data_8ROW
# 
_entry.id   8ROW 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.401 
_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   8ROW         pdb_00008row 10.2210/pdb8row/pdb 
WWPDB D_1292135873 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-01-29 
# 
_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             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8ROW 
_pdbx_database_status.recvd_initial_deposition_date   2024-01-12 
_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           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              marta.ferraroni@unifi.it 
_pdbx_contact_author.name_first         Marta 
_pdbx_contact_author.name_last          Ferraroni 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-7258-738X 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Baroni, C.'    1 ? 
'Ferraroni, M.' 2 ? 
# 
_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                     
;Human Carbonic Anhydrase II in complex with biguanide derivative inhibitor 1-carbamimidamido-N-[(4 sulfamoylphenyl)methyl]methanimidamide, using glycerol as cryoprotectant
;
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Baroni, C.'    1 ? 
primary 'Ferraroni, M.' 2 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Carbonic anhydrase 2'                                   29289.062 1   4.2.1.1 ? ? ? 
2 non-polymer syn 'ZINC ION'                                               65.409    1   ?       ? ? ? 
3 non-polymer syn '1-carbamimidoyl-3-[(4-sulfamoylphenyl)methyl]guanidine' 270.311   2   ?       ? ? ? 
4 non-polymer syn GLYCEROL                                                 92.094    1   ?       ? ? ? 
5 water       nat water                                                    18.015    235 ?       ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Carbonate dehydratase II,Carbonic anhydrase C,CAC,Carbonic anhydrase II,CA-II' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLK
GGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLK
GGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'ZINC ION'                                               ZN    
3 '1-carbamimidoyl-3-[(4-sulfamoylphenyl)methyl]guanidine' A1H15 
4 GLYCEROL                                                 GOL   
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  ASN n 
1 63  GLY n 
1 64  HIS n 
1 65  ALA n 
1 66  PHE n 
1 67  ASN n 
1 68  VAL n 
1 69  GLU n 
1 70  PHE n 
1 71  ASP n 
1 72  ASP n 
1 73  SER n 
1 74  GLN n 
1 75  ASP n 
1 76  LYS n 
1 77  ALA n 
1 78  VAL n 
1 79  LEU n 
1 80  LYS n 
1 81  GLY n 
1 82  GLY n 
1 83  PRO n 
1 84  LEU n 
1 85  ASP n 
1 86  GLY n 
1 87  THR n 
1 88  TYR n 
1 89  ARG n 
1 90  LEU n 
1 91  ILE n 
1 92  GLN n 
1 93  PHE n 
1 94  HIS n 
1 95  PHE n 
1 96  HIS n 
1 97  TRP n 
1 98  GLY n 
1 99  SER n 
1 100 LEU n 
1 101 ASP n 
1 102 GLY n 
1 103 GLN n 
1 104 GLY n 
1 105 SER n 
1 106 GLU n 
1 107 HIS n 
1 108 THR n 
1 109 VAL n 
1 110 ASP n 
1 111 LYS n 
1 112 LYS n 
1 113 LYS n 
1 114 TYR n 
1 115 ALA n 
1 116 ALA n 
1 117 GLU n 
1 118 LEU n 
1 119 HIS n 
1 120 LEU n 
1 121 VAL n 
1 122 HIS n 
1 123 TRP n 
1 124 ASN n 
1 125 THR n 
1 126 LYS n 
1 127 TYR n 
1 128 GLY n 
1 129 ASP n 
1 130 PHE n 
1 131 GLY n 
1 132 LYS n 
1 133 ALA n 
1 134 VAL n 
1 135 GLN n 
1 136 GLN n 
1 137 PRO n 
1 138 ASP n 
1 139 GLY n 
1 140 LEU n 
1 141 ALA n 
1 142 VAL n 
1 143 LEU n 
1 144 GLY n 
1 145 ILE n 
1 146 PHE n 
1 147 LEU n 
1 148 LYS n 
1 149 VAL n 
1 150 GLY n 
1 151 SER n 
1 152 ALA n 
1 153 LYS n 
1 154 PRO n 
1 155 GLY n 
1 156 LEU n 
1 157 GLN n 
1 158 LYS n 
1 159 VAL n 
1 160 VAL n 
1 161 ASP n 
1 162 VAL n 
1 163 LEU n 
1 164 ASP n 
1 165 SER n 
1 166 ILE n 
1 167 LYS n 
1 168 THR n 
1 169 LYS n 
1 170 GLY n 
1 171 LYS n 
1 172 SER n 
1 173 ALA n 
1 174 ASP n 
1 175 PHE n 
1 176 THR n 
1 177 ASN n 
1 178 PHE n 
1 179 ASP n 
1 180 PRO n 
1 181 ARG n 
1 182 GLY n 
1 183 LEU n 
1 184 LEU n 
1 185 PRO n 
1 186 GLU n 
1 187 SER n 
1 188 LEU n 
1 189 ASP n 
1 190 TYR n 
1 191 TRP n 
1 192 THR n 
1 193 TYR n 
1 194 PRO n 
1 195 GLY n 
1 196 SER n 
1 197 LEU n 
1 198 THR n 
1 199 THR n 
1 200 PRO n 
1 201 PRO n 
1 202 LEU n 
1 203 LEU n 
1 204 GLU n 
1 205 CYS n 
1 206 VAL n 
1 207 THR n 
1 208 TRP n 
1 209 ILE n 
1 210 VAL n 
1 211 LEU n 
1 212 LYS n 
1 213 GLU n 
1 214 PRO n 
1 215 ILE n 
1 216 SER n 
1 217 VAL n 
1 218 SER n 
1 219 SER n 
1 220 GLU n 
1 221 GLN n 
1 222 VAL n 
1 223 LEU n 
1 224 LYS n 
1 225 PHE n 
1 226 ARG n 
1 227 LYS n 
1 228 LEU n 
1 229 ASN n 
1 230 PHE n 
1 231 ASN n 
1 232 GLY n 
1 233 GLU n 
1 234 GLY n 
1 235 GLU n 
1 236 PRO n 
1 237 GLU n 
1 238 GLU n 
1 239 LEU n 
1 240 MET n 
1 241 VAL n 
1 242 ASP n 
1 243 ASN n 
1 244 TRP n 
1 245 ARG n 
1 246 PRO n 
1 247 ALA n 
1 248 GLN n 
1 249 PRO n 
1 250 LEU n 
1 251 LYS n 
1 252 ASN n 
1 253 ARG n 
1 254 GLN n 
1 255 ILE n 
1 256 LYS n 
1 257 ALA n 
1 258 SER n 
1 259 PHE n 
1 260 LYS n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   260 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 CA2 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1H15 non-polymer         . '1-carbamimidoyl-3-[(4-sulfamoylphenyl)methyl]guanidine' ?                               
'C9 H14 N6 O2 S' 270.311 
ALA   'L-peptide linking' y ALANINE                                                  ?                               'C3 H7 N O2' 
89.093  
ARG   'L-peptide linking' y ARGININE                                                 ?                               
'C6 H15 N4 O2 1' 175.209 
ASN   'L-peptide linking' y ASPARAGINE                                               ?                               'C4 H8 N2 O3' 
132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                          ?                               'C4 H7 N O4' 
133.103 
CYS   'L-peptide linking' y CYSTEINE                                                 ?                               
'C3 H7 N O2 S'   121.158 
GLN   'L-peptide linking' y GLUTAMINE                                                ?                               
'C5 H10 N2 O3'   146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                          ?                               'C5 H9 N O4' 
147.129 
GLY   'peptide linking'   y GLYCINE                                                  ?                               'C2 H5 N O2' 
75.067  
GOL   non-polymer         . GLYCEROL                                                 'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3' 
92.094  
HIS   'L-peptide linking' y HISTIDINE                                                ?                               
'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer         . WATER                                                    ?                               'H2 O' 18.015 
ILE   'L-peptide linking' y ISOLEUCINE                                               ?                               'C6 H13 N O2' 
131.173 
LEU   'L-peptide linking' y LEUCINE                                                  ?                               'C6 H13 N O2' 
131.173 
LYS   'L-peptide linking' y LYSINE                                                   ?                               
'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking' y METHIONINE                                               ?                               
'C5 H11 N O2 S'  149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                            ?                               'C9 H11 N O2' 
165.189 
PRO   'L-peptide linking' y PROLINE                                                  ?                               'C5 H9 N O2' 
115.130 
SER   'L-peptide linking' y SERINE                                                   ?                               'C3 H7 N O3' 
105.093 
THR   'L-peptide linking' y THREONINE                                                ?                               'C4 H9 N O3' 
119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                               ?                               
'C11 H12 N2 O2'  204.225 
TYR   'L-peptide linking' y TYROSINE                                                 ?                               'C9 H11 N O3' 
181.189 
VAL   'L-peptide linking' y VALINE                                                   ?                               'C5 H11 N O2' 
117.146 
ZN    non-polymer         . 'ZINC ION'                                               ?                               'Zn 2' 65.409 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   SER 2   2   ?   ?   ?   A . n 
A 1 3   HIS 3   3   ?   ?   ?   A . n 
A 1 4   HIS 4   4   4   HIS HIS A . n 
A 1 5   TRP 5   5   5   TRP TRP A . n 
A 1 6   GLY 6   6   6   GLY GLY A . n 
A 1 7   TYR 7   7   7   TYR TYR A . n 
A 1 8   GLY 8   8   8   GLY GLY A . n 
A 1 9   LYS 9   9   9   LYS LYS A . n 
A 1 10  HIS 10  10  10  HIS HIS A . n 
A 1 11  ASN 11  11  11  ASN ASN A . n 
A 1 12  GLY 12  12  12  GLY GLY A . n 
A 1 13  PRO 13  13  13  PRO PRO A . n 
A 1 14  GLU 14  14  14  GLU GLU A . n 
A 1 15  HIS 15  15  15  HIS HIS A . n 
A 1 16  TRP 16  16  16  TRP TRP A . n 
A 1 17  HIS 17  17  17  HIS HIS A . n 
A 1 18  LYS 18  18  18  LYS LYS A . n 
A 1 19  ASP 19  19  19  ASP ASP A . n 
A 1 20  PHE 20  20  20  PHE PHE A . n 
A 1 21  PRO 21  21  21  PRO PRO A . n 
A 1 22  ILE 22  22  22  ILE ILE A . n 
A 1 23  ALA 23  23  23  ALA ALA A . n 
A 1 24  LYS 24  24  24  LYS LYS A . n 
A 1 25  GLY 25  25  25  GLY GLY A . n 
A 1 26  GLU 26  26  26  GLU GLU A . n 
A 1 27  ARG 27  27  27  ARG ARG A . n 
A 1 28  GLN 28  28  28  GLN GLN A . n 
A 1 29  SER 29  29  29  SER SER A . n 
A 1 30  PRO 30  30  30  PRO PRO A . n 
A 1 31  VAL 31  31  31  VAL VAL A . n 
A 1 32  ASP 32  32  32  ASP ASP A . n 
A 1 33  ILE 33  33  33  ILE ILE A . n 
A 1 34  ASP 34  34  34  ASP ASP A . n 
A 1 35  THR 35  35  35  THR THR A . n 
A 1 36  HIS 36  36  36  HIS HIS A . n 
A 1 37  THR 37  37  37  THR THR A . n 
A 1 38  ALA 38  38  38  ALA ALA A . n 
A 1 39  LYS 39  39  39  LYS LYS A . n 
A 1 40  TYR 40  40  40  TYR TYR A . n 
A 1 41  ASP 41  41  41  ASP ASP A . n 
A 1 42  PRO 42  42  42  PRO PRO A . n 
A 1 43  SER 43  43  43  SER SER A . n 
A 1 44  LEU 44  44  44  LEU LEU A . n 
A 1 45  LYS 45  45  45  LYS LYS A . n 
A 1 46  PRO 46  46  46  PRO PRO A . n 
A 1 47  LEU 47  47  47  LEU LEU A . n 
A 1 48  SER 48  48  48  SER SER A . n 
A 1 49  VAL 49  49  49  VAL VAL A . n 
A 1 50  SER 50  50  50  SER SER A . n 
A 1 51  TYR 51  51  51  TYR TYR A . n 
A 1 52  ASP 52  52  52  ASP ASP A . n 
A 1 53  GLN 53  53  53  GLN GLN A . n 
A 1 54  ALA 54  54  54  ALA ALA A . n 
A 1 55  THR 55  55  55  THR THR A . n 
A 1 56  SER 56  56  56  SER SER A . n 
A 1 57  LEU 57  57  57  LEU LEU A . n 
A 1 58  ARG 58  58  58  ARG ARG A . n 
A 1 59  ILE 59  59  59  ILE ILE A . n 
A 1 60  LEU 60  60  60  LEU LEU A . n 
A 1 61  ASN 61  61  61  ASN ASN A . n 
A 1 62  ASN 62  62  62  ASN ASN A . n 
A 1 63  GLY 63  63  63  GLY GLY A . n 
A 1 64  HIS 64  64  64  HIS HIS A . n 
A 1 65  ALA 65  65  65  ALA ALA A . n 
A 1 66  PHE 66  66  66  PHE PHE A . n 
A 1 67  ASN 67  67  67  ASN ASN A . n 
A 1 68  VAL 68  68  68  VAL VAL A . n 
A 1 69  GLU 69  69  69  GLU GLU A . n 
A 1 70  PHE 70  70  70  PHE PHE A . n 
A 1 71  ASP 71  71  71  ASP ASP A . n 
A 1 72  ASP 72  72  72  ASP ASP A . n 
A 1 73  SER 73  73  73  SER SER A . n 
A 1 74  GLN 74  74  74  GLN GLN A . n 
A 1 75  ASP 75  75  75  ASP ASP A . n 
A 1 76  LYS 76  76  76  LYS LYS A . n 
A 1 77  ALA 77  77  77  ALA ALA A . n 
A 1 78  VAL 78  78  78  VAL VAL A . n 
A 1 79  LEU 79  79  79  LEU LEU A . n 
A 1 80  LYS 80  80  80  LYS LYS A . n 
A 1 81  GLY 81  81  81  GLY GLY A . n 
A 1 82  GLY 82  82  82  GLY GLY A . n 
A 1 83  PRO 83  83  83  PRO PRO A . n 
A 1 84  LEU 84  84  84  LEU LEU A . n 
A 1 85  ASP 85  85  85  ASP ASP A . n 
A 1 86  GLY 86  86  86  GLY GLY A . n 
A 1 87  THR 87  87  87  THR THR A . n 
A 1 88  TYR 88  88  88  TYR TYR A . n 
A 1 89  ARG 89  89  89  ARG ARG A . n 
A 1 90  LEU 90  90  90  LEU LEU A . n 
A 1 91  ILE 91  91  91  ILE ILE A . n 
A 1 92  GLN 92  92  92  GLN GLN A . n 
A 1 93  PHE 93  93  93  PHE PHE A . n 
A 1 94  HIS 94  94  94  HIS HIS A . n 
A 1 95  PHE 95  95  95  PHE PHE A . n 
A 1 96  HIS 96  96  96  HIS HIS A . n 
A 1 97  TRP 97  97  97  TRP TRP A . n 
A 1 98  GLY 98  98  98  GLY GLY A . n 
A 1 99  SER 99  99  99  SER SER A . n 
A 1 100 LEU 100 100 100 LEU LEU A . n 
A 1 101 ASP 101 101 101 ASP ASP A . n 
A 1 102 GLY 102 102 102 GLY GLY A . n 
A 1 103 GLN 103 103 103 GLN GLN A . n 
A 1 104 GLY 104 104 104 GLY GLY A . n 
A 1 105 SER 105 105 105 SER SER A . n 
A 1 106 GLU 106 106 106 GLU GLU A . n 
A 1 107 HIS 107 107 107 HIS HIS A . n 
A 1 108 THR 108 108 108 THR THR A . n 
A 1 109 VAL 109 109 109 VAL VAL A . n 
A 1 110 ASP 110 110 110 ASP ASP A . n 
A 1 111 LYS 111 111 111 LYS LYS A . n 
A 1 112 LYS 112 112 112 LYS LYS A . n 
A 1 113 LYS 113 113 113 LYS LYS A . n 
A 1 114 TYR 114 114 114 TYR TYR A . n 
A 1 115 ALA 115 115 115 ALA ALA A . n 
A 1 116 ALA 116 116 116 ALA ALA A . n 
A 1 117 GLU 117 117 117 GLU GLU A . n 
A 1 118 LEU 118 118 118 LEU LEU A . n 
A 1 119 HIS 119 119 119 HIS HIS A . n 
A 1 120 LEU 120 120 120 LEU LEU A . n 
A 1 121 VAL 121 121 121 VAL VAL A . n 
A 1 122 HIS 122 122 122 HIS HIS A . n 
A 1 123 TRP 123 123 123 TRP TRP A . n 
A 1 124 ASN 124 124 124 ASN ASN A . n 
A 1 125 THR 125 125 125 THR THR A . n 
A 1 126 LYS 126 127 127 LYS LYS A . n 
A 1 127 TYR 127 128 128 TYR TYR A . n 
A 1 128 GLY 128 129 129 GLY GLY A . n 
A 1 129 ASP 129 130 130 ASP ASP A . n 
A 1 130 PHE 130 131 131 PHE PHE A . n 
A 1 131 GLY 131 132 132 GLY GLY A . n 
A 1 132 LYS 132 133 133 LYS LYS A . n 
A 1 133 ALA 133 134 134 ALA ALA A . n 
A 1 134 VAL 134 135 135 VAL VAL A . n 
A 1 135 GLN 135 136 136 GLN GLN A . n 
A 1 136 GLN 136 137 137 GLN GLN A . n 
A 1 137 PRO 137 138 138 PRO PRO A . n 
A 1 138 ASP 138 139 139 ASP ASP A . n 
A 1 139 GLY 139 140 140 GLY GLY A . n 
A 1 140 LEU 140 141 141 LEU LEU A . n 
A 1 141 ALA 141 142 142 ALA ALA A . n 
A 1 142 VAL 142 143 143 VAL VAL A . n 
A 1 143 LEU 143 144 144 LEU LEU A . n 
A 1 144 GLY 144 145 145 GLY GLY A . n 
A 1 145 ILE 145 146 146 ILE ILE A . n 
A 1 146 PHE 146 147 147 PHE PHE A . n 
A 1 147 LEU 147 148 148 LEU LEU A . n 
A 1 148 LYS 148 149 149 LYS LYS A . n 
A 1 149 VAL 149 150 150 VAL VAL A . n 
A 1 150 GLY 150 151 151 GLY GLY A . n 
A 1 151 SER 151 152 152 SER SER A . n 
A 1 152 ALA 152 153 153 ALA ALA A . n 
A 1 153 LYS 153 154 154 LYS LYS A . n 
A 1 154 PRO 154 155 155 PRO PRO A . n 
A 1 155 GLY 155 156 156 GLY GLY A . n 
A 1 156 LEU 156 157 157 LEU LEU A . n 
A 1 157 GLN 157 158 158 GLN GLN A . n 
A 1 158 LYS 158 159 159 LYS LYS A . n 
A 1 159 VAL 159 160 160 VAL VAL A . n 
A 1 160 VAL 160 161 161 VAL VAL A . n 
A 1 161 ASP 161 162 162 ASP ASP A . n 
A 1 162 VAL 162 163 163 VAL VAL A . n 
A 1 163 LEU 163 164 164 LEU LEU A . n 
A 1 164 ASP 164 165 165 ASP ASP A . n 
A 1 165 SER 165 166 166 SER SER A . n 
A 1 166 ILE 166 167 167 ILE ILE A . n 
A 1 167 LYS 167 168 168 LYS LYS A . n 
A 1 168 THR 168 169 169 THR THR A . n 
A 1 169 LYS 169 170 170 LYS LYS A . n 
A 1 170 GLY 170 171 171 GLY GLY A . n 
A 1 171 LYS 171 172 172 LYS LYS A . n 
A 1 172 SER 172 173 173 SER SER A . n 
A 1 173 ALA 173 174 174 ALA ALA A . n 
A 1 174 ASP 174 175 175 ASP ASP A . n 
A 1 175 PHE 175 176 176 PHE PHE A . n 
A 1 176 THR 176 177 177 THR THR A . n 
A 1 177 ASN 177 178 178 ASN ASN A . n 
A 1 178 PHE 178 179 179 PHE PHE A . n 
A 1 179 ASP 179 180 180 ASP ASP A . n 
A 1 180 PRO 180 181 181 PRO PRO A . n 
A 1 181 ARG 181 182 182 ARG ARG A . n 
A 1 182 GLY 182 183 183 GLY GLY A . n 
A 1 183 LEU 183 184 184 LEU LEU A . n 
A 1 184 LEU 184 185 185 LEU LEU A . n 
A 1 185 PRO 185 186 186 PRO PRO A . n 
A 1 186 GLU 186 187 187 GLU GLU A . n 
A 1 187 SER 187 188 188 SER SER A . n 
A 1 188 LEU 188 189 189 LEU LEU A . n 
A 1 189 ASP 189 190 190 ASP ASP A . n 
A 1 190 TYR 190 191 191 TYR TYR A . n 
A 1 191 TRP 191 192 192 TRP TRP A . n 
A 1 192 THR 192 193 193 THR THR A . n 
A 1 193 TYR 193 194 194 TYR TYR A . n 
A 1 194 PRO 194 195 195 PRO PRO A . n 
A 1 195 GLY 195 196 196 GLY GLY A . n 
A 1 196 SER 196 197 197 SER SER A . n 
A 1 197 LEU 197 198 198 LEU LEU A . n 
A 1 198 THR 198 199 199 THR THR A . n 
A 1 199 THR 199 200 200 THR THR A . n 
A 1 200 PRO 200 201 201 PRO PRO A . n 
A 1 201 PRO 201 202 202 PRO PRO A . n 
A 1 202 LEU 202 203 203 LEU LEU A . n 
A 1 203 LEU 203 204 204 LEU LEU A . n 
A 1 204 GLU 204 205 205 GLU GLU A . n 
A 1 205 CYS 205 206 206 CYS CYS A . n 
A 1 206 VAL 206 207 207 VAL VAL A . n 
A 1 207 THR 207 208 208 THR THR A . n 
A 1 208 TRP 208 209 209 TRP TRP A . n 
A 1 209 ILE 209 210 210 ILE ILE A . n 
A 1 210 VAL 210 211 211 VAL VAL A . n 
A 1 211 LEU 211 212 212 LEU LEU A . n 
A 1 212 LYS 212 213 213 LYS LYS A . n 
A 1 213 GLU 213 214 214 GLU GLU A . n 
A 1 214 PRO 214 215 215 PRO PRO A . n 
A 1 215 ILE 215 216 216 ILE ILE A . n 
A 1 216 SER 216 217 217 SER SER A . n 
A 1 217 VAL 217 218 218 VAL VAL A . n 
A 1 218 SER 218 219 219 SER SER A . n 
A 1 219 SER 219 220 220 SER SER A . n 
A 1 220 GLU 220 221 221 GLU GLU A . n 
A 1 221 GLN 221 222 222 GLN GLN A . n 
A 1 222 VAL 222 223 223 VAL VAL A . n 
A 1 223 LEU 223 224 224 LEU LEU A . n 
A 1 224 LYS 224 225 225 LYS LYS A . n 
A 1 225 PHE 225 226 226 PHE PHE A . n 
A 1 226 ARG 226 227 227 ARG ARG A . n 
A 1 227 LYS 227 228 228 LYS LYS A . n 
A 1 228 LEU 228 229 229 LEU LEU A . n 
A 1 229 ASN 229 230 230 ASN ASN A . n 
A 1 230 PHE 230 231 231 PHE PHE A . n 
A 1 231 ASN 231 232 232 ASN ASN A . n 
A 1 232 GLY 232 233 233 GLY GLY A . n 
A 1 233 GLU 233 234 234 GLU GLU A . n 
A 1 234 GLY 234 235 235 GLY GLY A . n 
A 1 235 GLU 235 236 236 GLU GLU A . n 
A 1 236 PRO 236 237 237 PRO PRO A . n 
A 1 237 GLU 237 238 238 GLU GLU A . n 
A 1 238 GLU 238 239 239 GLU GLU A . n 
A 1 239 LEU 239 240 240 LEU LEU A . n 
A 1 240 MET 240 241 241 MET MET A . n 
A 1 241 VAL 241 242 242 VAL VAL A . n 
A 1 242 ASP 242 243 243 ASP ASP A . n 
A 1 243 ASN 243 244 244 ASN ASN A . n 
A 1 244 TRP 244 245 245 TRP TRP A . n 
A 1 245 ARG 245 246 246 ARG ARG A . n 
A 1 246 PRO 246 247 247 PRO PRO A . n 
A 1 247 ALA 247 248 248 ALA ALA A . n 
A 1 248 GLN 248 249 249 GLN GLN A . n 
A 1 249 PRO 249 250 250 PRO PRO A . n 
A 1 250 LEU 250 251 251 LEU LEU A . n 
A 1 251 LYS 251 252 252 LYS LYS A . n 
A 1 252 ASN 252 253 253 ASN ASN A . n 
A 1 253 ARG 253 254 254 ARG ARG A . n 
A 1 254 GLN 254 255 255 GLN GLN A . n 
A 1 255 ILE 255 256 256 ILE ILE A . n 
A 1 256 LYS 256 257 257 LYS LYS A . n 
A 1 257 ALA 257 258 258 ALA ALA A . n 
A 1 258 SER 258 259 259 SER SER A . n 
A 1 259 PHE 259 260 260 PHE PHE A . n 
A 1 260 LYS 260 261 261 LYS LYS A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1H15 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1H15 
_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        ? 
# 
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   301 301 ZN    ZN  A . 
C 3 A1H15 1   302 302 A1H15 GGG A . 
D 3 A1H15 1   303 401 A1H15 GGG A . 
E 4 GOL   1   304 402 GOL   GOL A . 
F 5 HOH   1   401 72  HOH   HOH A . 
F 5 HOH   2   402 69  HOH   HOH A . 
F 5 HOH   3   403 70  HOH   HOH A . 
F 5 HOH   4   404 55  HOH   HOH A . 
F 5 HOH   5   405 73  HOH   HOH A . 
F 5 HOH   6   406 86  HOH   HOH A . 
F 5 HOH   7   407 88  HOH   HOH A . 
F 5 HOH   8   408 71  HOH   HOH A . 
F 5 HOH   9   409 103 HOH   HOH A . 
F 5 HOH   10  410 10  HOH   HOH A . 
F 5 HOH   11  411 17  HOH   HOH A . 
F 5 HOH   12  412 126 HOH   HOH A . 
F 5 HOH   13  413 117 HOH   HOH A . 
F 5 HOH   14  414 105 HOH   HOH A . 
F 5 HOH   15  415 89  HOH   HOH A . 
F 5 HOH   16  416 45  HOH   HOH A . 
F 5 HOH   17  417 82  HOH   HOH A . 
F 5 HOH   18  418 1   HOH   HOH A . 
F 5 HOH   19  419 75  HOH   HOH A . 
F 5 HOH   20  420 87  HOH   HOH A . 
F 5 HOH   21  421 96  HOH   HOH A . 
F 5 HOH   22  422 152 HOH   HOH A . 
F 5 HOH   23  423 99  HOH   HOH A . 
F 5 HOH   24  424 105 HOH   HOH A . 
F 5 HOH   25  425 125 HOH   HOH A . 
F 5 HOH   26  426 91  HOH   HOH A . 
F 5 HOH   27  427 79  HOH   HOH A . 
F 5 HOH   28  428 106 HOH   HOH A . 
F 5 HOH   29  429 4   HOH   HOH A . 
F 5 HOH   30  430 5   HOH   HOH A . 
F 5 HOH   31  431 107 HOH   HOH A . 
F 5 HOH   32  432 103 HOH   HOH A . 
F 5 HOH   33  433 24  HOH   HOH A . 
F 5 HOH   34  434 110 HOH   HOH A . 
F 5 HOH   35  435 94  HOH   HOH A . 
F 5 HOH   36  436 35  HOH   HOH A . 
F 5 HOH   37  437 24  HOH   HOH A . 
F 5 HOH   38  438 95  HOH   HOH A . 
F 5 HOH   39  439 15  HOH   HOH A . 
F 5 HOH   40  440 79  HOH   HOH A . 
F 5 HOH   41  441 78  HOH   HOH A . 
F 5 HOH   42  442 38  HOH   HOH A . 
F 5 HOH   43  443 1   HOH   HOH A . 
F 5 HOH   44  444 144 HOH   HOH A . 
F 5 HOH   45  445 72  HOH   HOH A . 
F 5 HOH   46  446 11  HOH   HOH A . 
F 5 HOH   47  447 2   HOH   HOH A . 
F 5 HOH   48  448 27  HOH   HOH A . 
F 5 HOH   49  449 69  HOH   HOH A . 
F 5 HOH   50  450 31  HOH   HOH A . 
F 5 HOH   51  451 1   HOH   HOH A . 
F 5 HOH   52  452 13  HOH   HOH A . 
F 5 HOH   53  453 65  HOH   HOH A . 
F 5 HOH   54  454 81  HOH   HOH A . 
F 5 HOH   55  455 37  HOH   HOH A . 
F 5 HOH   56  456 16  HOH   HOH A . 
F 5 HOH   57  457 36  HOH   HOH A . 
F 5 HOH   58  458 4   HOH   HOH A . 
F 5 HOH   59  459 34  HOH   HOH A . 
F 5 HOH   60  460 22  HOH   HOH A . 
F 5 HOH   61  461 150 HOH   HOH A . 
F 5 HOH   62  462 33  HOH   HOH A . 
F 5 HOH   63  463 183 HOH   HOH A . 
F 5 HOH   64  464 6   HOH   HOH A . 
F 5 HOH   65  465 40  HOH   HOH A . 
F 5 HOH   66  466 30  HOH   HOH A . 
F 5 HOH   67  467 23  HOH   HOH A . 
F 5 HOH   68  468 123 HOH   HOH A . 
F 5 HOH   69  469 25  HOH   HOH A . 
F 5 HOH   70  470 7   HOH   HOH A . 
F 5 HOH   71  471 8   HOH   HOH A . 
F 5 HOH   72  472 120 HOH   HOH A . 
F 5 HOH   73  473 106 HOH   HOH A . 
F 5 HOH   74  474 62  HOH   HOH A . 
F 5 HOH   75  475 139 HOH   HOH A . 
F 5 HOH   76  476 109 HOH   HOH A . 
F 5 HOH   77  477 132 HOH   HOH A . 
F 5 HOH   78  478 15  HOH   HOH A . 
F 5 HOH   79  479 111 HOH   HOH A . 
F 5 HOH   80  480 46  HOH   HOH A . 
F 5 HOH   81  481 126 HOH   HOH A . 
F 5 HOH   82  482 16  HOH   HOH A . 
F 5 HOH   83  483 56  HOH   HOH A . 
F 5 HOH   84  484 93  HOH   HOH A . 
F 5 HOH   85  485 148 HOH   HOH A . 
F 5 HOH   86  486 174 HOH   HOH A . 
F 5 HOH   87  487 146 HOH   HOH A . 
F 5 HOH   88  488 50  HOH   HOH A . 
F 5 HOH   89  489 3   HOH   HOH A . 
F 5 HOH   90  490 88  HOH   HOH A . 
F 5 HOH   91  491 6   HOH   HOH A . 
F 5 HOH   92  492 2   HOH   HOH A . 
F 5 HOH   93  493 90  HOH   HOH A . 
F 5 HOH   94  494 48  HOH   HOH A . 
F 5 HOH   95  495 3   HOH   HOH A . 
F 5 HOH   96  496 114 HOH   HOH A . 
F 5 HOH   97  497 225 HOH   HOH A . 
F 5 HOH   98  498 20  HOH   HOH A . 
F 5 HOH   99  499 5   HOH   HOH A . 
F 5 HOH   100 500 92  HOH   HOH A . 
F 5 HOH   101 501 12  HOH   HOH A . 
F 5 HOH   102 502 27  HOH   HOH A . 
F 5 HOH   103 503 10  HOH   HOH A . 
F 5 HOH   104 504 9   HOH   HOH A . 
F 5 HOH   105 505 48  HOH   HOH A . 
F 5 HOH   106 506 127 HOH   HOH A . 
F 5 HOH   107 507 21  HOH   HOH A . 
F 5 HOH   108 508 59  HOH   HOH A . 
F 5 HOH   109 509 9   HOH   HOH A . 
F 5 HOH   110 510 26  HOH   HOH A . 
F 5 HOH   111 511 43  HOH   HOH A . 
F 5 HOH   112 512 43  HOH   HOH A . 
F 5 HOH   113 513 44  HOH   HOH A . 
F 5 HOH   114 514 100 HOH   HOH A . 
F 5 HOH   115 515 42  HOH   HOH A . 
F 5 HOH   116 516 159 HOH   HOH A . 
F 5 HOH   117 517 39  HOH   HOH A . 
F 5 HOH   118 518 80  HOH   HOH A . 
F 5 HOH   119 519 102 HOH   HOH A . 
F 5 HOH   120 520 67  HOH   HOH A . 
F 5 HOH   121 521 17  HOH   HOH A . 
F 5 HOH   122 522 110 HOH   HOH A . 
F 5 HOH   123 523 112 HOH   HOH A . 
F 5 HOH   124 524 1   HOH   HOH A . 
F 5 HOH   125 525 62  HOH   HOH A . 
F 5 HOH   126 526 31  HOH   HOH A . 
F 5 HOH   127 527 116 HOH   HOH A . 
F 5 HOH   128 528 231 HOH   HOH A . 
F 5 HOH   129 529 87  HOH   HOH A . 
F 5 HOH   130 530 124 HOH   HOH A . 
F 5 HOH   131 531 13  HOH   HOH A . 
F 5 HOH   132 532 60  HOH   HOH A . 
F 5 HOH   133 533 54  HOH   HOH A . 
F 5 HOH   134 534 5   HOH   HOH A . 
F 5 HOH   135 535 18  HOH   HOH A . 
F 5 HOH   136 536 73  HOH   HOH A . 
F 5 HOH   137 537 151 HOH   HOH A . 
F 5 HOH   138 538 43  HOH   HOH A . 
F 5 HOH   139 539 84  HOH   HOH A . 
F 5 HOH   140 540 30  HOH   HOH A . 
F 5 HOH   141 541 78  HOH   HOH A . 
F 5 HOH   142 542 113 HOH   HOH A . 
F 5 HOH   143 543 40  HOH   HOH A . 
F 5 HOH   144 544 14  HOH   HOH A . 
F 5 HOH   145 545 29  HOH   HOH A . 
F 5 HOH   146 546 76  HOH   HOH A . 
F 5 HOH   147 547 128 HOH   HOH A . 
F 5 HOH   148 548 90  HOH   HOH A . 
F 5 HOH   149 549 35  HOH   HOH A . 
F 5 HOH   150 550 130 HOH   HOH A . 
F 5 HOH   151 551 119 HOH   HOH A . 
F 5 HOH   152 552 129 HOH   HOH A . 
F 5 HOH   153 553 10  HOH   HOH A . 
F 5 HOH   154 554 54  HOH   HOH A . 
F 5 HOH   155 555 137 HOH   HOH A . 
F 5 HOH   156 556 23  HOH   HOH A . 
F 5 HOH   157 557 48  HOH   HOH A . 
F 5 HOH   158 558 28  HOH   HOH A . 
F 5 HOH   159 559 25  HOH   HOH A . 
F 5 HOH   160 560 2   HOH   HOH A . 
F 5 HOH   161 561 19  HOH   HOH A . 
F 5 HOH   162 562 82  HOH   HOH A . 
F 5 HOH   163 563 52  HOH   HOH A . 
F 5 HOH   164 564 123 HOH   HOH A . 
F 5 HOH   165 565 61  HOH   HOH A . 
F 5 HOH   166 566 18  HOH   HOH A . 
F 5 HOH   167 567 17  HOH   HOH A . 
F 5 HOH   168 568 14  HOH   HOH A . 
F 5 HOH   169 569 38  HOH   HOH A . 
F 5 HOH   170 570 28  HOH   HOH A . 
F 5 HOH   171 571 18  HOH   HOH A . 
F 5 HOH   172 572 26  HOH   HOH A . 
F 5 HOH   173 573 65  HOH   HOH A . 
F 5 HOH   174 574 109 HOH   HOH A . 
F 5 HOH   175 575 51  HOH   HOH A . 
F 5 HOH   176 576 116 HOH   HOH A . 
F 5 HOH   177 577 98  HOH   HOH A . 
F 5 HOH   178 578 53  HOH   HOH A . 
F 5 HOH   179 579 20  HOH   HOH A . 
F 5 HOH   180 580 4   HOH   HOH A . 
F 5 HOH   181 581 101 HOH   HOH A . 
F 5 HOH   182 582 59  HOH   HOH A . 
F 5 HOH   183 583 7   HOH   HOH A . 
F 5 HOH   184 584 112 HOH   HOH A . 
F 5 HOH   185 585 135 HOH   HOH A . 
F 5 HOH   186 586 338 HOH   HOH A . 
F 5 HOH   187 587 76  HOH   HOH A . 
F 5 HOH   188 588 81  HOH   HOH A . 
F 5 HOH   189 589 218 HOH   HOH A . 
F 5 HOH   190 590 86  HOH   HOH A . 
F 5 HOH   191 591 235 HOH   HOH A . 
F 5 HOH   192 592 212 HOH   HOH A . 
F 5 HOH   193 593 331 HOH   HOH A . 
F 5 HOH   194 594 334 HOH   HOH A . 
F 5 HOH   195 595 120 HOH   HOH A . 
F 5 HOH   196 596 52  HOH   HOH A . 
F 5 HOH   197 597 226 HOH   HOH A . 
F 5 HOH   198 598 70  HOH   HOH A . 
F 5 HOH   199 599 52  HOH   HOH A . 
F 5 HOH   200 600 100 HOH   HOH A . 
F 5 HOH   201 601 127 HOH   HOH A . 
F 5 HOH   202 602 351 HOH   HOH A . 
F 5 HOH   203 603 102 HOH   HOH A . 
F 5 HOH   204 604 96  HOH   HOH A . 
F 5 HOH   205 605 238 HOH   HOH A . 
F 5 HOH   206 606 121 HOH   HOH A . 
F 5 HOH   207 607 121 HOH   HOH A . 
F 5 HOH   208 608 79  HOH   HOH A . 
F 5 HOH   209 609 49  HOH   HOH A . 
F 5 HOH   210 610 114 HOH   HOH A . 
F 5 HOH   211 611 335 HOH   HOH A . 
F 5 HOH   212 612 92  HOH   HOH A . 
F 5 HOH   213 613 85  HOH   HOH A . 
F 5 HOH   214 614 343 HOH   HOH A . 
F 5 HOH   215 615 147 HOH   HOH A . 
F 5 HOH   216 616 64  HOH   HOH A . 
F 5 HOH   217 617 330 HOH   HOH A . 
F 5 HOH   218 618 37  HOH   HOH A . 
F 5 HOH   219 619 142 HOH   HOH A . 
F 5 HOH   220 620 115 HOH   HOH A . 
F 5 HOH   221 621 168 HOH   HOH A . 
F 5 HOH   222 622 344 HOH   HOH A . 
F 5 HOH   223 623 230 HOH   HOH A . 
F 5 HOH   224 624 122 HOH   HOH A . 
F 5 HOH   225 625 192 HOH   HOH A . 
F 5 HOH   226 626 243 HOH   HOH A . 
F 5 HOH   227 627 83  HOH   HOH A . 
F 5 HOH   228 628 197 HOH   HOH A . 
F 5 HOH   229 629 184 HOH   HOH A . 
F 5 HOH   230 630 339 HOH   HOH A . 
F 5 HOH   231 631 347 HOH   HOH A . 
F 5 HOH   232 632 341 HOH   HOH A . 
F 5 HOH   233 633 50  HOH   HOH A . 
F 5 HOH   234 634 33  HOH   HOH A . 
F 5 HOH   235 635 57  HOH   HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A HIS   4   ? CG  ? A HIS   4   CG  
2  1 Y 1 A HIS   4   ? ND1 ? A HIS   4   ND1 
3  1 Y 1 A HIS   4   ? CD2 ? A HIS   4   CD2 
4  1 Y 1 A HIS   4   ? CE1 ? A HIS   4   CE1 
5  1 Y 1 A HIS   4   ? NE2 ? A HIS   4   NE2 
6  1 Y 1 A LYS   9   ? CG  ? A LYS   9   CG  
7  1 Y 1 A LYS   9   ? CD  ? A LYS   9   CD  
8  1 Y 1 A LYS   9   ? CE  ? A LYS   9   CE  
9  1 Y 1 A LYS   9   ? NZ  ? A LYS   9   NZ  
10 1 Y 1 A GLU   14  ? CD  ? A GLU   14  CD  
11 1 Y 1 A GLU   14  ? OE1 ? A GLU   14  OE1 
12 1 Y 1 A GLU   14  ? OE2 ? A GLU   14  OE2 
13 1 Y 1 A LYS   45  ? CE  ? A LYS   45  CE  
14 1 Y 1 A LYS   45  ? NZ  ? A LYS   45  NZ  
15 1 Y 1 A LYS   80  ? CE  ? A LYS   80  CE  
16 1 Y 1 A LYS   80  ? NZ  ? A LYS   80  NZ  
17 1 Y 1 A ASP   85  ? CG  ? A ASP   85  CG  
18 1 Y 1 A ASP   85  ? OD1 ? A ASP   85  OD1 
19 1 Y 1 A ASP   85  ? OD2 ? A ASP   85  OD2 
20 1 Y 1 A LYS   127 ? NZ  ? A LYS   126 NZ  
21 1 Y 1 A LYS   133 ? CD  ? A LYS   132 CD  
22 1 Y 1 A LYS   133 ? CE  ? A LYS   132 CE  
23 1 Y 1 A LYS   133 ? NZ  ? A LYS   132 NZ  
24 1 Y 1 A LYS   149 ? CE  ? A LYS   148 CE  
25 1 Y 1 A LYS   149 ? NZ  ? A LYS   148 NZ  
26 1 Y 1 A LYS   159 ? CD  ? A LYS   158 CD  
27 1 Y 1 A LYS   159 ? CE  ? A LYS   158 CE  
28 1 Y 1 A LYS   159 ? NZ  ? A LYS   158 NZ  
29 1 Y 1 A ASP   165 ? CG  ? A ASP   164 CG  
30 1 Y 1 A ASP   165 ? OD1 ? A ASP   164 OD1 
31 1 Y 1 A ASP   165 ? OD2 ? A ASP   164 OD2 
32 1 Y 1 A LYS   170 ? NZ  ? A LYS   169 NZ  
33 1 Y 1 A LYS   172 ? CE  ? A LYS   171 CE  
34 1 Y 1 A LYS   172 ? NZ  ? A LYS   171 NZ  
35 1 Y 1 A LYS   228 ? CE  ? A LYS   227 CE  
36 1 Y 1 A LYS   228 ? NZ  ? A LYS   227 NZ  
37 1 Y 1 A LYS   257 ? CD  ? A LYS   256 CD  
38 1 Y 1 A LYS   257 ? CE  ? A LYS   256 CE  
39 1 Y 1 A LYS   257 ? NZ  ? A LYS   256 NZ  
40 1 Y 1 A LYS   261 ? CG  ? A LYS   260 CG  
41 1 Y 1 A LYS   261 ? CD  ? A LYS   260 CD  
42 1 Y 1 A LYS   261 ? CE  ? A LYS   260 CE  
43 1 Y 1 A LYS   261 ? NZ  ? A LYS   260 NZ  
44 1 N 1 A A1H15 303 ? N14 ? D A1H15 1   N14 
45 1 N 1 A A1H15 303 ? C15 ? D A1H15 1   C15 
46 1 N 1 A A1H15 303 ? N16 ? D A1H15 1   N16 
47 1 N 1 A A1H15 303 ? N18 ? D A1H15 1   N18 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC ? ? ? 5.8.0419 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XSCALE ? ? ? .        2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? REFMAC ? ? ? .        4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   104.29 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8ROW 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     42.440 
_cell.length_a_esd                 ? 
_cell.length_b                     41.300 
_cell.length_b_esd                 ? 
_cell.length_c                     72.030 
_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             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         8ROW 
_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                   8ROW 
_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             2.32 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          47 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '1.5 M sodium citrate, 50 mM Tris-HCl (pH 8.0)' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            296 
# 
_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         2023-06-26 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.9718 
_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                        'ELETTRA BEAMLINE 11.2C' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9718 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   11.2C 
_diffrn_source.pdbx_synchrotron_site       ELETTRA 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8ROW 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.050 
_reflns.d_resolution_low                               40.015 
_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                                     107024 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           95.0 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.1 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          16.7 
_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                                0.054 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.9990000000000001 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.049 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.050 
_reflns_shell.d_res_low                                     1.068 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           2.2 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             4661 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               4.5 
_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                               0.801 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.715 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          83.7 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.706 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            -0.04 
_refine.aniso_B[1][2]                            -0.00 
_refine.aniso_B[1][3]                            0.01 
_refine.aniso_B[2][2]                            -0.07 
_refine.aniso_B[2][3]                            0.00 
_refine.aniso_B[3][3]                            0.09 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               11.483 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.984 
_refine.correlation_coeff_Fo_to_Fc_free          0.977 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_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                                 8ROW 
_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                            1.05 
_refine.ls_d_res_low                             40.015 
_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                     101727 
_refine.ls_number_reflns_R_free                  5295 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    94.90 
_refine.ls_percent_reflns_R_free                 4.9 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.11711 
_refine.ls_R_factor_R_free                       0.13856 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.11603 
_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                          ? 
_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          'FOURIER SYNTHESIS' 
_refine.pdbx_starting_model                      ? 
_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                       0.022 
_refine.pdbx_overall_ESU_R_Free                  0.023 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_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                             0.615 
_refine.overall_SU_ML                            0.014 
_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                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.05 
_refine_hist.d_res_low                        40.015 
_refine_hist.number_atoms_solvent             254 
_refine_hist.number_atoms_total               2298 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        2005 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         39 
_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' ? 0.012  0.012  2268 ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.004  0.016  2047 ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.901  1.664  3110 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 0.718  1.600  4730 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 7.152  5.000  283  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 20.015 5.000  14   ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 11.680 10.000 325  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.107  0.200  323  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.012  0.020  2731 ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.002  0.020  534  ? r_gen_planes_other           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_refined                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_other                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_refined              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_other                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_refined        ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_other          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_refined          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_other            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_refined     ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_other       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_refined ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_other   ? ? 
'X-RAY DIFFRACTION' ? 3.921  1.116  1091 ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 3.900  1.116  1091 ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 5.661  2.012  1380 ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 5.664  2.014  1381 ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 5.843  1.312  1177 ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 5.841  1.312  1178 ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 7.896  2.308  1728 ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 10.711 16.57  2498 ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 10.276 14.53  2443 ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? 4.363  3.000  4315 ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.050 
_refine_ls_shell.d_res_low                        1.077 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             347 
_refine_ls_shell.number_reflns_R_work             6717 
_refine_ls_shell.percent_reflns_obs               84.78 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.221 
_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                    ? 
_refine_ls_shell.R_factor_R_free                  0.229 
# 
_struct.entry_id                     8ROW 
_struct.title                        
;Human Carbonic Anhydrase II in complex with biguanide derivative inhibitor 1-carbamimidamido-N-[(4 sulfamoylphenyl)methyl]methanimidamide, using glycerol as cryoprotectant
;
_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        8ROW 
_struct_keywords.text            'metalloenzyme, lyase, inhibitor' 
_struct_keywords.pdbx_keywords   LYASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 3 ? 
E N N 4 ? 
F N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    CAH2_HUMAN 
_struct_ref.pdbx_db_accession          P00918 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLK
GGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              8ROW 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 260 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P00918 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  260 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       261 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              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)' 300   ? 
1 MORE         -7    ? 
1 'SSA (A^2)'  11210 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 HIS A 15  ? ASP A 19  ? HIS A 15  ASP A 19  5 ? 5 
HELX_P HELX_P2 AA2 PHE A 20  ? GLY A 25  ? PHE A 20  GLY A 25  5 ? 6 
HELX_P HELX_P3 AA3 LYS A 126 ? GLY A 128 ? LYS A 127 GLY A 129 5 ? 3 
HELX_P HELX_P4 AA4 ASP A 129 ? VAL A 134 ? ASP A 130 VAL A 135 1 ? 6 
HELX_P HELX_P5 AA5 LYS A 153 ? GLY A 155 ? LYS A 154 GLY A 156 5 ? 3 
HELX_P HELX_P6 AA6 LEU A 156 ? LEU A 163 ? LEU A 157 LEU A 164 1 ? 8 
HELX_P HELX_P7 AA7 ASP A 164 ? LYS A 167 ? ASP A 165 LYS A 168 5 ? 4 
HELX_P HELX_P8 AA8 ASP A 179 ? LEU A 184 ? ASP A 180 LEU A 185 5 ? 6 
HELX_P HELX_P9 AA9 SER A 218 ? ARG A 226 ? SER A 219 ARG A 227 1 ? 9 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A HIS 94  NE2 ? ? ? 1_555 B ZN    . ZN ? ? A HIS 94  A ZN    301 1_555 ? ? ? ? ? ? ? 2.005 ? ? 
metalc2 metalc ? ? A HIS 96  NE2 ? ? ? 1_555 B ZN    . ZN ? ? A HIS 96  A ZN    301 1_555 ? ? ? ? ? ? ? 2.035 ? ? 
metalc3 metalc ? ? A HIS 119 ND1 ? ? ? 1_555 B ZN    . ZN ? ? A HIS 119 A ZN    301 1_555 ? ? ? ? ? ? ? 2.041 ? ? 
metalc4 metalc ? ? B ZN  .   ZN  ? ? ? 1_555 C A1H15 . N9 A ? A ZN  301 A A1H15 302 1_555 ? ? ? ? ? ? ? 1.965 ? ? 
metalc5 metalc ? ? B ZN  .   ZN  ? ? ? 1_555 C A1H15 . N9 B ? A ZN  301 A A1H15 302 1_555 ? ? ? ? ? ? ? 1.920 ? ? 
# 
_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_555 103.2 ? 
2  NE2 ? A HIS   94  ? A HIS   94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 ND1 ? A HIS   119 ? A HIS   119 ? 1_555 111.8 ? 
3  NE2 ? A HIS   96  ? A HIS   96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 ND1 ? A HIS   119 ? A HIS   119 ? 1_555 98.4  ? 
4  NE2 ? A HIS   94  ? A HIS   94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N9  A C A1H15 .   ? A A1H15 302 ? 1_555 110.1 ? 
5  NE2 ? A HIS   96  ? A HIS   96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N9  A C A1H15 .   ? A A1H15 302 ? 1_555 112.1 ? 
6  ND1 ? A HIS   119 ? A HIS   119 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N9  A C A1H15 .   ? A A1H15 302 ? 1_555 119.5 ? 
7  NE2 ? A HIS   94  ? A HIS   94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N9  B C A1H15 .   ? A A1H15 302 ? 1_555 112.6 ? 
8  NE2 ? A HIS   96  ? A HIS   96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N9  B C A1H15 .   ? A A1H15 302 ? 1_555 115.8 ? 
9  ND1 ? A HIS   119 ? A HIS   119 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N9  B C A1H15 .   ? A A1H15 302 ? 1_555 113.8 ? 
10 N9  A C A1H15 .   ? A A1H15 302 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N9  B C A1H15 .   ? A A1H15 302 ? 1_555 5.9   ? 
# 
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 -4.60 
2 PRO 200 A . ? PRO 201 A PRO 201 A ? PRO 202 A 1 10.75 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2  ? 
AA2 ? 10 ? 
AA3 ? 6  ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2  ? parallel      
AA2 1 2  ? parallel      
AA2 2 3  ? anti-parallel 
AA2 3 4  ? anti-parallel 
AA2 4 5  ? parallel      
AA2 5 6  ? anti-parallel 
AA2 6 7  ? anti-parallel 
AA2 7 8  ? anti-parallel 
AA2 8 9  ? anti-parallel 
AA2 9 10 ? anti-parallel 
AA3 1 2  ? anti-parallel 
AA3 2 3  ? anti-parallel 
AA3 3 4  ? anti-parallel 
AA3 4 5  ? anti-parallel 
AA3 5 6  ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1  ASP A 32  ? ILE A 33  ? ASP A 32  ILE A 33  
AA1 2  THR A 108 ? VAL A 109 ? THR A 108 VAL A 109 
AA2 1  LYS A 39  ? TYR A 40  ? LYS A 39  TYR A 40  
AA2 2  LYS A 256 ? ALA A 257 ? LYS A 257 ALA A 258 
AA2 3  TYR A 190 ? GLY A 195 ? TYR A 191 GLY A 196 
AA2 4  VAL A 206 ? LEU A 211 ? VAL A 207 LEU A 212 
AA2 5  LEU A 140 ? VAL A 149 ? LEU A 141 VAL A 150 
AA2 6  ALA A 116 ? ASN A 124 ? ALA A 116 ASN A 124 
AA2 7  TYR A 88  ? TRP A 97  ? TYR A 88  TRP A 97  
AA2 8  PHE A 66  ? PHE A 70  ? PHE A 66  PHE A 70  
AA2 9  SER A 56  ? ASN A 61  ? SER A 56  ASN A 61  
AA2 10 SER A 172 ? ASP A 174 ? SER A 173 ASP A 175 
AA3 1  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 141 VAL A 150 
AA3 6  ILE A 215 ? VAL A 217 ? ILE A 216 VAL A 218 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2  N ILE A 33  ? N ILE A 33  O THR A 108 ? O THR A 108 
AA2 1 2  N LYS A 39  ? N LYS A 39  O ALA A 257 ? O ALA A 258 
AA2 2 3  O LYS A 256 ? O LYS A 257 N THR A 192 ? N THR A 193 
AA2 3 4  N GLY A 195 ? N GLY A 196 O VAL A 206 ? O VAL A 207 
AA2 4 5  O LEU A 211 ? O LEU A 212 N GLY A 144 ? N GLY A 145 
AA2 5 6  O ILE A 145 ? O ILE A 146 N LEU A 118 ? N LEU A 118 
AA2 6 7  O HIS A 119 ? O HIS A 119 N HIS A 94  ? N HIS A 94  
AA2 7 8  O PHE A 93  ? O PHE A 93  N VAL A 68  ? N VAL A 68  
AA2 8 9  O GLU A 69  ? O GLU A 69  N 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 174 
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 146 
AA3 5 6  N PHE A 146 ? N PHE A 147 O ILE A 215 ? O ILE A 216 
# 
_pdbx_entry_details.entry_id                   8ROW 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 OE2 A GLU 214 ? B O A HOH 410 ? ? 1.83 
2 1 O   A PRO 46  ? A O A HOH 411 ? ? 2.03 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    O 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    HOH 
_pdbx_validate_symm_contact.auth_seq_id_1     435 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    O 
_pdbx_validate_symm_contact.auth_asym_id_2    A 
_pdbx_validate_symm_contact.auth_comp_id_2    HOH 
_pdbx_validate_symm_contact.auth_seq_id_2     634 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   2_555 
_pdbx_validate_symm_contact.dist              2.15 
# 
_pdbx_validate_rmsd_bond.id                        1 
_pdbx_validate_rmsd_bond.PDB_model_num             1 
_pdbx_validate_rmsd_bond.auth_atom_id_1            CD 
_pdbx_validate_rmsd_bond.auth_asym_id_1            A 
_pdbx_validate_rmsd_bond.auth_comp_id_1            GLU 
_pdbx_validate_rmsd_bond.auth_seq_id_1             234 
_pdbx_validate_rmsd_bond.PDB_ins_code_1            ? 
_pdbx_validate_rmsd_bond.label_alt_id_1            ? 
_pdbx_validate_rmsd_bond.auth_atom_id_2            OE1 
_pdbx_validate_rmsd_bond.auth_asym_id_2            A 
_pdbx_validate_rmsd_bond.auth_comp_id_2            GLU 
_pdbx_validate_rmsd_bond.auth_seq_id_2             234 
_pdbx_validate_rmsd_bond.PDB_ins_code_2            ? 
_pdbx_validate_rmsd_bond.label_alt_id_2            ? 
_pdbx_validate_rmsd_bond.bond_value                1.320 
_pdbx_validate_rmsd_bond.bond_target_value         1.252 
_pdbx_validate_rmsd_bond.bond_deviation            0.068 
_pdbx_validate_rmsd_bond.bond_standard_deviation   0.011 
_pdbx_validate_rmsd_bond.linker_flag               N 
# 
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 NE A ARG 27  ? ? CZ A ARG 27  ? ? NH1 A ARG 27  ? ? 123.34 120.30 3.04  0.50 N 
2 1 NE A ARG 27  ? ? CZ A ARG 27  ? ? NH2 A ARG 27  ? ? 116.42 120.30 -3.88 0.50 N 
3 1 CB A PHE 226 ? ? CG A PHE 226 ? ? CD1 A PHE 226 ? ? 125.59 120.80 4.79  0.70 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  ? ? -141.56 14.58   
2 1 ARG A 27  ? ? -142.26 55.03   
3 1 ALA A 65  ? ? -168.18 -169.61 
4 1 GLU A 106 ? ? -92.26  -60.16  
5 1 LYS A 111 ? ? 75.03   -3.12   
6 1 PHE A 176 ? ? -152.85 64.44   
7 1 PHE A 176 ? ? -151.86 64.44   
8 1 ASN A 244 ? ? -94.46  47.54   
9 1 LYS A 252 ? ? 55.14   -140.30 
# 
_pdbx_validate_main_chain_plane.id                       1 
_pdbx_validate_main_chain_plane.PDB_model_num            1 
_pdbx_validate_main_chain_plane.auth_comp_id             LEU 
_pdbx_validate_main_chain_plane.auth_asym_id             A 
_pdbx_validate_main_chain_plane.auth_seq_id              44 
_pdbx_validate_main_chain_plane.PDB_ins_code             ? 
_pdbx_validate_main_chain_plane.label_alt_id             ? 
_pdbx_validate_main_chain_plane.improper_torsion_angle   -10.18 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A MET 1 ? A MET 1 
2 1 Y 1 A SER 2 ? A SER 2 
3 1 Y 1 A HIS 3 ? A HIS 3 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
A1H15 C1   C  N N 1   
A1H15 C2   C  Y N 2   
A1H15 C3   C  Y N 3   
A1H15 C4   C  Y N 4   
A1H15 C5   C  Y N 5   
A1H15 C6   C  Y N 6   
A1H15 C7   C  Y N 7   
A1H15 S8   S  N N 8   
A1H15 N9   N  N N 9   
A1H15 O10  O  N N 10  
A1H15 O11  O  N N 11  
A1H15 N12  N  N N 12  
A1H15 C13  C  N N 13  
A1H15 N14  N  N N 14  
A1H15 C15  C  N N 15  
A1H15 N16  N  N N 16  
A1H15 N17  N  N N 17  
A1H15 N18  N  N N 18  
A1H15 H1   H  N N 19  
A1H15 H2   H  N N 20  
A1H15 H3   H  N N 21  
A1H15 H4   H  N N 22  
A1H15 H5   H  N N 23  
A1H15 H6   H  N N 24  
A1H15 H7   H  N N 25  
A1H15 H8   H  N N 26  
A1H15 H9   H  N N 27  
A1H15 H10  H  N N 28  
A1H15 H11  H  N N 29  
A1H15 H12  H  N N 30  
A1H15 H13  H  N N 31  
A1H15 H14  H  N N 32  
ALA   N    N  N N 33  
ALA   CA   C  N S 34  
ALA   C    C  N N 35  
ALA   O    O  N N 36  
ALA   CB   C  N N 37  
ALA   OXT  O  N N 38  
ALA   H    H  N N 39  
ALA   H2   H  N N 40  
ALA   HA   H  N N 41  
ALA   HB1  H  N N 42  
ALA   HB2  H  N N 43  
ALA   HB3  H  N N 44  
ALA   HXT  H  N N 45  
ARG   N    N  N N 46  
ARG   CA   C  N S 47  
ARG   C    C  N N 48  
ARG   O    O  N N 49  
ARG   CB   C  N N 50  
ARG   CG   C  N N 51  
ARG   CD   C  N N 52  
ARG   NE   N  N N 53  
ARG   CZ   C  N N 54  
ARG   NH1  N  N N 55  
ARG   NH2  N  N N 56  
ARG   OXT  O  N N 57  
ARG   H    H  N N 58  
ARG   H2   H  N N 59  
ARG   HA   H  N N 60  
ARG   HB2  H  N N 61  
ARG   HB3  H  N N 62  
ARG   HG2  H  N N 63  
ARG   HG3  H  N N 64  
ARG   HD2  H  N N 65  
ARG   HD3  H  N N 66  
ARG   HE   H  N N 67  
ARG   HH11 H  N N 68  
ARG   HH12 H  N N 69  
ARG   HH21 H  N N 70  
ARG   HH22 H  N N 71  
ARG   HXT  H  N N 72  
ASN   N    N  N N 73  
ASN   CA   C  N S 74  
ASN   C    C  N N 75  
ASN   O    O  N N 76  
ASN   CB   C  N N 77  
ASN   CG   C  N N 78  
ASN   OD1  O  N N 79  
ASN   ND2  N  N N 80  
ASN   OXT  O  N N 81  
ASN   H    H  N N 82  
ASN   H2   H  N N 83  
ASN   HA   H  N N 84  
ASN   HB2  H  N N 85  
ASN   HB3  H  N N 86  
ASN   HD21 H  N N 87  
ASN   HD22 H  N N 88  
ASN   HXT  H  N N 89  
ASP   N    N  N N 90  
ASP   CA   C  N S 91  
ASP   C    C  N N 92  
ASP   O    O  N N 93  
ASP   CB   C  N N 94  
ASP   CG   C  N N 95  
ASP   OD1  O  N N 96  
ASP   OD2  O  N N 97  
ASP   OXT  O  N N 98  
ASP   H    H  N N 99  
ASP   H2   H  N N 100 
ASP   HA   H  N N 101 
ASP   HB2  H  N N 102 
ASP   HB3  H  N N 103 
ASP   HD2  H  N N 104 
ASP   HXT  H  N N 105 
CYS   N    N  N N 106 
CYS   CA   C  N R 107 
CYS   C    C  N N 108 
CYS   O    O  N N 109 
CYS   CB   C  N N 110 
CYS   SG   S  N N 111 
CYS   OXT  O  N N 112 
CYS   H    H  N N 113 
CYS   H2   H  N N 114 
CYS   HA   H  N N 115 
CYS   HB2  H  N N 116 
CYS   HB3  H  N N 117 
CYS   HG   H  N N 118 
CYS   HXT  H  N N 119 
GLN   N    N  N N 120 
GLN   CA   C  N S 121 
GLN   C    C  N N 122 
GLN   O    O  N N 123 
GLN   CB   C  N N 124 
GLN   CG   C  N N 125 
GLN   CD   C  N N 126 
GLN   OE1  O  N N 127 
GLN   NE2  N  N N 128 
GLN   OXT  O  N N 129 
GLN   H    H  N N 130 
GLN   H2   H  N N 131 
GLN   HA   H  N N 132 
GLN   HB2  H  N N 133 
GLN   HB3  H  N N 134 
GLN   HG2  H  N N 135 
GLN   HG3  H  N N 136 
GLN   HE21 H  N N 137 
GLN   HE22 H  N N 138 
GLN   HXT  H  N N 139 
GLU   N    N  N N 140 
GLU   CA   C  N S 141 
GLU   C    C  N N 142 
GLU   O    O  N N 143 
GLU   CB   C  N N 144 
GLU   CG   C  N N 145 
GLU   CD   C  N N 146 
GLU   OE1  O  N N 147 
GLU   OE2  O  N N 148 
GLU   OXT  O  N N 149 
GLU   H    H  N N 150 
GLU   H2   H  N N 151 
GLU   HA   H  N N 152 
GLU   HB2  H  N N 153 
GLU   HB3  H  N N 154 
GLU   HG2  H  N N 155 
GLU   HG3  H  N N 156 
GLU   HE2  H  N N 157 
GLU   HXT  H  N N 158 
GLY   N    N  N N 159 
GLY   CA   C  N N 160 
GLY   C    C  N N 161 
GLY   O    O  N N 162 
GLY   OXT  O  N N 163 
GLY   H    H  N N 164 
GLY   H2   H  N N 165 
GLY   HA2  H  N N 166 
GLY   HA3  H  N N 167 
GLY   HXT  H  N N 168 
GOL   C1   C  N N 169 
GOL   O1   O  N N 170 
GOL   C2   C  N N 171 
GOL   O2   O  N N 172 
GOL   C3   C  N N 173 
GOL   O3   O  N N 174 
GOL   H11  H  N N 175 
GOL   H12  H  N N 176 
GOL   HO1  H  N N 177 
GOL   H2   H  N N 178 
GOL   HO2  H  N N 179 
GOL   H31  H  N N 180 
GOL   H32  H  N N 181 
GOL   HO3  H  N N 182 
HIS   N    N  N N 183 
HIS   CA   C  N S 184 
HIS   C    C  N N 185 
HIS   O    O  N N 186 
HIS   CB   C  N N 187 
HIS   CG   C  Y N 188 
HIS   ND1  N  Y N 189 
HIS   CD2  C  Y N 190 
HIS   CE1  C  Y N 191 
HIS   NE2  N  Y N 192 
HIS   OXT  O  N N 193 
HIS   H    H  N N 194 
HIS   H2   H  N N 195 
HIS   HA   H  N N 196 
HIS   HB2  H  N N 197 
HIS   HB3  H  N N 198 
HIS   HD1  H  N N 199 
HIS   HD2  H  N N 200 
HIS   HE1  H  N N 201 
HIS   HE2  H  N N 202 
HIS   HXT  H  N N 203 
HOH   O    O  N N 204 
HOH   H1   H  N N 205 
HOH   H2   H  N N 206 
ILE   N    N  N N 207 
ILE   CA   C  N S 208 
ILE   C    C  N N 209 
ILE   O    O  N N 210 
ILE   CB   C  N S 211 
ILE   CG1  C  N N 212 
ILE   CG2  C  N N 213 
ILE   CD1  C  N N 214 
ILE   OXT  O  N N 215 
ILE   H    H  N N 216 
ILE   H2   H  N N 217 
ILE   HA   H  N N 218 
ILE   HB   H  N N 219 
ILE   HG12 H  N N 220 
ILE   HG13 H  N N 221 
ILE   HG21 H  N N 222 
ILE   HG22 H  N N 223 
ILE   HG23 H  N N 224 
ILE   HD11 H  N N 225 
ILE   HD12 H  N N 226 
ILE   HD13 H  N N 227 
ILE   HXT  H  N N 228 
LEU   N    N  N N 229 
LEU   CA   C  N S 230 
LEU   C    C  N N 231 
LEU   O    O  N N 232 
LEU   CB   C  N N 233 
LEU   CG   C  N N 234 
LEU   CD1  C  N N 235 
LEU   CD2  C  N N 236 
LEU   OXT  O  N N 237 
LEU   H    H  N N 238 
LEU   H2   H  N N 239 
LEU   HA   H  N N 240 
LEU   HB2  H  N N 241 
LEU   HB3  H  N N 242 
LEU   HG   H  N N 243 
LEU   HD11 H  N N 244 
LEU   HD12 H  N N 245 
LEU   HD13 H  N N 246 
LEU   HD21 H  N N 247 
LEU   HD22 H  N N 248 
LEU   HD23 H  N N 249 
LEU   HXT  H  N N 250 
LYS   N    N  N N 251 
LYS   CA   C  N S 252 
LYS   C    C  N N 253 
LYS   O    O  N N 254 
LYS   CB   C  N N 255 
LYS   CG   C  N N 256 
LYS   CD   C  N N 257 
LYS   CE   C  N N 258 
LYS   NZ   N  N N 259 
LYS   OXT  O  N N 260 
LYS   H    H  N N 261 
LYS   H2   H  N N 262 
LYS   HA   H  N N 263 
LYS   HB2  H  N N 264 
LYS   HB3  H  N N 265 
LYS   HG2  H  N N 266 
LYS   HG3  H  N N 267 
LYS   HD2  H  N N 268 
LYS   HD3  H  N N 269 
LYS   HE2  H  N N 270 
LYS   HE3  H  N N 271 
LYS   HZ1  H  N N 272 
LYS   HZ2  H  N N 273 
LYS   HZ3  H  N N 274 
LYS   HXT  H  N N 275 
MET   N    N  N N 276 
MET   CA   C  N S 277 
MET   C    C  N N 278 
MET   O    O  N N 279 
MET   CB   C  N N 280 
MET   CG   C  N N 281 
MET   SD   S  N N 282 
MET   CE   C  N N 283 
MET   OXT  O  N N 284 
MET   H    H  N N 285 
MET   H2   H  N N 286 
MET   HA   H  N N 287 
MET   HB2  H  N N 288 
MET   HB3  H  N N 289 
MET   HG2  H  N N 290 
MET   HG3  H  N N 291 
MET   HE1  H  N N 292 
MET   HE2  H  N N 293 
MET   HE3  H  N N 294 
MET   HXT  H  N N 295 
PHE   N    N  N N 296 
PHE   CA   C  N S 297 
PHE   C    C  N N 298 
PHE   O    O  N N 299 
PHE   CB   C  N N 300 
PHE   CG   C  Y N 301 
PHE   CD1  C  Y N 302 
PHE   CD2  C  Y N 303 
PHE   CE1  C  Y N 304 
PHE   CE2  C  Y N 305 
PHE   CZ   C  Y N 306 
PHE   OXT  O  N N 307 
PHE   H    H  N N 308 
PHE   H2   H  N N 309 
PHE   HA   H  N N 310 
PHE   HB2  H  N N 311 
PHE   HB3  H  N N 312 
PHE   HD1  H  N N 313 
PHE   HD2  H  N N 314 
PHE   HE1  H  N N 315 
PHE   HE2  H  N N 316 
PHE   HZ   H  N N 317 
PHE   HXT  H  N N 318 
PRO   N    N  N N 319 
PRO   CA   C  N S 320 
PRO   C    C  N N 321 
PRO   O    O  N N 322 
PRO   CB   C  N N 323 
PRO   CG   C  N N 324 
PRO   CD   C  N N 325 
PRO   OXT  O  N N 326 
PRO   H    H  N N 327 
PRO   HA   H  N N 328 
PRO   HB2  H  N N 329 
PRO   HB3  H  N N 330 
PRO   HG2  H  N N 331 
PRO   HG3  H  N N 332 
PRO   HD2  H  N N 333 
PRO   HD3  H  N N 334 
PRO   HXT  H  N N 335 
SER   N    N  N N 336 
SER   CA   C  N S 337 
SER   C    C  N N 338 
SER   O    O  N N 339 
SER   CB   C  N N 340 
SER   OG   O  N N 341 
SER   OXT  O  N N 342 
SER   H    H  N N 343 
SER   H2   H  N N 344 
SER   HA   H  N N 345 
SER   HB2  H  N N 346 
SER   HB3  H  N N 347 
SER   HG   H  N N 348 
SER   HXT  H  N N 349 
THR   N    N  N N 350 
THR   CA   C  N S 351 
THR   C    C  N N 352 
THR   O    O  N N 353 
THR   CB   C  N R 354 
THR   OG1  O  N N 355 
THR   CG2  C  N N 356 
THR   OXT  O  N N 357 
THR   H    H  N N 358 
THR   H2   H  N N 359 
THR   HA   H  N N 360 
THR   HB   H  N N 361 
THR   HG1  H  N N 362 
THR   HG21 H  N N 363 
THR   HG22 H  N N 364 
THR   HG23 H  N N 365 
THR   HXT  H  N N 366 
TRP   N    N  N N 367 
TRP   CA   C  N S 368 
TRP   C    C  N N 369 
TRP   O    O  N N 370 
TRP   CB   C  N N 371 
TRP   CG   C  Y N 372 
TRP   CD1  C  Y N 373 
TRP   CD2  C  Y N 374 
TRP   NE1  N  Y N 375 
TRP   CE2  C  Y N 376 
TRP   CE3  C  Y N 377 
TRP   CZ2  C  Y N 378 
TRP   CZ3  C  Y N 379 
TRP   CH2  C  Y N 380 
TRP   OXT  O  N N 381 
TRP   H    H  N N 382 
TRP   H2   H  N N 383 
TRP   HA   H  N N 384 
TRP   HB2  H  N N 385 
TRP   HB3  H  N N 386 
TRP   HD1  H  N N 387 
TRP   HE1  H  N N 388 
TRP   HE3  H  N N 389 
TRP   HZ2  H  N N 390 
TRP   HZ3  H  N N 391 
TRP   HH2  H  N N 392 
TRP   HXT  H  N N 393 
TYR   N    N  N N 394 
TYR   CA   C  N S 395 
TYR   C    C  N N 396 
TYR   O    O  N N 397 
TYR   CB   C  N N 398 
TYR   CG   C  Y N 399 
TYR   CD1  C  Y N 400 
TYR   CD2  C  Y N 401 
TYR   CE1  C  Y N 402 
TYR   CE2  C  Y N 403 
TYR   CZ   C  Y N 404 
TYR   OH   O  N N 405 
TYR   OXT  O  N N 406 
TYR   H    H  N N 407 
TYR   H2   H  N N 408 
TYR   HA   H  N N 409 
TYR   HB2  H  N N 410 
TYR   HB3  H  N N 411 
TYR   HD1  H  N N 412 
TYR   HD2  H  N N 413 
TYR   HE1  H  N N 414 
TYR   HE2  H  N N 415 
TYR   HH   H  N N 416 
TYR   HXT  H  N N 417 
VAL   N    N  N N 418 
VAL   CA   C  N S 419 
VAL   C    C  N N 420 
VAL   O    O  N N 421 
VAL   CB   C  N N 422 
VAL   CG1  C  N N 423 
VAL   CG2  C  N N 424 
VAL   OXT  O  N N 425 
VAL   H    H  N N 426 
VAL   H2   H  N N 427 
VAL   HA   H  N N 428 
VAL   HB   H  N N 429 
VAL   HG11 H  N N 430 
VAL   HG12 H  N N 431 
VAL   HG13 H  N N 432 
VAL   HG21 H  N N 433 
VAL   HG22 H  N N 434 
VAL   HG23 H  N N 435 
VAL   HXT  H  N N 436 
ZN    ZN   ZN N N 437 
# 
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 
A1H15 N18 C15  doub N N 1   
A1H15 C15 N16  sing N N 2   
A1H15 C15 N14  sing N N 3   
A1H15 N14 C13  sing N N 4   
A1H15 C13 N12  sing N N 5   
A1H15 C13 N17  doub N N 6   
A1H15 N12 C1   sing N N 7   
A1H15 C1  C2   sing N N 8   
A1H15 C2  C7   doub Y N 9   
A1H15 C2  C3   sing Y N 10  
A1H15 C7  C6   sing Y N 11  
A1H15 C3  C4   doub Y N 12  
A1H15 C6  C5   doub Y N 13  
A1H15 C4  C5   sing Y N 14  
A1H15 C5  S8   sing N N 15  
A1H15 N9  S8   sing N N 16  
A1H15 O11 S8   doub N N 17  
A1H15 S8  O10  doub N N 18  
A1H15 C1  H1   sing N N 19  
A1H15 C1  H2   sing N N 20  
A1H15 C3  H3   sing N N 21  
A1H15 C4  H4   sing N N 22  
A1H15 C6  H5   sing N N 23  
A1H15 C7  H6   sing N N 24  
A1H15 N9  H7   sing N N 25  
A1H15 N9  H8   sing N N 26  
A1H15 N12 H9   sing N N 27  
A1H15 N14 H10  sing N N 28  
A1H15 N16 H11  sing N N 29  
A1H15 N16 H12  sing N N 30  
A1H15 N17 H13  sing N N 31  
A1H15 N18 H14  sing N N 32  
ALA   N   CA   sing N N 33  
ALA   N   H    sing N N 34  
ALA   N   H2   sing N N 35  
ALA   CA  C    sing N N 36  
ALA   CA  CB   sing N N 37  
ALA   CA  HA   sing N N 38  
ALA   C   O    doub N N 39  
ALA   C   OXT  sing N N 40  
ALA   CB  HB1  sing N N 41  
ALA   CB  HB2  sing N N 42  
ALA   CB  HB3  sing N N 43  
ALA   OXT HXT  sing N N 44  
ARG   N   CA   sing N N 45  
ARG   N   H    sing N N 46  
ARG   N   H2   sing N N 47  
ARG   CA  C    sing N N 48  
ARG   CA  CB   sing N N 49  
ARG   CA  HA   sing N N 50  
ARG   C   O    doub N N 51  
ARG   C   OXT  sing N N 52  
ARG   CB  CG   sing N N 53  
ARG   CB  HB2  sing N N 54  
ARG   CB  HB3  sing N N 55  
ARG   CG  CD   sing N N 56  
ARG   CG  HG2  sing N N 57  
ARG   CG  HG3  sing N N 58  
ARG   CD  NE   sing N N 59  
ARG   CD  HD2  sing N N 60  
ARG   CD  HD3  sing N N 61  
ARG   NE  CZ   sing N N 62  
ARG   NE  HE   sing N N 63  
ARG   CZ  NH1  sing N N 64  
ARG   CZ  NH2  doub N N 65  
ARG   NH1 HH11 sing N N 66  
ARG   NH1 HH12 sing N N 67  
ARG   NH2 HH21 sing N N 68  
ARG   NH2 HH22 sing N N 69  
ARG   OXT HXT  sing N N 70  
ASN   N   CA   sing N N 71  
ASN   N   H    sing N N 72  
ASN   N   H2   sing N N 73  
ASN   CA  C    sing N N 74  
ASN   CA  CB   sing N N 75  
ASN   CA  HA   sing N N 76  
ASN   C   O    doub N N 77  
ASN   C   OXT  sing N N 78  
ASN   CB  CG   sing N N 79  
ASN   CB  HB2  sing N N 80  
ASN   CB  HB3  sing N N 81  
ASN   CG  OD1  doub N N 82  
ASN   CG  ND2  sing N N 83  
ASN   ND2 HD21 sing N N 84  
ASN   ND2 HD22 sing N N 85  
ASN   OXT HXT  sing N N 86  
ASP   N   CA   sing N N 87  
ASP   N   H    sing N N 88  
ASP   N   H2   sing N N 89  
ASP   CA  C    sing N N 90  
ASP   CA  CB   sing N N 91  
ASP   CA  HA   sing N N 92  
ASP   C   O    doub N N 93  
ASP   C   OXT  sing N N 94  
ASP   CB  CG   sing N N 95  
ASP   CB  HB2  sing N N 96  
ASP   CB  HB3  sing N N 97  
ASP   CG  OD1  doub N N 98  
ASP   CG  OD2  sing N N 99  
ASP   OD2 HD2  sing N N 100 
ASP   OXT HXT  sing N N 101 
CYS   N   CA   sing N N 102 
CYS   N   H    sing N N 103 
CYS   N   H2   sing N N 104 
CYS   CA  C    sing N N 105 
CYS   CA  CB   sing N N 106 
CYS   CA  HA   sing N N 107 
CYS   C   O    doub N N 108 
CYS   C   OXT  sing N N 109 
CYS   CB  SG   sing N N 110 
CYS   CB  HB2  sing N N 111 
CYS   CB  HB3  sing N N 112 
CYS   SG  HG   sing N N 113 
CYS   OXT HXT  sing N N 114 
GLN   N   CA   sing N N 115 
GLN   N   H    sing N N 116 
GLN   N   H2   sing N N 117 
GLN   CA  C    sing N N 118 
GLN   CA  CB   sing N N 119 
GLN   CA  HA   sing N N 120 
GLN   C   O    doub N N 121 
GLN   C   OXT  sing N N 122 
GLN   CB  CG   sing N N 123 
GLN   CB  HB2  sing N N 124 
GLN   CB  HB3  sing N N 125 
GLN   CG  CD   sing N N 126 
GLN   CG  HG2  sing N N 127 
GLN   CG  HG3  sing N N 128 
GLN   CD  OE1  doub N N 129 
GLN   CD  NE2  sing N N 130 
GLN   NE2 HE21 sing N N 131 
GLN   NE2 HE22 sing N N 132 
GLN   OXT HXT  sing N N 133 
GLU   N   CA   sing N N 134 
GLU   N   H    sing N N 135 
GLU   N   H2   sing N N 136 
GLU   CA  C    sing N N 137 
GLU   CA  CB   sing N N 138 
GLU   CA  HA   sing N N 139 
GLU   C   O    doub N N 140 
GLU   C   OXT  sing N N 141 
GLU   CB  CG   sing N N 142 
GLU   CB  HB2  sing N N 143 
GLU   CB  HB3  sing N N 144 
GLU   CG  CD   sing N N 145 
GLU   CG  HG2  sing N N 146 
GLU   CG  HG3  sing N N 147 
GLU   CD  OE1  doub N N 148 
GLU   CD  OE2  sing N N 149 
GLU   OE2 HE2  sing N N 150 
GLU   OXT HXT  sing N N 151 
GLY   N   CA   sing N N 152 
GLY   N   H    sing N N 153 
GLY   N   H2   sing N N 154 
GLY   CA  C    sing N N 155 
GLY   CA  HA2  sing N N 156 
GLY   CA  HA3  sing N N 157 
GLY   C   O    doub N N 158 
GLY   C   OXT  sing N N 159 
GLY   OXT HXT  sing N N 160 
GOL   C1  O1   sing N N 161 
GOL   C1  C2   sing N N 162 
GOL   C1  H11  sing N N 163 
GOL   C1  H12  sing N N 164 
GOL   O1  HO1  sing N N 165 
GOL   C2  O2   sing N N 166 
GOL   C2  C3   sing N N 167 
GOL   C2  H2   sing N N 168 
GOL   O2  HO2  sing N N 169 
GOL   C3  O3   sing N N 170 
GOL   C3  H31  sing N N 171 
GOL   C3  H32  sing N N 172 
GOL   O3  HO3  sing N N 173 
HIS   N   CA   sing N N 174 
HIS   N   H    sing N N 175 
HIS   N   H2   sing N N 176 
HIS   CA  C    sing N N 177 
HIS   CA  CB   sing N N 178 
HIS   CA  HA   sing N N 179 
HIS   C   O    doub N N 180 
HIS   C   OXT  sing N N 181 
HIS   CB  CG   sing N N 182 
HIS   CB  HB2  sing N N 183 
HIS   CB  HB3  sing N N 184 
HIS   CG  ND1  sing Y N 185 
HIS   CG  CD2  doub Y N 186 
HIS   ND1 CE1  doub Y N 187 
HIS   ND1 HD1  sing N N 188 
HIS   CD2 NE2  sing Y N 189 
HIS   CD2 HD2  sing N N 190 
HIS   CE1 NE2  sing Y N 191 
HIS   CE1 HE1  sing N N 192 
HIS   NE2 HE2  sing N N 193 
HIS   OXT HXT  sing N N 194 
HOH   O   H1   sing N N 195 
HOH   O   H2   sing N N 196 
ILE   N   CA   sing N N 197 
ILE   N   H    sing N N 198 
ILE   N   H2   sing N N 199 
ILE   CA  C    sing N N 200 
ILE   CA  CB   sing N N 201 
ILE   CA  HA   sing N N 202 
ILE   C   O    doub N N 203 
ILE   C   OXT  sing N N 204 
ILE   CB  CG1  sing N N 205 
ILE   CB  CG2  sing N N 206 
ILE   CB  HB   sing N N 207 
ILE   CG1 CD1  sing N N 208 
ILE   CG1 HG12 sing N N 209 
ILE   CG1 HG13 sing N N 210 
ILE   CG2 HG21 sing N N 211 
ILE   CG2 HG22 sing N N 212 
ILE   CG2 HG23 sing N N 213 
ILE   CD1 HD11 sing N N 214 
ILE   CD1 HD12 sing N N 215 
ILE   CD1 HD13 sing N N 216 
ILE   OXT HXT  sing N N 217 
LEU   N   CA   sing N N 218 
LEU   N   H    sing N N 219 
LEU   N   H2   sing N N 220 
LEU   CA  C    sing N N 221 
LEU   CA  CB   sing N N 222 
LEU   CA  HA   sing N N 223 
LEU   C   O    doub N N 224 
LEU   C   OXT  sing N N 225 
LEU   CB  CG   sing N N 226 
LEU   CB  HB2  sing N N 227 
LEU   CB  HB3  sing N N 228 
LEU   CG  CD1  sing N N 229 
LEU   CG  CD2  sing N N 230 
LEU   CG  HG   sing N N 231 
LEU   CD1 HD11 sing N N 232 
LEU   CD1 HD12 sing N N 233 
LEU   CD1 HD13 sing N N 234 
LEU   CD2 HD21 sing N N 235 
LEU   CD2 HD22 sing N N 236 
LEU   CD2 HD23 sing N N 237 
LEU   OXT HXT  sing N N 238 
LYS   N   CA   sing N N 239 
LYS   N   H    sing N N 240 
LYS   N   H2   sing N N 241 
LYS   CA  C    sing N N 242 
LYS   CA  CB   sing N N 243 
LYS   CA  HA   sing N N 244 
LYS   C   O    doub N N 245 
LYS   C   OXT  sing N N 246 
LYS   CB  CG   sing N N 247 
LYS   CB  HB2  sing N N 248 
LYS   CB  HB3  sing N N 249 
LYS   CG  CD   sing N N 250 
LYS   CG  HG2  sing N N 251 
LYS   CG  HG3  sing N N 252 
LYS   CD  CE   sing N N 253 
LYS   CD  HD2  sing N N 254 
LYS   CD  HD3  sing N N 255 
LYS   CE  NZ   sing N N 256 
LYS   CE  HE2  sing N N 257 
LYS   CE  HE3  sing N N 258 
LYS   NZ  HZ1  sing N N 259 
LYS   NZ  HZ2  sing N N 260 
LYS   NZ  HZ3  sing N N 261 
LYS   OXT HXT  sing N N 262 
MET   N   CA   sing N N 263 
MET   N   H    sing N N 264 
MET   N   H2   sing N N 265 
MET   CA  C    sing N N 266 
MET   CA  CB   sing N N 267 
MET   CA  HA   sing N N 268 
MET   C   O    doub N N 269 
MET   C   OXT  sing N N 270 
MET   CB  CG   sing N N 271 
MET   CB  HB2  sing N N 272 
MET   CB  HB3  sing N N 273 
MET   CG  SD   sing N N 274 
MET   CG  HG2  sing N N 275 
MET   CG  HG3  sing N N 276 
MET   SD  CE   sing N N 277 
MET   CE  HE1  sing N N 278 
MET   CE  HE2  sing N N 279 
MET   CE  HE3  sing N N 280 
MET   OXT HXT  sing N N 281 
PHE   N   CA   sing N N 282 
PHE   N   H    sing N N 283 
PHE   N   H2   sing N N 284 
PHE   CA  C    sing N N 285 
PHE   CA  CB   sing N N 286 
PHE   CA  HA   sing N N 287 
PHE   C   O    doub N N 288 
PHE   C   OXT  sing N N 289 
PHE   CB  CG   sing N N 290 
PHE   CB  HB2  sing N N 291 
PHE   CB  HB3  sing N N 292 
PHE   CG  CD1  doub Y N 293 
PHE   CG  CD2  sing Y N 294 
PHE   CD1 CE1  sing Y N 295 
PHE   CD1 HD1  sing N N 296 
PHE   CD2 CE2  doub Y N 297 
PHE   CD2 HD2  sing N N 298 
PHE   CE1 CZ   doub Y N 299 
PHE   CE1 HE1  sing N N 300 
PHE   CE2 CZ   sing Y N 301 
PHE   CE2 HE2  sing N N 302 
PHE   CZ  HZ   sing N N 303 
PHE   OXT HXT  sing N N 304 
PRO   N   CA   sing N N 305 
PRO   N   CD   sing N N 306 
PRO   N   H    sing N N 307 
PRO   CA  C    sing N N 308 
PRO   CA  CB   sing N N 309 
PRO   CA  HA   sing N N 310 
PRO   C   O    doub N N 311 
PRO   C   OXT  sing N N 312 
PRO   CB  CG   sing N N 313 
PRO   CB  HB2  sing N N 314 
PRO   CB  HB3  sing N N 315 
PRO   CG  CD   sing N N 316 
PRO   CG  HG2  sing N N 317 
PRO   CG  HG3  sing N N 318 
PRO   CD  HD2  sing N N 319 
PRO   CD  HD3  sing N N 320 
PRO   OXT HXT  sing N N 321 
SER   N   CA   sing N N 322 
SER   N   H    sing N N 323 
SER   N   H2   sing N N 324 
SER   CA  C    sing N N 325 
SER   CA  CB   sing N N 326 
SER   CA  HA   sing N N 327 
SER   C   O    doub N N 328 
SER   C   OXT  sing N N 329 
SER   CB  OG   sing N N 330 
SER   CB  HB2  sing N N 331 
SER   CB  HB3  sing N N 332 
SER   OG  HG   sing N N 333 
SER   OXT HXT  sing N N 334 
THR   N   CA   sing N N 335 
THR   N   H    sing N N 336 
THR   N   H2   sing N N 337 
THR   CA  C    sing N N 338 
THR   CA  CB   sing N N 339 
THR   CA  HA   sing N N 340 
THR   C   O    doub N N 341 
THR   C   OXT  sing N N 342 
THR   CB  OG1  sing N N 343 
THR   CB  CG2  sing N N 344 
THR   CB  HB   sing N N 345 
THR   OG1 HG1  sing N N 346 
THR   CG2 HG21 sing N N 347 
THR   CG2 HG22 sing N N 348 
THR   CG2 HG23 sing N N 349 
THR   OXT HXT  sing N N 350 
TRP   N   CA   sing N N 351 
TRP   N   H    sing N N 352 
TRP   N   H2   sing N N 353 
TRP   CA  C    sing N N 354 
TRP   CA  CB   sing N N 355 
TRP   CA  HA   sing N N 356 
TRP   C   O    doub N N 357 
TRP   C   OXT  sing N N 358 
TRP   CB  CG   sing N N 359 
TRP   CB  HB2  sing N N 360 
TRP   CB  HB3  sing N N 361 
TRP   CG  CD1  doub Y N 362 
TRP   CG  CD2  sing Y N 363 
TRP   CD1 NE1  sing Y N 364 
TRP   CD1 HD1  sing N N 365 
TRP   CD2 CE2  doub Y N 366 
TRP   CD2 CE3  sing Y N 367 
TRP   NE1 CE2  sing Y N 368 
TRP   NE1 HE1  sing N N 369 
TRP   CE2 CZ2  sing Y N 370 
TRP   CE3 CZ3  doub Y N 371 
TRP   CE3 HE3  sing N N 372 
TRP   CZ2 CH2  doub Y N 373 
TRP   CZ2 HZ2  sing N N 374 
TRP   CZ3 CH2  sing Y N 375 
TRP   CZ3 HZ3  sing N N 376 
TRP   CH2 HH2  sing N N 377 
TRP   OXT HXT  sing N N 378 
TYR   N   CA   sing N N 379 
TYR   N   H    sing N N 380 
TYR   N   H2   sing N N 381 
TYR   CA  C    sing N N 382 
TYR   CA  CB   sing N N 383 
TYR   CA  HA   sing N N 384 
TYR   C   O    doub N N 385 
TYR   C   OXT  sing N N 386 
TYR   CB  CG   sing N N 387 
TYR   CB  HB2  sing N N 388 
TYR   CB  HB3  sing N N 389 
TYR   CG  CD1  doub Y N 390 
TYR   CG  CD2  sing Y N 391 
TYR   CD1 CE1  sing Y N 392 
TYR   CD1 HD1  sing N N 393 
TYR   CD2 CE2  doub Y N 394 
TYR   CD2 HD2  sing N N 395 
TYR   CE1 CZ   doub Y N 396 
TYR   CE1 HE1  sing N N 397 
TYR   CE2 CZ   sing Y N 398 
TYR   CE2 HE2  sing N N 399 
TYR   CZ  OH   sing N N 400 
TYR   OH  HH   sing N N 401 
TYR   OXT HXT  sing N N 402 
VAL   N   CA   sing N N 403 
VAL   N   H    sing N N 404 
VAL   N   H2   sing N N 405 
VAL   CA  C    sing N N 406 
VAL   CA  CB   sing N N 407 
VAL   CA  HA   sing N N 408 
VAL   C   O    doub N N 409 
VAL   C   OXT  sing N N 410 
VAL   CB  CG1  sing N N 411 
VAL   CB  CG2  sing N N 412 
VAL   CB  HB   sing N N 413 
VAL   CG1 HG11 sing N N 414 
VAL   CG1 HG12 sing N N 415 
VAL   CG1 HG13 sing N N 416 
VAL   CG2 HG21 sing N N 417 
VAL   CG2 HG22 sing N N 418 
VAL   CG2 HG23 sing N N 419 
VAL   OXT HXT  sing N N 420 
# 
_pdbx_audit_support.funding_organization   'European Union (EU)' 
_pdbx_audit_support.country                'European Union' 
_pdbx_audit_support.grant_number           B83C22003920001 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   3HS4 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8ROW 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.023563 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.006000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.024213 
_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]   0.014326 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . HIS   A 1 4   ? 9.269   1.561   8.789   1.00 32.85 ? 4   HIS   A N   1 
ATOM   2    C  CA  . HIS   A 1 4   ? 9.543   0.162   8.402   1.00 25.92 ? 4   HIS   A CA  1 
ATOM   3    C  C   . HIS   A 1 4   ? 9.110   -0.852  9.461   1.00 17.89 ? 4   HIS   A C   1 
ATOM   4    O  O   . HIS   A 1 4   ? 9.350   -2.046  9.238   1.00 18.80 ? 4   HIS   A O   1 
ATOM   5    C  CB  . HIS   A 1 4   ? 10.989  -0.211  8.079   1.00 24.55 ? 4   HIS   A CB  1 
ATOM   6    N  N   . TRP   A 1 5   ? 8.371   -0.464  10.520  1.00 15.22 ? 5   TRP   A N   1 
ATOM   7    C  CA  . TRP   A 1 5   ? 7.710   -1.442  11.365  1.00 12.91 ? 5   TRP   A CA  1 
ATOM   8    C  C   . TRP   A 1 5   ? 6.704   -2.261  10.555  1.00 12.26 ? 5   TRP   A C   1 
ATOM   9    O  O   . TRP   A 1 5   ? 6.150   -1.777  9.566   1.00 13.43 ? 5   TRP   A O   1 
ATOM   10   C  CB  . TRP   A 1 5   ? 7.010   -0.745  12.539  1.00 12.05 ? 5   TRP   A CB  1 
ATOM   11   C  CG  . TRP   A 1 5   ? 5.811   0.057   12.145  1.00 11.73 ? 5   TRP   A CG  1 
ATOM   12   C  CD1 . TRP   A 1 5   ? 5.760   1.383   11.851  1.00 13.05 ? 5   TRP   A CD1 1 
ATOM   13   C  CD2 . TRP   A 1 5   ? 4.463   -0.429  12.080  1.00 10.95 ? 5   TRP   A CD2 1 
ATOM   14   N  NE1 . TRP   A 1 5   ? 4.497   1.750   11.539  1.00 13.70 ? 5   TRP   A NE1 1 
ATOM   15   C  CE2 . TRP   A 1 5   ? 3.667   0.663   11.677  1.00 12.19 ? 5   TRP   A CE2 1 
ATOM   16   C  CE3 . TRP   A 1 5   ? 3.874   -1.665  12.342  1.00 10.63 ? 5   TRP   A CE3 1 
ATOM   17   C  CZ2 . TRP   A 1 5   ? 2.283   0.533   11.528  1.00 13.14 ? 5   TRP   A CZ2 1 
ATOM   18   C  CZ3 . TRP   A 1 5   ? 2.508   -1.780  12.189  1.00 11.33 ? 5   TRP   A CZ3 1 
ATOM   19   C  CH2 . TRP   A 1 5   ? 1.729   -0.686  11.788  1.00 12.35 ? 5   TRP   A CH2 1 
ATOM   20   N  N   . GLY   A 1 6   ? 6.450   -3.470  11.037  1.00 11.17 ? 6   GLY   A N   1 
ATOM   21   C  CA  . GLY   A 1 6   ? 5.436   -4.306  10.427  1.00 11.10 ? 6   GLY   A CA  1 
ATOM   22   C  C   . GLY   A 1 6   ? 5.122   -5.468  11.361  1.00 10.62 ? 6   GLY   A C   1 
ATOM   23   O  O   . GLY   A 1 6   ? 5.118   -5.342  12.584  1.00 10.92 ? 6   GLY   A O   1 
ATOM   24   N  N   . TYR   A 1 7   ? 4.812   -6.604  10.718  1.00 10.73 ? 7   TYR   A N   1 
ATOM   25   C  CA  . TYR   A 1 7   ? 4.409   -7.813  11.408  1.00 11.55 ? 7   TYR   A CA  1 
ATOM   26   C  C   . TYR   A 1 7   ? 5.265   -9.014  11.047  1.00 14.00 ? 7   TYR   A C   1 
ATOM   27   O  O   . TYR   A 1 7   ? 4.953   -10.156 11.390  1.00 17.04 ? 7   TYR   A O   1 
ATOM   28   C  CB  . TYR   A 1 7   ? 2.932   -8.105  11.179  1.00 10.96 ? 7   TYR   A CB  1 
ATOM   29   C  CG  . TYR   A 1 7   ? 2.024   -7.038  11.753  1.00 9.58  ? 7   TYR   A CG  1 
ATOM   30   C  CD1 . TYR   A 1 7   ? 1.653   -7.069  13.089  1.00 9.46  ? 7   TYR   A CD1 1 
ATOM   31   C  CD2 . TYR   A 1 7   ? 1.530   -6.027  10.978  1.00 9.80  ? 7   TYR   A CD2 1 
ATOM   32   C  CE1 . TYR   A 1 7   ? 0.807   -6.106  13.610  1.00 8.93  ? 7   TYR   A CE1 1 
ATOM   33   C  CE2 . TYR   A 1 7   ? 0.704   -5.063  11.498  1.00 9.73  ? 7   TYR   A CE2 1 
ATOM   34   C  CZ  . TYR   A 1 7   ? 0.314   -5.117  12.811  1.00 9.12  ? 7   TYR   A CZ  1 
ATOM   35   O  OH  . TYR   A 1 7   ? -0.526  -4.148  13.255  1.00 10.10 ? 7   TYR   A OH  1 
ATOM   36   N  N   . GLY   A 1 8   ? 6.402   -8.781  10.423  1.00 15.78 ? 8   GLY   A N   1 
ATOM   37   C  CA  . GLY   A 1 8   ? 7.344   -9.828  10.057  1.00 17.97 ? 8   GLY   A CA  1 
ATOM   38   C  C   . GLY   A 1 8   ? 8.266   -10.205 11.230  1.00 19.06 ? 8   GLY   A C   1 
ATOM   39   O  O   . GLY   A 1 8   ? 8.338   -9.571  12.280  1.00 20.29 ? 8   GLY   A O   1 
ATOM   40   N  N   . LYS   A 1 9   ? 9.161   -11.153 10.973  1.00 22.08 ? 9   LYS   A N   1 
ATOM   41   C  CA  . LYS   A 1 9   ? 10.130  -11.613 11.981  1.00 23.88 ? 9   LYS   A CA  1 
ATOM   42   C  C   . LYS   A 1 9   ? 11.114  -10.512 12.338  1.00 21.99 ? 9   LYS   A C   1 
ATOM   43   O  O   . LYS   A 1 9   ? 11.596  -10.367 13.475  1.00 21.05 ? 9   LYS   A O   1 
ATOM   44   C  CB  . LYS   A 1 9   ? 10.993  -12.778 11.472  1.00 25.13 ? 9   LYS   A CB  1 
ATOM   45   N  N   . HIS   A 1 10  ? 11.430  -9.735  11.307  1.00 19.05 ? 10  HIS   A N   1 
ATOM   46   C  CA  . HIS   A 1 10  ? 12.488  -8.788  11.507  1.00 19.85 ? 10  HIS   A CA  1 
ATOM   47   C  C   . HIS   A 1 10  ? 11.984  -7.396  11.884  1.00 16.88 ? 10  HIS   A C   1 
ATOM   48   O  O   . HIS   A 1 10  ? 12.788  -6.507  12.159  1.00 20.11 ? 10  HIS   A O   1 
ATOM   49   C  CB  . HIS   A 1 10  ? 13.386  -8.815  10.279  1.00 20.95 ? 10  HIS   A CB  1 
ATOM   50   C  CG  . HIS   A 1 10  ? 13.964  -10.179 10.048  1.00 25.07 ? 10  HIS   A CG  1 
ATOM   51   N  ND1 . HIS   A 1 10  ? 14.956  -10.663 10.868  1.00 27.75 ? 10  HIS   A ND1 1 
ATOM   52   C  CD2 . HIS   A 1 10  ? 13.730  -11.141 9.134   1.00 29.17 ? 10  HIS   A CD2 1 
ATOM   53   C  CE1 . HIS   A 1 10  ? 15.304  -11.881 10.471  1.00 25.21 ? 10  HIS   A CE1 1 
ATOM   54   N  NE2 . HIS   A 1 10  ? 14.560  -12.200 9.412   1.00 29.89 ? 10  HIS   A NE2 1 
ATOM   55   N  N   . ASN   A 1 11  ? 10.668  -7.145  11.831  1.00 15.55 ? 11  ASN   A N   1 
ATOM   56   C  CA  . ASN   A 1 11  ? 10.147  -5.795  12.065  1.00 14.09 ? 11  ASN   A CA  1 
ATOM   57   C  C   . ASN   A 1 11  ? 8.834   -5.801  12.863  1.00 12.81 ? 11  ASN   A C   1 
ATOM   58   O  O   . ASN   A 1 11  ? 8.157   -4.795  12.929  1.00 12.71 ? 11  ASN   A O   1 
ATOM   59   C  CB  . ASN   A 1 11  ? 9.962   -5.035  10.763  1.00 15.04 ? 11  ASN   A CB  1 
ATOM   60   C  CG  . ASN   A 1 11  ? 8.894   -5.624  9.878   1.00 15.40 ? 11  ASN   A CG  1 
ATOM   61   O  OD1 . ASN   A 1 11  ? 8.345   -6.677  10.157  1.00 17.02 ? 11  ASN   A OD1 1 
ATOM   62   N  ND2 . ASN   A 1 11  ? 8.572   -4.922  8.816   1.00 17.60 ? 11  ASN   A ND2 1 
ATOM   63   N  N   . GLY   A 1 12  ? 8.542   -6.941  13.462  1.00 13.06 ? 12  GLY   A N   1 
ATOM   64   C  CA  . GLY   A 1 12  ? 7.273   -7.150  14.140  1.00 12.45 ? 12  GLY   A CA  1 
ATOM   65   C  C   . GLY   A 1 12  ? 7.269   -6.611  15.561  1.00 11.14 ? 12  GLY   A C   1 
ATOM   66   O  O   . GLY   A 1 12  ? 8.163   -5.906  16.018  1.00 11.46 ? 12  GLY   A O   1 
ATOM   67   N  N   . PRO   A 1 13  ? 6.178   -6.907  16.290  1.00 10.66 ? 13  PRO   A N   1 
ATOM   68   C  CA  . PRO   A 1 13  ? 5.927   -6.330  17.605  1.00 11.05 ? 13  PRO   A CA  1 
ATOM   69   C  C   . PRO   A 1 13  ? 7.082   -6.363  18.576  1.00 10.57 ? 13  PRO   A C   1 
ATOM   70   O  O   . PRO   A 1 13  ? 7.174   -5.445  19.381  1.00 11.20 ? 13  PRO   A O   1 
ATOM   71   C  CB  . PRO   A 1 13  ? 4.706   -7.108  18.106  1.00 11.49 ? 13  PRO   A CB  1 
ATOM   72   C  CG  . PRO   A 1 13  ? 3.948   -7.408  16.845  1.00 11.96 ? 13  PRO   A CG  1 
ATOM   73   C  CD  . PRO   A 1 13  ? 5.012   -7.692  15.816  1.00 12.02 ? 13  PRO   A CD  1 
ATOM   74   N  N   . GLU   A 1 14  ? 7.947   -7.391  18.549  1.00 11.65 ? 14  GLU   A N   1 
ATOM   75   C  CA  . GLU   A 1 14  ? 9.067   -7.440  19.493  1.00 13.00 ? 14  GLU   A CA  1 
ATOM   76   C  C   . GLU   A 1 14  ? 10.159  -6.422  19.174  1.00 11.75 ? 14  GLU   A C   1 
ATOM   77   O  O   . GLU   A 1 14  ? 11.058  -6.211  20.016  1.00 13.97 ? 14  GLU   A O   1 
ATOM   78   C  CB  . GLU   A 1 14  ? 9.675   -8.838  19.526  1.00 17.05 ? 14  GLU   A CB  1 
ATOM   79   C  CG  . GLU   A 1 14  ? 8.687   -9.922  19.930  1.00 22.21 ? 14  GLU   A CG  1 
ATOM   80   N  N   . HIS   A 1 15  ? 10.123  -5.824  17.983  1.00 11.00 ? 15  HIS   A N   1 
ATOM   81   C  CA  . HIS   A 1 15  ? 11.110  -4.856  17.568  1.00 10.74 ? 15  HIS   A CA  1 
ATOM   82   C  C   . HIS   A 1 15  ? 10.627  -3.426  17.741  1.00 9.92  ? 15  HIS   A C   1 
ATOM   83   O  O   . HIS   A 1 15  ? 11.443  -2.505  17.691  1.00 10.46 ? 15  HIS   A O   1 
ATOM   84   C  CB  . HIS   A 1 15  ? 11.449  -5.042  16.097  1.00 11.34 ? 15  HIS   A CB  1 
ATOM   85   C  CG  . HIS   A 1 15  ? 12.193  -6.280  15.817  1.00 13.35 ? 15  HIS   A CG  1 
ATOM   86   N  ND1 . HIS   A 1 15  ? 13.576  -6.319  15.880  1.00 15.66 ? 15  HIS   A ND1 1 
ATOM   87   C  CD2 . HIS   A 1 15  ? 11.750  -7.488  15.419  1.00 15.67 ? 15  HIS   A CD2 1 
ATOM   88   C  CE1 . HIS   A 1 15  ? 13.953  -7.524  15.556  1.00 18.84 ? 15  HIS   A CE1 1 
ATOM   89   N  NE2 . HIS   A 1 15  ? 12.880  -8.273  15.272  1.00 18.10 ? 15  HIS   A NE2 1 
ATOM   90   N  N   . TRP   A 1 16  ? 9.312   -3.195  17.896  1.00 9.70  ? 16  TRP   A N   1 
ATOM   91   C  CA  . TRP   A 1 16  ? 8.762   -1.851  17.816  1.00 9.18  ? 16  TRP   A CA  1 
ATOM   92   C  C   . TRP   A 1 16  ? 9.365   -0.891  18.846  1.00 9.39  ? 16  TRP   A C   1 
ATOM   93   O  O   . TRP   A 1 16  ? 9.483   0.296   18.555  1.00 9.74  ? 16  TRP   A O   1 
ATOM   94   C  CB  . TRP   A 1 16  ? 7.235   -1.895  17.952  1.00 9.14  ? 16  TRP   A CB  1 
ATOM   95   C  CG  . TRP   A 1 16  ? 6.534   -2.613  16.829  1.00 8.68  ? 16  TRP   A CG  1 
ATOM   96   C  CD1 . TRP   A 1 16  ? 7.045   -3.032  15.638  1.00 9.69  ? 16  TRP   A CD1 1 
ATOM   97   C  CD2 . TRP   A 1 16  ? 5.129   -2.895  16.791  1.00 8.36  ? 16  TRP   A CD2 1 
ATOM   98   N  NE1 . TRP   A 1 16  ? 6.064   -3.610  14.874  1.00 9.74  ? 16  TRP   A NE1 1 
ATOM   99   C  CE2 . TRP   A 1 16  ? 4.860   -3.526  15.560  1.00 8.84  ? 16  TRP   A CE2 1 
ATOM   100  C  CE3 . TRP   A 1 16  ? 4.085   -2.730  17.692  1.00 8.69  ? 16  TRP   A CE3 1 
ATOM   101  C  CZ2 . TRP   A 1 16  ? 3.592   -3.978  15.211  1.00 9.05  ? 16  TRP   A CZ2 1 
ATOM   102  C  CZ3 . TRP   A 1 16  ? 2.814   -3.142  17.336  1.00 9.02  ? 16  TRP   A CZ3 1 
ATOM   103  C  CH2 . TRP   A 1 16  ? 2.581   -3.751  16.118  1.00 8.97  ? 16  TRP   A CH2 1 
ATOM   104  N  N   . HIS   A 1 17  ? 9.690   -1.415  20.024  1.00 9.36  ? 17  HIS   A N   1 
ATOM   105  C  CA  . HIS   A 1 17  ? 10.187  -0.567  21.079  1.00 10.07 ? 17  HIS   A CA  1 
ATOM   106  C  C   . HIS   A 1 17  ? 11.449  0.205   20.713  1.00 10.39 ? 17  HIS   A C   1 
ATOM   107  O  O   . HIS   A 1 17  ? 11.720  1.237   21.314  1.00 11.24 ? 17  HIS   A O   1 
ATOM   108  C  CB  . HIS   A 1 17  ? 10.487  -1.375  22.347  1.00 10.76 ? 17  HIS   A CB  1 
ATOM   109  C  CG  . HIS   A 1 17  ? 11.665  -2.283  22.243  1.00 11.34 ? 17  HIS   A CG  1 
ATOM   110  N  ND1 . HIS   A 1 17  ? 12.874  -1.894  22.803  1.00 13.46 ? 17  HIS   A ND1 1 
ATOM   111  C  CD2 . HIS   A 1 17  ? 11.821  -3.448  21.623  1.00 12.69 ? 17  HIS   A CD2 1 
ATOM   112  C  CE1 . HIS   A 1 17  ? 13.747  -2.847  22.524  1.00 14.07 ? 17  HIS   A CE1 1 
ATOM   113  N  NE2 . HIS   A 1 17  ? 13.160  -3.796  21.814  1.00 13.98 ? 17  HIS   A NE2 1 
ATOM   114  N  N   . LYS   A 1 18  ? 12.236  -0.287  19.742  1.00 10.07 ? 18  LYS   A N   1 
ATOM   115  C  CA  . LYS   A 1 18  ? 13.465  0.405   19.377  1.00 11.22 ? 18  LYS   A CA  1 
ATOM   116  C  C   . LYS   A 1 18  ? 13.212  1.746   18.708  1.00 11.96 ? 18  LYS   A C   1 
ATOM   117  O  O   . LYS   A 1 18  ? 14.042  2.642   18.799  1.00 16.04 ? 18  LYS   A O   1 
ATOM   118  C  CB  . LYS   A 1 18  ? 14.337  -0.485  18.486  1.00 11.62 ? 18  LYS   A CB  1 
ATOM   119  C  CG  . LYS   A 1 18  ? 14.902  -1.681  19.224  1.00 12.63 ? 18  LYS   A CG  1 
ATOM   120  C  CD  . LYS   A 1 18  ? 15.681  -2.599  18.365  1.00 12.57 ? 18  LYS   A CD  1 
ATOM   121  C  CE  . LYS   A 1 18  ? 14.766  -3.545  17.633  1.00 12.88 ? 18  LYS   A CE  1 
ATOM   122  N  NZ  . LYS   A 1 18  ? 15.422  -4.329  16.573  1.00 12.89 ? 18  LYS   A NZ  1 
ATOM   123  N  N   . ASP   A 1 19  ? 12.128  1.873   17.958  1.00 11.23 ? 19  ASP   A N   1 
ATOM   124  C  CA  . ASP   A 1 19  ? 11.729  3.146   17.386  1.00 11.82 ? 19  ASP   A CA  1 
ATOM   125  C  C   . ASP   A 1 19  ? 10.640  3.845   18.165  1.00 11.35 ? 19  ASP   A C   1 
ATOM   126  O  O   . ASP   A 1 19  ? 10.500  5.051   18.018  1.00 13.06 ? 19  ASP   A O   1 
ATOM   127  C  CB  . ASP   A 1 19  ? 11.358  3.004   15.914  1.00 13.64 ? 19  ASP   A CB  1 
ATOM   128  C  CG  . ASP   A 1 19  ? 12.613  2.799   15.075  1.00 16.38 ? 19  ASP   A CG  1 
ATOM   129  O  OD1 . ASP   A 1 19  ? 13.349  3.781   14.822  1.00 18.71 ? 19  ASP   A OD1 1 
ATOM   130  O  OD2 . ASP   A 1 19  ? 13.005  1.605   14.956  1.00 21.23 ? 19  ASP   A OD2 1 
ATOM   131  N  N   . PHE   A 1 20  ? 9.883   3.110   18.968  1.00 10.20 ? 20  PHE   A N   1 
ATOM   132  C  CA  . PHE   A 1 20  ? 8.714   3.614   19.674  1.00 10.17 ? 20  PHE   A CA  1 
ATOM   133  C  C   . PHE   A 1 20  ? 8.812   3.147   21.117  1.00 10.63 ? 20  PHE   A C   1 
ATOM   134  O  O   . PHE   A 1 20  ? 8.170   2.158   21.496  1.00 10.59 ? 20  PHE   A O   1 
ATOM   135  C  CB  . PHE   A 1 20  ? 7.416   3.140   19.019  1.00 10.51 ? 20  PHE   A CB  1 
ATOM   136  C  CG  . PHE   A 1 20  ? 7.339   3.501   17.559  1.00 10.81 ? 20  PHE   A CG  1 
ATOM   137  C  CD1 . PHE   A 1 20  ? 6.917   4.755   17.147  1.00 12.51 ? 20  PHE   A CD1 1 
ATOM   138  C  CD2 . PHE   A 1 20  ? 7.755   2.610   16.573  1.00 11.46 ? 20  PHE   A CD2 1 
ATOM   139  C  CE1 . PHE   A 1 20  ? 6.930   5.108   15.806  1.00 13.13 ? 20  PHE   A CE1 1 
ATOM   140  C  CE2 . PHE   A 1 20  ? 7.762   2.968   15.237  1.00 12.70 ? 20  PHE   A CE2 1 
ATOM   141  C  CZ  . PHE   A 1 20  ? 7.329   4.208   14.862  1.00 13.19 ? 20  PHE   A CZ  1 
ATOM   142  N  N   . PRO   A 1 21  ? 9.668   3.781   21.937  1.00 11.18 ? 21  PRO   A N   1 
ATOM   143  C  CA  . PRO   A 1 21  ? 9.918   3.244   23.269  1.00 11.51 ? 21  PRO   A CA  1 
ATOM   144  C  C   . PRO   A 1 21  ? 8.677   3.144   24.168  1.00 10.76 ? 21  PRO   A C   1 
ATOM   145  O  O   . PRO   A 1 21  ? 8.708   2.386   25.130  1.00 11.66 ? 21  PRO   A O   1 
ATOM   146  C  CB  . PRO   A 1 21  ? 10.975  4.187   23.864  1.00 14.62 ? 21  PRO   A CB  1 
ATOM   147  C  CG  . PRO   A 1 21  ? 10.906  5.400   22.984  1.00 17.48 ? 21  PRO   A CG  1 
ATOM   148  C  CD  . PRO   A 1 21  ? 10.560  4.893   21.597  1.00 13.56 ? 21  PRO   A CD  1 
ATOM   149  N  N   . ILE   A 1 22  ? 7.632   3.912   23.868  1.00 10.31 ? 22  ILE   A N   1 
ATOM   150  C  CA  . ILE   A 1 22  ? 6.364   3.813   24.596  1.00 9.91  ? 22  ILE   A CA  1 
ATOM   151  C  C   . ILE   A 1 22  ? 5.774   2.406   24.475  1.00 9.97  ? 22  ILE   A C   1 
ATOM   152  O  O   . ILE   A 1 22  ? 4.871   2.070   25.228  1.00 10.58 ? 22  ILE   A O   1 
ATOM   153  C  CB  . ILE   A 1 22  ? 5.388   4.910   24.134  1.00 10.86 ? 22  ILE   A CB  1 
ATOM   154  C  CG1 A ILE   A 1 22  ? 4.315   5.206   25.184  0.50 11.00 ? 22  ILE   A CG1 1 
ATOM   155  C  CG1 B ILE   A 1 22  ? 4.293   5.192   25.167  0.50 12.32 ? 22  ILE   A CG1 1 
ATOM   156  C  CG2 . ILE   A 1 22  ? 4.773   4.541   22.795  1.00 11.13 ? 22  ILE   A CG2 1 
ATOM   157  C  CD1 A ILE   A 1 22  ? 3.430   6.368   24.808  0.50 11.04 ? 22  ILE   A CD1 1 
ATOM   158  C  CD1 B ILE   A 1 22  ? 4.782   5.799   26.437  0.50 14.68 ? 22  ILE   A CD1 1 
ATOM   159  N  N   . ALA   A 1 23  ? 6.289   1.575   23.544  1.00 10.08 ? 23  ALA   A N   1 
ATOM   160  C  CA  . ALA   A 1 23  ? 5.851   0.183   23.452  1.00 9.79  ? 23  ALA   A CA  1 
ATOM   161  C  C   . ALA   A 1 23  ? 5.949   -0.537  24.790  1.00 10.37 ? 23  ALA   A C   1 
ATOM   162  O  O   . ALA   A 1 23  ? 5.239   -1.526  24.971  1.00 11.26 ? 23  ALA   A O   1 
ATOM   163  C  CB  . ALA   A 1 23  ? 6.686   -0.558  22.437  1.00 10.29 ? 23  ALA   A CB  1 
ATOM   164  N  N   . LYS   A 1 24  ? 6.854   -0.087  25.677  1.00 11.22 ? 24  LYS   A N   1 
ATOM   165  C  CA  . LYS   A 1 24  ? 7.035   -0.697  26.997  1.00 12.05 ? 24  LYS   A CA  1 
ATOM   166  C  C   . LYS   A 1 24  ? 6.405   0.178   28.086  1.00 13.05 ? 24  LYS   A C   1 
ATOM   167  O  O   . LYS   A 1 24  ? 6.788   0.095   29.250  1.00 14.96 ? 24  LYS   A O   1 
ATOM   168  C  CB  . LYS   A 1 24  ? 8.519   -0.965  27.284  1.00 14.33 ? 24  LYS   A CB  1 
ATOM   169  C  CG  . LYS   A 1 24  ? 9.158   -1.936  26.307  1.00 16.29 ? 24  LYS   A CG  1 
ATOM   170  C  CD  . LYS   A 1 24  ? 10.579  -2.272  26.647  1.00 19.54 ? 24  LYS   A CD  1 
ATOM   171  C  CE  A LYS   A 1 24  ? 11.141  -3.321  25.708  0.50 21.82 ? 24  LYS   A CE  1 
ATOM   172  C  CE  B LYS   A 1 24  ? 11.290  -3.246  25.735  0.50 21.55 ? 24  LYS   A CE  1 
ATOM   173  N  NZ  A LYS   A 1 24  ? 12.261  -4.063  26.312  0.50 23.90 ? 24  LYS   A NZ  1 
ATOM   174  N  NZ  B LYS   A 1 24  ? 10.934  -4.640  26.025  0.50 23.32 ? 24  LYS   A NZ  1 
ATOM   175  N  N   . GLY   A 1 25  ? 5.429   1.008   27.719  1.00 12.38 ? 25  GLY   A N   1 
ATOM   176  C  CA  . GLY   A 1 25  ? 4.801   1.964   28.622  1.00 13.25 ? 25  GLY   A CA  1 
ATOM   177  C  C   . GLY   A 1 25  ? 3.808   1.354   29.603  1.00 12.18 ? 25  GLY   A C   1 
ATOM   178  O  O   . GLY   A 1 25  ? 3.657   0.137   29.719  1.00 13.06 ? 25  GLY   A O   1 
ATOM   179  N  N   . GLU   A 1 26  ? 3.175   2.263   30.336  1.00 12.16 ? 26  GLU   A N   1 
ATOM   180  C  CA  . GLU   A 1 26  ? 2.312   1.917   31.445  1.00 13.00 ? 26  GLU   A CA  1 
ATOM   181  C  C   . GLU   A 1 26  ? 0.890   1.617   31.052  1.00 11.96 ? 26  GLU   A C   1 
ATOM   182  O  O   . GLU   A 1 26  ? 0.131   1.141   31.887  1.00 12.81 ? 26  GLU   A O   1 
ATOM   183  C  CB  . GLU   A 1 26  ? 2.352   3.051   32.487  1.00 15.54 ? 26  GLU   A CB  1 
ATOM   184  C  CG  . GLU   A 1 26  ? 3.736   3.258   33.065  1.00 18.87 ? 26  GLU   A CG  1 
ATOM   185  C  CD  . GLU   A 1 26  ? 4.301   1.996   33.710  1.00 24.03 ? 26  GLU   A CD  1 
ATOM   186  O  OE1 . GLU   A 1 26  ? 5.398   1.564   33.308  1.00 33.58 ? 26  GLU   A OE1 1 
ATOM   187  O  OE2 . GLU   A 1 26  ? 3.606   1.381   34.553  1.00 29.12 ? 26  GLU   A OE2 1 
ATOM   188  N  N   . ARG   A 1 27  ? 0.471   1.943   29.826  1.00 10.15 ? 27  ARG   A N   1 
ATOM   189  C  CA  . ARG   A 1 27  ? -0.918  1.710   29.453  1.00 9.81  ? 27  ARG   A CA  1 
ATOM   190  C  C   . ARG   A 1 27  ? -0.999  1.242   27.990  1.00 9.03  ? 27  ARG   A C   1 
ATOM   191  O  O   . ARG   A 1 27  ? -1.722  1.837   27.186  1.00 9.23  ? 27  ARG   A O   1 
ATOM   192  C  CB  . ARG   A 1 27  ? -1.854  2.882   29.765  1.00 12.17 ? 27  ARG   A CB  1 
ATOM   193  C  CG  . ARG   A 1 27  ? -1.491  4.229   29.196  1.00 13.03 ? 27  ARG   A CG  1 
ATOM   194  C  CD  . ARG   A 1 27  ? -2.502  5.380   29.392  1.00 14.51 ? 27  ARG   A CD  1 
ATOM   195  N  NE  . ARG   A 1 27  ? -3.655  5.271   28.483  1.00 12.87 ? 27  ARG   A NE  1 
ATOM   196  C  CZ  . ARG   A 1 27  ? -4.578  6.211   28.407  1.00 11.84 ? 27  ARG   A CZ  1 
ATOM   197  N  NH1 . ARG   A 1 27  ? -4.573  7.305   29.167  1.00 13.81 ? 27  ARG   A NH1 1 
ATOM   198  N  NH2 . ARG   A 1 27  ? -5.504  6.037   27.524  1.00 13.34 ? 27  ARG   A NH2 1 
ATOM   199  N  N   . GLN   A 1 28  ? -0.267  0.172   27.684  1.00 8.53  ? 28  GLN   A N   1 
ATOM   200  C  CA  . GLN   A 1 28  ? -0.260  -0.353  26.326  1.00 7.83  ? 28  GLN   A CA  1 
ATOM   201  C  C   . GLN   A 1 28  ? -1.406  -1.318  26.058  1.00 7.91  ? 28  GLN   A C   1 
ATOM   202  O  O   . GLN   A 1 28  ? -1.916  -1.982  26.954  1.00 8.98  ? 28  GLN   A O   1 
ATOM   203  C  CB  . GLN   A 1 28  ? 1.105   -1.022  26.081  1.00 8.38  ? 28  GLN   A CB  1 
ATOM   204  C  CG  . GLN   A 1 28  ? 2.239   -0.005  25.969  1.00 8.82  ? 28  GLN   A CG  1 
ATOM   205  C  CD  . GLN   A 1 28  ? 2.100   0.795   24.690  1.00 8.61  ? 28  GLN   A CD  1 
ATOM   206  O  OE1 . GLN   A 1 28  ? 2.300   0.249   23.594  1.00 8.77  ? 28  GLN   A OE1 1 
ATOM   207  N  NE2 . GLN   A 1 28  ? 1.773   2.074   24.789  1.00 8.44  ? 28  GLN   A NE2 1 
ATOM   208  N  N   . SER   A 1 29  ? -1.775  -1.397  24.787  1.00 7.52  ? 29  SER   A N   1 
ATOM   209  C  CA  . SER   A 1 29  ? -2.833  -2.274  24.305  1.00 7.23  ? 29  SER   A CA  1 
ATOM   210  C  C   . SER   A 1 29  ? -2.287  -3.154  23.199  1.00 6.95  ? 29  SER   A C   1 
ATOM   211  O  O   . SER   A 1 29  ? -1.351  -2.789  22.501  1.00 8.02  ? 29  SER   A O   1 
ATOM   212  C  CB  . SER   A 1 29  ? -3.976  -1.430  23.774  1.00 7.14  ? 29  SER   A CB  1 
ATOM   213  O  OG  . SER   A 1 29  ? -4.594  -0.689  24.825  1.00 7.75  ? 29  SER   A OG  1 
ATOM   214  N  N   . PRO   A 1 30  ? -2.941  -4.277  22.917  1.00 7.03  ? 30  PRO   A N   1 
ATOM   215  C  CA  . PRO   A 1 30  ? -4.106  -4.838  23.617  1.00 7.24  ? 30  PRO   A CA  1 
ATOM   216  C  C   . PRO   A 1 30  ? -3.693  -5.493  24.925  1.00 7.33  ? 30  PRO   A C   1 
ATOM   217  O  O   . PRO   A 1 30  ? -2.511  -5.531  25.266  1.00 8.24  ? 30  PRO   A O   1 
ATOM   218  C  CB  . PRO   A 1 30  ? -4.632  -5.859  22.619  1.00 7.83  ? 30  PRO   A CB  1 
ATOM   219  C  CG  . PRO   A 1 30  ? -3.347  -6.415  22.018  1.00 7.86  ? 30  PRO   A CG  1 
ATOM   220  C  CD  . PRO   A 1 30  ? -2.477  -5.191  21.871  1.00 7.68  ? 30  PRO   A CD  1 
ATOM   221  N  N   . VAL   A 1 31  ? -4.684  -6.030  25.620  1.00 7.77  ? 31  VAL   A N   1 
ATOM   222  C  CA  . VAL   A 1 31  ? -4.507  -6.773  26.871  1.00 7.97  ? 31  VAL   A CA  1 
ATOM   223  C  C   . VAL   A 1 31  ? -5.378  -8.014  26.800  1.00 8.23  ? 31  VAL   A C   1 
ATOM   224  O  O   . VAL   A 1 31  ? -6.355  -8.088  26.044  1.00 8.67  ? 31  VAL   A O   1 
ATOM   225  C  CB  . VAL   A 1 31  ? -4.849  -5.928  28.108  1.00 8.68  ? 31  VAL   A CB  1 
ATOM   226  C  CG1 . VAL   A 1 31  ? -3.926  -4.721  28.223  1.00 9.72  ? 31  VAL   A CG1 1 
ATOM   227  C  CG2 . VAL   A 1 31  ? -6.326  -5.528  28.143  1.00 9.53  ? 31  VAL   A CG2 1 
ATOM   228  N  N   . ASP   A 1 32  ? -5.059  -8.984  27.664  1.00 8.50  ? 32  ASP   A N   1 
ATOM   229  C  CA  . ASP   A 1 32  ? -5.961  -10.055 27.976  1.00 8.60  ? 32  ASP   A CA  1 
ATOM   230  C  C   . ASP   A 1 32  ? -7.021  -9.567  28.957  1.00 8.78  ? 32  ASP   A C   1 
ATOM   231  O  O   . ASP   A 1 32  ? -6.704  -8.882  29.943  1.00 10.91 ? 32  ASP   A O   1 
ATOM   232  C  CB  . ASP   A 1 32  ? -5.219  -11.233 28.575  1.00 9.81  ? 32  ASP   A CB  1 
ATOM   233  C  CG  . ASP   A 1 32  ? -6.147  -12.395 28.869  1.00 10.78 ? 32  ASP   A CG  1 
ATOM   234  O  OD1 . ASP   A 1 32  ? -6.849  -12.855 27.951  1.00 10.36 ? 32  ASP   A OD1 1 
ATOM   235  O  OD2 . ASP   A 1 32  ? -6.189  -12.834 30.084  1.00 13.51 ? 32  ASP   A OD2 1 
ATOM   236  N  N   . ILE   A 1 33  ? -8.267  -9.859  28.648  1.00 8.85  ? 33  ILE   A N   1 
ATOM   237  C  CA  . ILE   A 1 33  ? -9.392  -9.533  29.490  1.00 9.47  ? 33  ILE   A CA  1 
ATOM   238  C  C   . ILE   A 1 33  ? -9.698  -10.766 30.326  1.00 9.96  ? 33  ILE   A C   1 
ATOM   239  O  O   . ILE   A 1 33  ? -10.241 -11.743 29.843  1.00 10.61 ? 33  ILE   A O   1 
ATOM   240  C  CB  . ILE   A 1 33  ? -10.581 -9.090  28.661  1.00 9.82  ? 33  ILE   A CB  1 
ATOM   241  C  CG1 . ILE   A 1 33  ? -10.253 -7.882  27.830  1.00 10.75 ? 33  ILE   A CG1 1 
ATOM   242  C  CG2 . ILE   A 1 33  ? -11.787 -8.835  29.570  1.00 11.50 ? 33  ILE   A CG2 1 
ATOM   243  C  CD1 . ILE   A 1 33  ? -11.272 -7.588  26.726  1.00 11.73 ? 33  ILE   A CD1 1 
ATOM   244  N  N   . ASP   A 1 34  ? -9.313  -10.718 31.612  1.00 11.48 ? 34  ASP   A N   1 
ATOM   245  C  CA  . ASP   A 1 34  ? -9.592  -11.768 32.552  1.00 11.79 ? 34  ASP   A CA  1 
ATOM   246  C  C   . ASP   A 1 34  ? -11.000 -11.491 33.073  1.00 11.59 ? 34  ASP   A C   1 
ATOM   247  O  O   . ASP   A 1 34  ? -11.223 -10.563 33.847  1.00 13.58 ? 34  ASP   A O   1 
ATOM   248  C  CB  . ASP   A 1 34  ? -8.527  -11.817 33.636  1.00 13.65 ? 34  ASP   A CB  1 
ATOM   249  C  CG  A ASP   A 1 34  ? -8.697  -13.055 34.507  0.50 14.78 ? 34  ASP   A CG  1 
ATOM   250  C  CG  B ASP   A 1 34  ? -8.798  -12.784 34.790  0.50 15.18 ? 34  ASP   A CG  1 
ATOM   251  O  OD1 A ASP   A 1 34  ? -8.261  -14.152 34.099  0.50 15.64 ? 34  ASP   A OD1 1 
ATOM   252  O  OD1 B ASP   A 1 34  ? -9.962  -13.203 34.974  0.50 14.46 ? 34  ASP   A OD1 1 
ATOM   253  O  OD2 A ASP   A 1 34  ? -9.265  -12.912 35.572  0.50 17.41 ? 34  ASP   A OD2 1 
ATOM   254  O  OD2 B ASP   A 1 34  ? -7.843  -13.047 35.562  0.50 18.25 ? 34  ASP   A OD2 1 
ATOM   255  N  N   . THR   A 1 35  ? -11.962 -12.275 32.631  1.00 12.38 ? 35  THR   A N   1 
ATOM   256  C  CA  . THR   A 1 35  ? -13.360 -12.004 32.849  1.00 13.08 ? 35  THR   A CA  1 
ATOM   257  C  C   . THR   A 1 35  ? -13.736 -12.140 34.294  1.00 13.32 ? 35  THR   A C   1 
ATOM   258  O  O   . THR   A 1 35  ? -14.652 -11.454 34.743  1.00 16.08 ? 35  THR   A O   1 
ATOM   259  C  CB  . THR   A 1 35  ? -14.259 -12.902 32.008  1.00 14.87 ? 35  THR   A CB  1 
ATOM   260  O  OG1 . THR   A 1 35  ? -14.142 -14.237 32.454  1.00 15.93 ? 35  THR   A OG1 1 
ATOM   261  C  CG2 . THR   A 1 35  ? -13.973 -12.756 30.531  1.00 16.80 ? 35  THR   A CG2 1 
ATOM   262  N  N   A HIS   A 1 36  ? -13.223 -13.155 34.966  0.50 11.50 ? 36  HIS   A N   1 
ATOM   263  N  N   B HIS   A 1 36  ? -12.876 -12.788 35.145  0.50 13.10 ? 36  HIS   A N   1 
ATOM   264  C  CA  A HIS   A 1 36  ? -13.453 -13.202 36.388  0.50 12.83 ? 36  HIS   A CA  1 
ATOM   265  C  CA  B HIS   A 1 36  ? -13.198 -13.055 36.548  0.50 15.39 ? 36  HIS   A CA  1 
ATOM   266  C  C   A HIS   A 1 36  ? -12.867 -12.049 37.234  0.50 13.91 ? 36  HIS   A C   1 
ATOM   267  C  C   B HIS   A 1 36  ? -12.806 -11.839 37.345  0.50 16.36 ? 36  HIS   A C   1 
ATOM   268  O  O   A HIS   A 1 36  ? -13.527 -11.897 38.274  0.50 15.03 ? 36  HIS   A O   1 
ATOM   269  O  O   B HIS   A 1 36  ? -13.397 -11.347 38.314  0.50 17.02 ? 36  HIS   A O   1 
ATOM   270  C  CB  A HIS   A 1 36  ? -13.079 -14.591 36.879  0.50 11.09 ? 36  HIS   A CB  1 
ATOM   271  C  CB  B HIS   A 1 36  ? -12.390 -14.262 37.031  0.50 16.80 ? 36  HIS   A CB  1 
ATOM   272  C  CG  A HIS   A 1 36  ? -13.940 -15.674 36.381  0.50 11.07 ? 36  HIS   A CG  1 
ATOM   273  C  CG  B HIS   A 1 36  ? -12.804 -15.440 36.241  0.50 18.92 ? 36  HIS   A CG  1 
ATOM   274  N  ND1 A HIS   A 1 36  ? -15.269 -15.770 36.751  0.50 13.07 ? 36  HIS   A ND1 1 
ATOM   275  N  ND1 B HIS   A 1 36  ? -11.985 -15.896 35.241  0.50 22.25 ? 36  HIS   A ND1 1 
ATOM   276  C  CD2 A HIS   A 1 36  ? -13.724 -16.654 35.469  0.50 13.05 ? 36  HIS   A CD2 1 
ATOM   277  C  CD2 B HIS   A 1 36  ? -13.934 -16.152 36.165  0.50 21.45 ? 36  HIS   A CD2 1 
ATOM   278  C  CE1 A HIS   A 1 36  ? -15.805 -16.808 36.138  0.50 14.50 ? 36  HIS   A CE1 1 
ATOM   279  C  CE1 B HIS   A 1 36  ? -12.577 -16.896 34.622  0.50 22.30 ? 36  HIS   A CE1 1 
ATOM   280  N  NE2 A HIS   A 1 36  ? -14.919 -17.340 35.356  0.50 13.98 ? 36  HIS   A NE2 1 
ATOM   281  N  NE2 B HIS   A 1 36  ? -13.756 -17.081 35.158  0.50 21.37 ? 36  HIS   A NE2 1 
ATOM   282  N  N   . THR   A 1 37  ? -11.727 -11.317 36.863  1.00 16.16 ? 37  THR   A N   1 
ATOM   283  C  CA  . THR   A 1 37  ? -11.108 -10.202 37.576  1.00 17.55 ? 37  THR   A CA  1 
ATOM   284  C  C   . THR   A 1 37  ? -11.694 -8.845  37.172  1.00 16.59 ? 37  THR   A C   1 
ATOM   285  O  O   . THR   A 1 37  ? -11.559 -7.885  37.910  1.00 19.26 ? 37  THR   A O   1 
ATOM   286  C  CB  . THR   A 1 37  ? -9.584  -10.182 37.350  1.00 23.39 ? 37  THR   A CB  1 
ATOM   287  O  OG1 . THR   A 1 37  ? -9.060  -11.365 37.945  1.00 30.56 ? 37  THR   A OG1 1 
ATOM   288  C  CG2 . THR   A 1 37  ? -8.869  -9.014  37.999  1.00 26.12 ? 37  THR   A CG2 1 
ATOM   289  N  N   . ALA   A 1 38  ? -12.333 -8.735  36.013  1.00 14.21 ? 38  ALA   A N   1 
ATOM   290  C  CA  . ALA   A 1 38  ? -12.967 -7.490  35.616  1.00 13.36 ? 38  ALA   A CA  1 
ATOM   291  C  C   . ALA   A 1 38  ? -14.057 -7.207  36.626  1.00 15.61 ? 38  ALA   A C   1 
ATOM   292  O  O   . ALA   A 1 38  ? -14.629 -8.102  37.182  1.00 20.19 ? 38  ALA   A O   1 
ATOM   293  C  CB  . ALA   A 1 38  ? -13.477 -7.548  34.214  1.00 13.97 ? 38  ALA   A CB  1 
ATOM   294  N  N   . LYS   A 1 39  ? -14.273 -5.988  36.952  1.00 15.28 ? 39  LYS   A N   1 
ATOM   295  C  CA  . LYS   A 1 39  ? -15.374 -5.758  37.886  1.00 18.13 ? 39  LYS   A CA  1 
ATOM   296  C  C   . LYS   A 1 39  ? -16.462 -4.906  37.291  1.00 13.93 ? 39  LYS   A C   1 
ATOM   297  O  O   . LYS   A 1 39  ? -16.265 -3.904  36.604  1.00 12.61 ? 39  LYS   A O   1 
ATOM   298  C  CB  . LYS   A 1 39  ? -14.893 -5.107  39.131  1.00 20.53 ? 39  LYS   A CB  1 
ATOM   299  C  CG  . LYS   A 1 39  ? -15.887 -5.055  40.285  1.00 21.26 ? 39  LYS   A CG  1 
ATOM   300  C  CD  . LYS   A 1 39  ? -15.238 -4.179  41.254  1.00 20.27 ? 39  LYS   A CD  1 
ATOM   301  C  CE  . LYS   A 1 39  ? -16.162 -3.430  42.139  1.00 24.95 ? 39  LYS   A CE  1 
ATOM   302  N  NZ  . LYS   A 1 39  ? -16.366 -4.278  43.289  1.00 27.34 ? 39  LYS   A NZ  1 
ATOM   303  N  N   . TYR   A 1 40  ? -17.659 -5.326  37.619  1.00 16.43 ? 40  TYR   A N   1 
ATOM   304  C  CA  . TYR   A 1 40  ? -18.848 -4.626  37.235  1.00 16.39 ? 40  TYR   A CA  1 
ATOM   305  C  C   . TYR   A 1 40  ? -18.811 -3.244  37.848  1.00 14.76 ? 40  TYR   A C   1 
ATOM   306  O  O   . TYR   A 1 40  ? -18.609 -3.095  39.077  1.00 16.49 ? 40  TYR   A O   1 
ATOM   307  C  CB  . TYR   A 1 40  ? -20.106 -5.355  37.695  1.00 19.83 ? 40  TYR   A CB  1 
ATOM   308  C  CG  . TYR   A 1 40  ? -21.384 -4.562  37.544  1.00 27.62 ? 40  TYR   A CG  1 
ATOM   309  C  CD1 . TYR   A 1 40  ? -21.843 -4.235  36.279  1.00 27.71 ? 40  TYR   A CD1 1 
ATOM   310  C  CD2 . TYR   A 1 40  ? -22.187 -4.239  38.648  1.00 35.48 ? 40  TYR   A CD2 1 
ATOM   311  C  CE1 . TYR   A 1 40  ? -23.031 -3.550  36.104  1.00 40.72 ? 40  TYR   A CE1 1 
ATOM   312  C  CE2 . TYR   A 1 40  ? -23.359 -3.543  38.458  1.00 45.14 ? 40  TYR   A CE2 1 
ATOM   313  C  CZ  . TYR   A 1 40  ? -23.775 -3.152  37.198  1.00 56.94 ? 40  TYR   A CZ  1 
ATOM   314  O  OH  . TYR   A 1 40  ? -24.993 -2.543  36.891  1.00 39.89 ? 40  TYR   A OH  1 
ATOM   315  N  N   . ASP   A 1 41  ? -19.103 -2.244  37.061  1.00 14.52 ? 41  ASP   A N   1 
ATOM   316  C  CA  . ASP   A 1 41  ? -19.101 -0.861  37.493  1.00 16.92 ? 41  ASP   A CA  1 
ATOM   317  C  C   . ASP   A 1 41  ? -20.505 -0.328  37.265  1.00 19.10 ? 41  ASP   A C   1 
ATOM   318  O  O   . ASP   A 1 41  ? -20.838 0.051   36.155  1.00 19.96 ? 41  ASP   A O   1 
ATOM   319  C  CB  . ASP   A 1 41  ? -18.039 -0.050  36.748  1.00 18.42 ? 41  ASP   A CB  1 
ATOM   320  C  CG  . ASP   A 1 41  ? -17.868 1.378   37.199  1.00 23.94 ? 41  ASP   A CG  1 
ATOM   321  O  OD1 . ASP   A 1 41  ? -18.727 1.841   37.952  1.00 28.82 ? 41  ASP   A OD1 1 
ATOM   322  O  OD2 . ASP   A 1 41  ? -16.896 2.007   36.735  1.00 29.55 ? 41  ASP   A OD2 1 
ATOM   323  N  N   . PRO   A 1 42  ? -21.394 -0.350  38.310  1.00 24.12 ? 42  PRO   A N   1 
ATOM   324  C  CA  . PRO   A 1 42  ? -22.822 -0.057  38.115  1.00 27.31 ? 42  PRO   A CA  1 
ATOM   325  C  C   . PRO   A 1 42  ? -23.032 1.376   37.691  1.00 29.15 ? 42  PRO   A C   1 
ATOM   326  O  O   . PRO   A 1 42  ? -24.120 1.742   37.237  1.00 36.30 ? 42  PRO   A O   1 
ATOM   327  C  CB  . PRO   A 1 42  ? -23.484 -0.282  39.484  1.00 32.63 ? 42  PRO   A CB  1 
ATOM   328  C  CG  . PRO   A 1 42  ? -22.329 -0.197  40.457  1.00 31.94 ? 42  PRO   A CG  1 
ATOM   329  C  CD  . PRO   A 1 42  ? -21.084 -0.667  39.719  1.00 26.85 ? 42  PRO   A CD  1 
ATOM   330  N  N   . SER   A 1 43  ? -22.031 2.231   37.904  1.00 26.13 ? 43  SER   A N   1 
ATOM   331  C  CA  . SER   A 1 43  ? -22.200 3.610   37.474  1.00 30.08 ? 43  SER   A CA  1 
ATOM   332  C  C   . SER   A 1 43  ? -21.905 3.817   35.975  1.00 27.40 ? 43  SER   A C   1 
ATOM   333  O  O   . SER   A 1 43  ? -22.213 4.893   35.476  1.00 32.85 ? 43  SER   A O   1 
ATOM   334  C  CB  . SER   A 1 43  ? -21.287 4.485   38.233  1.00 34.79 ? 43  SER   A CB  1 
ATOM   335  O  OG  . SER   A 1 43  ? -19.956 4.201   37.890  1.00 38.62 ? 43  SER   A OG  1 
ATOM   336  N  N   . LEU   A 1 44  ? -21.252 2.884   35.264  1.00 26.59 ? 44  LEU   A N   1 
ATOM   337  C  CA  . LEU   A 1 44  ? -21.041 3.025   33.822  1.00 24.57 ? 44  LEU   A CA  1 
ATOM   338  C  C   . LEU   A 1 44  ? -22.395 3.221   33.154  1.00 27.93 ? 44  LEU   A C   1 
ATOM   339  O  O   . LEU   A 1 44  ? -23.319 2.447   33.418  1.00 34.12 ? 44  LEU   A O   1 
ATOM   340  C  CB  . LEU   A 1 44  ? -20.380 1.797   33.222  1.00 20.21 ? 44  LEU   A CB  1 
ATOM   341  C  CG  . LEU   A 1 44  ? -18.888 1.688   33.446  1.00 16.76 ? 44  LEU   A CG  1 
ATOM   342  C  CD1 . LEU   A 1 44  ? -18.484 0.277   33.086  1.00 17.68 ? 44  LEU   A CD1 1 
ATOM   343  C  CD2 . LEU   A 1 44  ? -18.106 2.709   32.651  1.00 17.10 ? 44  LEU   A CD2 1 
ATOM   344  N  N   A LYS   A 1 45  ? -22.525 4.467   32.618  0.50 26.83 ? 45  LYS   A N   1 
ATOM   345  N  N   B LYS   A 1 45  ? -22.446 3.953   32.060  0.50 20.06 ? 45  LYS   A N   1 
ATOM   346  C  CA  A LYS   A 1 45  ? -23.788 5.020   32.156  0.50 23.31 ? 45  LYS   A CA  1 
ATOM   347  C  CA  B LYS   A 1 45  ? -23.687 4.069   31.312  0.50 17.40 ? 45  LYS   A CA  1 
ATOM   348  C  C   A LYS   A 1 45  ? -23.968 4.546   30.738  0.50 17.32 ? 45  LYS   A C   1 
ATOM   349  C  C   B LYS   A 1 45  ? -23.741 3.103   30.132  0.50 14.60 ? 45  LYS   A C   1 
ATOM   350  O  O   A LYS   A 1 45  ? -23.057 3.943   30.195  0.50 12.79 ? 45  LYS   A O   1 
ATOM   351  O  O   B LYS   A 1 45  ? -22.720 2.629   29.647  0.50 13.82 ? 45  LYS   A O   1 
ATOM   352  C  CB  A LYS   A 1 45  ? -23.932 6.545   32.229  0.50 29.43 ? 45  LYS   A CB  1 
ATOM   353  C  CB  B LYS   A 1 45  ? -23.795 5.530   30.831  0.50 30.00 ? 45  LYS   A CB  1 
ATOM   354  C  CG  A LYS   A 1 45  ? -23.163 7.358   31.208  0.50 33.94 ? 45  LYS   A CG  1 
ATOM   355  C  CG  B LYS   A 1 45  ? -23.969 6.542   31.954  0.50 30.00 ? 45  LYS   A CG  1 
ATOM   356  C  CD  A LYS   A 1 45  ? -22.642 8.675   31.798  0.50 38.96 ? 45  LYS   A CD  1 
ATOM   357  C  CD  B LYS   A 1 45  ? -24.075 7.957   31.412  0.50 30.00 ? 45  LYS   A CD  1 
ATOM   358  N  N   A PRO   A 1 46  ? -25.213 4.518   30.251  0.50 15.89 ? 46  PRO   A N   1 
ATOM   359  N  N   B PRO   A 1 46  ? -24.948 2.889   29.561  0.50 13.89 ? 46  PRO   A N   1 
ATOM   360  C  CA  A PRO   A 1 46  ? -25.499 3.745   29.050  0.50 15.55 ? 46  PRO   A CA  1 
ATOM   361  C  CA  B PRO   A 1 46  ? -25.033 2.228   28.272  0.50 13.85 ? 46  PRO   A CA  1 
ATOM   362  C  C   A PRO   A 1 46  ? -24.608 4.177   27.886  0.50 14.35 ? 46  PRO   A C   1 
ATOM   363  C  C   B PRO   A 1 46  ? -24.268 3.032   27.233  0.50 12.39 ? 46  PRO   A C   1 
ATOM   364  O  O   A PRO   A 1 46  ? -24.367 5.365   27.704  0.50 14.83 ? 46  PRO   A O   1 
ATOM   365  O  O   B PRO   A 1 46  ? -24.209 4.258   27.291  0.50 11.79 ? 46  PRO   A O   1 
ATOM   366  C  CB  A PRO   A 1 46  ? -26.951 4.114   28.766  0.50 16.40 ? 46  PRO   A CB  1 
ATOM   367  C  CB  B PRO   A 1 46  ? -26.532 2.201   27.912  0.50 14.65 ? 46  PRO   A CB  1 
ATOM   368  C  CG  A PRO   A 1 46  ? -27.514 4.485   30.129  0.50 17.85 ? 46  PRO   A CG  1 
ATOM   369  C  CG  B PRO   A 1 46  ? -27.209 3.082   28.919  0.50 17.97 ? 46  PRO   A CG  1 
ATOM   370  C  CD  A PRO   A 1 46  ? -26.386 5.179   30.845  0.50 17.84 ? 46  PRO   A CD  1 
ATOM   371  C  CD  B PRO   A 1 46  ? -26.258 3.289   30.085  0.50 14.93 ? 46  PRO   A CD  1 
ATOM   372  N  N   A LEU   A 1 47  ? -24.162 3.215   27.068  0.50 12.98 ? 47  LEU   A N   1 
ATOM   373  N  N   B LEU   A 1 47  ? -23.685 2.321   26.275  0.50 12.12 ? 47  LEU   A N   1 
ATOM   374  C  CA  A LEU   A 1 47  ? -23.371 3.501   25.872  0.50 12.92 ? 47  LEU   A CA  1 
ATOM   375  C  CA  B LEU   A 1 47  ? -23.083 2.963   25.129  0.50 11.91 ? 47  LEU   A CA  1 
ATOM   376  C  C   A LEU   A 1 47  ? -24.312 3.863   24.724  0.50 12.36 ? 47  LEU   A C   1 
ATOM   377  C  C   B LEU   A 1 47  ? -24.167 3.574   24.282  0.50 12.70 ? 47  LEU   A C   1 
ATOM   378  O  O   A LEU   A 1 47  ? -25.377 3.290   24.628  0.50 11.77 ? 47  LEU   A O   1 
ATOM   379  O  O   B LEU   A 1 47  ? -25.145 2.923   23.980  0.50 14.30 ? 47  LEU   A O   1 
ATOM   380  C  CB  A LEU   A 1 47  ? -22.542 2.261   25.501  0.50 13.16 ? 47  LEU   A CB  1 
ATOM   381  C  CB  B LEU   A 1 47  ? -22.378 1.943   24.252  0.50 14.59 ? 47  LEU   A CB  1 
ATOM   382  C  CG  A LEU   A 1 47  ? -21.556 2.459   24.336  0.50 13.76 ? 47  LEU   A CG  1 
ATOM   383  C  CG  B LEU   A 1 47  ? -21.123 1.318   24.798  0.50 17.46 ? 47  LEU   A CG  1 
ATOM   384  C  CD1 A LEU   A 1 47  ? -20.400 3.343   24.770  0.50 14.99 ? 47  LEU   A CD1 1 
ATOM   385  C  CD1 B LEU   A 1 47  ? -20.552 0.367   23.757  0.50 17.22 ? 47  LEU   A CD1 1 
ATOM   386  C  CD2 A LEU   A 1 47  ? -21.009 1.152   23.781  0.50 16.29 ? 47  LEU   A CD2 1 
ATOM   387  C  CD2 B LEU   A 1 47  ? -20.128 2.397   25.166  0.50 18.64 ? 47  LEU   A CD2 1 
ATOM   388  N  N   . SER   A 1 48  ? -23.889 4.778   23.834  1.00 12.18 ? 48  SER   A N   1 
ATOM   389  C  CA  . SER   A 1 48  ? -24.714 5.380   22.782  1.00 12.16 ? 48  SER   A CA  1 
ATOM   390  C  C   . SER   A 1 48  ? -23.913 5.352   21.493  1.00 12.52 ? 48  SER   A C   1 
ATOM   391  O  O   . SER   A 1 48  ? -22.935 6.097   21.365  1.00 13.25 ? 48  SER   A O   1 
ATOM   392  C  CB  . SER   A 1 48  ? -25.091 6.779   23.166  1.00 14.20 ? 48  SER   A CB  1 
ATOM   393  O  OG  . SER   A 1 48  ? -25.765 7.458   22.151  1.00 19.29 ? 48  SER   A OG  1 
ATOM   394  N  N   . VAL   A 1 49  ? -24.328 4.490   20.568  1.00 13.11 ? 49  VAL   A N   1 
ATOM   395  C  CA  . VAL   A 1 49  ? -23.746 4.426   19.247  1.00 13.96 ? 49  VAL   A CA  1 
ATOM   396  C  C   . VAL   A 1 49  ? -24.737 5.081   18.271  1.00 14.53 ? 49  VAL   A C   1 
ATOM   397  O  O   . VAL   A 1 49  ? -25.857 4.597   18.106  1.00 18.12 ? 49  VAL   A O   1 
ATOM   398  C  CB  . VAL   A 1 49  ? -23.473 2.958   18.878  1.00 16.85 ? 49  VAL   A CB  1 
ATOM   399  C  CG1 . VAL   A 1 49  ? -22.737 2.854   17.564  1.00 19.18 ? 49  VAL   A CG1 1 
ATOM   400  C  CG2 . VAL   A 1 49  ? -22.674 2.256   19.970  1.00 18.23 ? 49  VAL   A CG2 1 
ATOM   401  N  N   . SER   A 1 50  ? -24.371 6.213   17.689  1.00 14.09 ? 50  SER   A N   1 
ATOM   402  C  CA  . SER   A 1 50  ? -25.279 6.972   16.837  1.00 15.36 ? 50  SER   A CA  1 
ATOM   403  C  C   . SER   A 1 50  ? -24.673 7.065   15.455  1.00 14.03 ? 50  SER   A C   1 
ATOM   404  O  O   . SER   A 1 50  ? -23.946 8.000   15.186  1.00 14.23 ? 50  SER   A O   1 
ATOM   405  C  CB  . SER   A 1 50  ? -25.587 8.350   17.386  1.00 19.71 ? 50  SER   A CB  1 
ATOM   406  O  OG  . SER   A 1 50  ? -26.203 8.225   18.652  1.00 26.81 ? 50  SER   A OG  1 
ATOM   407  N  N   . TYR   A 1 51  ? -24.951 6.061   14.622  1.00 13.90 ? 51  TYR   A N   1 
ATOM   408  C  CA  . TYR   A 1 51  ? -24.357 5.947   13.309  1.00 13.73 ? 51  TYR   A CA  1 
ATOM   409  C  C   . TYR   A 1 51  ? -25.356 6.165   12.176  1.00 15.58 ? 51  TYR   A C   1 
ATOM   410  O  O   . TYR   A 1 51  ? -24.990 5.981   11.027  1.00 15.74 ? 51  TYR   A O   1 
ATOM   411  C  CB  . TYR   A 1 51  ? -23.707 4.581   13.151  1.00 14.59 ? 51  TYR   A CB  1 
ATOM   412  C  CG  . TYR   A 1 51  ? -22.440 4.269   13.952  1.00 12.40 ? 51  TYR   A CG  1 
ATOM   413  C  CD1 . TYR   A 1 51  ? -21.732 5.228   14.637  1.00 12.41 ? 51  TYR   A CD1 1 
ATOM   414  C  CD2 . TYR   A 1 51  ? -21.957 2.969   13.995  1.00 12.24 ? 51  TYR   A CD2 1 
ATOM   415  C  CE1 . TYR   A 1 51  ? -20.536 4.917   15.285  1.00 11.26 ? 51  TYR   A CE1 1 
ATOM   416  C  CE2 . TYR   A 1 51  ? -20.768 2.636   14.617  1.00 11.06 ? 51  TYR   A CE2 1 
ATOM   417  C  CZ  . TYR   A 1 51  ? -20.058 3.623   15.282  1.00 10.83 ? 51  TYR   A CZ  1 
ATOM   418  O  OH  . TYR   A 1 51  ? -18.897 3.243   15.914  1.00 11.27 ? 51  TYR   A OH  1 
ATOM   419  N  N   . ASP   A 1 52  ? -26.572 6.623   12.456  1.00 16.77 ? 52  ASP   A N   1 
ATOM   420  C  CA  . ASP   A 1 52  ? -27.570 6.791   11.400  1.00 18.61 ? 52  ASP   A CA  1 
ATOM   421  C  C   . ASP   A 1 52  ? -27.128 7.755   10.280  1.00 17.14 ? 52  ASP   A C   1 
ATOM   422  O  O   . ASP   A 1 52  ? -27.530 7.579   9.126   1.00 20.15 ? 52  ASP   A O   1 
ATOM   423  C  CB  . ASP   A 1 52  ? -28.923 7.170   12.008  1.00 21.49 ? 52  ASP   A CB  1 
ATOM   424  C  CG  . ASP   A 1 52  ? -28.771 8.191   13.120  1.00 27.51 ? 52  ASP   A CG  1 
ATOM   425  O  OD1 . ASP   A 1 52  ? -28.204 7.822   14.229  1.00 34.84 ? 52  ASP   A OD1 1 
ATOM   426  O  OD2 . ASP   A 1 52  ? -29.109 9.361   12.850  1.00 37.81 ? 52  ASP   A OD2 1 
ATOM   427  N  N   . GLN   A 1 53  ? -26.345 8.796   10.576  1.00 16.06 ? 53  GLN   A N   1 
ATOM   428  C  CA  . GLN   A 1 53  ? -25.968 9.771   9.543   1.00 16.55 ? 53  GLN   A CA  1 
ATOM   429  C  C   . GLN   A 1 53  ? -24.515 9.553   9.083   1.00 14.21 ? 53  GLN   A C   1 
ATOM   430  O  O   . GLN   A 1 53  ? -23.928 10.442  8.472   1.00 16.48 ? 53  GLN   A O   1 
ATOM   431  C  CB  . GLN   A 1 53  ? -26.143 11.195  10.062  1.00 20.49 ? 53  GLN   A CB  1 
ATOM   432  C  CG  . GLN   A 1 53  ? -27.618 11.546  10.233  1.00 25.05 ? 53  GLN   A CG  1 
ATOM   433  C  CD  . GLN   A 1 53  ? -28.287 11.728  8.892   1.00 30.95 ? 53  GLN   A CD  1 
ATOM   434  O  OE1 . GLN   A 1 53  ? -27.972 12.652  8.139   1.00 40.38 ? 53  GLN   A OE1 1 
ATOM   435  N  NE2 . GLN   A 1 53  ? -29.211 10.836  8.571   1.00 33.91 ? 53  GLN   A NE2 1 
ATOM   436  N  N   . ALA   A 1 54  ? -23.938 8.380   9.335   1.00 13.44 ? 54  ALA   A N   1 
ATOM   437  C  CA  . ALA   A 1 54  ? -22.579 8.091   8.919   1.00 13.01 ? 54  ALA   A CA  1 
ATOM   438  C  C   . ALA   A 1 54  ? -22.400 8.280   7.424   1.00 13.40 ? 54  ALA   A C   1 
ATOM   439  O  O   . ALA   A 1 54  ? -23.268 7.880   6.641   1.00 16.42 ? 54  ALA   A O   1 
ATOM   440  C  CB  . ALA   A 1 54  ? -22.186 6.697   9.327   1.00 15.17 ? 54  ALA   A CB  1 
ATOM   441  N  N   . THR   A 1 55  ? -21.274 8.866   7.058   1.00 12.20 ? 55  THR   A N   1 
ATOM   442  C  CA  . THR   A 1 55  ? -20.902 9.062   5.669   1.00 12.25 ? 55  THR   A CA  1 
ATOM   443  C  C   . THR   A 1 55  ? -19.562 8.424   5.409   1.00 9.73  ? 55  THR   A C   1 
ATOM   444  O  O   . THR   A 1 55  ? -18.527 9.016   5.667   1.00 10.51 ? 55  THR   A O   1 
ATOM   445  C  CB  . THR   A 1 55  ? -20.817 10.552  5.256   1.00 15.44 ? 55  THR   A CB  1 
ATOM   446  O  OG1 . THR   A 1 55  ? -22.068 11.199  5.355   1.00 19.64 ? 55  THR   A OG1 1 
ATOM   447  C  CG2 . THR   A 1 55  ? -20.345 10.735  3.833   1.00 17.96 ? 55  THR   A CG2 1 
ATOM   448  N  N   . SER   A 1 56  ? -19.563 7.184   4.904   1.00 9.73  ? 56  SER   A N   1 
ATOM   449  C  CA  . SER   A 1 56  ? -18.318 6.547   4.497   1.00 9.48  ? 56  SER   A CA  1 
ATOM   450  C  C   . SER   A 1 56  ? -17.860 7.192   3.207   1.00 9.87  ? 56  SER   A C   1 
ATOM   451  O  O   . SER   A 1 56  ? -18.681 7.657   2.401   1.00 11.32 ? 56  SER   A O   1 
ATOM   452  C  CB  . SER   A 1 56  ? -18.456 5.067   4.339   1.00 9.87  ? 56  SER   A CB  1 
ATOM   453  O  OG  . SER   A 1 56  ? -19.345 4.724   3.250   1.00 10.81 ? 56  SER   A OG  1 
ATOM   454  N  N   . LEU   A 1 57  ? -16.549 7.236   3.018   1.00 9.44  ? 57  LEU   A N   1 
ATOM   455  C  CA  . LEU   A 1 57  ? -16.003 7.866   1.819   1.00 10.36 ? 57  LEU   A CA  1 
ATOM   456  C  C   . LEU   A 1 57  ? -15.174 6.921   0.961   1.00 9.51  ? 57  LEU   A C   1 
ATOM   457  O  O   . LEU   A 1 57  ? -15.244 6.960   -0.274  1.00 10.74 ? 57  LEU   A O   1 
ATOM   458  C  CB  . LEU   A 1 57  ? -15.154 9.059   2.225   1.00 12.41 ? 57  LEU   A CB  1 
ATOM   459  C  CG  . LEU   A 1 57  ? -15.986 10.213  2.801   1.00 15.67 ? 57  LEU   A CG  1 
ATOM   460  C  CD1 . LEU   A 1 57  ? -15.090 11.326  3.253   1.00 17.48 ? 57  LEU   A CD1 1 
ATOM   461  C  CD2 . LEU   A 1 57  ? -16.980 10.803  1.791   1.00 18.03 ? 57  LEU   A CD2 1 
ATOM   462  N  N   . ARG   A 1 58  ? -14.282 6.158   1.571   1.00 9.62  ? 58  ARG   A N   1 
ATOM   463  C  CA  . ARG   A 1 58  ? -13.204 5.508   0.834   1.00 9.40  ? 58  ARG   A CA  1 
ATOM   464  C  C   . ARG   A 1 58  ? -12.718 4.325   1.644   1.00 8.81  ? 58  ARG   A C   1 
ATOM   465  O  O   . ARG   A 1 58  ? -12.887 4.283   2.863   1.00 9.32  ? 58  ARG   A O   1 
ATOM   466  C  CB  . ARG   A 1 58  ? -12.056 6.500   0.642   1.00 12.29 ? 58  ARG   A CB  1 
ATOM   467  C  CG  . ARG   A 1 58  ? -10.962 6.141   -0.288  1.00 15.03 ? 58  ARG   A CG  1 
ATOM   468  C  CD  . ARG   A 1 58  ? -9.956  7.275   -0.412  1.00 16.96 ? 58  ARG   A CD  1 
ATOM   469  N  NE  . ARG   A 1 58  ? -9.141  7.407   0.775   1.00 17.07 ? 58  ARG   A NE  1 
ATOM   470  C  CZ  . ARG   A 1 58  ? -7.832  7.613   0.771   1.00 15.18 ? 58  ARG   A CZ  1 
ATOM   471  N  NH1 . ARG   A 1 58  ? -7.179  7.515   1.908   1.00 15.90 ? 58  ARG   A NH1 1 
ATOM   472  N  NH2 . ARG   A 1 58  ? -7.172  7.782   -0.346  1.00 16.78 ? 58  ARG   A NH2 1 
ATOM   473  N  N   . ILE   A 1 59  ? -12.078 3.393   0.969   1.00 8.45  ? 59  ILE   A N   1 
ATOM   474  C  CA  . ILE   A 1 59  ? -11.401 2.267   1.589   1.00 8.61  ? 59  ILE   A CA  1 
ATOM   475  C  C   . ILE   A 1 59  ? -9.971  2.259   1.073   1.00 8.55  ? 59  ILE   A C   1 
ATOM   476  O  O   . ILE   A 1 59  ? -9.722  2.461   -0.117  1.00 10.26 ? 59  ILE   A O   1 
ATOM   477  C  CB  . ILE   A 1 59  ? -12.149 0.944   1.353   1.00 8.87  ? 59  ILE   A CB  1 
ATOM   478  C  CG1 . ILE   A 1 59  ? -11.608 -0.178  2.227   1.00 9.33  ? 59  ILE   A CG1 1 
ATOM   479  C  CG2 . ILE   A 1 59  ? -12.229 0.558   -0.116  1.00 9.63  ? 59  ILE   A CG2 1 
ATOM   480  C  CD1 . ILE   A 1 59  ? -12.420 -1.439  2.188   1.00 10.01 ? 59  ILE   A CD1 1 
ATOM   481  N  N   . LEU   A 1 60  ? -9.008  2.078   1.991   1.00 8.79  ? 60  LEU   A N   1 
ATOM   482  C  CA  . LEU   A 1 60  ? -7.592  2.229   1.710   1.00 9.07  ? 60  LEU   A CA  1 
ATOM   483  C  C   . LEU   A 1 60  ? -6.813  1.038   2.275   1.00 8.35  ? 60  LEU   A C   1 
ATOM   484  O  O   . LEU   A 1 60  ? -6.966  0.708   3.440   1.00 8.94  ? 60  LEU   A O   1 
ATOM   485  C  CB  . LEU   A 1 60  ? -7.055  3.516   2.414   1.00 10.37 ? 60  LEU   A CB  1 
ATOM   486  C  CG  . LEU   A 1 60  ? -5.535  3.707   2.373   1.00 11.11 ? 60  LEU   A CG  1 
ATOM   487  C  CD1 . LEU   A 1 60  ? -5.021  3.977   0.980   1.00 12.23 ? 60  LEU   A CD1 1 
ATOM   488  C  CD2 . LEU   A 1 60  ? -5.112  4.801   3.353   1.00 12.69 ? 60  LEU   A CD2 1 
ATOM   489  N  N   . ASN   A 1 61  ? -5.944  0.429   1.465   1.00 8.40  ? 61  ASN   A N   1 
ATOM   490  C  CA  . ASN   A 1 61  ? -4.947  -0.524  1.953   1.00 8.49  ? 61  ASN   A CA  1 
ATOM   491  C  C   . ASN   A 1 61  ? -3.712  0.303   2.318   1.00 8.46  ? 61  ASN   A C   1 
ATOM   492  O  O   . ASN   A 1 61  ? -3.074  0.894   1.461   1.00 9.90  ? 61  ASN   A O   1 
ATOM   493  C  CB  . ASN   A 1 61  ? -4.597  -1.549  0.883   1.00 8.78  ? 61  ASN   A CB  1 
ATOM   494  C  CG  . ASN   A 1 61  ? -3.543  -2.538  1.311   1.00 8.89  ? 61  ASN   A CG  1 
ATOM   495  O  OD1 . ASN   A 1 61  ? -2.705  -2.242  2.161   1.00 9.50  ? 61  ASN   A OD1 1 
ATOM   496  N  ND2 . ASN   A 1 61  ? -3.559  -3.708  0.722   1.00 9.61  ? 61  ASN   A ND2 1 
ATOM   497  N  N   . ASN   A 1 62  ? -3.416  0.400   3.619   1.00 8.74  ? 62  ASN   A N   1 
ATOM   498  C  CA  . ASN   A 1 62  ? -2.313  1.235   4.079   1.00 9.81  ? 62  ASN   A CA  1 
ATOM   499  C  C   . ASN   A 1 62  ? -1.049  0.420   4.336   1.00 9.78  ? 62  ASN   A C   1 
ATOM   500  O  O   . ASN   A 1 62  ? -0.082  0.960   4.874   1.00 12.10 ? 62  ASN   A O   1 
ATOM   501  C  CB  . ASN   A 1 62  ? -2.687  2.060   5.314   1.00 10.39 ? 62  ASN   A CB  1 
ATOM   502  C  CG  . ASN   A 1 62  ? -3.030  1.200   6.490   1.00 10.29 ? 62  ASN   A CG  1 
ATOM   503  O  OD1 . ASN   A 1 62  ? -2.660  0.030   6.576   1.00 10.16 ? 62  ASN   A OD1 1 
ATOM   504  N  ND2 . ASN   A 1 62  ? -3.816  1.742   7.396   1.00 13.76 ? 62  ASN   A ND2 1 
ATOM   505  N  N   . GLY   A 1 63  ? -1.003  -0.834  3.917   1.00 9.58  ? 63  GLY   A N   1 
ATOM   506  C  CA  . GLY   A 1 63  ? 0.153   -1.683  4.122   1.00 10.21 ? 63  GLY   A CA  1 
ATOM   507  C  C   . GLY   A 1 63  ? 0.193   -2.428  5.436   1.00 10.06 ? 63  GLY   A C   1 
ATOM   508  O  O   . GLY   A 1 63  ? 1.059   -3.289  5.622   1.00 11.51 ? 63  GLY   A O   1 
ATOM   509  N  N   A HIS   A 1 64  ? -0.719  -2.081  6.349   0.50 9.61  ? 64  HIS   A N   1 
ATOM   510  N  N   B HIS   A 1 64  ? -0.739  -2.151  6.342   0.50 9.71  ? 64  HIS   A N   1 
ATOM   511  C  CA  A HIS   A 1 64  ? -0.854  -2.721  7.668   0.50 9.77  ? 64  HIS   A CA  1 
ATOM   512  C  CA  B HIS   A 1 64  ? -0.829  -2.927  7.587   0.50 9.90  ? 64  HIS   A CA  1 
ATOM   513  C  C   A HIS   A 1 64  ? -2.193  -3.464  7.766   0.50 9.62  ? 64  HIS   A C   1 
ATOM   514  C  C   B HIS   A 1 64  ? -2.246  -3.368  7.943   0.50 8.82  ? 64  HIS   A C   1 
ATOM   515  O  O   A HIS   A 1 64  ? -2.259  -4.627  8.199   0.50 10.61 ? 64  HIS   A O   1 
ATOM   516  O  O   B HIS   A 1 64  ? -2.401  -4.252  8.780   0.50 8.13  ? 64  HIS   A O   1 
ATOM   517  C  CB  A HIS   A 1 64  ? -0.615  -1.677  8.786   0.50 9.88  ? 64  HIS   A CB  1 
ATOM   518  C  CB  B HIS   A 1 64  ? -0.259  -2.201  8.821   0.50 11.43 ? 64  HIS   A CB  1 
ATOM   519  C  CG  A HIS   A 1 64  ? 0.740   -1.065  8.604   0.50 11.78 ? 64  HIS   A CG  1 
ATOM   520  C  CG  B HIS   A 1 64  ? -0.618  -0.758  9.022   0.50 14.32 ? 64  HIS   A CG  1 
ATOM   521  N  ND1 A HIS   A 1 64  ? 1.017   0.249   8.332   0.50 15.28 ? 64  HIS   A ND1 1 
ATOM   522  N  ND1 B HIS   A 1 64  ? 0.042   0.328   8.481   0.50 17.02 ? 64  HIS   A ND1 1 
ATOM   523  C  CD2 A HIS   A 1 64  ? 1.913   -1.684  8.708   0.50 11.99 ? 64  HIS   A CD2 1 
ATOM   524  C  CD2 B HIS   A 1 64  ? -1.538  -0.223  9.862   0.50 17.32 ? 64  HIS   A CD2 1 
ATOM   525  C  CE1 A HIS   A 1 64  ? 2.336   0.407   8.248   0.50 13.41 ? 64  HIS   A CE1 1 
ATOM   526  C  CE1 B HIS   A 1 64  ? -0.534  1.450   8.899   0.50 18.79 ? 64  HIS   A CE1 1 
ATOM   527  N  NE2 A HIS   A 1 64  ? 2.908   -0.741  8.511   0.50 14.32 ? 64  HIS   A NE2 1 
ATOM   528  N  NE2 B HIS   A 1 64  ? -1.452  1.140   9.779   0.50 19.91 ? 64  HIS   A NE2 1 
ATOM   529  N  N   . ALA   A 1 65  ? -3.248  -2.800  7.274   1.00 9.10  ? 65  ALA   A N   1 
ATOM   530  C  CA  . ALA   A 1 65  ? -4.624  -3.231  7.310   1.00 8.70  ? 65  ALA   A CA  1 
ATOM   531  C  C   . ALA   A 1 65  ? -5.344  -2.495  6.184   1.00 8.43  ? 65  ALA   A C   1 
ATOM   532  O  O   . ALA   A 1 65  ? -4.685  -1.846  5.364   1.00 9.94  ? 65  ALA   A O   1 
ATOM   533  C  CB  . ALA   A 1 65  ? -5.250  -2.980  8.675   1.00 9.85  ? 65  ALA   A CB  1 
ATOM   534  N  N   . PHE   A 1 66  ? -6.650  -2.560  6.140   1.00 8.55  ? 66  PHE   A N   1 
ATOM   535  C  CA  . PHE   A 1 66  ? -7.423  -1.650  5.315   1.00 8.75  ? 66  PHE   A CA  1 
ATOM   536  C  C   . PHE   A 1 66  ? -8.336  -0.829  6.199   1.00 8.48  ? 66  PHE   A C   1 
ATOM   537  O  O   . PHE   A 1 66  ? -8.946  -1.322  7.147   1.00 8.96  ? 66  PHE   A O   1 
ATOM   538  C  CB  . PHE   A 1 66  ? -8.191  -2.380  4.207   1.00 10.16 ? 66  PHE   A CB  1 
ATOM   539  C  CG  . PHE   A 1 66  ? -9.245  -3.345  4.678   1.00 9.98  ? 66  PHE   A CG  1 
ATOM   540  C  CD1 . PHE   A 1 66  ? -10.515 -2.889  5.001   1.00 10.53 ? 66  PHE   A CD1 1 
ATOM   541  C  CD2 . PHE   A 1 66  ? -8.980  -4.686  4.848   1.00 10.25 ? 66  PHE   A CD2 1 
ATOM   542  C  CE1 . PHE   A 1 66  ? -11.471 -3.737  5.470   1.00 11.49 ? 66  PHE   A CE1 1 
ATOM   543  C  CE2 . PHE   A 1 66  ? -9.961  -5.557  5.334   1.00 11.62 ? 66  PHE   A CE2 1 
ATOM   544  C  CZ  . PHE   A 1 66  ? -11.219 -5.067  5.640   1.00 11.29 ? 66  PHE   A CZ  1 
ATOM   545  N  N   . ASN   A 1 67  ? -8.432  0.452   5.860   1.00 8.26  ? 67  ASN   A N   1 
ATOM   546  C  CA  . ASN   A 1 67  ? -9.292  1.365   6.605   1.00 8.19  ? 67  ASN   A CA  1 
ATOM   547  C  C   . ASN   A 1 67  ? -10.484 1.781   5.759   1.00 7.97  ? 67  ASN   A C   1 
ATOM   548  O  O   . ASN   A 1 67  ? -10.292 2.208   4.608   1.00 8.94  ? 67  ASN   A O   1 
ATOM   549  C  CB  . ASN   A 1 67  ? -8.559  2.636   6.996   1.00 9.24  ? 67  ASN   A CB  1 
ATOM   550  C  CG  . ASN   A 1 67  ? -7.480  2.421   8.020   1.00 10.74 ? 67  ASN   A CG  1 
ATOM   551  O  OD1 . ASN   A 1 67  ? -7.361  1.366   8.611   1.00 12.23 ? 67  ASN   A OD1 1 
ATOM   552  N  ND2 . ASN   A 1 67  ? -6.739  3.472   8.278   1.00 14.15 ? 67  ASN   A ND2 1 
ATOM   553  N  N   . VAL   A 1 68  ? -11.677 1.685   6.324   1.00 7.41  ? 68  VAL   A N   1 
ATOM   554  C  CA  . VAL   A 1 68  ? -12.870 2.338   5.782   1.00 7.69  ? 68  VAL   A CA  1 
ATOM   555  C  C   . VAL   A 1 68  ? -12.970 3.684   6.469   1.00 7.92  ? 68  VAL   A C   1 
ATOM   556  O  O   . VAL   A 1 68  ? -13.128 3.744   7.695   1.00 8.11  ? 68  VAL   A O   1 
ATOM   557  C  CB  . VAL   A 1 68  ? -14.117 1.487   5.959   1.00 8.35  ? 68  VAL   A CB  1 
ATOM   558  C  CG1 . VAL   A 1 68  ? -15.338 2.277   5.511   1.00 9.68  ? 68  VAL   A CG1 1 
ATOM   559  C  CG2 . VAL   A 1 68  ? -14.019 0.197   5.174   1.00 9.20  ? 68  VAL   A CG2 1 
ATOM   560  N  N   . GLU   A 1 69  ? -12.884 4.749   5.693   1.00 8.22  ? 69  GLU   A N   1 
ATOM   561  C  CA  . GLU   A 1 69  ? -12.797 6.105   6.189   1.00 8.64  ? 69  GLU   A CA  1 
ATOM   562  C  C   . GLU   A 1 69  ? -14.134 6.823   6.094   1.00 8.83  ? 69  GLU   A C   1 
ATOM   563  O  O   . GLU   A 1 69  ? -14.888 6.573   5.129   1.00 10.11 ? 69  GLU   A O   1 
ATOM   564  C  CB  . GLU   A 1 69  ? -11.794 6.870   5.361   1.00 10.20 ? 69  GLU   A CB  1 
ATOM   565  C  CG  . GLU   A 1 69  ? -10.397 6.280   5.399   1.00 11.79 ? 69  GLU   A CG  1 
ATOM   566  C  CD  . GLU   A 1 69  ? -9.504  6.820   4.303   1.00 14.65 ? 69  GLU   A CD  1 
ATOM   567  O  OE1 . GLU   A 1 69  ? -10.016 7.537   3.376   1.00 16.24 ? 69  GLU   A OE1 1 
ATOM   568  O  OE2 . GLU   A 1 69  ? -8.313  6.510   4.335   1.00 17.38 ? 69  GLU   A OE2 1 
ATOM   569  N  N   . PHE   A 1 70  ? -14.391 7.691   7.064   1.00 8.64  ? 70  PHE   A N   1 
ATOM   570  C  CA  . PHE   A 1 70  ? -15.632 8.418   7.172   1.00 8.71  ? 70  PHE   A CA  1 
ATOM   571  C  C   . PHE   A 1 70  ? -15.392 9.920   7.133   1.00 9.61  ? 70  PHE   A C   1 
ATOM   572  O  O   . PHE   A 1 70  ? -14.325 10.415  7.500   1.00 10.61 ? 70  PHE   A O   1 
ATOM   573  C  CB  . PHE   A 1 70  ? -16.349 8.065   8.463   1.00 9.17  ? 70  PHE   A CB  1 
ATOM   574  C  CG  . PHE   A 1 70  ? -16.895 6.656   8.462   1.00 8.66  ? 70  PHE   A CG  1 
ATOM   575  C  CD1 . PHE   A 1 70  ? -16.091 5.565   8.661   1.00 9.31  ? 70  PHE   A CD1 1 
ATOM   576  C  CD2 . PHE   A 1 70  ? -18.229 6.428   8.138   1.00 9.06  ? 70  PHE   A CD2 1 
ATOM   577  C  CE1 . PHE   A 1 70  ? -16.582 4.289   8.500   1.00 10.01 ? 70  PHE   A CE1 1 
ATOM   578  C  CE2 . PHE   A 1 70  ? -18.733 5.145   7.982   1.00 9.71  ? 70  PHE   A CE2 1 
ATOM   579  C  CZ  . PHE   A 1 70  ? -17.896 4.072   8.183   1.00 10.11 ? 70  PHE   A CZ  1 
ATOM   580  N  N   . ASP   A 1 71  ? -16.418 10.667  6.738   1.00 10.48 ? 71  ASP   A N   1 
ATOM   581  C  CA  . ASP   A 1 71  ? -16.430 12.113  6.905   1.00 11.38 ? 71  ASP   A CA  1 
ATOM   582  C  C   . ASP   A 1 71  ? -16.570 12.454  8.379   1.00 11.52 ? 71  ASP   A C   1 
ATOM   583  O  O   . ASP   A 1 71  ? -17.627 12.193  8.997   1.00 14.08 ? 71  ASP   A O   1 
ATOM   584  C  CB  . ASP   A 1 71  ? -17.577 12.734  6.156   1.00 12.83 ? 71  ASP   A CB  1 
ATOM   585  C  CG  . ASP   A 1 71  ? -17.712 14.234  6.359   1.00 13.77 ? 71  ASP   A CG  1 
ATOM   586  O  OD1 . ASP   A 1 71  ? -16.787 14.856  6.892   1.00 15.32 ? 71  ASP   A OD1 1 
ATOM   587  O  OD2 . ASP   A 1 71  ? -18.748 14.781  5.936   1.00 17.43 ? 71  ASP   A OD2 1 
ATOM   588  N  N   . ASP   A 1 72  ? -15.528 12.978  8.982   1.00 11.71 ? 72  ASP   A N   1 
ATOM   589  C  CA  . ASP   A 1 72  ? -15.545 13.348  10.390  1.00 11.88 ? 72  ASP   A CA  1 
ATOM   590  C  C   . ASP   A 1 72  ? -15.450 14.874  10.561  1.00 13.71 ? 72  ASP   A C   1 
ATOM   591  O  O   . ASP   A 1 72  ? -14.945 15.334  11.582  1.00 15.88 ? 72  ASP   A O   1 
ATOM   592  C  CB  . ASP   A 1 72  ? -14.405 12.656  11.153  1.00 12.46 ? 72  ASP   A CB  1 
ATOM   593  C  CG  . ASP   A 1 72  ? -13.029 13.123  10.714  1.00 13.75 ? 72  ASP   A CG  1 
ATOM   594  O  OD1 . ASP   A 1 72  ? -12.945 13.801  9.638   1.00 16.90 ? 72  ASP   A OD1 1 
ATOM   595  O  OD2 . ASP   A 1 72  ? -12.050 12.821  11.404  1.00 15.30 ? 72  ASP   A OD2 1 
ATOM   596  N  N   . SER   A 1 73  ? -15.926 15.614  9.559   1.00 13.64 ? 73  SER   A N   1 
ATOM   597  C  CA  . SER   A 1 73  ? -15.920 17.078  9.643   1.00 14.74 ? 73  SER   A CA  1 
ATOM   598  C  C   . SER   A 1 73  ? -17.197 17.642  10.309  1.00 15.23 ? 73  SER   A C   1 
ATOM   599  O  O   . SER   A 1 73  ? -17.340 18.860  10.404  1.00 17.57 ? 73  SER   A O   1 
ATOM   600  C  CB  . SER   A 1 73  ? -15.667 17.690  8.310   1.00 16.57 ? 73  SER   A CB  1 
ATOM   601  O  OG  . SER   A 1 73  ? -16.787 17.507  7.477   1.00 16.07 ? 73  SER   A OG  1 
ATOM   602  N  N   . GLN   A 1 74  ? -18.140 16.785  10.705  1.00 16.03 ? 74  GLN   A N   1 
ATOM   603  C  CA  . GLN   A 1 74  ? -19.342 17.103  11.469  1.00 17.15 ? 74  GLN   A CA  1 
ATOM   604  C  C   . GLN   A 1 74  ? -19.689 15.923  12.344  1.00 16.54 ? 74  GLN   A C   1 
ATOM   605  O  O   . GLN   A 1 74  ? -19.190 14.869  12.056  1.00 16.28 ? 74  GLN   A O   1 
ATOM   606  C  CB  . GLN   A 1 74  ? -20.549 17.307  10.546  1.00 19.04 ? 74  GLN   A CB  1 
ATOM   607  C  CG  . GLN   A 1 74  ? -20.415 18.524  9.665   1.00 19.78 ? 74  GLN   A CG  1 
ATOM   608  C  CD  . GLN   A 1 74  ? -21.718 18.704  8.944   1.00 22.02 ? 74  GLN   A CD  1 
ATOM   609  O  OE1 . GLN   A 1 74  ? -22.660 19.270  9.491   1.00 24.30 ? 74  GLN   A OE1 1 
ATOM   610  N  NE2 . GLN   A 1 74  ? -21.776 18.217  7.727   1.00 20.79 ? 74  GLN   A NE2 1 
ATOM   611  N  N   . ASP   A 1 75  ? -20.601 16.098  13.318  1.00 18.96 ? 75  ASP   A N   1 
ATOM   612  C  CA  . ASP   A 1 75  ? -21.051 15.006  14.160  1.00 19.12 ? 75  ASP   A CA  1 
ATOM   613  C  C   . ASP   A 1 75  ? -22.098 14.190  13.414  1.00 20.94 ? 75  ASP   A C   1 
ATOM   614  O  O   . ASP   A 1 75  ? -23.288 14.488  13.481  1.00 33.19 ? 75  ASP   A O   1 
ATOM   615  C  CB  . ASP   A 1 75  ? -21.656 15.546  15.459  1.00 22.54 ? 75  ASP   A CB  1 
ATOM   616  C  CG  . ASP   A 1 75  ? -20.651 16.030  16.486  1.00 23.14 ? 75  ASP   A CG  1 
ATOM   617  O  OD1 . ASP   A 1 75  ? -19.487 15.718  16.366  1.00 28.46 ? 75  ASP   A OD1 1 
ATOM   618  O  OD2 . ASP   A 1 75  ? -21.071 16.679  17.442  1.00 29.71 ? 75  ASP   A OD2 1 
ATOM   619  N  N   . LYS   A 1 76  ? -21.614 13.312  12.577  1.00 17.53 ? 76  LYS   A N   1 
ATOM   620  C  CA  . LYS   A 1 76  ? -22.448 12.426  11.773  1.00 16.99 ? 76  LYS   A CA  1 
ATOM   621  C  C   . LYS   A 1 76  ? -22.563 11.008  12.328  1.00 16.66 ? 76  LYS   A C   1 
ATOM   622  O  O   . LYS   A 1 76  ? -23.538 10.302  12.067  1.00 20.48 ? 76  LYS   A O   1 
ATOM   623  C  CB  . LYS   A 1 76  ? -21.834 12.312  10.379  1.00 18.84 ? 76  LYS   A CB  1 
ATOM   624  C  CG  . LYS   A 1 76  ? -22.084 13.552  9.548   1.00 20.63 ? 76  LYS   A CG  1 
ATOM   625  C  CD  . LYS   A 1 76  ? -21.565 13.309  8.163   1.00 22.20 ? 76  LYS   A CD  1 
ATOM   626  C  CE  . LYS   A 1 76  ? -21.937 14.412  7.205   1.00 23.64 ? 76  LYS   A CE  1 
ATOM   627  N  NZ  . LYS   A 1 76  ? -21.522 14.059  5.834   1.00 23.20 ? 76  LYS   A NZ  1 
ATOM   628  N  N   . ALA   A 1 77  ? -21.500 10.477  12.839  1.00 16.00 ? 77  ALA   A N   1 
ATOM   629  C  CA  . ALA   A 1 77  ? -21.449 9.131   13.400  1.00 13.05 ? 77  ALA   A CA  1 
ATOM   630  C  C   . ALA   A 1 77  ? -20.652 9.286   14.675  1.00 12.83 ? 77  ALA   A C   1 
ATOM   631  O  O   . ALA   A 1 77  ? -19.454 9.571   14.603  1.00 15.01 ? 77  ALA   A O   1 
ATOM   632  C  CB  . ALA   A 1 77  ? -20.779 8.208   12.418  1.00 15.24 ? 77  ALA   A CB  1 
ATOM   633  N  N   . VAL   A 1 78  ? -21.301 9.156   15.818  1.00 12.16 ? 78  VAL   A N   1 
ATOM   634  C  CA  . VAL   A 1 78  ? -20.665 9.451   17.075  1.00 12.64 ? 78  VAL   A CA  1 
ATOM   635  C  C   . VAL   A 1 78  ? -20.930 8.358   18.098  1.00 12.18 ? 78  VAL   A C   1 
ATOM   636  O  O   . VAL   A 1 78  ? -21.940 7.668   18.094  1.00 14.25 ? 78  VAL   A O   1 
ATOM   637  C  CB  . VAL   A 1 78  ? -21.056 10.814  17.648  1.00 15.60 ? 78  VAL   A CB  1 
ATOM   638  C  CG1 . VAL   A 1 78  ? -20.727 11.959  16.707  1.00 15.46 ? 78  VAL   A CG1 1 
ATOM   639  C  CG2 . VAL   A 1 78  ? -22.497 10.840  17.998  1.00 17.50 ? 78  VAL   A CG2 1 
ATOM   640  N  N   . LEU   A 1 79  ? -19.985 8.265   19.017  1.00 10.96 ? 79  LEU   A N   1 
ATOM   641  C  CA  . LEU   A 1 79  ? -20.025 7.410   20.171  1.00 11.33 ? 79  LEU   A CA  1 
ATOM   642  C  C   . LEU   A 1 79  ? -20.015 8.295   21.406  1.00 11.31 ? 79  LEU   A C   1 
ATOM   643  O  O   . LEU   A 1 79  ? -19.221 9.233   21.502  1.00 12.70 ? 79  LEU   A O   1 
ATOM   644  C  CB  . LEU   A 1 79  ? -18.790 6.500   20.095  1.00 12.01 ? 79  LEU   A CB  1 
ATOM   645  C  CG  . LEU   A 1 79  ? -18.682 5.448   21.187  1.00 12.78 ? 79  LEU   A CG  1 
ATOM   646  C  CD1 . LEU   A 1 79  ? -19.783 4.454   21.064  1.00 14.72 ? 79  LEU   A CD1 1 
ATOM   647  C  CD2 . LEU   A 1 79  ? -17.316 4.768   21.078  1.00 13.55 ? 79  LEU   A CD2 1 
ATOM   648  N  N   . LYS   A 1 80  ? -20.910 7.994   22.343  1.00 11.57 ? 80  LYS   A N   1 
ATOM   649  C  CA  . LYS   A 1 80  ? -21.054 8.721   23.573  1.00 12.71 ? 80  LYS   A CA  1 
ATOM   650  C  C   . LYS   A 1 80  ? -21.453 7.737   24.651  1.00 12.01 ? 80  LYS   A C   1 
ATOM   651  O  O   . LYS   A 1 80  ? -21.751 6.589   24.390  1.00 12.15 ? 80  LYS   A O   1 
ATOM   652  C  CB  . LYS   A 1 80  ? -22.178 9.774   23.462  1.00 16.87 ? 80  LYS   A CB  1 
ATOM   653  C  CG  . LYS   A 1 80  ? -22.030 10.845  22.400  1.00 19.02 ? 80  LYS   A CG  1 
ATOM   654  C  CD  . LYS   A 1 80  ? -23.214 11.794  22.378  1.00 22.13 ? 80  LYS   A CD  1 
ATOM   655  N  N   . GLY   A 1 81  ? -21.475 8.218   25.885  1.00 13.20 ? 81  GLY   A N   1 
ATOM   656  C  CA  . GLY   A 1 81  ? -21.934 7.416   26.991  1.00 14.16 ? 81  GLY   A CA  1 
ATOM   657  C  C   . GLY   A 1 81  ? -20.905 6.373   27.386  1.00 13.43 ? 81  GLY   A C   1 
ATOM   658  O  O   . GLY   A 1 81  ? -19.702 6.529   27.170  1.00 12.68 ? 81  GLY   A O   1 
ATOM   659  N  N   . GLY   A 1 82  ? -21.356 5.369   28.127  1.00 15.60 ? 82  GLY   A N   1 
ATOM   660  C  CA  . GLY   A 1 82  ? -20.421 4.411   28.672  1.00 16.82 ? 82  GLY   A CA  1 
ATOM   661  C  C   . GLY   A 1 82  ? -19.433 5.083   29.598  1.00 15.43 ? 82  GLY   A C   1 
ATOM   662  O  O   . GLY   A 1 82  ? -19.831 5.855   30.475  1.00 18.61 ? 82  GLY   A O   1 
ATOM   663  N  N   . PRO   A 1 83  ? -18.123 4.803   29.420  1.00 12.96 ? 83  PRO   A N   1 
ATOM   664  C  CA  . PRO   A 1 83  ? -17.102 5.463   30.212  1.00 14.67 ? 83  PRO   A CA  1 
ATOM   665  C  C   . PRO   A 1 83  ? -16.747 6.869   29.755  1.00 14.43 ? 83  PRO   A C   1 
ATOM   666  O  O   . PRO   A 1 83  ? -15.912 7.486   30.375  1.00 18.20 ? 83  PRO   A O   1 
ATOM   667  C  CB  . PRO   A 1 83  ? -15.903 4.520   30.039  1.00 14.71 ? 83  PRO   A CB  1 
ATOM   668  C  CG  . PRO   A 1 83  ? -16.064 4.019   28.603  1.00 13.23 ? 83  PRO   A CG  1 
ATOM   669  C  CD  . PRO   A 1 83  ? -17.538 3.900   28.399  1.00 12.83 ? 83  PRO   A CD  1 
ATOM   670  N  N   . LEU   A 1 84  ? -17.322 7.314   28.636  1.00 12.19 ? 84  LEU   A N   1 
ATOM   671  C  CA  . LEU   A 1 84  ? -16.854 8.487   27.941  1.00 11.75 ? 84  LEU   A CA  1 
ATOM   672  C  C   . LEU   A 1 84  ? -17.501 9.742   28.487  1.00 12.99 ? 84  LEU   A C   1 
ATOM   673  O  O   . LEU   A 1 84  ? -18.704 9.775   28.732  1.00 15.31 ? 84  LEU   A O   1 
ATOM   674  C  CB  . LEU   A 1 84  ? -17.154 8.369   26.453  1.00 10.71 ? 84  LEU   A CB  1 
ATOM   675  C  CG  . LEU   A 1 84  ? -16.601 7.114   25.769  1.00 10.25 ? 84  LEU   A CG  1 
ATOM   676  C  CD1 . LEU   A 1 84  ? -17.114 7.050   24.331  1.00 11.49 ? 84  LEU   A CD1 1 
ATOM   677  C  CD2 . LEU   A 1 84  ? -15.083 7.077   25.827  1.00 10.89 ? 84  LEU   A CD2 1 
ATOM   678  N  N   . ASP   A 1 85  ? -16.715 10.802  28.529  1.00 14.45 ? 85  ASP   A N   1 
ATOM   679  C  CA  . ASP   A 1 85  ? -17.179 12.156  28.761  1.00 16.86 ? 85  ASP   A CA  1 
ATOM   680  C  C   . ASP   A 1 85  ? -17.159 12.851  27.388  1.00 17.48 ? 85  ASP   A C   1 
ATOM   681  O  O   . ASP   A 1 85  ? -16.125 12.867  26.711  1.00 21.73 ? 85  ASP   A O   1 
ATOM   682  C  CB  . ASP   A 1 85  ? -16.241 12.790  29.816  1.00 21.56 ? 85  ASP   A CB  1 
ATOM   683  N  N   . GLY   A 1 86  ? -18.265 13.416  26.930  1.00 18.52 ? 86  GLY   A N   1 
ATOM   684  C  CA  . GLY   A 1 86  ? -18.298 14.132  25.687  1.00 19.70 ? 86  GLY   A CA  1 
ATOM   685  C  C   . GLY   A 1 86  ? -18.549 13.224  24.486  1.00 17.05 ? 86  GLY   A C   1 
ATOM   686  O  O   . GLY   A 1 86  ? -19.071 12.112  24.585  1.00 19.64 ? 86  GLY   A O   1 
ATOM   687  N  N   . THR   A 1 87  ? -18.231 13.756  23.315  1.00 13.68 ? 87  THR   A N   1 
ATOM   688  C  CA  . THR   A 1 87  ? -18.659 13.190  22.052  1.00 13.24 ? 87  THR   A CA  1 
ATOM   689  C  C   . THR   A 1 87  ? -17.446 12.780  21.245  1.00 10.83 ? 87  THR   A C   1 
ATOM   690  O  O   . THR   A 1 87  ? -16.514 13.568  21.131  1.00 12.22 ? 87  THR   A O   1 
ATOM   691  C  CB  . THR   A 1 87  ? -19.453 14.252  21.282  1.00 16.20 ? 87  THR   A CB  1 
ATOM   692  O  OG1 . THR   A 1 87  ? -20.607 14.605  22.036  1.00 21.24 ? 87  THR   A OG1 1 
ATOM   693  C  CG2 . THR   A 1 87  ? -19.859 13.793  19.897  1.00 18.44 ? 87  THR   A CG2 1 
ATOM   694  N  N   . TYR   A 1 88  ? -17.471 11.548  20.738  1.00 10.43 ? 88  TYR   A N   1 
ATOM   695  C  CA  . TYR   A 1 88  ? -16.366 11.011  19.974  1.00 9.78  ? 88  TYR   A CA  1 
ATOM   696  C  C   . TYR   A 1 88  ? -16.865 10.697  18.570  1.00 10.33 ? 88  TYR   A C   1 
ATOM   697  O  O   . TYR   A 1 88  ? -17.817 9.954   18.373  1.00 13.15 ? 88  TYR   A O   1 
ATOM   698  C  CB  . TYR   A 1 88  ? -15.813 9.779   20.636  1.00 10.50 ? 88  TYR   A CB  1 
ATOM   699  C  CG  . TYR   A 1 88  ? -15.046 10.025  21.915  1.00 9.42  ? 88  TYR   A CG  1 
ATOM   700  C  CD1 . TYR   A 1 88  ? -15.650 10.434  23.082  1.00 10.40 ? 88  TYR   A CD1 1 
ATOM   701  C  CD2 . TYR   A 1 88  ? -13.669 9.829   21.957  1.00 9.04  ? 88  TYR   A CD2 1 
ATOM   702  C  CE1 . TYR   A 1 88  ? -14.933 10.637  24.247  1.00 9.94  ? 88  TYR   A CE1 1 
ATOM   703  C  CE2 . TYR   A 1 88  ? -12.925 10.006  23.106  1.00 9.28  ? 88  TYR   A CE2 1 
ATOM   704  C  CZ  . TYR   A 1 88  ? -13.569 10.390  24.251  1.00 9.40  ? 88  TYR   A CZ  1 
ATOM   705  O  OH  . TYR   A 1 88  ? -12.843 10.512  25.418  1.00 10.28 ? 88  TYR   A OH  1 
ATOM   706  N  N   A ARG   A 1 89  ? -16.228 11.294  17.542  0.50 9.50  ? 89  ARG   A N   1 
ATOM   707  N  N   B ARG   A 1 89  ? -16.129 11.174  17.602  0.50 9.26  ? 89  ARG   A N   1 
ATOM   708  C  CA  A ARG   A 1 89  ? -16.583 11.120  16.129  0.50 9.83  ? 89  ARG   A CA  1 
ATOM   709  C  CA  B ARG   A 1 89  ? -16.577 11.094  16.235  0.50 9.60  ? 89  ARG   A CA  1 
ATOM   710  C  C   A ARG   A 1 89  ? -15.858 9.945   15.520  0.50 8.65  ? 89  ARG   A C   1 
ATOM   711  C  C   B ARG   A 1 89  ? -15.852 9.990   15.472  0.50 8.51  ? 89  ARG   A C   1 
ATOM   712  O  O   A ARG   A 1 89  ? -14.644 9.815   15.676  0.50 8.31  ? 89  ARG   A O   1 
ATOM   713  O  O   B ARG   A 1 89  ? -14.622 9.909   15.478  0.50 8.23  ? 89  ARG   A O   1 
ATOM   714  C  CB  A ARG   A 1 89  ? -16.181 12.293  15.233  0.50 10.42 ? 89  ARG   A CB  1 
ATOM   715  C  CB  B ARG   A 1 89  ? -16.338 12.487  15.683  0.50 10.41 ? 89  ARG   A CB  1 
ATOM   716  C  CG  A ARG   A 1 89  ? -17.063 13.500  15.499  0.50 11.63 ? 89  ARG   A CG  1 
ATOM   717  C  CG  B ARG   A 1 89  ? -16.924 12.672  14.300  0.50 11.62 ? 89  ARG   A CG  1 
ATOM   718  C  CD  A ARG   A 1 89  ? -16.692 14.673  14.651  0.50 13.48 ? 89  ARG   A CD  1 
ATOM   719  C  CD  B ARG   A 1 89  ? -16.621 14.051  13.760  0.50 12.95 ? 89  ARG   A CD  1 
ATOM   720  N  NE  A ARG   A 1 89  ? -17.592 15.752  15.018  0.50 14.65 ? 89  ARG   A NE  1 
ATOM   721  N  NE  B ARG   A 1 89  ? -17.259 15.086  14.546  0.50 13.35 ? 89  ARG   A NE  1 
ATOM   722  C  CZ  A ARG   A 1 89  ? -17.377 17.001  14.675  0.50 15.99 ? 89  ARG   A CZ  1 
ATOM   723  C  CZ  B ARG   A 1 89  ? -16.992 16.388  14.419  0.50 13.11 ? 89  ARG   A CZ  1 
ATOM   724  N  NH1 A ARG   A 1 89  ? -16.295 17.280  13.972  0.50 14.60 ? 89  ARG   A NH1 1 
ATOM   725  N  NH1 B ARG   A 1 89  ? -17.531 17.235  15.280  0.50 14.75 ? 89  ARG   A NH1 1 
ATOM   726  N  NH2 A ARG   A 1 89  ? -18.158 17.982  15.105  0.50 18.21 ? 89  ARG   A NH2 1 
ATOM   727  N  NH2 B ARG   A 1 89  ? -16.177 16.876  13.482  0.50 15.92 ? 89  ARG   A NH2 1 
ATOM   728  N  N   . LEU   A 1 90  ? -16.615 9.145   14.751  1.00 8.80  ? 90  LEU   A N   1 
ATOM   729  C  CA  . LEU   A 1 90  ? -16.037 8.050   13.978  1.00 9.00  ? 90  LEU   A CA  1 
ATOM   730  C  C   . LEU   A 1 90  ? -15.200 8.593   12.826  1.00 8.71  ? 90  LEU   A C   1 
ATOM   731  O  O   . LEU   A 1 90  ? -15.694 9.390   11.999  1.00 10.98 ? 90  LEU   A O   1 
ATOM   732  C  CB  . LEU   A 1 90  ? -17.166 7.190   13.412  1.00 9.24  ? 90  LEU   A CB  1 
ATOM   733  C  CG  . LEU   A 1 90  ? -16.740 5.991   12.562  1.00 9.69  ? 90  LEU   A CG  1 
ATOM   734  C  CD1 . LEU   A 1 90  ? -15.951 4.942   13.352  1.00 9.91  ? 90  LEU   A CD1 1 
ATOM   735  C  CD2 . LEU   A 1 90  ? -17.960 5.357   11.927  1.00 10.79 ? 90  LEU   A CD2 1 
ATOM   736  N  N   . ILE   A 1 91  ? -13.943 8.157   12.738  1.00 8.07  ? 91  ILE   A N   1 
ATOM   737  C  CA  . ILE   A 1 91  ? -13.048 8.530   11.655  1.00 8.47  ? 91  ILE   A CA  1 
ATOM   738  C  C   . ILE   A 1 91  ? -12.803 7.383   10.692  1.00 7.54  ? 91  ILE   A C   1 
ATOM   739  O  O   . ILE   A 1 91  ? -12.718 7.573   9.493   1.00 8.25  ? 91  ILE   A O   1 
ATOM   740  C  CB  . ILE   A 1 91  ? -11.739 9.174   12.166  1.00 9.29  ? 91  ILE   A CB  1 
ATOM   741  C  CG1 . ILE   A 1 91  ? -10.796 9.548   11.030  1.00 10.86 ? 91  ILE   A CG1 1 
ATOM   742  C  CG2 . ILE   A 1 91  ? -11.029 8.342   13.218  1.00 9.26  ? 91  ILE   A CG2 1 
ATOM   743  C  CD1 . ILE   A 1 91  ? -9.661  10.450  11.436  1.00 13.68 ? 91  ILE   A CD1 1 
ATOM   744  N  N   . GLN   A 1 92  ? -12.635 6.155   11.201  1.00 7.73  ? 92  GLN   A N   1 
ATOM   745  C  CA  . GLN   A 1 92  ? -12.354 5.015   10.356  1.00 7.38  ? 92  GLN   A CA  1 
ATOM   746  C  C   . GLN   A 1 92  ? -12.624 3.737   11.132  1.00 7.09  ? 92  GLN   A C   1 
ATOM   747  O  O   . GLN   A 1 92  ? -12.630 3.768   12.364  1.00 7.93  ? 92  GLN   A O   1 
ATOM   748  C  CB  . GLN   A 1 92  ? -10.900 5.020   9.844   1.00 8.35  ? 92  GLN   A CB  1 
ATOM   749  C  CG  . GLN   A 1 92  ? -9.831  5.144   10.930  1.00 9.46  ? 92  GLN   A CG  1 
ATOM   750  C  CD  . GLN   A 1 92  ? -9.094  3.880   11.220  1.00 8.88  ? 92  GLN   A CD  1 
ATOM   751  O  OE1 . GLN   A 1 92  ? -9.618  2.773   11.138  1.00 9.33  ? 92  GLN   A OE1 1 
ATOM   752  N  NE2 . GLN   A 1 92  ? -7.879  4.040   11.704  1.00 11.29 ? 92  GLN   A NE2 1 
ATOM   753  N  N   . PHE   A 1 93  ? -12.839 2.652   10.411  1.00 6.85  ? 93  PHE   A N   1 
ATOM   754  C  CA  . PHE   A 1 93  ? -12.716 1.345   11.009  1.00 6.97  ? 93  PHE   A CA  1 
ATOM   755  C  C   . PHE   A 1 93  ? -11.749 0.487   10.207  1.00 6.72  ? 93  PHE   A C   1 
ATOM   756  O  O   . PHE   A 1 93  ? -11.522 0.695   9.017   1.00 7.51  ? 93  PHE   A O   1 
ATOM   757  C  CB  . PHE   A 1 93  ? -14.048 0.637   11.252  1.00 7.44  ? 93  PHE   A CB  1 
ATOM   758  C  CG  . PHE   A 1 93  ? -14.806 0.167   10.034  1.00 7.26  ? 93  PHE   A CG  1 
ATOM   759  C  CD1 . PHE   A 1 93  ? -14.436 -0.982  9.355   1.00 8.28  ? 93  PHE   A CD1 1 
ATOM   760  C  CD2 . PHE   A 1 93  ? -15.929 0.854   9.596   1.00 7.78  ? 93  PHE   A CD2 1 
ATOM   761  C  CE1 . PHE   A 1 93  ? -15.147 -1.418  8.254   1.00 8.20  ? 93  PHE   A CE1 1 
ATOM   762  C  CE2 . PHE   A 1 93  ? -16.618 0.404   8.486   1.00 8.64  ? 93  PHE   A CE2 1 
ATOM   763  C  CZ  . PHE   A 1 93  ? -16.245 -0.712  7.809   1.00 8.21  ? 93  PHE   A CZ  1 
ATOM   764  N  N   . HIS   A 1 94  ? -11.224 -0.535  10.874  1.00 6.77  ? 94  HIS   A N   1 
ATOM   765  C  CA  . HIS   A 1 94  ? -10.324 -1.512  10.276  1.00 6.71  ? 94  HIS   A CA  1 
ATOM   766  C  C   . HIS   A 1 94  ? -10.415 -2.779  11.089  1.00 6.27  ? 94  HIS   A C   1 
ATOM   767  O  O   . HIS   A 1 94  ? -11.035 -2.815  12.145  1.00 7.12  ? 94  HIS   A O   1 
ATOM   768  C  CB  . HIS   A 1 94  ? -8.889  -0.978  10.218  1.00 7.19  ? 94  HIS   A CB  1 
ATOM   769  C  CG  . HIS   A 1 94  ? -8.337  -0.705  11.574  1.00 6.78  ? 94  HIS   A CG  1 
ATOM   770  N  ND1 . HIS   A 1 94  ? -8.517  0.495   12.213  1.00 7.30  ? 94  HIS   A ND1 1 
ATOM   771  C  CD2 . HIS   A 1 94  ? -7.708  -1.525  12.439  1.00 7.01  ? 94  HIS   A CD2 1 
ATOM   772  C  CE1 . HIS   A 1 94  ? -7.979  0.372   13.448  1.00 7.03  ? 94  HIS   A CE1 1 
ATOM   773  N  NE2 . HIS   A 1 94  ? -7.499  -0.846  13.619  1.00 6.31  ? 94  HIS   A NE2 1 
ATOM   774  N  N   . PHE   A 1 95  ? -9.705  -3.802  10.619  1.00 6.71  ? 95  PHE   A N   1 
ATOM   775  C  CA  . PHE   A 1 95  ? -9.650  -5.097  11.270  1.00 6.60  ? 95  PHE   A CA  1 
ATOM   776  C  C   . PHE   A 1 95  ? -8.203  -5.516  11.470  1.00 6.81  ? 95  PHE   A C   1 
ATOM   777  O  O   . PHE   A 1 95  ? -7.292  -5.072  10.790  1.00 7.52  ? 95  PHE   A O   1 
ATOM   778  C  CB  . PHE   A 1 95  ? -10.355 -6.175  10.448  1.00 7.10  ? 95  PHE   A CB  1 
ATOM   779  C  CG  . PHE   A 1 95  ? -11.802 -5.894  10.104  1.00 7.24  ? 95  PHE   A CG  1 
ATOM   780  C  CD1 . PHE   A 1 95  ? -12.137 -5.046  9.067   1.00 7.76  ? 95  PHE   A CD1 1 
ATOM   781  C  CD2 . PHE   A 1 95  ? -12.849 -6.517  10.791  1.00 8.10  ? 95  PHE   A CD2 1 
ATOM   782  C  CE1 . PHE   A 1 95  ? -13.459 -4.839  8.725   1.00 8.65  ? 95  PHE   A CE1 1 
ATOM   783  C  CE2 . PHE   A 1 95  ? -14.162 -6.307  10.433  1.00 8.79  ? 95  PHE   A CE2 1 
ATOM   784  C  CZ  . PHE   A 1 95  ? -14.474 -5.448  9.402   1.00 8.89  ? 95  PHE   A CZ  1 
ATOM   785  N  N   . HIS   A 1 96  ? -8.032  -6.483  12.384  1.00 6.72  ? 96  HIS   A N   1 
ATOM   786  C  CA  . HIS   A 1 96  ? -6.832  -7.274  12.553  1.00 6.66  ? 96  HIS   A CA  1 
ATOM   787  C  C   . HIS   A 1 96  ? -7.256  -8.727  12.425  1.00 6.92  ? 96  HIS   A C   1 
ATOM   788  O  O   . HIS   A 1 96  ? -8.323  -9.086  12.935  1.00 7.43  ? 96  HIS   A O   1 
ATOM   789  C  CB  . HIS   A 1 96  ? -6.162  -7.035  13.907  1.00 7.47  ? 96  HIS   A CB  1 
ATOM   790  C  CG  . HIS   A 1 96  ? -5.880  -5.614  14.179  1.00 7.03  ? 96  HIS   A CG  1 
ATOM   791  N  ND1 . HIS   A 1 96  ? -4.656  -5.021  13.964  1.00 7.93  ? 96  HIS   A ND1 1 
ATOM   792  C  CD2 . HIS   A 1 96  ? -6.674  -4.578  14.599  1.00 7.17  ? 96  HIS   A CD2 1 
ATOM   793  C  CE1 . HIS   A 1 96  ? -4.734  -3.721  14.263  1.00 7.57  ? 96  HIS   A CE1 1 
ATOM   794  N  NE2 . HIS   A 1 96  ? -5.964  -3.419  14.643  1.00 6.96  ? 96  HIS   A NE2 1 
ATOM   795  N  N   . TRP   A 1 97  ? -6.469  -9.566  11.757  1.00 6.63  ? 97  TRP   A N   1 
ATOM   796  C  CA  . TRP   A 1 97  ? -6.881  -10.938 11.540  1.00 7.11  ? 97  TRP   A CA  1 
ATOM   797  C  C   . TRP   A 1 97  ? -5.687  -11.848 11.423  1.00 6.63  ? 97  TRP   A C   1 
ATOM   798  O  O   . TRP   A 1 97  ? -4.541  -11.431 11.318  1.00 7.48  ? 97  TRP   A O   1 
ATOM   799  C  CB  . TRP   A 1 97  ? -7.792  -11.053 10.296  1.00 7.45  ? 97  TRP   A CB  1 
ATOM   800  C  CG  . TRP   A 1 97  ? -7.113  -10.658 9.010   1.00 7.23  ? 97  TRP   A CG  1 
ATOM   801  C  CD1 . TRP   A 1 97  ? -6.444  -11.470 8.142   1.00 7.99  ? 97  TRP   A CD1 1 
ATOM   802  C  CD2 . TRP   A 1 97  ? -7.066  -9.343  8.456   1.00 7.33  ? 97  TRP   A CD2 1 
ATOM   803  N  NE1 . TRP   A 1 97  ? -6.027  -10.744 7.075   1.00 8.09  ? 97  TRP   A NE1 1 
ATOM   804  C  CE2 . TRP   A 1 97  ? -6.364  -9.437  7.243   1.00 7.42  ? 97  TRP   A CE2 1 
ATOM   805  C  CE3 . TRP   A 1 97  ? -7.537  -8.086  8.857   1.00 7.38  ? 97  TRP   A CE3 1 
ATOM   806  C  CZ2 . TRP   A 1 97  ? -6.177  -8.333  6.412   1.00 8.09  ? 97  TRP   A CZ2 1 
ATOM   807  C  CZ3 . TRP   A 1 97  ? -7.333  -6.987  8.055   1.00 8.03  ? 97  TRP   A CZ3 1 
ATOM   808  C  CH2 . TRP   A 1 97  ? -6.663  -7.113  6.834   1.00 8.25  ? 97  TRP   A CH2 1 
ATOM   809  N  N   . GLY   A 1 98  ? -5.977  -13.145 11.433  1.00 7.64  ? 98  GLY   A N   1 
ATOM   810  C  CA  . GLY   A 1 98  ? -4.977  -14.171 11.458  1.00 8.11  ? 98  GLY   A CA  1 
ATOM   811  C  C   . GLY   A 1 98  ? -4.785  -14.868 10.127  1.00 8.64  ? 98  GLY   A C   1 
ATOM   812  O  O   . GLY   A 1 98  ? -5.540  -14.706 9.178   1.00 9.46  ? 98  GLY   A O   1 
ATOM   813  N  N   . SER   A 1 99  ? -3.763  -15.733 10.123  1.00 8.91  ? 99  SER   A N   1 
ATOM   814  C  CA  . SER   A 1 99  ? -3.544  -16.664 9.019   1.00 10.09 ? 99  SER   A CA  1 
ATOM   815  C  C   . SER   A 1 99  ? -4.393  -17.927 9.151   1.00 11.21 ? 99  SER   A C   1 
ATOM   816  O  O   . SER   A 1 99  ? -4.508  -18.694 8.206   1.00 13.85 ? 99  SER   A O   1 
ATOM   817  C  CB  . SER   A 1 99  ? -2.083  -17.017 8.931   1.00 10.80 ? 99  SER   A CB  1 
ATOM   818  O  OG  . SER   A 1 99  ? -1.613  -17.523 10.144  1.00 11.62 ? 99  SER   A OG  1 
ATOM   819  N  N   . LEU   A 1 100 ? -4.952  -18.169 10.344  1.00 11.01 ? 100 LEU   A N   1 
ATOM   820  C  CA  . LEU   A 1 100 ? -5.714  -19.355 10.766  1.00 12.87 ? 100 LEU   A CA  1 
ATOM   821  C  C   . LEU   A 1 100 ? -6.865  -18.887 11.598  1.00 11.61 ? 100 LEU   A C   1 
ATOM   822  O  O   . LEU   A 1 100 ? -6.707  -17.875 12.270  1.00 11.55 ? 100 LEU   A O   1 
ATOM   823  C  CB  . LEU   A 1 100 ? -4.833  -20.271 11.701  1.00 16.49 ? 100 LEU   A CB  1 
ATOM   824  C  CG  . LEU   A 1 100 ? -3.554  -20.724 11.064  1.00 17.59 ? 100 LEU   A CG  1 
ATOM   825  C  CD1 . LEU   A 1 100 ? -2.572  -21.258 12.112  1.00 22.23 ? 100 LEU   A CD1 1 
ATOM   826  C  CD2 . LEU   A 1 100 ? -3.866  -21.824 10.082  1.00 20.74 ? 100 LEU   A CD2 1 
ATOM   827  N  N   . ASP   A 1 101 ? -7.939  -19.648 11.665  1.00 11.40 ? 101 ASP   A N   1 
ATOM   828  C  CA  . ASP   A 1 101 ? -9.108  -19.175 12.398  1.00 11.65 ? 101 ASP   A CA  1 
ATOM   829  C  C   . ASP   A 1 101 ? -8.843  -19.098 13.903  1.00 12.36 ? 101 ASP   A C   1 
ATOM   830  O  O   . ASP   A 1 101 ? -9.520  -18.378 14.591  1.00 14.69 ? 101 ASP   A O   1 
ATOM   831  C  CB  . ASP   A 1 101 ? -10.311 -20.077 12.135  1.00 12.59 ? 101 ASP   A CB  1 
ATOM   832  C  CG  . ASP   A 1 101 ? -10.846 -20.061 10.713  1.00 14.15 ? 101 ASP   A CG  1 
ATOM   833  O  OD1 . ASP   A 1 101 ? -10.418 -19.245 9.882   1.00 14.50 ? 101 ASP   A OD1 1 
ATOM   834  O  OD2 . ASP   A 1 101 ? -11.708 -20.885 10.414  1.00 18.54 ? 101 ASP   A OD2 1 
ATOM   835  N  N   . GLY   A 1 102 ? -7.827  -19.812 14.397  1.00 13.25 ? 102 GLY   A N   1 
ATOM   836  C  CA  . GLY   A 1 102 ? -7.493  -19.819 15.823  1.00 15.16 ? 102 GLY   A CA  1 
ATOM   837  C  C   . GLY   A 1 102 ? -6.666  -18.650 16.349  1.00 13.09 ? 102 GLY   A C   1 
ATOM   838  O  O   . GLY   A 1 102 ? -6.329  -18.640 17.527  1.00 14.38 ? 102 GLY   A O   1 
ATOM   839  N  N   . GLN   A 1 103 ? -6.428  -17.645 15.522  1.00 11.00 ? 103 GLN   A N   1 
ATOM   840  C  CA  . GLN   A 1 103 ? -5.721  -16.469 15.980  1.00 9.33  ? 103 GLN   A CA  1 
ATOM   841  C  C   . GLN   A 1 103 ? -6.134  -15.313 15.101  1.00 8.79  ? 103 GLN   A C   1 
ATOM   842  O  O   . GLN   A 1 103 ? -6.681  -15.493 14.011  1.00 9.48  ? 103 GLN   A O   1 
ATOM   843  C  CB  . GLN   A 1 103 ? -4.211  -16.687 15.949  1.00 9.96  ? 103 GLN   A CB  1 
ATOM   844  C  CG  . GLN   A 1 103 ? -3.685  -16.900 14.523  1.00 10.98 ? 103 GLN   A CG  1 
ATOM   845  C  CD  . GLN   A 1 103 ? -2.359  -17.549 14.490  1.00 13.36 ? 103 GLN   A CD  1 
ATOM   846  O  OE1 . GLN   A 1 103 ? -2.242  -18.613 15.073  1.00 19.50 ? 103 GLN   A OE1 1 
ATOM   847  N  NE2 . GLN   A 1 103 ? -1.414  -17.017 13.741  1.00 14.05 ? 103 GLN   A NE2 1 
ATOM   848  N  N   . GLY   A 1 104 ? -5.812  -14.085 15.556  1.00 8.20  ? 104 GLY   A N   1 
ATOM   849  C  CA  . GLY   A 1 104 ? -6.093  -12.912 14.764  1.00 7.98  ? 104 GLY   A CA  1 
ATOM   850  C  C   . GLY   A 1 104 ? -6.530  -11.721 15.582  1.00 7.88  ? 104 GLY   A C   1 
ATOM   851  O  O   . GLY   A 1 104 ? -6.280  -10.592 15.204  1.00 8.65  ? 104 GLY   A O   1 
ATOM   852  N  N   . SER   A 1 105 ? -7.228  -11.968 16.712  1.00 7.88  ? 105 SER   A N   1 
ATOM   853  C  CA  . SER   A 1 105 ? -7.612  -10.842 17.552  1.00 7.90  ? 105 SER   A CA  1 
ATOM   854  C  C   . SER   A 1 105 ? -6.412  -10.289 18.312  1.00 7.44  ? 105 SER   A C   1 
ATOM   855  O  O   . SER   A 1 105 ? -5.390  -10.949 18.515  1.00 8.62  ? 105 SER   A O   1 
ATOM   856  C  CB  . SER   A 1 105 ? -8.746  -11.198 18.478  1.00 7.93  ? 105 SER   A CB  1 
ATOM   857  O  OG  . SER   A 1 105 ? -8.391  -12.160 19.464  1.00 8.44  ? 105 SER   A OG  1 
ATOM   858  N  N   . GLU   A 1 106 ? -6.557  -9.038  18.720  1.00 7.63  ? 106 GLU   A N   1 
ATOM   859  C  CA  . GLU   A 1 106 ? -5.546  -8.331  19.519  1.00 7.30  ? 106 GLU   A CA  1 
ATOM   860  C  C   . GLU   A 1 106 ? -5.875  -8.519  21.000  1.00 7.27  ? 106 GLU   A C   1 
ATOM   861  O  O   . GLU   A 1 106 ? -5.093  -9.100  21.747  1.00 8.13  ? 106 GLU   A O   1 
ATOM   862  C  CB  . GLU   A 1 106 ? -5.505  -6.872  19.094  1.00 7.69  ? 106 GLU   A CB  1 
ATOM   863  C  CG  . GLU   A 1 106 ? -5.091  -6.732  17.644  1.00 8.75  ? 106 GLU   A CG  1 
ATOM   864  C  CD  . GLU   A 1 106 ? -4.376  -5.450  17.373  1.00 7.90  ? 106 GLU   A CD  1 
ATOM   865  O  OE1 . GLU   A 1 106 ? -4.972  -4.392  17.596  1.00 7.94  ? 106 GLU   A OE1 1 
ATOM   866  O  OE2 . GLU   A 1 106 ? -3.202  -5.517  16.920  1.00 9.30  ? 106 GLU   A OE2 1 
ATOM   867  N  N   . HIS   A 1 107 ? -7.052  -8.069  21.423  1.00 7.47  ? 107 HIS   A N   1 
ATOM   868  C  CA  . HIS   A 1 107 ? -7.511  -8.463  22.740  1.00 7.39  ? 107 HIS   A CA  1 
ATOM   869  C  C   . HIS   A 1 107 ? -7.796  -9.945  22.754  1.00 7.66  ? 107 HIS   A C   1 
ATOM   870  O  O   . HIS   A 1 107 ? -8.141  -10.561 21.742  1.00 8.08  ? 107 HIS   A O   1 
ATOM   871  C  CB  . HIS   A 1 107 ? -8.761  -7.652  23.118  1.00 7.55  ? 107 HIS   A CB  1 
ATOM   872  C  CG  . HIS   A 1 107 ? -8.472  -6.207  23.282  1.00 7.49  ? 107 HIS   A CG  1 
ATOM   873  N  ND1 . HIS   A 1 107 ? -8.517  -5.303  22.237  1.00 7.76  ? 107 HIS   A ND1 1 
ATOM   874  C  CD2 . HIS   A 1 107 ? -8.015  -5.489  24.350  1.00 7.52  ? 107 HIS   A CD2 1 
ATOM   875  C  CE1 . HIS   A 1 107 ? -8.084  -4.120  22.699  1.00 8.41  ? 107 HIS   A CE1 1 
ATOM   876  N  NE2 . HIS   A 1 107 ? -7.776  -4.189  23.992  1.00 7.99  ? 107 HIS   A NE2 1 
ATOM   877  N  N   . THR   A 1 108 ? -7.667  -10.519 23.954  1.00 7.99  ? 108 THR   A N   1 
ATOM   878  C  CA  . THR   A 1 108 ? -8.054  -11.899 24.227  1.00 8.35  ? 108 THR   A CA  1 
ATOM   879  C  C   . THR   A 1 108 ? -8.991  -11.885 25.413  1.00 8.12  ? 108 THR   A C   1 
ATOM   880  O  O   . THR   A 1 108 ? -9.013  -10.932 26.190  1.00 8.72  ? 108 THR   A O   1 
ATOM   881  C  CB  . THR   A 1 108 ? -6.829  -12.799 24.422  1.00 8.93  ? 108 THR   A CB  1 
ATOM   882  O  OG1 . THR   A 1 108 ? -5.998  -12.312 25.480  1.00 9.87  ? 108 THR   A OG1 1 
ATOM   883  C  CG2 . THR   A 1 108 ? -6.000  -12.858 23.158  1.00 10.03 ? 108 THR   A CG2 1 
ATOM   884  N  N   . VAL   A 1 109 ? -9.753  -12.973 25.548  1.00 8.79  ? 109 VAL   A N   1 
ATOM   885  C  CA  . VAL   A 1 109 ? -10.744 -13.081 26.614  1.00 9.44  ? 109 VAL   A CA  1 
ATOM   886  C  C   . VAL   A 1 109 ? -10.435 -14.371 27.356  1.00 9.70  ? 109 VAL   A C   1 
ATOM   887  O  O   . VAL   A 1 109 ? -10.559 -15.466 26.795  1.00 10.32 ? 109 VAL   A O   1 
ATOM   888  C  CB  . VAL   A 1 109 ? -12.172 -13.090 26.079  1.00 10.18 ? 109 VAL   A CB  1 
ATOM   889  C  CG1 . VAL   A 1 109 ? -13.177 -13.257 27.205  1.00 11.73 ? 109 VAL   A CG1 1 
ATOM   890  C  CG2 . VAL   A 1 109 ? -12.504 -11.843 25.294  1.00 10.75 ? 109 VAL   A CG2 1 
ATOM   891  N  N   . ASP   A 1 110 ? -9.944  -14.278 28.590  1.00 10.16 ? 110 ASP   A N   1 
ATOM   892  C  CA  . ASP   A 1 110 ? -9.478  -15.462 29.306  1.00 11.27 ? 110 ASP   A CA  1 
ATOM   893  C  C   . ASP   A 1 110 ? -8.498  -16.267 28.452  1.00 10.83 ? 110 ASP   A C   1 
ATOM   894  O  O   . ASP   A 1 110 ? -8.535  -17.498 28.390  1.00 12.31 ? 110 ASP   A O   1 
ATOM   895  C  CB  . ASP   A 1 110 ? -10.640 -16.309 29.797  1.00 12.80 ? 110 ASP   A CB  1 
ATOM   896  C  CG  . ASP   A 1 110 ? -11.485 -15.567 30.808  1.00 12.89 ? 110 ASP   A CG  1 
ATOM   897  O  OD1 . ASP   A 1 110 ? -10.953 -14.698 31.507  1.00 14.03 ? 110 ASP   A OD1 1 
ATOM   898  O  OD2 . ASP   A 1 110 ? -12.696 -15.896 30.879  1.00 16.42 ? 110 ASP   A OD2 1 
ATOM   899  N  N   . LYS   A 1 111 ? -7.611  -15.541 27.761  1.00 10.51 ? 111 LYS   A N   1 
ATOM   900  C  CA  . LYS   A 1 111 ? -6.547  -16.039 26.893  1.00 10.95 ? 111 LYS   A CA  1 
ATOM   901  C  C   . LYS   A 1 111 ? -7.072  -16.553 25.550  1.00 10.43 ? 111 LYS   A C   1 
ATOM   902  O  O   . LYS   A 1 111 ? -6.272  -16.898 24.699  1.00 12.51 ? 111 LYS   A O   1 
ATOM   903  C  CB  . LYS   A 1 111 ? -5.630  -17.051 27.594  1.00 12.87 ? 111 LYS   A CB  1 
ATOM   904  C  CG  . LYS   A 1 111 ? -4.979  -16.511 28.849  1.00 15.58 ? 111 LYS   A CG  1 
ATOM   905  C  CD  . LYS   A 1 111 ? -4.018  -15.353 28.538  1.00 20.54 ? 111 LYS   A CD  1 
ATOM   906  C  CE  . LYS   A 1 111 ? -3.293  -14.729 29.717  1.00 24.24 ? 111 LYS   A CE  1 
ATOM   907  N  NZ  . LYS   A 1 111 ? -2.095  -15.494 30.059  1.00 29.46 ? 111 LYS   A NZ  1 
ATOM   908  N  N   . LYS   A 1 112 ? -8.375  -16.563 25.328  1.00 10.53 ? 112 LYS   A N   1 
ATOM   909  C  CA  . LYS   A 1 112 ? -8.911  -16.973 24.046  1.00 11.02 ? 112 LYS   A CA  1 
ATOM   910  C  C   . LYS   A 1 112 ? -8.651  -15.913 22.978  1.00 10.05 ? 112 LYS   A C   1 
ATOM   911  O  O   . LYS   A 1 112 ? -8.990  -14.740 23.165  1.00 10.08 ? 112 LYS   A O   1 
ATOM   912  C  CB  . LYS   A 1 112 ? -10.423 -17.200 24.136  1.00 12.61 ? 112 LYS   A CB  1 
ATOM   913  C  CG  . LYS   A 1 112 ? -11.110 -17.556 22.818  1.00 14.91 ? 112 LYS   A CG  1 
ATOM   914  C  CD  . LYS   A 1 112 ? -12.636 -17.601 22.880  1.00 18.82 ? 112 LYS   A CD  1 
ATOM   915  C  CE  . LYS   A 1 112 ? -13.303 -17.811 21.545  1.00 21.47 ? 112 LYS   A CE  1 
ATOM   916  N  NZ  . LYS   A 1 112 ? -13.024 -19.123 20.974  1.00 25.21 ? 112 LYS   A NZ  1 
ATOM   917  N  N   A LYS   A 1 113 ? -8.014  -16.327 21.886  0.50 10.01 ? 113 LYS   A N   1 
ATOM   918  N  N   B LYS   A 1 113 ? -8.228  -16.390 21.805  0.50 10.03 ? 113 LYS   A N   1 
ATOM   919  C  CA  A LYS   A 1 113 ? -7.983  -15.564 20.651  0.50 9.81  ? 113 LYS   A CA  1 
ATOM   920  C  CA  B LYS   A 1 113 ? -7.954  -15.542 20.656  0.50 10.00 ? 113 LYS   A CA  1 
ATOM   921  C  C   A LYS   A 1 113 ? -9.212  -15.828 19.783  0.50 9.37  ? 113 LYS   A C   1 
ATOM   922  C  C   B LYS   A 1 113 ? -9.037  -15.814 19.631  0.50 9.39  ? 113 LYS   A C   1 
ATOM   923  O  O   A LYS   A 1 113 ? -9.711  -16.945 19.641  0.50 9.97  ? 113 LYS   A O   1 
ATOM   924  O  O   B LYS   A 1 113 ? -9.240  -16.958 19.253  0.50 9.65  ? 113 LYS   A O   1 
ATOM   925  C  CB  A LYS   A 1 113 ? -6.718  -15.955 19.887  0.50 10.14 ? 113 LYS   A CB  1 
ATOM   926  C  CB  B LYS   A 1 113 ? -6.596  -15.862 20.016  0.50 10.73 ? 113 LYS   A CB  1 
ATOM   927  C  CG  A LYS   A 1 113 ? -5.429  -15.665 20.640  0.50 10.27 ? 113 LYS   A CG  1 
ATOM   928  C  CG  B LYS   A 1 113 ? -5.378  -15.484 20.850  0.50 11.36 ? 113 LYS   A CG  1 
ATOM   929  C  CD  A LYS   A 1 113 ? -4.221  -16.263 19.945  0.50 11.29 ? 113 LYS   A CD  1 
ATOM   930  C  CD  B LYS   A 1 113 ? -4.092  -16.016 20.277  0.50 12.74 ? 113 LYS   A CD  1 
ATOM   931  C  CE  A LYS   A 1 113 ? -2.910  -15.739 20.490  0.50 12.96 ? 113 LYS   A CE  1 
ATOM   932  C  CE  B LYS   A 1 113 ? -2.899  -15.443 20.997  0.50 14.10 ? 113 LYS   A CE  1 
ATOM   933  N  NZ  A LYS   A 1 113 ? -2.545  -16.391 21.764  0.50 14.24 ? 113 LYS   A NZ  1 
ATOM   934  N  NZ  B LYS   A 1 113 ? -1.718  -16.297 20.771  0.50 16.40 ? 113 LYS   A NZ  1 
ATOM   935  N  N   . TYR   A 1 114 ? -9.687  -14.748 19.171  1.00 8.94  ? 114 TYR   A N   1 
ATOM   936  C  CA  . TYR   A 1 114 ? -10.692 -14.815 18.106  1.00 8.72  ? 114 TYR   A CA  1 
ATOM   937  C  C   . TYR   A 1 114 ? -9.997  -14.752 16.748  1.00 8.58  ? 114 TYR   A C   1 
ATOM   938  O  O   . TYR   A 1 114 ? -8.828  -14.448 16.626  1.00 8.82  ? 114 TYR   A O   1 
ATOM   939  C  CB  . TYR   A 1 114 ? -11.745 -13.712 18.282  1.00 8.90  ? 114 TYR   A CB  1 
ATOM   940  C  CG  . TYR   A 1 114 ? -12.670 -13.969 19.439  1.00 9.07  ? 114 TYR   A CG  1 
ATOM   941  C  CD1 . TYR   A 1 114 ? -12.409 -13.558 20.731  1.00 10.59 ? 114 TYR   A CD1 1 
ATOM   942  C  CD2 . TYR   A 1 114 ? -13.857 -14.636 19.217  1.00 10.46 ? 114 TYR   A CD2 1 
ATOM   943  C  CE1 . TYR   A 1 114 ? -13.316 -13.791 21.757  1.00 12.68 ? 114 TYR   A CE1 1 
ATOM   944  C  CE2 . TYR   A 1 114 ? -14.781 -14.869 20.223  1.00 12.92 ? 114 TYR   A CE2 1 
ATOM   945  C  CZ  . TYR   A 1 114 ? -14.495 -14.459 21.497  1.00 13.75 ? 114 TYR   A CZ  1 
ATOM   946  O  OH  . TYR   A 1 114 ? -15.355 -14.655 22.567  1.00 18.63 ? 114 TYR   A OH  1 
ATOM   947  N  N   . ALA   A 1 115 ? -10.760 -15.048 15.696  1.00 8.40  ? 115 ALA   A N   1 
ATOM   948  C  CA  . ALA   A 1 115 ? -10.237 -15.076 14.340  1.00 8.47  ? 115 ALA   A CA  1 
ATOM   949  C  C   . ALA   A 1 115 ? -9.868  -13.679 13.833  1.00 8.00  ? 115 ALA   A C   1 
ATOM   950  O  O   . ALA   A 1 115 ? -9.032  -13.538 12.945  1.00 8.43  ? 115 ALA   A O   1 
ATOM   951  C  CB  . ALA   A 1 115 ? -11.256 -15.696 13.422  1.00 9.37  ? 115 ALA   A CB  1 
ATOM   952  N  N   . ALA   A 1 116 ? -10.514 -12.651 14.361  1.00 8.01  ? 116 ALA   A N   1 
ATOM   953  C  CA  . ALA   A 1 116 ? -10.254 -11.290 13.923  1.00 7.48  ? 116 ALA   A CA  1 
ATOM   954  C  C   . ALA   A 1 116 ? -10.857 -10.346 14.951  1.00 6.92  ? 116 ALA   A C   1 
ATOM   955  O  O   . ALA   A 1 116 ? -11.599 -10.755 15.860  1.00 7.72  ? 116 ALA   A O   1 
ATOM   956  C  CB  . ALA   A 1 116 ? -10.786 -11.032 12.521  1.00 7.75  ? 116 ALA   A CB  1 
ATOM   957  N  N   . GLU   A 1 117 ? -10.550 -9.059  14.804  1.00 6.85  ? 117 GLU   A N   1 
ATOM   958  C  CA  . GLU   A 1 117 ? -11.078 -8.020  15.666  1.00 7.18  ? 117 GLU   A CA  1 
ATOM   959  C  C   . GLU   A 1 117 ? -11.292 -6.762  14.839  1.00 7.10  ? 117 GLU   A C   1 
ATOM   960  O  O   . GLU   A 1 117 ? -10.379 -6.350  14.106  1.00 8.56  ? 117 GLU   A O   1 
ATOM   961  C  CB  . GLU   A 1 117 ? -10.112 -7.783  16.823  1.00 7.72  ? 117 GLU   A CB  1 
ATOM   962  C  CG  . GLU   A 1 117 ? -10.592 -6.847  17.900  1.00 8.21  ? 117 GLU   A CG  1 
ATOM   963  C  CD  . GLU   A 1 117 ? -9.670  -6.767  19.120  1.00 7.72  ? 117 GLU   A CD  1 
ATOM   964  O  OE1 . GLU   A 1 117 ? -9.014  -7.778  19.420  1.00 9.22  ? 117 GLU   A OE1 1 
ATOM   965  O  OE2 . GLU   A 1 117 ? -9.617  -5.683  19.747  1.00 8.75  ? 117 GLU   A OE2 1 
ATOM   966  N  N   . LEU   A 1 118 ? -12.470 -6.181  14.956  1.00 6.81  ? 118 LEU   A N   1 
ATOM   967  C  CA  . LEU   A 1 118 ? -12.867 -4.937  14.317  1.00 6.43  ? 118 LEU   A CA  1 
ATOM   968  C  C   . LEU   A 1 118 ? -12.639 -3.790  15.291  1.00 6.16  ? 118 LEU   A C   1 
ATOM   969  O  O   . LEU   A 1 118 ? -13.039 -3.879  16.447  1.00 6.88  ? 118 LEU   A O   1 
ATOM   970  C  CB  . LEU   A 1 118 ? -14.368 -5.053  13.969  1.00 7.38  ? 118 LEU   A CB  1 
ATOM   971  C  CG  . LEU   A 1 118 ? -15.109 -3.776  13.593  1.00 7.59  ? 118 LEU   A CG  1 
ATOM   972  C  CD1 . LEU   A 1 118 ? -14.535 -3.078  12.384  1.00 8.03  ? 118 LEU   A CD1 1 
ATOM   973  C  CD2 . LEU   A 1 118 ? -16.561 -4.129  13.332  1.00 8.86  ? 118 LEU   A CD2 1 
ATOM   974  N  N   . HIS   A 1 119 ? -12.019 -2.728  14.805  1.00 6.03  ? 119 HIS   A N   1 
ATOM   975  C  CA  . HIS   A 1 119 ? -11.777 -1.524  15.562  1.00 6.17  ? 119 HIS   A CA  1 
ATOM   976  C  C   . HIS   A 1 119 ? -12.455 -0.346  14.882  1.00 6.03  ? 119 HIS   A C   1 
ATOM   977  O  O   . HIS   A 1 119 ? -12.083 0.024   13.771  1.00 7.21  ? 119 HIS   A O   1 
ATOM   978  C  CB  . HIS   A 1 119 ? -10.274 -1.230  15.638  1.00 6.68  ? 119 HIS   A CB  1 
ATOM   979  C  CG  . HIS   A 1 119 ? -9.562  -2.189  16.535  1.00 6.42  ? 119 HIS   A CG  1 
ATOM   980  N  ND1 . HIS   A 1 119 ? -8.197  -2.391  16.509  1.00 6.44  ? 119 HIS   A ND1 1 
ATOM   981  C  CD2 . HIS   A 1 119 ? -10.068 -3.028  17.462  1.00 6.97  ? 119 HIS   A CD2 1 
ATOM   982  C  CE1 . HIS   A 1 119 ? -7.898  -3.295  17.425  1.00 6.95  ? 119 HIS   A CE1 1 
ATOM   983  N  NE2 . HIS   A 1 119 ? -9.025  -3.713  18.027  1.00 7.47  ? 119 HIS   A NE2 1 
ATOM   984  N  N   . LEU   A 1 120 ? -13.460 0.239   15.554  1.00 6.44  ? 120 LEU   A N   1 
ATOM   985  C  CA  . LEU   A 1 120 ? -14.120 1.453   15.125  1.00 6.44  ? 120 LEU   A CA  1 
ATOM   986  C  C   . LEU   A 1 120 ? -13.492 2.594   15.908  1.00 6.33  ? 120 LEU   A C   1 
ATOM   987  O  O   . LEU   A 1 120 ? -13.620 2.644   17.129  1.00 6.85  ? 120 LEU   A O   1 
ATOM   988  C  CB  . LEU   A 1 120 ? -15.639 1.354   15.338  1.00 7.43  ? 120 LEU   A CB  1 
ATOM   989  C  CG  . LEU   A 1 120 ? -16.335 0.300   14.475  1.00 8.31  ? 120 LEU   A CG  1 
ATOM   990  C  CD1 . LEU   A 1 120 ? -17.174 -0.624  15.307  1.00 11.81 ? 120 LEU   A CD1 1 
ATOM   991  C  CD2 . LEU   A 1 120 ? -17.165 0.952   13.415  1.00 9.74  ? 120 LEU   A CD2 1 
ATOM   992  N  N   . VAL   A 1 121 ? -12.773 3.463   15.204  1.00 6.68  ? 121 VAL   A N   1 
ATOM   993  C  CA  . VAL   A 1 121 ? -11.917 4.473   15.813  1.00 6.68  ? 121 VAL   A CA  1 
ATOM   994  C  C   . VAL   A 1 121 ? -12.613 5.814   15.842  1.00 7.11  ? 121 VAL   A C   1 
ATOM   995  O  O   . VAL   A 1 121 ? -13.065 6.301   14.804  1.00 7.78  ? 121 VAL   A O   1 
ATOM   996  C  CB  . VAL   A 1 121 ? -10.593 4.572   15.020  1.00 7.43  ? 121 VAL   A CB  1 
ATOM   997  C  CG1 . VAL   A 1 121 ? -9.684  5.621   15.628  1.00 8.02  ? 121 VAL   A CG1 1 
ATOM   998  C  CG2 . VAL   A 1 121 ? -9.911  3.221   14.872  1.00 7.66  ? 121 VAL   A CG2 1 
ATOM   999  N  N   . HIS   A 1 122 ? -12.673 6.422   17.026  1.00 7.04  ? 122 HIS   A N   1 
ATOM   1000 C  CA  . HIS   A 1 122 ? -13.356 7.691   17.233  1.00 7.21  ? 122 HIS   A CA  1 
ATOM   1001 C  C   . HIS   A 1 122 ? -12.460 8.655   17.978  1.00 7.48  ? 122 HIS   A C   1 
ATOM   1002 O  O   . HIS   A 1 122 ? -11.682 8.230   18.835  1.00 8.32  ? 122 HIS   A O   1 
ATOM   1003 C  CB  . HIS   A 1 122 ? -14.639 7.511   18.075  1.00 7.47  ? 122 HIS   A CB  1 
ATOM   1004 C  CG  . HIS   A 1 122 ? -15.529 6.406   17.659  1.00 7.71  ? 122 HIS   A CG  1 
ATOM   1005 N  ND1 . HIS   A 1 122 ? -15.240 5.078   17.908  1.00 7.81  ? 122 HIS   A ND1 1 
ATOM   1006 C  CD2 . HIS   A 1 122 ? -16.757 6.362   17.067  1.00 8.35  ? 122 HIS   A CD2 1 
ATOM   1007 C  CE1 . HIS   A 1 122 ? -16.247 4.334   17.468  1.00 8.21  ? 122 HIS   A CE1 1 
ATOM   1008 N  NE2 . HIS   A 1 122 ? -17.189 5.081   16.950  1.00 8.53  ? 122 HIS   A NE2 1 
ATOM   1009 N  N   . TRP   A 1 123 ? -12.590 9.954   17.705  1.00 7.81  ? 123 TRP   A N   1 
ATOM   1010 C  CA  . TRP   A 1 123 ? -11.801 10.970  18.395  1.00 7.83  ? 123 TRP   A CA  1 
ATOM   1011 C  C   . TRP   A 1 123 ? -12.691 11.975  19.096  1.00 7.76  ? 123 TRP   A C   1 
ATOM   1012 O  O   . TRP   A 1 123 ? -13.780 12.316  18.671  1.00 8.56  ? 123 TRP   A O   1 
ATOM   1013 C  CB  . TRP   A 1 123 ? -10.776 11.642  17.457  1.00 9.45  ? 123 TRP   A CB  1 
ATOM   1014 C  CG  . TRP   A 1 123 ? -11.391 12.305  16.243  1.00 9.24  ? 123 TRP   A CG  1 
ATOM   1015 C  CD1 . TRP   A 1 123 ? -11.626 11.711  15.051  1.00 9.85  ? 123 TRP   A CD1 1 
ATOM   1016 C  CD2 . TRP   A 1 123 ? -11.794 13.678  16.117  1.00 9.73  ? 123 TRP   A CD2 1 
ATOM   1017 N  NE1 . TRP   A 1 123 ? -12.175 12.617  14.183  1.00 10.50 ? 123 TRP   A NE1 1 
ATOM   1018 C  CE2 . TRP   A 1 123 ? -12.289 13.823  14.817  1.00 10.64 ? 123 TRP   A CE2 1 
ATOM   1019 C  CE3 . TRP   A 1 123 ? -11.763 14.790  16.957  1.00 10.99 ? 123 TRP   A CE3 1 
ATOM   1020 C  CZ2 . TRP   A 1 123 ? -12.763 15.040  14.350  1.00 11.67 ? 123 TRP   A CZ2 1 
ATOM   1021 C  CZ3 . TRP   A 1 123 ? -12.266 15.980  16.493  1.00 12.85 ? 123 TRP   A CZ3 1 
ATOM   1022 C  CH2 . TRP   A 1 123 ? -12.762 16.099  15.215  1.00 12.90 ? 123 TRP   A CH2 1 
ATOM   1023 N  N   . ASN   A 1 124 ? -12.181 12.468  20.229  1.00 8.35  ? 124 ASN   A N   1 
ATOM   1024 C  CA  . ASN   A 1 124 ? -12.885 13.359  21.111  1.00 8.81  ? 124 ASN   A CA  1 
ATOM   1025 C  C   . ASN   A 1 124 ? -12.985 14.747  20.513  1.00 9.02  ? 124 ASN   A C   1 
ATOM   1026 O  O   . ASN   A 1 124 ? -11.968 15.397  20.277  1.00 9.43  ? 124 ASN   A O   1 
ATOM   1027 C  CB  . ASN   A 1 124 ? -12.130 13.394  22.435  1.00 9.39  ? 124 ASN   A CB  1 
ATOM   1028 C  CG  . ASN   A 1 124 ? -12.872 14.057  23.528  1.00 10.39 ? 124 ASN   A CG  1 
ATOM   1029 O  OD1 . ASN   A 1 124 ? -13.676 14.963  23.294  1.00 10.85 ? 124 ASN   A OD1 1 
ATOM   1030 N  ND2 . ASN   A 1 124 ? -12.622 13.620  24.750  1.00 11.87 ? 124 ASN   A ND2 1 
ATOM   1031 N  N   . THR   A 1 125 ? -14.205 15.214  20.267  1.00 9.54  ? 125 THR   A N   1 
ATOM   1032 C  CA  . THR   A 1 125 ? -14.391 16.449  19.539  1.00 10.91 ? 125 THR   A CA  1 
ATOM   1033 C  C   . THR   A 1 125 ? -13.843 17.665  20.265  1.00 10.88 ? 125 THR   A C   1 
ATOM   1034 O  O   . THR   A 1 125 ? -13.631 18.690  19.614  1.00 12.82 ? 125 THR   A O   1 
ATOM   1035 C  CB  . THR   A 1 125 ? -15.840 16.642  19.097  1.00 13.95 ? 125 THR   A CB  1 
ATOM   1036 O  OG1 . THR   A 1 125 ? -16.643 16.730  20.266  1.00 15.26 ? 125 THR   A OG1 1 
ATOM   1037 C  CG2 . THR   A 1 125 ? -16.311 15.529  18.186  1.00 15.88 ? 125 THR   A CG2 1 
ATOM   1038 N  N   . LYS   A 1 126 ? -13.633 17.565  21.567  1.00 10.55 ? 127 LYS   A N   1 
ATOM   1039 C  CA  . LYS   A 1 126 ? -13.072 18.718  22.249  1.00 12.37 ? 127 LYS   A CA  1 
ATOM   1040 C  C   . LYS   A 1 126 ? -11.645 19.051  21.793  1.00 11.19 ? 127 LYS   A C   1 
ATOM   1041 O  O   . LYS   A 1 126 ? -11.210 20.161  22.028  1.00 13.12 ? 127 LYS   A O   1 
ATOM   1042 C  CB  . LYS   A 1 126 ? -13.189 18.532  23.746  1.00 14.37 ? 127 LYS   A CB  1 
ATOM   1043 C  CG  . LYS   A 1 126 ? -12.151 17.672  24.344  1.00 15.82 ? 127 LYS   A CG  1 
ATOM   1044 C  CD  . LYS   A 1 126 ? -12.578 17.385  25.789  1.00 19.63 ? 127 LYS   A CD  1 
ATOM   1045 C  CE  . LYS   A 1 126 ? -11.546 16.553  26.484  1.00 22.29 ? 127 LYS   A CE  1 
ATOM   1046 N  N   . TYR   A 1 127 ? -10.967 18.135  21.096  1.00 10.10 ? 128 TYR   A N   1 
ATOM   1047 C  CA  . TYR   A 1 127 ? -9.622  18.372  20.614  1.00 10.63 ? 128 TYR   A CA  1 
ATOM   1048 C  C   . TYR   A 1 127 ? -9.557  18.813  19.152  1.00 11.14 ? 128 TYR   A C   1 
ATOM   1049 O  O   . TYR   A 1 127 ? -8.449  19.038  18.628  1.00 11.64 ? 128 TYR   A O   1 
ATOM   1050 C  CB  . TYR   A 1 127 ? -8.730  17.175  20.883  1.00 10.97 ? 128 TYR   A CB  1 
ATOM   1051 C  CG  . TYR   A 1 127 ? -8.660  16.875  22.362  1.00 11.04 ? 128 TYR   A CG  1 
ATOM   1052 C  CD1 . TYR   A 1 127 ? -8.212  17.822  23.277  1.00 11.98 ? 128 TYR   A CD1 1 
ATOM   1053 C  CD2 . TYR   A 1 127 ? -9.004  15.617  22.839  1.00 10.80 ? 128 TYR   A CD2 1 
ATOM   1054 C  CE1 . TYR   A 1 127 ? -8.218  17.543  24.630  1.00 12.19 ? 128 TYR   A CE1 1 
ATOM   1055 C  CE2 . TYR   A 1 127 ? -8.951  15.313  24.188  1.00 11.22 ? 128 TYR   A CE2 1 
ATOM   1056 C  CZ  . TYR   A 1 127 ? -8.553  16.295  25.089  1.00 12.23 ? 128 TYR   A CZ  1 
ATOM   1057 O  OH  . TYR   A 1 127 ? -8.488  16.076  26.426  1.00 14.58 ? 128 TYR   A OH  1 
ATOM   1058 N  N   . GLY   A 1 128 ? -10.706 18.923  18.503  1.00 10.63 ? 129 GLY   A N   1 
ATOM   1059 C  CA  . GLY   A 1 128 ? -10.744 19.604  17.213  1.00 11.68 ? 129 GLY   A CA  1 
ATOM   1060 C  C   . GLY   A 1 128 ? -10.401 18.769  15.986  1.00 11.30 ? 129 GLY   A C   1 
ATOM   1061 O  O   . GLY   A 1 128 ? -11.034 18.921  14.936  1.00 12.36 ? 129 GLY   A O   1 
ATOM   1062 N  N   . ASP   A 1 129 ? -9.376  17.922  16.072  1.00 11.46 ? 130 ASP   A N   1 
ATOM   1063 C  CA  A ASP   A 1 129 ? -8.898  17.098  14.950  0.50 11.34 ? 130 ASP   A CA  1 
ATOM   1064 C  CA  B ASP   A 1 129 ? -9.216  16.923  15.036  0.50 11.88 ? 130 ASP   A CA  1 
ATOM   1065 C  C   . ASP   A 1 129 ? -8.336  15.792  15.548  1.00 11.71 ? 130 ASP   A C   1 
ATOM   1066 O  O   . ASP   A 1 129 ? -7.845  15.795  16.690  1.00 11.94 ? 130 ASP   A O   1 
ATOM   1067 C  CB  A ASP   A 1 129 ? -7.975  17.854  13.945  0.50 10.94 ? 130 ASP   A CB  1 
ATOM   1068 C  CB  B ASP   A 1 129 ? -8.623  17.511  13.762  0.50 12.57 ? 130 ASP   A CB  1 
ATOM   1069 C  CG  A ASP   A 1 129 ? -6.572  18.258  14.384  0.50 11.75 ? 130 ASP   A CG  1 
ATOM   1070 C  CG  B ASP   A 1 129 ? -7.221  18.021  14.015  0.50 12.57 ? 130 ASP   A CG  1 
ATOM   1071 O  OD1 A ASP   A 1 129 ? -5.734  17.358  14.602  0.50 12.44 ? 130 ASP   A OD1 1 
ATOM   1072 O  OD1 B ASP   A 1 129 ? -6.637  17.697  15.077  0.50 16.69 ? 130 ASP   A OD1 1 
ATOM   1073 O  OD2 A ASP   A 1 129 ? -6.315  19.474  14.545  0.50 14.47 ? 130 ASP   A OD2 1 
ATOM   1074 O  OD2 B ASP   A 1 129 ? -6.734  18.746  13.160  0.50 15.46 ? 130 ASP   A OD2 1 
ATOM   1075 N  N   . PHE   A 1 130 ? -8.235  14.757  14.734  1.00 11.40 ? 131 PHE   A N   1 
ATOM   1076 C  CA  . PHE   A 1 130 ? -7.681  13.493  15.141  1.00 10.22 ? 131 PHE   A CA  1 
ATOM   1077 C  C   . PHE   A 1 130 ? -6.215  13.650  15.578  1.00 10.28 ? 131 PHE   A C   1 
ATOM   1078 O  O   . PHE   A 1 130 ? -5.785  13.055  16.547  1.00 10.19 ? 131 PHE   A O   1 
ATOM   1079 C  CB  . PHE   A 1 130 ? -7.842  12.497  13.989  1.00 11.05 ? 131 PHE   A CB  1 
ATOM   1080 C  CG  . PHE   A 1 130 ? -7.206  11.179  14.274  1.00 10.01 ? 131 PHE   A CG  1 
ATOM   1081 C  CD1 . PHE   A 1 130 ? -7.888  10.178  14.939  1.00 11.13 ? 131 PHE   A CD1 1 
ATOM   1082 C  CD2 . PHE   A 1 130 ? -5.905  10.890  13.912  1.00 12.32 ? 131 PHE   A CD2 1 
ATOM   1083 C  CE1 . PHE   A 1 130 ? -7.325  8.947   15.193  1.00 12.11 ? 131 PHE   A CE1 1 
ATOM   1084 C  CE2 . PHE   A 1 130 ? -5.333  9.663   14.173  1.00 13.96 ? 131 PHE   A CE2 1 
ATOM   1085 C  CZ  . PHE   A 1 130 ? -6.050  8.700   14.825  1.00 13.81 ? 131 PHE   A CZ  1 
ATOM   1086 N  N   . GLY   A 1 131 ? -5.430  14.412  14.808  1.00 11.50 ? 132 GLY   A N   1 
ATOM   1087 C  CA  . GLY   A 1 131 ? -4.019  14.563  15.109  1.00 12.07 ? 132 GLY   A CA  1 
ATOM   1088 C  C   . GLY   A 1 131 ? -3.744  15.200  16.467  1.00 11.32 ? 132 GLY   A C   1 
ATOM   1089 O  O   . GLY   A 1 131 ? -2.759  14.877  17.116  1.00 13.59 ? 132 GLY   A O   1 
ATOM   1090 N  N   . LYS   A 1 132 ? -4.593  16.134  16.885  1.00 11.33 ? 133 LYS   A N   1 
ATOM   1091 C  CA  . LYS   A 1 132 ? -4.502  16.707  18.220  1.00 10.94 ? 133 LYS   A CA  1 
ATOM   1092 C  C   . LYS   A 1 132 ? -4.987  15.698  19.257  1.00 10.31 ? 133 LYS   A C   1 
ATOM   1093 O  O   . LYS   A 1 132 ? -4.428  15.588  20.364  1.00 11.31 ? 133 LYS   A O   1 
ATOM   1094 C  CB  . LYS   A 1 132 ? -5.276  18.014  18.261  1.00 11.98 ? 133 LYS   A CB  1 
ATOM   1095 C  CG  . LYS   A 1 132 ? -4.694  19.105  17.389  1.00 18.34 ? 133 LYS   A CG  1 
ATOM   1096 N  N   . ALA   A 1 133 ? -6.075  14.987  18.955  1.00 9.91  ? 134 ALA   A N   1 
ATOM   1097 C  CA  . ALA   A 1 133 ? -6.646  14.051  19.905  1.00 8.93  ? 134 ALA   A CA  1 
ATOM   1098 C  C   . ALA   A 1 133 ? -5.669  12.974  20.312  1.00 9.40  ? 134 ALA   A C   1 
ATOM   1099 O  O   . ALA   A 1 133 ? -5.669  12.584  21.469  1.00 9.74  ? 134 ALA   A O   1 
ATOM   1100 C  CB  . ALA   A 1 133 ? -7.898  13.457  19.324  1.00 9.29  ? 134 ALA   A CB  1 
ATOM   1101 N  N   . VAL   A 1 134 ? -4.837  12.459  19.393  1.00 9.43  ? 135 VAL   A N   1 
ATOM   1102 C  CA  . VAL   A 1 134 ? -3.947  11.361  19.757  1.00 10.32 ? 135 VAL   A CA  1 
ATOM   1103 C  C   . VAL   A 1 134 ? -2.844  11.780  20.720  1.00 10.28 ? 135 VAL   A C   1 
ATOM   1104 O  O   . VAL   A 1 134 ? -2.162  10.930  21.278  1.00 11.32 ? 135 VAL   A O   1 
ATOM   1105 C  CB  . VAL   A 1 134 ? -3.307  10.661  18.550  1.00 11.15 ? 135 VAL   A CB  1 
ATOM   1106 C  CG1 . VAL   A 1 134 ? -4.371  9.996   17.708  1.00 12.14 ? 135 VAL   A CG1 1 
ATOM   1107 C  CG2 . VAL   A 1 134 ? -2.443  11.563  17.700  1.00 11.61 ? 135 VAL   A CG2 1 
ATOM   1108 N  N   . GLN   A 1 135 ? -2.707  13.091  20.938  1.00 10.42 ? 136 GLN   A N   1 
ATOM   1109 C  CA  . GLN   A 1 135 ? -1.751  13.623  21.902  1.00 11.63 ? 136 GLN   A CA  1 
ATOM   1110 C  C   . GLN   A 1 135 ? -2.328  13.760  23.293  1.00 11.19 ? 136 GLN   A C   1 
ATOM   1111 O  O   . GLN   A 1 135 ? -1.660  14.314  24.159  1.00 13.13 ? 136 GLN   A O   1 
ATOM   1112 C  CB  . GLN   A 1 135 ? -1.179  14.972  21.414  1.00 13.49 ? 136 GLN   A CB  1 
ATOM   1113 C  CG  . GLN   A 1 135 ? -0.563  14.872  20.027  1.00 17.35 ? 136 GLN   A CG  1 
ATOM   1114 C  CD  . GLN   A 1 135 ? -0.086  16.210  19.549  1.00 21.68 ? 136 GLN   A CD  1 
ATOM   1115 O  OE1 . GLN   A 1 135 ? 0.761   16.850  20.173  1.00 28.58 ? 136 GLN   A OE1 1 
ATOM   1116 N  NE2 . GLN   A 1 135 ? -0.619  16.640  18.415  1.00 23.55 ? 136 GLN   A NE2 1 
ATOM   1117 N  N   . GLN   A 1 136 ? -3.566  13.303  23.501  1.00 10.37 ? 137 GLN   A N   1 
ATOM   1118 C  CA  . GLN   A 1 136 ? -4.247  13.497  24.767  1.00 9.98  ? 137 GLN   A CA  1 
ATOM   1119 C  C   . GLN   A 1 136 ? -4.597  12.153  25.360  1.00 10.29 ? 137 GLN   A C   1 
ATOM   1120 O  O   . GLN   A 1 136 ? -4.938  11.200  24.657  1.00 10.10 ? 137 GLN   A O   1 
ATOM   1121 C  CB  . GLN   A 1 136 ? -5.552  14.251  24.566  1.00 10.64 ? 137 GLN   A CB  1 
ATOM   1122 C  CG  . GLN   A 1 136 ? -5.454  15.454  23.656  1.00 12.93 ? 137 GLN   A CG  1 
ATOM   1123 C  CD  . GLN   A 1 136 ? -4.419  16.384  24.096  1.00 14.39 ? 137 GLN   A CD  1 
ATOM   1124 O  OE1 . GLN   A 1 136 ? -4.239  16.622  25.302  1.00 15.47 ? 137 GLN   A OE1 1 
ATOM   1125 N  NE2 . GLN   A 1 136 ? -3.822  17.006  23.078  1.00 15.92 ? 137 GLN   A NE2 1 
ATOM   1126 N  N   . PRO   A 1 137 ? -4.606  12.045  26.711  1.00 10.49 ? 138 PRO   A N   1 
ATOM   1127 C  CA  . PRO   A 1 137 ? -4.878  10.772  27.349  1.00 11.24 ? 138 PRO   A CA  1 
ATOM   1128 C  C   . PRO   A 1 137 ? -6.309  10.272  27.174  1.00 10.95 ? 138 PRO   A C   1 
ATOM   1129 O  O   . PRO   A 1 137 ? -6.522  9.080   27.302  1.00 14.75 ? 138 PRO   A O   1 
ATOM   1130 C  CB  . PRO   A 1 137 ? -4.558  10.992  28.826  1.00 12.98 ? 138 PRO   A CB  1 
ATOM   1131 C  CG  . PRO   A 1 137 ? -4.560  12.447  28.990  1.00 16.50 ? 138 PRO   A CG  1 
ATOM   1132 C  CD  . PRO   A 1 137 ? -4.184  13.073  27.677  1.00 12.02 ? 138 PRO   A CD  1 
ATOM   1133 N  N   . ASP   A 1 138 ? -7.238  11.178  26.853  1.00 10.25 ? 139 ASP   A N   1 
ATOM   1134 C  CA  . ASP   A 1 138 ? -8.625  10.847  26.583  1.00 10.26 ? 139 ASP   A CA  1 
ATOM   1135 C  C   . ASP   A 1 138 ? -8.977  11.255  25.162  1.00 9.85  ? 139 ASP   A C   1 
ATOM   1136 O  O   . ASP   A 1 138 ? -10.099 11.680  24.883  1.00 11.35 ? 139 ASP   A O   1 
ATOM   1137 C  CB  . ASP   A 1 138 ? -9.570  11.476  27.580  1.00 12.64 ? 139 ASP   A CB  1 
ATOM   1138 C  CG  . ASP   A 1 138 ? -9.515  12.976  27.590  1.00 13.04 ? 139 ASP   A CG  1 
ATOM   1139 O  OD1 . ASP   A 1 138 ? -8.575  13.555  27.003  1.00 13.46 ? 139 ASP   A OD1 1 
ATOM   1140 O  OD2 . ASP   A 1 138 ? -10.368 13.565  28.265  1.00 16.49 ? 139 ASP   A OD2 1 
ATOM   1141 N  N   . GLY   A 1 139 ? -8.051  11.143  24.225  1.00 8.84  ? 140 GLY   A N   1 
ATOM   1142 C  CA  . GLY   A 1 139 ? -8.279  11.626  22.878  1.00 8.74  ? 140 GLY   A CA  1 
ATOM   1143 C  C   . GLY   A 1 139 ? -9.133  10.725  22.017  1.00 7.75  ? 140 GLY   A C   1 
ATOM   1144 O  O   . GLY   A 1 139 ? -9.820  11.236  21.139  1.00 8.36  ? 140 GLY   A O   1 
ATOM   1145 N  N   . LEU   A 1 140 ? -9.002  9.404   22.162  1.00 7.78  ? 141 LEU   A N   1 
ATOM   1146 C  CA  A LEU   A 1 140 ? -9.676  8.466   21.276  0.50 7.36  ? 141 LEU   A CA  1 
ATOM   1147 C  CA  B LEU   A 1 140 ? -9.638  8.443   21.289  0.50 7.80  ? 141 LEU   A CA  1 
ATOM   1148 C  C   . LEU   A 1 140 ? -10.534 7.517   22.093  1.00 7.33  ? 141 LEU   A C   1 
ATOM   1149 O  O   . LEU   A 1 140 ? -10.256 7.229   23.255  1.00 7.92  ? 141 LEU   A O   1 
ATOM   1150 C  CB  A LEU   A 1 140 ? -8.719  7.596   20.445  0.50 7.08  ? 141 LEU   A CB  1 
ATOM   1151 C  CB  B LEU   A 1 140 ? -8.569  7.601   20.590  0.50 8.38  ? 141 LEU   A CB  1 
ATOM   1152 C  CG  A LEU   A 1 140 ? -7.737  8.313   19.522  0.50 7.12  ? 141 LEU   A CG  1 
ATOM   1153 C  CG  B LEU   A 1 140 ? -8.184  8.062   19.192  0.50 9.25  ? 141 LEU   A CG  1 
ATOM   1154 C  CD1 A LEU   A 1 140 ? -6.984  7.291   18.668  0.50 7.55  ? 141 LEU   A CD1 1 
ATOM   1155 C  CD1 B LEU   A 1 140 ? -7.617  9.459   19.182  0.50 10.47 ? 141 LEU   A CD1 1 
ATOM   1156 C  CD2 A LEU   A 1 140 ? -8.446  9.317   18.621  0.50 7.11  ? 141 LEU   A CD2 1 
ATOM   1157 C  CD2 B LEU   A 1 140 ? -7.251  7.035   18.562  0.50 9.47  ? 141 LEU   A CD2 1 
ATOM   1158 N  N   . ALA   A 1 141 ? -11.557 6.974   21.429  1.00 7.39  ? 142 ALA   A N   1 
ATOM   1159 C  CA  . ALA   A 1 141 ? -12.338 5.852   21.920  1.00 7.67  ? 142 ALA   A CA  1 
ATOM   1160 C  C   . ALA   A 1 141 ? -12.383 4.839   20.801  1.00 7.37  ? 142 ALA   A C   1 
ATOM   1161 O  O   . ALA   A 1 141 ? -12.784 5.194   19.690  1.00 7.99  ? 142 ALA   A O   1 
ATOM   1162 C  CB  . ALA   A 1 141 ? -13.726 6.260   22.343  1.00 8.69  ? 142 ALA   A CB  1 
ATOM   1163 N  N   . VAL   A 1 142 ? -11.908 3.633   21.058  1.00 7.04  ? 143 VAL   A N   1 
ATOM   1164 C  CA  . VAL   A 1 142 ? -11.940 2.592   20.050  1.00 6.99  ? 143 VAL   A CA  1 
ATOM   1165 C  C   . VAL   A 1 142 ? -12.902 1.534   20.544  1.00 7.04  ? 143 VAL   A C   1 
ATOM   1166 O  O   . VAL   A 1 142 ? -12.757 1.016   21.657  1.00 7.62  ? 143 VAL   A O   1 
ATOM   1167 C  CB  . VAL   A 1 142 ? -10.562 2.018   19.683  1.00 7.37  ? 143 VAL   A CB  1 
ATOM   1168 C  CG1 . VAL   A 1 142 ? -10.727 0.998   18.558  1.00 8.28  ? 143 VAL   A CG1 1 
ATOM   1169 C  CG2 . VAL   A 1 142 ? -9.613  3.096   19.244  1.00 8.63  ? 143 VAL   A CG2 1 
ATOM   1170 N  N   . LEU   A 1 143 ? -13.904 1.258   19.718  1.00 7.31  ? 144 LEU   A N   1 
ATOM   1171 C  CA  . LEU   A 1 143 ? -14.882 0.201   19.944  1.00 7.58  ? 144 LEU   A CA  1 
ATOM   1172 C  C   . LEU   A 1 143 ? -14.367 -1.050  19.256  1.00 7.61  ? 144 LEU   A C   1 
ATOM   1173 O  O   . LEU   A 1 143 ? -14.192 -1.061  18.040  1.00 8.40  ? 144 LEU   A O   1 
ATOM   1174 C  CB  . LEU   A 1 143 ? -16.229 0.663   19.386  1.00 8.85  ? 144 LEU   A CB  1 
ATOM   1175 C  CG  . LEU   A 1 143 ? -17.410 -0.269  19.573  1.00 10.05 ? 144 LEU   A CG  1 
ATOM   1176 C  CD1 . LEU   A 1 143 ? -17.668 -0.582  21.016  1.00 12.27 ? 144 LEU   A CD1 1 
ATOM   1177 C  CD2 . LEU   A 1 143 ? -18.641 0.322   18.904  1.00 11.75 ? 144 LEU   A CD2 1 
ATOM   1178 N  N   . GLY   A 1 144 ? -14.056 -2.062  20.063  1.00 7.31  ? 145 GLY   A N   1 
ATOM   1179 C  CA  . GLY   A 1 144 ? -13.527 -3.313  19.570  1.00 7.43  ? 145 GLY   A CA  1 
ATOM   1180 C  C   . GLY   A 1 144 ? -14.572 -4.400  19.591  1.00 6.96  ? 145 GLY   A C   1 
ATOM   1181 O  O   . GLY   A 1 144 ? -15.293 -4.553  20.577  1.00 8.15  ? 145 GLY   A O   1 
ATOM   1182 N  N   . ILE   A 1 145 ? -14.639 -5.154  18.496  1.00 6.72  ? 146 ILE   A N   1 
ATOM   1183 C  CA  . ILE   A 1 145 ? -15.629 -6.191  18.313  1.00 6.99  ? 146 ILE   A CA  1 
ATOM   1184 C  C   . ILE   A 1 145 ? -14.910 -7.428  17.813  1.00 6.84  ? 146 ILE   A C   1 
ATOM   1185 O  O   . ILE   A 1 145 ? -14.207 -7.388  16.806  1.00 7.75  ? 146 ILE   A O   1 
ATOM   1186 C  CB  . ILE   A 1 145 ? -16.744 -5.737  17.345  1.00 7.71  ? 146 ILE   A CB  1 
ATOM   1187 C  CG1 . ILE   A 1 145 ? -17.383 -4.450  17.826  1.00 9.27  ? 146 ILE   A CG1 1 
ATOM   1188 C  CG2 . ILE   A 1 145 ? -17.774 -6.830  17.155  1.00 9.78  ? 146 ILE   A CG2 1 
ATOM   1189 C  CD1 . ILE   A 1 145 ? -18.430 -3.862  16.953  1.00 9.30  ? 146 ILE   A CD1 1 
ATOM   1190 N  N   . PHE   A 1 146 ? -15.083 -8.541  18.487  1.00 6.97  ? 147 PHE   A N   1 
ATOM   1191 C  CA  . PHE   A 1 146 ? -14.467 -9.794  18.075  1.00 7.18  ? 147 PHE   A CA  1 
ATOM   1192 C  C   . PHE   A 1 146 ? -15.240 -10.411 16.928  1.00 7.88  ? 147 PHE   A C   1 
ATOM   1193 O  O   . PHE   A 1 146 ? -16.471 -10.323 16.858  1.00 8.36  ? 147 PHE   A O   1 
ATOM   1194 C  CB  . PHE   A 1 146 ? -14.467 -10.765 19.258  1.00 7.37  ? 147 PHE   A CB  1 
ATOM   1195 C  CG  . PHE   A 1 146 ? -13.609 -10.314 20.415  1.00 7.63  ? 147 PHE   A CG  1 
ATOM   1196 C  CD1 . PHE   A 1 146 ? -12.257 -10.131 20.235  1.00 8.11  ? 147 PHE   A CD1 1 
ATOM   1197 C  CD2 . PHE   A 1 146 ? -14.144 -10.045 21.646  1.00 8.30  ? 147 PHE   A CD2 1 
ATOM   1198 C  CE1 . PHE   A 1 146 ? -11.438 -9.735  21.279  1.00 8.43  ? 147 PHE   A CE1 1 
ATOM   1199 C  CE2 . PHE   A 1 146 ? -13.331 -9.632  22.687  1.00 8.51  ? 147 PHE   A CE2 1 
ATOM   1200 C  CZ  . PHE   A 1 146 ? -11.989 -9.501  22.512  1.00 8.59  ? 147 PHE   A CZ  1 
ATOM   1201 N  N   . LEU   A 1 147 ? -14.501 -11.116 16.054  1.00 7.53  ? 148 LEU   A N   1 
ATOM   1202 C  CA  . LEU   A 1 147 ? -15.071 -11.919 14.975  1.00 7.66  ? 148 LEU   A CA  1 
ATOM   1203 C  C   . LEU   A 1 147 ? -14.726 -13.378 15.201  1.00 8.04  ? 148 LEU   A C   1 
ATOM   1204 O  O   . LEU   A 1 147 ? -13.553 -13.723 15.401  1.00 8.84  ? 148 LEU   A O   1 
ATOM   1205 C  CB  . LEU   A 1 147 ? -14.505 -11.512 13.602  1.00 8.41  ? 148 LEU   A CB  1 
ATOM   1206 C  CG  . LEU   A 1 147 ? -15.060 -10.261 12.942  1.00 8.20  ? 148 LEU   A CG  1 
ATOM   1207 C  CD1 . LEU   A 1 147 ? -14.849 -9.014  13.744  1.00 9.10  ? 148 LEU   A CD1 1 
ATOM   1208 C  CD2 . LEU   A 1 147 ? -14.451 -10.084 11.575  1.00 9.37  ? 148 LEU   A CD2 1 
ATOM   1209 N  N   . LYS   A 1 148 ? -15.741 -14.235 15.133  1.00 8.82  ? 149 LYS   A N   1 
ATOM   1210 C  CA  . LYS   A 1 148 ? -15.568 -15.669 15.077  1.00 9.67  ? 149 LYS   A CA  1 
ATOM   1211 C  C   . LYS   A 1 148 ? -16.052 -16.191 13.743  1.00 10.33 ? 149 LYS   A C   1 
ATOM   1212 O  O   . LYS   A 1 148 ? -16.858 -15.542 13.094  1.00 11.43 ? 149 LYS   A O   1 
ATOM   1213 C  CB  . LYS   A 1 148 ? -16.280 -16.370 16.209  1.00 11.87 ? 149 LYS   A CB  1 
ATOM   1214 C  CG  . LYS   A 1 148 ? -17.780 -16.220 16.238  1.00 14.25 ? 149 LYS   A CG  1 
ATOM   1215 C  CD  . LYS   A 1 148 ? -18.392 -16.883 17.467  1.00 19.51 ? 149 LYS   A CD  1 
ATOM   1216 N  N   . VAL   A 1 149 ? -15.525 -17.308 13.333  1.00 10.96 ? 150 VAL   A N   1 
ATOM   1217 C  CA  . VAL   A 1 149 ? -15.933 -17.919 12.057  1.00 10.88 ? 150 VAL   A CA  1 
ATOM   1218 C  C   . VAL   A 1 149 ? -17.126 -18.844 12.276  1.00 11.71 ? 150 VAL   A C   1 
ATOM   1219 O  O   . VAL   A 1 149 ? -17.069 -19.781 13.086  1.00 13.25 ? 150 VAL   A O   1 
ATOM   1220 C  CB  . VAL   A 1 149 ? -14.749 -18.641 11.402  1.00 11.92 ? 150 VAL   A CB  1 
ATOM   1221 C  CG1 . VAL   A 1 149 ? -15.176 -19.419 10.169  1.00 13.21 ? 150 VAL   A CG1 1 
ATOM   1222 C  CG2 . VAL   A 1 149 ? -13.650 -17.649 11.071  1.00 13.91 ? 150 VAL   A CG2 1 
ATOM   1223 N  N   . GLY   A 1 150 ? -18.190 -18.592 11.522  1.00 11.19 ? 151 GLY   A N   1 
ATOM   1224 C  CA  . GLY   A 1 150 ? -19.378 -19.420 11.547  1.00 12.44 ? 151 GLY   A CA  1 
ATOM   1225 C  C   . GLY   A 1 150 ? -20.277 -18.989 10.397  1.00 11.42 ? 151 GLY   A C   1 
ATOM   1226 O  O   . GLY   A 1 150 ? -19.901 -19.102 9.237   1.00 12.35 ? 151 GLY   A O   1 
ATOM   1227 N  N   . SER   A 1 151 ? -21.465 -18.478 10.719  1.00 12.16 ? 152 SER   A N   1 
ATOM   1228 C  CA  . SER   A 1 151 ? -22.354 -17.938 9.705   1.00 12.54 ? 152 SER   A CA  1 
ATOM   1229 C  C   . SER   A 1 151 ? -21.790 -16.625 9.156   1.00 11.84 ? 152 SER   A C   1 
ATOM   1230 O  O   . SER   A 1 151 ? -21.072 -15.908 9.819   1.00 11.54 ? 152 SER   A O   1 
ATOM   1231 C  CB  A SER   A 1 151 ? -23.752 -17.783 10.213  0.50 15.46 ? 152 SER   A CB  1 
ATOM   1232 C  CB  B SER   A 1 151 ? -23.752 -17.672 10.253  0.50 16.06 ? 152 SER   A CB  1 
ATOM   1233 O  OG  A SER   A 1 151 ? -23.776 -16.775 11.185  0.50 17.42 ? 152 SER   A OG  1 
ATOM   1234 O  OG  B SER   A 1 151 ? -24.283 -18.797 10.919  0.50 19.17 ? 152 SER   A OG  1 
ATOM   1235 N  N   . ALA   A 1 152 ? -22.111 -16.318 7.897   1.00 11.40 ? 153 ALA   A N   1 
ATOM   1236 C  CA  . ALA   A 1 152 ? -21.716 -15.064 7.297   1.00 11.01 ? 153 ALA   A CA  1 
ATOM   1237 C  C   . ALA   A 1 152 ? -22.344 -13.884 8.019   1.00 11.15 ? 153 ALA   A C   1 
ATOM   1238 O  O   . ALA   A 1 152 ? -23.432 -13.942 8.578   1.00 12.68 ? 153 ALA   A O   1 
ATOM   1239 C  CB  . ALA   A 1 152 ? -22.132 -15.036 5.850   1.00 13.34 ? 153 ALA   A CB  1 
ATOM   1240 N  N   . LYS   A 1 153 ? -21.641 -12.743 7.950   1.00 10.81 ? 154 LYS   A N   1 
ATOM   1241 C  CA  . LYS   A 1 153 ? -22.142 -11.462 8.389   1.00 11.01 ? 154 LYS   A CA  1 
ATOM   1242 C  C   . LYS   A 1 153 ? -22.601 -10.684 7.177   1.00 10.60 ? 154 LYS   A C   1 
ATOM   1243 O  O   . LYS   A 1 153 ? -21.774 -10.208 6.383   1.00 10.35 ? 154 LYS   A O   1 
ATOM   1244 C  CB  . LYS   A 1 153 ? -21.078 -10.684 9.136   1.00 11.46 ? 154 LYS   A CB  1 
ATOM   1245 C  CG  . LYS   A 1 153 ? -21.562 -9.460  9.871   1.00 12.42 ? 154 LYS   A CG  1 
ATOM   1246 C  CD  . LYS   A 1 153 ? -22.436 -9.778  11.051  1.00 14.31 ? 154 LYS   A CD  1 
ATOM   1247 C  CE  . LYS   A 1 153 ? -22.636 -8.589  11.949  1.00 15.03 ? 154 LYS   A CE  1 
ATOM   1248 N  NZ  . LYS   A 1 153 ? -23.538 -8.936  13.057  1.00 17.40 ? 154 LYS   A NZ  1 
ATOM   1249 N  N   . PRO   A 1 154 ? -23.924 -10.569 6.921   1.00 11.61 ? 155 PRO   A N   1 
ATOM   1250 C  CA  . PRO   A 1 154 ? -24.325 -9.960  5.653   1.00 12.67 ? 155 PRO   A CA  1 
ATOM   1251 C  C   . PRO   A 1 154 ? -23.819 -8.543  5.487   1.00 11.21 ? 155 PRO   A C   1 
ATOM   1252 O  O   . PRO   A 1 154 ? -23.446 -8.172  4.380   1.00 13.14 ? 155 PRO   A O   1 
ATOM   1253 C  CB  . PRO   A 1 154 ? -25.847 -10.087 5.677   1.00 14.98 ? 155 PRO   A CB  1 
ATOM   1254 C  CG  . PRO   A 1 154 ? -26.083 -11.281 6.571   1.00 17.48 ? 155 PRO   A CG  1 
ATOM   1255 C  CD  . PRO   A 1 154 ? -25.057 -11.117 7.689   1.00 14.07 ? 155 PRO   A CD  1 
ATOM   1256 N  N   . GLY   A 1 155 ? -23.790 -7.790  6.582   1.00 10.74 ? 156 GLY   A N   1 
ATOM   1257 C  CA  . GLY   A 1 155 ? -23.375 -6.404  6.516   1.00 11.53 ? 156 GLY   A CA  1 
ATOM   1258 C  C   . GLY   A 1 155 ? -21.876 -6.219  6.282   1.00 11.29 ? 156 GLY   A C   1 
ATOM   1259 O  O   . GLY   A 1 155 ? -21.444 -5.094  6.029   1.00 13.57 ? 156 GLY   A O   1 
ATOM   1260 N  N   . LEU   A 1 156 ? -21.079 -7.283  6.326   1.00 10.53 ? 157 LEU   A N   1 
ATOM   1261 C  CA  . LEU   A 1 156 ? -19.677 -7.218  5.984   1.00 9.99  ? 157 LEU   A CA  1 
ATOM   1262 C  C   . LEU   A 1 156 ? -19.438 -7.428  4.509   1.00 9.82  ? 157 LEU   A C   1 
ATOM   1263 O  O   . LEU   A 1 156 ? -18.343 -7.144  4.010   1.00 10.55 ? 157 LEU   A O   1 
ATOM   1264 C  CB  . LEU   A 1 156 ? -18.934 -8.277  6.797   1.00 10.52 ? 157 LEU   A CB  1 
ATOM   1265 C  CG  . LEU   A 1 156 ? -17.414 -8.369  6.657   1.00 11.10 ? 157 LEU   A CG  1 
ATOM   1266 C  CD1 . LEU   A 1 156 ? -16.720 -7.081  7.046   1.00 12.08 ? 157 LEU   A CD1 1 
ATOM   1267 C  CD2 . LEU   A 1 156 ? -16.881 -9.533  7.466   1.00 12.34 ? 157 LEU   A CD2 1 
ATOM   1268 N  N   . GLN   A 1 157 ? -20.395 -8.009  3.763   1.00 10.67 ? 158 GLN   A N   1 
ATOM   1269 C  CA  . GLN   A 1 157 ? -20.077 -8.498  2.430   1.00 10.74 ? 158 GLN   A CA  1 
ATOM   1270 C  C   . GLN   A 1 157 ? -19.658 -7.365  1.504   1.00 10.70 ? 158 GLN   A C   1 
ATOM   1271 O  O   . GLN   A 1 157 ? -18.803 -7.581  0.662   1.00 10.91 ? 158 GLN   A O   1 
ATOM   1272 C  CB  . GLN   A 1 157 ? -21.216 -9.317  1.871   1.00 11.69 ? 158 GLN   A CB  1 
ATOM   1273 C  CG  . GLN   A 1 157 ? -20.832 -10.033 0.585   1.00 12.33 ? 158 GLN   A CG  1 
ATOM   1274 C  CD  . GLN   A 1 157 ? -19.714 -11.028 0.796   1.00 11.69 ? 158 GLN   A CD  1 
ATOM   1275 O  OE1 . GLN   A 1 157 ? -19.543 -11.620 1.872   1.00 12.16 ? 158 GLN   A OE1 1 
ATOM   1276 N  NE2 . GLN   A 1 157 ? -18.948 -11.253 -0.254  1.00 13.59 ? 158 GLN   A NE2 1 
ATOM   1277 N  N   . LYS   A 1 158 ? -20.236 -6.154  1.624   1.00 10.89 ? 159 LYS   A N   1 
ATOM   1278 C  CA  . LYS   A 1 158 ? -19.825 -5.065  0.753   1.00 11.74 ? 159 LYS   A CA  1 
ATOM   1279 C  C   . LYS   A 1 158 ? -18.338 -4.734  0.907   1.00 11.43 ? 159 LYS   A C   1 
ATOM   1280 O  O   . LYS   A 1 158 ? -17.662 -4.327  -0.039  1.00 12.50 ? 159 LYS   A O   1 
ATOM   1281 C  CB  . LYS   A 1 158 ? -20.693 -3.846  1.024   1.00 14.43 ? 159 LYS   A CB  1 
ATOM   1282 C  CG  . LYS   A 1 158 ? -22.058 -3.905  0.358   1.00 20.25 ? 159 LYS   A CG  1 
ATOM   1283 N  N   . VAL   A 1 159 ? -17.849 -4.835  2.138   1.00 10.61 ? 160 VAL   A N   1 
ATOM   1284 C  CA  . VAL   A 1 159 ? -16.412 -4.669  2.390   1.00 10.16 ? 160 VAL   A CA  1 
ATOM   1285 C  C   . VAL   A 1 159 ? -15.604 -5.770  1.706   1.00 10.27 ? 160 VAL   A C   1 
ATOM   1286 O  O   . VAL   A 1 159 ? -14.664 -5.508  0.971   1.00 11.76 ? 160 VAL   A O   1 
ATOM   1287 C  CB  . VAL   A 1 159 ? -16.129 -4.652  3.900   1.00 10.90 ? 160 VAL   A CB  1 
ATOM   1288 C  CG1 . VAL   A 1 159 ? -14.622 -4.640  4.195   1.00 12.33 ? 160 VAL   A CG1 1 
ATOM   1289 C  CG2 . VAL   A 1 159 ? -16.789 -3.481  4.566   1.00 12.27 ? 160 VAL   A CG2 1 
ATOM   1290 N  N   . VAL   A 1 160 ? -15.994 -7.019  1.910   1.00 10.30 ? 161 VAL   A N   1 
ATOM   1291 C  CA  . VAL   A 1 160 ? -15.319 -8.158  1.316   1.00 12.30 ? 161 VAL   A CA  1 
ATOM   1292 C  C   . VAL   A 1 160 ? -15.188 -8.008  -0.179  1.00 12.14 ? 161 VAL   A C   1 
ATOM   1293 O  O   . VAL   A 1 160 ? -14.158 -8.304  -0.776  1.00 14.09 ? 161 VAL   A O   1 
ATOM   1294 C  CB  . VAL   A 1 160 ? -16.061 -9.486  1.692   1.00 14.61 ? 161 VAL   A CB  1 
ATOM   1295 C  CG1 . VAL   A 1 160 ? -15.555 -10.651 0.861   1.00 14.40 ? 161 VAL   A CG1 1 
ATOM   1296 C  CG2 . VAL   A 1 160 ? -15.948 -9.725  3.191   1.00 15.49 ? 161 VAL   A CG2 1 
ATOM   1297 N  N   . ASP   A 1 161 ? -16.275 -7.585  -0.797  1.00 12.61 ? 162 ASP   A N   1 
ATOM   1298 C  CA  . ASP   A 1 161 ? -16.287 -7.583  -2.238  1.00 14.61 ? 162 ASP   A CA  1 
ATOM   1299 C  C   . ASP   A 1 161 ? -15.437 -6.506  -2.889  1.00 14.14 ? 162 ASP   A C   1 
ATOM   1300 O  O   . ASP   A 1 161 ? -15.149 -6.615  -4.070  1.00 19.49 ? 162 ASP   A O   1 
ATOM   1301 C  CB  . ASP   A 1 161 ? -17.710 -7.527  -2.692  1.00 17.50 ? 162 ASP   A CB  1 
ATOM   1302 C  CG  . ASP   A 1 161 ? -18.311 -8.941  -2.639  1.00 19.20 ? 162 ASP   A CG  1 
ATOM   1303 O  OD1 . ASP   A 1 161 ? -17.565 -10.025 -2.680  1.00 22.40 ? 162 ASP   A OD1 1 
ATOM   1304 O  OD2 . ASP   A 1 161 ? -19.467 -8.996  -2.465  1.00 20.89 ? 162 ASP   A OD2 1 
ATOM   1305 N  N   . VAL   A 1 162 ? -15.059 -5.459  -2.167  1.00 12.13 ? 163 VAL   A N   1 
ATOM   1306 C  CA  . VAL   A 1 162 ? -14.210 -4.422  -2.724  1.00 12.89 ? 163 VAL   A CA  1 
ATOM   1307 C  C   . VAL   A 1 162 ? -12.721 -4.728  -2.548  1.00 12.28 ? 163 VAL   A C   1 
ATOM   1308 O  O   . VAL   A 1 162 ? -11.868 -4.027  -3.083  1.00 12.71 ? 163 VAL   A O   1 
ATOM   1309 C  CB  . VAL   A 1 162 ? -14.564 -3.040  -2.129  1.00 14.58 ? 163 VAL   A CB  1 
ATOM   1310 C  CG1 . VAL   A 1 162 ? -14.057 -2.855  -0.749  1.00 14.87 ? 163 VAL   A CG1 1 
ATOM   1311 C  CG2 . VAL   A 1 162 ? -14.164 -1.837  -2.964  1.00 16.80 ? 163 VAL   A CG2 1 
ATOM   1312 N  N   . LEU   A 1 163 ? -12.372 -5.729  -1.740  1.00 11.83 ? 164 LEU   A N   1 
ATOM   1313 C  CA  . LEU   A 1 163 ? -10.986 -5.947  -1.383  1.00 11.44 ? 164 LEU   A CA  1 
ATOM   1314 C  C   . LEU   A 1 163 ? -10.103 -6.272  -2.588  1.00 12.51 ? 164 LEU   A C   1 
ATOM   1315 O  O   . LEU   A 1 163 ? -8.937  -5.915  -2.575  1.00 12.70 ? 164 LEU   A O   1 
ATOM   1316 C  CB  . LEU   A 1 163 ? -10.849 -7.017  -0.302  1.00 11.85 ? 164 LEU   A CB  1 
ATOM   1317 C  CG  . LEU   A 1 163 ? -11.511 -6.683  1.044   1.00 11.42 ? 164 LEU   A CG  1 
ATOM   1318 C  CD1 . LEU   A 1 163 ? -11.276 -7.801  2.040   1.00 12.93 ? 164 LEU   A CD1 1 
ATOM   1319 C  CD2 . LEU   A 1 163 ? -11.039 -5.357  1.608   1.00 11.59 ? 164 LEU   A CD2 1 
ATOM   1320 N  N   . ASP   A 1 164 ? -10.664 -6.891  -3.608  1.00 14.99 ? 165 ASP   A N   1 
ATOM   1321 C  CA  . ASP   A 1 164 ? -9.904  -7.171  -4.817  1.00 18.16 ? 165 ASP   A CA  1 
ATOM   1322 C  C   . ASP   A 1 164 ? -9.384  -5.892  -5.468  1.00 16.63 ? 165 ASP   A C   1 
ATOM   1323 O  O   . ASP   A 1 164 ? -8.397  -5.960  -6.195  1.00 21.90 ? 165 ASP   A O   1 
ATOM   1324 C  CB  . ASP   A 1 164 ? -10.723 -8.019  -5.810  1.00 20.77 ? 165 ASP   A CB  1 
ATOM   1325 N  N   . SER   A 1 165 ? -10.057 -4.754  -5.279  1.00 13.30 ? 166 SER   A N   1 
ATOM   1326 C  CA  . SER   A 1 165 ? -9.673  -3.491  -5.854  1.00 13.90 ? 166 SER   A CA  1 
ATOM   1327 C  C   . SER   A 1 165 ? -8.590  -2.777  -5.065  1.00 12.46 ? 166 SER   A C   1 
ATOM   1328 O  O   . SER   A 1 165 ? -8.079  -1.777  -5.541  1.00 13.84 ? 166 SER   A O   1 
ATOM   1329 C  CB  A SER   A 1 165 ? -10.860 -2.673  -6.137  0.50 14.86 ? 166 SER   A CB  1 
ATOM   1330 C  CB  B SER   A 1 165 ? -10.872 -2.563  -5.921  0.50 17.43 ? 166 SER   A CB  1 
ATOM   1331 O  OG  A SER   A 1 165 ? -11.382 -2.148  -4.953  0.50 12.61 ? 166 SER   A OG  1 
ATOM   1332 O  OG  B SER   A 1 165 ? -11.874 -2.997  -6.828  0.50 22.18 ? 166 SER   A OG  1 
ATOM   1333 N  N   . ILE   A 1 166 ? -8.291  -3.243  -3.839  1.00 10.59 ? 167 ILE   A N   1 
ATOM   1334 C  CA  . ILE   A 1 166 ? -7.299  -2.601  -2.993  1.00 10.44 ? 167 ILE   A CA  1 
ATOM   1335 C  C   . ILE   A 1 166 ? -6.302  -3.649  -2.489  1.00 9.78  ? 167 ILE   A C   1 
ATOM   1336 O  O   . ILE   A 1 166 ? -5.893  -3.645  -1.337  1.00 10.01 ? 167 ILE   A O   1 
ATOM   1337 C  CB  . ILE   A 1 166 ? -7.924  -1.793  -1.858  1.00 10.87 ? 167 ILE   A CB  1 
ATOM   1338 C  CG1 . ILE   A 1 166 ? -8.785  -2.637  -0.940  1.00 10.54 ? 167 ILE   A CG1 1 
ATOM   1339 C  CG2 . ILE   A 1 166 ? -8.687  -0.596  -2.416  1.00 12.01 ? 167 ILE   A CG2 1 
ATOM   1340 C  CD1 . ILE   A 1 166 ? -8.850  -2.089  0.453   1.00 11.66 ? 167 ILE   A CD1 1 
ATOM   1341 N  N   . LYS   A 1 167 ? -5.866  -4.527  -3.393  1.00 10.21 ? 168 LYS   A N   1 
ATOM   1342 C  CA  . LYS   A 1 167 ? -5.090  -5.670  -2.966  1.00 10.01 ? 168 LYS   A CA  1 
ATOM   1343 C  C   . LYS   A 1 167 ? -3.776  -5.274  -2.304  1.00 9.67  ? 168 LYS   A C   1 
ATOM   1344 O  O   . LYS   A 1 167 ? -3.330  -5.937  -1.381  1.00 10.32 ? 168 LYS   A O   1 
ATOM   1345 C  CB  . LYS   A 1 167 ? -4.814  -6.599  -4.160  1.00 11.86 ? 168 LYS   A CB  1 
ATOM   1346 C  CG  . LYS   A 1 167 ? -4.081  -7.873  -3.778  1.00 13.29 ? 168 LYS   A CG  1 
ATOM   1347 C  CD  . LYS   A 1 167 ? -3.885  -8.764  -4.980  1.00 17.61 ? 168 LYS   A CD  1 
ATOM   1348 C  CE  . LYS   A 1 167 ? -3.154  -10.036 -4.690  1.00 21.89 ? 168 LYS   A CE  1 
ATOM   1349 N  NZ  . LYS   A 1 167 ? -2.934  -10.798 -5.934  1.00 27.52 ? 168 LYS   A NZ  1 
ATOM   1350 N  N   . THR   A 1 168 ? -3.136  -4.227  -2.821  1.00 9.98  ? 169 THR   A N   1 
ATOM   1351 C  CA  . THR   A 1 168 ? -1.796  -3.881  -2.447  1.00 10.07 ? 169 THR   A CA  1 
ATOM   1352 C  C   . THR   A 1 168 ? -1.716  -2.500  -1.779  1.00 9.34  ? 169 THR   A C   1 
ATOM   1353 O  O   . THR   A 1 168 ? -2.598  -1.636  -1.907  1.00 9.80  ? 169 THR   A O   1 
ATOM   1354 C  CB  . THR   A 1 168 ? -0.879  -3.927  -3.677  1.00 10.81 ? 169 THR   A CB  1 
ATOM   1355 O  OG1 . THR   A 1 168 ? -1.457  -3.140  -4.732  1.00 11.86 ? 169 THR   A OG1 1 
ATOM   1356 C  CG2 . THR   A 1 168 ? -0.668  -5.350  -4.165  1.00 11.77 ? 169 THR   A CG2 1 
ATOM   1357 N  N   . LYS   A 1 169 ? -0.632  -2.321  -1.036  1.00 10.28 ? 170 LYS   A N   1 
ATOM   1358 C  CA  . LYS   A 1 169 ? -0.377  -1.133  -0.258  1.00 10.20 ? 170 LYS   A CA  1 
ATOM   1359 C  C   . LYS   A 1 169 ? -0.458  0.125   -1.103  1.00 9.99  ? 170 LYS   A C   1 
ATOM   1360 O  O   . LYS   A 1 169 ? 0.150   0.207   -2.190  1.00 11.97 ? 170 LYS   A O   1 
ATOM   1361 C  CB  . LYS   A 1 169 ? 1.029   -1.215  0.331   1.00 11.60 ? 170 LYS   A CB  1 
ATOM   1362 C  CG  . LYS   A 1 169 ? 1.452   -0.024  1.175   1.00 12.26 ? 170 LYS   A CG  1 
ATOM   1363 C  CD  . LYS   A 1 169 ? 2.804   -0.185  1.848   1.00 15.21 ? 170 LYS   A CD  1 
ATOM   1364 C  CE  . LYS   A 1 169 ? 3.246   1.060   2.579   1.00 23.05 ? 170 LYS   A CE  1 
ATOM   1365 N  N   . GLY   A 1 170 ? -1.224  1.097   -0.630  1.00 10.63 ? 171 GLY   A N   1 
ATOM   1366 C  CA  . GLY   A 1 170 ? -1.374  2.363   -1.269  1.00 11.71 ? 171 GLY   A CA  1 
ATOM   1367 C  C   . GLY   A 1 170 ? -2.589  2.447   -2.172  1.00 11.64 ? 171 GLY   A C   1 
ATOM   1368 O  O   . GLY   A 1 170 ? -2.881  3.554   -2.655  1.00 14.59 ? 171 GLY   A O   1 
ATOM   1369 N  N   A LYS   A 1 171 ? -3.252  1.340   -2.458  0.50 11.04 ? 172 LYS   A N   1 
ATOM   1370 N  N   B LYS   A 1 171 ? -3.273  1.351   -2.449  0.50 10.74 ? 172 LYS   A N   1 
ATOM   1371 C  CA  A LYS   A 1 171 ? -4.461  1.371   -3.250  0.50 11.91 ? 172 LYS   A CA  1 
ATOM   1372 C  CA  B LYS   A 1 171 ? -4.448  1.404   -3.291  0.50 11.39 ? 172 LYS   A CA  1 
ATOM   1373 C  C   A LYS   A 1 171 ? -5.621  1.881   -2.405  0.50 10.50 ? 172 LYS   A C   1 
ATOM   1374 C  C   B LYS   A 1 171 ? -5.672  1.776   -2.468  0.50 10.35 ? 172 LYS   A C   1 
ATOM   1375 O  O   A LYS   A 1 171 ? -5.765  1.548   -1.228  0.50 9.50  ? 172 LYS   A O   1 
ATOM   1376 O  O   B LYS   A 1 171 ? -5.907  1.219   -1.393  0.50 9.08  ? 172 LYS   A O   1 
ATOM   1377 C  CB  A LYS   A 1 171 ? -4.757  -0.018  -3.811  0.50 12.43 ? 172 LYS   A CB  1 
ATOM   1378 C  CB  B LYS   A 1 171 ? -4.691  0.061   -3.968  0.50 11.33 ? 172 LYS   A CB  1 
ATOM   1379 C  CG  A LYS   A 1 171 ? -3.725  -0.515  -4.812  0.50 14.29 ? 172 LYS   A CG  1 
ATOM   1380 C  CG  B LYS   A 1 171 ? -3.745  -0.247  -5.118  0.50 12.21 ? 172 LYS   A CG  1 
ATOM   1381 C  CD  A LYS   A 1 171 ? -3.788  0.234   -6.103  0.50 16.08 ? 172 LYS   A CD  1 
ATOM   1382 C  CD  B LYS   A 1 171 ? -4.188  -1.447  -5.918  0.50 13.05 ? 172 LYS   A CD  1 
ATOM   1383 N  N   . SER   A 1 172 ? -6.506  2.638   -3.037  1.00 11.50 ? 173 SER   A N   1 
ATOM   1384 C  CA  . SER   A 1 172 ? -7.770  3.073   -2.449  1.00 11.96 ? 173 SER   A CA  1 
ATOM   1385 C  C   . SER   A 1 172 ? -8.895  2.916   -3.459  1.00 11.49 ? 173 SER   A C   1 
ATOM   1386 O  O   . SER   A 1 172 ? -8.661  2.867   -4.677  1.00 13.18 ? 173 SER   A O   1 
ATOM   1387 C  CB  . SER   A 1 172 ? -7.710  4.460   -1.915  1.00 13.78 ? 173 SER   A CB  1 
ATOM   1388 O  OG  . SER   A 1 172 ? -7.521  5.400   -2.949  1.00 16.20 ? 173 SER   A OG  1 
ATOM   1389 N  N   . ALA   A 1 173 ? -10.106 2.909   -2.960  1.00 11.73 ? 174 ALA   A N   1 
ATOM   1390 C  CA  . ALA   A 1 173 ? -11.300 2.892   -3.791  1.00 12.52 ? 174 ALA   A CA  1 
ATOM   1391 C  C   . ALA   A 1 173 ? -12.405 3.680   -3.144  1.00 11.35 ? 174 ALA   A C   1 
ATOM   1392 O  O   . ALA   A 1 173 ? -12.511 3.726   -1.918  1.00 10.71 ? 174 ALA   A O   1 
ATOM   1393 C  CB  . ALA   A 1 173 ? -11.769 1.483   -4.021  1.00 13.74 ? 174 ALA   A CB  1 
ATOM   1394 N  N   A ASP   A 1 174 ? -13.138 4.500   -3.894  0.50 11.12 ? 175 ASP   A N   1 
ATOM   1395 N  N   B ASP   A 1 174 ? -13.387 4.037   -3.983  0.50 11.00 ? 175 ASP   A N   1 
ATOM   1396 C  CA  A ASP   A 1 174 ? -14.341 5.093   -3.329  0.50 11.81 ? 175 ASP   A CA  1 
ATOM   1397 C  CA  B ASP   A 1 174 ? -14.568 4.703   -3.480  0.50 12.11 ? 175 ASP   A CA  1 
ATOM   1398 C  C   A ASP   A 1 174 ? -15.188 4.002   -2.659  0.50 11.66 ? 175 ASP   A C   1 
ATOM   1399 C  C   B ASP   A 1 174 ? -15.315 3.755   -2.583  0.50 12.25 ? 175 ASP   A C   1 
ATOM   1400 O  O   A ASP   A 1 174 ? -15.252 2.889   -3.170  0.50 12.68 ? 175 ASP   A O   1 
ATOM   1401 O  O   B ASP   A 1 174 ? -15.408 2.537   -2.809  0.50 13.13 ? 175 ASP   A O   1 
ATOM   1402 C  CB  A ASP   A 1 174 ? -15.197 5.757   -4.406  0.50 14.32 ? 175 ASP   A CB  1 
ATOM   1403 C  CB  B ASP   A 1 174 ? -15.566 5.136   -4.557  0.50 13.92 ? 175 ASP   A CB  1 
ATOM   1404 C  CG  A ASP   A 1 174 ? -14.534 6.784   -5.304  0.50 17.58 ? 175 ASP   A CG  1 
ATOM   1405 C  CG  B ASP   A 1 174 ? -16.695 5.972   -3.957  0.50 15.62 ? 175 ASP   A CG  1 
ATOM   1406 O  OD1 A ASP   A 1 174 ? -13.973 7.737   -4.744  0.50 19.36 ? 175 ASP   A OD1 1 
ATOM   1407 O  OD1 B ASP   A 1 174 ? -17.766 5.406   -3.489  0.50 16.34 ? 175 ASP   A OD1 1 
ATOM   1408 O  OD2 A ASP   A 1 174 ? -14.779 6.742   -6.560  0.50 21.48 ? 175 ASP   A OD2 1 
ATOM   1409 O  OD2 B ASP   A 1 174 ? -16.499 7.195   -3.884  0.50 20.27 ? 175 ASP   A OD2 1 
ATOM   1410 N  N   . PHE   A 1 175 ? -15.843 4.319   -1.512  1.00 11.07 ? 176 PHE   A N   1 
ATOM   1411 C  CA  . PHE   A 1 175 ? -16.579 3.402   -0.664  1.00 10.71 ? 176 PHE   A CA  1 
ATOM   1412 C  C   . PHE   A 1 175 ? -17.660 4.176   0.067   1.00 10.22 ? 176 PHE   A C   1 
ATOM   1413 O  O   . PHE   A 1 175 ? -17.589 4.354   1.274   1.00 13.68 ? 176 PHE   A O   1 
ATOM   1414 C  CB  . PHE   A 1 175 ? -15.649 2.630   0.273   1.00 11.15 ? 176 PHE   A CB  1 
ATOM   1415 C  CG  . PHE   A 1 175 ? -16.273 1.357   0.788   1.00 11.22 ? 176 PHE   A CG  1 
ATOM   1416 C  CD1 . PHE   A 1 175 ? -16.462 0.301   -0.044  1.00 12.52 ? 176 PHE   A CD1 1 
ATOM   1417 C  CD2 . PHE   A 1 175 ? -16.662 1.224   2.104   1.00 11.54 ? 176 PHE   A CD2 1 
ATOM   1418 C  CE1 . PHE   A 1 175 ? -17.009 -0.883  0.399   1.00 13.41 ? 176 PHE   A CE1 1 
ATOM   1419 C  CE2 . PHE   A 1 175 ? -17.184 0.024   2.576   1.00 11.73 ? 176 PHE   A CE2 1 
ATOM   1420 C  CZ  . PHE   A 1 175 ? -17.406 -1.010  1.705   1.00 12.28 ? 176 PHE   A CZ  1 
ATOM   1421 N  N   . THR   A 1 176 ? -18.606 4.711   -0.668  1.00 10.59 ? 177 THR   A N   1 
ATOM   1422 C  CA  . THR   A 1 176 ? -19.695 5.515   -0.132  1.00 9.99  ? 177 THR   A CA  1 
ATOM   1423 C  C   . THR   A 1 176 ? -20.866 4.657   0.297   1.00 9.55  ? 177 THR   A C   1 
ATOM   1424 O  O   . THR   A 1 176 ? -21.070 3.539   -0.158  1.00 10.74 ? 177 THR   A O   1 
ATOM   1425 C  CB  . THR   A 1 176 ? -20.082 6.591   -1.152  1.00 11.51 ? 177 THR   A CB  1 
ATOM   1426 O  OG1 . THR   A 1 176 ? -20.459 5.949   -2.377  1.00 15.39 ? 177 THR   A OG1 1 
ATOM   1427 C  CG2 . THR   A 1 176 ? -19.011 7.650   -1.298  1.00 15.24 ? 177 THR   A CG2 1 
ATOM   1428 N  N   . ASN   A 1 177 ? -21.708 5.235   1.153   1.00 9.68  ? 178 ASN   A N   1 
ATOM   1429 C  CA  . ASN   A 1 177 ? -22.972 4.663   1.566   1.00 10.80 ? 178 ASN   A CA  1 
ATOM   1430 C  C   . ASN   A 1 177 ? -22.852 3.319   2.271   1.00 10.71 ? 178 ASN   A C   1 
ATOM   1431 O  O   . ASN   A 1 177 ? -23.777 2.518   2.204   1.00 14.16 ? 178 ASN   A O   1 
ATOM   1432 C  CB  . ASN   A 1 177 ? -23.956 4.598   0.392   1.00 11.06 ? 178 ASN   A CB  1 
ATOM   1433 C  CG  . ASN   A 1 177 ? -24.186 5.971   -0.173  1.00 11.83 ? 178 ASN   A CG  1 
ATOM   1434 O  OD1 . ASN   A 1 177 ? -24.839 6.816   0.421   1.00 14.62 ? 178 ASN   A OD1 1 
ATOM   1435 N  ND2 . ASN   A 1 177 ? -23.606 6.203   -1.339  1.00 12.00 ? 178 ASN   A ND2 1 
ATOM   1436 N  N   . PHE   A 1 178 ? -21.760 3.085   2.968   1.00 9.74  ? 179 PHE   A N   1 
ATOM   1437 C  CA  . PHE   A 1 178 ? -21.636 1.891   3.783   1.00 9.78  ? 179 PHE   A CA  1 
ATOM   1438 C  C   . PHE   A 1 178 ? -22.130 2.183   5.187   1.00 10.04 ? 179 PHE   A C   1 
ATOM   1439 O  O   . PHE   A 1 178 ? -21.748 3.189   5.778   1.00 11.40 ? 179 PHE   A O   1 
ATOM   1440 C  CB  . PHE   A 1 178 ? -20.190 1.424   3.857   1.00 10.30 ? 179 PHE   A CB  1 
ATOM   1441 C  CG  . PHE   A 1 178 ? -20.055 0.189   4.697   1.00 9.74  ? 179 PHE   A CG  1 
ATOM   1442 C  CD1 . PHE   A 1 178 ? -20.398 -1.040  4.165   1.00 10.61 ? 179 PHE   A CD1 1 
ATOM   1443 C  CD2 . PHE   A 1 178 ? -19.662 0.253   6.015   1.00 9.67  ? 179 PHE   A CD2 1 
ATOM   1444 C  CE1 . PHE   A 1 178 ? -20.376 -2.193  4.947   1.00 11.31 ? 179 PHE   A CE1 1 
ATOM   1445 C  CE2 . PHE   A 1 178 ? -19.613 -0.896  6.783   1.00 9.71  ? 179 PHE   A CE2 1 
ATOM   1446 C  CZ  . PHE   A 1 178 ? -19.958 -2.113  6.256   1.00 10.18 ? 179 PHE   A CZ  1 
ATOM   1447 N  N   . ASP   A 1 179 ? -22.981 1.306   5.702   1.00 9.91  ? 180 ASP   A N   1 
ATOM   1448 C  CA  . ASP   A 1 179 ? -23.591 1.479   6.998   1.00 10.41 ? 180 ASP   A CA  1 
ATOM   1449 C  C   . ASP   A 1 179 ? -22.906 0.631   8.052   1.00 9.50  ? 180 ASP   A C   1 
ATOM   1450 O  O   . ASP   A 1 179 ? -23.091 -0.589  8.083   1.00 10.24 ? 180 ASP   A O   1 
ATOM   1451 C  CB  . ASP   A 1 179 ? -25.062 1.112   6.946   1.00 11.54 ? 180 ASP   A CB  1 
ATOM   1452 C  CG  . ASP   A 1 179 ? -25.819 1.386   8.230   1.00 14.13 ? 180 ASP   A CG  1 
ATOM   1453 O  OD1 . ASP   A 1 179 ? -25.231 1.748   9.226   1.00 12.81 ? 180 ASP   A OD1 1 
ATOM   1454 O  OD2 . ASP   A 1 179 ? -27.064 1.197   8.184   1.00 20.07 ? 180 ASP   A OD2 1 
ATOM   1455 N  N   . PRO   A 1 180 ? -22.086 1.229   8.942   1.00 9.81  ? 181 PRO   A N   1 
ATOM   1456 C  CA  . PRO   A 1 180 ? -21.364 0.409   9.926   1.00 10.38 ? 181 PRO   A CA  1 
ATOM   1457 C  C   . PRO   A 1 180 ? -22.245 -0.226  11.001  1.00 9.81  ? 181 PRO   A C   1 
ATOM   1458 O  O   . PRO   A 1 180 ? -21.793 -1.100  11.706  1.00 10.21 ? 181 PRO   A O   1 
ATOM   1459 C  CB  . PRO   A 1 180 ? -20.368 1.415   10.511  1.00 11.45 ? 181 PRO   A CB  1 
ATOM   1460 C  CG  . PRO   A 1 180 ? -21.029 2.761   10.390  1.00 11.64 ? 181 PRO   A CG  1 
ATOM   1461 C  CD  . PRO   A 1 180 ? -21.778 2.658   9.072   1.00 10.64 ? 181 PRO   A CD  1 
ATOM   1462 N  N   . ARG   A 1 181 ? -23.521 0.163   11.057  1.00 10.19 ? 182 ARG   A N   1 
ATOM   1463 C  CA  . ARG   A 1 181 ? -24.435 -0.502  11.998  1.00 10.45 ? 182 ARG   A CA  1 
ATOM   1464 C  C   . ARG   A 1 181 ? -24.578 -1.962  11.647  1.00 10.20 ? 182 ARG   A C   1 
ATOM   1465 O  O   . ARG   A 1 181 ? -24.910 -2.758  12.541  1.00 11.67 ? 182 ARG   A O   1 
ATOM   1466 C  CB  . ARG   A 1 181 ? -25.798 0.178   11.985  1.00 11.06 ? 182 ARG   A CB  1 
ATOM   1467 C  CG  . ARG   A 1 181 ? -25.710 1.595   12.518  1.00 12.91 ? 182 ARG   A CG  1 
ATOM   1468 C  CD  . ARG   A 1 181 ? -27.007 2.318   12.506  1.00 14.05 ? 182 ARG   A CD  1 
ATOM   1469 N  NE  . ARG   A 1 181 ? -27.400 2.552   11.134  1.00 15.20 ? 182 ARG   A NE  1 
ATOM   1470 C  CZ  . ARG   A 1 181 ? -28.527 3.145   10.806  1.00 17.59 ? 182 ARG   A CZ  1 
ATOM   1471 N  NH1 . ARG   A 1 181 ? -29.260 3.655   11.774  1.00 20.83 ? 182 ARG   A NH1 1 
ATOM   1472 N  NH2 . ARG   A 1 181 ? -28.877 3.250   9.535   1.00 20.71 ? 182 ARG   A NH2 1 
ATOM   1473 N  N   . GLY   A 1 182 ? -24.347 -2.355  10.389  1.00 10.19 ? 183 GLY   A N   1 
ATOM   1474 C  CA  . GLY   A 1 182 ? -24.440 -3.750  10.011  1.00 11.18 ? 183 GLY   A CA  1 
ATOM   1475 C  C   . GLY   A 1 182 ? -23.284 -4.611  10.499  1.00 10.88 ? 183 GLY   A C   1 
ATOM   1476 O  O   . GLY   A 1 182 ? -23.298 -5.799  10.215  1.00 13.14 ? 183 GLY   A O   1 
ATOM   1477 N  N   . LEU   A 1 183 ? -22.309 -4.031  11.222  1.00 9.95  ? 184 LEU   A N   1 
ATOM   1478 C  CA  . LEU   A 1 183 ? -21.205 -4.767  11.779  1.00 10.00 ? 184 LEU   A CA  1 
ATOM   1479 C  C   . LEU   A 1 183 ? -21.326 -4.977  13.282  1.00 10.20 ? 184 LEU   A C   1 
ATOM   1480 O  O   . LEU   A 1 183 ? -20.469 -5.610  13.895  1.00 12.61 ? 184 LEU   A O   1 
ATOM   1481 C  CB  . LEU   A 1 183 ? -19.878 -4.080  11.483  1.00 10.56 ? 184 LEU   A CB  1 
ATOM   1482 C  CG  . LEU   A 1 183 ? -19.566 -3.912  10.002  1.00 11.84 ? 184 LEU   A CG  1 
ATOM   1483 C  CD1 . LEU   A 1 183 ? -18.299 -3.154  9.788   1.00 13.44 ? 184 LEU   A CD1 1 
ATOM   1484 C  CD2 . LEU   A 1 183 ? -19.501 -5.222  9.295   1.00 13.77 ? 184 LEU   A CD2 1 
ATOM   1485 N  N   . LEU   A 1 184 ? -22.392 -4.497  13.917  1.00 10.45 ? 185 LEU   A N   1 
ATOM   1486 C  CA  . LEU   A 1 184 ? -22.522 -4.559  15.358  1.00 10.74 ? 185 LEU   A CA  1 
ATOM   1487 C  C   . LEU   A 1 184 ? -23.219 -5.840  15.770  1.00 12.35 ? 185 LEU   A C   1 
ATOM   1488 O  O   . LEU   A 1 184 ? -24.102 -6.323  15.096  1.00 17.05 ? 185 LEU   A O   1 
ATOM   1489 C  CB  . LEU   A 1 184 ? -23.299 -3.335  15.889  1.00 11.08 ? 185 LEU   A CB  1 
ATOM   1490 C  CG  . LEU   A 1 184 ? -22.749 -1.964  15.511  1.00 11.88 ? 185 LEU   A CG  1 
ATOM   1491 C  CD1 . LEU   A 1 184 ? -23.655 -0.816  15.951  1.00 13.54 ? 185 LEU   A CD1 1 
ATOM   1492 C  CD2 . LEU   A 1 184 ? -21.342 -1.815  16.016  1.00 14.62 ? 185 LEU   A CD2 1 
ATOM   1493 N  N   . PRO   A 1 185 ? -22.908 -6.414  16.941  1.00 10.54 ? 186 PRO   A N   1 
ATOM   1494 C  CA  . PRO   A 1 185 ? -23.688 -7.508  17.513  1.00 11.31 ? 186 PRO   A CA  1 
ATOM   1495 C  C   . PRO   A 1 185 ? -24.964 -6.952  18.139  1.00 10.68 ? 186 PRO   A C   1 
ATOM   1496 O  O   . PRO   A 1 185 ? -25.183 -5.747  18.224  1.00 12.19 ? 186 PRO   A O   1 
ATOM   1497 C  CB  . PRO   A 1 185 ? -22.757 -8.106  18.541  1.00 11.46 ? 186 PRO   A CB  1 
ATOM   1498 C  CG  . PRO   A 1 185 ? -22.026 -6.900  19.044  1.00 10.16 ? 186 PRO   A CG  1 
ATOM   1499 C  CD  . PRO   A 1 185 ? -21.786 -6.028  17.806  1.00 9.81  ? 186 PRO   A CD  1 
ATOM   1500 N  N   . GLU   A 1 186 ? -25.825 -7.857  18.604  1.00 11.27 ? 187 GLU   A N   1 
ATOM   1501 C  CA  . GLU   A 1 186 ? -27.080 -7.467  19.239  1.00 11.66 ? 187 GLU   A CA  1 
ATOM   1502 C  C   . GLU   A 1 186 ? -26.861 -6.698  20.526  1.00 10.97 ? 187 GLU   A C   1 
ATOM   1503 O  O   . GLU   A 1 186 ? -27.517 -5.675  20.754  1.00 13.89 ? 187 GLU   A O   1 
ATOM   1504 C  CB  A GLU   A 1 186 ? -27.816 -8.799  19.426  0.50 14.44 ? 187 GLU   A CB  1 
ATOM   1505 C  CB  B GLU   A 1 186 ? -27.966 -8.649  19.612  0.50 13.51 ? 187 GLU   A CB  1 
ATOM   1506 C  CG  A GLU   A 1 186 ? -29.050 -8.728  20.281  0.50 16.69 ? 187 GLU   A CG  1 
ATOM   1507 C  CG  B GLU   A 1 186 ? -28.621 -9.275  18.412  0.50 14.43 ? 187 GLU   A CG  1 
ATOM   1508 C  CD  A GLU   A 1 186 ? -29.616 -10.063 20.751  0.50 18.15 ? 187 GLU   A CD  1 
ATOM   1509 C  CD  B GLU   A 1 186 ? -29.459 -10.495 18.724  0.50 16.04 ? 187 GLU   A CD  1 
ATOM   1510 O  OE1 A GLU   A 1 186 ? -29.322 -11.101 20.107  0.50 20.96 ? 187 GLU   A OE1 1 
ATOM   1511 O  OE1 B GLU   A 1 186 ? -29.741 -10.717 19.916  0.50 19.43 ? 187 GLU   A OE1 1 
ATOM   1512 O  OE2 A GLU   A 1 186 ? -30.299 -10.053 21.790  0.50 21.68 ? 187 GLU   A OE2 1 
ATOM   1513 O  OE2 B GLU   A 1 186 ? -29.859 -11.171 17.781  0.50 19.39 ? 187 GLU   A OE2 1 
ATOM   1514 N  N   . SER   A 1 187 ? -25.963 -7.205  21.373  1.00 10.88 ? 188 SER   A N   1 
ATOM   1515 C  CA  . SER   A 1 187 ? -25.726 -6.614  22.682  1.00 11.20 ? 188 SER   A CA  1 
ATOM   1516 C  C   . SER   A 1 187 ? -24.617 -5.608  22.645  1.00 10.73 ? 188 SER   A C   1 
ATOM   1517 O  O   . SER   A 1 187 ? -23.565 -5.867  22.025  1.00 11.91 ? 188 SER   A O   1 
ATOM   1518 C  CB  . SER   A 1 187 ? -25.337 -7.711  23.668  1.00 12.56 ? 188 SER   A CB  1 
ATOM   1519 O  OG  . SER   A 1 187 ? -25.078 -7.140  24.962  1.00 13.60 ? 188 SER   A OG  1 
ATOM   1520 N  N   . LEU   A 1 188 ? -24.755 -4.511  23.407  1.00 10.82 ? 189 LEU   A N   1 
ATOM   1521 C  CA  . LEU   A 1 188 ? -23.667 -3.563  23.605  1.00 11.47 ? 189 LEU   A CA  1 
ATOM   1522 C  C   . LEU   A 1 188 ? -22.996 -3.726  24.974  1.00 11.12 ? 189 LEU   A C   1 
ATOM   1523 O  O   . LEU   A 1 188 ? -22.301 -2.799  25.386  1.00 13.61 ? 189 LEU   A O   1 
ATOM   1524 C  CB  . LEU   A 1 188 ? -24.153 -2.122  23.382  1.00 13.45 ? 189 LEU   A CB  1 
ATOM   1525 C  CG  . LEU   A 1 188 ? -24.634 -1.782  21.981  1.00 15.12 ? 189 LEU   A CG  1 
ATOM   1526 C  CD1 . LEU   A 1 188 ? -25.114 -0.334  21.901  1.00 17.38 ? 189 LEU   A CD1 1 
ATOM   1527 C  CD2 . LEU   A 1 188 ? -23.586 -2.106  20.935  1.00 16.97 ? 189 LEU   A CD2 1 
ATOM   1528 N  N   . ASP   A 1 189 ? -23.156 -4.847  25.658  1.00 10.45 ? 190 ASP   A N   1 
ATOM   1529 C  CA  . ASP   A 1 189 ? -22.380 -5.078  26.870  1.00 10.56 ? 190 ASP   A CA  1 
ATOM   1530 C  C   . ASP   A 1 189 ? -20.895 -5.043  26.546  1.00 9.49  ? 190 ASP   A C   1 
ATOM   1531 O  O   . ASP   A 1 189 ? -20.475 -5.549  25.520  1.00 9.56  ? 190 ASP   A O   1 
ATOM   1532 C  CB  . ASP   A 1 189 ? -22.720 -6.453  27.458  1.00 12.46 ? 190 ASP   A CB  1 
ATOM   1533 C  CG  . ASP   A 1 189 ? -24.104 -6.661  28.052  1.00 16.01 ? 190 ASP   A CG  1 
ATOM   1534 O  OD1 . ASP   A 1 189 ? -24.748 -5.687  28.326  1.00 19.14 ? 190 ASP   A OD1 1 
ATOM   1535 O  OD2 . ASP   A 1 189 ? -24.483 -7.807  28.301  1.00 20.44 ? 190 ASP   A OD2 1 
ATOM   1536 N  N   . TYR   A 1 190 ? -20.096 -4.473  27.468  1.00 9.33  ? 191 TYR   A N   1 
ATOM   1537 C  CA  . TYR   A 1 190 ? -18.695 -4.219  27.149  1.00 8.82  ? 191 TYR   A CA  1 
ATOM   1538 C  C   . TYR   A 1 190 ? -17.822 -4.271  28.391  1.00 8.57  ? 191 TYR   A C   1 
ATOM   1539 O  O   . TYR   A 1 190 ? -18.272 -4.141  29.534  1.00 9.17  ? 191 TYR   A O   1 
ATOM   1540 C  CB  . TYR   A 1 190 ? -18.533 -2.851  26.441  1.00 9.70  ? 191 TYR   A CB  1 
ATOM   1541 C  CG  . TYR   A 1 190 ? -18.921 -1.671  27.310  1.00 9.48  ? 191 TYR   A CG  1 
ATOM   1542 C  CD1 . TYR   A 1 190 ? -18.011 -1.046  28.132  1.00 10.47 ? 191 TYR   A CD1 1 
ATOM   1543 C  CD2 . TYR   A 1 190 ? -20.197 -1.147  27.245  1.00 10.26 ? 191 TYR   A CD2 1 
ATOM   1544 C  CE1 . TYR   A 1 190 ? -18.386 0.005   28.939  1.00 11.28 ? 191 TYR   A CE1 1 
ATOM   1545 C  CE2 . TYR   A 1 190 ? -20.582 -0.081  28.045  1.00 10.93 ? 191 TYR   A CE2 1 
ATOM   1546 C  CZ  . TYR   A 1 190 ? -19.668 0.499   28.914  1.00 10.83 ? 191 TYR   A CZ  1 
ATOM   1547 O  OH  . TYR   A 1 190 ? -20.002 1.526   29.761  1.00 12.17 ? 191 TYR   A OH  1 
ATOM   1548 N  N   . TRP   A 1 191 ? -16.525 -4.402  28.083  1.00 8.03  ? 192 TRP   A N   1 
ATOM   1549 C  CA  . TRP   A 1 191 ? -15.441 -4.122  29.020  1.00 8.17  ? 192 TRP   A CA  1 
ATOM   1550 C  C   . TRP   A 1 191 ? -14.748 -2.838  28.601  1.00 8.01  ? 192 TRP   A C   1 
ATOM   1551 O  O   . TRP   A 1 191 ? -14.695 -2.511  27.410  1.00 9.25  ? 192 TRP   A O   1 
ATOM   1552 C  CB  . TRP   A 1 191 ? -14.403 -5.247  29.016  1.00 8.78  ? 192 TRP   A CB  1 
ATOM   1553 C  CG  . TRP   A 1 191 ? -14.925 -6.575  29.453  1.00 8.92  ? 192 TRP   A CG  1 
ATOM   1554 C  CD1 . TRP   A 1 191 ? -15.159 -7.011  30.704  1.00 9.87  ? 192 TRP   A CD1 1 
ATOM   1555 C  CD2 . TRP   A 1 191 ? -15.201 -7.702  28.589  1.00 9.53  ? 192 TRP   A CD2 1 
ATOM   1556 N  NE1 . TRP   A 1 191 ? -15.567 -8.322  30.691  1.00 11.09 ? 192 TRP   A NE1 1 
ATOM   1557 C  CE2 . TRP   A 1 191 ? -15.595 -8.776  29.399  1.00 10.54 ? 192 TRP   A CE2 1 
ATOM   1558 C  CE3 . TRP   A 1 191 ? -15.125 -7.911  27.211  1.00 9.94  ? 192 TRP   A CE3 1 
ATOM   1559 C  CZ2 . TRP   A 1 191 ? -15.896 -10.029 28.882  1.00 11.38 ? 192 TRP   A CZ2 1 
ATOM   1560 C  CZ3 . TRP   A 1 191 ? -15.384 -9.153  26.695  1.00 11.42 ? 192 TRP   A CZ3 1 
ATOM   1561 C  CH2 . TRP   A 1 191 ? -15.796 -10.187 27.511  1.00 12.15 ? 192 TRP   A CH2 1 
ATOM   1562 N  N   . THR   A 1 192 ? -14.166 -2.119  29.557  1.00 7.93  ? 193 THR   A N   1 
ATOM   1563 C  CA  . THR   A 1 192 ? -13.437 -0.899  29.238  1.00 7.96  ? 193 THR   A CA  1 
ATOM   1564 C  C   . THR   A 1 192 ? -12.205 -0.745  30.096  1.00 8.02  ? 193 THR   A C   1 
ATOM   1565 O  O   . THR   A 1 192 ? -12.187 -1.134  31.267  1.00 8.67  ? 193 THR   A O   1 
ATOM   1566 C  CB  . THR   A 1 192 ? -14.373 0.321   29.338  1.00 8.32  ? 193 THR   A CB  1 
ATOM   1567 O  OG1 . THR   A 1 192 ? -13.709 1.496   28.922  1.00 9.03  ? 193 THR   A OG1 1 
ATOM   1568 C  CG2 . THR   A 1 192 ? -14.937 0.544   30.714  1.00 9.30  ? 193 THR   A CG2 1 
ATOM   1569 N  N   . TYR   A 1 193 ? -11.166 -0.140  29.516  1.00 7.83  ? 194 TYR   A N   1 
ATOM   1570 C  CA  . TYR   A 1 193 ? -9.932  0.165   30.233  1.00 8.05  ? 194 TYR   A CA  1 
ATOM   1571 C  C   . TYR   A 1 193 ? -9.174  1.219   29.441  1.00 7.52  ? 194 TYR   A C   1 
ATOM   1572 O  O   . TYR   A 1 193 ? -9.397  1.391   28.246  1.00 7.89  ? 194 TYR   A O   1 
ATOM   1573 C  CB  . TYR   A 1 193 ? -9.083  -1.101  30.419  1.00 8.26  ? 194 TYR   A CB  1 
ATOM   1574 C  CG  . TYR   A 1 193 ? -8.407  -1.587  29.164  1.00 8.05  ? 194 TYR   A CG  1 
ATOM   1575 C  CD1 . TYR   A 1 193 ? -9.091  -2.315  28.185  1.00 7.99  ? 194 TYR   A CD1 1 
ATOM   1576 C  CD2 . TYR   A 1 193 ? -7.092  -1.241  28.909  1.00 8.36  ? 194 TYR   A CD2 1 
ATOM   1577 C  CE1 . TYR   A 1 193 ? -8.456  -2.659  26.996  1.00 7.73  ? 194 TYR   A CE1 1 
ATOM   1578 C  CE2 . TYR   A 1 193 ? -6.458  -1.593  27.738  1.00 7.98  ? 194 TYR   A CE2 1 
ATOM   1579 C  CZ  . TYR   A 1 193 ? -7.148  -2.281  26.759  1.00 7.54  ? 194 TYR   A CZ  1 
ATOM   1580 O  OH  . TYR   A 1 193 ? -6.473  -2.577  25.597  1.00 8.09  ? 194 TYR   A OH  1 
ATOM   1581 N  N   . PRO   A 1 194 ? -8.235  1.916   30.101  1.00 8.03  ? 195 PRO   A N   1 
ATOM   1582 C  CA  . PRO   A 1 194 ? -7.403  2.907   29.417  1.00 8.11  ? 195 PRO   A CA  1 
ATOM   1583 C  C   . PRO   A 1 194 ? -6.192  2.243   28.763  1.00 7.33  ? 195 PRO   A C   1 
ATOM   1584 O  O   . PRO   A 1 194 ? -5.471  1.490   29.423  1.00 8.40  ? 195 PRO   A O   1 
ATOM   1585 C  CB  . PRO   A 1 194 ? -6.947  3.829   30.541  1.00 9.13  ? 195 PRO   A CB  1 
ATOM   1586 C  CG  . PRO   A 1 194 ? -6.938  2.936   31.765  1.00 9.75  ? 195 PRO   A CG  1 
ATOM   1587 C  CD  . PRO   A 1 194 ? -8.048  1.957   31.557  1.00 9.47  ? 195 PRO   A CD  1 
ATOM   1588 N  N   . GLY   A 1 195 ? -5.968  2.531   27.496  1.00 7.26  ? 196 GLY   A N   1 
ATOM   1589 C  CA  . GLY   A 1 195 ? -4.855  1.916   26.783  1.00 7.39  ? 196 GLY   A CA  1 
ATOM   1590 C  C   . GLY   A 1 195 ? -4.298  2.793   25.704  1.00 6.93  ? 196 GLY   A C   1 
ATOM   1591 O  O   . GLY   A 1 195 ? -4.200  4.010   25.828  1.00 7.98  ? 196 GLY   A O   1 
ATOM   1592 N  N   . SER   A 1 196 ? -3.903  2.138   24.623  1.00 7.32  ? 197 SER   A N   1 
ATOM   1593 C  CA  . SER   A 1 196 ? -3.067  2.761   23.601  1.00 7.41  ? 197 SER   A CA  1 
ATOM   1594 C  C   . SER   A 1 196 ? -3.531  2.372   22.213  1.00 6.95  ? 197 SER   A C   1 
ATOM   1595 O  O   . SER   A 1 196 ? -4.272  1.412   22.026  1.00 7.25  ? 197 SER   A O   1 
ATOM   1596 C  CB  . SER   A 1 196 ? -1.583  2.374   23.770  1.00 7.73  ? 197 SER   A CB  1 
ATOM   1597 O  OG  . SER   A 1 196 ? -1.324  1.029   23.329  1.00 7.79  ? 197 SER   A OG  1 
ATOM   1598 N  N   . LEU   A 1 197 ? -2.970  3.048   21.219  1.00 7.11  ? 198 LEU   A N   1 
ATOM   1599 C  CA  . LEU   A 1 197 ? -2.977  2.508   19.863  1.00 7.49  ? 198 LEU   A CA  1 
ATOM   1600 C  C   . LEU   A 1 197 ? -2.246  1.182   19.875  1.00 7.07  ? 198 LEU   A C   1 
ATOM   1601 O  O   . LEU   A 1 197 ? -1.226  1.016   20.571  1.00 7.85  ? 198 LEU   A O   1 
ATOM   1602 C  CB  . LEU   A 1 197 ? -2.231  3.445   18.898  1.00 7.86  ? 198 LEU   A CB  1 
ATOM   1603 C  CG  . LEU   A 1 197 ? -2.724  4.897   18.839  1.00 9.08  ? 198 LEU   A CG  1 
ATOM   1604 C  CD1 . LEU   A 1 197 ? -1.878  5.682   17.855  1.00 9.60  ? 198 LEU   A CD1 1 
ATOM   1605 C  CD2 . LEU   A 1 197 ? -4.189  5.009   18.517  1.00 10.18 ? 198 LEU   A CD2 1 
ATOM   1606 N  N   . THR   A 1 198 ? -2.706  0.210   19.065  1.00 7.09  ? 199 THR   A N   1 
ATOM   1607 C  CA  . THR   A 1 198 ? -2.049  -1.090  19.008  1.00 7.24  ? 199 THR   A CA  1 
ATOM   1608 C  C   . THR   A 1 198 ? -1.023  -1.199  17.884  1.00 7.35  ? 199 THR   A C   1 
ATOM   1609 O  O   . THR   A 1 198 ? -0.402  -2.256  17.722  1.00 8.06  ? 199 THR   A O   1 
ATOM   1610 C  CB  . THR   A 1 198 ? -3.042  -2.246  18.888  1.00 7.50  ? 199 THR   A CB  1 
ATOM   1611 O  OG1 . THR   A 1 198 ? -3.629  -2.157  17.574  1.00 7.67  ? 199 THR   A OG1 1 
ATOM   1612 C  CG2 . THR   A 1 198 ? -4.097  -2.226  19.974  1.00 8.01  ? 199 THR   A CG2 1 
ATOM   1613 N  N   . THR   A 1 199 ? -0.825  -0.117  17.130  1.00 7.91  ? 200 THR   A N   1 
ATOM   1614 C  CA  . THR   A 1 199 ? 0.249   -0.035  16.148  1.00 8.81  ? 200 THR   A CA  1 
ATOM   1615 C  C   . THR   A 1 199 ? 1.047   1.199   16.451  1.00 8.90  ? 200 THR   A C   1 
ATOM   1616 O  O   . THR   A 1 199 ? 0.554   2.153   17.045  1.00 8.97  ? 200 THR   A O   1 
ATOM   1617 C  CB  . THR   A 1 199 ? -0.276  0.048   14.717  1.00 9.32  ? 200 THR   A CB  1 
ATOM   1618 O  OG1 . THR   A 1 199 ? -1.061  1.219   14.524  1.00 14.36 ? 200 THR   A OG1 1 
ATOM   1619 C  CG2 . THR   A 1 199 ? -1.120  -1.108  14.310  1.00 11.15 ? 200 THR   A CG2 1 
ATOM   1620 N  N   . PRO   A 1 200 ? 2.319   1.243   15.999  1.00 8.90  ? 201 PRO   A N   1 
ATOM   1621 C  CA  . PRO   A 1 200 ? 3.081   2.488   16.042  1.00 9.61  ? 201 PRO   A CA  1 
ATOM   1622 C  C   . PRO   A 1 200 ? 2.253   3.616   15.527  1.00 9.94  ? 201 PRO   A C   1 
ATOM   1623 O  O   . PRO   A 1 200 ? 1.573   3.449   14.503  1.00 12.25 ? 201 PRO   A O   1 
ATOM   1624 C  CB  . PRO   A 1 200 ? 4.303   2.149   15.192  1.00 10.23 ? 201 PRO   A CB  1 
ATOM   1625 C  CG  . PRO   A 1 200 ? 4.523   0.705   15.455  1.00 10.56 ? 201 PRO   A CG  1 
ATOM   1626 C  CD  . PRO   A 1 200 ? 3.107   0.152   15.413  1.00 9.58  ? 201 PRO   A CD  1 
ATOM   1627 N  N   . PRO   A 1 201 ? 2.234   4.781   16.152  1.00 9.77  ? 202 PRO   A N   1 
ATOM   1628 C  CA  . PRO   A 1 201 ? 3.142   5.193   17.238  1.00 10.11 ? 202 PRO   A CA  1 
ATOM   1629 C  C   . PRO   A 1 201 ? 2.792   4.772   18.669  1.00 9.27  ? 202 PRO   A C   1 
ATOM   1630 O  O   . PRO   A 1 201 ? 3.454   5.219   19.597  1.00 10.06 ? 202 PRO   A O   1 
ATOM   1631 C  CB  . PRO   A 1 201 ? 3.146   6.726   17.048  1.00 11.66 ? 202 PRO   A CB  1 
ATOM   1632 C  CG  . PRO   A 1 201 ? 1.753   7.040   16.585  1.00 12.30 ? 202 PRO   A CG  1 
ATOM   1633 C  CD  . PRO   A 1 201 ? 1.441   5.914   15.629  1.00 11.39 ? 202 PRO   A CD  1 
ATOM   1634 N  N   . LEU   A 1 202 ? 1.784   3.909   18.862  1.00 8.44  ? 203 LEU   A N   1 
ATOM   1635 C  CA  . LEU   A 1 202 ? 1.536   3.252   20.171  1.00 8.34  ? 203 LEU   A CA  1 
ATOM   1636 C  C   . LEU   A 1 202 ? 1.182   4.280   21.253  1.00 7.96  ? 203 LEU   A C   1 
ATOM   1637 O  O   . LEU   A 1 202 ? 1.333   4.033   22.429  1.00 8.69  ? 203 LEU   A O   1 
ATOM   1638 C  CB  . LEU   A 1 202 ? 2.704   2.369   20.604  1.00 8.46  ? 203 LEU   A CB  1 
ATOM   1639 C  CG  . LEU   A 1 202 ? 3.036   1.224   19.646  1.00 8.67  ? 203 LEU   A CG  1 
ATOM   1640 C  CD1 . LEU   A 1 202 ? 4.348   0.587   20.039  1.00 9.85  ? 203 LEU   A CD1 1 
ATOM   1641 C  CD2 . LEU   A 1 202 ? 1.957   0.181   19.584  1.00 9.08  ? 203 LEU   A CD2 1 
ATOM   1642 N  N   . LEU   A 1 203 ? 0.587   5.396   20.835  1.00 8.67  ? 204 LEU   A N   1 
ATOM   1643 C  CA  . LEU   A 1 203 ? 0.296   6.498   21.738  1.00 8.78  ? 204 LEU   A CA  1 
ATOM   1644 C  C   . LEU   A 1 203 ? -0.763  6.085   22.736  1.00 8.22  ? 204 LEU   A C   1 
ATOM   1645 O  O   . LEU   A 1 203 ? -1.731  5.387   22.426  1.00 8.46  ? 204 LEU   A O   1 
ATOM   1646 C  CB  . LEU   A 1 203 ? -0.163  7.725   20.941  1.00 9.92  ? 204 LEU   A CB  1 
ATOM   1647 C  CG  . LEU   A 1 203 ? 0.907   8.301   20.010  1.00 11.34 ? 204 LEU   A CG  1 
ATOM   1648 C  CD1 . LEU   A 1 203 ? 0.316   9.359   19.113  1.00 12.43 ? 204 LEU   A CD1 1 
ATOM   1649 C  CD2 . LEU   A 1 203 ? 2.069   8.903   20.819  1.00 14.10 ? 204 LEU   A CD2 1 
ATOM   1650 N  N   . GLU   A 1 204 ? -0.592  6.547   23.970  1.00 8.56  ? 205 GLU   A N   1 
ATOM   1651 C  CA  . GLU   A 1 204 ? -1.436  6.186   25.097  1.00 8.66  ? 205 GLU   A CA  1 
ATOM   1652 C  C   . GLU   A 1 204 ? -2.599  7.155   25.253  1.00 8.86  ? 205 GLU   A C   1 
ATOM   1653 O  O   . GLU   A 1 204 ? -2.713  7.907   26.216  1.00 11.02 ? 205 GLU   A O   1 
ATOM   1654 C  CB  . GLU   A 1 204 ? -0.556  6.045   26.345  1.00 9.45  ? 205 GLU   A CB  1 
ATOM   1655 C  CG  . GLU   A 1 204 ? 0.339   4.829   26.236  1.00 9.93  ? 205 GLU   A CG  1 
ATOM   1656 C  CD  . GLU   A 1 204 ? 1.290   4.554   27.391  1.00 9.86  ? 205 GLU   A CD  1 
ATOM   1657 O  OE1 . GLU   A 1 204 ? 1.605   5.504   28.138  1.00 12.20 ? 205 GLU   A OE1 1 
ATOM   1658 O  OE2 . GLU   A 1 204 ? 1.682   3.371   27.558  1.00 10.53 ? 205 GLU   A OE2 1 
ATOM   1659 N  N   . CYS   A 1 205 ? -3.516  7.069   24.284  1.00 8.26  ? 206 CYS   A N   1 
ATOM   1660 C  CA  . CYS   A 1 205 ? -4.569  8.048   24.075  1.00 8.47  ? 206 CYS   A CA  1 
ATOM   1661 C  C   . CYS   A 1 205 ? -5.948  7.433   23.989  1.00 8.22  ? 206 CYS   A C   1 
ATOM   1662 O  O   . CYS   A 1 205 ? -6.889  8.140   23.664  1.00 9.80  ? 206 CYS   A O   1 
ATOM   1663 C  CB  . CYS   A 1 205 ? -4.298  8.871   22.824  1.00 9.14  ? 206 CYS   A CB  1 
ATOM   1664 S  SG  . CYS   A 1 205 ? -4.235  7.890   21.306  1.00 10.11 ? 206 CYS   A SG  1 
ATOM   1665 N  N   . VAL   A 1 206 ? -6.081  6.117   24.241  1.00 7.93  ? 207 VAL   A N   1 
ATOM   1666 C  CA  . VAL   A 1 206 ? -7.314  5.410   23.902  1.00 8.02  ? 207 VAL   A CA  1 
ATOM   1667 C  C   . VAL   A 1 206 ? -8.068  4.986   25.150  1.00 7.78  ? 207 VAL   A C   1 
ATOM   1668 O  O   . VAL   A 1 206 ? -7.532  4.304   26.017  1.00 9.00  ? 207 VAL   A O   1 
ATOM   1669 C  CB  . VAL   A 1 206 ? -7.027  4.163   23.041  1.00 8.20  ? 207 VAL   A CB  1 
ATOM   1670 C  CG1 . VAL   A 1 206 ? -8.320  3.446   22.683  1.00 8.16  ? 207 VAL   A CG1 1 
ATOM   1671 C  CG2 . VAL   A 1 206 ? -6.264  4.505   21.767  1.00 8.52  ? 207 VAL   A CG2 1 
ATOM   1672 N  N   . THR   A 1 207 ? -9.384  5.280   25.164  1.00 7.39  ? 208 THR   A N   1 
ATOM   1673 C  CA  . THR   A 1 207 ? -10.328 4.550   26.013  1.00 7.59  ? 208 THR   A CA  1 
ATOM   1674 C  C   . THR   A 1 207 ? -10.853 3.378   25.184  1.00 7.27  ? 208 THR   A C   1 
ATOM   1675 O  O   . THR   A 1 207 ? -11.546 3.584   24.179  1.00 7.93  ? 208 THR   A O   1 
ATOM   1676 C  CB  . THR   A 1 207 ? -11.494 5.433   26.479  1.00 8.28  ? 208 THR   A CB  1 
ATOM   1677 O  OG1 . THR   A 1 207 ? -10.977 6.555   27.218  1.00 9.64  ? 208 THR   A OG1 1 
ATOM   1678 C  CG2 . THR   A 1 207 ? -12.436 4.638   27.341  1.00 9.48  ? 208 THR   A CG2 1 
ATOM   1679 N  N   . TRP   A 1 208 ? -10.485 2.166   25.583  1.00 6.90  ? 209 TRP   A N   1 
ATOM   1680 C  CA  . TRP   A 1 208 ? -10.928 0.967   24.886  1.00 7.10  ? 209 TRP   A CA  1 
ATOM   1681 C  C   . TRP   A 1 208 ? -12.301 0.571   25.407  1.00 6.91  ? 209 TRP   A C   1 
ATOM   1682 O  O   . TRP   A 1 208 ? -12.518 0.517   26.630  1.00 7.72  ? 209 TRP   A O   1 
ATOM   1683 C  CB  . TRP   A 1 208 ? -9.923  -0.174  25.107  1.00 7.25  ? 209 TRP   A CB  1 
ATOM   1684 C  CG  . TRP   A 1 208 ? -8.796  -0.058  24.132  1.00 7.16  ? 209 TRP   A CG  1 
ATOM   1685 C  CD1 . TRP   A 1 208 ? -7.581  0.520   24.318  1.00 7.83  ? 209 TRP   A CD1 1 
ATOM   1686 C  CD2 . TRP   A 1 208 ? -8.845  -0.465  22.761  1.00 7.07  ? 209 TRP   A CD2 1 
ATOM   1687 N  NE1 . TRP   A 1 208 ? -6.883  0.509   23.148  1.00 7.90  ? 209 TRP   A NE1 1 
ATOM   1688 C  CE2 . TRP   A 1 208 ? -7.623  -0.097  22.170  1.00 7.49  ? 209 TRP   A CE2 1 
ATOM   1689 C  CE3 . TRP   A 1 208 ? -9.808  -1.102  21.976  1.00 7.21  ? 209 TRP   A CE3 1 
ATOM   1690 C  CZ2 . TRP   A 1 208 ? -7.349  -0.310  20.830  1.00 8.29  ? 209 TRP   A CZ2 1 
ATOM   1691 C  CZ3 . TRP   A 1 208 ? -9.533  -1.367  20.663  1.00 7.99  ? 209 TRP   A CZ3 1 
ATOM   1692 C  CH2 . TRP   A 1 208 ? -8.307  -0.977  20.106  1.00 8.32  ? 209 TRP   A CH2 1 
ATOM   1693 N  N   . ILE   A 1 209 ? -13.181 0.211   24.483  1.00 6.73  ? 210 ILE   A N   1 
ATOM   1694 C  CA  . ILE   A 1 209 ? -14.511 -0.315  24.778  1.00 7.15  ? 210 ILE   A CA  1 
ATOM   1695 C  C   . ILE   A 1 209 ? -14.639 -1.583  23.953  1.00 7.06  ? 210 ILE   A C   1 
ATOM   1696 O  O   . ILE   A 1 209 ? -14.715 -1.500  22.742  1.00 8.20  ? 210 ILE   A O   1 
ATOM   1697 C  CB  . ILE   A 1 209 ? -15.606 0.699   24.443  1.00 7.69  ? 210 ILE   A CB  1 
ATOM   1698 C  CG1 . ILE   A 1 209 ? -15.393 1.987   25.256  1.00 8.94  ? 210 ILE   A CG1 1 
ATOM   1699 C  CG2 . ILE   A 1 209 ? -16.968 0.091   24.671  1.00 8.30  ? 210 ILE   A CG2 1 
ATOM   1700 C  CD1 . ILE   A 1 209 ? -16.247 3.160   24.790  1.00 10.64 ? 210 ILE   A CD1 1 
ATOM   1701 N  N   . VAL   A 1 210 ? -14.539 -2.750  24.600  1.00 6.89  ? 211 VAL   A N   1 
ATOM   1702 C  CA  . VAL   A 1 210 ? -14.495 -4.026  23.912  1.00 7.26  ? 211 VAL   A CA  1 
ATOM   1703 C  C   . VAL   A 1 210 ? -15.801 -4.744  24.167  1.00 7.47  ? 211 VAL   A C   1 
ATOM   1704 O  O   . VAL   A 1 210 ? -16.149 -5.020  25.305  1.00 8.27  ? 211 VAL   A O   1 
ATOM   1705 C  CB  . VAL   A 1 210 ? -13.295 -4.875  24.338  1.00 7.87  ? 211 VAL   A CB  1 
ATOM   1706 C  CG1 . VAL   A 1 210 ? -13.301 -6.211  23.652  1.00 8.59  ? 211 VAL   A CG1 1 
ATOM   1707 C  CG2 . VAL   A 1 210 ? -11.992 -4.120  24.060  1.00 8.72  ? 211 VAL   A CG2 1 
ATOM   1708 N  N   . LEU   A 1 211 ? -16.574 -5.022  23.106  1.00 7.87  ? 212 LEU   A N   1 
ATOM   1709 C  CA  . LEU   A 1 211 ? -17.858 -5.662  23.284  1.00 8.30  ? 212 LEU   A CA  1 
ATOM   1710 C  C   . LEU   A 1 211 ? -17.680 -7.129  23.659  1.00 8.38  ? 212 LEU   A C   1 
ATOM   1711 O  O   . LEU   A 1 211 ? -16.842 -7.844  23.140  1.00 8.97  ? 212 LEU   A O   1 
ATOM   1712 C  CB  . LEU   A 1 211 ? -18.697 -5.570  22.008  1.00 8.81  ? 212 LEU   A CB  1 
ATOM   1713 C  CG  . LEU   A 1 211 ? -19.072 -4.156  21.572  1.00 9.24  ? 212 LEU   A CG  1 
ATOM   1714 C  CD1 . LEU   A 1 211 ? -20.110 -4.203  20.453  1.00 10.57 ? 212 LEU   A CD1 1 
ATOM   1715 C  CD2 . LEU   A 1 211 ? -19.612 -3.319  22.701  1.00 10.45 ? 212 LEU   A CD2 1 
ATOM   1716 N  N   . LYS   A 1 212 ? -18.554 -7.597  24.554  1.00 8.95  ? 213 LYS   A N   1 
ATOM   1717 C  CA  . LYS   A 1 212 ? -18.531 -8.981  24.966  1.00 10.05 ? 213 LYS   A CA  1 
ATOM   1718 C  C   . LYS   A 1 212 ? -18.999 -9.936  23.880  1.00 9.62  ? 213 LYS   A C   1 
ATOM   1719 O  O   . LYS   A 1 212 ? -18.495 -11.047 23.764  1.00 11.43 ? 213 LYS   A O   1 
ATOM   1720 C  CB  . LYS   A 1 212 ? -19.378 -9.160  26.214  1.00 12.90 ? 213 LYS   A CB  1 
ATOM   1721 C  CG  . LYS   A 1 212 ? -19.476 -10.610 26.681  1.00 16.59 ? 213 LYS   A CG  1 
ATOM   1722 C  CD  . LYS   A 1 212 ? -20.065 -10.793 27.982  1.00 21.95 ? 213 LYS   A CD  1 
ATOM   1723 C  CE  . LYS   A 1 212 ? -21.342 -9.974  28.008  1.00 27.90 ? 213 LYS   A CE  1 
ATOM   1724 N  NZ  . LYS   A 1 212 ? -22.395 -10.442 27.072  1.00 33.32 ? 213 LYS   A NZ  1 
ATOM   1725 N  N   . GLU   A 1 213 ? -20.011 -9.548  23.115  1.00 9.06  ? 214 GLU   A N   1 
ATOM   1726 C  CA  A GLU   A 1 213 ? -20.592 -10.447 22.142  0.50 8.93  ? 214 GLU   A CA  1 
ATOM   1727 C  CA  B GLU   A 1 213 ? -20.609 -10.435 22.135  0.50 9.38  ? 214 GLU   A CA  1 
ATOM   1728 C  C   . GLU   A 1 213 ? -19.859 -10.340 20.817  1.00 8.87  ? 214 GLU   A C   1 
ATOM   1729 O  O   . GLU   A 1 213 ? -19.787 -9.266  20.229  1.00 8.92  ? 214 GLU   A O   1 
ATOM   1730 C  CB  A GLU   A 1 213 ? -22.056 -10.117 21.894  0.50 9.20  ? 214 GLU   A CB  1 
ATOM   1731 C  CB  B GLU   A 1 213 ? -22.064 -10.045 21.903  0.50 10.30 ? 214 GLU   A CB  1 
ATOM   1732 C  CG  A GLU   A 1 213 ? -22.751 -11.145 21.055  0.50 10.58 ? 214 GLU   A CG  1 
ATOM   1733 C  CG  B GLU   A 1 213 ? -22.818 -10.906 20.923  0.50 12.47 ? 214 GLU   A CG  1 
ATOM   1734 C  CD  A GLU   A 1 213 ? -24.256 -10.989 20.827  0.50 11.91 ? 214 GLU   A CD  1 
ATOM   1735 C  CD  B GLU   A 1 213 ? -24.256 -10.464 20.654  0.50 14.40 ? 214 GLU   A CD  1 
ATOM   1736 O  OE1 A GLU   A 1 213 ? -24.828 -9.888  21.091  0.50 11.32 ? 214 GLU   A OE1 1 
ATOM   1737 O  OE1 B GLU   A 1 213 ? -24.915 -9.986  21.603  0.50 15.46 ? 214 GLU   A OE1 1 
ATOM   1738 O  OE2 A GLU   A 1 213 ? -24.850 -11.949 20.257  0.50 14.73 ? 214 GLU   A OE2 1 
ATOM   1739 O  OE2 B GLU   A 1 213 ? -24.733 -10.615 19.494  0.50 16.62 ? 214 GLU   A OE2 1 
ATOM   1740 N  N   A PRO   A 1 214 ? -19.230 -11.446 20.353  0.50 9.10  ? 215 PRO   A N   1 
ATOM   1741 N  N   B PRO   A 1 214 ? -19.323 -11.466 20.305  0.50 9.18  ? 215 PRO   A N   1 
ATOM   1742 C  CA  A PRO   A 1 214 ? -18.605 -11.437 19.025  0.50 9.16  ? 215 PRO   A CA  1 
ATOM   1743 C  CA  B PRO   A 1 214 ? -18.678 -11.414 18.999  0.50 9.18  ? 215 PRO   A CA  1 
ATOM   1744 C  C   A PRO   A 1 214 ? -19.628 -11.466 17.897  0.50 9.12  ? 215 PRO   A C   1 
ATOM   1745 C  C   B PRO   A 1 214 ? -19.733 -11.293 17.912  0.50 9.14  ? 215 PRO   A C   1 
ATOM   1746 O  O   A PRO   A 1 214 ? -20.739 -11.972 18.090  0.50 9.67  ? 215 PRO   A O   1 
ATOM   1747 O  O   B PRO   A 1 214 ? -20.932 -11.516 18.145  0.50 9.59  ? 215 PRO   A O   1 
ATOM   1748 C  CB  A PRO   A 1 214 ? -17.810 -12.747 18.968  0.50 9.92  ? 215 PRO   A CB  1 
ATOM   1749 C  CB  B PRO   A 1 214 ? -17.945 -12.754 18.899  0.50 10.01 ? 215 PRO   A CB  1 
ATOM   1750 C  CG  A PRO   A 1 214 ? -17.758 -13.236 20.378  0.50 10.66 ? 215 PRO   A CG  1 
ATOM   1751 C  CG  B PRO   A 1 214 ? -18.756 -13.692 19.757  0.50 10.95 ? 215 PRO   A CG  1 
ATOM   1752 C  CD  A PRO   A 1 214 ? -19.001 -12.718 21.044  0.50 9.73  ? 215 PRO   A CD  1 
ATOM   1753 C  CD  B PRO   A 1 214 ? -19.334 -12.825 20.849  0.50 10.23 ? 215 PRO   A CD  1 
ATOM   1754 N  N   . ILE   A 1 215 ? -19.250 -10.964 16.717  1.00 9.00  ? 216 ILE   A N   1 
ATOM   1755 C  CA  . ILE   A 1 215 ? -20.013 -11.195 15.516  1.00 9.17  ? 216 ILE   A CA  1 
ATOM   1756 C  C   . ILE   A 1 215 ? -19.453 -12.434 14.846  1.00 9.23  ? 216 ILE   A C   1 
ATOM   1757 O  O   . ILE   A 1 215 ? -18.298 -12.802 15.003  1.00 10.61 ? 216 ILE   A O   1 
ATOM   1758 C  CB  . ILE   A 1 215 ? -20.024 -9.977  14.596  1.00 9.46  ? 216 ILE   A CB  1 
ATOM   1759 C  CG1 . ILE   A 1 215 ? -18.642 -9.614  14.087  1.00 9.56  ? 216 ILE   A CG1 1 
ATOM   1760 C  CG2 . ILE   A 1 215 ? -20.719 -8.809  15.278  1.00 10.49 ? 216 ILE   A CG2 1 
ATOM   1761 C  CD1 . ILE   A 1 215 ? -18.633 -8.600  12.945  1.00 11.56 ? 216 ILE   A CD1 1 
ATOM   1762 N  N   A SER   A 1 216 ? -20.320 -13.053 14.029  0.50 9.78  ? 217 SER   A N   1 
ATOM   1763 N  N   C SER   A 1 216 ? -20.300 -13.155 14.112  0.50 10.41 ? 217 SER   A N   1 
ATOM   1764 C  CA  A SER   A 1 216 ? -19.978 -14.217 13.216  0.50 9.71  ? 217 SER   A CA  1 
ATOM   1765 C  CA  C SER   A 1 216 ? -19.790 -14.254 13.301  0.50 11.22 ? 217 SER   A CA  1 
ATOM   1766 C  C   A SER   A 1 216 ? -19.731 -13.790 11.782  0.50 10.21 ? 217 SER   A C   1 
ATOM   1767 C  C   C SER   A 1 216 ? -19.743 -13.861 11.844  0.50 10.62 ? 217 SER   A C   1 
ATOM   1768 O  O   A SER   A 1 216 ? -20.484 -12.994 11.219  0.50 11.10 ? 217 SER   A O   1 
ATOM   1769 O  O   C SER   A 1 216 ? -20.677 -13.212 11.354  0.50 10.62 ? 217 SER   A O   1 
ATOM   1770 C  CB  A SER   A 1 216 ? -21.034 -15.302 13.270  0.25 9.67  ? 217 SER   A CB  1 
ATOM   1771 C  CB  B SER   A 1 216 ? -21.188 -15.367 13.441  0.25 12.59 ? 217 SER   A CB  1 
ATOM   1772 C  CB  C SER   A 1 216 ? -20.583 -15.497 13.434  0.50 12.96 ? 217 SER   A CB  1 
ATOM   1773 O  OG  A SER   A 1 216 ? -21.029 -15.975 14.530  0.25 10.15 ? 217 SER   A OG  1 
ATOM   1774 O  OG  B SER   A 1 216 ? -20.740 -16.421 12.607  0.25 12.87 ? 217 SER   A OG  1 
ATOM   1775 O  OG  C SER   A 1 216 ? -21.929 -15.262 13.077  0.50 16.14 ? 217 SER   A OG  1 
ATOM   1776 N  N   . VAL   A 1 217 ? -18.634 -14.281 11.213  1.00 9.77  ? 218 VAL   A N   1 
ATOM   1777 C  CA  . VAL   A 1 217 ? -18.377 -14.099 9.799   1.00 9.68  ? 218 VAL   A CA  1 
ATOM   1778 C  C   . VAL   A 1 217 ? -18.137 -15.464 9.190   1.00 9.65  ? 218 VAL   A C   1 
ATOM   1779 O  O   . VAL   A 1 217 ? -17.756 -16.399 9.880   1.00 10.52 ? 218 VAL   A O   1 
ATOM   1780 C  CB  . VAL   A 1 217 ? -17.187 -13.162 9.560   1.00 10.70 ? 218 VAL   A CB  1 
ATOM   1781 C  CG1 . VAL   A 1 217 ? -17.402 -11.832 10.230  1.00 11.15 ? 218 VAL   A CG1 1 
ATOM   1782 C  CG2 . VAL   A 1 217 ? -15.863 -13.773 10.008  1.00 12.16 ? 218 VAL   A CG2 1 
ATOM   1783 N  N   . SER   A 1 218 ? -18.263 -15.608 7.878   1.00 9.69  ? 219 SER   A N   1 
ATOM   1784 C  CA  . SER   A 1 218 ? -18.054 -16.926 7.290   1.00 10.00 ? 219 SER   A CA  1 
ATOM   1785 C  C   . SER   A 1 218 ? -16.579 -17.176 6.966   1.00 10.34 ? 219 SER   A C   1 
ATOM   1786 O  O   . SER   A 1 218 ? -15.770 -16.242 6.853   1.00 10.35 ? 219 SER   A O   1 
ATOM   1787 C  CB  . SER   A 1 218 ? -18.876 -17.095 6.044   1.00 10.58 ? 219 SER   A CB  1 
ATOM   1788 O  OG  . SER   A 1 218 ? -18.440 -16.201 5.054   1.00 11.72 ? 219 SER   A OG  1 
ATOM   1789 N  N   . SER   A 1 219 ? -16.271 -18.447 6.784   1.00 10.31 ? 220 SER   A N   1 
ATOM   1790 C  CA  . SER   A 1 219 ? -14.921 -18.808 6.374   1.00 11.21 ? 220 SER   A CA  1 
ATOM   1791 C  C   . SER   A 1 219 ? -14.570 -18.102 5.066   1.00 11.08 ? 220 SER   A C   1 
ATOM   1792 O  O   . SER   A 1 219 ? -13.452 -17.663 4.869   1.00 12.26 ? 220 SER   A O   1 
ATOM   1793 C  CB  . SER   A 1 219 ? -14.817 -20.319 6.281   1.00 14.48 ? 220 SER   A CB  1 
ATOM   1794 O  OG  . SER   A 1 219 ? -15.839 -20.905 5.492   1.00 17.87 ? 220 SER   A OG  1 
ATOM   1795 N  N   . GLU   A 1 220 ? -15.522 -17.993 4.149   1.00 11.32 ? 221 GLU   A N   1 
ATOM   1796 C  CA  . GLU   A 1 220 ? -15.224 -17.351 2.877   1.00 11.61 ? 221 GLU   A CA  1 
ATOM   1797 C  C   . GLU   A 1 220 ? -14.909 -15.870 3.060   1.00 11.20 ? 221 GLU   A C   1 
ATOM   1798 O  O   . GLU   A 1 220 ? -14.064 -15.303 2.342   1.00 12.49 ? 221 GLU   A O   1 
ATOM   1799 C  CB  . GLU   A 1 220 ? -16.372 -17.495 1.898   1.00 13.17 ? 221 GLU   A CB  1 
ATOM   1800 C  CG  . GLU   A 1 220 ? -16.598 -18.910 1.404   1.00 15.08 ? 221 GLU   A CG  1 
ATOM   1801 C  CD  . GLU   A 1 220 ? -17.471 -19.742 2.318   1.00 16.75 ? 221 GLU   A CD  1 
ATOM   1802 O  OE1 . GLU   A 1 220 ? -18.000 -19.260 3.299   1.00 16.02 ? 221 GLU   A OE1 1 
ATOM   1803 O  OE2 . GLU   A 1 220 ? -17.693 -20.920 2.018   1.00 23.86 ? 221 GLU   A OE2 1 
ATOM   1804 N  N   . GLN   A 1 221 ? -15.605 -15.204 3.984   1.00 10.10 ? 222 GLN   A N   1 
ATOM   1805 C  CA  . GLN   A 1 221 ? -15.327 -13.806 4.241   1.00 9.69  ? 222 GLN   A CA  1 
ATOM   1806 C  C   . GLN   A 1 221 ? -13.915 -13.585 4.776   1.00 9.88  ? 222 GLN   A C   1 
ATOM   1807 O  O   . GLN   A 1 221 ? -13.173 -12.725 4.290   1.00 10.94 ? 222 GLN   A O   1 
ATOM   1808 C  CB  . GLN   A 1 221 ? -16.399 -13.225 5.156   1.00 9.61  ? 222 GLN   A CB  1 
ATOM   1809 C  CG  . GLN   A 1 221 ? -17.765 -13.112 4.500   1.00 9.69  ? 222 GLN   A CG  1 
ATOM   1810 C  CD  . GLN   A 1 221 ? -18.870 -12.582 5.380   1.00 9.56  ? 222 GLN   A CD  1 
ATOM   1811 O  OE1 . GLN   A 1 221 ? -18.987 -12.953 6.547   1.00 10.11 ? 222 GLN   A OE1 1 
ATOM   1812 N  NE2 . GLN   A 1 221 ? -19.679 -11.698 4.827   1.00 10.09 ? 222 GLN   A NE2 1 
ATOM   1813 N  N   . VAL   A 1 222 ? -13.517 -14.379 5.779   1.00 10.20 ? 223 VAL   A N   1 
ATOM   1814 C  CA  . VAL   A 1 222 ? -12.170 -14.188 6.325   1.00 11.32 ? 223 VAL   A CA  1 
ATOM   1815 C  C   . VAL   A 1 222 ? -11.116 -14.619 5.309   1.00 10.78 ? 223 VAL   A C   1 
ATOM   1816 O  O   . VAL   A 1 222 ? -10.045 -14.016 5.263   1.00 11.48 ? 223 VAL   A O   1 
ATOM   1817 C  CB  . VAL   A 1 222 ? -12.014 -14.851 7.693   1.00 13.45 ? 223 VAL   A CB  1 
ATOM   1818 C  CG1 . VAL   A 1 222 ? -11.983 -16.333 7.634   1.00 15.77 ? 223 VAL   A CG1 1 
ATOM   1819 C  CG2 . VAL   A 1 222 ? -10.785 -14.317 8.400   1.00 15.16 ? 223 VAL   A CG2 1 
ATOM   1820 N  N   . LEU   A 1 223 ? -11.413 -15.608 4.479   1.00 11.23 ? 224 LEU   A N   1 
ATOM   1821 C  CA  . LEU   A 1 223 ? -10.448 -15.997 3.467   1.00 12.70 ? 224 LEU   A CA  1 
ATOM   1822 C  C   . LEU   A 1 223 ? -10.136 -14.844 2.528   1.00 12.42 ? 224 LEU   A C   1 
ATOM   1823 O  O   . LEU   A 1 223 ? -8.997  -14.702 2.051   1.00 13.01 ? 224 LEU   A O   1 
ATOM   1824 C  CB  . LEU   A 1 223 ? -10.929 -17.235 2.719   1.00 14.76 ? 224 LEU   A CB  1 
ATOM   1825 C  CG  . LEU   A 1 223 ? -10.731 -18.556 3.484   1.00 18.21 ? 224 LEU   A CG  1 
ATOM   1826 C  CD1 . LEU   A 1 223 ? -11.533 -19.691 2.881   1.00 21.54 ? 224 LEU   A CD1 1 
ATOM   1827 C  CD2 . LEU   A 1 223 ? -9.259  -18.957 3.562   1.00 19.84 ? 224 LEU   A CD2 1 
ATOM   1828 N  N   . LYS   A 1 224 ? -11.127 -14.009 2.233   1.00 11.38 ? 225 LYS   A N   1 
ATOM   1829 C  CA  . LYS   A 1 224 ? -10.889 -12.849 1.389   1.00 12.00 ? 225 LYS   A CA  1 
ATOM   1830 C  C   . LYS   A 1 224 ? -10.015 -11.811 2.064   1.00 10.58 ? 225 LYS   A C   1 
ATOM   1831 O  O   . LYS   A 1 224 ? -9.215  -11.172 1.390   1.00 11.62 ? 225 LYS   A O   1 
ATOM   1832 C  CB  . LYS   A 1 224 ? -12.214 -12.314 0.848   1.00 14.38 ? 225 LYS   A CB  1 
ATOM   1833 C  CG  . LYS   A 1 224 ? -12.825 -13.318 -0.150  1.00 18.15 ? 225 LYS   A CG  1 
ATOM   1834 C  CD  . LYS   A 1 224 ? -14.099 -13.003 -0.881  1.00 22.22 ? 225 LYS   A CD  1 
ATOM   1835 C  CE  . LYS   A 1 224 ? -14.652 -14.139 -1.748  1.00 26.11 ? 225 LYS   A CE  1 
ATOM   1836 N  NZ  . LYS   A 1 224 ? -15.879 -13.809 -2.525  1.00 24.96 ? 225 LYS   A NZ  1 
ATOM   1837 N  N   . PHE   A 1 225 ? -10.132 -11.632 3.374   1.00 10.00 ? 226 PHE   A N   1 
ATOM   1838 C  CA  . PHE   A 1 225 ? -9.187  -10.774 4.055   1.00 9.66  ? 226 PHE   A CA  1 
ATOM   1839 C  C   . PHE   A 1 225 ? -7.754  -11.243 3.835   1.00 9.19  ? 226 PHE   A C   1 
ATOM   1840 O  O   . PHE   A 1 225 ? -6.823  -10.450 3.656   1.00 9.74  ? 226 PHE   A O   1 
ATOM   1841 C  CB  . PHE   A 1 225 ? -9.427  -10.757 5.558   1.00 10.14 ? 226 PHE   A CB  1 
ATOM   1842 C  CG  . PHE   A 1 225 ? -10.600 -9.981  6.109   1.00 9.93  ? 226 PHE   A CG  1 
ATOM   1843 C  CD1 . PHE   A 1 225 ? -11.710 -9.590  5.393   1.00 13.31 ? 226 PHE   A CD1 1 
ATOM   1844 C  CD2 . PHE   A 1 225 ? -10.668 -9.759  7.497   1.00 14.00 ? 226 PHE   A CD2 1 
ATOM   1845 C  CE1 . PHE   A 1 225 ? -12.759 -8.889  5.952   1.00 14.42 ? 226 PHE   A CE1 1 
ATOM   1846 C  CE2 . PHE   A 1 225 ? -11.731 -9.072  8.069   1.00 16.00 ? 226 PHE   A CE2 1 
ATOM   1847 C  CZ  . PHE   A 1 225 ? -12.738 -8.571  7.276   1.00 14.33 ? 226 PHE   A CZ  1 
ATOM   1848 N  N   . ARG   A 1 226 ? -7.568  -12.557 3.865   1.00 9.37  ? 227 ARG   A N   1 
ATOM   1849 C  CA  . ARG   A 1 226 ? -6.241  -13.154 3.797   1.00 9.84  ? 227 ARG   A CA  1 
ATOM   1850 C  C   . ARG   A 1 226 ? -5.636  -13.121 2.400   1.00 10.32 ? 227 ARG   A C   1 
ATOM   1851 O  O   . ARG   A 1 226 ? -4.483  -13.530 2.260   1.00 11.53 ? 227 ARG   A O   1 
ATOM   1852 C  CB  . ARG   A 1 226 ? -6.293  -14.593 4.307   1.00 10.31 ? 227 ARG   A CB  1 
ATOM   1853 C  CG  . ARG   A 1 226 ? -6.739  -14.716 5.753   1.00 9.93  ? 227 ARG   A CG  1 
ATOM   1854 C  CD  . ARG   A 1 226 ? -6.736  -16.149 6.204   1.00 11.67 ? 227 ARG   A CD  1 
ATOM   1855 N  NE  . ARG   A 1 226 ? -7.204  -16.324 7.566   1.00 10.97 ? 227 ARG   A NE  1 
ATOM   1856 C  CZ  . ARG   A 1 226 ? -8.058  -17.255 7.952   1.00 11.84 ? 227 ARG   A CZ  1 
ATOM   1857 N  NH1 . ARG   A 1 226 ? -8.467  -18.189 7.133   1.00 14.87 ? 227 ARG   A NH1 1 
ATOM   1858 N  NH2 . ARG   A 1 226 ? -8.528  -17.236 9.182   1.00 13.06 ? 227 ARG   A NH2 1 
ATOM   1859 N  N   . LYS   A 1 227 ? -6.351  -12.654 1.403   1.00 9.52  ? 228 LYS   A N   1 
ATOM   1860 C  CA  . LYS   A 1 227 ? -5.821  -12.477 0.052   1.00 10.76 ? 228 LYS   A CA  1 
ATOM   1861 C  C   . LYS   A 1 227 ? -5.198  -11.121 -0.144  1.00 10.03 ? 228 LYS   A C   1 
ATOM   1862 O  O   . LYS   A 1 227 ? -4.572  -10.893 -1.184  1.00 11.54 ? 228 LYS   A O   1 
ATOM   1863 C  CB  . LYS   A 1 227 ? -6.910  -12.717 -0.989  1.00 12.81 ? 228 LYS   A CB  1 
ATOM   1864 C  CG  . LYS   A 1 227 ? -7.458  -14.122 -1.004  1.00 16.43 ? 228 LYS   A CG  1 
ATOM   1865 C  CD  . LYS   A 1 227 ? -8.494  -14.357 -2.091  1.00 21.04 ? 228 LYS   A CD  1 
ATOM   1866 N  N   . LEU   A 1 228 ? -5.425  -10.192 0.776   1.00 9.42  ? 229 LEU   A N   1 
ATOM   1867 C  CA  . LEU   A 1 228 ? -4.786  -8.898  0.703   1.00 9.30  ? 229 LEU   A CA  1 
ATOM   1868 C  C   . LEU   A 1 228 ? -3.273  -9.037  0.805   1.00 9.00  ? 229 LEU   A C   1 
ATOM   1869 O  O   . LEU   A 1 228 ? -2.769  -10.070 1.233   1.00 9.73  ? 229 LEU   A O   1 
ATOM   1870 C  CB  . LEU   A 1 228 ? -5.320  -7.992  1.806   1.00 9.55  ? 229 LEU   A CB  1 
ATOM   1871 C  CG  . LEU   A 1 228 ? -6.748  -7.524  1.605   1.00 9.98  ? 229 LEU   A CG  1 
ATOM   1872 C  CD1 . LEU   A 1 228 ? -7.291  -6.979  2.881   1.00 10.83 ? 229 LEU   A CD1 1 
ATOM   1873 C  CD2 . LEU   A 1 228 ? -6.837  -6.473  0.519   1.00 12.11 ? 229 LEU   A CD2 1 
ATOM   1874 N  N   . ASN   A 1 229 ? -2.568  -7.983  0.418   1.00 9.28  ? 230 ASN   A N   1 
ATOM   1875 C  CA  . ASN   A 1 229 ? -1.125  -7.949  0.426   1.00 9.27  ? 230 ASN   A CA  1 
ATOM   1876 C  C   . ASN   A 1 229 ? -0.621  -6.809  1.313   1.00 9.12  ? 230 ASN   A C   1 
ATOM   1877 O  O   . ASN   A 1 229 ? -1.122  -5.696  1.256   1.00 9.99  ? 230 ASN   A O   1 
ATOM   1878 C  CB  . ASN   A 1 229 ? -0.547  -7.749  -0.968  1.00 10.27 ? 230 ASN   A CB  1 
ATOM   1879 C  CG  . ASN   A 1 229 ? -0.592  -8.892  -1.927  1.00 12.36 ? 230 ASN   A CG  1 
ATOM   1880 O  OD1 . ASN   A 1 229 ? -0.061  -8.710  -3.031  1.00 15.00 ? 230 ASN   A OD1 1 
ATOM   1881 N  ND2 . ASN   A 1 229 ? -1.195  -10.022 -1.575  1.00 12.63 ? 230 ASN   A ND2 1 
ATOM   1882 N  N   . PHE   A 1 230 ? 0.458   -7.078  2.062   1.00 9.37  ? 231 PHE   A N   1 
ATOM   1883 C  CA  . PHE   A 1 230 ? 1.200   -6.032  2.751   1.00 9.97  ? 231 PHE   A CA  1 
ATOM   1884 C  C   . PHE   A 1 230 ? 2.021   -5.162  1.793   1.00 10.51 ? 231 PHE   A C   1 
ATOM   1885 O  O   . PHE   A 1 230 ? 2.240   -3.976  2.049   1.00 11.88 ? 231 PHE   A O   1 
ATOM   1886 C  CB  . PHE   A 1 230 ? 2.193   -6.643  3.758   1.00 10.44 ? 231 PHE   A CB  1 
ATOM   1887 C  CG  . PHE   A 1 230 ? 1.652   -7.240  5.030   1.00 9.82  ? 231 PHE   A CG  1 
ATOM   1888 C  CD1 . PHE   A 1 230 ? 0.880   -6.489  5.903   1.00 10.20 ? 231 PHE   A CD1 1 
ATOM   1889 C  CD2 . PHE   A 1 230 ? 1.976   -8.535  5.404   1.00 10.74 ? 231 PHE   A CD2 1 
ATOM   1890 C  CE1 . PHE   A 1 230 ? 0.485   -7.019  7.116   1.00 10.50 ? 231 PHE   A CE1 1 
ATOM   1891 C  CE2 . PHE   A 1 230 ? 1.579   -9.050  6.621   1.00 10.76 ? 231 PHE   A CE2 1 
ATOM   1892 C  CZ  . PHE   A 1 230 ? 0.845   -8.281  7.492   1.00 10.86 ? 231 PHE   A CZ  1 
ATOM   1893 N  N   . ASN   A 1 231 ? 2.495   -5.776  0.714   1.00 10.87 ? 232 ASN   A N   1 
ATOM   1894 C  CA  . ASN   A 1 231 ? 3.379   -5.144  -0.250  1.00 12.21 ? 232 ASN   A CA  1 
ATOM   1895 C  C   . ASN   A 1 231 ? 2.606   -4.246  -1.197  1.00 11.32 ? 232 ASN   A C   1 
ATOM   1896 O  O   . ASN   A 1 231 ? 1.404   -4.365  -1.389  1.00 11.12 ? 232 ASN   A O   1 
ATOM   1897 C  CB  . ASN   A 1 231 ? 4.125   -6.218  -1.034  1.00 13.13 ? 232 ASN   A CB  1 
ATOM   1898 C  CG  . ASN   A 1 231 ? 3.143   -7.171  -1.653  1.00 12.80 ? 232 ASN   A CG  1 
ATOM   1899 O  OD1 . ASN   A 1 231 ? 2.610   -8.058  -0.985  1.00 12.96 ? 232 ASN   A OD1 1 
ATOM   1900 N  ND2 . ASN   A 1 231 ? 2.817   -6.982  -2.924  1.00 15.08 ? 232 ASN   A ND2 1 
ATOM   1901 N  N   . GLY   A 1 232 ? 3.370   -3.370  -1.861  1.00 12.78 ? 233 GLY   A N   1 
ATOM   1902 C  CA  . GLY   A 1 232 ? 2.861   -2.591  -2.959  1.00 12.35 ? 233 GLY   A CA  1 
ATOM   1903 C  C   . GLY   A 1 232 ? 2.854   -3.382  -4.265  1.00 12.13 ? 233 GLY   A C   1 
ATOM   1904 O  O   . GLY   A 1 232 ? 3.489   -4.427  -4.385  1.00 14.99 ? 233 GLY   A O   1 
ATOM   1905 N  N   . GLU   A 1 233 ? 2.097   -2.884  -5.243  1.00 12.43 ? 234 GLU   A N   1 
ATOM   1906 C  CA  . GLU   A 1 233 ? 2.039   -3.501  -6.560  1.00 13.26 ? 234 GLU   A CA  1 
ATOM   1907 C  C   . GLU   A 1 233 ? 3.443   -3.547  -7.178  1.00 14.17 ? 234 GLU   A C   1 
ATOM   1908 O  O   . GLU   A 1 233 ? 4.197   -2.576  -7.114  1.00 15.66 ? 234 GLU   A O   1 
ATOM   1909 C  CB  . GLU   A 1 233 ? 1.072   -2.736  -7.465  1.00 14.32 ? 234 GLU   A CB  1 
ATOM   1910 C  CG  . GLU   A 1 233 ? 0.838   -3.318  -8.847  1.00 17.68 ? 234 GLU   A CG  1 
ATOM   1911 C  CD  . GLU   A 1 233 ? -0.059  -2.441  -9.713  1.00 23.10 ? 234 GLU   A CD  1 
ATOM   1912 O  OE1 . GLU   A 1 233 ? -0.389  -1.220  -9.337  1.00 26.07 ? 234 GLU   A OE1 1 
ATOM   1913 O  OE2 . GLU   A 1 233 ? -0.303  -2.878  -10.828 1.00 28.07 ? 234 GLU   A OE2 1 
ATOM   1914 N  N   . GLY   A 1 234 ? 3.815   -4.677  -7.745  1.00 17.47 ? 235 GLY   A N   1 
ATOM   1915 C  CA  . GLY   A 1 234 ? 5.118   -4.817  -8.378  1.00 19.74 ? 235 GLY   A CA  1 
ATOM   1916 C  C   . GLY   A 1 234 ? 6.265   -5.118  -7.411  1.00 20.56 ? 235 GLY   A C   1 
ATOM   1917 O  O   . GLY   A 1 234 ? 7.413   -5.275  -7.831  1.00 22.88 ? 235 GLY   A O   1 
ATOM   1918 N  N   . GLU   A 1 235 ? 5.904   -5.346  -6.143  1.00 21.51 ? 236 GLU   A N   1 
ATOM   1919 C  CA  . GLU   A 1 235 ? 6.830   -5.810  -5.121  1.00 21.07 ? 236 GLU   A CA  1 
ATOM   1920 C  C   . GLU   A 1 235 ? 6.541   -7.266  -4.792  1.00 20.67 ? 236 GLU   A C   1 
ATOM   1921 O  O   . GLU   A 1 235 ? 5.480   -7.791  -5.142  1.00 21.26 ? 236 GLU   A O   1 
ATOM   1922 C  CB  . GLU   A 1 235 ? 6.679   -5.002  -3.838  1.00 23.13 ? 236 GLU   A CB  1 
ATOM   1923 C  CG  . GLU   A 1 235 ? 7.068   -3.562  -4.001  1.00 24.74 ? 236 GLU   A CG  1 
ATOM   1924 C  CD  . GLU   A 1 235 ? 6.877   -2.733  -2.752  1.00 28.87 ? 236 GLU   A CD  1 
ATOM   1925 O  OE1 . GLU   A 1 235 ? 6.263   -3.249  -1.770  1.00 28.82 ? 236 GLU   A OE1 1 
ATOM   1926 O  OE2 . GLU   A 1 235 ? 7.366   -1.579  -2.771  1.00 36.54 ? 236 GLU   A OE2 1 
ATOM   1927 N  N   . PRO   A 1 236 ? 7.481   -7.983  -4.156  1.00 21.44 ? 237 PRO   A N   1 
ATOM   1928 C  CA  . PRO   A 1 236 ? 7.244   -9.383  -3.799  1.00 20.84 ? 237 PRO   A CA  1 
ATOM   1929 C  C   . PRO   A 1 236 ? 5.978   -9.549  -2.946  1.00 18.04 ? 237 PRO   A C   1 
ATOM   1930 O  O   . PRO   A 1 236 ? 5.797   -8.802  -2.001  1.00 19.55 ? 237 PRO   A O   1 
ATOM   1931 C  CB  . PRO   A 1 236 ? 8.505   -9.810  -3.043  1.00 23.03 ? 237 PRO   A CB  1 
ATOM   1932 C  CG  . PRO   A 1 236 ? 9.593   -8.869  -3.502  1.00 25.76 ? 237 PRO   A CG  1 
ATOM   1933 C  CD  . PRO   A 1 236 ? 8.874   -7.582  -3.836  1.00 24.24 ? 237 PRO   A CD  1 
ATOM   1934 N  N   . GLU   A 1 237 ? 5.158   -10.544 -3.325  1.00 17.54 ? 238 GLU   A N   1 
ATOM   1935 C  CA  . GLU   A 1 237 ? 3.869   -10.739 -2.621  1.00 16.93 ? 238 GLU   A CA  1 
ATOM   1936 C  C   . GLU   A 1 237 ? 4.050   -11.321 -1.225  1.00 14.78 ? 238 GLU   A C   1 
ATOM   1937 O  O   . GLU   A 1 237 ? 4.615   -12.384 -1.021  1.00 16.15 ? 238 GLU   A O   1 
ATOM   1938 C  CB  . GLU   A 1 237 ? 2.916   -11.700 -3.349  1.00 20.28 ? 238 GLU   A CB  1 
ATOM   1939 C  CG  . GLU   A 1 237 ? 1.503   -11.793 -2.744  1.00 22.70 ? 238 GLU   A CG  1 
ATOM   1940 C  CD  . GLU   A 1 237 ? 0.415   -12.479 -3.574  1.00 24.88 ? 238 GLU   A CD  1 
ATOM   1941 O  OE1 . GLU   A 1 237 ? 0.802   -13.249 -4.512  1.00 34.94 ? 238 GLU   A OE1 1 
ATOM   1942 O  OE2 . GLU   A 1 237 ? -0.826  -12.307 -3.322  1.00 20.24 ? 238 GLU   A OE2 1 
ATOM   1943 N  N   . GLU   A 1 238 ? 3.483   -10.623 -0.252  1.00 12.77 ? 239 GLU   A N   1 
ATOM   1944 C  CA  . GLU   A 1 238 ? 3.445   -11.043 1.124   1.00 12.52 ? 239 GLU   A CA  1 
ATOM   1945 C  C   . GLU   A 1 238 ? 2.017   -10.866 1.619   1.00 10.88 ? 239 GLU   A C   1 
ATOM   1946 O  O   . GLU   A 1 238 ? 1.515   -9.738  1.695   1.00 12.31 ? 239 GLU   A O   1 
ATOM   1947 C  CB  . GLU   A 1 238 ? 4.425   -10.265 1.974   1.00 16.25 ? 239 GLU   A CB  1 
ATOM   1948 C  CG  . GLU   A 1 238 ? 4.649   -11.000 3.328   1.00 19.75 ? 239 GLU   A CG  1 
ATOM   1949 C  CD  . GLU   A 1 238 ? 5.012   -12.494 3.486   1.00 21.10 ? 239 GLU   A CD  1 
ATOM   1950 O  OE1 . GLU   A 1 238 ? 5.415   -13.224 2.510   1.00 24.40 ? 239 GLU   A OE1 1 
ATOM   1951 O  OE2 . GLU   A 1 238 ? 4.956   -12.964 4.647   1.00 28.30 ? 239 GLU   A OE2 1 
ATOM   1952 N  N   . LEU   A 1 239 ? 1.377   -11.982 1.904   1.00 10.27 ? 240 LEU   A N   1 
ATOM   1953 C  CA  . LEU   A 1 239 ? -0.028  -11.909 2.269   1.00 9.83  ? 240 LEU   A CA  1 
ATOM   1954 C  C   . LEU   A 1 239 ? -0.201  -11.131 3.561   1.00 9.56  ? 240 LEU   A C   1 
ATOM   1955 O  O   . LEU   A 1 239 ? 0.551   -11.287 4.530   1.00 10.02 ? 240 LEU   A O   1 
ATOM   1956 C  CB  . LEU   A 1 239 ? -0.571  -13.309 2.468   1.00 10.83 ? 240 LEU   A CB  1 
ATOM   1957 C  CG  . LEU   A 1 239 ? -0.638  -14.197 1.232   1.00 12.34 ? 240 LEU   A CG  1 
ATOM   1958 C  CD1 . LEU   A 1 239 ? -1.195  -15.575 1.608   1.00 14.60 ? 240 LEU   A CD1 1 
ATOM   1959 C  CD2 . LEU   A 1 239 ? -1.434  -13.577 0.113   1.00 13.54 ? 240 LEU   A CD2 1 
ATOM   1960 N  N   . MET   A 1 240 ? -1.239  -10.300 3.570   1.00 8.91  ? 241 MET   A N   1 
ATOM   1961 C  CA  . MET   A 1 240 ? -1.622  -9.518  4.742   1.00 9.08  ? 241 MET   A CA  1 
ATOM   1962 C  C   . MET   A 1 240 ? -2.422  -10.433 5.666   1.00 8.83  ? 241 MET   A C   1 
ATOM   1963 O  O   . MET   A 1 240 ? -3.626  -10.589 5.556   1.00 9.69  ? 241 MET   A O   1 
ATOM   1964 C  CB  . MET   A 1 240 ? -2.419  -8.290  4.334   1.00 9.28  ? 241 MET   A CB  1 
ATOM   1965 C  CG  . MET   A 1 240 ? -2.817  -7.393  5.504   1.00 9.49  ? 241 MET   A CG  1 
ATOM   1966 S  SD  . MET   A 1 240 ? -3.784  -5.959  5.026   1.00 10.10 ? 241 MET   A SD  1 
ATOM   1967 C  CE  . MET   A 1 240 ? -2.490  -4.927  4.331   1.00 10.75 ? 241 MET   A CE  1 
ATOM   1968 N  N   . VAL   A 1 241 ? -1.686  -11.082 6.595   1.00 8.53  ? 242 VAL   A N   1 
ATOM   1969 C  CA  . VAL   A 1 241 ? -2.224  -11.965 7.620   1.00 8.23  ? 242 VAL   A CA  1 
ATOM   1970 C  C   . VAL   A 1 241 ? -1.424  -11.765 8.874   1.00 8.15  ? 242 VAL   A C   1 
ATOM   1971 O  O   . VAL   A 1 241 ? -0.267  -11.352 8.841   1.00 8.83  ? 242 VAL   A O   1 
ATOM   1972 C  CB  . VAL   A 1 241 ? -2.161  -13.460 7.208   1.00 9.21  ? 242 VAL   A CB  1 
ATOM   1973 C  CG1 . VAL   A 1 241 ? -3.063  -13.745 6.017   1.00 10.30 ? 242 VAL   A CG1 1 
ATOM   1974 C  CG2 . VAL   A 1 241 ? -0.761  -13.941 6.947   1.00 10.36 ? 242 VAL   A CG2 1 
ATOM   1975 N  N   . ASP   A 1 242 ? -2.039  -12.087 10.019  1.00 7.83  ? 243 ASP   A N   1 
ATOM   1976 C  CA  . ASP   A 1 242 ? -1.366  -11.972 11.303  1.00 7.98  ? 243 ASP   A CA  1 
ATOM   1977 C  C   . ASP   A 1 242 ? -0.870  -10.557 11.559  1.00 7.70  ? 243 ASP   A C   1 
ATOM   1978 O  O   . ASP   A 1 242 ? 0.211   -10.318 12.094  1.00 8.89  ? 243 ASP   A O   1 
ATOM   1979 C  CB  . ASP   A 1 242 ? -0.303  -13.032 11.517  1.00 8.49  ? 243 ASP   A CB  1 
ATOM   1980 C  CG  . ASP   A 1 242 ? -0.889  -14.415 11.577  1.00 8.83  ? 243 ASP   A CG  1 
ATOM   1981 O  OD1 . ASP   A 1 242 ? -1.924  -14.604 12.248  1.00 8.96  ? 243 ASP   A OD1 1 
ATOM   1982 O  OD2 . ASP   A 1 242 ? -0.299  -15.336 10.949  1.00 10.70 ? 243 ASP   A OD2 1 
ATOM   1983 N  N   . ASN   A 1 243 ? -1.756  -9.592  11.287  1.00 7.14  ? 244 ASN   A N   1 
ATOM   1984 C  CA  . ASN   A 1 243 ? -1.502  -8.181  11.539  1.00 7.39  ? 244 ASN   A CA  1 
ATOM   1985 C  C   . ASN   A 1 243 ? -2.043  -7.729  12.893  1.00 7.06  ? 244 ASN   A C   1 
ATOM   1986 O  O   . ASN   A 1 243 ? -2.691  -6.699  13.000  1.00 8.80  ? 244 ASN   A O   1 
ATOM   1987 C  CB  . ASN   A 1 243 ? -2.025  -7.318  10.389  1.00 7.73  ? 244 ASN   A CB  1 
ATOM   1988 C  CG  . ASN   A 1 243 ? -3.512  -7.450  10.191  1.00 8.07  ? 244 ASN   A CG  1 
ATOM   1989 O  OD1 . ASN   A 1 243 ? -4.155  -8.358  10.722  1.00 8.97  ? 244 ASN   A OD1 1 
ATOM   1990 N  ND2 . ASN   A 1 243 ? -4.091  -6.536  9.444   1.00 10.77 ? 244 ASN   A ND2 1 
ATOM   1991 N  N   . TRP   A 1 244 ? -1.736  -8.526  13.917  1.00 7.13  ? 245 TRP   A N   1 
ATOM   1992 C  CA  . TRP   A 1 244 ? -2.165  -8.274  15.283  1.00 7.16  ? 245 TRP   A CA  1 
ATOM   1993 C  C   . TRP   A 1 244 ? -0.968  -8.201  16.201  1.00 7.34  ? 245 TRP   A C   1 
ATOM   1994 O  O   . TRP   A 1 244 ? 0.011   -8.928  16.063  1.00 8.72  ? 245 TRP   A O   1 
ATOM   1995 C  CB  . TRP   A 1 244 ? -3.142  -9.382  15.763  1.00 7.40  ? 245 TRP   A CB  1 
ATOM   1996 C  CG  . TRP   A 1 244 ? -2.679  -10.785 15.579  1.00 7.55  ? 245 TRP   A CG  1 
ATOM   1997 C  CD1 . TRP   A 1 244 ? -2.804  -11.521 14.435  1.00 7.73  ? 245 TRP   A CD1 1 
ATOM   1998 C  CD2 . TRP   A 1 244 ? -2.031  -11.647 16.523  1.00 8.06  ? 245 TRP   A CD2 1 
ATOM   1999 N  NE1 . TRP   A 1 244 ? -2.283  -12.785 14.607  1.00 8.01  ? 245 TRP   A NE1 1 
ATOM   2000 C  CE2 . TRP   A 1 244 ? -1.804  -12.882 15.886  1.00 8.44  ? 245 TRP   A CE2 1 
ATOM   2001 C  CE3 . TRP   A 1 244 ? -1.718  -11.510 17.883  1.00 9.16  ? 245 TRP   A CE3 1 
ATOM   2002 C  CZ2 . TRP   A 1 244 ? -1.207  -13.959 16.546  1.00 9.65  ? 245 TRP   A CZ2 1 
ATOM   2003 C  CZ3 . TRP   A 1 244 ? -1.160  -12.583 18.516  1.00 10.42 ? 245 TRP   A CZ3 1 
ATOM   2004 C  CH2 . TRP   A 1 244 ? -0.903  -13.795 17.868  1.00 10.80 ? 245 TRP   A CH2 1 
ATOM   2005 N  N   . ARG   A 1 245 ? -1.085  -7.319  17.183  1.00 7.63  ? 246 ARG   A N   1 
ATOM   2006 C  CA  . ARG   A 1 245 ? -0.140  -7.211  18.292  1.00 7.97  ? 246 ARG   A CA  1 
ATOM   2007 C  C   . ARG   A 1 245 ? -0.620  -8.126  19.412  1.00 8.26  ? 246 ARG   A C   1 
ATOM   2008 O  O   . ARG   A 1 245 ? -1.811  -8.127  19.727  1.00 8.94  ? 246 ARG   A O   1 
ATOM   2009 C  CB  . ARG   A 1 245 ? -0.071  -5.780  18.809  1.00 8.30  ? 246 ARG   A CB  1 
ATOM   2010 C  CG  . ARG   A 1 245 ? 1.047   -5.518  19.808  1.00 8.00  ? 246 ARG   A CG  1 
ATOM   2011 C  CD  . ARG   A 1 245 ? 0.978   -4.177  20.446  1.00 8.37  ? 246 ARG   A CD  1 
ATOM   2012 N  NE  . ARG   A 1 245 ? 2.205   -3.871  21.158  1.00 8.79  ? 246 ARG   A NE  1 
ATOM   2013 C  CZ  . ARG   A 1 245 ? 2.408   -2.847  21.962  1.00 8.59  ? 246 ARG   A CZ  1 
ATOM   2014 N  NH1 . ARG   A 1 245 ? 1.402   -2.078  22.355  1.00 9.05  ? 246 ARG   A NH1 1 
ATOM   2015 N  NH2 . ARG   A 1 245 ? 3.644   -2.599  22.399  1.00 10.20 ? 246 ARG   A NH2 1 
ATOM   2016 N  N   A PRO   A 1 246 ? 0.270   -8.891  20.068  0.50 7.87  ? 247 PRO   A N   1 
ATOM   2017 N  N   B PRO   A 1 246 ? 0.290   -8.914  20.025  0.50 9.27  ? 247 PRO   A N   1 
ATOM   2018 C  CA  A PRO   A 1 246 ? -0.221  -9.753  21.140  0.50 8.26  ? 247 PRO   A CA  1 
ATOM   2019 C  CA  B PRO   A 1 246 ? -0.068  -9.709  21.199  0.50 10.14 ? 247 PRO   A CA  1 
ATOM   2020 C  C   A PRO   A 1 246 ? -0.482  -8.905  22.396  0.50 8.56  ? 247 PRO   A C   1 
ATOM   2021 C  C   B PRO   A 1 246 ? -0.481  -8.874  22.420  0.50 9.31  ? 247 PRO   A C   1 
ATOM   2022 O  O   A PRO   A 1 246 ? -0.081  -7.743  22.514  0.50 9.07  ? 247 PRO   A O   1 
ATOM   2023 O  O   B PRO   A 1 246 ? -0.176  -7.691  22.553  0.50 9.30  ? 247 PRO   A O   1 
ATOM   2024 C  CB  A PRO   A 1 246 ? 0.912   -10.748 21.321  0.50 8.00  ? 247 PRO   A CB  1 
ATOM   2025 C  CB  B PRO   A 1 246 ? 1.222   -10.441 21.565  0.50 11.36 ? 247 PRO   A CB  1 
ATOM   2026 C  CG  A PRO   A 1 246 ? 2.163   -9.858  21.026  0.50 8.20  ? 247 PRO   A CG  1 
ATOM   2027 C  CG  B PRO   A 1 246 ? 1.970   -10.490 20.284  0.50 12.00 ? 247 PRO   A CG  1 
ATOM   2028 C  CD  A PRO   A 1 246 ? 1.718   -9.010  19.853  0.50 8.45  ? 247 PRO   A CD  1 
ATOM   2029 C  CD  B PRO   A 1 246 ? 1.663   -9.188  19.581  0.50 10.78 ? 247 PRO   A CD  1 
ATOM   2030 N  N   . ALA   A 1 247 ? -1.120  -9.559  23.373  1.00 9.29  ? 248 ALA   A N   1 
ATOM   2031 C  CA  . ALA   A 1 247 ? -1.479  -8.927  24.634  1.00 9.25  ? 248 ALA   A CA  1 
ATOM   2032 C  C   . ALA   A 1 247 ? -0.246  -8.405  25.369  1.00 9.48  ? 248 ALA   A C   1 
ATOM   2033 O  O   . ALA   A 1 247 ? 0.782   -9.087  25.430  1.00 10.81 ? 248 ALA   A O   1 
ATOM   2034 C  CB  . ALA   A 1 247 ? -2.257  -9.892  25.490  1.00 10.91 ? 248 ALA   A CB  1 
ATOM   2035 N  N   . GLN   A 1 248 ? -0.404  -7.225  25.950  1.00 9.18  ? 249 GLN   A N   1 
ATOM   2036 C  CA  . GLN   A 1 248 ? 0.620   -6.515  26.688  1.00 9.70  ? 249 GLN   A CA  1 
ATOM   2037 C  C   . GLN   A 1 248 ? 0.314   -6.537  28.168  1.00 9.85  ? 249 GLN   A C   1 
ATOM   2038 O  O   . GLN   A 1 248 ? -0.826  -6.754  28.590  1.00 10.86 ? 249 GLN   A O   1 
ATOM   2039 C  CB  . GLN   A 1 248 ? 0.686   -5.080  26.186  1.00 9.53  ? 249 GLN   A CB  1 
ATOM   2040 C  CG  . GLN   A 1 248 ? 0.987   -4.995  24.690  1.00 10.34 ? 249 GLN   A CG  1 
ATOM   2041 C  CD  . GLN   A 1 248 ? 2.321   -5.622  24.358  1.00 10.71 ? 249 GLN   A CD  1 
ATOM   2042 O  OE1 . GLN   A 1 248 ? 3.367   -5.291  24.916  1.00 13.52 ? 249 GLN   A OE1 1 
ATOM   2043 N  NE2 . GLN   A 1 248 ? 2.303   -6.553  23.426  1.00 11.14 ? 249 GLN   A NE2 1 
ATOM   2044 N  N   . PRO   A 1 249 ? 1.323   -6.249  29.028  1.00 11.37 ? 250 PRO   A N   1 
ATOM   2045 C  CA  . PRO   A 1 249 ? 1.080   -6.298  30.466  1.00 12.67 ? 250 PRO   A CA  1 
ATOM   2046 C  C   . PRO   A 1 249 ? 0.025   -5.301  30.894  1.00 11.00 ? 250 PRO   A C   1 
ATOM   2047 O  O   . PRO   A 1 249 ? 0.035   -4.144  30.545  1.00 10.92 ? 250 PRO   A O   1 
ATOM   2048 C  CB  . PRO   A 1 249 ? 2.463   -5.985  31.066  1.00 14.94 ? 250 PRO   A CB  1 
ATOM   2049 C  CG  . PRO   A 1 249 ? 3.475   -6.331  29.981  1.00 16.14 ? 250 PRO   A CG  1 
ATOM   2050 C  CD  . PRO   A 1 249 ? 2.747   -5.995  28.713  1.00 13.67 ? 250 PRO   A CD  1 
ATOM   2051 N  N   . LEU   A 1 250 ? -0.854  -5.770  31.792  1.00 11.60 ? 251 LEU   A N   1 
ATOM   2052 C  CA  . LEU   A 1 250 ? -1.894  -4.895  32.314  1.00 11.51 ? 251 LEU   A CA  1 
ATOM   2053 C  C   . LEU   A 1 250 ? -1.352  -3.784  33.200  1.00 10.70 ? 251 LEU   A C   1 
ATOM   2054 O  O   . LEU   A 1 250 ? -1.907  -2.684  33.249  1.00 10.96 ? 251 LEU   A O   1 
ATOM   2055 C  CB  . LEU   A 1 250 ? -2.946  -5.729  33.063  1.00 12.83 ? 251 LEU   A CB  1 
ATOM   2056 C  CG  . LEU   A 1 250 ? -4.236  -5.024  33.442  1.00 14.15 ? 251 LEU   A CG  1 
ATOM   2057 C  CD1 . LEU   A 1 250 ? -5.002  -4.494  32.234  1.00 14.63 ? 251 LEU   A CD1 1 
ATOM   2058 C  CD2 . LEU   A 1 250 ? -5.097  -5.994  34.228  1.00 17.07 ? 251 LEU   A CD2 1 
ATOM   2059 N  N   . LYS   A 1 251 ? -0.298  -4.062  33.957  1.00 11.41 ? 252 LYS   A N   1 
ATOM   2060 C  CA  . LYS   A 1 251 ? 0.310   -3.063  34.837  1.00 12.17 ? 252 LYS   A CA  1 
ATOM   2061 C  C   . LYS   A 1 251 ? -0.747  -2.490  35.780  1.00 12.86 ? 252 LYS   A C   1 
ATOM   2062 O  O   . LYS   A 1 251 ? -1.537  -3.277  36.303  1.00 14.87 ? 252 LYS   A O   1 
ATOM   2063 C  CB  . LYS   A 1 251 ? 1.114   -2.068  34.037  1.00 13.95 ? 252 LYS   A CB  1 
ATOM   2064 C  CG  . LYS   A 1 251 ? 2.266   -2.745  33.318  1.00 16.29 ? 252 LYS   A CG  1 
ATOM   2065 C  CD  . LYS   A 1 251 ? 3.223   -1.817  32.666  1.00 18.49 ? 252 LYS   A CD  1 
ATOM   2066 C  CE  . LYS   A 1 251 ? 4.307   -2.544  31.932  1.00 20.91 ? 252 LYS   A CE  1 
ATOM   2067 N  NZ  . LYS   A 1 251 ? 5.284   -1.613  31.342  1.00 22.37 ? 252 LYS   A NZ  1 
ATOM   2068 N  N   . ASN   A 1 252 ? -0.739  -1.208  36.058  1.00 11.86 ? 253 ASN   A N   1 
ATOM   2069 C  CA  . ASN   A 1 252 ? -1.574  -0.626  37.080  1.00 14.74 ? 253 ASN   A CA  1 
ATOM   2070 C  C   . ASN   A 1 252 ? -2.909  -0.193  36.497  1.00 13.88 ? 253 ASN   A C   1 
ATOM   2071 O  O   . ASN   A 1 252 ? -3.194  1.042   36.448  1.00 16.71 ? 253 ASN   A O   1 
ATOM   2072 C  CB  . ASN   A 1 252 ? -0.870  0.538   37.768  1.00 16.72 ? 253 ASN   A CB  1 
ATOM   2073 C  CG  . ASN   A 1 252 ? -1.654  1.046   38.951  1.00 20.88 ? 253 ASN   A CG  1 
ATOM   2074 O  OD1 . ASN   A 1 252 ? -2.182  0.228   39.696  1.00 26.01 ? 253 ASN   A OD1 1 
ATOM   2075 N  ND2 . ASN   A 1 252 ? -1.791  2.353   39.095  1.00 21.89 ? 253 ASN   A ND2 1 
ATOM   2076 N  N   . ARG   A 1 253 ? -3.681  -1.192  35.965  1.00 12.45 ? 254 ARG   A N   1 
ATOM   2077 C  CA  . ARG   A 1 253 ? -4.979  -0.946  35.392  1.00 10.90 ? 254 ARG   A CA  1 
ATOM   2078 C  C   . ARG   A 1 253 ? -5.978  -1.973  35.881  1.00 11.94 ? 254 ARG   A C   1 
ATOM   2079 O  O   . ARG   A 1 253 ? -5.634  -3.092  36.178  1.00 15.27 ? 254 ARG   A O   1 
ATOM   2080 C  CB  . ARG   A 1 253 ? -4.893  -0.981  33.874  1.00 10.50 ? 254 ARG   A CB  1 
ATOM   2081 C  CG  . ARG   A 1 253 ? -4.067  0.155   33.324  1.00 10.24 ? 254 ARG   A CG  1 
ATOM   2082 C  CD  . ARG   A 1 253 ? -3.953  0.133   31.806  1.00 9.58  ? 254 ARG   A CD  1 
ATOM   2083 N  NE  . ARG   A 1 253 ? -3.120  -0.958  31.362  1.00 9.44  ? 254 ARG   A NE  1 
ATOM   2084 C  CZ  . ARG   A 1 253 ? -2.842  -1.230  30.097  1.00 8.60  ? 254 ARG   A CZ  1 
ATOM   2085 N  NH1 . ARG   A 1 253 ? -3.436  -0.536  29.134  1.00 8.19  ? 254 ARG   A NH1 1 
ATOM   2086 N  NH2 . ARG   A 1 253 ? -1.973  -2.188  29.776  1.00 9.01  ? 254 ARG   A NH2 1 
ATOM   2087 N  N   . GLN   A 1 254 ? -7.234  -1.531  35.947  1.00 12.61 ? 255 GLN   A N   1 
ATOM   2088 C  CA  . GLN   A 1 254 ? -8.374  -2.384  36.211  1.00 14.45 ? 255 GLN   A CA  1 
ATOM   2089 C  C   . GLN   A 1 254 ? -9.287  -2.324  34.989  1.00 13.18 ? 255 GLN   A C   1 
ATOM   2090 O  O   . GLN   A 1 254 ? -9.552  -1.245  34.435  1.00 18.50 ? 255 GLN   A O   1 
ATOM   2091 C  CB  . GLN   A 1 254 ? -9.129  -1.931  37.432  1.00 17.66 ? 255 GLN   A CB  1 
ATOM   2092 C  CG  . GLN   A 1 254 ? -8.381  -2.138  38.708  1.00 21.95 ? 255 GLN   A CG  1 
ATOM   2093 C  CD  . GLN   A 1 254 ? -9.214  -1.879  39.927  1.00 24.70 ? 255 GLN   A CD  1 
ATOM   2094 O  OE1 . GLN   A 1 254 ? -9.094  -2.566  40.950  1.00 29.49 ? 255 GLN   A OE1 1 
ATOM   2095 N  NE2 . GLN   A 1 254 ? -10.035 -0.838  39.852  1.00 25.06 ? 255 GLN   A NE2 1 
ATOM   2096 N  N   . ILE   A 1 255 ? -9.734  -3.462  34.551  1.00 11.29 ? 256 ILE   A N   1 
ATOM   2097 C  CA  . ILE   A 1 255 ? -10.742 -3.554  33.501  1.00 10.19 ? 256 ILE   A CA  1 
ATOM   2098 C  C   . ILE   A 1 255 ? -12.127 -3.557  34.157  1.00 9.88  ? 256 ILE   A C   1 
ATOM   2099 O  O   . ILE   A 1 255 ? -12.348 -4.291  35.143  1.00 12.07 ? 256 ILE   A O   1 
ATOM   2100 C  CB  . ILE   A 1 255 ? -10.521 -4.801  32.648  1.00 11.00 ? 256 ILE   A CB  1 
ATOM   2101 C  CG1 . ILE   A 1 255 ? -9.098  -4.790  32.056  1.00 12.35 ? 256 ILE   A CG1 1 
ATOM   2102 C  CG2 . ILE   A 1 255 ? -11.609 -4.876  31.572  1.00 11.90 ? 256 ILE   A CG2 1 
ATOM   2103 C  CD1 . ILE   A 1 255 ? -8.755  -5.959  31.199  1.00 14.10 ? 256 ILE   A CD1 1 
ATOM   2104 N  N   . LYS   A 1 256 ? -13.008 -2.704  33.678  1.00 9.76  ? 257 LYS   A N   1 
ATOM   2105 C  CA  . LYS   A 1 256 ? -14.365 -2.595  34.196  1.00 10.04 ? 257 LYS   A CA  1 
ATOM   2106 C  C   . LYS   A 1 256 ? -15.329 -3.216  33.218  1.00 9.72  ? 257 LYS   A C   1 
ATOM   2107 O  O   . LYS   A 1 256 ? -15.139 -3.147  32.020  1.00 11.23 ? 257 LYS   A O   1 
ATOM   2108 C  CB  . LYS   A 1 256 ? -14.724 -1.139  34.440  1.00 11.75 ? 257 LYS   A CB  1 
ATOM   2109 C  CG  . LYS   A 1 256 ? -13.822 -0.434  35.458  1.00 16.62 ? 257 LYS   A CG  1 
ATOM   2110 N  N   . ALA   A 1 257 ? -16.401 -3.794  33.746  1.00 10.56 ? 258 ALA   A N   1 
ATOM   2111 C  CA  . ALA   A 1 257 ? -17.468 -4.393  32.969  1.00 10.57 ? 258 ALA   A CA  1 
ATOM   2112 C  C   . ALA   A 1 257 ? -18.726 -3.566  33.117  1.00 10.42 ? 258 ALA   A C   1 
ATOM   2113 O  O   . ALA   A 1 257 ? -19.072 -3.093  34.214  1.00 11.75 ? 258 ALA   A O   1 
ATOM   2114 C  CB  . ALA   A 1 257 ? -17.728 -5.819  33.404  1.00 12.45 ? 258 ALA   A CB  1 
ATOM   2115 N  N   . SER   A 1 258 ? -19.485 -3.465  32.020  1.00 9.80  ? 259 SER   A N   1 
ATOM   2116 C  CA  . SER   A 1 258 ? -20.756 -2.755  32.032  1.00 11.32 ? 259 SER   A CA  1 
ATOM   2117 C  C   . SER   A 1 258 ? -21.914 -3.625  32.496  1.00 12.28 ? 259 SER   A C   1 
ATOM   2118 O  O   . SER   A 1 258 ? -23.031 -3.145  32.617  1.00 15.14 ? 259 SER   A O   1 
ATOM   2119 C  CB  . SER   A 1 258 ? -21.070 -2.257  30.644  1.00 11.84 ? 259 SER   A CB  1 
ATOM   2120 O  OG  . SER   A 1 258 ? -21.498 -3.298  29.785  1.00 11.05 ? 259 SER   A OG  1 
ATOM   2121 N  N   . PHE   A 1 259 ? -21.628 -4.893  32.744  1.00 12.41 ? 260 PHE   A N   1 
ATOM   2122 C  CA  . PHE   A 1 259 ? -22.621 -5.944  32.926  1.00 15.48 ? 260 PHE   A CA  1 
ATOM   2123 C  C   . PHE   A 1 259 ? -22.180 -6.859  34.059  1.00 20.30 ? 260 PHE   A C   1 
ATOM   2124 O  O   . PHE   A 1 259 ? -20.982 -6.977  34.324  1.00 21.96 ? 260 PHE   A O   1 
ATOM   2125 C  CB  . PHE   A 1 259 ? -22.817 -6.759  31.644  1.00 14.48 ? 260 PHE   A CB  1 
ATOM   2126 C  CG  . PHE   A 1 259 ? -21.561 -7.463  31.207  1.00 14.41 ? 260 PHE   A CG  1 
ATOM   2127 C  CD1 . PHE   A 1 259 ? -20.583 -6.800  30.494  1.00 12.95 ? 260 PHE   A CD1 1 
ATOM   2128 C  CD2 . PHE   A 1 259 ? -21.330 -8.773  31.558  1.00 18.93 ? 260 PHE   A CD2 1 
ATOM   2129 C  CE1 . PHE   A 1 259 ? -19.403 -7.448  30.160  1.00 13.89 ? 260 PHE   A CE1 1 
ATOM   2130 C  CE2 . PHE   A 1 259 ? -20.160 -9.428  31.217  1.00 19.02 ? 260 PHE   A CE2 1 
ATOM   2131 C  CZ  . PHE   A 1 259 ? -19.180 -8.742  30.535  1.00 18.38 ? 260 PHE   A CZ  1 
ATOM   2132 N  N   . LYS   A 1 260 ? -23.165 -7.571  34.621  1.00 26.45 ? 261 LYS   A N   1 
ATOM   2133 C  CA  . LYS   A 1 260 ? -22.979 -8.467  35.755  1.00 32.59 ? 261 LYS   A CA  1 
ATOM   2134 C  C   . LYS   A 1 260 ? -22.722 -9.883  35.228  1.00 34.89 ? 261 LYS   A C   1 
ATOM   2135 O  O   . LYS   A 1 260 ? -23.376 -10.246 34.227  1.00 39.16 ? 261 LYS   A O   1 
ATOM   2136 C  CB  . LYS   A 1 260 ? -24.188 -8.435  36.704  1.00 36.62 ? 261 LYS   A CB  1 
HETATM 2137 ZN ZN  . ZN    B 2 .   ? -6.737  -1.651  15.290  1.00 6.61  ? 301 ZN    A ZN  1 
HETATM 2138 C  C1  A A1H15 C 3 .   ? -3.415  5.498   13.677  0.50 13.78 ? 302 A1H15 A C1  1 
HETATM 2139 C  C1  B A1H15 C 3 .   ? -3.749  5.688   14.287  0.50 12.09 ? 302 A1H15 A C1  1 
HETATM 2140 C  C2  A A1H15 C 3 .   ? -4.070  4.331   14.347  0.50 11.69 ? 302 A1H15 A C2  1 
HETATM 2141 C  C2  B A1H15 C 3 .   ? -4.336  4.518   14.960  0.50 10.96 ? 302 A1H15 A C2  1 
HETATM 2142 C  C3  A A1H15 C 3 .   ? -3.275  3.299   14.793  0.50 10.21 ? 302 A1H15 A C3  1 
HETATM 2143 C  C3  B A1H15 C 3 .   ? -3.509  3.465   15.280  0.50 10.68 ? 302 A1H15 A C3  1 
HETATM 2144 C  C4  A A1H15 C 3 .   ? -3.825  2.231   15.460  0.50 8.51  ? 302 A1H15 A C4  1 
HETATM 2145 C  C4  B A1H15 C 3 .   ? -4.018  2.362   15.917  0.50 9.70  ? 302 A1H15 A C4  1 
HETATM 2146 C  C5  A A1H15 C 3 .   ? -5.187  2.220   15.723  0.50 7.93  ? 302 A1H15 A C5  1 
HETATM 2147 C  C5  B A1H15 C 3 .   ? -5.389  2.247   16.116  0.50 8.30  ? 302 A1H15 A C5  1 
HETATM 2148 C  C6  A A1H15 C 3 .   ? -5.978  3.262   15.280  0.50 8.55  ? 302 A1H15 A C6  1 
HETATM 2149 C  C6  B A1H15 C 3 .   ? -6.219  3.323   15.798  0.50 9.23  ? 302 A1H15 A C6  1 
HETATM 2150 C  C7  A A1H15 C 3 .   ? -5.423  4.321   14.599  0.50 10.20 ? 302 A1H15 A C7  1 
HETATM 2151 C  C7  B A1H15 C 3 .   ? -5.698  4.443   15.205  0.50 9.72  ? 302 A1H15 A C7  1 
HETATM 2152 S  S8  A A1H15 C 3 .   ? -5.888  0.888   16.647  0.50 7.13  ? 302 A1H15 A S8  1 
HETATM 2153 S  S8  B A1H15 C 3 .   ? -6.012  0.810   16.947  0.50 6.87  ? 302 A1H15 A S8  1 
HETATM 2154 N  N9  A A1H15 C 3 .   ? -5.356  -0.471  16.040  0.50 7.37  ? 302 A1H15 A N9  1 
HETATM 2155 N  N9  B A1H15 C 3 .   ? -5.505  -0.477  16.180  0.50 7.09  ? 302 A1H15 A N9  1 
HETATM 2156 O  O10 A A1H15 C 3 .   ? -5.339  1.054   17.980  0.50 7.78  ? 302 A1H15 A O10 1 
HETATM 2157 O  O10 B A1H15 C 3 .   ? -5.442  0.867   18.273  0.50 7.36  ? 302 A1H15 A O10 1 
HETATM 2158 O  O11 A A1H15 C 3 .   ? -7.316  1.009   16.477  0.50 6.53  ? 302 A1H15 A O11 1 
HETATM 2159 O  O11 B A1H15 C 3 .   ? -7.446  0.859   16.829  0.50 6.90  ? 302 A1H15 A O11 1 
HETATM 2160 N  N12 A A1H15 C 3 .   ? -4.240  6.273   12.773  0.50 18.06 ? 302 A1H15 A N12 1 
HETATM 2161 N  N12 B A1H15 C 3 .   ? -3.673  5.372   12.879  0.50 17.97 ? 302 A1H15 A N12 1 
HETATM 2162 C  C13 A A1H15 C 3 .   ? -3.899  7.423   12.185  0.70 24.59 ? 302 A1H15 A C13 1 
HETATM 2163 C  C13 B A1H15 C 3 .   ? -4.649  5.474   12.018  0.30 16.87 ? 302 A1H15 A C13 1 
HETATM 2164 N  N14 A A1H15 C 3 .   ? -2.893  8.117   12.820  0.70 27.90 ? 302 A1H15 A N14 1 
HETATM 2165 N  N14 B A1H15 C 3 .   ? -5.652  6.329   12.427  0.30 15.08 ? 302 A1H15 A N14 1 
HETATM 2166 C  C15 A A1H15 C 3 .   ? -1.948  7.586   13.635  0.70 22.80 ? 302 A1H15 A C15 1 
HETATM 2167 C  C15 B A1H15 C 3 .   ? -6.479  6.898   11.492  0.30 15.07 ? 302 A1H15 A C15 1 
HETATM 2168 N  N16 A A1H15 C 3 .   ? -1.819  8.026   14.849  0.70 23.89 ? 302 A1H15 A N16 1 
HETATM 2169 N  N16 B A1H15 C 3 .   ? -6.392  6.490   10.245  0.30 14.14 ? 302 A1H15 A N16 1 
HETATM 2170 N  N17 A A1H15 C 3 .   ? -4.471  7.878   11.081  0.70 30.54 ? 302 A1H15 A N17 1 
HETATM 2171 N  N17 B A1H15 C 3 .   ? -4.668  4.811   10.870  0.30 19.09 ? 302 A1H15 A N17 1 
HETATM 2172 N  N18 A A1H15 C 3 .   ? -1.127  6.670   13.156  0.70 29.31 ? 302 A1H15 A N18 1 
HETATM 2173 N  N18 B A1H15 C 3 .   ? -7.338  7.834   11.770  0.30 15.68 ? 302 A1H15 A N18 1 
HETATM 2174 C  C1  . A1H15 D 3 .   ? 14.446  -1.329  9.445   1.00 21.11 ? 303 A1H15 A C1  1 
HETATM 2175 C  C2  . A1H15 D 3 .   ? 13.518  -1.340  10.623  1.00 21.90 ? 303 A1H15 A C2  1 
HETATM 2176 C  C3  . A1H15 D 3 .   ? 13.436  -2.353  11.573  1.00 25.64 ? 303 A1H15 A C3  1 
HETATM 2177 C  C4  . A1H15 D 3 .   ? 12.585  -2.243  12.658  1.00 23.44 ? 303 A1H15 A C4  1 
HETATM 2178 C  C5  . A1H15 D 3 .   ? 11.805  -1.104  12.776  1.00 20.33 ? 303 A1H15 A C5  1 
HETATM 2179 C  C6  . A1H15 D 3 .   ? 11.972  -0.056  11.887  1.00 22.37 ? 303 A1H15 A C6  1 
HETATM 2180 C  C7  . A1H15 D 3 .   ? 12.754  -0.210  10.772  1.00 25.18 ? 303 A1H15 A C7  1 
HETATM 2181 S  S8  . A1H15 D 3 .   ? 10.706  -0.852  14.126  1.00 18.64 ? 303 A1H15 A S8  1 
HETATM 2182 N  N9  . A1H15 D 3 .   ? 9.969   -2.198  14.296  1.00 18.06 ? 303 A1H15 A N9  1 
HETATM 2183 O  O10 . A1H15 D 3 .   ? 11.439  -0.678  15.400  1.00 22.74 ? 303 A1H15 A O10 1 
HETATM 2184 O  O11 . A1H15 D 3 .   ? 9.922   0.296   13.823  1.00 21.52 ? 303 A1H15 A O11 1 
HETATM 2185 N  N12 . A1H15 D 3 .   ? 14.768  -2.540  8.738   1.00 25.42 ? 303 A1H15 A N12 1 
HETATM 2186 C  C13 . A1H15 D 3 .   ? 14.556  -3.823  8.928   1.00 22.67 ? 303 A1H15 A C13 1 
HETATM 2187 N  N17 . A1H15 D 3 .   ? 14.399  -4.417  10.103  1.00 34.46 ? 303 A1H15 A N17 1 
HETATM 2188 C  C1  . GOL   E 4 .   ? -5.374  1.977   11.848  0.70 20.49 ? 304 GOL   A C1  1 
HETATM 2189 O  O1  . GOL   E 4 .   ? -5.292  3.124   11.006  0.70 18.75 ? 304 GOL   A O1  1 
HETATM 2190 C  C2  . GOL   E 4 .   ? -4.643  0.872   11.133  0.70 18.82 ? 304 GOL   A C2  1 
HETATM 2191 O  O2  . GOL   E 4 .   ? -5.074  0.660   9.796   0.70 12.22 ? 304 GOL   A O2  1 
HETATM 2192 C  C3  . GOL   E 4 .   ? -4.397  -0.462  11.769  0.70 17.11 ? 304 GOL   A C3  1 
HETATM 2193 O  O3  . GOL   E 4 .   ? -3.132  -0.793  11.251  0.70 14.83 ? 304 GOL   A O3  1 
HETATM 2194 O  O   . HOH   F 5 .   ? -5.220  0.497   10.578  0.30 21.95 ? 401 HOH   A O   1 
HETATM 2195 O  O   . HOH   F 5 .   ? -6.614  7.158   10.921  0.70 42.96 ? 402 HOH   A O   1 
HETATM 2196 O  O   . HOH   F 5 .   ? -3.154  7.114   12.338  0.30 11.17 ? 403 HOH   A O   1 
HETATM 2197 O  O   . HOH   F 5 .   ? 3.608   -1.652  8.737   0.50 20.91 ? 404 HOH   A O   1 
HETATM 2198 O  O   . HOH   F 5 .   ? -4.344  -1.371  11.512  0.30 11.50 ? 405 HOH   A O   1 
HETATM 2199 O  O   . HOH   F 5 .   ? -3.904  4.620   9.708   0.70 30.47 ? 406 HOH   A O   1 
HETATM 2200 O  O   . HOH   F 5 .   ? -11.211 -15.190 34.174  0.50 14.66 ? 407 HOH   A O   1 
HETATM 2201 O  O   . HOH   F 5 .   ? -5.431  2.370   12.318  0.30 8.74  ? 408 HOH   A O   1 
HETATM 2202 O  O   . HOH   F 5 .   ? -1.121  1.290   11.500  0.50 17.67 ? 409 HOH   A O   1 
HETATM 2203 O  O   . HOH   F 5 .   ? -25.559 -10.684 17.864  1.00 21.84 ? 410 HOH   A O   1 
HETATM 2204 O  O   . HOH   F 5 .   ? -25.997 6.491   27.245  1.00 34.06 ? 411 HOH   A O   1 
HETATM 2205 O  O   . HOH   F 5 .   ? -19.010 3.594   -3.453  1.00 28.86 ? 412 HOH   A O   1 
HETATM 2206 O  O   . HOH   F 5 .   ? -7.532  -18.726 29.939  1.00 41.07 ? 413 HOH   A O   1 
HETATM 2207 O  O   . HOH   F 5 .   ? -23.249 0.735   34.885  1.00 25.49 ? 414 HOH   A O   1 
HETATM 2208 O  O   . HOH   F 5 .   ? -22.644 -14.514 11.018  0.50 11.87 ? 415 HOH   A O   1 
HETATM 2209 O  O   . HOH   F 5 .   ? -15.354 -10.453 37.358  1.00 22.73 ? 416 HOH   A O   1 
HETATM 2210 O  O   . HOH   F 5 .   ? -13.264 -22.561 11.298  1.00 27.37 ? 417 HOH   A O   1 
HETATM 2211 O  O   . HOH   F 5 .   ? -28.696 -0.027  6.627   1.00 31.19 ? 418 HOH   A O   1 
HETATM 2212 O  O   . HOH   F 5 .   ? -24.179 -3.547  29.642  0.50 14.05 ? 419 HOH   A O   1 
HETATM 2213 O  O   . HOH   F 5 .   ? -21.002 -6.996  -1.924  1.00 30.77 ? 420 HOH   A O   1 
HETATM 2214 O  O   . HOH   F 5 .   ? 9.262   2.021   12.015  1.00 25.05 ? 421 HOH   A O   1 
HETATM 2215 O  O   . HOH   F 5 .   ? 15.247  0.358   15.272  1.00 27.56 ? 422 HOH   A O   1 
HETATM 2216 O  O   . HOH   F 5 .   ? -12.571 12.556  29.181  1.00 25.19 ? 423 HOH   A O   1 
HETATM 2217 O  O   . HOH   F 5 .   ? -14.137 14.465  27.170  1.00 25.96 ? 424 HOH   A O   1 
HETATM 2218 O  O   . HOH   F 5 .   ? -13.993 10.871  27.713  0.50 16.67 ? 425 HOH   A O   1 
HETATM 2219 O  O   . HOH   F 5 .   ? 7.473   -7.546  -0.465  1.00 31.09 ? 426 HOH   A O   1 
HETATM 2220 O  O   . HOH   F 5 .   ? -19.990 -16.660 3.020   1.00 21.92 ? 427 HOH   A O   1 
HETATM 2221 O  O   . HOH   F 5 .   ? -22.168 -13.967 18.953  1.00 35.66 ? 428 HOH   A O   1 
HETATM 2222 O  O   . HOH   F 5 .   ? -8.799  -3.816  7.924   1.00 8.11  ? 429 HOH   A O   1 
HETATM 2223 O  O   . HOH   F 5 .   ? -1.223  -4.166  15.793  1.00 9.77  ? 430 HOH   A O   1 
HETATM 2224 O  O   . HOH   F 5 .   ? -0.034  9.962   14.972  0.70 26.68 ? 431 HOH   A O   1 
HETATM 2225 O  O   . HOH   F 5 .   ? -15.795 8.994   -2.083  1.00 23.34 ? 432 HOH   A O   1 
HETATM 2226 O  O   . HOH   F 5 .   ? 4.207   -3.421  26.598  1.00 18.85 ? 433 HOH   A O   1 
HETATM 2227 O  O   . HOH   F 5 .   ? -25.844 -5.093  13.510  1.00 23.76 ? 434 HOH   A O   1 
HETATM 2228 O  O   . HOH   F 5 .   ? 8.122   -5.855  -10.329 1.00 28.94 ? 435 HOH   A O   1 
HETATM 2229 O  O   . HOH   F 5 .   ? -6.246  -4.403  -6.376  1.00 22.28 ? 436 HOH   A O   1 
HETATM 2230 O  O   . HOH   F 5 .   ? -17.002 -14.018 37.769  1.00 30.52 ? 437 HOH   A O   1 
HETATM 2231 O  O   . HOH   F 5 .   ? -25.746 9.573   13.373  1.00 29.78 ? 438 HOH   A O   1 
HETATM 2232 O  O   . HOH   F 5 .   ? 3.590   5.012   29.853  1.00 17.59 ? 439 HOH   A O   1 
HETATM 2233 O  O   . HOH   F 5 .   ? -31.855 -10.841 16.040  1.00 23.96 ? 440 HOH   A O   1 
HETATM 2234 O  O   . HOH   F 5 .   ? 9.992   -4.576  -7.786  1.00 26.43 ? 441 HOH   A O   1 
HETATM 2235 O  O   . HOH   F 5 .   ? -24.193 8.740   20.339  1.00 20.66 ? 442 HOH   A O   1 
HETATM 2236 O  O   . HOH   F 5 .   ? -18.028 10.554  11.407  1.00 16.41 ? 443 HOH   A O   1 
HETATM 2237 O  O   . HOH   F 5 .   ? -19.037 17.531  18.961  1.00 25.58 ? 444 HOH   A O   1 
HETATM 2238 O  O   . HOH   F 5 .   ? -22.176 -18.450 13.603  1.00 24.17 ? 445 HOH   A O   1 
HETATM 2239 O  O   . HOH   F 5 .   ? -10.744 8.687   25.612  1.00 11.45 ? 446 HOH   A O   1 
HETATM 2240 O  O   . HOH   F 5 .   ? -7.030  5.941   6.619   1.00 19.04 ? 447 HOH   A O   1 
HETATM 2241 O  O   . HOH   F 5 .   ? -14.399 -16.647 28.944  1.00 20.91 ? 448 HOH   A O   1 
HETATM 2242 O  O   . HOH   F 5 .   ? -14.452 -18.596 18.757  1.00 19.45 ? 449 HOH   A O   1 
HETATM 2243 O  O   . HOH   F 5 .   ? -1.315  9.172   28.135  1.00 21.30 ? 450 HOH   A O   1 
HETATM 2244 O  O   . HOH   F 5 .   ? -10.354 -18.332 17.222  1.00 15.31 ? 451 HOH   A O   1 
HETATM 2245 O  O   . HOH   F 5 .   ? -0.459  13.869  16.141  1.00 26.28 ? 452 HOH   A O   1 
HETATM 2246 O  O   . HOH   F 5 .   ? -17.350 -16.354 21.938  1.00 27.26 ? 453 HOH   A O   1 
HETATM 2247 O  O   . HOH   F 5 .   ? -23.406 -11.360 17.084  1.00 27.19 ? 454 HOH   A O   1 
HETATM 2248 O  O   . HOH   F 5 .   ? -21.339 7.859   1.979   1.00 13.75 ? 455 HOH   A O   1 
HETATM 2249 O  O   . HOH   F 5 .   ? -2.558  -8.739  29.186  1.00 12.06 ? 456 HOH   A O   1 
HETATM 2250 O  O   . HOH   F 5 .   ? -10.500 -19.511 19.950  1.00 26.43 ? 457 HOH   A O   1 
HETATM 2251 O  O   . HOH   F 5 .   ? -2.550  -3.423  11.489  1.00 13.28 ? 458 HOH   A O   1 
HETATM 2252 O  O   . HOH   F 5 .   ? 4.247   -2.474  28.992  1.00 24.66 ? 459 HOH   A O   1 
HETATM 2253 O  O   . HOH   F 5 .   ? 0.060   -0.889  -4.666  1.00 12.72 ? 460 HOH   A O   1 
HETATM 2254 O  O   . HOH   F 5 .   ? -27.499 -7.483  26.131  1.00 33.22 ? 461 HOH   A O   1 
HETATM 2255 O  O   . HOH   F 5 .   ? -3.659  -12.825 -2.870  1.00 20.19 ? 462 HOH   A O   1 
HETATM 2256 O  O   . HOH   F 5 .   ? -3.164  -20.544 6.727   1.00 22.61 ? 463 HOH   A O   1 
HETATM 2257 O  O   . HOH   F 5 .   ? -8.027  -15.537 11.384  1.00 10.52 ? 464 HOH   A O   1 
HETATM 2258 O  O   . HOH   F 5 .   ? -0.015  1.122   34.612  1.00 19.07 ? 465 HOH   A O   1 
HETATM 2259 O  O   . HOH   F 5 .   ? 1.211   -11.758 25.065  1.00 24.74 ? 466 HOH   A O   1 
HETATM 2260 O  O   . HOH   F 5 .   ? -22.933 -6.007  2.798   1.00 17.21 ? 467 HOH   A O   1 
HETATM 2261 O  O   . HOH   F 5 .   ? -2.372  -4.403  -6.973  1.00 28.23 ? 468 HOH   A O   1 
HETATM 2262 O  O   . HOH   F 5 .   ? -20.349 10.787  26.604  1.00 17.38 ? 469 HOH   A O   1 
HETATM 2263 O  O   . HOH   F 5 .   ? -4.524  -13.492 18.002  1.00 9.77  ? 470 HOH   A O   1 
HETATM 2264 O  O   . HOH   F 5 .   ? -3.983  0.210   13.649  0.30 6.35  ? 471 HOH   A O   1 
HETATM 2265 O  O   . HOH   F 5 .   ? 13.961  2.022   22.685  1.00 21.56 ? 472 HOH   A O   1 
HETATM 2266 O  O   . HOH   F 5 .   ? -12.158 10.750  5.850   1.00 24.56 ? 473 HOH   A O   1 
HETATM 2267 O  O   . HOH   F 5 .   ? -14.792 20.153  17.601  1.00 21.72 ? 474 HOH   A O   1 
HETATM 2268 O  O   . HOH   F 5 .   ? -7.147  -8.282  -6.965  1.00 31.11 ? 475 HOH   A O   1 
HETATM 2269 O  O   . HOH   F 5 .   ? -11.965 9.471   3.279   1.00 18.60 ? 476 HOH   A O   1 
HETATM 2270 O  O   . HOH   F 5 .   ? -19.790 -3.987  41.393  1.00 30.35 ? 477 HOH   A O   1 
HETATM 2271 O  O   . HOH   F 5 .   ? -3.519  -11.189 20.899  1.00 10.38 ? 478 HOH   A O   1 
HETATM 2272 O  O   . HOH   F 5 .   ? -1.276  -6.001  36.589  1.00 33.45 ? 479 HOH   A O   1 
HETATM 2273 O  O   . HOH   F 5 .   ? -23.252 -3.073  6.906   1.00 20.46 ? 480 HOH   A O   1 
HETATM 2274 O  O   . HOH   F 5 .   ? -18.451 -3.691  -2.600  1.00 26.84 ? 481 HOH   A O   1 
HETATM 2275 O  O   . HOH   F 5 .   ? 5.393   7.056   20.276  1.00 16.15 ? 482 HOH   A O   1 
HETATM 2276 O  O   . HOH   F 5 .   ? 13.428  0.196   24.512  1.00 20.55 ? 483 HOH   A O   1 
HETATM 2277 O  O   . HOH   F 5 .   ? -8.203  6.996   27.960  1.00 25.97 ? 484 HOH   A O   1 
HETATM 2278 O  O   . HOH   F 5 .   ? -5.996  16.818  27.419  1.00 25.99 ? 485 HOH   A O   1 
HETATM 2279 O  O   . HOH   F 5 .   ? -25.687 -15.362 7.866   1.00 28.19 ? 486 HOH   A O   1 
HETATM 2280 O  O   . HOH   F 5 .   ? -26.017 8.127   6.540   1.00 30.96 ? 487 HOH   A O   1 
HETATM 2281 O  O   . HOH   F 5 .   ? 16.012  3.665   15.547  1.00 20.05 ? 488 HOH   A O   1 
HETATM 2282 O  O   . HOH   F 5 .   ? -8.172  7.815   8.598   1.00 23.80 ? 489 HOH   A O   1 
HETATM 2283 O  O   . HOH   F 5 .   ? -8.872  0.752   -6.450  1.00 23.87 ? 490 HOH   A O   1 
HETATM 2284 O  O   . HOH   F 5 .   ? -23.445 -13.345 11.319  0.50 18.00 ? 491 HOH   A O   1 
HETATM 2285 O  O   . HOH   F 5 .   ? -21.661 -7.178  23.616  1.00 11.61 ? 492 HOH   A O   1 
HETATM 2286 O  O   . HOH   F 5 .   ? -6.751  21.042  19.515  0.50 12.33 ? 493 HOH   A O   1 
HETATM 2287 O  O   . HOH   F 5 .   ? -24.931 -7.786  9.177   1.00 15.76 ? 494 HOH   A O   1 
HETATM 2288 O  O   . HOH   F 5 .   ? -17.093 -8.486  20.453  1.00 9.15  ? 495 HOH   A O   1 
HETATM 2289 O  O   . HOH   F 5 .   ? -17.963 -2.902  45.098  1.00 36.28 ? 496 HOH   A O   1 
HETATM 2290 O  O   . HOH   F 5 .   ? -18.823 -20.817 14.975  1.00 30.84 ? 497 HOH   A O   1 
HETATM 2291 O  O   . HOH   F 5 .   ? -3.703  -15.873 24.426  1.00 14.09 ? 498 HOH   A O   1 
HETATM 2292 O  O   . HOH   F 5 .   ? -15.208 -21.847 13.088  1.00 18.82 ? 499 HOH   A O   1 
HETATM 2293 O  O   . HOH   F 5 .   ? -19.501 17.453  6.105   1.00 17.50 ? 500 HOH   A O   1 
HETATM 2294 O  O   . HOH   F 5 .   ? -22.088 5.789   4.847   1.00 12.56 ? 501 HOH   A O   1 
HETATM 2295 O  O   . HOH   F 5 .   ? 9.289   7.476   18.648  1.00 38.34 ? 502 HOH   A O   1 
HETATM 2296 O  O   . HOH   F 5 .   ? -12.923 -8.820  -3.216  1.00 29.30 ? 503 HOH   A O   1 
HETATM 2297 O  O   . HOH   F 5 .   ? -0.529  10.755  23.527  1.00 19.17 ? 504 HOH   A O   1 
HETATM 2298 O  O   . HOH   F 5 .   ? 10.520  -9.015  8.774   1.00 32.11 ? 505 HOH   A O   1 
HETATM 2299 O  O   . HOH   F 5 .   ? -23.999 -2.387  28.958  0.50 22.08 ? 506 HOH   A O   1 
HETATM 2300 O  O   . HOH   F 5 .   ? -7.432  -8.710  32.629  1.00 15.77 ? 507 HOH   A O   1 
HETATM 2301 O  O   . HOH   F 5 .   ? -16.281 15.951  23.447  1.00 20.06 ? 508 HOH   A O   1 
HETATM 2302 O  O   . HOH   F 5 .   ? -13.814 10.262  28.024  0.50 10.49 ? 509 HOH   A O   1 
HETATM 2303 O  O   . HOH   F 5 .   ? -9.454  -10.126 -1.189  1.00 20.03 ? 510 HOH   A O   1 
HETATM 2304 O  O   . HOH   F 5 .   ? 1.121   14.569  24.285  1.00 34.80 ? 511 HOH   A O   1 
HETATM 2305 O  O   . HOH   F 5 .   ? -10.387 -12.566 40.100  1.00 27.73 ? 512 HOH   A O   1 
HETATM 2306 O  O   . HOH   F 5 .   ? -8.036  -22.083 10.279  1.00 26.23 ? 513 HOH   A O   1 
HETATM 2307 O  O   . HOH   F 5 .   ? -12.513 -18.385 32.157  1.00 23.72 ? 514 HOH   A O   1 
HETATM 2308 O  O   . HOH   F 5 .   ? -26.512 2.759   20.891  1.00 19.13 ? 515 HOH   A O   1 
HETATM 2309 O  O   . HOH   F 5 .   ? -25.853 -8.790  11.478  1.00 24.48 ? 516 HOH   A O   1 
HETATM 2310 O  O   . HOH   F 5 .   ? -2.973  6.167   -1.635  1.00 18.57 ? 517 HOH   A O   1 
HETATM 2311 O  O   . HOH   F 5 .   ? -12.841 7.947   28.788  1.00 21.79 ? 518 HOH   A O   1 
HETATM 2312 O  O   . HOH   F 5 .   ? -24.997 4.534   8.618   1.00 26.83 ? 519 HOH   A O   1 
HETATM 2313 O  O   . HOH   F 5 .   ? -1.524  4.781   -4.791  1.00 22.88 ? 520 HOH   A O   1 
HETATM 2314 O  O   . HOH   F 5 .   ? -3.359  -13.248 25.206  1.00 11.71 ? 521 HOH   A O   1 
HETATM 2315 O  O   . HOH   F 5 .   ? -13.548 -0.791  -6.131  1.00 28.19 ? 522 HOH   A O   1 
HETATM 2316 O  O   . HOH   F 5 .   ? 7.124   -3.446  30.251  1.00 37.11 ? 523 HOH   A O   1 
HETATM 2317 O  O   . HOH   F 5 .   ? -18.989 12.240  13.080  1.00 22.57 ? 524 HOH   A O   1 
HETATM 2318 O  O   . HOH   F 5 .   ? -9.999  6.133   -4.102  1.00 34.26 ? 525 HOH   A O   1 
HETATM 2319 O  O   . HOH   F 5 .   ? 3.591   -3.063  4.372   1.00 23.38 ? 526 HOH   A O   1 
HETATM 2320 O  O   . HOH   F 5 .   ? -7.195  -16.801 1.437   1.00 20.02 ? 527 HOH   A O   1 
HETATM 2321 O  O   . HOH   F 5 .   ? -11.180 0.838   33.390  1.00 27.81 ? 528 HOH   A O   1 
HETATM 2322 O  O   . HOH   F 5 .   ? 2.594   -4.188  7.841   1.00 18.66 ? 529 HOH   A O   1 
HETATM 2323 O  O   . HOH   F 5 .   ? -21.452 0.763   0.340   1.00 36.60 ? 530 HOH   A O   1 
HETATM 2324 O  O   . HOH   F 5 .   ? -16.380 -9.981  33.024  1.00 17.59 ? 531 HOH   A O   1 
HETATM 2325 O  O   . HOH   F 5 .   ? -26.804 -2.345  14.629  1.00 18.75 ? 532 HOH   A O   1 
HETATM 2326 O  O   . HOH   F 5 .   ? -13.027 -16.874 26.576  1.00 17.14 ? 533 HOH   A O   1 
HETATM 2327 O  O   . HOH   F 5 .   ? -19.447 10.000  8.983   1.00 12.42 ? 534 HOH   A O   1 
HETATM 2328 O  O   . HOH   F 5 .   ? 4.913   -4.901  21.030  1.00 12.86 ? 535 HOH   A O   1 
HETATM 2329 O  O   . HOH   F 5 .   ? -4.631  -15.936 0.730   1.00 20.03 ? 536 HOH   A O   1 
HETATM 2330 O  O   . HOH   F 5 .   ? 8.182   2.951   27.879  1.00 33.60 ? 537 HOH   A O   1 
HETATM 2331 O  O   . HOH   F 5 .   ? -13.286 -18.530 14.625  1.00 16.82 ? 538 HOH   A O   1 
HETATM 2332 O  O   . HOH   F 5 .   ? 11.206  1.249   25.941  1.00 21.15 ? 539 HOH   A O   1 
HETATM 2333 O  O   . HOH   F 5 .   ? -11.978 2.877   30.745  1.00 19.68 ? 540 HOH   A O   1 
HETATM 2334 O  O   . HOH   F 5 .   ? -26.992 -4.017  25.133  1.00 19.73 ? 541 HOH   A O   1 
HETATM 2335 O  O   . HOH   F 5 .   ? -12.891 3.723   -6.792  1.00 22.76 ? 542 HOH   A O   1 
HETATM 2336 O  O   . HOH   F 5 .   ? -7.615  -4.907  40.176  1.00 28.10 ? 543 HOH   A O   1 
HETATM 2337 O  O   . HOH   F 5 .   ? 1.166   8.767   24.473  1.00 16.56 ? 544 HOH   A O   1 
HETATM 2338 O  O   . HOH   F 5 .   ? -9.058  -5.875  35.969  1.00 18.02 ? 545 HOH   A O   1 
HETATM 2339 O  O   . HOH   F 5 .   ? -3.925  -20.837 15.792  1.00 28.31 ? 546 HOH   A O   1 
HETATM 2340 O  O   . HOH   F 5 .   ? -10.625 8.568   7.781   1.00 22.01 ? 547 HOH   A O   1 
HETATM 2341 O  O   . HOH   F 5 .   ? -13.519 -16.553 -0.197  1.00 29.87 ? 548 HOH   A O   1 
HETATM 2342 O  O   . HOH   F 5 .   ? -23.407 -0.231  32.351  1.00 24.77 ? 549 HOH   A O   1 
HETATM 2343 O  O   . HOH   F 5 .   ? -23.401 -18.339 6.294   1.00 29.81 ? 550 HOH   A O   1 
HETATM 2344 O  O   . HOH   F 5 .   ? -25.827 -3.588  32.056  1.00 38.84 ? 551 HOH   A O   1 
HETATM 2345 O  O   . HOH   F 5 .   ? -21.020 18.912  13.839  1.00 26.99 ? 552 HOH   A O   1 
HETATM 2346 O  O   . HOH   F 5 .   ? -23.961 -0.839  4.027   1.00 16.76 ? 553 HOH   A O   1 
HETATM 2347 O  O   . HOH   F 5 .   ? -28.364 5.632   19.119  1.00 30.42 ? 554 HOH   A O   1 
HETATM 2348 O  O   . HOH   F 5 .   ? -11.155 17.541  12.388  1.00 24.06 ? 555 HOH   A O   1 
HETATM 2349 O  O   . HOH   F 5 .   ? 4.228   -6.438  7.879   1.00 19.09 ? 556 HOH   A O   1 
HETATM 2350 O  O   . HOH   F 5 .   ? -15.071 -16.036 25.110  1.00 36.90 ? 557 HOH   A O   1 
HETATM 2351 O  O   . HOH   F 5 .   ? 1.371   -6.378  34.516  1.00 23.38 ? 558 HOH   A O   1 
HETATM 2352 O  O   . HOH   F 5 .   ? -0.218  -14.244 22.185  1.00 18.53 ? 559 HOH   A O   1 
HETATM 2353 O  O   . HOH   F 5 .   ? -13.900 14.620  6.576   1.00 34.75 ? 560 HOH   A O   1 
HETATM 2354 O  O   . HOH   F 5 .   ? 1.186   -1.569  29.514  1.00 14.28 ? 561 HOH   A O   1 
HETATM 2355 O  O   . HOH   F 5 .   ? -10.204 13.854  8.619   1.00 37.08 ? 562 HOH   A O   1 
HETATM 2356 O  O   . HOH   F 5 .   ? -24.029 -0.582  26.511  1.00 20.24 ? 563 HOH   A O   1 
HETATM 2357 O  O   . HOH   F 5 .   ? -20.540 13.628  28.784  1.00 39.02 ? 564 HOH   A O   1 
HETATM 2358 O  O   . HOH   F 5 .   ? -24.868 12.226  6.327   1.00 31.28 ? 565 HOH   A O   1 
HETATM 2359 O  O   . HOH   F 5 .   ? -8.086  21.758  19.700  0.50 15.97 ? 566 HOH   A O   1 
HETATM 2360 O  O   . HOH   F 5 .   ? -17.917 20.625  8.115   1.00 13.17 ? 567 HOH   A O   1 
HETATM 2361 O  O   . HOH   F 5 .   ? -2.085  -12.315 22.893  1.00 10.65 ? 568 HOH   A O   1 
HETATM 2362 O  O   . HOH   F 5 .   ? -7.444  1.286   35.063  1.00 28.16 ? 569 HOH   A O   1 
HETATM 2363 O  O   . HOH   F 5 .   ? -23.030 -11.684 14.055  1.00 18.30 ? 570 HOH   A O   1 
HETATM 2364 O  O   . HOH   F 5 .   ? -9.904  14.735  12.153  1.00 19.11 ? 571 HOH   A O   1 
HETATM 2365 O  O   . HOH   F 5 .   ? 4.904   -7.445  22.280  1.00 20.76 ? 572 HOH   A O   1 
HETATM 2366 O  O   . HOH   F 5 .   ? 6.890   -1.291  -7.243  1.00 28.72 ? 573 HOH   A O   1 
HETATM 2367 O  O   . HOH   F 5 .   ? -5.606  3.367   -5.807  1.00 31.89 ? 574 HOH   A O   1 
HETATM 2368 O  O   . HOH   F 5 .   ? 6.612   -5.668  6.656   1.00 33.35 ? 575 HOH   A O   1 
HETATM 2369 O  O   . HOH   F 5 .   ? -25.909 -6.573  33.869  1.00 36.42 ? 576 HOH   A O   1 
HETATM 2370 O  O   . HOH   F 5 .   ? -1.405  4.702   37.243  1.00 32.50 ? 577 HOH   A O   1 
HETATM 2371 O  O   . HOH   F 5 .   ? -7.401  -8.495  -2.245  1.00 22.26 ? 578 HOH   A O   1 
HETATM 2372 O  O   . HOH   F 5 .   ? 7.568   6.060   21.739  1.00 14.71 ? 579 HOH   A O   1 
HETATM 2373 O  O   . HOH   F 5 .   ? -9.592  -8.031  34.145  1.00 21.23 ? 580 HOH   A O   1 
HETATM 2374 O  O   . HOH   F 5 .   ? -5.915  15.341  11.966  1.00 28.95 ? 581 HOH   A O   1 
HETATM 2375 O  O   . HOH   F 5 .   ? -25.450 -9.862  15.246  1.00 30.75 ? 582 HOH   A O   1 
HETATM 2376 O  O   . HOH   F 5 .   ? -4.194  4.766   7.012   1.00 23.47 ? 583 HOH   A O   1 
HETATM 2377 O  O   . HOH   F 5 .   ? -8.433  -19.923 26.491  1.00 28.09 ? 584 HOH   A O   1 
HETATM 2378 O  O   . HOH   F 5 .   ? -24.769 -9.579  1.954   1.00 22.24 ? 585 HOH   A O   1 
HETATM 2379 O  O   . HOH   F 5 .   ? -30.925 -7.064  22.475  1.00 26.48 ? 586 HOH   A O   1 
HETATM 2380 O  O   . HOH   F 5 .   ? -23.670 8.326   3.567   1.00 18.72 ? 587 HOH   A O   1 
HETATM 2381 O  O   . HOH   F 5 .   ? -8.528  9.355   -2.702  1.00 34.25 ? 588 HOH   A O   1 
HETATM 2382 O  O   . HOH   F 5 .   ? -5.614  -12.239 -5.040  1.00 33.62 ? 589 HOH   A O   1 
HETATM 2383 O  O   . HOH   F 5 .   ? -17.674 19.992  17.522  1.00 27.73 ? 590 HOH   A O   1 
HETATM 2384 O  O   . HOH   F 5 .   ? -6.081  8.524   5.457   1.00 28.96 ? 591 HOH   A O   1 
HETATM 2385 O  O   . HOH   F 5 .   ? -22.715 -21.316 12.207  1.00 28.27 ? 592 HOH   A O   1 
HETATM 2386 O  O   . HOH   F 5 .   ? -1.454  11.463  26.189  1.00 24.64 ? 593 HOH   A O   1 
HETATM 2387 O  O   . HOH   F 5 .   ? -12.839 -17.267 16.884  1.00 14.71 ? 594 HOH   A O   1 
HETATM 2388 O  O   . HOH   F 5 .   ? -6.672  -20.125 24.002  1.00 32.78 ? 595 HOH   A O   1 
HETATM 2389 O  O   . HOH   F 5 .   ? -8.415  -17.421 34.962  1.00 33.67 ? 596 HOH   A O   1 
HETATM 2390 O  O   . HOH   F 5 .   ? -18.279 -9.007  34.611  1.00 37.97 ? 597 HOH   A O   1 
HETATM 2391 O  O   . HOH   F 5 .   ? 0.337   0.862   -6.704  1.00 23.92 ? 598 HOH   A O   1 
HETATM 2392 O  O   . HOH   F 5 .   ? -18.762 -20.731 -1.256  1.00 32.81 ? 599 HOH   A O   1 
HETATM 2393 O  O   . HOH   F 5 .   ? -25.611 4.551   4.346   1.00 40.83 ? 600 HOH   A O   1 
HETATM 2394 O  O   . HOH   F 5 .   ? 6.677   0.886   -5.263  1.00 31.78 ? 601 HOH   A O   1 
HETATM 2395 O  O   . HOH   F 5 .   ? -21.145 21.648  6.696   1.00 23.81 ? 602 HOH   A O   1 
HETATM 2396 O  O   . HOH   F 5 .   ? -16.678 -18.149 20.351  1.00 38.61 ? 603 HOH   A O   1 
HETATM 2397 O  O   . HOH   F 5 .   ? -10.513 4.920   30.900  1.00 29.48 ? 604 HOH   A O   1 
HETATM 2398 O  O   . HOH   F 5 .   ? 0.946   3.410   2.033   1.00 38.81 ? 605 HOH   A O   1 
HETATM 2399 O  O   . HOH   F 5 .   ? 5.852   -9.666  20.964  1.00 30.37 ? 606 HOH   A O   1 
HETATM 2400 O  O   . HOH   F 5 .   ? -16.956 -14.102 26.277  1.00 26.89 ? 607 HOH   A O   1 
HETATM 2401 O  O   . HOH   F 5 .   ? -1.842  -17.400 25.674  1.00 30.61 ? 608 HOH   A O   1 
HETATM 2402 O  O   . HOH   F 5 .   ? -23.985 -7.255  0.316   1.00 33.14 ? 609 HOH   A O   1 
HETATM 2403 O  O   . HOH   F 5 .   ? -15.921 16.983  26.763  1.00 40.94 ? 610 HOH   A O   1 
HETATM 2404 O  O   . HOH   F 5 .   ? -29.214 -5.800  24.527  1.00 24.21 ? 611 HOH   A O   1 
HETATM 2405 O  O   . HOH   F 5 .   ? -27.133 -6.384  11.795  1.00 31.30 ? 612 HOH   A O   1 
HETATM 2406 O  O   . HOH   F 5 .   ? 6.330   -4.910  27.890  1.00 40.34 ? 613 HOH   A O   1 
HETATM 2407 O  O   . HOH   F 5 .   ? -19.389 20.460  5.029   1.00 19.77 ? 614 HOH   A O   1 
HETATM 2408 O  O   . HOH   F 5 .   ? 1.791   12.351  22.556  1.00 33.57 ? 615 HOH   A O   1 
HETATM 2409 O  O   . HOH   F 5 .   ? -11.209 -11.050 -2.735  1.00 30.02 ? 616 HOH   A O   1 
HETATM 2410 O  O   . HOH   F 5 .   ? -13.554 -21.262 15.038  1.00 18.82 ? 617 HOH   A O   1 
HETATM 2411 O  O   . HOH   F 5 .   ? 1.961   -14.064 20.528  1.00 24.80 ? 618 HOH   A O   1 
HETATM 2412 O  O   . HOH   F 5 .   ? -11.842 10.852  0.886   1.00 26.87 ? 619 HOH   A O   1 
HETATM 2413 O  O   . HOH   F 5 .   ? 0.638   3.309   -5.277  1.00 34.28 ? 620 HOH   A O   1 
HETATM 2414 O  O   . HOH   F 5 .   ? -12.957 13.282  31.858  1.00 26.81 ? 621 HOH   A O   1 
HETATM 2415 O  O   . HOH   F 5 .   ? -11.135 15.317  32.277  1.00 19.23 ? 622 HOH   A O   1 
HETATM 2416 O  O   . HOH   F 5 .   ? -7.251  -10.025 -4.705  1.00 30.23 ? 623 HOH   A O   1 
HETATM 2417 O  O   . HOH   F 5 .   ? -17.957 -12.070 31.518  1.00 29.15 ? 624 HOH   A O   1 
HETATM 2418 O  O   . HOH   F 5 .   ? -9.199  5.330   32.905  1.00 29.26 ? 625 HOH   A O   1 
HETATM 2419 O  O   . HOH   F 5 .   ? -16.546 -14.967 28.652  1.00 35.93 ? 626 HOH   A O   1 
HETATM 2420 O  O   . HOH   F 5 .   ? -3.768  -15.583 -1.994  1.00 26.59 ? 627 HOH   A O   1 
HETATM 2421 O  O   . HOH   F 5 .   ? -2.379  6.335   1.048   1.00 25.61 ? 628 HOH   A O   1 
HETATM 2422 O  O   . HOH   F 5 .   ? 6.564   8.277   17.946  1.00 31.69 ? 629 HOH   A O   1 
HETATM 2423 O  O   . HOH   F 5 .   ? -2.355  7.469   -5.258  1.00 16.51 ? 630 HOH   A O   1 
HETATM 2424 O  O   . HOH   F 5 .   ? -12.808 -19.625 26.313  1.00 28.33 ? 631 HOH   A O   1 
HETATM 2425 O  O   . HOH   F 5 .   ? -34.152 -9.365  16.500  1.00 20.43 ? 632 HOH   A O   1 
HETATM 2426 O  O   . HOH   F 5 .   ? 5.388   9.047   22.096  1.00 28.07 ? 633 HOH   A O   1 
HETATM 2427 O  O   . HOH   F 5 .   ? -7.349  -24.522 10.629  1.00 30.77 ? 634 HOH   A O   1 
HETATM 2428 O  O   . HOH   F 5 .   ? 3.627   9.884   23.874  1.00 27.71 ? 635 HOH   A O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N  N   . HIS   A 4   ? 0.4439 0.4004 0.4038 -0.0646 0.1434  0.0893  4   HIS   A N   
2    C  CA  . HIS   A 4   ? 0.2989 0.3340 0.3518 -0.0874 0.1514  0.0350  4   HIS   A CA  
3    C  C   . HIS   A 4   ? 0.2087 0.2291 0.2418 -0.0398 0.0875  0.0034  4   HIS   A C   
4    O  O   . HIS   A 4   ? 0.2245 0.2514 0.2383 -0.0051 0.0947  -0.0185 4   HIS   A O   
5    C  CB  . HIS   A 4   ? 0.2812 0.3501 0.3012 -0.0812 0.1351  0.0110  4   HIS   A CB  
6    N  N   . TRP   A 5   ? 0.1688 0.1927 0.2166 -0.0382 0.0595  -0.0143 5   TRP   A N   
7    C  CA  . TRP   A 5   ? 0.1346 0.1725 0.1834 -0.0318 0.0346  -0.0120 5   TRP   A CA  
8    C  C   . TRP   A 5   ? 0.1376 0.1700 0.1579 -0.0082 0.0218  -0.0040 5   TRP   A C   
9    O  O   . TRP   A 5   ? 0.1622 0.1796 0.1683 -0.0245 0.0260  -0.0036 5   TRP   A O   
10   C  CB  . TRP   A 5   ? 0.1328 0.1586 0.1662 -0.0318 0.0232  -0.0125 5   TRP   A CB  
11   C  CG  . TRP   A 5   ? 0.1489 0.1480 0.1487 -0.0153 0.0236  -0.0018 5   TRP   A CG  
12   C  CD1 . TRP   A 5   ? 0.1733 0.1689 0.1534 -0.0188 0.0402  0.0145  5   TRP   A CD1 
13   C  CD2 . TRP   A 5   ? 0.1391 0.1503 0.1263 -0.0006 0.0208  -0.0069 5   TRP   A CD2 
14   N  NE1 . TRP   A 5   ? 0.1979 0.1664 0.1561 -0.0006 0.0254  0.0166  5   TRP   A NE1 
15   C  CE2 . TRP   A 5   ? 0.1637 0.1734 0.1259 0.0014  0.0147  0.0089  5   TRP   A CE2 
16   C  CE3 . TRP   A 5   ? 0.1314 0.1483 0.1240 -0.0085 0.0198  -0.0166 5   TRP   A CE3 
17   C  CZ2 . TRP   A 5   ? 0.1764 0.1991 0.1236 0.0241  0.0031  -0.0038 5   TRP   A CZ2 
18   C  CZ3 . TRP   A 5   ? 0.1321 0.1671 0.1310 -0.0147 0.0172  -0.0264 5   TRP   A CZ3 
19   C  CH2 . TRP   A 5   ? 0.1473 0.1984 0.1234 0.0006  0.0046  -0.0306 5   TRP   A CH2 
20   N  N   . GLY   A 6   ? 0.1210 0.1573 0.1459 -0.0101 0.0144  -0.0158 6   GLY   A N   
21   C  CA  . GLY   A 6   ? 0.1309 0.1484 0.1424 -0.0059 0.0098  -0.0222 6   GLY   A CA  
22   C  C   . GLY   A 6   ? 0.1239 0.1519 0.1278 0.0033  0.0102  -0.0180 6   GLY   A C   
23   O  O   . GLY   A 6   ? 0.1180 0.1653 0.1316 -0.0103 0.0085  -0.0222 6   GLY   A O   
24   N  N   . TYR   A 7   ? 0.1193 0.1500 0.1381 -0.0063 0.0247  -0.0208 7   TYR   A N   
25   C  CA  . TYR   A 7   ? 0.1280 0.1466 0.1639 -0.0008 0.0187  -0.0175 7   TYR   A CA  
26   C  C   . TYR   A 7   ? 0.1472 0.1593 0.2255 0.0105  0.0424  -0.0259 7   TYR   A C   
27   O  O   . TYR   A 7   ? 0.1588 0.1751 0.3136 0.0090  0.0596  0.0060  7   TYR   A O   
28   C  CB  . TYR   A 7   ? 0.1219 0.1410 0.1535 -0.0088 0.0140  -0.0254 7   TYR   A CB  
29   C  CG  . TYR   A 7   ? 0.1117 0.1257 0.1265 -0.0168 0.0047  -0.0137 7   TYR   A CG  
30   C  CD1 . TYR   A 7   ? 0.1070 0.1253 0.1271 -0.0107 0.0004  -0.0076 7   TYR   A CD1 
31   C  CD2 . TYR   A 7   ? 0.1301 0.1253 0.1166 -0.0235 0.0093  -0.0168 7   TYR   A CD2 
32   C  CE1 . TYR   A 7   ? 0.1096 0.1136 0.1159 -0.0126 -0.0026 -0.0075 7   TYR   A CE1 
33   C  CE2 . TYR   A 7   ? 0.1190 0.1275 0.1232 -0.0169 0.0014  -0.0014 7   TYR   A CE2 
34   C  CZ  . TYR   A 7   ? 0.1135 0.1191 0.1139 -0.0065 -0.0024 -0.0124 7   TYR   A CZ  
35   O  OH  . TYR   A 7   ? 0.1417 0.1161 0.1260 -0.0007 0.0062  -0.0089 7   TYR   A OH  
36   N  N   . GLY   A 8   ? 0.1597 0.1987 0.2411 0.0035  0.0564  -0.0510 8   GLY   A N   
37   C  CA  . GLY   A 8   ? 0.2010 0.2198 0.2617 0.0411  0.0588  -0.0347 8   GLY   A CA  
38   C  C   . GLY   A 8   ? 0.1941 0.2204 0.3097 0.0445  0.0308  -0.0430 8   GLY   A C   
39   O  O   . GLY   A 8   ? 0.2037 0.2913 0.2758 0.0236  0.0652  -0.0215 8   GLY   A O   
40   N  N   . LYS   A 9   ? 0.2154 0.2286 0.3948 0.0619  0.0333  -0.0165 9   LYS   A N   
41   C  CA  . LYS   A 9   ? 0.2413 0.2734 0.3926 0.0528  0.0077  -0.0036 9   LYS   A CA  
42   C  C   . LYS   A 9   ? 0.2098 0.3256 0.2997 0.0370  0.0512  0.0068  9   LYS   A C   
43   O  O   . LYS   A 9   ? 0.2235 0.2777 0.2985 -0.0010 0.0256  0.0075  9   LYS   A O   
44   C  CB  . LYS   A 9   ? 0.2729 0.2713 0.4106 0.0880  -0.0164 0.0294  9   LYS   A CB  
45   N  N   . HIS   A 10  ? 0.1948 0.2533 0.2756 0.0480  0.0668  0.0013  10  HIS   A N   
46   C  CA  . HIS   A 10  ? 0.1820 0.2796 0.2923 0.0394  0.0817  -0.0310 10  HIS   A CA  
47   C  C   . HIS   A 10  ? 0.1587 0.2357 0.2470 0.0158  0.0721  -0.0078 10  HIS   A C   
48   O  O   . HIS   A 10  ? 0.1480 0.2955 0.3204 0.0185  0.0353  -0.0365 10  HIS   A O   
49   C  CB  . HIS   A 10  ? 0.2029 0.2820 0.3109 0.0241  0.1143  -0.0349 10  HIS   A CB  
50   C  CG  . HIS   A 10  ? 0.2774 0.2931 0.3821 0.0126  0.1407  -0.0249 10  HIS   A CG  
51   N  ND1 . HIS   A 10  ? 0.3479 0.2773 0.4289 0.0670  0.1381  0.0088  10  HIS   A ND1 
52   C  CD2 . HIS   A 10  ? 0.3394 0.3231 0.4458 0.0461  0.1422  -0.0284 10  HIS   A CD2 
53   C  CE1 . HIS   A 10  ? 0.2969 0.2250 0.4358 0.0440  0.1537  0.0497  10  HIS   A CE1 
54   N  NE2 . HIS   A 10  ? 0.3705 0.3036 0.4613 0.0471  0.1454  -0.0055 10  HIS   A NE2 
55   N  N   . ASN   A 11  ? 0.1503 0.2210 0.2192 0.0135  0.0514  -0.0119 11  ASN   A N   
56   C  CA  . ASN   A 11  ? 0.1341 0.2107 0.1904 0.0004  0.0388  -0.0256 11  ASN   A CA  
57   C  C   . ASN   A 11  ? 0.1226 0.1950 0.1689 0.0035  0.0195  -0.0213 11  ASN   A C   
58   O  O   . ASN   A 11  ? 0.1331 0.1913 0.1581 -0.0028 0.0298  -0.0164 11  ASN   A O   
59   C  CB  . ASN   A 11  ? 0.1391 0.2397 0.1925 0.0032  0.0475  -0.0127 11  ASN   A CB  
60   C  CG  . ASN   A 11  ? 0.1728 0.2525 0.1597 0.0010  0.0579  -0.0186 11  ASN   A CG  
61   O  OD1 . ASN   A 11  ? 0.1988 0.2673 0.1807 -0.0243 0.0310  -0.0250 11  ASN   A OD1 
62   N  ND2 . ASN   A 11  ? 0.1940 0.2681 0.2064 -0.0187 0.0443  0.0077  11  ASN   A ND2 
63   N  N   . GLY   A 12  ? 0.1183 0.2074 0.1702 0.0162  0.0242  -0.0216 12  GLY   A N   
64   C  CA  . GLY   A 12  ? 0.1254 0.1937 0.1538 0.0092  0.0219  -0.0221 12  GLY   A CA  
65   C  C   . GLY   A 12  ? 0.1268 0.1504 0.1459 0.0000  0.0132  -0.0074 12  GLY   A C   
66   O  O   . GLY   A 12  ? 0.1178 0.1640 0.1534 -0.0022 0.0082  -0.0049 12  GLY   A O   
67   N  N   . PRO   A 13  ? 0.1188 0.1498 0.1362 -0.0066 0.0173  -0.0112 13  PRO   A N   
68   C  CA  . PRO   A 13  ? 0.1262 0.1388 0.1546 -0.0025 0.0222  -0.0218 13  PRO   A CA  
69   C  C   . PRO   A 13  ? 0.1358 0.1275 0.1380 -0.0058 0.0178  -0.0045 13  PRO   A C   
70   O  O   . PRO   A 13  ? 0.1126 0.1542 0.1586 -0.0112 0.0096  -0.0220 13  PRO   A O   
71   C  CB  . PRO   A 13  ? 0.1330 0.1462 0.1573 -0.0101 0.0282  -0.0146 13  PRO   A CB  
72   C  CG  . PRO   A 13  ? 0.1398 0.1568 0.1576 -0.0171 0.0249  -0.0143 13  PRO   A CG  
73   C  CD  . PRO   A 13  ? 0.1349 0.1601 0.1615 -0.0116 0.0229  -0.0281 13  PRO   A CD  
74   N  N   . GLU   A 14  ? 0.1509 0.1369 0.1547 0.0009  0.0002  0.0041  14  GLU   A N   
75   C  CA  . GLU   A 14  ? 0.1664 0.1532 0.1744 0.0134  -0.0085 0.0241  14  GLU   A CA  
76   C  C   . GLU   A 14  ? 0.1251 0.1428 0.1784 0.0195  -0.0070 -0.0064 14  GLU   A C   
77   O  O   . GLU   A 14  ? 0.1668 0.1788 0.1848 0.0191  -0.0324 0.0128  14  GLU   A O   
78   C  CB  . GLU   A 14  ? 0.2167 0.1719 0.2588 0.0110  -0.0364 0.0406  14  GLU   A CB  
79   C  CG  . GLU   A 14  ? 0.3106 0.2020 0.3311 -0.0263 -0.0098 0.0363  14  GLU   A CG  
80   N  N   . HIS   A 15  ? 0.1142 0.1403 0.1632 0.0193  -0.0086 -0.0022 15  HIS   A N   
81   C  CA  . HIS   A 15  ? 0.1030 0.1411 0.1639 0.0094  -0.0017 -0.0079 15  HIS   A CA  
82   C  C   . HIS   A 15  ? 0.0988 0.1345 0.1434 0.0074  0.0079  -0.0057 15  HIS   A C   
83   O  O   . HIS   A 15  ? 0.0904 0.1468 0.1599 0.0045  0.0078  -0.0083 15  HIS   A O   
84   C  CB  . HIS   A 15  ? 0.1002 0.1514 0.1792 0.0229  -0.0025 -0.0180 15  HIS   A CB  
85   C  CG  . HIS   A 15  ? 0.1286 0.1699 0.2084 0.0339  0.0047  -0.0223 15  HIS   A CG  
86   N  ND1 . HIS   A 15  ? 0.1359 0.2306 0.2284 0.0525  0.0041  -0.0536 15  HIS   A ND1 
87   C  CD2 . HIS   A 15  ? 0.1659 0.1731 0.2564 0.0450  -0.0136 -0.0364 15  HIS   A CD2 
88   C  CE1 . HIS   A 15  ? 0.1861 0.2451 0.2843 0.0708  -0.0128 -0.0884 15  HIS   A CE1 
89   N  NE2 . HIS   A 15  ? 0.1862 0.2010 0.3004 0.0635  0.0024  -0.0665 15  HIS   A NE2 
90   N  N   . TRP   A 16  ? 0.0925 0.1283 0.1475 0.0061  0.0029  -0.0070 16  TRP   A N   
91   C  CA  . TRP   A 16  ? 0.0816 0.1302 0.1370 0.0074  0.0079  -0.0048 16  TRP   A CA  
92   C  C   . TRP   A 16  ? 0.0801 0.1273 0.1490 0.0047  0.0063  -0.0013 16  TRP   A C   
93   O  O   . TRP   A 16  ? 0.0922 0.1278 0.1500 -0.0024 -0.0076 -0.0013 16  TRP   A O   
94   C  CB  . TRP   A 16  ? 0.0770 0.1308 0.1392 0.0030  0.0072  -0.0126 16  TRP   A CB  
95   C  CG  . TRP   A 16  ? 0.0846 0.1270 0.1181 -0.0003 0.0042  -0.0086 16  TRP   A CG  
96   C  CD1 . TRP   A 16  ? 0.0941 0.1475 0.1264 -0.0040 0.0084  -0.0168 16  TRP   A CD1 
97   C  CD2 . TRP   A 16  ? 0.0898 0.1070 0.1207 0.0006  0.0080  -0.0067 16  TRP   A CD2 
98   N  NE1 . TRP   A 16  ? 0.0937 0.1559 0.1202 -0.0003 0.0125  -0.0242 16  TRP   A NE1 
99   C  CE2 . TRP   A 16  ? 0.0939 0.1203 0.1217 -0.0022 0.0041  -0.0068 16  TRP   A CE2 
100  C  CE3 . TRP   A 16  ? 0.0960 0.1102 0.1239 0.0036  0.0054  -0.0101 16  TRP   A CE3 
101  C  CZ2 . TRP   A 16  ? 0.0990 0.1259 0.1189 -0.0109 0.0040  -0.0122 16  TRP   A CZ2 
102  C  CZ3 . TRP   A 16  ? 0.0940 0.1250 0.1236 -0.0048 0.0161  -0.0079 16  TRP   A CZ3 
103  C  CH2 . TRP   A 16  ? 0.0914 0.1261 0.1232 0.0008  0.0069  -0.0021 16  TRP   A CH2 
104  N  N   . HIS   A 17  ? 0.0849 0.1345 0.1362 -0.0034 0.0063  -0.0041 17  HIS   A N   
105  C  CA  . HIS   A 17  ? 0.0902 0.1470 0.1453 0.0055  -0.0042 -0.0061 17  HIS   A CA  
106  C  C   . HIS   A 17  ? 0.0976 0.1616 0.1355 -0.0033 -0.0057 -0.0104 17  HIS   A C   
107  O  O   . HIS   A 17  ? 0.0988 0.1705 0.1575 -0.0138 -0.0041 -0.0244 17  HIS   A O   
108  C  CB  . HIS   A 17  ? 0.1081 0.1573 0.1432 0.0097  -0.0023 -0.0068 17  HIS   A CB  
109  C  CG  . HIS   A 17  ? 0.1088 0.1705 0.1514 0.0109  -0.0109 0.0133  17  HIS   A CG  
110  N  ND1 . HIS   A 17  ? 0.1204 0.2226 0.1683 0.0156  -0.0123 0.0046  17  HIS   A ND1 
111  C  CD2 . HIS   A 17  ? 0.1282 0.1713 0.1825 0.0243  -0.0019 0.0109  17  HIS   A CD2 
112  C  CE1 . HIS   A 17  ? 0.1259 0.2373 0.1712 0.0336  -0.0008 0.0107  17  HIS   A CE1 
113  N  NE2 . HIS   A 17  ? 0.1430 0.1974 0.1907 0.0422  0.0038  0.0262  17  HIS   A NE2 
114  N  N   . LYS   A 18  ? 0.0828 0.1496 0.1499 -0.0094 -0.0029 -0.0053 18  LYS   A N   
115  C  CA  . LYS   A 18  ? 0.0823 0.1835 0.1603 -0.0070 0.0015  -0.0030 18  LYS   A CA  
116  C  C   . LYS   A 18  ? 0.1061 0.1748 0.1735 -0.0232 0.0000  -0.0027 18  LYS   A C   
117  O  O   . LYS   A 18  ? 0.1465 0.1954 0.2674 -0.0474 -0.0457 0.0279  18  LYS   A O   
118  C  CB  . LYS   A 18  ? 0.0915 0.1855 0.1642 0.0119  0.0000  0.0016  18  LYS   A CB  
119  C  CG  . LYS   A 18  ? 0.1101 0.2036 0.1663 0.0295  0.0065  0.0128  18  LYS   A CG  
120  C  CD  . LYS   A 18  ? 0.1082 0.2053 0.1637 0.0278  0.0133  0.0170  18  LYS   A CD  
121  C  CE  . LYS   A 18  ? 0.1226 0.1937 0.1728 0.0314  0.0176  0.0157  18  LYS   A CE  
122  N  NZ  . LYS   A 18  ? 0.1005 0.2081 0.1811 0.0397  0.0044  0.0172  18  LYS   A NZ  
123  N  N   . ASP   A 19  ? 0.1004 0.1641 0.1619 -0.0091 0.0006  0.0055  19  ASP   A N   
124  C  CA  . ASP   A 19  ? 0.1083 0.1636 0.1772 -0.0054 0.0138  0.0116  19  ASP   A CA  
125  C  C   . ASP   A 19  ? 0.1025 0.1421 0.1865 -0.0098 0.0142  0.0038  19  ASP   A C   
126  O  O   . ASP   A 19  ? 0.1383 0.1429 0.2149 -0.0191 0.0315  0.0078  19  ASP   A O   
127  C  CB  . ASP   A 19  ? 0.1351 0.1988 0.1843 0.0114  0.0102  0.0211  19  ASP   A CB  
128  C  CG  . ASP   A 19  ? 0.1864 0.2017 0.2340 -0.0058 0.0410  0.0086  19  ASP   A CG  
129  O  OD1 . ASP   A 19  ? 0.1991 0.2552 0.2566 -0.0107 0.0398  0.0231  19  ASP   A OD1 
130  O  OD2 . ASP   A 19  ? 0.2423 0.2656 0.2986 0.0335  0.0516  -0.0090 19  ASP   A OD2 
131  N  N   . PHE   A 20  ? 0.0932 0.1287 0.1656 -0.0086 0.0056  -0.0032 20  PHE   A N   
132  C  CA  . PHE   A 20  ? 0.0932 0.1271 0.1660 -0.0106 0.0089  -0.0102 20  PHE   A CA  
133  C  C   . PHE   A 20  ? 0.1031 0.1421 0.1584 -0.0129 0.0142  -0.0188 20  PHE   A C   
134  O  O   . PHE   A 20  ? 0.1083 0.1401 0.1539 -0.0124 0.0075  -0.0109 20  PHE   A O   
135  C  CB  . PHE   A 20  ? 0.0967 0.1419 0.1605 -0.0089 0.0171  -0.0065 20  PHE   A CB  
136  C  CG  . PHE   A 20  ? 0.0929 0.1517 0.1661 -0.0051 0.0028  0.0045  20  PHE   A CG  
137  C  CD1 . PHE   A 20  ? 0.1278 0.1661 0.1813 -0.0165 0.0006  0.0100  20  PHE   A CD1 
138  C  CD2 . PHE   A 20  ? 0.1024 0.1673 0.1654 -0.0158 0.0007  0.0063  20  PHE   A CD2 
139  C  CE1 . PHE   A 20  ? 0.1285 0.1744 0.1957 -0.0087 -0.0032 0.0308  20  PHE   A CE1 
140  C  CE2 . PHE   A 20  ? 0.1062 0.2029 0.1732 -0.0095 0.0067  -0.0056 20  PHE   A CE2 
141  C  CZ  . PHE   A 20  ? 0.1127 0.2052 0.1832 -0.0217 0.0052  0.0195  20  PHE   A CZ  
142  N  N   . PRO   A 21  ? 0.1084 0.1463 0.1700 -0.0206 0.0052  -0.0187 21  PRO   A N   
143  C  CA  . PRO   A 21  ? 0.0987 0.1678 0.1708 -0.0135 0.0021  -0.0168 21  PRO   A CA  
144  C  C   . PRO   A 21  ? 0.1098 0.1459 0.1531 -0.0133 -0.0177 -0.0146 21  PRO   A C   
145  O  O   . PRO   A 21  ? 0.1048 0.1769 0.1610 -0.0004 -0.0140 -0.0079 21  PRO   A O   
146  C  CB  . PRO   A 21  ? 0.1189 0.2337 0.2027 -0.0348 -0.0148 -0.0177 21  PRO   A CB  
147  C  CG  . PRO   A 21  ? 0.1789 0.2219 0.2633 -0.0537 -0.0210 -0.0321 21  PRO   A CG  
148  C  CD  . PRO   A 21  ? 0.1257 0.1768 0.2127 -0.0343 -0.0117 -0.0071 21  PRO   A CD  
149  N  N   . ILE   A 22  ? 0.1055 0.1317 0.1545 -0.0175 -0.0008 -0.0211 22  ILE   A N   
150  C  CA  . ILE   A 22  ? 0.0981 0.1351 0.1431 -0.0089 0.0005  -0.0210 22  ILE   A CA  
151  C  C   . ILE   A 22  ? 0.0969 0.1451 0.1365 -0.0080 -0.0018 -0.0209 22  ILE   A C   
152  O  O   . ILE   A 22  ? 0.0982 0.1541 0.1495 -0.0111 0.0083  -0.0187 22  ILE   A O   
153  C  CB  . ILE   A 22  ? 0.1134 0.1411 0.1581 -0.0133 0.0003  -0.0254 22  ILE   A CB  
154  C  CG1 A ILE   A 22  ? 0.1127 0.1377 0.1672 -0.0087 0.0019  -0.0356 22  ILE   A CG1 
155  C  CG1 B ILE   A 22  ? 0.1243 0.1602 0.1836 -0.0077 0.0088  -0.0276 22  ILE   A CG1 
156  C  CG2 . ILE   A 22  ? 0.1047 0.1559 0.1622 -0.0136 -0.0187 -0.0148 22  ILE   A CG2 
157  C  CD1 A ILE   A 22  ? 0.1202 0.1345 0.1645 -0.0079 0.0045  -0.0408 22  ILE   A CD1 
158  C  CD1 B ILE   A 22  ? 0.1642 0.1960 0.1973 -0.0166 0.0071  -0.0264 22  ILE   A CD1 
159  N  N   . ALA   A 23  ? 0.1086 0.1337 0.1404 -0.0150 0.0043  -0.0211 23  ALA   A N   
160  C  CA  . ALA   A 23  ? 0.0964 0.1279 0.1477 -0.0012 -0.0016 -0.0169 23  ALA   A CA  
161  C  C   . ALA   A 23  ? 0.1069 0.1360 0.1512 -0.0025 -0.0033 -0.0191 23  ALA   A C   
162  O  O   . ALA   A 23  ? 0.1135 0.1516 0.1628 -0.0075 -0.0039 -0.0049 23  ALA   A O   
163  C  CB  . ALA   A 23  ? 0.0926 0.1449 0.1531 -0.0055 -0.0024 -0.0206 23  ALA   A CB  
164  N  N   . LYS   A 24  ? 0.1175 0.1589 0.1498 -0.0049 -0.0067 -0.0057 24  LYS   A N   
165  C  CA  . LYS   A 24  ? 0.1204 0.1842 0.1531 -0.0005 -0.0040 -0.0045 24  LYS   A CA  
166  C  C   . LYS   A 24  ? 0.1389 0.2174 0.1395 -0.0001 -0.0170 -0.0089 24  LYS   A C   
167  O  O   . LYS   A 24  ? 0.1409 0.2573 0.1700 0.0038  -0.0146 0.0030  24  LYS   A O   
168  C  CB  . LYS   A 24  ? 0.1404 0.2135 0.1903 0.0241  -0.0172 0.0086  24  LYS   A CB  
169  C  CG  . LYS   A 24  ? 0.1575 0.2632 0.1982 0.0451  -0.0009 0.0098  24  LYS   A CG  
170  C  CD  . LYS   A 24  ? 0.1686 0.3153 0.2584 0.0537  0.0130  0.0214  24  LYS   A CD  
171  C  CE  A LYS   A 24  ? 0.2076 0.3422 0.2790 0.0539  0.0216  0.0146  24  LYS   A CE  
172  C  CE  B LYS   A 24  ? 0.1926 0.3477 0.2783 0.0688  0.0162  0.0129  24  LYS   A CE  
173  N  NZ  A LYS   A 24  ? 0.2377 0.3544 0.3160 0.0593  0.0036  0.0190  24  LYS   A NZ  
174  N  NZ  B LYS   A 24  ? 0.2296 0.3487 0.3075 0.0669  0.0087  0.0077  24  LYS   A NZ  
175  N  N   . GLY   A 25  ? 0.1340 0.1927 0.1435 -0.0023 -0.0037 -0.0174 25  GLY   A N   
176  C  CA  . GLY   A 25  ? 0.1394 0.2019 0.1621 -0.0114 0.0007  -0.0242 25  GLY   A CA  
177  C  C   . GLY   A 25  ? 0.1348 0.1930 0.1348 0.0007  -0.0083 -0.0254 25  GLY   A C   
178  O  O   . GLY   A 25  ? 0.1475 0.2005 0.1480 -0.0033 -0.0042 -0.0108 25  GLY   A O   
179  N  N   . GLU   A 26  ? 0.1261 0.2020 0.1339 -0.0041 -0.0138 -0.0346 26  GLU   A N   
180  C  CA  . GLU   A 26  ? 0.1415 0.2257 0.1265 -0.0061 -0.0110 -0.0314 26  GLU   A CA  
181  C  C   . GLU   A 26  ? 0.1348 0.1789 0.1407 -0.0070 0.0057  -0.0117 26  GLU   A C   
182  O  O   . GLU   A 26  ? 0.1601 0.2141 0.1125 -0.0158 -0.0100 -0.0017 26  GLU   A O   
183  C  CB  . GLU   A 26  ? 0.1777 0.2696 0.1430 -0.0223 -0.0174 -0.0655 26  GLU   A CB  
184  C  CG  . GLU   A 26  ? 0.2119 0.3199 0.1851 -0.0420 -0.0261 -0.0618 26  GLU   A CG  
185  C  CD  . GLU   A 26  ? 0.2493 0.4057 0.2579 -0.0288 -0.0489 -0.0442 26  GLU   A CD  
186  O  OE1 . GLU   A 26  ? 0.3114 0.5671 0.3972 0.0616  -0.0779 -0.0482 26  GLU   A OE1 
187  O  OE2 . GLU   A 26  ? 0.3826 0.4514 0.2721 -0.0191 -0.0502 -0.0052 26  GLU   A OE2 
188  N  N   . ARG   A 27  ? 0.1237 0.1519 0.1100 -0.0161 -0.0049 -0.0145 27  ARG   A N   
189  C  CA  . ARG   A 27  ? 0.1178 0.1338 0.1211 -0.0003 -0.0044 -0.0202 27  ARG   A CA  
190  C  C   . ARG   A 27  ? 0.1127 0.1220 0.1083 -0.0045 -0.0023 -0.0109 27  ARG   A C   
191  O  O   . ARG   A 27  ? 0.1089 0.1262 0.1153 -0.0022 -0.0022 -0.0091 27  ARG   A O   
192  C  CB  . ARG   A 27  ? 0.1725 0.1667 0.1230 0.0017  -0.0207 -0.0334 27  ARG   A CB  
193  C  CG  . ARG   A 27  ? 0.1510 0.1825 0.1615 -0.0033 -0.0054 -0.0296 27  ARG   A CG  
194  C  CD  . ARG   A 27  ? 0.2129 0.1685 0.1699 0.0051  -0.0089 -0.0281 27  ARG   A CD  
195  N  NE  . ARG   A 27  ? 0.1801 0.1602 0.1486 0.0000  0.0113  -0.0052 27  ARG   A NE  
196  C  CZ  . ARG   A 27  ? 0.1617 0.1530 0.1351 0.0123  0.0150  -0.0119 27  ARG   A CZ  
197  N  NH1 . ARG   A 27  ? 0.1581 0.1923 0.1742 0.0092  0.0017  -0.0684 27  ARG   A NH1 
198  N  NH2 . ARG   A 27  ? 0.1780 0.1573 0.1714 0.0006  0.0073  -0.0289 27  ARG   A NH2 
199  N  N   . GLN   A 28  ? 0.1073 0.1148 0.1018 0.0009  -0.0064 -0.0103 28  GLN   A N   
200  C  CA  . GLN   A 28  ? 0.1019 0.1024 0.0929 -0.0025 -0.0080 -0.0109 28  GLN   A CA  
201  C  C   . GLN   A 28  ? 0.1023 0.0992 0.0989 -0.0032 -0.0007 -0.0023 28  GLN   A C   
202  O  O   . GLN   A 28  ? 0.1198 0.1218 0.0995 -0.0146 -0.0056 -0.0044 28  GLN   A O   
203  C  CB  . GLN   A 28  ? 0.0929 0.1150 0.1105 -0.0021 -0.0128 -0.0066 28  GLN   A CB  
204  C  CG  . GLN   A 28  ? 0.0951 0.1194 0.1206 0.0010  -0.0069 -0.0132 28  GLN   A CG  
205  C  CD  . GLN   A 28  ? 0.0950 0.1168 0.1154 -0.0069 -0.0041 -0.0168 28  GLN   A CD  
206  O  OE1 . GLN   A 28  ? 0.0991 0.1179 0.1160 -0.0082 0.0001  -0.0118 28  GLN   A OE1 
207  N  NE2 . GLN   A 28  ? 0.0973 0.1141 0.1094 -0.0005 -0.0050 -0.0083 28  GLN   A NE2 
208  N  N   . SER   A 29  ? 0.0931 0.0987 0.0938 -0.0037 -0.0047 -0.0117 29  SER   A N   
209  C  CA  . SER   A 29  ? 0.0934 0.0910 0.0902 -0.0021 0.0013  -0.0059 29  SER   A CA  
210  C  C   . SER   A 29  ? 0.0820 0.0923 0.0896 0.0037  0.0015  -0.0021 29  SER   A C   
211  O  O   . SER   A 29  ? 0.0937 0.1032 0.1076 -0.0050 0.0098  -0.0043 29  SER   A O   
212  C  CB  . SER   A 29  ? 0.0898 0.0898 0.0917 -0.0020 0.0053  -0.0050 29  SER   A CB  
213  O  OG  . SER   A 29  ? 0.0908 0.0979 0.1057 0.0052  0.0031  -0.0121 29  SER   A OG  
214  N  N   . PRO   A 30  ? 0.0857 0.0877 0.0937 0.0005  0.0034  -0.0063 30  PRO   A N   
215  C  CA  . PRO   A 30  ? 0.0871 0.0878 0.0999 0.0041  0.0020  -0.0004 30  PRO   A CA  
216  C  C   . PRO   A 30  ? 0.0929 0.0865 0.0988 0.0037  0.0052  -0.0057 30  PRO   A C   
217  O  O   . PRO   A 30  ? 0.0970 0.1108 0.1050 0.0030  0.0014  -0.0020 30  PRO   A O   
218  C  CB  . PRO   A 30  ? 0.0971 0.0954 0.1049 -0.0017 0.0015  -0.0078 30  PRO   A CB  
219  C  CG  . PRO   A 30  ? 0.1016 0.0952 0.1016 0.0010  0.0006  -0.0093 30  PRO   A CG  
220  C  CD  . PRO   A 30  ? 0.1001 0.0950 0.0964 0.0024  0.0040  -0.0090 30  PRO   A CD  
221  N  N   . VAL   A 31  ? 0.0993 0.1039 0.0919 0.0042  0.0034  0.0107  31  VAL   A N   
222  C  CA  . VAL   A 31  ? 0.1038 0.1029 0.0960 0.0047  -0.0036 0.0111  31  VAL   A CA  
223  C  C   . VAL   A 31  ? 0.1036 0.1046 0.1044 0.0085  0.0056  0.0103  31  VAL   A C   
224  O  O   . VAL   A 31  ? 0.1054 0.1110 0.1130 -0.0020 -0.0026 0.0144  31  VAL   A O   
225  C  CB  . VAL   A 31  ? 0.1189 0.1083 0.1025 0.0016  0.0054  -0.0002 31  VAL   A CB  
226  C  CG1 . VAL   A 31  ? 0.1374 0.1194 0.1126 -0.0057 0.0066  -0.0103 31  VAL   A CG1 
227  C  CG2 . VAL   A 31  ? 0.1303 0.1222 0.1094 0.0086  0.0144  0.0005  31  VAL   A CG2 
228  N  N   . ASP   A 32  ? 0.1127 0.1062 0.1038 0.0058  -0.0035 0.0125  32  ASP   A N   
229  C  CA  . ASP   A 32  ? 0.1208 0.0988 0.1068 0.0047  -0.0013 0.0122  32  ASP   A CA  
230  C  C   . ASP   A 32  ? 0.1218 0.1066 0.1048 0.0025  0.0069  0.0075  32  ASP   A C   
231  O  O   . ASP   A 32  ? 0.1406 0.1539 0.1199 -0.0038 -0.0001 -0.0099 32  ASP   A O   
232  C  CB  . ASP   A 32  ? 0.1324 0.1197 0.1205 0.0102  -0.0046 0.0168  32  ASP   A CB  
233  C  CG  . ASP   A 32  ? 0.1607 0.1186 0.1303 0.0071  -0.0038 0.0257  32  ASP   A CG  
234  O  OD1 . ASP   A 32  ? 0.1490 0.1175 0.1271 -0.0015 -0.0043 0.0208  32  ASP   A OD1 
235  O  OD2 . ASP   A 32  ? 0.2126 0.1669 0.1336 -0.0132 -0.0111 0.0359  32  ASP   A OD2 
236  N  N   . ILE   A 33  ? 0.1202 0.1181 0.0979 0.0115  0.0089  0.0046  33  ILE   A N   
237  C  CA  . ILE   A 33  ? 0.1319 0.1166 0.1112 0.0150  0.0085  0.0088  33  ILE   A CA  
238  C  C   . ILE   A 33  ? 0.1334 0.1246 0.1205 0.0172  0.0235  0.0062  33  ILE   A C   
239  O  O   . ILE   A 33  ? 0.1443 0.1350 0.1238 0.0037  0.0139  0.0156  33  ILE   A O   
240  C  CB  . ILE   A 33  ? 0.1296 0.1184 0.1250 0.0176  0.0089  0.0074  33  ILE   A CB  
241  C  CG1 . ILE   A 33  ? 0.1335 0.1287 0.1461 0.0198  0.0009  0.0156  33  ILE   A CG1 
242  C  CG2 . ILE   A 33  ? 0.1436 0.1494 0.1440 0.0187  0.0185  0.0086  33  ILE   A CG2 
243  C  CD1 . ILE   A 33  ? 0.1357 0.1504 0.1594 0.0198  0.0004  0.0304  33  ILE   A CD1 
244  N  N   . ASP   A 34  ? 0.1772 0.1365 0.1222 0.0128  0.0058  0.0200  34  ASP   A N   
245  C  CA  . ASP   A 34  ? 0.1799 0.1424 0.1253 0.0239  0.0152  0.0270  34  ASP   A CA  
246  C  C   . ASP   A 34  ? 0.1788 0.1569 0.1046 0.0311  0.0174  0.0387  34  ASP   A C   
247  O  O   . ASP   A 34  ? 0.2117 0.1801 0.1242 0.0433  0.0296  0.0183  34  ASP   A O   
248  C  CB  . ASP   A 34  ? 0.2034 0.1678 0.1474 0.0288  0.0029  0.0321  34  ASP   A CB  
249  C  CG  A ASP   A 34  ? 0.2413 0.1740 0.1460 0.0348  0.0065  0.0298  34  ASP   A CG  
250  C  CG  B ASP   A 34  ? 0.2089 0.2122 0.1554 0.0153  -0.0004 0.0466  34  ASP   A CG  
251  O  OD1 A ASP   A 34  ? 0.2671 0.1605 0.1665 0.0544  0.0158  0.0398  34  ASP   A OD1 
252  O  OD1 B ASP   A 34  ? 0.2029 0.1968 0.1495 0.0160  -0.0011 0.0542  34  ASP   A OD1 
253  O  OD2 A ASP   A 34  ? 0.2806 0.2180 0.1628 0.0308  0.0370  0.0214  34  ASP   A OD2 
254  O  OD2 B ASP   A 34  ? 0.2598 0.2650 0.1683 0.0161  -0.0225 0.0740  34  ASP   A OD2 
255  N  N   . THR   A 35  ? 0.1747 0.1740 0.1214 0.0313  0.0283  0.0375  35  THR   A N   
256  C  CA  . THR   A 35  ? 0.1768 0.1789 0.1411 0.0366  0.0367  0.0471  35  THR   A CA  
257  C  C   . THR   A 35  ? 0.1956 0.1588 0.1515 0.0406  0.0402  0.0428  35  THR   A C   
258  O  O   . THR   A 35  ? 0.2267 0.2109 0.1731 0.0687  0.0497  0.0333  35  THR   A O   
259  C  CB  . THR   A 35  ? 0.1849 0.2110 0.1690 0.0353  0.0297  0.0354  35  THR   A CB  
260  O  OG1 . THR   A 35  ? 0.1923 0.2369 0.1759 0.0032  0.0293  0.0399  35  THR   A OG1 
261  C  CG2 . THR   A 35  ? 0.2136 0.2486 0.1761 0.0421  0.0311  0.0327  35  THR   A CG2 
262  N  N   A HIS   A 36  ? 0.1881 0.1369 0.1120 0.0283  0.0240  0.0375  36  HIS   A N   
263  N  N   B HIS   A 36  ? 0.2278 0.1407 0.1289 0.0377  0.0522  0.0386  36  HIS   A N   
264  C  CA  A HIS   A 36  ? 0.2148 0.1516 0.1211 0.0319  0.0254  0.0397  36  HIS   A CA  
265  C  CA  B HIS   A 36  ? 0.2834 0.1561 0.1450 0.0334  0.0526  0.0483  36  HIS   A CA  
266  C  C   A HIS   A 36  ? 0.2553 0.1711 0.1020 0.0400  0.0295  0.0226  36  HIS   A C   
267  C  C   B HIS   A 36  ? 0.2872 0.1950 0.1394 0.0426  0.0549  0.0136  36  HIS   A C   
268  O  O   A HIS   A 36  ? 0.2582 0.1973 0.1154 0.0538  0.0294  0.0177  36  HIS   A O   
269  O  O   B HIS   A 36  ? 0.2537 0.2460 0.1470 0.0396  0.0365  -0.0155 36  HIS   A O   
270  C  CB  A HIS   A 36  ? 0.1798 0.1337 0.1077 0.0067  0.0140  0.0232  36  HIS   A CB  
271  C  CB  B HIS   A 36  ? 0.3252 0.1592 0.1536 0.0287  0.0427  0.0549  36  HIS   A CB  
272  C  CG  A HIS   A 36  ? 0.1831 0.1242 0.1130 0.0071  0.0035  0.0206  36  HIS   A CG  
273  C  CG  B HIS   A 36  ? 0.3649 0.1562 0.1975 0.0546  -0.0012 0.0581  36  HIS   A CG  
274  N  ND1 A HIS   A 36  ? 0.1914 0.1736 0.1315 -0.0136 -0.0069 0.0224  36  HIS   A ND1 
275  N  ND1 B HIS   A 36  ? 0.4127 0.2162 0.2164 0.0545  -0.0072 0.0414  36  HIS   A ND1 
276  C  CD2 A HIS   A 36  ? 0.2256 0.1336 0.1366 0.0131  -0.0100 0.0197  36  HIS   A CD2 
277  C  CD2 B HIS   A 36  ? 0.3693 0.2104 0.2351 0.0691  -0.0088 0.0453  36  HIS   A CD2 
278  C  CE1 A HIS   A 36  ? 0.2238 0.1718 0.1552 -0.0170 -0.0061 0.0303  36  HIS   A CE1 
279  C  CE1 B HIS   A 36  ? 0.3947 0.2156 0.2369 0.0600  -0.0321 0.0408  36  HIS   A CE1 
280  N  NE2 A HIS   A 36  ? 0.2183 0.1472 0.1653 0.0050  -0.0033 0.0485  36  HIS   A NE2 
281  N  NE2 B HIS   A 36  ? 0.3752 0.2097 0.2267 0.0736  -0.0191 0.0438  36  HIS   A NE2 
282  N  N   . THR   A 37  ? 0.2699 0.1855 0.1585 0.0568  0.0566  0.0214  37  THR   A N   
283  C  CA  . THR   A 37  ? 0.3121 0.2082 0.1464 0.0602  0.0203  0.0473  37  THR   A CA  
284  C  C   . THR   A 37  ? 0.2566 0.1959 0.1776 0.0736  0.0078  0.0167  37  THR   A C   
285  O  O   . THR   A 37  ? 0.3075 0.2171 0.2072 0.0712  -0.0504 0.0023  37  THR   A O   
286  C  CB  . THR   A 37  ? 0.3182 0.2325 0.3376 0.0788  -0.0734 0.0533  37  THR   A CB  
287  O  OG1 . THR   A 37  ? 0.4247 0.2800 0.4564 0.1503  -0.0369 0.0608  37  THR   A OG1 
288  C  CG2 . THR   A 37  ? 0.3524 0.3380 0.3018 0.0824  -0.0671 0.0459  37  THR   A CG2 
289  N  N   . ALA   A 38  ? 0.2324 0.1706 0.1370 0.0535  0.0237  0.0165  38  ALA   A N   
290  C  CA  . ALA   A 38  ? 0.2047 0.1742 0.1287 0.0454  0.0307  0.0250  38  ALA   A CA  
291  C  C   . ALA   A 38  ? 0.2328 0.2001 0.1600 0.0476  0.0562  0.0202  38  ALA   A C   
292  O  O   . ALA   A 38  ? 0.2823 0.2581 0.2264 0.0378  0.0962  0.0457  38  ALA   A O   
293  C  CB  . ALA   A 38  ? 0.1979 0.1809 0.1518 0.0273  0.0102  0.0257  38  ALA   A CB  
294  N  N   . LYS   A 39  ? 0.2406 0.2044 0.1354 0.0854  0.0297  0.0078  39  LYS   A N   
295  C  CA  . LYS   A 39  ? 0.2674 0.2592 0.1620 0.1134  0.0186  0.0094  39  LYS   A CA  
296  C  C   . LYS   A 39  ? 0.2050 0.2043 0.1199 0.0614  0.0154  0.0067  39  LYS   A C   
297  O  O   . LYS   A 39  ? 0.1712 0.1947 0.1131 0.0356  0.0084  0.0187  39  LYS   A O   
298  C  CB  . LYS   A 39  ? 0.2718 0.2741 0.2341 0.1089  -0.0134 -0.0198 39  LYS   A CB  
299  C  CG  . LYS   A 39  ? 0.2533 0.3157 0.2387 0.0957  -0.0240 0.0095  39  LYS   A CG  
300  C  CD  . LYS   A 39  ? 0.2538 0.2995 0.2166 0.0753  -0.0242 0.0209  39  LYS   A CD  
301  C  CE  . LYS   A 39  ? 0.2687 0.3803 0.2989 0.0652  -0.0004 0.0078  39  LYS   A CE  
302  N  NZ  . LYS   A 39  ? 0.2342 0.4085 0.3960 0.0603  0.0232  0.0901  39  LYS   A NZ  
303  N  N   . TYR   A 40  ? 0.2562 0.2390 0.1289 0.0101  0.0526  0.0320  40  TYR   A N   
304  C  CA  . TYR   A 40  ? 0.2118 0.2803 0.1306 -0.0101 0.0446  0.0024  40  TYR   A CA  
305  C  C   . TYR   A 40  ? 0.1629 0.2681 0.1298 0.0223  0.0303  -0.0032 40  TYR   A C   
306  O  O   . TYR   A 40  ? 0.1891 0.3145 0.1230 0.0520  0.0082  -0.0103 40  TYR   A O   
307  C  CB  . TYR   A 40  ? 0.2882 0.3439 0.1214 -0.0633 0.0194  0.0034  40  TYR   A CB  
308  C  CG  . TYR   A 40  ? 0.3051 0.4699 0.2743 -0.0582 -0.0514 0.0124  40  TYR   A CG  
309  C  CD1 . TYR   A 40  ? 0.3060 0.5266 0.2201 -0.0595 -0.0550 -0.0272 40  TYR   A CD1 
310  C  CD2 . TYR   A 40  ? 0.5086 0.5736 0.2658 0.0179  0.0144  -0.0681 40  TYR   A CD2 
311  C  CE1 . TYR   A 40  ? 0.4233 0.6393 0.4845 -0.0083 -0.2142 -0.0508 40  TYR   A CE1 
312  C  CE2 . TYR   A 40  ? 0.5486 0.6494 0.5171 0.0025  0.0104  0.0209  40  TYR   A CE2 
313  C  CZ  . TYR   A 40  ? 0.6053 0.9443 0.6137 0.2000  -0.0540 -0.0732 40  TYR   A CZ  
314  O  OH  . TYR   A 40  ? 0.3093 0.6881 0.5181 0.0731  0.0702  -0.0508 40  TYR   A OH  
315  N  N   . ASP   A 41  ? 0.1603 0.2644 0.1267 0.0389  0.0207  -0.0147 41  ASP   A N   
316  C  CA  . ASP   A 41  ? 0.2230 0.2789 0.1407 0.0775  -0.0212 -0.0181 41  ASP   A CA  
317  C  C   . ASP   A 41  ? 0.2368 0.3578 0.1310 0.1213  0.0109  0.0079  41  ASP   A C   
318  O  O   . ASP   A 41  ? 0.2113 0.4016 0.1453 0.1012  0.0058  0.0167  41  ASP   A O   
319  C  CB  . ASP   A 41  ? 0.2430 0.2452 0.2113 0.0512  -0.0589 -0.0375 41  ASP   A CB  
320  C  CG  . ASP   A 41  ? 0.3416 0.3008 0.2672 0.0292  -0.0680 -0.0031 41  ASP   A CG  
321  O  OD1 . ASP   A 41  ? 0.5102 0.3188 0.2658 0.0988  -0.0843 -0.0836 41  ASP   A OD1 
322  O  OD2 . ASP   A 41  ? 0.4039 0.3915 0.3274 -0.0516 -0.0899 -0.0224 41  ASP   A OD2 
323  N  N   . PRO   A 42  ? 0.2770 0.4577 0.1815 0.1822  0.0343  0.0316  42  PRO   A N   
324  C  CA  . PRO   A 42  ? 0.2923 0.5349 0.2102 0.1748  0.0744  0.0411  42  PRO   A CA  
325  C  C   . PRO   A 42  ? 0.3501 0.5230 0.2343 0.1689  0.0632  -0.0027 42  PRO   A C   
326  O  O   . PRO   A 42  ? 0.3902 0.6705 0.3184 0.2605  0.0623  0.0631  42  PRO   A O   
327  C  CB  . PRO   A 42  ? 0.3627 0.6254 0.2515 0.1644  0.1278  0.0590  42  PRO   A CB  
328  C  CG  . PRO   A 42  ? 0.3741 0.6063 0.2331 0.1779  0.0957  0.0242  42  PRO   A CG  
329  C  CD  . PRO   A 42  ? 0.3472 0.4939 0.1789 0.2005  0.0468  0.0431  42  PRO   A CD  
330  N  N   . SER   A 43  ? 0.3748 0.4480 0.1698 0.1821  0.0232  -0.0247 43  SER   A N   
331  C  CA  . SER   A 43  ? 0.5239 0.4172 0.2019 0.1867  0.0084  -0.0553 43  SER   A CA  
332  C  C   . SER   A 43  ? 0.4388 0.4040 0.1981 0.1593  0.0113  -0.0243 43  SER   A C   
333  O  O   . SER   A 43  ? 0.4983 0.4240 0.3257 0.1583  -0.0186 0.0526  43  SER   A O   
334  C  CB  . SER   A 43  ? 0.6022 0.4587 0.2608 0.1601  -0.0180 -0.0531 43  SER   A CB  
335  O  OG  . SER   A 43  ? 0.6473 0.6041 0.2159 0.1722  0.0041  -0.0654 43  SER   A OG  
336  N  N   . LEU   A 44  ? 0.3454 0.4830 0.1818 0.1580  -0.0095 -0.0069 44  LEU   A N   
337  C  CA  . LEU   A 44  ? 0.2652 0.4677 0.2006 0.0768  -0.0157 0.0041  44  LEU   A CA  
338  C  C   . LEU   A 44  ? 0.2664 0.5103 0.2846 0.0363  -0.0237 0.0845  44  LEU   A C   
339  O  O   . LEU   A 44  ? 0.3042 0.6540 0.3381 0.0081  -0.0337 0.1868  44  LEU   A O   
340  C  CB  . LEU   A 44  ? 0.2177 0.4046 0.1453 0.0051  0.0107  -0.0162 44  LEU   A CB  
341  C  CG  . LEU   A 44  ? 0.1931 0.2961 0.1476 -0.0066 0.0077  0.0033  44  LEU   A CG  
342  C  CD1 . LEU   A 44  ? 0.2603 0.2631 0.1480 -0.0441 0.0161  -0.0119 44  LEU   A CD1 
343  C  CD2 . LEU   A 44  ? 0.2119 0.2508 0.1868 -0.0099 -0.0067 -0.0069 44  LEU   A CD2 
344  N  N   A LYS   A 45  ? 0.2848 0.4932 0.2414 0.0659  -0.0233 0.0411  45  LYS   A N   
345  N  N   B LYS   A 45  ? 0.2079 0.3864 0.1678 0.0327  0.0015  -0.0015 45  LYS   A N   
346  C  CA  A LYS   A 45  ? 0.2557 0.3697 0.2601 0.0460  -0.0229 -0.0204 45  LYS   A CA  
347  C  CA  B LYS   A 45  ? 0.1684 0.2885 0.2041 0.0229  0.0158  -0.0273 45  LYS   A CA  
348  C  C   A LYS   A 45  ? 0.1457 0.3240 0.1881 0.0580  0.0247  0.0192  45  LYS   A C   
349  C  C   B LYS   A 45  ? 0.1470 0.2189 0.1888 0.0210  0.0218  -0.0080 45  LYS   A C   
350  O  O   A LYS   A 45  ? 0.1365 0.1956 0.1540 0.0131  0.0264  0.0250  45  LYS   A O   
351  O  O   B LYS   A 45  ? 0.1562 0.1864 0.1823 0.0205  0.0295  0.0004  45  LYS   A O   
352  C  CB  A LYS   A 45  ? 0.3597 0.4002 0.3580 0.0404  -0.0770 -0.0408 45  LYS   A CB  
353  C  CB  B LYS   A 45  ? 0.3799 0.3799 0.3799 0.0000  0.0000  0.0000  45  LYS   A CB  
354  C  CG  A LYS   A 45  ? 0.4081 0.4481 0.4333 0.0325  -0.0956 -0.0260 45  LYS   A CG  
355  C  CG  B LYS   A 45  ? 0.3799 0.3799 0.3799 0.0000  0.0000  0.0000  45  LYS   A CG  
356  C  CD  A LYS   A 45  ? 0.4157 0.5255 0.5388 0.0242  -0.1204 -0.0695 45  LYS   A CD  
357  C  CD  B LYS   A 45  ? 0.3799 0.3799 0.3799 0.0000  0.0000  0.0000  45  LYS   A CD  
358  N  N   A PRO   A 46  ? 0.1348 0.2573 0.2114 0.0187  0.0431  0.0277  46  PRO   A N   
359  N  N   B PRO   A 46  ? 0.1326 0.1857 0.2095 -0.0041 0.0280  0.0030  46  PRO   A N   
360  C  CA  A PRO   A 46  ? 0.1380 0.2425 0.2103 -0.0062 0.0381  0.0345  46  PRO   A CA  
361  C  CA  B PRO   A 46  ? 0.1470 0.1758 0.2034 -0.0062 0.0225  0.0117  46  PRO   A CA  
362  C  C   A PRO   A 46  ? 0.1181 0.2238 0.2032 -0.0082 0.0260  0.0226  46  PRO   A C   
363  C  C   B PRO   A 46  ? 0.1188 0.1733 0.1784 -0.0110 0.0076  -0.0003 46  PRO   A C   
364  O  O   A PRO   A 46  ? 0.1424 0.2211 0.1998 0.0176  0.0359  0.0098  46  PRO   A O   
365  O  O   B PRO   A 46  ? 0.1165 0.1637 0.1679 -0.0165 0.0076  -0.0122 46  PRO   A O   
366  C  CB  A PRO   A 46  ? 0.1390 0.2579 0.2261 -0.0183 0.0400  0.0509  46  PRO   A CB  
367  C  CB  B PRO   A 46  ? 0.1412 0.1975 0.2178 -0.0181 0.0285  0.0142  46  PRO   A CB  
368  C  CG  A PRO   A 46  ? 0.1450 0.2898 0.2432 0.0043  0.0520  0.0303  46  PRO   A CG  
369  C  CG  B PRO   A 46  ? 0.1756 0.2456 0.2614 0.0000  0.0147  -0.0061 46  PRO   A CG  
370  C  CD  A PRO   A 46  ? 0.1531 0.2976 0.2271 0.0243  0.0522  0.0239  46  PRO   A CD  
371  C  CD  B PRO   A 46  ? 0.1403 0.2123 0.2147 0.0025  0.0377  -0.0160 46  PRO   A CD  
372  N  N   A LEU   A 47  ? 0.1068 0.2081 0.1783 -0.0180 0.0106  0.0188  47  LEU   A N   
373  N  N   B LEU   A 47  ? 0.1195 0.1465 0.1944 0.0068  -0.0059 0.0011  47  LEU   A N   
374  C  CA  A LEU   A 47  ? 0.1167 0.1975 0.1766 -0.0213 -0.0054 0.0363  47  LEU   A CA  
375  C  CA  B LEU   A 47  ? 0.1089 0.1602 0.1832 0.0063  0.0046  -0.0089 47  LEU   A CA  
376  C  C   A LEU   A 47  ? 0.1079 0.1733 0.1883 -0.0167 -0.0073 0.0215  47  LEU   A C   
377  C  C   B LEU   A 47  ? 0.1203 0.1647 0.1973 -0.0100 -0.0053 -0.0017 47  LEU   A C   
378  O  O   A LEU   A 47  ? 0.1107 0.1758 0.1605 -0.0370 0.0033  0.0090  47  LEU   A O   
379  O  O   B LEU   A 47  ? 0.1286 0.1959 0.2187 -0.0405 -0.0002 -0.0025 47  LEU   A O   
380  C  CB  A LEU   A 47  ? 0.1077 0.1999 0.1921 -0.0212 -0.0131 0.0349  47  LEU   A CB  
381  C  CB  B LEU   A 47  ? 0.1444 0.1953 0.2143 -0.0007 0.0276  -0.0289 47  LEU   A CB  
382  C  CG  A LEU   A 47  ? 0.1150 0.2042 0.2035 -0.0080 -0.0200 0.0415  47  LEU   A CG  
383  C  CG  B LEU   A 47  ? 0.1720 0.2409 0.2503 -0.0041 -0.0001 -0.0324 47  LEU   A CG  
384  C  CD1 A LEU   A 47  ? 0.1297 0.2003 0.2393 -0.0124 -0.0235 0.0424  47  LEU   A CD1 
385  C  CD1 B LEU   A 47  ? 0.1440 0.2410 0.2694 -0.0039 -0.0076 -0.0569 47  LEU   A CD1 
386  C  CD2 A LEU   A 47  ? 0.1458 0.2296 0.2433 -0.0065 -0.0383 0.0317  47  LEU   A CD2 
387  C  CD2 B LEU   A 47  ? 0.1448 0.2810 0.2824 -0.0060 -0.0045 -0.0383 47  LEU   A CD2 
388  N  N   . SER   A 48  ? 0.1152 0.1665 0.1807 -0.0179 -0.0129 0.0162  48  SER   A N   
389  C  CA  . SER   A 48  ? 0.1310 0.1715 0.1595 -0.0227 0.0018  0.0065  48  SER   A CA  
390  C  C   . SER   A 48  ? 0.1350 0.1785 0.1620 -0.0290 0.0127  -0.0102 48  SER   A C   
391  O  O   . SER   A 48  ? 0.1455 0.1828 0.1751 -0.0462 0.0148  -0.0232 48  SER   A O   
392  C  CB  . SER   A 48  ? 0.1431 0.1988 0.1976 0.0197  0.0090  0.0022  48  SER   A CB  
393  O  OG  . SER   A 48  ? 0.2266 0.2441 0.2621 0.0273  0.0064  0.0264  48  SER   A OG  
394  N  N   . VAL   A 49  ? 0.1444 0.1916 0.1621 -0.0591 0.0191  -0.0067 49  VAL   A N   
395  C  CA  . VAL   A 49  ? 0.1570 0.1952 0.1779 -0.0661 0.0239  -0.0230 49  VAL   A CA  
396  C  C   . VAL   A 49  ? 0.1544 0.2306 0.1669 -0.0601 -0.0081 -0.0237 49  VAL   A C   
397  O  O   . VAL   A 49  ? 0.1735 0.3155 0.1993 -0.1118 -0.0180 -0.0022 49  VAL   A O   
398  C  CB  . VAL   A 49  ? 0.2376 0.2072 0.1954 -0.0698 0.0329  -0.0377 49  VAL   A CB  
399  C  CG1 . VAL   A 49  ? 0.2952 0.2197 0.2135 -0.0676 0.0494  -0.0524 49  VAL   A CG1 
400  C  CG2 . VAL   A 49  ? 0.2091 0.2036 0.2798 -0.0619 0.0345  -0.0324 49  VAL   A CG2 
401  N  N   . SER   A 50  ? 0.1374 0.2263 0.1713 -0.0553 0.0017  -0.0242 50  SER   A N   
402  C  CA  . SER   A 50  ? 0.1402 0.2359 0.2073 -0.0430 0.0088  -0.0271 50  SER   A CA  
403  C  C   . SER   A 50  ? 0.1214 0.2216 0.1899 -0.0215 -0.0039 -0.0073 50  SER   A C   
404  O  O   . SER   A 50  ? 0.1357 0.2104 0.1945 -0.0102 0.0005  -0.0023 50  SER   A O   
405  C  CB  . SER   A 50  ? 0.2116 0.2875 0.2496 -0.0189 0.0147  -0.0369 50  SER   A CB  
406  O  OG  . SER   A 50  ? 0.2973 0.4078 0.3135 0.0099  0.0407  -0.0633 50  SER   A OG  
407  N  N   . TYR   A 51  ? 0.1270 0.2171 0.1838 -0.0245 0.0108  -0.0125 51  TYR   A N   
408  C  CA  . TYR   A 51  ? 0.1314 0.2137 0.1767 -0.0125 -0.0030 -0.0015 51  TYR   A CA  
409  C  C   . TYR   A 51  ? 0.1544 0.2410 0.1964 0.0124  -0.0017 0.0104  51  TYR   A C   
410  O  O   . TYR   A 51  ? 0.1700 0.2418 0.1862 0.0136  -0.0233 -0.0024 51  TYR   A O   
411  C  CB  . TYR   A 51  ? 0.1527 0.2229 0.1787 -0.0020 -0.0128 -0.0230 51  TYR   A CB  
412  C  CG  . TYR   A 51  ? 0.1346 0.1769 0.1596 -0.0187 -0.0074 -0.0126 51  TYR   A CG  
413  C  CD1 . TYR   A 51  ? 0.1256 0.1686 0.1773 -0.0151 -0.0060 -0.0146 51  TYR   A CD1 
414  C  CD2 . TYR   A 51  ? 0.1335 0.1767 0.1547 -0.0186 0.0008  -0.0151 51  TYR   A CD2 
415  C  CE1 . TYR   A 51  ? 0.1189 0.1503 0.1586 -0.0203 -0.0063 -0.0142 51  TYR   A CE1 
416  C  CE2 . TYR   A 51  ? 0.1336 0.1363 0.1500 -0.0141 0.0020  -0.0179 51  TYR   A CE2 
417  C  CZ  . TYR   A 51  ? 0.1255 0.1393 0.1465 -0.0162 -0.0020 -0.0073 51  TYR   A CZ  
418  O  OH  . TYR   A 51  ? 0.1236 0.1360 0.1684 -0.0089 -0.0082 -0.0099 51  TYR   A OH  
419  N  N   . ASP   A 52  ? 0.1403 0.2939 0.2027 0.0161  -0.0027 0.0178  52  ASP   A N   
420  C  CA  . ASP   A 52  ? 0.1592 0.3031 0.2445 0.0209  -0.0087 0.0250  52  ASP   A CA  
421  C  C   . ASP   A 52  ? 0.1725 0.2485 0.2300 0.0229  -0.0394 0.0128  52  ASP   A C   
422  O  O   . ASP   A 52  ? 0.2496 0.2773 0.2384 -0.0198 -0.0518 0.0225  52  ASP   A O   
423  C  CB  . ASP   A 52  ? 0.1843 0.3551 0.2771 0.0136  -0.0155 0.0468  52  ASP   A CB  
424  C  CG  . ASP   A 52  ? 0.3092 0.3668 0.3690 0.0725  0.0590  0.0220  52  ASP   A CG  
425  O  OD1 . ASP   A 52  ? 0.3891 0.4944 0.4400 0.0555  0.1460  0.0625  52  ASP   A OD1 
426  O  OD2 . ASP   A 52  ? 0.5282 0.4347 0.4738 0.1204  0.0103  0.0684  52  ASP   A OD2 
427  N  N   . GLN   A 53  ? 0.1463 0.2282 0.2356 0.0390  -0.0195 -0.0039 53  GLN   A N   
428  C  CA  . GLN   A 53  ? 0.1587 0.2165 0.2532 0.0327  -0.0216 0.0084  53  GLN   A CA  
429  C  C   . GLN   A 53  ? 0.1549 0.1834 0.2013 0.0252  -0.0084 -0.0201 53  GLN   A C   
430  O  O   . GLN   A 53  ? 0.1990 0.2012 0.2259 0.0051  -0.0110 -0.0124 53  GLN   A O   
431  C  CB  . GLN   A 53  ? 0.2038 0.2415 0.3330 0.0746  0.0002  -0.0193 53  GLN   A CB  
432  C  CG  . GLN   A 53  ? 0.2246 0.3349 0.3920 0.0689  -0.0030 -0.0145 53  GLN   A CG  
433  C  CD  . GLN   A 53  ? 0.3047 0.4027 0.4685 0.0511  -0.0315 0.0476  53  GLN   A CD  
434  O  OE1 . GLN   A 53  ? 0.4667 0.5522 0.5153 0.0318  -0.0090 0.1354  53  GLN   A OE1 
435  N  NE2 . GLN   A 53  ? 0.3524 0.4184 0.5175 0.0582  -0.0559 0.1150  53  GLN   A NE2 
436  N  N   . ALA   A 54  ? 0.1389 0.1705 0.2009 -0.0011 -0.0004 -0.0049 54  ALA   A N   
437  C  CA  . ALA   A 54  ? 0.1303 0.1775 0.1861 0.0109  -0.0140 -0.0262 54  ALA   A CA  
438  C  C   . ALA   A 54  ? 0.1441 0.1924 0.1726 -0.0088 -0.0100 -0.0408 54  ALA   A C   
439  O  O   . ALA   A 54  ? 0.1539 0.2758 0.1940 -0.0248 -0.0186 -0.0599 54  ALA   A O   
440  C  CB  . ALA   A 54  ? 0.1477 0.1892 0.2392 0.0061  0.0067  -0.0193 54  ALA   A CB  
441  N  N   . THR   A 55  ? 0.1346 0.1581 0.1708 0.0076  -0.0177 -0.0113 55  THR   A N   
442  C  CA  . THR   A 55  ? 0.1406 0.1414 0.1833 0.0245  -0.0264 0.0051  55  THR   A CA  
443  C  C   . THR   A 55  ? 0.1356 0.1104 0.1236 0.0041  -0.0178 0.0115  55  THR   A C   
444  O  O   . THR   A 55  ? 0.1369 0.1018 0.1605 0.0010  -0.0163 0.0083  55  THR   A O   
445  C  CB  . THR   A 55  ? 0.1859 0.1517 0.2488 0.0372  -0.0424 0.0019  55  THR   A CB  
446  O  OG1 . THR   A 55  ? 0.2341 0.1724 0.3397 0.0607  -0.0569 -0.0010 55  THR   A OG1 
447  C  CG2 . THR   A 55  ? 0.2632 0.1658 0.2531 0.0495  -0.0510 0.0330  55  THR   A CG2 
448  N  N   . SER   A 56  ? 0.1224 0.1092 0.1379 0.0012  -0.0190 0.0089  56  SER   A N   
449  C  CA  . SER   A 56  ? 0.1212 0.1067 0.1320 0.0082  -0.0236 0.0107  56  SER   A CA  
450  C  C   . SER   A 56  ? 0.1338 0.1029 0.1382 0.0132  -0.0191 0.0164  56  SER   A C   
451  O  O   . SER   A 56  ? 0.1477 0.1339 0.1482 0.0228  -0.0239 0.0269  56  SER   A O   
452  C  CB  . SER   A 56  ? 0.1439 0.1059 0.1253 0.0019  -0.0212 0.0131  56  SER   A CB  
453  O  OG  . SER   A 56  ? 0.1487 0.1140 0.1477 -0.0130 -0.0279 0.0133  56  SER   A OG  
454  N  N   . LEU   A 57  ? 0.1339 0.1027 0.1220 0.0103  -0.0162 0.0130  57  LEU   A N   
455  C  CA  . LEU   A 57  ? 0.1467 0.1057 0.1411 0.0134  -0.0088 0.0171  57  LEU   A CA  
456  C  C   . LEU   A 57  ? 0.1320 0.1040 0.1253 0.0118  -0.0045 0.0179  57  LEU   A C   
457  O  O   . LEU   A 57  ? 0.1535 0.1315 0.1229 0.0204  -0.0101 0.0213  57  LEU   A O   
458  C  CB  . LEU   A 57  ? 0.1956 0.1026 0.1731 -0.0090 0.0110  0.0197  57  LEU   A CB  
459  C  CG  . LEU   A 57  ? 0.2531 0.1317 0.2103 0.0056  0.0241  0.0002  57  LEU   A CG  
460  C  CD1 . LEU   A 57  ? 0.2877 0.1353 0.2409 -0.0138 0.0370  -0.0091 57  LEU   A CD1 
461  C  CD2 . LEU   A 57  ? 0.2880 0.1371 0.2598 0.0328  0.0142  0.0256  57  LEU   A CD2 
462  N  N   . ARG   A 58  ? 0.1367 0.1069 0.1218 0.0132  -0.0110 0.0179  58  ARG   A N   
463  C  CA  . ARG   A 58  ? 0.1250 0.1070 0.1250 0.0131  -0.0066 0.0200  58  ARG   A CA  
464  C  C   . ARG   A 58  ? 0.1210 0.1098 0.1039 0.0087  -0.0052 0.0122  58  ARG   A C   
465  O  O   . ARG   A 58  ? 0.1375 0.1113 0.1052 0.0178  -0.0034 0.0067  58  ARG   A O   
466  C  CB  . ARG   A 58  ? 0.1666 0.1261 0.1741 0.0119  0.0040  0.0473  58  ARG   A CB  
467  C  CG  . ARG   A 58  ? 0.2029 0.1746 0.1933 -0.0040 0.0040  0.0300  58  ARG   A CG  
468  C  CD  . ARG   A 58  ? 0.2059 0.2189 0.2196 -0.0201 0.0100  0.0503  58  ARG   A CD  
469  N  NE  . ARG   A 58  ? 0.1862 0.2274 0.2350 -0.0506 0.0188  0.0354  58  ARG   A NE  
470  C  CZ  . ARG   A 58  ? 0.1782 0.1779 0.2204 -0.0500 0.0396  0.0427  58  ARG   A CZ  
471  N  NH1 . ARG   A 58  ? 0.1873 0.1890 0.2277 -0.0547 0.0349  0.0251  58  ARG   A NH1 
472  N  NH2 . ARG   A 58  ? 0.2039 0.2001 0.2333 -0.0558 0.0528  0.0216  58  ARG   A NH2 
473  N  N   . ILE   A 59  ? 0.1237 0.1061 0.0910 0.0126  -0.0029 0.0132  59  ILE   A N   
474  C  CA  . ILE   A 59  ? 0.1270 0.1034 0.0965 0.0103  -0.0026 0.0131  59  ILE   A CA  
475  C  C   . ILE   A 59  ? 0.1207 0.1074 0.0966 0.0109  0.0024  0.0137  59  ILE   A C   
476  O  O   . ILE   A 59  ? 0.1310 0.1586 0.1000 0.0165  0.0031  0.0165  59  ILE   A O   
477  C  CB  . ILE   A 59  ? 0.1203 0.1103 0.1064 0.0098  0.0004  0.0058  59  ILE   A CB  
478  C  CG1 . ILE   A 59  ? 0.1390 0.1015 0.1139 0.0078  0.0016  0.0111  59  ILE   A CG1 
479  C  CG2 . ILE   A 59  ? 0.1418 0.1132 0.1108 0.0063  -0.0109 -0.0021 59  ILE   A CG2 
480  C  CD1 . ILE   A 59  ? 0.1543 0.1143 0.1115 0.0110  -0.0067 0.0046  59  ILE   A CD1 
481  N  N   . LEU   A 60  ? 0.1150 0.1130 0.1060 0.0022  -0.0002 0.0168  60  LEU   A N   
482  C  CA  . LEU   A 60  ? 0.1183 0.1118 0.1142 0.0036  0.0032  0.0252  60  LEU   A CA  
483  C  C   . LEU   A 60  ? 0.1067 0.1037 0.1068 0.0007  0.0037  0.0182  60  LEU   A C   
484  O  O   . LEU   A 60  ? 0.1177 0.1201 0.1018 0.0174  0.0089  0.0182  60  LEU   A O   
485  C  CB  . LEU   A 60  ? 0.1337 0.0912 0.1691 0.0046  0.0044  0.0256  60  LEU   A CB  
486  C  CG  . LEU   A 60  ? 0.1424 0.1246 0.1548 -0.0096 0.0023  0.0175  60  LEU   A CG  
487  C  CD1 . LEU   A 60  ? 0.1650 0.1344 0.1653 -0.0201 0.0079  0.0186  60  LEU   A CD1 
488  C  CD2 . LEU   A 60  ? 0.1614 0.1481 0.1727 -0.0170 -0.0019 0.0119  60  LEU   A CD2 
489  N  N   . ASN   A 61  ? 0.1245 0.1044 0.0901 0.0063  0.0066  0.0121  61  ASN   A N   
490  C  CA  . ASN   A 61  ? 0.1220 0.1091 0.0912 -0.0021 0.0044  0.0122  61  ASN   A CA  
491  C  C   . ASN   A 61  ? 0.1237 0.0976 0.1000 0.0025  0.0082  0.0127  61  ASN   A C   
492  O  O   . ASN   A 61  ? 0.1342 0.1211 0.1208 -0.0027 0.0172  0.0144  61  ASN   A O   
493  C  CB  . ASN   A 61  ? 0.1281 0.1030 0.1023 -0.0019 0.0075  0.0068  61  ASN   A CB  
494  C  CG  . ASN   A 61  ? 0.1322 0.1008 0.1045 -0.0022 0.0113  0.0014  61  ASN   A CG  
495  O  OD1 . ASN   A 61  ? 0.1336 0.1061 0.1210 0.0079  -0.0037 -0.0015 61  ASN   A OD1 
496  N  ND2 . ASN   A 61  ? 0.1355 0.1138 0.1157 0.0011  0.0076  -0.0077 61  ASN   A ND2 
497  N  N   . ASN   A 62  ? 0.1233 0.1024 0.1061 -0.0038 0.0060  0.0122  62  ASN   A N   
498  C  CA  . ASN   A 62  ? 0.1426 0.1066 0.1234 -0.0113 0.0078  0.0082  62  ASN   A CA  
499  C  C   . ASN   A 62  ? 0.1231 0.1255 0.1230 -0.0239 0.0059  0.0022  62  ASN   A C   
500  O  O   . ASN   A 62  ? 0.1442 0.1479 0.1676 -0.0217 -0.0030 0.0006  62  ASN   A O   
501  C  CB  . ASN   A 62  ? 0.1400 0.1123 0.1422 -0.0089 -0.0055 -0.0049 62  ASN   A CB  
502  C  CG  . ASN   A 62  ? 0.1510 0.1108 0.1292 0.0039  -0.0063 -0.0073 62  ASN   A CG  
503  O  OD1 . ASN   A 62  ? 0.1425 0.1177 0.1256 -0.0041 0.0057  0.0010  62  ASN   A OD1 
504  N  ND2 . ASN   A 62  ? 0.2234 0.1287 0.1707 0.0098  0.0348  0.0061  62  ASN   A ND2 
505  N  N   . GLY   A 63  ? 0.1216 0.1181 0.1242 -0.0100 0.0050  0.0071  63  GLY   A N   
506  C  CA  . GLY   A 63  ? 0.1265 0.1326 0.1286 -0.0122 0.0142  0.0128  63  GLY   A CA  
507  C  C   . GLY   A 63  ? 0.1310 0.1185 0.1327 -0.0011 0.0030  0.0095  63  GLY   A C   
508  O  O   . GLY   A 63  ? 0.1434 0.1437 0.1501 0.0142  0.0065  0.0134  63  GLY   A O   
509  N  N   A HIS   A 64  ? 0.1260 0.1161 0.1229 -0.0049 0.0060  0.0164  64  HIS   A N   
510  N  N   B HIS   A 64  ? 0.1260 0.1209 0.1219 -0.0043 0.0047  0.0195  64  HIS   A N   
511  C  CA  A HIS   A 64  ? 0.1257 0.1263 0.1190 -0.0084 0.0072  0.0083  64  HIS   A CA  
512  C  CA  B HIS   A 64  ? 0.1244 0.1360 0.1155 -0.0001 0.0056  0.0173  64  HIS   A CA  
513  C  C   A HIS   A 64  ? 0.1281 0.1140 0.1231 -0.0062 -0.0039 0.0208  64  HIS   A C   
514  C  C   B HIS   A 64  ? 0.1245 0.1067 0.1038 -0.0008 0.0029  0.0155  64  HIS   A C   
515  O  O   A HIS   A 64  ? 0.1359 0.1261 0.1409 0.0082  0.0037  0.0264  64  HIS   A O   
516  O  O   B HIS   A 64  ? 0.1207 0.0991 0.0888 -0.0035 0.0057  0.0001  64  HIS   A O   
517  C  CB  A HIS   A 64  ? 0.1204 0.1401 0.1147 -0.0183 -0.0006 0.0027  64  HIS   A CB  
518  C  CB  B HIS   A 64  ? 0.1355 0.1726 0.1259 -0.0076 -0.0087 0.0239  64  HIS   A CB  
519  C  CG  A HIS   A 64  ? 0.1493 0.1841 0.1139 -0.0323 0.0026  -0.0039 64  HIS   A CG  
520  C  CG  B HIS   A 64  ? 0.1655 0.2246 0.1536 0.0135  -0.0329 -0.0158 64  HIS   A CG  
521  N  ND1 A HIS   A 64  ? 0.1807 0.2224 0.1772 -0.0509 0.0039  -0.0049 64  HIS   A ND1 
522  N  ND1 B HIS   A 64  ? 0.1990 0.2289 0.2186 0.0101  -0.0483 -0.0327 64  HIS   A ND1 
523  C  CD2 A HIS   A 64  ? 0.1449 0.1905 0.1202 -0.0318 -0.0021 -0.0184 64  HIS   A CD2 
524  C  CD2 B HIS   A 64  ? 0.2117 0.2688 0.1774 0.0081  -0.0382 -0.0404 64  HIS   A CD2 
525  C  CE1 A HIS   A 64  ? 0.1688 0.1891 0.1517 -0.0534 0.0215  0.0048  64  HIS   A CE1 
526  C  CE1 B HIS   A 64  ? 0.2630 0.2298 0.2211 -0.0006 -0.0577 -0.0514 64  HIS   A CE1 
527  N  NE2 A HIS   A 64  ? 0.1667 0.2183 0.1589 -0.0312 0.0104  0.0016  64  HIS   A NE2 
528  N  NE2 B HIS   A 64  ? 0.2617 0.2589 0.2356 0.0023  -0.0487 -0.0493 64  HIS   A NE2 
529  N  N   . ALA   A 65  ? 0.1207 0.1057 0.1192 -0.0041 0.0094  0.0173  65  ALA   A N   
530  C  CA  . ALA   A 65  ? 0.1155 0.1041 0.1107 -0.0008 0.0053  0.0054  65  ALA   A CA  
531  C  C   . ALA   A 65  ? 0.1205 0.0989 0.1010 0.0005  0.0102  0.0088  65  ALA   A C   
532  O  O   . ALA   A 65  ? 0.1282 0.1273 0.1221 -0.0057 0.0049  0.0195  65  ALA   A O   
533  C  CB  . ALA   A 65  ? 0.1223 0.1351 0.1165 0.0015  -0.0065 0.0056  65  ALA   A CB  
534  N  N   . PHE   A 66  ? 0.1184 0.1051 0.1012 0.0073  0.0111  0.0173  66  PHE   A N   
535  C  CA  . PHE   A 66  ? 0.1302 0.1053 0.0967 0.0152  0.0060  0.0111  66  PHE   A CA  
536  C  C   . PHE   A 66  ? 0.1254 0.0994 0.0972 0.0053  0.0062  0.0043  66  PHE   A C   
537  O  O   . PHE   A 66  ? 0.1413 0.1017 0.0973 0.0104  0.0118  0.0116  66  PHE   A O   
538  C  CB  . PHE   A 66  ? 0.1468 0.1323 0.1067 0.0194  0.0008  0.0034  66  PHE   A CB  
539  C  CG  . PHE   A 66  ? 0.1416 0.1328 0.1045 0.0101  -0.0128 -0.0104 66  PHE   A CG  
540  C  CD1 . PHE   A 66  ? 0.1412 0.1434 0.1153 0.0155  -0.0191 -0.0070 66  PHE   A CD1 
541  C  CD2 . PHE   A 66  ? 0.1486 0.1340 0.1065 0.0177  -0.0084 -0.0245 66  PHE   A CD2 
542  C  CE1 . PHE   A 66  ? 0.1454 0.1610 0.1302 -0.0012 -0.0224 -0.0046 66  PHE   A CE1 
543  C  CE2 . PHE   A 66  ? 0.1736 0.1420 0.1257 0.0017  -0.0203 -0.0213 66  PHE   A CE2 
544  C  CZ  . PHE   A 66  ? 0.1490 0.1593 0.1204 -0.0170 -0.0161 -0.0125 66  PHE   A CZ  
545  N  N   . ASN   A 67  ? 0.1174 0.1000 0.0963 0.0158  0.0062  0.0128  67  ASN   A N   
546  C  CA  . ASN   A 67  ? 0.1194 0.0948 0.0967 0.0034  0.0026  0.0085  67  ASN   A CA  
547  C  C   . ASN   A 67  ? 0.1187 0.0890 0.0952 0.0067  -0.0037 0.0112  67  ASN   A C   
548  O  O   . ASN   A 67  ? 0.1265 0.1170 0.0961 0.0036  0.0009  0.0211  67  ASN   A O   
549  C  CB  . ASN   A 67  ? 0.1284 0.1114 0.1111 -0.0014 -0.0036 0.0084  67  ASN   A CB  
550  C  CG  . ASN   A 67  ? 0.1324 0.1322 0.1434 -0.0135 -0.0025 0.0032  67  ASN   A CG  
551  O  OD1 . ASN   A 67  ? 0.1591 0.1724 0.1331 -0.0176 -0.0280 0.0275  67  ASN   A OD1 
552  N  ND2 . ASN   A 67  ? 0.1677 0.1494 0.2205 -0.0138 -0.0595 -0.0116 67  ASN   A ND2 
553  N  N   . VAL   A 68  ? 0.1056 0.0812 0.0945 0.0084  -0.0012 0.0135  68  VAL   A N   
554  C  CA  . VAL   A 68  ? 0.1114 0.0933 0.0872 0.0090  -0.0043 0.0076  68  VAL   A CA  
555  C  C   . VAL   A 68  ? 0.1113 0.0881 0.1015 0.0117  -0.0054 0.0114  68  VAL   A C   
556  O  O   . VAL   A 68  ? 0.1248 0.0892 0.0941 0.0106  -0.0073 0.0038  68  VAL   A O   
557  C  CB  . VAL   A 68  ? 0.1101 0.1008 0.1062 0.0039  -0.0078 -0.0008 68  VAL   A CB  
558  C  CG1 . VAL   A 68  ? 0.1180 0.1314 0.1182 0.0112  -0.0197 0.0001  68  VAL   A CG1 
559  C  CG2 . VAL   A 68  ? 0.1161 0.1196 0.1137 -0.0035 -0.0066 -0.0115 68  VAL   A CG2 
560  N  N   . GLU   A 69  ? 0.1290 0.0822 0.1009 0.0058  -0.0009 0.0071  69  GLU   A N   
561  C  CA  . GLU   A 69  ? 0.1249 0.0982 0.1051 0.0033  0.0019  0.0032  69  GLU   A CA  
562  C  C   . GLU   A 69  ? 0.1320 0.0829 0.1205 0.0137  -0.0065 0.0078  69  GLU   A C   
563  O  O   . GLU   A 69  ? 0.1449 0.1054 0.1338 0.0123  -0.0205 -0.0003 69  GLU   A O   
564  C  CB  . GLU   A 69  ? 0.1413 0.1017 0.1445 0.0049  0.0097  0.0149  69  GLU   A CB  
565  C  CG  . GLU   A 69  ? 0.1420 0.1307 0.1754 -0.0104 0.0198  0.0072  69  GLU   A CG  
566  C  CD  . GLU   A 69  ? 0.1664 0.1665 0.2236 0.0194  0.0152  0.0340  69  GLU   A CD  
567  O  OE1 . GLU   A 69  ? 0.2088 0.1873 0.2210 0.0146  0.0386  0.0556  69  GLU   A OE1 
568  O  OE2 . GLU   A 69  ? 0.1684 0.1934 0.2983 0.0060  0.0438  0.0383  69  GLU   A OE2 
569  N  N   . PHE   A 70  ? 0.1247 0.0867 0.1168 0.0069  -0.0074 0.0005  70  PHE   A N   
570  C  CA  . PHE   A 70  ? 0.1241 0.0804 0.1264 0.0068  -0.0110 0.0002  70  PHE   A CA  
571  C  C   . PHE   A 70  ? 0.1410 0.0867 0.1373 0.0141  -0.0056 -0.0010 70  PHE   A C   
572  O  O   . PHE   A 70  ? 0.1435 0.0910 0.1683 -0.0010 -0.0132 0.0080  70  PHE   A O   
573  C  CB  . PHE   A 70  ? 0.1294 0.0902 0.1285 0.0141  -0.0015 0.0031  70  PHE   A CB  
574  C  CG  . PHE   A 70  ? 0.1277 0.0877 0.1135 0.0155  -0.0005 0.0062  70  PHE   A CG  
575  C  CD1 . PHE   A 70  ? 0.1266 0.0980 0.1291 0.0172  0.0118  0.0186  70  PHE   A CD1 
576  C  CD2 . PHE   A 70  ? 0.1322 0.0875 0.1244 0.0101  -0.0060 0.0144  70  PHE   A CD2 
577  C  CE1 . PHE   A 70  ? 0.1512 0.0964 0.1326 0.0163  0.0132  0.0167  70  PHE   A CE1 
578  C  CE2 . PHE   A 70  ? 0.1387 0.1017 0.1284 -0.0006 -0.0067 0.0039  70  PHE   A CE2 
579  C  CZ  . PHE   A 70  ? 0.1535 0.0902 0.1401 0.0017  0.0116  0.0070  70  PHE   A CZ  
580  N  N   . ASP   A 71  ? 0.1510 0.0814 0.1655 0.0105  -0.0179 0.0066  71  ASP   A N   
581  C  CA  . ASP   A 71  ? 0.1686 0.0812 0.1826 0.0128  -0.0180 0.0237  71  ASP   A CA  
582  C  C   . ASP   A 71  ? 0.1579 0.0874 0.1923 0.0035  -0.0021 0.0014  71  ASP   A C   
583  O  O   . ASP   A 71  ? 0.1785 0.1382 0.2183 -0.0123 -0.0003 -0.0111 71  ASP   A O   
584  C  CB  . ASP   A 71  ? 0.1843 0.1034 0.1998 0.0106  -0.0314 0.0234  71  ASP   A CB  
585  C  CG  . ASP   A 71  ? 0.1925 0.0989 0.2315 0.0280  -0.0408 0.0156  71  ASP   A CG  
586  O  OD1 . ASP   A 71  ? 0.2270 0.0995 0.2554 0.0151  -0.0405 0.0229  71  ASP   A OD1 
587  O  OD2 . ASP   A 71  ? 0.2368 0.1262 0.2992 0.0153  -0.0583 0.0076  71  ASP   A OD2 
588  N  N   . ASP   A 72  ? 0.1588 0.0970 0.1888 0.0009  -0.0103 0.0112  72  ASP   A N   
589  C  CA  . ASP   A 72  ? 0.1640 0.0990 0.1884 -0.0046 0.0003  0.0038  72  ASP   A CA  
590  C  C   . ASP   A 72  ? 0.2141 0.1047 0.2019 -0.0077 -0.0216 0.0142  72  ASP   A C   
591  O  O   . ASP   A 72  ? 0.2615 0.1029 0.2386 -0.0022 -0.0467 -0.0037 72  ASP   A O   
592  C  CB  . ASP   A 72  ? 0.1793 0.1048 0.1891 0.0046  0.0000  0.0108  72  ASP   A CB  
593  C  CG  . ASP   A 72  ? 0.1914 0.1549 0.1759 0.0041  -0.0083 0.0150  72  ASP   A CG  
594  O  OD1 . ASP   A 72  ? 0.2291 0.2189 0.1938 -0.0298 -0.0148 0.0439  72  ASP   A OD1 
595  O  OD2 . ASP   A 72  ? 0.1909 0.2170 0.1734 0.0063  -0.0050 0.0164  72  ASP   A OD2 
596  N  N   . SER   A 73  ? 0.2099 0.0961 0.2120 -0.0011 -0.0233 0.0082  73  SER   A N   
597  C  CA  . SER   A 73  ? 0.2079 0.1017 0.2505 -0.0210 -0.0377 0.0028  73  SER   A CA  
598  C  C   . SER   A 73  ? 0.2381 0.1010 0.2394 -0.0069 -0.0277 -0.0129 73  SER   A C   
599  O  O   . SER   A 73  ? 0.2897 0.0973 0.2806 0.0082  -0.0552 -0.0078 73  SER   A O   
600  C  CB  . SER   A 73  ? 0.2318 0.1125 0.2852 -0.0208 -0.0487 0.0335  73  SER   A CB  
601  O  OG  . SER   A 73  ? 0.2502 0.1103 0.2500 0.0074  -0.0320 0.0187  73  SER   A OG  
602  N  N   . GLN   A 74  ? 0.2362 0.1126 0.2599 0.0049  -0.0276 -0.0073 74  GLN   A N   
603  C  CA  . GLN   A 74  ? 0.2575 0.1484 0.2454 0.0321  -0.0296 0.0029  74  GLN   A CA  
604  C  C   . GLN   A 74  ? 0.2299 0.1632 0.2352 0.0111  -0.0505 -0.0139 74  GLN   A C   
605  O  O   . GLN   A 74  ? 0.2328 0.1414 0.2444 -0.0065 -0.0399 -0.0270 74  GLN   A O   
606  C  CB  . GLN   A 74  ? 0.2663 0.1570 0.2999 0.0299  -0.0250 0.0089  74  GLN   A CB  
607  C  CG  . GLN   A 74  ? 0.2682 0.1818 0.3012 0.0012  -0.0206 -0.0100 74  GLN   A CG  
608  C  CD  . GLN   A 74  ? 0.2836 0.2587 0.2942 0.0198  -0.0330 0.0216  74  GLN   A CD  
609  O  OE1 . GLN   A 74  ? 0.2926 0.3128 0.3179 0.0029  -0.0122 0.0270  74  GLN   A OE1 
610  N  NE2 . GLN   A 74  ? 0.2519 0.2530 0.2850 0.0135  -0.0355 0.0044  74  GLN   A NE2 
611  N  N   . ASP   A 75  ? 0.2664 0.2055 0.2485 0.0287  -0.0584 -0.0243 75  ASP   A N   
612  C  CA  . ASP   A 75  ? 0.2520 0.2206 0.2536 0.0354  -0.0428 -0.0256 75  ASP   A CA  
613  C  C   . ASP   A 75  ? 0.2350 0.2803 0.2802 0.0504  -0.0928 -0.0460 75  ASP   A C   
614  O  O   . ASP   A 75  ? 0.2761 0.5497 0.4353 -0.0131 -0.0517 -0.1481 75  ASP   A O   
615  C  CB  . ASP   A 75  ? 0.3286 0.2542 0.2733 0.0734  -0.0439 -0.0200 75  ASP   A CB  
616  C  CG  . ASP   A 75  ? 0.3704 0.2543 0.2545 0.0370  -0.0093 -0.0515 75  ASP   A CG  
617  O  OD1 . ASP   A 75  ? 0.3903 0.4536 0.2373 -0.0117 -0.0502 -0.0746 75  ASP   A OD1 
618  O  OD2 . ASP   A 75  ? 0.4760 0.3672 0.2853 0.0547  -0.0116 -0.0720 75  ASP   A OD2 
619  N  N   . LYS   A 76  ? 0.2206 0.1894 0.2558 0.0203  -0.0679 -0.0109 76  LYS   A N   
620  C  CA  . LYS   A 76  ? 0.2049 0.1712 0.2691 0.0040  -0.0616 0.0046  76  LYS   A CA  
621  C  C   . LYS   A 76  ? 0.2023 0.1843 0.2464 0.0105  -0.0333 0.0038  76  LYS   A C   
622  O  O   . LYS   A 76  ? 0.2203 0.2845 0.2730 -0.0159 -0.0529 -0.0008 76  LYS   A O   
623  C  CB  . LYS   A 76  ? 0.2692 0.1653 0.2811 -0.0215 -0.0635 -0.0014 76  LYS   A CB  
624  C  CG  . LYS   A 76  ? 0.2746 0.1924 0.3169 -0.0129 -0.0410 0.0250  76  LYS   A CG  
625  C  CD  . LYS   A 76  ? 0.3016 0.2219 0.3200 -0.0294 -0.0158 0.0301  76  LYS   A CD  
626  C  CE  . LYS   A 76  ? 0.3151 0.2423 0.3405 -0.0135 -0.0317 0.0196  76  LYS   A CE  
627  N  NZ  . LYS   A 76  ? 0.2879 0.2207 0.3726 -0.0058 -0.0350 -0.0062 76  LYS   A NZ  
628  N  N   . ALA   A 77  ? 0.1833 0.1892 0.2351 0.0223  -0.0213 0.0334  77  ALA   A N   
629  C  CA  . ALA   A 77  ? 0.1438 0.1761 0.1757 0.0088  -0.0223 0.0187  77  ALA   A CA  
630  C  C   . ALA   A 77  ? 0.1308 0.1616 0.1947 -0.0148 -0.0200 0.0020  77  ALA   A C   
631  O  O   . ALA   A 77  ? 0.1247 0.2299 0.2157 -0.0173 0.0009  -0.0214 77  ALA   A O   
632  C  CB  . ALA   A 77  ? 0.1813 0.2259 0.1716 0.0252  -0.0343 -0.0063 77  ALA   A CB  
633  N  N   . VAL   A 78  ? 0.1363 0.1541 0.1714 -0.0002 -0.0155 0.0030  78  VAL   A N   
634  C  CA  . VAL   A 78  ? 0.1591 0.1419 0.1792 -0.0149 -0.0165 0.0019  78  VAL   A CA  
635  C  C   . VAL   A 78  ? 0.1461 0.1372 0.1794 -0.0169 -0.0153 0.0050  78  VAL   A C   
636  O  O   . VAL   A 78  ? 0.1580 0.1821 0.2011 -0.0471 -0.0388 0.0264  78  VAL   A O   
637  C  CB  . VAL   A 78  ? 0.2013 0.1696 0.2218 -0.0069 -0.0219 -0.0129 78  VAL   A CB  
638  C  CG1 . VAL   A 78  ? 0.2081 0.1496 0.2295 0.0077  -0.0203 -0.0094 78  VAL   A CG1 
639  C  CG2 . VAL   A 78  ? 0.2133 0.1899 0.2616 0.0042  0.0013  -0.0053 78  VAL   A CG2 
640  N  N   . LEU   A 79  ? 0.1281 0.1323 0.1560 -0.0169 -0.0038 0.0080  79  LEU   A N   
641  C  CA  . LEU   A 79  ? 0.1369 0.1357 0.1577 -0.0166 -0.0091 0.0032  79  LEU   A CA  
642  C  C   . LEU   A 79  ? 0.1552 0.1247 0.1495 -0.0132 -0.0044 -0.0002 79  LEU   A C   
643  O  O   . LEU   A 79  ? 0.1665 0.1482 0.1678 -0.0366 -0.0009 -0.0127 79  LEU   A O   
644  C  CB  . LEU   A 79  ? 0.1345 0.1570 0.1646 -0.0200 -0.0037 0.0023  79  LEU   A CB  
645  C  CG  . LEU   A 79  ? 0.1454 0.1606 0.1795 0.0033  0.0096  -0.0056 79  LEU   A CG  
646  C  CD1 . LEU   A 79  ? 0.1574 0.1754 0.2262 -0.0016 0.0163  0.0339  79  LEU   A CD1 
647  C  CD2 . LEU   A 79  ? 0.1479 0.1848 0.1820 0.0186  0.0071  -0.0039 79  LEU   A CD2 
648  N  N   . LYS   A 80  ? 0.1430 0.1486 0.1479 -0.0144 0.0062  -0.0092 80  LYS   A N   
649  C  CA  . LYS   A 80  ? 0.1699 0.1453 0.1677 -0.0106 0.0194  -0.0089 80  LYS   A CA  
650  C  C   . LYS   A 80  ? 0.1404 0.1436 0.1721 0.0040  0.0097  -0.0026 80  LYS   A C   
651  O  O   . LYS   A 80  ? 0.1390 0.1516 0.1707 -0.0232 -0.0053 0.0000  80  LYS   A O   
652  C  CB  . LYS   A 80  ? 0.2682 0.1712 0.2013 0.0132  0.0235  -0.0017 80  LYS   A CB  
653  C  CG  . LYS   A 80  ? 0.2628 0.2100 0.2496 -0.0098 0.0306  0.0056  80  LYS   A CG  
654  C  CD  . LYS   A 80  ? 0.2616 0.2570 0.3220 0.0171  -0.0252 0.0103  80  LYS   A CD  
655  N  N   . GLY   A 81  ? 0.1656 0.1512 0.1847 -0.0011 0.0257  0.0025  81  GLY   A N   
656  C  CA  . GLY   A 81  ? 0.1675 0.1766 0.1938 0.0034  0.0435  0.0082  81  GLY   A CA  
657  C  C   . GLY   A 81  ? 0.1519 0.1593 0.1989 -0.0001 0.0363  -0.0043 81  GLY   A C   
658  O  O   . GLY   A 81  ? 0.1425 0.1685 0.1705 -0.0225 0.0310  -0.0140 81  GLY   A O   
659  N  N   . GLY   A 82  ? 0.1352 0.1971 0.2602 -0.0015 0.0554  0.0346  82  GLY   A N   
660  C  CA  . GLY   A 82  ? 0.1653 0.1934 0.2804 0.0050  0.0528  0.0386  82  GLY   A CA  
661  C  C   . GLY   A 82  ? 0.1795 0.1781 0.2284 0.0266  0.0521  0.0109  82  GLY   A C   
662  O  O   . GLY   A 82  ? 0.2089 0.2635 0.2346 0.0459  0.0636  -0.0194 82  GLY   A O   
663  N  N   . PRO   A 83  ? 0.1535 0.1481 0.1908 0.0247  0.0376  0.0098  83  PRO   A N   
664  C  CA  . PRO   A 83  ? 0.1931 0.1859 0.1783 0.0148  0.0206  0.0046  83  PRO   A CA  
665  C  C   . PRO   A 83  ? 0.1765 0.1817 0.1899 0.0178  0.0126  -0.0113 83  PRO   A C   
666  O  O   . PRO   A 83  ? 0.2344 0.2368 0.2203 -0.0182 -0.0295 -0.0012 83  PRO   A O   
667  C  CB  . PRO   A 83  ? 0.1776 0.1926 0.1883 0.0142  0.0044  0.0293  83  PRO   A CB  
668  C  CG  . PRO   A 83  ? 0.1475 0.1727 0.1825 0.0326  0.0242  0.0233  83  PRO   A CG  
669  C  CD  . PRO   A 83  ? 0.1590 0.1450 0.1833 0.0136  0.0376  0.0102  83  PRO   A CD  
670  N  N   . LEU   A 84  ? 0.1673 0.1415 0.1544 0.0127  0.0216  -0.0168 84  LEU   A N   
671  C  CA  . LEU   A 84  ? 0.1443 0.1402 0.1619 0.0124  0.0122  -0.0218 84  LEU   A CA  
672  C  C   . LEU   A 84  ? 0.1668 0.1456 0.1808 0.0127  0.0226  -0.0391 84  LEU   A C   
673  O  O   . LEU   A 84  ? 0.1695 0.1726 0.2397 0.0219  0.0322  -0.0602 84  LEU   A O   
674  C  CB  . LEU   A 84  ? 0.1325 0.1135 0.1609 0.0088  0.0239  -0.0065 84  LEU   A CB  
675  C  CG  . LEU   A 84  ? 0.1349 0.1123 0.1420 0.0020  0.0198  -0.0196 84  LEU   A CG  
676  C  CD1 . LEU   A 84  ? 0.1464 0.1342 0.1560 0.0104  0.0051  -0.0175 84  LEU   A CD1 
677  C  CD2 . LEU   A 84  ? 0.1405 0.1201 0.1531 0.0028  0.0250  -0.0145 84  LEU   A CD2 
678  N  N   . ASP   A 85  ? 0.1998 0.1477 0.2015 -0.0059 0.0257  -0.0659 85  ASP   A N   
679  C  CA  . ASP   A 85  ? 0.2584 0.1524 0.2298 -0.0107 0.0302  -0.0797 85  ASP   A CA  
680  C  C   . ASP   A 85  ? 0.2311 0.1463 0.2868 -0.0014 0.0364  -0.0245 85  ASP   A C   
681  O  O   . ASP   A 85  ? 0.2915 0.2480 0.2860 0.0287  0.0861  -0.0283 85  ASP   A O   
682  C  CB  . ASP   A 85  ? 0.3693 0.1603 0.2892 -0.0148 -0.0079 -0.0866 85  ASP   A CB  
683  N  N   . GLY   A 86  ? 0.2619 0.1948 0.2467 -0.0446 0.0206  -0.0220 86  GLY   A N   
684  C  CA  . GLY   A 86  ? 0.3031 0.1822 0.2629 -0.0391 0.0105  -0.0396 86  GLY   A CA  
685  C  C   . GLY   A 86  ? 0.2563 0.1539 0.2377 -0.0433 0.0115  -0.0375 86  GLY   A C   
686  O  O   . GLY   A 86  ? 0.3112 0.1898 0.2449 -0.0897 -0.0045 -0.0161 86  GLY   A O   
687  N  N   . THR   A 87  ? 0.1820 0.1329 0.2046 -0.0141 0.0183  -0.0427 87  THR   A N   
688  C  CA  . THR   A 87  ? 0.1454 0.1532 0.2042 0.0040  0.0261  -0.0368 87  THR   A CA  
689  C  C   . THR   A 87  ? 0.1255 0.1073 0.1788 -0.0033 0.0078  -0.0203 87  THR   A C   
690  O  O   . THR   A 87  ? 0.1529 0.1063 0.2050 -0.0135 0.0162  -0.0244 87  THR   A O   
691  C  CB  . THR   A 87  ? 0.1614 0.2163 0.2376 0.0640  0.0098  -0.0495 87  THR   A CB  
692  O  OG1 . THR   A 87  ? 0.1995 0.2906 0.3169 0.0859  0.0107  -0.0694 87  THR   A OG1 
693  C  CG2 . THR   A 87  ? 0.1883 0.2291 0.2832 0.0612  -0.0190 -0.0327 87  THR   A CG2 
694  N  N   . TYR   A 88  ? 0.1250 0.1096 0.1615 -0.0092 0.0018  -0.0218 88  TYR   A N   
695  C  CA  . TYR   A 88  ? 0.1147 0.1054 0.1513 -0.0048 0.0044  -0.0228 88  TYR   A CA  
696  C  C   . TYR   A 88  ? 0.1142 0.1201 0.1581 0.0013  -0.0042 -0.0155 88  TYR   A C   
697  O  O   . TYR   A 88  ? 0.1418 0.1712 0.1867 -0.0420 -0.0196 0.0012  88  TYR   A O   
698  C  CB  . TYR   A 88  ? 0.1342 0.0979 0.1667 0.0105  0.0060  -0.0327 88  TYR   A CB  
699  C  CG  . TYR   A 88  ? 0.1172 0.0942 0.1463 0.0078  0.0130  -0.0209 88  TYR   A CG  
700  C  CD1 . TYR   A 88  ? 0.1268 0.1137 0.1543 0.0022  0.0175  -0.0158 88  TYR   A CD1 
701  C  CD2 . TYR   A 88  ? 0.1166 0.0912 0.1355 0.0104  0.0158  -0.0179 88  TYR   A CD2 
702  C  CE1 . TYR   A 88  ? 0.1276 0.1135 0.1366 0.0038  0.0240  -0.0185 88  TYR   A CE1 
703  C  CE2 . TYR   A 88  ? 0.1226 0.0939 0.1360 -0.0012 0.0140  -0.0088 88  TYR   A CE2 
704  C  CZ  . TYR   A 88  ? 0.1236 0.0934 0.1399 -0.0076 0.0133  -0.0182 88  TYR   A CZ  
705  O  OH  . TYR   A 88  ? 0.1243 0.1253 0.1409 -0.0023 0.0147  -0.0244 88  TYR   A OH  
706  N  N   A ARG   A 89  ? 0.1165 0.0970 0.1474 0.0082  -0.0033 -0.0213 89  ARG   A N   
707  N  N   B ARG   A 89  ? 0.1204 0.0894 0.1420 0.0059  0.0022  -0.0155 89  ARG   A N   
708  C  CA  A ARG   A 89  ? 0.1248 0.0939 0.1546 0.0151  -0.0125 -0.0093 89  ARG   A CA  
709  C  CA  B ARG   A 89  ? 0.1280 0.0898 0.1469 0.0104  0.0002  0.0003  89  ARG   A CA  
710  C  C   A ARG   A 89  ? 0.1195 0.0917 0.1173 0.0072  0.0021  -0.0041 89  ARG   A C   
711  C  C   B ARG   A 89  ? 0.1197 0.0878 0.1159 0.0033  0.0042  0.0009  89  ARG   A C   
712  O  O   A ARG   A 89  ? 0.1141 0.0912 0.1103 0.0066  0.0000  0.0046  89  ARG   A O   
713  O  O   B ARG   A 89  ? 0.1127 0.0912 0.1086 0.0047  -0.0006 0.0038  89  ARG   A O   
714  C  CB  A ARG   A 89  ? 0.1431 0.0903 0.1624 0.0314  -0.0268 -0.0091 89  ARG   A CB  
715  C  CB  B ARG   A 89  ? 0.1469 0.0940 0.1545 0.0160  0.0016  0.0052  89  ARG   A CB  
716  C  CG  A ARG   A 89  ? 0.1528 0.1093 0.1798 0.0493  -0.0374 -0.0195 89  ARG   A CG  
717  C  CG  B ARG   A 89  ? 0.1776 0.1116 0.1523 0.0257  0.0063  0.0044  89  ARG   A CG  
718  C  CD  A ARG   A 89  ? 0.1894 0.1254 0.1971 0.0417  -0.0432 -0.0133 89  ARG   A CD  
719  C  CD  B ARG   A 89  ? 0.2015 0.1342 0.1563 0.0416  -0.0003 0.0140  89  ARG   A CD  
720  N  NE  A ARG   A 89  ? 0.2196 0.1250 0.2118 0.0410  -0.0297 -0.0063 89  ARG   A NE  
721  N  NE  B ARG   A 89  ? 0.2225 0.1468 0.1378 0.0364  0.0075  0.0127  89  ARG   A NE  
722  C  CZ  A ARG   A 89  ? 0.2567 0.1283 0.2225 0.0231  -0.0122 0.0146  89  ARG   A CZ  
723  C  CZ  B ARG   A 89  ? 0.2352 0.1304 0.1322 0.0212  0.0028  0.0185  89  ARG   A CZ  
724  N  NH1 A ARG   A 89  ? 0.2590 0.0768 0.2187 -0.0005 -0.0152 0.0004  89  ARG   A NH1 
725  N  NH1 B ARG   A 89  ? 0.2526 0.1527 0.1549 0.0283  0.0208  0.0327  89  ARG   A NH1 
726  N  NH2 A ARG   A 89  ? 0.2766 0.1522 0.2629 0.0505  -0.0156 -0.0095 89  ARG   A NH2 
727  N  NH2 B ARG   A 89  ? 0.3024 0.1342 0.1682 0.0402  0.0067  0.0167  89  ARG   A NH2 
728  N  N   . LEU   A 90  ? 0.1166 0.0925 0.1249 0.0090  -0.0091 0.0004  90  LEU   A N   
729  C  CA  . LEU   A 90  ? 0.1280 0.0962 0.1177 -0.0011 -0.0123 0.0033  90  LEU   A CA  
730  C  C   . LEU   A 90  ? 0.1284 0.0922 0.1104 -0.0077 -0.0145 0.0111  90  LEU   A C   
731  O  O   . LEU   A 90  ? 0.1381 0.1344 0.1445 0.0074  -0.0104 0.0359  90  LEU   A O   
732  C  CB  . LEU   A 90  ? 0.1286 0.1084 0.1140 -0.0100 -0.0093 0.0055  90  LEU   A CB  
733  C  CG  . LEU   A 90  ? 0.1320 0.1193 0.1166 -0.0199 -0.0029 -0.0025 90  LEU   A CG  
734  C  CD1 . LEU   A 90  ? 0.1519 0.0991 0.1255 -0.0155 -0.0056 -0.0087 90  LEU   A CD1 
735  C  CD2 . LEU   A 90  ? 0.1416 0.1399 0.1283 -0.0256 -0.0025 -0.0074 90  LEU   A CD2 
736  N  N   . ILE   A 91  ? 0.1243 0.0789 0.1032 0.0063  -0.0019 0.0039  91  ILE   A N   
737  C  CA  . ILE   A 91  ? 0.1358 0.0777 0.1082 0.0054  -0.0027 0.0010  91  ILE   A CA  
738  C  C   . ILE   A 91  ? 0.1153 0.0690 0.1019 -0.0003 -0.0110 -0.0008 91  ILE   A C   
739  O  O   . ILE   A 91  ? 0.1304 0.0825 0.1003 0.0027  -0.0064 -0.0010 91  ILE   A O   
740  C  CB  . ILE   A 91  ? 0.1497 0.0833 0.1199 -0.0124 0.0033  -0.0083 91  ILE   A CB  
741  C  CG1 . ILE   A 91  ? 0.1564 0.1228 0.1333 -0.0295 0.0002  -0.0041 91  ILE   A CG1 
742  C  CG2 . ILE   A 91  ? 0.1469 0.0895 0.1154 -0.0165 -0.0015 -0.0136 91  ILE   A CG2 
743  C  CD1 . ILE   A 91  ? 0.1844 0.1618 0.1733 -0.0556 0.0049  -0.0089 91  ILE   A CD1 
744  N  N   . GLN   A 92  ? 0.1216 0.0697 0.1023 -0.0007 -0.0096 -0.0027 92  GLN   A N   
745  C  CA  . GLN   A 92  ? 0.1172 0.0697 0.0932 0.0020  -0.0015 0.0024  92  GLN   A CA  
746  C  C   . GLN   A 92  ? 0.1052 0.0731 0.0910 0.0034  -0.0061 0.0034  92  GLN   A C   
747  O  O   . GLN   A 92  ? 0.1350 0.0739 0.0921 0.0017  0.0001  0.0000  92  GLN   A O   
748  C  CB  . GLN   A 92  ? 0.1230 0.0814 0.1128 0.0007  -0.0016 0.0141  92  GLN   A CB  
749  C  CG  . GLN   A 92  ? 0.1272 0.0855 0.1465 -0.0038 -0.0072 0.0030  92  GLN   A CG  
750  C  CD  . GLN   A 92  ? 0.1164 0.1025 0.1183 -0.0021 -0.0050 0.0010  92  GLN   A CD  
751  O  OE1 . GLN   A 92  ? 0.1292 0.0898 0.1353 0.0071  -0.0173 0.0064  92  GLN   A OE1 
752  N  NE2 . GLN   A 92  ? 0.1268 0.1297 0.1725 0.0033  -0.0057 -0.0010 92  GLN   A NE2 
753  N  N   . PHE   A 93  ? 0.1086 0.0696 0.0820 0.0071  -0.0018 0.0019  93  PHE   A N   
754  C  CA  . PHE   A 93  ? 0.1040 0.0698 0.0906 0.0060  -0.0046 0.0018  93  PHE   A CA  
755  C  C   . PHE   A 93  ? 0.0964 0.0771 0.0818 -0.0014 -0.0011 0.0026  93  PHE   A C   
756  O  O   . PHE   A 93  ? 0.1050 0.0910 0.0891 0.0060  -0.0001 0.0042  93  PHE   A O   
757  C  CB  . PHE   A 93  ? 0.1100 0.0742 0.0982 -0.0003 -0.0015 0.0066  93  PHE   A CB  
758  C  CG  . PHE   A 93  ? 0.1004 0.0736 0.1015 -0.0024 0.0005  0.0016  93  PHE   A CG  
759  C  CD1 . PHE   A 93  ? 0.1179 0.0819 0.1146 0.0065  -0.0057 -0.0038 93  PHE   A CD1 
760  C  CD2 . PHE   A 93  ? 0.1138 0.0747 0.1069 0.0066  -0.0047 0.0047  93  PHE   A CD2 
761  C  CE1 . PHE   A 93  ? 0.1127 0.0796 0.1190 0.0101  -0.0074 -0.0091 93  PHE   A CE1 
762  C  CE2 . PHE   A 93  ? 0.1061 0.0966 0.1256 0.0059  -0.0113 -0.0014 93  PHE   A CE2 
763  C  CZ  . PHE   A 93  ? 0.1110 0.0909 0.1099 -0.0017 -0.0153 0.0001  93  PHE   A CZ  
764  N  N   . HIS   A 94  ? 0.0925 0.0782 0.0864 0.0078  -0.0014 0.0026  94  HIS   A N   
765  C  CA  . HIS   A 94  ? 0.0985 0.0756 0.0806 0.0053  -0.0018 -0.0006 94  HIS   A CA  
766  C  C   . HIS   A 94  ? 0.0895 0.0729 0.0757 0.0055  -0.0017 -0.0022 94  HIS   A C   
767  O  O   . HIS   A 94  ? 0.1111 0.0734 0.0861 0.0128  0.0066  0.0038  94  HIS   A O   
768  C  CB  . HIS   A 94  ? 0.1105 0.0744 0.0882 -0.0043 0.0032  0.0018  94  HIS   A CB  
769  C  CG  . HIS   A 94  ? 0.0937 0.0765 0.0870 0.0008  0.0025  0.0021  94  HIS   A CG  
770  N  ND1 . HIS   A 94  ? 0.1068 0.0760 0.0946 -0.0083 -0.0044 0.0027  94  HIS   A ND1 
771  C  CD2 . HIS   A 94  ? 0.0981 0.0807 0.0872 0.0059  -0.0028 -0.0032 94  HIS   A CD2 
772  C  CE1 . HIS   A 94  ? 0.1125 0.0679 0.0864 -0.0025 0.0044  -0.0058 94  HIS   A CE1 
773  N  NE2 . HIS   A 94  ? 0.0905 0.0721 0.0770 0.0057  -0.0078 0.0043  94  HIS   A NE2 
774  N  N   . PHE   A 95  ? 0.0968 0.0708 0.0873 0.0036  0.0061  0.0050  95  PHE   A N   
775  C  CA  . PHE   A 95  ? 0.0976 0.0716 0.0814 0.0035  0.0043  0.0044  95  PHE   A CA  
776  C  C   . PHE   A 95  ? 0.1007 0.0720 0.0858 -0.0005 0.0035  -0.0031 95  PHE   A C   
777  O  O   . PHE   A 95  ? 0.0981 0.0867 0.1009 0.0003  0.0030  0.0070  95  PHE   A O   
778  C  CB  . PHE   A 95  ? 0.0973 0.0738 0.0985 0.0026  0.0071  0.0003  95  PHE   A CB  
779  C  CG  . PHE   A 95  ? 0.1032 0.0735 0.0984 0.0037  -0.0039 -0.0108 95  PHE   A CG  
780  C  CD1 . PHE   A 95  ? 0.1056 0.0899 0.0991 0.0048  -0.0056 -0.0065 95  PHE   A CD1 
781  C  CD2 . PHE   A 95  ? 0.1141 0.0842 0.1094 -0.0020 -0.0030 -0.0122 95  PHE   A CD2 
782  C  CE1 . PHE   A 95  ? 0.1153 0.1012 0.1118 0.0104  -0.0147 -0.0010 95  PHE   A CE1 
783  C  CE2 . PHE   A 95  ? 0.1112 0.0951 0.1275 -0.0012 0.0030  -0.0209 95  PHE   A CE2 
784  C  CZ  . PHE   A 95  ? 0.1020 0.1095 0.1262 0.0121  -0.0146 -0.0256 95  PHE   A CZ  
785  N  N   . HIS   A 96  ? 0.0901 0.0723 0.0929 0.0003  0.0057  0.0020  96  HIS   A N   
786  C  CA  . HIS   A 96  ? 0.0877 0.0764 0.0890 0.0031  0.0066  0.0003  96  HIS   A CA  
787  C  C   . HIS   A 96  ? 0.0973 0.0727 0.0927 0.0056  0.0045  -0.0019 96  HIS   A C   
788  O  O   . HIS   A 96  ? 0.0979 0.0816 0.1027 0.0036  0.0105  -0.0043 96  HIS   A O   
789  C  CB  . HIS   A 96  ? 0.1020 0.0787 0.1027 0.0046  0.0020  -0.0002 96  HIS   A CB  
790  C  CG  . HIS   A 96  ? 0.0928 0.0788 0.0954 0.0035  -0.0060 -0.0023 96  HIS   A CG  
791  N  ND1 . HIS   A 96  ? 0.0956 0.0784 0.1272 0.0001  -0.0033 -0.0090 96  HIS   A ND1 
792  C  CD2 . HIS   A 96  ? 0.0957 0.0741 0.1026 -0.0005 0.0000  -0.0034 96  HIS   A CD2 
793  C  CE1 . HIS   A 96  ? 0.0897 0.0749 0.1228 -0.0010 0.0002  -0.0111 96  HIS   A CE1 
794  N  NE2 . HIS   A 96  ? 0.0917 0.0743 0.0983 0.0010  0.0006  -0.0023 96  HIS   A NE2 
795  N  N   . TRP   A 97  ? 0.0903 0.0718 0.0897 -0.0013 0.0109  -0.0029 97  TRP   A N   
796  C  CA  . TRP   A 97  ? 0.1032 0.0726 0.0944 -0.0003 0.0008  -0.0073 97  TRP   A CA  
797  C  C   . TRP   A 97  ? 0.0946 0.0671 0.0900 0.0003  0.0063  -0.0050 97  TRP   A C   
798  O  O   . TRP   A 97  ? 0.0978 0.0764 0.1097 0.0052  0.0112  0.0017  97  TRP   A O   
799  C  CB  . TRP   A 97  ? 0.0977 0.0788 0.1063 0.0045  0.0010  -0.0084 97  TRP   A CB  
800  C  CG  . TRP   A 97  ? 0.1066 0.0727 0.0954 0.0016  -0.0026 -0.0079 97  TRP   A CG  
801  C  CD1 . TRP   A 97  ? 0.1192 0.0851 0.0993 0.0053  0.0049  -0.0069 97  TRP   A CD1 
802  C  CD2 . TRP   A 97  ? 0.1062 0.0793 0.0928 -0.0005 -0.0006 0.0003  97  TRP   A CD2 
803  N  NE1 . TRP   A 97  ? 0.1175 0.0969 0.0928 0.0081  0.0125  -0.0076 97  TRP   A NE1 
804  C  CE2 . TRP   A 97  ? 0.1073 0.0846 0.0901 -0.0012 0.0010  -0.0049 97  TRP   A CE2 
805  C  CE3 . TRP   A 97  ? 0.1064 0.0877 0.0863 0.0043  -0.0014 -0.0019 97  TRP   A CE3 
806  C  CZ2 . TRP   A 97  ? 0.1146 0.1012 0.0915 0.0020  0.0088  0.0047  97  TRP   A CZ2 
807  C  CZ3 . TRP   A 97  ? 0.1220 0.0843 0.0986 0.0055  -0.0002 0.0001  97  TRP   A CZ3 
808  C  CH2 . TRP   A 97  ? 0.1217 0.0890 0.1025 0.0031  0.0043  0.0062  97  TRP   A CH2 
809  N  N   . GLY   A 98  ? 0.1092 0.0776 0.1033 -0.0027 0.0050  -0.0024 98  GLY   A N   
810  C  CA  . GLY   A 98  ? 0.1242 0.0754 0.1083 0.0005  0.0112  0.0039  98  GLY   A CA  
811  C  C   . GLY   A 98  ? 0.1279 0.0813 0.1188 0.0008  0.0047  -0.0026 98  GLY   A C   
812  O  O   . GLY   A 98  ? 0.1498 0.0833 0.1260 0.0076  -0.0038 -0.0114 98  GLY   A O   
813  N  N   . SER   A 99  ? 0.1358 0.0849 0.1177 0.0104  0.0005  -0.0158 99  SER   A N   
814  C  CA  . SER   A 99  ? 0.1529 0.0991 0.1311 0.0198  0.0016  -0.0234 99  SER   A CA  
815  C  C   . SER   A 99  ? 0.1759 0.0933 0.1564 0.0155  -0.0047 -0.0362 99  SER   A C   
816  O  O   . SER   A 99  ? 0.1980 0.1268 0.2014 0.0133  -0.0092 -0.0681 99  SER   A O   
817  C  CB  . SER   A 99  ? 0.1661 0.0981 0.1459 0.0182  0.0177  -0.0217 99  SER   A CB  
818  O  OG  . SER   A 99  ? 0.1435 0.1062 0.1916 0.0226  0.0175  -0.0099 99  SER   A OG  
819  N  N   . LEU   A 100 ? 0.1513 0.0871 0.1799 -0.0030 0.0136  -0.0297 100 LEU   A N   
820  C  CA  . LEU   A 100 ? 0.1734 0.0799 0.2357 0.0087  0.0315  -0.0278 100 LEU   A CA  
821  C  C   . LEU   A 100 ? 0.1645 0.0783 0.1983 0.0016  0.0103  -0.0185 100 LEU   A C   
822  O  O   . LEU   A 100 ? 0.1759 0.0835 0.1795 0.0020  0.0070  -0.0173 100 LEU   A O   
823  C  CB  . LEU   A 100 ? 0.2512 0.1231 0.2523 0.0288  0.0532  -0.0101 100 LEU   A CB  
824  C  CG  . LEU   A 100 ? 0.2670 0.1696 0.2316 0.0420  0.0408  -0.0137 100 LEU   A CG  
825  C  CD1 . LEU   A 100 ? 0.2740 0.2638 0.3068 0.1045  0.0184  -0.0026 100 LEU   A CD1 
826  C  CD2 . LEU   A 100 ? 0.2998 0.2008 0.2873 0.0429  0.0667  -0.0762 100 LEU   A CD2 
827  N  N   . ASP   A 101 ? 0.1587 0.0782 0.1962 -0.0025 0.0094  -0.0216 101 ASP   A N   
828  C  CA  . ASP   A 101 ? 0.1622 0.0953 0.1849 -0.0108 0.0059  0.0044  101 ASP   A CA  
829  C  C   . ASP   A 101 ? 0.1799 0.0963 0.1934 -0.0163 0.0046  0.0056  101 ASP   A C   
830  O  O   . ASP   A 101 ? 0.2431 0.1417 0.1732 0.0058  0.0187  0.0162  101 ASP   A O   
831  C  CB  . ASP   A 101 ? 0.1657 0.1090 0.2034 -0.0136 0.0111  0.0207  101 ASP   A CB  
832  C  CG  . ASP   A 101 ? 0.1897 0.1311 0.2168 -0.0206 0.0019  -0.0075 101 ASP   A CG  
833  O  OD1 . ASP   A 101 ? 0.2127 0.1540 0.1840 -0.0201 0.0049  -0.0101 101 ASP   A OD1 
834  O  OD2 . ASP   A 101 ? 0.2280 0.1919 0.2844 -0.0453 -0.0135 -0.0261 101 ASP   A OD2 
835  N  N   . GLY   A 102 ? 0.1947 0.1038 0.2050 -0.0241 -0.0149 0.0269  102 GLY   A N   
836  C  CA  . GLY   A 102 ? 0.2169 0.1385 0.2203 -0.0522 -0.0147 0.0490  102 GLY   A CA  
837  C  C   . GLY   A 102 ? 0.1881 0.1317 0.1772 -0.0265 -0.0049 0.0319  102 GLY   A C   
838  O  O   . GLY   A 102 ? 0.2157 0.1580 0.1725 -0.0302 -0.0008 0.0530  102 GLY   A O   
839  N  N   . GLN   A 103 ? 0.1597 0.1151 0.1429 -0.0236 0.0041  0.0204  103 GLN   A N   
840  C  CA  . GLN   A 103 ? 0.1409 0.0882 0.1253 -0.0037 0.0147  -0.0025 103 GLN   A CA  
841  C  C   . GLN   A 103 ? 0.1274 0.0896 0.1166 -0.0041 0.0182  -0.0023 103 GLN   A C   
842  O  O   . GLN   A 103 ? 0.1373 0.0996 0.1232 -0.0069 0.0123  -0.0056 103 GLN   A O   
843  C  CB  . GLN   A 103 ? 0.1512 0.0932 0.1338 0.0070  0.0166  0.0054  103 GLN   A CB  
844  C  CG  . GLN   A 103 ? 0.1634 0.1015 0.1521 0.0176  0.0281  0.0157  103 GLN   A CG  
845  C  CD  . GLN   A 103 ? 0.1982 0.1229 0.1862 0.0554  0.0416  0.0486  103 GLN   A CD  
846  O  OE1 . GLN   A 103 ? 0.2683 0.1818 0.2907 0.0903  0.0696  0.0960  103 GLN   A OE1 
847  N  NE2 . GLN   A 103 ? 0.1918 0.1374 0.2045 0.0540  0.0483  0.0466  103 GLN   A NE2 
848  N  N   . GLY   A 104 ? 0.1160 0.0899 0.1054 -0.0012 0.0076  -0.0049 104 GLY   A N   
849  C  CA  . GLY   A 104 ? 0.1084 0.0863 0.1084 0.0028  0.0088  0.0002  104 GLY   A CA  
850  C  C   . GLY   A 104 ? 0.1040 0.0918 0.1036 -0.0027 0.0007  0.0055  104 GLY   A C   
851  O  O   . GLY   A 104 ? 0.1221 0.0937 0.1128 -0.0037 0.0070  0.0057  104 GLY   A O   
852  N  N   . SER   A 105 ? 0.1153 0.0836 0.1005 -0.0064 0.0115  -0.0017 105 SER   A N   
853  C  CA  . SER   A 105 ? 0.1113 0.0790 0.1099 0.0006  0.0018  -0.0018 105 SER   A CA  
854  C  C   . SER   A 105 ? 0.0996 0.0863 0.0967 -0.0067 0.0057  -0.0030 105 SER   A C   
855  O  O   . SER   A 105 ? 0.1219 0.0867 0.1187 0.0083  -0.0080 -0.0047 105 SER   A O   
856  C  CB  . SER   A 105 ? 0.1115 0.0822 0.1072 -0.0009 0.0023  0.0009  105 SER   A CB  
857  O  OG  . SER   A 105 ? 0.1219 0.0858 0.1129 -0.0004 0.0056  0.0041  105 SER   A OG  
858  N  N   . GLU   A 106 ? 0.1045 0.0784 0.1067 0.0011  0.0027  -0.0022 106 GLU   A N   
859  C  CA  . GLU   A 106 ? 0.0986 0.0847 0.0938 -0.0046 0.0044  -0.0023 106 GLU   A CA  
860  C  C   . GLU   A 106 ? 0.1034 0.0780 0.0946 0.0001  0.0006  -0.0015 106 GLU   A C   
861  O  O   . GLU   A 106 ? 0.1146 0.0960 0.0981 0.0058  -0.0007 0.0023  106 GLU   A O   
862  C  CB  . GLU   A 106 ? 0.1092 0.0851 0.0976 -0.0078 0.0025  -0.0005 106 GLU   A CB  
863  C  CG  . GLU   A 106 ? 0.1331 0.0920 0.1071 -0.0036 0.0148  -0.0031 106 GLU   A CG  
864  C  CD  . GLU   A 106 ? 0.1063 0.0901 0.1037 -0.0020 0.0009  -0.0007 106 GLU   A CD  
865  O  OE1 . GLU   A 106 ? 0.0957 0.0857 0.1200 -0.0007 0.0029  -0.0045 106 GLU   A OE1 
866  O  OE2 . GLU   A 106 ? 0.1077 0.1121 0.1336 0.0079  0.0135  -0.0027 106 GLU   A OE2 
867  N  N   . HIS   A 107 ? 0.1054 0.0842 0.0941 0.0034  0.0018  0.0065  107 HIS   A N   
868  C  CA  . HIS   A 107 ? 0.1002 0.0881 0.0921 -0.0005 0.0002  0.0020  107 HIS   A CA  
869  C  C   . HIS   A 107 ? 0.1045 0.0926 0.0937 0.0015  0.0025  0.0022  107 HIS   A C   
870  O  O   . HIS   A 107 ? 0.1193 0.0877 0.0997 -0.0063 0.0025  0.0022  107 HIS   A O   
871  C  CB  . HIS   A 107 ? 0.1023 0.0939 0.0904 -0.0043 0.0051  0.0014  107 HIS   A CB  
872  C  CG  . HIS   A 107 ? 0.0960 0.0913 0.0970 0.0085  0.0031  0.0021  107 HIS   A CG  
873  N  ND1 . HIS   A 107 ? 0.1102 0.0822 0.1025 0.0034  -0.0019 0.0047  107 HIS   A ND1 
874  C  CD2 . HIS   A 107 ? 0.1006 0.0941 0.0910 0.0095  0.0001  -0.0011 107 HIS   A CD2 
875  C  CE1 . HIS   A 107 ? 0.1273 0.0804 0.1117 0.0072  -0.0033 0.0007  107 HIS   A CE1 
876  N  NE2 . HIS   A 107 ? 0.1111 0.0951 0.0973 0.0095  -0.0002 -0.0048 107 HIS   A NE2 
877  N  N   . THR   A 108 ? 0.1214 0.0840 0.0983 -0.0057 -0.0005 0.0089  108 THR   A N   
878  C  CA  . THR   A 108 ? 0.1255 0.0841 0.1075 0.0024  0.0123  0.0152  108 THR   A CA  
879  C  C   . THR   A 108 ? 0.1166 0.0867 0.1050 0.0039  -0.0016 0.0117  108 THR   A C   
880  O  O   . THR   A 108 ? 0.1238 0.0980 0.1093 0.0025  0.0072  0.0060  108 THR   A O   
881  C  CB  . THR   A 108 ? 0.1313 0.0931 0.1148 0.0106  0.0068  0.0056  108 THR   A CB  
882  O  OG1 . THR   A 108 ? 0.1371 0.1132 0.1244 0.0179  0.0031  0.0106  108 THR   A OG1 
883  C  CG2 . THR   A 108 ? 0.1337 0.1187 0.1284 0.0115  0.0088  0.0025  108 THR   A CG2 
884  N  N   . VAL   A 109 ? 0.1245 0.0947 0.1145 -0.0023 0.0112  0.0095  109 VAL   A N   
885  C  CA  . VAL   A 109 ? 0.1359 0.1059 0.1167 -0.0002 0.0080  0.0197  109 VAL   A CA  
886  C  C   . VAL   A 109 ? 0.1413 0.1053 0.1221 0.0003  0.0124  0.0151  109 VAL   A C   
887  O  O   . VAL   A 109 ? 0.1533 0.1026 0.1363 -0.0019 0.0077  0.0219  109 VAL   A O   
888  C  CB  . VAL   A 109 ? 0.1304 0.1259 0.1305 0.0029  0.0089  0.0296  109 VAL   A CB  
889  C  CG1 . VAL   A 109 ? 0.1424 0.1553 0.1480 0.0088  0.0201  0.0376  109 VAL   A CG1 
890  C  CG2 . VAL   A 109 ? 0.1368 0.1305 0.1410 0.0035  0.0117  0.0335  109 VAL   A CG2 
891  N  N   . ASP   A 110 ? 0.1565 0.1118 0.1176 0.0061  0.0139  0.0229  110 ASP   A N   
892  C  CA  . ASP   A 110 ? 0.1670 0.1255 0.1355 0.0070  0.0099  0.0357  110 ASP   A CA  
893  C  C   . ASP   A 110 ? 0.1803 0.0988 0.1323 0.0093  0.0102  0.0360  110 ASP   A C   
894  O  O   . ASP   A 110 ? 0.1938 0.1140 0.1596 0.0176  0.0127  0.0403  110 ASP   A O   
895  C  CB  . ASP   A 110 ? 0.1996 0.1387 0.1479 -0.0043 0.0182  0.0528  110 ASP   A CB  
896  C  CG  . ASP   A 110 ? 0.1790 0.1694 0.1414 -0.0106 0.0125  0.0437  110 ASP   A CG  
897  O  OD1 . ASP   A 110 ? 0.1866 0.1821 0.1642 0.0058  0.0348  0.0308  110 ASP   A OD1 
898  O  OD2 . ASP   A 110 ? 0.1979 0.2366 0.1891 -0.0076 0.0313  0.0294  110 ASP   A OD2 
899  N  N   . LYS   A 111 ? 0.1564 0.1125 0.1305 0.0073  0.0139  0.0212  111 LYS   A N   
900  C  CA  . LYS   A 111 ? 0.1671 0.1101 0.1389 0.0179  0.0172  0.0256  111 LYS   A CA  
901  C  C   . LYS   A 111 ? 0.1715 0.0979 0.1269 0.0107  0.0231  0.0158  111 LYS   A C   
902  O  O   . LYS   A 111 ? 0.1800 0.1359 0.1594 0.0229  0.0303  0.0106  111 LYS   A O   
903  C  CB  . LYS   A 111 ? 0.1735 0.1477 0.1678 0.0286  0.0068  0.0383  111 LYS   A CB  
904  C  CG  . LYS   A 111 ? 0.2055 0.2007 0.1855 0.0613  -0.0169 0.0352  111 LYS   A CG  
905  C  CD  . LYS   A 111 ? 0.2577 0.2916 0.2311 0.0247  -0.0350 0.0095  111 LYS   A CD  
906  C  CE  . LYS   A 111 ? 0.3078 0.3601 0.2529 0.0348  -0.0523 0.0187  111 LYS   A CE  
907  N  NZ  . LYS   A 111 ? 0.3436 0.4408 0.3350 0.0493  -0.0774 0.0433  111 LYS   A NZ  
908  N  N   . LYS   A 112 ? 0.1741 0.1056 0.1200 0.0065  0.0165  0.0107  112 LYS   A N   
909  C  CA  . LYS   A 112 ? 0.1790 0.0986 0.1411 -0.0012 0.0097  0.0132  112 LYS   A CA  
910  C  C   . LYS   A 112 ? 0.1484 0.0914 0.1419 0.0100  0.0018  0.0123  112 LYS   A C   
911  O  O   . LYS   A 112 ? 0.1562 0.0925 0.1343 -0.0002 0.0044  0.0051  112 LYS   A O   
912  C  CB  . LYS   A 112 ? 0.1922 0.1231 0.1635 -0.0353 0.0151  -0.0050 112 LYS   A CB  
913  C  CG  . LYS   A 112 ? 0.2030 0.1663 0.1970 -0.0564 0.0259  -0.0238 112 LYS   A CG  
914  C  CD  . LYS   A 112 ? 0.2557 0.2009 0.2585 -0.0436 0.0032  -0.0051 112 LYS   A CD  
915  C  CE  . LYS   A 112 ? 0.2799 0.2602 0.2755 -0.0218 -0.0071 -0.0031 112 LYS   A CE  
916  N  NZ  . LYS   A 112 ? 0.3031 0.3261 0.3286 -0.0154 -0.0593 0.0122  112 LYS   A NZ  
917  N  N   A LYS   A 113 ? 0.1519 0.0942 0.1341 0.0163  0.0033  0.0157  113 LYS   A N   
918  N  N   B LYS   A 113 ? 0.1577 0.0885 0.1350 0.0217  0.0007  0.0140  113 LYS   A N   
919  C  CA  A LYS   A 113 ? 0.1566 0.0917 0.1245 0.0177  -0.0013 0.0105  113 LYS   A CA  
920  C  CA  B LYS   A 113 ? 0.1613 0.0919 0.1267 0.0192  -0.0038 0.0125  113 LYS   A CA  
921  C  C   A LYS   A 113 ? 0.1442 0.0749 0.1367 0.0100  0.0129  0.0104  113 LYS   A C   
922  C  C   B LYS   A 113 ? 0.1469 0.0804 0.1292 0.0120  0.0116  0.0084  113 LYS   A C   
923  O  O   A LYS   A 113 ? 0.1496 0.0835 0.1456 -0.0028 0.0124  0.0092  113 LYS   A O   
924  O  O   B LYS   A 113 ? 0.1492 0.0785 0.1387 0.0121  0.0130  0.0035  113 LYS   A O   
925  C  CB  A LYS   A 113 ? 0.1497 0.1113 0.1242 0.0158  -0.0052 0.0019  113 LYS   A CB  
926  C  CB  B LYS   A 113 ? 0.1588 0.1147 0.1340 0.0156  -0.0062 0.0033  113 LYS   A CB  
927  C  CG  A LYS   A 113 ? 0.1472 0.1228 0.1200 0.0220  0.0046  -0.0052 113 LYS   A CG  
928  C  CG  B LYS   A 113 ? 0.1579 0.1214 0.1520 0.0145  -0.0050 0.0073  113 LYS   A CG  
929  C  CD  A LYS   A 113 ? 0.1523 0.1303 0.1462 0.0346  0.0063  -0.0038 113 LYS   A CD  
930  C  CD  B LYS   A 113 ? 0.1596 0.1441 0.1803 0.0140  -0.0056 -0.0039 113 LYS   A CD  
931  C  CE  A LYS   A 113 ? 0.1654 0.1641 0.1630 0.0335  -0.0004 -0.0181 113 LYS   A CE  
932  C  CE  B LYS   A 113 ? 0.1671 0.1781 0.1904 0.0007  -0.0053 0.0033  113 LYS   A CE  
933  N  NZ  A LYS   A 113 ? 0.1796 0.1844 0.1770 0.0499  0.0024  -0.0098 113 LYS   A NZ  
934  N  NZ  B LYS   A 113 ? 0.1958 0.1966 0.2305 0.0095  0.0051  -0.0081 113 LYS   A NZ  
935  N  N   . TYR   A 114 ? 0.1352 0.0742 0.1299 0.0035  0.0024  0.0044  114 TYR   A N   
936  C  CA  . TYR   A 114 ? 0.1191 0.0787 0.1331 -0.0053 0.0019  0.0052  114 TYR   A CA  
937  C  C   . TYR   A 114 ? 0.1175 0.0775 0.1307 -0.0033 0.0074  0.0023  114 TYR   A C   
938  O  O   . TYR   A 114 ? 0.1110 0.0925 0.1315 -0.0052 0.0116  -0.0072 114 TYR   A O   
939  C  CB  . TYR   A 114 ? 0.1203 0.0834 0.1345 -0.0016 0.0139  0.0066  114 TYR   A CB  
940  C  CG  . TYR   A 114 ? 0.1296 0.0844 0.1305 0.0124  0.0040  0.0103  114 TYR   A CG  
941  C  CD1 . TYR   A 114 ? 0.1697 0.0977 0.1350 0.0055  0.0154  0.0091  114 TYR   A CD1 
942  C  CD2 . TYR   A 114 ? 0.1322 0.1185 0.1468 -0.0042 0.0185  0.0123  114 TYR   A CD2 
943  C  CE1 . TYR   A 114 ? 0.2015 0.1468 0.1333 0.0268  0.0200  0.0119  114 TYR   A CE1 
944  C  CE2 . TYR   A 114 ? 0.1518 0.1422 0.1968 -0.0038 0.0316  0.0180  114 TYR   A CE2 
945  C  CZ  . TYR   A 114 ? 0.1844 0.1693 0.1684 0.0203  0.0453  0.0364  114 TYR   A CZ  
946  O  OH  . TYR   A 114 ? 0.2358 0.2698 0.2022 0.0333  0.0749  0.0627  114 TYR   A OH  
947  N  N   . ALA   A 115 ? 0.1083 0.0833 0.1274 -0.0072 0.0065  -0.0028 115 ALA   A N   
948  C  CA  . ALA   A 115 ? 0.1232 0.0727 0.1257 -0.0028 0.0051  -0.0120 115 ALA   A CA  
949  C  C   . ALA   A 115 ? 0.1156 0.0745 0.1135 0.0003  0.0093  -0.0044 115 ALA   A C   
950  O  O   . ALA   A 115 ? 0.1139 0.0787 0.1275 -0.0008 0.0148  -0.0093 115 ALA   A O   
951  C  CB  . ALA   A 115 ? 0.1346 0.0877 0.1335 -0.0150 0.0081  -0.0047 115 ALA   A CB  
952  N  N   . ALA   A 116 ? 0.1128 0.0741 0.1171 -0.0022 0.0143  -0.0011 116 ALA   A N   
953  C  CA  . ALA   A 116 ? 0.1069 0.0740 0.1030 -0.0053 0.0096  -0.0022 116 ALA   A CA  
954  C  C   . ALA   A 116 ? 0.0941 0.0733 0.0956 0.0028  0.0040  0.0015  116 ALA   A C   
955  O  O   . ALA   A 116 ? 0.1077 0.0768 0.1086 -0.0015 0.0086  0.0005  116 ALA   A O   
956  C  CB  . ALA   A 116 ? 0.1020 0.0825 0.1099 -0.0023 0.0062  -0.0089 116 ALA   A CB  
957  N  N   . GLU   A 117 ? 0.0951 0.0715 0.0936 0.0037  0.0123  0.0049  117 GLU   A N   
958  C  CA  . GLU   A 117 ? 0.1001 0.0741 0.0983 0.0018  0.0105  0.0026  117 GLU   A CA  
959  C  C   . GLU   A 117 ? 0.0989 0.0832 0.0875 0.0025  0.0101  -0.0002 117 GLU   A C   
960  O  O   . GLU   A 117 ? 0.0994 0.0995 0.1262 0.0147  0.0167  0.0216  117 GLU   A O   
961  C  CB  . GLU   A 117 ? 0.1122 0.0833 0.0978 -0.0018 0.0037  0.0031  117 GLU   A CB  
962  C  CG  . GLU   A 117 ? 0.1100 0.0971 0.1045 -0.0043 -0.0015 0.0076  117 GLU   A CG  
963  C  CD  . GLU   A 117 ? 0.1125 0.0850 0.0957 -0.0022 0.0022  0.0056  117 GLU   A CD  
964  O  OE1 . GLU   A 117 ? 0.1289 0.1096 0.1118 0.0071  -0.0081 0.0010  117 GLU   A OE1 
965  O  OE2 . GLU   A 117 ? 0.1395 0.0953 0.0976 -0.0048 -0.0124 0.0003  117 GLU   A OE2 
966  N  N   . LEU   A 118 ? 0.0917 0.0753 0.0915 0.0002  0.0034  -0.0048 118 LEU   A N   
967  C  CA  . LEU   A 118 ? 0.0890 0.0685 0.0867 0.0050  0.0022  0.0048  118 LEU   A CA  
968  C  C   . LEU   A 118 ? 0.0804 0.0666 0.0868 0.0037  0.0051  0.0001  118 LEU   A C   
969  O  O   . LEU   A 118 ? 0.0958 0.0753 0.0900 -0.0030 0.0023  -0.0005 118 LEU   A O   
970  C  CB  . LEU   A 118 ? 0.0996 0.0821 0.0985 -0.0027 -0.0032 0.0057  118 LEU   A CB  
971  C  CG  . LEU   A 118 ? 0.0943 0.0919 0.1020 0.0046  -0.0106 -0.0007 118 LEU   A CG  
972  C  CD1 . LEU   A 118 ? 0.1105 0.0861 0.1084 0.0027  -0.0128 0.0004  118 LEU   A CD1 
973  C  CD2 . LEU   A 118 ? 0.1005 0.1165 0.1196 0.0049  -0.0086 0.0043  118 LEU   A CD2 
974  N  N   . HIS   A 119 ? 0.0824 0.0653 0.0813 -0.0020 0.0015  -0.0046 119 HIS   A N   
975  C  CA  . HIS   A 119 ? 0.0864 0.0665 0.0813 0.0003  0.0011  -0.0012 119 HIS   A CA  
976  C  C   . HIS   A 119 ? 0.0836 0.0677 0.0777 -0.0087 -0.0027 -0.0036 119 HIS   A C   
977  O  O   . HIS   A 119 ? 0.0982 0.0882 0.0872 0.0089  0.0046  0.0011  119 HIS   A O   
978  C  CB  . HIS   A 119 ? 0.0950 0.0711 0.0876 0.0008  0.0026  -0.0007 119 HIS   A CB  
979  C  CG  . HIS   A 119 ? 0.0806 0.0744 0.0888 -0.0007 0.0037  -0.0040 119 HIS   A CG  
980  N  ND1 . HIS   A 119 ? 0.0754 0.0804 0.0888 -0.0063 0.0048  -0.0007 119 HIS   A ND1 
981  C  CD2 . HIS   A 119 ? 0.0814 0.0876 0.0956 0.0030  -0.0039 0.0061  119 HIS   A CD2 
982  C  CE1 . HIS   A 119 ? 0.0864 0.0802 0.0972 0.0052  -0.0077 -0.0024 119 HIS   A CE1 
983  N  NE2 . HIS   A 119 ? 0.0910 0.0929 0.0999 0.0051  -0.0036 0.0016  119 HIS   A NE2 
984  N  N   . LEU   A 120 ? 0.0867 0.0699 0.0881 0.0030  -0.0001 0.0005  120 LEU   A N   
985  C  CA  . LEU   A 120 ? 0.0880 0.0709 0.0856 0.0074  -0.0055 0.0004  120 LEU   A CA  
986  C  C   . LEU   A 120 ? 0.0829 0.0665 0.0908 0.0096  -0.0011 -0.0005 120 LEU   A C   
987  O  O   . LEU   A 120 ? 0.0918 0.0776 0.0908 0.0006  0.0011  -0.0012 120 LEU   A O   
988  C  CB  . LEU   A 120 ? 0.0946 0.0782 0.1092 0.0068  -0.0022 -0.0008 120 LEU   A CB  
989  C  CG  . LEU   A 120 ? 0.1085 0.0915 0.1156 -0.0012 -0.0058 -0.0049 120 LEU   A CG  
990  C  CD1 . LEU   A 120 ? 0.1783 0.1336 0.1368 -0.0515 -0.0040 -0.0094 120 LEU   A CD1 
991  C  CD2 . LEU   A 120 ? 0.1145 0.1254 0.1302 0.0080  -0.0243 -0.0212 120 LEU   A CD2 
992  N  N   . VAL   A 121 ? 0.0958 0.0715 0.0863 -0.0022 -0.0039 0.0013  121 VAL   A N   
993  C  CA  . VAL   A 121 ? 0.0929 0.0736 0.0871 -0.0032 -0.0078 0.0027  121 VAL   A CA  
994  C  C   . VAL   A 121 ? 0.0965 0.0775 0.0959 -0.0013 -0.0010 -0.0028 121 VAL   A C   
995  O  O   . VAL   A 121 ? 0.1140 0.0825 0.0989 0.0055  -0.0037 -0.0027 121 VAL   A O   
996  C  CB  . VAL   A 121 ? 0.1077 0.0772 0.0972 -0.0088 -0.0011 -0.0012 121 VAL   A CB  
997  C  CG1 . VAL   A 121 ? 0.1012 0.0886 0.1147 -0.0099 0.0101  -0.0047 121 VAL   A CG1 
998  C  CG2 . VAL   A 121 ? 0.1045 0.0861 0.1002 -0.0039 -0.0006 -0.0006 121 VAL   A CG2 
999  N  N   . HIS   A 122 ? 0.0963 0.0741 0.0970 0.0007  -0.0062 -0.0011 122 HIS   A N   
1000 C  CA  . HIS   A 122 ? 0.1001 0.0688 0.1049 0.0015  -0.0031 0.0001  122 HIS   A CA  
1001 C  C   . HIS   A 122 ? 0.1067 0.0703 0.1071 -0.0018 0.0066  -0.0024 122 HIS   A C   
1002 O  O   . HIS   A 122 ? 0.1174 0.0832 0.1154 -0.0112 -0.0113 0.0026  122 HIS   A O   
1003 C  CB  . HIS   A 122 ? 0.1020 0.0700 0.1118 0.0091  -0.0071 -0.0076 122 HIS   A CB  
1004 C  CG  . HIS   A 122 ? 0.1055 0.0751 0.1120 0.0039  0.0052  -0.0054 122 HIS   A CG  
1005 N  ND1 . HIS   A 122 ? 0.1024 0.0758 0.1184 -0.0066 0.0026  -0.0041 122 HIS   A ND1 
1006 C  CD2 . HIS   A 122 ? 0.1133 0.0884 0.1153 0.0059  0.0068  0.0009  122 HIS   A CD2 
1007 C  CE1 . HIS   A 122 ? 0.1026 0.0834 0.1260 -0.0039 0.0064  -0.0065 122 HIS   A CE1 
1008 N  NE2 . HIS   A 122 ? 0.1015 0.1025 0.1201 -0.0077 -0.0018 -0.0047 122 HIS   A NE2 
1009 N  N   . TRP   A 123 ? 0.1121 0.0711 0.1136 0.0026  -0.0059 -0.0090 123 TRP   A N   
1010 C  CA  . TRP   A 123 ? 0.1115 0.0715 0.1145 0.0002  -0.0040 -0.0073 123 TRP   A CA  
1011 C  C   . TRP   A 123 ? 0.1052 0.0719 0.1178 0.0050  -0.0019 -0.0078 123 TRP   A C   
1012 O  O   . TRP   A 123 ? 0.1102 0.0773 0.1375 0.0012  -0.0055 -0.0097 123 TRP   A O   
1013 C  CB  . TRP   A 123 ? 0.1278 0.1005 0.1306 -0.0110 0.0072  -0.0137 123 TRP   A CB  
1014 C  CG  . TRP   A 123 ? 0.1358 0.0830 0.1323 -0.0166 0.0006  -0.0090 123 TRP   A CG  
1015 C  CD1 . TRP   A 123 ? 0.1583 0.0849 0.1309 -0.0023 -0.0042 -0.0089 123 TRP   A CD1 
1016 C  CD2 . TRP   A 123 ? 0.1539 0.0848 0.1310 -0.0226 0.0091  -0.0103 123 TRP   A CD2 
1017 N  NE1 . TRP   A 123 ? 0.1760 0.0907 0.1322 -0.0054 -0.0167 -0.0090 123 TRP   A NE1 
1018 C  CE2 . TRP   A 123 ? 0.1758 0.0849 0.1434 -0.0103 -0.0037 -0.0044 123 TRP   A CE2 
1019 C  CE3 . TRP   A 123 ? 0.1879 0.0862 0.1434 -0.0335 0.0070  -0.0092 123 TRP   A CE3 
1020 C  CZ2 . TRP   A 123 ? 0.1890 0.0923 0.1618 -0.0049 -0.0071 0.0020  123 TRP   A CZ2 
1021 C  CZ3 . TRP   A 123 ? 0.2351 0.0854 0.1677 -0.0266 0.0003  -0.0056 123 TRP   A CZ3 
1022 C  CH2 . TRP   A 123 ? 0.2259 0.0771 0.1871 -0.0024 -0.0017 0.0060  123 TRP   A CH2 
1023 N  N   . ASN   A 124 ? 0.1126 0.0766 0.1281 0.0059  -0.0016 -0.0164 124 ASN   A N   
1024 C  CA  . ASN   A 124 ? 0.1229 0.0824 0.1293 -0.0041 0.0067  -0.0178 124 ASN   A CA  
1025 C  C   . ASN   A 124 ? 0.1258 0.0850 0.1318 0.0014  0.0037  -0.0190 124 ASN   A C   
1026 O  O   . ASN   A 124 ? 0.1284 0.0950 0.1347 -0.0067 0.0066  -0.0170 124 ASN   A O   
1027 C  CB  . ASN   A 124 ? 0.1439 0.0860 0.1266 -0.0071 0.0074  -0.0153 124 ASN   A CB  
1028 C  CG  . ASN   A 124 ? 0.1585 0.1001 0.1359 -0.0082 0.0103  -0.0127 124 ASN   A CG  
1029 O  OD1 . ASN   A 124 ? 0.1497 0.1123 0.1499 0.0031  0.0147  -0.0245 124 ASN   A OD1 
1030 N  ND2 . ASN   A 124 ? 0.1946 0.1192 0.1369 0.0076  0.0140  -0.0236 124 ASN   A ND2 
1031 N  N   . THR   A 125 ? 0.1294 0.0812 0.1515 0.0028  -0.0001 -0.0130 125 THR   A N   
1032 C  CA  . THR   A 125 ? 0.1497 0.0955 0.1693 0.0092  -0.0075 -0.0083 125 THR   A CA  
1033 C  C   . THR   A 125 ? 0.1467 0.0820 0.1846 0.0138  0.0118  -0.0012 125 THR   A C   
1034 O  O   . THR   A 125 ? 0.1743 0.1005 0.2123 0.0136  0.0017  0.0075  125 THR   A O   
1035 C  CB  . THR   A 125 ? 0.1788 0.1200 0.2312 0.0100  -0.0312 0.0091  125 THR   A CB  
1036 O  OG1 . THR   A 125 ? 0.1584 0.1423 0.2790 0.0239  -0.0086 -0.0117 125 THR   A OG1 
1037 C  CG2 . THR   A 125 ? 0.2022 0.1640 0.2369 -0.0155 -0.0489 0.0023  125 THR   A CG2 
1038 N  N   . LYS   A 126 ? 0.1646 0.0714 0.1648 0.0021  0.0215  -0.0234 127 LYS   A N   
1039 C  CA  . LYS   A 126 ? 0.1863 0.0949 0.1886 -0.0055 0.0303  -0.0392 127 LYS   A CA  
1040 C  C   . LYS   A 126 ? 0.1707 0.0827 0.1714 -0.0106 0.0044  -0.0351 127 LYS   A C   
1041 O  O   . LYS   A 126 ? 0.1779 0.0990 0.2214 -0.0194 0.0198  -0.0423 127 LYS   A O   
1042 C  CB  . LYS   A 126 ? 0.2043 0.1410 0.2006 -0.0412 0.0178  -0.0539 127 LYS   A CB  
1043 C  CG  . LYS   A 126 ? 0.2237 0.1819 0.1955 -0.0433 0.0160  -0.0478 127 LYS   A CG  
1044 C  CD  . LYS   A 126 ? 0.2470 0.2624 0.2363 -0.0615 0.0388  -0.0524 127 LYS   A CD  
1045 C  CE  . LYS   A 126 ? 0.2458 0.3151 0.2859 -0.0494 0.0216  -0.0201 127 LYS   A CE  
1046 N  N   . TYR   A 127 ? 0.1537 0.0824 0.1475 0.0019  0.0020  -0.0181 128 TYR   A N   
1047 C  CA  . TYR   A 127 ? 0.1575 0.0910 0.1553 -0.0055 0.0053  -0.0238 128 TYR   A CA  
1048 C  C   . TYR   A 127 ? 0.1477 0.0945 0.1811 -0.0100 0.0024  -0.0200 128 TYR   A C   
1049 O  O   . TYR   A 127 ? 0.1595 0.1119 0.1707 -0.0084 0.0100  -0.0057 128 TYR   A O   
1050 C  CB  . TYR   A 127 ? 0.1591 0.0959 0.1616 -0.0088 0.0080  -0.0190 128 TYR   A CB  
1051 C  CG  . TYR   A 127 ? 0.1574 0.0995 0.1623 0.0031  0.0000  -0.0232 128 TYR   A CG  
1052 C  CD1 . TYR   A 127 ? 0.1691 0.1188 0.1673 -0.0076 -0.0117 -0.0298 128 TYR   A CD1 
1053 C  CD2 . TYR   A 127 ? 0.1505 0.1062 0.1535 -0.0015 -0.0024 -0.0236 128 TYR   A CD2 
1054 C  CE1 . TYR   A 127 ? 0.1804 0.1233 0.1593 0.0018  -0.0110 -0.0367 128 TYR   A CE1 
1055 C  CE2 . TYR   A 127 ? 0.1660 0.1129 0.1473 0.0069  0.0020  -0.0245 128 TYR   A CE2 
1056 C  CZ  . TYR   A 127 ? 0.1735 0.1313 0.1596 0.0172  -0.0007 -0.0221 128 TYR   A CZ  
1057 O  OH  . TYR   A 127 ? 0.2378 0.1614 0.1547 0.0218  -0.0121 -0.0437 128 TYR   A OH  
1058 N  N   . GLY   A 128 ? 0.1477 0.1002 0.1559 -0.0096 0.0078  -0.0046 129 GLY   A N   
1059 C  CA  . GLY   A 128 ? 0.1600 0.0968 0.1868 0.0023  0.0125  0.0113  129 GLY   A CA  
1060 C  C   . GLY   A 128 ? 0.1720 0.0985 0.1587 0.0028  -0.0032 0.0158  129 GLY   A C   
1061 O  O   . GLY   A 128 ? 0.1988 0.1060 0.1647 0.0138  -0.0114 0.0210  129 GLY   A O   
1062 N  N   . ASP   A 129 ? 0.1763 0.1145 0.1443 0.0225  -0.0060 0.0075  130 ASP   A N   
1063 C  CA  A ASP   A 129 ? 0.1802 0.1145 0.1360 0.0164  -0.0096 0.0074  130 ASP   A CA  
1064 C  CA  B ASP   A 129 ? 0.1884 0.1090 0.1539 0.0079  0.0008  0.0066  130 ASP   A CA  
1065 C  C   . ASP   A 129 ? 0.1914 0.1083 0.1450 0.0190  -0.0056 0.0013  130 ASP   A C   
1066 O  O   . ASP   A 129 ? 0.2044 0.1173 0.1319 0.0247  -0.0047 -0.0047 130 ASP   A O   
1067 C  CB  A ASP   A 129 ? 0.1619 0.1138 0.1398 0.0264  0.0002  0.0112  130 ASP   A CB  
1068 C  CB  B ASP   A 129 ? 0.1969 0.1173 0.1634 0.0031  0.0101  0.0091  130 ASP   A CB  
1069 C  CG  A ASP   A 129 ? 0.1670 0.1283 0.1511 0.0284  -0.0026 0.0216  130 ASP   A CG  
1070 C  CG  B ASP   A 129 ? 0.1985 0.1193 0.1594 -0.0017 0.0258  0.0265  130 ASP   A CG  
1071 O  OD1 A ASP   A 129 ? 0.1723 0.1302 0.1700 0.0285  0.0103  0.0370  130 ASP   A OD1 
1072 O  OD1 B ASP   A 129 ? 0.2276 0.1842 0.2222 0.0142  0.0059  0.0398  130 ASP   A OD1 
1073 O  OD2 A ASP   A 129 ? 0.1877 0.1418 0.2200 0.0131  -0.0099 0.0373  130 ASP   A OD2 
1074 O  OD2 B ASP   A 129 ? 0.2264 0.1465 0.2143 -0.0095 0.0507  0.0525  130 ASP   A OD2 
1075 N  N   . PHE   A 130 ? 0.1959 0.1124 0.1247 0.0274  -0.0026 -0.0030 131 PHE   A N   
1076 C  CA  . PHE   A 130 ? 0.1738 0.1000 0.1141 0.0110  0.0087  -0.0065 131 PHE   A CA  
1077 C  C   . PHE   A 130 ? 0.1606 0.0932 0.1365 -0.0024 0.0124  0.0034  131 PHE   A C   
1078 O  O   . PHE   A 130 ? 0.1578 0.1098 0.1193 -0.0050 0.0103  -0.0015 131 PHE   A O   
1079 C  CB  . PHE   A 130 ? 0.1592 0.1246 0.1360 0.0019  -0.0030 -0.0047 131 PHE   A CB  
1080 C  CG  . PHE   A 130 ? 0.1555 0.1002 0.1244 -0.0042 0.0059  -0.0159 131 PHE   A CG  
1081 C  CD1 . PHE   A 130 ? 0.1728 0.1203 0.1296 -0.0232 0.0036  -0.0062 131 PHE   A CD1 
1082 C  CD2 . PHE   A 130 ? 0.1736 0.1254 0.1689 -0.0058 0.0194  -0.0059 131 PHE   A CD2 
1083 C  CE1 . PHE   A 130 ? 0.1864 0.1182 0.1555 -0.0394 -0.0171 -0.0109 131 PHE   A CE1 
1084 C  CE2 . PHE   A 130 ? 0.1826 0.1428 0.2048 0.0092  0.0143  -0.0189 131 PHE   A CE2 
1085 C  CZ  . PHE   A 130 ? 0.2195 0.1093 0.1956 -0.0119 -0.0139 -0.0126 131 PHE   A CZ  
1086 N  N   . GLY   A 131 ? 0.1755 0.1215 0.1400 -0.0092 0.0164  0.0159  132 GLY   A N   
1087 C  CA  . GLY   A 131 ? 0.1733 0.1319 0.1532 -0.0135 0.0380  0.0218  132 GLY   A CA  
1088 C  C   . GLY   A 131 ? 0.1607 0.1247 0.1446 -0.0149 0.0290  0.0188  132 GLY   A C   
1089 O  O   . GLY   A 131 ? 0.1660 0.1497 0.2005 -0.0044 0.0110  -0.0186 132 GLY   A O   
1090 N  N   . LYS   A 132 ? 0.1595 0.1122 0.1586 -0.0172 0.0123  0.0136  133 LYS   A N   
1091 C  CA  . LYS   A 132 ? 0.1570 0.0985 0.1600 -0.0240 -0.0042 -0.0018 133 LYS   A CA  
1092 C  C   . LYS   A 132 ? 0.1361 0.1106 0.1451 -0.0241 0.0082  -0.0091 133 LYS   A C   
1093 O  O   . LYS   A 132 ? 0.1546 0.1231 0.1520 -0.0388 -0.0021 -0.0089 133 LYS   A O   
1094 C  CB  . LYS   A 132 ? 0.1573 0.1244 0.1734 -0.0203 0.0033  -0.0144 133 LYS   A CB  
1095 C  CG  . LYS   A 132 ? 0.2422 0.1594 0.2953 -0.0068 -0.0051 0.0088  133 LYS   A CG  
1096 N  N   . ALA   A 133 ? 0.1418 0.1100 0.1248 -0.0285 0.0083  -0.0033 134 ALA   A N   
1097 C  CA  . ALA   A 133 ? 0.1296 0.1038 0.1059 -0.0254 0.0040  -0.0061 134 ALA   A CA  
1098 C  C   . ALA   A 133 ? 0.1357 0.1068 0.1145 -0.0192 0.0094  -0.0068 134 ALA   A C   
1099 O  O   . ALA   A 133 ? 0.1239 0.1317 0.1143 -0.0177 0.0018  -0.0025 134 ALA   A O   
1100 C  CB  . ALA   A 133 ? 0.1305 0.1032 0.1190 -0.0147 0.0011  -0.0065 134 ALA   A CB  
1101 N  N   . VAL   A 134 ? 0.1367 0.1062 0.1153 -0.0199 0.0199  0.0004  135 VAL   A N   
1102 C  CA  . VAL   A 134 ? 0.1529 0.1060 0.1332 -0.0080 0.0160  -0.0011 135 VAL   A CA  
1103 C  C   . VAL   A 134 ? 0.1363 0.1231 0.1310 -0.0099 0.0224  0.0012  135 VAL   A C   
1104 O  O   . VAL   A 134 ? 0.1360 0.1416 0.1522 -0.0008 0.0151  0.0084  135 VAL   A O   
1105 C  CB  . VAL   A 134 ? 0.1574 0.1203 0.1458 -0.0051 0.0171  -0.0021 135 VAL   A CB  
1106 C  CG1 . VAL   A 134 ? 0.1797 0.1368 0.1447 -0.0084 0.0141  -0.0020 135 VAL   A CG1 
1107 C  CG2 . VAL   A 134 ? 0.1564 0.1330 0.1518 -0.0095 0.0291  -0.0043 135 VAL   A CG2 
1108 N  N   . GLN   A 135 ? 0.1355 0.1229 0.1374 -0.0180 0.0133  -0.0023 136 GLN   A N   
1109 C  CA  . GLN   A 135 ? 0.1451 0.1413 0.1552 -0.0371 -0.0028 -0.0043 136 GLN   A CA  
1110 C  C   . GLN   A 135 ? 0.1302 0.1472 0.1477 -0.0265 -0.0070 -0.0057 136 GLN   A C   
1111 O  O   . GLN   A 135 ? 0.1522 0.1877 0.1587 -0.0399 -0.0060 -0.0196 136 GLN   A O   
1112 C  CB  . GLN   A 135 ? 0.1531 0.1857 0.1737 -0.0543 0.0043  0.0035  136 GLN   A CB  
1113 C  CG  . GLN   A 135 ? 0.2076 0.2355 0.2161 -0.0770 0.0223  0.0190  136 GLN   A CG  
1114 C  CD  . GLN   A 135 ? 0.2527 0.2944 0.2765 -0.0963 -0.0012 0.0265  136 GLN   A CD  
1115 O  OE1 . GLN   A 135 ? 0.3683 0.3552 0.3623 -0.1598 -0.0362 0.0197  136 GLN   A OE1 
1116 N  NE2 . GLN   A 135 ? 0.2811 0.3145 0.2991 -0.0596 -0.0098 0.0478  136 GLN   A NE2 
1117 N  N   . GLN   A 136 ? 0.1273 0.1378 0.1289 -0.0219 -0.0036 -0.0166 137 GLN   A N   
1118 C  CA  . GLN   A 136 ? 0.1362 0.1231 0.1197 -0.0144 -0.0061 -0.0223 137 GLN   A CA  
1119 C  C   . GLN   A 136 ? 0.1405 0.1327 0.1175 -0.0096 -0.0009 -0.0187 137 GLN   A C   
1120 O  O   . GLN   A 136 ? 0.1526 0.1192 0.1120 -0.0076 -0.0007 -0.0175 137 GLN   A O   
1121 C  CB  . GLN   A 136 ? 0.1538 0.1153 0.1348 -0.0047 0.0036  -0.0190 137 GLN   A CB  
1122 C  CG  . GLN   A 136 ? 0.1854 0.1453 0.1603 -0.0023 0.0097  0.0036  137 GLN   A CG  
1123 C  CD  . GLN   A 136 ? 0.2131 0.1563 0.1774 -0.0242 -0.0050 0.0096  137 GLN   A CD  
1124 O  OE1 . GLN   A 136 ? 0.2268 0.1503 0.2104 -0.0298 -0.0185 -0.0455 137 GLN   A OE1 
1125 N  NE2 . GLN   A 136 ? 0.2398 0.1871 0.1779 -0.0450 -0.0018 -0.0035 137 GLN   A NE2 
1126 N  N   . PRO   A 137 ? 0.1350 0.1487 0.1149 -0.0041 -0.0032 -0.0191 138 PRO   A N   
1127 C  CA  . PRO   A 137 ? 0.1508 0.1553 0.1208 -0.0007 -0.0060 0.0000  138 PRO   A CA  
1128 C  C   . PRO   A 137 ? 0.1438 0.1404 0.1315 -0.0059 0.0001  0.0021  138 PRO   A C   
1129 O  O   . PRO   A 137 ? 0.1635 0.1636 0.2331 -0.0058 -0.0104 0.0290  138 PRO   A O   
1130 C  CB  . PRO   A 137 ? 0.1767 0.1927 0.1235 0.0019  -0.0103 0.0026  138 PRO   A CB  
1131 C  CG  . PRO   A 137 ? 0.2506 0.2312 0.1451 -0.0253 -0.0108 -0.0235 138 PRO   A CG  
1132 C  CD  . PRO   A 137 ? 0.1615 0.1686 0.1266 -0.0170 -0.0097 -0.0216 138 PRO   A CD  
1133 N  N   . ASP   A 138 ? 0.1280 0.1391 0.1223 -0.0045 0.0002  -0.0038 139 ASP   A N   
1134 C  CA  . ASP   A 138 ? 0.1257 0.1346 0.1295 -0.0170 0.0041  -0.0123 139 ASP   A CA  
1135 C  C   . ASP   A 138 ? 0.1281 0.1131 0.1328 -0.0112 0.0047  -0.0057 139 ASP   A C   
1136 O  O   . ASP   A 138 ? 0.1420 0.1462 0.1430 0.0057  0.0137  0.0000  139 ASP   A O   
1137 C  CB  . ASP   A 138 ? 0.1541 0.1959 0.1301 -0.0156 0.0185  -0.0107 139 ASP   A CB  
1138 C  CG  . ASP   A 138 ? 0.1388 0.1986 0.1580 0.0064  0.0151  -0.0318 139 ASP   A CG  
1139 O  OD1 . ASP   A 138 ? 0.1969 0.1478 0.1664 0.0041  0.0132  -0.0291 139 ASP   A OD1 
1140 O  OD2 . ASP   A 138 ? 0.1996 0.2238 0.2032 0.0112  0.0398  -0.0602 139 ASP   A OD2 
1141 N  N   . GLY   A 139 ? 0.1174 0.1004 0.1179 -0.0033 0.0032  -0.0104 140 GLY   A N   
1142 C  CA  . GLY   A 139 ? 0.1262 0.0933 0.1124 -0.0125 -0.0051 -0.0050 140 GLY   A CA  
1143 C  C   . GLY   A 139 ? 0.1010 0.0844 0.1089 -0.0040 0.0076  -0.0073 140 GLY   A C   
1144 O  O   . GLY   A 139 ? 0.1195 0.0842 0.1139 -0.0013 -0.0016 -0.0050 140 GLY   A O   
1145 N  N   . LEU   A 140 ? 0.1012 0.0827 0.1116 -0.0070 -0.0003 -0.0091 141 LEU   A N   
1146 C  CA  A LEU   A 140 ? 0.1001 0.0733 0.1061 -0.0033 -0.0002 -0.0061 141 LEU   A CA  
1147 C  CA  B LEU   A 140 ? 0.1038 0.0805 0.1120 -0.0046 -0.0024 -0.0067 141 LEU   A CA  
1148 C  C   . LEU   A 140 ? 0.0953 0.0758 0.1071 0.0042  0.0016  -0.0049 141 LEU   A C   
1149 O  O   . LEU   A 140 ? 0.1034 0.0904 0.1071 -0.0058 -0.0025 -0.0080 141 LEU   A O   
1150 C  CB  A LEU   A 140 ? 0.0902 0.0773 0.1014 -0.0040 0.0033  -0.0028 141 LEU   A CB  
1151 C  CB  B LEU   A 140 ? 0.0997 0.0981 0.1205 -0.0013 -0.0007 -0.0080 141 LEU   A CB  
1152 C  CG  A LEU   A 140 ? 0.0919 0.0735 0.1050 -0.0039 0.0064  -0.0062 141 LEU   A CG  
1153 C  CG  B LEU   A 140 ? 0.1059 0.1134 0.1321 0.0019  -0.0025 -0.0091 141 LEU   A CG  
1154 C  CD1 A LEU   A 140 ? 0.0968 0.0827 0.1071 0.0021  0.0033  -0.0037 141 LEU   A CD1 
1155 C  CD1 B LEU   A 140 ? 0.1264 0.1140 0.1574 -0.0010 0.0068  -0.0082 141 LEU   A CD1 
1156 C  CD2 A LEU   A 140 ? 0.0929 0.0767 0.1002 -0.0027 0.0137  -0.0020 141 LEU   A CD2 
1157 C  CD2 B LEU   A 140 ? 0.1162 0.1183 0.1252 -0.0096 -0.0013 -0.0155 141 LEU   A CD2 
1158 N  N   . ALA   A 141 ? 0.1044 0.0760 0.1004 -0.0046 -0.0021 -0.0031 142 ALA   A N   
1159 C  CA  . ALA   A 141 ? 0.1099 0.0792 0.1021 -0.0116 -0.0023 -0.0044 142 ALA   A CA  
1160 C  C   . ALA   A 141 ? 0.1027 0.0790 0.0983 -0.0065 -0.0028 0.0000  142 ALA   A C   
1161 O  O   . ALA   A 141 ? 0.1206 0.0805 0.1022 -0.0031 -0.0080 0.0018  142 ALA   A O   
1162 C  CB  . ALA   A 141 ? 0.1159 0.0951 0.1189 -0.0175 0.0041  -0.0088 142 ALA   A CB  
1163 N  N   . VAL   A 142 ? 0.0996 0.0793 0.0886 0.0004  -0.0056 -0.0003 143 VAL   A N   
1164 C  CA  . VAL   A 142 ? 0.0997 0.0789 0.0869 0.0020  -0.0078 -0.0017 143 VAL   A CA  
1165 C  C   . VAL   A 142 ? 0.1078 0.0774 0.0821 -0.0038 0.0002  -0.0107 143 VAL   A C   
1166 O  O   . VAL   A 142 ? 0.1096 0.0873 0.0925 -0.0042 -0.0012 0.0034  143 VAL   A O   
1167 C  CB  . VAL   A 142 ? 0.1009 0.0917 0.0874 0.0070  -0.0057 0.0024  143 VAL   A CB  
1168 C  CG1 . VAL   A 142 ? 0.1084 0.1027 0.1034 0.0153  -0.0027 -0.0029 143 VAL   A CG1 
1169 C  CG2 . VAL   A 142 ? 0.1138 0.1192 0.0949 -0.0003 -0.0051 0.0053  143 VAL   A CG2 
1170 N  N   . LEU   A 143 ? 0.1086 0.0783 0.0907 -0.0046 -0.0004 0.0010  144 LEU   A N   
1171 C  CA  . LEU   A 143 ? 0.1056 0.0857 0.0966 -0.0057 0.0010  -0.0006 144 LEU   A CA  
1172 C  C   . LEU   A 143 ? 0.1065 0.0864 0.0959 -0.0139 0.0051  0.0026  144 LEU   A C   
1173 O  O   . LEU   A 143 ? 0.1299 0.0929 0.0961 -0.0057 0.0062  -0.0006 144 LEU   A O   
1174 C  CB  . LEU   A 143 ? 0.1209 0.1136 0.1018 -0.0006 -0.0011 0.0098  144 LEU   A CB  
1175 C  CG  . LEU   A 143 ? 0.1250 0.1092 0.1476 -0.0036 0.0015  -0.0032 144 LEU   A CG  
1176 C  CD1 . LEU   A 143 ? 0.1276 0.1655 0.1729 -0.0158 -0.0022 0.0133  144 LEU   A CD1 
1177 C  CD2 . LEU   A 143 ? 0.1248 0.1696 0.1518 0.0024  -0.0033 -0.0107 144 LEU   A CD2 
1178 N  N   . GLY   A 144 ? 0.1093 0.0785 0.0898 -0.0082 0.0039  -0.0064 145 GLY   A N   
1179 C  CA  . GLY   A 144 ? 0.0998 0.0872 0.0951 -0.0051 0.0026  -0.0039 145 GLY   A CA  
1180 C  C   . GLY   A 144 ? 0.0931 0.0822 0.0890 -0.0062 0.0039  -0.0010 145 GLY   A C   
1181 O  O   . GLY   A 144 ? 0.1150 0.1019 0.0925 -0.0116 0.0137  -0.0042 145 GLY   A O   
1182 N  N   . ILE   A 145 ? 0.0980 0.0674 0.0896 -0.0058 0.0076  -0.0049 146 ILE   A N   
1183 C  CA  . ILE   A 145 ? 0.0948 0.0737 0.0970 -0.0024 0.0017  0.0035  146 ILE   A CA  
1184 C  C   . ILE   A 145 ? 0.0949 0.0694 0.0953 -0.0032 0.0037  0.0000  146 ILE   A C   
1185 O  O   . ILE   A 145 ? 0.1116 0.0771 0.1056 -0.0050 0.0100  -0.0056 146 ILE   A O   
1186 C  CB  . ILE   A 145 ? 0.1005 0.0855 0.1069 0.0011  0.0037  0.0020  146 ILE   A CB  
1187 C  CG1 . ILE   A 145 ? 0.1221 0.0974 0.1325 0.0134  -0.0027 -0.0029 146 ILE   A CG1 
1188 C  CG2 . ILE   A 145 ? 0.1218 0.0969 0.1528 0.0005  -0.0147 0.0004  146 ILE   A CG2 
1189 C  CD1 . ILE   A 145 ? 0.1170 0.1083 0.1279 0.0073  0.0005  0.0008  146 ILE   A CD1 
1190 N  N   . PHE   A 146 ? 0.1003 0.0699 0.0943 -0.0018 0.0078  -0.0068 147 PHE   A N   
1191 C  CA  . PHE   A 146 ? 0.0999 0.0689 0.1038 -0.0021 0.0030  -0.0017 147 PHE   A CA  
1192 C  C   . PHE   A 146 ? 0.1008 0.0873 0.1112 -0.0050 0.0118  -0.0012 147 PHE   A C   
1193 O  O   . PHE   A 146 ? 0.1001 0.0992 0.1181 -0.0025 0.0032  -0.0134 147 PHE   A O   
1194 C  CB  . PHE   A 146 ? 0.0963 0.0764 0.1070 0.0001  0.0021  0.0012  147 PHE   A CB  
1195 C  CG  . PHE   A 146 ? 0.1103 0.0741 0.1054 -0.0019 0.0010  0.0060  147 PHE   A CG  
1196 C  CD1 . PHE   A 146 ? 0.1133 0.0919 0.1030 0.0013  -0.0003 -0.0041 147 PHE   A CD1 
1197 C  CD2 . PHE   A 146 ? 0.1164 0.0895 0.1094 -0.0008 0.0060  0.0125  147 PHE   A CD2 
1198 C  CE1 . PHE   A 146 ? 0.1060 0.0976 0.1167 -0.0001 0.0000  0.0060  147 PHE   A CE1 
1199 C  CE2 . PHE   A 146 ? 0.1271 0.0945 0.1018 -0.0013 0.0091  0.0042  147 PHE   A CE2 
1200 C  CZ  . PHE   A 146 ? 0.1218 0.0956 0.1090 -0.0056 -0.0088 0.0039  147 PHE   A CZ  
1201 N  N   . LEU   A 147 ? 0.0953 0.0807 0.1098 -0.0039 0.0051  -0.0051 148 LEU   A N   
1202 C  CA  . LEU   A 147 ? 0.0988 0.0814 0.1109 -0.0066 -0.0014 -0.0076 148 LEU   A CA  
1203 C  C   . LEU   A 147 ? 0.1162 0.0867 0.1024 -0.0122 0.0038  -0.0070 148 LEU   A C   
1204 O  O   . LEU   A 147 ? 0.1203 0.0859 0.1295 -0.0039 0.0045  -0.0035 148 LEU   A O   
1205 C  CB  . LEU   A 147 ? 0.1159 0.0854 0.1182 -0.0031 0.0042  -0.0080 148 LEU   A CB  
1206 C  CG  . LEU   A 147 ? 0.1189 0.0819 0.1105 -0.0119 -0.0085 -0.0072 148 LEU   A CG  
1207 C  CD1 . LEU   A 147 ? 0.1463 0.0817 0.1178 -0.0101 -0.0055 -0.0041 148 LEU   A CD1 
1208 C  CD2 . LEU   A 147 ? 0.1285 0.1042 0.1233 -0.0091 -0.0105 -0.0037 148 LEU   A CD2 
1209 N  N   . LYS   A 148 ? 0.1210 0.0824 0.1315 -0.0059 -0.0110 -0.0049 149 LYS   A N   
1210 C  CA  . LYS   A 148 ? 0.1505 0.0764 0.1405 -0.0048 -0.0238 0.0004  149 LYS   A CA  
1211 C  C   . LYS   A 148 ? 0.1600 0.0854 0.1469 0.0070  -0.0233 -0.0064 149 LYS   A C   
1212 O  O   . LYS   A 148 ? 0.1724 0.1194 0.1422 0.0254  -0.0291 -0.0191 149 LYS   A O   
1213 C  CB  . LYS   A 148 ? 0.1898 0.1107 0.1505 -0.0294 -0.0311 0.0121  149 LYS   A CB  
1214 C  CG  . LYS   A 148 ? 0.2152 0.1339 0.1921 -0.0338 -0.0150 0.0168  149 LYS   A CG  
1215 C  CD  . LYS   A 148 ? 0.2853 0.1960 0.2600 -0.0297 0.0031  0.0537  149 LYS   A CD  
1216 N  N   . VAL   A 149 ? 0.1739 0.0817 0.1608 0.0099  -0.0340 -0.0151 150 VAL   A N   
1217 C  CA  . VAL   A 149 ? 0.1674 0.0845 0.1615 0.0048  -0.0268 -0.0105 150 VAL   A CA  
1218 C  C   . VAL   A 149 ? 0.1846 0.0945 0.1655 0.0026  -0.0207 0.0016  150 VAL   A C   
1219 O  O   . VAL   A 149 ? 0.2037 0.1218 0.1778 -0.0159 -0.0317 0.0196  150 VAL   A O   
1220 C  CB  . VAL   A 149 ? 0.1838 0.0990 0.1699 0.0114  -0.0212 -0.0077 150 VAL   A CB  
1221 C  CG1 . VAL   A 149 ? 0.2008 0.1303 0.1709 0.0167  -0.0167 -0.0118 150 VAL   A CG1 
1222 C  CG2 . VAL   A 149 ? 0.1738 0.1465 0.2083 0.0103  -0.0180 -0.0123 150 VAL   A CG2 
1223 N  N   . GLY   A 150 ? 0.1711 0.0939 0.1599 -0.0179 -0.0226 0.0039  151 GLY   A N   
1224 C  CA  . GLY   A 150 ? 0.1786 0.1226 0.1713 -0.0241 -0.0166 0.0110  151 GLY   A CA  
1225 C  C   . GLY   A 150 ? 0.1669 0.1023 0.1643 -0.0285 -0.0111 0.0052  151 GLY   A C   
1226 O  O   . GLY   A 150 ? 0.1864 0.1211 0.1615 -0.0149 -0.0092 -0.0004 151 GLY   A O   
1227 N  N   . SER   A 151 ? 0.1715 0.1302 0.1603 -0.0290 -0.0038 0.0031  152 SER   A N   
1228 C  CA  . SER   A 151 ? 0.1673 0.1335 0.1755 -0.0414 -0.0053 -0.0065 152 SER   A CA  
1229 C  C   . SER   A 151 ? 0.1592 0.1271 0.1634 -0.0312 -0.0132 -0.0164 152 SER   A C   
1230 O  O   . SER   A 151 ? 0.1651 0.1272 0.1462 -0.0278 -0.0209 -0.0117 152 SER   A O   
1231 C  CB  A SER   A 151 ? 0.1818 0.1790 0.2266 -0.0436 -0.0041 0.0077  152 SER   A CB  
1232 C  CB  B SER   A 151 ? 0.1837 0.1835 0.2430 -0.0345 0.0022  0.0070  152 SER   A CB  
1233 O  OG  A SER   A 151 ? 0.2135 0.2234 0.2246 -0.0565 -0.0061 0.0002  152 SER   A OG  
1234 O  OG  B SER   A 151 ? 0.2080 0.2201 0.3002 -0.0269 0.0059  0.0468  152 SER   A OG  
1235 N  N   . ALA   A 152 ? 0.1713 0.1138 0.1480 -0.0262 -0.0219 -0.0187 153 ALA   A N   
1236 C  CA  . ALA   A 152 ? 0.1514 0.1261 0.1406 -0.0193 -0.0201 -0.0098 153 ALA   A CA  
1237 C  C   . ALA   A 152 ? 0.1536 0.1186 0.1512 -0.0203 -0.0098 -0.0075 153 ALA   A C   
1238 O  O   . ALA   A 152 ? 0.1617 0.1306 0.1892 -0.0208 -0.0072 -0.0004 153 ALA   A O   
1239 C  CB  . ALA   A 152 ? 0.2040 0.1531 0.1497 -0.0133 -0.0216 -0.0097 153 ALA   A CB  
1240 N  N   . LYS   A 153 ? 0.1468 0.1141 0.1497 -0.0020 -0.0007 0.0032  154 LYS   A N   
1241 C  CA  . LYS   A 153 ? 0.1505 0.1069 0.1606 -0.0082 -0.0009 0.0032  154 LYS   A CA  
1242 C  C   . LYS   A 153 ? 0.1237 0.1230 0.1559 0.0036  -0.0050 -0.0036 154 LYS   A C   
1243 O  O   . LYS   A 153 ? 0.1211 0.1273 0.1448 -0.0036 -0.0103 -0.0077 154 LYS   A O   
1244 C  CB  . LYS   A 153 ? 0.1684 0.1084 0.1585 -0.0147 -0.0204 0.0068  154 LYS   A CB  
1245 C  CG  . LYS   A 153 ? 0.1835 0.1211 0.1671 -0.0061 -0.0193 0.0031  154 LYS   A CG  
1246 C  CD  . LYS   A 153 ? 0.2120 0.1522 0.1793 -0.0039 -0.0086 -0.0045 154 LYS   A CD  
1247 C  CE  . LYS   A 153 ? 0.2239 0.1597 0.1875 0.0211  -0.0111 0.0037  154 LYS   A CE  
1248 N  NZ  . LYS   A 153 ? 0.2428 0.2024 0.2158 0.0141  -0.0070 -0.0067 154 LYS   A NZ  
1249 N  N   . PRO   A 154 ? 0.1347 0.1269 0.1795 -0.0092 -0.0120 0.0113  155 PRO   A N   
1250 C  CA  . PRO   A 154 ? 0.1255 0.1545 0.2014 -0.0220 -0.0221 0.0042  155 PRO   A CA  
1251 C  C   . PRO   A 154 ? 0.1224 0.1473 0.1560 0.0063  -0.0086 0.0129  155 PRO   A C   
1252 O  O   . PRO   A 154 ? 0.1496 0.1781 0.1714 0.0059  -0.0190 0.0243  155 PRO   A O   
1253 C  CB  . PRO   A 154 ? 0.1375 0.1902 0.2411 -0.0209 -0.0264 0.0163  155 PRO   A CB  
1254 C  CG  . PRO   A 154 ? 0.1651 0.2168 0.2821 -0.0205 -0.0142 0.0321  155 PRO   A CG  
1255 C  CD  . PRO   A 154 ? 0.1420 0.1684 0.2241 0.0012  -0.0032 0.0193  155 PRO   A CD  
1256 N  N   . GLY   A 155 ? 0.1184 0.1200 0.1694 0.0094  -0.0067 0.0149  156 GLY   A N   
1257 C  CA  . GLY   A 155 ? 0.1383 0.1237 0.1758 0.0034  0.0011  0.0143  156 GLY   A CA  
1258 C  C   . GLY   A 155 ? 0.1469 0.1148 0.1670 -0.0085 -0.0020 0.0055  156 GLY   A C   
1259 O  O   . GLY   A 155 ? 0.1566 0.1254 0.2335 -0.0063 -0.0107 0.0183  156 GLY   A O   
1260 N  N   . LEU   A 156 ? 0.1310 0.1045 0.1644 -0.0153 -0.0051 0.0016  157 LEU   A N   
1261 C  CA  . LEU   A 156 ? 0.1226 0.1097 0.1471 -0.0179 -0.0048 -0.0079 157 LEU   A CA  
1262 C  C   . LEU   A 156 ? 0.1177 0.1180 0.1372 -0.0153 -0.0073 -0.0014 157 LEU   A C   
1263 O  O   . LEU   A 156 ? 0.1309 0.1261 0.1435 -0.0239 -0.0057 -0.0010 157 LEU   A O   
1264 C  CB  . LEU   A 156 ? 0.1352 0.1201 0.1444 -0.0129 -0.0139 -0.0046 157 LEU   A CB  
1265 C  CG  . LEU   A 156 ? 0.1318 0.1469 0.1431 -0.0166 -0.0152 -0.0050 157 LEU   A CG  
1266 C  CD1 . LEU   A 156 ? 0.1354 0.1581 0.1652 -0.0249 -0.0273 -0.0026 157 LEU   A CD1 
1267 C  CD2 . LEU   A 156 ? 0.1335 0.1699 0.1654 0.0050  -0.0200 0.0022  157 LEU   A CD2 
1268 N  N   . GLN   A 157 ? 0.1331 0.1219 0.1503 -0.0266 -0.0173 -0.0022 158 GLN   A N   
1269 C  CA  . GLN   A 157 ? 0.1388 0.1241 0.1450 -0.0189 -0.0171 -0.0111 158 GLN   A CA  
1270 C  C   . GLN   A 157 ? 0.1379 0.1180 0.1504 -0.0173 -0.0211 -0.0127 158 GLN   A C   
1271 O  O   . GLN   A 157 ? 0.1405 0.1286 0.1453 -0.0214 -0.0141 -0.0111 158 GLN   A O   
1272 C  CB  . GLN   A 157 ? 0.1355 0.1307 0.1777 -0.0238 -0.0285 0.0017  158 GLN   A CB  
1273 C  CG  . GLN   A 157 ? 0.1637 0.1442 0.1605 -0.0299 -0.0285 -0.0077 158 GLN   A CG  
1274 C  CD  . GLN   A 157 ? 0.1639 0.1243 0.1560 -0.0293 -0.0144 -0.0162 158 GLN   A CD  
1275 O  OE1 . GLN   A 157 ? 0.1826 0.1322 0.1471 -0.0048 -0.0066 -0.0134 158 GLN   A OE1 
1276 N  NE2 . GLN   A 157 ? 0.1998 0.1711 0.1452 -0.0124 -0.0140 -0.0294 158 GLN   A NE2 
1277 N  N   . LYS   A 158 ? 0.1396 0.1382 0.1358 -0.0125 -0.0217 -0.0034 159 LYS   A N   
1278 C  CA  . LYS   A 158 ? 0.1587 0.1269 0.1602 -0.0072 -0.0318 0.0073  159 LYS   A CA  
1279 C  C   . LYS   A 158 ? 0.1620 0.1412 0.1307 -0.0277 -0.0135 -0.0008 159 LYS   A C   
1280 O  O   . LYS   A 158 ? 0.1797 0.1530 0.1422 -0.0362 -0.0220 -0.0029 159 LYS   A O   
1281 C  CB  . LYS   A 158 ? 0.2124 0.1392 0.1966 -0.0078 -0.0367 0.0335  159 LYS   A CB  
1282 C  CG  . LYS   A 158 ? 0.2457 0.2517 0.2720 0.0100  -0.0328 0.0345  159 LYS   A CG  
1283 N  N   . VAL   A 159 ? 0.1474 0.1197 0.1358 -0.0147 -0.0100 -0.0079 160 VAL   A N   
1284 C  CA  . VAL   A 159 ? 0.1397 0.1160 0.1301 -0.0291 -0.0018 -0.0039 160 VAL   A CA  
1285 C  C   . VAL   A 159 ? 0.1367 0.1153 0.1381 -0.0210 -0.0057 -0.0094 160 VAL   A C   
1286 O  O   . VAL   A 159 ? 0.1482 0.1393 0.1592 -0.0223 0.0016  -0.0057 160 VAL   A O   
1287 C  CB  . VAL   A 159 ? 0.1555 0.1267 0.1318 -0.0220 -0.0034 -0.0068 160 VAL   A CB  
1288 C  CG1 . VAL   A 159 ? 0.1556 0.1551 0.1575 -0.0293 0.0000  -0.0067 160 VAL   A CG1 
1289 C  CG2 . VAL   A 159 ? 0.1826 0.1426 0.1407 -0.0013 -0.0198 -0.0164 160 VAL   A CG2 
1290 N  N   . VAL   A 160 ? 0.1489 0.1073 0.1349 -0.0097 0.0011  -0.0101 161 VAL   A N   
1291 C  CA  . VAL   A 160 ? 0.1842 0.1190 0.1638 0.0044  0.0075  -0.0030 161 VAL   A CA  
1292 C  C   . VAL   A 160 ? 0.1707 0.1196 0.1709 -0.0234 0.0090  -0.0177 161 VAL   A C   
1293 O  O   . VAL   A 160 ? 0.2070 0.1490 0.1791 -0.0201 0.0272  -0.0198 161 VAL   A O   
1294 C  CB  . VAL   A 160 ? 0.2141 0.1409 0.2001 0.0106  0.0073  -0.0190 161 VAL   A CB  
1295 C  CG1 . VAL   A 160 ? 0.1747 0.1553 0.2169 -0.0046 -0.0123 -0.0307 161 VAL   A CG1 
1296 C  CG2 . VAL   A 160 ? 0.2335 0.1443 0.2104 0.0057  0.0077  0.0011  161 VAL   A CG2 
1297 N  N   . ASP   A 161 ? 0.1867 0.1525 0.1398 -0.0400 0.0036  -0.0231 162 ASP   A N   
1298 C  CA  . ASP   A 161 ? 0.2243 0.1816 0.1493 -0.0595 -0.0173 -0.0273 162 ASP   A CA  
1299 C  C   . ASP   A 161 ? 0.2158 0.1842 0.1373 -0.0465 0.0009  -0.0183 162 ASP   A C   
1300 O  O   . ASP   A 161 ? 0.3353 0.2499 0.1551 -0.0824 0.0243  -0.0439 162 ASP   A O   
1301 C  CB  . ASP   A 161 ? 0.2612 0.2630 0.1405 -0.0565 -0.0084 -0.0181 162 ASP   A CB  
1302 C  CG  . ASP   A 161 ? 0.2661 0.2548 0.2085 -0.0376 -0.0258 -0.0367 162 ASP   A CG  
1303 O  OD1 . ASP   A 161 ? 0.2826 0.2688 0.2993 -0.0551 -0.0210 -0.0420 162 ASP   A OD1 
1304 O  OD2 . ASP   A 161 ? 0.2450 0.2909 0.2577 -0.0246 -0.0146 -0.0313 162 ASP   A OD2 
1305 N  N   . VAL   A 162 ? 0.1785 0.1565 0.1257 -0.0371 -0.0214 -0.0162 163 VAL   A N   
1306 C  CA  . VAL   A 162 ? 0.1878 0.1657 0.1363 -0.0378 -0.0146 0.0063  163 VAL   A CA  
1307 C  C   . VAL   A 162 ? 0.1813 0.1425 0.1426 -0.0148 -0.0079 0.0039  163 VAL   A C   
1308 O  O   . VAL   A 162 ? 0.1849 0.1590 0.1387 -0.0272 0.0058  0.0047  163 VAL   A O   
1309 C  CB  . VAL   A 162 ? 0.1870 0.1652 0.2018 -0.0252 -0.0142 0.0135  163 VAL   A CB  
1310 C  CG1 . VAL   A 162 ? 0.2175 0.1599 0.1876 -0.0238 0.0102  -0.0130 163 VAL   A CG1 
1311 C  CG2 . VAL   A 162 ? 0.2437 0.2036 0.1910 -0.0058 -0.0073 0.0198  163 VAL   A CG2 
1312 N  N   . LEU   A 163 ? 0.1727 0.1362 0.1405 -0.0152 -0.0038 -0.0038 164 LEU   A N   
1313 C  CA  . LEU   A 163 ? 0.1600 0.1371 0.1374 -0.0146 0.0024  -0.0080 164 LEU   A CA  
1314 C  C   . LEU   A 163 ? 0.2016 0.1377 0.1358 -0.0081 0.0067  -0.0119 164 LEU   A C   
1315 O  O   . LEU   A 163 ? 0.1800 0.1633 0.1391 0.0017  0.0055  0.0125  164 LEU   A O   
1316 C  CB  . LEU   A 163 ? 0.1735 0.1334 0.1433 -0.0030 -0.0007 -0.0113 164 LEU   A CB  
1317 C  CG  . LEU   A 163 ? 0.1552 0.1366 0.1420 -0.0030 -0.0001 0.0087  164 LEU   A CG  
1318 C  CD1 . LEU   A 163 ? 0.1749 0.1419 0.1745 -0.0045 -0.0022 0.0227  164 LEU   A CD1 
1319 C  CD2 . LEU   A 163 ? 0.1455 0.1582 0.1365 0.0033  -0.0139 -0.0019 164 LEU   A CD2 
1320 N  N   . ASP   A 164 ? 0.2235 0.1933 0.1527 -0.0222 0.0116  -0.0385 165 ASP   A N   
1321 C  CA  . ASP   A 164 ? 0.2876 0.2220 0.1801 -0.0231 0.0498  -0.0450 165 ASP   A CA  
1322 C  C   . ASP   A 164 ? 0.2455 0.2228 0.1633 -0.0263 0.0377  -0.0203 165 ASP   A C   
1323 O  O   . ASP   A 164 ? 0.3092 0.2833 0.2394 0.0162  0.1021  -0.0104 165 ASP   A O   
1324 C  CB  . ASP   A 164 ? 0.3489 0.2388 0.2012 -0.0552 0.0516  -0.0728 165 ASP   A CB  
1325 N  N   . SER   A 165 ? 0.1704 0.2166 0.1183 -0.0221 -0.0130 -0.0028 166 SER   A N   
1326 C  CA  . SER   A 165 ? 0.1873 0.2180 0.1228 -0.0095 -0.0004 0.0190  166 SER   A CA  
1327 C  C   . SER   A 165 ? 0.1635 0.1835 0.1265 -0.0079 0.0045  0.0231  166 SER   A C   
1328 O  O   . SER   A 165 ? 0.1934 0.2012 0.1310 -0.0094 -0.0055 0.0320  166 SER   A O   
1329 C  CB  A SER   A 165 ? 0.1843 0.2257 0.1546 -0.0129 -0.0107 0.0216  166 SER   A CB  
1330 C  CB  B SER   A 165 ? 0.2217 0.2616 0.1790 -0.0120 -0.0194 0.0404  166 SER   A CB  
1331 O  OG  A SER   A 165 ? 0.1496 0.1765 0.1528 0.0138  -0.0109 0.0203  166 SER   A OG  
1332 O  OG  B SER   A 165 ? 0.2899 0.3408 0.2119 -0.0257 -0.0525 0.0325  166 SER   A OG  
1333 N  N   . ILE   A 166 ? 0.1497 0.1456 0.1068 0.0009  0.0039  0.0138  167 ILE   A N   
1334 C  CA  . ILE   A 166 ? 0.1452 0.1340 0.1172 -0.0004 0.0053  0.0036  167 ILE   A CA  
1335 C  C   . ILE   A 166 ? 0.1424 0.1208 0.1082 -0.0023 0.0113  -0.0023 167 ILE   A C   
1336 O  O   . ILE   A 166 ? 0.1402 0.1271 0.1130 -0.0035 0.0082  -0.0022 167 ILE   A O   
1337 C  CB  . ILE   A 166 ? 0.1576 0.1273 0.1278 0.0072  0.0057  -0.0010 167 ILE   A CB  
1338 C  CG1 . ILE   A 166 ? 0.1393 0.1438 0.1174 -0.0017 -0.0012 -0.0063 167 ILE   A CG1 
1339 C  CG2 . ILE   A 166 ? 0.1598 0.1464 0.1499 0.0136  -0.0013 0.0089  167 ILE   A CG2 
1340 C  CD1 . ILE   A 166 ? 0.1594 0.1571 0.1264 -0.0120 0.0118  -0.0103 167 ILE   A CD1 
1341 N  N   . LYS   A 167 ? 0.1566 0.1259 0.1053 0.0046  0.0050  -0.0006 168 LYS   A N   
1342 C  CA  . LYS   A 167 ? 0.1538 0.1136 0.1127 -0.0007 0.0036  -0.0089 168 LYS   A CA  
1343 C  C   . LYS   A 167 ? 0.1447 0.1083 0.1142 0.0004  0.0120  -0.0003 168 LYS   A C   
1344 O  O   . LYS   A 167 ? 0.1555 0.1088 0.1276 0.0069  0.0085  0.0108  168 LYS   A O   
1345 C  CB  . LYS   A 167 ? 0.1710 0.1341 0.1455 -0.0022 0.0094  -0.0246 168 LYS   A CB  
1346 C  CG  . LYS   A 167 ? 0.1996 0.1336 0.1715 0.0007  -0.0018 -0.0231 168 LYS   A CG  
1347 C  CD  . LYS   A 167 ? 0.2786 0.1669 0.2235 0.0086  -0.0048 -0.0500 168 LYS   A CD  
1348 C  CE  . LYS   A 167 ? 0.3315 0.2175 0.2824 0.0298  -0.0063 -0.0325 168 LYS   A CE  
1349 N  NZ  . LYS   A 167 ? 0.4312 0.2802 0.3341 0.0267  0.0148  -0.0653 168 LYS   A NZ  
1350 N  N   . THR   A 168 ? 0.1387 0.1214 0.1187 0.0025  0.0098  0.0161  169 THR   A N   
1351 C  CA  . THR   A 168 ? 0.1356 0.1173 0.1297 -0.0029 0.0200  0.0135  169 THR   A CA  
1352 C  C   . THR   A 168 ? 0.1229 0.1223 0.1096 0.0008  0.0152  0.0125  169 THR   A C   
1353 O  O   . THR   A 168 ? 0.1324 0.1166 0.1233 0.0024  0.0133  0.0091  169 THR   A O   
1354 C  CB  . THR   A 168 ? 0.1473 0.1283 0.1349 0.0109  0.0194  0.0059  169 THR   A CB  
1355 O  OG1 . THR   A 168 ? 0.1624 0.1526 0.1357 0.0135  0.0260  0.0155  169 THR   A OG1 
1356 C  CG2 . THR   A 168 ? 0.1617 0.1370 0.1484 0.0139  0.0325  0.0020  169 THR   A CG2 
1357 N  N   . LYS   A 169 ? 0.1320 0.1205 0.1378 0.0070  0.0120  0.0036  170 LYS   A N   
1358 C  CA  . LYS   A 169 ? 0.1311 0.1329 0.1236 -0.0032 0.0195  0.0084  170 LYS   A CA  
1359 C  C   . LYS   A 169 ? 0.1355 0.1220 0.1220 -0.0099 0.0181  0.0070  170 LYS   A C   
1360 O  O   . LYS   A 169 ? 0.1642 0.1598 0.1304 -0.0169 0.0351  0.0167  170 LYS   A O   
1361 C  CB  . LYS   A 169 ? 0.1495 0.1571 0.1339 -0.0071 0.0202  0.0147  170 LYS   A CB  
1362 C  CG  . LYS   A 169 ? 0.1542 0.1715 0.1398 -0.0222 0.0096  0.0111  170 LYS   A CG  
1363 C  CD  . LYS   A 169 ? 0.1858 0.2014 0.1906 -0.0011 0.0094  0.0143  170 LYS   A CD  
1364 C  CE  . LYS   A 169 ? 0.2929 0.3055 0.2772 -0.0194 -0.0374 -0.0192 170 LYS   A CE  
1365 N  N   . GLY   A 170 ? 0.1385 0.1114 0.1538 -0.0121 0.0226  0.0168  171 GLY   A N   
1366 C  CA  . GLY   A 170 ? 0.1505 0.1146 0.1795 -0.0072 0.0093  0.0153  171 GLY   A CA  
1367 C  C   . GLY   A 170 ? 0.1628 0.1165 0.1628 -0.0055 0.0169  0.0337  171 GLY   A C   
1368 O  O   . GLY   A 170 ? 0.2187 0.1224 0.2132 -0.0005 0.0024  0.0429  171 GLY   A O   
1369 N  N   A LYS   A 171 ? 0.1502 0.1242 0.1448 -0.0051 0.0170  0.0350  172 LYS   A N   
1370 N  N   B LYS   A 171 ? 0.1440 0.1216 0.1423 -0.0041 0.0170  0.0340  172 LYS   A N   
1371 C  CA  A LYS   A 171 ? 0.1595 0.1505 0.1423 0.0113  0.0199  0.0274  172 LYS   A CA  
1372 C  CA  B LYS   A 171 ? 0.1504 0.1437 0.1385 0.0096  0.0198  0.0272  172 LYS   A CA  
1373 C  C   A LYS   A 171 ? 0.1436 0.1397 0.1154 0.0083  0.0113  0.0229  172 LYS   A C   
1374 C  C   B LYS   A 171 ? 0.1439 0.1349 0.1141 0.0088  0.0141  0.0229  172 LYS   A C   
1375 O  O   A LYS   A 171 ? 0.1344 0.1214 0.1050 0.0006  0.0059  0.0119  172 LYS   A O   
1376 O  O   B LYS   A 171 ? 0.1284 0.1154 0.1010 -0.0054 0.0050  0.0140  172 LYS   A O   
1377 C  CB  A LYS   A 171 ? 0.1655 0.1785 0.1283 0.0147  0.0063  0.0094  172 LYS   A CB  
1378 C  CB  B LYS   A 171 ? 0.1420 0.1632 0.1252 0.0099  0.0087  0.0153  172 LYS   A CB  
1379 C  CG  A LYS   A 171 ? 0.1911 0.2103 0.1414 0.0306  0.0218  -0.0022 172 LYS   A CG  
1380 C  CG  B LYS   A 171 ? 0.1484 0.1855 0.1298 0.0163  0.0121  0.0156  172 LYS   A CG  
1381 C  CD  A LYS   A 171 ? 0.2084 0.2603 0.1423 0.0535  0.0466  -0.0008 172 LYS   A CD  
1382 C  CD  B LYS   A 171 ? 0.1700 0.2089 0.1167 0.0453  -0.0035 -0.0004 172 LYS   A CD  
1383 N  N   . SER   A 172 ? 0.1605 0.1653 0.1111 0.0292  0.0200  0.0443  173 SER   A N   
1384 C  CA  . SER   A 172 ? 0.1536 0.1773 0.1233 0.0376  0.0088  0.0241  173 SER   A CA  
1385 C  C   . SER   A 172 ? 0.1511 0.1801 0.1050 0.0428  0.0037  0.0179  173 SER   A C   
1386 O  O   . SER   A 172 ? 0.1756 0.2173 0.1077 0.0382  0.0056  0.0230  173 SER   A O   
1387 C  CB  . SER   A 172 ? 0.1780 0.2098 0.1358 0.0448  -0.0037 0.0075  173 SER   A CB  
1388 O  OG  . SER   A 172 ? 0.2347 0.1904 0.1905 0.0233  -0.0213 0.0335  173 SER   A OG  
1389 N  N   . ALA   A 173 ? 0.1571 0.1833 0.1053 0.0322  -0.0052 0.0254  174 ALA   A N   
1390 C  CA  . ALA   A 173 ? 0.1729 0.1900 0.1128 0.0349  -0.0103 0.0188  174 ALA   A CA  
1391 C  C   . ALA   A 173 ? 0.1471 0.1711 0.1128 0.0243  -0.0135 0.0138  174 ALA   A C   
1392 O  O   . ALA   A 173 ? 0.1460 0.1584 0.1023 0.0334  -0.0040 0.0216  174 ALA   A O   
1393 C  CB  . ALA   A 173 ? 0.1953 0.2142 0.1125 0.0357  -0.0182 -0.0057 174 ALA   A CB  
1394 N  N   A ASP   A 174 ? 0.1615 0.1589 0.1021 0.0172  -0.0209 0.0188  175 ASP   A N   
1395 N  N   B ASP   A 174 ? 0.1418 0.1566 0.1195 0.0273  -0.0153 0.0176  175 ASP   A N   
1396 C  CA  A ASP   A 174 ? 0.1627 0.1746 0.1111 0.0184  -0.0305 0.0127  175 ASP   A CA  
1397 C  CA  B ASP   A 174 ? 0.1551 0.1661 0.1389 0.0315  -0.0233 0.0010  175 ASP   A CA  
1398 C  C   A ASP   A 174 ? 0.1457 0.1610 0.1362 0.0258  -0.0165 0.0044  175 ASP   A C   
1399 C  C   B ASP   A 174 ? 0.1551 0.1490 0.1611 0.0196  -0.0143 -0.0106 175 ASP   A C   
1400 O  O   A ASP   A 174 ? 0.1818 0.1722 0.1277 0.0092  0.0095  0.0003  175 ASP   A O   
1401 O  O   B ASP   A 174 ? 0.1646 0.1530 0.1812 0.0010  -0.0106 -0.0211 175 ASP   A O   
1402 C  CB  A ASP   A 174 ? 0.1789 0.2150 0.1501 0.0162  -0.0388 0.0305  175 ASP   A CB  
1403 C  CB  B ASP   A 174 ? 0.1876 0.1713 0.1699 0.0309  -0.0376 0.0033  175 ASP   A CB  
1404 C  CG  A ASP   A 174 ? 0.2217 0.2609 0.1850 0.0013  -0.0344 0.0375  175 ASP   A CG  
1405 C  CG  B ASP   A 174 ? 0.2089 0.2039 0.1805 0.0194  -0.0106 0.0045  175 ASP   A CG  
1406 O  OD1 A ASP   A 174 ? 0.1955 0.2960 0.2438 -0.0203 -0.0500 0.0379  175 ASP   A OD1 
1407 O  OD1 B ASP   A 174 ? 0.1870 0.2363 0.1975 0.0356  -0.0202 0.0322  175 ASP   A OD1 
1408 O  OD2 A ASP   A 174 ? 0.2925 0.3189 0.2047 -0.0339 -0.0390 0.0279  175 ASP   A OD2 
1409 O  OD2 B ASP   A 174 ? 0.3027 0.2136 0.2539 0.0234  0.0000  0.0217  175 ASP   A OD2 
1410 N  N   . PHE   A 175 ? 0.1329 0.1498 0.1378 0.0096  -0.0059 -0.0011 176 PHE   A N   
1411 C  CA  . PHE   A 175 ? 0.1232 0.1297 0.1540 0.0017  -0.0140 -0.0070 176 PHE   A CA  
1412 C  C   . PHE   A 175 ? 0.1315 0.1186 0.1380 0.0048  -0.0192 0.0014  176 PHE   A C   
1413 O  O   . PHE   A 175 ? 0.1654 0.1990 0.1554 0.0615  -0.0393 -0.0268 176 PHE   A O   
1414 C  CB  . PHE   A 175 ? 0.1383 0.1111 0.1742 0.0097  -0.0159 -0.0043 176 PHE   A CB  
1415 C  CG  . PHE   A 175 ? 0.1543 0.1083 0.1634 0.0019  -0.0037 -0.0100 176 PHE   A CG  
1416 C  CD1 . PHE   A 175 ? 0.1862 0.1178 0.1714 0.0007  0.0141  -0.0075 176 PHE   A CD1 
1417 C  CD2 . PHE   A 175 ? 0.1528 0.1279 0.1577 0.0026  -0.0281 -0.0115 176 PHE   A CD2 
1418 C  CE1 . PHE   A 175 ? 0.1959 0.1344 0.1790 -0.0120 0.0137  -0.0071 176 PHE   A CE1 
1419 C  CE2 . PHE   A 175 ? 0.1370 0.1424 0.1661 0.0088  -0.0099 0.0051  176 PHE   A CE2 
1420 C  CZ  . PHE   A 175 ? 0.1636 0.1348 0.1682 -0.0083 -0.0017 -0.0019 176 PHE   A CZ  
1421 N  N   . THR   A 176 ? 0.1319 0.1512 0.1192 0.0192  -0.0044 0.0234  177 THR   A N   
1422 C  CA  . THR   A 176 ? 0.1176 0.1321 0.1296 0.0113  -0.0107 0.0305  177 THR   A CA  
1423 C  C   . THR   A 176 ? 0.1331 0.1127 0.1169 0.0030  -0.0166 0.0256  177 THR   A C   
1424 O  O   . THR   A 176 ? 0.1559 0.1255 0.1265 -0.0025 -0.0106 0.0201  177 THR   A O   
1425 C  CB  . THR   A 176 ? 0.1414 0.1446 0.1510 0.0168  -0.0044 0.0487  177 THR   A CB  
1426 O  OG1 . THR   A 176 ? 0.2395 0.2021 0.1430 0.0607  -0.0229 0.0456  177 THR   A OG1 
1427 C  CG2 . THR   A 176 ? 0.1758 0.1733 0.2298 0.0107  0.0064  0.0729  177 THR   A CG2 
1428 N  N   . ASN   A 177 ? 0.1280 0.1180 0.1217 0.0018  -0.0117 0.0201  178 ASN   A N   
1429 C  CA  . ASN   A 177 ? 0.1341 0.1439 0.1324 -0.0036 -0.0120 0.0274  178 ASN   A CA  
1430 C  C   . ASN   A 177 ? 0.1330 0.1413 0.1327 -0.0209 -0.0068 0.0212  178 ASN   A C   
1431 O  O   . ASN   A 177 ? 0.1675 0.1719 0.1983 -0.0367 -0.0377 0.0768  178 ASN   A O   
1432 C  CB  . ASN   A 177 ? 0.1247 0.1536 0.1419 -0.0038 -0.0199 0.0359  178 ASN   A CB  
1433 C  CG  . ASN   A 177 ? 0.1492 0.1599 0.1401 0.0070  -0.0265 0.0242  178 ASN   A CG  
1434 O  OD1 . ASN   A 177 ? 0.1714 0.1918 0.1922 0.0207  0.0014  0.0337  178 ASN   A OD1 
1435 N  ND2 . ASN   A 177 ? 0.1699 0.1412 0.1446 0.0092  -0.0243 0.0378  178 ASN   A ND2 
1436 N  N   . PHE   A 178 ? 0.1380 0.1184 0.1134 -0.0036 -0.0110 0.0280  179 PHE   A N   
1437 C  CA  . PHE   A 178 ? 0.1402 0.1126 0.1187 -0.0124 -0.0034 0.0263  179 PHE   A CA  
1438 C  C   . PHE   A 178 ? 0.1488 0.1074 0.1252 -0.0062 -0.0165 0.0197  179 PHE   A C   
1439 O  O   . PHE   A 178 ? 0.1870 0.1261 0.1198 -0.0201 -0.0068 0.0160  179 PHE   A O   
1440 C  CB  . PHE   A 178 ? 0.1536 0.1152 0.1226 -0.0008 -0.0013 0.0244  179 PHE   A CB  
1441 C  CG  . PHE   A 178 ? 0.1293 0.1135 0.1270 0.0015  -0.0038 0.0217  179 PHE   A CG  
1442 C  CD1 . PHE   A 178 ? 0.1564 0.1167 0.1297 0.0022  -0.0096 0.0178  179 PHE   A CD1 
1443 C  CD2 . PHE   A 178 ? 0.1248 0.1153 0.1270 -0.0059 -0.0088 0.0198  179 PHE   A CD2 
1444 C  CE1 . PHE   A 178 ? 0.1674 0.1165 0.1458 -0.0073 -0.0047 0.0148  179 PHE   A CE1 
1445 C  CE2 . PHE   A 178 ? 0.1218 0.1205 0.1265 0.0030  -0.0056 0.0224  179 PHE   A CE2 
1446 C  CZ  . PHE   A 178 ? 0.1418 0.1139 0.1309 0.0004  0.0020  0.0244  179 PHE   A CZ  
1447 N  N   . ASP   A 179 ? 0.1379 0.1240 0.1142 0.0018  -0.0048 0.0095  180 ASP   A N   
1448 C  CA  . ASP   A 179 ? 0.1415 0.1261 0.1279 0.0063  -0.0011 0.0069  180 ASP   A CA  
1449 C  C   . ASP   A 179 ? 0.1319 0.1120 0.1170 0.0046  0.0065  0.0086  180 ASP   A C   
1450 O  O   . ASP   A 179 ? 0.1416 0.1169 0.1306 0.0008  0.0029  0.0043  180 ASP   A O   
1451 C  CB  . ASP   A 179 ? 0.1391 0.1556 0.1436 0.0137  -0.0037 0.0063  180 ASP   A CB  
1452 C  CG  . ASP   A 179 ? 0.1390 0.2191 0.1787 0.0207  0.0102  -0.0031 180 ASP   A CG  
1453 O  OD1 . ASP   A 179 ? 0.1587 0.1765 0.1515 0.0339  0.0064  0.0136  180 ASP   A OD1 
1454 O  OD2 . ASP   A 179 ? 0.1669 0.3535 0.2421 0.0042  0.0185  -0.0311 180 ASP   A OD2 
1455 N  N   . PRO   A 180 ? 0.1366 0.1163 0.1196 0.0034  0.0036  0.0163  181 PRO   A N   
1456 C  CA  . PRO   A 180 ? 0.1408 0.1296 0.1239 0.0070  0.0015  0.0145  181 PRO   A CA  
1457 C  C   . PRO   A 180 ? 0.1301 0.1260 0.1165 0.0096  -0.0046 0.0092  181 PRO   A C   
1458 O  O   . PRO   A 180 ? 0.1305 0.1264 0.1310 0.0055  -0.0152 0.0183  181 PRO   A O   
1459 C  CB  . PRO   A 180 ? 0.1369 0.1586 0.1395 -0.0129 0.0004  0.0219  181 PRO   A CB  
1460 C  CG  . PRO   A 180 ? 0.1577 0.1525 0.1319 -0.0111 -0.0044 0.0124  181 PRO   A CG  
1461 C  CD  . PRO   A 180 ? 0.1504 0.1272 0.1263 -0.0052 0.0029  0.0154  181 PRO   A CD  
1462 N  N   . ARG   A 181 ? 0.1288 0.1400 0.1182 0.0075  0.0073  0.0153  182 ARG   A N   
1463 C  CA  . ARG   A 181 ? 0.1307 0.1401 0.1260 -0.0031 0.0065  0.0063  182 ARG   A CA  
1464 C  C   . ARG   A 181 ? 0.1157 0.1355 0.1363 0.0020  0.0052  0.0091  182 ARG   A C   
1465 O  O   . ARG   A 181 ? 0.1535 0.1361 0.1537 -0.0023 0.0098  0.0182  182 ARG   A O   
1466 C  CB  . ARG   A 181 ? 0.1495 0.1352 0.1352 0.0003  0.0220  0.0015  182 ARG   A CB  
1467 C  CG  . ARG   A 181 ? 0.1913 0.1513 0.1478 0.0088  0.0260  -0.0031 182 ARG   A CG  
1468 C  CD  . ARG   A 181 ? 0.2079 0.1525 0.1733 0.0270  0.0410  0.0061  182 ARG   A CD  
1469 N  NE  . ARG   A 181 ? 0.2032 0.1834 0.1910 0.0514  0.0407  0.0185  182 ARG   A NE  
1470 C  CZ  . ARG   A 181 ? 0.2211 0.2361 0.2111 0.0722  0.0375  0.0293  182 ARG   A CZ  
1471 N  NH1 . ARG   A 181 ? 0.2143 0.3049 0.2720 0.1193  0.0308  0.0209  182 ARG   A NH1 
1472 N  NH2 . ARG   A 181 ? 0.2142 0.3183 0.2543 0.1041  0.0378  0.0208  182 ARG   A NH2 
1473 N  N   . GLY   A 182 ? 0.1229 0.1305 0.1338 0.0062  -0.0068 0.0075  183 GLY   A N   
1474 C  CA  . GLY   A 182 ? 0.1406 0.1349 0.1492 -0.0019 -0.0094 0.0024  183 GLY   A CA  
1475 C  C   . GLY   A 182 ? 0.1467 0.1139 0.1526 -0.0013 -0.0141 0.0060  183 GLY   A C   
1476 O  O   . GLY   A 182 ? 0.1826 0.1263 0.1903 -0.0057 -0.0256 -0.0021 183 GLY   A O   
1477 N  N   . LEU   A 183 ? 0.1329 0.1095 0.1355 0.0027  -0.0085 0.0056  184 LEU   A N   
1478 C  CA  . LEU   A 183 ? 0.1318 0.1063 0.1417 0.0053  -0.0069 0.0115  184 LEU   A CA  
1479 C  C   . LEU   A 183 ? 0.1298 0.1177 0.1397 -0.0040 -0.0102 0.0152  184 LEU   A C   
1480 O  O   . LEU   A 183 ? 0.1629 0.1487 0.1672 0.0159  -0.0063 0.0395  184 LEU   A O   
1481 C  CB  . LEU   A 183 ? 0.1268 0.1296 0.1447 0.0117  -0.0072 0.0176  184 LEU   A CB  
1482 C  CG  . LEU   A 183 ? 0.1456 0.1579 0.1462 0.0199  -0.0022 0.0249  184 LEU   A CG  
1483 C  CD1 . LEU   A 183 ? 0.1662 0.1922 0.1522 0.0099  -0.0098 0.0391  184 LEU   A CD1 
1484 C  CD2 . LEU   A 183 ? 0.2000 0.1707 0.1523 0.0319  0.0077  0.0038  184 LEU   A CD2 
1485 N  N   . LEU   A 184 ? 0.1331 0.1268 0.1370 -0.0060 -0.0093 0.0208  185 LEU   A N   
1486 C  CA  . LEU   A 184 ? 0.1285 0.1399 0.1395 -0.0278 -0.0132 0.0194  185 LEU   A CA  
1487 C  C   . LEU   A 184 ? 0.1663 0.1516 0.1512 -0.0425 -0.0257 0.0252  185 LEU   A C   
1488 O  O   . LEU   A 184 ? 0.2400 0.2095 0.1981 -0.0948 -0.0832 0.0725  185 LEU   A O   
1489 C  CB  . LEU   A 184 ? 0.1338 0.1623 0.1247 -0.0228 -0.0063 0.0148  185 LEU   A CB  
1490 C  CG  . LEU   A 184 ? 0.1334 0.1611 0.1566 -0.0058 -0.0014 0.0048  185 LEU   A CG  
1491 C  CD1 . LEU   A 184 ? 0.1516 0.1915 0.1714 0.0089  0.0020  0.0081  185 LEU   A CD1 
1492 C  CD2 . LEU   A 184 ? 0.1579 0.1733 0.2242 0.0040  -0.0401 0.0172  185 LEU   A CD2 
1493 N  N   . PRO   A 185 ? 0.1359 0.1302 0.1340 -0.0158 -0.0088 0.0227  186 PRO   A N   
1494 C  CA  . PRO   A 185 ? 0.1437 0.1270 0.1589 -0.0102 -0.0106 0.0201  186 PRO   A CA  
1495 C  C   . PRO   A 185 ? 0.1170 0.1227 0.1658 -0.0242 -0.0190 0.0205  186 PRO   A C   
1496 O  O   . PRO   A 185 ? 0.1156 0.1315 0.2157 -0.0109 -0.0186 0.0270  186 PRO   A O   
1497 C  CB  . PRO   A 185 ? 0.1349 0.1389 0.1614 0.0030  0.0086  0.0274  186 PRO   A CB  
1498 C  CG  . PRO   A 185 ? 0.1275 0.1260 0.1323 0.0198  0.0038  0.0115  186 PRO   A CG  
1499 C  CD  . PRO   A 185 ? 0.1112 0.1348 0.1268 0.0080  0.0077  0.0084  186 PRO   A CD  
1500 N  N   . GLU   A 186 ? 0.1379 0.1355 0.1546 -0.0305 -0.0054 0.0184  187 GLU   A N   
1501 C  CA  . GLU   A 186 ? 0.1146 0.1630 0.1653 -0.0257 -0.0160 0.0143  187 GLU   A CA  
1502 C  C   . GLU   A 186 ? 0.1030 0.1396 0.1741 -0.0106 -0.0060 0.0075  187 GLU   A C   
1503 O  O   . GLU   A 186 ? 0.1311 0.1782 0.2184 0.0184  -0.0072 0.0024  187 GLU   A O   
1504 C  CB  A GLU   A 186 ? 0.1371 0.1930 0.2182 -0.0400 -0.0174 0.0087  187 GLU   A CB  
1505 C  CB  B GLU   A 186 ? 0.1394 0.1809 0.1929 -0.0450 -0.0262 0.0019  187 GLU   A CB  
1506 C  CG  A GLU   A 186 ? 0.1501 0.2203 0.2637 -0.0298 -0.0087 0.0210  187 GLU   A CG  
1507 C  CG  B GLU   A 186 ? 0.1706 0.1674 0.2100 -0.0348 -0.0404 0.0006  187 GLU   A CG  
1508 C  CD  A GLU   A 186 ? 0.1657 0.2173 0.3066 -0.0174 -0.0020 0.0258  187 GLU   A CD  
1509 C  CD  B GLU   A 186 ? 0.1775 0.1768 0.2550 -0.0417 -0.0567 0.0015  187 GLU   A CD  
1510 O  OE1 A GLU   A 186 ? 0.2260 0.2107 0.3594 -0.0333 -0.0130 0.0214  187 GLU   A OE1 
1511 O  OE1 B GLU   A 186 ? 0.1927 0.2221 0.3234 -0.0471 -0.0319 0.0092  187 GLU   A OE1 
1512 O  OE2 A GLU   A 186 ? 0.2506 0.2312 0.3419 -0.0327 0.0375  0.0957  187 GLU   A OE2 
1513 O  OE2 B GLU   A 186 ? 0.2054 0.1971 0.3342 -0.0214 -0.0921 -0.0116 187 GLU   A OE2 
1514 N  N   . SER   A 187 ? 0.1054 0.1449 0.1628 -0.0070 -0.0143 0.0056  188 SER   A N   
1515 C  CA  . SER   A 187 ? 0.1168 0.1474 0.1613 -0.0123 0.0106  0.0013  188 SER   A CA  
1516 C  C   . SER   A 187 ? 0.0994 0.1624 0.1457 -0.0129 -0.0056 0.0022  188 SER   A C   
1517 O  O   . SER   A 187 ? 0.1104 0.1896 0.1523 -0.0189 0.0044  -0.0181 188 SER   A O   
1518 C  CB  . SER   A 187 ? 0.1377 0.1720 0.1674 -0.0171 -0.0094 0.0137  188 SER   A CB  
1519 O  OG  . SER   A 187 ? 0.1666 0.1878 0.1621 -0.0248 -0.0077 0.0146  188 SER   A OG  
1520 N  N   . LEU   A 188 ? 0.1066 0.1487 0.1557 -0.0119 -0.0039 -0.0095 189 LEU   A N   
1521 C  CA  . LEU   A 188 ? 0.1187 0.1489 0.1680 -0.0141 -0.0198 0.0018  189 LEU   A CA  
1522 C  C   . LEU   A 188 ? 0.1154 0.1551 0.1519 -0.0261 -0.0031 -0.0062 189 LEU   A C   
1523 O  O   . LEU   A 188 ? 0.1612 0.1838 0.1720 -0.0439 -0.0232 -0.0051 189 LEU   A O   
1524 C  CB  . LEU   A 188 ? 0.1456 0.1568 0.2085 -0.0211 -0.0179 0.0131  189 LEU   A CB  
1525 C  CG  . LEU   A 188 ? 0.1425 0.1930 0.2387 -0.0212 -0.0286 0.0429  189 LEU   A CG  
1526 C  CD1 . LEU   A 188 ? 0.1988 0.1757 0.2856 -0.0151 -0.0404 0.0515  189 LEU   A CD1 
1527 C  CD2 . LEU   A 188 ? 0.1800 0.2642 0.2004 -0.0225 -0.0455 0.0477  189 LEU   A CD2 
1528 N  N   . ASP   A 189 ? 0.1033 0.1623 0.1314 -0.0126 0.0120  -0.0101 190 ASP   A N   
1529 C  CA  . ASP   A 189 ? 0.1095 0.1697 0.1217 -0.0151 0.0094  -0.0101 190 ASP   A CA  
1530 C  C   . ASP   A 189 ? 0.1012 0.1447 0.1144 -0.0144 0.0068  -0.0093 190 ASP   A C   
1531 O  O   . ASP   A 189 ? 0.0988 0.1471 0.1171 -0.0173 0.0019  -0.0134 190 ASP   A O   
1532 C  CB  . ASP   A 189 ? 0.1203 0.2038 0.1493 -0.0400 0.0081  0.0140  190 ASP   A CB  
1533 C  CG  . ASP   A 189 ? 0.1640 0.2472 0.1969 -0.0583 0.0131  0.0148  190 ASP   A CG  
1534 O  OD1 . ASP   A 189 ? 0.1606 0.3347 0.2316 -0.0293 0.0450  -0.0307 190 ASP   A OD1 
1535 O  OD2 . ASP   A 189 ? 0.2221 0.3173 0.2371 -0.0792 0.0325  0.0547  190 ASP   A OD2 
1536 N  N   . TYR   A 190 ? 0.1028 0.1479 0.1036 -0.0116 0.0099  -0.0009 191 TYR   A N   
1537 C  CA  . TYR   A 190 ? 0.0967 0.1408 0.0977 -0.0096 0.0073  0.0070  191 TYR   A CA  
1538 C  C   . TYR   A 190 ? 0.1021 0.1269 0.0964 -0.0041 0.0084  0.0108  191 TYR   A C   
1539 O  O   . TYR   A 190 ? 0.1065 0.1412 0.1007 -0.0047 0.0127  0.0042  191 TYR   A O   
1540 C  CB  . TYR   A 190 ? 0.1126 0.1494 0.1065 -0.0155 -0.0015 0.0146  191 TYR   A CB  
1541 C  CG  . TYR   A 190 ? 0.1229 0.1283 0.1090 -0.0143 -0.0062 0.0214  191 TYR   A CG  
1542 C  CD1 . TYR   A 190 ? 0.1278 0.1490 0.1210 -0.0250 -0.0071 0.0105  191 TYR   A CD1 
1543 C  CD2 . TYR   A 190 ? 0.1287 0.1373 0.1235 -0.0152 -0.0058 0.0121  191 TYR   A CD2 
1544 C  CE1 . TYR   A 190 ? 0.1343 0.1428 0.1511 -0.0240 -0.0130 0.0097  191 TYR   A CE1 
1545 C  CE2 . TYR   A 190 ? 0.1327 0.1397 0.1428 -0.0069 -0.0124 0.0155  191 TYR   A CE2 
1546 C  CZ  . TYR   A 190 ? 0.1384 0.1273 0.1457 -0.0205 -0.0067 0.0032  191 TYR   A CZ  
1547 O  OH  . TYR   A 190 ? 0.1624 0.1460 0.1538 -0.0038 -0.0160 0.0016  191 TYR   A OH  
1548 N  N   . TRP   A 191 ? 0.0982 0.1191 0.0876 -0.0052 0.0065  -0.0015 192 TRP   A N   
1549 C  CA  . TRP   A 191 ? 0.1007 0.1160 0.0935 -0.0073 0.0072  0.0018  192 TRP   A CA  
1550 C  C   . TRP   A 191 ? 0.1037 0.1105 0.0902 -0.0010 0.0084  -0.0069 192 TRP   A C   
1551 O  O   . TRP   A 191 ? 0.1267 0.1358 0.0888 -0.0240 -0.0003 0.0057  192 TRP   A O   
1552 C  CB  . TRP   A 191 ? 0.1061 0.1201 0.1073 -0.0028 0.0046  0.0013  192 TRP   A CB  
1553 C  CG  . TRP   A 191 ? 0.0976 0.1221 0.1192 0.0090  0.0046  0.0140  192 TRP   A CG  
1554 C  CD1 . TRP   A 191 ? 0.1282 0.1280 0.1188 0.0061  -0.0030 0.0122  192 TRP   A CD1 
1555 C  CD2 . TRP   A 191 ? 0.1047 0.1300 0.1272 0.0120  0.0035  0.0074  192 TRP   A CD2 
1556 N  NE1 . TRP   A 191 ? 0.1586 0.1246 0.1381 0.0092  0.0056  0.0269  192 TRP   A NE1 
1557 C  CE2 . TRP   A 191 ? 0.1356 0.1218 0.1429 0.0066  -0.0021 0.0107  192 TRP   A CE2 
1558 C  CE3 . TRP   A 191 ? 0.0958 0.1467 0.1350 0.0068  0.0092  -0.0036 192 TRP   A CE3 
1559 C  CZ2 . TRP   A 191 ? 0.1376 0.1188 0.1756 0.0035  -0.0032 0.0104  192 TRP   A CZ2 
1560 C  CZ3 . TRP   A 191 ? 0.1097 0.1646 0.1596 0.0060  0.0055  -0.0218 192 TRP   A CZ3 
1561 C  CH2 . TRP   A 191 ? 0.1343 0.1432 0.1841 0.0072  -0.0130 -0.0237 192 TRP   A CH2 
1562 N  N   . THR   A 192 ? 0.1021 0.1153 0.0837 -0.0087 0.0012  0.0011  193 THR   A N   
1563 C  CA  . THR   A 192 ? 0.0953 0.1217 0.0855 -0.0048 0.0037  -0.0013 193 THR   A CA  
1564 C  C   . THR   A 192 ? 0.1031 0.1179 0.0836 -0.0056 0.0037  -0.0035 193 THR   A C   
1565 O  O   . THR   A 192 ? 0.1005 0.1378 0.0908 -0.0085 0.0055  0.0003  193 THR   A O   
1566 C  CB  . THR   A 192 ? 0.1051 0.1161 0.0946 -0.0019 0.0040  -0.0044 193 THR   A CB  
1567 O  OG1 . THR   A 192 ? 0.1156 0.1147 0.1127 0.0068  0.0050  -0.0046 193 THR   A OG1 
1568 C  CG2 . THR   A 192 ? 0.1087 0.1381 0.1065 0.0060  0.0176  -0.0026 193 THR   A CG2 
1569 N  N   . TYR   A 193 ? 0.0955 0.1157 0.0862 -0.0024 -0.0010 -0.0025 194 TYR   A N   
1570 C  CA  . TYR   A 193 ? 0.1003 0.1189 0.0863 0.0007  -0.0012 -0.0042 194 TYR   A CA  
1571 C  C   . TYR   A 193 ? 0.0863 0.1104 0.0889 0.0028  0.0013  -0.0049 194 TYR   A C   
1572 O  O   . TYR   A 193 ? 0.0977 0.1128 0.0893 -0.0005 -0.0027 -0.0031 194 TYR   A O   
1573 C  CB  . TYR   A 193 ? 0.1051 0.1179 0.0906 -0.0046 -0.0047 0.0061  194 TYR   A CB  
1574 C  CG  . TYR   A 193 ? 0.0980 0.1058 0.1018 -0.0002 -0.0009 -0.0040 194 TYR   A CG  
1575 C  CD1 . TYR   A 193 ? 0.0949 0.1034 0.1050 0.0023  0.0020  -0.0005 194 TYR   A CD1 
1576 C  CD2 . TYR   A 193 ? 0.1019 0.1164 0.0990 0.0052  -0.0074 -0.0065 194 TYR   A CD2 
1577 C  CE1 . TYR   A 193 ? 0.0932 0.0950 0.1053 0.0049  -0.0057 -0.0031 194 TYR   A CE1 
1578 C  CE2 . TYR   A 193 ? 0.0963 0.1064 0.1003 -0.0021 0.0022  -0.0023 194 TYR   A CE2 
1579 C  CZ  . TYR   A 193 ? 0.0917 0.0959 0.0987 0.0042  0.0005  -0.0003 194 TYR   A CZ  
1580 O  OH  . TYR   A 193 ? 0.1032 0.1024 0.1015 0.0018  0.0058  -0.0016 194 TYR   A OH  
1581 N  N   . PRO   A 194 ? 0.1006 0.1176 0.0868 -0.0033 0.0003  -0.0149 195 PRO   A N   
1582 C  CA  . PRO   A 194 ? 0.0931 0.1123 0.1024 0.0045  -0.0007 -0.0146 195 PRO   A CA  
1583 C  C   . PRO   A 194 ? 0.0944 0.0895 0.0945 -0.0007 0.0003  -0.0061 195 PRO   A C   
1584 O  O   . PRO   A 194 ? 0.1017 0.1212 0.0963 0.0111  0.0020  -0.0025 195 PRO   A O   
1585 C  CB  . PRO   A 194 ? 0.1090 0.1238 0.1141 -0.0054 0.0055  -0.0239 195 PRO   A CB  
1586 C  CG  . PRO   A 194 ? 0.1210 0.1493 0.1001 -0.0038 0.0002  -0.0305 195 PRO   A CG  
1587 C  CD  . PRO   A 194 ? 0.1189 0.1462 0.0943 -0.0097 0.0061  -0.0078 195 PRO   A CD  
1588 N  N   . GLY   A 195 ? 0.0897 0.0967 0.0895 0.0078  0.0025  -0.0047 196 GLY   A N   
1589 C  CA  . GLY   A 195 ? 0.0904 0.0932 0.0969 0.0042  0.0027  -0.0039 196 GLY   A CA  
1590 C  C   . GLY   A 195 ? 0.0861 0.0816 0.0953 -0.0071 -0.0039 -0.0095 196 GLY   A C   
1591 O  O   . GLY   A 195 ? 0.1043 0.0940 0.1049 -0.0055 0.0084  -0.0152 196 GLY   A O   
1592 N  N   . SER   A 196 ? 0.0889 0.0934 0.0957 -0.0074 0.0035  -0.0112 197 SER   A N   
1593 C  CA  . SER   A 196 ? 0.0864 0.0946 0.1003 -0.0094 0.0083  -0.0088 197 SER   A CA  
1594 C  C   . SER   A 196 ? 0.0793 0.0853 0.0995 -0.0044 0.0025  -0.0059 197 SER   A C   
1595 O  O   . SER   A 196 ? 0.0872 0.0896 0.0987 -0.0037 0.0042  -0.0043 197 SER   A O   
1596 C  CB  . SER   A 196 ? 0.0920 0.0957 0.1058 -0.0104 0.0033  -0.0081 197 SER   A CB  
1597 O  OG  . SER   A 196 ? 0.0882 0.0975 0.1101 -0.0066 0.0008  -0.0060 197 SER   A OG  
1598 N  N   . LEU   A 197 ? 0.0853 0.0907 0.0939 -0.0041 0.0059  -0.0130 198 LEU   A N   
1599 C  CA  . LEU   A 197 ? 0.0872 0.0983 0.0990 -0.0049 0.0038  -0.0053 198 LEU   A CA  
1600 C  C   . LEU   A 197 ? 0.0845 0.0936 0.0903 -0.0022 0.0061  -0.0054 198 LEU   A C   
1601 O  O   . LEU   A 197 ? 0.0848 0.1080 0.1055 0.0005  -0.0034 -0.0112 198 LEU   A O   
1602 C  CB  . LEU   A 197 ? 0.0885 0.1008 0.1090 -0.0057 0.0032  0.0013  198 LEU   A CB  
1603 C  CG  . LEU   A 197 ? 0.1179 0.1042 0.1228 -0.0113 0.0058  0.0074  198 LEU   A CG  
1604 C  CD1 . LEU   A 197 ? 0.1174 0.1086 0.1387 -0.0158 0.0061  0.0074  198 LEU   A CD1 
1605 C  CD2 . LEU   A 197 ? 0.1286 0.1125 0.1456 0.0140  0.0176  0.0167  198 LEU   A CD2 
1606 N  N   . THR   A 198 ? 0.0857 0.0919 0.0917 0.0034  -0.0011 -0.0078 199 THR   A N   
1607 C  CA  . THR   A 198 ? 0.0876 0.0945 0.0927 0.0024  -0.0067 -0.0047 199 THR   A CA  
1608 C  C   . THR   A 198 ? 0.0770 0.0966 0.1057 0.0028  -0.0063 -0.0076 199 THR   A C   
1609 O  O   . THR   A 198 ? 0.0886 0.1054 0.1123 0.0059  0.0049  -0.0068 199 THR   A O   
1610 C  CB  . THR   A 198 ? 0.0985 0.0889 0.0973 0.0004  -0.0023 -0.0128 199 THR   A CB  
1611 O  OG1 . THR   A 198 ? 0.0994 0.0923 0.0996 -0.0046 -0.0039 -0.0030 199 THR   A OG1 
1612 C  CG2 . THR   A 198 ? 0.1000 0.0968 0.1073 -0.0035 0.0061  -0.0037 199 THR   A CG2 
1613 N  N   . THR   A 199 ? 0.0841 0.1076 0.1088 0.0007  0.0054  -0.0097 200 THR   A N   
1614 C  CA  . THR   A 199 ? 0.1025 0.1093 0.1228 -0.0041 0.0149  -0.0127 200 THR   A CA  
1615 C  C   . THR   A 199 ? 0.0968 0.1149 0.1264 -0.0045 0.0105  -0.0147 200 THR   A C   
1616 O  O   . THR   A 199 ? 0.1024 0.1113 0.1269 -0.0196 0.0138  -0.0161 200 THR   A O   
1617 C  CB  . THR   A 199 ? 0.1116 0.1230 0.1195 -0.0068 0.0105  -0.0080 200 THR   A CB  
1618 O  OG1 . THR   A 199 ? 0.2677 0.1491 0.1288 0.0407  -0.0184 0.0008  200 THR   A OG1 
1619 C  CG2 . THR   A 199 ? 0.1561 0.1397 0.1275 -0.0245 -0.0109 -0.0083 200 THR   A CG2 
1620 N  N   . PRO   A 200 ? 0.0915 0.1261 0.1203 -0.0100 0.0090  -0.0152 201 PRO   A N   
1621 C  CA  . PRO   A 200 ? 0.1066 0.1289 0.1296 -0.0211 0.0076  -0.0086 201 PRO   A CA  
1622 C  C   . PRO   A 200 ? 0.1223 0.1384 0.1169 -0.0232 0.0072  -0.0032 201 PRO   A C   
1623 O  O   . PRO   A 200 ? 0.1656 0.1695 0.1303 -0.0061 -0.0082 -0.0100 201 PRO   A O   
1624 C  CB  . PRO   A 200 ? 0.0983 0.1544 0.1358 -0.0211 0.0150  -0.0077 201 PRO   A CB  
1625 C  CG  . PRO   A 200 ? 0.1066 0.1561 0.1383 -0.0098 0.0129  -0.0159 201 PRO   A CG  
1626 C  CD  . PRO   A 200 ? 0.1007 0.1418 0.1212 -0.0136 0.0119  -0.0161 201 PRO   A CD  
1627 N  N   . PRO   A 201 ? 0.1219 0.1288 0.1203 -0.0227 0.0045  0.0032  202 PRO   A N   
1628 C  CA  . PRO   A 201 ? 0.1268 0.1307 0.1267 -0.0262 0.0105  -0.0071 202 PRO   A CA  
1629 C  C   . PRO   A 201 ? 0.1020 0.1173 0.1326 -0.0171 0.0097  -0.0099 202 PRO   A C   
1630 O  O   . PRO   A 201 ? 0.1110 0.1243 0.1468 -0.0226 0.0043  -0.0136 202 PRO   A O   
1631 C  CB  . PRO   A 201 ? 0.1509 0.1447 0.1474 -0.0308 0.0196  0.0044  202 PRO   A CB  
1632 C  CG  . PRO   A 201 ? 0.1676 0.1485 0.1513 -0.0128 0.0073  0.0074  202 PRO   A CG  
1633 C  CD  . PRO   A 201 ? 0.1552 0.1352 0.1423 -0.0062 0.0153  0.0128  202 PRO   A CD  
1634 N  N   . LEU   A 202 ? 0.0946 0.1097 0.1161 -0.0115 0.0022  -0.0077 203 LEU   A N   
1635 C  CA  . LEU   A 202 ? 0.0906 0.1073 0.1188 -0.0031 0.0013  -0.0068 203 LEU   A CA  
1636 C  C   . LEU   A 202 ? 0.0803 0.1021 0.1199 -0.0089 0.0002  -0.0059 203 LEU   A C   
1637 O  O   . LEU   A 202 ? 0.0990 0.1133 0.1177 -0.0045 0.0003  -0.0163 203 LEU   A O   
1638 C  CB  . LEU   A 202 ? 0.0895 0.1236 0.1083 0.0000  0.0037  -0.0113 203 LEU   A CB  
1639 C  CG  . LEU   A 202 ? 0.0946 0.1239 0.1107 -0.0005 0.0043  -0.0120 203 LEU   A CG  
1640 C  CD1 . LEU   A 202 ? 0.0996 0.1296 0.1449 0.0042  0.0019  -0.0138 203 LEU   A CD1 
1641 C  CD2 . LEU   A 202 ? 0.1031 0.1102 0.1317 0.0034  -0.0035 -0.0132 203 LEU   A CD2 
1642 N  N   . LEU   A 203 ? 0.1066 0.1026 0.1202 -0.0054 0.0052  -0.0083 204 LEU   A N   
1643 C  CA  . LEU   A 203 ? 0.0977 0.0972 0.1386 -0.0060 0.0076  -0.0127 204 LEU   A CA  
1644 C  C   . LEU   A 203 ? 0.0929 0.0921 0.1271 -0.0051 0.0023  -0.0073 204 LEU   A C   
1645 O  O   . LEU   A 203 ? 0.1019 0.1030 0.1163 -0.0137 -0.0021 -0.0169 204 LEU   A O   
1646 C  CB  . LEU   A 203 ? 0.1159 0.1033 0.1578 -0.0033 0.0180  -0.0066 204 LEU   A CB  
1647 C  CG  . LEU   A 203 ? 0.1345 0.1117 0.1845 -0.0029 0.0345  0.0080  204 LEU   A CG  
1648 C  CD1 . LEU   A 203 ? 0.1498 0.1199 0.2023 -0.0038 0.0430  0.0218  204 LEU   A CD1 
1649 C  CD2 . LEU   A 203 ? 0.1473 0.1537 0.2347 -0.0438 0.0239  0.0222  204 LEU   A CD2 
1650 N  N   . GLU   A 204 ? 0.1009 0.1017 0.1226 -0.0135 -0.0004 -0.0143 205 GLU   A N   
1651 C  CA  . GLU   A 204 ? 0.1070 0.1045 0.1172 -0.0092 -0.0045 -0.0239 205 GLU   A CA  
1652 C  C   . GLU   A 204 ? 0.1039 0.1109 0.1216 -0.0048 0.0003  -0.0229 205 GLU   A C   
1653 O  O   . GLU   A 204 ? 0.1332 0.1518 0.1336 0.0163  -0.0082 -0.0348 205 GLU   A O   
1654 C  CB  . GLU   A 204 ? 0.1152 0.1214 0.1224 -0.0106 -0.0119 -0.0177 205 GLU   A CB  
1655 C  CG  . GLU   A 204 ? 0.1208 0.1251 0.1315 0.0010  -0.0124 -0.0189 205 GLU   A CG  
1656 C  CD  . GLU   A 204 ? 0.1092 0.1319 0.1333 -0.0069 -0.0090 -0.0208 205 GLU   A CD  
1657 O  OE1 . GLU   A 204 ? 0.1383 0.1615 0.1636 0.0013  -0.0319 -0.0341 205 GLU   A OE1 
1658 O  OE2 . GLU   A 204 ? 0.1234 0.1408 0.1358 -0.0036 -0.0131 -0.0132 205 GLU   A OE2 
1659 N  N   . CYS   A 205 ? 0.0993 0.0932 0.1211 -0.0092 -0.0060 -0.0208 206 CYS   A N   
1660 C  CA  . CYS   A 205 ? 0.1025 0.0967 0.1223 -0.0059 -0.0057 -0.0117 206 CYS   A CA  
1661 C  C   . CYS   A 205 ? 0.1040 0.0883 0.1201 0.0011  -0.0057 -0.0154 206 CYS   A C   
1662 O  O   . CYS   A 205 ? 0.1115 0.0901 0.1706 0.0010  -0.0230 0.0015  206 CYS   A O   
1663 C  CB  . CYS   A 205 ? 0.1111 0.0964 0.1396 -0.0070 0.0040  -0.0054 206 CYS   A CB  
1664 S  SG  . CYS   A 205 ? 0.1438 0.1118 0.1283 -0.0010 -0.0013 -0.0069 206 CYS   A SG  
1665 N  N   . VAL   A 206 ? 0.0938 0.0867 0.1207 0.0014  -0.0069 -0.0051 207 VAL   A N   
1666 C  CA  . VAL   A 206 ? 0.0992 0.0765 0.1289 -0.0081 -0.0057 -0.0009 207 VAL   A CA  
1667 C  C   . VAL   A 206 ? 0.0981 0.0828 0.1147 -0.0010 -0.0076 -0.0035 207 VAL   A C   
1668 O  O   . VAL   A 206 ? 0.1041 0.1127 0.1249 0.0029  0.0010  0.0153  207 VAL   A O   
1669 C  CB  . VAL   A 206 ? 0.0990 0.0880 0.1246 -0.0010 0.0029  0.0008  207 VAL   A CB  
1670 C  CG1 . VAL   A 206 ? 0.1066 0.0925 0.1109 -0.0026 -0.0020 -0.0092 207 VAL   A CG1 
1671 C  CG2 . VAL   A 206 ? 0.1081 0.0952 0.1202 0.0011  0.0035  0.0004  207 VAL   A CG2 
1672 N  N   . THR   A 207 ? 0.0966 0.0797 0.1042 -0.0045 -0.0038 0.0035  208 THR   A N   
1673 C  CA  . THR   A 207 ? 0.1033 0.0902 0.0948 -0.0006 -0.0034 -0.0012 208 THR   A CA  
1674 C  C   . THR   A 207 ? 0.0920 0.0923 0.0916 -0.0011 -0.0002 -0.0020 208 THR   A C   
1675 O  O   . THR   A 207 ? 0.1095 0.0886 0.1032 -0.0002 -0.0106 -0.0022 208 THR   A O   
1676 C  CB  . THR   A 207 ? 0.1012 0.1038 0.1094 -0.0044 0.0051  -0.0104 208 THR   A CB  
1677 O  OG1 . THR   A 207 ? 0.1302 0.1111 0.1246 -0.0040 0.0053  -0.0231 208 THR   A OG1 
1678 C  CG2 . THR   A 207 ? 0.1093 0.1153 0.1355 -0.0051 0.0127  -0.0067 208 THR   A CG2 
1679 N  N   . TRP   A 208 ? 0.0846 0.0905 0.0868 0.0049  -0.0001 -0.0031 209 TRP   A N   
1680 C  CA  . TRP   A 208 ? 0.0956 0.0879 0.0863 -0.0064 0.0004  -0.0036 209 TRP   A CA  
1681 C  C   . TRP   A 208 ? 0.0887 0.0857 0.0879 0.0060  0.0045  -0.0026 209 TRP   A C   
1682 O  O   . TRP   A 208 ? 0.0984 0.1040 0.0908 -0.0070 0.0045  -0.0033 209 TRP   A O   
1683 C  CB  . TRP   A 208 ? 0.0995 0.0920 0.0838 -0.0028 -0.0015 -0.0006 209 TRP   A CB  
1684 C  CG  . TRP   A 208 ? 0.0916 0.0804 0.0998 0.0057  0.0019  0.0000  209 TRP   A CG  
1685 C  CD1 . TRP   A 208 ? 0.0976 0.0966 0.1030 0.0002  0.0016  -0.0046 209 TRP   A CD1 
1686 C  CD2 . TRP   A 208 ? 0.0903 0.0802 0.0981 -0.0006 -0.0006 0.0010  209 TRP   A CD2 
1687 N  NE1 . TRP   A 208 ? 0.0847 0.1003 0.1151 0.0030  0.0052  -0.0002 209 TRP   A NE1 
1688 C  CE2 . TRP   A 208 ? 0.0876 0.0865 0.1103 0.0089  0.0013  -0.0062 209 TRP   A CE2 
1689 C  CE3 . TRP   A 208 ? 0.0940 0.0830 0.0969 0.0006  0.0045  -0.0007 209 TRP   A CE3 
1690 C  CZ2 . TRP   A 208 ? 0.1050 0.0923 0.1178 0.0184  0.0164  0.0017  209 TRP   A CZ2 
1691 C  CZ3 . TRP   A 208 ? 0.1029 0.1001 0.1006 0.0109  -0.0060 -0.0067 209 TRP   A CZ3 
1692 C  CH2 . TRP   A 208 ? 0.1186 0.0929 0.1044 0.0126  0.0103  -0.0054 209 TRP   A CH2 
1693 N  N   . ILE   A 209 ? 0.0893 0.0894 0.0768 -0.0046 0.0073  -0.0031 210 ILE   A N   
1694 C  CA  . ILE   A 209 ? 0.0854 0.0947 0.0914 -0.0060 0.0051  -0.0010 210 ILE   A CA  
1695 C  C   . ILE   A 209 ? 0.0920 0.0852 0.0908 -0.0006 0.0077  0.0031  210 ILE   A C   
1696 O  O   . ILE   A 209 ? 0.1293 0.0914 0.0908 -0.0008 -0.0001 0.0024  210 ILE   A O   
1697 C  CB  . ILE   A 209 ? 0.0894 0.0999 0.1028 0.0035  0.0071  -0.0032 210 ILE   A CB  
1698 C  CG1 . ILE   A 209 ? 0.1002 0.1047 0.1346 0.0129  -0.0010 -0.0164 210 ILE   A CG1 
1699 C  CG2 . ILE   A 209 ? 0.0882 0.1144 0.1125 0.0022  0.0017  -0.0051 210 ILE   A CG2 
1700 C  CD1 . ILE   A 209 ? 0.1257 0.1095 0.1689 0.0188  -0.0070 -0.0045 210 ILE   A CD1 
1701 N  N   . VAL   A 210 ? 0.0960 0.0844 0.0812 -0.0035 0.0030  0.0012  211 VAL   A N   
1702 C  CA  . VAL   A 210 ? 0.1004 0.0850 0.0902 -0.0022 0.0009  -0.0007 211 VAL   A CA  
1703 C  C   . VAL   A 210 ? 0.0983 0.0973 0.0880 -0.0028 0.0039  0.0031  211 VAL   A C   
1704 O  O   . VAL   A 210 ? 0.1114 0.1102 0.0925 -0.0159 0.0040  0.0053  211 VAL   A O   
1705 C  CB  . VAL   A 210 ? 0.1005 0.0971 0.1014 0.0013  0.0031  0.0039  211 VAL   A CB  
1706 C  CG1 . VAL   A 210 ? 0.1152 0.0906 0.1204 0.0041  -0.0023 -0.0019 211 VAL   A CG1 
1707 C  CG2 . VAL   A 210 ? 0.1047 0.1003 0.1261 0.0046  0.0025  0.0025  211 VAL   A CG2 
1708 N  N   . LEU   A 211 ? 0.0945 0.1080 0.0963 -0.0151 0.0096  0.0051  212 LEU   A N   
1709 C  CA  . LEU   A 211 ? 0.1025 0.1158 0.0969 -0.0121 0.0116  -0.0046 212 LEU   A CA  
1710 C  C   . LEU   A 211 ? 0.1052 0.1138 0.0993 -0.0139 0.0040  0.0064  212 LEU   A C   
1711 O  O   . LEU   A 211 ? 0.1136 0.1129 0.1144 -0.0118 0.0035  0.0015  212 LEU   A O   
1712 C  CB  . LEU   A 211 ? 0.1070 0.1255 0.1020 -0.0121 0.0056  0.0000  212 LEU   A CB  
1713 C  CG  . LEU   A 211 ? 0.1090 0.1276 0.1141 -0.0085 -0.0006 0.0013  212 LEU   A CG  
1714 C  CD1 . LEU   A 211 ? 0.1212 0.1446 0.1356 -0.0058 -0.0155 0.0121  212 LEU   A CD1 
1715 C  CD2 . LEU   A 211 ? 0.1308 0.1309 0.1353 -0.0017 0.0162  0.0057  212 LEU   A CD2 
1716 N  N   . LYS   A 212 ? 0.1051 0.1206 0.1143 -0.0192 0.0066  0.0096  213 LYS   A N   
1717 C  CA  . LYS   A 212 ? 0.1377 0.1263 0.1176 -0.0221 -0.0014 0.0190  213 LYS   A CA  
1718 C  C   . LYS   A 212 ? 0.1287 0.0988 0.1379 -0.0121 0.0015  0.0168  213 LYS   A C   
1719 O  O   . LYS   A 212 ? 0.1467 0.1220 0.1655 -0.0014 -0.0275 0.0163  213 LYS   A O   
1720 C  CB  . LYS   A 212 ? 0.1925 0.1684 0.1291 -0.0627 0.0000  0.0123  213 LYS   A CB  
1721 C  CG  . LYS   A 212 ? 0.2510 0.2084 0.1707 -0.0804 -0.0073 0.0289  213 LYS   A CG  
1722 C  CD  . LYS   A 212 ? 0.3437 0.2554 0.2347 -0.0705 0.0176  0.0438  213 LYS   A CD  
1723 C  CE  . LYS   A 212 ? 0.3192 0.3735 0.3673 -0.0668 0.0591  0.0079  213 LYS   A CE  
1724 N  NZ  . LYS   A 212 ? 0.4285 0.4323 0.4050 -0.0648 0.0378  -0.0032 213 LYS   A NZ  
1725 N  N   . GLU   A 213 ? 0.1126 0.1138 0.1178 -0.0142 -0.0008 0.0054  214 GLU   A N   
1726 C  CA  A GLU   A 213 ? 0.1098 0.1031 0.1261 -0.0122 0.0048  0.0078  214 GLU   A CA  
1727 C  CA  B GLU   A 213 ? 0.1189 0.1090 0.1283 -0.0164 0.0064  0.0063  214 GLU   A CA  
1728 C  C   . GLU   A 213 ? 0.1151 0.0985 0.1231 -0.0133 0.0007  0.0069  214 GLU   A C   
1729 O  O   . GLU   A 213 ? 0.1063 0.1066 0.1261 0.0005  0.0040  0.0100  214 GLU   A O   
1730 C  CB  A GLU   A 213 ? 0.1083 0.1102 0.1310 -0.0154 0.0115  0.0095  214 GLU   A CB  
1731 C  CB  B GLU   A 213 ? 0.1236 0.1283 0.1392 -0.0202 0.0148  0.0082  214 GLU   A CB  
1732 C  CG  A GLU   A 213 ? 0.1338 0.1229 0.1453 -0.0143 -0.0075 0.0066  214 GLU   A CG  
1733 C  CG  B GLU   A 213 ? 0.1624 0.1527 0.1587 -0.0290 -0.0017 -0.0003 214 GLU   A CG  
1734 C  CD  A GLU   A 213 ? 0.1296 0.1369 0.1858 -0.0238 -0.0035 0.0006  214 GLU   A CD  
1735 C  CD  B GLU   A 213 ? 0.1798 0.1858 0.1816 -0.0139 0.0005  -0.0072 214 GLU   A CD  
1736 O  OE1 A GLU   A 213 ? 0.1042 0.1445 0.1814 -0.0169 0.0001  0.0096  214 GLU   A OE1 
1737 O  OE1 B GLU   A 213 ? 0.1674 0.2306 0.1893 -0.0163 0.0053  -0.0144 214 GLU   A OE1 
1738 O  OE2 A GLU   A 213 ? 0.1619 0.1436 0.2542 -0.0275 -0.0210 -0.0121 214 GLU   A OE2 
1739 O  OE2 B GLU   A 213 ? 0.1866 0.2420 0.2026 -0.0191 -0.0142 0.0084  214 GLU   A OE2 
1740 N  N   A PRO   A 214 ? 0.1248 0.0972 0.1238 -0.0065 -0.0012 0.0076  215 PRO   A N   
1741 N  N   B PRO   A 214 ? 0.1216 0.0994 0.1277 -0.0105 0.0013  0.0069  215 PRO   A N   
1742 C  CA  A PRO   A 214 ? 0.1253 0.1054 0.1170 -0.0029 0.0047  -0.0023 215 PRO   A CA  
1743 C  CA  B PRO   A 214 ? 0.1249 0.1076 0.1163 -0.0050 0.0069  -0.0051 215 PRO   A CA  
1744 C  C   A PRO   A 214 ? 0.1193 0.0980 0.1292 -0.0199 -0.0034 -0.0056 215 PRO   A C   
1745 C  C   B PRO   A 214 ? 0.1172 0.1055 0.1243 -0.0197 0.0022  -0.0091 215 PRO   A C   
1746 O  O   A PRO   A 214 ? 0.1152 0.1130 0.1391 -0.0193 -0.0015 -0.0030 215 PRO   A O   
1747 O  O   B PRO   A 214 ? 0.1150 0.1175 0.1315 -0.0093 0.0063  -0.0089 215 PRO   A O   
1748 C  CB  A PRO   A 214 ? 0.1287 0.1037 0.1444 -0.0030 -0.0001 -0.0025 215 PRO   A CB  
1749 C  CB  B PRO   A 214 ? 0.1332 0.1034 0.1438 -0.0091 0.0035  -0.0074 215 PRO   A CB  
1750 C  CG  A PRO   A 214 ? 0.1398 0.1040 0.1609 -0.0095 0.0071  0.0032  215 PRO   A CG  
1751 C  CG  B PRO   A 214 ? 0.1403 0.1112 0.1644 -0.0156 -0.0050 0.0033  215 PRO   A CG  
1752 C  CD  A PRO   A 214 ? 0.1339 0.0954 0.1404 -0.0059 0.0043  0.0084  215 PRO   A CD  
1753 C  CD  B PRO   A 214 ? 0.1338 0.0992 0.1554 -0.0139 -0.0018 0.0074  215 PRO   A CD  
1754 N  N   . ILE   A 215 ? 0.1133 0.1079 0.1206 -0.0167 0.0013  -0.0103 216 ILE   A N   
1755 C  CA  . ILE   A 215 ? 0.1201 0.1081 0.1201 -0.0103 0.0014  -0.0118 216 ILE   A CA  
1756 C  C   . ILE   A 215 ? 0.1253 0.0989 0.1262 -0.0129 -0.0009 -0.0124 216 ILE   A C   
1757 O  O   . ILE   A 215 ? 0.1299 0.1061 0.1669 -0.0061 -0.0006 -0.0258 216 ILE   A O   
1758 C  CB  . ILE   A 215 ? 0.1240 0.1140 0.1213 0.0033  -0.0004 -0.0131 216 ILE   A CB  
1759 C  CG1 . ILE   A 215 ? 0.1279 0.1144 0.1208 -0.0057 -0.0016 -0.0025 216 ILE   A CG1 
1760 C  CG2 . ILE   A 215 ? 0.1376 0.1223 0.1386 0.0079  0.0025  -0.0126 216 ILE   A CG2 
1761 C  CD1 . ILE   A 215 ? 0.1553 0.1398 0.1441 0.0032  0.0094  0.0101  216 ILE   A CD1 
1762 N  N   A SER   A 216 ? 0.1302 0.1057 0.1353 -0.0052 -0.0161 -0.0162 217 SER   A N   
1763 N  N   C SER   A 216 ? 0.1352 0.1214 0.1387 -0.0072 -0.0222 -0.0134 217 SER   A N   
1764 C  CA  A SER   A 216 ? 0.1382 0.0939 0.1366 -0.0110 -0.0217 -0.0118 217 SER   A CA  
1765 C  CA  C SER   A 216 ? 0.1630 0.1135 0.1498 -0.0091 -0.0279 -0.0087 217 SER   A CA  
1766 C  C   A SER   A 216 ? 0.1536 0.0964 0.1377 -0.0050 -0.0232 -0.0103 217 SER   A C   
1767 C  C   C SER   A 216 ? 0.1595 0.0983 0.1456 -0.0075 -0.0257 -0.0109 217 SER   A C   
1768 O  O   A SER   A 216 ? 0.1557 0.1208 0.1451 0.0126  -0.0108 0.0070  217 SER   A O   
1769 O  O   C SER   A 216 ? 0.1414 0.1197 0.1421 -0.0052 -0.0133 0.0011  217 SER   A O   
1770 C  CB  A SER   A 216 ? 0.1334 0.0977 0.1364 -0.0132 -0.0231 0.0005  217 SER   A CB  
1771 C  CB  B SER   A 216 ? 0.1897 0.1110 0.1773 -0.0222 -0.0428 -0.0225 217 SER   A CB  
1772 C  CB  C SER   A 216 ? 0.1866 0.1320 0.1738 -0.0222 -0.0307 -0.0073 217 SER   A CB  
1773 O  OG  A SER   A 216 ? 0.1398 0.1065 0.1392 -0.0401 -0.0197 0.0098  217 SER   A OG  
1774 O  OG  B SER   A 216 ? 0.2199 0.1104 0.1585 -0.0417 -0.0354 -0.0281 217 SER   A OG  
1775 O  OG  C SER   A 216 ? 0.1951 0.2047 0.2133 -0.0331 -0.0399 0.0157  217 SER   A OG  
1776 N  N   . VAL   A 217 ? 0.1445 0.0960 0.1307 -0.0112 -0.0289 -0.0082 218 VAL   A N   
1777 C  CA  . VAL   A 217 ? 0.1418 0.0868 0.1391 -0.0102 -0.0305 -0.0123 218 VAL   A CA  
1778 C  C   . VAL   A 217 ? 0.1424 0.0885 0.1357 -0.0126 -0.0156 -0.0110 218 VAL   A C   
1779 O  O   . VAL   A 217 ? 0.1623 0.0910 0.1465 -0.0103 -0.0206 -0.0065 218 VAL   A O   
1780 C  CB  . VAL   A 217 ? 0.1527 0.0956 0.1582 -0.0137 -0.0209 -0.0008 218 VAL   A CB  
1781 C  CG1 . VAL   A 217 ? 0.1563 0.0967 0.1704 -0.0143 -0.0301 -0.0088 218 VAL   A CG1 
1782 C  CG2 . VAL   A 217 ? 0.1597 0.1029 0.1992 -0.0105 -0.0205 -0.0116 218 VAL   A CG2 
1783 N  N   . SER   A 218 ? 0.1469 0.0928 0.1284 -0.0067 -0.0138 -0.0089 219 SER   A N   
1784 C  CA  . SER   A 218 ? 0.1596 0.0751 0.1451 -0.0226 -0.0057 -0.0143 219 SER   A CA  
1785 C  C   . SER   A 218 ? 0.1580 0.0836 0.1511 -0.0145 -0.0093 -0.0024 219 SER   A C   
1786 O  O   . SER   A 218 ? 0.1489 0.0883 0.1559 -0.0116 -0.0176 0.0001  219 SER   A O   
1787 C  CB  . SER   A 218 ? 0.1497 0.1023 0.1497 -0.0176 -0.0013 -0.0151 219 SER   A CB  
1788 O  OG  . SER   A 218 ? 0.1631 0.1190 0.1631 -0.0197 -0.0163 -0.0047 219 SER   A OG  
1789 N  N   . SER   A 219 ? 0.1474 0.0758 0.1682 -0.0158 0.0018  -0.0041 220 SER   A N   
1790 C  CA  . SER   A 219 ? 0.1443 0.0950 0.1864 -0.0055 -0.0154 0.0009  220 SER   A CA  
1791 C  C   . SER   A 219 ? 0.1464 0.0982 0.1763 -0.0094 -0.0074 -0.0096 220 SER   A C   
1792 O  O   . SER   A 219 ? 0.1321 0.1209 0.2128 -0.0010 -0.0023 0.0112  220 SER   A O   
1793 C  CB  . SER   A 219 ? 0.1761 0.1355 0.2386 0.0233  -0.0026 -0.0161 220 SER   A CB  
1794 O  OG  . SER   A 219 ? 0.2613 0.1543 0.2631 0.0102  -0.0062 -0.0115 220 SER   A OG  
1795 N  N   . GLU   A 220 ? 0.1480 0.1104 0.1715 -0.0028 -0.0029 -0.0188 221 GLU   A N   
1796 C  CA  . GLU   A 220 ? 0.1591 0.1217 0.1600 0.0117  0.0003  -0.0178 221 GLU   A CA  
1797 C  C   . GLU   A 220 ? 0.1550 0.1183 0.1520 0.0042  -0.0008 -0.0091 221 GLU   A C   
1798 O  O   . GLU   A 220 ? 0.1661 0.1512 0.1569 -0.0003 0.0166  -0.0100 221 GLU   A O   
1799 C  CB  . GLU   A 220 ? 0.1816 0.1459 0.1726 0.0017  -0.0124 -0.0294 221 GLU   A CB  
1800 C  CG  . GLU   A 220 ? 0.2193 0.1618 0.1916 -0.0014 -0.0270 -0.0497 221 GLU   A CG  
1801 C  CD  . GLU   A 220 ? 0.2628 0.1457 0.2279 -0.0134 -0.0292 -0.0432 221 GLU   A CD  
1802 O  OE1 . GLU   A 220 ? 0.2191 0.1652 0.2243 -0.0282 -0.0160 -0.0249 221 GLU   A OE1 
1803 O  OE2 . GLU   A 220 ? 0.4133 0.1606 0.3325 -0.0460 0.0194  -0.0660 221 GLU   A OE2 
1804 N  N   . GLN   A 221 ? 0.1370 0.1000 0.1465 -0.0055 -0.0025 -0.0064 222 GLN   A N   
1805 C  CA  . GLN   A 221 ? 0.1369 0.0978 0.1333 -0.0122 -0.0095 -0.0006 222 GLN   A CA  
1806 C  C   . GLN   A 221 ? 0.1302 0.1109 0.1340 -0.0071 -0.0024 0.0089  222 GLN   A C   
1807 O  O   . GLN   A 221 ? 0.1454 0.1241 0.1461 -0.0146 0.0004  0.0140  222 GLN   A O   
1808 C  CB  . GLN   A 221 ? 0.1374 0.1062 0.1213 -0.0106 -0.0074 -0.0078 222 GLN   A CB  
1809 C  CG  . GLN   A 221 ? 0.1386 0.1037 0.1257 -0.0112 -0.0120 -0.0036 222 GLN   A CG  
1810 C  CD  . GLN   A 221 ? 0.1313 0.0946 0.1371 -0.0052 -0.0095 0.0003  222 GLN   A CD  
1811 O  OE1 . GLN   A 221 ? 0.1467 0.1039 0.1334 -0.0055 -0.0041 -0.0004 222 GLN   A OE1 
1812 N  NE2 . GLN   A 221 ? 0.1405 0.1091 0.1336 0.0044  -0.0016 -0.0009 222 GLN   A NE2 
1813 N  N   . VAL   A 222 ? 0.1372 0.1081 0.1419 -0.0084 -0.0015 0.0201  223 VAL   A N   
1814 C  CA  . VAL   A 222 ? 0.1457 0.1362 0.1483 -0.0175 -0.0135 0.0150  223 VAL   A CA  
1815 C  C   . VAL   A 222 ? 0.1355 0.1204 0.1535 -0.0129 -0.0087 0.0195  223 VAL   A C   
1816 O  O   . VAL   A 222 ? 0.1399 0.1361 0.1599 -0.0149 -0.0108 0.0255  223 VAL   A O   
1817 C  CB  . VAL   A 222 ? 0.1566 0.1852 0.1693 -0.0119 -0.0099 0.0390  223 VAL   A CB  
1818 C  CG1 . VAL   A 222 ? 0.1654 0.2159 0.2176 -0.0415 -0.0163 0.0385  223 VAL   A CG1 
1819 C  CG2 . VAL   A 222 ? 0.1885 0.2094 0.1779 -0.0226 -0.0146 0.0331  223 VAL   A CG2 
1820 N  N   . LEU   A 223 ? 0.1311 0.1235 0.1720 -0.0103 0.0052  0.0084  224 LEU   A N   
1821 C  CA  . LEU   A 223 ? 0.1498 0.1391 0.1936 -0.0060 0.0099  0.0020  224 LEU   A CA  
1822 C  C   . LEU   A 223 ? 0.1501 0.1388 0.1828 -0.0072 0.0108  -0.0068 224 LEU   A C   
1823 O  O   . LEU   A 223 ? 0.1397 0.1588 0.1958 -0.0074 0.0166  -0.0019 224 LEU   A O   
1824 C  CB  . LEU   A 223 ? 0.1602 0.1602 0.2403 -0.0103 0.0162  -0.0255 224 LEU   A CB  
1825 C  CG  . LEU   A 223 ? 0.2410 0.1636 0.2870 -0.0019 0.0257  -0.0247 224 LEU   A CG  
1826 C  CD1 . LEU   A 223 ? 0.2870 0.2129 0.3184 -0.0192 -0.0123 -0.0110 224 LEU   A CD1 
1827 C  CD2 . LEU   A 223 ? 0.2603 0.1919 0.3016 0.0205  -0.0081 -0.0260 224 LEU   A CD2 
1828 N  N   . LYS   A 224 ? 0.1325 0.1448 0.1549 -0.0086 0.0061  -0.0012 225 LYS   A N   
1829 C  CA  . LYS   A 224 ? 0.1465 0.1560 0.1531 -0.0128 0.0083  0.0008  225 LYS   A CA  
1830 C  C   . LYS   A 224 ? 0.1405 0.1273 0.1342 -0.0045 -0.0008 0.0101  225 LYS   A C   
1831 O  O   . LYS   A 224 ? 0.1557 0.1515 0.1343 -0.0111 0.0036  0.0142  225 LYS   A O   
1832 C  CB  . LYS   A 224 ? 0.1560 0.2148 0.1754 -0.0252 -0.0063 0.0269  225 LYS   A CB  
1833 C  CG  . LYS   A 224 ? 0.2076 0.2762 0.2057 -0.0462 -0.0248 0.0176  225 LYS   A CG  
1834 C  CD  . LYS   A 224 ? 0.2286 0.3504 0.2653 -0.0479 -0.0234 0.0016  225 LYS   A CD  
1835 C  CE  . LYS   A 224 ? 0.3139 0.3740 0.3041 -0.0297 0.0093  -0.0414 225 LYS   A CE  
1836 N  NZ  . LYS   A 224 ? 0.3100 0.3537 0.2846 -0.0349 0.0551  -0.0442 225 LYS   A NZ  
1837 N  N   . PHE   A 225 ? 0.1360 0.1230 0.1209 0.0059  0.0063  0.0105  226 PHE   A N   
1838 C  CA  . PHE   A 225 ? 0.1290 0.1123 0.1255 0.0007  0.0022  0.0131  226 PHE   A CA  
1839 C  C   . PHE   A 225 ? 0.1291 0.1058 0.1141 -0.0006 0.0071  0.0007  226 PHE   A C   
1840 O  O   . PHE   A 225 ? 0.1315 0.1147 0.1238 -0.0046 0.0101  -0.0049 226 PHE   A O   
1841 C  CB  . PHE   A 225 ? 0.1354 0.1216 0.1281 0.0132  0.0164  0.0030  226 PHE   A CB  
1842 C  CG  . PHE   A 225 ? 0.1151 0.1130 0.1490 -0.0008 0.0108  -0.0188 226 PHE   A CG  
1843 C  CD1 . PHE   A 225 ? 0.1617 0.1891 0.1548 0.0427  0.0192  -0.0096 226 PHE   A CD1 
1844 C  CD2 . PHE   A 225 ? 0.1564 0.1854 0.1902 0.0116  -0.0039 -0.0567 226 PHE   A CD2 
1845 C  CE1 . PHE   A 225 ? 0.1657 0.1832 0.1987 0.0394  0.0300  0.0072  226 PHE   A CE1 
1846 C  CE2 . PHE   A 225 ? 0.1842 0.2133 0.2101 0.0099  0.0027  -0.0750 226 PHE   A CE2 
1847 C  CZ  . PHE   A 225 ? 0.1380 0.1605 0.2459 0.0032  0.0081  -0.0703 226 PHE   A CZ  
1848 N  N   . ARG   A 226 ? 0.1232 0.1063 0.1264 0.0049  0.0063  0.0042  227 ARG   A N   
1849 C  CA  . ARG   A 226 ? 0.1340 0.1164 0.1232 0.0072  -0.0026 0.0047  227 ARG   A CA  
1850 C  C   . ARG   A 226 ? 0.1347 0.1150 0.1422 0.0040  0.0151  -0.0006 227 ARG   A C   
1851 O  O   . ARG   A 226 ? 0.1341 0.1523 0.1516 0.0205  0.0165  0.0018  227 ARG   A O   
1852 C  CB  . ARG   A 226 ? 0.1447 0.1093 0.1375 0.0064  0.0026  -0.0035 227 ARG   A CB  
1853 C  CG  . ARG   A 226 ? 0.1247 0.1122 0.1403 0.0062  0.0015  0.0076  227 ARG   A CG  
1854 C  CD  . ARG   A 226 ? 0.1802 0.1185 0.1446 0.0045  -0.0032 0.0035  227 ARG   A CD  
1855 N  NE  . ARG   A 226 ? 0.1681 0.1063 0.1424 -0.0147 -0.0085 -0.0027 227 ARG   A NE  
1856 C  CZ  . ARG   A 226 ? 0.1778 0.1277 0.1440 -0.0329 -0.0168 -0.0121 227 ARG   A CZ  
1857 N  NH1 . ARG   A 226 ? 0.2274 0.1531 0.1844 -0.0652 -0.0064 -0.0249 227 ARG   A NH1 
1858 N  NH2 . ARG   A 226 ? 0.2109 0.1286 0.1564 -0.0439 0.0073  -0.0066 227 ARG   A NH2 
1859 N  N   . LYS   A 227 ? 0.1331 0.1144 0.1141 -0.0029 0.0101  -0.0092 228 LYS   A N   
1860 C  CA  . LYS   A 227 ? 0.1547 0.1283 0.1258 -0.0111 0.0146  -0.0262 228 LYS   A CA  
1861 C  C   . LYS   A 227 ? 0.1456 0.1215 0.1139 -0.0076 0.0145  -0.0142 228 LYS   A C   
1862 O  O   . LYS   A 227 ? 0.1894 0.1339 0.1149 -0.0097 0.0192  -0.0165 228 LYS   A O   
1863 C  CB  . LYS   A 227 ? 0.1952 0.1669 0.1246 -0.0136 0.0078  -0.0390 228 LYS   A CB  
1864 C  CG  . LYS   A 227 ? 0.2265 0.2142 0.1833 -0.0598 0.0183  -0.0635 228 LYS   A CG  
1865 C  CD  . LYS   A 227 ? 0.2653 0.2883 0.2458 -0.0889 -0.0028 -0.0469 228 LYS   A CD  
1866 N  N   . LEU   A 228 ? 0.1384 0.1076 0.1117 -0.0042 0.0058  -0.0124 229 LEU   A N   
1867 C  CA  . LEU   A 228 ? 0.1365 0.1073 0.1094 0.0017  0.0133  -0.0054 229 LEU   A CA  
1868 C  C   . LEU   A 228 ? 0.1396 0.0997 0.1025 0.0071  0.0144  -0.0045 229 LEU   A C   
1869 O  O   . LEU   A 228 ? 0.1431 0.1067 0.1197 0.0076  0.0114  -0.0069 229 LEU   A O   
1870 C  CB  . LEU   A 228 ? 0.1385 0.1104 0.1138 0.0027  0.0113  -0.0087 229 LEU   A CB  
1871 C  CG  . LEU   A 228 ? 0.1392 0.1283 0.1118 0.0062  0.0059  0.0007  229 LEU   A CG  
1872 C  CD1 . LEU   A 228 ? 0.1402 0.1460 0.1251 0.0111  0.0034  -0.0151 229 LEU   A CD1 
1873 C  CD2 . LEU   A 228 ? 0.1417 0.1596 0.1585 0.0232  0.0179  0.0192  229 LEU   A CD2 
1874 N  N   . ASN   A 229 ? 0.1328 0.1051 0.1145 0.0070  0.0073  0.0045  230 ASN   A N   
1875 C  CA  . ASN   A 229 ? 0.1367 0.1063 0.1089 0.0106  0.0129  0.0014  230 ASN   A CA  
1876 C  C   . ASN   A 229 ? 0.1225 0.1140 0.1099 0.0114  0.0226  0.0092  230 ASN   A C   
1877 O  O   . ASN   A 229 ? 0.1406 0.1130 0.1260 0.0123  0.0147  0.0037  230 ASN   A O   
1878 C  CB  . ASN   A 229 ? 0.1367 0.1372 0.1161 0.0022  0.0211  -0.0023 230 ASN   A CB  
1879 C  CG  . ASN   A 229 ? 0.1834 0.1476 0.1387 0.0161  0.0284  -0.0088 230 ASN   A CG  
1880 O  OD1 . ASN   A 229 ? 0.2609 0.1739 0.1350 0.0217  0.0439  -0.0097 230 ASN   A OD1 
1881 N  ND2 . ASN   A 229 ? 0.1919 0.1456 0.1421 0.0012  0.0237  -0.0364 230 ASN   A ND2 
1882 N  N   . PHE   A 230 ? 0.1271 0.1118 0.1170 0.0099  0.0185  0.0072  231 PHE   A N   
1883 C  CA  . PHE   A 230 ? 0.1313 0.1227 0.1247 0.0018  0.0190  0.0075  231 PHE   A CA  
1884 C  C   . PHE   A 230 ? 0.1373 0.1254 0.1364 -0.0031 0.0127  0.0036  231 PHE   A C   
1885 O  O   . PHE   A 230 ? 0.1592 0.1433 0.1486 -0.0188 0.0062  0.0101  231 PHE   A O   
1886 C  CB  . PHE   A 230 ? 0.1429 0.1319 0.1220 0.0000  0.0127  0.0093  231 PHE   A CB  
1887 C  CG  . PHE   A 230 ? 0.1266 0.1305 0.1159 -0.0041 0.0116  0.0042  231 PHE   A CG  
1888 C  CD1 . PHE   A 230 ? 0.1461 0.1211 0.1203 0.0025  0.0059  0.0019  231 PHE   A CD1 
1889 C  CD2 . PHE   A 230 ? 0.1488 0.1293 0.1297 0.0081  0.0107  -0.0002 231 PHE   A CD2 
1890 C  CE1 . PHE   A 230 ? 0.1502 0.1310 0.1176 -0.0095 0.0076  0.0032  231 PHE   A CE1 
1891 C  CE2 . PHE   A 230 ? 0.1477 0.1228 0.1382 0.0022  -0.0004 0.0112  231 PHE   A CE2 
1892 C  CZ  . PHE   A 230 ? 0.1522 0.1413 0.1189 -0.0149 0.0027  0.0043  231 PHE   A CZ  
1893 N  N   . ASN   A 231 ? 0.1356 0.1489 0.1285 -0.0084 0.0263  0.0121  232 ASN   A N   
1894 C  CA  . ASN   A 231 ? 0.1355 0.1833 0.1450 0.0002  0.0211  0.0217  232 ASN   A CA  
1895 C  C   . ASN   A 231 ? 0.1470 0.1537 0.1291 0.0060  0.0334  0.0201  232 ASN   A C   
1896 O  O   . ASN   A 231 ? 0.1389 0.1539 0.1296 0.0118  0.0178  0.0059  232 ASN   A O   
1897 C  CB  . ASN   A 231 ? 0.1421 0.1926 0.1641 0.0222  0.0376  0.0410  232 ASN   A CB  
1898 C  CG  . ASN   A 231 ? 0.1622 0.1725 0.1515 0.0440  0.0415  0.0153  232 ASN   A CG  
1899 O  OD1 . ASN   A 231 ? 0.1617 0.1648 0.1658 0.0290  0.0430  0.0155  232 ASN   A OD1 
1900 N  ND2 . ASN   A 231 ? 0.2316 0.1852 0.1562 0.0436  0.0302  0.0116  232 ASN   A ND2 
1901 N  N   . GLY   A 232 ? 0.1496 0.1819 0.1538 0.0005  0.0283  0.0330  233 GLY   A N   
1902 C  CA  . GLY   A 232 ? 0.1549 0.1597 0.1545 0.0154  0.0315  0.0318  233 GLY   A CA  
1903 C  C   . GLY   A 232 ? 0.1422 0.1665 0.1522 0.0283  0.0357  0.0298  233 GLY   A C   
1904 O  O   . GLY   A 232 ? 0.2130 0.2003 0.1562 0.0511  0.0533  0.0338  233 GLY   A O   
1905 N  N   . GLU   A 233 ? 0.1690 0.1599 0.1432 0.0149  0.0305  0.0161  234 GLU   A N   
1906 C  CA  . GLU   A 233 ? 0.1789 0.1778 0.1471 0.0032  0.0394  0.0035  234 GLU   A CA  
1907 C  C   . GLU   A 233 ? 0.2153 0.1684 0.1545 0.0327  0.0368  0.0093  234 GLU   A C   
1908 O  O   . GLU   A 233 ? 0.1936 0.2318 0.1696 0.0037  0.0434  0.0201  234 GLU   A O   
1909 C  CB  . GLU   A 233 ? 0.1924 0.1960 0.1555 -0.0113 0.0223  0.0094  234 GLU   A CB  
1910 C  CG  . GLU   A 233 ? 0.2499 0.2579 0.1636 -0.0478 0.0538  0.0205  234 GLU   A CG  
1911 C  CD  . GLU   A 233 ? 0.3157 0.3557 0.2061 -0.0016 0.0077  -0.0063 234 GLU   A CD  
1912 O  OE1 . GLU   A 233 ? 0.3380 0.3639 0.2886 0.0326  0.0239  0.0518  234 GLU   A OE1 
1913 O  OE2 . GLU   A 233 ? 0.4066 0.4599 0.1999 -0.0337 -0.0318 0.0276  234 GLU   A OE2 
1914 N  N   . GLY   A 234 ? 0.2863 0.2167 0.1605 0.0504  0.0792  0.0138  235 GLY   A N   
1915 C  CA  . GLY   A 234 ? 0.2809 0.2684 0.2007 0.0659  0.0800  0.0326  235 GLY   A CA  
1916 C  C   . GLY   A 234 ? 0.2777 0.3060 0.1972 0.0733  0.1089  0.0280  235 GLY   A C   
1917 O  O   . GLY   A 234 ? 0.2947 0.3598 0.2147 0.0706  0.1047  0.0332  235 GLY   A O   
1918 N  N   . GLU   A 235 ? 0.2611 0.3547 0.2012 0.0930  0.0874  0.0691  236 GLU   A N   
1919 C  CA  . GLU   A 235 ? 0.1959 0.3493 0.2551 0.0942  0.0732  0.0826  236 GLU   A CA  
1920 C  C   . GLU   A 235 ? 0.2369 0.3183 0.2299 0.0796  0.0767  0.0564  236 GLU   A C   
1921 O  O   . GLU   A 235 ? 0.2823 0.3082 0.2172 0.0822  0.0501  0.0609  236 GLU   A O   
1922 C  CB  . GLU   A 235 ? 0.2442 0.3790 0.2553 0.0741  0.0782  0.0752  236 GLU   A CB  
1923 C  CG  . GLU   A 235 ? 0.2532 0.3928 0.2938 0.0214  0.0876  0.0608  236 GLU   A CG  
1924 C  CD  . GLU   A 235 ? 0.3287 0.4153 0.3529 -0.0462 0.1010  0.0245  236 GLU   A CD  
1925 O  OE1 . GLU   A 235 ? 0.2435 0.4990 0.3525 -0.0456 0.0321  0.0787  236 GLU   A OE1 
1926 O  OE2 . GLU   A 235 ? 0.5287 0.4859 0.3735 -0.1135 0.1121  0.0428  236 GLU   A OE2 
1927 N  N   . PRO   A 236 ? 0.2083 0.3253 0.2809 0.0832  0.1095  0.1054  237 PRO   A N   
1928 C  CA  . PRO   A 236 ? 0.2141 0.3002 0.2776 0.0742  0.0921  0.0772  237 PRO   A CA  
1929 C  C   . PRO   A 236 ? 0.2151 0.2684 0.2019 0.0771  0.0477  0.0356  237 PRO   A C   
1930 O  O   . PRO   A 236 ? 0.2073 0.3194 0.2161 0.0570  0.0712  0.0364  237 PRO   A O   
1931 C  CB  . PRO   A 236 ? 0.2045 0.3577 0.3128 0.0945  0.1070  0.0913  237 PRO   A CB  
1932 C  CG  . PRO   A 236 ? 0.2270 0.3874 0.3641 0.0824  0.0784  0.0941  237 PRO   A CG  
1933 C  CD  . PRO   A 236 ? 0.2108 0.3713 0.3390 0.0694  0.0822  0.1250  237 PRO   A CD  
1934 N  N   . GLU   A 237 ? 0.1993 0.2821 0.1851 0.0897  0.0493  0.0018  238 GLU   A N   
1935 C  CA  . GLU   A 237 ? 0.2171 0.2485 0.1774 0.0744  0.0663  -0.0153 238 GLU   A CA  
1936 C  C   . GLU   A 237 ? 0.1805 0.1873 0.1937 0.0589  0.0451  0.0000  238 GLU   A C   
1937 O  O   . GLU   A 237 ? 0.1925 0.2017 0.2193 0.0733  0.0408  0.0020  238 GLU   A O   
1938 C  CB  . GLU   A 237 ? 0.2746 0.2792 0.2165 0.0991  0.0288  -0.0672 238 GLU   A CB  
1939 C  CG  . GLU   A 237 ? 0.3084 0.2832 0.2709 0.0778  0.0094  -0.0926 238 GLU   A CG  
1940 C  CD  . GLU   A 237 ? 0.3383 0.2999 0.3071 0.0363  0.0300  -0.1203 238 GLU   A CD  
1941 O  OE1 . GLU   A 237 ? 0.5078 0.4261 0.3935 0.0591  0.0017  -0.1914 238 GLU   A OE1 
1942 O  OE2 . GLU   A 237 ? 0.3367 0.2232 0.2091 0.0302  0.0256  -0.0685 238 GLU   A OE2 
1943 N  N   . GLU   A 238 ? 0.1523 0.1696 0.1630 0.0289  0.0394  0.0078  239 GLU   A N   
1944 C  CA  . GLU   A 238 ? 0.1417 0.1609 0.1729 0.0081  0.0311  0.0130  239 GLU   A CA  
1945 C  C   . GLU   A 238 ? 0.1425 0.1218 0.1490 0.0212  0.0235  0.0080  239 GLU   A C   
1946 O  O   . GLU   A 238 ? 0.1670 0.1297 0.1709 0.0146  0.0385  0.0130  239 GLU   A O   
1947 C  CB  . GLU   A 238 ? 0.1585 0.2389 0.2198 -0.0262 0.0368  0.0173  239 GLU   A CB  
1948 C  CG  . GLU   A 238 ? 0.2053 0.2887 0.2562 0.0233  0.0117  0.0007  239 GLU   A CG  
1949 C  CD  . GLU   A 238 ? 0.2510 0.2939 0.2566 0.1109  0.0328  -0.0055 239 GLU   A CD  
1950 O  OE1 . GLU   A 238 ? 0.2894 0.3490 0.2884 0.0322  0.0443  -0.0403 239 GLU   A OE1 
1951 O  OE2 . GLU   A 238 ? 0.3202 0.3961 0.3587 0.0782  0.0863  0.0166  239 GLU   A OE2 
1952 N  N   . LEU   A 239 ? 0.1389 0.1225 0.1285 0.0225  0.0309  -0.0038 240 LEU   A N   
1953 C  CA  . LEU   A 239 ? 0.1250 0.1224 0.1262 0.0153  0.0170  -0.0046 240 LEU   A CA  
1954 C  C   . LEU   A 239 ? 0.1176 0.1197 0.1258 0.0157  0.0165  0.0081  240 LEU   A C   
1955 O  O   . LEU   A 239 ? 0.1297 0.1250 0.1258 0.0168  0.0201  0.0048  240 LEU   A O   
1956 C  CB  . LEU   A 239 ? 0.1456 0.1277 0.1380 0.0293  0.0182  -0.0035 240 LEU   A CB  
1957 C  CG  . LEU   A 239 ? 0.1592 0.1338 0.1758 0.0244  0.0208  -0.0288 240 LEU   A CG  
1958 C  CD1 . LEU   A 239 ? 0.1844 0.1314 0.2390 0.0275  -0.0101 -0.0285 240 LEU   A CD1 
1959 C  CD2 . LEU   A 239 ? 0.2088 0.1441 0.1613 0.0103  0.0215  -0.0320 240 LEU   A CD2 
1960 N  N   . MET   A 240 ? 0.1239 0.1174 0.0971 0.0197  0.0137  0.0001  241 MET   A N   
1961 C  CA  . MET   A 240 ? 0.1266 0.1080 0.1102 0.0100  0.0218  -0.0006 241 MET   A CA  
1962 C  C   . MET   A 240 ? 0.1185 0.1089 0.1080 0.0041  0.0160  -0.0077 241 MET   A C   
1963 O  O   . MET   A 240 ? 0.1283 0.1316 0.1082 0.0035  0.0115  -0.0028 241 MET   A O   
1964 C  CB  . MET   A 240 ? 0.1366 0.1086 0.1075 0.0068  0.0201  0.0003  241 MET   A CB  
1965 C  CG  . MET   A 240 ? 0.1393 0.1104 0.1108 -0.0100 0.0184  -0.0126 241 MET   A CG  
1966 S  SD  . MET   A 240 ? 0.1392 0.1083 0.1360 0.0035  0.0219  -0.0054 241 MET   A SD  
1967 C  CE  . MET   A 240 ? 0.1478 0.1119 0.1485 -0.0066 0.0222  0.0102  241 MET   A CE  
1968 N  N   . VAL   A 241 ? 0.1168 0.1063 0.1010 0.0019  0.0143  -0.0031 242 VAL   A N   
1969 C  CA  . VAL   A 241 ? 0.1130 0.0952 0.1044 0.0037  0.0088  -0.0033 242 VAL   A CA  
1970 C  C   . VAL   A 241 ? 0.1144 0.0868 0.1084 -0.0013 0.0080  -0.0038 242 VAL   A C   
1971 O  O   . VAL   A 241 ? 0.1195 0.1123 0.1036 0.0028  0.0097  -0.0053 242 VAL   A O   
1972 C  CB  . VAL   A 241 ? 0.1309 0.1084 0.1107 -0.0062 0.0118  -0.0068 242 VAL   A CB  
1973 C  CG1 . VAL   A 241 ? 0.1477 0.1162 0.1271 -0.0156 0.0085  -0.0175 242 VAL   A CG1 
1974 C  CG2 . VAL   A 241 ? 0.1598 0.1076 0.1262 0.0102  0.0109  -0.0168 242 VAL   A CG2 
1975 N  N   . ASP   A 242 ? 0.1129 0.0877 0.0967 -0.0043 0.0036  -0.0057 243 ASP   A N   
1976 C  CA  . ASP   A 242 ? 0.1138 0.0854 0.1037 0.0083  0.0088  -0.0067 243 ASP   A CA  
1977 C  C   . ASP   A 242 ? 0.1012 0.0877 0.1034 0.0057  0.0071  -0.0097 243 ASP   A C   
1978 O  O   . ASP   A 242 ? 0.1157 0.0888 0.1333 0.0066  -0.0092 -0.0062 243 ASP   A O   
1979 C  CB  . ASP   A 242 ? 0.1192 0.0870 0.1162 0.0121  0.0055  -0.0020 243 ASP   A CB  
1980 C  CG  . ASP   A 242 ? 0.1243 0.0862 0.1249 0.0099  0.0094  -0.0090 243 ASP   A CG  
1981 O  OD1 . ASP   A 242 ? 0.1257 0.0893 0.1251 0.0051  0.0094  0.0023  243 ASP   A OD1 
1982 O  OD2 . ASP   A 242 ? 0.1465 0.0993 0.1606 0.0063  0.0261  -0.0140 243 ASP   A OD2 
1983 N  N   . ASN   A 243 ? 0.0955 0.0762 0.0993 0.0022  0.0043  -0.0089 244 ASN   A N   
1984 C  CA  . ASN   A 243 ? 0.0973 0.0762 0.1069 0.0014  0.0133  -0.0023 244 ASN   A CA  
1985 C  C   . ASN   A 243 ? 0.0903 0.0781 0.0995 0.0017  0.0084  -0.0006 244 ASN   A C   
1986 O  O   . ASN   A 243 ? 0.1304 0.0977 0.1061 0.0273  0.0126  0.0014  244 ASN   A O   
1987 C  CB  . ASN   A 243 ? 0.0956 0.0918 0.1061 -0.0037 0.0092  0.0022  244 ASN   A CB  
1988 C  CG  . ASN   A 243 ? 0.1041 0.0922 0.1104 -0.0033 0.0054  0.0135  244 ASN   A CG  
1989 O  OD1 . ASN   A 243 ? 0.0995 0.1004 0.1406 -0.0005 0.0076  0.0178  244 ASN   A OD1 
1990 N  ND2 . ASN   A 243 ? 0.1057 0.1398 0.1637 -0.0189 -0.0193 0.0492  244 ASN   A ND2 
1991 N  N   . TRP   A 244 ? 0.0946 0.0884 0.0878 0.0080  0.0021  -0.0031 245 TRP   A N   
1992 C  CA  . TRP   A 244 ? 0.0983 0.0822 0.0914 0.0063  0.0015  -0.0037 245 TRP   A CA  
1993 C  C   . TRP   A 244 ? 0.0966 0.0895 0.0927 0.0069  0.0020  -0.0055 245 TRP   A C   
1994 O  O   . TRP   A 244 ? 0.1106 0.1056 0.1151 0.0212  -0.0092 -0.0135 245 TRP   A O   
1995 C  CB  . TRP   A 244 ? 0.0939 0.0912 0.0958 0.0035  0.0057  -0.0084 245 TRP   A CB  
1996 C  CG  . TRP   A 244 ? 0.1009 0.0875 0.0985 0.0040  0.0124  -0.0041 245 TRP   A CG  
1997 C  CD1 . TRP   A 244 ? 0.1070 0.0914 0.0952 0.0031  0.0086  -0.0048 245 TRP   A CD1 
1998 C  CD2 . TRP   A 244 ? 0.1115 0.0932 0.1013 0.0032  0.0054  -0.0036 245 TRP   A CD2 
1999 N  NE1 . TRP   A 244 ? 0.1144 0.0942 0.0956 -0.0014 0.0140  -0.0050 245 TRP   A NE1 
2000 C  CE2 . TRP   A 244 ? 0.1119 0.0935 0.1150 0.0038  0.0097  0.0040  245 TRP   A CE2 
2001 C  CE3 . TRP   A 244 ? 0.1271 0.1088 0.1121 0.0056  0.0034  -0.0009 245 TRP   A CE3 
2002 C  CZ2 . TRP   A 244 ? 0.1514 0.0875 0.1277 0.0112  0.0026  0.0065  245 TRP   A CZ2 
2003 C  CZ3 . TRP   A 244 ? 0.1592 0.1172 0.1193 0.0065  -0.0098 0.0108  245 TRP   A CZ3 
2004 C  CH2 . TRP   A 244 ? 0.1682 0.1069 0.1352 0.0110  -0.0046 0.0205  245 TRP   A CH2 
2005 N  N   . ARG   A 245 ? 0.0891 0.0998 0.1009 0.0116  0.0026  -0.0129 246 ARG   A N   
2006 C  CA  . ARG   A 245 ? 0.0922 0.1059 0.1047 0.0031  0.0031  -0.0058 246 ARG   A CA  
2007 C  C   . ARG   A 245 ? 0.1003 0.1072 0.1062 0.0016  -0.0016 -0.0118 246 ARG   A C   
2008 O  O   . ARG   A 245 ? 0.1098 0.1149 0.1149 -0.0053 0.0073  -0.0143 246 ARG   A O   
2009 C  CB  . ARG   A 245 ? 0.0925 0.1150 0.1077 -0.0049 0.0029  -0.0134 246 ARG   A CB  
2010 C  CG  . ARG   A 245 ? 0.0976 0.1041 0.1020 0.0023  0.0066  -0.0056 246 ARG   A CG  
2011 C  CD  . ARG   A 245 ? 0.0927 0.1157 0.1095 -0.0011 0.0055  -0.0130 246 ARG   A CD  
2012 N  NE  . ARG   A 245 ? 0.0964 0.1163 0.1212 -0.0074 -0.0028 -0.0188 246 ARG   A NE  
2013 C  CZ  . ARG   A 245 ? 0.0930 0.1215 0.1117 -0.0152 0.0082  -0.0127 246 ARG   A CZ  
2014 N  NH1 . ARG   A 245 ? 0.1055 0.1213 0.1171 -0.0209 0.0092  -0.0215 246 ARG   A NH1 
2015 N  NH2 . ARG   A 245 ? 0.1074 0.1493 0.1307 -0.0224 0.0062  -0.0295 246 ARG   A NH2 
2016 N  N   A PRO   A 246 ? 0.1006 0.0949 0.1032 0.0042  0.0024  -0.0030 247 PRO   A N   
2017 N  N   B PRO   A 246 ? 0.1178 0.1151 0.1194 0.0078  0.0016  0.0009  247 PRO   A N   
2018 C  CA  A PRO   A 246 ? 0.1156 0.0986 0.0993 0.0096  -0.0035 -0.0044 247 PRO   A CA  
2019 C  CA  B PRO   A 246 ? 0.1383 0.1277 0.1190 0.0121  -0.0006 -0.0019 247 PRO   A CA  
2020 C  C   A PRO   A 246 ? 0.1189 0.1007 0.1056 0.0136  -0.0030 -0.0004 247 PRO   A C   
2021 C  C   B PRO   A 246 ? 0.1270 0.1081 0.1185 0.0142  -0.0022 0.0053  247 PRO   A C   
2022 O  O   A PRO   A 246 ? 0.1309 0.1095 0.1040 0.0073  -0.0053 -0.0037 247 PRO   A O   
2023 O  O   B PRO   A 246 ? 0.1287 0.1119 0.1127 0.0100  -0.0041 -0.0004 247 PRO   A O   
2024 C  CB  A PRO   A 246 ? 0.1189 0.0944 0.0903 0.0167  -0.0114 -0.0045 247 PRO   A CB  
2025 C  CB  B PRO   A 246 ? 0.1592 0.1371 0.1352 0.0268  -0.0058 0.0017  247 PRO   A CB  
2026 C  CG  A PRO   A 246 ? 0.1087 0.0966 0.1059 0.0226  -0.0098 -0.0150 247 PRO   A CG  
2027 C  CG  B PRO   A 246 ? 0.1598 0.1509 0.1452 0.0279  -0.0032 -0.0052 247 PRO   A CG  
2028 C  CD  A PRO   A 246 ? 0.1054 0.1055 0.1100 0.0174  -0.0106 -0.0109 247 PRO   A CD  
2029 C  CD  B PRO   A 246 ? 0.1344 0.1385 0.1367 0.0274  -0.0092 -0.0078 247 PRO   A CD  
2030 N  N   . ALA   A 247 ? 0.1325 0.1115 0.1089 0.0079  0.0084  -0.0026 248 ALA   A N   
2031 C  CA  . ALA   A 247 ? 0.1318 0.1053 0.1143 0.0133  0.0102  -0.0018 248 ALA   A CA  
2032 C  C   . ALA   A 247 ? 0.1279 0.1254 0.1067 0.0190  0.0030  0.0050  248 ALA   A C   
2033 O  O   . ALA   A 247 ? 0.1407 0.1339 0.1360 0.0315  -0.0023 -0.0039 248 ALA   A O   
2034 C  CB  . ALA   A 247 ? 0.1469 0.1375 0.1299 0.0015  0.0266  -0.0054 248 ALA   A CB  
2035 N  N   . GLN   A 248 ? 0.1167 0.1216 0.1103 0.0137  -0.0041 -0.0008 249 GLN   A N   
2036 C  CA  . GLN   A 248 ? 0.1181 0.1332 0.1172 0.0104  0.0005  -0.0032 249 GLN   A CA  
2037 C  C   . GLN   A 248 ? 0.1235 0.1305 0.1200 0.0139  -0.0049 0.0000  249 GLN   A C   
2038 O  O   . GLN   A 248 ? 0.1354 0.1527 0.1243 0.0130  0.0067  0.0085  249 GLN   A O   
2039 C  CB  . GLN   A 248 ? 0.1050 0.1263 0.1305 -0.0041 -0.0135 -0.0051 249 GLN   A CB  
2040 C  CG  . GLN   A 248 ? 0.1391 0.1279 0.1258 -0.0045 0.0009  0.0024  249 GLN   A CG  
2041 C  CD  . GLN   A 248 ? 0.1234 0.1545 0.1291 -0.0185 0.0022  -0.0047 249 GLN   A CD  
2042 O  OE1 . GLN   A 248 ? 0.1399 0.2102 0.1632 -0.0237 0.0117  -0.0267 249 GLN   A OE1 
2043 N  NE2 . GLN   A 248 ? 0.1353 0.1640 0.1239 -0.0062 0.0053  -0.0073 249 GLN   A NE2 
2044 N  N   . PRO   A 249 ? 0.1362 0.1757 0.1199 0.0323  -0.0067 -0.0052 250 PRO   A N   
2045 C  CA  . PRO   A 249 ? 0.1569 0.1931 0.1310 0.0471  -0.0128 -0.0010 250 PRO   A CA  
2046 C  C   . PRO   A 249 ? 0.1541 0.1342 0.1296 0.0210  -0.0195 0.0035  250 PRO   A C   
2047 O  O   . PRO   A 249 ? 0.1389 0.1499 0.1259 0.0320  -0.0057 0.0094  250 PRO   A O   
2048 C  CB  . PRO   A 249 ? 0.1653 0.2470 0.1551 0.0606  -0.0423 -0.0352 250 PRO   A CB  
2049 C  CG  . PRO   A 249 ? 0.1739 0.2727 0.1665 0.0272  -0.0341 -0.0317 250 PRO   A CG  
2050 C  CD  . PRO   A 249 ? 0.1475 0.2164 0.1555 0.0304  -0.0333 -0.0295 250 PRO   A CD  
2051 N  N   . LEU   A 250 ? 0.1630 0.1528 0.1250 0.0319  -0.0137 0.0089  251 LEU   A N   
2052 C  CA  . LEU   A 250 ? 0.1603 0.1442 0.1325 0.0189  -0.0054 0.0069  251 LEU   A CA  
2053 C  C   . LEU   A 250 ? 0.1325 0.1504 0.1234 0.0220  -0.0037 0.0065  251 LEU   A C   
2054 O  O   . LEU   A 250 ? 0.1395 0.1444 0.1324 0.0252  -0.0082 -0.0037 251 LEU   A O   
2055 C  CB  . LEU   A 250 ? 0.1789 0.1608 0.1477 0.0048  0.0062  0.0041  251 LEU   A CB  
2056 C  CG  . LEU   A 250 ? 0.1935 0.1873 0.1567 -0.0131 0.0242  -0.0106 251 LEU   A CG  
2057 C  CD1 . LEU   A 250 ? 0.1720 0.2134 0.1703 -0.0094 0.0132  -0.0286 251 LEU   A CD1 
2058 C  CD2 . LEU   A 250 ? 0.2404 0.2138 0.1943 -0.0289 0.0516  0.0007  251 LEU   A CD2 
2059 N  N   . LYS   A 251 ? 0.1508 0.1682 0.1146 0.0476  -0.0151 0.0027  252 LYS   A N   
2060 C  CA  . LYS   A 251 ? 0.1596 0.1908 0.1117 0.0400  -0.0241 -0.0095 252 LYS   A CA  
2061 C  C   . LYS   A 251 ? 0.1629 0.1795 0.1458 0.0310  -0.0135 -0.0006 252 LYS   A C   
2062 O  O   . LYS   A 251 ? 0.2176 0.2066 0.1406 0.0124  0.0161  -0.0029 252 LYS   A O   
2063 C  CB  . LYS   A 251 ? 0.1728 0.2097 0.1475 0.0158  -0.0203 -0.0294 252 LYS   A CB  
2064 C  CG  . LYS   A 251 ? 0.1910 0.2436 0.1841 0.0194  0.0072  -0.0231 252 LYS   A CG  
2065 C  CD  . LYS   A 251 ? 0.2193 0.2668 0.2161 0.0259  0.0191  -0.0167 252 LYS   A CD  
2066 C  CE  . LYS   A 251 ? 0.2044 0.2876 0.3023 0.0517  0.0335  0.0013  252 LYS   A CE  
2067 N  NZ  . LYS   A 251 ? 0.2342 0.2755 0.3402 0.0646  0.0236  0.0179  252 LYS   A NZ  
2068 N  N   . ASN   A 252 ? 0.1525 0.1853 0.1127 0.0141  -0.0033 -0.0134 253 ASN   A N   
2069 C  CA  . ASN   A 252 ? 0.1851 0.2291 0.1459 0.0233  -0.0123 -0.0296 253 ASN   A CA  
2070 C  C   . ASN   A 252 ? 0.1673 0.1975 0.1625 0.0314  0.0032  -0.0212 253 ASN   A C   
2071 O  O   . ASN   A 252 ? 0.2278 0.2056 0.2014 0.0374  -0.0053 -0.0277 253 ASN   A O   
2072 C  CB  . ASN   A 252 ? 0.2165 0.2439 0.1748 0.0106  -0.0060 -0.0440 253 ASN   A CB  
2073 C  CG  . ASN   A 252 ? 0.2937 0.2821 0.2174 0.0296  0.0136  -0.0716 253 ASN   A CG  
2074 O  OD1 . ASN   A 252 ? 0.3750 0.3615 0.2518 -0.0102 0.0350  -0.0602 253 ASN   A OD1 
2075 N  ND2 . ASN   A 252 ? 0.3053 0.2768 0.2493 0.0003  0.0415  -0.0982 253 ASN   A ND2 
2076 N  N   . ARG   A 253 ? 0.1569 0.1965 0.1194 0.0213  -0.0009 0.0134  254 ARG   A N   
2077 C  CA  . ARG   A 253 ? 0.1341 0.1675 0.1122 0.0242  0.0019  0.0003  254 ARG   A CA  
2078 C  C   . ARG   A 253 ? 0.1596 0.1791 0.1147 0.0230  0.0107  0.0039  254 ARG   A C   
2079 O  O   . ARG   A 253 ? 0.1956 0.1928 0.1917 0.0199  0.0482  0.0250  254 ARG   A O   
2080 C  CB  . ARG   A 253 ? 0.1327 0.1541 0.1119 0.0136  -0.0066 -0.0038 254 ARG   A CB  
2081 C  CG  . ARG   A 253 ? 0.1322 0.1495 0.1073 0.0139  -0.0013 -0.0050 254 ARG   A CG  
2082 C  CD  . ARG   A 253 ? 0.1347 0.1303 0.0989 0.0115  0.0019  0.0040  254 ARG   A CD  
2083 N  NE  . ARG   A 253 ? 0.1318 0.1283 0.0984 0.0215  -0.0058 0.0043  254 ARG   A NE  
2084 C  CZ  . ARG   A 253 ? 0.1113 0.1237 0.0916 0.0033  -0.0032 0.0065  254 ARG   A CZ  
2085 N  NH1 . ARG   A 253 ? 0.1067 0.1105 0.0938 0.0067  0.0008  -0.0003 254 ARG   A NH1 
2086 N  NH2 . ARG   A 253 ? 0.1162 0.1222 0.1037 0.0134  -0.0094 0.0092  254 ARG   A NH2 
2087 N  N   . GLN   A 254 ? 0.1495 0.1871 0.1422 0.0058  -0.0046 -0.0165 255 GLN   A N   
2088 C  CA  . GLN   A 254 ? 0.1670 0.2331 0.1488 -0.0135 -0.0063 -0.0249 255 GLN   A CA  
2089 C  C   . GLN   A 254 ? 0.1456 0.1832 0.1720 0.0040  -0.0164 -0.0024 255 GLN   A C   
2090 O  O   . GLN   A 254 ? 0.2292 0.1884 0.2852 -0.0003 -0.0840 -0.0153 255 GLN   A O   
2091 C  CB  . GLN   A 254 ? 0.2017 0.2906 0.1786 -0.0231 0.0322  -0.0141 255 GLN   A CB  
2092 C  CG  . GLN   A 254 ? 0.2906 0.3207 0.2225 -0.0040 0.0185  0.0081  255 GLN   A CG  
2093 C  CD  . GLN   A 254 ? 0.3550 0.3446 0.2389 0.0211  0.0387  0.0317  255 GLN   A CD  
2094 O  OE1 . GLN   A 254 ? 0.4029 0.4465 0.2708 0.0189  0.0416  0.0991  255 GLN   A OE1 
2095 N  NE2 . GLN   A 254 ? 0.3763 0.3184 0.2573 0.0136  0.0240  0.0140  255 GLN   A NE2 
2096 N  N   . ILE   A 255 ? 0.1410 0.1597 0.1282 -0.0003 -0.0025 0.0082  256 ILE   A N   
2097 C  CA  . ILE   A 255 ? 0.1225 0.1543 0.1102 0.0085  0.0015  0.0126  256 ILE   A CA  
2098 C  C   . ILE   A 255 ? 0.1203 0.1430 0.1120 0.0033  0.0084  0.0143  256 ILE   A C   
2099 O  O   . ILE   A 255 ? 0.1517 0.1721 0.1347 0.0198  0.0075  0.0314  256 ILE   A O   
2100 C  CB  . ILE   A 255 ? 0.1469 0.1506 0.1204 0.0153  -0.0012 0.0023  256 ILE   A CB  
2101 C  CG1 . ILE   A 255 ? 0.1578 0.1661 0.1454 0.0232  -0.0027 -0.0006 256 ILE   A CG1 
2102 C  CG2 . ILE   A 255 ? 0.1543 0.1683 0.1293 0.0112  -0.0026 -0.0087 256 ILE   A CG2 
2103 C  CD1 . ILE   A 255 ? 0.1786 0.2008 0.1563 0.0151  0.0126  -0.0155 256 ILE   A CD1 
2104 N  N   . LYS   A 256 ? 0.1198 0.1520 0.0988 0.0016  0.0046  0.0152  257 LYS   A N   
2105 C  CA  . LYS   A 256 ? 0.1287 0.1534 0.0993 0.0004  0.0107  0.0137  257 LYS   A CA  
2106 C  C   . LYS   A 256 ? 0.1174 0.1487 0.1030 -0.0017 -0.0012 0.0129  257 LYS   A C   
2107 O  O   . LYS   A 256 ? 0.1514 0.1819 0.0931 -0.0296 0.0123  0.0080  257 LYS   A O   
2108 C  CB  . LYS   A 256 ? 0.1482 0.1733 0.1249 0.0102  0.0210  -0.0107 257 LYS   A CB  
2109 C  CG  . LYS   A 256 ? 0.2323 0.2183 0.1810 -0.0132 0.0214  -0.0305 257 LYS   A CG  
2110 N  N   . ALA   A 257 ? 0.1247 0.1793 0.0971 -0.0109 0.0209  0.0061  258 ALA   A N   
2111 C  CA  . ALA   A 257 ? 0.1284 0.1632 0.1097 -0.0015 0.0124  -0.0017 258 ALA   A CA  
2112 C  C   . ALA   A 257 ? 0.1152 0.1659 0.1145 -0.0076 0.0256  -0.0028 258 ALA   A C   
2113 O  O   . ALA   A 257 ? 0.1253 0.2049 0.1161 0.0058  0.0196  -0.0157 258 ALA   A O   
2114 C  CB  . ALA   A 257 ? 0.1490 0.1765 0.1474 -0.0018 0.0109  0.0060  258 ALA   A CB  
2115 N  N   . SER   A 258 ? 0.1177 0.1536 0.1010 -0.0052 0.0134  -0.0045 259 SER   A N   
2116 C  CA  . SER   A 258 ? 0.1331 0.1720 0.1250 0.0041  0.0147  -0.0131 259 SER   A CA  
2117 C  C   . SER   A 258 ? 0.1244 0.1968 0.1452 0.0028  0.0217  -0.0031 259 SER   A C   
2118 O  O   . SER   A 258 ? 0.1395 0.2614 0.1741 0.0070  0.0375  -0.0091 259 SER   A O   
2119 C  CB  . SER   A 258 ? 0.1393 0.1518 0.1588 0.0056  -0.0001 0.0074  259 SER   A CB  
2120 O  OG  . SER   A 258 ? 0.1251 0.1685 0.1262 -0.0022 0.0094  -0.0028 259 SER   A OG  
2121 N  N   . PHE   A 259 ? 0.1345 0.1897 0.1473 -0.0220 0.0296  -0.0044 260 PHE   A N   
2122 C  CA  . PHE   A 259 ? 0.1728 0.2254 0.1897 -0.0484 0.0142  0.0342  260 PHE   A CA  
2123 C  C   . PHE   A 259 ? 0.2298 0.3109 0.2303 -0.0670 0.0346  0.0941  260 PHE   A C   
2124 O  O   . PHE   A 259 ? 0.2909 0.3028 0.2405 -0.0887 -0.0280 0.1134  260 PHE   A O   
2125 C  CB  . PHE   A 259 ? 0.1636 0.1851 0.2013 -0.0414 0.0073  0.0262  260 PHE   A CB  
2126 C  CG  . PHE   A 259 ? 0.1709 0.1685 0.2081 -0.0200 -0.0006 0.0286  260 PHE   A CG  
2127 C  CD1 . PHE   A 259 ? 0.1635 0.1658 0.1626 -0.0254 -0.0048 0.0089  260 PHE   A CD1 
2128 C  CD2 . PHE   A 259 ? 0.2202 0.2020 0.2971 -0.0235 0.0119  0.0639  260 PHE   A CD2 
2129 C  CE1 . PHE   A 259 ? 0.1771 0.1642 0.1863 -0.0152 -0.0117 -0.0001 260 PHE   A CE1 
2130 C  CE2 . PHE   A 259 ? 0.2388 0.1828 0.3008 0.0015  0.0095  0.0537  260 PHE   A CE2 
2131 C  CZ  . PHE   A 259 ? 0.2049 0.1891 0.3043 0.0086  -0.0047 0.0148  260 PHE   A CZ  
2132 N  N   . LYS   A 260 ? 0.3203 0.4045 0.2800 -0.1538 0.0284  0.1242  261 LYS   A N   
2133 C  CA  . LYS   A 260 ? 0.4639 0.4282 0.3461 -0.1434 0.0225  0.1698  261 LYS   A CA  
2134 C  C   . LYS   A 260 ? 0.4975 0.4319 0.3960 -0.1862 0.0235  0.1136  261 LYS   A C   
2135 O  O   . LYS   A 260 ? 0.6251 0.3821 0.4805 -0.1611 -0.0047 0.1334  261 LYS   A O   
2136 C  CB  . LYS   A 260 ? 0.5084 0.4616 0.4215 -0.1298 0.0642  0.1970  261 LYS   A CB  
2137 ZN ZN  . ZN    B .   ? 0.0859 0.0758 0.0893 0.0018  -0.0015 -0.0022 301 ZN    A ZN  
2138 C  C1  A A1H15 C .   ? 0.2264 0.1451 0.1520 -0.0482 0.0394  -0.0325 302 A1H15 A C1  
2139 C  C1  B A1H15 C .   ? 0.1649 0.0826 0.2118 -0.0151 0.0334  0.0031  302 A1H15 A C1  
2140 C  C2  A A1H15 C .   ? 0.1818 0.1130 0.1491 -0.0184 0.0249  0.0011  302 A1H15 A C2  
2141 C  C2  B A1H15 C .   ? 0.1549 0.1036 0.1578 -0.0140 0.0261  0.0081  302 A1H15 A C2  
2142 C  C3  A A1H15 C .   ? 0.1391 0.1135 0.1351 -0.0215 0.0249  0.0000  302 A1H15 A C3  
2143 C  C3  B A1H15 C .   ? 0.1369 0.1182 0.1506 -0.0092 0.0187  -0.0033 302 A1H15 A C3  
2144 C  C4  A A1H15 C .   ? 0.1087 0.0965 0.1181 -0.0147 0.0094  0.0031  302 A1H15 A C4  
2145 C  C4  B A1H15 C .   ? 0.1185 0.1103 0.1397 -0.0076 0.0126  0.0000  302 A1H15 A C4  
2146 C  C5  A A1H15 C .   ? 0.1112 0.0852 0.1046 -0.0026 0.0002  0.0028  302 A1H15 A C5  
2147 C  C5  B A1H15 C .   ? 0.1082 0.0921 0.1148 -0.0042 0.0094  -0.0046 302 A1H15 A C5  
2148 C  C6  A A1H15 C .   ? 0.1272 0.0824 0.1153 -0.0019 -0.0126 0.0077  302 A1H15 A C6  
2149 C  C6  B A1H15 C .   ? 0.1244 0.0914 0.1348 -0.0045 0.0090  0.0097  302 A1H15 A C6  
2150 C  C7  A A1H15 C .   ? 0.1595 0.0925 0.1353 0.0007  -0.0034 0.0111  302 A1H15 A C7  
2151 C  C7  B A1H15 C .   ? 0.1380 0.0848 0.1462 0.0060  0.0130  0.0048  302 A1H15 A C7  
2152 S  S8  A A1H15 C .   ? 0.0955 0.0808 0.0945 -0.0026 -0.0018 -0.0027 302 A1H15 A S8  
2153 S  S8  B A1H15 C .   ? 0.0904 0.0817 0.0888 -0.0038 0.0020  -0.0021 302 A1H15 A S8  
2154 N  N9  A A1H15 C .   ? 0.0996 0.0857 0.0945 0.0000  0.0043  -0.0018 302 A1H15 A N9  
2155 N  N9  B A1H15 C .   ? 0.1064 0.0737 0.0891 -0.0005 0.0007  -0.0018 302 A1H15 A N9  
2156 O  O10 A A1H15 C .   ? 0.1060 0.0957 0.0939 0.0024  -0.0042 -0.0042 302 A1H15 A O10 
2157 O  O10 B A1H15 C .   ? 0.0978 0.0898 0.0920 -0.0025 -0.0008 0.0018  302 A1H15 A O10 
2158 O  O11 A A1H15 C .   ? 0.0884 0.0787 0.0808 0.0025  0.0018  0.0046  302 A1H15 A O11 
2159 O  O11 B A1H15 C .   ? 0.0814 0.0916 0.0889 0.0029  0.0060  -0.0026 302 A1H15 A O11 
2160 N  N12 A A1H15 C .   ? 0.2790 0.1897 0.2175 -0.0403 0.0237  -0.0158 302 A1H15 A N12 
2161 N  N12 B A1H15 C .   ? 0.2281 0.2117 0.2427 0.0049  0.0318  0.0320  302 A1H15 A N12 
2162 C  C13 A A1H15 C .   ? 0.3404 0.2476 0.3463 -0.0542 0.0231  0.0251  302 A1H15 A C13 
2163 C  C13 B A1H15 C .   ? 0.2181 0.1950 0.2278 -0.0100 0.0199  0.0145  302 A1H15 A C13 
2164 N  N14 A A1H15 C .   ? 0.3258 0.3158 0.4182 -0.0494 0.0327  0.0208  302 A1H15 A N14 
2165 N  N14 B A1H15 C .   ? 0.2254 0.1616 0.1858 0.0119  -0.0046 0.0282  302 A1H15 A N14 
2166 C  C15 A A1H15 C .   ? 0.2430 0.2011 0.4221 -0.0534 0.0634  0.0394  302 A1H15 A C15 
2167 C  C15 B A1H15 C .   ? 0.2545 0.1489 0.1691 0.0054  -0.0234 0.0210  302 A1H15 A C15 
2168 N  N16 A A1H15 C .   ? 0.2622 0.2573 0.3883 0.0462  0.0649  0.0481  302 A1H15 A N16 
2169 N  N16 B A1H15 C .   ? 0.2593 0.1103 0.1675 0.0212  -0.0170 0.0268  302 A1H15 A N16 
2170 N  N17 A A1H15 C .   ? 0.4277 0.3163 0.4164 -0.0441 -0.0205 0.0409  302 A1H15 A N17 
2171 N  N17 B A1H15 C .   ? 0.2251 0.2457 0.2544 0.0062  0.0340  0.0278  302 A1H15 A N17 
2172 N  N18 A A1H15 C .   ? 0.3364 0.3377 0.4395 0.0326  0.0435  0.0144  302 A1H15 A N18 
2173 N  N18 B A1H15 C .   ? 0.2403 0.2021 0.1534 0.0058  -0.0240 0.0077  302 A1H15 A N18 
2174 C  C1  . A1H15 D .   ? 0.1770 0.3234 0.3017 -0.0165 0.0038  -0.0138 303 A1H15 A C1  
2175 C  C2  . A1H15 D .   ? 0.2239 0.3063 0.3016 -0.0067 0.0244  0.0128  303 A1H15 A C2  
2176 C  C3  . A1H15 D .   ? 0.3316 0.3114 0.3311 0.0414  0.0669  0.0204  303 A1H15 A C3  
2177 C  C4  . A1H15 D .   ? 0.2919 0.3070 0.2917 0.0481  0.0559  0.0189  303 A1H15 A C4  
2178 C  C5  . A1H15 D .   ? 0.2333 0.2762 0.2629 0.0091  0.0317  0.0185  303 A1H15 A C5  
2179 C  C6  . A1H15 D .   ? 0.2830 0.2842 0.2826 0.0086  0.0815  0.0518  303 A1H15 A C6  
2180 C  C7  . A1H15 D .   ? 0.2875 0.3145 0.3548 0.0289  0.0781  0.0463  303 A1H15 A C7  
2181 S  S8  . A1H15 D .   ? 0.1785 0.2733 0.2563 -0.0275 0.0101  0.0072  303 A1H15 A S8  
2182 N  N9  . A1H15 D .   ? 0.1578 0.2800 0.2482 -0.0583 0.0110  0.0308  303 A1H15 A N9  
2183 O  O10 . A1H15 D .   ? 0.2700 0.3466 0.2474 -0.0143 0.0074  0.0250  303 A1H15 A O10 
2184 O  O11 . A1H15 D .   ? 0.1916 0.2860 0.3400 0.0371  -0.0043 -0.0189 303 A1H15 A O11 
2185 N  N12 . A1H15 D .   ? 0.2678 0.3700 0.3278 0.0299  -0.0458 -0.0296 303 A1H15 A N12 
2186 C  C13 . A1H15 D .   ? 0.1910 0.3334 0.3367 0.0050  -0.0375 0.0779  303 A1H15 A C13 
2187 N  N17 . A1H15 D .   ? 0.3829 0.4683 0.4579 -0.0510 -0.0135 0.1136  303 A1H15 A N17 
2188 C  C1  . GOL   E .   ? 0.3098 0.2218 0.2469 0.0261  -0.0172 -0.0187 304 GOL   A C1  
2189 O  O1  . GOL   E .   ? 0.2334 0.1999 0.2791 0.0222  -0.0461 -0.0231 304 GOL   A O1  
2190 C  C2  . GOL   E .   ? 0.2484 0.2683 0.1981 0.0428  -0.0087 -0.0010 304 GOL   A C2  
2191 O  O2  . GOL   E .   ? 0.1704 0.1758 0.1179 0.0294  0.0016  0.0199  304 GOL   A O2  
2192 C  C3  . GOL   E .   ? 0.2038 0.2320 0.2143 0.0245  0.0128  -0.0182 304 GOL   A C3  
2193 O  O3  . GOL   E .   ? 0.1979 0.1964 0.1691 0.0318  0.0071  -0.0196 304 GOL   A O3  
2194 O  O   . HOH   F .   ? 0.0798 0.1432 0.6107 -0.0144 -0.0028 0.0694  401 HOH   A O   
2195 O  O   . HOH   F .   ? 0.5999 0.4970 0.5353 -0.0785 0.0187  0.0468  402 HOH   A O   
2196 O  O   . HOH   F .   ? 0.1478 0.1075 0.1689 -0.0364 0.0210  0.0320  403 HOH   A O   
2197 O  O   . HOH   F .   ? 0.2727 0.2183 0.3033 -0.0135 -0.0692 0.0689  404 HOH   A O   
2198 O  O   . HOH   F .   ? 0.1929 0.1572 0.0868 0.0248  -0.0093 -0.0074 405 HOH   A O   
2199 O  O   . HOH   F .   ? 0.5168 0.3822 0.2584 0.1464  -0.0320 -0.0268 406 HOH   A O   
2200 O  O   . HOH   F .   ? 0.2226 0.1611 0.1729 0.0388  0.0165  0.0252  407 HOH   A O   
2201 O  O   . HOH   F .   ? 0.1089 0.1132 0.1101 0.0057  -0.0206 -0.0217 408 HOH   A O   
2202 O  O   . HOH   F .   ? 0.1999 0.2237 0.2477 0.0018  0.0065  0.0074  409 HOH   A O   
2203 O  O   . HOH   F .   ? 0.2591 0.2313 0.3392 -0.0354 -0.0201 -0.0310 410 HOH   A O   
2204 O  O   . HOH   F .   ? 0.2390 0.4788 0.5762 0.0094  0.0274  0.0048  411 HOH   A O   
2205 O  O   . HOH   F .   ? 0.4561 0.4175 0.2227 0.1703  -0.1282 -0.0110 412 HOH   A O   
2206 O  O   . HOH   F .   ? 0.6500 0.4606 0.4496 -0.0057 -0.1219 0.3426  413 HOH   A O   
2207 O  O   . HOH   F .   ? 0.2692 0.4035 0.2958 0.0703  -0.0134 -0.0045 414 HOH   A O   
2208 O  O   . HOH   F .   ? 0.1381 0.1648 0.1481 -0.0254 -0.0260 0.0027  415 HOH   A O   
2209 O  O   . HOH   F .   ? 0.3187 0.2021 0.3427 0.0112  0.0703  0.0428  416 HOH   A O   
2210 O  O   . HOH   F .   ? 0.3079 0.2899 0.4420 -0.0357 -0.0192 0.0281  417 HOH   A O   
2211 O  O   . HOH   F .   ? 0.3277 0.4651 0.3922 0.0583  -0.0434 -0.0300 418 HOH   A O   
2212 O  O   . HOH   F .   ? 0.0898 0.2077 0.2363 0.0062  0.0001  -0.0379 419 HOH   A O   
2213 O  O   . HOH   F .   ? 0.5023 0.2945 0.3722 -0.0569 -0.1971 -0.0764 420 HOH   A O   
2214 O  O   . HOH   F .   ? 0.2617 0.3120 0.3780 -0.0529 0.0514  -0.0732 421 HOH   A O   
2215 O  O   . HOH   F .   ? 0.4337 0.3889 0.2245 0.1581  0.1091  0.0977  422 HOH   A O   
2216 O  O   . HOH   F .   ? 0.2717 0.4008 0.2843 -0.1049 0.0755  -0.1662 423 HOH   A O   
2217 O  O   . HOH   F .   ? 0.3728 0.3577 0.2559 -0.1120 0.1328  -0.0938 424 HOH   A O   
2218 O  O   . HOH   F .   ? 0.2052 0.2625 0.1655 0.0066  0.0231  0.0036  425 HOH   A O   
2219 O  O   . HOH   F .   ? 0.2240 0.4390 0.5181 0.0546  -0.0119 0.0512  426 HOH   A O   
2220 O  O   . HOH   F .   ? 0.2210 0.4671 0.1447 -0.1053 -0.0422 0.0134  427 HOH   A O   
2221 O  O   . HOH   F .   ? 0.5657 0.4022 0.3869 -0.2753 0.0940  -0.0104 428 HOH   A O   
2222 O  O   . HOH   F .   ? 0.1170 0.0983 0.0925 0.0027  -0.0008 0.0070  429 HOH   A O   
2223 O  O   . HOH   F .   ? 0.1312 0.1209 0.1188 0.0000  0.0050  -0.0154 430 HOH   A O   
2224 O  O   . HOH   F .   ? 0.2846 0.3879 0.3410 -0.0390 0.0026  0.0863  431 HOH   A O   
2225 O  O   . HOH   F .   ? 0.3013 0.2670 0.3182 0.0243  0.0242  0.1653  432 HOH   A O   
2226 O  O   . HOH   F .   ? 0.3173 0.2044 0.1944 -0.0823 -0.0138 0.0025  433 HOH   A O   
2227 O  O   . HOH   F .   ? 0.2467 0.3363 0.3195 -0.0105 -0.0469 0.0896  434 HOH   A O   
2228 O  O   . HOH   F .   ? 0.4310 0.3541 0.3145 0.0896  0.1001  -0.0099 435 HOH   A O   
2229 O  O   . HOH   F .   ? 0.3824 0.2932 0.1709 0.0489  0.0009  0.0052  436 HOH   A O   
2230 O  O   . HOH   F .   ? 0.4618 0.4087 0.2890 0.0584  0.0807  0.0822  437 HOH   A O   
2231 O  O   . HOH   F .   ? 0.3329 0.3495 0.4490 -0.0522 -0.1152 0.0558  438 HOH   A O   
2232 O  O   . HOH   F .   ? 0.2007 0.2127 0.2547 -0.0051 -0.0876 -0.0458 439 HOH   A O   
2233 O  O   . HOH   F .   ? 0.2807 0.2740 0.3554 0.0018  -0.0347 -0.0218 440 HOH   A O   
2234 O  O   . HOH   F .   ? 0.2855 0.3384 0.3800 0.1106  0.0548  0.0018  441 HOH   A O   
2235 O  O   . HOH   F .   ? 0.2776 0.2448 0.2626 0.0143  0.0091  0.0028  442 HOH   A O   
2236 O  O   . HOH   F .   ? 0.2015 0.2287 0.1931 0.0253  -0.0370 -0.0071 443 HOH   A O   
2237 O  O   . HOH   F .   ? 0.2124 0.3008 0.4584 0.0467  -0.0689 -0.0545 444 HOH   A O   
2238 O  O   . HOH   F .   ? 0.4010 0.2466 0.2706 -0.0006 0.0705  0.0022  445 HOH   A O   
2239 O  O   . HOH   F .   ? 0.1602 0.1338 0.1410 -0.0158 0.0173  -0.0132 446 HOH   A O   
2240 O  O   . HOH   F .   ? 0.2064 0.1537 0.3631 -0.0106 -0.0191 -0.0242 447 HOH   A O   
2241 O  O   . HOH   F .   ? 0.2499 0.3199 0.2246 -0.0554 0.0348  0.0398  448 HOH   A O   
2242 O  O   . HOH   F .   ? 0.2939 0.2098 0.2350 -0.0239 -0.0081 0.0193  449 HOH   A O   
2243 O  O   . HOH   F .   ? 0.2477 0.2861 0.2753 0.0125  -0.0666 -0.1445 450 HOH   A O   
2244 O  O   . HOH   F .   ? 0.2312 0.1382 0.2123 -0.0308 0.0006  0.0141  451 HOH   A O   
2245 O  O   . HOH   F .   ? 0.2705 0.3479 0.3798 0.0099  0.1090  0.0573  452 HOH   A O   
2246 O  O   . HOH   F .   ? 0.3381 0.3153 0.3820 -0.0142 0.1198  0.0873  453 HOH   A O   
2247 O  O   . HOH   F .   ? 0.2221 0.4863 0.3246 -0.0570 -0.0394 0.0338  454 HOH   A O   
2248 O  O   . HOH   F .   ? 0.1688 0.1395 0.2139 0.0222  -0.0434 0.0049  455 HOH   A O   
2249 O  O   . HOH   F .   ? 0.1441 0.1667 0.1474 0.0080  -0.0192 0.0186  456 HOH   A O   
2250 O  O   . HOH   F .   ? 0.4698 0.2151 0.3192 -0.0387 0.0621  -0.0206 457 HOH   A O   
2251 O  O   . HOH   F .   ? 0.1486 0.2007 0.1552 0.0262  0.0154  0.0002  458 HOH   A O   
2252 O  O   . HOH   F .   ? 0.3479 0.3045 0.2845 -0.0905 0.0783  -0.0987 459 HOH   A O   
2253 O  O   . HOH   F .   ? 0.1771 0.1621 0.1438 -0.0022 0.0356  0.0192  460 HOH   A O   
2254 O  O   . HOH   F .   ? 0.2706 0.5529 0.4386 -0.0983 0.1009  -0.0617 461 HOH   A O   
2255 O  O   . HOH   F .   ? 0.2998 0.2548 0.2123 0.0180  0.0422  -0.0645 462 HOH   A O   
2256 O  O   . HOH   F .   ? 0.3719 0.2324 0.2547 -0.0010 0.0793  -0.0565 463 HOH   A O   
2257 O  O   . HOH   F .   ? 0.1405 0.1264 0.1328 0.0035  0.0125  -0.0137 464 HOH   A O   
2258 O  O   . HOH   F .   ? 0.3863 0.2061 0.1322 0.0015  0.0175  -0.0061 465 HOH   A O   
2259 O  O   . HOH   F .   ? 0.4250 0.1996 0.3153 0.0997  -0.0775 -0.0240 466 HOH   A O   
2260 O  O   . HOH   F .   ? 0.1893 0.2142 0.2502 0.0225  0.0068  0.0306  467 HOH   A O   
2261 O  O   . HOH   F .   ? 0.4852 0.3319 0.2552 -0.1277 -0.0921 0.0058  468 HOH   A O   
2262 O  O   . HOH   F .   ? 0.2286 0.1794 0.2521 -0.0145 0.0182  -0.0191 469 HOH   A O   
2263 O  O   . HOH   F .   ? 0.1334 0.1058 0.1321 0.0130  -0.0038 -0.0115 470 HOH   A O   
2264 O  O   . HOH   F .   ? 0.0869 0.0874 0.0668 0.0004  0.0025  -0.0053 471 HOH   A O   
2265 O  O   . HOH   F .   ? 0.1572 0.3580 0.3038 -0.0250 -0.0154 -0.0549 472 HOH   A O   
2266 O  O   . HOH   F .   ? 0.2612 0.2943 0.3776 -0.0444 0.1080  -0.0339 473 HOH   A O   
2267 O  O   . HOH   F .   ? 0.3590 0.2247 0.2414 -0.0109 -0.0563 0.0071  474 HOH   A O   
2268 O  O   . HOH   F .   ? 0.5222 0.3516 0.3080 0.0414  0.0332  -0.0432 475 HOH   A O   
2269 O  O   . HOH   F .   ? 0.2464 0.1939 0.2662 -0.0082 0.0117  0.0338  476 HOH   A O   
2270 O  O   . HOH   F .   ? 0.3532 0.5940 0.2059 -0.0342 0.0109  0.0766  477 HOH   A O   
2271 O  O   . HOH   F .   ? 0.1325 0.1388 0.1230 0.0233  0.0002  0.0012  478 HOH   A O   
2272 O  O   . HOH   F .   ? 0.7071 0.2952 0.2685 0.0448  0.0045  0.1282  479 HOH   A O   
2273 O  O   . HOH   F .   ? 0.2473 0.1638 0.3661 -0.0117 0.0678  -0.0437 480 HOH   A O   
2274 O  O   . HOH   F .   ? 0.4127 0.3888 0.2180 -0.0431 -0.0871 0.0673  481 HOH   A O   
2275 O  O   . HOH   F .   ? 0.1596 0.1641 0.2896 -0.0349 -0.0476 0.0006  482 HOH   A O   
2276 O  O   . HOH   F .   ? 0.2122 0.3038 0.2647 0.0016  -0.0386 -0.0386 483 HOH   A O   
2277 O  O   . HOH   F .   ? 0.2636 0.3082 0.4147 0.0660  -0.0810 -0.1207 484 HOH   A O   
2278 O  O   . HOH   F .   ? 0.2620 0.4981 0.2272 0.0289  -0.0052 -0.0674 485 HOH   A O   
2279 O  O   . HOH   F .   ? 0.2519 0.3486 0.4705 -0.0959 -0.1184 0.0025  486 HOH   A O   
2280 O  O   . HOH   F .   ? 0.2465 0.4788 0.4509 -0.0221 -0.0924 -0.0231 487 HOH   A O   
2281 O  O   . HOH   F .   ? 0.2181 0.3524 0.1911 -0.0678 -0.0050 -0.0226 488 HOH   A O   
2282 O  O   . HOH   F .   ? 0.2704 0.3142 0.3197 0.0516  0.0285  0.0527  489 HOH   A O   
2283 O  O   . HOH   F .   ? 0.4679 0.2365 0.2023 0.0414  0.0326  0.0055  490 HOH   A O   
2284 O  O   . HOH   F .   ? 0.2251 0.2524 0.2065 -0.0198 -0.0724 0.0304  491 HOH   A O   
2285 O  O   . HOH   F .   ? 0.1124 0.1602 0.1685 -0.0083 -0.0072 -0.0309 492 HOH   A O   
2286 O  O   . HOH   F .   ? 0.2010 0.1225 0.1447 -0.0168 -0.0031 0.0078  493 HOH   A O   
2287 O  O   . HOH   F .   ? 0.1961 0.1983 0.2043 -0.0056 -0.0011 -0.0016 494 HOH   A O   
2288 O  O   . HOH   F .   ? 0.1128 0.1152 0.1197 -0.0074 0.0223  -0.0084 495 HOH   A O   
2289 O  O   . HOH   F .   ? 0.3883 0.5461 0.4441 0.0741  -0.0191 -0.0816 496 HOH   A O   
2290 O  O   . HOH   F .   ? 0.4400 0.4088 0.3230 -0.0686 -0.0277 0.1635  497 HOH   A O   
2291 O  O   . HOH   F .   ? 0.1813 0.1618 0.1923 0.0249  0.0130  0.0117  498 HOH   A O   
2292 O  O   . HOH   F .   ? 0.2609 0.1766 0.2776 0.0038  -0.0461 0.0468  499 HOH   A O   
2293 O  O   . HOH   F .   ? 0.2486 0.1409 0.2752 0.0069  -0.0237 0.0287  500 HOH   A O   
2294 O  O   . HOH   F .   ? 0.1722 0.1267 0.1783 -0.0066 -0.0099 0.0024  501 HOH   A O   
2295 O  O   . HOH   F .   ? 0.3447 0.3274 0.7847 0.0195  0.0336  0.0757  502 HOH   A O   
2296 O  O   . HOH   F .   ? 0.4306 0.3297 0.3527 -0.0945 0.1414  -0.1892 503 HOH   A O   
2297 O  O   . HOH   F .   ? 0.2532 0.2152 0.2597 0.0194  -0.0653 -0.0480 504 HOH   A O   
2298 O  O   . HOH   F .   ? 0.2998 0.5337 0.3865 0.0115  0.0506  0.0631  505 HOH   A O   
2299 O  O   . HOH   F .   ? 0.1963 0.3403 0.3021 -0.0145 -0.0060 0.0571  506 HOH   A O   
2300 O  O   . HOH   F .   ? 0.2179 0.2025 0.1785 -0.0055 0.0034  -0.0005 507 HOH   A O   
2301 O  O   . HOH   F .   ? 0.2253 0.1550 0.3816 -0.0327 0.0513  -0.0393 508 HOH   A O   
2302 O  O   . HOH   F .   ? 0.1391 0.1260 0.1333 0.0083  0.0194  -0.0029 509 HOH   A O   
2303 O  O   . HOH   F .   ? 0.3574 0.2420 0.1615 0.0808  0.0180  0.0259  510 HOH   A O   
2304 O  O   . HOH   F .   ? 0.2954 0.5946 0.4322 -0.0542 -0.0980 -0.0154 511 HOH   A O   
2305 O  O   . HOH   F .   ? 0.3930 0.3542 0.3065 -0.0214 0.0248  0.0599  512 HOH   A O   
2306 O  O   . HOH   F .   ? 0.4087 0.2212 0.3668 -0.0153 -0.0121 -0.1384 513 HOH   A O   
2307 O  O   . HOH   F .   ? 0.2307 0.2890 0.3815 -0.0084 0.0203  0.1051  514 HOH   A O   
2308 O  O   . HOH   F .   ? 0.2129 0.2706 0.2433 -0.1007 -0.0350 0.0322  515 HOH   A O   
2309 O  O   . HOH   F .   ? 0.2658 0.3575 0.3065 0.0254  -0.0168 -0.0174 516 HOH   A O   
2310 O  O   . HOH   F .   ? 0.1944 0.1507 0.3602 -0.0324 0.0316  0.0275  517 HOH   A O   
2311 O  O   . HOH   F .   ? 0.2936 0.2542 0.2801 0.0638  0.0448  -0.0260 518 HOH   A O   
2312 O  O   . HOH   F .   ? 0.3899 0.2759 0.3533 -0.0022 -0.0499 -0.0754 519 HOH   A O   
2313 O  O   . HOH   F .   ? 0.3511 0.2540 0.2641 -0.0394 0.0793  0.0560  520 HOH   A O   
2314 O  O   . HOH   F .   ? 0.1512 0.1417 0.1520 0.0192  -0.0066 0.0173  521 HOH   A O   
2315 O  O   . HOH   F .   ? 0.3058 0.3015 0.4635 0.0553  -0.0698 -0.0310 522 HOH   A O   
2316 O  O   . HOH   F .   ? 0.3935 0.5609 0.4554 0.1616  0.0766  0.0040  523 HOH   A O   
2317 O  O   . HOH   F .   ? 0.2711 0.2390 0.3473 0.0397  -0.0741 -0.0263 524 HOH   A O   
2318 O  O   . HOH   F .   ? 0.4527 0.4336 0.4154 0.0573  -0.0506 0.0402  525 HOH   A O   
2319 O  O   . HOH   F .   ? 0.2988 0.2936 0.2959 0.0054  0.0049  -0.0203 526 HOH   A O   
2320 O  O   . HOH   F .   ? 0.2198 0.2401 0.3005 0.0029  0.0129  -0.0418 527 HOH   A O   
2321 O  O   . HOH   F .   ? 0.3893 0.4316 0.2355 -0.0631 0.0833  -0.0210 528 HOH   A O   
2322 O  O   . HOH   F .   ? 0.2369 0.2274 0.2445 0.0156  -0.0467 -0.0055 529 HOH   A O   
2323 O  O   . HOH   F .   ? 0.7080 0.2419 0.4403 -0.1227 0.0135  0.0344  530 HOH   A O   
2324 O  O   . HOH   F .   ? 0.2410 0.2032 0.2240 0.0471  0.0330  0.0794  531 HOH   A O   
2325 O  O   . HOH   F .   ? 0.2333 0.2691 0.2098 0.0501  0.0543  0.0779  532 HOH   A O   
2326 O  O   . HOH   F .   ? 0.2225 0.1897 0.2388 -0.0300 0.0325  -0.0013 533 HOH   A O   
2327 O  O   . HOH   F .   ? 0.1588 0.1410 0.1718 0.0009  -0.0228 -0.0043 534 HOH   A O   
2328 O  O   . HOH   F .   ? 0.1081 0.2118 0.1685 0.0122  0.0057  -0.0261 535 HOH   A O   
2329 O  O   . HOH   F .   ? 0.2105 0.2079 0.3426 0.0082  0.0097  -0.0342 536 HOH   A O   
2330 O  O   . HOH   F .   ? 0.4329 0.5663 0.2773 -0.0599 0.0653  -0.0096 537 HOH   A O   
2331 O  O   . HOH   F .   ? 0.2605 0.1491 0.2293 0.0275  -0.0247 0.0122  538 HOH   A O   
2332 O  O   . HOH   F .   ? 0.1754 0.3571 0.2711 0.0300  -0.0103 0.0555  539 HOH   A O   
2333 O  O   . HOH   F .   ? 0.2644 0.2636 0.2195 -0.0223 -0.0337 -0.0864 540 HOH   A O   
2334 O  O   . HOH   F .   ? 0.1889 0.2941 0.2664 0.0721  0.0416  -0.0038 541 HOH   A O   
2335 O  O   . HOH   F .   ? 0.3268 0.3643 0.1734 0.0860  -0.0126 0.0014  542 HOH   A O   
2336 O  O   . HOH   F .   ? 0.4592 0.2935 0.3150 0.0687  0.1404  0.1121  543 HOH   A O   
2337 O  O   . HOH   F .   ? 0.1923 0.1818 0.2549 -0.0553 -0.0312 -0.0215 544 HOH   A O   
2338 O  O   . HOH   F .   ? 0.2352 0.2327 0.2165 0.0292  -0.0217 0.0527  545 HOH   A O   
2339 O  O   . HOH   F .   ? 0.3914 0.3007 0.3834 0.0027  -0.0189 0.0930  546 HOH   A O   
2340 O  O   . HOH   F .   ? 0.2868 0.3400 0.2093 -0.0826 0.0339  -0.0158 547 HOH   A O   
2341 O  O   . HOH   F .   ? 0.4152 0.4462 0.2732 0.0483  0.0283  -0.1157 548 HOH   A O   
2342 O  O   . HOH   F .   ? 0.3332 0.3408 0.2669 0.0306  0.0748  0.0026  549 HOH   A O   
2343 O  O   . HOH   F .   ? 0.4363 0.3866 0.3097 -0.1743 -0.0890 -0.0427 550 HOH   A O   
2344 O  O   . HOH   F .   ? 0.2512 0.5814 0.6431 -0.1033 0.0601  -0.0750 551 HOH   A O   
2345 O  O   . HOH   F .   ? 0.4024 0.2323 0.3905 0.0812  0.0152  -0.0369 552 HOH   A O   
2346 O  O   . HOH   F .   ? 0.2310 0.1959 0.2099 -0.0512 -0.0102 -0.0279 553 HOH   A O   
2347 O  O   . HOH   F .   ? 0.2347 0.3140 0.6069 -0.0389 0.0025  0.0173  554 HOH   A O   
2348 O  O   . HOH   F .   ? 0.2872 0.2840 0.3428 -0.0034 -0.0430 0.0035  555 HOH   A O   
2349 O  O   . HOH   F .   ? 0.2457 0.2948 0.1848 0.0188  -0.0034 0.0033  556 HOH   A O   
2350 O  O   . HOH   F .   ? 0.4699 0.4906 0.4415 0.2467  -0.0994 -0.0911 557 HOH   A O   
2351 O  O   . HOH   F .   ? 0.3711 0.2889 0.2280 0.1439  -0.0375 0.0291  558 HOH   A O   
2352 O  O   . HOH   F .   ? 0.2080 0.1917 0.3043 0.0599  -0.0008 0.0025  559 HOH   A O   
2353 O  O   . HOH   F .   ? 0.3297 0.3759 0.6148 -0.0823 -0.0095 -0.0404 560 HOH   A O   
2354 O  O   . HOH   F .   ? 0.1430 0.2435 0.1560 -0.0058 -0.0247 0.0481  561 HOH   A O   
2355 O  O   . HOH   F .   ? 0.4872 0.6153 0.3061 0.1237  0.0178  0.0812  562 HOH   A O   
2356 O  O   . HOH   F .   ? 0.2320 0.2497 0.2869 -0.0323 -0.0222 -0.0384 563 HOH   A O   
2357 O  O   . HOH   F .   ? 0.3609 0.5554 0.5664 0.0630  0.0993  -0.1388 564 HOH   A O   
2358 O  O   . HOH   F .   ? 0.4714 0.3735 0.3437 0.0364  -0.0696 0.0727  565 HOH   A O   
2359 O  O   . HOH   F .   ? 0.2413 0.1468 0.2187 -0.0246 -0.0013 0.0074  566 HOH   A O   
2360 O  O   . HOH   F .   ? 0.1785 0.1334 0.1885 -0.0168 -0.0023 -0.0086 567 HOH   A O   
2361 O  O   . HOH   F .   ? 0.1393 0.1179 0.1474 0.0067  -0.0075 -0.0015 568 HOH   A O   
2362 O  O   . HOH   F .   ? 0.3297 0.3589 0.3814 0.0699  0.1166  0.0962  569 HOH   A O   
2363 O  O   . HOH   F .   ? 0.1727 0.2710 0.2516 0.0116  -0.0260 0.0167  570 HOH   A O   
2364 O  O   . HOH   F .   ? 0.2707 0.2726 0.1828 0.0485  -0.0204 0.0253  571 HOH   A O   
2365 O  O   . HOH   F .   ? 0.2209 0.2745 0.2933 0.0136  0.0537  0.0156  572 HOH   A O   
2366 O  O   . HOH   F .   ? 0.2983 0.2514 0.5415 0.0240  0.0627  0.0295  573 HOH   A O   
2367 O  O   . HOH   F .   ? 0.3399 0.5790 0.2927 0.1128  0.0673  0.2329  574 HOH   A O   
2368 O  O   . HOH   F .   ? 0.3286 0.6034 0.3349 -0.0472 0.0248  -0.0364 575 HOH   A O   
2369 O  O   . HOH   F .   ? 0.2289 0.5364 0.6185 -0.0863 0.1045  0.0805  576 HOH   A O   
2370 O  O   . HOH   F .   ? 0.3352 0.5429 0.3566 0.0582  0.0000  -0.1320 577 HOH   A O   
2371 O  O   . HOH   F .   ? 0.2806 0.2910 0.2739 0.0133  0.0194  0.0024  578 HOH   A O   
2372 O  O   . HOH   F .   ? 0.1223 0.1937 0.2426 -0.0224 0.0128  0.0006  579 HOH   A O   
2373 O  O   . HOH   F .   ? 0.3034 0.2291 0.2739 0.0704  0.0763  0.0614  580 HOH   A O   
2374 O  O   . HOH   F .   ? 0.4778 0.4031 0.2190 0.0894  0.0992  0.1089  581 HOH   A O   
2375 O  O   . HOH   F .   ? 0.4947 0.3313 0.3423 0.0220  0.0313  -0.0369 582 HOH   A O   
2376 O  O   . HOH   F .   ? 0.4104 0.1972 0.2839 0.0240  0.0219  -0.0041 583 HOH   A O   
2377 O  O   . HOH   F .   ? 0.4992 0.2989 0.2689 0.0315  -0.0131 -0.0115 584 HOH   A O   
2378 O  O   . HOH   F .   ? 0.2997 0.2990 0.2462 -0.0162 -0.0245 -0.0097 585 HOH   A O   
2379 O  O   . HOH   F .   ? 0.3985 0.3585 0.2490 0.0179  -0.0600 0.0565  586 HOH   A O   
2380 O  O   . HOH   F .   ? 0.2293 0.2674 0.2146 0.0453  -0.0237 0.0185  587 HOH   A O   
2381 O  O   . HOH   F .   ? 0.4552 0.4603 0.3856 -0.1092 0.0277  0.1153  588 HOH   A O   
2382 O  O   . HOH   F .   ? 0.5199 0.4588 0.2987 -0.0988 -0.0124 -0.0144 589 HOH   A O   
2383 O  O   . HOH   F .   ? 0.3588 0.3606 0.3339 0.0368  -0.0258 0.0484  590 HOH   A O   
2384 O  O   . HOH   F .   ? 0.4684 0.3522 0.2797 -0.1500 0.0149  0.0687  591 HOH   A O   
2385 O  O   . HOH   F .   ? 0.4957 0.2374 0.3410 -0.0283 0.0406  -0.0145 592 HOH   A O   
2386 O  O   . HOH   F .   ? 0.2731 0.3824 0.2804 0.0581  0.0363  -0.0461 593 HOH   A O   
2387 O  O   . HOH   F .   ? 0.1989 0.1424 0.2176 -0.0088 -0.0169 -0.0096 594 HOH   A O   
2388 O  O   . HOH   F .   ? 0.6418 0.1891 0.4146 0.1515  -0.1134 -0.0451 595 HOH   A O   
2389 O  O   . HOH   F .   ? 0.4650 0.5106 0.3034 -0.0377 0.0871  0.1162  596 HOH   A O   
2390 O  O   . HOH   F .   ? 0.6571 0.2663 0.5191 0.0327  0.1959  0.0740  597 HOH   A O   
2391 O  O   . HOH   F .   ? 0.4376 0.2288 0.2422 -0.0098 0.0722  0.0895  598 HOH   A O   
2392 O  O   . HOH   F .   ? 0.5575 0.3318 0.3573 -0.0181 -0.0297 -0.0501 599 HOH   A O   
2393 O  O   . HOH   F .   ? 0.3920 0.5442 0.6150 0.1247  0.1388  0.0104  600 HOH   A O   
2394 O  O   . HOH   F .   ? 0.3808 0.4706 0.3557 -0.1303 0.0679  0.0231  601 HOH   A O   
2395 O  O   . HOH   F .   ? 0.3246 0.3195 0.2604 -0.0242 -0.0235 -0.0132 602 HOH   A O   
2396 O  O   . HOH   F .   ? 0.4814 0.5067 0.4787 -0.1430 0.1572  -0.0628 603 HOH   A O   
2397 O  O   . HOH   F .   ? 0.3533 0.3531 0.4136 -0.0963 -0.0700 -0.0590 604 HOH   A O   
2398 O  O   . HOH   F .   ? 0.6029 0.3431 0.5284 0.0703  0.0669  0.0124  605 HOH   A O   
2399 O  O   . HOH   F .   ? 0.4174 0.3551 0.3811 0.1248  0.0013  -0.0365 606 HOH   A O   
2400 O  O   . HOH   F .   ? 0.2933 0.3856 0.3424 0.0036  0.0048  0.0615  607 HOH   A O   
2401 O  O   . HOH   F .   ? 0.3864 0.3630 0.4134 0.1393  -0.0678 0.0289  608 HOH   A O   
2402 O  O   . HOH   F .   ? 0.5309 0.3499 0.3782 -0.0546 -0.1999 0.0809  609 HOH   A O   
2403 O  O   . HOH   F .   ? 0.5195 0.4007 0.6352 0.0156  0.2272  -0.1056 610 HOH   A O   
2404 O  O   . HOH   F .   ? 0.2294 0.3627 0.3276 -0.0153 0.0194  0.0771  611 HOH   A O   
2405 O  O   . HOH   F .   ? 0.2103 0.5442 0.4347 0.0076  0.0422  -0.0134 612 HOH   A O   
2406 O  O   . HOH   F .   ? 0.3253 0.6872 0.5200 0.0521  -0.0195 0.2878  613 HOH   A O   
2407 O  O   . HOH   F .   ? 0.2907 0.1984 0.2618 -0.0166 -0.0324 0.0268  614 HOH   A O   
2408 O  O   . HOH   F .   ? 0.3123 0.3575 0.6054 -0.1073 -0.0137 -0.0438 615 HOH   A O   
2409 O  O   . HOH   F .   ? 0.4629 0.3294 0.3482 0.0059  -0.0131 -0.0502 616 HOH   A O   
2410 O  O   . HOH   F .   ? 0.2750 0.1422 0.2976 0.0152  -0.0554 0.0051  617 HOH   A O   
2411 O  O   . HOH   F .   ? 0.2719 0.3295 0.3406 0.0933  0.0225  0.0664  618 HOH   A O   
2412 O  O   . HOH   F .   ? 0.3646 0.3419 0.3142 -0.0555 -0.0055 0.1172  619 HOH   A O   
2413 O  O   . HOH   F .   ? 0.6105 0.2418 0.4500 0.0052  0.1668  0.0651  620 HOH   A O   
2414 O  O   . HOH   F .   ? 0.3218 0.3423 0.3542 -0.0757 0.0600  -0.1426 621 HOH   A O   
2415 O  O   . HOH   F .   ? 0.2509 0.2596 0.2201 -0.0101 0.0245  -0.0418 622 HOH   A O   
2416 O  O   . HOH   F .   ? 0.3852 0.3849 0.3782 0.0569  -0.0054 -0.0578 623 HOH   A O   
2417 O  O   . HOH   F .   ? 0.3325 0.3042 0.4708 0.0199  -0.0390 0.0458  624 HOH   A O   
2418 O  O   . HOH   F .   ? 0.3293 0.3267 0.4554 0.0124  0.0102  -0.2079 625 HOH   A O   
2419 O  O   . HOH   F .   ? 0.4907 0.4969 0.3776 0.0924  -0.0129 0.0862  626 HOH   A O   
2420 O  O   . HOH   F .   ? 0.3458 0.3130 0.3514 -0.0586 0.0286  -0.0544 627 HOH   A O   
2421 O  O   . HOH   F .   ? 0.3154 0.3411 0.3162 -0.1001 0.0548  -0.0127 628 HOH   A O   
2422 O  O   . HOH   F .   ? 0.4206 0.3449 0.4385 -0.1493 0.0246  0.0329  629 HOH   A O   
2423 O  O   . HOH   F .   ? 0.1901 0.2035 0.2337 -0.0634 0.0028  0.0058  630 HOH   A O   
2424 O  O   . HOH   F .   ? 0.4155 0.2193 0.4414 0.0102  0.1200  -0.0088 631 HOH   A O   
2425 O  O   . HOH   F .   ? 0.2409 0.2482 0.2869 0.0655  -0.0444 -0.0864 632 HOH   A O   
2426 O  O   . HOH   F .   ? 0.2782 0.3287 0.4596 -0.0469 -0.0343 -0.1225 633 HOH   A O   
2427 O  O   . HOH   F .   ? 0.3794 0.5300 0.2595 0.0686  0.0877  -0.0166 634 HOH   A O   
2428 O  O   . HOH   F .   ? 0.2684 0.3646 0.4197 -0.1174 -0.0079 -0.0670 635 HOH   A O   
# 
