0.0854 0.1834 -0.0163 0.0034  0.0297  70  PHE A CB  
532  C  CG  . PHE A 70  ? 0.1583 0.0894 0.1923 -0.0072 0.0130  0.0358  70  PHE A CG  
533  C  CD1 . PHE A 70  ? 0.1780 0.0946 0.1908 0.0154  0.0120  0.0434  70  PHE A CD1 
534  C  CD2 . PHE A 70  ? 0.1640 0.1353 0.1567 -0.0403 0.0073  0.0215  70  PHE A CD2 
535  C  CE1 . PHE A 70  ? 0.1714 0.1174 0.1964 -0.0094 0.0326  0.0377  70  PHE A CE1 
536  C  CE2 . PHE A 70  ? 0.1712 0.1009 0.1610 -0.0076 0.0248  0.0252  70  PHE A CE2 
537  C  CZ  . PHE A 70  ? 0.1779 0.1158 0.1971 0.0074  0.0480  -0.0102 70  PHE A CZ  
538  N  N   . ASP A 71  ? 0.2088 0.0734 0.2519 -0.0027 -0.0159 0.0293  71  ASP A N   
539  C  CA  . ASP A 71  ? 0.2564 0.0609 0.2598 -0.0038 -0.0179 0.0300  71  ASP A CA  
540  C  C   . ASP A 71  ? 0.1762 0.0766 0.2698 0.0035  0.0161  0.0074  71  ASP A C   
541  O  O   . ASP A 71  ? 0.2045 0.1558 0.3887 -0.0318 0.0719  -0.0113 71  ASP A O   
542  C  CB  . ASP A 71  ? 0.2451 0.1518 0.3369 0.0010  -0.0441 0.0589  71  ASP A CB  
543  C  CG  . ASP A 71  ? 0.3164 0.1745 0.3097 0.0024  -0.1008 0.0289  71  ASP A CG  
544  O  OD1 . ASP A 71  ? 0.2913 0.1339 0.3565 0.0251  -0.0617 0.0519  71  ASP A OD1 
545  O  OD2 . ASP A 71  ? 0.3011 0.1382 0.4454 -0.0055 -0.1016 0.0615  71  ASP A OD2 
546  N  N   . ASP A 72  ? 0.2071 0.1048 0.2749 -0.0144 -0.0055 0.0454  72  ASP A N   
547  C  CA  . ASP A 72  ? 0.2376 0.0648 0.2569 -0.0053 0.0197  0.0408  72  ASP A CA  
548  C  C   . ASP A 72  ? 0.2463 0.0729 0.3154 -0.0410 -0.0227 0.0380  72  ASP A C   
549  O  O   . ASP A 72  ? 0.2987 0.0996 0.2924 -0.0034 -0.0310 0.0395  72  ASP A O   
550  C  CB  . ASP A 72  ? 0.1898 0.1138 0.3074 0.0031  0.0279  0.0465  72  ASP A CB  
551  C  CG  . ASP A 72  ? 0.1937 0.1550 0.2082 -0.0133 -0.0019 0.0494  72  ASP A CG  
552  O  OD1 . ASP A 72  ? 0.2536 0.1813 0.2341 -0.0116 0.0170  0.0730  72  ASP A OD1 
553  O  OD2 . ASP A 72  ? 0.2759 0.1447 0.1831 0.0121  -0.0248 0.0156  72  ASP A OD2 
554  N  N   . SER A 73  ? 0.2463 0.1410 0.2976 -0.0034 0.0046  0.0314  73  SER A N   
555  C  CA  . SER A 73  ? 0.2599 0.1590 0.2661 0.0023  -0.0577 0.0362  73  SER A CA  
556  C  C   . SER A 73  ? 0.3302 0.1603 0.2872 -0.0084 0.0309  -0.0285 73  SER A C   
557  O  O   . SER A 73  ? 0.4199 0.1802 0.2884 -0.0065 -0.0417 0.0156  73  SER A O   
558  C  CB  . SER A 73  ? 0.3012 0.1443 0.3051 -0.0424 -0.0055 0.0839  73  SER A CB  
559  O  OG  . SER A 73  ? 0.3319 0.1093 0.2988 0.0121  0.0060  0.0699  73  SER A OG  
560  N  N   . GLN A 74  ? 0.2712 0.1190 0.3228 0.0204  0.0044  0.0521  74  GLN A N   
561  C  CA  . GLN A 74  ? 0.3234 0.1923 0.2612 0.0086  0.0469  -0.0029 74  GLN A CA  
562  C  C   . GLN A 74  ? 0.3407 0.1817 0.2960 -0.0521 -0.0283 -0.0183 74  GLN A C   
563  O  O   . GLN A 74  ? 0.3073 0.1720 0.2953 -0.0602 0.0035  -0.0088 74  GLN A O   
564  C  CB  . GLN A 74  ? 0.2973 0.1989 0.5389 0.0418  -0.0139 0.0933  74  GLN A CB  
565  C  CG  . GLN A 74  ? 0.3580 0.5012 0.4926 0.0878  0.0025  0.1003  74  GLN A CG  
566  C  CD  . GLN A 74  ? 0.3994 0.3035 0.4457 0.0579  -0.0528 0.0293  74  GLN A CD  
567  O  OE1 . GLN A 74  ? 0.3915 0.4279 0.4070 -0.0108 0.0009  0.0945  74  GLN A OE1 
568  N  NE2 . GLN A 74  ? 0.4868 0.3161 0.4148 0.0030  -0.0542 0.0858  74  GLN A NE2 
569  N  N   . ASP A 75  ? 0.3730 0.2476 0.2836 -0.0109 -0.0334 0.0021  75  ASP A N   
570  C  CA  . ASP A 75  ? 0.3644 0.4287 0.2879 -0.1153 -0.0276 0.0674  75  ASP A CA  
571  C  C   . ASP A 75  ? 0.2749 0.2561 0.4431 0.0781  -0.1053 0.0170  75  ASP A C   
572  O  O   . ASP A 75  ? 0.2256 0.9467 0.6472 0.0438  -0.0624 -0.1784 75  ASP A O   
573  C  CB  . ASP A 75  ? 0.4458 0.3616 0.3486 0.1693  -0.1096 -0.0066 75  ASP A CB  
574  C  CG  . ASP A 75  ? 0.2889 0.5295 0.3673 -0.1049 0.1309  -0.0606 75  ASP A CG  
575  O  OD1 . ASP A 75  ? 0.3228 0.7894 0.3966 0.0080  -0.0092 -0.1882 75  ASP A OD1 
576  O  OD2 . ASP A 75  ? 0.6372 0.5771 0.3840 0.1647  0.1744  -0.0266 75  ASP A OD2 
577  N  N   . LYS A 76  ? 0.2598 0.2246 0.3504 -0.0126 -0.0466 0.0509  76  LYS A N   
578  C  CA  . LYS A 76  ? 0.4211 0.1952 0.3976 -0.0690 -0.1028 0.0557  76  LYS A CA  
579  C  C   . LYS A 76  ? 0.3690 0.2134 0.5432 0.0666  -0.0366 0.1324  76  LYS A C   
580  O  O   . LYS A 76  ? 0.4402 0.4070 1.0295 -0.0372 0.1859  0.2964  76  LYS A O   
581  C  CB  . LYS A 76  ? 0.3326 0.1946 0.4070 -0.0163 -0.0948 0.0798  76  LYS A CB  
582  C  CG  . LYS A 76  ? 0.4881 0.2846 0.3193 -0.0206 -0.0732 0.1009  76  LYS A CG  
583  C  CD  . LYS A 76  ? 0.5238 0.1777 0.3001 -0.0528 -0.0171 0.0557  76  LYS A CD  
584  C  CE  . LYS A 76  ? 0.4003 0.2621 0.3770 0.0457  -0.1423 0.0444  76  LYS A CE  
585  N  NZ  . LYS A 76  ? 0.3604 0.3501 0.3896 -0.0364 -0.0734 0.0570  76  LYS A NZ  
586  N  N   . ALA A 77  ? 0.2501 0.2449 0.3931 0.0044  -0.0555 0.0965  77  ALA A N   
587  C  CA  . ALA A 77  ? 0.1905 0.2513 0.2665 -0.0190 0.0095  0.0521  77  ALA A CA  
588  C  C   . ALA A 77  ? 0.1684 0.2395 0.3171 -0.0231 -0.0128 0.0598  77  ALA A C   
589  O  O   . ALA A 77  ? 0.1539 0.2861 0.3327 -0.0055 -0.0184 0.0484  77  ALA A O   
590  C  CB  . ALA A 77  ? 0.2053 0.2736 0.2991 0.0584  -0.0373 0.0059  77  ALA A CB  
591  N  N   . VAL A 78  ? 0.1872 0.1382 0.2654 0.0266  -0.0352 0.0241  78  VAL A N   
592  C  CA  . VAL A 78  ? 0.2024 0.1468 0.2495 0.0167  -0.0127 0.0458  78  VAL A CA  
593  C  C   . VAL A 78  ? 0.1404 0.1247 0.2470 -0.0074 0.0021  0.0214  78  VAL A C   
594  O  O   . VAL A 78  ? 0.1734 0.1784 0.3242 -0.0547 -0.0225 0.0631  78  VAL A O   
595  C  CB  . VAL A 78  ? 0.2716 0.1456 0.3553 0.0158  -0.0263 0.0234  78  VAL A CB  
596  C  CG1 . VAL A 78  ? 0.2779 0.1273 0.3830 0.0079  -0.0104 0.0147  78  VAL A CG1 
597  C  CG2 . VAL A 78  ? 0.2836 0.2512 0.3565 0.0735  0.0704  -0.0016 78  VAL A CG2 
598  N  N   . LEU A 79  ? 0.1675 0.1274 0.2102 0.0190  0.0049  0.0044  79  LEU A N   
599  C  CA  . LEU A 79  ? 0.1612 0.1301 0.2316 0.0089  0.0068  0.0350  79  LEU A CA  
600  C  C   . LEU A 79  ? 0.1558 0.1023 0.2499 -0.0114 0.0621  0.0099  79  LEU A C   
601  O  O   . LEU A 79  ? 0.1768 0.1301 0.2708 -0.0326 0.0396  -0.0181 79  LEU A O   
602  C  CB  . LEU A 79  ? 0.1495 0.1490 0.2222 0.0006  0.0179  0.0132  79  LEU A CB  
603  C  CG  . LEU A 79  ? 0.1770 0.1536 0.2233 0.0001  0.0217  0.0212  79  LEU A CG  
604  C  CD1 . LEU A 79  ? 0.2007 0.1569 0.3050 -0.0150 0.0629  0.0516  79  LEU A CD1 
605  C  CD2 . LEU A 79  ? 0.1860 0.1903 0.2402 0.0214  0.0436  0.0097  79  LEU A CD2 
606  N  N   . LYS A 80  ? 0.1557 0.1402 0.2448 -0.0069 0.0500  0.0204  80  LYS A N   
607  C  CA  . LYS A 80  ? 0.2086 0.1654 0.2345 -0.0023 0.0917  -0.0080 80  LYS A CA  
608  C  C   . LYS A 80  ? 0.1560 0.1971 0.2290 -0.0161 0.0587  -0.0073 80  LYS A C   
609  O  O   . LYS A 80  ? 0.1407 0.1601 0.2902 -0.0103 0.0359  0.0201  80  LYS A O   
610  C  CB  . LYS A 80  ? 0.4325 0.1684 0.3208 0.1032  0.1010  0.0384  80  LYS A CB  
611  C  CG  . LYS A 80  ? 0.3718 0.2143 0.4264 0.0229  0.0577  0.0769  80  LYS A CG  
612  C  CD  . LYS A 80  ? 0.3211 0.4088 0.6443 0.1313  -0.0797 0.0055  80  LYS A CD  
613  N  N   . GLY A 81  ? 0.2066 0.1726 0.2226 0.0375  0.0766  0.0285  81  GLY A N   
614  C  CA  . GLY A 81  ? 0.1556 0.1921 0.2726 0.0222  0.0819  0.0524  81  GLY A CA  
615  C  C   . GLY A 81  ? 0.1497 0.1596 0.2785 -0.0019 0.0672  0.0287  81  GLY A C   
616  O  O   . GLY A 81  ? 0.1583 0.1751 0.2476 -0.0189 0.0574  -0.0036 81  GLY A O   
617  N  N   . GLY A 82  ? 0.1788 0.1806 0.3483 -0.0066 0.0424  0.0776  82  GLY A N   
618  C  CA  . GLY A 82  ? 0.1765 0.1973 0.3833 -0.0049 0.0392  0.1154  82  GLY A CA  
619  C  C   . GLY A 82  ? 0.2043 0.1980 0.3435 0.0694  0.0767  0.0243  82  GLY A C   
620  O  O   . GLY A 82  ? 0.2365 0.2150 0.3586 0.0900  0.1264  0.0259  82  GLY A O   
621  N  N   . PRO A 83  ? 0.1806 0.1348 0.3114 0.0557  0.0696  0.0342  83  PRO A N   
622  C  CA  . PRO A 83  ? 0.2289 0.1569 0.3453 0.0227  0.0585  0.0176  83  PRO A CA  
623  C  C   . PRO A 83  ? 0.2029 0.1784 0.2570 0.0606  0.0604  0.0017  83  PRO A C   
624  O  O   . PRO A 83  ? 0.2810 0.2927 0.3014 0.0092  -0.0114 0.0091  83  PRO A O   
625  C  CB  . PRO A 83  ? 0.2468 0.1894 0.2586 0.0460  0.0566  -0.0008 83  PRO A CB  
626  C  CG  . PRO A 83  ? 0.1684 0.1657 0.2584 0.0276  0.0288  -0.0009 83  PRO A CG  
627  C  CD  . PRO A 83  ? 0.1485 0.1374 0.3005 0.0201  0.0718  0.0108  83  PRO A CD  
628  N  N   . LEU A 84  ? 0.2121 0.1683 0.2460 0.0482  0.0723  0.0174  84  LEU A N   
629  C  CA  . LEU A 84  ? 0.1880 0.1295 0.2560 0.0312  0.0528  -0.0084 84  LEU A CA  
630  C  C   . LEU A 84  ? 0.1797 0.1615 0.2672 0.0433  0.0703  -0.0124 84  LEU A C   
631  O  O   . LEU A 84  ? 0.2214 0.2099 0.3693 0.0486  0.0868  -0.0694 84  LEU A O   
632  C  CB  . LEU A 84  ? 0.1766 0.0991 0.2507 0.0136  0.0396  -0.0260 84  LEU A CB  
633  C  CG  . LEU A 84  ? 0.1439 0.1199 0.2321 0.0411  0.0458  -0.0037 84  LEU A CG  
634  C  CD1 . LEU A 84  ? 0.2122 0.1600 0.2309 0.0141  0.0194  0.0098  84  LEU A CD1 
635  C  CD2 . LEU A 84  ? 0.1463 0.1432 0.2481 0.0048  0.0485  -0.0203 84  LEU A CD2 
636  N  N   . ASP A 85  ? 0.2669 0.1465 0.2841 0.0106  0.1201  -0.0743 85  ASP A N   
637  C  CA  . ASP A 85  ? 0.3585 0.1244 0.3829 0.0100  0.0981  -0.0769 85  ASP A CA  
638  C  C   . ASP A 85  ? 0.2438 0.1801 0.3957 0.0209  0.1094  -0.0337 85  ASP A C   
639  O  O   . ASP A 85  ? 0.3068 0.2538 0.4571 0.0111  0.1097  -0.1000 85  ASP A O   
640  C  CB  . ASP A 85  ? 0.3856 0.3701 0.4440 0.0038  0.0177  -0.0864 85  ASP A CB  
641  C  CG  . ASP A 85  ? 0.3226 0.5556 0.6118 0.1143  -0.0229 0.0523  85  ASP A CG  
642  O  OD1 . ASP A 85  ? 0.3364 0.9385 0.7856 -0.0133 0.1216  -0.0757 85  ASP A OD1 
643  O  OD2 . ASP A 85  ? 0.3769 0.4956 0.5808 0.1174  -0.0214 -0.1667 85  ASP A OD2 
644  N  N   . GLY A 86  ? 0.3215 0.1698 0.5100 0.0157  0.1200  0.0965  86  GLY A N   
645  C  CA  . GLY A 86  ? 0.2950 0.2039 0.3351 -0.0515 0.0244  0.0144  86  GLY A CA  
646  C  C   . GLY A 86  ? 0.3721 0.2196 0.3443 -0.0627 0.1028  -0.0291 86  GLY A C   
647  O  O   . GLY A 86  ? 0.3773 0.2902 0.3486 -0.1238 0.0439  0.0621  86  GLY A O   
648  N  N   . THR A 87  ? 0.2628 0.1653 0.2975 0.0203  0.0881  -0.0374 87  THR A N   
649  C  CA  . THR A 87  ? 0.2357 0.1863 0.2953 0.0356  0.0665  -0.0253 87  THR A CA  
650  C  C   . THR A 87  ? 0.1890 0.1018 0.3399 -0.0162 0.0592  -0.0215 87  THR A C   
651  O  O   . THR A 87  ? 0.2224 0.0937 0.3799 -0.0099 0.0886  -0.0385 87  THR A O   
652  C  CB  . THR A 87  ? 0.5210 0.3342 0.3507 0.0284  -0.1714 0.0903  87  THR A CB  
653  O  OG1 . THR A 87  ? 0.4815 0.7669 0.4655 -0.0234 0.0098  0.0554  87  THR A OG1 
654  C  CG2 . THR A 87  ? 0.2851 0.3433 0.3843 0.0801  0.0356  0.0583  87  THR A CG2 
655  N  N   . TYR A 88  ? 0.1461 0.1041 0.2525 -0.0148 0.0468  -0.0128 88  TYR A N   
656  C  CA  . TYR A 88  ? 0.1443 0.0897 0.2652 0.0029  0.0383  -0.0195 88  TYR A CA  
657  C  C   . TYR A 88  ? 0.1539 0.0892 0.2588 0.0179  0.0284  0.0019  88  TYR A C   
658  O  O   . TYR A 88  ? 0.1526 0.1770 0.3193 -0.0403 0.0047  0.0491  88  TYR A O   
659  C  CB  . TYR A 88  ? 0.2084 0.0651 0.2513 -0.0046 0.0139  -0.0212 88  TYR A CB  
660  C  CG  . TYR A 88  ? 0.1561 0.0540 0.2054 -0.0049 0.0434  -0.0166 88  TYR A CG  
661  C  CD1 . TYR A 88  ? 0.1898 0.0980 0.2097 -0.0181 0.0550  -0.0328 88  TYR A CD1 
662  C  CD2 . TYR A 88  ? 0.1601 0.0734 0.2092 0.0179  0.0281  0.0036  88  TYR A CD2 
663  C  CE1 . TYR A 88  ? 0.1658 0.1460 0.2332 -0.0199 0.0410  -0.0427 88  TYR A CE1 
664  C  CE2 . TYR A 88  ? 0.1737 0.0724 0.1876 -0.0036 0.0370  0.0006  88  TYR A CE2 
665  C  CZ  . TYR A 88  ? 0.1658 0.0973 0.1973 -0.0114 0.0337  -0.0270 88  TYR A CZ  
666  O  OH  . TYR A 88  ? 0.1826 0.1596 0.2045 -0.0384 0.0540  -0.0468 88  TYR A OH  
667  N  N   . ARG A 89  ? 0.1553 0.1005 0.2249 0.0175  0.0307  -0.0120 89  ARG A N   
668  C  CA  . ARG A 89  ? 0.1673 0.0919 0.2368 0.0209  0.0038  0.0236  89  ARG A CA  
669  C  C   . ARG A 89  ? 0.1384 0.0774 0.1845 0.0103  -0.0184 0.0233  89  ARG A C   
670  O  O   . ARG A 89  ? 0.1339 0.0770 0.1849 0.0106  0.0106  0.0126  89  ARG A O   
671  C  CB  . ARG A 89  ? 0.2598 0.0768 0.3550 -0.0168 0.0413  0.0154  89  ARG A CB  
672  C  CG  . ARG A 89  ? 0.3389 0.3307 0.4516 0.0731  0.0092  0.1781  89  ARG A CG  
673  C  CD  . ARG A 89  ? 0.2832 0.1658 0.4427 -0.0066 -0.0278 0.1419  89  ARG A CD  
674  N  NE  . ARG A 89  ? 0.4384 0.3550 0.2077 0.0325  -0.0640 -0.0030 89  ARG A NE  
675  C  CZ  . ARG A 89  ? 0.4978 0.1830 0.2631 0.1008  -0.1248 -0.0358 89  ARG A CZ  
676  N  NH1 . ARG A 89  ? 0.5797 0.2699 0.2205 0.0863  -0.0385 0.0065  89  ARG A NH1 
677  N  NH2 . ARG A 89  ? 0.3709 0.4290 0.6204 0.1360  -0.1367 -0.2741 89  ARG A NH2 
678  N  N   . LEU A 90  ? 0.1497 0.0594 0.2013 0.0132  -0.0113 0.0225  90  LEU A N   
679  C  CA  . LEU A 90  ? 0.1522 0.0644 0.1669 -0.0044 0.0048  0.0339  90  LEU A CA  
680  C  C   . LEU A 90  ? 0.1421 0.0846 0.1597 -0.0277 -0.0222 0.0443  90  LEU A C   
681  O  O   . LEU A 90  ? 0.1738 0.1303 0.1964 0.0035  -0.0238 0.0655  90  LEU A O   
682  C  CB  . LEU A 90  ? 0.1386 0.1079 0.1605 -0.0108 -0.0039 0.0205  90  LEU A CB  
683  C  CG  . LEU A 90  ? 0.1691 0.1075 0.1856 -0.0201 -0.0240 0.0044  90  LEU A CG  
684  C  CD1 . LEU A 90  ? 0.1967 0.0953 0.1874 -0.0076 0.0051  0.0273  90  LEU A CD1 
685  C  CD2 . LEU A 90  ? 0.1772 0.1467 0.1949 -0.0491 -0.0260 0.0098  90  LEU A CD2 
686  N  N   . LYS A 91  ? 0.1400 0.0822 0.1569 0.0073  0.0154  0.0178  91  LYS A N   
687  C  CA  . LYS A 91  ? 0.1425 0.1079 0.1580 0.0000  0.0100  0.0004  91  LYS A CA  
688  C  C   . LYS A 91  ? 0.1429 0.0840 0.1528 0.0333  -0.0006 0.0225  91  LYS A C   
689  O  O   . LYS A 91  ? 0.1773 0.0794 0.1495 -0.0102 -0.0033 0.0266  91  LYS A O   
690  C  CB  . LYS A 91  ? 0.1529 0.1143 0.1700 -0.0432 0.0157  0.0089  91  LYS A CB  
691  C  CG  . LYS A 91  ? 0.1648 0.0867 0.1845 -0.0019 0.0059  -0.0157 91  LYS A CG  
692  C  CD  . LYS A 91  ? 0.1813 0.0863 0.2208 -0.0376 0.0219  -0.0362 91  LYS A CD  
693  C  CE  . LYS A 91  ? 0.2061 0.1263 0.2169 -0.0120 0.0500  -0.0269 91  LYS A CE  
694  N  NZ  . LYS A 91  ? 0.3211 0.2050 0.2357 -0.0848 -0.0040 0.0144  91  LYS A NZ  
695  N  N   . GLN A 92  ? 0.1679 0.0691 0.1474 -0.0015 -0.0002 0.0143  92  GLN A N   
696  C  CA  . GLN A 92  ? 0.1732 0.0671 0.1543 0.0182  0.0184  0.0194  92  GLN A CA  
697  C  C   . GLN A 92  ? 0.1465 0.0749 0.1411 -0.0095 0.0100  0.0107  92  GLN A C   
698  O  O   . GLN A 92  ? 0.1684 0.0687 0.1350 -0.0022 0.0149  0.0098  92  GLN A O   
699  C  CB  . GLN A 92  ? 0.1553 0.1027 0.1507 -0.0145 -0.0005 0.0186  92  GLN A CB  
700  C  CG  . GLN A 92  ? 0.1891 0.1146 0.1697 0.0184  -0.0279 0.0017  92  GLN A CG  
701  C  CD  . GLN A 92  ? 0.1777 0.0822 0.2149 -0.0179 -0.0074 -0.0103 92  GLN A CD  
702  O  OE1 . GLN A 92  ? 0.1858 0.0876 0.2114 -0.0037 -0.0295 0.0050  92  GLN A OE1 
703  N  NE2 . GLN A 92  ? 0.1747 0.2523 0.2701 -0.0148 0.0272  -0.0732 92  GLN A NE2 
704  N  N   . PHE A 93  ? 0.1392 0.0651 0.1292 0.0050  -0.0046 0.0146  93  PHE A N   
705  C  CA  . PHE A 93  ? 0.1190 0.0610 0.1648 0.0163  0.0071  0.0223  93  PHE A CA  
706  C  C   . PHE A 93  ? 0.0993 0.1110 0.1217 0.0120  -0.0096 0.0129  93  PHE A C   
707  O  O   . PHE A 93  ? 0.1427 0.0809 0.1237 0.0074  -0.0035 0.0120  93  PHE A O   
708  C  CB  . PHE A 93  ? 0.1259 0.0763 0.1350 -0.0063 -0.0106 0.0132  93  PHE A CB  
709  C  CG  . PHE A 93  ? 0.1298 0.0734 0.1337 -0.0053 -0.0038 0.0177  93  PHE A CG  
710  C  CD1 . PHE A 93  ? 0.1623 0.0858 0.1280 0.0039  0.0092  -0.0002 93  PHE A CD1 
711  C  CD2 . PHE A 93  ? 0.1195 0.1155 0.1320 0.0002  -0.0124 0.0279  93  PHE A CD2 
712  C  CE1 . PHE A 93  ? 0.1520 0.1041 0.1608 0.0053  -0.0195 -0.0027 93  PHE A CE1 
713  C  CE2 . PHE A 93  ? 0.1529 0.1285 0.1192 -0.0078 -0.0080 0.0036  93  PHE A CE2 
714  C  CZ  . PHE A 93  ? 0.1493 0.1144 0.1489 0.0050  0.0000  0.0179  93  PHE A CZ  
715  N  N   . HIS A 94  ? 0.1090 0.0628 0.1438 0.0097  -0.0111 0.0011  94  HIS A N   
716  C  CA  . HIS A 94  ? 0.1097 0.0609 0.1296 0.0070  0.0142  0.0198  94  HIS A CA  
717  C  C   . HIS A 94  ? 0.1147 0.0621 0.1089 -0.0075 0.0082  0.0091  94  HIS A C   
718  O  O   . HIS A 94  ? 0.1276 0.0815 0.1143 -0.0052 0.0173  -0.0031 94  HIS A O   
719  C  CB  . HIS A 94  ? 0.1249 0.0813 0.1244 -0.0174 -0.0094 0.0128  94  HIS A CB  
720  C  CG  . HIS A 94  ? 0.1136 0.0718 0.1167 -0.0113 0.0044  0.0059  94  HIS A CG  
721  N  ND1 . HIS A 94  ? 0.1224 0.0783 0.1346 -0.0291 -0.0018 -0.0038 94  HIS A ND1 
722  C  CD2 . HIS A 94  ? 0.1156 0.0924 0.1083 -0.0063 0.0272  0.0218  94  HIS A CD2 
723  C  CE1 . HIS A 94  ? 0.1023 0.0560 0.1393 -0.0027 -0.0042 0.0168  94  HIS A CE1 
724  N  NE2 . HIS A 94  ? 0.1110 0.0537 0.1246 0.0041  0.0000  0.0194  94  HIS A NE2 
725  N  N   . PHE A 95  ? 0.1185 0.0615 0.1273 0.0030  0.0017  0.0039  95  PHE A N   
726  C  CA  . PHE A 95  ? 0.1186 0.0502 0.1400 0.0065  -0.0078 0.0005  95  PHE A CA  
727  C  C   . PHE A 95  ? 0.1147 0.0590 0.1190 -0.0125 -0.0008 -0.0098 95  PHE A C   
728  O  O   . PHE A 95  ? 0.1213 0.0669 0.1497 -0.0098 0.0075  0.0031  95  PHE A O   
729  C  CB  . PHE A 95  ? 0.1255 0.0797 0.1515 -0.0122 -0.0098 -0.0062 95  PHE A CB  
730  C  CG  . PHE A 95  ? 0.1210 0.0846 0.1429 -0.0106 -0.0054 -0.0198 95  PHE A CG  
731  C  CD1 . PHE A 95  ? 0.1454 0.1059 0.1500 0.0034  -0.0203 -0.0271 95  PHE A CD1 
732  C  CD2 . PHE A 95  ? 0.1183 0.0921 0.1622 -0.0238 -0.0021 -0.0322 95  PHE A CD2 
733  C  CE1 . PHE A 95  ? 0.1653 0.1154 0.1763 0.0144  -0.0263 -0.0295 95  PHE A CE1 
734  C  CE2 . PHE A 95  ? 0.1217 0.1084 0.1773 -0.0145 -0.0129 -0.0111 95  PHE A CE2 
735  C  CZ  . PHE A 95  ? 0.1715 0.1147 0.1841 -0.0052 -0.0143 -0.0303 95  PHE A CZ  
736  N  N   . HIS A 96  ? 0.1102 0.0817 0.1241 -0.0059 -0.0065 0.0009  96  HIS A N   
737  C  CA  . HIS A 96  ? 0.1093 0.0671 0.1288 -0.0023 -0.0020 0.0210  96  HIS A CA  
738  C  C   . HIS A 96  ? 0.1014 0.0743 0.1346 -0.0115 0.0201  -0.0072 96  HIS A C   
739  O  O   . HIS A 96  ? 0.1126 0.0842 0.1449 -0.0233 0.0219  -0.0139 96  HIS A O   
740  C  CB  . HIS A 96  ? 0.1450 0.0396 0.1407 -0.0038 0.0061  -0.0120 96  HIS A CB  
741  C  CG  . HIS A 96  ? 0.1189 0.0303 0.1364 -0.0032 -0.0029 0.0030  96  HIS A CG  
742  N  ND1 . HIS A 96  ? 0.1088 0.0576 0.1269 -0.0186 0.0128  -0.0073 96  HIS A ND1 
743  C  CD2 . HIS A 96  ? 0.1385 0.0182 0.1321 0.0037  0.0081  -0.0083 96  HIS A CD2 
744  C  CE1 . HIS A 96  ? 0.1323 0.0615 0.1357 0.0002  0.0066  -0.0064 96  HIS A CE1 
745  N  NE2 . HIS A 96  ? 0.1259 0.0400 0.1479 -0.0097 -0.0088 0.0017  96  HIS A NE2 
746  N  N   . TRP A 97  ? 0.1298 0.0551 0.1216 -0.0050 0.0126  -0.0074 97  TRP A N   
747  C  CA  . TRP A 97  ? 0.1436 0.0584 0.1242 -0.0135 0.0067  -0.0051 97  TRP A CA  
748  C  C   . TRP A 97  ? 0.1337 0.0686 0.1276 -0.0124 0.0103  -0.0124 97  TRP A C   
749  O  O   . TRP A 97  ? 0.1404 0.0689 0.1302 -0.0027 0.0248  0.0009  97  TRP A O   
750  C  CB  . TRP A 97  ? 0.1370 0.0878 0.1192 -0.0294 0.0156  -0.0168 97  TRP A CB  
751  C  CG  . TRP A 97  ? 0.1406 0.0682 0.1327 -0.0125 0.0209  -0.0058 97  TRP A CG  
752  C  CD1 . TRP A 97  ? 0.1349 0.1016 0.1247 0.0011  0.0161  -0.0131 97  TRP A CD1 
753  C  CD2 . TRP A 97  ? 0.1140 0.0763 0.1174 -0.0126 0.0055  -0.0091 97  TRP A CD2 
754  N  NE1 . TRP A 97  ? 0.1790 0.0748 0.1280 -0.0005 0.0272  -0.0212 97  TRP A NE1 
755  C  CE2 . TRP A 97  ? 0.1298 0.0732 0.1285 -0.0159 0.0308  -0.0072 97  TRP A CE2 
756  C  CE3 . TRP A 97  ? 0.1307 0.0747 0.1362 0.0065  0.0050  0.0089  97  TRP A CE3 
757  C  CZ2 . TRP A 97  ? 0.1639 0.0885 0.1326 -0.0114 0.0233  0.0006  97  TRP A CZ2 
758  C  CZ3 . TRP A 97  ? 0.1443 0.0833 0.1460 0.0067  0.0148  0.0231  97  TRP A CZ3 
759  C  CH2 . TRP A 97  ? 0.1459 0.0894 0.1350 -0.0013 0.0172  0.0041  97  TRP A CH2 
760  N  N   . GLY A 98  ? 0.1366 0.0625 0.1456 -0.0043 0.0124  -0.0208 98  GLY A N   
761  C  CA  . GLY A 98  ? 0.1658 0.0662 0.1360 0.0154  0.0313  -0.0178 98  GLY A CA  
762  C  C   . GLY A 98  ? 0.1468 0.0779 0.1244 -0.0086 0.0124  -0.0126 98  GLY A C   
763  O  O   . GLY A 98  ? 0.1790 0.0817 0.1395 -0.0053 -0.0001 -0.0168 98  GLY A O   
764  N  N   . SER A 99  ? 0.1632 0.0696 0.1600 0.0039  0.0287  -0.0164 99  SER A N   
765  C  CA  . SER A 99  ? 0.1869 0.0608 0.1856 0.0119  0.0279  -0.0240 99  SER A CA  
766  C  C   . SER A 99  ? 0.1982 0.0585 0.1615 0.0057  0.0231  -0.0182 99  SER A C   
767  O  O   . SER A 99  ? 0.2462 0.0849 0.2075 -0.0177 0.0303  -0.0491 99  SER A O   
768  C  CB  . SER A 99  ? 0.1938 0.1065 0.1917 0.0362  0.0247  -0.0261 99  SER A CB  
769  O  OG  . SER A 99  ? 0.1804 0.0883 0.2366 0.0277  0.0254  0.0171  99  SER A OG  
770  N  N   . LEU A 100 ? 0.1689 0.0759 0.1793 -0.0094 0.0273  -0.0020 100 LEU A N   
771  C  CA  . LEU A 100 ? 0.1550 0.0510 0.2222 -0.0085 0.0343  -0.0082 100 LEU A CA  
772  C  C   . LEU A 100 ? 0.2337 0.0597 0.1806 -0.0253 0.0752  -0.0104 100 LEU A C   
773  O  O   . LEU A 100 ? 0.2260 0.0610 0.1747 -0.0006 0.0440  -0.0162 100 LEU A O   
774  C  CB  . LEU A 100 ? 0.2203 0.0951 0.1881 0.0077  0.0379  -0.0089 100 LEU A CB  
775  C  CG  . LEU A 100 ? 0.2389 0.0946 0.2079 0.0345  0.0146  -0.0295 100 LEU A CG  
776  C  CD1 . LEU A 100 ? 0.2075 0.1671 0.2763 0.0788  0.0018  -0.0333 100 LEU A CD1 
777  C  CD2 . LEU A 100 ? 0.2600 0.1597 0.2296 0.0128  0.0397  -0.0828 100 LEU A CD2 
778  N  N   . ASP A 101 ? 0.1817 0.0749 0.2081 0.0021  0.0329  0.0011  101 ASP A N   
779  C  CA  . ASP A 101 ? 0.1905 0.1113 0.1880 -0.0193 0.0563  0.0099  101 ASP A CA  
780  C  C   . ASP A 101 ? 0.2462 0.0684 0.1975 -0.0029 0.0563  0.0153  101 ASP A C   
781  O  O   . ASP A 101 ? 0.3062 0.0900 0.2610 0.0221  0.0925  0.0001  101 ASP A O   
782  C  CB  . ASP A 101 ? 0.1716 0.1110 0.2348 -0.0230 0.0070  0.0368  101 ASP A CB  
783  C  CG  . ASP A 101 ? 0.2488 0.1092 0.2518 -0.0013 0.0302  -0.0006 101 ASP A CG  
784  O  OD1 . ASP A 101 ? 0.2255 0.1074 0.2474 0.0006  0.0453  -0.0039 101 ASP A OD1 
785  O  OD2 . ASP A 101 ? 0.3071 0.1872 0.3328 -0.0767 0.0027  -0.0380 101 ASP A OD2 
786  N  N   . GLY A 102 ? 0.2373 0.1095 0.1849 -0.0517 0.0063  0.0105  102 GLY A N   
787  C  CA  . GLY A 102 ? 0.3004 0.1335 0.2007 -0.0758 0.0283  0.0041  102 GLY A CA  
788  C  C   . GLY A 102 ? 0.2635 0.0971 0.1754 -0.0463 0.0480  -0.0011 102 GLY A C   
789  O  O   . GLY A 102 ? 0.2609 0.1064 0.2032 -0.0480 0.0163  0.0156  102 GLY A O   
790  N  N   . GLN A 103 ? 0.2086 0.0817 0.1676 -0.0201 0.0468  -0.0093 103 GLN A N   
791  C  CA  . GLN A 103 ? 0.1664 0.0804 0.1914 -0.0214 0.0066  -0.0083 103 GLN A CA  
792  C  C   . GLN A 103 ? 0.1138 0.0982 0.1672 -0.0125 0.0268  -0.0214 103 GLN A C   
793  O  O   . GLN A 103 ? 0.1558 0.0785 0.1632 -0.0138 0.0170  -0.0134 103 GLN A O   
794  C  CB  . GLN A 103 ? 0.1831 0.0791 0.1614 -0.0166 0.0291  -0.0023 103 GLN A CB  
795  C  CG  . GLN A 103 ? 0.1738 0.0982 0.1567 0.0031  0.0447  0.0063  103 GLN A CG  
796  C  CD  . GLN A 103 ? 0.1888 0.0964 0.1996 0.0015  0.0420  0.0274  103 GLN A CD  
797  O  OE1 . GLN A 103 ? 0.2204 0.1183 0.2527 0.0206  0.0500  0.0471  103 GLN A OE1 
798  N  NE2 . GLN A 103 ? 0.1605 0.1023 0.2341 0.0100  0.0398  0.0122  103 GLN A NE2 
799  N  N   . GLY A 104 ? 0.1507 0.0671 0.1684 0.0047  0.0378  -0.0073 104 GLY A N   
800  C  CA  . GLY A 104 ? 0.1303 0.0801 0.1278 0.0026  0.0146  -0.0097 104 GLY A CA  
801  C  C   . GLY A 104 ? 0.1176 0.0810 0.1244 -0.0059 0.0154  -0.0065 104 GLY A C   
802  O  O   . GLY A 104 ? 0.1410 0.0891 0.1442 -0.0215 0.0228  0.0055  104 GLY A O   
803  N  N   . SER A 105 ? 0.1292 0.0668 0.1156 -0.0053 0.0187  -0.0058 105 SER A N   
804  C  CA  . SER A 105 ? 0.1187 0.0754 0.1270 -0.0168 0.0171  -0.0313 105 SER A CA  
805  C  C   . SER A 105 ? 0.1181 0.0716 0.1270 -0.0027 0.0098  -0.0144 105 SER A C   
806  O  O   . SER A 105 ? 0.1303 0.0630 0.1632 0.0029  0.0061  -0.0096 105 SER A O   
807  C  CB  . SER A 105 ? 0.1310 0.0826 0.1256 0.0001  0.0206  0.0026  105 SER A CB  
808  O  OG  . SER A 105 ? 0.1363 0.0639 0.1479 -0.0065 0.0069  -0.0001 105 SER A OG  
809  N  N   . GLU A 106 ? 0.1324 0.0680 0.1256 -0.0122 0.0225  -0.0139 106 GLU A N   
810  C  CA  . GLU A 106 ? 0.1301 0.0621 0.1192 -0.0195 0.0093  0.0051  106 GLU A CA  
811  C  C   . GLU A 106 ? 0.1119 0.0698 0.1249 -0.0083 0.0042  -0.0024 106 GLU A C   
812  O  O   . GLU A 106 ? 0.1194 0.0741 0.1341 -0.0022 0.0042  0.0057  106 GLU A O   
813  C  CB  . GLU A 106 ? 0.1447 0.0714 0.1277 -0.0138 0.0156  0.0218  106 GLU A CB  
814  C  CG  . GLU A 106 ? 0.1689 0.0829 0.1407 -0.0098 0.0397  0.0062  106 GLU A CG  
815  C  CD  . GLU A 106 ? 0.1229 0.0881 0.1360 -0.0038 0.0201  -0.0063 106 GLU A CD  
816  O  OE1 . GLU A 106 ? 0.0955 0.0986 0.1696 -0.0046 0.0115  -0.0066 106 GLU A OE1 
817  O  OE2 . GLU A 106 ? 0.1181 0.1098 0.1522 0.0093  0.0193  -0.0035 106 GLU A OE2 
818  N  N   . HIS A 107 ? 0.1102 0.0713 0.1443 -0.0114 0.0272  0.0050  107 HIS A N   
819  C  CA  . HIS A 107 ? 0.1165 0.0659 0.1350 0.0084  0.0215  0.0108  107 HIS A CA  
820  C  C   . HIS A 107 ? 0.0987 0.0790 0.1212 -0.0145 0.0216  0.0120  107 HIS A C   
821  O  O   . HIS A 107 ? 0.1323 0.0748 0.1339 -0.0127 0.0175  0.0041  107 HIS A O   
822  C  CB  . HIS A 107 ? 0.1156 0.0660 0.1382 0.0162  0.0135  -0.0001 107 HIS A CB  
823  C  CG  . HIS A 107 ? 0.0986 0.0786 0.1217 0.0146  0.0204  -0.0034 107 HIS A CG  
824  N  ND1 . HIS A 107 ? 0.1276 0.0766 0.1198 -0.0052 0.0192  0.0032  107 HIS A ND1 
825  C  CD2 . HIS A 107 ? 0.1230 0.0539 0.1463 0.0134  0.0064  -0.0079 107 HIS A CD2 
826  C  CE1 . HIS A 107 ? 0.1110 0.1073 0.1400 -0.0070 0.0046  -0.0251 107 HIS A CE1 
827  N  NE2 . HIS A 107 ? 0.1262 0.0590 0.1435 0.0055  0.0149  -0.0149 107 HIS A NE2 
828  N  N   . THR A 108 ? 0.1425 0.0712 0.1262 -0.0215 0.0055  0.0226  108 THR A N   
829  C  CA  . THR A 108 ? 0.1183 0.0679 0.1597 -0.0153 0.0062  0.0337  108 THR A CA  
830  C  C   . THR A 108 ? 0.1421 0.0644 0.1529 -0.0037 0.0071  0.0245  108 THR A C   
831  O  O   . THR A 108 ? 0.1453 0.0971 0.1515 0.0083  0.0107  0.0110  108 THR A O   
832  C  CB  . THR A 108 ? 0.1449 0.1059 0.1693 0.0190  -0.0032 0.0262  108 THR A CB  
833  O  OG1 . THR A 108 ? 0.1441 0.0971 0.1812 0.0127  -0.0061 0.0170  108 THR A OG1 
834  C  CG2 . THR A 108 ? 0.1867 0.1023 0.1640 0.0047  0.0126  -0.0009 108 THR A CG2 
835  N  N   . VAL A 109 ? 0.1630 0.0919 0.1547 -0.0325 0.0087  0.0414  109 VAL A N   
836  C  CA  . VAL A 109 ? 0.1826 0.1128 0.1860 -0.0447 0.0170  0.0471  109 VAL A CA  
837  C  C   . VAL A 109 ? 0.1752 0.1070 0.2048 -0.0421 0.0225  0.0487  109 VAL A C   
838  O  O   . VAL A 109 ? 0.1860 0.0995 0.2412 -0.0392 -0.0024 0.0531  109 VAL A O   
839  C  CB  . VAL A 109 ? 0.1640 0.1161 0.1912 -0.0178 0.0155  0.0386  109 VAL A CB  
840  C  CG1 . VAL A 109 ? 0.1629 0.1840 0.2343 -0.0065 0.0392  0.0520  109 VAL A CG1 
841  C  CG2 . VAL A 109 ? 0.1720 0.1199 0.2237 0.0051  0.0312  0.0525  109 VAL A CG2 
842  N  N   . ASP A 110 ? 0.2013 0.0988 0.1673 0.0053  0.0281  0.0574  110 ASP A N   
843  C  CA  . ASP A 110 ? 0.2131 0.1208 0.2197 0.0149  0.0245  0.0947  110 ASP A CA  
844  C  C   . ASP A 110 ? 0.2317 0.1167 0.1903 -0.0233 0.0111  0.0593  110 ASP A C   
845  O  O   . ASP A 110 ? 0.2501 0.1165 0.2304 0.0052  -0.0031 0.0646  110 ASP A O   
846  C  CB  . ASP A 110 ? 0.2724 0.1669 0.2375 -0.0231 0.0513  0.0903  110 ASP A CB  
847  C  CG  . ASP A 110 ? 0.2480 0.2273 0.2256 -0.0367 0.0352  0.1294  110 ASP A CG  
848  O  OD1 . ASP A 110 ? 0.2251 0.2064 0.2745 0.0158  0.0833  0.0793  110 ASP A OD1 
849  O  OD2 . ASP A 110 ? 0.2364 0.3416 0.2983 -0.0097 0.0652  0.1028  110 ASP A OD2 
850  N  N   . LYS A 111 ? 0.1593 0.1307 0.1952 -0.0002 0.0089  0.0461  111 LYS A N   
851  C  CA  . LYS A 111 ? 0.1974 0.1138 0.1852 0.0275  0.0041  0.0473  111 LYS A CA  
852  C  C   . LYS A 111 ? 0.2000 0.1065 0.2002 -0.0016 -0.0019 0.0310  111 LYS A C   
853  O  O   . LYS A 111 ? 0.2147 0.1199 0.2323 0.0025  0.0093  0.0166  111 LYS A O   
854  C  CB  . LYS A 111 ? 0.2305 0.1280 0.2301 0.0707  -0.0108 0.0460  111 LYS A CB  
855  C  CG  . LYS A 111 ? 0.3429 0.1935 0.2622 0.0927  -0.0976 0.0743  111 LYS A CG  
856  C  CD  . LYS A 111 ? 0.3343 0.2899 0.2229 0.0414  -0.0263 -0.0089 111 LYS A CD  
857  C  CE  . LYS A 111 ? 0.3519 0.3895 0.3735 0.0122  -0.1448 0.0321  111 LYS A CE  
858  N  NZ  . LYS A 111 ? 0.4946 0.4382 0.4092 0.1099  -0.1447 0.0173  111 LYS A NZ  
859  N  N   A LYS A 112 ? 0.2053 0.1144 0.1808 -0.0115 -0.0189 0.0525  112 LYS A N   
860  N  N   B LYS A 112 ? 0.2014 0.1203 0.1858 -0.0230 -0.0144 0.0396  112 LYS A N   
861  C  CA  A LYS A 112 ? 0.2303 0.0721 0.2011 -0.0173 -0.0170 0.0502  112 LYS A CA  
862  C  CA  B LYS A 112 ? 0.1890 0.1235 0.2042 -0.0332 -0.0182 0.0450  112 LYS A CA  
863  C  C   A LYS A 112 ? 0.1966 0.0603 0.1894 0.0171  0.0066  0.0398  112 LYS A C   
864  C  C   B LYS A 112 ? 0.1967 0.0952 0.1776 -0.0002 -0.0058 0.0259  112 LYS A C   
865  O  O   A LYS A 112 ? 0.1614 0.0716 0.1576 0.0033  0.0183  0.0199  112 LYS A O   
866  O  O   B LYS A 112 ? 0.1896 0.1125 0.1776 -0.0075 -0.0141 -0.0054 112 LYS A O   
867  C  CB  A LYS A 112 ? 0.2373 0.0976 0.2605 -0.0601 -0.0300 0.0502  112 LYS A CB  
868  C  CB  B LYS A 112 ? 0.1953 0.1619 0.2667 -0.1127 -0.0236 0.0428  112 LYS A CB  
869  C  CG  A LYS A 112 ? 0.2752 0.1696 0.2293 -0.0143 -0.0485 0.0583  112 LYS A CG  
870  C  CG  B LYS A 112 ? 0.1755 0.1757 0.2989 -0.0355 -0.0296 -0.0790 112 LYS A CG  
871  C  CD  A LYS A 112 ? 0.2942 0.2055 0.2570 -0.0413 -0.0466 0.0432  112 LYS A CD  
872  C  CD  B LYS A 112 ? 0.2073 0.2296 0.3325 -0.0601 0.0003  0.0171  112 LYS A CD  
873  C  CE  A LYS A 112 ? 0.2667 0.2235 0.2998 -0.0252 -0.0853 -0.0068 112 LYS A CE  
874  C  CE  B LYS A 112 ? 0.1898 0.2032 0.3226 -0.0099 -0.0281 0.0490  112 LYS A CE  
875  N  NZ  A LYS A 112 ? 0.3450 0.1920 0.3199 0.0145  -0.1254 0.0355  112 LYS A NZ  
876  N  NZ  B LYS A 112 ? 0.1723 0.2208 0.3574 0.0305  -0.0351 -0.0499 112 LYS A NZ  
877  N  N   . LYS A 113 ? 0.2011 0.0917 0.1756 0.0018  0.0021  0.0234  113 LYS A N   
878  C  CA  . LYS A 113 ? 0.1790 0.1009 0.1678 0.0096  -0.0111 0.0210  113 LYS A CA  
879  C  C   . LYS A 113 ? 0.1711 0.0903 0.1518 -0.0194 -0.0030 0.0125  113 LYS A C   
880  O  O   . LYS A 113 ? 0.2679 0.0861 0.2691 -0.0192 -0.0518 0.0160  113 LYS A O   
881  C  CB  . LYS A 113 ? 0.1655 0.1154 0.2215 0.0197  -0.0064 -0.0250 113 LYS A CB  
882  C  CG  . LYS A 113 ? 0.1716 0.1493 0.1621 0.0306  -0.0009 -0.0111 113 LYS A CG  
883  C  CD  . LYS A 113 ? 0.1565 0.1287 0.2581 0.0351  0.0027  -0.0204 113 LYS A CD  
884  C  CE  . LYS A 113 ? 0.1648 0.1835 0.2886 -0.0296 -0.0194 0.0293  113 LYS A CE  
885  N  NZ  . LYS A 113 ? 0.3727 0.1831 0.6220 0.0630  -0.1901 -0.0179 113 LYS A NZ  
886  N  N   . TYR A 114 ? 0.1468 0.1102 0.1597 0.0129  0.0195  0.0272  114 TYR A N   
887  C  CA  . TYR A 114 ? 0.1377 0.0826 0.1676 0.0110  0.0082  -0.0006 114 TYR A CA  
888  C  C   . TYR A 114 ? 0.1400 0.0443 0.1811 -0.0062 0.0107  -0.0142 114 TYR A C   
889  O  O   . TYR A 114 ? 0.1332 0.0849 0.1848 -0.0138 0.0227  -0.0220 114 TYR A O   
890  C  CB  . TYR A 114 ? 0.1350 0.0682 0.1783 0.0119  0.0317  -0.0080 114 TYR A CB  
891  C  CG  . TYR A 114 ? 0.1368 0.0935 0.1582 -0.0011 -0.0037 0.0167  114 TYR A CG  
892  C  CD1 . TYR A 114 ? 0.2117 0.1070 0.1551 0.0352  0.0151  0.0097  114 TYR A CD1 
893  C  CD2 . TYR A 114 ? 0.1468 0.1075 0.1970 -0.0143 0.0279  0.0389  114 TYR A CD2 
894  C  CE1 . TYR A 114 ? 0.2391 0.1729 0.1885 0.0559  0.0455  0.0328  114 TYR A CE1 
895  C  CE2 . TYR A 114 ? 0.2088 0.1831 0.2362 -0.0061 0.0803  0.0728  114 TYR A CE2 
896  C  CZ  . TYR A 114 ? 0.2520 0.1784 0.2104 0.0345  0.0723  0.0866  114 TYR A CZ  
897  O  OH  . TYR A 114 ? 0.3304 0.3355 0.2806 0.1062  0.1561  0.0986  114 TYR A OH  
898  N  N   . ALA A 115 ? 0.1637 0.0594 0.1499 -0.0160 0.0089  -0.0155 115 ALA A N   
899  C  CA  . ALA A 115 ? 0.1493 0.0765 0.1500 -0.0214 0.0034  -0.0053 115 ALA A CA  
900  C  C   . ALA A 115 ? 0.1450 0.0628 0.1546 -0.0098 0.0062  -0.0162 115 ALA A C   
901  O  O   . ALA A 115 ? 0.1483 0.0648 0.1712 -0.0078 0.0243  -0.0140 115 ALA A O   
902  C  CB  . ALA A 115 ? 0.1447 0.0957 0.1881 -0.0128 -0.0133 -0.0199 115 ALA A CB  
903  N  N   . ALA A 116 ? 0.1389 0.0488 0.1569 -0.0151 0.0062  -0.0122 116 ALA A N   
904  C  CA  . ALA A 116 ? 0.1608 0.0497 0.1287 -0.0002 0.0286  -0.0038 116 ALA A CA  
905  C  C   . ALA A 116 ? 0.1219 0.0650 0.1278 -0.0103 0.0170  -0.0022 116 ALA A C   
906  O  O   . ALA A 116 ? 0.1204 0.0700 0.1386 -0.0071 0.0222  -0.0030 116 ALA A O   
907  C  CB  . ALA A 116 ? 0.1619 0.0849 0.1496 -0.0074 -0.0048 -0.0148 116 ALA A CB  
908  N  N   . GLU A 117 ? 0.1217 0.0617 0.1307 -0.0057 0.0093  0.0065  117 GLU A N   
909  C  CA  . GLU A 117 ? 0.1404 0.0566 0.1260 0.0102  0.0043  0.0001  117 GLU A CA  
910  C  C   . GLU A 117 ? 0.1027 0.0621 0.1342 -0.0128 0.0013  0.0024  117 GLU A C   
911  O  O   . GLU A 117 ? 0.1104 0.0838 0.1668 -0.0038 0.0237  0.0173  117 GLU A O   
912  C  CB  . GLU A 117 ? 0.1251 0.0653 0.1235 -0.0037 0.0158  0.0068  117 GLU A CB  
913  C  CG  . GLU A 117 ? 0.1518 0.0603 0.1221 0.0163  0.0008  0.0087  117 GLU A CG  
914  C  CD  . GLU A 117 ? 0.1364 0.0818 0.1172 0.0000  0.0153  0.0080  117 GLU A CD  
915  O  OE1 . GLU A 117 ? 0.1242 0.0957 0.1443 0.0069  -0.0016 -0.0006 117 GLU A OE1 
916  O  OE2 . GLU A 117 ? 0.1562 0.0853 0.1363 -0.0053 -0.0042 -0.0006 117 GLU A OE2 
917  N  N   . LEU A 118 ? 0.1120 0.0682 0.1289 0.0051  -0.0040 0.0039  118 LEU A N   
918  C  CA  . LEU A 118 ? 0.1088 0.0610 0.1252 0.0081  -0.0032 0.0000  118 LEU A CA  
919  C  C   . LEU A 118 ? 0.0962 0.0754 0.1223 0.0027  0.0150  0.0019  118 LEU A C   
920  O  O   . LEU A 118 ? 0.1144 0.0609 0.1276 -0.0030 0.0134  0.0083  118 LEU A O   
921  C  CB  . LEU A 118 ? 0.1125 0.0734 0.1550 0.0003  -0.0184 0.0079  118 LEU A CB  
922  C  CG  . LEU A 118 ? 0.1036 0.0809 0.1456 -0.0001 -0.0118 0.0152  118 LEU A CG  
923  C  CD1 . LEU A 118 ? 0.1389 0.0864 0.1486 -0.0024 -0.0077 0.0228  118 LEU A CD1 
924  C  CD2 . LEU A 118 ? 0.1100 0.1384 0.1629 -0.0141 -0.0178 0.0049  118 LEU A CD2 
925  N  N   . HIS A 119 ? 0.1188 0.0531 0.1136 -0.0032 0.0048  0.0036  119 HIS A N   
926  C  CA  . HIS A 119 ? 0.1086 0.0657 0.1274 0.0015  -0.0074 -0.0095 119 HIS A CA  
927  C  C   . HIS A 119 ? 0.0944 0.0750 0.1081 -0.0055 0.0044  0.0008  119 HIS A C   
928  O  O   . HIS A 119 ? 0.1330 0.0876 0.1145 0.0066  0.0135  0.0006  119 HIS A O   
929  C  CB  . HIS A 119 ? 0.1029 0.0662 0.1364 0.0076  -0.0029 -0.0057 119 HIS A CB  
930  C  CG  . HIS A 119 ? 0.0795 0.0689 0.1274 -0.0033 0.0107  -0.0051 119 HIS A CG  
931  N  ND1 . HIS A 119 ? 0.0824 0.0765 0.1235 -0.0100 0.0139  0.0053  119 HIS A ND1 
932  C  CD2 . HIS A 119 ? 0.0828 0.0860 0.1226 -0.0051 0.0097  0.0054  119 HIS A CD2 
933  C  CE1 . HIS A 119 ? 0.1221 0.0709 0.1040 0.0002  -0.0004 0.0064  119 HIS A CE1 
934  N  NE2 . HIS A 119 ? 0.0976 0.0846 0.1203 0.0128  0.0026  -0.0011 119 HIS A NE2 
935  N  N   . LEU A 120 ? 0.1041 0.0576 0.1312 0.0016  0.0138  0.0030  120 LEU A N   
936  C  CA  . LEU A 120 ? 0.1037 0.0639 0.1381 0.0106  0.0143  0.0000  120 LEU A CA  
937  C  C   . LEU A 120 ? 0.1174 0.0630 0.1237 0.0168  0.0182  -0.0001 120 LEU A C   
938  O  O   . LEU A 120 ? 0.1176 0.0713 0.1298 0.0005  0.0055  0.0133  120 LEU A O   
939  C  CB  . LEU A 120 ? 0.1045 0.0697 0.1664 -0.0040 -0.0009 -0.0074 120 LEU A CB  
940  C  CG  . LEU A 120 ? 0.1258 0.1065 0.1432 -0.0225 -0.0159 0.0035  120 LEU A CG  
941  C  CD1 . LEU A 120 ? 0.2491 0.1064 0.1816 -0.0650 0.0143  0.0100  120 LEU A CD1 
942  C  CD2 . LEU A 120 ? 0.1612 0.1418 0.1877 0.0366  -0.0583 -0.0343 120 LEU A CD2 
943  N  N   . VAL A 121 ? 0.1231 0.0621 0.1603 -0.0140 0.0017  0.0087  121 VAL A N   
944  C  CA  . VAL A 121 ? 0.1081 0.0641 0.1486 -0.0074 0.0144  -0.0044 121 VAL A CA  
945  C  C   . VAL A 121 ? 0.1244 0.0700 0.1285 -0.0035 0.0214  0.0216  121 VAL A C   
946  O  O   . VAL A 121 ? 0.1529 0.0761 0.1391 0.0070  -0.0010 0.0062  121 VAL A O   
947  C  CB  . VAL A 121 ? 0.1072 0.0702 0.1738 0.0004  0.0150  -0.0026 121 VAL A CB  
948  C  CG1 . VAL A 121 ? 0.1405 0.0750 0.2398 -0.0223 0.0164  -0.0258 121 VAL A CG1 
949  C  CG2 . VAL A 121 ? 0.1425 0.0603 0.1894 0.0182  -0.0069 0.0073  121 VAL A CG2 
950  N  N   . HIS A 122 ? 0.1146 0.0698 0.1386 0.0096  0.0111  0.0031  122 HIS A N   
951  C  CA  . HIS A 122 ? 0.1174 0.0551 0.1569 0.0048  0.0083  -0.0052 122 HIS A CA  
952  C  C   . HIS A 122 ? 0.1122 0.0646 0.1400 0.0049  0.0218  0.0113  122 HIS A C   
953  O  O   . HIS A 122 ? 0.1349 0.0874 0.1737 -0.0073 -0.0102 0.0179  122 HIS A O   
954  C  CB  . HIS A 122 ? 0.1122 0.0575 0.1847 0.0026  0.0130  0.0071  122 HIS A CB  
955  C  CG  . HIS A 122 ? 0.1231 0.0553 0.1636 -0.0042 0.0190  0.0193  122 HIS A CG  
956  N  ND1 . HIS A 122 ? 0.1137 0.0594 0.1799 0.0100  0.0121  0.0217  122 HIS A ND1 
957  C  CD2 . HIS A 122 ? 0.1305 0.0901 0.1587 -0.0103 0.0136  -0.0027 122 HIS A CD2 
958  C  CE1 . HIS A 122 ? 0.1009 0.1174 0.1679 0.0011  0.0099  -0.0051 122 HIS A CE1 
959  N  NE2 . HIS A 122 ? 0.1041 0.1072 0.1696 -0.0195 0.0017  0.0034  122 HIS A NE2 
960  N  N   . TRP A 123 ? 0.1368 0.0539 0.1442 -0.0074 0.0111  0.0026  123 TRP A N   
961  C  CA  . TRP A 123 ? 0.1235 0.0612 0.1610 -0.0194 0.0148  -0.0012 123 TRP A CA  
962  C  C   . TRP A 123 ? 0.1518 0.0743 0.1560 0.0042  0.0172  0.0170  123 TRP A C   
963  O  O   . TRP A 123 ? 0.1567 0.0515 0.2009 0.0029  0.0156  -0.0017 123 TRP A O   
964  C  CB  . TRP A 123 ? 0.1302 0.1364 0.1471 -0.0234 0.0188  0.0050  123 TRP A CB  
965  C  CG  . TRP A 123 ? 0.1741 0.0804 0.1539 -0.0279 0.0097  0.0108  123 TRP A CG  
966  C  CD1 . TRP A 123 ? 0.1978 0.1206 0.1360 -0.0325 -0.0111 0.0138  123 TRP A CD1 
967  C  CD2 . TRP A 123 ? 0.1747 0.0662 0.1781 -0.0447 -0.0053 0.0084  123 TRP A CD2 
968  N  NE1 . TRP A 123 ? 0.2323 0.0822 0.1561 -0.0381 -0.0244 0.0117  123 TRP A NE1 
969  C  CE2 . TRP A 123 ? 0.2006 0.0935 0.1903 -0.0466 -0.0248 -0.0074 123 TRP A CE2 
970  C  CE3 . TRP A 123 ? 0.1910 0.0677 0.2043 -0.0321 -0.0104 -0.0033 123 TRP A CE3 
971  C  CZ2 . TRP A 123 ? 0.2823 0.1018 0.2093 -0.0432 0.0026  0.0242  123 TRP A CZ2 
972  C  CZ3 . TRP A 123 ? 0.3055 0.0655 0.2072 -0.0577 -0.0092 0.0352  123 TRP A CZ3 
973  C  CH2 . TRP A 123 ? 0.2816 0.1122 0.1932 -0.0267 0.0040  0.0179  123 TRP A CH2 
974  N  N   . ASN A 124 ? 0.1579 0.0646 0.1526 -0.0197 0.0211  -0.0044 124 ASN A N   
975  C  CA  . ASN A 124 ? 0.2032 0.0809 0.1775 0.0052  0.0329  -0.0051 124 ASN A CA  
976  C  C   . ASN A 124 ? 0.1813 0.0822 0.1980 -0.0188 0.0253  -0.0117 124 ASN A C   
977  O  O   . ASN A 124 ? 0.1795 0.0739 0.1747 -0.0206 0.0365  -0.0274 124 ASN A O   
978  C  CB  . ASN A 124 ? 0.2437 0.1165 0.1443 -0.0347 0.0387  -0.0010 124 ASN A CB  
979  C  CG  . ASN A 124 ? 0.2525 0.1465 0.2151 -0.0411 0.0770  0.0030  124 ASN A CG  
980  O  OD1 . ASN A 124 ? 0.2543 0.1421 0.2319 -0.0274 0.0782  -0.0421 124 ASN A OD1 
981  N  ND2 . ASN A 124 ? 0.3231 0.1219 0.1973 -0.0296 0.0714  -0.0342 124 ASN A ND2 
982  N  N   . THR A 125 ? 0.1838 0.0487 0.2484 0.0136  0.0324  -0.0111 125 THR A N   
983  C  CA  . THR A 125 ? 0.2171 0.0894 0.2535 0.0339  0.0065  -0.0053 125 THR A CA  
984  C  C   . THR A 125 ? 0.1898 0.1095 0.2625 0.0087  0.0705  -0.0239 125 THR A C   
985  O  O   . THR A 125 ? 0.2172 0.0854 0.3299 0.0025  0.0320  -0.0031 125 THR A O   
986  C  CB  . THR A 125 ? 0.2161 0.1669 0.2991 0.0546  -0.0107 -0.0050 125 THR A CB  
987  O  OG1 . THR A 125 ? 0.2846 0.1450 0.4340 0.0223  0.1084  -0.0220 125 THR A OG1 
988  C  CG2 . THR A 125 ? 0.2963 0.1496 0.3925 -0.0073 -0.0602 -0.0087 125 THR A CG2 
989  N  N   . LYS A 126 ? 0.2532 0.0988 0.2189 0.0055  0.0620  -0.0333 126 LYS A N   
990  C  CA  . LYS A 126 ? 0.2429 0.1364 0.2497 -0.0316 0.0825  -0.0572 126 LYS A CA  
991  C  C   . LYS A 126 ? 0.2005 0.1350 0.2719 0.0110  0.0528  -0.0032 126 LYS A C   
992  O  O   . LYS A 126 ? 0.3379 0.1618 0.3503 -0.0675 0.1267  -0.0590 126 LYS A O   
993  C  CB  . LYS A 126 ? 0.3208 0.1544 0.2511 -0.0423 0.0531  -0.0741 126 LYS A CB  
994  C  CG  . LYS A 126 ? 0.4028 0.2538 0.2280 0.0210  0.0334  -0.0586 126 LYS A CG  
995  C  CD  . LYS A 126 ? 0.3468 0.3917 0.2441 -0.0750 0.0576  -0.0015 126 LYS A CD  
996  C  CE  . LYS A 126 ? 0.5157 0.5240 0.2312 0.0505  0.0719  0.0772  126 LYS A CE  
997  N  NZ  . LYS A 126 ? 0.7832 0.8713 0.2075 0.0055  0.0845  0.0517  126 LYS A NZ  
998  N  N   . TYR A 127 ? 0.2127 0.0958 0.1941 -0.0108 0.0375  -0.0082 127 TYR A N   
999  C  CA  . TYR A 127 ? 0.1888 0.0885 0.1856 -0.0173 0.0198  -0.0008 127 TYR A CA  
1000 C  C   . TYR A 127 ? 0.2176 0.0806 0.1978 -0.0379 0.0282  0.0011  127 TYR A C   
1001 O  O   . TYR A 127 ? 0.1898 0.1189 0.2161 -0.0379 0.0113  0.0068  127 TYR A O   
1002 C  CB  . TYR A 127 ? 0.2312 0.0901 0.1802 -0.0105 0.0160  -0.0200 127 TYR A CB  
1003 C  CG  . TYR A 127 ? 0.2912 0.0810 0.1799 -0.0085 0.0035  -0.0293 127 TYR A CG  
1004 C  CD1 . TYR A 127 ? 0.2950 0.1138 0.2034 -0.0376 0.0089  -0.0484 127 TYR A CD1 
1005 C  CD2 . TYR A 127 ? 0.2394 0.1159 0.1978 -0.0341 0.0120  -0.0029 127 TYR A CD2 
1006 C  CE1 . TYR A 127 ? 0.3791 0.1131 0.1984 0.0157  0.0058  0.0011  127 TYR A CE1 
1007 C  CE2 . TYR A 127 ? 0.2813 0.1115 0.1659 0.0120  0.0257  -0.0295 127 TYR A CE2 
1008 C  CZ  . TYR A 127 ? 0.3772 0.1083 0.1632 -0.0128 0.0385  -0.0318 127 TYR A CZ  
1009 O  OH  . TYR A 127 ? 0.4492 0.1590 0.1738 0.0140  0.0066  -0.0442 127 TYR A OH  
1010 N  N   . GLY A 128 ? 0.1949 0.0892 0.1892 -0.0200 0.0197  -0.0036 128 GLY A N   
1011 C  CA  . GLY A 128 ? 0.2152 0.0765 0.1962 -0.0008 0.0185  0.0187  128 GLY A CA  
1012 C  C   . GLY A 128 ? 0.2136 0.1000 0.2039 -0.0372 0.0030  0.0038  128 GLY A C   
1013 O  O   . GLY A 128 ? 0.2512 0.1091 0.2251 -0.0093 -0.0005 0.0109  128 GLY A O   
1014 N  N   . ASP A 129 ? 0.2141 0.1159 0.1738 -0.0129 0.0076  -0.0140 129 ASP A N   
1015 C  CA  . ASP A 129 ? 0.2450 0.0944 0.1529 0.0000  -0.0145 0.0018  129 ASP A CA  
1016 C  C   . ASP A 129 ? 0.1956 0.0969 0.1758 -0.0082 -0.0222 -0.0208 129 ASP A C   
1017 O  O   . ASP A 129 ? 0.2507 0.1025 0.1687 -0.0286 -0.0301 -0.0092 129 ASP A O   
1018 C  CB  . ASP A 129 ? 0.2284 0.1346 0.1626 -0.0037 0.0016  0.0159  129 ASP A CB  
1019 C  CG  . ASP A 129 ? 0.2257 0.1126 0.2301 0.0178  -0.0185 -0.0343 129 ASP A CG  
1020 O  OD1 . ASP A 129 ? 0.2773 0.1246 0.2138 -0.0024 0.0039  0.0157  129 ASP A OD1 
1021 O  OD2 . ASP A 129 ? 0.2318 0.1386 0.2818 -0.0228 0.0076  0.0017  129 ASP A OD2 
1022 N  N   . TYR A 130 ? 0.2269 0.0761 0.1622 -0.0111 0.0013  -0.0102 130 TYR A N   
1023 C  CA  . TYR A 130 ? 0.2073 0.0556 0.2046 -0.0234 0.0023  0.0042  130 TYR A CA  
1024 C  C   . TYR A 130 ? 0.1919 0.1267 0.1619 -0.0358 0.0161  0.0113  130 TYR A C   
1025 O  O   . TYR A 130 ? 0.1874 0.1323 0.1700 -0.0220 0.0152  0.0066  130 TYR A O   
1026 C  CB  . TYR A 130 ? 0.2232 0.0826 0.1793 -0.0389 0.0397  -0.0149 130 TYR A CB  
1027 C  CG  . TYR A 130 ? 0.2108 0.0885 0.1928 -0.0586 0.0335  -0.0071 130 TYR A CG  
1028 C  CD1 . TYR A 130 ? 0.3126 0.1093 0.1802 -0.0519 0.0521  0.0091  130 TYR A CD1 
1029 C  CD2 . TYR A 130 ? 0.2362 0.1424 0.2703 -0.0069 0.0490  -0.0895 130 TYR A CD2 
1030 C  CE1 . TYR A 130 ? 0.2902 0.1547 0.2525 -0.0762 0.0878  -0.0392 130 TYR A CE1 
1031 C  CE2 . TYR A 130 ? 0.2987 0.1987 0.2709 -0.0380 0.0732  -0.1039 130 TYR A CE2 
1032 C  CZ  . TYR A 130 ? 0.2488 0.2498 0.2337 -0.0751 0.1005  -0.0945 130 TYR A CZ  
1033 O  OH  . TYR A 130 ? 0.3898 0.3040 0.2764 -0.0829 0.1619  -0.1071 130 TYR A OH  
1034 N  N   . GLY A 131 ? 0.1777 0.1339 0.2086 -0.0451 0.0171  0.0167  131 GLY A N   
1035 C  CA  . GLY A 131 ? 0.1935 0.2080 0.1896 -0.0626 -0.0109 0.0381  131 GLY A CA  
1036 C  C   . GLY A 131 ? 0.2287 0.1865 0.1989 -0.0641 0.0167  0.0227  131 GLY A C   
1037 O  O   . GLY A 131 ? 0.2183 0.3237 0.2429 -0.0490 -0.0158 0.0109  131 GLY A O   
1038 N  N   A LYS A 132 ? 0.1977 0.1468 0.2240 -0.0675 -0.0125 0.0283  132 LYS A N   
1039 N  N   B LYS A 132 ? 0.1962 0.1483 0.2172 -0.0732 -0.0141 0.0236  132 LYS A N   
1040 C  CA  A LYS A 132 ? 0.2509 0.1608 0.2115 -0.0966 -0.0218 0.0421  132 LYS A CA  
1041 C  CA  B LYS A 132 ? 0.2416 0.1520 0.2082 -0.1080 -0.0179 0.0331  132 LYS A CA  
1042 C  C   A LYS A 132 ? 0.2341 0.2248 0.2222 -0.1327 0.0094  0.0771  132 LYS A C   
1043 C  C   B LYS A 132 ? 0.2444 0.2125 0.2418 -0.1517 0.0381  0.0730  132 LYS A C   
1044 O  O   A LYS A 132 ? 0.3492 0.2931 0.1942 -0.1139 -0.0828 0.0038  132 LYS A O   
1045 O  O   B LYS A 132 ? 0.3488 0.3231 0.2521 -0.0983 -0.0688 0.0096  132 LYS A O   
1046 C  CB  A LYS A 132 ? 0.2882 0.2187 0.2898 -0.0107 -0.0270 -0.0131 132 LYS A CB  
1047 C  CB  B LYS A 132 ? 0.3185 0.1611 0.2317 -0.0430 -0.0263 -0.0340 132 LYS A CB  
1048 C  CG  A LYS A 132 ? 0.4459 0.3052 0.2497 0.0092  0.0588  0.0885  132 LYS A CG  
1049 C  CG  B LYS A 132 ? 0.3723 0.1107 0.1507 -0.0148 0.0316  0.0318  132 LYS A CG  
1050 C  CD  A LYS A 132 ? 0.4263 0.2253 0.3822 0.0507  0.0928  0.0498  132 LYS A CD  
1051 C  CD  B LYS A 132 ? 0.4443 0.2698 0.2258 -0.1251 -0.0498 -0.0399 132 LYS A CD  
1052 C  CE  A LYS A 132 ? 0.7100 0.3462 0.1776 0.0694  0.0392  0.0214  132 LYS A CE  
1053 C  CE  B LYS A 132 ? 0.4540 0.3228 0.4752 -0.1656 -0.0817 0.0536  132 LYS A CE  
1054 N  NZ  A LYS A 132 ? 0.4202 0.1732 0.3599 -0.0173 0.0087  -0.0451 132 LYS A NZ  
1055 N  NZ  B LYS A 132 ? 0.4595 0.3289 0.5126 -0.0967 -0.0430 0.0943  132 LYS A NZ  
1056 N  N   . ALA A 133 ? 0.2442 0.1380 0.1916 -0.1047 0.0080  0.0073  133 ALA A N   
1057 C  CA  . ALA A 133 ? 0.1831 0.1238 0.1659 -0.0497 0.0098  0.0168  133 ALA A CA  
1058 C  C   . ALA A 133 ? 0.1885 0.1186 0.1805 -0.0590 0.0033  0.0220  133 ALA A C   
1059 O  O   . ALA A 133 ? 0.2136 0.2355 0.1647 -0.0710 0.0001  0.0291  133 ALA A O   
1060 C  CB  . ALA A 133 ? 0.2068 0.1072 0.1725 -0.0722 -0.0175 0.0085  133 ALA A CB  
1061 N  N   A VAL A 134 ? 0.1761 0.1196 0.1895 -0.0552 0.0046  0.0190  134 VAL A N   
1062 N  N   B VAL A 134 ? 0.1626 0.1313 0.2020 -0.0527 0.0002  0.0104  134 VAL A N   
1063 C  CA  A VAL A 134 ? 0.1946 0.1679 0.1707 -0.0118 0.0162  0.0352  134 VAL A CA  
1064 C  CA  B VAL A 134 ? 0.1289 0.1720 0.2321 -0.0578 -0.0100 0.0543  134 VAL A CA  
1065 C  C   A VAL A 134 ? 0.2007 0.1822 0.2085 -0.0829 0.0157  0.0967  134 VAL A C   
1066 C  C   B VAL A 134 ? 0.2042 0.1957 0.2366 -0.0233 -0.0394 0.0231  134 VAL A C   
1067 O  O   A VAL A 134 ? 0.1447 0.2146 0.2809 -0.0668 0.0231  0.0781  134 VAL A O   
1068 O  O   B VAL A 134 ? 0.2452 0.2136 0.2846 0.0075  -0.0886 -0.0059 134 VAL A O   
1069 C  CB  A VAL A 134 ? 0.1736 0.1260 0.2050 -0.0120 0.0237  0.0256  134 VAL A CB  
1070 C  CB  B VAL A 134 ? 0.1675 0.2011 0.2840 -0.0226 -0.0329 -0.0267 134 VAL A CB  
1071 C  CG1 A VAL A 134 ? 0.2189 0.0357 0.1844 -0.0304 -0.0030 0.0065  134 VAL A CG1 
1072 C  CG1 B VAL A 134 ? 0.2612 0.4105 0.3879 -0.0642 0.0739  0.0869  134 VAL A CG1 
1073 C  CG2 A VAL A 134 ? 0.2889 0.1991 0.2743 -0.0047 0.0366  0.1628  134 VAL A CG2 
1074 C  CG2 B VAL A 134 ? 0.1533 0.2305 0.2952 0.0181  0.0337  -0.0880 134 VAL A CG2 
1075 N  N   A GLN A 135 ? 0.2152 0.2023 0.1683 -0.0806 -0.0048 0.0365  135 GLN A N   
1076 N  N   B GLN A 135 ? 0.1558 0.1959 0.2595 -0.0544 -0.0284 0.0658  135 GLN A N   
1077 C  CA  A GLN A 135 ? 0.2251 0.2689 0.1917 -0.1251 0.0076  0.0089  135 GLN A CA  
1078 C  CA  B GLN A 135 ? 0.2093 0.2244 0.2430 -0.0782 -0.0443 0.0719  135 GLN A CA  
1079 C  C   A GLN A 135 ? 0.1956 0.2726 0.2043 -0.0611 0.0105  0.0352  135 GLN A C   
1080 C  C   B GLN A 135 ? 0.2147 0.1970 0.2236 -0.0966 -0.0741 0.0318  135 GLN A C   
1081 O  O   A GLN A 135 ? 0.1905 0.4490 0.1910 -0.0944 -0.0152 0.0427  135 GLN A O   
1082 O  O   B GLN A 135 ? 0.4196 0.2711 0.2323 -0.0992 -0.1548 0.0236  135 GLN A O   
1083 C  CB  A GLN A 135 ? 0.1712 0.2745 0.2759 -0.1604 -0.0008 -0.0326 135 GLN A CB  
1084 C  CB  B GLN A 135 ? 0.1795 0.2122 0.3018 -0.0902 -0.0413 0.0722  135 GLN A CB  
1085 C  CG  A GLN A 135 ? 0.3333 0.4143 0.2857 -0.0550 0.0421  0.0286  135 GLN A CG  
1086 C  CG  B GLN A 135 ? 0.1993 0.3440 0.3044 -0.0623 -0.0275 0.1188  135 GLN A CG  
1087 C  CD  A GLN A 135 ? 0.2075 0.3543 0.3590 -0.1384 0.1137  0.0434  135 GLN A CD  
1088 C  CD  B GLN A 135 ? 0.2438 0.3911 0.4424 -0.1033 -0.0724 0.1911  135 GLN A CD  
1089 O  OE1 A GLN A 135 ? 0.4012 0.4606 0.5540 0.0555  0.0179  0.2065  135 GLN A OE1 
1090 O  OE1 B GLN A 135 ? 0.2207 0.3146 0.3495 -0.0615 -0.0170 0.0915  135 GLN A OE1 
1091 N  NE2 A GLN A 135 ? 0.2077 0.4577 0.4818 -0.0785 0.0521  -0.1685 135 GLN A NE2 
1092 N  NE2 B GLN A 135 ? 0.1784 0.3977 0.4032 -0.0697 -0.0186 0.1267  135 GLN A NE2 
1093 N  N   . GLN A 136 ? 0.1970 0.1776 0.1892 -0.0592 -0.0184 0.0390  136 GLN A N   
1094 C  CA  . GLN A 136 ? 0.2361 0.1000 0.1849 -0.0280 -0.0329 -0.0075 136 GLN A CA  
1095 C  C   . GLN A 136 ? 0.2222 0.1165 0.1830 0.0119  -0.0284 -0.0024 136 GLN A C   
1096 O  O   . GLN A 136 ? 0.2215 0.1158 0.1733 -0.0087 0.0063  -0.0153 136 GLN A O   
1097 C  CB  . GLN A 136 ? 0.2728 0.0988 0.2199 0.0006  -0.0669 0.0128  136 GLN A CB  
1098 C  CG  . GLN A 136 ? 0.3064 0.1049 0.2163 -0.0381 -0.0122 0.0155  136 GLN A CG  
1099 C  CD  . GLN A 136 ? 0.3364 0.1630 0.2068 -0.0640 -0.0276 0.0070  136 GLN A CD  
1100 O  OE1 . GLN A 136 ? 0.3291 0.1799 0.2333 -0.0342 -0.0601 -0.0434 136 GLN A OE1 
1101 N  NE2 . GLN A 136 ? 0.4353 0.3346 0.2371 -0.1303 0.0161  0.0385  136 GLN A NE2 
1102 N  N   . PRO A 137 ? 0.2187 0.1769 0.1589 0.0457  0.0038  -0.0199 137 PRO A N   
1103 C  CA  . PRO A 137 ? 0.2462 0.1932 0.1628 0.0612  0.0084  0.0038  137 PRO A CA  
1104 C  C   . PRO A 137 ? 0.2357 0.2089 0.1385 0.0141  0.0547  0.0289  137 PRO A C   
1105 O  O   . PRO A 137 ? 0.2619 0.1869 0.2591 0.0242  0.0547  0.0370  137 PRO A O   
1106 C  CB  . PRO A 137 ? 0.2559 0.3880 0.1447 0.0589  -0.0280 0.0217  137 PRO A CB  
1107 C  CG  . PRO A 137 ? 0.4465 0.4326 0.2072 -0.0456 -0.0579 -0.0422 137 PRO A CG  
1108 C  CD  . PRO A 137 ? 0.3198 0.3095 0.1786 -0.0153 -0.0531 -0.0627 137 PRO A CD  
1109 N  N   . ASP A 138 ? 0.1921 0.1960 0.1590 0.0065  0.0044  -0.0124 138 ASP A N   
1110 C  CA  . ASP A 138 ? 0.1974 0.2192 0.1249 0.0033  0.0206  -0.0017 138 ASP A CA  
1111 C  C   . ASP A 138 ? 0.1648 0.1513 0.1344 -0.0276 0.0058  -0.0228 138 ASP A C   
1112 O  O   . ASP A 138 ? 0.1637 0.1899 0.1944 0.0171  0.0212  0.0099  138 ASP A O   
1113 C  CB  . ASP A 138 ? 0.2508 0.2053 0.1611 0.0341  0.0493  0.0013  138 ASP A CB  
1114 C  CG  . ASP A 138 ? 0.2409 0.2390 0.1678 0.0429  0.0400  -0.0008 138 ASP A CG  
1115 O  OD1 . ASP A 138 ? 0.2739 0.1775 0.2064 0.0356  0.0467  -0.0006 138 ASP A OD1 
1116 O  OD2 . ASP A 138 ? 0.2758 0.2509 0.2448 0.0474  0.0508  -0.0666 138 ASP A OD2 
1117 N  N   . GLY A 139 ? 0.1966 0.1055 0.1172 -0.0147 0.0218  -0.0046 139 GLY A N   
1118 C  CA  . GLY A 139 ? 0.2006 0.1061 0.1213 -0.0305 -0.0049 -0.0068 139 GLY A CA  
1119 C  C   . GLY A 139 ? 0.1421 0.0869 0.1371 -0.0146 0.0034  0.0057  139 GLY A C   
1120 O  O   . GLY A 139 ? 0.1691 0.0777 0.1497 -0.0026 -0.0126 -0.0135 139 GLY A O   
1121 N  N   . LEU A 140 ? 0.1201 0.0820 0.1389 -0.0074 0.0267  -0.0148 140 LEU A N   
1122 C  CA  . LEU A 140 ? 0.1111 0.0745 0.1271 -0.0027 0.0204  -0.0115 140 LEU A CA  
1123 C  C   . LEU A 140 ? 0.1296 0.0635 0.1398 0.0066  0.0209  -0.0065 140 LEU A C   
1124 O  O   . LEU A 140 ? 0.1271 0.0757 0.1483 0.0026  0.0013  -0.0027 140 LEU A O   
1125 C  CB  . LEU A 140 ? 0.1213 0.0915 0.1364 0.0020  0.0270  -0.0183 140 LEU A CB  
1126 C  CG  . LEU A 140 ? 0.1374 0.1337 0.1605 0.0227  0.0486  -0.0051 140 LEU A CG  
1127 C  CD1 . LEU A 140 ? 0.1594 0.1208 0.1894 0.0261  0.0526  -0.0106 140 LEU A CD1 
1128 C  CD2 . LEU A 140 ? 0.1858 0.1260 0.1817 0.0166  0.0234  0.0214  140 LEU A CD2 
1129 N  N   . ALA A 141 ? 0.1307 0.0661 0.1456 -0.0091 0.0063  0.0008  141 ALA A N   
1130 C  CA  . ALA A 141 ? 0.1307 0.0537 0.1557 -0.0092 0.0209  -0.0082 141 ALA A CA  
1131 C  C   . ALA A 141 ? 0.1125 0.0700 0.1321 -0.0174 0.0034  0.0156  141 ALA A C   
1132 O  O   . ALA A 141 ? 0.1488 0.0657 0.1317 0.0069  -0.0035 0.0086  141 ALA A O   
1133 C  CB  . ALA A 141 ? 0.1187 0.1025 0.1992 -0.0047 0.0315  0.0084  141 ALA A CB  
1134 N  N   . VAL A 142 ? 0.1258 0.0673 0.1547 -0.0065 0.0000  -0.0002 142 VAL A N   
1135 C  CA  . VAL A 142 ? 0.1242 0.0680 0.1558 -0.0201 0.0145  -0.0128 142 VAL A CA  
1136 C  C   . VAL A 142 ? 0.1246 0.0565 0.1217 0.0038  0.0032  0.0128  142 VAL A C   
1137 O  O   . VAL A 142 ? 0.1292 0.0905 0.1222 0.0119  -0.0162 0.0187  142 VAL A O   
1138 C  CB  . VAL A 142 ? 0.1058 0.0946 0.1391 -0.0155 0.0012  0.0004  142 VAL A CB  
1139 C  CG1 . VAL A 142 ? 0.1324 0.1099 0.1528 0.0111  -0.0032 -0.0254 142 VAL A CG1 
1140 C  CG2 . VAL A 142 ? 0.1339 0.1163 0.1386 -0.0298 0.0154  0.0157  142 VAL A CG2 
1141 N  N   . LEU A 143 ? 0.1210 0.0648 0.1280 -0.0044 -0.0095 0.0069  143 LEU A N   
1142 C  CA  . LEU A 143 ? 0.1126 0.0729 0.1463 -0.0108 0.0103  -0.0031 143 LEU A CA  
1143 C  C   . LEU A 143 ? 0.1393 0.0741 0.1186 -0.0190 0.0026  0.0010  143 LEU A C   
1144 O  O   . LEU A 143 ? 0.1664 0.0855 0.1253 -0.0176 0.0216  0.0074  143 LEU A O   
1145 C  CB  . LEU A 143 ? 0.1170 0.1167 0.1720 -0.0039 0.0049  0.0238  143 LEU A CB  
1146 C  CG  . LEU A 143 ? 0.1238 0.1221 0.2054 -0.0066 0.0095  0.0156  143 LEU A CG  
1147 C  CD1 . LEU A 143 ? 0.1449 0.1698 0.2265 -0.0342 0.0037  0.0671  143 LEU A CD1 
1148 C  CD2 . LEU A 143 ? 0.1201 0.2168 0.2222 0.0003  -0.0187 0.0226  143 LEU A CD2 
1149 N  N   . GLY A 144 ? 0.1174 0.0691 0.1360 -0.0110 0.0004  0.0098  144 GLY A N   
1150 C  CA  . GLY A 144 ? 0.1267 0.0593 0.1296 -0.0200 0.0093  -0.0066 144 GLY A CA  
1151 C  C   . GLY A 144 ? 0.1037 0.0624 0.1186 -0.0057 0.0110  0.0148  144 GLY A C   
1152 O  O   . GLY A 144 ? 0.1328 0.0982 0.1284 -0.0134 0.0270  -0.0013 144 GLY A O   
1153 N  N   . ILE A 145 ? 0.1138 0.0590 0.1357 -0.0030 0.0000  -0.0135 145 ILE A N   
1154 C  CA  . ILE A 145 ? 0.0996 0.0730 0.1303 -0.0108 -0.0063 -0.0156 145 ILE A CA  
1155 C  C   . ILE A 145 ? 0.0919 0.0653 0.1411 -0.0225 0.0117  0.0031  145 ILE A C   
1156 O  O   . ILE A 145 ? 0.1210 0.0797 0.1472 -0.0033 0.0326  0.0036  145 ILE A O   
1157 C  CB  . ILE A 145 ? 0.1186 0.0824 0.1532 -0.0033 -0.0057 0.0013  145 ILE A CB  
1158 C  CG1 . ILE A 145 ? 0.1650 0.1260 0.1775 0.0451  0.0074  -0.0024 145 ILE A CG1 
1159 C  CG2 . ILE A 145 ? 0.1186 0.1004 0.2242 -0.0198 -0.0266 -0.0058 145 ILE A CG2 
1160 C  CD1 . ILE A 145 ? 0.1550 0.1071 0.1632 0.0163  0.0062  0.0162  145 ILE A CD1 
1161 N  N   . PHE A 146 ? 0.1120 0.0531 0.1386 -0.0138 0.0142  -0.0053 146 PHE A N   
1162 C  CA  . PHE A 146 ? 0.1180 0.0549 0.1313 -0.0019 0.0125  -0.0046 146 PHE A CA  
1163 C  C   . PHE A 146 ? 0.1375 0.0479 0.1357 -0.0264 0.0114  0.0036  146 PHE A C   
1164 O  O   . PHE A 146 ? 0.1197 0.0982 0.1687 -0.0132 0.0092  -0.0117 146 PHE A O   
1165 C  CB  . PHE A 146 ? 0.1395 0.0867 0.1402 -0.0142 -0.0124 0.0168  146 PHE A CB  
1166 C  CG  . PHE A 146 ? 0.1203 0.0530 0.1335 -0.0082 0.0000  0.0086  146 PHE A CG  
1167 C  CD1 . PHE A 146 ? 0.1192 0.0901 0.1583 -0.0152 0.0026  0.0008  146 PHE A CD1 
1168 C  CD2 . PHE A 146 ? 0.1359 0.0817 0.1486 -0.0272 0.0104  0.0388  146 PHE A CD2 
1169 C  CE1 . PHE A 146 ? 0.1644 0.0978 0.1265 0.0069  -0.0044 0.0170  146 PHE A CE1 
1170 C  CE2 . PHE A 146 ? 0.1285 0.0820 0.1543 -0.0214 0.0044  0.0108  146 PHE A CE2 
1171 C  CZ  . PHE A 146 ? 0.1212 0.0849 0.1371 -0.0087 0.0058  0.0137  146 PHE A CZ  
1172 N  N   . LEU A 147 ? 0.1276 0.0849 0.1339 -0.0165 0.0182  -0.0106 147 LEU A N   
1173 C  CA  . LEU A 147 ? 0.1468 0.0675 0.1393 -0.0129 0.0023  -0.0085 147 LEU A CA  
1174 C  C   . LEU A 147 ? 0.1450 0.0835 0.1406 -0.0127 0.0000  0.0155  147 LEU A C   
1175 O  O   . LEU A 147 ? 0.1447 0.0732 0.1732 -0.0176 0.0048  -0.0002 147 LEU A O   
1176 C  CB  . LEU A 147 ? 0.1556 0.0781 0.1493 -0.0001 0.0062  0.0047  147 LEU A CB  
1177 C  CG  . LEU A 147 ? 0.1342 0.0686 0.1601 -0.0238 -0.0066 0.0068  147 LEU A CG  
1178 C  CD1 . LEU A 147 ? 0.1917 0.0849 0.1858 -0.0464 -0.0137 -0.0118 147 LEU A CD1 
1179 C  CD2 . LEU A 147 ? 0.1784 0.1007 0.1526 -0.0256 -0.0041 0.0114  147 LEU A CD2 
1180 N  N   . LYS A 148 ? 0.1654 0.0705 0.1666 -0.0308 -0.0085 0.0017  148 LYS A N   
1181 C  CA  . LYS A 148 ? 0.1849 0.0731 0.1618 -0.0189 -0.0044 0.0094  148 LYS A CA  
1182 C  C   . LYS A 148 ? 0.1522 0.0939 0.2179 -0.0285 -0.0425 -0.0048 148 LYS A C   
1183 O  O   . LYS A 148 ? 0.2053 0.1352 0.2066 0.0293  -0.0604 -0.0298 148 LYS A O   
1184 C  CB  . LYS A 148 ? 0.2018 0.1604 0.1608 -0.0301 -0.0096 0.0243  148 LYS A CB  
1185 C  CG  . LYS A 148 ? 0.1856 0.1840 0.1912 -0.0348 0.0387  0.0046  148 LYS A CG  
1186 C  CD  . LYS A 148 ? 0.2913 0.2513 0.2657 -0.0623 0.0085  0.1128  148 LYS A CD  
1187 C  CE  . LYS A 148 ? 0.3249 0.4440 0.4213 -0.0526 0.0903  0.1242  148 LYS A CE  
1188 N  NZ  . LYS A 148 ? 0.4806 0.4688 0.4748 -0.1489 0.0672  0.1761  148 LYS A NZ  
1189 N  N   . VAL A 149 ? 0.2226 0.0732 0.2136 -0.0134 -0.0356 -0.0160 149 VAL A N   
1190 C  CA  . VAL A 149 ? 0.1747 0.1028 0.2111 -0.0166 -0.0268 -0.0155 149 VAL A CA  
1191 C  C   . VAL A 149 ? 0.2098 0.0960 0.1590 -0.0341 -0.0122 -0.0013 149 VAL A C   
1192 O  O   . VAL A 149 ? 0.2608 0.1133 0.2240 -0.0413 -0.0425 0.0408  149 VAL A O   
1193 C  CB  . VAL A 149 ? 0.1741 0.1162 0.2077 -0.0107 -0.0195 0.0004  149 VAL A CB  
1194 C  CG1 . VAL A 149 ? 0.2167 0.1382 0.2506 0.0002  -0.0405 -0.0458 149 VAL A CG1 
1195 C  CG2 . VAL A 149 ? 0.1895 0.1149 0.2297 0.0002  0.0022  0.0107  149 VAL A CG2 
1196 N  N   . GLY A 150 ? 0.2108 0.0851 0.2122 -0.0461 -0.0369 0.0119  150 GLY A N   
1197 C  CA  . GLY A 150 ? 0.1944 0.1303 0.1964 -0.0524 -0.0228 0.0229  150 GLY A CA  
1198 C  C   . GLY A 150 ? 0.2111 0.0856 0.1848 -0.0408 -0.0106 0.0079  150 GLY A C   
1199 O  O   . GLY A 150 ? 0.2124 0.0987 0.1939 -0.0231 -0.0162 0.0068  150 GLY A O   
1200 N  N   . SER A 151 ? 0.2011 0.1059 0.2344 -0.0310 -0.0184 0.0110  151 SER A N   
1201 C  CA  . SER A 151 ? 0.1998 0.1071 0.2325 -0.0278 -0.0105 0.0022  151 SER A CA  
1202 C  C   . SER A 151 ? 0.1952 0.0952 0.2206 -0.0276 -0.0220 -0.0157 151 SER A C   
1203 O  O   . SER A 151 ? 0.2039 0.1155 0.2142 -0.0212 -0.0425 -0.0220 151 SER A O   
1204 C  CB  . SER A 151 ? 0.1926 0.2196 0.2930 0.0055  -0.0038 -0.0576 151 SER A CB  
1205 O  OG  . SER A 151 ? 0.2996 0.2682 0.3165 -0.0590 0.0297  -0.0464 151 SER A OG  
1206 N  N   . ALA A 152 ? 0.1892 0.1199 0.2298 -0.0337 -0.0256 0.0102  152 ALA A N   
1207 C  CA  . ALA A 152 ? 0.2221 0.1135 0.1791 -0.0334 -0.0300 -0.0089 152 ALA A CA  
1208 C  C   . ALA A 152 ? 0.1808 0.1348 0.2036 -0.0427 -0.0374 -0.0144 152 ALA A C   
1209 O  O   . ALA A 152 ? 0.1874 0.1400 0.3037 -0.0446 -0.0087 -0.0055 152 ALA A O   
1210 C  CB  . ALA A 152 ? 0.2526 0.2034 0.1737 0.0011  -0.0433 -0.0257 152 ALA A CB  
1211 N  N   . LYS A 153 ? 0.1826 0.0901 0.2268 -0.0152 -0.0302 0.0162  153 LYS A N   
1212 C  CA  . LYS A 153 ? 0.1820 0.1158 0.1957 -0.0193 -0.0140 -0.0021 153 LYS A CA  
1213 C  C   . LYS A 153 ? 0.1551 0.1718 0.2406 -0.0298 -0.0386 0.0096  153 LYS A C   
1214 O  O   . LYS A 153 ? 0.1831 0.1013 0.2353 -0.0301 -0.0425 0.0164  153 LYS A O   
1215 C  CB  . LYS A 153 ? 0.1630 0.1151 0.2171 -0.0091 -0.0464 0.0079  153 LYS A CB  
1216 C  CG  . LYS A 153 ? 0.2176 0.1115 0.2394 -0.0287 -0.0300 -0.0005 153 LYS A CG  
1217 C  CD  . LYS A 153 ? 0.2506 0.1615 0.2394 -0.0344 -0.0111 -0.0091 153 LYS A CD  
1218 C  CE  . LYS A 153 ? 0.2899 0.1820 0.2649 0.0262  -0.0324 -0.0037 153 LYS A CE  
1219 N  NZ  . LYS A 153 ? 0.2813 0.3508 0.3165 -0.0318 -0.0214 0.1145  153 LYS A NZ  
1220 N  N   . PRO A 154 ? 0.1522 0.1531 0.2470 -0.0403 -0.0409 0.0096  154 PRO A N   
1221 C  CA  . PRO A 154 ? 0.1618 0.1808 0.3362 -0.0634 -0.1005 0.0507  154 PRO A CA  
1222 C  C   . PRO A 154 ? 0.1583 0.1787 0.3006 -0.0318 -0.0561 0.0690  154 PRO A C   
1223 O  O   . PRO A 154 ? 0.1867 0.2169 0.3149 -0.0212 -0.0351 0.1094  154 PRO A O   
1224 C  CB  . PRO A 154 ? 0.1496 0.1787 0.4189 -0.0173 -0.0793 0.0710  154 PRO A CB  
1225 C  CG  . PRO A 154 ? 0.1766 0.2716 0.3512 -0.0301 -0.0524 0.1072  154 PRO A CG  
1226 C  CD  . PRO A 154 ? 0.1467 0.1945 0.3172 -0.0282 -0.0042 0.0565  154 PRO A CD  
1227 N  N   . GLY A 155 ? 0.1626 0.1332 0.3093 -0.0055 -0.0513 0.0425  155 GLY A N   
1228 C  CA  . GLY A 155 ? 0.1504 0.1342 0.3804 0.0005  -0.0128 0.0299  155 GLY A CA  
1229 C  C   . GLY A 155 ? 0.1647 0.1032 0.2825 -0.0201 -0.0185 0.0441  155 GLY A C   
1230 O  O   . GLY A 155 ? 0.2179 0.1058 0.3971 -0.0311 -0.0035 0.0471  155 GLY A O   
1231 N  N   . LEU A 156 ? 0.1392 0.1204 0.2695 -0.0029 -0.0220 0.0384  156 LEU A N   
1232 C  CA  . LEU A 156 ? 0.1533 0.0892 0.2327 -0.0038 -0.0115 0.0234  156 LEU A CA  
1233 C  C   . LEU A 156 ? 0.1708 0.1016 0.2206 -0.0233 -0.0433 0.0188  156 LEU A C   
1234 O  O   . LEU A 156 ? 0.1571 0.1388 0.2161 -0.0129 -0.0335 0.0242  156 LEU A O   
1235 C  CB  . LEU A 156 ? 0.1316 0.1111 0.2445 -0.0307 -0.0355 0.0286  156 LEU A CB  
1236 C  CG  . LEU A 156 ? 0.1331 0.1044 0.1944 -0.0182 -0.0127 -0.0009 156 LEU A CG  
1237 C  CD1 . LEU A 156 ? 0.1521 0.1258 0.2154 -0.0504 -0.0310 0.0136  156 LEU A CD1 
1238 C  CD2 . LEU A 156 ? 0.1725 0.1012 0.2301 -0.0001 -0.0289 0.0091  156 LEU A CD2 
1239 N  N   . GLN A 157 ? 0.2045 0.0878 0.2445 -0.0495 -0.0577 0.0276  157 GLN A N   
1240 C  CA  . GLN A 157 ? 0.2271 0.1518 0.2427 -0.0587 -0.0469 0.0310  157 GLN A CA  
1241 C  C   . GLN A 157 ? 0.2068 0.1431 0.2185 -0.0317 -0.0619 0.0129  157 GLN A C   
1242 O  O   . GLN A 157 ? 0.2082 0.1201 0.2200 -0.0352 -0.0537 0.0109  157 GLN A O   
1243 C  CB  . GLN A 157 ? 0.2373 0.1429 0.3063 -0.0399 -0.0910 0.0083  157 GLN A CB  
1244 C  CG  . GLN A 157 ? 0.2685 0.1553 0.3418 -0.0454 -0.0657 -0.0057 157 GLN A CG  
1245 C  CD  . GLN A 157 ? 0.2649 0.1339 0.2416 -0.0488 -0.0461 0.0044  157 GLN A CD  
1246 O  OE1 . GLN A 157 ? 0.2948 0.1165 0.2154 -0.0544 -0.0396 0.0108  157 GLN A OE1 
1247 N  NE2 . GLN A 157 ? 0.3177 0.2063 0.2298 -0.0736 -0.0298 -0.0282 157 GLN A NE2 
1248 N  N   . LYS A 158 ? 0.2075 0.1332 0.2158 -0.0322 -0.0636 0.0081  158 LYS A N   
1249 C  CA  . LYS A 158 ? 0.1808 0.1772 0.2244 -0.0137 -0.0534 0.0480  158 LYS A CA  
1250 C  C   . LYS A 158 ? 0.2034 0.1284 0.2142 -0.0012 -0.0523 0.0125  158 LYS A C   
1251 O  O   . LYS A 158 ? 0.2792 0.1436 0.1786 -0.0464 -0.0465 0.0053  158 LYS A O   
1252 C  CB  . LYS A 158 ? 0.2720 0.1830 0.2993 0.0168  -0.0809 0.0373  158 LYS A CB  
1253 C  CG  . LYS A 158 ? 0.2764 0.3965 0.3619 0.0165  -0.0628 0.0203  158 LYS A CG  
1254 C  CD  . LYS A 158 ? 0.7179 0.5246 0.5893 0.2758  -0.0813 0.3470  158 LYS A CD  
1255 C  CE  . LYS A 158 ? 0.8442 0.9300 1.0983 0.1318  -0.4220 0.0077  158 LYS A CE  
1256 N  NZ  . LYS A 158 ? 0.7535 0.8104 0.5238 -0.1722 -0.2285 0.0266  158 LYS A NZ  
1257 N  N   . VAL A 159 ? 0.2061 0.0804 0.1928 -0.0248 -0.0607 0.0005  159 VAL A N   
1258 C  CA  . VAL A 159 ? 0.1896 0.1217 0.1722 -0.0370 -0.0249 -0.0078 159 VAL A CA  
1259 C  C   . VAL A 159 ? 0.1974 0.1174 0.1769 -0.0247 -0.0147 0.0064  159 VAL A C   
1260 O  O   . VAL A 159 ? 0.1993 0.1219 0.1996 -0.0299 -0.0141 0.0053  159 VAL A O   
1261 C  CB  . VAL A 159 ? 0.1903 0.1226 0.1618 -0.0402 -0.0204 0.0002  159 VAL A CB  
1262 C  CG1 . VAL A 159 ? 0.1734 0.1948 0.2149 -0.0604 -0.0059 0.0414  159 VAL A CG1 
1263 C  CG2 . VAL A 159 ? 0.2509 0.1226 0.1874 -0.0026 -0.0297 -0.0240 159 VAL A CG2 
1264 N  N   . VAL A 160 ? 0.2257 0.0989 0.1759 -0.0136 -0.0299 -0.0017 160 VAL A N   
1265 C  CA  . VAL A 160 ? 0.2350 0.1240 0.2348 -0.0093 0.0182  0.0070  160 VAL A CA  
1266 C  C   . VAL A 160 ? 0.2096 0.1553 0.2381 -0.0754 -0.0282 0.0091  160 VAL A C   
1267 O  O   . VAL A 160 ? 0.2708 0.1226 0.2092 -0.0560 -0.0024 -0.0117 160 VAL A O   
1268 C  CB  . VAL A 160 ? 0.3138 0.1255 0.2152 0.0006  0.0268  0.0435  160 VAL A CB  
1269 C  CG1 . VAL A 160 ? 0.3124 0.1802 0.3123 -0.0211 -0.0381 -0.0006 160 VAL A CG1 
1270 C  CG2 . VAL A 160 ? 0.3270 0.1395 0.2219 0.0238  -0.0146 0.0274  160 VAL A CG2 
1271 N  N   . ASP A 161 ? 0.2542 0.1425 0.1804 -0.0570 -0.0604 -0.0170 161 ASP A N   
1272 C  CA  . ASP A 161 ? 0.3397 0.1400 0.1923 -0.0514 -0.0466 -0.0116 161 ASP A CA  
1273 C  C   . ASP A 161 ? 0.3024 0.1743 0.2002 -0.0531 -0.0283 -0.0005 161 ASP A C   
1274 O  O   . ASP A 161 ? 0.5635 0.2508 0.1881 -0.0819 -0.0048 -0.0002 161 ASP A O   
1275 C  CB  . ASP A 161 ? 0.4072 0.2798 0.2257 -0.0712 -0.1148 0.0068  161 ASP A CB  
1276 C  CG  . ASP A 161 ? 0.4720 0.2038 0.2761 -0.0151 -0.0548 -0.0641 161 ASP A CG  
1277 O  OD1 . ASP A 161 ? 0.4458 0.2797 0.4597 -0.0444 -0.0119 -0.0343 161 ASP A OD1 
1278 O  OD2 . ASP A 161 ? 0.4031 0.4247 0.5447 0.0122  -0.1417 -0.0750 161 ASP A OD2 
1279 N  N   A VAL A 162 ? 0.2369 0.1258 0.2096 -0.0210 -0.0438 0.0222  162 VAL A N   
1280 N  N   B VAL A 162 ? 0.2583 0.1366 0.2107 -0.0303 -0.0716 0.0288  162 VAL A N   
1281 C  CA  A VAL A 162 ? 0.2138 0.1295 0.1483 0.0069  -0.0080 0.0107  162 VAL A CA  
1282 C  CA  B VAL A 162 ? 0.2595 0.1896 0.1945 -0.0397 -0.0413 0.0182  162 VAL A CA  
1283 C  C   A VAL A 162 ? 0.2108 0.1453 0.1712 0.0148  0.0113  0.0176  162 VAL A C   
1284 C  C   B VAL A 162 ? 0.2649 0.1709 0.1511 0.0053  -0.0094 0.0253  162 VAL A C   
1285 O  O   A VAL A 162 ? 0.2077 0.1493 0.1632 0.0150  -0.0065 0.0124  162 VAL A O   
1286 O  O   B VAL A 162 ? 0.3177 0.1549 0.1607 -0.0081 -0.0245 0.0292  162 VAL A O   
1287 C  CB  A VAL A 162 ? 0.2468 0.1005 0.1872 0.0129  -0.0020 0.0301  162 VAL A CB  
1288 C  CB  B VAL A 162 ? 0.3063 0.1632 0.2769 0.0013  -0.0532 0.0961  162 VAL A CB  
1289 C  CG1 A VAL A 162 ? 0.2524 0.1122 0.1788 0.0252  0.0064  -0.0390 162 VAL A CG1 
1290 C  CG1 B VAL A 162 ? 0.2569 0.1120 0.4002 -0.0197 -0.0105 0.0317  162 VAL A CG1 
1291 C  CG2 A VAL A 162 ? 0.2250 0.1303 0.1757 0.0561  0.0690  0.0335  162 VAL A CG2 
1292 C  CG2 B VAL A 162 ? 0.3405 0.0856 0.2925 -0.0295 -0.0396 0.0701  162 VAL A CG2 
1293 N  N   . LEU A 163 ? 0.2585 0.1450 0.1666 0.0102  -0.0237 -0.0006 163 LEU A N   
1294 C  CA  . LEU A 163 ? 0.2005 0.1280 0.1691 0.0026  0.0153  0.0077  163 LEU A CA  
1295 C  C   . LEU A 163 ? 0.2450 0.1274 0.1733 -0.0048 0.0144  0.0198  163 LEU A C   
1296 O  O   . LEU A 163 ? 0.2508 0.1637 0.1734 0.0013  0.0125  0.0143  163 LEU A O   
1297 C  CB  . LEU A 163 ? 0.2592 0.1081 0.1770 0.0033  0.0158  0.0064  163 LEU A CB  
1298 C  CG  . LEU A 163 ? 0.2525 0.1036 0.1503 -0.0135 0.0108  0.0121  163 LEU A CG  
1299 C  CD1 . LEU A 163 ? 0.2631 0.1673 0.2104 0.0301  -0.0188 0.0534  163 LEU A CD1 
1300 C  CD2 . LEU A 163 ? 0.2333 0.1324 0.1691 -0.0117 -0.0053 -0.0085 163 LEU A CD2 
1301 N  N   . ASP A 164 ? 0.3925 0.1474 0.1740 -0.0074 0.0207  -0.0161 164 ASP A N   
1302 C  CA  . ASP A 164 ? 0.3771 0.2703 0.2160 0.0053  0.0807  0.0330  164 ASP A CA  
1303 C  C   . ASP A 164 ? 0.3905 0.2371 0.1704 0.0158  0.0414  -0.0114 164 ASP A C   
1304 O  O   . ASP A 164 ? 0.4238 0.2964 0.2687 0.0546  0.0996  0.0445  164 ASP A O   
1305 C  CB  . ASP A 164 ? 0.6753 0.4820 0.1987 -0.1047 0.1147  -0.1687 164 ASP A CB  
1306 C  CG  . ASP A 164 ? 0.9782 0.5578 1.3090 -0.2801 -0.7469 -0.3703 164 ASP A CG  
1307 O  OD1 . ASP A 164 ? 0.6941 0.9992 0.8054 0.0182  -0.0483 -0.1312 164 ASP A OD1 
1308 O  OD2 . ASP A 164 ? 1.0362 2.1587 0.1425 0.2407  0.2758  0.1807  164 ASP A OD2 
1309 N  N   . SER A 165 ? 0.2663 0.2104 0.1723 -0.0209 -0.0365 0.0033  165 SER A N   
1310 C  CA  . SER A 165 ? 0.2576 0.2307 0.1855 -0.0012 -0.0209 0.0340  165 SER A CA  
1311 C  C   . SER A 165 ? 0.2175 0.2042 0.1386 0.0122  0.0257  0.0300  165 SER A C   
1312 O  O   . SER A 165 ? 0.2896 0.2050 0.1745 0.0118  0.0209  0.0650  165 SER A O   
1313 C  CB  . SER A 165 ? 0.3269 0.3387 0.2282 0.0718  0.0140  0.0318  165 SER A CB  
1314 O  OG  . SER A 165 ? 0.2848 0.2253 0.2713 0.0195  -0.0423 0.0323  165 SER A OG  
1315 N  N   . ILE A 166 ? 0.2041 0.1603 0.1324 0.0151  0.0102  0.0256  166 ILE A N   
1316 C  CA  . ILE A 166 ? 0.1985 0.1357 0.1698 0.0161  0.0293  0.0182  166 ILE A CA  
1317 C  C   . ILE A 166 ? 0.1935 0.1346 0.1407 0.0011  0.0111  0.0084  166 ILE A C   
1318 O  O   . ILE A 166 ? 0.1754 0.1429 0.1427 0.0079  0.0064  0.0141  166 ILE A O   
1319 C  CB  . ILE A 166 ? 0.1888 0.1176 0.1601 -0.0043 0.0176  0.0017  166 ILE A CB  
1320 C  CG1 . ILE A 166 ? 0.2206 0.1273 0.1411 -0.0111 0.0321  -0.0059 166 ILE A CG1 
1321 C  CG2 . ILE A 166 ? 0.2233 0.1168 0.2432 0.0261  -0.0098 0.0093  166 ILE A CG2 
1322 C  CD1 . ILE A 166 ? 0.2481 0.1709 0.1672 0.0268  0.0435  -0.0278 166 ILE A CD1 
1323 N  N   . LYS A 167 ? 0.2426 0.1332 0.1727 0.0345  0.0271  -0.0010 167 LYS A N   
1324 C  CA  . LYS A 167 ? 0.2086 0.1417 0.1637 0.0323  0.0048  -0.0174 167 LYS A CA  
1325 C  C   . LYS A 167 ? 0.1890 0.1407 0.1319 -0.0037 0.0444  0.0192  167 LYS A C   
1326 O  O   . LYS A 167 ? 0.2018 0.1216 0.1486 0.0002  0.0072  0.0176  167 LYS A O   
1327 C  CB  . LYS A 167 ? 0.2449 0.1503 0.1650 0.0385  0.0158  -0.0264 167 LYS A CB  
1328 C  CG  . LYS A 167 ? 0.2254 0.1621 0.2291 0.0395  -0.0012 -0.0119 167 LYS A CG  
1329 C  CD  . LYS A 167 ? 0.3426 0.1639 0.3051 0.0293  -0.0228 -0.0828 167 LYS A CD  
1330 C  CE  . LYS A 167 ? 0.5252 0.2781 0.4461 0.1468  -0.0196 -0.0687 167 LYS A CE  
1331 N  N   . THR A 168 ? 0.1655 0.1091 0.1528 0.0095  0.0441  0.0046  168 THR A N   
1332 C  CA  . THR A 168 ? 0.1562 0.1543 0.1636 -0.0221 0.0612  -0.0107 168 THR A CA  
1333 C  C   . THR A 168 ? 0.1759 0.1255 0.1337 0.0201  0.0335  0.0022  168 THR A C   
1334 O  O   . THR A 168 ? 0.1852 0.1298 0.1720 0.0189  0.0398  0.0222  168 THR A O   
1335 C  CB  . THR A 168 ? 0.1797 0.1320 0.1684 0.0297  0.0612  0.0234  168 THR A CB  
1336 O  OG1 . THR A 168 ? 0.2147 0.1711 0.1575 0.0285  0.0432  0.0305  168 THR A OG1 
1337 C  CG2 . THR A 168 ? 0.2558 0.1212 0.1772 0.0345  0.0735  0.0080  168 THR A CG2 
1338 N  N   A LYS A 169 ? 0.1878 0.1145 0.1525 -0.0223 0.0350  -0.0024 169 LYS A N   
1339 N  N   B LYS A 169 ? 0.1826 0.1271 0.1486 -0.0222 0.0402  0.0135  169 LYS A N   
1340 C  CA  A LYS A 169 ? 0.1923 0.0899 0.1726 -0.0315 0.0193  0.0139  169 LYS A CA  
1341 C  CA  B LYS A 169 ? 0.1781 0.1137 0.1535 -0.0212 0.0363  0.0217  169 LYS A CA  
1342 C  C   A LYS A 169 ? 0.1770 0.1070 0.1858 0.0024  0.0537  0.0296  169 LYS A C   
1343 C  C   B LYS A 169 ? 0.1650 0.1234 0.1743 0.0026  0.0580  0.0350  169 LYS A C   
1344 O  O   A LYS A 169 ? 0.2278 0.0907 0.1937 -0.0137 0.0715  0.0305  169 LYS A O   
1345 O  O   B LYS A 169 ? 0.1727 0.2024 0.1949 -0.0211 0.0823  0.0365  169 LYS A O   
1346 C  CB  A LYS A 169 ? 0.1996 0.1083 0.1991 -0.0044 -0.0012 0.0066  169 LYS A CB  
1347 C  CB  B LYS A 169 ? 0.1761 0.1525 0.1738 -0.0029 0.0326  0.0113  169 LYS A CB  
1348 C  CG  A LYS A 169 ? 0.2559 0.1092 0.2332 -0.0550 -0.0279 0.0339  169 LYS A CG  
1349 C  CG  B LYS A 169 ? 0.1955 0.1450 0.2149 -0.0313 0.0467  0.0229  169 LYS A CG  
1350 C  CD  A LYS A 169 ? 0.2623 0.1725 0.2866 -0.0829 -0.0244 0.0311  169 LYS A CD  
1351 C  CD  B LYS A 169 ? 0.1869 0.2566 0.2039 -0.0166 0.0702  -0.0142 169 LYS A CD  
1352 C  CE  A LYS A 169 ? 0.3503 0.3142 0.3276 -0.1324 -0.1174 -0.0326 169 LYS A CE  
1353 C  CE  B LYS A 169 ? 0.1740 0.2256 0.2578 -0.0505 0.0864  -0.0514 169 LYS A CE  
1354 N  NZ  A LYS A 169 ? 0.3160 0.4449 0.4955 0.1423  -0.0527 -0.0468 169 LYS A NZ  
1355 N  NZ  B LYS A 169 ? 0.1926 0.3644 0.3613 -0.0657 0.0760  0.0158  169 LYS A NZ  
1356 N  N   . GLY A 170 ? 0.1812 0.0907 0.2079 -0.0008 0.0505  0.0195  170 GLY A N   
1357 C  CA  . GLY A 170 ? 0.2201 0.1111 0.2469 -0.0174 0.0173  0.0596  170 GLY A CA  
1358 C  C   . GLY A 170 ? 0.2232 0.1176 0.2079 0.0019  0.0340  0.0540  170 GLY A C   
1359 O  O   . GLY A 170 ? 0.3039 0.1292 0.2699 0.0064  0.0284  0.0783  170 GLY A O   
1360 N  N   A LYS A 171 ? 0.2036 0.1303 0.1960 -0.0161 0.0579  0.0550  171 LYS A N   
1361 N  N   B LYS A 171 ? 0.2099 0.1106 0.1946 0.0027  0.0484  0.0425  171 LYS A N   
1362 C  CA  A LYS A 171 ? 0.2046 0.1694 0.1644 -0.0197 0.0606  0.0313  171 LYS A CA  
1363 C  CA  B LYS A 171 ? 0.1944 0.1280 0.1745 -0.0081 0.0576  0.0336  171 LYS A CA  
1364 C  C   A LYS A 171 ? 0.1985 0.1337 0.1536 0.0171  0.0266  0.0306  171 LYS A C   
1365 C  C   B LYS A 171 ? 0.2011 0.1395 0.1124 0.0158  0.0297  0.0353  171 LYS A C   
1366 O  O   A LYS A 171 ? 0.2042 0.1359 0.1490 -0.0197 0.0299  0.0006  171 LYS A O   
1367 O  O   B LYS A 171 ? 0.1601 0.0926 0.1344 0.0043  0.0075  0.0413  171 LYS A O   
1368 C  CB  A LYS A 171 ? 0.2147 0.1214 0.2143 0.0118  0.0621  0.0441  171 LYS A CB  
1369 C  CB  B LYS A 171 ? 0.1824 0.1463 0.1963 0.0113  0.0401  0.0052  171 LYS A CB  
1370 C  CG  A LYS A 171 ? 0.2425 0.1927 0.2534 0.0372  0.0728  0.0019  171 LYS A CG  
1371 C  CG  B LYS A 171 ? 0.2219 0.1599 0.2106 0.0181  0.0604  -0.0164 171 LYS A CG  
1372 C  CD  A LYS A 171 ? 0.2547 0.2894 0.2355 0.0727  0.0464  -0.0314 171 LYS A CD  
1373 C  CD  B LYS A 171 ? 0.2017 0.2222 0.2454 0.0031  0.0458  0.0359  171 LYS A CD  
1374 C  CE  A LYS A 171 ? 0.2042 0.3758 0.3155 0.1053  0.0950  0.0600  171 LYS A CE  
1375 C  CE  B LYS A 171 ? 0.2877 0.3458 0.2395 -0.0432 0.1100  0.0403  171 LYS A CE  
1376 N  NZ  A LYS A 171 ? 0.4070 0.5877 0.4671 0.2060  -0.2027 0.1265  171 LYS A NZ  
1377 N  NZ  B LYS A 171 ? 0.3716 0.4593 0.2200 0.0121  0.1001  0.0714  171 LYS A NZ  
1378 N  N   . SER A 172 ? 0.2211 0.1522 0.1529 0.0302  0.0306  0.0529  172 SER A N   
1379 C  CA  . SER A 172 ? 0.2249 0.1812 0.1364 0.0266  0.0110  0.0242  172 SER A CA  
1380 C  C   . SER A 172 ? 0.2093 0.1185 0.1450 0.0217  0.0072  0.0151  172 SER A C   
1381 O  O   . SER A 172 ? 0.2401 0.2305 0.1424 0.0690  0.0251  0.0222  172 SER A O   
1382 C  CB  . SER A 172 ? 0.2391 0.1845 0.1607 0.0141  0.0181  0.0201  172 SER A CB  
1383 O  OG  . SER A 172 ? 0.3059 0.1791 0.1949 0.0376  0.0100  0.0243  172 SER A OG  
1384 N  N   . ALA A 173 ? 0.1953 0.1951 0.1812 0.0505  0.0145  0.0332  173 ALA A N   
1385 C  CA  . ALA A 173 ? 0.2253 0.1956 0.1585 0.0512  0.0041  0.0044  173 ALA A CA  
1386 C  C   . ALA A 173 ? 0.2082 0.1587 0.1493 0.0160  -0.0004 0.0194  173 ALA A C   
1387 O  O   . ALA A 173 ? 0.2136 0.1392 0.1377 0.0372  -0.0050 0.0089  173 ALA A O   
1388 C  CB  . ALA A 173 ? 0.3256 0.1851 0.1763 0.0171  -0.0026 0.0111  173 ALA A CB  
1389 N  N   . ASP A 174 ? 0.2027 0.1780 0.1899 0.0447  -0.0034 0.0244  174 ASP A N   
1390 C  CA  . ASP A 174 ? 0.2113 0.2680 0.1772 0.0638  -0.0143 0.0142  174 ASP A CA  
1391 C  C   . ASP A 174 ? 0.1909 0.1770 0.2382 0.0515  -0.0025 -0.0195 174 ASP A C   
1392 O  O   . ASP A 174 ? 0.2330 0.2157 0.2652 0.0312  -0.0147 -0.0710 174 ASP A O   
1393 C  CB  . ASP A 174 ? 0.3403 0.3823 0.1944 0.1716  -0.0209 0.0409  174 ASP A CB  
1394 C  CG  . ASP A 174 ? 0.7765 0.6221 0.4040 0.0540  -0.3523 0.2633  174 ASP A CG  
1395 O  OD1 . ASP A 174 ? 0.8620 0.6140 0.4750 0.0447  -0.1855 0.1585  174 ASP A OD1 
1396 O  OD2 . ASP A 174 ? 0.9116 0.5225 0.3602 0.0739  -0.1462 0.0065  174 ASP A OD2 
1397 N  N   . PHE A 175 ? 0.1453 0.1623 0.2081 0.0208  0.0099  0.0103  175 PHE A N   
1398 C  CA  . PHE A 175 ? 0.1587 0.1321 0.1811 0.0134  -0.0082 0.0061  175 PHE A CA  
1399 C  C   . PHE A 175 ? 0.1769 0.1213 0.1964 0.0164  -0.0060 0.0097  175 PHE A C   
1400 O  O   . PHE A 175 ? 0.2706 0.2043 0.2303 0.0831  -0.0911 -0.0458 175 PHE A O   
1401 C  CB  . PHE A 175 ? 0.2159 0.0987 0.2233 0.0039  -0.0419 0.0223  175 PHE A CB  
1402 C  CG  . PHE A 175 ? 0.1956 0.0856 0.2205 0.0272  -0.0181 0.0089  175 PHE A CG  
1403 C  CD1 . PHE A 175 ? 0.2280 0.1143 0.1959 -0.0038 0.0190  -0.0038 175 PHE A CD1 
1404 C  CD2 . PHE A 175 ? 0.1808 0.1280 0.2226 0.0379  -0.0400 0.0015  175 PHE A CD2 
1405 C  CE1 . PHE A 175 ? 0.2679 0.1164 0.2188 -0.0328 0.0254  -0.0006 175 PHE A CE1 
1406 C  CE2 . PHE A 175 ? 0.1709 0.1434 0.2125 0.0324  -0.0225 0.0081  175 PHE A CE2 
1407 C  CZ  . PHE A 175 ? 0.2327 0.1700 0.2158 -0.0197 -0.0017 -0.0057 175 PHE A CZ  
1408 N  N   . THR A 176 ? 0.1891 0.1414 0.1777 0.0297  -0.0074 0.0312  176 THR A N   
1409 C  CA  . THR A 176 ? 0.1662 0.1375 0.1899 0.0400  -0.0006 0.0574  176 THR A CA  
1410 C  C   . THR A 176 ? 0.1683 0.1127 0.1482 0.0254  -0.0078 0.0394  176 THR A C   
1411 O  O   . THR A 176 ? 0.1919 0.1432 0.1913 0.0132  -0.0351 0.0267  176 THR A O   
1412 C  CB  . THR A 176 ? 0.1932 0.2164 0.2132 0.0679  -0.0029 0.1040  176 THR A CB  
1413 O  OG1 . THR A 176 ? 0.3716 0.2540 0.1802 0.1270  -0.0002 0.0707  176 THR A OG1 
1414 C  CG2 . THR A 176 ? 0.2186 0.2636 0.3159 0.0105  0.0514  0.1145  176 THR A CG2 
1415 N  N   . ASN A 177 ? 0.1665 0.1791 0.1511 0.0139  0.0038  0.0307  177 ASN A N   
1416 C  CA  . ASN A 177 ? 0.1562 0.1514 0.1919 0.0156  -0.0262 0.0469  177 ASN A CA  
1417 C  C   . ASN A 177 ? 0.2046 0.1278 0.1823 0.0167  -0.0428 0.0210  177 ASN A C   
1418 O  O   . ASN A 177 ? 0.2383 0.1715 0.3211 -0.0205 -0.0725 0.0672  177 ASN A O   
1419 C  CB  . ASN A 177 ? 0.1841 0.1766 0.2125 0.0286  -0.0703 0.0519  177 ASN A CB  
1420 C  CG  . ASN A 177 ? 0.1905 0.1712 0.1996 0.0559  -0.0352 0.0414  177 ASN A CG  
1421 O  OD1 . ASN A 177 ? 0.2634 0.2039 0.2861 0.0868  -0.0048 0.0278  177 ASN A OD1 
1422 N  ND2 . ASN A 177 ? 0.2507 0.1866 0.1590 0.0095  -0.0367 0.0422  177 ASN A ND2 
1423 N  N   . PHE A 178 ? 0.1939 0.1280 0.1583 -0.0111 -0.0346 0.0482  178 PHE A N   
1424 C  CA  . PHE A 178 ? 0.1901 0.1392 0.1398 -0.0064 -0.0339 0.0580  178 PHE A CA  
1425 C  C   . PHE A 178 ? 0.1860 0.1319 0.1368 -0.0399 -0.0342 0.0340  178 PHE A C   
1426 O  O   . PHE A 178 ? 0.2154 0.1298 0.1650 -0.0463 -0.0105 0.0292  178 PHE A O   
1427 C  CB  . PHE A 178 ? 0.2000 0.1235 0.1682 0.0156  -0.0165 0.0325  178 PHE A CB  
1428 C  CG  . PHE A 178 ? 0.1712 0.1306 0.1815 -0.0097 -0.0231 0.0424  178 PHE A CG  
1429 C  CD1 . PHE A 178 ? 0.2036 0.1045 0.2242 -0.0144 -0.0177 0.0325  178 PHE A CD1 
1430 C  CD2 . PHE A 178 ? 0.1416 0.1612 0.1720 -0.0080 0.0106  0.0486  178 PHE A CD2 
1431 C  CE1 . PHE A 178 ? 0.1880 0.1502 0.1964 -0.0046 -0.0019 0.0376  178 PHE A CE1 
1432 C  CE2 . PHE A 178 ? 0.1284 0.1594 0.1799 -0.0067 -0.0153 0.0436  178 PHE A CE2 
1433 C  CZ  . PHE A 178 ? 0.1533 0.1847 0.1831 -0.0239 -0.0171 0.0238  178 PHE A CZ  
1434 N  N   . ASP A 179 ? 0.1901 0.1659 0.1582 -0.0359 -0.0140 0.0519  179 ASP A N   
1435 C  CA  . ASP A 179 ? 0.1618 0.2098 0.1533 -0.0176 -0.0353 0.0308  179 ASP A CA  
1436 C  C   . ASP A 179 ? 0.1511 0.1346 0.1536 -0.0069 -0.0020 0.0247  179 ASP A C   
1437 O  O   . ASP A 179 ? 0.1747 0.1381 0.1988 -0.0164 -0.0018 0.0245  179 ASP A O   
1438 C  CB  . ASP A 179 ? 0.1456 0.2841 0.2106 0.0137  -0.0168 0.0766  179 ASP A CB  
1439 C  CG  . ASP A 179 ? 0.1738 0.2445 0.2703 0.0004  0.0063  0.0167  179 ASP A CG  
1440 O  OD1 . ASP A 179 ? 0.1777 0.1786 0.2368 0.0085  -0.0087 0.0487  179 ASP A OD1 
1441 O  OD2 . ASP A 179 ? 0.1845 0.5509 0.2519 -0.0469 -0.0118 -0.0321 179 ASP A OD2 
1442 N  N   . PRO A 180 ? 0.1608 0.1093 0.1557 -0.0057 -0.0116 0.0316  180 PRO A N   
1443 C  CA  . PRO A 180 ? 0.1574 0.1346 0.1407 -0.0221 -0.0170 0.0336  180 PRO A CA  
1444 C  C   . PRO A 180 ? 0.1306 0.1453 0.1698 -0.0189 -0.0069 0.0242  180 PRO A C   
1445 O  O   . PRO A 180 ? 0.1486 0.1483 0.1618 -0.0130 -0.0153 0.0244  180 PRO A O   
1446 C  CB  . PRO A 180 ? 0.1659 0.1371 0.2071 -0.0456 -0.0238 0.0466  180 PRO A CB  
1447 C  CG  . PRO A 180 ? 0.1823 0.1650 0.1621 -0.0023 -0.0097 0.0331  180 PRO A CG  
1448 C  CD  . PRO A 180 ? 0.1910 0.1128 0.1824 0.0000  -0.0232 0.0243  180 PRO A CD  
1449 N  N   . ARG A 181 ? 0.1183 0.1508 0.1585 -0.0173 -0.0009 0.0111  181 ARG A N   
1450 C  CA  . ARG A 181 ? 0.1149 0.1665 0.1941 -0.0184 0.0156  0.0181  181 ARG A CA  
1451 C  C   . ARG A 181 ? 0.1450 0.1626 0.1826 -0.0278 -0.0200 0.0292  181 ARG A C   
1452 O  O   . ARG A 181 ? 0.1373 0.1614 0.2253 -0.0207 -0.0026 0.0385  181 ARG A O   
1453 C  CB  . ARG A 181 ? 0.1400 0.1331 0.2341 -0.0036 0.0178  0.0380  181 ARG A CB  
1454 C  CG  . ARG A 181 ? 0.1988 0.1474 0.2365 0.0098  0.0234  0.0148  181 ARG A CG  
1455 C  CD  . ARG A 181 ? 0.1937 0.2093 0.2675 0.0210  0.0026  0.0607  181 ARG A CD  
1456 N  NE  . ARG A 181 ? 0.2477 0.1838 0.2817 0.0359  0.0130  0.0587  181 ARG A NE  
1457 C  CZ  . ARG A 181 ? 0.2377 0.1964 0.3389 0.0377  0.0303  0.0483  181 ARG A CZ  
1458 N  NH1 . ARG A 181 ? 0.1975 0.3325 0.4032 0.0549  0.0323  -0.0516 181 ARG A NH1 
1459 N  NH2 . ARG A 181 ? 0.2559 0.3029 0.3632 0.0475  -0.0183 0.0886  181 ARG A NH2 
1460 N  N   . GLY A 182 ? 0.1481 0.1403 0.2115 -0.0196 -0.0308 0.0079  182 GLY A N   
1461 C  CA  . GLY A 182 ? 0.1364 0.1375 0.2468 0.0009  -0.0521 -0.0126 182 GLY A CA  
1462 C  C   . GLY A 182 ? 0.1371 0.1490 0.2103 -0.0052 -0.0399 0.0100  182 GLY A C   
1463 O  O   . GLY A 182 ? 0.2013 0.1230 0.3008 -0.0010 -0.0527 -0.0088 182 GLY A O   
1464 N  N   . LEU A 183 ? 0.1303 0.1328 0.1884 -0.0091 -0.0378 0.0302  183 LEU A N   
1465 C  CA  . LEU A 183 ? 0.1313 0.1216 0.1896 -0.0060 -0.0364 0.0384  183 LEU A CA  
1466 C  C   . LEU A 183 ? 0.1424 0.1143 0.1856 -0.0209 -0.0201 0.0242  183 LEU A C   
1467 O  O   . LEU A 183 ? 0.1666 0.1443 0.1953 0.0264  -0.0099 0.0391  183 LEU A O   
1468 C  CB  . LEU A 183 ? 0.1418 0.1450 0.1927 -0.0048 -0.0126 0.0414  183 LEU A CB  
1469 C  CG  . LEU A 183 ? 0.1738 0.1623 0.1815 -0.0062 0.0137  0.0291  183 LEU A CG  
1470 C  CD1 . LEU A 183 ? 0.1420 0.2455 0.2452 -0.0037 0.0175  0.0773  183 LEU A CD1 
1471 C  CD2 . LEU A 183 ? 0.2414 0.1617 0.2558 0.0285  0.0203  -0.0137 183 LEU A CD2 
1472 N  N   . LEU A 184 ? 0.1404 0.1424 0.1715 -0.0071 0.0096  0.0227  184 LEU A N   
1473 C  CA  . LEU A 184 ? 0.1460 0.1357 0.1916 -0.0396 -0.0119 0.0541  184 LEU A CA  
1474 C  C   . LEU A 184 ? 0.1474 0.1770 0.2038 -0.0683 -0.0403 0.0749  184 LEU A C   
1475 O  O   . LEU A 184 ? 0.2238 0.2606 0.2683 -0.1220 -0.0999 0.1192  184 LEU A O   
1476 C  CB  . LEU A 184 ? 0.1371 0.1858 0.2189 -0.0089 0.0034  0.0631  184 LEU A CB  
1477 C  CG  . LEU A 184 ? 0.1356 0.1716 0.2432 -0.0034 0.0054  0.0370  184 LEU A CG  
1478 C  CD1 . LEU A 184 ? 0.2011 0.2187 0.2397 -0.0076 0.0516  -0.0092 184 LEU A CD1 
1479 C  CD2 . LEU A 184 ? 0.1629 0.2359 0.3072 -0.0070 -0.0469 0.0315  184 LEU A CD2 
1480 N  N   . PRO A 185 ? 0.1370 0.1461 0.1720 -0.0133 -0.0168 0.0451  185 PRO A N   
1481 C  CA  . PRO A 185 ? 0.1454 0.1643 0.1826 -0.0259 0.0103  0.0472  185 PRO A CA  
1482 C  C   . PRO A 185 ? 0.1324 0.1467 0.2203 -0.0096 -0.0006 0.0572  185 PRO A C   
1483 O  O   . PRO A 185 ? 0.1107 0.1407 0.3021 -0.0106 -0.0142 0.0668  185 PRO A O   
1484 C  CB  . PRO A 185 ? 0.1630 0.1680 0.1784 -0.0126 0.0136  0.0323  185 PRO A CB  
1485 C  CG  . PRO A 185 ? 0.1515 0.1346 0.1720 0.0209  -0.0055 0.0197  185 PRO A CG  
1486 C  CD  . PRO A 185 ? 0.1161 0.1353 0.1472 0.0085  -0.0122 0.0190  185 PRO A CD  
1487 N  N   A GLU A 186 ? 0.1446 0.1659 0.2267 -0.0358 -0.0042 0.0563  186 GLU A N   
1488 N  N   B GLU A 186 ? 0.1296 0.1737 0.2147 -0.0355 -0.0013 0.0502  186 GLU A N   
1489 C  CA  A GLU A 186 ? 0.1303 0.2111 0.2369 -0.0416 -0.0139 0.0274  186 GLU A CA  
1490 C  CA  B GLU A 186 ? 0.1201 0.1587 0.2232 -0.0385 -0.0109 0.0422  186 GLU A CA  
1491 C  C   A GLU A 186 ? 0.1172 0.1726 0.2383 -0.0158 -0.0237 0.0307  186 GLU A C   
1492 C  C   B GLU A 186 ? 0.1100 0.1550 0.2298 -0.0177 -0.0146 0.0287  186 GLU A C   
1493 O  O   A GLU A 186 ? 0.1052 0.2043 0.2932 0.0022  -0.0027 0.0319  186 GLU A O   
1494 O  O   B GLU A 186 ? 0.1226 0.2017 0.2459 0.0157  0.0024  0.0288  186 GLU A O   
1495 C  CB  A GLU A 186 ? 0.1788 0.2301 0.2859 -0.0660 0.0113  0.0120  186 GLU A CB  
1496 C  CB  B GLU A 186 ? 0.1150 0.1461 0.2243 -0.0198 0.0107  0.0392  186 GLU A CB  
1497 C  CG  A GLU A 186 ? 0.3247 0.2901 0.3474 -0.0461 -0.0634 -0.0201 186 GLU A CG  
1498 C  CG  B GLU A 186 ? 0.0924 0.2023 0.2533 -0.0066 0.0102  0.0768  186 GLU A CG  
1499 C  CD  A GLU A 186 ? 0.4014 0.3925 0.5018 -0.1193 0.0189  -0.0234 186 GLU A CD  
1500 C  CD  B GLU A 186 ? 0.1439 0.2433 0.2741 -0.0716 0.0158  0.0749  186 GLU A CD  
1501 O  OE1 A GLU A 186 ? 0.4264 0.2679 0.6488 0.0041  0.0089  -0.0789 186 GLU A OE1 
1502 O  OE1 B GLU A 186 ? 0.2060 0.2529 0.3600 -0.0664 0.0281  0.0522  186 GLU A OE1 
1503 O  OE2 A GLU A 186 ? 0.3076 0.3972 0.4382 0.0055  -0.0480 0.1172  186 GLU A OE2 
1504 O  OE2 B GLU A 186 ? 0.1812 0.3005 0.3358 -0.0497 0.0326  0.0747  186 GLU A OE2 
1505 N  N   . SER A 187 ? 0.1102 0.1644 0.1881 -0.0329 -0.0036 0.0318  187 SER A N   
1506 C  CA  . SER A 187 ? 0.1416 0.1528 0.1888 -0.0315 -0.0097 0.0239  187 SER A CA  
1507 C  C   . SER A 187 ? 0.0910 0.1705 0.1884 -0.0148 -0.0053 0.0210  187 SER A C   
1508 O  O   . SER A 187 ? 0.1151 0.1948 0.2498 -0.0261 0.0203  0.0233  187 SER A O   
1509 C  CB  . SER A 187 ? 0.1630 0.2336 0.1835 -0.0081 -0.0120 0.0570  187 SER A CB  
1510 O  OG  . SER A 187 ? 0.1653 0.2009 0.2068 -0.0380 0.0111  0.0403  187 SER A OG  
1511 N  N   . LEU A 188 ? 0.1255 0.1506 0.2217 -0.0220 -0.0040 0.0159  188 LEU A N   
1512 C  CA  . LEU A 188 ? 0.1449 0.1414 0.2477 -0.0315 -0.0326 0.0092  188 LEU A CA  
1513 C  C   . LEU A 188 ? 0.1028 0.1935 0.2014 -0.0159 0.0212  0.0034  188 LEU A C   
1514 O  O   . LEU A 188 ? 0.1612 0.2096 0.2211 -0.0402 -0.0184 -0.0021 188 LEU A O   
1515 C  CB  . LEU A 188 ? 0.1720 0.1533 0.3222 -0.0010 -0.0570 0.0369  188 LEU A CB  
1516 C  CG  . LEU A 188 ? 0.1988 0.2020 0.3310 -0.0192 -0.0339 0.1007  188 LEU A CG  
1517 C  CD1 . LEU A 188 ? 0.2332 0.2118 0.5028 0.0035  -0.0276 0.1544  188 LEU A CD1 
1518 C  CD2 . LEU A 188 ? 0.1795 0.4128 0.3132 -0.0619 -0.0342 0.1764  188 LEU A CD2 
1519 N  N   . ASP A 189 ? 0.1053 0.1928 0.1957 0.0049  0.0256  0.0089  189 ASP A N   
1520 C  CA  . ASP A 189 ? 0.1059 0.1982 0.1781 -0.0374 0.0243  0.0082  189 ASP A CA  
1521 C  C   . ASP A 189 ? 0.0982 0.1450 0.1793 0.0126  0.0148  -0.0036 189 ASP A C   
1522 O  O   . ASP A 189 ? 0.1174 0.1335 0.1811 0.0047  0.0249  0.0035  189 ASP A O   
1523 C  CB  . ASP A 189 ? 0.1698 0.2140 0.1784 -0.0478 0.0316  -0.0023 189 ASP A CB  
1524 C  CG  . ASP A 189 ? 0.2100 0.2655 0.2682 -0.0939 0.0547  0.0117  189 ASP A CG  
1525 O  OD1 . ASP A 189 ? 0.1424 0.4532 0.3120 -0.0116 0.0646  -0.0406 189 ASP A OD1 
1526 O  OD2 . ASP A 189 ? 0.2665 0.3292 0.3587 -0.1462 0.0541  0.0411  189 ASP A OD2 
1527 N  N   . TYR A 190 ? 0.1037 0.1375 0.1586 -0.0041 0.0262  0.0164  190 TYR A N   
1528 C  CA  . TYR A 190 ? 0.1058 0.1156 0.1514 -0.0134 0.0145  0.0277  190 TYR A CA  
1529 C  C   . TYR A 190 ? 0.1192 0.0966 0.1375 0.0008  0.0260  -0.0044 190 TYR A C   
1530 O  O   . TYR A 190 ? 0.1289 0.1454 0.1443 0.0079  0.0275  0.0003  190 TYR A O   
1531 C  CB  . TYR A 190 ? 0.1439 0.0976 0.1464 -0.0190 0.0091  0.0167  190 TYR A CB  
1532 C  CG  . TYR A 190 ? 0.1263 0.1234 0.1560 -0.0193 0.0216  0.0258  190 TYR A CG  
1533 C  CD1 . TYR A 190 ? 0.1535 0.1280 0.1468 -0.0228 0.0227  -0.0035 190 TYR A CD1 
1534 C  CD2 . TYR A 190 ? 0.1472 0.1497 0.1733 0.0188  0.0489  0.0223  190 TYR A CD2 
1535 C  CE1 . TYR A 190 ? 0.1492 0.1122 0.2043 -0.0030 0.0198  0.0029  190 TYR A CE1 
1536 C  CE2 . TYR A 190 ? 0.1317 0.1493 0.1811 0.0128  0.0207  0.0001  190 TYR A CE2 
1537 C  CZ  . TYR A 190 ? 0.1630 0.1147 0.1953 -0.0005 0.0164  -0.0010 190 TYR A CZ  
1538 O  OH  . TYR A 190 ? 0.1848 0.1252 0.2117 0.0060  0.0062  -0.0160 190 TYR A OH  
1539 N  N   . TRP A 191 ? 0.1025 0.1330 0.1392 -0.0096 0.0175  0.0094  191 TRP A N   
1540 C  CA  . TRP A 191 ? 0.1084 0.1194 0.1402 -0.0092 0.0100  0.0146  191 TRP A CA  
1541 C  C   . TRP A 191 ? 0.1171 0.1177 0.1186 -0.0092 0.0135  0.0030  191 TRP A C   
1542 O  O   . TRP A 191 ? 0.1544 0.1485 0.1092 -0.0266 0.0153  -0.0053 191 TRP A O   
1543 C  CB  . TRP A 191 ? 0.1531 0.1004 0.1542 0.0158  0.0138  0.0049  191 TRP A CB  
1544 C  CG  . TRP A 191 ? 0.1335 0.1086 0.1585 0.0204  0.0084  0.0072  191 TRP A CG  
1545 C  CD1 . TRP A 191 ? 0.1467 0.1353 0.1729 0.0027  0.0216  0.0173  191 TRP A CD1 
1546 C  CD2 . TRP A 191 ? 0.1314 0.1111 0.1585 0.0064  0.0173  0.0184  191 TRP A CD2 
1547 N  NE1 . TRP A 191 ? 0.1618 0.1328 0.1770 -0.0038 0.0236  0.0295  191 TRP A NE1 
1548 C  CE2 . TRP A 191 ? 0.1456 0.1235 0.1747 0.0105  0.0116  0.0388  191 TRP A CE2 
1549 C  CE3 . TRP A 191 ? 0.1030 0.1590 0.1770 0.0103  -0.0055 -0.0062 191 TRP A CE3 
1550 C  CZ2 . TRP A 191 ? 0.1657 0.1177 0.2170 0.0105  -0.0068 0.0457  191 TRP A CZ2 
1551 C  CZ3 . TRP A 191 ? 0.1210 0.1453 0.1894 -0.0032 0.0135  -0.0013 191 TRP A CZ3 
1552 C  CH2 . TRP A 191 ? 0.1486 0.1532 0.2129 -0.0006 -0.0183 0.0127  191 TRP A CH2 
1553 N  N   . THR A 192 ? 0.1072 0.1221 0.1226 -0.0088 0.0091  -0.0017 192 THR A N   
1554 C  CA  . THR A 192 ? 0.1099 0.1083 0.1206 -0.0008 -0.0039 -0.0012 192 THR A CA  
1555 C  C   . THR A 192 ? 0.0985 0.1221 0.1332 0.0032  0.0051  -0.0064 192 THR A C   
1556 O  O   . THR A 192 ? 0.1204 0.1441 0.1217 0.0005  -0.0018 0.0006  192 THR A O   
1557 C  CB  . THR A 192 ? 0.1294 0.1127 0.1263 0.0248  0.0266  0.0023  192 THR A CB  
1558 O  OG1 . THR A 192 ? 0.1215 0.1287 0.1632 0.0085  0.0158  -0.0044 192 THR A OG1 
1559 C  CG2 . THR A 192 ? 0.1571 0.1734 0.1262 0.0369  0.0240  -0.0024 192 THR A CG2 
1560 N  N   . TYR A 193 ? 0.1005 0.1201 0.1417 -0.0023 0.0113  -0.0125 193 TYR A N   
1561 C  CA  . TYR A 193 ? 0.1142 0.0967 0.1298 0.0110  0.0006  -0.0010 193 TYR A CA  
1562 C  C   . TYR A 193 ? 0.1271 0.1056 0.1095 0.0196  0.0156  -0.0214 193 TYR A C   
1563 O  O   . TYR A 193 ? 0.1303 0.1066 0.1145 0.0027  0.0054  -0.0058 193 TYR A O   
1564 C  CB  . TYR A 193 ? 0.1321 0.1003 0.1454 0.0326  0.0023  -0.0285 193 TYR A CB  
1565 C  CG  . TYR A 193 ? 0.1186 0.0531 0.1540 0.0126  0.0012  -0.0102 193 TYR A CG  
1566 C  CD1 . TYR A 193 ? 0.1292 0.0903 0.1270 0.0153  -0.0044 -0.0193 193 TYR A CD1 
1567 C  CD2 . TYR A 193 ? 0.1158 0.0930 0.1518 0.0149  0.0159  0.0027  193 TYR A CD2 
1568 C  CE1 . TYR A 193 ? 0.1143 0.0782 0.1399 0.0133  0.0179  -0.0015 193 TYR A CE1 
1569 C  CE2 . TYR A 193 ? 0.1292 0.0910 0.1324 0.0104  0.0020  -0.0116 193 TYR A CE2 
1570 C  CZ  . TYR A 193 ? 0.1023 0.0749 0.1241 0.0252  0.0120  -0.0140 193 TYR A CZ  
1571 O  OH  . TYR A 193 ? 0.1098 0.0818 0.1468 -0.0075 0.0161  -0.0015 193 TYR A OH  
1572 N  N   . PRO A 194 ? 0.1288 0.1195 0.1120 0.0013  0.0079  -0.0201 194 PRO A N   
1573 C  CA  . PRO A 194 ? 0.1235 0.0926 0.1453 0.0059  0.0268  -0.0386 194 PRO A CA  
1574 C  C   . PRO A 194 ? 0.1090 0.1022 0.1298 0.0187  0.0034  -0.0298 194 PRO A C   
1575 O  O   . PRO A 194 ? 0.1180 0.1194 0.1411 0.0241  0.0015  -0.0173 194 PRO A O   
1576 C  CB  . PRO A 194 ? 0.1632 0.1468 0.1535 0.0173  -0.0072 -0.0486 194 PRO A CB  
1577 C  CG  . PRO A 194 ? 0.1608 0.1439 0.1565 -0.0160 -0.0197 -0.0452 194 PRO A CG  
1578 C  CD  . PRO A 194 ? 0.1714 0.1914 0.1158 -0.0416 -0.0194 -0.0306 194 PRO A CD  
1579 N  N   . GLY A 195 ? 0.1040 0.0961 0.1345 -0.0068 0.0163  -0.0309 195 GLY A N   
1580 C  CA  . GLY A 195 ? 0.1119 0.1023 0.1381 0.0109  0.0383  0.0052  195 GLY A CA  
1581 C  C   . GLY A 195 ? 0.0957 0.0740 0.1546 -0.0216 0.0167  -0.0038 195 GLY A C   
1582 O  O   . GLY A 195 ? 0.1124 0.0675 0.1777 -0.0127 0.0022  0.0008  195 GLY A O   
1583 N  N   . SER A 196 ? 0.1086 0.0853 0.1292 -0.0004 0.0111  0.0052  196 SER A N   
1584 C  CA  . SER A 196 ? 0.0982 0.1028 0.1278 0.0100  0.0187  -0.0060 196 SER A CA  
1585 C  C   . SER A 196 ? 0.0924 0.0718 0.1395 -0.0071 -0.0037 -0.0075 196 SER A C   
1586 O  O   . SER A 196 ? 0.0994 0.0686 0.1510 -0.0168 0.0033  -0.0011 196 SER A O   
1587 C  CB  . SER A 196 ? 0.1016 0.0797 0.1646 0.0046  -0.0013 -0.0261 196 SER A CB  
1588 O  OG  . SER A 196 ? 0.0988 0.0811 0.1586 0.0003  0.0166  -0.0016 196 SER A OG  
1589 N  N   . LEU A 197 ? 0.1007 0.0847 0.1324 -0.0006 0.0141  -0.0057 197 LEU A N   
1590 C  CA  . LEU A 197 ? 0.0949 0.0883 0.1395 -0.0058 0.0085  0.0037  197 LEU A CA  
1591 C  C   . LEU A 197 ? 0.1007 0.0818 0.1553 -0.0074 -0.0079 0.0048  197 LEU A C   
1592 O  O   . LEU A 197 ? 0.1142 0.0935 0.1403 0.0048  -0.0018 -0.0164 197 LEU A O   
1593 C  CB  . LEU A 197 ? 0.1219 0.0757 0.1682 -0.0052 0.0336  0.0102  197 LEU A CB  
1594 C  CG  . LEU A 197 ? 0.1587 0.0739 0.1775 0.0033  0.0167  0.0271  197 LEU A CG  
1595 C  CD1 . LEU A 197 ? 0.2193 0.0952 0.2122 -0.0403 0.0249  0.0225  197 LEU A CD1 
1596 C  CD2 . LEU A 197 ? 0.1360 0.1238 0.2372 0.0345  0.0477  0.0544  197 LEU A CD2 
1597 N  N   . THR A 198 ? 0.1092 0.0743 0.1503 -0.0072 -0.0020 0.0032  198 THR A N   
1598 C  CA  . THR A 198 ? 0.1083 0.0748 0.1550 0.0030  0.0104  0.0066  198 THR A CA  
1599 C  C   . THR A 198 ? 0.1208 0.1190 0.1423 -0.0179 0.0043  -0.0199 198 THR A C   
1600 O  O   . THR A 198 ? 0.1055 0.1459 0.2150 -0.0223 0.0272  -0.0776 198 THR A O   
1601 C  CB  . THR A 198 ? 0.1180 0.0917 0.1319 -0.0074 0.0025  -0.0099 198 THR A CB  
1602 O  OG1 . THR A 198 ? 0.1034 0.0879 0.1382 -0.0062 0.0016  0.0050  198 THR A OG1 
1603 C  CG2 . THR A 198 ? 0.1353 0.1197 0.1515 -0.0061 0.0325  -0.0072 198 THR A CG2 
1604 N  N   A THR A 199 ? 0.1449 0.1518 0.1500 -0.0456 0.0190  0.0061  199 THR A N   
1605 N  N   B THR A 199 ? 0.1151 0.1630 0.1719 -0.0418 0.0344  0.0201  199 THR A N   
1606 C  CA  A THR A 199 ? 0.1539 0.2391 0.1780 -0.0800 0.0232  -0.0335 199 THR A CA  
1607 C  CA  B THR A 199 ? 0.1553 0.2240 0.1482 -0.0571 0.0351  -0.0106 199 THR A CA  
1608 C  C   A THR A 199 ? 0.1428 0.2127 0.1989 -0.0604 0.0189  -0.0111 199 THR A C   
1609 C  C   B THR A 199 ? 0.1374 0.2321 0.1569 -0.0450 0.0017  -0.0011 199 THR A C   
1610 O  O   A THR A 199 ? 0.1377 0.1560 0.1885 -0.0489 0.0030  0.0232  199 THR A O   
1611 O  O   B THR A 199 ? 0.1326 0.1596 0.1888 -0.0383 0.0038  0.0283  199 THR A O   
1612 C  CB  A THR A 199 ? 0.2129 0.2936 0.2233 -0.1724 -0.0762 -0.0447 199 THR A CB  
1613 C  CB  B THR A 199 ? 0.2154 0.3064 0.1269 -0.0622 0.0384  -0.0182 199 THR A CB  
1614 O  OG1 A THR A 199 ? 0.2222 0.2269 0.2114 -0.1773 -0.0558 0.0851  199 THR A OG1 
1615 O  OG1 B THR A 199 ? 0.4485 0.2944 0.3728 -0.1477 -0.0879 0.0701  199 THR A OG1 
1616 C  CG2 A THR A 199 ? 0.2298 0.1960 0.2451 -0.0751 -0.0106 -0.0305 199 THR A CG2 
1617 C  CG2 B THR A 199 ? 0.1377 0.1500 0.1661 -0.0575 -0.0432 0.0544  199 THR A CG2 
1618 N  N   . PRO A 200 ? 0.1395 0.2649 0.1747 -0.0847 0.0208  -0.0148 200 PRO A N   
1619 C  CA  . PRO A 200 ? 0.1414 0.2507 0.2020 -0.1038 0.0203  0.0170  200 PRO A CA  
1620 C  C   . PRO A 200 ? 0.1553 0.2551 0.2068 -0.1131 -0.0084 0.0087  200 PRO A C   
1621 O  O   . PRO A 200 ? 0.1860 0.3633 0.2108 -0.1120 -0.0215 0.0522  200 PRO A O   
1622 C  CB  . PRO A 200 ? 0.1222 0.3327 0.2189 -0.0702 0.0192  0.0133  200 PRO A CB  
1623 C  CG  . PRO A 200 ? 0.1549 0.3374 0.2359 -0.0660 0.0339  -0.0125 200 PRO A CG  
1624 C  CD  . PRO A 200 ? 0.1558 0.3013 0.2127 -0.0565 0.0301  -0.0421 200 PRO A CD  
1625 N  N   . PRO A 201 ? 0.1628 0.2426 0.2074 -0.0795 -0.0044 0.0507  201 PRO A N   
1626 C  CA  . PRO A 201 ? 0.2116 0.2125 0.2104 -0.1291 -0.0097 0.0359  201 PRO A CA  
1627 C  C   . PRO A 201 ? 0.1385 0.1659 0.1992 -0.0353 0.0067  0.0258  201 PRO A C   
1628 O  O   . PRO A 201 ? 0.1324 0.1780 0.2296 -0.0436 -0.0001 0.0234  201 PRO A O   
1629 C  CB  . PRO A 201 ? 0.2531 0.2309 0.2543 -0.1103 0.0083  0.0388  201 PRO A CB  
1630 C  CG  . PRO A 201 ? 0.3097 0.2291 0.3756 -0.1045 -0.0550 0.1037  201 PRO A CG  
1631 C  CD  . PRO A 201 ? 0.2568 0.2316 0.2718 -0.0540 -0.0430 0.1220  201 PRO A CD  
1632 N  N   . LEU A 202 ? 0.1208 0.1278 0.1766 -0.0212 0.0117  0.0177  202 LEU A N   
1633 C  CA  . LEU A 202 ? 0.1381 0.0901 0.1849 -0.0030 0.0092  0.0258  202 LEU A CA  
1634 C  C   . LEU A 202 ? 0.0856 0.0709 0.2082 -0.0171 -0.0161 -0.0001 202 LEU A C   
1635 O  O   . LEU A 202 ? 0.1097 0.1034 0.1982 -0.0011 0.0008  -0.0025 202 LEU A O   
1636 C  CB  . LEU A 202 ? 0.1109 0.1244 0.1687 0.0059  0.0019  -0.0022 202 LEU A CB  
1637 C  CG  . LEU A 202 ? 0.1044 0.1499 0.1927 -0.0116 0.0173  -0.0284 202 LEU A CG  
1638 C  CD1 . LEU A 202 ? 0.1038 0.1852 0.2481 -0.0134 0.0008  -0.0153 202 LEU A CD1 
1639 C  CD2 . LEU A 202 ? 0.1074 0.1578 0.1842 -0.0158 -0.0020 -0.0234 202 LEU A CD2 
1640 N  N   A THR A 203 ? 0.1118 0.0894 0.2689 -0.0053 0.0095  0.0348  203 THR A N   
1641 N  N   B THR A 203 ? 0.1181 0.0678 0.2684 -0.0100 0.0162  0.0141  203 THR A N   
1642 C  CA  A THR A 203 ? 0.0946 0.1208 0.2996 0.0203  0.0223  0.0127  203 THR A CA  
1643 C  CA  B THR A 203 ? 0.1337 0.0788 0.2972 0.0154  0.0467  0.0098  203 THR A CA  
1644 C  C   A THR A 203 ? 0.1067 0.0775 0.2543 -0.0043 -0.0073 0.0188  203 THR A C   
1645 C  C   B THR A 203 ? 0.1153 0.0589 0.2577 -0.0047 0.0010  0.0147  203 THR A C   
1646 O  O   A THR A 203 ? 0.1233 0.0772 0.2110 -0.0067 -0.0012 -0.0004 203 THR A O   
1647 O  O   B THR A 203 ? 0.1224 0.0750 0.2134 -0.0037 -0.0006 -0.0023 203 THR A O   
1648 C  CB  A THR A 203 ? 0.2702 0.1845 0.4259 0.0283  -0.0668 0.0743  203 THR A CB  
1649 C  CB  B THR A 203 ? 0.1492 0.0892 0.2865 -0.0199 0.0695  0.0242  203 THR A CB  
1650 O  OG1 A THR A 203 ? 0.5104 0.2386 0.5030 0.0632  -0.1815 0.0085  203 THR A OG1 
1651 O  OG1 B THR A 203 ? 0.2060 0.0768 0.2908 -0.0033 0.1176  0.0598  203 THR A OG1 
1652 C  CG2 A THR A 203 ? 0.1622 0.2038 0.2742 0.0093  0.0391  0.1134  203 THR A CG2 
1653 C  CG2 B THR A 203 ? 0.1301 0.1872 0.2557 -0.0038 0.0391  -0.0570 203 THR A CG2 
1654 N  N   . GLU A 204 ? 0.1447 0.0867 0.2554 -0.0172 -0.0179 -0.0132 204 GLU A N   
1655 C  CA  . GLU A 204 ? 0.1072 0.1393 0.2264 0.0038  -0.0322 -0.0237 204 GLU A CA  
1656 C  C   . GLU A 204 ? 0.1324 0.1177 0.2221 0.0019  -0.0230 -0.0430 204 GLU A C   
1657 O  O   . GLU A 204 ? 0.2050 0.1576 0.2398 0.0606  -0.0801 -0.0864 204 GLU A O   
1658 C  CB  . GLU A 204 ? 0.1319 0.1317 0.2194 0.0209  -0.0373 -0.0348 204 GLU A CB  
1659 C  CG  . GLU A 204 ? 0.1178 0.1565 0.2427 0.0331  -0.0147 -0.0100 204 GLU A CG  
1660 C  CD  . GLU A 204 ? 0.1362 0.1637 0.2373 0.0148  -0.0215 -0.0238 204 GLU A CD  
1661 O  OE1 . GLU A 204 ? 0.1646 0.1770 0.3290 0.0021  -0.0798 -0.0605 204 GLU A OE1 
1662 O  OE2 . GLU A 204 ? 0.1418 0.1450 0.2032 0.0011  -0.0276 -0.0035 204 GLU A OE2 
1663 N  N   . CYS A 205 ? 0.1210 0.0617 0.2115 -0.0080 -0.0262 -0.0075 205 CYS A N   
1664 C  CA  . CYS A 205 ? 0.1179 0.0736 0.1722 0.0023  -0.0107 0.0121  205 CYS A CA  
1665 C  C   . CYS A 205 ? 0.1215 0.0811 0.1579 0.0048  -0.0139 -0.0027 205 CYS A C   
1666 O  O   . CYS A 205 ? 0.1335 0.0698 0.1960 0.0065  -0.0324 -0.0012 205 CYS A O   
1667 C  CB  . CYS A 205 ? 0.1539 0.0820 0.1567 0.0018  0.0173  -0.0135 205 CYS A CB  
1668 S  SG  . CYS A 205 ? 0.1788 0.1113 0.1787 0.0113  0.0027  -0.0189 205 CYS A SG  
1669 N  N   . VAL A 206 ? 0.1039 0.0774 0.1672 -0.0038 0.0052  -0.0078 206 VAL A N   
1670 C  CA  . VAL A 206 ? 0.1128 0.0740 0.1434 -0.0064 -0.0036 -0.0082 206 VAL A CA  
1671 C  C   . VAL A 206 ? 0.1158 0.0738 0.1518 -0.0110 -0.0057 -0.0034 206 VAL A C   
1672 O  O   . VAL A 206 ? 0.1276 0.1055 0.1720 0.0120  0.0042  0.0113  206 VAL A O   
1673 C  CB  . VAL A 206 ? 0.1134 0.0698 0.1558 -0.0050 -0.0006 -0.0064 206 VAL A CB  
1674 C  CG1 . VAL A 206 ? 0.1058 0.0894 0.1612 -0.0021 -0.0257 -0.0185 206 VAL A CG1 
1675 C  CG2 . VAL A 206 ? 0.1540 0.0838 0.1716 0.0148  0.0242  0.0038  206 VAL A CG2 
1676 N  N   . THR A 207 ? 0.1062 0.0727 0.1391 -0.0071 0.0015  -0.0105 207 THR A N   
1677 C  CA  . THR A 207 ? 0.1058 0.0863 0.1607 -0.0200 0.0131  -0.0175 207 THR A CA  
1678 C  C   . THR A 207 ? 0.1030 0.0824 0.1319 -0.0128 0.0012  0.0013  207 THR A C   
1679 O  O   . THR A 207 ? 0.1208 0.0754 0.1428 0.0001  -0.0011 -0.0023 207 THR A O   
1680 C  CB  . THR A 207 ? 0.0948 0.1098 0.1682 -0.0077 0.0050  -0.0284 207 THR A CB  
1681 O  OG1 . THR A 207 ? 0.1424 0.1134 0.1826 -0.0081 -0.0013 -0.0401 207 THR A OG1 
1682 C  CG2 . THR A 207 ? 0.1486 0.1493 0.1666 -0.0108 0.0341  -0.0163 207 THR A CG2 
1683 N  N   . TRP A 208 ? 0.1158 0.0715 0.1439 0.0068  0.0082  -0.0100 208 TRP A N   
1684 C  CA  . TRP A 208 ? 0.0973 0.0657 0.1344 0.0061  0.0083  -0.0073 208 TRP A CA  
1685 C  C   . TRP A 208 ? 0.1065 0.0767 0.1181 0.0157  0.0054  0.0087  208 TRP A C   
1686 O  O   . TRP A 208 ? 0.1244 0.0908 0.1221 0.0031  0.0043  0.0070  208 TRP A O   
1687 C  CB  . TRP A 208 ? 0.1050 0.0819 0.1357 0.0214  0.0175  0.0011  208 TRP A CB  
1688 C  CG  . TRP A 208 ? 0.0955 0.0750 0.1301 0.0065  -0.0015 0.0001  208 TRP A CG  
1689 C  CD1 . TRP A 208 ? 0.1080 0.0853 0.1549 -0.0100 0.0115  -0.0108 208 TRP A CD1 
1690 C  CD2 . TRP A 208 ? 0.1110 0.0646 0.1434 0.0024  0.0006  -0.0164 208 TRP A CD2 
1691 N  NE1 . TRP A 208 ? 0.0953 0.0840 0.1686 0.0055  0.0116  -0.0138 208 TRP A NE1 
1692 C  CE2 . TRP A 208 ? 0.1037 0.0705 0.1556 0.0035  0.0099  -0.0059 208 TRP A CE2 
1693 C  CE3 . TRP A 208 ? 0.1260 0.0551 0.1317 0.0176  -0.0173 -0.0136 208 TRP A CE3 
1694 C  CZ2 . TRP A 208 ? 0.1375 0.0627 0.1687 0.0324  0.0218  0.0037  208 TRP A CZ2 
1695 C  CZ3 . TRP A 208 ? 0.1395 0.0697 0.1395 0.0212  0.0046  -0.0189 208 TRP A CZ3 
1696 C  CH2 . TRP A 208 ? 0.1607 0.0788 0.1650 0.0314  0.0162  0.0052  208 TRP A CH2 
1697 N  N   . ILE A 209 ? 0.1014 0.0813 0.1328 -0.0005 0.0058  -0.0023 209 ILE A N   
1698 C  CA  . ILE A 209 ? 0.0937 0.0743 0.1339 0.0016  0.0069  -0.0011 209 ILE A CA  
1699 C  C   . ILE A 209 ? 0.1151 0.0880 0.1217 -0.0129 0.0012  0.0039  209 ILE A C   
1700 O  O   . ILE A 209 ? 0.1375 0.0948 0.1190 -0.0016 0.0025  0.0035  209 ILE A O   
1701 C  CB  . ILE A 209 ? 0.1052 0.0806 0.1683 0.0130  -0.0024 -0.0100 209 ILE A CB  
1702 C  CG1 . ILE A 209 ? 0.1350 0.0779 0.2106 0.0160  0.0033  -0.0273 209 ILE A CG1 
1703 C  CG2 . ILE A 209 ? 0.1023 0.1342 0.2104 0.0023  0.0260  0.0129  209 ILE A CG2 
1704 C  CD1 . ILE A 209 ? 0.1507 0.0959 0.2602 0.0358  -0.0039 -0.0166 209 ILE A CD1 
1705 N  N   . VAL A 210 ? 0.1007 0.0734 0.1463 0.0088  0.0125  -0.0027 210 VAL A N   
1706 C  CA  . VAL A 210 ? 0.0926 0.0747 0.1477 -0.0044 0.0064  -0.0125 210 VAL A CA  
1707 C  C   . VAL A 210 ? 0.1129 0.0662 0.1221 -0.0089 0.0150  0.0070  210 VAL A C   
1708 O  O   . VAL A 210 ? 0.1438 0.1016 0.1170 -0.0099 0.0190  0.0084  210 VAL A O   
1709 C  CB  . VAL A 210 ? 0.0943 0.0777 0.1398 -0.0060 0.0039  -0.0042 210 VAL A CB  
1710 C  CG1 . VAL A 210 ? 0.1303 0.0763 0.1899 0.0183  0.0099  -0.0281 210 VAL A CG1 
1711 C  CG2 . VAL A 210 ? 0.0937 0.1189 0.1675 -0.0080 0.0162  0.0044  210 VAL A CG2 
1712 N  N   . LEU A 211 ? 0.1073 0.0856 0.1589 -0.0218 0.0040  0.0114  211 LEU A N   
1713 C  CA  . LEU A 211 ? 0.0971 0.1107 0.1637 -0.0215 0.0027  0.0218  211 LEU A CA  
1714 C  C   . LEU A 211 ? 0.1116 0.1045 0.1490 -0.0194 0.0121  0.0156  211 LEU A C   
1715 O  O   . LEU A 211 ? 0.1194 0.1233 0.1447 -0.0152 0.0132  -0.0100 211 LEU A O   
1716 C  CB  . LEU A 211 ? 0.1249 0.1127 0.1504 -0.0181 0.0131  0.0143  211 LEU A CB  
1717 C  CG  . LEU A 211 ? 0.1328 0.1368 0.1463 -0.0114 -0.0004 0.0325  211 LEU A CG  
1718 C  CD1 . LEU A 211 ? 0.1615 0.2154 0.1678 -0.0118 -0.0210 0.0263  211 LEU A CD1 
1719 C  CD2 . LEU A 211 ? 0.1453 0.1632 0.1564 0.0053  0.0260  0.0271  211 LEU A CD2 
1720 N  N   . LYS A 212 ? 0.1224 0.1129 0.1623 -0.0203 0.0129  0.0281  212 LYS A N   
1721 C  CA  . LYS A 212 ? 0.1991 0.1039 0.1630 -0.0022 -0.0083 0.0199  212 LYS A CA  
1722 C  C   . LYS A 212 ? 0.1374 0.1220 0.1798 -0.0128 0.0082  0.0287  212 LYS A C   
1723 O  O   . LYS A 212 ? 0.1468 0.1228 0.2441 -0.0128 -0.0141 0.0212  212 LYS A O   
1724 C  CB  . LYS A 212 ? 0.2436 0.1449 0.1648 -0.0561 0.0067  0.0140  212 LYS A CB  
1725 C  CG  . LYS A 212 ? 0.2936 0.1714 0.2393 -0.0636 -0.0339 0.0517  212 LYS A CG  
1726 C  CD  . LYS A 212 ? 0.4933 0.3466 0.2784 -0.1337 0.0293  0.0567  212 LYS A CD  
1727 N  N   . GLU A 213 ? 0.1115 0.1214 0.1467 -0.0228 0.0059  0.0223  213 GLU A N   
1728 C  CA  . GLU A 213 ? 0.1149 0.1231 0.1617 -0.0250 0.0001  0.0322  213 GLU A CA  
1729 C  C   . GLU A 213 ? 0.1429 0.1034 0.1650 -0.0233 0.0104  0.0254  213 GLU A C   
1730 O  O   . GLU A 213 ? 0.1317 0.1054 0.1630 -0.0164 0.0146  0.0296  213 GLU A O   
1731 C  CB  . GLU A 213 ? 0.1156 0.1271 0.1957 -0.0283 0.0027  0.0097  213 GLU A CB  
1732 C  CG  . GLU A 213 ? 0.1429 0.1314 0.2667 -0.0359 -0.0223 -0.0198 213 GLU A CG  
1733 C  CD  . GLU A 213 ? 0.1377 0.1993 0.4075 -0.0284 0.0259  -0.0376 213 GLU A CD  
1734 O  OE1 . GLU A 213 ? 0.1497 0.1569 0.2924 -0.0285 -0.0190 0.0168  213 GLU A OE1 
1735 O  OE2 . GLU A 213 ? 0.1870 0.3356 0.4957 -0.0583 -0.0195 -0.1284 213 GLU A OE2 
1736 N  N   A PRO A 214 ? 0.1328 0.1028 0.1407 -0.0145 -0.0067 0.0262  214 PRO A N   
1737 N  N   B PRO A 214 ? 0.1371 0.0934 0.1623 -0.0230 -0.0042 0.0259  214 PRO A N   
1738 C  CA  A PRO A 214 ? 0.1321 0.0987 0.1522 -0.0057 0.0165  0.0002  214 PRO A CA  
1739 C  CA  B PRO A 214 ? 0.1380 0.1009 0.1635 0.0032  0.0099  -0.0062 214 PRO A CA  
1740 C  C   A PRO A 214 ? 0.1435 0.1210 0.1497 -0.0171 0.0129  -0.0064 214 PRO A C   
1741 C  C   B PRO A 214 ? 0.1450 0.1210 0.1508 -0.0184 0.0129  -0.0051 214 PRO A C   
1742 O  O   A PRO A 214 ? 0.1454 0.1597 0.1914 -0.0343 0.0044  0.0133  214 PRO A O   
1743 O  O   B PRO A 214 ? 0.1515 0.1594 0.1934 -0.0434 -0.0025 0.0210  214 PRO A O   
1744 C  CB  A PRO A 214 ? 0.1549 0.0946 0.1804 -0.0003 0.0240  0.0132  214 PRO A CB  
1745 C  CB  B PRO A 214 ? 0.1479 0.0630 0.2240 -0.0232 0.0058  -0.0050 214 PRO A CB  
1746 C  CG  A PRO A 214 ? 0.1441 0.1082 0.2086 -0.0179 0.0392  -0.0015 214 PRO A CG  
1747 C  CG  B PRO A 214 ? 0.1450 0.1108 0.2294 -0.0207 0.0171  0.0089  214 PRO A CG  
1748 C  CD  A PRO A 214 ? 0.1472 0.0851 0.1848 -0.0130 0.0340  0.0155  214 PRO A CD  
1749 C  CD  B PRO A 214 ? 0.1005 0.0775 0.2604 -0.0058 -0.0161 0.0315  214 PRO A CD  
1750 N  N   . ILE A 215 ? 0.1518 0.1007 0.1427 0.0002  0.0010  -0.0033 215 ILE A N   
1751 C  CA  . ILE A 215 ? 0.1407 0.1127 0.1510 0.0052  -0.0119 -0.0043 215 ILE A CA  
1752 C  C   . ILE A 215 ? 0.1434 0.0932 0.1508 -0.0211 0.0033  0.0115  215 ILE A C   
1753 O  O   . ILE A 215 ? 0.1421 0.1076 0.2043 -0.0107 -0.0002 -0.0199 215 ILE A O   
1754 C  CB  . ILE A 215 ? 0.1335 0.1032 0.1817 0.0066  -0.0132 -0.0047 215 ILE A CB  
1755 C  CG1 . ILE A 215 ? 0.1435 0.0980 0.1784 -0.0063 0.0095  0.0194  215 ILE A CG1 
1756 C  CG2 . ILE A 215 ? 0.1676 0.1172 0.2082 0.0142  0.0020  -0.0378 215 ILE A CG2 
1757 C  CD1 . ILE A 215 ? 0.1881 0.1398 0.1611 -0.0073 0.0034  0.0252  215 ILE A CD1 
1758 N  N   A SER A 216 ? 0.1535 0.0885 0.2020 -0.0061 -0.0146 -0.0266 216 SER A N   
1759 N  N   B SER A 216 ? 0.1410 0.1335 0.1715 -0.0300 -0.0075 0.0027  216 SER A N   
1760 C  CA  A SER A 216 ? 0.1837 0.1038 0.1704 -0.0245 -0.0220 -0.0323 216 SER A CA  
1761 C  CA  B SER A 216 ? 0.1874 0.1474 0.1722 -0.0451 0.0256  -0.0008 216 SER A CA  
1762 C  C   A SER A 216 ? 0.1851 0.0980 0.2000 -0.0143 0.0010  -0.0086 216 SER A C   
1763 C  C   B SER A 216 ? 0.1608 0.0463 0.1795 -0.0357 -0.0100 0.0050  216 SER A C   
1764 O  O   A SER A 216 ? 0.1896 0.1247 0.2488 -0.0445 -0.0378 0.0079  216 SER A O   
1765 O  O   B SER A 216 ? 0.1901 0.1055 0.1680 -0.0068 -0.0113 0.0138  216 SER A O   
1766 C  CB  A SER A 216 ? 0.2041 0.1154 0.2226 -0.0400 -0.0266 -0.0236 216 SER A CB  
1767 C  CB  B SER A 216 ? 0.1676 0.1439 0.2485 -0.0228 0.0205  0.0521  216 SER A CB  
1768 O  OG  A SER A 216 ? 0.3016 0.1987 0.2578 -0.0856 -0.0226 0.0054  216 SER A OG  
1769 O  OG  B SER A 216 ? 0.1564 0.1600 0.2402 -0.0522 -0.0075 -0.0040 216 SER A OG  
1770 N  N   . VAL A 217 ? 0.1600 0.0958 0.1777 -0.0265 -0.0120 -0.0083 217 VAL A N   
1771 C  CA  . VAL A 217 ? 0.1831 0.0820 0.1714 -0.0442 -0.0199 -0.0013 217 VAL A CA  
1772 C  C   . VAL A 217 ? 0.1658 0.0809 0.1913 -0.0219 -0.0441 -0.0048 217 VAL A C   
1773 O  O   . VAL A 217 ? 0.1942 0.0961 0.1885 -0.0227 -0.0447 0.0100  217 VAL A O   
1774 C  CB  . VAL A 217 ? 0.1669 0.0588 0.2334 -0.0304 -0.0030 -0.0046 217 VAL A CB  
1775 C  CG1 . VAL A 217 ? 0.2036 0.0518 0.2563 -0.0461 -0.0273 -0.0166 217 VAL A CG1 
1776 C  CG2 . VAL A 217 ? 0.1732 0.0982 0.2678 -0.0351 -0.0059 -0.0378 217 VAL A CG2 
1777 N  N   . SER A 218 ? 0.1799 0.0829 0.1698 -0.0149 -0.0358 -0.0024 218 SER A N   
1778 C  CA  . SER A 218 ? 0.1808 0.0833 0.1729 -0.0066 -0.0178 -0.0089 218 SER A CA  
1779 C  C   . SER A 218 ? 0.1826 0.0827 0.1779 -0.0188 -0.0103 0.0044  218 SER A C   
1780 O  O   . SER A 218 ? 0.2071 0.0657 0.1885 -0.0315 -0.0155 0.0066  218 SER A O   
1781 C  CB  . SER A 218 ? 0.2220 0.1077 0.1483 -0.0299 -0.0052 -0.0118 218 SER A CB  
1782 O  OG  . SER A 218 ? 0.2175 0.1136 0.1741 -0.0350 -0.0409 0.0111  218 SER A OG  
1783 N  N   . SER A 219 ? 0.2279 0.0759 0.1905 -0.0008 0.0137  -0.0067 219 SER A N   
1784 C  CA  . SER A 219 ? 0.1942 0.1553 0.2153 -0.0206 0.0055  0.0161  219 SER A CA  
1785 C  C   . SER A 219 ? 0.2114 0.0506 0.2574 -0.0387 -0.0032 0.0317  219 SER A C   
1786 O  O   . SER A 219 ? 0.2007 0.1061 0.2699 -0.0222 0.0121  0.0138  219 SER A O   
1787 C  CB  . SER A 219 ? 0.3413 0.0801 0.2791 0.0103  -0.0209 0.0033  219 SER A CB  
1788 O  OG  . SER A 219 ? 0.3356 0.1256 0.3386 0.0190  -0.0108 -0.0252 219 SER A OG  
1789 N  N   . GLU A 220 ? 0.2097 0.0837 0.2178 -0.0242 0.0050  0.0029  220 GLU A N   
1790 C  CA  . GLU A 220 ? 0.2388 0.1150 0.2242 -0.0386 0.0061  0.0093  220 GLU A CA  
1791 C  C   . GLU A 220 ? 0.2179 0.1141 0.2075 -0.0336 -0.0012 -0.0190 220 GLU A C   
1792 O  O   . GLU A 220 ? 0.2229 0.1080 0.2461 -0.0233 0.0232  0.0025  220 GLU A O   
1793 C  CB  . GLU A 220 ? 0.2761 0.1386 0.2543 -0.0453 -0.0399 -0.0187 220 GLU A CB  
1794 C  CG  . GLU A 220 ? 0.4119 0.1122 0.3516 -0.0317 -0.0225 -0.1300 220 GLU A CG  
1795 C  CD  . GLU A 220 ? 0.4308 0.2476 0.4368 -0.0113 0.0217  -0.0621 220 GLU A CD  
1796 O  OE1 . GLU A 220 ? 0.2878 0.2028 0.3554 -0.0814 -0.0102 -0.0514 220 GLU A OE1 
1797 O  OE2 . GLU A 220 ? 0.5971 0.2459 0.5228 -0.0691 0.0950  -0.1035 220 GLU A OE2 
1798 N  N   . GLN A 221 ? 0.2159 0.0763 0.1890 -0.0127 -0.0065 0.0206  221 GLN A N   
1799 C  CA  . GLN A 221 ? 0.1680 0.0700 0.1942 -0.0250 -0.0275 0.0252  221 GLN A CA  
1800 C  C   . GLN A 221 ? 0.1723 0.0989 0.1806 -0.0057 -0.0231 0.0079  221 GLN A C   
1801 O  O   . GLN A 221 ? 0.2036 0.0883 0.1923 -0.0121 0.0022  0.0159  221 GLN A O   
1802 C  CB  . GLN A 221 ? 0.1492 0.1179 0.2064 -0.0094 -0.0198 0.0311  221 GLN A CB  
1803 C  CG  . GLN A 221 ? 0.1690 0.1102 0.2115 -0.0119 -0.0375 -0.0043 221 GLN A CG  
1804 C  CD  . GLN A 221 ? 0.1917 0.0712 0.1824 -0.0444 -0.0162 0.0055  221 GLN A CD  
1805 O  OE1 . GLN A 221 ? 0.1838 0.0867 0.1877 -0.0066 -0.0039 0.0107  221 GLN A OE1 
1806 N  NE2 . GLN A 221 ? 0.1822 0.1005 0.2257 -0.0116 -0.0171 0.0162  221 GLN A NE2 
1807 N  N   . VAL A 222 ? 0.1788 0.1009 0.1793 0.0019  -0.0273 0.0166  222 VAL A N   
1808 C  CA  . VAL A 222 ? 0.1666 0.1370 0.1723 -0.0193 -0.0111 0.0316  222 VAL A CA  
1809 C  C   . VAL A 222 ? 0.1592 0.1271 0.2091 -0.0062 -0.0044 0.0163  222 VAL A C   
1810 O  O   . VAL A 222 ? 0.1700 0.1446 0.1806 -0.0179 0.0089  0.0303  222 VAL A O   
1811 C  CB  . VAL A 222 ? 0.2192 0.1806 0.2481 -0.0330 -0.0550 0.1105  222 VAL A CB  
1812 C  CG1 . VAL A 222 ? 0.1844 0.1840 0.3123 -0.0341 -0.0370 0.0768  222 VAL A CG1 
1813 C  CG2 . VAL A 222 ? 0.2467 0.2154 0.2348 -0.0389 -0.0620 0.0486  222 VAL A CG2 
1814 N  N   . LEU A 223 ? 0.1856 0.0944 0.2499 -0.0034 -0.0001 0.0062  223 LEU A N   
1815 C  CA  . LEU A 223 ? 0.2333 0.1023 0.3253 -0.0292 0.0450  -0.0057 223 LEU A CA  
1816 C  C   . LEU A 223 ? 0.1727 0.1155 0.2341 -0.0279 -0.0006 -0.0381 223 LEU A C   
1817 O  O   . LEU A 223 ? 0.1776 0.1427 0.2661 -0.0187 0.0274  -0.0157 223 LEU A O   
1818 C  CB  . LEU A 223 ? 0.3412 0.1192 0.3010 -0.0586 0.0305  -0.0064 223 LEU A CB  
1819 C  CG  . LEU A 223 ? 0.5161 0.6679 0.4000 0.2043  0.0442  -0.1498 223 LEU A CG  
1820 C  CD1 . LEU A 223 ? 0.3560 0.3290 0.8325 0.0715  -0.0472 -0.0348 223 LEU A CD1 
1821 C  CD2 . LEU A 223 ? 0.6139 0.4936 0.9561 -0.2972 -0.1302 -0.1973 223 LEU A CD2 
1822 N  N   . LYS A 224 ? 0.1751 0.1454 0.1985 -0.0186 -0.0044 -0.0212 224 LYS A N   
1823 C  CA  . LYS A 224 ? 0.1956 0.1439 0.1903 -0.0216 0.0237  -0.0217 224 LYS A CA  
1824 C  C   . LYS A 224 ? 0.1835 0.1034 0.1395 0.0013  0.0200  0.0107  224 LYS A C   
1825 O  O   . LYS A 224 ? 0.2085 0.1314 0.1479 -0.0238 0.0175  0.0156  224 LYS A O   
1826 C  CB  . LYS A 224 ? 0.2317 0.1883 0.2125 -0.0128 0.0178  0.0577  224 LYS A CB  
1827 C  CG  . LYS A 224 ? 0.2532 0.2897 0.3037 -0.0760 -0.0053 -0.0152 224 LYS A CG  
1828 C  CD  . LYS A 224 ? 0.3198 0.2843 0.2895 -0.0761 -0.0158 -0.0463 224 LYS A CD  
1829 C  CE  . LYS A 224 ? 0.4257 0.4792 0.3364 -0.1122 -0.0590 -0.1703 224 LYS A CE  
1830 N  NZ  . LYS A 224 ? 0.4044 0.3596 0.3042 -0.1346 0.0505  -0.0781 224 LYS A NZ  
1831 N  N   . PHE A 225 ? 0.1801 0.1065 0.1276 0.0049  0.0003  -0.0039 225 PHE A N   
1832 C  CA  . PHE A 225 ? 0.1776 0.0982 0.1324 -0.0102 0.0172  -0.0024 225 PHE A CA  
1833 C  C   . PHE A 225 ? 0.1894 0.1011 0.1504 -0.0111 0.0373  0.0037  225 PHE A C   
1834 O  O   . PHE A 225 ? 0.1888 0.1049 0.1536 -0.0066 0.0356  -0.0074 225 PHE A O   
1835 C  CB  . PHE A 225 ? 0.2038 0.0781 0.1371 0.0147  0.0035  0.0016  225 PHE A CB  
1836 C  CG  . PHE A 225 ? 0.1669 0.0704 0.1734 -0.0118 0.0134  -0.0027 225 PHE A CG  
1837 C  CD1 . PHE A 225 ? 0.1791 0.1082 0.1773 -0.0004 0.0155  0.0197  225 PHE A CD1 
1838 C  CD2 . PHE A 225 ? 0.1574 0.1258 0.1736 -0.0250 0.0236  -0.0332 225 PHE A CD2 
1839 C  CE1 . PHE A 225 ? 0.2208 0.1224 0.2029 -0.0184 0.0441  -0.0168 225 PHE A CE1 
1840 C  CE2 . PHE A 225 ? 0.1672 0.1888 0.2150 0.0061  0.0073  -0.0535 225 PHE A CE2 
1841 C  CZ  . PHE A 225 ? 0.1781 0.0937 0.2111 -0.0131 0.0139  -0.0301 225 PHE A CZ  
1842 N  N   . ARG A 226 ? 0.1798 0.0919 0.1546 0.0082  0.0151  -0.0095 226 ARG A N   
1843 C  CA  . ARG A 226 ? 0.1826 0.1070 0.1464 0.0065  0.0358  0.0314  226 ARG A CA  
1844 C  C   . ARG A 226 ? 0.1601 0.0962 0.1673 -0.0185 0.0397  -0.0055 226 ARG A C   
1845 O  O   . ARG A 226 ? 0.1817 0.1529 0.1967 0.0144  0.0368  -0.0041 226 ARG A O   
1846 C  CB  . ARG A 226 ? 0.2201 0.1163 0.1500 0.0022  0.0233  0.0348  226 ARG A CB  
1847 C  CG  . ARG A 226 ? 0.2108 0.0982 0.1481 -0.0006 0.0198  0.0326  226 ARG A CG  
1848 C  CD  . ARG A 226 ? 0.3008 0.0937 0.1659 0.0106  0.0209  0.0186  226 ARG A CD  
1849 N  NE  . ARG A 226 ? 0.2118 0.1092 0.1612 -0.0411 -0.0201 0.0176  226 ARG A NE  
1850 C  CZ  . ARG A 226 ? 0.1819 0.1162 0.1914 -0.0359 0.0200  -0.0308 226 ARG A CZ  
1851 N  NH1 . ARG A 226 ? 0.2396 0.1456 0.2588 -0.0460 -0.0350 -0.0706 226 ARG A NH1 
1852 N  NH2 . ARG A 226 ? 0.2253 0.0858 0.2143 -0.0120 0.0563  -0.0100 226 ARG A NH2 
1853 N  N   . LYS A 227 ? 0.2384 0.1028 0.1360 -0.0136 0.0239  -0.0053 227 LYS A N   
1854 C  CA  . LYS A 227 ? 0.2269 0.1197 0.1481 -0.0240 0.0311  -0.0219 227 LYS A CA  
1855 C  C   . LYS A 227 ? 0.2597 0.1061 0.1285 -0.0032 0.0466  0.0031  227 LYS A C   
1856 O  O   . LYS A 227 ? 0.2564 0.1332 0.1449 -0.0200 0.0524  -0.0162 227 LYS A O   
1857 C  CB  . LYS A 227 ? 0.2789 0.1493 0.1822 -0.0430 0.0135  -0.0419 227 LYS A CB  
1858 C  CG  . LYS A 227 ? 0.3479 0.1605 0.2002 -0.0867 0.0232  -0.0497 227 LYS A CG  
1859 C  CD  . LYS A 227 ? 0.4024 0.4252 0.2726 -0.0926 -0.0276 -0.1380 227 LYS A CD  
1860 C  CE  . LYS A 227 ? 0.5005 0.4440 0.3395 -0.0642 0.0348  -0.0811 227 LYS A CE  
1861 N  NZ  . LYS A 227 ? 0.7398 0.5467 0.6462 -0.1340 -0.0927 -0.2290 227 LYS A NZ  
1862 N  N   . LEU A 228 ? 0.2050 0.0882 0.1662 -0.0036 0.0219  0.0004  228 LEU A N   
1863 C  CA  . LEU A 228 ? 0.1740 0.0910 0.1371 -0.0055 0.0330  -0.0078 228 LEU A CA  
1864 C  C   . LEU A 228 ? 0.1852 0.1127 0.1403 0.0111  0.0335  -0.0008 228 LEU A C   
1865 O  O   . LEU A 228 ? 0.1787 0.1190 0.1450 0.0160  0.0125  -0.0066 228 LEU A O   
1866 C  CB  . LEU A 228 ? 0.1787 0.1110 0.1363 -0.0109 0.0343  -0.0272 228 LEU A CB  
1867 C  CG  . LEU A 228 ? 0.1650 0.1375 0.1367 -0.0144 0.0300  0.0131  228 LEU A CG  
1868 C  CD1 . LEU A 228 ? 0.1849 0.1332 0.1508 0.0188  0.0350  -0.0062 228 LEU A CD1 
1869 C  CD2 . LEU A 228 ? 0.2681 0.1454 0.1450 0.0136  0.0580  0.0268  228 LEU A CD2 
1870 N  N   . ASN A 229 ? 0.1780 0.1371 0.1384 -0.0203 0.0381  -0.0060 229 ASN A N   
1871 C  CA  . ASN A 229 ? 0.1567 0.1363 0.1294 0.0134  0.0298  -0.0103 229 ASN A CA  
1872 C  C   . ASN A 229 ? 0.1630 0.1285 0.1472 0.0016  0.0363  0.0031  229 ASN A C   
1873 O  O   . ASN A 229 ? 0.1941 0.1266 0.1529 0.0119  0.0414  0.0146  229 ASN A O   
1874 C  CB  . ASN A 229 ? 0.2043 0.1424 0.1567 -0.0058 0.0452  0.0036  229 ASN A CB  
1875 C  CG  . ASN A 229 ? 0.2661 0.1386 0.1665 0.0194  0.0502  0.0082  229 ASN A CG  
1876 O  OD1 . ASN A 229 ? 0.2777 0.2100 0.1614 0.0280  0.0482  -0.0082 229 ASN A OD1 
1877 N  ND2 . ASN A 229 ? 0.2583 0.1327 0.1806 0.0019  0.0585  -0.0250 229 ASN A ND2 
1878 N  N   . PHE A 230 ? 0.1648 0.1160 0.1310 -0.0042 0.0303  -0.0100 230 PHE A N   
1879 C  CA  . PHE A 230 ? 0.1601 0.1125 0.1259 -0.0124 0.0326  -0.0020 230 PHE A CA  
1880 C  C   . PHE A 230 ? 0.1971 0.1032 0.1425 0.0072  0.0370  0.0085  230 PHE A C   
1881 O  O   . PHE A 230 ? 0.2240 0.1183 0.1615 -0.0171 0.0496  -0.0008 230 PHE A O   
1882 C  CB  . PHE A 230 ? 0.1583 0.1338 0.1400 -0.0242 0.0185  0.0029  230 PHE A CB  
1883 C  CG  . PHE A 230 ? 0.1626 0.1099 0.1442 -0.0214 0.0359  -0.0103 230 PHE A CG  
1884 C  CD1 . PHE A 230 ? 0.1831 0.1032 0.1461 -0.0124 0.0414  -0.0064 230 PHE A CD1 
1885 C  CD2 . PHE A 230 ? 0.2018 0.0944 0.1747 -0.0171 0.0359  -0.0031 230 PHE A CD2 
1886 C  CE1 . PHE A 230 ? 0.2212 0.1155 0.1298 -0.0260 0.0085  0.0182  230 PHE A CE1 
1887 C  CE2 . PHE A 230 ? 0.2110 0.1265 0.1608 -0.0269 0.0407  -0.0106 230 PHE A CE2 
1888 C  CZ  . PHE A 230 ? 0.1960 0.1244 0.1432 0.0086  0.0143  0.0085  230 PHE A CZ  
1889 N  N   . ASN A 231 ? 0.1766 0.1511 0.1468 0.0000  0.0583  0.0050  231 ASN A N   
1890 C  CA  . ASN A 231 ? 0.2031 0.1077 0.1680 -0.0054 0.0537  0.0116  231 ASN A CA  
1891 C  C   . ASN A 231 ? 0.1700 0.1441 0.1436 -0.0137 0.0482  0.0104  231 ASN A C   
1892 O  O   . ASN A 231 ? 0.1917 0.1206 0.1686 0.0255  0.0551  0.0013  231 ASN A O   
1893 C  CB  . ASN A 231 ? 0.2039 0.1324 0.1844 0.0166  0.0643  -0.0041 231 ASN A CB  
1894 C  CG  . ASN A 231 ? 0.1885 0.1181 0.1662 0.0309  0.0502  0.0161  231 ASN A CG  
1895 O  OD1 . ASN A 231 ? 0.2262 0.1125 0.1741 0.0004  0.0610  0.0104  231 ASN A OD1 
1896 N  ND2 . ASN A 231 ? 0.2238 0.1514 0.1644 0.0421  0.0258  0.0138  231 ASN A ND2 
1897 N  N   . GLY A 232 ? 0.2005 0.1145 0.1766 0.0057  0.0526  0.0375  232 GLY A N   
1898 C  CA  . GLY A 232 ? 0.2160 0.1323 0.1596 0.0185  0.0414  0.0322  232 GLY A CA  
1899 C  C   . GLY A 232 ? 0.2100 0.1395 0.1666 0.0253  0.0421  0.0234  232 GLY A C   
1900 O  O   . GLY A 232 ? 0.2205 0.1608 0.1793 0.0384  0.0624  0.0222  232 GLY A O   
1901 N  N   . GLU A 233 ? 0.1985 0.1569 0.1576 0.0283  0.0515  0.0245  233 GLU A N   
1902 C  CA  . GLU A 233 ? 0.2025 0.1763 0.1518 0.0323  0.0346  0.0295  233 GLU A CA  
1903 C  C   . GLU A 233 ? 0.2020 0.1862 0.1632 -0.0002 0.0408  0.0294  233 GLU A C   
1904 O  O   . GLU A 233 ? 0.1901 0.1770 0.1744 0.0243  0.0559  0.0159  233 GLU A O   
1905 C  CB  . GLU A 233 ? 0.2268 0.1858 0.1852 0.0757  0.0502  0.0381  233 GLU A CB  
1906 C  CG  . GLU A 233 ? 0.1964 0.2748 0.1980 -0.0114 0.0076  0.0399  233 GLU A CG  
1907 C  CD  . GLU A 233 ? 0.3015 0.3386 0.3063 0.0854  -0.0088 0.0155  233 GLU A CD  
1908 O  OE1 . GLU A 233 ? 0.3071 0.2538 0.3694 0.0291  0.0613  0.1066  233 GLU A OE1 
1909 O  OE2 . GLU A 233 ? 0.3279 0.3389 0.3657 -0.0005 -0.0652 0.0044  233 GLU A OE2 
1910 N  N   . GLY A 234 ? 0.2321 0.1801 0.1720 0.0185  0.0680  0.0290  234 GLY A N   
1911 C  CA  . GLY A 234 ? 0.2154 0.1738 0.1794 0.0332  0.0594  0.0582  234 GLY A CA  
1912 C  C   . GLY A 234 ? 0.2127 0.1224 0.1521 0.0363  0.0568  0.0089  234 GLY A C   
1913 O  O   . GLY A 234 ? 0.2104 0.1597 0.1901 0.0185  0.0650  0.0255  234 GLY A O   
1914 N  N   . GLU A 235 ? 0.2063 0.1569 0.1655 0.0203  0.0556  0.0285  235 GLU A N   
1915 C  CA  . GLU A 235 ? 0.2093 0.1542 0.1790 0.0269  0.0316  0.0286  235 GLU A CA  
1916 C  C   . GLU A 235 ? 0.1838 0.1942 0.2157 0.0289  0.0813  0.0302  235 GLU A C   
1917 O  O   . GLU A 235 ? 0.2124 0.1506 0.1895 0.0243  0.0576  0.0105  235 GLU A O   
1918 C  CB  . GLU A 235 ? 0.2231 0.1417 0.2344 0.0189  0.0016  -0.0188 235 GLU A CB  
1919 C  CG  . GLU A 235 ? 0.2582 0.1668 0.2893 -0.0164 0.0387  0.0244  235 GLU A CG  
1920 C  CD  . GLU A 235 ? 0.4716 0.2913 0.2997 -0.0759 0.0502  -0.0215 235 GLU A CD  
1921 O  OE1 . GLU A 235 ? 0.2566 0.2175 0.3520 -0.0288 0.0283  -0.0103 235 GLU A OE1 
1922 O  OE2 . GLU A 235 ? 0.6880 0.2876 0.4876 -0.0511 0.2828  -0.0139 235 GLU A OE2 
1923 N  N   . PRO A 236 ? 0.1823 0.1439 0.2071 0.0173  0.0579  0.0273  236 PRO A N   
1924 C  CA  . PRO A 236 ? 0.1761 0.1650 0.2396 0.0189  0.0842  0.0484  236 PRO A CA  
1925 C  C   . PRO A 236 ? 0.1860 0.1360 0.1597 0.0182  0.0697  0.0150  236 PRO A C   
1926 O  O   . PRO A 236 ? 0.2089 0.1400 0.1718 0.0309  0.0439  0.0030  236 PRO A O   
1927 C  CB  . PRO A 236 ? 0.1594 0.2643 0.2575 0.0293  0.0873  0.0661  236 PRO A CB  
1928 C  CG  . PRO A 236 ? 0.1736 0.2266 0.3397 0.0451  0.0695  0.0995  236 PRO A CG  
1929 C  CD  . PRO A 236 ? 0.1798 0.2095 0.2853 0.0296  0.0469  0.0539  236 PRO A CD  
1930 N  N   . GLU A 237 ? 0.1874 0.1334 0.2041 0.0194  0.0697  0.0042  237 GLU A N   
1931 C  CA  . GLU A 237 ? 0.1905 0.1409 0.1665 -0.0047 0.0640  -0.0157 237 GLU A CA  
1932 C  C   . GLU A 237 ? 0.2057 0.1109 0.1896 -0.0243 0.0600  -0.0036 237 GLU A C   
1933 O  O   . GLU A 237 ? 0.2319 0.1345 0.2071 0.0220  0.0709  0.0023  237 GLU A O   
1934 C  CB  . GLU A 237 ? 0.2221 0.1769 0.2437 -0.0469 0.0498  -0.0546 237 GLU A CB  
1935 C  CG  . GLU A 237 ? 0.2240 0.2470 0.2929 -0.0208 0.0521  -0.0280 237 GLU A CG  
1936 C  CD  . GLU A 237 ? 0.2114 0.3368 0.2758 -0.0326 0.0660  -0.0793 237 GLU A CD  
1937 O  OE1 . GLU A 237 ? 0.4312 0.5127 0.7219 0.0025  0.0309  -0.3344 237 GLU A OE1 
1938 O  OE2 . GLU A 237 ? 0.3057 0.2393 0.2843 -0.0069 0.1191  -0.0563 237 GLU A OE2 
1939 N  N   . GLU A 238 ? 0.1959 0.1500 0.1443 -0.0206 0.0668  -0.0061 238 GLU A N   
1940 C  CA  . GLU A 238 ? 0.1641 0.1974 0.1543 -0.0062 0.0593  0.0008  238 GLU A CA  
1941 C  C   . GLU A 238 ? 0.1738 0.1120 0.1608 0.0110  0.0806  0.0037  238 GLU A C   
1942 O  O   . GLU A 238 ? 0.2211 0.0864 0.2151 0.0070  0.0662  0.0068  238 GLU A O   
1943 C  CB  . GLU A 238 ? 0.2394 0.2944 0.1465 -0.0776 0.0176  -0.0021 238 GLU A CB  
1944 C  CG  . GLU A 238 ? 0.2569 0.4322 0.3665 -0.0612 0.0435  0.0604  238 GLU A CG  
1945 C  CD  . GLU A 238 ? 0.4950 0.6292 0.5848 -0.2024 -0.1509 0.0409  238 GLU A CD  
1946 O  OE1 . GLU A 238 ? 0.6736 0.8326 0.6081 -0.1751 -0.1565 0.1641  238 GLU A OE1 
1947 O  OE2 . GLU A 238 ? 0.6699 0.6903 0.7323 -0.2771 -0.0038 0.1215  238 GLU A OE2 
1948 N  N   . LEU A 239 ? 0.1725 0.1206 0.1544 -0.0219 0.0485  -0.0129 239 LEU A N   
1949 C  CA  . LEU A 239 ? 0.1608 0.1164 0.1546 -0.0440 0.0434  -0.0284 239 LEU A CA  
1950 C  C   . LEU A 239 ? 0.1474 0.0967 0.1421 0.0073  0.0337  -0.0089 239 LEU A C   
1951 O  O   . LEU A 239 ? 0.1657 0.1092 0.1538 0.0052  0.0433  -0.0089 239 LEU A O   
1952 C  CB  . LEU A 239 ? 0.1783 0.0978 0.1945 -0.0073 0.0143  -0.0209 239 LEU A CB  
1953 C  CG  . LEU A 239 ? 0.1978 0.1231 0.2140 0.0086  0.0311  -0.0569 239 LEU A CG  
1954 C  CD1 . LEU A 239 ? 0.2128 0.0957 0.4259 -0.0110 -0.0321 -0.0700 239 LEU A CD1 
1955 C  CD2 . LEU A 239 ? 0.2670 0.1496 0.2023 -0.0181 0.0267  -0.0406 239 LEU A CD2 
1956 N  N   . MET A 240 ? 0.1687 0.0781 0.1296 0.0108  0.0547  -0.0034 240 MET A N   
1957 C  CA  . MET A 240 ? 0.1801 0.0867 0.1192 0.0205  0.0478  -0.0023 240 MET A CA  
1958 C  C   . MET A 240 ? 0.1414 0.1120 0.1204 0.0006  0.0308  -0.0163 240 MET A C   
1959 O  O   . MET A 240 ? 0.1502 0.1009 0.1375 -0.0046 0.0193  -0.0074 240 MET A O   
1960 C  CB  . MET A 240 ? 0.1903 0.0874 0.1316 0.0423  0.0306  -0.0096 240 MET A CB  
1961 C  CG  . MET A 240 ? 0.1666 0.0820 0.1567 0.0071  0.0409  -0.0225 240 MET A CG  
1962 S  SD  . MET A 240 ? 0.1944 0.0856 0.1562 0.0084  0.0369  -0.0053 240 MET A SD  
1963 C  CE  . MET A 240 ? 0.2146 0.0827 0.1520 -0.0064 0.0542  0.0154  240 MET A CE  
1964 N  N   . VAL A 241 ? 0.1664 0.0863 0.1050 0.0019  0.0231  0.0070  241 VAL A N   
1965 C  CA  . VAL A 241 ? 0.1752 0.0829 0.1099 -0.0165 0.0274  0.0011  241 VAL A CA  
1966 C  C   . VAL A 241 ? 0.1341 0.0811 0.1259 0.0070  0.0163  -0.0037 241 VAL A C   
1967 O  O   . VAL A 241 ? 0.1465 0.1048 0.1446 0.0046  0.0280  -0.0063 241 VAL A O   
1968 C  CB  . VAL A 241 ? 0.1543 0.0828 0.1553 -0.0143 0.0297  -0.0179 241 VAL A CB  
1969 C  CG1 . VAL A 241 ? 0.2002 0.1059 0.1948 -0.0222 -0.0156 -0.0331 241 VAL A CG1 
1970 C  CG2 . VAL A 241 ? 0.1852 0.0892 0.1838 -0.0022 0.0465  -0.0025 241 VAL A CG2 
1971 N  N   . ASP A 242 ? 0.1650 0.0864 0.1045 0.0120  0.0244  -0.0071 242 ASP A N   
1972 C  CA  . ASP A 242 ? 0.1207 0.0891 0.1375 0.0009  0.0098  -0.0124 242 ASP A CA  
1973 C  C   . ASP A 242 ? 0.1022 0.0949 0.1270 -0.0084 0.0171  -0.0140 242 ASP A C   
1974 O  O   . ASP A 242 ? 0.1303 0.0905 0.2143 0.0029  -0.0184 -0.0283 242 ASP A O   
1975 C  CB  . ASP A 242 ? 0.1500 0.0767 0.1964 0.0188  0.0272  -0.0055 242 ASP A CB  
1976 C  CG  . ASP A 242 ? 0.1676 0.0725 0.1434 0.0183  0.0346  0.0031  242 ASP A CG  
1977 O  OD1 . ASP A 242 ? 0.1526 0.0745 0.1569 0.0079  0.0275  -0.0023 242 ASP A OD1 
1978 O  OD2 . ASP A 242 ? 0.2210 0.0775 0.2057 0.0102  0.0719  -0.0184 242 ASP A OD2 
1979 N  N   . ASN A 243 ? 0.1212 0.0662 0.1374 -0.0004 0.0178  -0.0146 243 ASN A N   
1980 C  CA  . ASN A 243 ? 0.1331 0.0695 0.1074 -0.0146 0.0237  -0.0098 243 ASN A CA  
1981 C  C   . ASN A 243 ? 0.0970 0.0838 0.1162 -0.0077 0.0258  -0.0070 243 ASN A C   
1982 O  O   . ASN A 243 ? 0.1377 0.1007 0.1497 0.0221  0.0364  0.0060  243 ASN A O   
1983 C  CB  . ASN A 243 ? 0.1298 0.1075 0.1177 -0.0212 0.0113  0.0087  243 ASN A CB  
1984 C  CG  . ASN A 243 ? 0.1253 0.0777 0.1192 -0.0107 0.0278  0.0048  243 ASN A CG  
1985 O  OD1 . ASN A 243 ? 0.1260 0.0923 0.1586 -0.0149 0.0256  0.0229  243 ASN A OD1 
1986 N  ND2 . ASN A 243 ? 0.1531 0.0998 0.1233 0.0031  0.0223  0.0059  243 ASN A ND2 
1987 N  N   . TRP A 244 ? 0.1256 0.0856 0.1032 -0.0104 0.0133  -0.0085 244 TRP A N   
1988 C  CA  . TRP A 244 ? 0.1158 0.0792 0.1028 -0.0058 0.0109  0.0013  244 TRP A CA  
1989 C  C   . TRP A 244 ? 0.1029 0.0817 0.1307 0.0013  0.0205  -0.0077 244 TRP A C   
1990 O  O   . TRP A 244 ? 0.1093 0.1030 0.1571 0.0172  0.0091  -0.0179 244 TRP A O   
1991 C  CB  . TRP A 244 ? 0.1215 0.0598 0.1421 -0.0021 0.0190  0.0117  244 TRP A CB  
1992 C  CG  . TRP A 244 ? 0.1216 0.0721 0.1223 -0.0059 0.0124  -0.0031 244 TRP A CG  
1993 C  CD1 . TRP A 244 ? 0.1059 0.0761 0.1355 0.0033  0.0248  -0.0111 244 TRP A CD1 
1994 C  CD2 . TRP A 244 ? 0.1506 0.0818 0.1167 0.0002  0.0127  0.0063  244 TRP A CD2 
1995 N  NE1 . TRP A 244 ? 0.1249 0.0869 0.1296 0.0044  0.0278  0.0022  244 TRP A NE1 
1996 C  CE2 . TRP A 244 ? 0.1342 0.0863 0.1344 0.0093  0.0164  0.0046  244 TRP A CE2 
1997 C  CE3 . TRP A 244 ? 0.1504 0.0976 0.1324 -0.0084 -0.0040 0.0105  244 TRP A CE3 
1998 C  CZ2 . TRP A 244 ? 0.1463 0.1050 0.1461 0.0100  0.0022  0.0147  244 TRP A CZ2 
1999 C  CZ3 . TRP A 244 ? 0.1820 0.1063 0.1672 0.0399  0.0199  0.0136  244 TRP A CZ3 
2000 C  CH2 . TRP A 244 ? 0.1654 0.0968 0.1507 0.0087  -0.0002 0.0214  244 TRP A CH2 
2001 N  N   . ARG A 245 ? 0.1210 0.0955 0.1039 -0.0163 0.0121  -0.0100 245 ARG A N   
2002 C  CA  . ARG A 245 ? 0.1288 0.0829 0.1221 -0.0016 0.0088  -0.0201 245 ARG A CA  
2003 C  C   . ARG A 245 ? 0.1190 0.1070 0.1238 -0.0079 -0.0114 -0.0080 245 ARG A C   
2004 O  O   . ARG A 245 ? 0.1307 0.1040 0.1582 -0.0054 0.0071  -0.0136 245 ARG A O   
2005 C  CB  . ARG A 245 ? 0.1073 0.0849 0.1478 -0.0076 0.0040  -0.0396 245 ARG A CB  
2006 C  CG  . ARG A 245 ? 0.0979 0.0988 0.1626 -0.0078 0.0006  -0.0236 245 ARG A CG  
2007 C  CD  . ARG A 245 ? 0.1021 0.1206 0.1536 -0.0364 0.0152  -0.0454 245 ARG A CD  
2008 N  NE  . ARG A 245 ? 0.1031 0.1298 0.1596 -0.0333 -0.0003 -0.0266 245 ARG A NE  
2009 C  CZ  . ARG A 245 ? 0.1127 0.1377 0.1511 -0.0438 0.0072  -0.0359 245 ARG A CZ  
2010 N  NH1 . ARG A 245 ? 0.1392 0.1647 0.1668 -0.0206 0.0411  -0.0303 245 ARG A NH1 
2011 N  NH2 . ARG A 245 ? 0.1176 0.1714 0.1684 -0.0622 0.0062  -0.0207 245 ARG A NH2 
2012 N  N   . PRO A 246 ? 0.1301 0.1192 0.1256 0.0091  0.0047  -0.0051 246 PRO A N   
2013 C  CA  . PRO A 246 ? 0.1356 0.1284 0.1285 0.0232  0.0138  0.0091  246 PRO A CA  
2014 C  C   . PRO A 246 ? 0.1389 0.1142 0.1374 0.0097  0.0098  -0.0067 246 PRO A C   
2015 O  O   . PRO A 246 ? 0.1363 0.1046 0.1654 0.0042  0.0043  -0.0017 246 PRO A O   
2016 C  CB  . PRO A 246 ? 0.1813 0.1604 0.1826 0.0825  0.0111  -0.0121 246 PRO A CB  
2017 C  CG  . PRO A 246 ? 0.2018 0.2337 0.3360 0.0694  0.0479  0.1189  246 PRO A CG  
2018 C  CD  . PRO A 246 ? 0.1190 0.1447 0.2228 0.0352  0.0000  0.0047  246 PRO A CD  
2019 N  N   . ALA A 247 ? 0.1432 0.1068 0.1391 0.0226  0.0108  -0.0071 247 ALA A N   
2020 C  CA  . ALA A 247 ? 0.1424 0.1263 0.1267 -0.0025 0.0070  -0.0245 247 ALA A CA  
2021 C  C   . ALA A 247 ? 0.1353 0.1110 0.1338 0.0122  0.0027  -0.0006 247 ALA A C   
2022 O  O   . ALA A 247 ? 0.1571 0.1395 0.1607 0.0432  -0.0037 0.0065  247 ALA A O   
2023 C  CB  . ALA A 247 ? 0.1903 0.1420 0.1772 -0.0055 0.0367  0.0002  247 ALA A CB  
2024 N  N   . GLN A 248 ? 0.1447 0.1059 0.1294 -0.0081 0.0080  -0.0054 248 GLN A N   
2025 C  CA  . GLN A 248 ? 0.1244 0.1111 0.1367 0.0054  0.0055  -0.0016 248 GLN A CA  
2026 C  C   . GLN A 248 ? 0.1247 0.1222 0.1479 0.0309  -0.0017 0.0023  248 GLN A C   
2027 O  O   . GLN A 248 ? 0.1483 0.1356 0.1626 0.0075  0.0161  0.0067  248 GLN A O   
2028 C  CB  . GLN A 248 ? 0.1723 0.1044 0.1647 0.0203  0.0096  0.0118  248 GLN A CB  
2029 C  CG  . GLN A 248 ? 0.1605 0.0989 0.1550 -0.0145 0.0179  0.0133  248 GLN A CG  
2030 C  CD  . GLN A 248 ? 0.1360 0.1373 0.1758 -0.0133 0.0100  -0.0113 248 GLN A CD  
2031 O  OE1 . GLN A 248 ? 0.1453 0.2294 0.2081 -0.0285 0.0037  -0.0398 248 GLN A OE1 
2032 N  NE2 . GLN A 248 ? 0.1687 0.1562 0.1708 0.0039  0.0283  -0.0002 248 GLN A NE2 
2033 N  N   . PRO A 249 ? 0.1553 0.1934 0.1479 0.0450  -0.0132 0.0003  249 PRO A N   
2034 C  CA  . PRO A 249 ? 0.1647 0.2412 0.1449 0.0709  0.0193  0.0068  249 PRO A CA  
2035 C  C   . PRO A 249 ? 0.1615 0.1650 0.1560 0.0477  0.0024  0.0074  249 PRO A C   
2036 O  O   . PRO A 249 ? 0.1540 0.1675 0.1655 0.0376  0.0001  0.0038  249 PRO A O   
2037 C  CB  . PRO A 249 ? 0.1745 0.3288 0.2096 0.1399  -0.0522 -0.0923 249 PRO A CB  
2038 C  CG  . PRO A 249 ? 0.2077 0.3495 0.1678 0.0372  -0.0287 -0.0420 249 PRO A CG  
2039 C  CD  . PRO A 249 ? 0.1165 0.2608 0.2030 0.0313  -0.0375 -0.0368 249 PRO A CD  
2040 N  N   . LEU A 250 ? 0.1905 0.1705 0.1414 0.0714  0.0066  0.0161  250 LEU A N   
2041 C  CA  . LEU A 250 ? 0.1826 0.1432 0.1436 0.0263  0.0255  -0.0258 250 LEU A CA  
2042 C  C   . LEU A 250 ? 0.1684 0.1208 0.1590 0.0230  -0.0119 0.0040  250 LEU A C   
2043 O  O   . LEU A 250 ? 0.1745 0.1348 0.1709 0.0319  -0.0097 0.0062  250 LEU A O   
2044 C  CB  . LEU A 250 ? 0.1881 0.1967 0.1966 0.0184  0.0363  0.0359  250 LEU A CB  
2045 C  CG  . LEU A 250 ? 0.1988 0.1932 0.1783 -0.0203 0.0436  0.0102  250 LEU A CG  
2046 C  CD1 . LEU A 250 ? 0.1635 0.2408 0.1709 0.0003  0.0165  0.0042  250 LEU A CD1 
2047 C  CD2 . LEU A 250 ? 0.2713 0.2036 0.2056 -0.0516 0.0601  0.0266  250 LEU A CD2 
2048 N  N   . LYS A 251 ? 0.1863 0.2080 0.1416 0.0582  -0.0216 -0.0044 251 LYS A N   
2049 C  CA  . LYS A 251 ? 0.2078 0.2965 0.1345 0.0403  -0.0051 -0.0419 251 LYS A CA  
2050 C  C   . LYS A 251 ? 0.1935 0.3094 0.1981 0.0643  -0.0067 -0.0533 251 LYS A C   
2051 O  O   . LYS A 251 ? 0.3126 0.3928 0.2093 0.0025  0.0839  -0.0493 251 LYS A O   
2052 C  CB  . LYS A 251 ? 0.2082 0.2508 0.2046 -0.0039 -0.0057 -0.0823 251 LYS A CB  
2053 C  CG  . LYS A 251 ? 0.3037 0.3886 0.2622 -0.0209 0.1242  -0.1020 251 LYS A CG  
2054 C  CD  . LYS A 251 ? 0.3147 0.4363 0.3103 -0.0495 0.0690  -0.1084 251 LYS A CD  
2055 C  CE  . LYS A 251 ? 0.4029 0.3521 0.3489 -0.0555 0.1455  -0.1333 251 LYS A CE  
2056 N  NZ  . LYS A 251 ? 0.4017 0.3491 0.4574 -0.0239 0.1324  -0.0031 251 LYS A NZ  
2057 N  N   A ASN A 252 ? 0.1759 0.3523 0.2404 0.0779  -0.0375 -0.1451 252 ASN A N   
2058 N  N   B ASN A 252 ? 0.1532 0.2839 0.1307 0.0480  -0.0239 -0.0384 252 ASN A N   
2059 C  CA  A ASN A 252 ? 0.1848 0.5011 0.2939 0.0813  -0.0058 -0.0903 252 ASN A CA  
2060 C  CA  B ASN A 252 ? 0.1937 0.2616 0.1757 0.0285  -0.0247 -0.0871 252 ASN A CA  
2061 C  C   A ASN A 252 ? 0.2183 0.4819 0.1481 0.0886  -0.0392 -0.0278 252 ASN A C   
2062 C  C   B ASN A 252 ? 0.1883 0.1896 0.2262 0.0162  -0.0064 -0.0099 252 ASN A C   
2063 O  O   A ASN A 252 ? 0.2547 0.5875 0.1296 0.1477  -0.0399 -0.0255 252 ASN A O   
2064 O  O   B ASN A 252 ? 0.3010 0.2152 0.2810 0.0693  -0.0306 -0.1029 252 ASN A O   
2065 C  CB  A ASN A 252 ? 0.2963 0.6132 0.3642 0.1066  -0.0849 -0.1496 252 ASN A CB  
2066 C  CB  B ASN A 252 ? 0.1679 0.2578 0.2321 -0.0160 -0.0005 -0.0847 252 ASN A CB  
2067 C  CG  A ASN A 252 ? 0.3176 0.6791 0.3414 0.1410  0.0027  -0.0451 252 ASN A CG  
2068 C  CG  B ASN A 252 ? 0.2230 0.3558 0.2922 0.0402  0.0232  -0.1163 252 ASN A CG  
2069 O  OD1 A ASN A 252 ? 0.5505 0.8088 0.4988 -0.0098 -0.1363 0.0287  252 ASN A OD1 
2070 O  OD1 B ASN A 252 ? 0.3441 0.4188 0.2588 -0.0143 0.0756  -0.1210 252 ASN A OD1 
2071 N  ND2 A ASN A 252 ? 0.3775 0.6603 0.3283 0.1603  -0.1376 -0.0402 252 ASN A ND2 
2072 N  ND2 B ASN A 252 ? 0.2002 0.3414 0.2859 0.0269  -0.0381 -0.1488 252 ASN A ND2 
2073 N  N   A ARG A 253 ? 0.1781 0.1822 0.1716 -0.0375 -0.0128 0.0009  253 ARG A N   
2074 N  N   B ARG A 253 ? 0.1099 0.2298 0.1723 0.0343  0.0093  -0.0206 253 ARG A N   
2075 C  CA  A ARG A 253 ? 0.1805 0.1583 0.1531 -0.0144 0.0015  -0.0365 253 ARG A CA  
2076 C  CA  B ARG A 253 ? 0.0994 0.1975 0.1698 0.0203  0.0134  -0.0163 253 ARG A CA  
2077 C  C   A ARG A 253 ? 0.1920 0.1770 0.1945 -0.0230 -0.0073 0.0079  253 ARG A C   
2078 C  C   B ARG A 253 ? 0.1608 0.2108 0.1727 -0.0368 -0.0113 -0.0294 253 ARG A C   
2079 O  O   A ARG A 253 ? 0.2513 0.1655 0.2886 0.0212  0.0682  -0.0016 253 ARG A O   
2080 O  O   B ARG A 253 ? 0.2226 0.2233 0.2062 -0.0247 0.0669  0.0335  253 ARG A O   
2081 C  CB  A ARG A 253 ? 0.1586 0.1470 0.1485 -0.0021 0.0065  -0.0187 253 ARG A CB  
2082 C  CB  B ARG A 253 ? 0.1298 0.1342 0.1605 0.0034  0.0100  -0.0190 253 ARG A CB  
2083 C  CG  A ARG A 253 ? 0.1856 0.1526 0.1395 -0.0150 0.0009  -0.0186 253 ARG A CG  
2084 C  CG  B ARG A 253 ? 0.1619 0.1301 0.1274 -0.0142 -0.0040 -0.0252 253 ARG A CG  
2085 C  CD  A ARG A 253 ? 0.1705 0.1474 0.1454 0.0267  0.0364  -0.0225 253 ARG A CD  
2086 C  CD  B ARG A 253 ? 0.1404 0.1271 0.1309 0.0141  0.0274  -0.0225 253 ARG A CD  
2087 N  NE  A ARG A 253 ? 0.1421 0.1230 0.1414 0.0189  0.0117  -0.0183 253 ARG A NE  
2088 N  NE  B ARG A 253 ? 0.1292 0.1129 0.1360 0.0167  0.0097  -0.0190 253 ARG A NE  
2089 C  CZ  A ARG A 253 ? 0.1104 0.0982 0.1267 0.0099  -0.0012 -0.0001 253 ARG A CZ  
2090 C  CZ  B ARG A 253 ? 0.1047 0.0944 0.1221 0.0087  -0.0001 -0.0009 253 ARG A CZ  
2091 N  NH1 A ARG A 253 ? 0.1076 0.1009 0.1356 -0.0008 -0.0115 0.0107  253 ARG A NH1 
2092 N  NH1 B ARG A 253 ? 0.1053 0.0989 0.1328 -0.0002 -0.0114 0.0105  253 ARG A NH1 
2093 N  NH2 A ARG A 253 ? 0.1328 0.0860 0.1625 0.0111  0.0016  -0.0165 253 ARG A NH2 
2094 N  NH2 B ARG A 253 ? 0.1274 0.0838 0.1567 0.0114  0.0013  -0.0154 253 ARG A NH2 
2095 N  N   . GLN A 254 ? 0.1696 0.2291 0.1496 -0.0204 0.0044  -0.0339 254 GLN A N   
2096 C  CA  . GLN A 254 ? 0.1891 0.2720 0.1849 -0.0475 -0.0139 -0.0296 254 GLN A CA  
2097 C  C   . GLN A 254 ? 0.1934 0.2215 0.1575 -0.0107 -0.0089 0.0209  254 GLN A C   
2098 O  O   . GLN A 254 ? 0.2525 0.2104 0.2803 0.0010  -0.0818 0.0055  254 GLN A O   
2099 C  CB  . GLN A 254 ? 0.2357 0.3583 0.1953 -0.0006 0.0515  0.0167  254 GLN A CB  
2100 C  CG  . GLN A 254 ? 0.3482 0.5060 0.2197 0.0198  -0.0043 0.0006  254 GLN A CG  
2101 N  N   . ILE A 255 ? 0.1648 0.1948 0.1461 -0.0084 0.0122  0.0207  255 ILE A N   
2102 C  CA  . ILE A 255 ? 0.1331 0.2046 0.1429 0.0230  0.0249  0.0013  255 ILE A CA  
2103 C  C   . ILE A 255 ? 0.1323 0.1770 0.1317 0.0216  0.0241  0.0257  255 ILE A C   
2104 O  O   . ILE A 255 ? 0.1757 0.1729 0.1862 0.0234  0.0370  0.0693  255 ILE A O   
2105 C  CB  . ILE A 255 ? 0.1508 0.1644 0.1524 0.0385  0.0000  0.0136  255 ILE A CB  
2106 C  CG1 . ILE A 255 ? 0.1808 0.1470 0.1862 0.0528  0.0301  0.0078  255 ILE A CG1 
2107 C  CG2 . ILE A 255 ? 0.1723 0.1795 0.1694 -0.0024 -0.0039 0.0350  255 ILE A CG2 
2108 C  CD1 . ILE A 255 ? 0.2046 0.2041 0.2153 0.0129  0.0659  -0.0339 255 ILE A CD1 
2109 N  N   . LYS A 256 ? 0.1113 0.1795 0.1696 0.0152  -0.0079 0.0105  256 LYS A N   
2110 C  CA  . LYS A 256 ? 0.1201 0.1787 0.1465 0.0210  0.0017  0.0016  256 LYS A CA  
2111 C  C   . LYS A 256 ? 0.1185 0.1779 0.1271 -0.0068 0.0165  0.0118  256 LYS A C   
2112 O  O   . LYS A 256 ? 0.1777 0.2075 0.1176 -0.0399 0.0316  0.0039  256 LYS A O   
2113 C  CB  . LYS A 256 ? 0.1867 0.1819 0.1896 0.0223  0.0248  0.0005  256 LYS A CB  
2114 C  CG  . LYS A 256 ? 0.2028 0.2437 0.2984 -0.0302 0.0283  -0.0438 256 LYS A CG  
2115 N  N   . ALA A 257 ? 0.1346 0.1842 0.1443 -0.0143 0.0402  0.0117  257 ALA A N   
2116 C  CA  . ALA A 257 ? 0.1479 0.1662 0.1597 -0.0035 0.0182  0.0295  257 ALA A CA  
2117 C  C   . ALA A 257 ? 0.1357 0.1823 0.1068 -0.0120 0.0256  0.0187  257 ALA A C   
2118 O  O   . ALA A 257 ? 0.1561 0.2199 0.1395 0.0009  0.0275  -0.0165 257 ALA A O   
2119 C  CB  . ALA A 257 ? 0.2052 0.1607 0.1690 -0.0089 0.0554  0.0269  257 ALA A CB  
2120 N  N   . SER A 258 ? 0.1533 0.1600 0.1374 0.0047  0.0062  -0.0006 258 SER A N   
2121 C  CA  . SER A 258 ? 0.1400 0.2247 0.1791 0.0152  0.0223  0.0161  258 SER A CA  
2122 C  C   . SER A 258 ? 0.1447 0.2343 0.1650 0.0122  0.0591  -0.0178 258 SER A C   
2123 O  O   . SER A 258 ? 0.1536 0.3463 0.2337 0.0301  0.0722  -0.0009 258 SER A O   
2124 C  CB  . SER A 258 ? 0.2154 0.1414 0.1862 -0.0054 -0.0055 0.0113  258 SER A CB  
2125 O  OG  . SER A 258 ? 0.1464 0.1817 0.1696 -0.0073 0.0207  0.0006  258 SER A OG  
2126 N  N   . PHE A 259 ? 0.1274 0.2533 0.2116 -0.0229 0.0488  -0.0111 259 PHE A N   
2127 C  CA  . PHE A 259 ? 0.1694 0.2951 0.2530 -0.0803 0.0508  -0.0245 259 PHE A CA  
2128 C  C   . PHE A 259 ? 0.4719 0.4121 0.2090 -0.0109 -0.0108 -0.0432 259 PHE A C   
2129 O  O   . PHE A 259 ? 0.4621 0.3996 0.2858 -0.1870 -0.0262 0.1240  259 PHE A O   
2130 C  CB  . PHE A 259 ? 0.1960 0.2695 0.2585 -0.0587 0.0256  -0.0158 259 PHE A CB  
2131 C  CG  . PHE A 259 ? 0.1637 0.2208 0.2651 -0.0425 -0.0067 0.0828  259 PHE A CG  
2132 C  CD1 . PHE A 259 ? 0.1723 0.1745 0.1841 -0.0374 -0.0005 0.0190  259 PHE A CD1 
2133 C  CD2 . PHE A 259 ? 0.2366 0.2240 0.3297 -0.0113 0.0232  0.0841  259 PHE A CD2 
2134 C  CE1 . PHE A 259 ? 0.1894 0.1684 0.2892 -0.0366 -0.0089 -0.0333 259 PHE A CE1 
2135 C  CE2 . PHE A 259 ? 0.2093 0.2337 0.4084 -0.0111 -0.0394 0.0539  259 PHE A CE2 
2136 C  CZ  . PHE A 259 ? 0.1912 0.1801 0.4141 -0.0285 -0.0033 -0.0413 259 PHE A CZ  
2137 N  N   . LYS A 260 ? 0.8321 0.9975 0.6100 -0.3531 0.4470  0.0889  260 LYS A N   
2138 C  CA  . LYS A 260 ? 0.8998 0.7928 0.4604 -0.0157 0.4649  0.4002  260 LYS A CA  
2139 C  C   . LYS A 260 ? 0.6822 1.5649 0.6967 -0.2280 0.2623  0.3950  260 LYS A C   
2140 O  O   . LYS A 260 ? 1.1160 1.0160 1.1794 -0.4083 0.2915  0.0420  260 LYS A O   
2141 C  CB  . LYS A 260 ? 1.2176 0.8816 0.8616 -0.0971 0.3574  0.2731  260 LYS A CB  
2142 O  OXT . LYS A 260 ? 0.7535 1.1281 0.4766 0.0036  -0.0038 0.2069  260 LYS A OXT 
2143 ZN ZN  . ZN  B .   ? 0.1101 0.0609 0.1337 -0.0075 0.0052  0.0000  301 ZN  A ZN  
2144 S  S   . DMS C .   ? 0.2495 0.2869 0.2975 -0.0182 0.0121  -0.0145 302 DMS A S   
2145 O  O   . DMS C .   ? 0.4040 0.3224 0.3563 0.1089  0.0256  -0.0932 302 DMS A O   
2146 C  C1  . DMS C .   ? 0.2179 0.2498 0.2394 0.0011  0.0066  -0.0352 302 DMS A C1  
2147 C  C2  . DMS C .   ? 0.2391 0.2117 0.5863 -0.0559 0.0435  -0.1302 302 DMS A C2  
2148 F  F18 . V90 D .   ? 0.2096 0.1680 0.2151 -0.0150 0.0164  0.0453  303 V90 A F18 
2149 C  C5  . V90 D .   ? 0.1817 0.0986 0.1944 -0.0436 0.0093  0.0168  303 V90 A C5  
2150 C  C6  . V90 D .   ? 0.1808 0.1273 0.1561 -0.0582 0.0130  0.0053  303 V90 A C6  
2151 S  S12 . V90 D .   ? 0.2116 0.1899 0.1952 -0.0572 0.0227  -0.0184 303 V90 A S12 
2152 C  C13 . V90 D .   ? 0.2211 0.3257 0.2352 -0.0942 0.0719  -0.0004 303 V90 A C13 
2153 C  C14 . V90 D .   ? 0.5642 0.2549 0.4479 -0.2049 0.0046  0.0566  303 V90 A C14 
2154 O  O15 . V90 D .   ? 0.5674 0.6285 0.5620 -0.1609 -0.1329 0.2061  303 V90 A O15 
2155 C  C1  . V90 D .   ? 0.1601 0.0973 0.1952 -0.0129 0.0127  -0.0034 303 V90 A C1  
2156 F  F17 . V90 D .   ? 0.1737 0.1274 0.2262 -0.0193 0.0375  -0.0439 303 V90 A F17 
2157 C  C4  . V90 D .   ? 0.1423 0.0917 0.2070 -0.0272 0.0031  0.0111  303 V90 A C4  
2158 C  C3  . V90 D .   ? 0.1277 0.1111 0.1675 -0.0284 0.0086  -0.0078 303 V90 A C3  
2159 S  S8  . V90 D .   ? 0.1332 0.0687 0.1738 -0.0182 -0.0107 -0.0019 303 V90 A S8  
2160 O  O10 . V90 D .   ? 0.1244 0.0644 0.1770 0.0122  -0.0102 0.0062  303 V90 A O10 
2161 N  N11 . V90 D .   ? 0.1197 0.0480 0.1427 -0.0192 -0.0085 -0.0047 303 V90 A N11 
2162 O  O9  . V90 D .   ? 0.1357 0.0700 0.1799 -0.0230 -0.0282 0.0019  303 V90 A O9  
2163 C  C2  . V90 D .   ? 0.1273 0.0985 0.1824 -0.0198 0.0053  0.0029  303 V90 A C2  
2164 F  F16 . V90 D .   ? 0.1569 0.1005 0.2154 -0.0047 0.0266  0.0015  303 V90 A F16 
2165 N  N7  . V90 D .   ? 0.1571 0.1052 0.2357 -0.0102 -0.0064 0.0373  303 V90 A N7  
2166 C  C19 . V90 D .   ? 0.2165 0.1167 0.2613 -0.0076 0.0398  0.0365  303 V90 A C19 
2167 C  C26 . V90 D .   ? 0.2978 0.0919 0.3325 0.0697  0.0996  0.0077  303 V90 A C26 
2168 C  C25 . V90 D .   ? 0.3019 0.1550 0.3669 0.0462  -0.0617 0.0201  303 V90 A C25 
2169 C  C24 . V90 D .   ? 0.3845 0.3438 0.4390 -0.0066 -0.1855 -0.0845 303 V90 A C24 
2170 C  C23 . V90 D .   ? 0.4152 0.2950 0.3449 0.0638  -0.1129 -0.0229 303 V90 A C23 
2171 C  C22 . V90 D .   ? 0.4462 0.2294 0.4143 0.1029  -0.0249 -0.2216 303 V90 A C22 
2172 C  C21 . V90 D .   ? 0.4591 0.2481 0.4359 0.0888  -0.1391 -0.0275 303 V90 A C21 
2173 C  C20 . V90 D .   ? 0.2371 0.0919 0.4599 -0.0649 0.0425  0.0156  303 V90 A C20 
2174 O  O   . HOH E .   ? 0.3883 0.3244 0.4367 -0.1488 -0.1095 0.0567  401 HOH A O   
2175 O  O   . HOH E .   ? 0.7270 0.4154 0.4544 -0.0985 -0.0702 0.0170  402 HOH A O   
2176 O  O   . HOH E .   ? 0.3899 0.5650 0.9130 0.0084  0.0023  0.0805  403 HOH A O   
2177 O  O   . HOH E .   ? 0.2640 0.7076 0.3239 -0.0439 0.0800  -0.2529 404 HOH A O   
2178 O  O   . HOH E .   ? 0.4796 0.6197 0.3816 -0.0722 0.0935  0.0326  405 HOH A O   
2179 O  O   . HOH E .   ? 0.2808 0.1068 0.2745 -0.0287 -0.0041 0.0008  406 HOH A O   
2180 O  O   . HOH E .   ? 0.5880 0.3504 0.5183 -0.0529 -0.2150 -0.0622 407 HOH A O   
2181 O  O   . HOH E .   ? 0.3755 0.8080 0.5156 0.0431  -0.0311 0.0208  408 HOH A O   
2182 O  O   . HOH E .   ? 0.2271 0.2298 0.2465 -0.0822 -0.0203 0.0013  409 HOH A O   
2183 O  O   . HOH E .   ? 0.4125 0.5651 0.7360 0.0290  -0.3109 -0.0861 410 HOH A O   
2184 O  O   . HOH E .   ? 0.4150 0.2825 0.5174 0.1229  -0.0549 -0.1762 411 HOH A O   
2185 O  O   . HOH E .   ? 0.3938 0.4464 1.0691 -0.0934 -0.0290 -0.1776 412 HOH A O   
2186 O  O   . HOH E .   ? 0.5727 0.3413 0.4197 -0.2132 -0.0119 -0.0251 413 HOH A O   
2187 O  O   . HOH E .   ? 0.3705 0.1838 0.4349 -0.0356 -0.0642 0.0671  414 HOH A O   
2188 O  O   . HOH E .   ? 0.4119 0.2827 0.5748 0.0348  -0.1318 -0.1109 415 HOH A O   
2189 O  O   . HOH E .   ? 0.4040 0.3949 0.4443 0.0495  0.2362  0.0233  416 HOH A O   
2190 O  O   . HOH E .   ? 0.3749 0.2341 0.3389 -0.0064 0.0161  0.0498  417 HOH A O   
2191 O  O   . HOH E .   ? 0.7108 0.2906 0.3209 0.0352  -0.0164 0.0053  418 HOH A O   
2192 O  O   . HOH E .   ? 0.3411 0.2339 0.3294 -0.0177 0.0732  -0.0725 419 HOH A O   
2193 O  O   . HOH E .   ? 0.4514 0.5985 0.8054 0.2271  0.1240  0.1170  420 HOH A O   
2194 O  O   . HOH E .   ? 0.4458 0.6955 0.6560 -0.2360 0.1189  0.1375  421 HOH A O   
2195 O  O   . HOH E .   ? 0.3093 0.1874 0.3035 -0.0023 0.0000  -0.0251 422 HOH A O   
2196 O  O   . HOH E .   ? 0.1781 0.5495 0.4089 0.0016  0.0002  -0.1456 423 HOH A O   
2197 O  O   . HOH E .   ? 0.4986 0.6610 0.4807 -0.1949 -0.1465 0.2681  424 HOH A O   
2198 O  O   . HOH E .   ? 0.6670 0.6875 0.3588 -0.1356 -0.1165 0.1058  425 HOH A O   
2199 O  O   . HOH E .   ? 0.3125 0.2183 0.3643 -0.0717 -0.0201 0.0817  426 HOH A O   
2200 O  O   . HOH E .   ? 0.2653 0.3615 0.5474 0.0292  0.0566  0.0464  427 HOH A O   
2201 O  O   . HOH E .   ? 0.3776 0.7176 0.6896 0.1560  -0.0222 -0.0183 428 HOH A O   
2202 O  O   . HOH E .   ? 0.4176 0.3191 0.1851 -0.0570 0.0439  -0.0660 429 HOH A O   
2203 O  O   . HOH E .   ? 0.3691 0.4038 0.3559 -0.1524 0.0858  -0.1332 430 HOH A O   
2204 O  O   . HOH E .   ? 0.4131 0.5995 0.2781 -0.0296 0.0831  0.0070  431 HOH A O   
2205 O  O   . HOH E .   ? 0.3521 0.3748 0.2005 0.0737  -0.0389 0.0284  432 HOH A O   
2206 O  O   . HOH E .   ? 0.2556 0.1176 0.2236 -0.0483 0.0419  -0.0146 433 HOH A O   
2207 O  O   . HOH E .   ? 0.3113 0.1619 0.3793 -0.0066 -0.1442 -0.0662 434 HOH A O   
2208 O  O   . HOH E .   ? 0.3255 0.3269 0.3256 0.0243  0.0419  -0.0401 435 HOH A O   
2209 O  O   . HOH E .   ? 0.2749 0.2769 0.2972 0.0591  0.0061  0.0115  436 HOH A O   
2210 O  O   . HOH E .   ? 0.6109 0.6149 0.4671 -0.0303 0.1571  0.0240  437 HOH A O   
2211 O  O   . HOH E .   ? 0.3909 0.4275 0.6433 0.0146  -0.0599 -0.0637 438 HOH A O   
2212 O  O   . HOH E .   ? 0.4748 0.2354 0.6363 0.0066  -0.1832 0.0329  439 HOH A O   
2213 O  O   . HOH E .   ? 0.2400 0.2226 0.3145 0.0539  -0.0340 -0.0136 440 HOH A O   
2214 O  O   . HOH E .   ? 0.4945 0.3646 0.5026 0.1649  -0.1437 -0.1786 441 HOH A O   
2215 O  O   . HOH E .   ? 0.3708 0.2286 0.2438 -0.0135 -0.0293 0.0586  442 HOH A O   
2216 O  O   . HOH E .   ? 0.3276 0.2995 0.4145 0.0945  -0.1550 -0.1207 443 HOH A O   
2217 O  O   . HOH E .   ? 0.5231 0.5065 0.7043 -0.2364 0.1298  -0.0016 444 HOH A O   
2218 O  O   . HOH E .   ? 0.1718 0.1910 0.5184 0.0074  0.0557  0.0407  445 HOH A O   
2219 O  O   . HOH E .   ? 0.5152 0.5799 0.4397 0.2120  0.0983  0.1324  446 HOH A O   
2220 O  O   . HOH E .   ? 0.3251 0.2059 0.2596 -0.0708 -0.0027 -0.0400 447 HOH A O   
2221 O  O   . HOH E .   ? 0.2736 0.4338 0.1680 -0.1441 -0.0394 0.0272  448 HOH A O   
2222 O  O   . HOH E .   ? 0.4453 0.3495 0.6799 -0.0080 0.0314  -0.0844 449 HOH A O   
2223 O  O   . HOH E .   ? 0.4175 0.4247 0.4572 -0.1086 0.1349  -0.2318 450 HOH A O   
2224 O  O   . HOH E .   ? 0.2790 0.1729 0.1752 -0.0507 0.0144  0.0122  451 HOH A O   
2225 O  O   . HOH E .   ? 0.4833 0.4914 0.6955 -0.0810 0.0361  0.0951  452 HOH A O   
2226 O  O   . HOH E .   ? 0.5945 0.3010 0.3717 -0.1089 -0.0348 0.0518  453 HOH A O   
2227 O  O   . HOH E .   ? 0.2247 0.3377 0.2921 0.0355  0.0809  0.0443  454 HOH A O   
2228 O  O   . HOH E .   ? 0.4373 0.4934 0.4230 -0.1442 -0.0499 0.0911  455 HOH A O   
2229 O  O   . HOH E .   ? 0.8199 0.7422 0.6876 -0.1459 0.2647  -0.0833 456 HOH A O   
2230 O  O   . HOH E .   ? 0.2187 0.1515 0.2013 0.0357  0.0724  0.0411  457 HOH A O   
2231 O  O   . HOH E .   ? 0.2515 0.7568 0.4750 -0.1242 0.0697  -0.2000 458 HOH A O   
2232 O  O   . HOH E .   ? 0.1357 0.1260 0.1823 -0.0215 0.0325  -0.0089 459 HOH A O   
2233 O  O   . HOH E .   ? 0.4555 0.3791 0.4822 0.0013  -0.0038 -0.0250 460 HOH A O   
2234 O  O   . HOH E .   ? 0.4239 0.6594 0.2809 -0.0026 0.0857  0.1455  461 HOH A O   
2235 O  O   . HOH E .   ? 0.5066 0.3714 0.4162 0.1376  -0.0157 -0.0895 462 HOH A O   
2236 O  O   . HOH E .   ? 0.2291 0.1618 0.2481 0.0207  -0.0574 0.0244  463 HOH A O   
2237 O  O   . HOH E .   ? 0.2011 0.2075 0.3708 0.0275  -0.1057 -0.0916 464 HOH A O   
2238 O  O   . HOH E .   ? 0.2543 0.2488 0.3006 -0.0653 -0.0109 0.0754  465 HOH A O   
2239 O  O   . HOH E .   ? 0.2574 0.3405 0.4166 0.0348  0.0086  0.0916  466 HOH A O   
2240 O  O   . HOH E .   ? 0.2746 0.3053 0.2829 0.0411  0.0586  0.0343  467 HOH A O   
2241 O  O   . HOH E .   ? 0.4573 0.4798 0.2813 0.0458  -0.0655 0.1046  468 HOH A O   
2242 O  O   . HOH E .   ? 0.2616 0.1962 0.2420 0.0515  0.0362  0.0434  469 HOH A O   
2243 O  O   . HOH E .   ? 0.2409 0.1461 0.4216 -0.0249 0.0860  -0.0626 470 HOH A O   
2244 O  O   . HOH E .   ? 0.2567 0.3866 0.3461 -0.0919 0.0013  0.0044  471 HOH A O   
2245 O  O   . HOH E .   ? 0.1869 0.2267 0.2444 0.0238  -0.0021 -0.0016 472 HOH A O   
2246 O  O   . HOH E .   ? 0.3926 0.3345 0.6639 0.0315  -0.0091 0.1459  473 HOH A O   
2247 O  O   . HOH E .   ? 0.4684 0.4104 0.4924 0.0093  -0.1499 0.1103  474 HOH A O   
2248 O  O   . HOH E .   ? 0.1635 0.0942 0.1798 -0.0077 0.0288  -0.0244 475 HOH A O   
2249 O  O   . HOH E .   ? 0.3754 0.1831 0.4223 -0.0278 0.0245  0.0157  476 HOH A O   
2250 O  O   . HOH E .   ? 0.4801 0.3654 0.2991 -0.0705 -0.0416 0.0289  477 HOH A O   
2251 O  O   . HOH E .   ? 0.4723 0.2066 0.3856 -0.0219 0.0550  -0.0495 478 HOH A O   
2252 O  O   . HOH E .   ? 0.3432 0.2470 0.3661 -0.0722 -0.0675 -0.0209 479 HOH A O   
2253 O  O   . HOH E .   ? 0.2326 0.3358 0.3788 -0.0078 -0.0197 0.0068  480 HOH A O   
2254 O  O   . HOH E .   ? 0.4985 0.2325 0.2580 -0.0690 0.0638  0.0524  481 HOH A O   
2255 O  O   . HOH E .   ? 0.3037 0.3448 0.5353 -0.0643 -0.0925 -0.0602 482 HOH A O   
2256 O  O   . HOH E .   ? 0.1186 0.1680 0.2346 -0.0009 0.0093  -0.0434 483 HOH A O   
2257 O  O   . HOH E .   ? 0.3283 0.1571 0.4882 -0.0015 -0.1333 0.0341  484 HOH A O   
2258 O  O   . HOH E .   ? 0.1521 0.1581 0.2034 0.0117  -0.0286 0.0325  485 HOH A O   
2259 O  O   . HOH E .   ? 0.3034 0.8540 0.4150 -0.0515 -0.0455 0.0842  486 HOH A O   
2260 O  O   . HOH E .   ? 0.1571 0.0935 0.1623 0.0243  0.0167  -0.0168 487 HOH A O   
2261 O  O   . HOH E .   ? 0.2895 0.2570 0.4539 -0.0035 -0.0006 0.1192  488 HOH A O   
2262 O  O   . HOH E .   ? 0.1230 0.0996 0.1587 -0.0184 0.0304  0.0054  489 HOH A O   
2263 O  O   . HOH E .   ? 0.2129 0.1967 0.4455 -0.0846 -0.1197 0.0558  490 HOH A O   
2264 O  O   . HOH E .   ? 0.2624 0.3027 0.7397 -0.0008 0.0575  0.0641  491 HOH A O   
2265 O  O   . HOH E .   ? 0.4247 0.2128 0.2520 -0.0266 0.0713  -0.0345 492 HOH A O   
2266 O  O   . HOH E .   ? 0.5389 0.5387 0.2930 0.1194  0.0820  0.1210  493 HOH A O   
2267 O  O   . HOH E .   ? 0.2609 0.0962 0.3164 -0.0348 0.0471  -0.0033 494 HOH A O   
2268 O  O   . HOH E .   ? 0.2490 0.1815 0.4618 0.0021  0.0321  -0.0523 495 HOH A O   
2269 O  O   . HOH E .   ? 0.2558 0.3119 0.3365 -0.0472 0.0916  -0.0339 496 HOH A O   
2270 O  O   . HOH E .   ? 0.2577 0.1601 0.3942 -0.0100 0.0791  0.0047  497 HOH A O   
2271 O  O   . HOH E .   ? 0.2332 0.2507 0.2636 0.0350  -0.0520 -0.0010 498 HOH A O   
2272 O  O   . HOH E .   ? 0.4979 0.2078 0.3884 -0.1224 0.1442  -0.0403 499 HOH A O   
2273 O  O   . HOH E .   ? 0.6387 0.4159 0.3679 0.2744  0.0221  -0.0671 500 HOH A O   
2274 O  O   . HOH E .   ? 0.5667 0.2506 0.2232 0.0672  0.0168  -0.0231 501 HOH A O   
2275 O  O   . HOH E .   ? 0.4142 0.3863 0.2970 -0.1229 -0.0571 -0.0136 502 HOH A O   
2276 O  O   . HOH E .   ? 0.1644 0.1122 0.1676 0.0170  0.0196  0.0005  503 HOH A O   
2277 O  O   . HOH E .   ? 0.2465 0.2661 0.3879 -0.0211 -0.0380 -0.0370 504 HOH A O   
2278 O  O   . HOH E .   ? 0.2346 0.3541 0.2781 0.0053  -0.0002 -0.0826 505 HOH A O   
2279 O  O   . HOH E .   ? 0.3485 0.3915 0.2854 -0.1521 0.0284  -0.0138 506 HOH A O   
2280 O  O   . HOH E .   ? 0.2362 0.2261 0.2272 0.0025  0.0960  -0.0302 507 HOH A O   
2281 O  O   . HOH E .   ? 0.3406 0.3725 0.5866 0.1623  0.0287  0.0906  508 HOH A O   
2282 O  O   . HOH E .   ? 0.5808 0.4106 0.5339 0.0370  0.0561  0.0958  509 HOH A O   
2283 O  O   . HOH E .   ? 0.2000 0.1790 0.2390 -0.0242 -0.0268 0.0417  510 HOH A O   
2284 O  O   . HOH E .   ? 0.3166 0.6298 0.3307 -0.1018 -0.0550 0.1018  511 HOH A O   
2285 O  O   . HOH E .   ? 0.4854 0.3137 0.2743 -0.1764 0.0594  -0.1203 512 HOH A O   
2286 O  O   . HOH E .   ? 0.7654 0.6725 0.4983 0.1599  0.3953  0.0501  513 HOH A O   
2287 O  O   . HOH E .   ? 0.6055 0.5218 0.3943 0.0383  0.0969  -0.1778 514 HOH A O   
2288 O  O   . HOH E .   ? 0.3468 0.2362 0.2706 -0.0727 0.0270  0.0142  515 HOH A O   
2289 O  O   . HOH E .   ? 0.6840 0.8023 1.0391 0.1865  0.1139  0.2658  516 HOH A O   
2290 O  O   . HOH E .   ? 0.4473 0.2440 0.3595 0.1301  -0.0916 -0.0432 517 HOH A O   
2291 O  O   . HOH E .   ? 0.4488 0.3054 0.3553 0.0013  -0.0220 -0.0002 518 HOH A O   
2292 O  O   . HOH E .   ? 0.5446 0.4109 0.6193 0.0302  -0.0944 -0.0527 519 HOH A O   
2293 O  O   . HOH E .   ? 0.2445 0.3389 0.2648 0.0728  0.0960  0.1222  520 HOH A O   
2294 O  O   . HOH E .   ? 0.3952 0.2689 0.4904 -0.0161 0.0130  -0.0745 521 HOH A O   
2295 O  O   . HOH E .   ? 0.2803 0.2285 0.2062 -0.0051 0.0244  0.0020  522 HOH A O   
2296 O  O   . HOH E .   ? 0.3418 0.2894 0.4970 0.0791  -0.1664 -0.0873 523 HOH A O   
2297 O  O   . HOH E .   ? 0.4219 0.4199 0.4831 0.0576  0.0757  -0.0100 524 HOH A O   
2298 O  O   . HOH E .   ? 0.5952 0.3064 0.3775 -0.1678 0.2170  -0.1014 525 HOH A O   
2299 O  O   . HOH E .   ? 0.3391 0.2398 0.5267 0.0183  -0.0622 0.0713  526 HOH A O   
2300 O  O   . HOH E .   ? 0.2521 0.1119 0.2576 0.0238  0.0177  -0.0013 527 HOH A O   
2301 O  O   . HOH E .   ? 0.2251 0.2885 0.3470 -0.1203 0.0026  0.0700  528 HOH A O   
2302 O  O   . HOH E .   ? 0.1643 0.1538 0.2629 -0.0089 -0.0243 0.0094  529 HOH A O   
2303 O  O   . HOH E .   ? 0.2943 0.1571 0.4803 -0.0294 0.1246  -0.0646 530 HOH A O   
2304 O  O   . HOH E .   ? 0.5510 0.6061 0.7039 -0.0561 0.1870  0.0089  531 HOH A O   
2305 O  O   . HOH E .   ? 0.2521 0.2552 0.3143 -0.0436 -0.0533 0.0245  532 HOH A O   
2306 O  O   . HOH E .   ? 0.4511 0.6418 0.3937 0.0612  0.0064  0.0189  533 HOH A O   
2307 O  O   . HOH E .   ? 0.3055 0.4985 0.3896 -0.1741 0.0190  0.1395  534 HOH A O   
2308 O  O   . HOH E .   ? 0.5456 0.3144 0.3587 -0.0530 -0.0280 0.0514  535 HOH A O   
2309 O  O   . HOH E .   ? 0.1612 0.2400 0.2424 -0.0132 0.0240  -0.0257 536 HOH A O   
2310 O  O   . HOH E .   ? 0.2415 0.3265 0.4580 0.0351  0.0488  0.2068  537 HOH A O   
2311 O  O   . HOH E .   ? 0.5833 0.3431 0.5217 -0.0353 -0.1051 -0.0275 538 HOH A O   
2312 O  O   . HOH E .   ? 0.2659 0.6674 0.4740 0.0000  0.1690  0.0461  539 HOH A O   
2313 O  O   . HOH E .   ? 0.1360 0.2692 0.2341 0.0154  0.0049  -0.0111 540 HOH A O   
2314 O  O   . HOH E .   ? 0.1780 0.1283 0.1862 0.0120  -0.0063 0.0163  541 HOH A O   
2315 O  O   . HOH E .   ? 0.3916 0.7876 0.4641 -0.0516 0.0512  -0.1348 542 HOH A O   
2316 O  O   . HOH E .   ? 0.2084 0.2031 0.3791 -0.0810 -0.0602 -0.0693 543 HOH A O   
2317 O  O   . HOH E .   ? 0.2258 0.5628 0.4426 0.0401  0.0173  -0.2093 544 HOH A O   
2318 O  O   . HOH E .   ? 0.5087 0.2397 0.2881 -0.0693 0.0359  0.0719  545 HOH A O   
2319 O  O   . HOH E .   ? 0.3235 0.1854 0.2604 -0.0836 0.0747  0.0212  546 HOH A O   
2320 O  O   . HOH E .   ? 0.2913 0.2552 0.4096 0.0010  0.0546  -0.0176 547 HOH A O   
2321 O  O   . HOH E .   ? 0.3339 0.2470 0.2569 -0.0929 -0.0240 0.0521  548 HOH A O   
2322 O  O   . HOH E .   ? 0.2688 0.2557 0.3092 0.0324  0.0530  0.1390  549 HOH A O   
2323 O  O   . HOH E .   ? 0.2824 0.2380 0.2699 0.0105  -0.0186 -0.0784 550 HOH A O   
2324 O  O   . HOH E .   ? 0.5335 0.2992 0.2980 -0.1801 -0.0881 0.0177  551 HOH A O   
2325 O  O   . HOH E .   ? 0.1877 0.3538 0.4177 -0.0026 -0.0164 0.0697  552 HOH A O   
2326 O  O   . HOH E .   ? 0.2301 0.2673 0.3397 0.0392  0.0563  0.0800  553 HOH A O   
2327 O  O   . HOH E .   ? 0.2790 0.2702 0.7006 -0.0324 0.0319  -0.1005 554 HOH A O   
2328 O  O   . HOH E .   ? 0.1575 0.5890 0.6704 -0.0998 -0.0443 0.0750  555 HOH A O   
2329 O  O   . HOH E .   ? 0.3583 0.2637 0.2967 -0.0628 0.0100  0.0316  556 HOH A O   
2330 O  O   . HOH E .   ? 0.5074 0.2586 0.2460 0.1136  -0.0052 0.0085  557 HOH A O   
2331 O  O   . HOH E .   ? 0.4472 0.3822 0.2228 -0.1606 0.1350  -0.0615 558 HOH A O   
2332 O  O   . HOH E .   ? 0.5237 0.1847 0.2809 -0.0585 0.0519  -0.0432 559 HOH A O   
2333 O  O   . HOH E .   ? 0.6593 0.5212 0.7694 -0.1258 -0.0365 0.2505  560 HOH A O   
2334 O  O   . HOH E .   ? 0.2107 0.2748 0.2740 0.0000  -0.0134 0.1089  561 HOH A O   
2335 O  O   . HOH E .   ? 0.4549 1.0091 0.5793 -0.0436 0.2017  0.1198  562 HOH A O   
2336 O  O   . HOH E .   ? 0.2539 0.1916 0.4031 -0.0831 0.0421  0.0091  563 HOH A O   
2337 O  O   . HOH E .   ? 0.6457 0.3659 0.2647 -0.2213 -0.0788 0.0527  564 HOH A O   
2338 O  O   . HOH E .   ? 0.2980 0.1849 0.2458 -0.0653 -0.0474 -0.0163 565 HOH A O   
2339 O  O   . HOH E .   ? 0.3710 0.3068 0.8143 -0.1186 0.0850  -0.0513 566 HOH A O   
2340 O  O   . HOH E .   ? 0.5077 0.2946 0.3928 0.0941  -0.0154 0.0917  567 HOH A O   
2341 O  O   . HOH E .   ? 0.4995 0.2748 0.3177 0.0198  0.0136  0.0468  568 HOH A O   
2342 O  O   . HOH E .   ? 0.4695 0.2497 0.4821 -0.0088 -0.1048 -0.0418 569 HOH A O   
2343 O  O   . HOH E .   ? 0.3822 0.2952 0.2508 0.1085  -0.0427 -0.0006 570 HOH A O   
2344 O  O   . HOH E .   ? 0.2075 0.3261 0.3272 0.1037  0.0351  0.0311  571 HOH A O   
2345 O  O   . HOH E .   ? 0.4365 0.2147 0.3337 0.0647  0.0517  0.0662  572 HOH A O   
2346 O  O   . HOH E .   ? 0.2690 0.3557 0.4241 0.0178  0.0398  0.0991  573 HOH A O   
2347 O  O   . HOH E .   ? 0.3158 0.2526 0.3885 0.0697  0.1212  0.1112  574 HOH A O   
2348 O  O   . HOH E .   ? 0.4806 0.3860 0.5325 0.0533  0.2425  -0.0440 575 HOH A O   
2349 O  O   . HOH E .   ? 0.1590 0.1881 0.1841 0.0087  -0.0055 0.0225  576 HOH A O   
2350 O  O   . HOH E .   ? 0.3263 0.4873 0.5260 0.0964  0.0293  -0.0162 577 HOH A O   
2351 O  O   . HOH E .   ? 0.2045 0.2548 0.3340 0.0234  -0.0501 -0.0129 578 HOH A O   
2352 O  O   . HOH E .   ? 0.3806 0.4185 0.1676 0.1320  -0.0043 0.0104  579 HOH A O   
2353 O  O   . HOH E .   ? 0.6551 0.2993 0.4483 -0.1322 0.1200  -0.0292 580 HOH A O   
2354 O  O   . HOH E .   ? 0.3862 0.8417 0.4744 -0.1347 -0.0809 -0.0163 581 HOH A O   
2355 O  O   . HOH E .   ? 0.2840 0.2305 0.3005 0.0332  -0.0021 0.0396  582 HOH A O   
2356 O  O   . HOH E .   ? 0.1666 0.0970 0.1883 0.0106  0.0042  -0.0002 583 HOH A O   
2357 O  O   . HOH E .   ? 0.3240 0.1953 0.3685 -0.0290 0.0204  0.0491  584 HOH A O   
2358 O  O   . HOH E .   ? 0.2951 0.3486 0.6964 -0.0820 0.0606  -0.1454 585 HOH A O   
2359 O  O   . HOH E .   ? 0.3813 0.4597 0.4177 0.0802  0.1386  0.0794  586 HOH A O   
2360 O  O   . HOH E .   ? 0.2262 0.1543 0.2092 -0.0005 -0.0019 -0.0178 587 HOH A O   
2361 O  O   . HOH E .   ? 0.2507 0.2139 0.3835 0.0517  0.0002  -0.0188 588 HOH A O   
2362 O  O   . HOH E .   ? 0.3377 0.5364 0.3524 0.1127  0.0794  0.1897  589 HOH A O   
2363 O  O   . HOH E .   ? 0.7133 0.1838 0.3456 0.0842  0.0849  -0.0068 590 HOH A O   
2364 O  O   . HOH E .   ? 0.4849 0.3593 0.3463 0.0935  -0.0205 -0.1260 591 HOH A O   
2365 O  O   . HOH E .   ? 0.2879 0.6677 0.4578 -0.0369 -0.0530 0.0763  592 HOH A O   
2366 O  O   . HOH E .   ? 0.3520 0.2636 0.5359 0.0849  0.1703  0.0623  593 HOH A O   
2367 O  O   . HOH E .   ? 0.2878 0.7094 0.6391 -0.1537 -0.0103 0.0581  594 HOH A O   
2368 O  O   . HOH E .   ? 0.4275 0.3149 0.4088 0.0025  0.0442  0.0148  595 HOH A O   
2369 O  O   . HOH E .   ? 0.1571 0.2111 0.3180 -0.0173 -0.0052 0.0188  596 HOH A O   
2370 O  O   . HOH E .   ? 0.4760 0.5210 0.4809 0.0697  -0.0537 0.1534  597 HOH A O   
2371 O  O   . HOH E .   ? 0.4276 0.4727 0.3424 0.2073  0.1509  0.1220  598 HOH A O   
2372 O  O   . HOH E .   ? 0.4946 0.3480 0.4504 -0.1297 -0.0776 0.1553  599 HOH A O   
2373 O  O   . HOH E .   ? 0.4334 0.3990 0.5890 -0.0368 0.0049  0.0194  600 HOH A O   
2374 O  O   . HOH E .   ? 0.4797 0.3236 0.5516 -0.0490 0.1653  -0.1362 601 HOH A O   
2375 O  O   . HOH E .   ? 0.5475 0.6197 0.6715 0.0086  -0.3932 -0.0790 602 HOH A O   
2376 O  O   . HOH E .   ? 0.4262 0.3104 0.2115 -0.1014 -0.0344 0.0269  603 HOH A O   
2377 O  O   . HOH E .   ? 0.4320 0.3357 0.3506 0.0914  -0.0218 -0.0104 604 HOH A O   
2378 O  O   . HOH E .   ? 0.4577 0.4595 0.2753 0.0253  0.0314  0.0196  605 HOH A O   
2379 O  O   . HOH E .   ? 0.7325 0.3097 0.4918 0.0301  0.0196  -0.0081 606 HOH A O   
2380 O  O   . HOH E .   ? 0.4832 0.3570 0.3951 -0.1192 -0.0727 -0.0407 607 HOH A O   
2381 O  O   . HOH E .   ? 0.9187 0.3833 0.5169 -0.0048 0.0322  0.2075  608 HOH A O   
2382 O  O   . HOH E .   ? 0.6153 0.3558 0.3351 0.1097  -0.1483 0.0081  609 HOH A O   
2383 O  O   . HOH E .   ? 0.6231 0.4751 0.5097 0.0066  0.0022  -0.1711 610 HOH A O   
2384 O  O   . HOH E .   ? 0.7056 0.6320 0.2196 -0.0908 0.0060  -0.1253 611 HOH A O   
2385 O  O   . HOH E .   ? 0.3125 0.4615 0.4712 0.0103  -0.1196 -0.1347 612 HOH A O   
2386 O  O   . HOH E .   ? 0.4154 0.6179 0.4379 0.1566  -0.0089 -0.1040 613 HOH A O   
2387 O  O   . HOH E .   ? 0.4450 0.4879 0.6405 0.3024  0.3116  0.1514  614 HOH A O   
2388 O  O   . HOH E .   ? 0.5473 0.5935 0.4632 0.2458  -0.1769 -0.1458 615 HOH A O   
2389 O  O   . HOH E .   ? 0.2456 0.3116 0.3606 -0.0473 -0.0005 0.0267  616 HOH A O   
2390 O  O   . HOH E .   ? 0.5546 0.4183 0.7371 -0.1483 0.2891  -0.1533 617 HOH A O   
2391 O  O   . HOH E .   ? 0.4333 0.4156 0.5590 0.1384  -0.0154 -0.0223 618 HOH A O   
2392 O  O   . HOH E .   ? 0.6315 0.3621 0.6899 0.0077  0.0531  0.0064  619 HOH A O   
2393 O  O   . HOH E .   ? 0.3328 0.1654 0.5499 -0.0356 -0.1104 0.0151  620 HOH A O   
2394 O  O   . HOH E .   ? 0.6434 0.3218 0.7494 0.1942  -0.0624 -0.1238 621 HOH A O   
2395 O  O   . HOH E .   ? 0.3819 0.6674 0.4260 0.0452  -0.0309 0.0625  622 HOH A O   
2396 O  O   . HOH E .   ? 0.4242 1.0231 0.5323 0.2511  0.1703  0.2331  623 HOH A O   
2397 O  O   . HOH E .   ? 0.5286 1.0099 0.3157 -0.0771 -0.0445 -0.0298 624 HOH A O   
2398 O  O   . HOH E .   ? 0.3173 0.5281 0.5385 0.0977  0.0597  0.0268  625 HOH A O   
2399 O  O   . HOH E .   ? 0.4463 0.3139 0.3865 0.0561  -0.0305 0.0546  626 HOH A O   
2400 O  O   . HOH E .   ? 0.4581 0.3582 0.5396 0.0709  0.1239  0.3391  627 HOH A O   
2401 O  O   . HOH E .   ? 0.5146 0.2450 0.4154 0.0031  0.0750  0.0405  628 HOH A O   
2402 O  O   . HOH E .   ? 0.3529 0.2131 0.2564 -0.0794 0.0006  0.0015  629 HOH A O   
2403 O  O   . HOH E .   ? 0.8740 0.5570 0.6657 0.1744  0.2672  0.1423  630 HOH A O   
2404 O  O   . HOH E .   ? 0.4413 0.4090 0.6118 0.0063  -0.0077 -0.0628 631 HOH A O   
2405 O  O   . HOH E .   ? 0.3783 0.6512 0.7329 0.1811  0.1901  0.1243  632 HOH A O   
2406 O  O   . HOH E .   ? 0.4353 0.4431 0.3078 -0.2134 0.0270  0.0787  633 HOH A O   
2407 O  O   . HOH E .   ? 0.4970 0.5755 0.6632 0.0345  0.2833  -0.1129 634 HOH A O   
2408 O  O   . HOH E .   ? 0.6172 0.6669 0.5687 -0.4150 -0.0418 0.0951  635 HOH A O   
2409 O  O   . HOH E .   ? 0.4307 0.5712 0.3696 0.0168  -0.0023 0.0510  636 HOH A O   
2410 O  O   . HOH E .   ? 0.3182 0.3705 0.4314 0.0482  0.0732  0.0905  637 HOH A O   
2411 O  O   . HOH E .   ? 0.3716 0.2883 0.4507 -0.0420 -0.0750 -0.0427 638 HOH A O   
2412 O  O   . HOH E .   ? 0.3858 0.6839 0.4068 -0.1400 -0.0279 -0.0730 639 HOH A O   
2413 O  O   . HOH E .   ? 0.5507 0.3389 0.7605 0.1073  0.0214  0.0612  640 HOH A O   
2414 O  O   . HOH E .   ? 0.5689 0.3000 0.4526 0.1676  0.2017  0.1263  641 HOH A O   
2415 O  O   . HOH E .   ? 0.4997 0.3834 0.3693 -0.0157 0.0987  0.1368  642 HOH A O   
2416 O  O   . HOH E .   ? 0.5684 0.6518 0.7469 -0.0225 0.0259  0.1494  643 HOH A O   
2417 O  O   . HOH E .   ? 0.3662 0.4628 0.9364 0.1220  0.1877  0.1261  644 HOH A O   
2418 O  O   . HOH E .   ? 0.3486 0.6575 0.3890 0.0696  0.0078  -0.0153 645 HOH A O   
2419 O  O   . HOH E .   ? 0.5862 0.4609 0.4520 -0.0858 0.0272  0.0135  646 HOH A O   
2420 O  O   . HOH E .   ? 0.4667 0.4262 0.4977 -0.0943 -0.1579 0.0359  647 HOH A O   
2421 O  O   . HOH E .   ? 0.3840 0.2997 0.4349 0.1190  -0.1817 -0.0507 648 HOH A O   
2422 O  O   . HOH E .   ? 0.7559 0.4601 0.5572 0.1054  -0.1891 -0.1324 649 HOH A O   
2423 O  O   . HOH E .   ? 0.8056 0.5434 0.7294 0.0002  -0.0723 0.3005  650 HOH A O   
2424 O  O   . HOH E .   ? 0.7501 0.5368 0.2929 0.2414  0.1103  0.0480  651 HOH A O   
2425 O  O   . HOH E .   ? 0.3189 0.6099 0.2636 0.0782  0.0619  0.1100  652 HOH A O   
2426 O  O   . HOH E .   ? 0.2032 0.3634 0.7123 -0.0719 0.1214  -0.0606 653 HOH A O   
2427 O  O   . HOH E .   ? 0.4277 0.3322 0.3091 -0.0842 -0.0480 0.1012  654 HOH A O   
2428 O  O   . HOH E .   ? 0.4528 0.3872 0.5763 -0.0697 -0.0184 0.1342  655 HOH A O   
2429 O  O   . HOH E .   ? 0.7650 0.3422 0.5107 0.1538  -0.0770 -0.0954 656 HOH A O   
2430 O  O   . HOH E .   ? 0.2422 0.3273 0.3965 0.0131  0.0480  0.0624  657 HOH A O   
2431 O  O   . HOH E .   ? 0.3296 0.2615 0.3746 -0.0229 0.0068  0.0411  658 HOH A O   
2432 O  O   . HOH E .   ? 0.6220 0.3426 0.4443 0.0803  0.0250  0.0087  659 HOH A O   
2433 O  O   . HOH E .   ? 0.2920 0.2165 0.3401 -0.0212 0.0452  0.0745  660 HOH A O   
2434 O  O   . HOH E .   ? 0.4648 0.3751 0.6399 -0.0779 0.1231  -0.1359 661 HOH A O   
2435 O  O   . HOH E .   ? 0.2524 0.2064 0.3321 0.0806  -0.0543 0.0173  662 HOH A O   
2436 O  O   . HOH E .   ? 0.2330 0.2002 0.1795 -0.0348 0.0469  -0.0357 663 HOH A O   
2437 O  O   . HOH E .   ? 0.3039 0.4328 0.6210 -0.0136 -0.0432 -0.0774 664 HOH A O   
2438 O  O   . HOH E .   ? 0.4116 0.3486 0.5085 -0.0910 0.1266  -0.0429 665 HOH A O   
2439 O  O   . HOH E .   ? 0.5651 0.2630 0.4154 -0.0691 0.0339  0.0071  666 HOH A O   
2440 O  O   . HOH E .   ? 0.3417 0.3401 0.5718 -0.0432 0.0505  0.0587  667 HOH A O   
2441 O  O   . HOH E .   ? 0.4471 0.6330 0.3126 -0.0019 0.0296  0.0340  668 HOH A O   
2442 O  O   . HOH E .   ? 0.6750 0.5583 0.8575 -0.0539 -0.0013 0.2715  669 HOH A O   
2443 O  O   . HOH E .   ? 0.3435 0.3777 0.5274 0.0925  -0.0963 0.0214  670 HOH A O   
2444 O  O   . HOH E .   ? 0.4683 0.3988 0.4440 -0.0601 0.0276  -0.1324 671 HOH A O   
2445 O  O   . HOH E .   ? 0.5498 0.3244 0.3551 0.1716  0.1789  0.0374  672 HOH A O   
2446 O  O   . HOH E .   ? 0.4223 0.3312 0.5133 0.1190  0.0757  0.0524  673 HOH A O   
2447 O  O   . HOH E .   ? 0.4143 0.2768 0.5256 -0.0484 0.1388  -0.0311 674 HOH A O   
2448 O  O   . HOH E .   ? 0.5640 0.3295 0.3949 0.1286  -0.1445 -0.0612 675 HOH A O   
2449 O  O   . HOH E .   ? 0.5018 0.5743 0.5121 0.2777  -0.0851 -0.0279 676 HOH A O   
2450 O  O   . HOH E .   ? 0.3658 0.5520 0.4194 -0.0261 0.0966  -0.1454 677 HOH A O   
2451 O  O   . HOH E .   ? 0.4653 0.3321 0.2669 0.0889  0.0841  0.0992  678 HOH A O   
2452 O  O   . HOH E .   ? 0.5107 0.2866 0.3302 -0.0579 0.1152  -0.0131 679 HOH A O   
2453 O  O   . HOH E .   ? 0.4761 0.1838 0.2975 0.0127  0.0712  -0.0436 680 HOH A O   
2454 O  O   . HOH E .   ? 0.5830 0.7431 0.5137 -0.2061 0.0142  0.0582  681 HOH A O   
2455 O  O   . HOH E .   ? 0.7421 0.5800 0.3860 0.0952  -0.0634 0.0431  682 HOH A O   
2456 O  O   . HOH E .   ? 0.3753 0.5041 0.4488 -0.0127 -0.0881 -0.0745 683 HOH A O   
2457 O  O   . HOH E .   ? 0.4145 0.3682 0.4066 0.1203  -0.1026 0.0022  684 HOH A O   
2458 O  O   . HOH E .   ? 0.4877 0.3828 0.6350 -0.0342 -0.0322 -0.1337 685 HOH A O   
2459 O  O   . HOH E .   ? 0.5534 0.2266 0.4380 0.0248  0.0589  -0.0176 686 HOH A O   
2460 O  O   . HOH E .   ? 0.3343 0.5090 0.4601 -0.1091 0.0746  0.0057  687 HOH A O   
2461 O  O   . HOH E .   ? 0.3816 0.4773 0.3690 0.0983  0.0841  -0.0078 688 HOH A O   
# 
