data_8RNS
# 
_entry.id   8RNS 
# 
_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   8RNS         pdb_00008rns 10.2210/pdb8rns/pdb 
WWPDB D_1292135849 ?            ?                   
# 
_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                        8RNS 
_pdbx_database_status.recvd_initial_deposition_date   2024-01-10 
_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 XII mimic in complex with biguanide derivative inhibitor 1-carbamimidamido-N-[(4 sulfamoylphenyl)methyl]methanimidamide
;
_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'                                   29233.855 1   4.2.1.1,4.2.1.69 
'A65S N67K E69N I91T F131A G132S V135S L203N C206T' ? ? 
2 non-polymer syn 'ZINC ION'                                               65.409    1   ?                ? ? ? 
3 non-polymer syn '1-carbamimidoyl-3-[(4-sulfamoylphenyl)methyl]guanidine' 270.311   1   ?                ? ? ? 
4 water       nat water                                                    18.015    240 ?                ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        
'Carbonate dehydratase II,Carbonic anhydrase C,CAC,Carbonic anhydrase II,CA-II,Cyanamide hydratase CA2' 
# 
_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       
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHSFKVNFDDSQDKAVLK
GGPLDGTYRLTQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDASKASQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLNETVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHSFKVNFDDSQDKAVLK
GGPLDGTYRLTQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDASKASQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLNETVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
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 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  SER n 
1 66  PHE n 
1 67  LYS n 
1 68  VAL n 
1 69  ASN 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  THR 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 ALA n 
1 131 SER n 
1 132 LYS n 
1 133 ALA n 
1 134 SER 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 ASN n 
1 204 GLU n 
1 205 THR 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  
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   3   HIS HIS A . n 
A 1 4   HIS 4   4   4   HIS HIS A . n 
A 1 5   TRP 5   5   5   TRP TRP A . n 
A 1 6   GLY 6   6   6   GLY GLY A . n 
A 1 7   TYR 7   7   7   TYR TYR A . n 
A 1 8   GLY 8   8   8   GLY GLY A . n 
A 1 9   LYS 9   9   9   LYS LYS A . n 
A 1 10  HIS 10  10  10  HIS HIS A . n 
A 1 11  ASN 11  11  11  ASN ASN A . n 
A 1 12  GLY 12  12  12  GLY GLY A . n 
A 1 13  PRO 13  13  13  PRO PRO A . n 
A 1 14  GLU 14  14  14  GLU GLU A . n 
A 1 15  HIS 15  15  15  HIS HIS A . n 
A 1 16  TRP 16  16  16  TRP TRP A . n 
A 1 17  HIS 17  17  17  HIS HIS A . n 
A 1 18  LYS 18  18  18  LYS LYS A . n 
A 1 19  ASP 19  19  19  ASP ASP A . n 
A 1 20  PHE 20  20  20  PHE PHE A . n 
A 1 21  PRO 21  21  21  PRO PRO A . n 
A 1 22  ILE 22  22  22  ILE ILE A . n 
A 1 23  ALA 23  23  23  ALA ALA A . n 
A 1 24  LYS 24  24  24  LYS LYS A . n 
A 1 25  GLY 25  25  25  GLY GLY A . n 
A 1 26  GLU 26  26  26  GLU GLU A . n 
A 1 27  ARG 27  27  27  ARG ARG A . n 
A 1 28  GLN 28  28  28  GLN GLN A . n 
A 1 29  SER 29  29  29  SER SER A . n 
A 1 30  PRO 30  30  30  PRO PRO A . n 
A 1 31  VAL 31  31  31  VAL VAL A . n 
A 1 32  ASP 32  32  32  ASP ASP A . n 
A 1 33  ILE 33  33  33  ILE ILE A . n 
A 1 34  ASP 34  34  34  ASP ASP A . n 
A 1 35  THR 35  35  35  THR THR A . n 
A 1 36  HIS 36  36  36  HIS HIS A . n 
A 1 37  THR 37  37  37  THR THR A . n 
A 1 38  ALA 38  38  38  ALA ALA A . n 
A 1 39  LYS 39  39  39  LYS LYS A . n 
A 1 40  TYR 40  40  40  TYR TYR A . n 
A 1 41  ASP 41  41  41  ASP ASP A . n 
A 1 42  PRO 42  42  42  PRO PRO A . n 
A 1 43  SER 43  43  43  SER SER A . n 
A 1 44  LEU 44  44  44  LEU LEU A . n 
A 1 45  LYS 45  45  45  LYS LYS A . n 
A 1 46  PRO 46  46  46  PRO PRO A . n 
A 1 47  LEU 47  47  47  LEU LEU A . n 
A 1 48  SER 48  48  48  SER SER A . n 
A 1 49  VAL 49  49  49  VAL VAL A . n 
A 1 50  SER 50  50  50  SER SER A . n 
A 1 51  TYR 51  51  51  TYR TYR A . n 
A 1 52  ASP 52  52  52  ASP ASP A . n 
A 1 53  GLN 53  53  53  GLN GLN A . n 
A 1 54  ALA 54  54  54  ALA ALA A . n 
A 1 55  THR 55  55  55  THR THR A . n 
A 1 56  SER 56  56  56  SER SER A . n 
A 1 57  LEU 57  57  57  LEU LEU A . n 
A 1 58  ARG 58  58  58  ARG ARG A . n 
A 1 59  ILE 59  59  59  ILE ILE A . n 
A 1 60  LEU 60  60  60  LEU LEU A . n 
A 1 61  ASN 61  61  61  ASN ASN A . n 
A 1 62  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  SER 65  65  65  SER SER A . n 
A 1 66  PHE 66  66  66  PHE PHE A . n 
A 1 67  LYS 67  67  67  LYS LYS A . n 
A 1 68  VAL 68  68  68  VAL VAL A . n 
A 1 69  ASN 69  69  69  ASN ASN 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  THR 91  91  91  THR THR A . n 
A 1 92  GLN 92  92  92  GLN GLN A . n 
A 1 93  PHE 93  93  93  PHE PHE A . n 
A 1 94  HIS 94  94  94  HIS HIS A . n 
A 1 95  PHE 95  95  95  PHE PHE A . n 
A 1 96  HIS 96  96  96  HIS HIS A . n 
A 1 97  TRP 97  97  97  TRP TRP A . n 
A 1 98  GLY 98  98  98  GLY GLY A . n 
A 1 99  SER 99  99  99  SER SER A . n 
A 1 100 LEU 100 100 100 LEU LEU A . n 
A 1 101 ASP 101 101 101 ASP ASP A . n 
A 1 102 GLY 102 102 102 GLY GLY A . n 
A 1 103 GLN 103 103 103 GLN GLN A . n 
A 1 104 GLY 104 104 104 GLY GLY A . n 
A 1 105 SER 105 105 105 SER SER A . n 
A 1 106 GLU 106 106 106 GLU GLU A . n 
A 1 107 HIS 107 107 107 HIS HIS A . n 
A 1 108 THR 108 108 108 THR THR A . n 
A 1 109 VAL 109 109 109 VAL VAL A . n 
A 1 110 ASP 110 110 110 ASP ASP A . n 
A 1 111 LYS 111 111 111 LYS LYS A . n 
A 1 112 LYS 112 112 112 LYS LYS A . n 
A 1 113 LYS 113 113 113 LYS LYS A . n 
A 1 114 TYR 114 114 114 TYR TYR A . n 
A 1 115 ALA 115 115 115 ALA ALA A . n 
A 1 116 ALA 116 116 116 ALA ALA A . n 
A 1 117 GLU 117 117 117 GLU GLU A . n 
A 1 118 LEU 118 118 118 LEU LEU A . n 
A 1 119 HIS 119 119 119 HIS HIS A . n 
A 1 120 LEU 120 120 120 LEU LEU A . n 
A 1 121 VAL 121 121 121 VAL VAL A . n 
A 1 122 HIS 122 122 122 HIS HIS A . n 
A 1 123 TRP 123 123 123 TRP TRP A . n 
A 1 124 ASN 124 124 124 ASN ASN A . n 
A 1 125 THR 125 125 125 THR THR A . n 
A 1 126 LYS 126 126 126 LYS LYS A . n 
A 1 127 TYR 127 127 127 TYR TYR A . n 
A 1 128 GLY 128 128 128 GLY GLY A . n 
A 1 129 ASP 129 129 129 ASP ASP A . n 
A 1 130 ALA 130 130 130 ALA ALA A . n 
A 1 131 SER 131 131 131 SER SER A . n 
A 1 132 LYS 132 132 132 LYS LYS A . n 
A 1 133 ALA 133 133 133 ALA ALA A . n 
A 1 134 SER 134 134 134 SER SER A . n 
A 1 135 GLN 135 135 135 GLN GLN A . n 
A 1 136 GLN 136 136 136 GLN GLN A . n 
A 1 137 PRO 137 137 137 PRO PRO A . n 
A 1 138 ASP 138 138 138 ASP ASP A . n 
A 1 139 GLY 139 139 139 GLY GLY A . n 
A 1 140 LEU 140 140 140 LEU LEU A . n 
A 1 141 ALA 141 141 141 ALA ALA A . n 
A 1 142 VAL 142 142 142 VAL VAL A . n 
A 1 143 LEU 143 143 143 LEU LEU A . n 
A 1 144 GLY 144 144 144 GLY GLY A . n 
A 1 145 ILE 145 145 145 ILE ILE A . n 
A 1 146 PHE 146 146 146 PHE PHE A . n 
A 1 147 LEU 147 147 147 LEU LEU A . n 
A 1 148 LYS 148 148 148 LYS LYS A . n 
A 1 149 VAL 149 149 149 VAL VAL A . n 
A 1 150 GLY 150 150 150 GLY GLY A . n 
A 1 151 SER 151 151 151 SER SER A . n 
A 1 152 ALA 152 152 152 ALA ALA A . n 
A 1 153 LYS 153 153 153 LYS LYS A . n 
A 1 154 PRO 154 154 154 PRO PRO A . n 
A 1 155 GLY 155 155 155 GLY GLY A . n 
A 1 156 LEU 156 156 156 LEU LEU A . n 
A 1 157 GLN 157 157 157 GLN GLN A . n 
A 1 158 LYS 158 158 158 LYS LYS A . n 
A 1 159 VAL 159 159 159 VAL VAL A . n 
A 1 160 VAL 160 160 160 VAL VAL A . n 
A 1 161 ASP 161 161 161 ASP ASP A . n 
A 1 162 VAL 162 162 162 VAL VAL A . n 
A 1 163 LEU 163 163 163 LEU LEU A . n 
A 1 164 ASP 164 164 164 ASP ASP A . n 
A 1 165 SER 165 165 165 SER SER A . n 
A 1 166 ILE 166 166 166 ILE ILE A . n 
A 1 167 LYS 167 167 167 LYS LYS A . n 
A 1 168 THR 168 168 168 THR THR A . n 
A 1 169 LYS 169 169 169 LYS LYS A . n 
A 1 170 GLY 170 170 170 GLY GLY A . n 
A 1 171 LYS 171 171 171 LYS LYS A . n 
A 1 172 SER 172 172 172 SER SER A . n 
A 1 173 ALA 173 173 173 ALA ALA A . n 
A 1 174 ASP 174 174 174 ASP ASP A . n 
A 1 175 PHE 175 175 175 PHE PHE A . n 
A 1 176 THR 176 176 176 THR THR A . n 
A 1 177 ASN 177 177 177 ASN ASN A . n 
A 1 178 PHE 178 178 178 PHE PHE A . n 
A 1 179 ASP 179 179 179 ASP ASP A . n 
A 1 180 PRO 180 180 180 PRO PRO A . n 
A 1 181 ARG 181 181 181 ARG ARG A . n 
A 1 182 GLY 182 182 182 GLY GLY A . n 
A 1 183 LEU 183 183 183 LEU LEU A . n 
A 1 184 LEU 184 184 184 LEU LEU A . n 
A 1 185 PRO 185 185 185 PRO PRO A . n 
A 1 186 GLU 186 186 186 GLU GLU A . n 
A 1 187 SER 187 187 187 SER SER A . n 
A 1 188 LEU 188 188 188 LEU LEU A . n 
A 1 189 ASP 189 189 189 ASP ASP A . n 
A 1 190 TYR 190 190 190 TYR TYR A . n 
A 1 191 TRP 191 191 191 TRP TRP A . n 
A 1 192 THR 192 192 192 THR THR A . n 
A 1 193 TYR 193 193 193 TYR TYR A . n 
A 1 194 PRO 194 194 194 PRO PRO A . n 
A 1 195 GLY 195 195 195 GLY GLY A . n 
A 1 196 SER 196 196 196 SER SER A . n 
A 1 197 LEU 197 197 197 LEU LEU A . n 
A 1 198 THR 198 198 198 THR THR A . n 
A 1 199 THR 199 199 199 THR THR A . n 
A 1 200 PRO 200 200 200 PRO PRO A . n 
A 1 201 PRO 201 201 201 PRO PRO A . n 
A 1 202 LEU 202 202 202 LEU LEU A . n 
A 1 203 ASN 203 203 203 ASN ASN A . n 
A 1 204 GLU 204 204 204 GLU GLU A . n 
A 1 205 THR 205 205 205 THR THR A . n 
A 1 206 VAL 206 206 206 VAL VAL A . n 
A 1 207 THR 207 207 207 THR THR A . n 
A 1 208 TRP 208 208 208 TRP TRP A . n 
A 1 209 ILE 209 209 209 ILE ILE A . n 
A 1 210 VAL 210 210 210 VAL VAL A . n 
A 1 211 LEU 211 211 211 LEU LEU A . n 
A 1 212 LYS 212 212 212 LYS LYS A . n 
A 1 213 GLU 213 213 213 GLU GLU A . n 
A 1 214 PRO 214 214 214 PRO PRO A . n 
A 1 215 ILE 215 215 215 ILE ILE A . n 
A 1 216 SER 216 216 216 SER SER A . n 
A 1 217 VAL 217 217 217 VAL VAL A . n 
A 1 218 SER 218 218 218 SER SER A . n 
A 1 219 SER 219 219 219 SER SER A . n 
A 1 220 GLU 220 220 220 GLU GLU A . n 
A 1 221 GLN 221 221 221 GLN GLN A . n 
A 1 222 VAL 222 222 222 VAL VAL A . n 
A 1 223 LEU 223 223 223 LEU LEU A . n 
A 1 224 LYS 224 224 224 LYS LYS A . n 
A 1 225 PHE 225 225 225 PHE PHE A . n 
A 1 226 ARG 226 226 226 ARG ARG A . n 
A 1 227 LYS 227 227 227 LYS LYS A . n 
A 1 228 LEU 228 228 228 LEU LEU A . n 
A 1 229 ASN 229 229 229 ASN ASN A . n 
A 1 230 PHE 230 230 230 PHE PHE A . n 
A 1 231 ASN 231 231 231 ASN ASN A . n 
A 1 232 GLY 232 232 232 GLY GLY A . n 
A 1 233 GLU 233 233 233 GLU GLU A . n 
A 1 234 GLY 234 234 234 GLY GLY A . n 
A 1 235 GLU 235 235 235 GLU GLU A . n 
A 1 236 PRO 236 236 236 PRO PRO A . n 
A 1 237 GLU 237 237 237 GLU GLU A . n 
A 1 238 GLU 238 238 238 GLU GLU A . n 
A 1 239 LEU 239 239 239 LEU LEU A . n 
A 1 240 MET 240 240 240 MET MET A . n 
A 1 241 VAL 241 241 241 VAL VAL A . n 
A 1 242 ASP 242 242 242 ASP ASP A . n 
A 1 243 ASN 243 243 243 ASN ASN A . n 
A 1 244 TRP 244 244 244 TRP TRP A . n 
A 1 245 ARG 245 245 245 ARG ARG A . n 
A 1 246 PRO 246 246 246 PRO PRO A . n 
A 1 247 ALA 247 247 247 ALA ALA A . n 
A 1 248 GLN 248 248 248 GLN GLN A . n 
A 1 249 PRO 249 249 249 PRO PRO A . n 
A 1 250 LEU 250 250 250 LEU LEU A . n 
A 1 251 LYS 251 251 251 LYS LYS A . n 
A 1 252 ASN 252 252 252 ASN ASN A . n 
A 1 253 ARG 253 253 253 ARG ARG A . n 
A 1 254 GLN 254 254 254 GLN GLN A . n 
A 1 255 ILE 255 255 255 ILE ILE A . n 
A 1 256 LYS 256 256 256 LYS LYS A . n 
A 1 257 ALA 257 257 257 ALA ALA A . n 
A 1 258 SER 258 258 258 SER SER A . n 
A 1 259 PHE 259 259 259 PHE PHE A . n 
A 1 260 LYS 260 260 260 LYS LYS A . n 
# 
_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 4 HOH   1   401 456 HOH   HOH A . 
D 4 HOH   2   402 494 HOH   HOH A . 
D 4 HOH   3   403 455 HOH   HOH A . 
D 4 HOH   4   404 480 HOH   HOH A . 
D 4 HOH   5   405 530 HOH   HOH A . 
D 4 HOH   6   406 6   HOH   HOH A . 
D 4 HOH   7   407 531 HOH   HOH A . 
D 4 HOH   8   408 415 HOH   HOH A . 
D 4 HOH   9   409 169 HOH   HOH A . 
D 4 HOH   10  410 152 HOH   HOH A . 
D 4 HOH   11  411 3   HOH   HOH A . 
D 4 HOH   12  412 411 HOH   HOH A . 
D 4 HOH   13  413 470 HOH   HOH A . 
D 4 HOH   14  414 29  HOH   HOH A . 
D 4 HOH   15  415 19  HOH   HOH A . 
D 4 HOH   16  416 89  HOH   HOH A . 
D 4 HOH   17  417 10  HOH   HOH A . 
D 4 HOH   18  418 284 HOH   HOH A . 
D 4 HOH   19  419 502 HOH   HOH A . 
D 4 HOH   20  420 191 HOH   HOH A . 
D 4 HOH   21  421 433 HOH   HOH A . 
D 4 HOH   22  422 160 HOH   HOH A . 
D 4 HOH   23  423 144 HOH   HOH A . 
D 4 HOH   24  424 443 HOH   HOH A . 
D 4 HOH   25  425 18  HOH   HOH A . 
D 4 HOH   26  426 108 HOH   HOH A . 
D 4 HOH   27  427 109 HOH   HOH A . 
D 4 HOH   28  428 316 HOH   HOH A . 
D 4 HOH   29  429 5   HOH   HOH A . 
D 4 HOH   30  430 20  HOH   HOH A . 
D 4 HOH   31  431 173 HOH   HOH A . 
D 4 HOH   32  432 101 HOH   HOH A . 
D 4 HOH   33  433 12  HOH   HOH A . 
D 4 HOH   34  434 247 HOH   HOH A . 
D 4 HOH   35  435 43  HOH   HOH A . 
D 4 HOH   36  436 512 HOH   HOH A . 
D 4 HOH   37  437 527 HOH   HOH A . 
D 4 HOH   38  438 163 HOH   HOH A . 
D 4 HOH   39  439 96  HOH   HOH A . 
D 4 HOH   40  440 17  HOH   HOH A . 
D 4 HOH   41  441 533 HOH   HOH A . 
D 4 HOH   42  442 45  HOH   HOH A . 
D 4 HOH   43  443 83  HOH   HOH A . 
D 4 HOH   44  444 172 HOH   HOH A . 
D 4 HOH   45  445 187 HOH   HOH A . 
D 4 HOH   46  446 24  HOH   HOH A . 
D 4 HOH   47  447 57  HOH   HOH A . 
D 4 HOH   48  448 221 HOH   HOH A . 
D 4 HOH   49  449 100 HOH   HOH A . 
D 4 HOH   50  450 85  HOH   HOH A . 
D 4 HOH   51  451 21  HOH   HOH A . 
D 4 HOH   52  452 22  HOH   HOH A . 
D 4 HOH   53  453 532 HOH   HOH A . 
D 4 HOH   54  454 13  HOH   HOH A . 
D 4 HOH   55  455 40  HOH   HOH A . 
D 4 HOH   56  456 19  HOH   HOH A . 
D 4 HOH   57  457 196 HOH   HOH A . 
D 4 HOH   58  458 46  HOH   HOH A . 
D 4 HOH   59  459 6   HOH   HOH A . 
D 4 HOH   60  460 127 HOH   HOH A . 
D 4 HOH   61  461 135 HOH   HOH A . 
D 4 HOH   62  462 73  HOH   HOH A . 
D 4 HOH   63  463 275 HOH   HOH A . 
D 4 HOH   64  464 500 HOH   HOH A . 
D 4 HOH   65  465 80  HOH   HOH A . 
D 4 HOH   66  466 13  HOH   HOH A . 
D 4 HOH   67  467 136 HOH   HOH A . 
D 4 HOH   68  468 18  HOH   HOH A . 
D 4 HOH   69  469 452 HOH   HOH A . 
D 4 HOH   70  470 35  HOH   HOH A . 
D 4 HOH   71  471 33  HOH   HOH A . 
D 4 HOH   72  472 43  HOH   HOH A . 
D 4 HOH   73  473 116 HOH   HOH A . 
D 4 HOH   74  474 16  HOH   HOH A . 
D 4 HOH   75  475 205 HOH   HOH A . 
D 4 HOH   76  476 28  HOH   HOH A . 
D 4 HOH   77  477 58  HOH   HOH A . 
D 4 HOH   78  478 161 HOH   HOH A . 
D 4 HOH   79  479 197 HOH   HOH A . 
D 4 HOH   80  480 118 HOH   HOH A . 
D 4 HOH   81  481 42  HOH   HOH A . 
D 4 HOH   82  482 97  HOH   HOH A . 
D 4 HOH   83  483 60  HOH   HOH A . 
D 4 HOH   84  484 15  HOH   HOH A . 
D 4 HOH   85  485 167 HOH   HOH A . 
D 4 HOH   86  486 22  HOH   HOH A . 
D 4 HOH   87  487 3   HOH   HOH A . 
D 4 HOH   88  488 98  HOH   HOH A . 
D 4 HOH   89  489 20  HOH   HOH A . 
D 4 HOH   90  490 427 HOH   HOH A . 
D 4 HOH   91  491 25  HOH   HOH A . 
D 4 HOH   92  492 417 HOH   HOH A . 
D 4 HOH   93  493 54  HOH   HOH A . 
D 4 HOH   94  494 487 HOH   HOH A . 
D 4 HOH   95  495 69  HOH   HOH A . 
D 4 HOH   96  496 38  HOH   HOH A . 
D 4 HOH   97  497 99  HOH   HOH A . 
D 4 HOH   98  498 52  HOH   HOH A . 
D 4 HOH   99  499 155 HOH   HOH A . 
D 4 HOH   100 500 534 HOH   HOH A . 
D 4 HOH   101 501 82  HOH   HOH A . 
D 4 HOH   102 502 23  HOH   HOH A . 
D 4 HOH   103 503 113 HOH   HOH A . 
D 4 HOH   104 504 1   HOH   HOH A . 
D 4 HOH   105 505 121 HOH   HOH A . 
D 4 HOH   106 506 147 HOH   HOH A . 
D 4 HOH   107 507 59  HOH   HOH A . 
D 4 HOH   108 508 48  HOH   HOH A . 
D 4 HOH   109 509 7   HOH   HOH A . 
D 4 HOH   110 510 2   HOH   HOH A . 
D 4 HOH   111 511 7   HOH   HOH A . 
D 4 HOH   112 512 110 HOH   HOH A . 
D 4 HOH   113 513 70  HOH   HOH A . 
D 4 HOH   114 514 91  HOH   HOH A . 
D 4 HOH   115 515 88  HOH   HOH A . 
D 4 HOH   116 516 56  HOH   HOH A . 
D 4 HOH   117 517 120 HOH   HOH A . 
D 4 HOH   118 518 21  HOH   HOH A . 
D 4 HOH   119 519 137 HOH   HOH A . 
D 4 HOH   120 520 32  HOH   HOH A . 
D 4 HOH   121 521 25  HOH   HOH A . 
D 4 HOH   122 522 21  HOH   HOH A . 
D 4 HOH   123 523 14  HOH   HOH A . 
D 4 HOH   124 524 61  HOH   HOH A . 
D 4 HOH   125 525 525 HOH   HOH A . 
D 4 HOH   126 526 53  HOH   HOH A . 
D 4 HOH   127 527 142 HOH   HOH A . 
D 4 HOH   128 528 495 HOH   HOH A . 
D 4 HOH   129 529 22  HOH   HOH A . 
D 4 HOH   130 530 103 HOH   HOH A . 
D 4 HOH   131 531 490 HOH   HOH A . 
D 4 HOH   132 532 434 HOH   HOH A . 
D 4 HOH   133 533 49  HOH   HOH A . 
D 4 HOH   134 534 1   HOH   HOH A . 
D 4 HOH   135 535 26  HOH   HOH A . 
D 4 HOH   136 536 192 HOH   HOH A . 
D 4 HOH   137 537 200 HOH   HOH A . 
D 4 HOH   138 538 119 HOH   HOH A . 
D 4 HOH   139 539 65  HOH   HOH A . 
D 4 HOH   140 540 23  HOH   HOH A . 
D 4 HOH   141 541 130 HOH   HOH A . 
D 4 HOH   142 542 90  HOH   HOH A . 
D 4 HOH   143 543 76  HOH   HOH A . 
D 4 HOH   144 544 522 HOH   HOH A . 
D 4 HOH   145 545 145 HOH   HOH A . 
D 4 HOH   146 546 139 HOH   HOH A . 
D 4 HOH   147 547 14  HOH   HOH A . 
D 4 HOH   148 548 93  HOH   HOH A . 
D 4 HOH   149 549 50  HOH   HOH A . 
D 4 HOH   150 550 148 HOH   HOH A . 
D 4 HOH   151 551 44  HOH   HOH A . 
D 4 HOH   152 552 145 HOH   HOH A . 
D 4 HOH   153 553 174 HOH   HOH A . 
D 4 HOH   154 554 107 HOH   HOH A . 
D 4 HOH   155 555 12  HOH   HOH A . 
D 4 HOH   156 556 286 HOH   HOH A . 
D 4 HOH   157 557 141 HOH   HOH A . 
D 4 HOH   158 558 180 HOH   HOH A . 
D 4 HOH   159 559 112 HOH   HOH A . 
D 4 HOH   160 560 519 HOH   HOH A . 
D 4 HOH   161 561 489 HOH   HOH A . 
D 4 HOH   162 562 33  HOH   HOH A . 
D 4 HOH   163 563 81  HOH   HOH A . 
D 4 HOH   164 564 12  HOH   HOH A . 
D 4 HOH   165 565 74  HOH   HOH A . 
D 4 HOH   166 566 47  HOH   HOH A . 
D 4 HOH   167 567 20  HOH   HOH A . 
D 4 HOH   168 568 66  HOH   HOH A . 
D 4 HOH   169 569 31  HOH   HOH A . 
D 4 HOH   170 570 514 HOH   HOH A . 
D 4 HOH   171 571 441 HOH   HOH A . 
D 4 HOH   172 572 492 HOH   HOH A . 
D 4 HOH   173 573 30  HOH   HOH A . 
D 4 HOH   174 574 171 HOH   HOH A . 
D 4 HOH   175 575 64  HOH   HOH A . 
D 4 HOH   176 576 11  HOH   HOH A . 
D 4 HOH   177 577 486 HOH   HOH A . 
D 4 HOH   178 578 380 HOH   HOH A . 
D 4 HOH   179 579 29  HOH   HOH A . 
D 4 HOH   180 580 114 HOH   HOH A . 
D 4 HOH   181 581 154 HOH   HOH A . 
D 4 HOH   182 582 55  HOH   HOH A . 
D 4 HOH   183 583 184 HOH   HOH A . 
D 4 HOH   184 584 122 HOH   HOH A . 
D 4 HOH   185 585 133 HOH   HOH A . 
D 4 HOH   186 586 149 HOH   HOH A . 
D 4 HOH   187 587 44  HOH   HOH A . 
D 4 HOH   188 588 10  HOH   HOH A . 
D 4 HOH   189 589 177 HOH   HOH A . 
D 4 HOH   190 590 146 HOH   HOH A . 
D 4 HOH   191 591 39  HOH   HOH A . 
D 4 HOH   192 592 102 HOH   HOH A . 
D 4 HOH   193 593 111 HOH   HOH A . 
D 4 HOH   194 594 54  HOH   HOH A . 
D 4 HOH   195 595 8   HOH   HOH A . 
D 4 HOH   196 596 126 HOH   HOH A . 
D 4 HOH   197 597 493 HOH   HOH A . 
D 4 HOH   198 598 409 HOH   HOH A . 
D 4 HOH   199 599 516 HOH   HOH A . 
D 4 HOH   200 600 151 HOH   HOH A . 
D 4 HOH   201 601 170 HOH   HOH A . 
D 4 HOH   202 602 86  HOH   HOH A . 
D 4 HOH   203 603 75  HOH   HOH A . 
D 4 HOH   204 604 518 HOH   HOH A . 
D 4 HOH   205 605 204 HOH   HOH A . 
D 4 HOH   206 606 511 HOH   HOH A . 
D 4 HOH   207 607 123 HOH   HOH A . 
D 4 HOH   208 608 461 HOH   HOH A . 
D 4 HOH   209 609 62  HOH   HOH A . 
D 4 HOH   210 610 156 HOH   HOH A . 
D 4 HOH   211 611 412 HOH   HOH A . 
D 4 HOH   212 612 87  HOH   HOH A . 
D 4 HOH   213 613 235 HOH   HOH A . 
D 4 HOH   214 614 210 HOH   HOH A . 
D 4 HOH   215 615 496 HOH   HOH A . 
D 4 HOH   216 616 243 HOH   HOH A . 
D 4 HOH   217 617 53  HOH   HOH A . 
D 4 HOH   218 618 77  HOH   HOH A . 
D 4 HOH   219 619 208 HOH   HOH A . 
D 4 HOH   220 620 503 HOH   HOH A . 
D 4 HOH   221 621 159 HOH   HOH A . 
D 4 HOH   222 622 78  HOH   HOH A . 
D 4 HOH   223 623 526 HOH   HOH A . 
D 4 HOH   224 624 373 HOH   HOH A . 
D 4 HOH   225 625 185 HOH   HOH A . 
D 4 HOH   226 626 521 HOH   HOH A . 
D 4 HOH   227 627 424 HOH   HOH A . 
D 4 HOH   228 628 429 HOH   HOH A . 
D 4 HOH   229 629 174 HOH   HOH A . 
D 4 HOH   230 630 153 HOH   HOH A . 
D 4 HOH   231 631 68  HOH   HOH A . 
D 4 HOH   232 632 96  HOH   HOH A . 
D 4 HOH   233 633 253 HOH   HOH A . 
D 4 HOH   234 634 375 HOH   HOH A . 
D 4 HOH   235 635 416 HOH   HOH A . 
D 4 HOH   236 636 104 HOH   HOH A . 
D 4 HOH   237 637 471 HOH   HOH A . 
D 4 HOH   238 638 36  HOH   HOH A . 
D 4 HOH   239 639 238 HOH   HOH A . 
D 4 HOH   240 640 157 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 LYS 45  ? CD  ? A LYS 45  CD  
11 1 Y 1 A LYS 45  ? CE  ? A LYS 45  CE  
12 1 Y 1 A LYS 45  ? NZ  ? A LYS 45  NZ  
13 1 Y 1 A LYS 80  ? CD  ? A LYS 80  CD  
14 1 Y 1 A LYS 80  ? CE  ? A LYS 80  CE  
15 1 Y 1 A LYS 80  ? NZ  ? A LYS 80  NZ  
16 1 Y 1 A LYS 126 ? NZ  ? A LYS 126 NZ  
17 1 Y 1 A LYS 132 ? CE  ? A LYS 132 CE  
18 1 Y 1 A LYS 132 ? NZ  ? A LYS 132 NZ  
19 1 Y 1 A LYS 148 ? CE  ? A LYS 148 CE  
20 1 Y 1 A LYS 148 ? NZ  ? A LYS 148 NZ  
21 1 Y 1 A LYS 158 ? CD  ? A LYS 158 CD  
22 1 Y 1 A LYS 158 ? CE  ? A LYS 158 CE  
23 1 Y 1 A LYS 158 ? NZ  ? A LYS 158 NZ  
24 1 Y 1 A ASP 164 ? CG  ? A ASP 164 CG  
25 1 Y 1 A ASP 164 ? OD1 ? A ASP 164 OD1 
26 1 Y 1 A ASP 164 ? OD2 ? A ASP 164 OD2 
27 1 Y 1 A LYS 171 ? CE  ? A LYS 171 CE  
28 1 Y 1 A LYS 171 ? NZ  ? A LYS 171 NZ  
29 1 Y 1 A LYS 212 ? NZ  ? A LYS 212 NZ  
30 1 Y 1 A LYS 224 ? CD  ? A LYS 224 CD  
31 1 Y 1 A LYS 224 ? CE  ? A LYS 224 CE  
32 1 Y 1 A LYS 224 ? NZ  ? A LYS 224 NZ  
33 1 Y 1 A GLU 238 ? CG  ? A GLU 238 CG  
34 1 Y 1 A GLU 238 ? CD  ? A GLU 238 CD  
35 1 Y 1 A GLU 238 ? OE1 ? A GLU 238 OE1 
36 1 Y 1 A GLU 238 ? OE2 ? A GLU 238 OE2 
37 1 Y 1 A LYS 251 ? NZ  ? A LYS 251 NZ  
38 1 Y 1 A ASN 252 ? CG  ? A ASN 252 CG  
39 1 Y 1 A ASN 252 ? OD1 ? A ASN 252 OD1 
40 1 Y 1 A ASN 252 ? ND2 ? A ASN 252 ND2 
41 1 Y 1 A GLN 254 ? CG  ? A GLN 254 CG  
42 1 Y 1 A GLN 254 ? CD  ? A GLN 254 CD  
43 1 Y 1 A GLN 254 ? OE1 ? A GLN 254 OE1 
44 1 Y 1 A GLN 254 ? NE2 ? A GLN 254 NE2 
45 1 Y 1 A LYS 256 ? CD  ? A LYS 256 CD  
46 1 Y 1 A LYS 256 ? CE  ? A LYS 256 CE  
47 1 Y 1 A LYS 256 ? NZ  ? A LYS 256 NZ  
48 1 Y 1 A LYS 260 ? CG  ? A LYS 260 CG  
49 1 Y 1 A LYS 260 ? CD  ? A LYS 260 CD  
50 1 Y 1 A LYS 260 ? CE  ? A LYS 260 CE  
51 1 Y 1 A LYS 260 ? NZ  ? A LYS 260 NZ  
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? 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                   103.87 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8RNS 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     41.980 
_cell.length_a_esd                 ? 
_cell.length_b                     41.330 
_cell.length_b_esd                 ? 
_cell.length_c                     71.810 
_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                         8RNS 
_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                   8RNS 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.06 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          40.23 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.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 M sodium citrate, 50 mM Tris-HCl (pH 7.5)' 
_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         2023-09-20 
_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   1.0001 
_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        1.0001 
_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                                       8RNS 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.1 
_reflns.d_resolution_low                               40.8 
_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                                     85727 
_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                           98.2 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                5.9 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          12.0 
_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                                0.08 
_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                              0.07 
_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                                    1.14 
_reflns_shell.d_res_low                                     1.16 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.1 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             3897 
_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                               4.3 
_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                               1.547 
_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                                  0.368 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          90.0 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  1.351 
_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]                            0.14 
_refine.aniso_B[1][2]                            -0.00 
_refine.aniso_B[1][3]                            0.24 
_refine.aniso_B[2][2]                            -0.45 
_refine.aniso_B[2][3]                            0.00 
_refine.aniso_B[3][3]                            0.17 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               14.926 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.981 
_refine.correlation_coeff_Fo_to_Fc_free          0.978 
_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                                 8RNS 
_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                            1.14 
_refine.ls_d_res_low                             40.79 
_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                     81295 
_refine.ls_number_reflns_R_free                  4353 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.15 
_refine.ls_percent_reflns_R_free                 5.1 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.14252 
_refine.ls_R_factor_R_free                       0.16139 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.14149 
_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                       0.034 
_refine.pdbx_overall_ESU_R_Free                  0.033 
_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                             1.382 
_refine.overall_SU_ML                            0.027 
_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                       1.14 
_refine_hist.d_res_low                        40.79 
_refine_hist.number_atoms_solvent             241 
_refine_hist.number_atoms_total               2264 
_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        2023 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         0 
_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' ? 0.011  0.012  2289 ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.016  2024 ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.766  1.661  3153 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 0.644  1.597  4698 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 6.980  5.000  301  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 26.120 5.000  12   ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 12.120 10.000 328  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.097  0.200  327  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.011  0.020  2851 ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.003  0.020  539  ? 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' ? 4.864  1.518  1144 ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 4.785  1.517  1144 ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 6.819  2.733  1465 ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 6.829  2.735  1466 ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 6.390  1.705  1145 ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 6.393  1.708  1146 ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 8.921  3.025  1688 ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 13.286 18.67  2528 ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 12.247 17.04  2468 ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? 3.917  3.000  4313 ? 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                       1.140 
_refine_ls_shell.d_res_low                        1.170 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             293 
_refine_ls_shell.number_reflns_R_work             5480 
_refine_ls_shell.percent_reflns_obs               90.23 
_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                  0.314 
_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                  0.311 
# 
_struct.entry_id                     8RNS 
_struct.title                        
;Human Carbonic Anhydrase XII mimic in complex with biguanide derivative inhibitor 1-carbamimidamido-N-[(4 sulfamoylphenyl)methyl]methanimidamide
;
_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        8RNS 
_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 4 ? 
# 
_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           0 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              8RNS 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 260 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P00918 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  260 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       260 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 8RNS SER A 65  ? UNP P00918 ALA 65  'engineered mutation' 65  1 
1 8RNS LYS A 67  ? UNP P00918 ASN 67  'engineered mutation' 67  2 
1 8RNS ASN A 69  ? UNP P00918 GLU 69  'engineered mutation' 69  3 
1 8RNS THR A 91  ? UNP P00918 ILE 91  'engineered mutation' 91  4 
1 8RNS ALA A 130 ? UNP P00918 PHE 130 'engineered mutation' 130 5 
1 8RNS SER A 131 ? UNP P00918 GLY 131 'engineered mutation' 131 6 
1 8RNS SER A 134 ? UNP P00918 VAL 134 'engineered mutation' 134 7 
1 8RNS ASN A 203 ? UNP P00918 LEU 203 'engineered mutation' 203 8 
1 8RNS THR A 205 ? UNP P00918 CYS 205 'engineered mutation' 205 9 
# 
_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)' 0     ? 
1 MORE         0     ? 
1 'SSA (A^2)'  11320 ? 
# 
_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 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 GLY A 12  ? ASP A 19  ? GLY A 12  ASP A 19  5 ? 8 
HELX_P HELX_P2 AA2 PHE A 20  ? GLY A 25  ? PHE A 20  GLY A 25  5 ? 6 
HELX_P HELX_P3 AA3 LYS A 126 ? GLY A 128 ? LYS A 126 GLY A 128 5 ? 3 
HELX_P HELX_P4 AA4 ASP A 129 ? SER A 134 ? ASP A 129 SER A 134 1 ? 6 
HELX_P HELX_P5 AA5 LYS A 153 ? GLY A 155 ? LYS A 153 GLY A 155 5 ? 3 
HELX_P HELX_P6 AA6 LEU A 156 ? LEU A 163 ? LEU A 156 LEU A 163 1 ? 8 
HELX_P HELX_P7 AA7 ASP A 164 ? LYS A 167 ? ASP A 164 LYS A 167 5 ? 4 
HELX_P HELX_P8 AA8 ASP A 179 ? LEU A 184 ? ASP A 179 LEU A 184 5 ? 6 
HELX_P HELX_P9 AA9 SER A 218 ? ARG A 226 ? SER A 218 ARG A 226 1 ? 9 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A HIS 94  NE2 ? ? ? 1_555 B ZN    . ZN ? ? A HIS 94  A ZN    301 1_555 ? ? ? ? ? ? ? 2.011 ? ? 
metalc2 metalc ? ? A HIS 96  NE2 ? ? ? 1_555 B ZN    . ZN ? ? A HIS 96  A ZN    301 1_555 ? ? ? ? ? ? ? 2.047 ? ? 
metalc3 metalc ? ? A HIS 119 ND1 ? ? ? 1_555 B ZN    . ZN ? ? A HIS 119 A ZN    301 1_555 ? ? ? ? ? ? ? 2.024 ? ? 
metalc4 metalc ? ? B ZN  .   ZN  ? ? ? 1_555 C A1H15 . N9 ? ? A ZN  301 A A1H15 302 1_555 ? ? ? ? ? ? ? 1.950 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1 NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 NE2 ? A HIS   96  ? A HIS   96  ? 1_555 103.9 ? 
2 NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 ND1 ? A HIS   119 ? A HIS   119 ? 1_555 112.2 ? 
3 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 ND1 ? A HIS   119 ? A HIS   119 ? 1_555 99.0  ? 
4 NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N9  ? C A1H15 .   ? A A1H15 302 ? 1_555 108.2 ? 
5 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N9  ? C A1H15 .   ? A A1H15 302 ? 1_555 114.1 ? 
6 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N9  ? C A1H15 .   ? A A1H15 302 ? 1_555 118.5 ? 
# 
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 -5.75 
2 PRO 200 A . ? PRO 200 A PRO 201 A ? PRO 201 A 1 7.57  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2  ? 
AA2 ? 10 ? 
AA3 ? 6  ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2  ? parallel      
AA2 1 2  ? parallel      
AA2 2 3  ? anti-parallel 
AA2 3 4  ? anti-parallel 
AA2 4 5  ? parallel      
AA2 5 6  ? anti-parallel 
AA2 6 7  ? anti-parallel 
AA2 7 8  ? anti-parallel 
AA2 8 9  ? anti-parallel 
AA2 9 10 ? anti-parallel 
AA3 1 2  ? anti-parallel 
AA3 2 3  ? anti-parallel 
AA3 3 4  ? anti-parallel 
AA3 4 5  ? anti-parallel 
AA3 5 6  ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1  ASP A 32  ? ILE A 33  ? ASP A 32  ILE A 33  
AA1 2  THR A 108 ? VAL A 109 ? THR A 108 VAL A 109 
AA2 1  LYS A 39  ? TYR A 40  ? LYS A 39  TYR A 40  
AA2 2  LYS A 256 ? ALA A 257 ? LYS A 256 ALA A 257 
AA2 3  TYR A 190 ? GLY A 195 ? TYR A 190 GLY A 195 
AA2 4  VAL A 206 ? LEU A 211 ? VAL A 206 LEU A 211 
AA2 5  LEU A 140 ? VAL A 149 ? LEU A 140 VAL A 149 
AA2 6  ALA A 116 ? ASN A 124 ? ALA A 116 ASN A 124 
AA2 7  TYR A 88  ? TRP A 97  ? TYR A 88  TRP A 97  
AA2 8  PHE A 66  ? PHE A 70  ? PHE A 66  PHE A 70  
AA2 9  SER A 56  ? ASN A 61  ? SER A 56  ASN A 61  
AA2 10 SER A 172 ? ASP A 174 ? SER A 172 ASP A 174 
AA3 1  LEU A 47  ? SER A 50  ? LEU A 47  SER A 50  
AA3 2  VAL A 78  ? GLY A 81  ? VAL A 78  GLY A 81  
AA3 3  TYR A 88  ? TRP A 97  ? TYR A 88  TRP A 97  
AA3 4  ALA A 116 ? ASN A 124 ? ALA A 116 ASN A 124 
AA3 5  LEU A 140 ? VAL A 149 ? LEU A 140 VAL A 149 
AA3 6  ILE A 215 ? VAL A 217 ? ILE A 215 VAL A 217 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2  N ILE A 33  ? N ILE A 33  O THR A 108 ? O THR A 108 
AA2 1 2  N LYS A 39  ? N LYS A 39  O ALA A 257 ? O ALA A 257 
AA2 2 3  O LYS A 256 ? O LYS A 256 N THR A 192 ? N THR A 192 
AA2 3 4  N GLY A 195 ? N GLY A 195 O VAL A 206 ? O VAL A 206 
AA2 4 5  O ILE A 209 ? O ILE A 209 N GLY A 144 ? N GLY A 144 
AA2 5 6  O ILE A 145 ? O ILE A 145 N LEU A 118 ? N LEU A 118 
AA2 6 7  O VAL A 121 ? O VAL A 121 N GLN A 92  ? N GLN A 92  
AA2 7 8  O PHE A 93  ? O PHE A 93  N VAL A 68  ? N VAL A 68  
AA2 8 9  O ASN A 69  ? O ASN A 69  N LEU A 57  ? N LEU A 57  
AA2 9 10 N ILE A 59  ? N ILE A 59  O ALA A 173 ? O ALA A 173 
AA3 1 2  N SER A 50  ? N SER A 50  O VAL A 78  ? O VAL A 78  
AA3 2 3  N LEU A 79  ? N LEU A 79  O TYR A 88  ? O TYR A 88  
AA3 3 4  N GLN A 92  ? N GLN A 92  O VAL A 121 ? O VAL A 121 
AA3 4 5  N LEU A 118 ? N LEU A 118 O ILE A 145 ? O ILE A 145 
AA3 5 6  N PHE A 146 ? N PHE A 146 O ILE A 215 ? O ILE A 215 
# 
_pdbx_entry_details.entry_id                   8RNS 
_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 
# 
_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             213 
_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             213 
_pdbx_validate_rmsd_bond.PDB_ins_code_2            ? 
_pdbx_validate_rmsd_bond.label_alt_id_2            ? 
_pdbx_validate_rmsd_bond.bond_value                1.149 
_pdbx_validate_rmsd_bond.bond_target_value         1.252 
_pdbx_validate_rmsd_bond.bond_deviation            -0.103 
_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  ? B CZ A ARG 27  ? B NH1 A ARG 27  ? B 115.88 120.30 -4.42 0.50 N 
2 1 NE A ARG 27  ? B CZ A ARG 27  ? B NH2 A ARG 27  ? B 124.12 120.30 3.82  0.50 N 
3 1 CB A PHE 225 ? ? CG A PHE 225 ? ? CD1 A PHE 225 ? ? 125.03 120.80 4.23  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 ARG A 27  ? A -144.54 46.82   
2 1 SER A 65  ? A -162.69 -168.52 
3 1 LYS A 76  ? B -123.51 -76.98  
4 1 GLU A 106 ? ? -91.95  -61.49  
5 1 LYS A 111 ? ? 74.77   -3.20   
6 1 PHE A 175 ? ? -150.75 60.90   
7 1 ASN A 243 ? ? -93.95  47.39   
8 1 LYS A 251 ? ? 57.98   -139.06 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A MET 1 ? A MET 1 
2 1 Y 1 A SER 2 ? A SER 2 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
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 
HIS   N    N  N N 169 
HIS   CA   C  N S 170 
HIS   C    C  N N 171 
HIS   O    O  N N 172 
HIS   CB   C  N N 173 
HIS   CG   C  Y N 174 
HIS   ND1  N  Y N 175 
HIS   CD2  C  Y N 176 
HIS   CE1  C  Y N 177 
HIS   NE2  N  Y N 178 
HIS   OXT  O  N N 179 
HIS   H    H  N N 180 
HIS   H2   H  N N 181 
HIS   HA   H  N N 182 
HIS   HB2  H  N N 183 
HIS   HB3  H  N N 184 
HIS   HD1  H  N N 185 
HIS   HD2  H  N N 186 
HIS   HE1  H  N N 187 
HIS   HE2  H  N N 188 
HIS   HXT  H  N N 189 
HOH   O    O  N N 190 
HOH   H1   H  N N 191 
HOH   H2   H  N N 192 
ILE   N    N  N N 193 
ILE   CA   C  N S 194 
ILE   C    C  N N 195 
ILE   O    O  N N 196 
ILE   CB   C  N S 197 
ILE   CG1  C  N N 198 
ILE   CG2  C  N N 199 
ILE   CD1  C  N N 200 
ILE   OXT  O  N N 201 
ILE   H    H  N N 202 
ILE   H2   H  N N 203 
ILE   HA   H  N N 204 
ILE   HB   H  N N 205 
ILE   HG12 H  N N 206 
ILE   HG13 H  N N 207 
ILE   HG21 H  N N 208 
ILE   HG22 H  N N 209 
ILE   HG23 H  N N 210 
ILE   HD11 H  N N 211 
ILE   HD12 H  N N 212 
ILE   HD13 H  N N 213 
ILE   HXT  H  N N 214 
LEU   N    N  N N 215 
LEU   CA   C  N S 216 
LEU   C    C  N N 217 
LEU   O    O  N N 218 
LEU   CB   C  N N 219 
LEU   CG   C  N N 220 
LEU   CD1  C  N N 221 
LEU   CD2  C  N N 222 
LEU   OXT  O  N N 223 
LEU   H    H  N N 224 
LEU   H2   H  N N 225 
LEU   HA   H  N N 226 
LEU   HB2  H  N N 227 
LEU   HB3  H  N N 228 
LEU   HG   H  N N 229 
LEU   HD11 H  N N 230 
LEU   HD12 H  N N 231 
LEU   HD13 H  N N 232 
LEU   HD21 H  N N 233 
LEU   HD22 H  N N 234 
LEU   HD23 H  N N 235 
LEU   HXT  H  N N 236 
LYS   N    N  N N 237 
LYS   CA   C  N S 238 
LYS   C    C  N N 239 
LYS   O    O  N N 240 
LYS   CB   C  N N 241 
LYS   CG   C  N N 242 
LYS   CD   C  N N 243 
LYS   CE   C  N N 244 
LYS   NZ   N  N N 245 
LYS   OXT  O  N N 246 
LYS   H    H  N N 247 
LYS   H2   H  N N 248 
LYS   HA   H  N N 249 
LYS   HB2  H  N N 250 
LYS   HB3  H  N N 251 
LYS   HG2  H  N N 252 
LYS   HG3  H  N N 253 
LYS   HD2  H  N N 254 
LYS   HD3  H  N N 255 
LYS   HE2  H  N N 256 
LYS   HE3  H  N N 257 
LYS   HZ1  H  N N 258 
LYS   HZ2  H  N N 259 
LYS   HZ3  H  N N 260 
LYS   HXT  H  N N 261 
MET   N    N  N N 262 
MET   CA   C  N S 263 
MET   C    C  N N 264 
MET   O    O  N N 265 
MET   CB   C  N N 266 
MET   CG   C  N N 267 
MET   SD   S  N N 268 
MET   CE   C  N N 269 
MET   OXT  O  N N 270 
MET   H    H  N N 271 
MET   H2   H  N N 272 
MET   HA   H  N N 273 
MET   HB2  H  N N 274 
MET   HB3  H  N N 275 
MET   HG2  H  N N 276 
MET   HG3  H  N N 277 
MET   HE1  H  N N 278 
MET   HE2  H  N N 279 
MET   HE3  H  N N 280 
MET   HXT  H  N N 281 
PHE   N    N  N N 282 
PHE   CA   C  N S 283 
PHE   C    C  N N 284 
PHE   O    O  N N 285 
PHE   CB   C  N N 286 
PHE   CG   C  Y N 287 
PHE   CD1  C  Y N 288 
PHE   CD2  C  Y N 289 
PHE   CE1  C  Y N 290 
PHE   CE2  C  Y N 291 
PHE   CZ   C  Y N 292 
PHE   OXT  O  N N 293 
PHE   H    H  N N 294 
PHE   H2   H  N N 295 
PHE   HA   H  N N 296 
PHE   HB2  H  N N 297 
PHE   HB3  H  N N 298 
PHE   HD1  H  N N 299 
PHE   HD2  H  N N 300 
PHE   HE1  H  N N 301 
PHE   HE2  H  N N 302 
PHE   HZ   H  N N 303 
PHE   HXT  H  N N 304 
PRO   N    N  N N 305 
PRO   CA   C  N S 306 
PRO   C    C  N N 307 
PRO   O    O  N N 308 
PRO   CB   C  N N 309 
PRO   CG   C  N N 310 
PRO   CD   C  N N 311 
PRO   OXT  O  N N 312 
PRO   H    H  N N 313 
PRO   HA   H  N N 314 
PRO   HB2  H  N N 315 
PRO   HB3  H  N N 316 
PRO   HG2  H  N N 317 
PRO   HG3  H  N N 318 
PRO   HD2  H  N N 319 
PRO   HD3  H  N N 320 
PRO   HXT  H  N N 321 
SER   N    N  N N 322 
SER   CA   C  N S 323 
SER   C    C  N N 324 
SER   O    O  N N 325 
SER   CB   C  N N 326 
SER   OG   O  N N 327 
SER   OXT  O  N N 328 
SER   H    H  N N 329 
SER   H2   H  N N 330 
SER   HA   H  N N 331 
SER   HB2  H  N N 332 
SER   HB3  H  N N 333 
SER   HG   H  N N 334 
SER   HXT  H  N N 335 
THR   N    N  N N 336 
THR   CA   C  N S 337 
THR   C    C  N N 338 
THR   O    O  N N 339 
THR   CB   C  N R 340 
THR   OG1  O  N N 341 
THR   CG2  C  N N 342 
THR   OXT  O  N N 343 
THR   H    H  N N 344 
THR   H2   H  N N 345 
THR   HA   H  N N 346 
THR   HB   H  N N 347 
THR   HG1  H  N N 348 
THR   HG21 H  N N 349 
THR   HG22 H  N N 350 
THR   HG23 H  N N 351 
THR   HXT  H  N N 352 
TRP   N    N  N N 353 
TRP   CA   C  N S 354 
TRP   C    C  N N 355 
TRP   O    O  N N 356 
TRP   CB   C  N N 357 
TRP   CG   C  Y N 358 
TRP   CD1  C  Y N 359 
TRP   CD2  C  Y N 360 
TRP   NE1  N  Y N 361 
TRP   CE2  C  Y N 362 
TRP   CE3  C  Y N 363 
TRP   CZ2  C  Y N 364 
TRP   CZ3  C  Y N 365 
TRP   CH2  C  Y N 366 
TRP   OXT  O  N N 367 
TRP   H    H  N N 368 
TRP   H2   H  N N 369 
TRP   HA   H  N N 370 
TRP   HB2  H  N N 371 
TRP   HB3  H  N N 372 
TRP   HD1  H  N N 373 
TRP   HE1  H  N N 374 
TRP   HE3  H  N N 375 
TRP   HZ2  H  N N 376 
TRP   HZ3  H  N N 377 
TRP   HH2  H  N N 378 
TRP   HXT  H  N N 379 
TYR   N    N  N N 380 
TYR   CA   C  N S 381 
TYR   C    C  N N 382 
TYR   O    O  N N 383 
TYR   CB   C  N N 384 
TYR   CG   C  Y N 385 
TYR   CD1  C  Y N 386 
TYR   CD2  C  Y N 387 
TYR   CE1  C  Y N 388 
TYR   CE2  C  Y N 389 
TYR   CZ   C  Y N 390 
TYR   OH   O  N N 391 
TYR   OXT  O  N N 392 
TYR   H    H  N N 393 
TYR   H2   H  N N 394 
TYR   HA   H  N N 395 
TYR   HB2  H  N N 396 
TYR   HB3  H  N N 397 
TYR   HD1  H  N N 398 
TYR   HD2  H  N N 399 
TYR   HE1  H  N N 400 
TYR   HE2  H  N N 401 
TYR   HH   H  N N 402 
TYR   HXT  H  N N 403 
VAL   N    N  N N 404 
VAL   CA   C  N S 405 
VAL   C    C  N N 406 
VAL   O    O  N N 407 
VAL   CB   C  N N 408 
VAL   CG1  C  N N 409 
VAL   CG2  C  N N 410 
VAL   OXT  O  N N 411 
VAL   H    H  N N 412 
VAL   H2   H  N N 413 
VAL   HA   H  N N 414 
VAL   HB   H  N N 415 
VAL   HG11 H  N N 416 
VAL   HG12 H  N N 417 
VAL   HG13 H  N N 418 
VAL   HG21 H  N N 419 
VAL   HG22 H  N N 420 
VAL   HG23 H  N N 421 
VAL   HXT  H  N N 422 
ZN    ZN   ZN N N 423 
# 
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 
HIS   N   CA   sing N N 161 
HIS   N   H    sing N N 162 
HIS   N   H2   sing N N 163 
HIS   CA  C    sing N N 164 
HIS   CA  CB   sing N N 165 
HIS   CA  HA   sing N N 166 
HIS   C   O    doub N N 167 
HIS   C   OXT  sing N N 168 
HIS   CB  CG   sing N N 169 
HIS   CB  HB2  sing N N 170 
HIS   CB  HB3  sing N N 171 
HIS   CG  ND1  sing Y N 172 
HIS   CG  CD2  doub Y N 173 
HIS   ND1 CE1  doub Y N 174 
HIS   ND1 HD1  sing N N 175 
HIS   CD2 NE2  sing Y N 176 
HIS   CD2 HD2  sing N N 177 
HIS   CE1 NE2  sing Y N 178 
HIS   CE1 HE1  sing N N 179 
HIS   NE2 HE2  sing N N 180 
HIS   OXT HXT  sing N N 181 
HOH   O   H1   sing N N 182 
HOH   O   H2   sing N N 183 
ILE   N   CA   sing N N 184 
ILE   N   H    sing N N 185 
ILE   N   H2   sing N N 186 
ILE   CA  C    sing N N 187 
ILE   CA  CB   sing N N 188 
ILE   CA  HA   sing N N 189 
ILE   C   O    doub N N 190 
ILE   C   OXT  sing N N 191 
ILE   CB  CG1  sing N N 192 
ILE   CB  CG2  sing N N 193 
ILE   CB  HB   sing N N 194 
ILE   CG1 CD1  sing N N 195 
ILE   CG1 HG12 sing N N 196 
ILE   CG1 HG13 sing N N 197 
ILE   CG2 HG21 sing N N 198 
ILE   CG2 HG22 sing N N 199 
ILE   CG2 HG23 sing N N 200 
ILE   CD1 HD11 sing N N 201 
ILE   CD1 HD12 sing N N 202 
ILE   CD1 HD13 sing N N 203 
ILE   OXT HXT  sing N N 204 
LEU   N   CA   sing N N 205 
LEU   N   H    sing N N 206 
LEU   N   H2   sing N N 207 
LEU   CA  C    sing N N 208 
LEU   CA  CB   sing N N 209 
LEU   CA  HA   sing N N 210 
LEU   C   O    doub N N 211 
LEU   C   OXT  sing N N 212 
LEU   CB  CG   sing N N 213 
LEU   CB  HB2  sing N N 214 
LEU   CB  HB3  sing N N 215 
LEU   CG  CD1  sing N N 216 
LEU   CG  CD2  sing N N 217 
LEU   CG  HG   sing N N 218 
LEU   CD1 HD11 sing N N 219 
LEU   CD1 HD12 sing N N 220 
LEU   CD1 HD13 sing N N 221 
LEU   CD2 HD21 sing N N 222 
LEU   CD2 HD22 sing N N 223 
LEU   CD2 HD23 sing N N 224 
LEU   OXT HXT  sing N N 225 
LYS   N   CA   sing N N 226 
LYS   N   H    sing N N 227 
LYS   N   H2   sing N N 228 
LYS   CA  C    sing N N 229 
LYS   CA  CB   sing N N 230 
LYS   CA  HA   sing N N 231 
LYS   C   O    doub N N 232 
LYS   C   OXT  sing N N 233 
LYS   CB  CG   sing N N 234 
LYS   CB  HB2  sing N N 235 
LYS   CB  HB3  sing N N 236 
LYS   CG  CD   sing N N 237 
LYS   CG  HG2  sing N N 238 
LYS   CG  HG3  sing N N 239 
LYS   CD  CE   sing N N 240 
LYS   CD  HD2  sing N N 241 
LYS   CD  HD3  sing N N 242 
LYS   CE  NZ   sing N N 243 
LYS   CE  HE2  sing N N 244 
LYS   CE  HE3  sing N N 245 
LYS   NZ  HZ1  sing N N 246 
LYS   NZ  HZ2  sing N N 247 
LYS   NZ  HZ3  sing N N 248 
LYS   OXT HXT  sing N N 249 
MET   N   CA   sing N N 250 
MET   N   H    sing N N 251 
MET   N   H2   sing N N 252 
MET   CA  C    sing N N 253 
MET   CA  CB   sing N N 254 
MET   CA  HA   sing N N 255 
MET   C   O    doub N N 256 
MET   C   OXT  sing N N 257 
MET   CB  CG   sing N N 258 
MET   CB  HB2  sing N N 259 
MET   CB  HB3  sing N N 260 
MET   CG  SD   sing N N 261 
MET   CG  HG2  sing N N 262 
MET   CG  HG3  sing N N 263 
MET   SD  CE   sing N N 264 
MET   CE  HE1  sing N N 265 
MET   CE  HE2  sing N N 266 
MET   CE  HE3  sing N N 267 
MET   OXT HXT  sing N N 268 
PHE   N   CA   sing N N 269 
PHE   N   H    sing N N 270 
PHE   N   H2   sing N N 271 
PHE   CA  C    sing N N 272 
PHE   CA  CB   sing N N 273 
PHE   CA  HA   sing N N 274 
PHE   C   O    doub N N 275 
PHE   C   OXT  sing N N 276 
PHE   CB  CG   sing N N 277 
PHE   CB  HB2  sing N N 278 
PHE   CB  HB3  sing N N 279 
PHE   CG  CD1  doub Y N 280 
PHE   CG  CD2  sing Y N 281 
PHE   CD1 CE1  sing Y N 282 
PHE   CD1 HD1  sing N N 283 
PHE   CD2 CE2  doub Y N 284 
PHE   CD2 HD2  sing N N 285 
PHE   CE1 CZ   doub Y N 286 
PHE   CE1 HE1  sing N N 287 
PHE   CE2 CZ   sing Y N 288 
PHE   CE2 HE2  sing N N 289 
PHE   CZ  HZ   sing N N 290 
PHE   OXT HXT  sing N N 291 
PRO   N   CA   sing N N 292 
PRO   N   CD   sing N N 293 
PRO   N   H    sing N N 294 
PRO   CA  C    sing N N 295 
PRO   CA  CB   sing N N 296 
PRO   CA  HA   sing N N 297 
PRO   C   O    doub N N 298 
PRO   C   OXT  sing N N 299 
PRO   CB  CG   sing N N 300 
PRO   CB  HB2  sing N N 301 
PRO   CB  HB3  sing N N 302 
PRO   CG  CD   sing N N 303 
PRO   CG  HG2  sing N N 304 
PRO   CG  HG3  sing N N 305 
PRO   CD  HD2  sing N N 306 
PRO   CD  HD3  sing N N 307 
PRO   OXT HXT  sing N N 308 
SER   N   CA   sing N N 309 
SER   N   H    sing N N 310 
SER   N   H2   sing N N 311 
SER   CA  C    sing N N 312 
SER   CA  CB   sing N N 313 
SER   CA  HA   sing N N 314 
SER   C   O    doub N N 315 
SER   C   OXT  sing N N 316 
SER   CB  OG   sing N N 317 
SER   CB  HB2  sing N N 318 
SER   CB  HB3  sing N N 319 
SER   OG  HG   sing N N 320 
SER   OXT HXT  sing N N 321 
THR   N   CA   sing N N 322 
THR   N   H    sing N N 323 
THR   N   H2   sing N N 324 
THR   CA  C    sing N N 325 
THR   CA  CB   sing N N 326 
THR   CA  HA   sing N N 327 
THR   C   O    doub N N 328 
THR   C   OXT  sing N N 329 
THR   CB  OG1  sing N N 330 
THR   CB  CG2  sing N N 331 
THR   CB  HB   sing N N 332 
THR   OG1 HG1  sing N N 333 
THR   CG2 HG21 sing N N 334 
THR   CG2 HG22 sing N N 335 
THR   CG2 HG23 sing N N 336 
THR   OXT HXT  sing N N 337 
TRP   N   CA   sing N N 338 
TRP   N   H    sing N N 339 
TRP   N   H2   sing N N 340 
TRP   CA  C    sing N N 341 
TRP   CA  CB   sing N N 342 
TRP   CA  HA   sing N N 343 
TRP   C   O    doub N N 344 
TRP   C   OXT  sing N N 345 
TRP   CB  CG   sing N N 346 
TRP   CB  HB2  sing N N 347 
TRP   CB  HB3  sing N N 348 
TRP   CG  CD1  doub Y N 349 
TRP   CG  CD2  sing Y N 350 
TRP   CD1 NE1  sing Y N 351 
TRP   CD1 HD1  sing N N 352 
TRP   CD2 CE2  doub Y N 353 
TRP   CD2 CE3  sing Y N 354 
TRP   NE1 CE2  sing Y N 355 
TRP   NE1 HE1  sing N N 356 
TRP   CE2 CZ2  sing Y N 357 
TRP   CE3 CZ3  doub Y N 358 
TRP   CE3 HE3  sing N N 359 
TRP   CZ2 CH2  doub Y N 360 
TRP   CZ2 HZ2  sing N N 361 
TRP   CZ3 CH2  sing Y N 362 
TRP   CZ3 HZ3  sing N N 363 
TRP   CH2 HH2  sing N N 364 
TRP   OXT HXT  sing N N 365 
TYR   N   CA   sing N N 366 
TYR   N   H    sing N N 367 
TYR   N   H2   sing N N 368 
TYR   CA  C    sing N N 369 
TYR   CA  CB   sing N N 370 
TYR   CA  HA   sing N N 371 
TYR   C   O    doub N N 372 
TYR   C   OXT  sing N N 373 
TYR   CB  CG   sing N N 374 
TYR   CB  HB2  sing N N 375 
TYR   CB  HB3  sing N N 376 
TYR   CG  CD1  doub Y N 377 
TYR   CG  CD2  sing Y N 378 
TYR   CD1 CE1  sing Y N 379 
TYR   CD1 HD1  sing N N 380 
TYR   CD2 CE2  doub Y N 381 
TYR   CD2 HD2  sing N N 382 
TYR   CE1 CZ   doub Y N 383 
TYR   CE1 HE1  sing N N 384 
TYR   CE2 CZ   sing Y N 385 
TYR   CE2 HE2  sing N N 386 
TYR   CZ  OH   sing N N 387 
TYR   OH  HH   sing N N 388 
TYR   OXT HXT  sing N N 389 
VAL   N   CA   sing N N 390 
VAL   N   H    sing N N 391 
VAL   N   H2   sing N N 392 
VAL   CA  C    sing N N 393 
VAL   CA  CB   sing N N 394 
VAL   CA  HA   sing N N 395 
VAL   C   O    doub N N 396 
VAL   C   OXT  sing N N 397 
VAL   CB  CG1  sing N N 398 
VAL   CB  CG2  sing N N 399 
VAL   CB  HB   sing N N 400 
VAL   CG1 HG11 sing N N 401 
VAL   CG1 HG12 sing N N 402 
VAL   CG1 HG13 sing N N 403 
VAL   CG2 HG21 sing N N 404 
VAL   CG2 HG22 sing N N 405 
VAL   CG2 HG23 sing N N 406 
VAL   OXT HXT  sing N N 407 
# 
_pdbx_audit_support.funding_organization   'European Union (EU)' 
_pdbx_audit_support.country                'European Union' 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_atom_sites.entry_id                    8RNS 
_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]   0.023821 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.005883 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.024195 
_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]   0.014344 
_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 3   ? 34.868 2.078   6.763   1.00 30.80 ? 3   HIS   A N   1 
ATOM   2    C  CA  . HIS   A 1 3   ? 34.511 1.034   7.767   1.00 34.49 ? 3   HIS   A CA  1 
ATOM   3    C  C   . HIS   A 1 3   ? 33.331 1.475   8.649   1.00 32.07 ? 3   HIS   A C   1 
ATOM   4    O  O   . HIS   A 1 3   ? 33.501 1.601   9.881   1.00 37.51 ? 3   HIS   A O   1 
ATOM   5    C  CB  . HIS   A 1 3   ? 35.731 0.698   8.645   1.00 33.57 ? 3   HIS   A CB  1 
ATOM   6    C  CG  . HIS   A 1 3   ? 35.664 -0.646  9.249   1.00 32.05 ? 3   HIS   A CG  1 
ATOM   7    N  ND1 . HIS   A 1 3   ? 35.604 -1.797  8.361   1.00 34.74 ? 3   HIS   A ND1 1 
ATOM   8    C  CD2 . HIS   A 1 3   ? 35.405 -1.066  10.521  1.00 35.97 ? 3   HIS   A CD2 1 
ATOM   9    C  CE1 . HIS   A 1 3   ? 35.525 -2.873  9.179   1.00 38.82 ? 3   HIS   A CE1 1 
ATOM   10   N  NE2 . HIS   A 1 3   ? 35.348 -2.453  10.465  1.00 39.43 ? 3   HIS   A NE2 1 
ATOM   11   N  N   . HIS   A 1 4   ? 32.175 1.717   7.987   1.00 26.74 ? 4   HIS   A N   1 
ATOM   12   C  CA  . HIS   A 1 4   ? 30.924 2.185   8.563   1.00 25.54 ? 4   HIS   A CA  1 
ATOM   13   C  C   . HIS   A 1 4   ? 30.303 1.078   9.397   1.00 20.14 ? 4   HIS   A C   1 
ATOM   14   O  O   . HIS   A 1 4   ? 30.542 -0.093  9.168   1.00 20.68 ? 4   HIS   A O   1 
ATOM   15   C  CB  . HIS   A 1 4   ? 29.949 2.620   7.460   1.00 29.79 ? 4   HIS   A CB  1 
ATOM   16   N  N   . TRP   A 1 5   ? 29.506 1.463   10.392  1.00 17.98 ? 5   TRP   A N   1 
ATOM   17   C  CA  . TRP   A 1 5   ? 28.864 0.498   11.276  1.00 15.19 ? 5   TRP   A CA  1 
ATOM   18   C  C   . TRP   A 1 5   ? 27.840 -0.320  10.494  1.00 15.65 ? 5   TRP   A C   1 
ATOM   19   O  O   . TRP   A 1 5   ? 27.315 0.132   9.478   1.00 17.23 ? 5   TRP   A O   1 
ATOM   20   C  CB  . TRP   A 1 5   ? 28.189 1.194   12.462  1.00 15.43 ? 5   TRP   A CB  1 
ATOM   21   C  CG  . TRP   A 1 5   ? 27.017 2.039   12.083  1.00 15.33 ? 5   TRP   A CG  1 
ATOM   22   C  CD1 . TRP   A 1 5   ? 27.002 3.362   11.788  1.00 17.45 ? 5   TRP   A CD1 1 
ATOM   23   C  CD2 . TRP   A 1 5   ? 25.645 1.598   11.981  1.00 14.63 ? 5   TRP   A CD2 1 
ATOM   24   N  NE1 . TRP   A 1 5   ? 25.733 3.782   11.497  1.00 17.46 ? 5   TRP   A NE1 1 
ATOM   25   C  CE2 . TRP   A 1 5   ? 24.873 2.729   11.646  1.00 15.43 ? 5   TRP   A CE2 1 
ATOM   26   C  CE3 . TRP   A 1 5   ? 24.995 0.380   12.240  1.00 14.38 ? 5   TRP   A CE3 1 
ATOM   27   C  CZ2 . TRP   A 1 5   ? 23.490 2.653   11.473  1.00 16.56 ? 5   TRP   A CZ2 1 
ATOM   28   C  CZ3 . TRP   A 1 5   ? 23.630 0.316   12.063  1.00 15.66 ? 5   TRP   A CZ3 1 
ATOM   29   C  CH2 . TRP   A 1 5   ? 22.893 1.441   11.709  1.00 16.02 ? 5   TRP   A CH2 1 
ATOM   30   N  N   . GLY   A 1 6   ? 27.603 -1.530  10.963  1.00 14.19 ? 6   GLY   A N   1 
ATOM   31   C  CA  . GLY   A 1 6   ? 26.608 -2.427  10.393  1.00 15.15 ? 6   GLY   A CA  1 
ATOM   32   C  C   . GLY   A 1 6   ? 26.297 -3.544  11.376  1.00 15.38 ? 6   GLY   A C   1 
ATOM   33   O  O   . GLY   A 1 6   ? 26.267 -3.319  12.585  1.00 14.71 ? 6   GLY   A O   1 
ATOM   34   N  N   . TYR   A 1 7   ? 26.053 -4.735  10.818  1.00 15.57 ? 7   TYR   A N   1 
ATOM   35   C  CA  . TYR   A 1 7   ? 25.663 -5.892  11.595  1.00 16.55 ? 7   TYR   A CA  1 
ATOM   36   C  C   . TYR   A 1 7   ? 26.557 -7.091  11.303  1.00 19.09 ? 7   TYR   A C   1 
ATOM   37   O  O   . TYR   A 1 7   ? 26.251 -8.186  11.725  1.00 25.02 ? 7   TYR   A O   1 
ATOM   38   C  CB  . TYR   A 1 7   ? 24.180 -6.216  11.354  1.00 15.75 ? 7   TYR   A CB  1 
ATOM   39   C  CG  . TYR   A 1 7   ? 23.243 -5.144  11.867  1.00 13.97 ? 7   TYR   A CG  1 
ATOM   40   C  CD1 . TYR   A 1 7   ? 22.852 -5.123  13.201  1.00 12.62 ? 7   TYR   A CD1 1 
ATOM   41   C  CD2 . TYR   A 1 7   ? 22.836 -4.104  11.052  1.00 13.22 ? 7   TYR   A CD2 1 
ATOM   42   C  CE1 . TYR   A 1 7   ? 21.997 -4.144  13.678  1.00 12.53 ? 7   TYR   A CE1 1 
ATOM   43   C  CE2 . TYR   A 1 7   ? 21.987 -3.118  11.504  1.00 12.97 ? 7   TYR   A CE2 1 
ATOM   44   C  CZ  . TYR   A 1 7   ? 21.557 -3.146  12.822  1.00 12.27 ? 7   TYR   A CZ  1 
ATOM   45   O  OH  . TYR   A 1 7   ? 20.725 -2.165  13.243  1.00 13.39 ? 7   TYR   A OH  1 
ATOM   46   N  N   . GLY   A 1 8   ? 27.671 -6.887  10.627  1.00 20.66 ? 8   GLY   A N   1 
ATOM   47   C  CA  . GLY   A 1 8   ? 28.572 -7.986  10.308  1.00 23.35 ? 8   GLY   A CA  1 
ATOM   48   C  C   . GLY   A 1 8   ? 29.536 -8.274  11.456  1.00 23.90 ? 8   GLY   A C   1 
ATOM   49   O  O   . GLY   A 1 8   ? 29.607 -7.554  12.445  1.00 23.31 ? 8   GLY   A O   1 
ATOM   50   N  N   . LYS   A 1 9   ? 30.350 -9.306  11.270  1.00 23.84 ? 9   LYS   A N   1 
ATOM   51   C  CA  . LYS   A 1 9   ? 31.363 -9.717  12.243  1.00 25.09 ? 9   LYS   A CA  1 
ATOM   52   C  C   . LYS   A 1 9   ? 32.323 -8.567  12.558  1.00 24.24 ? 9   LYS   A C   1 
ATOM   53   O  O   . LYS   A 1 9   ? 32.710 -8.351  13.704  1.00 23.84 ? 9   LYS   A O   1 
ATOM   54   C  CB  . LYS   A 1 9   ? 32.121 -10.916 11.675  1.00 26.84 ? 9   LYS   A CB  1 
ATOM   55   N  N   . HIS   A 1 10  ? 32.671 -7.780  11.553  1.00 22.60 ? 10  HIS   A N   1 
ATOM   56   C  CA  . HIS   A 1 10  ? 33.735 -6.803  11.734  1.00 23.17 ? 10  HIS   A CA  1 
ATOM   57   C  C   . HIS   A 1 10  ? 33.204 -5.403  12.006  1.00 20.91 ? 10  HIS   A C   1 
ATOM   58   O  O   . HIS   A 1 10  ? 33.998 -4.525  12.344  1.00 23.25 ? 10  HIS   A O   1 
ATOM   59   C  CB  . HIS   A 1 10  ? 34.734 -6.851  10.572  1.00 25.12 ? 10  HIS   A CB  1 
ATOM   60   C  CG  . HIS   A 1 10  ? 35.422 -8.173  10.565  1.00 25.69 ? 10  HIS   A CG  1 
ATOM   61   N  ND1 . HIS   A 1 10  ? 36.411 -8.567  11.446  1.00 26.76 ? 10  HIS   A ND1 1 
ATOM   62   C  CD2 . HIS   A 1 10  ? 35.182 -9.202  9.765   1.00 27.22 ? 10  HIS   A CD2 1 
ATOM   63   C  CE1 . HIS   A 1 10  ? 36.737 -9.806  11.167  1.00 27.24 ? 10  HIS   A CE1 1 
ATOM   64   N  NE2 . HIS   A 1 10  ? 36.011 -10.206 10.127  1.00 26.07 ? 10  HIS   A NE2 1 
ATOM   65   N  N   . ASN   A 1 11  ? 31.884 -5.184  11.880  1.00 19.01 ? 11  ASN   A N   1 
ATOM   66   C  CA  . ASN   A 1 11  ? 31.331 -3.848  12.075  1.00 17.92 ? 11  ASN   A CA  1 
ATOM   67   C  C   . ASN   A 1 11  ? 30.037 -3.818  12.908  1.00 16.04 ? 11  ASN   A C   1 
ATOM   68   O  O   . ASN   A 1 11  ? 29.355 -2.798  12.941  1.00 16.03 ? 11  ASN   A O   1 
ATOM   69   C  CB  . ASN   A 1 11  ? 31.142 -3.116  10.743  1.00 19.12 ? 11  ASN   A CB  1 
ATOM   70   C  CG  . ASN   A 1 11  ? 30.071 -3.745  9.874   1.00 20.06 ? 11  ASN   A CG  1 
ATOM   71   O  OD1 . ASN   A 1 11  ? 29.537 -4.793  10.186  1.00 20.00 ? 11  ASN   A OD1 1 
ATOM   72   N  ND2 . ASN   A 1 11  ? 29.713 -3.082  8.785   1.00 23.07 ? 11  ASN   A ND2 1 
ATOM   73   N  N   . GLY   A 1 12  ? 29.698 -4.935  13.514  1.00 16.57 ? 12  GLY   A N   1 
ATOM   74   C  CA  . GLY   A 1 12  ? 28.430 -5.120  14.177  1.00 16.14 ? 12  GLY   A CA  1 
ATOM   75   C  C   . GLY   A 1 12  ? 28.416 -4.560  15.586  1.00 14.12 ? 12  GLY   A C   1 
ATOM   76   O  O   . GLY   A 1 12  ? 29.327 -3.836  16.017  1.00 14.42 ? 12  GLY   A O   1 
ATOM   77   N  N   . PRO   A 1 13  ? 27.330 -4.842  16.311  1.00 13.62 ? 13  PRO   A N   1 
ATOM   78   C  CA  . PRO   A 1 13  ? 27.097 -4.298  17.644  1.00 13.69 ? 13  PRO   A CA  1 
ATOM   79   C  C   . PRO   A 1 13  ? 28.255 -4.290  18.621  1.00 14.05 ? 13  PRO   A C   1 
ATOM   80   O  O   . PRO   A 1 13  ? 28.357 -3.339  19.386  1.00 13.77 ? 13  PRO   A O   1 
ATOM   81   C  CB  . PRO   A 1 13  ? 25.915 -5.152  18.144  1.00 14.37 ? 13  PRO   A CB  1 
ATOM   82   C  CG  . PRO   A 1 13  ? 25.087 -5.352  16.879  1.00 14.62 ? 13  PRO   A CG  1 
ATOM   83   C  CD  . PRO   A 1 13  ? 26.154 -5.590  15.828  1.00 14.47 ? 13  PRO   A CD  1 
ATOM   84   N  N   . GLU   A 1 14  ? 29.111 -5.317  18.598  1.00 14.56 ? 14  GLU   A N   1 
ATOM   85   C  CA  . GLU   A 1 14  ? 30.235 -5.358  19.538  1.00 15.96 ? 14  GLU   A CA  1 
ATOM   86   C  C   . GLU   A 1 14  ? 31.344 -4.359  19.182  1.00 15.08 ? 14  GLU   A C   1 
ATOM   87   O  O   . GLU   A 1 14  ? 32.237 -4.144  20.013  1.00 16.71 ? 14  GLU   A O   1 
ATOM   88   C  CB  . GLU   A 1 14  ? 30.821 -6.764  19.623  1.00 19.71 ? 14  GLU   A CB  1 
ATOM   89   C  CG  . GLU   A 1 14  ? 29.773 -7.809  20.018  1.00 23.99 ? 14  GLU   A CG  1 
ATOM   90   C  CD  . GLU   A 1 14  ? 28.912 -7.444  21.217  1.00 31.30 ? 14  GLU   A CD  1 
ATOM   91   O  OE1 . GLU   A 1 14  ? 29.517 -7.026  22.238  1.00 36.65 ? 14  GLU   A OE1 1 
ATOM   92   O  OE2 . GLU   A 1 14  ? 27.617 -7.537  21.111  1.00 35.61 ? 14  GLU   A OE2 1 
ATOM   93   N  N   . HIS   A 1 15  ? 31.282 -3.768  17.981  1.00 14.32 ? 15  HIS   A N   1 
ATOM   94   C  CA  . HIS   A 1 15  ? 32.251 -2.785  17.539  1.00 14.21 ? 15  HIS   A CA  1 
ATOM   95   C  C   . HIS   A 1 15  ? 31.777 -1.354  17.727  1.00 13.40 ? 15  HIS   A C   1 
ATOM   96   O  O   . HIS   A 1 15  ? 32.601 -0.440  17.634  1.00 13.63 ? 15  HIS   A O   1 
ATOM   97   C  CB  . HIS   A 1 15  ? 32.589 -2.970  16.066  1.00 14.60 ? 15  HIS   A CB  1 
ATOM   98   C  CG  . HIS   A 1 15  ? 33.335 -4.203  15.766  1.00 16.50 ? 15  HIS   A CG  1 
ATOM   99   N  ND1 . HIS   A 1 15  ? 34.729 -4.244  15.801  1.00 17.86 ? 15  HIS   A ND1 1 
ATOM   100  C  CD2 . HIS   A 1 15  ? 32.905 -5.413  15.411  1.00 18.34 ? 15  HIS   A CD2 1 
ATOM   101  C  CE1 . HIS   A 1 15  ? 35.119 -5.442  15.438  1.00 21.23 ? 15  HIS   A CE1 1 
ATOM   102  N  NE2 . HIS   A 1 15  ? 34.035 -6.208  15.248  1.00 20.85 ? 15  HIS   A NE2 1 
ATOM   103  N  N   . TRP   A 1 16  ? 30.456 -1.137  17.905  1.00 12.80 ? 16  TRP   A N   1 
ATOM   104  C  CA  . TRP   A 1 16  ? 29.923 0.211   17.796  1.00 12.40 ? 16  TRP   A CA  1 
ATOM   105  C  C   . TRP   A 1 16  ? 30.511 1.186   18.811  1.00 12.61 ? 16  TRP   A C   1 
ATOM   106  O  O   . TRP   A 1 16  ? 30.604 2.365   18.515  1.00 12.91 ? 16  TRP   A O   1 
ATOM   107  C  CB  . TRP   A 1 16  ? 28.396 0.185   17.908  1.00 12.02 ? 16  TRP   A CB  1 
ATOM   108  C  CG  . TRP   A 1 16  ? 27.704 -0.539  16.793  1.00 12.17 ? 16  TRP   A CG  1 
ATOM   109  C  CD1 . TRP   A 1 16  ? 28.188 -0.989  15.615  1.00 12.70 ? 16  TRP   A CD1 1 
ATOM   110  C  CD2 . TRP   A 1 16  ? 26.291 -0.854  16.768  1.00 11.79 ? 16  TRP   A CD2 1 
ATOM   111  N  NE1 . TRP   A 1 16  ? 27.215 -1.576  14.863  1.00 13.24 ? 16  TRP   A NE1 1 
ATOM   112  C  CE2 . TRP   A 1 16  ? 26.034 -1.498  15.551  1.00 11.83 ? 16  TRP   A CE2 1 
ATOM   113  C  CE3 . TRP   A 1 16  ? 25.237 -0.640  17.660  1.00 12.04 ? 16  TRP   A CE3 1 
ATOM   114  C  CZ2 . TRP   A 1 16  ? 24.755 -1.959  15.205  1.00 11.87 ? 16  TRP   A CZ2 1 
ATOM   115  C  CZ3 . TRP   A 1 16  ? 23.980 -1.095  17.315  1.00 12.40 ? 16  TRP   A CZ3 1 
ATOM   116  C  CH2 . TRP   A 1 16  ? 23.734 -1.704  16.090  1.00 12.10 ? 16  TRP   A CH2 1 
ATOM   117  N  N   . HIS   A 1 17  ? 30.863 0.669   20.008  1.00 12.51 ? 17  HIS   A N   1 
ATOM   118  C  CA  . HIS   A 1 17  ? 31.336 1.548   21.067  1.00 13.11 ? 17  HIS   A CA  1 
ATOM   119  C  C   . HIS   A 1 17  ? 32.574 2.329   20.634  1.00 13.32 ? 17  HIS   A C   1 
ATOM   120  O  O   . HIS   A 1 17  ? 32.859 3.357   21.233  1.00 14.07 ? 17  HIS   A O   1 
ATOM   121  C  CB  . HIS   A 1 17  ? 31.631 0.775   22.364  1.00 13.78 ? 17  HIS   A CB  1 
ATOM   122  C  CG  . HIS   A 1 17  ? 32.834 -0.106  22.236  1.00 14.25 ? 17  HIS   A CG  1 
ATOM   123  N  ND1 . HIS   A 1 17  ? 34.062 0.288   22.737  1.00 16.23 ? 17  HIS   A ND1 1 
ATOM   124  C  CD2 . HIS   A 1 17  ? 33.018 -1.301  21.671  1.00 15.23 ? 17  HIS   A CD2 1 
ATOM   125  C  CE1 . HIS   A 1 17  ? 34.926 -0.658  22.416  1.00 16.05 ? 17  HIS   A CE1 1 
ATOM   126  N  NE2 . HIS   A 1 17  ? 34.340 -1.651  21.810  1.00 16.67 ? 17  HIS   A NE2 1 
ATOM   127  N  N   . LYS   A 1 18  ? 33.371 1.829   19.678  1.00 13.44 ? 18  LYS   A N   1 
ATOM   128  C  CA  . LYS   A 1 18  ? 34.581 2.536   19.284  1.00 14.72 ? 18  LYS   A CA  1 
ATOM   129  C  C   . LYS   A 1 18  ? 34.279 3.875   18.646  1.00 15.35 ? 18  LYS   A C   1 
ATOM   130  O  O   . LYS   A 1 18  ? 35.012 4.832   18.810  1.00 20.21 ? 18  LYS   A O   1 
ATOM   131  C  CB  . LYS   A 1 18  ? 35.465 1.662   18.378  1.00 15.04 ? 18  LYS   A CB  1 
ATOM   132  C  CG  . LYS   A 1 18  ? 36.034 0.439   19.084  1.00 15.40 ? 18  LYS   A CG  1 
ATOM   133  C  CD  . LYS   A 1 18  ? 36.764 -0.495  18.197  1.00 16.39 ? 18  LYS   A CD  1 
ATOM   134  C  CE  . LYS   A 1 18  ? 35.828 -1.446  17.498  1.00 16.15 ? 18  LYS   A CE  1 
ATOM   135  N  NZ  . LYS   A 1 18  ? 36.465 -2.228  16.456  1.00 16.96 ? 18  LYS   A NZ  1 
ATOM   136  N  N   A ASP   A 1 19  ? 33.215 3.962   17.868  0.50 14.61 ? 19  ASP   A N   1 
ATOM   137  N  N   B ASP   A 1 19  ? 33.236 3.948   17.830  0.50 15.30 ? 19  ASP   A N   1 
ATOM   138  C  CA  A ASP   A 1 19  ? 32.870 5.232   17.264  0.50 14.49 ? 19  ASP   A CA  1 
ATOM   139  C  CA  B ASP   A 1 19  ? 32.821 5.197   17.217  0.50 15.56 ? 19  ASP   A CA  1 
ATOM   140  C  C   A ASP   A 1 19  ? 31.703 5.907   17.958  0.50 14.53 ? 19  ASP   A C   1 
ATOM   141  C  C   B ASP   A 1 19  ? 31.811 5.937   18.091  0.50 15.36 ? 19  ASP   A C   1 
ATOM   142  O  O   A ASP   A 1 19  ? 31.430 7.045   17.607  0.50 14.59 ? 19  ASP   A O   1 
ATOM   143  O  O   B ASP   A 1 19  ? 31.762 7.162   18.058  0.50 15.79 ? 19  ASP   A O   1 
ATOM   144  C  CB  A ASP   A 1 19  ? 32.561 5.099   15.776  0.50 15.23 ? 19  ASP   A CB  1 
ATOM   145  C  CB  B ASP   A 1 19  ? 32.247 4.965   15.816  0.50 17.41 ? 19  ASP   A CB  1 
ATOM   146  C  CG  A ASP   A 1 19  ? 33.808 4.848   14.964  0.50 16.70 ? 19  ASP   A CG  1 
ATOM   147  C  CG  B ASP   A 1 19  ? 33.258 4.956   14.680  0.50 19.07 ? 19  ASP   A CG  1 
ATOM   148  O  OD1 A ASP   A 1 19  ? 34.534 5.842   14.679  0.50 17.93 ? 19  ASP   A OD1 1 
ATOM   149  O  OD1 B ASP   A 1 19  ? 34.420 5.335   14.921  0.50 21.08 ? 19  ASP   A OD1 1 
ATOM   150  O  OD2 A ASP   A 1 19  ? 34.101 3.669   14.748  0.50 18.11 ? 19  ASP   A OD2 1 
ATOM   151  O  OD2 B ASP   A 1 19  ? 32.869 4.556   13.562  0.50 23.82 ? 19  ASP   A OD2 1 
ATOM   152  N  N   . PHE   A 1 20  ? 31.004 5.184   18.850  1.00 13.58 ? 20  PHE   A N   1 
ATOM   153  C  CA  . PHE   A 1 20  ? 29.881 5.729   19.598  1.00 13.97 ? 20  PHE   A CA  1 
ATOM   154  C  C   . PHE   A 1 20  ? 29.991 5.237   21.041  1.00 14.10 ? 20  PHE   A C   1 
ATOM   155  O  O   . PHE   A 1 20  ? 29.357 4.238   21.431  1.00 13.39 ? 20  PHE   A O   1 
ATOM   156  C  CB  . PHE   A 1 20  ? 28.568 5.251   18.959  1.00 14.77 ? 20  PHE   A CB  1 
ATOM   157  C  CG  . PHE   A 1 20  ? 28.472 5.624   17.500  1.00 15.19 ? 20  PHE   A CG  1 
ATOM   158  C  CD1 . PHE   A 1 20  ? 28.099 6.908   17.102  1.00 17.40 ? 20  PHE   A CD1 1 
ATOM   159  C  CD2 . PHE   A 1 20  ? 28.891 4.710   16.542  1.00 16.15 ? 20  PHE   A CD2 1 
ATOM   160  C  CE1 . PHE   A 1 20  ? 28.153 7.250   15.762  1.00 17.94 ? 20  PHE   A CE1 1 
ATOM   161  C  CE2 . PHE   A 1 20  ? 28.884 5.049   15.198  1.00 17.88 ? 20  PHE   A CE2 1 
ATOM   162  C  CZ  . PHE   A 1 20  ? 28.543 6.315   14.832  1.00 18.37 ? 20  PHE   A CZ  1 
ATOM   163  N  N   . PRO   A 1 21  ? 30.863 5.872   21.863  1.00 15.05 ? 21  PRO   A N   1 
ATOM   164  C  CA  . PRO   A 1 21  ? 31.122 5.365   23.207  1.00 16.05 ? 21  PRO   A CA  1 
ATOM   165  C  C   . PRO   A 1 21  ? 29.914 5.215   24.132  1.00 14.31 ? 21  PRO   A C   1 
ATOM   166  O  O   . PRO   A 1 21  ? 29.967 4.442   25.078  1.00 15.82 ? 21  PRO   A O   1 
ATOM   167  C  CB  . PRO   A 1 21  ? 32.159 6.307   23.809  1.00 18.08 ? 21  PRO   A CB  1 
ATOM   168  C  CG  . PRO   A 1 21  ? 32.419 7.331   22.763  1.00 21.38 ? 21  PRO   A CG  1 
ATOM   169  C  CD  . PRO   A 1 21  ? 31.751 6.954   21.469  1.00 17.12 ? 21  PRO   A CD  1 
ATOM   170  N  N   A ILE   A 1 22  ? 28.819 5.947   23.865  0.50 13.83 ? 22  ILE   A N   1 
ATOM   171  N  N   B ILE   A 1 22  ? 28.850 5.963   23.821  0.50 13.52 ? 22  ILE   A N   1 
ATOM   172  C  CA  A ILE   A 1 22  ? 27.598 5.789   24.658  0.50 13.41 ? 22  ILE   A CA  1 
ATOM   173  C  CA  B ILE   A 1 22  ? 27.605 5.851   24.565  0.50 13.32 ? 22  ILE   A CA  1 
ATOM   174  C  C   A ILE   A 1 22  ? 27.013 4.385   24.496  0.50 13.00 ? 22  ILE   A C   1 
ATOM   175  C  C   B ILE   A 1 22  ? 26.978 4.463   24.414  0.50 12.62 ? 22  ILE   A C   1 
ATOM   176  O  O   A ILE   A 1 22  ? 26.195 3.973   25.305  0.50 13.09 ? 22  ILE   A O   1 
ATOM   177  O  O   B ILE   A 1 22  ? 26.071 4.161   25.163  0.50 13.11 ? 22  ILE   A O   1 
ATOM   178  C  CB  A ILE   A 1 22  ? 26.557 6.851   24.278  0.50 13.45 ? 22  ILE   A CB  1 
ATOM   179  C  CB  B ILE   A 1 22  ? 26.638 6.954   24.121  0.50 13.59 ? 22  ILE   A CB  1 
ATOM   180  C  CG1 A ILE   A 1 22  ? 25.545 7.143   25.385  0.50 13.85 ? 22  ILE   A CG1 1 
ATOM   181  C  CG1 B ILE   A 1 22  ? 25.568 7.210   25.179  0.50 15.07 ? 22  ILE   A CG1 1 
ATOM   182  C  CG2 A ILE   A 1 22  ? 25.850 6.429   23.007  0.50 13.61 ? 22  ILE   A CG2 1 
ATOM   183  C  CG2 B ILE   A 1 22  ? 26.049 6.626   22.760  0.50 13.56 ? 22  ILE   A CG2 1 
ATOM   184  C  CD1 A ILE   A 1 22  ? 24.630 8.314   25.044  0.50 14.25 ? 22  ILE   A CD1 1 
ATOM   185  C  CD1 B ILE   A 1 22  ? 26.135 7.719   26.501  0.50 16.68 ? 22  ILE   A CD1 1 
ATOM   186  N  N   . ALA   A 1 23  ? 27.524 3.597   23.553  1.00 12.78 ? 23  ALA   A N   1 
ATOM   187  C  CA  . ALA   A 1 23  ? 27.092 2.215   23.433  1.00 12.60 ? 23  ALA   A CA  1 
ATOM   188  C  C   . ALA   A 1 23  ? 27.250 1.461   24.751  1.00 12.84 ? 23  ALA   A C   1 
ATOM   189  O  O   . ALA   A 1 23  ? 26.521 0.483   24.931  1.00 14.40 ? 23  ALA   A O   1 
ATOM   190  C  CB  . ALA   A 1 23  ? 27.925 1.530   22.370  1.00 13.14 ? 23  ALA   A CB  1 
ATOM   191  N  N   . LYS   A 1 24  ? 28.169 1.916   25.641  1.00 13.78 ? 24  LYS   A N   1 
ATOM   192  C  CA  . LYS   A 1 24  ? 28.355 1.279   26.935  1.00 15.45 ? 24  LYS   A CA  1 
ATOM   193  C  C   . LYS   A 1 24  ? 27.708 2.096   28.038  1.00 15.58 ? 24  LYS   A C   1 
ATOM   194  O  O   . LYS   A 1 24  ? 28.119 2.010   29.208  1.00 18.46 ? 24  LYS   A O   1 
ATOM   195  C  CB  . LYS   A 1 24  ? 29.837 1.070   27.219  1.00 18.22 ? 24  LYS   A CB  1 
ATOM   196  C  CG  . LYS   A 1 24  ? 30.477 0.067   26.304  1.00 19.54 ? 24  LYS   A CG  1 
ATOM   197  C  CD  . LYS   A 1 24  ? 31.902 -0.124  26.716  1.00 22.90 ? 24  LYS   A CD  1 
ATOM   198  C  CE  . LYS   A 1 24  ? 32.658 -1.000  25.759  1.00 24.95 ? 24  LYS   A CE  1 
ATOM   199  N  NZ  . LYS   A 1 24  ? 32.113 -2.368  25.789  1.00 28.99 ? 24  LYS   A NZ  1 
ATOM   200  N  N   . GLY   A 1 25  ? 26.732 2.935   27.692  1.00 15.47 ? 25  GLY   A N   1 
ATOM   201  C  CA  . GLY   A 1 25  ? 26.085 3.872   28.605  1.00 15.97 ? 25  GLY   A CA  1 
ATOM   202  C  C   . GLY   A 1 25  ? 25.141 3.214   29.599  1.00 15.05 ? 25  GLY   A C   1 
ATOM   203  O  O   . GLY   A 1 25  ? 24.954 1.992   29.626  1.00 16.67 ? 25  GLY   A O   1 
ATOM   204  N  N   . GLU   A 1 26  ? 24.489 4.095   30.369  1.00 16.18 ? 26  GLU   A N   1 
ATOM   205  C  CA  . GLU   A 1 26  ? 23.613 3.689   31.437  1.00 16.03 ? 26  GLU   A CA  1 
ATOM   206  C  C   . GLU   A 1 26  ? 22.167 3.492   31.020  1.00 14.91 ? 26  GLU   A C   1 
ATOM   207  O  O   . GLU   A 1 26  ? 21.365 3.033   31.825  1.00 15.77 ? 26  GLU   A O   1 
ATOM   208  C  CB  . GLU   A 1 26  ? 23.682 4.724   32.560  1.00 20.01 ? 26  GLU   A CB  1 
ATOM   209  C  CG  . GLU   A 1 26  ? 25.053 4.929   33.130  1.00 23.13 ? 26  GLU   A CG  1 
ATOM   210  C  CD  . GLU   A 1 26  ? 25.630 3.654   33.704  1.00 29.84 ? 26  GLU   A CD  1 
ATOM   211  O  OE1 . GLU   A 1 26  ? 24.996 3.088   34.601  1.00 34.85 ? 26  GLU   A OE1 1 
ATOM   212  O  OE2 . GLU   A 1 26  ? 26.712 3.254   33.256  1.00 37.26 ? 26  GLU   A OE2 1 
ATOM   213  N  N   A ARG   A 1 27  ? 21.874 3.788   29.757  0.50 12.47 ? 27  ARG   A N   1 
ATOM   214  N  N   B ARG   A 1 27  ? 21.757 3.936   29.825  0.50 12.46 ? 27  ARG   A N   1 
ATOM   215  C  CA  A ARG   A 1 27  ? 20.479 3.831   29.335  0.50 12.14 ? 27  ARG   A CA  1 
ATOM   216  C  CA  B ARG   A 1 27  ? 20.356 3.710   29.432  0.50 12.00 ? 27  ARG   A CA  1 
ATOM   217  C  C   A ARG   A 1 27  ? 20.360 3.318   27.907  0.50 11.17 ? 27  ARG   A C   1 
ATOM   218  C  C   B ARG   A 1 27  ? 20.291 3.266   27.970  0.50 10.96 ? 27  ARG   A C   1 
ATOM   219  O  O   A ARG   A 1 27  ? 19.703 3.930   27.062  0.50 11.66 ? 27  ARG   A O   1 
ATOM   220  O  O   B ARG   A 1 27  ? 19.536 3.827   27.177  0.50 11.96 ? 27  ARG   A O   1 
ATOM   221  C  CB  A ARG   A 1 27  ? 20.001 5.270   29.510  0.50 13.51 ? 27  ARG   A CB  1 
ATOM   222  C  CB  B ARG   A 1 27  ? 19.418 4.891   29.763  0.50 12.56 ? 27  ARG   A CB  1 
ATOM   223  C  CG  A ARG   A 1 27  ? 18.571 5.516   29.075  0.50 14.45 ? 27  ARG   A CG  1 
ATOM   224  C  CG  B ARG   A 1 27  ? 19.797 6.239   29.150  0.50 14.97 ? 27  ARG   A CG  1 
ATOM   225  C  CD  A ARG   A 1 27  ? 18.061 6.903   29.379  0.50 13.97 ? 27  ARG   A CD  1 
ATOM   226  C  CD  B ARG   A 1 27  ? 18.890 7.462   29.367  0.50 16.92 ? 27  ARG   A CD  1 
ATOM   227  N  NE  A ARG   A 1 27  ? 17.032 7.297   28.423  0.50 14.29 ? 27  ARG   A NE  1 
ATOM   228  N  NE  B ARG   A 1 27  ? 17.755 7.427   28.479  0.50 15.91 ? 27  ARG   A NE  1 
ATOM   229  C  CZ  A ARG   A 1 27  ? 16.361 8.435   28.496  0.50 14.09 ? 27  ARG   A CZ  1 
ATOM   230  C  CZ  B ARG   A 1 27  ? 16.834 8.376   28.327  0.50 13.80 ? 27  ARG   A CZ  1 
ATOM   231  N  NH1 A ARG   A 1 27  ? 15.426 8.735   27.618  0.50 15.39 ? 27  ARG   A NH1 1 
ATOM   232  N  NH1 B ARG   A 1 27  ? 15.872 8.106   27.492  0.50 13.76 ? 27  ARG   A NH1 1 
ATOM   233  N  NH2 A ARG   A 1 27  ? 16.651 9.310   29.441  0.50 16.10 ? 27  ARG   A NH2 1 
ATOM   234  N  NH2 B ARG   A 1 27  ? 16.887 9.567   28.914  0.50 13.72 ? 27  ARG   A NH2 1 
ATOM   235  N  N   . GLN   A 1 28  ? 21.008 2.186   27.639  1.00 10.67 ? 28  GLN   A N   1 
ATOM   236  C  CA  . GLN   A 1 28  ? 21.031 1.647   26.284  1.00 10.14 ? 28  GLN   A CA  1 
ATOM   237  C  C   . GLN   A 1 28  ? 19.852 0.686   26.042  1.00 9.69  ? 28  GLN   A C   1 
ATOM   238  O  O   . GLN   A 1 28  ? 19.344 0.034   26.939  1.00 10.80 ? 28  GLN   A O   1 
ATOM   239  C  CB  . GLN   A 1 28  ? 22.373 0.938   26.037  1.00 10.87 ? 28  GLN   A CB  1 
ATOM   240  C  CG  . GLN   A 1 28  ? 23.511 1.954   25.926  1.00 11.27 ? 28  GLN   A CG  1 
ATOM   241  C  CD  . GLN   A 1 28  ? 23.407 2.760   24.640  1.00 11.38 ? 28  GLN   A CD  1 
ATOM   242  O  OE1 . GLN   A 1 28  ? 23.576 2.213   23.538  1.00 11.22 ? 28  GLN   A OE1 1 
ATOM   243  N  NE2 . GLN   A 1 28  ? 23.079 4.045   24.759  1.00 11.03 ? 28  GLN   A NE2 1 
ATOM   244  N  N   . SER   A 1 29  ? 19.493 0.608   24.742  1.00 10.27 ? 29  SER   A N   1 
ATOM   245  C  CA  . SER   A 1 29  ? 18.401 -0.242  24.278  1.00 9.31  ? 29  SER   A CA  1 
ATOM   246  C  C   . SER   A 1 29  ? 18.933 -1.115  23.166  1.00 10.18 ? 29  SER   A C   1 
ATOM   247  O  O   . SER   A 1 29  ? 19.878 -0.737  22.458  1.00 10.65 ? 29  SER   A O   1 
ATOM   248  C  CB  . SER   A 1 29  ? 17.266 0.637   23.779  1.00 9.68  ? 29  SER   A CB  1 
ATOM   249  O  OG  . SER   A 1 29  ? 16.655 1.350   24.828  1.00 9.59  ? 29  SER   A OG  1 
ATOM   250  N  N   . PRO   A 1 30  ? 18.272 -2.235  22.862  1.00 9.50  ? 30  PRO   A N   1 
ATOM   251  C  CA  . PRO   A 1 30  ? 17.124 -2.779  23.584  1.00 9.47  ? 30  PRO   A CA  1 
ATOM   252  C  C   . PRO   A 1 30  ? 17.539 -3.449  24.888  1.00 9.87  ? 30  PRO   A C   1 
ATOM   253  O  O   . PRO   A 1 30  ? 18.715 -3.487  25.257  1.00 10.81 ? 30  PRO   A O   1 
ATOM   254  C  CB  . PRO   A 1 30  ? 16.598 -3.809  22.604  1.00 9.91  ? 30  PRO   A CB  1 
ATOM   255  C  CG  . PRO   A 1 30  ? 17.883 -4.426  21.998  1.00 9.58  ? 30  PRO   A CG  1 
ATOM   256  C  CD  . PRO   A 1 30  ? 18.724 -3.181  21.823  1.00 10.06 ? 30  PRO   A CD  1 
ATOM   257  N  N   . VAL   A 1 31  ? 16.576 -4.010  25.625  1.00 9.96  ? 31  VAL   A N   1 
ATOM   258  C  CA  . VAL   A 1 31  ? 16.737 -4.745  26.868  1.00 9.81  ? 31  VAL   A CA  1 
ATOM   259  C  C   . VAL   A 1 31  ? 15.831 -5.963  26.821  1.00 11.19 ? 31  VAL   A C   1 
ATOM   260  O  O   . VAL   A 1 31  ? 14.876 -6.041  26.044  1.00 11.41 ? 31  VAL   A O   1 
ATOM   261  C  CB  . VAL   A 1 31  ? 16.419 -3.876  28.099  1.00 11.07 ? 31  VAL   A CB  1 
ATOM   262  C  CG1 . VAL   A 1 31  ? 17.351 -2.689  28.181  1.00 11.93 ? 31  VAL   A CG1 1 
ATOM   263  C  CG2 . VAL   A 1 31  ? 14.971 -3.448  28.128  1.00 11.24 ? 31  VAL   A CG2 1 
ATOM   264  N  N   . ASP   A 1 32  ? 16.195 -6.919  27.655  1.00 10.56 ? 32  ASP   A N   1 
ATOM   265  C  CA  . ASP   A 1 32  ? 15.292 -7.997  27.985  1.00 10.17 ? 32  ASP   A CA  1 
ATOM   266  C  C   . ASP   A 1 32  ? 14.254 -7.475  28.972  1.00 10.59 ? 32  ASP   A C   1 
ATOM   267  O  O   . ASP   A 1 32  ? 14.577 -6.831  29.960  1.00 12.92 ? 32  ASP   A O   1 
ATOM   268  C  CB  . ASP   A 1 32  ? 16.048 -9.187  28.565  1.00 11.10 ? 32  ASP   A CB  1 
ATOM   269  C  CG  . ASP   A 1 32  ? 15.101 -10.332 28.902  1.00 11.78 ? 32  ASP   A CG  1 
ATOM   270  O  OD1 . ASP   A 1 32  ? 14.397 -10.794 27.981  1.00 12.03 ? 32  ASP   A OD1 1 
ATOM   271  O  OD2 . ASP   A 1 32  ? 15.077 -10.779 30.090  1.00 15.04 ? 32  ASP   A OD2 1 
ATOM   272  N  N   . ILE   A 1 33  ? 12.977 -7.787  28.676  1.00 11.43 ? 33  ILE   A N   1 
ATOM   273  C  CA  . ILE   A 1 33  ? 11.879 -7.417  29.539  1.00 12.14 ? 33  ILE   A CA  1 
ATOM   274  C  C   . ILE   A 1 33  ? 11.569 -8.640  30.390  1.00 12.55 ? 33  ILE   A C   1 
ATOM   275  O  O   . ILE   A 1 33  ? 11.022 -9.642  29.935  1.00 13.58 ? 33  ILE   A O   1 
ATOM   276  C  CB  . ILE   A 1 33  ? 10.653 -6.975  28.719  1.00 12.80 ? 33  ILE   A CB  1 
ATOM   277  C  CG1 . ILE   A 1 33  ? 11.015 -5.776  27.850  1.00 12.77 ? 33  ILE   A CG1 1 
ATOM   278  C  CG2 . ILE   A 1 33  ? 9.472  -6.694  29.664  1.00 13.86 ? 33  ILE   A CG2 1 
ATOM   279  C  CD1 . ILE   A 1 33  ? 10.000 -5.436  26.801  1.00 13.25 ? 33  ILE   A CD1 1 
ATOM   280  N  N   A ASP   A 1 34  ? 11.956 -8.545  31.660  0.50 13.63 ? 34  ASP   A N   1 
ATOM   281  N  N   B ASP   A 1 34  ? 11.978 -8.570  31.648  0.50 13.69 ? 34  ASP   A N   1 
ATOM   282  C  CA  A ASP   A 1 34  ? 11.667 -9.567  32.656  0.50 14.63 ? 34  ASP   A CA  1 
ATOM   283  C  CA  B ASP   A 1 34  ? 11.681 -9.632  32.592  0.50 14.79 ? 34  ASP   A CA  1 
ATOM   284  C  C   A ASP   A 1 34  ? 10.265 -9.276  33.161  0.50 15.31 ? 34  ASP   A C   1 
ATOM   285  C  C   B ASP   A 1 34  ? 10.306 -9.315  33.157  0.50 15.25 ? 34  ASP   A C   1 
ATOM   286  O  O   A ASP   A 1 34  ? 10.049 -8.309  33.897  0.50 16.76 ? 34  ASP   A O   1 
ATOM   287  O  O   B ASP   A 1 34  ? 10.159 -8.375  33.941  0.50 15.92 ? 34  ASP   A O   1 
ATOM   288  C  CB  A ASP   A 1 34  ? 12.697 -9.554  33.799  0.50 15.74 ? 34  ASP   A CB  1 
ATOM   289  C  CB  B ASP   A 1 34  ? 12.756 -9.742  33.684  0.50 16.43 ? 34  ASP   A CB  1 
ATOM   290  C  CG  A ASP   A 1 34  ? 12.422 -10.522 34.938  0.50 17.03 ? 34  ASP   A CG  1 
ATOM   291  C  CG  B ASP   A 1 34  ? 12.605 -10.985 34.535  0.50 17.86 ? 34  ASP   A CG  1 
ATOM   292  O  OD1 A ASP   A 1 34  ? 11.264 -10.958 35.102  0.50 17.58 ? 34  ASP   A OD1 1 
ATOM   293  O  OD1 B ASP   A 1 34  ? 13.026 -12.072 34.075  0.50 19.76 ? 34  ASP   A OD1 1 
ATOM   294  O  OD2 A ASP   A 1 34  ? 13.374 -10.850 35.681  0.50 20.18 ? 34  ASP   A OD2 1 
ATOM   295  O  OD2 B ASP   A 1 34  ? 12.055 -10.859 35.646  0.50 21.43 ? 34  ASP   A OD2 1 
ATOM   296  N  N   . THR   A 1 35  ? 9.319  -10.112 32.747  1.00 15.73 ? 35  THR   A N   1 
ATOM   297  C  CA  . THR   A 1 35  ? 7.924  -9.783  32.979  1.00 16.58 ? 35  THR   A CA  1 
ATOM   298  C  C   . THR   A 1 35  ? 7.563  -9.871  34.444  1.00 17.94 ? 35  THR   A C   1 
ATOM   299  O  O   . THR   A 1 35  ? 6.643  -9.195  34.889  1.00 20.59 ? 35  THR   A O   1 
ATOM   300  C  CB  . THR   A 1 35  ? 6.996  -10.717 32.176  1.00 18.49 ? 35  THR   A CB  1 
ATOM   301  O  OG1 . THR   A 1 35  ? 7.106  -12.070 32.643  1.00 17.46 ? 35  THR   A OG1 1 
ATOM   302  C  CG2 . THR   A 1 35  ? 7.256  -10.579 30.690  1.00 18.79 ? 35  THR   A CG2 1 
ATOM   303  N  N   A HIS   A 1 36  ? 8.330  -10.658 35.223  0.50 18.98 ? 36  HIS   A N   1 
ATOM   304  N  N   B HIS   A 1 36  ? 8.309  -10.700 35.185  0.50 18.39 ? 36  HIS   A N   1 
ATOM   305  C  CA  A HIS   A 1 36  ? 8.076  -10.873 36.639  0.50 20.57 ? 36  HIS   A CA  1 
ATOM   306  C  CA  B HIS   A 1 36  ? 8.117  -10.862 36.608  0.50 19.22 ? 36  HIS   A CA  1 
ATOM   307  C  C   A HIS   A 1 36  ? 8.858  -9.882  37.528  0.50 24.10 ? 36  HIS   A C   1 
ATOM   308  C  C   B HIS   A 1 36  ? 8.530  -9.607  37.374  0.50 18.91 ? 36  HIS   A C   1 
ATOM   309  O  O   A HIS   A 1 36  ? 8.770  -9.915  38.744  0.50 28.62 ? 36  HIS   A O   1 
ATOM   310  O  O   B HIS   A 1 36  ? 7.842  -9.295  38.361  0.50 16.82 ? 36  HIS   A O   1 
ATOM   311  C  CB  A HIS   A 1 36  ? 8.358  -12.341 36.997  0.50 19.59 ? 36  HIS   A CB  1 
ATOM   312  C  CB  B HIS   A 1 36  ? 8.880  -12.097 37.085  0.50 19.65 ? 36  HIS   A CB  1 
ATOM   313  C  CG  A HIS   A 1 36  ? 7.362  -13.353 36.498  0.50 19.99 ? 36  HIS   A CG  1 
ATOM   314  C  CG  B HIS   A 1 36  ? 8.335  -13.272 36.362  0.50 20.17 ? 36  HIS   A CG  1 
ATOM   315  N  ND1 A HIS   A 1 36  ? 7.624  -14.307 35.525  0.50 20.43 ? 36  HIS   A ND1 1 
ATOM   316  N  ND1 B HIS   A 1 36  ? 8.864  -13.896 35.251  0.50 20.26 ? 36  HIS   A ND1 1 
ATOM   317  C  CD2 A HIS   A 1 36  ? 6.082  -13.539 36.867  0.50 20.87 ? 36  HIS   A CD2 1 
ATOM   318  C  CD2 B HIS   A 1 36  ? 7.174  -13.878 36.628  0.50 20.61 ? 36  HIS   A CD2 1 
ATOM   319  C  CE1 A HIS   A 1 36  ? 6.532  -15.052 35.343  0.50 21.89 ? 36  HIS   A CE1 1 
ATOM   320  C  CE1 B HIS   A 1 36  ? 8.066  -14.889 34.904  0.50 19.75 ? 36  HIS   A CE1 1 
ATOM   321  N  NE2 A HIS   A 1 36  ? 5.596  -14.608 36.153  0.50 22.93 ? 36  HIS   A NE2 1 
ATOM   322  N  NE2 B HIS   A 1 36  ? 7.019  -14.883 35.708  0.50 22.38 ? 36  HIS   A NE2 1 
ATOM   323  N  N   . THR   A 1 37  ? 9.664  -9.006  36.950  1.00 21.86 ? 37  THR   A N   1 
ATOM   324  C  CA  . THR   A 1 37  ? 10.296 -7.882  37.629  1.00 23.81 ? 37  THR   A CA  1 
ATOM   325  C  C   . THR   A 1 37  ? 9.658  -6.548  37.225  1.00 19.86 ? 37  THR   A C   1 
ATOM   326  O  O   . THR   A 1 37  ? 9.688  -5.594  38.000  1.00 23.43 ? 37  THR   A O   1 
ATOM   327  C  CB  . THR   A 1 37  ? 11.796 -7.848  37.308  1.00 26.30 ? 37  THR   A CB  1 
ATOM   328  O  OG1 . THR   A 1 37  ? 12.323 -9.022  37.929  1.00 36.12 ? 37  THR   A OG1 1 
ATOM   329  C  CG2 . THR   A 1 37  ? 12.507 -6.629  37.880  1.00 29.81 ? 37  THR   A CG2 1 
ATOM   330  N  N   . ALA   A 1 38  ? 9.041  -6.474  36.040  1.00 18.96 ? 38  ALA   A N   1 
ATOM   331  C  CA  . ALA   A 1 38  ? 8.369  -5.264  35.624  1.00 17.92 ? 38  ALA   A CA  1 
ATOM   332  C  C   . ALA   A 1 38  ? 7.233  -4.982  36.591  1.00 19.75 ? 38  ALA   A C   1 
ATOM   333  O  O   . ALA   A 1 38  ? 6.557  -5.888  37.018  1.00 25.85 ? 38  ALA   A O   1 
ATOM   334  C  CB  . ALA   A 1 38  ? 7.889  -5.383  34.204  1.00 17.24 ? 38  ALA   A CB  1 
ATOM   335  N  N   . LYS   A 1 39  ? 7.094  -3.736  36.979  1.00 19.39 ? 39  LYS   A N   1 
ATOM   336  C  CA  . LYS   A 1 39  ? 6.093  -3.339  37.960  1.00 20.87 ? 39  LYS   A CA  1 
ATOM   337  C  C   . LYS   A 1 39  ? 4.878  -2.711  37.276  1.00 18.72 ? 39  LYS   A C   1 
ATOM   338  O  O   . LYS   A 1 39  ? 4.998  -1.750  36.553  1.00 16.73 ? 39  LYS   A O   1 
ATOM   339  C  CB  . LYS   A 1 39  ? 6.796  -2.338  38.874  1.00 25.85 ? 39  LYS   A CB  1 
ATOM   340  C  CG  . LYS   A 1 39  ? 5.945  -1.478  39.764  1.00 32.22 ? 39  LYS   A CG  1 
ATOM   341  C  CD  . LYS   A 1 39  ? 5.953  -1.865  41.171  1.00 30.52 ? 39  LYS   A CD  1 
ATOM   342  C  CE  . LYS   A 1 39  ? 5.085  -0.971  42.011  1.00 33.68 ? 39  LYS   A CE  1 
ATOM   343  N  NZ  . LYS   A 1 39  ? 4.952  -1.584  43.334  1.00 38.20 ? 39  LYS   A NZ  1 
ATOM   344  N  N   . TYR   A 1 40  ? 3.698  -3.239  37.558  1.00 21.19 ? 40  TYR   A N   1 
ATOM   345  C  CA  . TYR   A 1 40  ? 2.477  -2.572  37.168  1.00 19.67 ? 40  TYR   A CA  1 
ATOM   346  C  C   . TYR   A 1 40  ? 2.429  -1.189  37.803  1.00 19.56 ? 40  TYR   A C   1 
ATOM   347  O  O   . TYR   A 1 40  ? 2.642  -1.039  39.027  1.00 21.01 ? 40  TYR   A O   1 
ATOM   348  C  CB  . TYR   A 1 40  ? 1.293  -3.434  37.616  1.00 22.99 ? 40  TYR   A CB  1 
ATOM   349  C  CG  . TYR   A 1 40  ? -0.013 -2.691  37.472  1.00 25.26 ? 40  TYR   A CG  1 
ATOM   350  C  CD1 . TYR   A 1 40  ? -0.444 -2.260  36.226  1.00 24.65 ? 40  TYR   A CD1 1 
ATOM   351  C  CD2 . TYR   A 1 40  ? -0.816 -2.430  38.580  1.00 28.18 ? 40  TYR   A CD2 1 
ATOM   352  C  CE1 . TYR   A 1 40  ? -1.632 -1.571  36.076  1.00 27.79 ? 40  TYR   A CE1 1 
ATOM   353  C  CE2 . TYR   A 1 40  ? -2.015 -1.754  38.442  1.00 30.47 ? 40  TYR   A CE2 1 
ATOM   354  C  CZ  . TYR   A 1 40  ? -2.415 -1.321  37.191  1.00 29.97 ? 40  TYR   A CZ  1 
ATOM   355  O  OH  . TYR   A 1 40  ? -3.601 -0.651  37.095  1.00 39.91 ? 40  TYR   A OH  1 
ATOM   356  N  N   . ASP   A 1 41  ? 2.126  -0.191  36.976  1.00 19.24 ? 41  ASP   A N   1 
ATOM   357  C  CA  . ASP   A 1 41  ? 2.082  1.198   37.417  1.00 20.33 ? 41  ASP   A CA  1 
ATOM   358  C  C   . ASP   A 1 41  ? 0.686  1.756   37.172  1.00 22.40 ? 41  ASP   A C   1 
ATOM   359  O  O   . ASP   A 1 41  ? 0.361  2.143   36.036  1.00 22.56 ? 41  ASP   A O   1 
ATOM   360  C  CB  . ASP   A 1 41  ? 3.155  2.053   36.725  1.00 22.00 ? 41  ASP   A CB  1 
ATOM   361  C  CG  . ASP   A 1 41  ? 3.201  3.484   37.212  1.00 25.66 ? 41  ASP   A CG  1 
ATOM   362  O  OD1 . ASP   A 1 41  ? 2.278  3.885   37.969  1.00 26.25 ? 41  ASP   A OD1 1 
ATOM   363  O  OD2 . ASP   A 1 41  ? 4.165  4.182   36.855  1.00 31.60 ? 41  ASP   A OD2 1 
ATOM   364  N  N   . PRO   A 1 42  ? -0.161 1.837   38.227  1.00 26.37 ? 42  PRO   A N   1 
ATOM   365  C  CA  . PRO   A 1 42  ? -1.552 2.258   38.062  1.00 29.36 ? 42  PRO   A CA  1 
ATOM   366  C  C   . PRO   A 1 42  ? -1.666 3.739   37.696  1.00 29.67 ? 42  PRO   A C   1 
ATOM   367  O  O   . PRO   A 1 42  ? -2.716 4.225   37.274  1.00 32.27 ? 42  PRO   A O   1 
ATOM   368  C  CB  . PRO   A 1 42  ? -2.170 1.895   39.424  1.00 32.38 ? 42  PRO   A CB  1 
ATOM   369  C  CG  . PRO   A 1 42  ? -1.025 1.987   40.398  1.00 31.54 ? 42  PRO   A CG  1 
ATOM   370  C  CD  . PRO   A 1 42  ? 0.168  1.469   39.626  1.00 28.62 ? 42  PRO   A CD  1 
ATOM   371  N  N   . SER   A 1 43  ? -0.568 4.476   37.840  1.00 28.02 ? 43  SER   A N   1 
ATOM   372  C  CA  . SER   A 1 43  ? -0.536 5.878   37.466  1.00 29.43 ? 43  SER   A CA  1 
ATOM   373  C  C   . SER   A 1 43  ? -0.380 6.094   35.959  1.00 29.98 ? 43  SER   A C   1 
ATOM   374  O  O   . SER   A 1 43  ? -0.713 7.172   35.469  1.00 33.00 ? 43  SER   A O   1 
ATOM   375  C  CB  . SER   A 1 43  ? 0.533  6.612   38.214  1.00 31.87 ? 43  SER   A CB  1 
ATOM   376  O  OG  . SER   A 1 43  ? 1.818  6.381   37.680  1.00 34.43 ? 43  SER   A OG  1 
ATOM   377  N  N   . LEU   A 1 44  ? 0.080  5.078   35.224  1.00 27.97 ? 44  LEU   A N   1 
ATOM   378  C  CA  . LEU   A 1 44  ? 0.206  5.193   33.776  1.00 27.60 ? 44  LEU   A CA  1 
ATOM   379  C  C   . LEU   A 1 44  ? -1.163 5.392   33.130  1.00 31.90 ? 44  LEU   A C   1 
ATOM   380  O  O   . LEU   A 1 44  ? -2.171 4.800   33.516  1.00 34.20 ? 44  LEU   A O   1 
ATOM   381  C  CB  . LEU   A 1 44  ? 0.841  3.927   33.185  1.00 27.17 ? 44  LEU   A CB  1 
ATOM   382  C  CG  . LEU   A 1 44  ? 2.340  3.755   33.385  1.00 23.27 ? 44  LEU   A CG  1 
ATOM   383  C  CD1 . LEU   A 1 44  ? 2.758  2.381   32.920  1.00 23.46 ? 44  LEU   A CD1 1 
ATOM   384  C  CD2 . LEU   A 1 44  ? 3.119  4.818   32.635  1.00 22.77 ? 44  LEU   A CD2 1 
ATOM   385  N  N   . LYS   A 1 45  ? -1.150 6.129   32.035  1.00 39.09 ? 45  LYS   A N   1 
ATOM   386  C  CA  . LYS   A 1 45  ? -2.348 6.362   31.247  1.00 39.93 ? 45  LYS   A CA  1 
ATOM   387  C  C   . LYS   A 1 45  ? -2.427 5.327   30.136  1.00 36.91 ? 45  LYS   A C   1 
ATOM   388  O  O   . LYS   A 1 45  ? -1.437 4.630   29.762  1.00 33.86 ? 45  LYS   A O   1 
ATOM   389  C  CB  . LYS   A 1 45  ? -2.356 7.806   30.760  1.00 37.00 ? 45  LYS   A CB  1 
ATOM   390  C  CG  . LYS   A 1 45  ? -2.262 8.839   31.875  1.00 36.88 ? 45  LYS   A CG  1 
ATOM   391  N  N   . PRO   A 1 46  ? -3.669 5.140   29.570  1.00 32.00 ? 46  PRO   A N   1 
ATOM   392  C  CA  . PRO   A 1 46  ? -3.816 4.430   28.312  1.00 32.90 ? 46  PRO   A CA  1 
ATOM   393  C  C   . PRO   A 1 46  ? -2.984 5.231   27.338  1.00 23.89 ? 46  PRO   A C   1 
ATOM   394  O  O   . PRO   A 1 46  ? -2.914 6.458   27.364  1.00 24.78 ? 46  PRO   A O   1 
ATOM   395  C  CB  . PRO   A 1 46  ? -5.302 4.452   27.921  1.00 32.38 ? 46  PRO   A CB  1 
ATOM   396  C  CG  . PRO   A 1 46  ? -6.002 4.847   29.212  1.00 35.78 ? 46  PRO   A CG  1 
ATOM   397  C  CD  . PRO   A 1 46  ? -4.982 5.561   30.087  1.00 34.67 ? 46  PRO   A CD  1 
ATOM   398  N  N   . LEU   A 1 47  ? -2.359 4.483   26.475  1.00 25.46 ? 47  LEU   A N   1 
ATOM   399  C  CA  . LEU   A 1 47  ? -1.678 5.114   25.403  1.00 21.06 ? 47  LEU   A CA  1 
ATOM   400  C  C   . LEU   A 1 47  ? -2.736 5.636   24.447  1.00 19.89 ? 47  LEU   A C   1 
ATOM   401  O  O   . LEU   A 1 47  ? -3.747 4.981   24.267  1.00 22.56 ? 47  LEU   A O   1 
ATOM   402  C  CB  . LEU   A 1 47  ? -0.815 4.006   24.832  1.00 26.59 ? 47  LEU   A CB  1 
ATOM   403  C  CG  . LEU   A 1 47  ? 0.191  4.403   23.799  1.00 26.97 ? 47  LEU   A CG  1 
ATOM   404  C  CD1 . LEU   A 1 47  ? 1.246  5.275   24.451  1.00 26.01 ? 47  LEU   A CD1 1 
ATOM   405  C  CD2 . LEU   A 1 47  ? 0.783  3.136   23.210  1.00 28.31 ? 47  LEU   A CD2 1 
ATOM   406  N  N   . SER   A 1 48  ? -2.448 6.757   23.808  1.00 15.63 ? 48  SER   A N   1 
ATOM   407  C  CA  . SER   A 1 48  ? -3.252 7.352   22.755  1.00 16.52 ? 48  SER   A CA  1 
ATOM   408  C  C   . SER   A 1 48  ? -2.449 7.337   21.469  1.00 15.38 ? 48  SER   A C   1 
ATOM   409  O  O   . SER   A 1 48  ? -1.487 8.072   21.320  1.00 16.46 ? 48  SER   A O   1 
ATOM   410  C  CB  . SER   A 1 48  ? -3.626 8.790   23.113  1.00 18.29 ? 48  SER   A CB  1 
ATOM   411  O  OG  . SER   A 1 48  ? -4.310 9.399   22.042  1.00 22.27 ? 48  SER   A OG  1 
ATOM   412  N  N   . VAL   A 1 49  ? -2.824 6.458   20.564  1.00 15.89 ? 49  VAL   A N   1 
ATOM   413  C  CA  . VAL   A 1 49  ? -2.233 6.341   19.237  1.00 17.57 ? 49  VAL   A CA  1 
ATOM   414  C  C   . VAL   A 1 49  ? -3.240 6.920   18.236  1.00 18.46 ? 49  VAL   A C   1 
ATOM   415  O  O   . VAL   A 1 49  ? -4.274 6.326   18.017  1.00 22.54 ? 49  VAL   A O   1 
ATOM   416  C  CB  . VAL   A 1 49  ? -1.910 4.873   18.934  1.00 19.33 ? 49  VAL   A CB  1 
ATOM   417  C  CG1 . VAL   A 1 49  ? -1.152 4.733   17.634  1.00 22.29 ? 49  VAL   A CG1 1 
ATOM   418  C  CG2 . VAL   A 1 49  ? -1.158 4.186   20.065  1.00 21.85 ? 49  VAL   A CG2 1 
ATOM   419  N  N   . SER   A 1 50  ? -2.930 8.078   17.645  1.00 17.77 ? 50  SER   A N   1 
ATOM   420  C  CA  . SER   A 1 50  ? -3.865 8.832   16.798  1.00 18.87 ? 50  SER   A CA  1 
ATOM   421  C  C   . SER   A 1 50  ? -3.261 8.948   15.410  1.00 18.15 ? 50  SER   A C   1 
ATOM   422  O  O   . SER   A 1 50  ? -2.596 9.936   15.113  1.00 19.13 ? 50  SER   A O   1 
ATOM   423  C  CB  . SER   A 1 50  ? -4.170 10.184  17.361  1.00 22.93 ? 50  SER   A CB  1 
ATOM   424  O  OG  . SER   A 1 50  ? -4.829 10.034  18.613  1.00 30.93 ? 50  SER   A OG  1 
ATOM   425  N  N   . TYR   A 1 51  ? -3.490 7.916   14.574  1.00 17.33 ? 51  TYR   A N   1 
ATOM   426  C  CA  . TYR   A 1 51  ? -2.855 7.802   13.269  1.00 16.42 ? 51  TYR   A CA  1 
ATOM   427  C  C   . TYR   A 1 51  ? -3.794 8.048   12.092  1.00 18.80 ? 51  TYR   A C   1 
ATOM   428  O  O   . TYR   A 1 51  ? -3.384 7.896   10.939  1.00 17.41 ? 51  TYR   A O   1 
ATOM   429  C  CB  . TYR   A 1 51  ? -2.190 6.434   13.103  1.00 16.24 ? 51  TYR   A CB  1 
ATOM   430  C  CG  . TYR   A 1 51  ? -0.924 6.164   13.901  1.00 13.69 ? 51  TYR   A CG  1 
ATOM   431  C  CD1 . TYR   A 1 51  ? -0.239 7.153   14.602  1.00 14.42 ? 51  TYR   A CD1 1 
ATOM   432  C  CD2 . TYR   A 1 51  ? -0.391 4.898   13.917  1.00 12.94 ? 51  TYR   A CD2 1 
ATOM   433  C  CE1 . TYR   A 1 51  ? 0.931  6.850   15.293  1.00 13.07 ? 51  TYR   A CE1 1 
ATOM   434  C  CE2 . TYR   A 1 51  ? 0.778  4.584   14.591  1.00 13.14 ? 51  TYR   A CE2 1 
ATOM   435  C  CZ  . TYR   A 1 51  ? 1.468  5.579   15.274  1.00 12.74 ? 51  TYR   A CZ  1 
ATOM   436  O  OH  . TYR   A 1 51  ? 2.636  5.221   15.909  1.00 13.35 ? 51  TYR   A OH  1 
ATOM   437  N  N   . ASP   A 1 52  ? -5.057 8.419   12.344  1.00 20.98 ? 52  ASP   A N   1 
ATOM   438  C  CA  . ASP   A 1 52  ? -6.003 8.563   11.224  1.00 22.21 ? 52  ASP   A CA  1 
ATOM   439  C  C   . ASP   A 1 52  ? -5.559 9.545   10.124  1.00 20.21 ? 52  ASP   A C   1 
ATOM   440  O  O   . ASP   A 1 52  ? -5.877 9.334   8.957   1.00 22.50 ? 52  ASP   A O   1 
ATOM   441  C  CB  . ASP   A 1 52  ? -7.385 8.982   11.705  1.00 24.23 ? 52  ASP   A CB  1 
ATOM   442  C  CG  . ASP   A 1 52  ? -7.330 10.097  12.729  1.00 32.67 ? 52  ASP   A CG  1 
ATOM   443  O  OD1 . ASP   A 1 52  ? -6.816 9.828   13.859  1.00 41.51 ? 52  ASP   A OD1 1 
ATOM   444  O  OD2 . ASP   A 1 52  ? -7.742 11.219  12.388  1.00 45.10 ? 52  ASP   A OD2 1 
ATOM   445  N  N   . GLN   A 1 53  ? -4.850 10.638  10.457  1.00 20.03 ? 53  GLN   A N   1 
ATOM   446  C  CA  . GLN   A 1 53  ? -4.456 11.613  9.448   1.00 20.95 ? 53  GLN   A CA  1 
ATOM   447  C  C   . GLN   A 1 53  ? -3.009 11.432  9.004   1.00 17.68 ? 53  GLN   A C   1 
ATOM   448  O  O   . GLN   A 1 53  ? -2.447 12.307  8.369   1.00 19.02 ? 53  GLN   A O   1 
ATOM   449  C  CB  . GLN   A 1 53  ? -4.667 13.052  9.951   1.00 23.72 ? 53  GLN   A CB  1 
ATOM   450  C  CG  . GLN   A 1 53  ? -6.124 13.452  10.132  1.00 29.06 ? 53  GLN   A CG  1 
ATOM   451  C  CD  . GLN   A 1 53  ? -6.934 13.329  8.867   1.00 33.09 ? 53  GLN   A CD  1 
ATOM   452  O  OE1 . GLN   A 1 53  ? -7.965 12.655  8.826   1.00 40.58 ? 53  GLN   A OE1 1 
ATOM   453  N  NE2 . GLN   A 1 53  ? -6.441 13.954  7.808   1.00 35.54 ? 53  GLN   A NE2 1 
ATOM   454  N  N   . ALA   A 1 54  ? -2.406 10.267  9.261   1.00 16.84 ? 54  ALA   A N   1 
ATOM   455  C  CA  . ALA   A 1 54  ? -1.041 10.012  8.814   1.00 16.35 ? 54  ALA   A CA  1 
ATOM   456  C  C   . ALA   A 1 54  ? -0.904 10.203  7.312   1.00 16.72 ? 54  ALA   A C   1 
ATOM   457  O  O   . ALA   A 1 54  ? -1.779 9.805   6.532   1.00 19.84 ? 54  ALA   A O   1 
ATOM   458  C  CB  . ALA   A 1 54  ? -0.633 8.630   9.249   1.00 18.49 ? 54  ALA   A CB  1 
ATOM   459  N  N   . THR   A 1 55  ? 0.230  10.800  6.906   1.00 14.90 ? 55  THR   A N   1 
ATOM   460  C  CA  . THR   A 1 55  ? 0.583  10.960  5.504   1.00 14.39 ? 55  THR   A CA  1 
ATOM   461  C  C   . THR   A 1 55  ? 1.929  10.295  5.281   1.00 13.23 ? 55  THR   A C   1 
ATOM   462  O  O   . THR   A 1 55  ? 2.928  10.938  5.562   1.00 14.20 ? 55  THR   A O   1 
ATOM   463  C  CB  . THR   A 1 55  ? 0.713  12.442  5.097   1.00 17.76 ? 55  THR   A CB  1 
ATOM   464  O  OG1 . THR   A 1 55  ? -0.527 13.089  5.237   1.00 20.88 ? 55  THR   A OG1 1 
ATOM   465  C  CG2 . THR   A 1 55  ? 1.181  12.649  3.678   1.00 19.95 ? 55  THR   A CG2 1 
ATOM   466  N  N   . SER   A 1 56  ? 1.945  9.078   4.775   1.00 12.54 ? 56  SER   A N   1 
ATOM   467  C  CA  . SER   A 1 56  ? 3.192  8.441   4.379   1.00 12.42 ? 56  SER   A CA  1 
ATOM   468  C  C   . SER   A 1 56  ? 3.694  9.091   3.092   1.00 13.35 ? 56  SER   A C   1 
ATOM   469  O  O   . SER   A 1 56  ? 2.919  9.602   2.273   1.00 14.42 ? 56  SER   A O   1 
ATOM   470  C  CB  . SER   A 1 56  ? 3.014  6.958   4.233   1.00 12.74 ? 56  SER   A CB  1 
ATOM   471  O  OG  . SER   A 1 56  ? 2.170  6.649   3.122   1.00 14.45 ? 56  SER   A OG  1 
ATOM   472  N  N   . LEU   A 1 57  ? 5.018  9.104   2.905   1.00 13.54 ? 57  LEU   A N   1 
ATOM   473  C  CA  . LEU   A 1 57  ? 5.643  9.763   1.763   1.00 14.11 ? 57  LEU   A CA  1 
ATOM   474  C  C   . LEU   A 1 57  ? 6.413  8.792   0.892   1.00 13.99 ? 57  LEU   A C   1 
ATOM   475  O  O   . LEU   A 1 57  ? 6.173  8.692   -0.317  1.00 18.33 ? 57  LEU   A O   1 
ATOM   476  C  CB  . LEU   A 1 57  ? 6.542  10.914  2.209   1.00 14.79 ? 57  LEU   A CB  1 
ATOM   477  C  CG  . LEU   A 1 57  ? 5.805  12.070  2.883   1.00 17.56 ? 57  LEU   A CG  1 
ATOM   478  C  CD1 . LEU   A 1 57  ? 6.815  13.042  3.484   1.00 19.61 ? 57  LEU   A CD1 1 
ATOM   479  C  CD2 . LEU   A 1 57  ? 4.826  12.789  1.937   1.00 22.20 ? 57  LEU   A CD2 1 
ATOM   480  N  N   . ARG   A 1 58  ? 7.439  8.159   1.449   1.00 14.00 ? 58  ARG   A N   1 
ATOM   481  C  CA  . ARG   A 1 58  ? 8.386  7.382   0.666   1.00 13.75 ? 58  ARG   A CA  1 
ATOM   482  C  C   . ARG   A 1 58  ? 8.844  6.192   1.498   1.00 13.08 ? 58  ARG   A C   1 
ATOM   483  O  O   . ARG   A 1 58  ? 8.722  6.199   2.730   1.00 14.27 ? 58  ARG   A O   1 
ATOM   484  C  CB  . ARG   A 1 58  ? 9.618  8.207   0.258   1.00 18.38 ? 58  ARG   A CB  1 
ATOM   485  C  CG  . ARG   A 1 58  ? 9.312  9.429   -0.608  1.00 25.61 ? 58  ARG   A CG  1 
ATOM   486  C  CD  . ARG   A 1 58  ? 10.416 10.010  -1.489  1.00 33.38 ? 58  ARG   A CD  1 
ATOM   487  N  NE  . ARG   A 1 58  ? 11.121 9.074   -2.366  1.00 37.18 ? 58  ARG   A NE  1 
ATOM   488  C  CZ  . ARG   A 1 58  ? 10.770 8.723   -3.602  1.00 36.93 ? 58  ARG   A CZ  1 
ATOM   489  N  NH1 . ARG   A 1 58  ? 9.596  9.091   -4.080  1.00 40.97 ? 58  ARG   A NH1 1 
ATOM   490  N  NH2 . ARG   A 1 58  ? 11.567 7.956   -4.339  1.00 36.56 ? 58  ARG   A NH2 1 
ATOM   491  N  N   . ILE   A 1 59  ? 9.382  5.171   0.817   1.00 13.01 ? 59  ILE   A N   1 
ATOM   492  C  CA  . ILE   A 1 59  ? 10.016 4.042   1.443   1.00 13.20 ? 59  ILE   A CA  1 
ATOM   493  C  C   . ILE   A 1 59  ? 11.432 3.981   0.896   1.00 13.49 ? 59  ILE   A C   1 
ATOM   494  O  O   . ILE   A 1 59  ? 11.668 4.200   -0.272  1.00 14.61 ? 59  ILE   A O   1 
ATOM   495  C  CB  . ILE   A 1 59  ? 9.194  2.753   1.253   1.00 13.13 ? 59  ILE   A CB  1 
ATOM   496  C  CG1 . ILE   A 1 59  ? 9.687  1.609   2.134   1.00 13.45 ? 59  ILE   A CG1 1 
ATOM   497  C  CG2 . ILE   A 1 59  ? 9.102  2.349   -0.208  1.00 14.61 ? 59  ILE   A CG2 1 
ATOM   498  C  CD1 . ILE   A 1 59  ? 8.800  0.409   2.173   1.00 15.02 ? 59  ILE   A CD1 1 
ATOM   499  N  N   A LEU   A 1 60  ? 12.394 3.659   1.789   0.50 13.61 ? 60  LEU   A N   1 
ATOM   500  N  N   B LEU   A 1 60  ? 12.401 3.651   1.782   0.50 13.53 ? 60  LEU   A N   1 
ATOM   501  C  CA  A LEU   A 1 60  ? 13.808 3.699   1.453   0.50 14.67 ? 60  LEU   A CA  1 
ATOM   502  C  CA  B LEU   A 1 60  ? 13.813 3.717   1.435   0.50 14.48 ? 60  LEU   A CA  1 
ATOM   503  C  C   A LEU   A 1 60  ? 14.508 2.468   2.026   0.50 13.21 ? 60  LEU   A C   1 
ATOM   504  C  C   B LEU   A 1 60  ? 14.579 2.554   2.063   0.50 13.01 ? 60  LEU   A C   1 
ATOM   505  O  O   A LEU   A 1 60  ? 14.142 1.993   3.093   0.50 13.53 ? 60  LEU   A O   1 
ATOM   506  O  O   B LEU   A 1 60  ? 14.408 2.302   3.255   0.50 12.89 ? 60  LEU   A O   1 
ATOM   507  C  CB  A LEU   A 1 60  ? 14.422 4.973   2.063   0.50 16.38 ? 60  LEU   A CB  1 
ATOM   508  C  CB  B LEU   A 1 60  ? 14.409 5.018   1.996   0.50 16.33 ? 60  LEU   A CB  1 
ATOM   509  C  CG  A LEU   A 1 60  ? 15.941 5.102   2.132   0.50 19.42 ? 60  LEU   A CG  1 
ATOM   510  C  CG  B LEU   A 1 60  ? 15.928 5.113   2.122   0.50 19.42 ? 60  LEU   A CG  1 
ATOM   511  C  CD1 . LEU   A 1 60  ? 16.516 5.298   0.751   1.00 20.12 ? 60  LEU   A CD1 1 
ATOM   512  C  CD2 . LEU   A 1 60  ? 16.334 6.262   3.032   1.00 20.47 ? 60  LEU   A CD2 1 
ATOM   513  N  N   . ASN   A 1 61  ? 15.471 1.937   1.279   1.00 13.74 ? 61  ASN   A N   1 
ATOM   514  C  CA  . ASN   A 1 61  ? 16.476 0.996   1.805   1.00 14.01 ? 61  ASN   A CA  1 
ATOM   515  C  C   . ASN   A 1 61  ? 17.713 1.831   2.125   1.00 13.94 ? 61  ASN   A C   1 
ATOM   516  O  O   . ASN   A 1 61  ? 18.341 2.363   1.228   1.00 15.09 ? 61  ASN   A O   1 
ATOM   517  C  CB  . ASN   A 1 61  ? 16.790 -0.089  0.773   1.00 14.93 ? 61  ASN   A CB  1 
ATOM   518  C  CG  . ASN   A 1 61  ? 17.863 -1.078  1.194   1.00 14.08 ? 61  ASN   A CG  1 
ATOM   519  O  OD1 . ASN   A 1 61  ? 18.676 -0.755  2.049   1.00 14.99 ? 61  ASN   A OD1 1 
ATOM   520  N  ND2 . ASN   A 1 61  ? 17.865 -2.255  0.606   1.00 15.33 ? 61  ASN   A ND2 1 
ATOM   521  N  N   A ASN   A 1 62  ? 18.067 1.950   3.403   0.50 14.65 ? 62  ASN   A N   1 
ATOM   522  N  N   B ASN   A 1 62  ? 18.044 1.905   3.413   0.50 14.12 ? 62  ASN   A N   1 
ATOM   523  C  CA  A ASN   A 1 62  ? 19.226 2.774   3.747   0.50 15.86 ? 62  ASN   A CA  1 
ATOM   524  C  CA  B ASN   A 1 62  ? 19.162 2.730   3.860   0.50 15.12 ? 62  ASN   A CA  1 
ATOM   525  C  C   A ASN   A 1 62  ? 20.475 1.928   4.013   0.50 15.79 ? 62  ASN   A C   1 
ATOM   526  C  C   B ASN   A 1 62  ? 20.390 1.878   4.192   0.50 15.61 ? 62  ASN   A C   1 
ATOM   527  O  O   A ASN   A 1 62  ? 21.490 2.467   4.455   0.50 17.25 ? 62  ASN   A O   1 
ATOM   528  O  O   B ASN   A 1 62  ? 21.295 2.365   4.875   0.50 17.92 ? 62  ASN   A O   1 
ATOM   529  C  CB  A ASN   A 1 62  ? 18.946 3.700   4.928   0.50 17.45 ? 62  ASN   A CB  1 
ATOM   530  C  CB  B ASN   A 1 62  ? 18.746 3.591   5.049   0.50 16.25 ? 62  ASN   A CB  1 
ATOM   531  C  CG  A ASN   A 1 62  ? 18.868 2.953   6.243   0.50 17.70 ? 62  ASN   A CG  1 
ATOM   532  C  CG  B ASN   A 1 62  ? 18.221 2.768   6.208   0.50 15.36 ? 62  ASN   A CG  1 
ATOM   533  O  OD1 A ASN   A 1 62  ? 18.753 1.727   6.271   0.50 16.67 ? 62  ASN   A OD1 1 
ATOM   534  O  OD1 B ASN   A 1 62  ? 18.538 1.584   6.346   0.50 15.36 ? 62  ASN   A OD1 1 
ATOM   535  N  ND2 A ASN   A 1 62  ? 18.949 3.680   7.343   0.50 20.68 ? 62  ASN   A ND2 1 
ATOM   536  N  ND2 B ASN   A 1 62  ? 17.481 3.409   7.084   0.50 16.10 ? 62  ASN   A ND2 1 
ATOM   537  N  N   . GLY   A 1 63  ? 20.419 0.633   3.722   1.00 14.80 ? 63  GLY   A N   1 
ATOM   538  C  CA  . GLY   A 1 63  ? 21.537 -0.255  3.969   1.00 15.50 ? 63  GLY   A CA  1 
ATOM   539  C  C   . GLY   A 1 63  ? 21.527 -0.914  5.343   1.00 14.46 ? 63  GLY   A C   1 
ATOM   540  O  O   . GLY   A 1 63  ? 22.365 -1.777  5.565   1.00 16.81 ? 63  GLY   A O   1 
ATOM   541  N  N   A HIS   A 1 64  ? 20.566 -0.538  6.196   0.50 12.76 ? 64  HIS   A N   1 
ATOM   542  N  N   B HIS   A 1 64  ? 20.669 -0.477  6.270   0.50 15.47 ? 64  HIS   A N   1 
ATOM   543  C  CA  A HIS   A 1 64  ? 20.444 -1.065  7.544   0.50 12.04 ? 64  HIS   A CA  1 
ATOM   544  C  CA  B HIS   A 1 64  ? 20.509 -1.219  7.512   0.50 17.14 ? 64  HIS   A CA  1 
ATOM   545  C  C   A HIS   A 1 64  ? 19.062 -1.624  7.856   0.50 11.70 ? 64  HIS   A C   1 
ATOM   546  C  C   B HIS   A 1 64  ? 19.150 -1.898  7.595   0.50 15.94 ? 64  HIS   A C   1 
ATOM   547  O  O   A HIS   A 1 64  ? 18.892 -2.440  8.759   0.50 11.96 ? 64  HIS   A O   1 
ATOM   548  O  O   B HIS   A 1 64  ? 19.078 -3.058  7.998   0.50 16.81 ? 64  HIS   A O   1 
ATOM   549  C  CB  A HIS   A 1 64  ? 20.710 0.015   8.582   0.50 11.78 ? 64  HIS   A CB  1 
ATOM   550  C  CB  B HIS   A 1 64  ? 20.870 -0.445  8.785   0.50 18.95 ? 64  HIS   A CB  1 
ATOM   551  C  CG  A HIS   A 1 64  ? 22.058 0.642   8.479   0.50 12.95 ? 64  HIS   A CG  1 
ATOM   552  C  CG  B HIS   A 1 64  ? 20.558 1.005   8.877   0.50 23.05 ? 64  HIS   A CG  1 
ATOM   553  N  ND1 A HIS   A 1 64  ? 23.248 -0.022  8.669   0.50 13.20 ? 64  HIS   A ND1 1 
ATOM   554  N  ND1 B HIS   A 1 64  ? 21.301 1.969   8.233   0.50 25.91 ? 64  HIS   A ND1 1 
ATOM   555  C  CD2 A HIS   A 1 64  ? 22.371 1.905   8.238   0.50 14.12 ? 64  HIS   A CD2 1 
ATOM   556  C  CD2 B HIS   A 1 64  ? 19.657 1.669   9.621   0.50 23.78 ? 64  HIS   A CD2 1 
ATOM   557  C  CE1 A HIS   A 1 64  ? 24.238 0.869   8.621   0.50 14.31 ? 64  HIS   A CE1 1 
ATOM   558  C  CE1 B HIS   A 1 64  ? 20.819 3.171   8.536   0.50 25.95 ? 64  HIS   A CE1 1 
ATOM   559  N  NE2 A HIS   A 1 64  ? 23.724 2.042   8.332   0.50 14.42 ? 64  HIS   A NE2 1 
ATOM   560  N  NE2 B HIS   A 1 64  ? 19.842 3.016   9.395   0.50 25.30 ? 64  HIS   A NE2 1 
ATOM   561  N  N   A SER   A 1 65  ? 18.058 -1.101  7.157   0.50 11.77 ? 65  SER   A N   1 
ATOM   562  N  N   B SER   A 1 65  ? 18.104 -1.166  7.206   0.50 15.33 ? 65  SER   A N   1 
ATOM   563  C  CA  A SER   A 1 65  ? 16.674 -1.529  7.277   0.50 11.87 ? 65  SER   A CA  1 
ATOM   564  C  CA  B SER   A 1 65  ? 16.736 -1.658  7.182   0.50 14.61 ? 65  SER   A CA  1 
ATOM   565  C  C   A SER   A 1 65  ? 15.997 -0.992  6.022   0.50 12.37 ? 65  SER   A C   1 
ATOM   566  C  C   B SER   A 1 65  ? 16.000 -0.890  6.083   0.50 14.07 ? 65  SER   A C   1 
ATOM   567  O  O   A SER   A 1 65  ? 16.655 -0.527  5.089   0.50 12.68 ? 65  SER   A O   1 
ATOM   568  O  O   B SER   A 1 65  ? 16.609 -0.137  5.314   0.50 14.32 ? 65  SER   A O   1 
ATOM   569  C  CB  A SER   A 1 65  ? 16.055 -1.006  8.560   0.50 11.87 ? 65  SER   A CB  1 
ATOM   570  C  CB  B SER   A 1 65  ? 16.093 -1.531  8.548   0.50 14.95 ? 65  SER   A CB  1 
ATOM   571  O  OG  A SER   A 1 65  ? 14.737 -1.504  8.765   0.50 12.99 ? 65  SER   A OG  1 
ATOM   572  O  OG  B SER   A 1 65  ? 15.905 -0.192  8.932   0.50 16.00 ? 65  SER   A OG  1 
ATOM   573  N  N   . PHE   A 1 66  ? 14.682 -1.059  6.032   1.00 13.17 ? 66  PHE   A N   1 
ATOM   574  C  CA  . PHE   A 1 66  ? 13.870 -0.201  5.182   1.00 13.06 ? 66  PHE   A CA  1 
ATOM   575  C  C   . PHE   A 1 66  ? 12.988 0.658   6.071   1.00 12.68 ? 66  PHE   A C   1 
ATOM   576  O  O   . PHE   A 1 66  ? 12.559 0.255   7.141   1.00 12.92 ? 66  PHE   A O   1 
ATOM   577  C  CB  . PHE   A 1 66  ? 13.062 -0.980  4.145   1.00 13.91 ? 66  PHE   A CB  1 
ATOM   578  C  CG  . PHE   A 1 66  ? 11.958 -1.831  4.722   1.00 13.62 ? 66  PHE   A CG  1 
ATOM   579  C  CD1 . PHE   A 1 66  ? 10.713 -1.277  4.970   1.00 14.80 ? 66  PHE   A CD1 1 
ATOM   580  C  CD2 . PHE   A 1 66  ? 12.173 -3.158  5.068   1.00 14.87 ? 66  PHE   A CD2 1 
ATOM   581  C  CE1 . PHE   A 1 66  ? 9.727  -2.059  5.521   1.00 14.89 ? 66  PHE   A CE1 1 
ATOM   582  C  CE2 . PHE   A 1 66  ? 11.165 -3.938  5.624   1.00 15.71 ? 66  PHE   A CE2 1 
ATOM   583  C  CZ  . PHE   A 1 66  ? 9.934  -3.366  5.831   1.00 14.84 ? 66  PHE   A CZ  1 
ATOM   584  N  N   . LYS   A 1 67  ? 12.740 1.874   5.593   1.00 13.39 ? 67  LYS   A N   1 
ATOM   585  C  CA  . LYS   A 1 67  ? 12.069 2.881   6.373   1.00 13.38 ? 67  LYS   A CA  1 
ATOM   586  C  C   . LYS   A 1 67  ? 11.011 3.596   5.560   1.00 12.79 ? 67  LYS   A C   1 
ATOM   587  O  O   . LYS   A 1 67  ? 11.274 3.950   4.412   1.00 13.67 ? 67  LYS   A O   1 
ATOM   588  C  CB  . LYS   A 1 67  ? 13.131 3.896   6.831   1.00 17.20 ? 67  LYS   A CB  1 
ATOM   589  C  CG  . LYS   A 1 67  ? 12.636 5.074   7.613   1.00 20.34 ? 67  LYS   A CG  1 
ATOM   590  C  CD  . LYS   A 1 67  ? 13.704 6.017   8.091   1.00 24.64 ? 67  LYS   A CD  1 
ATOM   591  C  CE  . LYS   A 1 67  ? 14.654 6.565   7.074   1.00 30.60 ? 67  LYS   A CE  1 
ATOM   592  N  NZ  . LYS   A 1 67  ? 15.541 7.527   7.780   1.00 36.40 ? 67  LYS   A NZ  1 
ATOM   593  N  N   . VAL   A 1 68  ? 9.835  3.772   6.177   1.00 11.53 ? 68  VAL   A N   1 
ATOM   594  C  CA  . VAL   A 1 68  ? 8.775  4.595   5.596   1.00 11.03 ? 68  VAL   A CA  1 
ATOM   595  C  C   . VAL   A 1 68  ? 8.772  5.911   6.342   1.00 11.70 ? 68  VAL   A C   1 
ATOM   596  O  O   . VAL   A 1 68  ? 8.604  5.898   7.568   1.00 11.76 ? 68  VAL   A O   1 
ATOM   597  C  CB  . VAL   A 1 68  ? 7.435  3.873   5.699   1.00 11.82 ? 68  VAL   A CB  1 
ATOM   598  C  CG1 . VAL   A 1 68  ? 6.279  4.793   5.290   1.00 12.24 ? 68  VAL   A CG1 1 
ATOM   599  C  CG2 . VAL   A 1 68  ? 7.424  2.578   4.885   1.00 13.14 ? 68  VAL   A CG2 1 
ATOM   600  N  N   A ASN   A 1 69  ? 8.949  7.016   5.595   0.50 11.61 ? 69  ASN   A N   1 
ATOM   601  N  N   B ASN   A 1 69  ? 8.937  7.022   5.627   0.50 12.41 ? 69  ASN   A N   1 
ATOM   602  C  CA  A ASN   A 1 69  ? 8.868  8.364   6.143   0.50 11.35 ? 69  ASN   A CA  1 
ATOM   603  C  CA  B ASN   A 1 69  ? 8.843  8.309   6.284   0.50 13.11 ? 69  ASN   A CA  1 
ATOM   604  C  C   A ASN   A 1 69  ? 7.436  8.905   6.060   0.50 11.87 ? 69  ASN   A C   1 
ATOM   605  C  C   B ASN   A 1 69  ? 7.509  8.992   6.010   0.50 12.73 ? 69  ASN   A C   1 
ATOM   606  O  O   A ASN   A 1 69  ? 6.625  8.489   5.201   0.50 11.89 ? 69  ASN   A O   1 
ATOM   607  O  O   B ASN   A 1 69  ? 6.910  8.821   4.924   0.50 12.62 ? 69  ASN   A O   1 
ATOM   608  C  CB  A ASN   A 1 69  ? 9.925  9.293   5.520   0.50 12.82 ? 69  ASN   A CB  1 
ATOM   609  C  CB  B ASN   A 1 69  ? 9.911  9.274   5.816   0.50 15.64 ? 69  ASN   A CB  1 
ATOM   610  C  CG  A ASN   A 1 69  ? 11.289 9.170   6.191   0.50 14.26 ? 69  ASN   A CG  1 
ATOM   611  C  CG  B ASN   A 1 69  ? 9.542  9.734   4.436   0.50 18.68 ? 69  ASN   A CG  1 
ATOM   612  O  OD1 A ASN   A 1 69  ? 11.539 9.712   7.269   0.50 16.39 ? 69  ASN   A OD1 1 
ATOM   613  O  OD1 B ASN   A 1 69  ? 9.374  8.918   3.543   0.50 18.47 ? 69  ASN   A OD1 1 
ATOM   614  N  ND2 A ASN   A 1 69  ? 12.170 8.419   5.587   0.50 15.10 ? 69  ASN   A ND2 1 
ATOM   615  N  ND2 B ASN   A 1 69  ? 9.347  11.028  4.282   0.50 22.18 ? 69  ASN   A ND2 1 
ATOM   616  N  N   . PHE   A 1 70  ? 7.121  9.795   7.000   1.00 11.86 ? 70  PHE   A N   1 
ATOM   617  C  CA  . PHE   A 1 70  ? 5.855  10.490  7.068   1.00 12.11 ? 70  PHE   A CA  1 
ATOM   618  C  C   . PHE   A 1 70  ? 6.034  11.995  7.035   1.00 13.00 ? 70  PHE   A C   1 
ATOM   619  O  O   . PHE   A 1 70  ? 7.046  12.554  7.413   1.00 15.03 ? 70  PHE   A O   1 
ATOM   620  C  CB  . PHE   A 1 70  ? 5.110  10.123  8.348   1.00 12.19 ? 70  PHE   A CB  1 
ATOM   621  C  CG  . PHE   A 1 70  ? 4.592  8.720   8.347   1.00 12.25 ? 70  PHE   A CG  1 
ATOM   622  C  CD1 . PHE   A 1 70  ? 5.466  7.669   8.573   1.00 12.94 ? 70  PHE   A CD1 1 
ATOM   623  C  CD2 . PHE   A 1 70  ? 3.276  8.417   7.992   1.00 12.73 ? 70  PHE   A CD2 1 
ATOM   624  C  CE1 . PHE   A 1 70  ? 5.014  6.376   8.478   1.00 13.28 ? 70  PHE   A CE1 1 
ATOM   625  C  CE2 . PHE   A 1 70  ? 2.818  7.118   7.913   1.00 12.80 ? 70  PHE   A CE2 1 
ATOM   626  C  CZ  . PHE   A 1 70  ? 3.703  6.093   8.143   1.00 13.40 ? 70  PHE   A CZ  1 
ATOM   627  N  N   . ASP   A 1 71  ? 4.991  12.703  6.580   1.00 14.13 ? 71  ASP   A N   1 
ATOM   628  C  CA  . ASP   A 1 71  ? 4.929  14.137  6.700   1.00 15.80 ? 71  ASP   A CA  1 
ATOM   629  C  C   . ASP   A 1 71  ? 4.699  14.450  8.176   1.00 15.80 ? 71  ASP   A C   1 
ATOM   630  O  O   . ASP   A 1 71  ? 3.620  14.225  8.713   1.00 20.13 ? 71  ASP   A O   1 
ATOM   631  C  CB  . ASP   A 1 71  ? 3.817  14.723  5.823   1.00 18.15 ? 71  ASP   A CB  1 
ATOM   632  C  CG  . ASP   A 1 71  ? 3.585  16.205  6.103   1.00 20.45 ? 71  ASP   A CG  1 
ATOM   633  O  OD1 . ASP   A 1 71  ? 4.442  16.841  6.725   1.00 21.61 ? 71  ASP   A OD1 1 
ATOM   634  O  OD2 . ASP   A 1 71  ? 2.536  16.712  5.748   1.00 27.21 ? 71  ASP   A OD2 1 
ATOM   635  N  N   . ASP   A 1 72  ? 5.709  15.006  8.832   1.00 15.88 ? 72  ASP   A N   1 
ATOM   636  C  CA  . ASP   A 1 72  ? 5.631  15.391  10.239  1.00 16.46 ? 72  ASP   A CA  1 
ATOM   637  C  C   . ASP   A 1 72  ? 5.717  16.915  10.389  1.00 18.52 ? 72  ASP   A C   1 
ATOM   638  O  O   . ASP   A 1 72  ? 6.152  17.400  11.417  1.00 20.58 ? 72  ASP   A O   1 
ATOM   639  C  CB  . ASP   A 1 72  ? 6.701  14.673  11.052  1.00 17.34 ? 72  ASP   A CB  1 
ATOM   640  C  CG  . ASP   A 1 72  ? 8.105  14.996  10.609  1.00 17.55 ? 72  ASP   A CG  1 
ATOM   641  O  OD1 . ASP   A 1 72  ? 8.255  15.693  9.559   1.00 18.34 ? 72  ASP   A OD1 1 
ATOM   642  O  OD2 . ASP   A 1 72  ? 9.047  14.488  11.288  1.00 18.36 ? 72  ASP   A OD2 1 
ATOM   643  N  N   . SER   A 1 73  ? 5.262  17.656  9.374   1.00 19.53 ? 73  SER   A N   1 
ATOM   644  C  CA  . SER   A 1 73  ? 5.326  19.117  9.400   1.00 21.26 ? 73  SER   A CA  1 
ATOM   645  C  C   . SER   A 1 73  ? 4.100  19.728  10.090  1.00 22.48 ? 73  SER   A C   1 
ATOM   646  O  O   . SER   A 1 73  ? 3.985  20.954  10.179  1.00 24.53 ? 73  SER   A O   1 
ATOM   647  C  CB  . SER   A 1 73  ? 5.540  19.675  8.028   1.00 23.39 ? 73  SER   A CB  1 
ATOM   648  O  OG  . SER   A 1 73  ? 4.408  19.470  7.213   1.00 23.54 ? 73  SER   A OG  1 
ATOM   649  N  N   . GLN   A 1 74  ? 3.156  18.884  10.522  1.00 24.22 ? 74  GLN   A N   1 
ATOM   650  C  CA  . GLN   A 1 74  ? 2.099  19.316  11.430  1.00 26.49 ? 74  GLN   A CA  1 
ATOM   651  C  C   . GLN   A 1 74  ? 1.581  18.095  12.179  1.00 24.86 ? 74  GLN   A C   1 
ATOM   652  O  O   . GLN   A 1 74  ? 2.023  17.019  11.879  1.00 22.08 ? 74  GLN   A O   1 
ATOM   653  C  CB  . GLN   A 1 74  ? 1.027  20.077  10.653  1.00 33.52 ? 74  GLN   A CB  1 
ATOM   654  C  CG  . GLN   A 1 74  ? 0.303  19.298  9.586   1.00 34.04 ? 74  GLN   A CG  1 
ATOM   655  C  CD  . GLN   A 1 74  ? -0.512 20.294  8.785   1.00 37.53 ? 74  GLN   A CD  1 
ATOM   656  O  OE1 . GLN   A 1 74  ? -1.052 21.274  9.320   1.00 37.49 ? 74  GLN   A OE1 1 
ATOM   657  N  NE2 . GLN   A 1 74  ? -0.563 20.085  7.478   1.00 34.92 ? 74  GLN   A NE2 1 
ATOM   658  N  N   A ASP   A 1 75  ? 0.628  18.195  13.122  0.50 26.57 ? 75  ASP   A N   1 
ATOM   659  N  N   B ASP   A 1 75  ? 0.814  18.384  13.241  0.50 26.73 ? 75  ASP   A N   1 
ATOM   660  C  CA  A ASP   A 1 75  ? 0.359  17.066  14.019  0.50 26.89 ? 75  ASP   A CA  1 
ATOM   661  C  CA  B ASP   A 1 75  ? 0.210  17.369  14.076  0.50 26.55 ? 75  ASP   A CA  1 
ATOM   662  C  C   A ASP   A 1 75  ? -0.614 16.036  13.416  0.50 24.45 ? 75  ASP   A C   1 
ATOM   663  C  C   B ASP   A 1 75  ? -0.820 16.640  13.229  0.50 22.82 ? 75  ASP   A C   1 
ATOM   664  O  O   A ASP   A 1 75  ? -1.674 15.763  13.979  0.50 27.94 ? 75  ASP   A O   1 
ATOM   665  O  O   B ASP   A 1 75  ? -1.908 17.121  12.955  0.50 24.33 ? 75  ASP   A O   1 
ATOM   666  C  CB  A ASP   A 1 75  ? -0.202 17.514  15.374  0.50 25.75 ? 75  ASP   A CB  1 
ATOM   667  C  CB  B ASP   A 1 75  ? -0.386 17.911  15.380  0.50 29.57 ? 75  ASP   A CB  1 
ATOM   668  C  CG  A ASP   A 1 75  ? 0.761  18.143  16.381  0.50 25.10 ? 75  ASP   A CG  1 
ATOM   669  C  CG  B ASP   A 1 75  ? 0.634  18.144  16.483  0.50 27.99 ? 75  ASP   A CG  1 
ATOM   670  O  OD1 A ASP   A 1 75  ? 2.006  18.316  16.106  0.50 23.34 ? 75  ASP   A OD1 1 
ATOM   671  O  OD1 B ASP   A 1 75  ? 1.476  17.227  16.737  0.50 25.26 ? 75  ASP   A OD1 1 
ATOM   672  O  OD2 A ASP   A 1 75  ? 0.259  18.440  17.478  0.50 26.96 ? 75  ASP   A OD2 1 
ATOM   673  O  OD2 B ASP   A 1 75  ? 0.561  19.229  17.104  0.50 32.09 ? 75  ASP   A OD2 1 
ATOM   674  N  N   A LYS   A 1 76  ? -0.177 15.347  12.362  0.50 22.22 ? 76  LYS   A N   1 
ATOM   675  N  N   B LYS   A 1 76  ? -0.417 15.467  12.793  0.50 20.32 ? 76  LYS   A N   1 
ATOM   676  C  CA  A LYS   A 1 76  ? -0.995 14.447  11.552  0.50 21.47 ? 76  LYS   A CA  1 
ATOM   677  C  CA  B LYS   A 1 76  ? -1.312 14.536  12.155  0.50 22.33 ? 76  LYS   A CA  1 
ATOM   678  C  C   A LYS   A 1 76  ? -1.215 13.062  12.181  0.50 20.78 ? 76  LYS   A C   1 
ATOM   679  C  C   B LYS   A 1 76  ? -1.245 13.240  12.942  0.50 23.52 ? 76  LYS   A C   1 
ATOM   680  O  O   A LYS   A 1 76  ? -2.210 12.411  11.972  0.50 21.71 ? 76  LYS   A O   1 
ATOM   681  O  O   B LYS   A 1 76  ? -2.082 12.973  13.803  0.50 26.05 ? 76  LYS   A O   1 
ATOM   682  C  CB  A LYS   A 1 76  ? -0.283 14.254  10.207  0.50 22.31 ? 76  LYS   A CB  1 
ATOM   683  C  CB  B LYS   A 1 76  ? -0.889 14.356  10.701  0.50 22.85 ? 76  LYS   A CB  1 
ATOM   684  C  CG  A LYS   A 1 76  ? -0.336 15.458  9.280   0.50 24.09 ? 76  LYS   A CG  1 
ATOM   685  C  CG  B LYS   A 1 76  ? -1.166 15.529  9.779   0.50 24.13 ? 76  LYS   A CG  1 
ATOM   686  C  CD  A LYS   A 1 76  ? 0.140  15.189  7.869   0.50 25.05 ? 76  LYS   A CD  1 
ATOM   687  C  CD  B LYS   A 1 76  ? -0.644 15.255  8.397   0.50 23.67 ? 76  LYS   A CD  1 
ATOM   688  C  CE  A LYS   A 1 76  ? -0.376 16.239  6.910   0.50 26.21 ? 76  LYS   A CE  1 
ATOM   689  C  CE  B LYS   A 1 76  ? -0.903 16.370  7.415   0.50 24.16 ? 76  LYS   A CE  1 
ATOM   690  N  NZ  A LYS   A 1 76  ? -0.048 15.916  5.506   0.50 28.19 ? 76  LYS   A NZ  1 
ATOM   691  N  NZ  B LYS   A 1 76  ? -0.562 15.957  6.039   0.50 23.24 ? 76  LYS   A NZ  1 
ATOM   692  N  N   . ALA   A 1 77  ? -0.176 12.489  12.731  1.00 23.08 ? 77  ALA   A N   1 
ATOM   693  C  CA  . ALA   A 1 77  ? -0.140 11.177  13.349  1.00 19.29 ? 77  ALA   A CA  1 
ATOM   694  C  C   . ALA   A 1 77  ? 0.658  11.322  14.633  1.00 17.92 ? 77  ALA   A C   1 
ATOM   695  O  O   . ALA   A 1 77  ? 1.869  11.598  14.550  1.00 21.98 ? 77  ALA   A O   1 
ATOM   696  C  CB  . ALA   A 1 77  ? 0.534  10.226  12.400  1.00 21.57 ? 77  ALA   A CB  1 
ATOM   697  N  N   . VAL   A 1 78  ? 0.005  11.175  15.789  1.00 17.40 ? 78  VAL   A N   1 
ATOM   698  C  CA  . VAL   A 1 78  ? 0.665  11.457  17.049  1.00 17.77 ? 78  VAL   A CA  1 
ATOM   699  C  C   . VAL   A 1 78  ? 0.388  10.383  18.095  1.00 16.59 ? 78  VAL   A C   1 
ATOM   700  O  O   . VAL   A 1 78  ? -0.630 9.683   18.099  1.00 18.95 ? 78  VAL   A O   1 
ATOM   701  C  CB  . VAL   A 1 78  ? 0.239  12.817  17.603  1.00 20.61 ? 78  VAL   A CB  1 
ATOM   702  C  CG1 . VAL   A 1 78  ? 0.505  13.931  16.618  1.00 21.95 ? 78  VAL   A CG1 1 
ATOM   703  C  CG2 . VAL   A 1 78  ? -1.206 12.784  18.023  1.00 21.25 ? 78  VAL   A CG2 1 
ATOM   704  N  N   . LEU   A 1 79  ? 1.363  10.320  19.005  1.00 14.48 ? 79  LEU   A N   1 
ATOM   705  C  CA  . LEU   A 1 79  ? 1.379  9.486   20.174  1.00 14.90 ? 79  LEU   A CA  1 
ATOM   706  C  C   . LEU   A 1 79  ? 1.349  10.385  21.384  1.00 15.49 ? 79  LEU   A C   1 
ATOM   707  O  O   . LEU   A 1 79  ? 2.146  11.306  21.474  1.00 16.71 ? 79  LEU   A O   1 
ATOM   708  C  CB  . LEU   A 1 79  ? 2.628  8.617   20.081  1.00 14.79 ? 79  LEU   A CB  1 
ATOM   709  C  CG  . LEU   A 1 79  ? 2.794  7.537   21.111  1.00 17.06 ? 79  LEU   A CG  1 
ATOM   710  C  CD1 . LEU   A 1 79  ? 1.719  6.494   20.969  1.00 19.45 ? 79  LEU   A CD1 1 
ATOM   711  C  CD2 . LEU   A 1 79  ? 4.131  6.890   20.975  1.00 16.07 ? 79  LEU   A CD2 1 
ATOM   712  N  N   A LYS   A 1 80  ? 0.428  10.077  22.301  0.50 16.01 ? 80  LYS   A N   1 
ATOM   713  N  N   B LYS   A 1 80  ? 0.494  10.058  22.341  0.50 16.43 ? 80  LYS   A N   1 
ATOM   714  C  CA  A LYS   A 1 80  ? 0.225  10.816  23.538  0.50 16.64 ? 80  LYS   A CA  1 
ATOM   715  C  CA  B LYS   A 1 80  ? 0.527  10.739  23.619  0.50 17.13 ? 80  LYS   A CA  1 
ATOM   716  C  C   A LYS   A 1 80  ? -0.092 9.833   24.660  0.50 16.96 ? 80  LYS   A C   1 
ATOM   717  C  C   B LYS   A 1 80  ? -0.051 9.816   24.678  0.50 16.99 ? 80  LYS   A C   1 
ATOM   718  O  O   A LYS   A 1 80  ? -0.325 8.664   24.405  0.50 16.94 ? 80  LYS   A O   1 
ATOM   719  O  O   B LYS   A 1 80  ? -0.425 8.691   24.395  0.50 17.09 ? 80  LYS   A O   1 
ATOM   720  C  CB  A LYS   A 1 80  ? -0.930 11.806  23.366  0.50 17.54 ? 80  LYS   A CB  1 
ATOM   721  C  CB  B LYS   A 1 80  ? -0.255 12.049  23.529  0.50 18.77 ? 80  LYS   A CB  1 
ATOM   722  C  CG  A LYS   A 1 80  ? -0.697 12.878  22.310  0.50 17.85 ? 80  LYS   A CG  1 
ATOM   723  C  CG  B LYS   A 1 80  ? -1.760 11.892  23.366  0.50 18.93 ? 80  LYS   A CG  1 
ATOM   724  N  N   . GLY   A 1 81  ? -0.158 10.327  25.903  1.00 17.48 ? 81  GLY   A N   1 
ATOM   725  C  CA  . GLY   A 1 81  ? -0.617 9.542   27.033  1.00 18.22 ? 81  GLY   A CA  1 
ATOM   726  C  C   . GLY   A 1 81  ? 0.408  8.482   27.404  1.00 17.53 ? 81  GLY   A C   1 
ATOM   727  O  O   . GLY   A 1 81  ? 1.594  8.624   27.107  1.00 16.44 ? 81  GLY   A O   1 
ATOM   728  N  N   . GLY   A 1 82  ? -0.063 7.432   28.060  1.00 20.62 ? 82  GLY   A N   1 
ATOM   729  C  CA  . GLY   A 1 82  ? 0.880  6.476   28.615  1.00 22.27 ? 82  GLY   A CA  1 
ATOM   730  C  C   . GLY   A 1 82  ? 1.904  7.155   29.507  1.00 21.63 ? 82  GLY   A C   1 
ATOM   731  O  O   . GLY   A 1 82  ? 1.573  7.968   30.370  1.00 24.86 ? 82  GLY   A O   1 
ATOM   732  N  N   . PRO   A 1 83  ? 3.208  6.861   29.318  1.00 18.15 ? 83  PRO   A N   1 
ATOM   733  C  CA  . PRO   A 1 83  ? 4.234  7.483   30.137  1.00 18.16 ? 83  PRO   A CA  1 
ATOM   734  C  C   . PRO   A 1 83  ? 4.617  8.868   29.641  1.00 17.02 ? 83  PRO   A C   1 
ATOM   735  O  O   . PRO   A 1 83  ? 5.477  9.499   30.224  1.00 23.09 ? 83  PRO   A O   1 
ATOM   736  C  CB  . PRO   A 1 83  ? 5.399  6.506   29.918  1.00 17.06 ? 83  PRO   A CB  1 
ATOM   737  C  CG  . PRO   A 1 83  ? 5.246  6.106   28.448  1.00 16.49 ? 83  PRO   A CG  1 
ATOM   738  C  CD  . PRO   A 1 83  ? 3.755  5.962   28.287  1.00 16.88 ? 83  PRO   A CD  1 
ATOM   739  N  N   . LEU   A 1 84  ? 4.018  9.333   28.532  1.00 15.49 ? 84  LEU   A N   1 
ATOM   740  C  CA  . LEU   A 1 84  ? 4.492  10.540  27.877  1.00 14.80 ? 84  LEU   A CA  1 
ATOM   741  C  C   . LEU   A 1 84  ? 3.806  11.772  28.449  1.00 17.36 ? 84  LEU   A C   1 
ATOM   742  O  O   . LEU   A 1 84  ? 2.619  11.766  28.760  1.00 20.48 ? 84  LEU   A O   1 
ATOM   743  C  CB  . LEU   A 1 84  ? 4.197  10.442  26.381  1.00 14.57 ? 84  LEU   A CB  1 
ATOM   744  C  CG  . LEU   A 1 84  ? 4.771  9.213   25.684  1.00 13.79 ? 84  LEU   A CG  1 
ATOM   745  C  CD1 . LEU   A 1 84  ? 4.296  9.130   24.253  1.00 14.98 ? 84  LEU   A CD1 1 
ATOM   746  C  CD2 . LEU   A 1 84  ? 6.311  9.202   25.724  1.00 14.22 ? 84  LEU   A CD2 1 
ATOM   747  N  N   . ASP   A 1 85  ? 4.570  12.861  28.460  1.00 17.45 ? 85  ASP   A N   1 
ATOM   748  C  CA  . ASP   A 1 85  ? 4.052  14.191  28.727  1.00 20.77 ? 85  ASP   A CA  1 
ATOM   749  C  C   . ASP   A 1 85  ? 4.154  14.912  27.392  1.00 23.43 ? 85  ASP   A C   1 
ATOM   750  O  O   . ASP   A 1 85  ? 5.223  14.938  26.777  1.00 29.02 ? 85  ASP   A O   1 
ATOM   751  C  CB  . ASP   A 1 85  ? 4.923  14.927  29.748  1.00 25.79 ? 85  ASP   A CB  1 
ATOM   752  C  CG  . ASP   A 1 85  ? 4.841  14.367  31.147  1.00 35.31 ? 85  ASP   A CG  1 
ATOM   753  O  OD1 . ASP   A 1 85  ? 3.811  13.715  31.457  1.00 42.79 ? 85  ASP   A OD1 1 
ATOM   754  O  OD2 . ASP   A 1 85  ? 5.837  14.580  31.921  1.00 45.07 ? 85  ASP   A OD2 1 
ATOM   755  N  N   . GLY   A 1 86  ? 3.064  15.458  26.911  1.00 25.52 ? 86  GLY   A N   1 
ATOM   756  C  CA  . GLY   A 1 86  ? 3.085  16.168  25.660  1.00 25.60 ? 86  GLY   A CA  1 
ATOM   757  C  C   . GLY   A 1 86  ? 2.816  15.241  24.476  1.00 22.73 ? 86  GLY   A C   1 
ATOM   758  O  O   . GLY   A 1 86  ? 2.346  14.108  24.591  1.00 26.40 ? 86  GLY   A O   1 
ATOM   759  N  N   . THR   A 1 87  ? 3.083  15.799  23.313  1.00 19.15 ? 87  THR   A N   1 
ATOM   760  C  CA  . THR   A 1 87  ? 2.639  15.253  22.053  1.00 18.27 ? 87  THR   A CA  1 
ATOM   761  C  C   . THR   A 1 87  ? 3.854  14.829  21.255  1.00 16.11 ? 87  THR   A C   1 
ATOM   762  O  O   . THR   A 1 87  ? 4.794  15.615  21.131  1.00 16.88 ? 87  THR   A O   1 
ATOM   763  C  CB  . THR   A 1 87  ? 1.858  16.308  21.255  1.00 21.84 ? 87  THR   A CB  1 
ATOM   764  O  OG1 . THR   A 1 87  ? 0.694  16.621  22.012  1.00 27.91 ? 87  THR   A OG1 1 
ATOM   765  C  CG2 . THR   A 1 87  ? 1.481  15.838  19.860  1.00 22.19 ? 87  THR   A CG2 1 
ATOM   766  N  N   . TYR   A 1 88  ? 3.811  13.616  20.732  1.00 15.11 ? 88  TYR   A N   1 
ATOM   767  C  CA  . TYR   A 1 88  ? 4.920  13.079  19.980  1.00 14.02 ? 88  TYR   A CA  1 
ATOM   768  C  C   . TYR   A 1 88  ? 4.446  12.757  18.566  1.00 14.56 ? 88  TYR   A C   1 
ATOM   769  O  O   . TYR   A 1 88  ? 3.487  12.007  18.388  1.00 19.12 ? 88  TYR   A O   1 
ATOM   770  C  CB  . TYR   A 1 88  ? 5.568  11.848  20.590  1.00 14.31 ? 88  TYR   A CB  1 
ATOM   771  C  CG  . TYR   A 1 88  ? 6.327  12.131  21.872  1.00 13.45 ? 88  TYR   A CG  1 
ATOM   772  C  CD1 . TYR   A 1 88  ? 5.709  12.536  23.036  1.00 13.82 ? 88  TYR   A CD1 1 
ATOM   773  C  CD2 . TYR   A 1 88  ? 7.691  11.862  21.937  1.00 13.11 ? 88  TYR   A CD2 1 
ATOM   774  C  CE1 . TYR   A 1 88  ? 6.424  12.780  24.204  1.00 14.00 ? 88  TYR   A CE1 1 
ATOM   775  C  CE2 . TYR   A 1 88  ? 8.400  12.058  23.092  1.00 13.07 ? 88  TYR   A CE2 1 
ATOM   776  C  CZ  . TYR   A 1 88  ? 7.775  12.466  24.236  1.00 13.43 ? 88  TYR   A CZ  1 
ATOM   777  O  OH  . TYR   A 1 88  ? 8.492  12.587  25.407  1.00 13.90 ? 88  TYR   A OH  1 
ATOM   778  N  N   A ARG   A 1 89  ? 5.086  13.369  17.547  0.50 13.55 ? 89  ARG   A N   1 
ATOM   779  N  N   B ARG   A 1 89  ? 5.156  13.229  17.569  0.50 13.41 ? 89  ARG   A N   1 
ATOM   780  C  CA  A ARG   A 1 89  ? 4.741  13.220  16.124  0.50 14.57 ? 89  ARG   A CA  1 
ATOM   781  C  CA  B ARG   A 1 89  ? 4.651  13.122  16.218  0.50 13.89 ? 89  ARG   A CA  1 
ATOM   782  C  C   A ARG   A 1 89  ? 5.448  12.026  15.488  0.50 12.50 ? 89  ARG   A C   1 
ATOM   783  C  C   B ARG   A 1 89  ? 5.437  12.081  15.430  0.50 12.30 ? 89  ARG   A C   1 
ATOM   784  O  O   A ARG   A 1 89  ? 6.666  11.854  15.622  0.50 11.72 ? 89  ARG   A O   1 
ATOM   785  O  O   B ARG   A 1 89  ? 6.672  12.038  15.465  0.50 12.57 ? 89  ARG   A O   1 
ATOM   786  C  CB  A ARG   A 1 89  ? 5.209  14.397  15.243  0.50 16.28 ? 89  ARG   A CB  1 
ATOM   787  C  CB  B ARG   A 1 89  ? 4.738  14.519  15.624  0.50 15.00 ? 89  ARG   A CB  1 
ATOM   788  C  CG  A ARG   A 1 89  ? 4.350  15.663  15.263  0.50 16.98 ? 89  ARG   A CG  1 
ATOM   789  C  CG  B ARG   A 1 89  ? 4.036  14.661  14.285  0.50 15.09 ? 89  ARG   A CG  1 
ATOM   790  C  CD  A ARG   A 1 89  ? 4.845  16.731  14.277  0.50 18.03 ? 89  ARG   A CD  1 
ATOM   791  C  CD  B ARG   A 1 89  ? 4.218  16.084  13.802  0.50 15.62 ? 89  ARG   A CD  1 
ATOM   792  N  NE  A ARG   A 1 89  ? 4.228  18.035  14.484  0.50 19.91 ? 89  ARG   A NE  1 
ATOM   793  N  NE  B ARG   A 1 89  ? 3.591  17.101  14.660  0.50 16.38 ? 89  ARG   A NE  1 
ATOM   794  C  CZ  A ARG   A 1 89  ? 4.726  19.218  14.106  0.50 20.55 ? 89  ARG   A CZ  1 
ATOM   795  C  CZ  B ARG   A 1 89  ? 3.713  18.411  14.458  0.50 18.64 ? 89  ARG   A CZ  1 
ATOM   796  N  NH1 A ARG   A 1 89  ? 5.795  19.310  13.339  0.50 19.75 ? 89  ARG   A NH1 1 
ATOM   797  N  NH1 B ARG   A 1 89  ? 3.191  19.287  15.295  0.50 18.78 ? 89  ARG   A NH1 1 
ATOM   798  N  NH2 A ARG   A 1 89  ? 4.135  20.335  14.492  0.50 24.59 ? 89  ARG   A NH2 1 
ATOM   799  N  NH2 B ARG   A 1 89  ? 4.434  18.850  13.447  0.50 18.44 ? 89  ARG   A NH2 1 
ATOM   800  N  N   . LEU   A 1 90  ? 4.685  11.196  14.753  1.00 12.20 ? 90  LEU   A N   1 
ATOM   801  C  CA  . LEU   A 1 90  ? 5.256  10.102  13.984  1.00 11.57 ? 90  LEU   A CA  1 
ATOM   802  C  C   . LEU   A 1 90  ? 6.070  10.647  12.828  1.00 11.71 ? 90  LEU   A C   1 
ATOM   803  O  O   . LEU   A 1 90  ? 5.564  11.429  12.030  1.00 13.72 ? 90  LEU   A O   1 
ATOM   804  C  CB  . LEU   A 1 90  ? 4.136  9.206   13.424  1.00 11.77 ? 90  LEU   A CB  1 
ATOM   805  C  CG  . LEU   A 1 90  ? 4.587  8.036   12.548  1.00 12.52 ? 90  LEU   A CG  1 
ATOM   806  C  CD1 . LEU   A 1 90  ? 5.382  7.001   13.337  1.00 12.77 ? 90  LEU   A CD1 1 
ATOM   807  C  CD2 . LEU   A 1 90  ? 3.392  7.347   11.939  1.00 13.55 ? 90  LEU   A CD2 1 
ATOM   808  N  N   . THR   A 1 91  ? 7.336  10.208  12.695  1.00 11.40 ? 91  THR   A N   1 
ATOM   809  C  CA  . THR   A 1 91  ? 8.179  10.613  11.589  1.00 11.15 ? 91  THR   A CA  1 
ATOM   810  C  C   . THR   A 1 91  ? 8.528  9.458   10.649  1.00 10.60 ? 91  THR   A C   1 
ATOM   811  O  O   . THR   A 1 91  ? 8.670  9.674   9.455   1.00 11.18 ? 91  THR   A O   1 
ATOM   812  C  CB  . THR   A 1 91  ? 9.394  11.356  12.152  1.00 12.96 ? 91  THR   A CB  1 
ATOM   813  O  OG1 . THR   A 1 91  ? 10.113 11.889  11.044  1.00 16.48 ? 91  THR   A OG1 1 
ATOM   814  C  CG2 . THR   A 1 91  ? 10.322 10.506  12.987  1.00 12.87 ? 91  THR   A CG2 1 
ATOM   815  N  N   . GLN   A 1 92  ? 8.698  8.237   11.174  1.00 10.26 ? 92  GLN   A N   1 
ATOM   816  C  CA  . GLN   A 1 92  ? 9.088  7.128   10.352  1.00 10.13 ? 92  GLN   A CA  1 
ATOM   817  C  C   . GLN   A 1 92  ? 8.783  5.819   11.063  1.00 9.60  ? 92  GLN   A C   1 
ATOM   818  O  O   . GLN   A 1 92  ? 8.703  5.800   12.298  1.00 10.56 ? 92  GLN   A O   1 
ATOM   819  C  CB  . GLN   A 1 92  ? 10.565 7.168   9.911   1.00 11.58 ? 92  GLN   A CB  1 
ATOM   820  C  CG  . GLN   A 1 92  ? 11.551 7.231   11.090  1.00 11.61 ? 92  GLN   A CG  1 
ATOM   821  C  CD  . GLN   A 1 92  ? 12.317 5.960   11.275  1.00 11.92 ? 92  GLN   A CD  1 
ATOM   822  O  OE1 . GLN   A 1 92  ? 11.800 4.858   11.111  1.00 12.29 ? 92  GLN   A OE1 1 
ATOM   823  N  NE2 . GLN   A 1 92  ? 13.547 6.114   11.710  1.00 14.24 ? 92  GLN   A NE2 1 
ATOM   824  N  N   . PHE   A 1 93  ? 8.652  4.736   10.282  1.00 9.98  ? 93  PHE   A N   1 
ATOM   825  C  CA  . PHE   A 1 93  ? 8.761  3.416   10.863  1.00 10.24 ? 93  PHE   A CA  1 
ATOM   826  C  C   . PHE   A 1 93  ? 9.759  2.569   10.068  1.00 9.70  ? 93  PHE   A C   1 
ATOM   827  O  O   . PHE   A 1 93  ? 10.010 2.781   8.870   1.00 10.57 ? 93  PHE   A O   1 
ATOM   828  C  CB  . PHE   A 1 93  ? 7.426  2.687   11.049  1.00 9.61  ? 93  PHE   A CB  1 
ATOM   829  C  CG  . PHE   A 1 93  ? 6.717  2.253   9.788   1.00 10.21 ? 93  PHE   A CG  1 
ATOM   830  C  CD1 . PHE   A 1 93  ? 7.137  1.181   9.078   1.00 10.80 ? 93  PHE   A CD1 1 
ATOM   831  C  CD2 . PHE   A 1 93  ? 5.559  2.880   9.397   1.00 10.77 ? 93  PHE   A CD2 1 
ATOM   832  C  CE1 . PHE   A 1 93  ? 6.478  0.739   7.943   1.00 11.10 ? 93  PHE   A CE1 1 
ATOM   833  C  CE2 . PHE   A 1 93  ? 4.873  2.434   8.268   1.00 11.03 ? 93  PHE   A CE2 1 
ATOM   834  C  CZ  . PHE   A 1 93  ? 5.343  1.414   7.535   1.00 10.96 ? 93  PHE   A CZ  1 
ATOM   835  N  N   . HIS   A 1 94  ? 10.274 1.546   10.745  1.00 9.91  ? 94  HIS   A N   1 
ATOM   836  C  CA  . HIS   A 1 94  ? 11.174 0.587   10.144  1.00 9.93  ? 94  HIS   A CA  1 
ATOM   837  C  C   . HIS   A 1 94  ? 11.101 -0.700  10.945  1.00 9.30  ? 94  HIS   A C   1 
ATOM   838  O  O   . HIS   A 1 94  ? 10.450 -0.748  11.985  1.00 10.09 ? 94  HIS   A O   1 
ATOM   839  C  CB  . HIS   A 1 94  ? 12.612 1.128   10.079  1.00 10.34 ? 94  HIS   A CB  1 
ATOM   840  C  CG  . HIS   A 1 94  ? 13.144 1.398   11.458  1.00 10.30 ? 94  HIS   A CG  1 
ATOM   841  N  ND1 . HIS   A 1 94  ? 12.902 2.552   12.154  1.00 10.33 ? 94  HIS   A ND1 1 
ATOM   842  C  CD2 . HIS   A 1 94  ? 13.752 0.532   12.328  1.00 9.75  ? 94  HIS   A CD2 1 
ATOM   843  C  CE1 . HIS   A 1 94  ? 13.400 2.414   13.391  1.00 9.54  ? 94  HIS   A CE1 1 
ATOM   844  N  NE2 . HIS   A 1 94  ? 13.898 1.182   13.539  1.00 9.91  ? 94  HIS   A NE2 1 
ATOM   845  N  N   . PHE   A 1 95  ? 11.798 -1.722  10.470  1.00 10.47 ? 95  PHE   A N   1 
ATOM   846  C  CA  . PHE   A 1 95  ? 11.793 -3.019  11.131  1.00 9.85  ? 95  PHE   A CA  1 
ATOM   847  C  C   . PHE   A 1 95  ? 13.211 -3.547  11.347  1.00 9.68  ? 95  PHE   A C   1 
ATOM   848  O  O   . PHE   A 1 95  ? 14.163 -3.106  10.697  1.00 11.20 ? 95  PHE   A O   1 
ATOM   849  C  CB  . PHE   A 1 95  ? 11.068 -4.085  10.270  1.00 10.25 ? 95  PHE   A CB  1 
ATOM   850  C  CG  . PHE   A 1 95  ? 9.599  -3.823  10.003  1.00 10.28 ? 95  PHE   A CG  1 
ATOM   851  C  CD1 . PHE   A 1 95  ? 9.196  -2.940  9.051   1.00 11.47 ? 95  PHE   A CD1 1 
ATOM   852  C  CD2 . PHE   A 1 95  ? 8.634  -4.561  10.674  1.00 10.59 ? 95  PHE   A CD2 1 
ATOM   853  C  CE1 . PHE   A 1 95  ? 7.842  -2.765  8.767   1.00 12.22 ? 95  PHE   A CE1 1 
ATOM   854  C  CE2 . PHE   A 1 95  ? 7.285  -4.343  10.432  1.00 11.40 ? 95  PHE   A CE2 1 
ATOM   855  C  CZ  . PHE   A 1 95  ? 6.913  -3.468  9.464   1.00 12.11 ? 95  PHE   A CZ  1 
ATOM   856  N  N   . HIS   A 1 96  ? 13.322 -4.490  12.261  1.00 9.49  ? 96  HIS   A N   1 
ATOM   857  C  CA  . HIS   A 1 96  ? 14.500 -5.322  12.482  1.00 9.92  ? 96  HIS   A CA  1 
ATOM   858  C  C   . HIS   A 1 96  ? 14.026 -6.765  12.382  1.00 10.71 ? 96  HIS   A C   1 
ATOM   859  O  O   . HIS   A 1 96  ? 12.951 -7.091  12.868  1.00 10.50 ? 96  HIS   A O   1 
ATOM   860  C  CB  . HIS   A 1 96  ? 15.112 -5.054  13.866  1.00 10.42 ? 96  HIS   A CB  1 
ATOM   861  C  CG  . HIS   A 1 96  ? 15.429 -3.624  14.133  1.00 10.24 ? 96  HIS   A CG  1 
ATOM   862  N  ND1 . HIS   A 1 96  ? 16.646 -3.077  13.874  1.00 10.77 ? 96  HIS   A ND1 1 
ATOM   863  C  CD2 . HIS   A 1 96  ? 14.639 -2.612  14.530  1.00 9.79  ? 96  HIS   A CD2 1 
ATOM   864  C  CE1 . HIS   A 1 96  ? 16.594 -1.788  14.187  1.00 10.34 ? 96  HIS   A CE1 1 
ATOM   865  N  NE2 . HIS   A 1 96  ? 15.394 -1.444  14.572  1.00 9.60  ? 96  HIS   A NE2 1 
ATOM   866  N  N   . TRP   A 1 97  ? 14.834 -7.634  11.763  1.00 9.85  ? 97  TRP   A N   1 
ATOM   867  C  CA  . TRP   A 1 97  ? 14.396 -9.007  11.572  1.00 10.47 ? 97  TRP   A CA  1 
ATOM   868  C  C   . TRP   A 1 97  ? 15.591 -9.963  11.461  1.00 10.25 ? 97  TRP   A C   1 
ATOM   869  O  O   . TRP   A 1 97  ? 16.753 -9.526  11.381  1.00 11.13 ? 97  TRP   A O   1 
ATOM   870  C  CB  . TRP   A 1 97  ? 13.513 -9.132  10.311  1.00 10.41 ? 97  TRP   A CB  1 
ATOM   871  C  CG  . TRP   A 1 97  ? 14.193 -8.783  9.028   1.00 10.51 ? 97  TRP   A CG  1 
ATOM   872  C  CD1 . TRP   A 1 97  ? 14.892 -9.627  8.218   1.00 11.15 ? 97  TRP   A CD1 1 
ATOM   873  C  CD2 . TRP   A 1 97  ? 14.259 -7.477  8.425   1.00 10.30 ? 97  TRP   A CD2 1 
ATOM   874  N  NE1 . TRP   A 1 97  ? 15.357 -8.947  7.133   1.00 11.40 ? 97  TRP   A NE1 1 
ATOM   875  C  CE2 . TRP   A 1 97  ? 15.001 -7.627  7.235   1.00 11.36 ? 97  TRP   A CE2 1 
ATOM   876  C  CE3 . TRP   A 1 97  ? 13.779 -6.222  8.772   1.00 10.61 ? 97  TRP   A CE3 1 
ATOM   877  C  CZ2 . TRP   A 1 97  ? 15.272 -6.555  6.391   1.00 12.03 ? 97  TRP   A CZ2 1 
ATOM   878  C  CZ3 . TRP   A 1 97  ? 14.035 -5.163  7.925   1.00 11.19 ? 97  TRP   A CZ3 1 
ATOM   879  C  CH2 . TRP   A 1 97  ? 14.722 -5.341  6.736   1.00 11.77 ? 97  TRP   A CH2 1 
ATOM   880  N  N   . GLY   A 1 98  ? 15.290 -11.233 11.445  1.00 10.44 ? 98  GLY   A N   1 
ATOM   881  C  CA  . GLY   A 1 98  ? 16.281 -12.268 11.554  1.00 11.09 ? 98  GLY   A CA  1 
ATOM   882  C  C   . GLY   A 1 98  ? 16.496 -13.038 10.262  1.00 11.73 ? 98  GLY   A C   1 
ATOM   883  O  O   . GLY   A 1 98  ? 15.796 -12.852 9.260   1.00 12.39 ? 98  GLY   A O   1 
ATOM   884  N  N   . SER   A 1 99  ? 17.481 -13.922 10.272  1.00 12.52 ? 99  SER   A N   1 
ATOM   885  C  CA  . SER   A 1 99  ? 17.746 -14.897 9.215   1.00 13.68 ? 99  SER   A CA  1 
ATOM   886  C  C   . SER   A 1 99  ? 16.813 -16.121 9.290   1.00 13.74 ? 99  SER   A C   1 
ATOM   887  O  O   . SER   A 1 99  ? 16.708 -16.892 8.322   1.00 16.78 ? 99  SER   A O   1 
ATOM   888  C  CB  . SER   A 1 99  ? 19.189 -15.303 9.235   1.00 14.77 ? 99  SER   A CB  1 
ATOM   889  O  OG  . SER   A 1 99  ? 19.607 -15.750 10.515  1.00 15.43 ? 99  SER   A OG  1 
ATOM   890  N  N   . LEU   A 1 100 ? 16.228 -16.324 10.464  1.00 13.36 ? 100 LEU   A N   1 
ATOM   891  C  CA  . LEU   A 1 100 ? 15.369 -17.452 10.794  1.00 15.81 ? 100 LEU   A CA  1 
ATOM   892  C  C   . LEU   A 1 100 ? 14.234 -16.918 11.639  1.00 14.02 ? 100 LEU   A C   1 
ATOM   893  O  O   . LEU   A 1 100 ? 14.419 -15.906 12.306  1.00 14.16 ? 100 LEU   A O   1 
ATOM   894  C  CB  . LEU   A 1 100 ? 16.122 -18.488 11.668  1.00 19.90 ? 100 LEU   A CB  1 
ATOM   895  C  CG  . LEU   A 1 100 ? 17.312 -19.182 11.038  1.00 23.73 ? 100 LEU   A CG  1 
ATOM   896  C  CD1 . LEU   A 1 100 ? 18.129 -19.986 12.046  1.00 26.29 ? 100 LEU   A CD1 1 
ATOM   897  C  CD2 . LEU   A 1 100 ? 16.828 -20.131 9.959   1.00 27.55 ? 100 LEU   A CD2 1 
ATOM   898  N  N   . ASP   A 1 101 ? 13.117 -17.657 11.739  1.00 14.96 ? 101 ASP   A N   1 
ATOM   899  C  CA  . ASP   A 1 101 ? 11.978 -17.120 12.462  1.00 14.07 ? 101 ASP   A CA  1 
ATOM   900  C  C   . ASP   A 1 101 ? 12.216 -17.016 13.978  1.00 14.40 ? 101 ASP   A C   1 
ATOM   901  O  O   . ASP   A 1 101 ? 11.533 -16.259 14.660  1.00 16.60 ? 101 ASP   A O   1 
ATOM   902  C  CB  . ASP   A 1 101 ? 10.757 -18.004 12.233  1.00 15.33 ? 101 ASP   A CB  1 
ATOM   903  C  CG  . ASP   A 1 101 ? 10.222 -18.051 10.806  1.00 16.03 ? 101 ASP   A CG  1 
ATOM   904  O  OD1 . ASP   A 1 101 ? 10.645 -17.237 9.955   1.00 16.82 ? 101 ASP   A OD1 1 
ATOM   905  O  OD2 . ASP   A 1 101 ? 9.344  -18.923 10.552  1.00 18.73 ? 101 ASP   A OD2 1 
ATOM   906  N  N   . GLY   A 1 102 ? 13.214 -17.754 14.484  1.00 15.94 ? 102 GLY   A N   1 
ATOM   907  C  CA  . GLY   A 1 102 ? 13.519 -17.797 15.907  1.00 17.49 ? 102 GLY   A CA  1 
ATOM   908  C  C   . GLY   A 1 102 ? 14.369 -16.649 16.432  1.00 15.96 ? 102 GLY   A C   1 
ATOM   909  O  O   . GLY   A 1 102 ? 14.714 -16.649 17.619  1.00 17.82 ? 102 GLY   A O   1 
ATOM   910  N  N   A GLN   A 1 103 ? 14.688 -15.665 15.586  0.50 14.09 ? 103 GLN   A N   1 
ATOM   911  N  N   B GLN   A 1 103 ? 14.701 -15.668 15.590  0.50 14.97 ? 103 GLN   A N   1 
ATOM   912  C  CA  A GLN   A 1 103 ? 15.439 -14.489 16.012  0.50 12.20 ? 103 GLN   A CA  1 
ATOM   913  C  CA  B GLN   A 1 103 ? 15.411 -14.484 16.055  0.50 13.52 ? 103 GLN   A CA  1 
ATOM   914  C  C   A GLN   A 1 103 ? 14.999 -13.313 15.154  0.50 11.53 ? 103 GLN   A C   1 
ATOM   915  C  C   B GLN   A 1 103 ? 15.083 -13.328 15.123  0.50 12.52 ? 103 GLN   A C   1 
ATOM   916  O  O   A GLN   A 1 103 ? 14.385 -13.507 14.114  0.50 11.54 ? 103 GLN   A O   1 
ATOM   917  O  O   B GLN   A 1 103 ? 14.643 -13.550 14.003  0.50 13.08 ? 103 GLN   A O   1 
ATOM   918  C  CB  A GLN   A 1 103 ? 16.949 -14.752 15.928  0.50 12.20 ? 103 GLN   A CB  1 
ATOM   919  C  CB  B GLN   A 1 103 ? 16.915 -14.763 16.176  0.50 13.68 ? 103 GLN   A CB  1 
ATOM   920  C  CG  A GLN   A 1 103 ? 17.421 -15.047 14.509  0.50 12.20 ? 103 GLN   A CG  1 
ATOM   921  C  CG  B GLN   A 1 103 ? 17.628 -14.954 14.841  0.50 14.41 ? 103 GLN   A CG  1 
ATOM   922  C  CD  A GLN   A 1 103 ? 18.748 -15.752 14.464  0.50 13.78 ? 103 GLN   A CD  1 
ATOM   923  C  CD  B GLN   A 1 103 ? 19.062 -15.400 15.018  0.50 16.72 ? 103 GLN   A CD  1 
ATOM   924  O  OE1 A GLN   A 1 103 ? 19.715 -15.214 13.926  0.50 15.62 ? 103 GLN   A OE1 1 
ATOM   925  O  OE1 B GLN   A 1 103 ? 19.429 -16.120 15.946  0.50 17.64 ? 103 GLN   A OE1 1 
ATOM   926  N  NE2 A GLN   A 1 103 ? 18.834 -16.907 15.096  0.50 13.79 ? 103 GLN   A NE2 1 
ATOM   927  N  NE2 B GLN   A 1 103 ? 19.901 -14.940 14.104  0.50 17.65 ? 103 GLN   A NE2 1 
ATOM   928  N  N   . GLY   A 1 104 ? 15.389 -12.110 15.569  1.00 11.58 ? 104 GLY   A N   1 
ATOM   929  C  CA  . GLY   A 1 104 ? 15.121 -10.929 14.781  1.00 11.18 ? 104 GLY   A CA  1 
ATOM   930  C  C   . GLY   A 1 104 ? 14.678 -9.735  15.610  1.00 10.22 ? 104 GLY   A C   1 
ATOM   931  O  O   . GLY   A 1 104 ? 14.957 -8.614  15.214  1.00 11.74 ? 104 GLY   A O   1 
ATOM   932  N  N   . SER   A 1 105 ? 13.984 -9.957  16.723  1.00 10.32 ? 105 SER   A N   1 
ATOM   933  C  CA  . SER   A 1 105 ? 13.599 -8.834  17.568  1.00 10.36 ? 105 SER   A CA  1 
ATOM   934  C  C   . SER   A 1 105 ? 14.822 -8.276  18.324  1.00 10.15 ? 105 SER   A C   1 
ATOM   935  O  O   . SER   A 1 105 ? 15.860 -8.968  18.508  1.00 10.97 ? 105 SER   A O   1 
ATOM   936  C  CB  . SER   A 1 105 ? 12.465 -9.170  18.503  1.00 10.01 ? 105 SER   A CB  1 
ATOM   937  O  OG  . SER   A 1 105 ? 12.853 -10.114 19.485  1.00 10.45 ? 105 SER   A OG  1 
ATOM   938  N  N   . GLU   A 1 106 ? 14.676 -7.047  18.712  1.00 9.62  ? 106 GLU   A N   1 
ATOM   939  C  CA  . GLU   A 1 106 ? 15.682 -6.343  19.513  1.00 9.81  ? 106 GLU   A CA  1 
ATOM   940  C  C   . GLU   A 1 106 ? 15.357 -6.519  20.998  1.00 9.51  ? 106 GLU   A C   1 
ATOM   941  O  O   . GLU   A 1 106 ? 16.138 -7.096  21.756  1.00 10.32 ? 106 GLU   A O   1 
ATOM   942  C  CB  . GLU   A 1 106 ? 15.699 -4.873  19.064  1.00 9.75  ? 106 GLU   A CB  1 
ATOM   943  C  CG  . GLU   A 1 106 ? 16.121 -4.719  17.620  1.00 10.41 ? 106 GLU   A CG  1 
ATOM   944  C  CD  . GLU   A 1 106 ? 16.867 -3.458  17.326  1.00 9.75  ? 106 GLU   A CD  1 
ATOM   945  O  OE1 . GLU   A 1 106 ? 16.299 -2.410  17.581  1.00 9.84  ? 106 GLU   A OE1 1 
ATOM   946  O  OE2 . GLU   A 1 106 ? 18.017 -3.551  16.832  1.00 11.41 ? 106 GLU   A OE2 1 
ATOM   947  N  N   . HIS   A 1 107 ? 14.184 -6.032  21.422  1.00 9.34  ? 107 HIS   A N   1 
ATOM   948  C  CA  . HIS   A 1 107 ? 13.697 -6.402  22.724  1.00 9.46  ? 107 HIS   A CA  1 
ATOM   949  C  C   . HIS   A 1 107 ? 13.389 -7.897  22.771  1.00 9.81  ? 107 HIS   A C   1 
ATOM   950  O  O   . HIS   A 1 107 ? 13.064 -8.529  21.757  1.00 10.09 ? 107 HIS   A O   1 
ATOM   951  C  CB  . HIS   A 1 107 ? 12.466 -5.577  23.118  1.00 9.73  ? 107 HIS   A CB  1 
ATOM   952  C  CG  . HIS   A 1 107 ? 12.786 -4.140  23.250  1.00 9.53  ? 107 HIS   A CG  1 
ATOM   953  N  ND1 . HIS   A 1 107 ? 12.741 -3.251  22.199  1.00 9.71  ? 107 HIS   A ND1 1 
ATOM   954  C  CD2 . HIS   A 1 107 ? 13.237 -3.438  24.326  1.00 9.72  ? 107 HIS   A CD2 1 
ATOM   955  C  CE1 . HIS   A 1 107 ? 13.197 -2.070  22.647  1.00 9.21  ? 107 HIS   A CE1 1 
ATOM   956  N  NE2 . HIS   A 1 107 ? 13.492 -2.130  23.948  1.00 9.62  ? 107 HIS   A NE2 1 
ATOM   957  N  N   . THR   A 1 108 ? 13.515 -8.459  23.985  1.00 10.29 ? 108 THR   A N   1 
ATOM   958  C  CA  . THR   A 1 108 ? 13.126 -9.821  24.268  1.00 9.83  ? 108 THR   A CA  1 
ATOM   959  C  C   . THR   A 1 108 ? 12.187 -9.805  25.470  1.00 10.12 ? 108 THR   A C   1 
ATOM   960  O  O   . THR   A 1 108 ? 12.182 -8.846  26.243  1.00 11.15 ? 108 THR   A O   1 
ATOM   961  C  CB  . THR   A 1 108 ? 14.354 -10.721 24.446  1.00 10.80 ? 108 THR   A CB  1 
ATOM   962  O  OG1 . THR   A 1 108 ? 15.179 -10.244 25.513  1.00 11.48 ? 108 THR   A OG1 1 
ATOM   963  C  CG2 . THR   A 1 108 ? 15.169 -10.797 23.196  1.00 10.91 ? 108 THR   A CG2 1 
ATOM   964  N  N   . VAL   A 1 109 ? 11.410 -10.869 25.620  1.00 10.86 ? 109 VAL   A N   1 
ATOM   965  C  CA  . VAL   A 1 109 ? 10.437 -10.984 26.705  1.00 11.81 ? 109 VAL   A CA  1 
ATOM   966  C  C   . VAL   A 1 109 ? 10.752 -12.281 27.437  1.00 12.28 ? 109 VAL   A C   1 
ATOM   967  O  O   . VAL   A 1 109 ? 10.570 -13.371 26.894  1.00 12.57 ? 109 VAL   A O   1 
ATOM   968  C  CB  . VAL   A 1 109 ? 8.985  -10.953 26.191  1.00 11.91 ? 109 VAL   A CB  1 
ATOM   969  C  CG1 . VAL   A 1 109 ? 8.007  -11.057 27.356  1.00 13.08 ? 109 VAL   A CG1 1 
ATOM   970  C  CG2 . VAL   A 1 109 ? 8.742  -9.682  25.375  1.00 12.75 ? 109 VAL   A CG2 1 
ATOM   971  N  N   . ASP   A 1 110 ? 11.248 -12.172 28.679  1.00 11.90 ? 110 ASP   A N   1 
ATOM   972  C  CA  . ASP   A 1 110 ? 11.730 -13.345 29.397  1.00 13.19 ? 110 ASP   A CA  1 
ATOM   973  C  C   . ASP   A 1 110 ? 12.673 -14.173 28.529  1.00 13.25 ? 110 ASP   A C   1 
ATOM   974  O  O   . ASP   A 1 110 ? 12.593 -15.388 28.482  1.00 14.83 ? 110 ASP   A O   1 
ATOM   975  C  CB  . ASP   A 1 110 ? 10.567 -14.156 29.930  1.00 14.98 ? 110 ASP   A CB  1 
ATOM   976  C  CG  . ASP   A 1 110 ? 9.733  -13.388 30.936  1.00 15.04 ? 110 ASP   A CG  1 
ATOM   977  O  OD1 . ASP   A 1 110 ? 10.291 -12.484 31.588  1.00 16.77 ? 110 ASP   A OD1 1 
ATOM   978  O  OD2 . ASP   A 1 110 ? 8.545  -13.709 31.078  1.00 17.77 ? 110 ASP   A OD2 1 
ATOM   979  N  N   . LYS   A 1 111 ? 13.560 -13.457 27.829  1.00 12.41 ? 111 LYS   A N   1 
ATOM   980  C  CA  . LYS   A 1 111 ? 14.594 -13.992 26.929  1.00 13.49 ? 111 LYS   A CA  1 
ATOM   981  C  C   . LYS   A 1 111 ? 14.054 -14.495 25.594  1.00 13.11 ? 111 LYS   A C   1 
ATOM   982  O  O   . LYS   A 1 111 ? 14.861 -14.831 24.731  1.00 14.88 ? 111 LYS   A O   1 
ATOM   983  C  CB  . LYS   A 1 111 ? 15.493 -15.032 27.597  1.00 15.73 ? 111 LYS   A CB  1 
ATOM   984  C  CG  . LYS   A 1 111 ? 16.213 -14.516 28.828  1.00 18.44 ? 111 LYS   A CG  1 
ATOM   985  C  CD  . LYS   A 1 111 ? 17.177 -13.334 28.521  1.00 22.60 ? 111 LYS   A CD  1 
ATOM   986  C  CE  . LYS   A 1 111 ? 17.891 -12.690 29.709  1.00 25.58 ? 111 LYS   A CE  1 
ATOM   987  N  NZ  . LYS   A 1 111 ? 19.128 -13.383 30.077  1.00 30.31 ? 111 LYS   A NZ  1 
ATOM   988  N  N   . LYS   A 1 112 ? 12.732 -14.470 25.391  1.00 12.79 ? 112 LYS   A N   1 
ATOM   989  C  CA  . LYS   A 1 112 ? 12.179 -14.868 24.110  1.00 13.13 ? 112 LYS   A CA  1 
ATOM   990  C  C   . LYS   A 1 112 ? 12.448 -13.828 23.029  1.00 11.92 ? 112 LYS   A C   1 
ATOM   991  O  O   . LYS   A 1 112 ? 12.165 -12.650 23.207  1.00 12.19 ? 112 LYS   A O   1 
ATOM   992  C  CB  . LYS   A 1 112 ? 10.654 -15.030 24.191  1.00 14.50 ? 112 LYS   A CB  1 
ATOM   993  C  CG  . LYS   A 1 112 ? 9.977  -15.456 22.892  1.00 17.10 ? 112 LYS   A CG  1 
ATOM   994  C  CD  . LYS   A 1 112 ? 8.468  -15.505 23.015  1.00 20.88 ? 112 LYS   A CD  1 
ATOM   995  C  CE  . LYS   A 1 112 ? 7.809  -15.711 21.671  1.00 24.07 ? 112 LYS   A CE  1 
ATOM   996  N  NZ  . LYS   A 1 112 ? 8.227  -16.953 21.002  1.00 27.01 ? 112 LYS   A NZ  1 
ATOM   997  N  N   A LYS   A 1 113 ? 13.026 -14.309 21.928  0.50 12.10 ? 113 LYS   A N   1 
ATOM   998  N  N   B LYS   A 1 113 ? 12.962 -14.314 21.900  0.50 12.03 ? 113 LYS   A N   1 
ATOM   999  C  CA  A LYS   A 1 113 ? 13.182 -13.534 20.713  0.50 12.67 ? 113 LYS   A CA  1 
ATOM   1000 C  CA  B LYS   A 1 113 ? 13.180 -13.498 20.720  0.50 12.57 ? 113 LYS   A CA  1 
ATOM   1001 C  C   A LYS   A 1 113 ? 11.972 -13.768 19.817  0.50 12.20 ? 113 LYS   A C   1 
ATOM   1002 C  C   B LYS   A 1 113 ? 12.105 -13.774 19.683  0.50 11.90 ? 113 LYS   A C   1 
ATOM   1003 O  O   A LYS   A 1 113 ? 11.443 -14.874 19.695  0.50 12.63 ? 113 LYS   A O   1 
ATOM   1004 O  O   B LYS   A 1 113 ? 11.860 -14.913 19.284  0.50 12.11 ? 113 LYS   A O   1 
ATOM   1005 C  CB  A LYS   A 1 113 ? 14.453 -13.938 19.967  0.50 13.33 ? 113 LYS   A CB  1 
ATOM   1006 C  CB  B LYS   A 1 113 ? 14.515 -13.822 20.066  0.50 13.25 ? 113 LYS   A CB  1 
ATOM   1007 C  CG  A LYS   A 1 113 ? 15.752 -13.763 20.749  0.50 13.68 ? 113 LYS   A CG  1 
ATOM   1008 C  CG  B LYS   A 1 113 ? 15.714 -13.361 20.868  0.50 13.70 ? 113 LYS   A CG  1 
ATOM   1009 C  CD  A LYS   A 1 113 ? 16.960 -14.259 19.962  0.50 14.38 ? 113 LYS   A CD  1 
ATOM   1010 C  CD  B LYS   A 1 113 ? 16.969 -14.048 20.451  0.50 15.12 ? 113 LYS   A CD  1 
ATOM   1011 C  CE  A LYS   A 1 113 ? 18.300 -13.870 20.569  0.50 15.18 ? 113 LYS   A CE  1 
ATOM   1012 C  CE  B LYS   A 1 113 ? 18.166 -13.438 21.141  0.50 16.72 ? 113 LYS   A CE  1 
ATOM   1013 N  NZ  A LYS   A 1 113 ? 18.530 -14.432 21.930  0.50 15.36 ? 113 LYS   A NZ  1 
ATOM   1014 N  NZ  B LYS   A 1 113 ? 19.381 -14.246 20.924  0.50 17.64 ? 113 LYS   A NZ  1 
ATOM   1015 N  N   . TYR   A 1 114 ? 11.514 -12.690 19.188  1.00 11.16 ? 114 TYR   A N   1 
ATOM   1016 C  CA  . TYR   A 1 114 ? 10.504 -12.779 18.137  1.00 11.12 ? 114 TYR   A CA  1 
ATOM   1017 C  C   . TYR   A 1 114 ? 11.178 -12.732 16.775  1.00 11.50 ? 114 TYR   A C   1 
ATOM   1018 O  O   . TYR   A 1 114 ? 12.375 -12.450 16.639  1.00 11.79 ? 114 TYR   A O   1 
ATOM   1019 C  CB  . TYR   A 1 114 ? 9.463  -11.677 18.272  1.00 11.35 ? 114 TYR   A CB  1 
ATOM   1020 C  CG  . TYR   A 1 114 ? 8.541  -11.854 19.463  1.00 11.09 ? 114 TYR   A CG  1 
ATOM   1021 C  CD1 . TYR   A 1 114 ? 8.843  -11.424 20.741  1.00 12.86 ? 114 TYR   A CD1 1 
ATOM   1022 C  CD2 . TYR   A 1 114 ? 7.374  -12.580 19.316  1.00 13.01 ? 114 TYR   A CD2 1 
ATOM   1023 C  CE1 . TYR   A 1 114 ? 7.963  -11.619 21.793  1.00 14.68 ? 114 TYR   A CE1 1 
ATOM   1024 C  CE2 . TYR   A 1 114 ? 6.484  -12.741 20.356  1.00 14.61 ? 114 TYR   A CE2 1 
ATOM   1025 C  CZ  . TYR   A 1 114 ? 6.783  -12.301 21.608  1.00 15.49 ? 114 TYR   A CZ  1 
ATOM   1026 O  OH  . TYR   A 1 114 ? 5.944  -12.429 22.688  1.00 20.03 ? 114 TYR   A OH  1 
ATOM   1027 N  N   . ALA   A 1 115 ? 10.417 -13.014 15.701  1.00 11.14 ? 115 ALA   A N   1 
ATOM   1028 C  CA  . ALA   A 1 115 ? 10.934 -13.041 14.342  1.00 11.62 ? 115 ALA   A CA  1 
ATOM   1029 C  C   . ALA   A 1 115 ? 11.353 -11.666 13.845  1.00 11.12 ? 115 ALA   A C   1 
ATOM   1030 O  O   . ALA   A 1 115 ? 12.206 -11.545 12.971  1.00 11.58 ? 115 ALA   A O   1 
ATOM   1031 C  CB  . ALA   A 1 115 ? 9.904  -13.658 13.401  1.00 12.36 ? 115 ALA   A CB  1 
ATOM   1032 N  N   . ALA   A 1 116 ? 10.723 -10.635 14.349  1.00 10.22 ? 116 ALA   A N   1 
ATOM   1033 C  CA  . ALA   A 1 116 ? 11.023 -9.276  13.917  1.00 10.23 ? 116 ALA   A CA  1 
ATOM   1034 C  C   . ALA   A 1 116 ? 10.416 -8.288  14.917  1.00 9.68  ? 116 ALA   A C   1 
ATOM   1035 O  O   . ALA   A 1 116 ? 9.703  -8.673  15.830  1.00 10.12 ? 116 ALA   A O   1 
ATOM   1036 C  CB  . ALA   A 1 116 ? 10.480 -8.998  12.507  1.00 10.21 ? 116 ALA   A CB  1 
ATOM   1037 N  N   . GLU   A 1 117 ? 10.772 -7.020  14.741  1.00 9.32  ? 117 GLU   A N   1 
ATOM   1038 C  CA  . GLU   A 1 117 ? 10.278 -5.962  15.604  1.00 9.47  ? 117 GLU   A CA  1 
ATOM   1039 C  C   . GLU   A 1 117 ? 10.098 -4.735  14.725  1.00 9.28  ? 117 GLU   A C   1 
ATOM   1040 O  O   . GLU   A 1 117 ? 11.007 -4.320  14.007  1.00 10.57 ? 117 GLU   A O   1 
ATOM   1041 C  CB  . GLU   A 1 117 ? 11.236 -5.712  16.770  1.00 9.72  ? 117 GLU   A CB  1 
ATOM   1042 C  CG  . GLU   A 1 117 ? 10.698 -4.755  17.850  1.00 9.42  ? 117 GLU   A CG  1 
ATOM   1043 C  CD  . GLU   A 1 117 ? 11.622 -4.691  19.061  1.00 9.76  ? 117 GLU   A CD  1 
ATOM   1044 O  OE1 . GLU   A 1 117 ? 12.254 -5.736  19.378  1.00 10.36 ? 117 GLU   A OE1 1 
ATOM   1045 O  OE2 . GLU   A 1 117 ? 11.710 -3.615  19.686  1.00 10.46 ? 117 GLU   A OE2 1 
ATOM   1046 N  N   . LEU   A 1 118 ? 8.929  -4.109  14.844  1.00 9.10  ? 118 LEU   A N   1 
ATOM   1047 C  CA  . LEU   A 1 118 ? 8.541  -2.867  14.199  1.00 9.08  ? 118 LEU   A CA  1 
ATOM   1048 C  C   . LEU   A 1 118 ? 8.759  -1.721  15.182  1.00 8.81  ? 118 LEU   A C   1 
ATOM   1049 O  O   . LEU   A 1 118 ? 8.352  -1.806  16.330  1.00 9.11  ? 118 LEU   A O   1 
ATOM   1050 C  CB  . LEU   A 1 118 ? 7.045  -2.964  13.824  1.00 10.10 ? 118 LEU   A CB  1 
ATOM   1051 C  CG  . LEU   A 1 118 ? 6.320  -1.663  13.462  1.00 10.00 ? 118 LEU   A CG  1 
ATOM   1052 C  CD1 . LEU   A 1 118 ? 6.908  -1.020  12.223  1.00 10.08 ? 118 LEU   A CD1 1 
ATOM   1053 C  CD2 . LEU   A 1 118 ? 4.838  -1.968  13.220  1.00 11.04 ? 118 LEU   A CD2 1 
ATOM   1054 N  N   . HIS   A 1 119 ? 9.398  -0.647  14.684  1.00 8.47  ? 119 HIS   A N   1 
ATOM   1055 C  CA  . HIS   A 1 119 ? 9.618  0.558   15.462  1.00 9.23  ? 119 HIS   A CA  1 
ATOM   1056 C  C   . HIS   A 1 119 ? 8.942  1.732   14.746  1.00 8.74  ? 119 HIS   A C   1 
ATOM   1057 O  O   . HIS   A 1 119 ? 9.320  2.085   13.624  1.00 9.85  ? 119 HIS   A O   1 
ATOM   1058 C  CB  . HIS   A 1 119 ? 11.120 0.832   15.575  1.00 9.11  ? 119 HIS   A CB  1 
ATOM   1059 C  CG  . HIS   A 1 119 ? 11.810 -0.120  16.456  1.00 9.04  ? 119 HIS   A CG  1 
ATOM   1060 N  ND1 . HIS   A 1 119 ? 13.175 -0.347  16.430  1.00 8.93  ? 119 HIS   A ND1 1 
ATOM   1061 C  CD2 . HIS   A 1 119 ? 11.274 -0.912  17.404  1.00 9.30  ? 119 HIS   A CD2 1 
ATOM   1062 C  CE1 . HIS   A 1 119 ? 13.446 -1.224  17.358  1.00 9.14  ? 119 HIS   A CE1 1 
ATOM   1063 N  NE2 . HIS   A 1 119 ? 12.326 -1.655  17.966  1.00 9.61  ? 119 HIS   A NE2 1 
ATOM   1064 N  N   . LEU   A 1 120 ? 7.973  2.331   15.441  1.00 8.97  ? 120 LEU   A N   1 
ATOM   1065 C  CA  . LEU   A 1 120 ? 7.306  3.553   15.028  1.00 9.36  ? 120 LEU   A CA  1 
ATOM   1066 C  C   . LEU   A 1 120 ? 7.945  4.681   15.844  1.00 8.58  ? 120 LEU   A C   1 
ATOM   1067 O  O   . LEU   A 1 120 ? 7.817  4.706   17.072  1.00 9.28  ? 120 LEU   A O   1 
ATOM   1068 C  CB  . LEU   A 1 120 ? 5.798  3.440   15.222  1.00 10.26 ? 120 LEU   A CB  1 
ATOM   1069 C  CG  . LEU   A 1 120 ? 5.119  2.381   14.351  1.00 10.88 ? 120 LEU   A CG  1 
ATOM   1070 C  CD1 . LEU   A 1 120 ? 4.207  1.497   15.177  1.00 13.16 ? 120 LEU   A CD1 1 
ATOM   1071 C  CD2 . LEU   A 1 120 ? 4.331  3.049   13.257  1.00 11.24 ? 120 LEU   A CD2 1 
ATOM   1072 N  N   . VAL   A 1 121 ? 8.643  5.568   15.134  1.00 9.10  ? 121 VAL   A N   1 
ATOM   1073 C  CA  . VAL   A 1 121 ? 9.497  6.573   15.754  1.00 9.98  ? 121 VAL   A CA  1 
ATOM   1074 C  C   . VAL   A 1 121 ? 8.796  7.919   15.767  1.00 9.70  ? 121 VAL   A C   1 
ATOM   1075 O  O   . VAL   A 1 121 ? 8.351  8.394   14.732  1.00 10.87 ? 121 VAL   A O   1 
ATOM   1076 C  CB  . VAL   A 1 121 ? 10.813 6.666   14.960  1.00 10.25 ? 121 VAL   A CB  1 
ATOM   1077 C  CG1 . VAL   A 1 121 ? 11.764 7.681   15.628  1.00 10.94 ? 121 VAL   A CG1 1 
ATOM   1078 C  CG2 . VAL   A 1 121 ? 11.462 5.306   14.815  1.00 11.37 ? 121 VAL   A CG2 1 
ATOM   1079 N  N   . HIS   A 1 122 ? 8.763  8.547   16.963  1.00 9.64  ? 122 HIS   A N   1 
ATOM   1080 C  CA  . HIS   A 1 122 ? 8.046  9.782   17.198  1.00 10.30 ? 122 HIS   A CA  1 
ATOM   1081 C  C   . HIS   A 1 122 ? 8.962  10.783  17.916  1.00 10.98 ? 122 HIS   A C   1 
ATOM   1082 O  O   . HIS   A 1 122 ? 9.785  10.365  18.734  1.00 12.51 ? 122 HIS   A O   1 
ATOM   1083 C  CB  . HIS   A 1 122 ? 6.787  9.577   18.058  1.00 11.05 ? 122 HIS   A CB  1 
ATOM   1084 C  CG  . HIS   A 1 122 ? 5.892  8.456   17.677  1.00 10.73 ? 122 HIS   A CG  1 
ATOM   1085 N  ND1 . HIS   A 1 122 ? 6.247  7.158   17.881  1.00 10.63 ? 122 HIS   A ND1 1 
ATOM   1086 C  CD2 . HIS   A 1 122 ? 4.682  8.422   17.072  1.00 11.33 ? 122 HIS   A CD2 1 
ATOM   1087 C  CE1 . HIS   A 1 122 ? 5.239  6.343   17.444  1.00 10.32 ? 122 HIS   A CE1 1 
ATOM   1088 N  NE2 . HIS   A 1 122 ? 4.260  7.135   16.953  1.00 11.33 ? 122 HIS   A NE2 1 
ATOM   1089 N  N   . TRP   A 1 123 ? 8.737  12.081  17.664  1.00 10.92 ? 123 TRP   A N   1 
ATOM   1090 C  CA  . TRP   A 1 123 ? 9.496  13.116  18.359  1.00 11.12 ? 123 TRP   A CA  1 
ATOM   1091 C  C   . TRP   A 1 123 ? 8.577  14.077  19.085  1.00 12.35 ? 123 TRP   A C   1 
ATOM   1092 O  O   . TRP   A 1 123 ? 7.479  14.438  18.645  1.00 13.27 ? 123 TRP   A O   1 
ATOM   1093 C  CB  . TRP   A 1 123 ? 10.439 13.859  17.402  1.00 13.75 ? 123 TRP   A CB  1 
ATOM   1094 C  CG  . TRP   A 1 123 ? 9.772  14.459  16.204  1.00 15.14 ? 123 TRP   A CG  1 
ATOM   1095 C  CD1 . TRP   A 1 123 ? 9.564  13.830  15.010  1.00 16.02 ? 123 TRP   A CD1 1 
ATOM   1096 C  CD2 . TRP   A 1 123 ? 9.318  15.809  16.033  1.00 16.54 ? 123 TRP   A CD2 1 
ATOM   1097 N  NE1 . TRP   A 1 123 ? 8.941  14.680  14.141  1.00 17.23 ? 123 TRP   A NE1 1 
ATOM   1098 C  CE2 . TRP   A 1 123 ? 8.791  15.910  14.735  1.00 17.31 ? 123 TRP   A CE2 1 
ATOM   1099 C  CE3 . TRP   A 1 123 ? 9.329  16.943  16.846  1.00 18.52 ? 123 TRP   A CE3 1 
ATOM   1100 C  CZ2 . TRP   A 1 123 ? 8.273  17.101  14.260  1.00 19.80 ? 123 TRP   A CZ2 1 
ATOM   1101 C  CZ3 . TRP   A 1 123 ? 8.781  18.107  16.360  1.00 19.91 ? 123 TRP   A CZ3 1 
ATOM   1102 C  CH2 . TRP   A 1 123 ? 8.312  18.206  15.063  1.00 21.12 ? 123 TRP   A CH2 1 
ATOM   1103 N  N   . ASN   A 1 124 ? 9.117  14.596  20.192  1.00 12.45 ? 124 ASN   A N   1 
ATOM   1104 C  CA  . ASN   A 1 124 ? 8.374  15.452  21.098  1.00 12.25 ? 124 ASN   A CA  1 
ATOM   1105 C  C   . ASN   A 1 124 ? 8.276  16.826  20.473  1.00 13.23 ? 124 ASN   A C   1 
ATOM   1106 O  O   . ASN   A 1 124 ? 9.285  17.504  20.230  1.00 13.48 ? 124 ASN   A O   1 
ATOM   1107 C  CB  . ASN   A 1 124 ? 9.133  15.535  22.412  1.00 12.82 ? 124 ASN   A CB  1 
ATOM   1108 C  CG  . ASN   A 1 124 ? 8.365  16.187  23.515  1.00 13.92 ? 124 ASN   A CG  1 
ATOM   1109 O  OD1 . ASN   A 1 124 ? 7.532  17.080  23.271  1.00 15.06 ? 124 ASN   A OD1 1 
ATOM   1110 N  ND2 . ASN   A 1 124 ? 8.604  15.761  24.739  1.00 15.08 ? 124 ASN   A ND2 1 
ATOM   1111 N  N   . THR   A 1 125 ? 7.047  17.297  20.238  1.00 13.87 ? 125 THR   A N   1 
ATOM   1112 C  CA  . THR   A 1 125 ? 6.836  18.526  19.492  1.00 15.90 ? 125 THR   A CA  1 
ATOM   1113 C  C   . THR   A 1 125 ? 7.336  19.756  20.223  1.00 15.64 ? 125 THR   A C   1 
ATOM   1114 O  O   . THR   A 1 125 ? 7.519  20.805  19.601  1.00 17.65 ? 125 THR   A O   1 
ATOM   1115 C  CB  . THR   A 1 125 ? 5.375  18.703  19.069  1.00 18.92 ? 125 THR   A CB  1 
ATOM   1116 O  OG1 . THR   A 1 125 ? 4.587  18.823  20.250  1.00 20.53 ? 125 THR   A OG1 1 
ATOM   1117 C  CG2 . THR   A 1 125 ? 4.869  17.545  18.225  1.00 20.19 ? 125 THR   A CG2 1 
ATOM   1118 N  N   . LYS   A 1 126 ? 7.576  19.666  21.539  1.00 14.51 ? 126 LYS   A N   1 
ATOM   1119 C  CA  . LYS   A 1 126 ? 8.114  20.807  22.266  1.00 16.43 ? 126 LYS   A CA  1 
ATOM   1120 C  C   . LYS   A 1 126 ? 9.500  21.189  21.772  1.00 15.45 ? 126 LYS   A C   1 
ATOM   1121 O  O   . LYS   A 1 126 ? 9.942  22.311  22.013  1.00 18.01 ? 126 LYS   A O   1 
ATOM   1122 C  CB  . LYS   A 1 126 ? 8.034  20.590  23.774  1.00 18.93 ? 126 LYS   A CB  1 
ATOM   1123 C  CG  . LYS   A 1 126 ? 9.060  19.674  24.397  1.00 19.90 ? 126 LYS   A CG  1 
ATOM   1124 C  CD  . LYS   A 1 126 ? 8.723  19.471  25.873  1.00 23.45 ? 126 LYS   A CD  1 
ATOM   1125 C  CE  . LYS   A 1 126 ? 9.687  18.609  26.646  1.00 26.38 ? 126 LYS   A CE  1 
ATOM   1126 N  N   . TYR   A 1 127 ? 10.192 20.280  21.084  1.00 13.51 ? 127 TYR   A N   1 
ATOM   1127 C  CA  . TYR   A 1 127 ? 11.511 20.589  20.547  1.00 14.03 ? 127 TYR   A CA  1 
ATOM   1128 C  C   . TYR   A 1 127 ? 11.514 20.940  19.065  1.00 15.30 ? 127 TYR   A C   1 
ATOM   1129 O  O   . TYR   A 1 127 ? 12.584 21.192  18.506  1.00 16.49 ? 127 TYR   A O   1 
ATOM   1130 C  CB  . TYR   A 1 127 ? 12.458 19.408  20.787  1.00 13.96 ? 127 TYR   A CB  1 
ATOM   1131 C  CG  . TYR   A 1 127 ? 12.589 19.115  22.262  1.00 13.63 ? 127 TYR   A CG  1 
ATOM   1132 C  CD1 . TYR   A 1 127 ? 13.065 20.075  23.138  1.00 14.80 ? 127 TYR   A CD1 1 
ATOM   1133 C  CD2 . TYR   A 1 127 ? 12.239 17.873  22.785  1.00 13.26 ? 127 TYR   A CD2 1 
ATOM   1134 C  CE1 . TYR   A 1 127 ? 13.169 19.820  24.501  1.00 15.50 ? 127 TYR   A CE1 1 
ATOM   1135 C  CE2 . TYR   A 1 127 ? 12.355 17.608  24.137  1.00 13.32 ? 127 TYR   A CE2 1 
ATOM   1136 C  CZ  . TYR   A 1 127 ? 12.794 18.586  25.003  1.00 14.38 ? 127 TYR   A CZ  1 
ATOM   1137 O  OH  . TYR   A 1 127 ? 12.940 18.372  26.333  1.00 16.59 ? 127 TYR   A OH  1 
ATOM   1138 N  N   . GLY   A 1 128 ? 10.336 21.071  18.444  1.00 15.48 ? 128 GLY   A N   1 
ATOM   1139 C  CA  . GLY   A 1 128 ? 10.227 21.733  17.165  1.00 15.17 ? 128 GLY   A CA  1 
ATOM   1140 C  C   . GLY   A 1 128 ? 10.558 20.915  15.926  1.00 16.04 ? 128 GLY   A C   1 
ATOM   1141 O  O   . GLY   A 1 128 ? 9.898  21.079  14.907  1.00 19.36 ? 128 GLY   A O   1 
ATOM   1142 N  N   . ASP   A 1 129 ? 11.632 20.096  15.974  1.00 17.91 ? 129 ASP   A N   1 
ATOM   1143 C  CA  . ASP   A 1 129 ? 12.021 19.235  14.874  1.00 20.15 ? 129 ASP   A CA  1 
ATOM   1144 C  C   . ASP   A 1 129 ? 12.624 17.958  15.460  1.00 19.46 ? 129 ASP   A C   1 
ATOM   1145 O  O   . ASP   A 1 129 ? 13.021 17.899  16.630  1.00 18.39 ? 129 ASP   A O   1 
ATOM   1146 C  CB  . ASP   A 1 129 ? 13.019 19.918  13.895  1.00 19.28 ? 129 ASP   A CB  1 
ATOM   1147 C  CG  . ASP   A 1 129 ? 14.410 20.251  14.452  1.00 23.91 ? 129 ASP   A CG  1 
ATOM   1148 O  OD1 . ASP   A 1 129 ? 15.220 19.335  14.634  1.00 25.69 ? 129 ASP   A OD1 1 
ATOM   1149 O  OD2 . ASP   A 1 129 ? 14.775 21.473  14.540  1.00 25.56 ? 129 ASP   A OD2 1 
ATOM   1150 N  N   . ALA   A 1 130 ? 12.651 16.928  14.620  1.00 19.88 ? 130 ALA   A N   1 
ATOM   1151 C  CA  . ALA   A 1 130 ? 13.189 15.644  15.019  1.00 18.44 ? 130 ALA   A CA  1 
ATOM   1152 C  C   . ALA   A 1 130 ? 14.688 15.691  15.329  1.00 18.37 ? 130 ALA   A C   1 
ATOM   1153 O  O   . ALA   A 1 130 ? 15.103 14.928  16.183  1.00 17.54 ? 130 ALA   A O   1 
ATOM   1154 C  CB  . ALA   A 1 130 ? 12.893 14.587  13.968  1.00 18.38 ? 130 ALA   A CB  1 
ATOM   1155 N  N   . SER   A 1 131 ? 15.493 16.510  14.632  1.00 21.44 ? 131 SER   A N   1 
ATOM   1156 C  CA  . SER   A 1 131 ? 16.935 16.580  14.877  1.00 24.00 ? 131 SER   A CA  1 
ATOM   1157 C  C   . SER   A 1 131 ? 17.213 17.077  16.289  1.00 19.20 ? 131 SER   A C   1 
ATOM   1158 O  O   . SER   A 1 131 ? 17.926 16.448  17.056  1.00 22.96 ? 131 SER   A O   1 
ATOM   1159 C  CB  . SER   A 1 131 ? 17.624 17.482  13.877  1.00 28.69 ? 131 SER   A CB  1 
ATOM   1160 O  OG  . SER   A 1 131 ? 17.276 17.064  12.563  1.00 37.32 ? 131 SER   A OG  1 
ATOM   1161 N  N   . LYS   A 1 132 ? 16.549 18.183  16.677  1.00 19.75 ? 132 LYS   A N   1 
ATOM   1162 C  CA  . LYS   A 1 132 ? 16.698 18.763  17.990  1.00 19.22 ? 132 LYS   A CA  1 
ATOM   1163 C  C   . LYS   A 1 132 ? 16.119 17.821  19.036  1.00 16.41 ? 132 LYS   A C   1 
ATOM   1164 O  O   . LYS   A 1 132 ? 16.742 17.569  20.073  1.00 18.78 ? 132 LYS   A O   1 
ATOM   1165 C  CB  . LYS   A 1 132 ? 16.002 20.117  18.033  1.00 20.54 ? 132 LYS   A CB  1 
ATOM   1166 C  CG  . LYS   A 1 132 ? 16.609 21.213  17.155  1.00 26.89 ? 132 LYS   A CG  1 
ATOM   1167 C  CD  . LYS   A 1 132 ? 18.094 21.169  16.965  1.00 30.92 ? 132 LYS   A CD  1 
ATOM   1168 N  N   . ALA   A 1 133 ? 14.941 17.234  18.752  1.00 15.11 ? 133 ALA   A N   1 
ATOM   1169 C  CA  . ALA   A 1 133 ? 14.353 16.328  19.711  1.00 13.79 ? 133 ALA   A CA  1 
ATOM   1170 C  C   . ALA   A 1 133 ? 15.257 15.125  20.009  1.00 14.09 ? 133 ALA   A C   1 
ATOM   1171 O  O   . ALA   A 1 133 ? 15.306 14.666  21.143  1.00 13.87 ? 133 ALA   A O   1 
ATOM   1172 C  CB  . ALA   A 1 133 ? 13.012 15.820  19.221  1.00 13.29 ? 133 ALA   A CB  1 
ATOM   1173 N  N   A SER   A 1 134 ? 15.971 14.621  18.992  0.50 13.99 ? 134 SER   A N   1 
ATOM   1174 N  N   B SER   A 1 134 ? 15.965 14.627  18.988  0.50 15.16 ? 134 SER   A N   1 
ATOM   1175 C  CA  A SER   A 1 134 ? 16.790 13.420  19.134  0.50 14.73 ? 134 SER   A CA  1 
ATOM   1176 C  CA  B SER   A 1 134 ? 16.773 13.420  19.114  0.50 17.04 ? 134 SER   A CA  1 
ATOM   1177 C  C   A SER   A 1 134 ? 17.916 13.584  20.155  0.50 14.96 ? 134 SER   A C   1 
ATOM   1178 C  C   B SER   A 1 134 ? 17.966 13.594  20.063  0.50 16.98 ? 134 SER   A C   1 
ATOM   1179 O  O   A SER   A 1 134 ? 18.471 12.577  20.593  0.50 15.61 ? 134 SER   A O   1 
ATOM   1180 O  O   B SER   A 1 134 ? 18.624 12.593  20.349  0.50 17.14 ? 134 SER   A O   1 
ATOM   1181 C  CB  A SER   A 1 134 ? 17.351 13.008  17.806  0.50 15.36 ? 134 SER   A CB  1 
ATOM   1182 C  CB  B SER   A 1 134 ? 17.232 12.961  17.750  0.50 19.58 ? 134 SER   A CB  1 
ATOM   1183 O  OG  A SER   A 1 134 ? 18.412 13.865  17.386  0.50 13.88 ? 134 SER   A OG  1 
ATOM   1184 O  OG  B SER   A 1 134 ? 16.141 12.562  16.915  0.50 22.56 ? 134 SER   A OG  1 
ATOM   1185 N  N   . GLN   A 1 135 ? 18.230 14.831  20.507  1.00 16.40 ? 135 GLN   A N   1 
ATOM   1186 C  CA  . GLN   A 1 135 ? 19.293 15.149  21.446  1.00 18.22 ? 135 GLN   A CA  1 
ATOM   1187 C  C   . GLN   A 1 135 ? 18.801 15.440  22.856  1.00 17.46 ? 135 GLN   A C   1 
ATOM   1188 O  O   . GLN   A 1 135 ? 19.611 15.766  23.734  1.00 21.71 ? 135 GLN   A O   1 
ATOM   1189 C  CB  . GLN   A 1 135 ? 20.109 16.331  20.922  1.00 22.16 ? 135 GLN   A CB  1 
ATOM   1190 C  CG  . GLN   A 1 135 ? 20.620 16.111  19.509  1.00 25.72 ? 135 GLN   A CG  1 
ATOM   1191 C  CD  . GLN   A 1 135 ? 21.682 15.030  19.420  1.00 30.54 ? 135 GLN   A CD  1 
ATOM   1192 O  OE1 . GLN   A 1 135 ? 22.425 14.747  20.370  1.00 40.63 ? 135 GLN   A OE1 1 
ATOM   1193 N  NE2 . GLN   A 1 135 ? 21.786 14.421  18.248  1.00 39.16 ? 135 GLN   A NE2 1 
ATOM   1194 N  N   . GLN   A 1 136 ? 17.494 15.316  23.097  1.00 14.47 ? 136 GLN   A N   1 
ATOM   1195 C  CA  . GLN   A 1 136 ? 16.943 15.658  24.399  1.00 13.78 ? 136 GLN   A CA  1 
ATOM   1196 C  C   . GLN   A 1 136 ? 16.539 14.398  25.137  1.00 13.93 ? 136 GLN   A C   1 
ATOM   1197 O  O   . GLN   A 1 136 ? 16.067 13.432  24.536  1.00 14.12 ? 136 GLN   A O   1 
ATOM   1198 C  CB  . GLN   A 1 136 ? 15.698 16.544  24.279  1.00 14.62 ? 136 GLN   A CB  1 
ATOM   1199 C  CG  . GLN   A 1 136 ? 15.901 17.801  23.456  1.00 17.26 ? 136 GLN   A CG  1 
ATOM   1200 C  CD  . GLN   A 1 136 ? 17.004 18.631  24.032  1.00 20.76 ? 136 GLN   A CD  1 
ATOM   1201 O  OE1 . GLN   A 1 136 ? 17.176 18.733  25.254  1.00 22.29 ? 136 GLN   A OE1 1 
ATOM   1202 N  NE2 . GLN   A 1 136 ? 17.829 19.120  23.119  1.00 28.66 ? 136 GLN   A NE2 1 
ATOM   1203 N  N   . PRO   A 1 137 ? 16.680 14.370  26.476  1.00 15.47 ? 137 PRO   A N   1 
ATOM   1204 C  CA  . PRO   A 1 137 ? 16.395 13.145  27.223  1.00 16.09 ? 137 PRO   A CA  1 
ATOM   1205 C  C   . PRO   A 1 137 ? 14.979 12.606  27.103  1.00 14.88 ? 137 PRO   A C   1 
ATOM   1206 O  O   . PRO   A 1 137 ? 14.765 11.394  27.204  1.00 18.21 ? 137 PRO   A O   1 
ATOM   1207 C  CB  . PRO   A 1 137 ? 16.738 13.408  28.674  1.00 18.90 ? 137 PRO   A CB  1 
ATOM   1208 C  CG  . PRO   A 1 137 ? 17.158 14.823  28.674  1.00 21.65 ? 137 PRO   A CG  1 
ATOM   1209 C  CD  . PRO   A 1 137 ? 17.285 15.425  27.301  1.00 18.18 ? 137 PRO   A CD  1 
ATOM   1210 N  N   . ASP   A 1 138 ? 14.029 13.527  26.869  1.00 13.42 ? 138 ASP   A N   1 
ATOM   1211 C  CA  . ASP   A 1 138 ? 12.634 13.145  26.639  1.00 13.32 ? 138 ASP   A CA  1 
ATOM   1212 C  C   . ASP   A 1 138 ? 12.229 13.516  25.208  1.00 12.80 ? 138 ASP   A C   1 
ATOM   1213 O  O   . ASP   A 1 138 ? 11.093 13.940  24.963  1.00 13.32 ? 138 ASP   A O   1 
ATOM   1214 C  CB  . ASP   A 1 138 ? 11.704 13.816  27.623  1.00 15.53 ? 138 ASP   A CB  1 
ATOM   1215 C  CG  . ASP   A 1 138 ? 11.762 15.319  27.618  1.00 15.80 ? 138 ASP   A CG  1 
ATOM   1216 O  OD1 . ASP   A 1 138 ? 12.698 15.899  26.972  1.00 16.77 ? 138 ASP   A OD1 1 
ATOM   1217 O  OD2 . ASP   A 1 138 ? 10.874 15.939  28.238  1.00 19.63 ? 138 ASP   A OD2 1 
ATOM   1218 N  N   . GLY   A 1 139 ? 13.151 13.416  24.252  1.00 11.77 ? 139 GLY   A N   1 
ATOM   1219 C  CA  . GLY   A 1 139 ? 12.897 13.908  22.920  1.00 11.05 ? 139 GLY   A CA  1 
ATOM   1220 C  C   . GLY   A 1 139 ? 12.174 12.939  22.001  1.00 10.74 ? 139 GLY   A C   1 
ATOM   1221 O  O   . GLY   A 1 139 ? 11.496 13.418  21.087  1.00 11.07 ? 139 GLY   A O   1 
ATOM   1222 N  N   . LEU   A 1 140 ? 12.373 11.650  22.185  1.00 10.10 ? 140 LEU   A N   1 
ATOM   1223 C  CA  . LEU   A 1 140 ? 11.820 10.677  21.257  1.00 9.72  ? 140 LEU   A CA  1 
ATOM   1224 C  C   . LEU   A 1 140 ? 10.976 9.669   22.018  1.00 9.82  ? 140 LEU   A C   1 
ATOM   1225 O  O   . LEU   A 1 140 ? 11.218 9.370   23.192  1.00 10.51 ? 140 LEU   A O   1 
ATOM   1226 C  CB  . LEU   A 1 140 ? 12.954 9.960   20.527  1.00 10.30 ? 140 LEU   A CB  1 
ATOM   1227 C  CG  . LEU   A 1 140 ? 13.907 10.820  19.721  1.00 12.26 ? 140 LEU   A CG  1 
ATOM   1228 C  CD1 . LEU   A 1 140 ? 15.012 9.963   19.163  1.00 13.38 ? 140 LEU   A CD1 1 
ATOM   1229 C  CD2 . LEU   A 1 140 ? 13.212 11.565  18.618  1.00 13.58 ? 140 LEU   A CD2 1 
ATOM   1230 N  N   . ALA   A 1 141 ? 10.014 9.053   21.310  1.00 10.36 ? 141 ALA   A N   1 
ATOM   1231 C  CA  . ALA   A 1 141 ? 9.228  7.933   21.808  1.00 10.60 ? 141 ALA   A CA  1 
ATOM   1232 C  C   . ALA   A 1 141 ? 9.133  6.918   20.686  1.00 9.65  ? 141 ALA   A C   1 
ATOM   1233 O  O   . ALA   A 1 141 ? 8.768  7.276   19.562  1.00 10.87 ? 141 ALA   A O   1 
ATOM   1234 C  CB  . ALA   A 1 141 ? 7.845  8.336   22.303  1.00 11.69 ? 141 ALA   A CB  1 
ATOM   1235 N  N   . VAL   A 1 142 ? 9.587  5.697   20.946  1.00 9.48  ? 142 VAL   A N   1 
ATOM   1236 C  CA  . VAL   A 1 142 ? 9.514  4.636   19.975  1.00 9.71  ? 142 VAL   A CA  1 
ATOM   1237 C  C   . VAL   A 1 142 ? 8.513  3.624   20.485  1.00 9.61  ? 142 VAL   A C   1 
ATOM   1238 O  O   . VAL   A 1 142 ? 8.627  3.123   21.599  1.00 9.77  ? 142 VAL   A O   1 
ATOM   1239 C  CB  . VAL   A 1 142 ? 10.877 4.005   19.603  1.00 9.68  ? 142 VAL   A CB  1 
ATOM   1240 C  CG1 . VAL   A 1 142 ? 10.655 2.977   18.493  1.00 10.52 ? 142 VAL   A CG1 1 
ATOM   1241 C  CG2 . VAL   A 1 142 ? 11.839 5.081   19.138  1.00 10.67 ? 142 VAL   A CG2 1 
ATOM   1242 N  N   . LEU   A 1 143 ? 7.492  3.359   19.640  1.00 9.27  ? 143 LEU   A N   1 
ATOM   1243 C  CA  . LEU   A 1 143 ? 6.532  2.304   19.871  1.00 9.87  ? 143 LEU   A CA  1 
ATOM   1244 C  C   . LEU   A 1 143 ? 7.043  1.053   19.174  1.00 8.85  ? 143 LEU   A C   1 
ATOM   1245 O  O   . LEU   A 1 143 ? 7.188  1.047   17.960  1.00 10.00 ? 143 LEU   A O   1 
ATOM   1246 C  CB  . LEU   A 1 143 ? 5.162  2.766   19.324  1.00 10.51 ? 143 LEU   A CB  1 
ATOM   1247 C  CG  . LEU   A 1 143 ? 3.997  1.816   19.498  1.00 11.67 ? 143 LEU   A CG  1 
ATOM   1248 C  CD1 . LEU   A 1 143 ? 3.733  1.535   20.951  1.00 13.87 ? 143 LEU   A CD1 1 
ATOM   1249 C  CD2 . LEU   A 1 143 ? 2.720  2.410   18.842  1.00 12.80 ? 143 LEU   A CD2 1 
ATOM   1250 N  N   . GLY   A 1 144 ? 7.349  0.028   19.967  1.00 9.16  ? 144 GLY   A N   1 
ATOM   1251 C  CA  . GLY   A 1 144 ? 7.894  -1.230  19.484  1.00 9.16  ? 144 GLY   A CA  1 
ATOM   1252 C  C   . GLY   A 1 144 ? 6.816  -2.303  19.512  1.00 8.92  ? 144 GLY   A C   1 
ATOM   1253 O  O   . GLY   A 1 144 ? 6.084  -2.446  20.482  1.00 9.71  ? 144 GLY   A O   1 
ATOM   1254 N  N   . ILE   A 1 145 ? 6.752  -3.038  18.393  1.00 8.81  ? 145 ILE   A N   1 
ATOM   1255 C  CA  . ILE   A 1 145 ? 5.734  -4.068  18.202  1.00 9.18  ? 145 ILE   A CA  1 
ATOM   1256 C  C   . ILE   A 1 145 ? 6.453  -5.319  17.703  1.00 9.04  ? 145 ILE   A C   1 
ATOM   1257 O  O   . ILE   A 1 145 ? 7.157  -5.283  16.698  1.00 10.18 ? 145 ILE   A O   1 
ATOM   1258 C  CB  . ILE   A 1 145 ? 4.633  -3.590  17.240  1.00 10.14 ? 145 ILE   A CB  1 
ATOM   1259 C  CG1 . ILE   A 1 145 ? 3.985  -2.324  17.763  1.00 11.51 ? 145 ILE   A CG1 1 
ATOM   1260 C  CG2 . ILE   A 1 145 ? 3.626  -4.684  16.991  1.00 11.65 ? 145 ILE   A CG2 1 
ATOM   1261 C  CD1 . ILE   A 1 145 ? 2.952  -1.710  16.834  1.00 11.26 ? 145 ILE   A CD1 1 
ATOM   1262 N  N   . PHE   A 1 146 ? 6.238  -6.435  18.391  1.00 9.41  ? 146 PHE   A N   1 
ATOM   1263 C  CA  . PHE   A 1 146 ? 6.819  -7.696  17.988  1.00 9.82  ? 146 PHE   A CA  1 
ATOM   1264 C  C   . PHE   A 1 146 ? 6.063  -8.326  16.830  1.00 10.56 ? 146 PHE   A C   1 
ATOM   1265 O  O   . PHE   A 1 146 ? 4.834  -8.180  16.777  1.00 10.78 ? 146 PHE   A O   1 
ATOM   1266 C  CB  . PHE   A 1 146 ? 6.810  -8.669  19.176  1.00 9.93  ? 146 PHE   A CB  1 
ATOM   1267 C  CG  . PHE   A 1 146 ? 7.647  -8.188  20.336  1.00 9.93  ? 146 PHE   A CG  1 
ATOM   1268 C  CD1 . PHE   A 1 146 ? 9.019  -8.009  20.183  1.00 10.15 ? 146 PHE   A CD1 1 
ATOM   1269 C  CD2 . PHE   A 1 146 ? 7.113  -7.966  21.558  1.00 10.13 ? 146 PHE   A CD2 1 
ATOM   1270 C  CE1 . PHE   A 1 146 ? 9.821  -7.637  21.244  1.00 10.34 ? 146 PHE   A CE1 1 
ATOM   1271 C  CE2 . PHE   A 1 146 ? 7.900  -7.563  22.627  1.00 11.03 ? 146 PHE   A CE2 1 
ATOM   1272 C  CZ  . PHE   A 1 146 ? 9.274  -7.431  22.476  1.00 10.83 ? 146 PHE   A CZ  1 
ATOM   1273 N  N   . LEU   A 1 147 ? 6.774  -9.053  15.991  1.00 10.34 ? 147 LEU   A N   1 
ATOM   1274 C  CA  . LEU   A 1 147 ? 6.207  -9.850  14.921  1.00 10.51 ? 147 LEU   A CA  1 
ATOM   1275 C  C   . LEU   A 1 147 ? 6.517  -11.303 15.211  1.00 11.27 ? 147 LEU   A C   1 
ATOM   1276 O  O   . LEU   A 1 147 ? 7.680  -11.695 15.409  1.00 11.67 ? 147 LEU   A O   1 
ATOM   1277 C  CB  . LEU   A 1 147 ? 6.784  -9.490  13.543  1.00 11.04 ? 147 LEU   A CB  1 
ATOM   1278 C  CG  . LEU   A 1 147 ? 6.241  -8.239  12.850  1.00 10.73 ? 147 LEU   A CG  1 
ATOM   1279 C  CD1 . LEU   A 1 147 ? 6.485  -6.976  13.659  1.00 12.65 ? 147 LEU   A CD1 1 
ATOM   1280 C  CD2 . LEU   A 1 147 ? 6.875  -8.107  11.474  1.00 11.93 ? 147 LEU   A CD2 1 
ATOM   1281 N  N   . LYS   A 1 148 ? 5.489  -12.174 15.153  1.00 11.58 ? 148 LYS   A N   1 
ATOM   1282 C  CA  . LYS   A 1 148 ? 5.641  -13.614 15.131  1.00 12.62 ? 148 LYS   A CA  1 
ATOM   1283 C  C   . LYS   A 1 148 ? 5.110  -14.141 13.804  1.00 13.23 ? 148 LYS   A C   1 
ATOM   1284 O  O   . LYS   A 1 148 ? 4.311  -13.476 13.157  1.00 14.35 ? 148 LYS   A O   1 
ATOM   1285 C  CB  . LYS   A 1 148 ? 4.888  -14.254 16.284  1.00 14.77 ? 148 LYS   A CB  1 
ATOM   1286 C  CG  . LYS   A 1 148 ? 3.370  -14.175 16.308  1.00 17.42 ? 148 LYS   A CG  1 
ATOM   1287 C  CD  . LYS   A 1 148 ? 2.740  -14.860 17.549  1.00 22.75 ? 148 LYS   A CD  1 
ATOM   1288 N  N   . VAL   A 1 149 ? 5.608  -15.285 13.396  1.00 13.96 ? 149 VAL   A N   1 
ATOM   1289 C  CA  . VAL   A 1 149 ? 5.178  -15.901 12.156  1.00 13.80 ? 149 VAL   A CA  1 
ATOM   1290 C  C   . VAL   A 1 149 ? 3.985  -16.839 12.385  1.00 15.49 ? 149 VAL   A C   1 
ATOM   1291 O  O   . VAL   A 1 149 ? 4.025  -17.766 13.198  1.00 16.84 ? 149 VAL   A O   1 
ATOM   1292 C  CB  . VAL   A 1 149 ? 6.369  -16.638 11.524  1.00 14.57 ? 149 VAL   A CB  1 
ATOM   1293 C  CG1 . VAL   A 1 149 ? 6.007  -17.469 10.304  1.00 16.55 ? 149 VAL   A CG1 1 
ATOM   1294 C  CG2 . VAL   A 1 149 ? 7.450  -15.626 11.221  1.00 15.62 ? 149 VAL   A CG2 1 
ATOM   1295 N  N   . GLY   A 1 150 ? 2.946  -16.549 11.631  1.00 14.96 ? 150 GLY   A N   1 
ATOM   1296 C  CA  . GLY   A 1 150 ? 1.760  -17.392 11.639  1.00 16.35 ? 150 GLY   A CA  1 
ATOM   1297 C  C   . GLY   A 1 150 ? 0.853  -16.954 10.511  1.00 15.61 ? 150 GLY   A C   1 
ATOM   1298 O  O   . GLY   A 1 150 ? 1.223  -17.072 9.355   1.00 16.18 ? 150 GLY   A O   1 
ATOM   1299 N  N   A SER   A 1 151 ? -0.309 -16.396 10.878  0.50 16.11 ? 151 SER   A N   1 
ATOM   1300 N  N   B SER   A 1 151 ? -0.335 -16.444 10.850  0.50 16.12 ? 151 SER   A N   1 
ATOM   1301 C  CA  A SER   A 1 151 ? -1.249 -15.809 9.930   0.50 16.46 ? 151 SER   A CA  1 
ATOM   1302 C  CA  B SER   A 1 151 ? -1.207 -15.893 9.822   0.50 16.32 ? 151 SER   A CA  1 
ATOM   1303 C  C   A SER   A 1 151 ? -0.692 -14.519 9.322   0.50 15.07 ? 151 SER   A C   1 
ATOM   1304 C  C   B SER   A 1 151 ? -0.583 -14.618 9.254   0.50 14.47 ? 151 SER   A C   1 
ATOM   1305 O  O   A SER   A 1 151 ? -0.092 -13.706 10.038  0.50 14.59 ? 151 SER   A O   1 
ATOM   1306 O  O   B SER   A 1 151 ? 0.240  -13.965 9.900   0.50 14.11 ? 151 SER   A O   1 
ATOM   1307 C  CB  A SER   A 1 151 ? -2.562 -15.553 10.633  0.50 18.12 ? 151 SER   A CB  1 
ATOM   1308 C  CB  B SER   A 1 151 ? -2.605 -15.659 10.346  0.50 18.37 ? 151 SER   A CB  1 
ATOM   1309 O  OG  A SER   A 1 151 ? -3.127 -16.766 11.114  0.50 20.51 ? 151 SER   A OG  1 
ATOM   1310 O  OG  B SER   A 1 151 ? -2.622 -14.644 11.337  0.50 21.23 ? 151 SER   A OG  1 
ATOM   1311 N  N   . ALA   A 1 152 ? -1.006 -14.266 8.029   1.00 14.98 ? 152 ALA   A N   1 
ATOM   1312 C  CA  . ALA   A 1 152 ? -0.587 -13.029 7.394   1.00 14.71 ? 152 ALA   A CA  1 
ATOM   1313 C  C   . ALA   A 1 152 ? -1.180 -11.812 8.071   1.00 13.74 ? 152 ALA   A C   1 
ATOM   1314 O  O   . ALA   A 1 152 ? -2.276 -11.859 8.605   1.00 15.34 ? 152 ALA   A O   1 
ATOM   1315 C  CB  . ALA   A 1 152 ? -0.983 -13.065 5.930   1.00 16.97 ? 152 ALA   A CB  1 
ATOM   1316 N  N   . LYS   A 1 153 ? -0.439 -10.698 8.015   1.00 13.04 ? 153 LYS   A N   1 
ATOM   1317 C  CA  . LYS   A 1 153 ? -0.948 -9.408  8.437   1.00 13.30 ? 153 LYS   A CA  1 
ATOM   1318 C  C   . LYS   A 1 153 ? -1.377 -8.635  7.196   1.00 13.02 ? 153 LYS   A C   1 
ATOM   1319 O  O   . LYS   A 1 153 ? -0.546 -8.171  6.408   1.00 13.34 ? 153 LYS   A O   1 
ATOM   1320 C  CB  . LYS   A 1 153 ? 0.100  -8.626  9.234   1.00 14.11 ? 153 LYS   A CB  1 
ATOM   1321 C  CG  . LYS   A 1 153 ? -0.433 -7.389  9.921   1.00 15.48 ? 153 LYS   A CG  1 
ATOM   1322 C  CD  . LYS   A 1 153 ? -1.303 -7.696  11.066  1.00 16.83 ? 153 LYS   A CD  1 
ATOM   1323 C  CE  . LYS   A 1 153 ? -1.453 -6.505  11.968  1.00 20.22 ? 153 LYS   A CE  1 
ATOM   1324 N  NZ  . LYS   A 1 153 ? -2.407 -6.838  13.033  1.00 23.05 ? 153 LYS   A NZ  1 
ATOM   1325 N  N   . PRO   A 1 154 ? -2.691 -8.474  6.932   1.00 14.07 ? 154 PRO   A N   1 
ATOM   1326 C  CA  . PRO   A 1 154 ? -3.105 -7.858  5.661   1.00 14.78 ? 154 PRO   A CA  1 
ATOM   1327 C  C   . PRO   A 1 154 ? -2.563 -6.456  5.477   1.00 14.51 ? 154 PRO   A C   1 
ATOM   1328 O  O   . PRO   A 1 154 ? -2.121 -6.117  4.379   1.00 14.95 ? 154 PRO   A O   1 
ATOM   1329 C  CB  . PRO   A 1 154 ? -4.635 -7.905  5.734   1.00 17.69 ? 154 PRO   A CB  1 
ATOM   1330 C  CG  . PRO   A 1 154 ? -4.892 -9.092  6.618   1.00 20.43 ? 154 PRO   A CG  1 
ATOM   1331 C  CD  . PRO   A 1 154 ? -3.838 -9.013  7.691   1.00 17.34 ? 154 PRO   A CD  1 
ATOM   1332 N  N   . GLY   A 1 155 ? -2.508 -5.686  6.561   1.00 15.11 ? 155 GLY   A N   1 
ATOM   1333 C  CA  . GLY   A 1 155 ? -2.016 -4.313  6.505   1.00 15.73 ? 155 GLY   A CA  1 
ATOM   1334 C  C   . GLY   A 1 155 ? -0.516 -4.178  6.261   1.00 14.62 ? 155 GLY   A C   1 
ATOM   1335 O  O   . GLY   A 1 155 ? -0.065 -3.067  6.053   1.00 17.16 ? 155 GLY   A O   1 
ATOM   1336 N  N   . LEU   A 1 156 ? 0.230  -5.276  6.317   1.00 13.12 ? 156 LEU   A N   1 
ATOM   1337 C  CA  . LEU   A 1 156 ? 1.624  -5.257  5.956   1.00 12.68 ? 156 LEU   A CA  1 
ATOM   1338 C  C   . LEU   A 1 156 ? 1.871  -5.505  4.474   1.00 12.74 ? 156 LEU   A C   1 
ATOM   1339 O  O   . LEU   A 1 156 ? 2.973  -5.262  3.964   1.00 12.83 ? 156 LEU   A O   1 
ATOM   1340 C  CB  . LEU   A 1 156 ? 2.343  -6.322  6.794   1.00 12.45 ? 156 LEU   A CB  1 
ATOM   1341 C  CG  . LEU   A 1 156 ? 3.872  -6.436  6.636   1.00 12.61 ? 156 LEU   A CG  1 
ATOM   1342 C  CD1 . LEU   A 1 156 ? 4.627  -5.157  6.978   1.00 13.03 ? 156 LEU   A CD1 1 
ATOM   1343 C  CD2 . LEU   A 1 156 ? 4.366  -7.601  7.479   1.00 13.53 ? 156 LEU   A CD2 1 
ATOM   1344 N  N   . GLN   A 1 157 ? 0.896  -6.073  3.727   1.00 12.93 ? 157 GLN   A N   1 
ATOM   1345 C  CA  . GLN   A 1 157 ? 1.179  -6.577  2.390   1.00 12.75 ? 157 GLN   A CA  1 
ATOM   1346 C  C   . GLN   A 1 157 ? 1.616  -5.460  1.459   1.00 12.90 ? 157 GLN   A C   1 
ATOM   1347 O  O   . GLN   A 1 157 ? 2.454  -5.689  0.627   1.00 13.57 ? 157 GLN   A O   1 
ATOM   1348 C  CB  . GLN   A 1 157 ? -0.021 -7.365  1.856   1.00 14.39 ? 157 GLN   A CB  1 
ATOM   1349 C  CG  . GLN   A 1 157 ? 0.286  -8.164  0.605   1.00 15.88 ? 157 GLN   A CG  1 
ATOM   1350 C  CD  . GLN   A 1 157 ? 1.374  -9.180  0.838   1.00 14.50 ? 157 GLN   A CD  1 
ATOM   1351 O  OE1 . GLN   A 1 157 ? 1.506  -9.746  1.915   1.00 15.57 ? 157 GLN   A OE1 1 
ATOM   1352 N  NE2 . GLN   A 1 157 ? 2.160  -9.412  -0.199  1.00 16.11 ? 157 GLN   A NE2 1 
ATOM   1353 N  N   . LYS   A 1 158 ? 1.065  -4.244  1.568   1.00 13.91 ? 158 LYS   A N   1 
ATOM   1354 C  CA  . LYS   A 1 158 ? 1.518  -3.181  0.677   1.00 14.12 ? 158 LYS   A CA  1 
ATOM   1355 C  C   . LYS   A 1 158 ? 3.014  -2.904  0.835   1.00 13.38 ? 158 LYS   A C   1 
ATOM   1356 O  O   . LYS   A 1 158 ? 3.693  -2.572  -0.125  1.00 14.35 ? 158 LYS   A O   1 
ATOM   1357 C  CB  . LYS   A 1 158 ? 0.735  -1.908  0.944   1.00 16.88 ? 158 LYS   A CB  1 
ATOM   1358 C  CG  . LYS   A 1 158 ? 0.969  -0.811  -0.061  1.00 20.53 ? 158 LYS   A CG  1 
ATOM   1359 N  N   . VAL   A 1 159 ? 3.491  -3.013  2.065   1.00 12.81 ? 159 VAL   A N   1 
ATOM   1360 C  CA  . VAL   A 1 159 ? 4.926  -2.874  2.329   1.00 12.99 ? 159 VAL   A CA  1 
ATOM   1361 C  C   . VAL   A 1 159 ? 5.717  -3.983  1.649   1.00 12.59 ? 159 VAL   A C   1 
ATOM   1362 O  O   . VAL   A 1 159 ? 6.652  -3.729  0.914   1.00 14.16 ? 159 VAL   A O   1 
ATOM   1363 C  CB  . VAL   A 1 159 ? 5.216  -2.856  3.834   1.00 14.09 ? 159 VAL   A CB  1 
ATOM   1364 C  CG1 . VAL   A 1 159 ? 6.718  -2.896  4.114   1.00 16.24 ? 159 VAL   A CG1 1 
ATOM   1365 C  CG2 . VAL   A 1 159 ? 4.614  -1.650  4.507   1.00 15.53 ? 159 VAL   A CG2 1 
ATOM   1366 N  N   A VAL   A 1 160 ? 5.354  -5.231  1.867   0.50 13.35 ? 160 VAL   A N   1 
ATOM   1367 N  N   B VAL   A 1 160 ? 5.318  -5.216  1.935   0.50 12.47 ? 160 VAL   A N   1 
ATOM   1368 C  CA  A VAL   A 1 160 ? 6.230  -6.257  1.330   0.50 14.08 ? 160 VAL   A CA  1 
ATOM   1369 C  CA  B VAL   A 1 160 ? 5.958  -6.389  1.361   0.50 12.61 ? 160 VAL   A CA  1 
ATOM   1370 C  C   A VAL   A 1 160 ? 6.120  -6.311  -0.195  0.50 15.19 ? 160 VAL   A C   1 
ATOM   1371 C  C   B VAL   A 1 160 ? 6.109  -6.223  -0.144  0.50 14.10 ? 160 VAL   A C   1 
ATOM   1372 O  O   A VAL   A 1 160 ? 7.072  -6.717  -0.853  0.50 15.73 ? 160 VAL   A O   1 
ATOM   1373 O  O   B VAL   A 1 160 ? 7.176  -6.447  -0.708  0.50 14.94 ? 160 VAL   A O   1 
ATOM   1374 C  CB  A VAL   A 1 160 ? 6.030  -7.602  2.039   0.50 15.41 ? 160 VAL   A CB  1 
ATOM   1375 C  CB  B VAL   A 1 160 ? 5.168  -7.662  1.722   0.50 12.42 ? 160 VAL   A CB  1 
ATOM   1376 C  CG1 A VAL   A 1 160 ? 6.369  -7.527  3.515   0.50 16.30 ? 160 VAL   A CG1 1 
ATOM   1377 C  CG1 B VAL   A 1 160 ? 5.651  -8.873  0.937   0.50 12.39 ? 160 VAL   A CG1 1 
ATOM   1378 C  CG2 A VAL   A 1 160 ? 4.637  -8.134  1.853   0.50 15.26 ? 160 VAL   A CG2 1 
ATOM   1379 C  CG2 B VAL   A 1 160 ? 5.282  -7.919  3.216   0.50 12.67 ? 160 VAL   A CG2 1 
ATOM   1380 N  N   . ASP   A 1 161 ? 5.018  -5.856  -0.798  1.00 14.78 ? 161 ASP   A N   1 
ATOM   1381 C  CA  . ASP   A 1 161 ? 4.966  -5.859  -2.248  1.00 15.98 ? 161 ASP   A CA  1 
ATOM   1382 C  C   . ASP   A 1 161 ? 5.823  -4.771  -2.903  1.00 16.69 ? 161 ASP   A C   1 
ATOM   1383 O  O   . ASP   A 1 161 ? 6.103  -4.898  -4.084  1.00 23.16 ? 161 ASP   A O   1 
ATOM   1384 C  CB  . ASP   A 1 161 ? 3.533  -5.777  -2.724  1.00 18.73 ? 161 ASP   A CB  1 
ATOM   1385 C  CG  . ASP   A 1 161 ? 2.841  -7.128  -2.651  1.00 19.56 ? 161 ASP   A CG  1 
ATOM   1386 O  OD1 . ASP   A 1 161 ? 3.536  -8.184  -2.650  1.00 23.62 ? 161 ASP   A OD1 1 
ATOM   1387 O  OD2 . ASP   A 1 161 ? 1.646  -7.128  -2.564  1.00 21.43 ? 161 ASP   A OD2 1 
ATOM   1388 N  N   . VAL   A 1 162 ? 6.226  -3.719  -2.199  1.00 15.13 ? 162 VAL   A N   1 
ATOM   1389 C  CA  . VAL   A 1 162 ? 7.077  -2.685  -2.776  1.00 16.48 ? 162 VAL   A CA  1 
ATOM   1390 C  C   . VAL   A 1 162 ? 8.566  -3.004  -2.560  1.00 15.12 ? 162 VAL   A C   1 
ATOM   1391 O  O   . VAL   A 1 162 ? 9.428  -2.348  -3.127  1.00 16.10 ? 162 VAL   A O   1 
ATOM   1392 C  CB  . VAL   A 1 162 ? 6.714  -1.312  -2.169  1.00 17.99 ? 162 VAL   A CB  1 
ATOM   1393 C  CG1 . VAL   A 1 162 ? 7.269  -1.080  -0.787  1.00 18.41 ? 162 VAL   A CG1 1 
ATOM   1394 C  CG2 . VAL   A 1 162 ? 7.094  -0.145  -3.040  1.00 21.50 ? 162 VAL   A CG2 1 
ATOM   1395 N  N   . LEU   A 1 163 ? 8.906  -4.013  -1.741  1.00 14.80 ? 163 LEU   A N   1 
ATOM   1396 C  CA  . LEU   A 1 163 ? 10.307 -4.237  -1.384  1.00 14.59 ? 163 LEU   A CA  1 
ATOM   1397 C  C   . LEU   A 1 163 ? 11.187 -4.623  -2.568  1.00 15.97 ? 163 LEU   A C   1 
ATOM   1398 O  O   . LEU   A 1 163 ? 12.368 -4.260  -2.579  1.00 16.39 ? 163 LEU   A O   1 
ATOM   1399 C  CB  . LEU   A 1 163 ? 10.443 -5.271  -0.272  1.00 14.12 ? 163 LEU   A CB  1 
ATOM   1400 C  CG  . LEU   A 1 163 ? 9.800  -4.914  1.055   1.00 13.90 ? 163 LEU   A CG  1 
ATOM   1401 C  CD1 . LEU   A 1 163 ? 10.068 -5.988  2.091   1.00 14.60 ? 163 LEU   A CD1 1 
ATOM   1402 C  CD2 . LEU   A 1 163 ? 10.307 -3.573  1.560   1.00 14.71 ? 163 LEU   A CD2 1 
ATOM   1403 N  N   . ASP   A 1 164 ? 10.625 -5.297  -3.584  1.00 18.17 ? 164 ASP   A N   1 
ATOM   1404 C  CA  . ASP   A 1 164 ? 11.382 -5.663  -4.768  1.00 21.58 ? 164 ASP   A CA  1 
ATOM   1405 C  C   . ASP   A 1 164 ? 11.891 -4.413  -5.499  1.00 19.54 ? 164 ASP   A C   1 
ATOM   1406 O  O   . ASP   A 1 164 ? 12.863 -4.518  -6.246  1.00 28.16 ? 164 ASP   A O   1 
ATOM   1407 C  CB  . ASP   A 1 164 ? 10.573 -6.629  -5.651  1.00 25.93 ? 164 ASP   A CB  1 
ATOM   1408 N  N   . SER   A 1 165 ? 11.250 -3.242  -5.309  1.00 17.89 ? 165 SER   A N   1 
ATOM   1409 C  CA  . SER   A 1 165 ? 11.675 -1.997  -5.924  1.00 18.54 ? 165 SER   A CA  1 
ATOM   1410 C  C   . SER   A 1 165 ? 12.752 -1.216  -5.173  1.00 17.90 ? 165 SER   A C   1 
ATOM   1411 O  O   . SER   A 1 165 ? 13.289 -0.208  -5.685  1.00 20.04 ? 165 SER   A O   1 
ATOM   1412 C  CB  . SER   A 1 165 ? 10.498 -1.134  -6.220  1.00 19.80 ? 165 SER   A CB  1 
ATOM   1413 O  OG  . SER   A 1 165 ? 9.992  -0.486  -5.081  1.00 21.39 ? 165 SER   A OG  1 
ATOM   1414 N  N   . ILE   A 1 166 ? 13.086 -1.673  -3.967  1.00 15.69 ? 166 ILE   A N   1 
ATOM   1415 C  CA  . ILE   A 1 166 ? 14.087 -1.022  -3.138  1.00 16.59 ? 166 ILE   A CA  1 
ATOM   1416 C  C   . ILE   A 1 166 ? 15.050 -2.082  -2.607  1.00 14.76 ? 166 ILE   A C   1 
ATOM   1417 O  O   . ILE   A 1 166 ? 15.435 -2.079  -1.450  1.00 15.29 ? 166 ILE   A O   1 
ATOM   1418 C  CB  . ILE   A 1 166 ? 13.458 -0.181  -2.004  1.00 16.28 ? 166 ILE   A CB  1 
ATOM   1419 C  CG1 . ILE   A 1 166 ? 12.587 -0.983  -1.039  1.00 15.09 ? 166 ILE   A CG1 1 
ATOM   1420 C  CG2 . ILE   A 1 166 ? 12.695 0.994   -2.616  1.00 17.46 ? 166 ILE   A CG2 1 
ATOM   1421 C  CD1 . ILE   A 1 166 ? 12.464 -0.370  0.327   1.00 16.17 ? 166 ILE   A CD1 1 
ATOM   1422 N  N   . LYS   A 1 167 ? 15.498 -2.960  -3.499  1.00 16.49 ? 167 LYS   A N   1 
ATOM   1423 C  CA  . LYS   A 1 167 ? 16.250 -4.128  -3.046  1.00 16.52 ? 167 LYS   A CA  1 
ATOM   1424 C  C   . LYS   A 1 167 ? 17.600 -3.770  -2.413  1.00 16.54 ? 167 LYS   A C   1 
ATOM   1425 O  O   . LYS   A 1 167 ? 18.000 -4.414  -1.455  1.00 16.33 ? 167 LYS   A O   1 
ATOM   1426 C  CB  . LYS   A 1 167 ? 16.503 -5.093  -4.202  1.00 20.15 ? 167 LYS   A CB  1 
ATOM   1427 C  CG  . LYS   A 1 167 ? 17.242 -6.386  -3.844  1.00 23.18 ? 167 LYS   A CG  1 
ATOM   1428 C  CD  . LYS   A 1 167 ? 17.487 -7.290  -5.048  1.00 28.21 ? 167 LYS   A CD  1 
ATOM   1429 C  CE  . LYS   A 1 167 ? 18.250 -8.543  -4.693  1.00 35.35 ? 167 LYS   A CE  1 
ATOM   1430 N  NZ  . LYS   A 1 167 ? 18.470 -9.397  -5.881  1.00 43.31 ? 167 LYS   A NZ  1 
ATOM   1431 N  N   . THR   A 1 168 ? 18.253 -2.734  -2.930  1.00 16.20 ? 168 THR   A N   1 
ATOM   1432 C  CA  . THR   A 1 168 ? 19.608 -2.395  -2.550  1.00 17.38 ? 168 THR   A CA  1 
ATOM   1433 C  C   . THR   A 1 168 ? 19.691 -1.024  -1.895  1.00 15.94 ? 168 THR   A C   1 
ATOM   1434 O  O   . THR   A 1 168 ? 18.819 -0.156  -2.032  1.00 16.70 ? 168 THR   A O   1 
ATOM   1435 C  CB  . THR   A 1 168 ? 20.494 -2.473  -3.798  1.00 18.87 ? 168 THR   A CB  1 
ATOM   1436 O  OG1 . THR   A 1 168 ? 19.941 -1.712  -4.878  1.00 20.58 ? 168 THR   A OG1 1 
ATOM   1437 C  CG2 . THR   A 1 168 ? 20.702 -3.900  -4.246  1.00 20.20 ? 168 THR   A CG2 1 
ATOM   1438 N  N   . LYS   A 1 169 ? 20.783 -0.859  -1.142  1.00 17.30 ? 169 LYS   A N   1 
ATOM   1439 C  CA  . LYS   A 1 169 ? 21.065 0.344   -0.384  1.00 16.64 ? 169 LYS   A CA  1 
ATOM   1440 C  C   . LYS   A 1 169 ? 20.997 1.556   -1.292  1.00 18.29 ? 169 LYS   A C   1 
ATOM   1441 O  O   . LYS   A 1 169 ? 21.647 1.595   -2.337  1.00 19.20 ? 169 LYS   A O   1 
ATOM   1442 C  CB  . LYS   A 1 169 ? 22.441 0.208   0.249   1.00 17.40 ? 169 LYS   A CB  1 
ATOM   1443 C  CG  . LYS   A 1 169 ? 22.882 1.422   1.041   1.00 19.27 ? 169 LYS   A CG  1 
ATOM   1444 C  CD  . LYS   A 1 169 ? 24.247 1.244   1.714   1.00 24.20 ? 169 LYS   A CD  1 
ATOM   1445 C  CE  . LYS   A 1 169 ? 24.624 2.530   2.405   1.00 30.69 ? 169 LYS   A CE  1 
ATOM   1446 N  NZ  . LYS   A 1 169 ? 25.782 2.321   3.275   1.00 35.45 ? 169 LYS   A NZ  1 
ATOM   1447 N  N   . GLY   A 1 170 ? 20.232 2.549   -0.830  1.00 17.38 ? 170 GLY   A N   1 
ATOM   1448 C  CA  . GLY   A 1 170 ? 20.089 3.838   -1.487  1.00 19.00 ? 170 GLY   A CA  1 
ATOM   1449 C  C   . GLY   A 1 170 ? 18.849 3.961   -2.354  1.00 18.57 ? 170 GLY   A C   1 
ATOM   1450 O  O   . GLY   A 1 170 ? 18.528 5.070   -2.774  1.00 24.40 ? 170 GLY   A O   1 
ATOM   1451 N  N   . LYS   A 1 171 ? 18.158 2.856   -2.631  1.00 16.94 ? 171 LYS   A N   1 
ATOM   1452 C  CA  . LYS   A 1 171 ? 16.959 2.916   -3.446  1.00 17.35 ? 171 LYS   A CA  1 
ATOM   1453 C  C   . LYS   A 1 171 ? 15.762 3.365   -2.600  1.00 16.67 ? 171 LYS   A C   1 
ATOM   1454 O  O   . LYS   A 1 171 ? 15.566 2.946   -1.463  1.00 16.87 ? 171 LYS   A O   1 
ATOM   1455 C  CB  . LYS   A 1 171 ? 16.672 1.546   -4.076  1.00 18.62 ? 171 LYS   A CB  1 
ATOM   1456 C  CG  . LYS   A 1 171 ? 17.670 1.146   -5.162  1.00 20.96 ? 171 LYS   A CG  1 
ATOM   1457 C  CD  . LYS   A 1 171 ? 17.236 0.076   -6.133  1.00 26.37 ? 171 LYS   A CD  1 
ATOM   1458 N  N   . SER   A 1 172 ? 14.946 4.242   -3.181  1.00 17.43 ? 172 SER   A N   1 
ATOM   1459 C  CA  . SER   A 1 172 ? 13.695 4.679   -2.593  1.00 18.39 ? 172 SER   A CA  1 
ATOM   1460 C  C   . SER   A 1 172 ? 12.563 4.556   -3.625  1.00 18.57 ? 172 SER   A C   1 
ATOM   1461 O  O   . SER   A 1 172 ? 12.788 4.517   -4.835  1.00 20.16 ? 172 SER   A O   1 
ATOM   1462 C  CB  . SER   A 1 172 ? 13.828 6.091   -2.071  1.00 20.78 ? 172 SER   A CB  1 
ATOM   1463 O  OG  . SER   A 1 172 ? 14.038 6.988   -3.144  1.00 25.01 ? 172 SER   A OG  1 
ATOM   1464 N  N   . ALA   A 1 173 ? 11.329 4.618   -3.120  1.00 18.32 ? 173 ALA   A N   1 
ATOM   1465 C  CA  . ALA   A 1 173 ? 10.131 4.602   -3.967  1.00 19.09 ? 173 ALA   A CA  1 
ATOM   1466 C  C   . ALA   A 1 173 ? 9.029  5.432   -3.304  1.00 18.22 ? 173 ALA   A C   1 
ATOM   1467 O  O   . ALA   A 1 173 ? 8.946  5.550   -2.072  1.00 16.60 ? 173 ALA   A O   1 
ATOM   1468 C  CB  . ALA   A 1 173 ? 9.667  3.188   -4.189  1.00 21.27 ? 173 ALA   A CB  1 
ATOM   1469 N  N   . ASP   A 1 174 ? 8.114  5.954   -4.130  1.00 20.86 ? 174 ASP   A N   1 
ATOM   1470 C  CA  . ASP   A 1 174 ? 6.938  6.611   -3.585  1.00 21.66 ? 174 ASP   A CA  1 
ATOM   1471 C  C   . ASP   A 1 174 ? 6.176  5.637   -2.721  1.00 19.28 ? 174 ASP   A C   1 
ATOM   1472 O  O   . ASP   A 1 174 ? 6.066  4.457   -3.064  1.00 22.63 ? 174 ASP   A O   1 
ATOM   1473 C  CB  . ASP   A 1 174 ? 5.900  7.006   -4.655  1.00 24.82 ? 174 ASP   A CB  1 
ATOM   1474 C  CG  . ASP   A 1 174 ? 4.602  7.639   -4.132  1.00 31.47 ? 174 ASP   A CG  1 
ATOM   1475 O  OD1 . ASP   A 1 174 ? 3.567  6.880   -3.737  1.00 31.67 ? 174 ASP   A OD1 1 
ATOM   1476 O  OD2 . ASP   A 1 174 ? 4.601  8.903   -4.126  1.00 39.56 ? 174 ASP   A OD2 1 
ATOM   1477 N  N   . PHE   A 1 175 ? 5.637  6.123   -1.596  1.00 16.16 ? 175 PHE   A N   1 
ATOM   1478 C  CA  . PHE   A 1 175 ? 4.866  5.231   -0.739  1.00 14.86 ? 175 PHE   A CA  1 
ATOM   1479 C  C   . PHE   A 1 175 ? 3.805  6.007   0.008   1.00 14.43 ? 175 PHE   A C   1 
ATOM   1480 O  O   . PHE   A 1 175 ? 3.774  6.053   1.237   1.00 19.33 ? 175 PHE   A O   1 
ATOM   1481 C  CB  . PHE   A 1 175 ? 5.787  4.445   0.189   1.00 14.90 ? 175 PHE   A CB  1 
ATOM   1482 C  CG  . PHE   A 1 175 ? 5.191  3.173   0.715   1.00 15.11 ? 175 PHE   A CG  1 
ATOM   1483 C  CD1 . PHE   A 1 175 ? 4.929  2.132   -0.148  1.00 15.65 ? 175 PHE   A CD1 1 
ATOM   1484 C  CD2 . PHE   A 1 175 ? 4.888  3.025   2.055   1.00 15.49 ? 175 PHE   A CD2 1 
ATOM   1485 C  CE1 . PHE   A 1 175 ? 4.328  0.976   0.305   1.00 16.67 ? 175 PHE   A CE1 1 
ATOM   1486 C  CE2 . PHE   A 1 175 ? 4.314  1.851   2.519   1.00 16.42 ? 175 PHE   A CE2 1 
ATOM   1487 C  CZ  . PHE   A 1 175 ? 4.067  0.830   1.633   1.00 16.93 ? 175 PHE   A CZ  1 
ATOM   1488 N  N   . THR   A 1 176 ? 2.908  6.621   -0.772  1.00 12.93 ? 176 THR   A N   1 
ATOM   1489 C  CA  . THR   A 1 176 ? 1.828  7.430   -0.224  1.00 13.70 ? 176 THR   A CA  1 
ATOM   1490 C  C   . THR   A 1 176 ? 0.632  6.546   0.137   1.00 11.64 ? 176 THR   A C   1 
ATOM   1491 O  O   . THR   A 1 176 ? 0.465  5.427   -0.313  1.00 12.91 ? 176 THR   A O   1 
ATOM   1492 C  CB  . THR   A 1 176 ? 1.432  8.530   -1.219  1.00 14.05 ? 176 THR   A CB  1 
ATOM   1493 O  OG1 . THR   A 1 176 ? 1.156  7.943   -2.484  1.00 16.89 ? 176 THR   A OG1 1 
ATOM   1494 C  CG2 . THR   A 1 176 ? 2.497  9.599   -1.313  1.00 16.85 ? 176 THR   A CG2 1 
ATOM   1495 N  N   . ASN   A 1 177 ? -0.216 7.113   0.988   1.00 12.59 ? 177 ASN   A N   1 
ATOM   1496 C  CA  . ASN   A 1 177 ? -1.484 6.515   1.382   1.00 13.68 ? 177 ASN   A CA  1 
ATOM   1497 C  C   . ASN   A 1 177 ? -1.328 5.184   2.087   1.00 13.42 ? 177 ASN   A C   1 
ATOM   1498 O  O   . ASN   A 1 177 ? -2.203 4.335   1.977   1.00 16.61 ? 177 ASN   A O   1 
ATOM   1499 C  CB  . ASN   A 1 177 ? -2.456 6.438   0.203   1.00 14.31 ? 177 ASN   A CB  1 
ATOM   1500 C  CG  . ASN   A 1 177 ? -2.757 7.821   -0.318  1.00 14.68 ? 177 ASN   A CG  1 
ATOM   1501 O  OD1 . ASN   A 1 177 ? -3.393 8.643   0.335   1.00 17.47 ? 177 ASN   A OD1 1 
ATOM   1502 N  ND2 . ASN   A 1 177 ? -2.180 8.124   -1.448  1.00 14.57 ? 177 ASN   A ND2 1 
ATOM   1503 N  N   . PHE   A 1 178 ? -0.227 4.985   2.799   1.00 12.49 ? 178 PHE   A N   1 
ATOM   1504 C  CA  . PHE   A 1 178 ? -0.084 3.795   3.627   1.00 12.43 ? 178 PHE   A CA  1 
ATOM   1505 C  C   . PHE   A 1 178 ? -0.562 4.131   5.028   1.00 11.96 ? 178 PHE   A C   1 
ATOM   1506 O  O   . PHE   A 1 178 ? -0.065 5.097   5.630   1.00 13.54 ? 178 PHE   A O   1 
ATOM   1507 C  CB  . PHE   A 1 178 ? 1.361  3.282   3.636   1.00 12.96 ? 178 PHE   A CB  1 
ATOM   1508 C  CG  . PHE   A 1 178 ? 1.485  2.066   4.513   1.00 12.73 ? 178 PHE   A CG  1 
ATOM   1509 C  CD1 . PHE   A 1 178 ? 1.062  0.834   4.045   1.00 13.69 ? 178 PHE   A CD1 1 
ATOM   1510 C  CD2 . PHE   A 1 178 ? 1.902  2.147   5.837   1.00 12.64 ? 178 PHE   A CD2 1 
ATOM   1511 C  CE1 . PHE   A 1 178 ? 1.092  -0.277  4.864   1.00 14.65 ? 178 PHE   A CE1 1 
ATOM   1512 C  CE2 . PHE   A 1 178 ? 1.910  1.032   6.660   1.00 12.44 ? 178 PHE   A CE2 1 
ATOM   1513 C  CZ  . PHE   A 1 178 ? 1.500  -0.183  6.174   1.00 13.19 ? 178 PHE   A CZ  1 
ATOM   1514 N  N   . ASP   A 1 179 ? -1.409 3.288   5.593   1.00 12.18 ? 179 ASP   A N   1 
ATOM   1515 C  CA  . ASP   A 1 179 ? -2.020 3.529   6.880   1.00 12.54 ? 179 ASP   A CA  1 
ATOM   1516 C  C   . ASP   A 1 179 ? -1.324 2.659   7.931   1.00 12.83 ? 179 ASP   A C   1 
ATOM   1517 O  O   . ASP   A 1 179 ? -1.546 1.448   7.989   1.00 13.31 ? 179 ASP   A O   1 
ATOM   1518 C  CB  . ASP   A 1 179 ? -3.513 3.228   6.868   1.00 14.69 ? 179 ASP   A CB  1 
ATOM   1519 C  CG  . ASP   A 1 179 ? -4.215 3.620   8.155   1.00 17.16 ? 179 ASP   A CG  1 
ATOM   1520 O  OD1 . ASP   A 1 179 ? -3.575 3.940   9.158   1.00 16.29 ? 179 ASP   A OD1 1 
ATOM   1521 O  OD2 . ASP   A 1 179 ? -5.424 3.630   8.137   1.00 25.42 ? 179 ASP   A OD2 1 
ATOM   1522 N  N   . PRO   A 1 180 ? -0.538 3.266   8.842   1.00 11.91 ? 180 PRO   A N   1 
ATOM   1523 C  CA  . PRO   A 1 180 ? 0.172  2.438   9.839   1.00 11.58 ? 180 PRO   A CA  1 
ATOM   1524 C  C   . PRO   A 1 180 ? -0.745 1.824   10.878  1.00 12.75 ? 180 PRO   A C   1 
ATOM   1525 O  O   . PRO   A 1 180 ? -0.326 0.936   11.624  1.00 12.67 ? 180 PRO   A O   1 
ATOM   1526 C  CB  . PRO   A 1 180 ? 1.193  3.436   10.407  1.00 12.94 ? 180 PRO   A CB  1 
ATOM   1527 C  CG  . PRO   A 1 180 ? 0.500  4.770   10.307  1.00 13.66 ? 180 PRO   A CG  1 
ATOM   1528 C  CD  . PRO   A 1 180 ? -0.206 4.693   8.969   1.00 13.57 ? 180 PRO   A CD  1 
ATOM   1529 N  N   . ARG   A 1 181 ? -2.028 2.240   10.907  1.00 12.91 ? 181 ARG   A N   1 
ATOM   1530 C  CA  . ARG   A 1 181 ? -2.931 1.565   11.829  1.00 12.78 ? 181 ARG   A CA  1 
ATOM   1531 C  C   . ARG   A 1 181 ? -3.054 0.082   11.508  1.00 12.65 ? 181 ARG   A C   1 
ATOM   1532 O  O   . ARG   A 1 181 ? -3.403 -0.692  12.396  1.00 13.89 ? 181 ARG   A O   1 
ATOM   1533 C  CB  . ARG   A 1 181 ? -4.304 2.222   11.792  1.00 13.73 ? 181 ARG   A CB  1 
ATOM   1534 C  CG  . ARG   A 1 181 ? -4.288 3.624   12.352  1.00 16.12 ? 181 ARG   A CG  1 
ATOM   1535 C  CD  . ARG   A 1 181 ? -5.609 4.335   12.318  1.00 18.21 ? 181 ARG   A CD  1 
ATOM   1536 N  NE  . ARG   A 1 181 ? -6.003 4.557   10.957  1.00 18.90 ? 181 ARG   A NE  1 
ATOM   1537 C  CZ  . ARG   A 1 181 ? -7.117 5.174   10.641  1.00 20.43 ? 181 ARG   A CZ  1 
ATOM   1538 N  NH1 . ARG   A 1 181 ? -7.881 5.623   11.611  1.00 23.45 ? 181 ARG   A NH1 1 
ATOM   1539 N  NH2 . ARG   A 1 181 ? -7.443 5.331   9.370   1.00 23.12 ? 181 ARG   A NH2 1 
ATOM   1540 N  N   . GLY   A 1 182 ? -2.803 -0.285  10.249  1.00 13.09 ? 182 GLY   A N   1 
ATOM   1541 C  CA  . GLY   A 1 182 ? -2.887 -1.678  9.853   1.00 13.91 ? 182 GLY   A CA  1 
ATOM   1542 C  C   . GLY   A 1 182 ? -1.768 -2.565  10.392  1.00 12.81 ? 182 GLY   A C   1 
ATOM   1543 O  O   . GLY   A 1 182 ? -1.763 -3.768  10.123  1.00 14.31 ? 182 GLY   A O   1 
ATOM   1544 N  N   . LEU   A 1 183 ? -0.785 -1.948  11.101  1.00 12.93 ? 183 LEU   A N   1 
ATOM   1545 C  CA  . LEU   A 1 183 ? 0.329  -2.696  11.662  1.00 12.11 ? 183 LEU   A CA  1 
ATOM   1546 C  C   . LEU   A 1 183 ? 0.177  -2.927  13.165  1.00 12.88 ? 183 LEU   A C   1 
ATOM   1547 O  O   . LEU   A 1 183 ? 1.063  -3.531  13.774  1.00 14.89 ? 183 LEU   A O   1 
ATOM   1548 C  CB  . LEU   A 1 183 ? 1.624  -1.929  11.371  1.00 12.87 ? 183 LEU   A CB  1 
ATOM   1549 C  CG  . LEU   A 1 183 ? 1.940  -1.786  9.889   1.00 13.47 ? 183 LEU   A CG  1 
ATOM   1550 C  CD1 . LEU   A 1 183 ? 3.190  -0.978  9.696   1.00 14.38 ? 183 LEU   A CD1 1 
ATOM   1551 C  CD2 . LEU   A 1 183 ? 2.078  -3.122  9.189   1.00 15.69 ? 183 LEU   A CD2 1 
ATOM   1552 N  N   . LEU   A 1 184 ? -0.914 -2.479  13.794  1.00 12.91 ? 184 LEU   A N   1 
ATOM   1553 C  CA  . LEU   A 1 184 ? -1.064 -2.498  15.251  1.00 12.62 ? 184 LEU   A CA  1 
ATOM   1554 C  C   . LEU   A 1 184 ? -1.821 -3.764  15.666  1.00 14.19 ? 184 LEU   A C   1 
ATOM   1555 O  O   . LEU   A 1 184 ? -2.726 -4.247  14.992  1.00 20.63 ? 184 LEU   A O   1 
ATOM   1556 C  CB  . LEU   A 1 184 ? -1.862 -1.262  15.726  1.00 13.34 ? 184 LEU   A CB  1 
ATOM   1557 C  CG  . LEU   A 1 184 ? -1.312 0.105   15.319  1.00 14.66 ? 184 LEU   A CG  1 
ATOM   1558 C  CD1 . LEU   A 1 184 ? -2.191 1.220   15.815  1.00 15.83 ? 184 LEU   A CD1 1 
ATOM   1559 C  CD2 . LEU   A 1 184 ? 0.085  0.256   15.831  1.00 16.20 ? 184 LEU   A CD2 1 
ATOM   1560 N  N   . PRO   A 1 185 ? -1.472 -4.334  16.839  1.00 12.97 ? 185 PRO   A N   1 
ATOM   1561 C  CA  . PRO   A 1 185 ? -2.228 -5.440  17.409  1.00 13.88 ? 185 PRO   A CA  1 
ATOM   1562 C  C   . PRO   A 1 185 ? -3.519 -4.877  18.010  1.00 13.48 ? 185 PRO   A C   1 
ATOM   1563 O  O   . PRO   A 1 185 ? -3.737 -3.677  18.056  1.00 15.00 ? 185 PRO   A O   1 
ATOM   1564 C  CB  . PRO   A 1 185 ? -1.279 -5.997  18.462  1.00 13.64 ? 185 PRO   A CB  1 
ATOM   1565 C  CG  . PRO   A 1 185 ? -0.569 -4.756  18.948  1.00 12.74 ? 185 PRO   A CG  1 
ATOM   1566 C  CD  . PRO   A 1 185 ? -0.360 -3.910  17.690  1.00 12.31 ? 185 PRO   A CD  1 
ATOM   1567 N  N   . GLU   A 1 186 ? -4.387 -5.781  18.502  1.00 14.19 ? 186 GLU   A N   1 
ATOM   1568 C  CA  . GLU   A 1 186 ? -5.625 -5.358  19.120  1.00 14.78 ? 186 GLU   A CA  1 
ATOM   1569 C  C   . GLU   A 1 186 ? -5.406 -4.561  20.396  1.00 13.90 ? 186 GLU   A C   1 
ATOM   1570 O  O   . GLU   A 1 186 ? -6.000 -3.498  20.583  1.00 16.53 ? 186 GLU   A O   1 
ATOM   1571 C  CB  . GLU   A 1 186 ? -6.488 -6.552  19.529  1.00 19.26 ? 186 GLU   A CB  1 
ATOM   1572 C  CG  . GLU   A 1 186 ? -7.238 -7.209  18.434  1.00 22.10 ? 186 GLU   A CG  1 
ATOM   1573 C  CD  . GLU   A 1 186 ? -7.989 -8.437  18.889  1.00 22.97 ? 186 GLU   A CD  1 
ATOM   1574 O  OE1 . GLU   A 1 186 ? -8.051 -8.733  20.137  1.00 24.23 ? 186 GLU   A OE1 1 
ATOM   1575 O  OE2 . GLU   A 1 186 ? -8.461 -9.125  17.989  1.00 27.80 ? 186 GLU   A OE2 1 
ATOM   1576 N  N   . SER   A 1 187 ? -4.568 -5.097  21.305  1.00 13.58 ? 187 SER   A N   1 
ATOM   1577 C  CA  . SER   A 1 187 ? -4.346 -4.534  22.616  1.00 14.43 ? 187 SER   A CA  1 
ATOM   1578 C  C   . SER   A 1 187 ? -3.221 -3.502  22.571  1.00 13.89 ? 187 SER   A C   1 
ATOM   1579 O  O   . SER   A 1 187 ? -2.207 -3.722  21.896  1.00 14.78 ? 187 SER   A O   1 
ATOM   1580 C  CB  . SER   A 1 187 ? -3.939 -5.589  23.617  1.00 15.26 ? 187 SER   A CB  1 
ATOM   1581 O  OG  . SER   A 1 187 ? -3.696 -5.015  24.892  1.00 16.37 ? 187 SER   A OG  1 
ATOM   1582 N  N   . LEU   A 1 188 ? -3.395 -2.416  23.324  1.00 14.03 ? 188 LEU   A N   1 
ATOM   1583 C  CA  . LEU   A 1 188 ? -2.336 -1.436  23.554  1.00 14.55 ? 188 LEU   A CA  1 
ATOM   1584 C  C   . LEU   A 1 188 ? -1.688 -1.602  24.935  1.00 14.44 ? 188 LEU   A C   1 
ATOM   1585 O  O   . LEU   A 1 188 ? -1.046 -0.669  25.404  1.00 16.22 ? 188 LEU   A O   1 
ATOM   1586 C  CB  . LEU   A 1 188 ? -2.837 0.002   23.365  1.00 16.19 ? 188 LEU   A CB  1 
ATOM   1587 C  CG  . LEU   A 1 188 ? -3.269 0.375   21.948  1.00 17.29 ? 188 LEU   A CG  1 
ATOM   1588 C  CD1 . LEU   A 1 188 ? -3.775 1.825   21.884  1.00 18.37 ? 188 LEU   A CD1 1 
ATOM   1589 C  CD2 . LEU   A 1 188 ? -2.128 0.167   20.937  1.00 17.60 ? 188 LEU   A CD2 1 
ATOM   1590 N  N   . ASP   A 1 189 ? -1.840 -2.761  25.574  1.00 14.22 ? 189 ASP   A N   1 
ATOM   1591 C  CA  . ASP   A 1 189 ? -1.065 -3.046  26.785  1.00 15.03 ? 189 ASP   A CA  1 
ATOM   1592 C  C   . ASP   A 1 189 ? 0.428  -2.965  26.452  1.00 12.54 ? 189 ASP   A C   1 
ATOM   1593 O  O   . ASP   A 1 189 ? 0.879  -3.436  25.435  1.00 12.52 ? 189 ASP   A O   1 
ATOM   1594 C  CB  . ASP   A 1 189 ? -1.404 -4.435  27.341  1.00 16.74 ? 189 ASP   A CB  1 
ATOM   1595 C  CG  . ASP   A 1 189 ? -2.771 -4.610  27.975  1.00 21.15 ? 189 ASP   A CG  1 
ATOM   1596 O  OD1 . ASP   A 1 189 ? -3.397 -3.605  28.246  1.00 24.99 ? 189 ASP   A OD1 1 
ATOM   1597 O  OD2 . ASP   A 1 189 ? -3.134 -5.760  28.232  1.00 26.63 ? 189 ASP   A OD2 1 
ATOM   1598 N  N   . TYR   A 1 190 ? 1.214  -2.371  27.363  1.00 12.02 ? 190 TYR   A N   1 
ATOM   1599 C  CA  . TYR   A 1 190 ? 2.613  -2.125  27.061  1.00 11.27 ? 190 TYR   A CA  1 
ATOM   1600 C  C   . TYR   A 1 190 ? 3.487  -2.185  28.311  1.00 11.49 ? 190 TYR   A C   1 
ATOM   1601 O  O   . TYR   A 1 190 ? 3.036  -2.054  29.444  1.00 12.03 ? 190 TYR   A O   1 
ATOM   1602 C  CB  . TYR   A 1 190 ? 2.823  -0.769  26.367  1.00 11.99 ? 190 TYR   A CB  1 
ATOM   1603 C  CG  . TYR   A 1 190 ? 2.421  0.399   27.231  1.00 11.71 ? 190 TYR   A CG  1 
ATOM   1604 C  CD1 . TYR   A 1 190 ? 3.323  1.030   28.079  1.00 12.76 ? 190 TYR   A CD1 1 
ATOM   1605 C  CD2 . TYR   A 1 190 ? 1.138  0.944   27.189  1.00 12.88 ? 190 TYR   A CD2 1 
ATOM   1606 C  CE1 . TYR   A 1 190 ? 2.943  2.078   28.896  1.00 13.31 ? 190 TYR   A CE1 1 
ATOM   1607 C  CE2 . TYR   A 1 190 ? 0.764  2.001   27.980  1.00 13.59 ? 190 TYR   A CE2 1 
ATOM   1608 C  CZ  . TYR   A 1 190 ? 1.661  2.593   28.849  1.00 13.91 ? 190 TYR   A CZ  1 
ATOM   1609 O  OH  . TYR   A 1 190 ? 1.298  3.602   29.695  1.00 15.59 ? 190 TYR   A OH  1 
ATOM   1610 N  N   . TRP   A 1 191 ? 4.796  -2.339  28.025  1.00 10.36 ? 191 TRP   A N   1 
ATOM   1611 C  CA  . TRP   A 1 191 ? 5.876  -2.035  28.959  1.00 10.73 ? 191 TRP   A CA  1 
ATOM   1612 C  C   . TRP   A 1 191 ? 6.564  -0.746  28.523  1.00 10.40 ? 191 TRP   A C   1 
ATOM   1613 O  O   . TRP   A 1 191 ? 6.653  -0.451  27.342  1.00 12.00 ? 191 TRP   A O   1 
ATOM   1614 C  CB  . TRP   A 1 191 ? 6.898  -3.168  28.976  1.00 11.13 ? 191 TRP   A CB  1 
ATOM   1615 C  CG  . TRP   A 1 191 ? 6.364  -4.493  29.409  1.00 11.42 ? 191 TRP   A CG  1 
ATOM   1616 C  CD1 . TRP   A 1 191 ? 6.133  -4.914  30.669  1.00 12.96 ? 191 TRP   A CD1 1 
ATOM   1617 C  CD2 . TRP   A 1 191 ? 6.088  -5.626  28.560  1.00 11.86 ? 191 TRP   A CD2 1 
ATOM   1618 N  NE1 . TRP   A 1 191 ? 5.668  -6.204  30.673  1.00 13.67 ? 191 TRP   A NE1 1 
ATOM   1619 C  CE2 . TRP   A 1 191 ? 5.648  -6.688  29.388  1.00 12.64 ? 191 TRP   A CE2 1 
ATOM   1620 C  CE3 . TRP   A 1 191 ? 6.167  -5.851  27.184  1.00 11.72 ? 191 TRP   A CE3 1 
ATOM   1621 C  CZ2 . TRP   A 1 191 ? 5.310  -7.932  28.876  1.00 13.70 ? 191 TRP   A CZ2 1 
ATOM   1622 C  CZ3 . TRP   A 1 191 ? 5.888  -7.110  26.695  1.00 13.69 ? 191 TRP   A CZ3 1 
ATOM   1623 C  CH2 . TRP   A 1 191 ? 5.453  -8.125  27.520  1.00 13.95 ? 191 TRP   A CH2 1 
ATOM   1624 N  N   . THR   A 1 192 ? 7.127  -0.014  29.503  1.00 10.09 ? 192 THR   A N   1 
ATOM   1625 C  CA  . THR   A 1 192 ? 7.834  1.212   29.177  1.00 10.16 ? 192 THR   A CA  1 
ATOM   1626 C  C   . THR   A 1 192 ? 9.096  1.339   30.037  1.00 10.26 ? 192 THR   A C   1 
ATOM   1627 O  O   . THR   A 1 192 ? 9.084  0.959   31.212  1.00 11.15 ? 192 THR   A O   1 
ATOM   1628 C  CB  . THR   A 1 192 ? 6.919  2.440   29.273  1.00 10.38 ? 192 THR   A CB  1 
ATOM   1629 O  OG1 . THR   A 1 192 ? 7.621  3.623   28.868  1.00 11.08 ? 192 THR   A OG1 1 
ATOM   1630 C  CG2 . THR   A 1 192 ? 6.352  2.631   30.666  1.00 11.05 ? 192 THR   A CG2 1 
ATOM   1631 N  N   . TYR   A 1 193 ? 10.122 1.955   29.460  1.00 9.94  ? 193 TYR   A N   1 
ATOM   1632 C  CA  . TYR   A 1 193 ? 11.357 2.222   30.208  1.00 10.54 ? 193 TYR   A CA  1 
ATOM   1633 C  C   . TYR   A 1 193 ? 12.130 3.281   29.442  1.00 9.70  ? 193 TYR   A C   1 
ATOM   1634 O  O   . TYR   A 1 193 ? 11.919 3.468   28.231  1.00 9.97  ? 193 TYR   A O   1 
ATOM   1635 C  CB  . TYR   A 1 193 ? 12.190 0.941   30.388  1.00 9.76  ? 193 TYR   A CB  1 
ATOM   1636 C  CG  . TYR   A 1 193 ? 12.879 0.454   29.122  1.00 10.46 ? 193 TYR   A CG  1 
ATOM   1637 C  CD1 . TYR   A 1 193 ? 12.207 -0.259  28.126  1.00 10.35 ? 193 TYR   A CD1 1 
ATOM   1638 C  CD2 . TYR   A 1 193 ? 14.210 0.840   28.862  1.00 10.34 ? 193 TYR   A CD2 1 
ATOM   1639 C  CE1 . TYR   A 1 193 ? 12.814 -0.615  26.944  1.00 10.25 ? 193 TYR   A CE1 1 
ATOM   1640 C  CE2 . TYR   A 1 193 ? 14.846 0.450   27.708  1.00 9.97  ? 193 TYR   A CE2 1 
ATOM   1641 C  CZ  . TYR   A 1 193 ? 14.138 -0.233  26.725  1.00 9.65  ? 193 TYR   A CZ  1 
ATOM   1642 O  OH  . TYR   A 1 193 ? 14.785 -0.549  25.583  1.00 9.87  ? 193 TYR   A OH  1 
ATOM   1643 N  N   . PRO   A 1 194 ? 13.059 3.996   30.112  1.00 10.10 ? 194 PRO   A N   1 
ATOM   1644 C  CA  . PRO   A 1 194 ? 13.902 4.977   29.434  1.00 10.38 ? 194 PRO   A CA  1 
ATOM   1645 C  C   . PRO   A 1 194 ? 15.075 4.301   28.765  1.00 9.91  ? 194 PRO   A C   1 
ATOM   1646 O  O   . PRO   A 1 194 ? 15.791 3.515   29.417  1.00 10.80 ? 194 PRO   A O   1 
ATOM   1647 C  CB  . PRO   A 1 194 ? 14.378 5.884   30.561  1.00 11.53 ? 194 PRO   A CB  1 
ATOM   1648 C  CG  . PRO   A 1 194 ? 14.395 4.962   31.777  1.00 12.27 ? 194 PRO   A CG  1 
ATOM   1649 C  CD  . PRO   A 1 194 ? 13.226 4.001   31.566  1.00 11.07 ? 194 PRO   A CD  1 
ATOM   1650 N  N   . GLY   A 1 195 ? 15.327 4.617   27.507  1.00 9.67  ? 195 GLY   A N   1 
ATOM   1651 C  CA  . GLY   A 1 195 ? 16.393 3.975   26.777  1.00 10.12 ? 195 GLY   A CA  1 
ATOM   1652 C  C   . GLY   A 1 195 ? 16.961 4.853   25.681  1.00 9.90  ? 195 GLY   A C   1 
ATOM   1653 O  O   . GLY   A 1 195 ? 17.101 6.062   25.812  1.00 9.97  ? 195 GLY   A O   1 
ATOM   1654 N  N   . SER   A 1 196 ? 17.398 4.168   24.620  1.00 9.54  ? 196 SER   A N   1 
ATOM   1655 C  CA  . SER   A 1 196 ? 18.203 4.791   23.587  1.00 9.41  ? 196 SER   A CA  1 
ATOM   1656 C  C   . SER   A 1 196 ? 17.760 4.389   22.189  1.00 8.37  ? 196 SER   A C   1 
ATOM   1657 O  O   . SER   A 1 196 ? 17.005 3.443   21.996  1.00 9.71  ? 196 SER   A O   1 
ATOM   1658 C  CB  . SER   A 1 196 ? 19.695 4.375   23.758  1.00 10.52 ? 196 SER   A CB  1 
ATOM   1659 O  OG  . SER   A 1 196 ? 19.944 3.039   23.294  1.00 10.52 ? 196 SER   A OG  1 
ATOM   1660 N  N   . LEU   A 1 197 ? 18.311 5.078   21.195  1.00 9.39  ? 197 LEU   A N   1 
ATOM   1661 C  CA  . LEU   A 1 197 ? 18.300 4.551   19.835  1.00 9.77  ? 197 LEU   A CA  1 
ATOM   1662 C  C   . LEU   A 1 197 ? 19.038 3.215   19.837  1.00 9.63  ? 197 LEU   A C   1 
ATOM   1663 O  O   . LEU   A 1 197 ? 20.056 3.049   20.538  1.00 9.98  ? 197 LEU   A O   1 
ATOM   1664 C  CB  . LEU   A 1 197 ? 19.030 5.513   18.894  1.00 10.26 ? 197 LEU   A CB  1 
ATOM   1665 C  CG  . LEU   A 1 197 ? 18.467 6.923   18.859  1.00 11.65 ? 197 LEU   A CG  1 
ATOM   1666 C  CD1 . LEU   A 1 197 ? 19.332 7.763   17.945  1.00 12.65 ? 197 LEU   A CD1 1 
ATOM   1667 C  CD2 . LEU   A 1 197 ? 17.004 6.955   18.410  1.00 13.07 ? 197 LEU   A CD2 1 
ATOM   1668 N  N   . THR   A 1 198 ? 18.585 2.233   19.020  1.00 9.39  ? 198 THR   A N   1 
ATOM   1669 C  CA  . THR   A 1 198 ? 19.219 0.935   18.979  1.00 9.74  ? 198 THR   A CA  1 
ATOM   1670 C  C   . THR   A 1 198 ? 20.213 0.794   17.843  1.00 10.02 ? 198 THR   A C   1 
ATOM   1671 O  O   . THR   A 1 198 ? 20.822 -0.256  17.695  1.00 10.52 ? 198 THR   A O   1 
ATOM   1672 C  CB  . THR   A 1 198 ? 18.204 -0.191  18.876  1.00 9.27  ? 198 THR   A CB  1 
ATOM   1673 O  OG1 . THR   A 1 198 ? 17.626 -0.119  17.562  1.00 9.36  ? 198 THR   A OG1 1 
ATOM   1674 C  CG2 . THR   A 1 198 ? 17.183 -0.144  19.981  1.00 9.87  ? 198 THR   A CG2 1 
ATOM   1675 N  N   . THR   A 1 199 ? 20.435 1.873   17.090  1.00 10.82 ? 199 THR   A N   1 
ATOM   1676 C  CA  . THR   A 1 199 ? 21.506 1.946   16.129  1.00 11.34 ? 199 THR   A CA  1 
ATOM   1677 C  C   . THR   A 1 199 ? 22.323 3.179   16.457  1.00 11.70 ? 199 THR   A C   1 
ATOM   1678 O  O   . THR   A 1 199 ? 21.808 4.146   17.029  1.00 12.72 ? 199 THR   A O   1 
ATOM   1679 C  CB  . THR   A 1 199 ? 21.044 2.061   14.667  1.00 11.81 ? 199 THR   A CB  1 
ATOM   1680 O  OG1 . THR   A 1 199 ? 20.441 3.320   14.455  1.00 16.81 ? 199 THR   A OG1 1 
ATOM   1681 C  CG2 . THR   A 1 199 ? 20.153 0.918   14.285  1.00 12.37 ? 199 THR   A CG2 1 
ATOM   1682 N  N   . PRO   A 1 200 ? 23.574 3.242   15.952  1.00 12.22 ? 200 PRO   A N   1 
ATOM   1683 C  CA  . PRO   A 1 200 ? 24.306 4.502   15.983  1.00 12.29 ? 200 PRO   A CA  1 
ATOM   1684 C  C   . PRO   A 1 200 ? 23.412 5.632   15.509  1.00 12.96 ? 200 PRO   A C   1 
ATOM   1685 O  O   . PRO   A 1 200 ? 22.699 5.427   14.501  1.00 14.40 ? 200 PRO   A O   1 
ATOM   1686 C  CB  . PRO   A 1 200 ? 25.504 4.189   15.096  1.00 13.38 ? 200 PRO   A CB  1 
ATOM   1687 C  CG  . PRO   A 1 200 ? 25.776 2.760   15.369  1.00 13.80 ? 200 PRO   A CG  1 
ATOM   1688 C  CD  . PRO   A 1 200 ? 24.392 2.153   15.390  1.00 12.42 ? 200 PRO   A CD  1 
ATOM   1689 N  N   . PRO   A 1 201 ? 23.418 6.822   16.121  1.00 12.80 ? 201 PRO   A N   1 
ATOM   1690 C  CA  . PRO   A 1 201 ? 24.357 7.229   17.173  1.00 13.37 ? 201 PRO   A CA  1 
ATOM   1691 C  C   . PRO   A 1 201 ? 24.056 6.812   18.606  1.00 11.48 ? 201 PRO   A C   1 
ATOM   1692 O  O   . PRO   A 1 201 ? 24.764 7.232   19.512  1.00 13.19 ? 201 PRO   A O   1 
ATOM   1693 C  CB  . PRO   A 1 201 ? 24.355 8.757   17.008  1.00 14.98 ? 201 PRO   A CB  1 
ATOM   1694 C  CG  . PRO   A 1 201 ? 22.934 9.087   16.523  1.00 15.62 ? 201 PRO   A CG  1 
ATOM   1695 C  CD  . PRO   A 1 201 ? 22.624 7.939   15.608  1.00 14.72 ? 201 PRO   A CD  1 
ATOM   1696 N  N   . LEU   A 1 202 ? 23.004 6.002   18.825  1.00 11.35 ? 202 LEU   A N   1 
ATOM   1697 C  CA  . LEU   A 1 202 ? 22.771 5.373   20.128  1.00 10.88 ? 202 LEU   A CA  1 
ATOM   1698 C  C   . LEU   A 1 202 ? 22.384 6.373   21.210  1.00 10.45 ? 202 LEU   A C   1 
ATOM   1699 O  O   . LEU   A 1 202 ? 22.450 6.081   22.406  1.00 11.61 ? 202 LEU   A O   1 
ATOM   1700 C  CB  . LEU   A 1 202 ? 23.950 4.478   20.563  1.00 12.15 ? 202 LEU   A CB  1 
ATOM   1701 C  CG  . LEU   A 1 202 ? 24.281 3.324   19.626  1.00 11.73 ? 202 LEU   A CG  1 
ATOM   1702 C  CD1 . LEU   A 1 202 ? 25.588 2.693   20.052  1.00 13.15 ? 202 LEU   A CD1 1 
ATOM   1703 C  CD2 . LEU   A 1 202 ? 23.186 2.272   19.571  1.00 12.38 ? 202 LEU   A CD2 1 
ATOM   1704 N  N   . ASN   A 1 203 ? 21.854 7.521   20.801  1.00 11.71 ? 203 ASN   A N   1 
ATOM   1705 C  CA  . ASN   A 1 203 ? 21.509 8.584   21.725  1.00 11.65 ? 203 ASN   A CA  1 
ATOM   1706 C  C   . ASN   A 1 203 ? 20.546 8.097   22.793  1.00 10.61 ? 203 ASN   A C   1 
ATOM   1707 O  O   . ASN   A 1 203 ? 19.566 7.397   22.487  1.00 11.03 ? 203 ASN   A O   1 
ATOM   1708 C  CB  . ASN   A 1 203 ? 20.840 9.771   21.052  1.00 13.00 ? 203 ASN   A CB  1 
ATOM   1709 C  CG  . ASN   A 1 203 ? 21.615 10.441  19.959  1.00 16.13 ? 203 ASN   A CG  1 
ATOM   1710 O  OD1 . ASN   A 1 203 ? 22.716 10.061  19.631  1.00 18.84 ? 203 ASN   A OD1 1 
ATOM   1711 N  ND2 . ASN   A 1 203 ? 21.007 11.450  19.376  1.00 19.02 ? 203 ASN   A ND2 1 
ATOM   1712 N  N   . GLU   A 1 204 ? 20.768 8.515   24.039  1.00 11.24 ? 204 GLU   A N   1 
ATOM   1713 C  CA  . GLU   A 1 204 ? 19.961 8.127   25.183  1.00 11.48 ? 204 GLU   A CA  1 
ATOM   1714 C  C   . GLU   A 1 204 ? 18.789 9.081   25.384  1.00 11.93 ? 204 GLU   A C   1 
ATOM   1715 O  O   . GLU   A 1 204 ? 18.687 9.751   26.403  1.00 14.33 ? 204 GLU   A O   1 
ATOM   1716 C  CB  . GLU   A 1 204 ? 20.858 8.001   26.413  1.00 12.72 ? 204 GLU   A CB  1 
ATOM   1717 C  CG  . GLU   A 1 204 ? 21.743 6.783   26.285  1.00 12.81 ? 204 GLU   A CG  1 
ATOM   1718 C  CD  . GLU   A 1 204 ? 22.671 6.457   27.439  1.00 12.95 ? 204 GLU   A CD  1 
ATOM   1719 O  OE1 . GLU   A 1 204 ? 22.971 7.384   28.236  1.00 15.08 ? 204 GLU   A OE1 1 
ATOM   1720 O  OE2 . GLU   A 1 204 ? 23.087 5.285   27.523  1.00 13.15 ? 204 GLU   A OE2 1 
ATOM   1721 N  N   . THR   A 1 205 ? 17.887 9.071   24.394  1.00 11.10 ? 205 THR   A N   1 
ATOM   1722 C  CA  . THR   A 1 205 ? 16.878 10.105  24.261  1.00 11.19 ? 205 THR   A CA  1 
ATOM   1723 C  C   . THR   A 1 205 ? 15.489 9.530   23.956  1.00 10.40 ? 205 THR   A C   1 
ATOM   1724 O  O   . THR   A 1 205 ? 14.610 10.282  23.548  1.00 11.97 ? 205 THR   A O   1 
ATOM   1725 C  CB  . THR   A 1 205 ? 17.356 11.082  23.193  1.00 12.90 ? 205 THR   A CB  1 
ATOM   1726 O  OG1 . THR   A 1 205 ? 17.526 10.318  21.995  1.00 12.97 ? 205 THR   A OG1 1 
ATOM   1727 C  CG2 . THR   A 1 205 ? 18.629 11.787  23.588  1.00 13.90 ? 205 THR   A CG2 1 
ATOM   1728 N  N   . VAL   A 1 206 ? 15.306 8.236   24.214  1.00 10.07 ? 206 VAL   A N   1 
ATOM   1729 C  CA  . VAL   A 1 206 ? 14.088 7.526   23.828  1.00 9.92  ? 206 VAL   A CA  1 
ATOM   1730 C  C   . VAL   A 1 206 ? 13.333 7.069   25.059  1.00 9.89  ? 206 VAL   A C   1 
ATOM   1731 O  O   . VAL   A 1 206 ? 13.872 6.408   25.941  1.00 11.19 ? 206 VAL   A O   1 
ATOM   1732 C  CB  . VAL   A 1 206 ? 14.382 6.313   22.934  1.00 10.44 ? 206 VAL   A CB  1 
ATOM   1733 C  CG1 . VAL   A 1 206 ? 13.078 5.580   22.591  1.00 10.26 ? 206 VAL   A CG1 1 
ATOM   1734 C  CG2 . VAL   A 1 206 ? 15.138 6.701   21.706  1.00 11.08 ? 206 VAL   A CG2 1 
ATOM   1735 N  N   . THR   A 1 207 ? 11.996 7.380   25.111  1.00 10.14 ? 207 THR   A N   1 
ATOM   1736 C  CA  . THR   A 1 207 ? 11.041 6.664   25.946  1.00 10.35 ? 207 THR   A CA  1 
ATOM   1737 C  C   . THR   A 1 207 ? 10.505 5.493   25.132  1.00 9.60  ? 207 THR   A C   1 
ATOM   1738 O  O   . THR   A 1 207 ? 9.882  5.677   24.097  1.00 10.55 ? 207 THR   A O   1 
ATOM   1739 C  CB  . THR   A 1 207 ? 9.888  7.563   26.406  1.00 10.88 ? 207 THR   A CB  1 
ATOM   1740 O  OG1 . THR   A 1 207 ? 10.413 8.664   27.138  1.00 11.95 ? 207 THR   A OG1 1 
ATOM   1741 C  CG2 . THR   A 1 207 ? 8.948  6.760   27.268  1.00 11.94 ? 207 THR   A CG2 1 
ATOM   1742 N  N   . TRP   A 1 208 ? 10.864 4.280   25.540  1.00 9.08  ? 208 TRP   A N   1 
ATOM   1743 C  CA  . TRP   A 1 208 ? 10.401 3.086   24.871  1.00 9.00  ? 208 TRP   A CA  1 
ATOM   1744 C  C   . TRP   A 1 208 ? 9.026  2.689   25.379  1.00 9.15  ? 208 TRP   A C   1 
ATOM   1745 O  O   . TRP   A 1 208 ? 8.790  2.645   26.585  1.00 9.94  ? 208 TRP   A O   1 
ATOM   1746 C  CB  . TRP   A 1 208 ? 11.404 1.927   25.082  1.00 8.94  ? 208 TRP   A CB  1 
ATOM   1747 C  CG  . TRP   A 1 208 ? 12.526 2.020   24.100  1.00 9.04  ? 208 TRP   A CG  1 
ATOM   1748 C  CD1 . TRP   A 1 208 ? 13.738 2.638   24.241  1.00 9.09  ? 208 TRP   A CD1 1 
ATOM   1749 C  CD2 . TRP   A 1 208 ? 12.477 1.593   22.733  1.00 9.32  ? 208 TRP   A CD2 1 
ATOM   1750 N  NE1 . TRP   A 1 208 ? 14.444 2.589   23.094  1.00 9.89  ? 208 TRP   A NE1 1 
ATOM   1751 C  CE2 . TRP   A 1 208 ? 13.692 1.975   22.121  1.00 9.59  ? 208 TRP   A CE2 1 
ATOM   1752 C  CE3 . TRP   A 1 208 ? 11.501 0.940   21.957  1.00 9.66  ? 208 TRP   A CE3 1 
ATOM   1753 C  CZ2 . TRP   A 1 208 ? 13.962 1.723   20.790  1.00 10.36 ? 208 TRP   A CZ2 1 
ATOM   1754 C  CZ3 . TRP   A 1 208 ? 11.798 0.661   20.660  1.00 10.06 ? 208 TRP   A CZ3 1 
ATOM   1755 C  CH2 . TRP   A 1 208 ? 12.987 1.038   20.083  1.00 10.42 ? 208 TRP   A CH2 1 
ATOM   1756 N  N   . ILE   A 1 209 ? 8.161  2.305   24.425  1.00 9.45  ? 209 ILE   A N   1 
ATOM   1757 C  CA  . ILE   A 1 209 ? 6.840  1.762   24.695  1.00 9.18  ? 209 ILE   A CA  1 
ATOM   1758 C  C   . ILE   A 1 209 ? 6.742  0.505   23.860  1.00 9.44  ? 209 ILE   A C   1 
ATOM   1759 O  O   . ILE   A 1 209 ? 6.696  0.601   22.634  1.00 10.22 ? 209 ILE   A O   1 
ATOM   1760 C  CB  . ILE   A 1 209 ? 5.755  2.795   24.348  1.00 10.24 ? 209 ILE   A CB  1 
ATOM   1761 C  CG1 . ILE   A 1 209 ? 5.939  4.093   25.140  1.00 11.92 ? 209 ILE   A CG1 1 
ATOM   1762 C  CG2 . ILE   A 1 209 ? 4.371  2.191   24.600  1.00 11.78 ? 209 ILE   A CG2 1 
ATOM   1763 C  CD1 . ILE   A 1 209 ? 5.113  5.252   24.667  1.00 12.98 ? 209 ILE   A CD1 1 
ATOM   1764 N  N   . VAL   A 1 210 ? 6.781  -0.651  24.518  1.00 9.62  ? 210 VAL   A N   1 
ATOM   1765 C  CA  . VAL   A 1 210 ? 6.829  -1.928  23.837  1.00 9.46  ? 210 VAL   A CA  1 
ATOM   1766 C  C   . VAL   A 1 210 ? 5.517  -2.659  24.091  1.00 9.64  ? 210 VAL   A C   1 
ATOM   1767 O  O   . VAL   A 1 210 ? 5.156  -2.929  25.217  1.00 10.47 ? 210 VAL   A O   1 
ATOM   1768 C  CB  . VAL   A 1 210 ? 8.024  -2.790  24.275  1.00 9.88  ? 210 VAL   A CB  1 
ATOM   1769 C  CG1 . VAL   A 1 210 ? 8.042  -4.124  23.584  1.00 10.43 ? 210 VAL   A CG1 1 
ATOM   1770 C  CG2 . VAL   A 1 210 ? 9.331  -2.047  24.050  1.00 10.61 ? 210 VAL   A CG2 1 
ATOM   1771 N  N   . LEU   A 1 211 ? 4.759  -2.905  23.013  1.00 9.99  ? 211 LEU   A N   1 
ATOM   1772 C  CA  . LEU   A 1 211 ? 3.481  -3.544  23.160  1.00 10.13 ? 211 LEU   A CA  1 
ATOM   1773 C  C   . LEU   A 1 211 ? 3.664  -5.006  23.547  1.00 10.81 ? 211 LEU   A C   1 
ATOM   1774 O  O   . LEU   A 1 211 ? 4.487  -5.749  23.014  1.00 11.22 ? 211 LEU   A O   1 
ATOM   1775 C  CB  . LEU   A 1 211 ? 2.667  -3.429  21.861  1.00 10.26 ? 211 LEU   A CB  1 
ATOM   1776 C  CG  . LEU   A 1 211 ? 2.273  -2.012  21.488  1.00 11.83 ? 211 LEU   A CG  1 
ATOM   1777 C  CD1 . LEU   A 1 211 ? 1.253  -2.030  20.363  1.00 13.18 ? 211 LEU   A CD1 1 
ATOM   1778 C  CD2 . LEU   A 1 211 ? 1.735  -1.192  22.652  1.00 12.87 ? 211 LEU   A CD2 1 
ATOM   1779 N  N   . LYS   A 1 212 ? 2.790  -5.467  24.442  1.00 11.22 ? 212 LYS   A N   1 
ATOM   1780 C  CA  . LYS   A 1 212 ? 2.805  -6.856  24.883  1.00 12.10 ? 212 LYS   A CA  1 
ATOM   1781 C  C   . LYS   A 1 212 ? 2.338  -7.839  23.812  1.00 11.55 ? 212 LYS   A C   1 
ATOM   1782 O  O   . LYS   A 1 212 ? 2.861  -8.935  23.727  1.00 13.67 ? 212 LYS   A O   1 
ATOM   1783 C  CB  . LYS   A 1 212 ? 1.982  -7.050  26.151  1.00 15.25 ? 212 LYS   A CB  1 
ATOM   1784 C  CG  . LYS   A 1 212 ? 1.861  -8.497  26.592  1.00 18.97 ? 212 LYS   A CG  1 
ATOM   1785 C  CD  . LYS   A 1 212 ? 1.303  -8.671  27.976  1.00 24.67 ? 212 LYS   A CD  1 
ATOM   1786 C  CE  . LYS   A 1 212 ? 0.852  -10.081 28.300  1.00 28.32 ? 212 LYS   A CE  1 
ATOM   1787 N  N   . GLU   A 1 213 ? 1.336  -7.448  23.029  1.00 11.01 ? 213 GLU   A N   1 
ATOM   1788 C  CA  . GLU   A 1 213 ? 0.727  -8.349  22.064  1.00 11.26 ? 213 GLU   A CA  1 
ATOM   1789 C  C   . GLU   A 1 213 ? 1.488  -8.247  20.759  1.00 10.97 ? 213 GLU   A C   1 
ATOM   1790 O  O   . GLU   A 1 213 ? 1.536  -7.165  20.139  1.00 11.35 ? 213 GLU   A O   1 
ATOM   1791 C  CB  . GLU   A 1 213 ? -0.735 -7.961  21.842  1.00 12.64 ? 213 GLU   A CB  1 
ATOM   1792 C  CG  . GLU   A 1 213 ? -1.491 -8.864  20.890  1.00 15.36 ? 213 GLU   A CG  1 
ATOM   1793 C  CD  . GLU   A 1 213 ? -2.927 -8.409  20.577  1.00 16.92 ? 213 GLU   A CD  1 
ATOM   1794 O  OE1 . GLU   A 1 213 ? -3.534 -7.830  21.362  1.00 17.54 ? 213 GLU   A OE1 1 
ATOM   1795 O  OE2 . GLU   A 1 213 ? -3.391 -8.569  19.419  1.00 23.65 ? 213 GLU   A OE2 1 
ATOM   1796 N  N   A PRO   A 1 214 ? 2.039  -9.360  20.226  0.50 11.28 ? 214 PRO   A N   1 
ATOM   1797 N  N   B PRO   A 1 214 ? 2.124  -9.335  20.289  0.50 11.65 ? 214 PRO   A N   1 
ATOM   1798 C  CA  A PRO   A 1 214 ? 2.735  -9.328  18.948  0.50 11.20 ? 214 PRO   A CA  1 
ATOM   1799 C  CA  B PRO   A 1 214 ? 2.700  -9.364  18.949  0.50 11.67 ? 214 PRO   A CA  1 
ATOM   1800 C  C   A PRO   A 1 214 ? 1.691  -9.368  17.838  0.50 11.97 ? 214 PRO   A C   1 
ATOM   1801 C  C   B PRO   A 1 214 ? 1.620  -9.210  17.878  0.50 11.69 ? 214 PRO   A C   1 
ATOM   1802 O  O   A PRO   A 1 214 ? 0.615  -9.944  18.035  0.50 12.30 ? 214 PRO   A O   1 
ATOM   1803 O  O   B PRO   A 1 214 ? 0.448  -9.491  18.139  0.50 11.88 ? 214 PRO   A O   1 
ATOM   1804 C  CB  A PRO   A 1 214 ? 3.549  -10.631 18.971  0.50 11.23 ? 214 PRO   A CB  1 
ATOM   1805 C  CB  B PRO   A 1 214 ? 3.338  -10.764 18.848  0.50 12.22 ? 214 PRO   A CB  1 
ATOM   1806 C  CG  A PRO   A 1 214 ? 2.635  -11.594 19.673  0.50 11.44 ? 214 PRO   A CG  1 
ATOM   1807 C  CG  B PRO   A 1 214 ? 3.553  -11.175 20.282  0.50 13.31 ? 214 PRO   A CG  1 
ATOM   1808 C  CD  A PRO   A 1 214 ? 1.957  -10.737 20.736  0.50 12.00 ? 214 PRO   A CD  1 
ATOM   1809 C  CD  B PRO   A 1 214 ? 2.383  -10.579 21.024  0.50 12.37 ? 214 PRO   A CD  1 
ATOM   1810 N  N   . ILE   A 1 215 ? 2.066  -8.839  16.676  1.00 11.75 ? 215 ILE   A N   1 
ATOM   1811 C  CA  . ILE   A 1 215 ? 1.297  -9.068  15.466  1.00 12.54 ? 215 ILE   A CA  1 
ATOM   1812 C  C   . ILE   A 1 215 ? 1.796  -10.344 14.825  1.00 12.39 ? 215 ILE   A C   1 
ATOM   1813 O  O   . ILE   A 1 215 ? 2.956  -10.704 14.942  1.00 13.46 ? 215 ILE   A O   1 
ATOM   1814 C  CB  . ILE   A 1 215 ? 1.292  -7.875  14.495  1.00 13.07 ? 215 ILE   A CB  1 
ATOM   1815 C  CG1 . ILE   A 1 215 ? 2.704  -7.547  13.980  1.00 12.07 ? 215 ILE   A CG1 1 
ATOM   1816 C  CG2 . ILE   A 1 215 ? 0.621  -6.667  15.141  1.00 13.34 ? 215 ILE   A CG2 1 
ATOM   1817 C  CD1 . ILE   A 1 215 ? 2.713  -6.550  12.807  1.00 13.44 ? 215 ILE   A CD1 1 
ATOM   1818 N  N   A SER   A 1 216 ? 0.887  -11.069 14.147  0.50 12.78 ? 216 SER   A N   1 
ATOM   1819 N  N   B SER   A 1 216 ? 0.884  -11.018 14.115  0.50 13.46 ? 216 SER   A N   1 
ATOM   1820 C  CA  A SER   A 1 216 ? 1.244  -12.216 13.318  0.50 12.88 ? 216 SER   A CA  1 
ATOM   1821 C  CA  B SER   A 1 216 ? 1.207  -12.197 13.330  0.50 14.17 ? 216 SER   A CA  1 
ATOM   1822 C  C   A SER   A 1 216 ? 1.454  -11.737 11.899  0.50 12.46 ? 216 SER   A C   1 
ATOM   1823 C  C   B SER   A 1 216 ? 1.427  -11.769 11.889  0.50 13.28 ? 216 SER   A C   1 
ATOM   1824 O  O   A SER   A 1 216 ? 0.626  -10.968 11.378  0.50 13.51 ? 216 SER   A O   1 
ATOM   1825 O  O   B SER   A 1 216 ? 0.584  -11.044 11.333  0.50 14.70 ? 216 SER   A O   1 
ATOM   1826 C  CB  A SER   A 1 216 ? 0.222  -13.323 13.355  0.50 14.65 ? 216 SER   A CB  1 
ATOM   1827 C  CB  B SER   A 1 216 ? 0.127  -13.242 13.443  0.50 17.15 ? 216 SER   A CB  1 
ATOM   1828 O  OG  A SER   A 1 216 ? 0.176  -13.887 14.640  0.50 14.79 ? 216 SER   A OG  1 
ATOM   1829 O  OG  B SER   A 1 216 ? 0.521  -14.400 12.741  0.50 20.52 ? 216 SER   A OG  1 
ATOM   1830 N  N   . VAL   A 1 217 ? 2.532  -12.233 11.296  1.00 12.90 ? 217 VAL   A N   1 
ATOM   1831 C  CA  . VAL   A 1 217 ? 2.775  -12.081 9.873   1.00 12.32 ? 217 VAL   A CA  1 
ATOM   1832 C  C   . VAL   A 1 217 ? 3.032  -13.451 9.288   1.00 13.26 ? 217 VAL   A C   1 
ATOM   1833 O  O   . VAL   A 1 217 ? 3.411  -14.364 10.004  1.00 13.93 ? 217 VAL   A O   1 
ATOM   1834 C  CB  . VAL   A 1 217 ? 3.962  -11.144 9.628   1.00 13.09 ? 217 VAL   A CB  1 
ATOM   1835 C  CG1 . VAL   A 1 217 ? 3.768  -9.796  10.302  1.00 13.52 ? 217 VAL   A CG1 1 
ATOM   1836 C  CG2 . VAL   A 1 217 ? 5.273  -11.782 10.116  1.00 14.46 ? 217 VAL   A CG2 1 
ATOM   1837 N  N   . SER   A 1 218 ? 2.846  -13.590 7.984   1.00 12.84 ? 218 SER   A N   1 
ATOM   1838 C  CA  . SER   A 1 218 ? 3.065  -14.899 7.388   1.00 13.69 ? 218 SER   A CA  1 
ATOM   1839 C  C   . SER   A 1 218 ? 4.536  -15.151 7.113   1.00 14.29 ? 218 SER   A C   1 
ATOM   1840 O  O   . SER   A 1 218 ? 5.345  -14.242 6.964   1.00 14.04 ? 218 SER   A O   1 
ATOM   1841 C  CB  . SER   A 1 218 ? 2.239  -15.124 6.150   1.00 13.63 ? 218 SER   A CB  1 
ATOM   1842 O  OG  . SER   A 1 218 ? 2.674  -14.214 5.175   1.00 14.13 ? 218 SER   A OG  1 
ATOM   1843 N  N   A SER   A 1 219 ? 4.852  -16.438 6.954   0.50 14.68 ? 219 SER   A N   1 
ATOM   1844 N  N   B SER   A 1 219 ? 4.874  -16.414 6.932   0.50 14.86 ? 219 SER   A N   1 
ATOM   1845 C  CA  A SER   A 1 219 ? 6.176  -16.844 6.519   0.50 15.99 ? 219 SER   A CA  1 
ATOM   1846 C  CA  B SER   A 1 219 ? 6.219  -16.777 6.545   0.50 16.37 ? 219 SER   A CA  1 
ATOM   1847 C  C   A SER   A 1 219 ? 6.536  -16.100 5.235   0.50 15.67 ? 219 SER   A C   1 
ATOM   1848 C  C   B SER   A 1 219 ? 6.578  -16.174 5.180   0.50 15.64 ? 219 SER   A C   1 
ATOM   1849 O  O   A SER   A 1 219 ? 7.595  -15.487 5.156   0.50 15.53 ? 219 SER   A O   1 
ATOM   1850 O  O   B SER   A 1 219 ? 7.710  -15.773 4.940   0.50 16.38 ? 219 SER   A O   1 
ATOM   1851 C  CB  A SER   A 1 219 ? 6.293  -18.369 6.364   0.50 17.02 ? 219 SER   A CB  1 
ATOM   1852 C  CB  B SER   A 1 219 ? 6.293  -18.274 6.553   0.50 17.90 ? 219 SER   A CB  1 
ATOM   1853 O  OG  A SER   A 1 219 ? 5.421  -18.943 5.385   0.50 16.56 ? 219 SER   A OG  1 
ATOM   1854 O  OG  B SER   A 1 219 ? 7.585  -18.721 6.222   0.50 19.16 ? 219 SER   A OG  1 
ATOM   1855 N  N   . GLU   A 1 220 ? 5.588  -16.033 4.274   1.00 15.38 ? 220 GLU   A N   1 
ATOM   1856 C  CA  . GLU   A 1 220 ? 5.857  -15.420 2.978   1.00 15.89 ? 220 GLU   A CA  1 
ATOM   1857 C  C   . GLU   A 1 220 ? 6.235  -13.945 3.151   1.00 13.96 ? 220 GLU   A C   1 
ATOM   1858 O  O   . GLU   A 1 220 ? 7.047  -13.392 2.411   1.00 15.69 ? 220 GLU   A O   1 
ATOM   1859 C  CB  . GLU   A 1 220 ? 4.680  -15.538 2.012   1.00 16.18 ? 220 GLU   A CB  1 
ATOM   1860 C  CG  . GLU   A 1 220 ? 4.386  -16.952 1.640   1.00 18.72 ? 220 GLU   A CG  1 
ATOM   1861 C  CD  . GLU   A 1 220 ? 3.374  -17.654 2.519   1.00 21.20 ? 220 GLU   A CD  1 
ATOM   1862 O  OE1 . GLU   A 1 220 ? 3.171  -17.283 3.653   1.00 21.02 ? 220 GLU   A OE1 1 
ATOM   1863 O  OE2 . GLU   A 1 220 ? 2.754  -18.590 2.016   1.00 30.49 ? 220 GLU   A OE2 1 
ATOM   1864 N  N   . GLN   A 1 221 ? 5.548  -13.263 4.080   1.00 13.87 ? 221 GLN   A N   1 
ATOM   1865 C  CA  . GLN   A 1 221 ? 5.816  -11.855 4.316   1.00 13.78 ? 221 GLN   A CA  1 
ATOM   1866 C  C   . GLN   A 1 221 ? 7.245  -11.650 4.844   1.00 13.13 ? 221 GLN   A C   1 
ATOM   1867 O  O   . GLN   A 1 221 ? 7.975  -10.794 4.354   1.00 13.70 ? 221 GLN   A O   1 
ATOM   1868 C  CB  . GLN   A 1 221 ? 4.753  -11.281 5.243   1.00 12.68 ? 221 GLN   A CB  1 
ATOM   1869 C  CG  . GLN   A 1 221 ? 3.381  -11.143 4.567   1.00 12.80 ? 221 GLN   A CG  1 
ATOM   1870 C  CD  . GLN   A 1 221 ? 2.295  -10.595 5.450   1.00 12.37 ? 221 GLN   A CD  1 
ATOM   1871 O  OE1 . GLN   A 1 221 ? 2.153  -10.937 6.623   1.00 12.79 ? 221 GLN   A OE1 1 
ATOM   1872 N  NE2 . GLN   A 1 221 ? 1.479  -9.750  4.849   1.00 13.36 ? 221 GLN   A NE2 1 
ATOM   1873 N  N   . VAL   A 1 222 ? 7.650  -12.395 5.895   1.00 13.75 ? 222 VAL   A N   1 
ATOM   1874 C  CA  . VAL   A 1 222 ? 8.961  -12.166 6.474   1.00 14.47 ? 222 VAL   A CA  1 
ATOM   1875 C  C   . VAL   A 1 222 ? 10.049 -12.657 5.501   1.00 14.87 ? 222 VAL   A C   1 
ATOM   1876 O  O   . VAL   A 1 222 ? 11.114 -12.060 5.422   1.00 15.16 ? 222 VAL   A O   1 
ATOM   1877 C  CB  . VAL   A 1 222 ? 9.062  -12.781 7.887   1.00 17.30 ? 222 VAL   A CB  1 
ATOM   1878 C  CG1 . VAL   A 1 222 ? 9.096  -14.293 7.884   1.00 20.12 ? 222 VAL   A CG1 1 
ATOM   1879 C  CG2 . VAL   A 1 222 ? 10.319 -12.257 8.600   1.00 18.72 ? 222 VAL   A CG2 1 
ATOM   1880 N  N   . LEU   A 1 223 ? 9.784  -13.681 4.681   1.00 15.60 ? 223 LEU   A N   1 
ATOM   1881 C  CA  . LEU   A 1 223 ? 10.736 -14.123 3.671   1.00 16.88 ? 223 LEU   A CA  1 
ATOM   1882 C  C   . LEU   A 1 223 ? 11.049 -12.998 2.700   1.00 16.53 ? 223 LEU   A C   1 
ATOM   1883 O  O   . LEU   A 1 223 ? 12.188 -12.895 2.234   1.00 18.10 ? 223 LEU   A O   1 
ATOM   1884 C  CB  . LEU   A 1 223 ? 10.254 -15.397 2.977   1.00 20.06 ? 223 LEU   A CB  1 
ATOM   1885 C  CG  . LEU   A 1 223 ? 10.529 -16.667 3.782   1.00 23.65 ? 223 LEU   A CG  1 
ATOM   1886 C  CD1 . LEU   A 1 223 ? 9.688  -17.830 3.260   1.00 26.01 ? 223 LEU   A CD1 1 
ATOM   1887 C  CD2 . LEU   A 1 223 ? 12.021 -17.008 3.821   1.00 25.66 ? 223 LEU   A CD2 1 
ATOM   1888 N  N   . LYS   A 1 224 ? 10.086 -12.121 2.419   1.00 15.53 ? 224 LYS   A N   1 
ATOM   1889 C  CA  . LYS   A 1 224 ? 10.357 -11.018 1.522   1.00 16.50 ? 224 LYS   A CA  1 
ATOM   1890 C  C   . LYS   A 1 224 ? 11.253 -9.962  2.167   1.00 14.42 ? 224 LYS   A C   1 
ATOM   1891 O  O   . LYS   A 1 224 ? 12.064 -9.355  1.480   1.00 15.59 ? 224 LYS   A O   1 
ATOM   1892 C  CB  . LYS   A 1 224 ? 9.026  -10.472 0.998   1.00 18.81 ? 224 LYS   A CB  1 
ATOM   1893 C  CG  . LYS   A 1 224 ? 8.249  -11.430 0.093   1.00 22.68 ? 224 LYS   A CG  1 
ATOM   1894 N  N   . PHE   A 1 225 ? 11.144 -9.761  3.475   1.00 13.27 ? 225 PHE   A N   1 
ATOM   1895 C  CA  . PHE   A 1 225 ? 12.101 -8.893  4.152   1.00 12.59 ? 225 PHE   A CA  1 
ATOM   1896 C  C   . PHE   A 1 225 ? 13.514 -9.405  3.918   1.00 13.06 ? 225 PHE   A C   1 
ATOM   1897 O  O   . PHE   A 1 225 ? 14.454 -8.613  3.714   1.00 13.51 ? 225 PHE   A O   1 
ATOM   1898 C  CB  . PHE   A 1 225 ? 11.889 -8.868  5.674   1.00 12.56 ? 225 PHE   A CB  1 
ATOM   1899 C  CG  . PHE   A 1 225 ? 10.691 -8.143  6.237   1.00 13.19 ? 225 PHE   A CG  1 
ATOM   1900 C  CD1 . PHE   A 1 225 ? 9.616  -7.694  5.496   1.00 14.27 ? 225 PHE   A CD1 1 
ATOM   1901 C  CD2 . PHE   A 1 225 ? 10.602 -7.975  7.622   1.00 14.15 ? 225 PHE   A CD2 1 
ATOM   1902 C  CE1 . PHE   A 1 225 ? 8.570  -7.011  6.098   1.00 15.78 ? 225 PHE   A CE1 1 
ATOM   1903 C  CE2 . PHE   A 1 225 ? 9.550  -7.317  8.224   1.00 16.22 ? 225 PHE   A CE2 1 
ATOM   1904 C  CZ  . PHE   A 1 225 ? 8.530  -6.825  7.450   1.00 15.90 ? 225 PHE   A CZ  1 
ATOM   1905 N  N   . ARG   A 1 226 ? 13.689 -10.727 3.994   1.00 12.75 ? 226 ARG   A N   1 
ATOM   1906 C  CA  . ARG   A 1 226 ? 15.010 -11.353 3.921   1.00 13.62 ? 226 ARG   A CA  1 
ATOM   1907 C  C   . ARG   A 1 226 ? 15.595 -11.374 2.516   1.00 14.64 ? 226 ARG   A C   1 
ATOM   1908 O  O   . ARG   A 1 226 ? 16.726 -11.825 2.343   1.00 17.25 ? 226 ARG   A O   1 
ATOM   1909 C  CB  . ARG   A 1 226 ? 14.943 -12.776 4.475   1.00 14.90 ? 226 ARG   A CB  1 
ATOM   1910 C  CG  . ARG   A 1 226 ? 14.498 -12.874 5.925   1.00 13.72 ? 226 ARG   A CG  1 
ATOM   1911 C  CD  . ARG   A 1 226 ? 14.547 -14.287 6.418   1.00 15.20 ? 226 ARG   A CD  1 
ATOM   1912 N  NE  . ARG   A 1 226 ? 14.019 -14.465 7.744   1.00 14.56 ? 226 ARG   A NE  1 
ATOM   1913 C  CZ  . ARG   A 1 226 ? 13.063 -15.307 8.074   1.00 15.35 ? 226 ARG   A CZ  1 
ATOM   1914 N  NH1 . ARG   A 1 226 ? 12.596 -16.185 7.208   1.00 18.67 ? 226 ARG   A NH1 1 
ATOM   1915 N  NH2 . ARG   A 1 226 ? 12.527 -15.199 9.269   1.00 17.08 ? 226 ARG   A NH2 1 
ATOM   1916 N  N   . LYS   A 1 227 ? 14.859 -10.861 1.508   1.00 14.27 ? 227 LYS   A N   1 
ATOM   1917 C  CA  . LYS   A 1 227 ? 15.366 -10.768 0.150   1.00 16.21 ? 227 LYS   A CA  1 
ATOM   1918 C  C   . LYS   A 1 227 ? 16.041 -9.422  -0.082  1.00 15.61 ? 227 LYS   A C   1 
ATOM   1919 O  O   . LYS   A 1 227 ? 16.663 -9.227  -1.134  1.00 17.45 ? 227 LYS   A O   1 
ATOM   1920 C  CB  . LYS   A 1 227 ? 14.252 -11.000 -0.886  1.00 19.16 ? 227 LYS   A CB  1 
ATOM   1921 C  CG  . LYS   A 1 227 ? 13.807 -12.452 -0.944  1.00 24.79 ? 227 LYS   A CG  1 
ATOM   1922 C  CD  . LYS   A 1 227 ? 12.736 -12.722 -1.959  1.00 32.09 ? 227 LYS   A CD  1 
ATOM   1923 C  CE  . LYS   A 1 227 ? 12.765 -14.151 -2.467  1.00 41.37 ? 227 LYS   A CE  1 
ATOM   1924 N  NZ  . LYS   A 1 227 ? 12.696 -15.140 -1.357  1.00 46.24 ? 227 LYS   A NZ  1 
ATOM   1925 N  N   . LEU   A 1 228 ? 15.822 -8.465  0.824   1.00 15.03 ? 228 LEU   A N   1 
ATOM   1926 C  CA  . LEU   A 1 228 ? 16.524 -7.186  0.739   1.00 14.52 ? 228 LEU   A CA  1 
ATOM   1927 C  C   . LEU   A 1 228 ? 18.028 -7.395  0.834   1.00 15.56 ? 228 LEU   A C   1 
ATOM   1928 O  O   . LEU   A 1 228 ? 18.483 -8.434  1.300   1.00 15.41 ? 228 LEU   A O   1 
ATOM   1929 C  CB  . LEU   A 1 228 ? 16.020 -6.242  1.829   1.00 14.29 ? 228 LEU   A CB  1 
ATOM   1930 C  CG  . LEU   A 1 228 ? 14.588 -5.740  1.620   1.00 14.93 ? 228 LEU   A CG  1 
ATOM   1931 C  CD1 . LEU   A 1 228 ? 14.081 -5.105  2.898   1.00 15.20 ? 228 LEU   A CD1 1 
ATOM   1932 C  CD2 . LEU   A 1 228 ? 14.474 -4.784  0.452   1.00 16.84 ? 228 LEU   A CD2 1 
ATOM   1933 N  N   . ASN   A 1 229 ? 18.767 -6.367  0.402   1.00 16.44 ? 229 ASN   A N   1 
ATOM   1934 C  CA  . ASN   A 1 229 ? 20.232 -6.397  0.393   1.00 17.18 ? 229 ASN   A CA  1 
ATOM   1935 C  C   . ASN   A 1 229 ? 20.805 -5.261  1.240   1.00 16.01 ? 229 ASN   A C   1 
ATOM   1936 O  O   . ASN   A 1 229 ? 20.301 -4.131  1.200   1.00 15.77 ? 229 ASN   A O   1 
ATOM   1937 C  CB  . ASN   A 1 229 ? 20.786 -6.197  -1.023  1.00 18.56 ? 229 ASN   A CB  1 
ATOM   1938 C  CG  . ASN   A 1 229 ? 20.677 -7.383  -1.953  1.00 20.86 ? 229 ASN   A CG  1 
ATOM   1939 O  OD1 . ASN   A 1 229 ? 21.209 -7.309  -3.058  1.00 25.57 ? 229 ASN   A OD1 1 
ATOM   1940 N  ND2 . ASN   A 1 229 ? 20.081 -8.488  -1.535  1.00 21.87 ? 229 ASN   A ND2 1 
ATOM   1941 N  N   . PHE   A 1 230 ? 21.841 -5.584  2.016   1.00 16.02 ? 230 PHE   A N   1 
ATOM   1942 C  CA  . PHE   A 1 230 ? 22.631 -4.564  2.713   1.00 16.40 ? 230 PHE   A CA  1 
ATOM   1943 C  C   . PHE   A 1 230 ? 23.424 -3.709  1.733   1.00 16.95 ? 230 PHE   A C   1 
ATOM   1944 O  O   . PHE   A 1 230 ? 23.689 -2.537  1.991   1.00 17.18 ? 230 PHE   A O   1 
ATOM   1945 C  CB  . PHE   A 1 230 ? 23.639 -5.213  3.669   1.00 16.79 ? 230 PHE   A CB  1 
ATOM   1946 C  CG  . PHE   A 1 230 ? 23.090 -5.757  4.967   1.00 15.92 ? 230 PHE   A CG  1 
ATOM   1947 C  CD1 . PHE   A 1 230 ? 22.353 -4.949  5.838   1.00 16.75 ? 230 PHE   A CD1 1 
ATOM   1948 C  CD2 . PHE   A 1 230 ? 23.409 -7.044  5.358   1.00 17.51 ? 230 PHE   A CD2 1 
ATOM   1949 C  CE1 . PHE   A 1 230 ? 21.959 -5.444  7.072   1.00 16.29 ? 230 PHE   A CE1 1 
ATOM   1950 C  CE2 . PHE   A 1 230 ? 22.983 -7.536  6.582   1.00 16.59 ? 230 PHE   A CE2 1 
ATOM   1951 C  CZ  . PHE   A 1 230 ? 22.274 -6.728  7.440   1.00 15.81 ? 230 PHE   A CZ  1 
ATOM   1952 N  N   . ASN   A 1 231 ? 23.909 -4.359  0.677   1.00 16.93 ? 231 ASN   A N   1 
ATOM   1953 C  CA  . ASN   A 1 231 ? 24.801 -3.770  -0.298  1.00 18.02 ? 231 ASN   A CA  1 
ATOM   1954 C  C   . ASN   A 1 231 ? 24.054 -2.862  -1.265  1.00 19.23 ? 231 ASN   A C   1 
ATOM   1955 O  O   . ASN   A 1 231 ? 22.837 -2.947  -1.434  1.00 18.81 ? 231 ASN   A O   1 
ATOM   1956 C  CB  . ASN   A 1 231 ? 25.503 -4.853  -1.102  1.00 20.67 ? 231 ASN   A CB  1 
ATOM   1957 C  CG  . ASN   A 1 231 ? 24.473 -5.791  -1.694  1.00 19.76 ? 231 ASN   A CG  1 
ATOM   1958 O  OD1 . ASN   A 1 231 ? 23.972 -6.671  -0.996  1.00 21.04 ? 231 ASN   A OD1 1 
ATOM   1959 N  ND2 . ASN   A 1 231 ? 24.180 -5.618  -2.976  1.00 24.66 ? 231 ASN   A ND2 1 
ATOM   1960 N  N   . GLY   A 1 232 ? 24.830 -1.986  -1.919  1.00 20.31 ? 232 GLY   A N   1 
ATOM   1961 C  CA  . GLY   A 1 232 ? 24.304 -1.211  -3.036  1.00 21.76 ? 232 GLY   A CA  1 
ATOM   1962 C  C   . GLY   A 1 232 ? 24.267 -2.016  -4.332  1.00 23.37 ? 232 GLY   A C   1 
ATOM   1963 O  O   . GLY   A 1 232 ? 24.867 -3.076  -4.432  1.00 25.87 ? 232 GLY   A O   1 
ATOM   1964 N  N   . GLU   A 1 233 ? 23.540 -1.479  -5.318  1.00 25.95 ? 233 GLU   A N   1 
ATOM   1965 C  CA  . GLU   A 1 233 ? 23.447 -2.052  -6.652  1.00 30.11 ? 233 GLU   A CA  1 
ATOM   1966 C  C   . GLU   A 1 233 ? 24.858 -2.160  -7.221  1.00 31.13 ? 233 GLU   A C   1 
ATOM   1967 O  O   . GLU   A 1 233 ? 25.663 -1.252  -7.074  1.00 31.34 ? 233 GLU   A O   1 
ATOM   1968 C  CB  . GLU   A 1 233 ? 22.525 -1.186  -7.522  1.00 33.25 ? 233 GLU   A CB  1 
ATOM   1969 C  CG  . GLU   A 1 233 ? 22.175 -1.756  -8.896  1.00 35.61 ? 233 GLU   A CG  1 
ATOM   1970 C  CD  . GLU   A 1 233 ? 21.326 -0.820  -9.740  1.00 39.78 ? 233 GLU   A CD  1 
ATOM   1971 O  OE1 . GLU   A 1 233 ? 21.118 0.357   -9.329  1.00 41.41 ? 233 GLU   A OE1 1 
ATOM   1972 O  OE2 . GLU   A 1 233 ? 20.928 -1.242  -10.834 1.00 45.94 ? 233 GLU   A OE2 1 
ATOM   1973 N  N   . GLY   A 1 234 ? 25.161 -3.314  -7.807  1.00 35.77 ? 234 GLY   A N   1 
ATOM   1974 C  CA  . GLY   A 1 234 ? 26.437 -3.535  -8.466  1.00 39.37 ? 234 GLY   A CA  1 
ATOM   1975 C  C   . GLY   A 1 234 ? 27.587 -3.760  -7.487  1.00 39.91 ? 234 GLY   A C   1 
ATOM   1976 O  O   . GLY   A 1 234 ? 28.742 -3.590  -7.883  1.00 43.53 ? 234 GLY   A O   1 
ATOM   1977 N  N   . GLU   A 1 235 ? 27.245 -4.087  -6.225  1.00 37.94 ? 235 GLU   A N   1 
ATOM   1978 C  CA  . GLU   A 1 235 ? 28.173 -4.634  -5.243  1.00 35.77 ? 235 GLU   A CA  1 
ATOM   1979 C  C   . GLU   A 1 235 ? 27.798 -6.085  -4.982  1.00 34.94 ? 235 GLU   A C   1 
ATOM   1980 O  O   . GLU   A 1 235 ? 26.687 -6.504  -5.294  1.00 35.07 ? 235 GLU   A O   1 
ATOM   1981 C  CB  . GLU   A 1 235 ? 28.114 -3.882  -3.914  1.00 34.70 ? 235 GLU   A CB  1 
ATOM   1982 C  CG  . GLU   A 1 235 ? 28.549 -2.441  -4.037  1.00 35.36 ? 235 GLU   A CG  1 
ATOM   1983 C  CD  . GLU   A 1 235 ? 28.248 -1.544  -2.846  1.00 38.83 ? 235 GLU   A CD  1 
ATOM   1984 O  OE1 . GLU   A 1 235 ? 27.727 -2.042  -1.820  1.00 35.25 ? 235 GLU   A OE1 1 
ATOM   1985 O  OE2 . GLU   A 1 235 ? 28.532 -0.326  -2.964  1.00 42.36 ? 235 GLU   A OE2 1 
ATOM   1986 N  N   . PRO   A 1 236 ? 28.711 -6.900  -4.408  1.00 35.44 ? 236 PRO   A N   1 
ATOM   1987 C  CA  . PRO   A 1 236 ? 28.401 -8.294  -4.087  1.00 34.56 ? 236 PRO   A CA  1 
ATOM   1988 C  C   . PRO   A 1 236 ? 27.196 -8.359  -3.153  1.00 30.74 ? 236 PRO   A C   1 
ATOM   1989 O  O   . PRO   A 1 236 ? 27.044 -7.523  -2.260  1.00 33.31 ? 236 PRO   A O   1 
ATOM   1990 C  CB  . PRO   A 1 236 ? 29.669 -8.794  -3.390  1.00 36.54 ? 236 PRO   A CB  1 
ATOM   1991 C  CG  . PRO   A 1 236 ? 30.752 -7.900  -3.974  1.00 37.25 ? 236 PRO   A CG  1 
ATOM   1992 C  CD  . PRO   A 1 236 ? 30.099 -6.540  -4.078  1.00 36.06 ? 236 PRO   A CD  1 
ATOM   1993 N  N   . GLU   A 1 237 ? 26.325 -9.347  -3.398  1.00 30.69 ? 237 GLU   A N   1 
ATOM   1994 C  CA  . GLU   A 1 237 ? 25.045 -9.403  -2.703  1.00 28.80 ? 237 GLU   A CA  1 
ATOM   1995 C  C   . GLU   A 1 237 ? 25.249 -9.959  -1.293  1.00 26.59 ? 237 GLU   A C   1 
ATOM   1996 O  O   . GLU   A 1 237 ? 25.788 -11.057 -1.134  1.00 30.13 ? 237 GLU   A O   1 
ATOM   1997 C  CB  . GLU   A 1 237 ? 24.052 -10.296 -3.468  1.00 33.65 ? 237 GLU   A CB  1 
ATOM   1998 C  CG  . GLU   A 1 237 ? 22.671 -10.402 -2.804  1.00 36.79 ? 237 GLU   A CG  1 
ATOM   1999 C  CD  . GLU   A 1 237 ? 21.519 -11.075 -3.553  1.00 40.54 ? 237 GLU   A CD  1 
ATOM   2000 O  OE1 . GLU   A 1 237 ? 21.806 -11.853 -4.477  1.00 48.68 ? 237 GLU   A OE1 1 
ATOM   2001 O  OE2 . GLU   A 1 237 ? 20.312 -10.816 -3.232  1.00 34.63 ? 237 GLU   A OE2 1 
ATOM   2002 N  N   . GLU   A 1 238 ? 24.738 -9.230  -0.302  1.00 21.38 ? 238 GLU   A N   1 
ATOM   2003 C  CA  . GLU   A 1 238 ? 24.704 -9.686  1.073   1.00 20.14 ? 238 GLU   A CA  1 
ATOM   2004 C  C   . GLU   A 1 238 ? 23.305 -9.436  1.589   1.00 19.47 ? 238 GLU   A C   1 
ATOM   2005 O  O   . GLU   A 1 238 ? 22.829 -8.289  1.561   1.00 21.33 ? 238 GLU   A O   1 
ATOM   2006 C  CB  . GLU   A 1 238 ? 25.694 -8.928  1.953   1.00 21.54 ? 238 GLU   A CB  1 
ATOM   2007 N  N   . LEU   A 1 239 ? 22.606 -10.544 1.911   1.00 17.00 ? 239 LEU   A N   1 
ATOM   2008 C  CA  . LEU   A 1 239 ? 21.223 -10.395 2.313   1.00 16.35 ? 239 LEU   A CA  1 
ATOM   2009 C  C   . LEU   A 1 239 ? 21.105 -9.561  3.580   1.00 14.56 ? 239 LEU   A C   1 
ATOM   2010 O  O   . LEU   A 1 239 ? 21.842 -9.797  4.558   1.00 16.39 ? 239 LEU   A O   1 
ATOM   2011 C  CB  . LEU   A 1 239 ? 20.591 -11.775 2.534   1.00 18.18 ? 239 LEU   A CB  1 
ATOM   2012 C  CG  . LEU   A 1 239 ? 20.450 -12.676 1.311   1.00 20.55 ? 239 LEU   A CG  1 
ATOM   2013 C  CD1 . LEU   A 1 239 ? 19.741 -13.982 1.705   1.00 23.06 ? 239 LEU   A CD1 1 
ATOM   2014 C  CD2 . LEU   A 1 239 ? 19.677 -11.957 0.236   1.00 20.28 ? 239 LEU   A CD2 1 
ATOM   2015 N  N   . MET   A 1 240 ? 20.075 -8.686  3.609   1.00 13.77 ? 240 MET   A N   1 
ATOM   2016 C  CA  . MET   A 1 240 ? 19.735 -7.899  4.783   1.00 13.61 ? 240 MET   A CA  1 
ATOM   2017 C  C   . MET   A 1 240 ? 18.933 -8.794  5.724   1.00 13.15 ? 240 MET   A C   1 
ATOM   2018 O  O   . MET   A 1 240 ? 17.714 -8.933  5.603   1.00 13.64 ? 240 MET   A O   1 
ATOM   2019 C  CB  . MET   A 1 240 ? 18.942 -6.662  4.360   1.00 13.83 ? 240 MET   A CB  1 
ATOM   2020 C  CG  . MET   A 1 240 ? 18.617 -5.729  5.538   1.00 13.88 ? 240 MET   A CG  1 
ATOM   2021 S  SD  . MET   A 1 240 ? 17.677 -4.292  5.049   1.00 15.01 ? 240 MET   A SD  1 
ATOM   2022 C  CE  . MET   A 1 240 ? 18.954 -3.278  4.306   1.00 14.77 ? 240 MET   A CE  1 
ATOM   2023 N  N   . VAL   A 1 241 ? 19.664 -9.409  6.680   1.00 13.06 ? 241 VAL   A N   1 
ATOM   2024 C  CA  . VAL   A 1 241 ? 19.089 -10.263 7.697   1.00 12.99 ? 241 VAL   A CA  1 
ATOM   2025 C  C   . VAL   A 1 241 ? 19.891 -10.032 8.970   1.00 12.34 ? 241 VAL   A C   1 
ATOM   2026 O  O   . VAL   A 1 241 ? 21.048 -9.597  8.912   1.00 13.34 ? 241 VAL   A O   1 
ATOM   2027 C  CB  . VAL   A 1 241 ? 19.093 -11.769 7.352   1.00 13.93 ? 241 VAL   A CB  1 
ATOM   2028 C  CG1 . VAL   A 1 241 ? 18.149 -12.092 6.190   1.00 15.34 ? 241 VAL   A CG1 1 
ATOM   2029 C  CG2 . VAL   A 1 241 ? 20.499 -12.301 7.087   1.00 14.17 ? 241 VAL   A CG2 1 
ATOM   2030 N  N   . ASP   A 1 242 ? 19.267 -10.294 10.120  1.00 11.49 ? 242 ASP   A N   1 
ATOM   2031 C  CA  . ASP   A 1 242 ? 19.917 -10.148 11.415  1.00 11.42 ? 242 ASP   A CA  1 
ATOM   2032 C  C   . ASP   A 1 242 ? 20.429 -8.726  11.645  1.00 11.47 ? 242 ASP   A C   1 
ATOM   2033 O  O   . ASP   A 1 242 ? 21.520 -8.477  12.186  1.00 13.28 ? 242 ASP   A O   1 
ATOM   2034 C  CB  . ASP   A 1 242 ? 20.996 -11.218 11.662  1.00 12.17 ? 242 ASP   A CB  1 
ATOM   2035 C  CG  . ASP   A 1 242 ? 20.369 -12.599 11.709  1.00 12.63 ? 242 ASP   A CG  1 
ATOM   2036 O  OD1 . ASP   A 1 242 ? 19.341 -12.763 12.381  1.00 13.10 ? 242 ASP   A OD1 1 
ATOM   2037 O  OD2 . ASP   A 1 242 ? 20.988 -13.526 11.159  1.00 15.23 ? 242 ASP   A OD2 1 
ATOM   2038 N  N   . ASN   A 1 243 ? 19.553 -7.761  11.318  1.00 10.99 ? 243 ASN   A N   1 
ATOM   2039 C  CA  . ASN   A 1 243 ? 19.813 -6.342  11.546  1.00 10.40 ? 243 ASN   A CA  1 
ATOM   2040 C  C   . ASN   A 1 243 ? 19.240 -5.858  12.883  1.00 10.02 ? 243 ASN   A C   1 
ATOM   2041 O  O   . ASN   A 1 243 ? 18.578 -4.828  12.951  1.00 12.25 ? 243 ASN   A O   1 
ATOM   2042 C  CB  . ASN   A 1 243 ? 19.302 -5.507  10.379  1.00 11.47 ? 243 ASN   A CB  1 
ATOM   2043 C  CG  . ASN   A 1 243 ? 17.815 -5.689  10.110  1.00 11.46 ? 243 ASN   A CG  1 
ATOM   2044 O  OD1 . ASN   A 1 243 ? 17.166 -6.561  10.662  1.00 12.78 ? 243 ASN   A OD1 1 
ATOM   2045 N  ND2 . ASN   A 1 243 ? 17.251 -4.829  9.292   1.00 12.52 ? 243 ASN   A ND2 1 
ATOM   2046 N  N   . TRP   A 1 244 ? 19.509 -6.629  13.926  1.00 10.14 ? 244 TRP   A N   1 
ATOM   2047 C  CA  . TRP   A 1 244 ? 19.071 -6.357  15.284  1.00 10.02 ? 244 TRP   A CA  1 
ATOM   2048 C  C   . TRP   A 1 244 ? 20.276 -6.237  16.216  1.00 10.74 ? 244 TRP   A C   1 
ATOM   2049 O  O   . TRP   A 1 244 ? 21.237 -6.983  16.065  1.00 11.78 ? 244 TRP   A O   1 
ATOM   2050 C  CB  . TRP   A 1 244 ? 18.091 -7.447  15.782  1.00 10.77 ? 244 TRP   A CB  1 
ATOM   2051 C  CG  . TRP   A 1 244 ? 18.547 -8.849  15.618  1.00 10.78 ? 244 TRP   A CG  1 
ATOM   2052 C  CD1 . TRP   A 1 244 ? 18.413 -9.616  14.496  1.00 11.52 ? 244 TRP   A CD1 1 
ATOM   2053 C  CD2 . TRP   A 1 244 ? 19.155 -9.709  16.596  1.00 11.27 ? 244 TRP   A CD2 1 
ATOM   2054 N  NE1 . TRP   A 1 244 ? 18.947 -10.869 14.675  1.00 11.82 ? 244 TRP   A NE1 1 
ATOM   2055 C  CE2 . TRP   A 1 244 ? 19.394 -10.948 15.967  1.00 12.27 ? 244 TRP   A CE2 1 
ATOM   2056 C  CE3 . TRP   A 1 244 ? 19.488 -9.552  17.943  1.00 12.30 ? 244 TRP   A CE3 1 
ATOM   2057 C  CZ2 . TRP   A 1 244 ? 19.983 -12.015 16.639  1.00 13.67 ? 244 TRP   A CZ2 1 
ATOM   2058 C  CZ3 . TRP   A 1 244 ? 20.054 -10.610 18.615  1.00 12.95 ? 244 TRP   A CZ3 1 
ATOM   2059 C  CH2 . TRP   A 1 244 ? 20.306 -11.810 17.966  1.00 13.28 ? 244 TRP   A CH2 1 
ATOM   2060 N  N   . ARG   A 1 245 ? 20.141 -5.330  17.164  1.00 11.30 ? 245 ARG   A N   1 
ATOM   2061 C  CA  . ARG   A 1 245 ? 21.051 -5.213  18.304  1.00 10.95 ? 245 ARG   A CA  1 
ATOM   2062 C  C   . ARG   A 1 245 ? 20.587 -6.121  19.407  1.00 11.52 ? 245 ARG   A C   1 
ATOM   2063 O  O   . ARG   A 1 245 ? 19.406 -6.128  19.748  1.00 12.49 ? 245 ARG   A O   1 
ATOM   2064 C  CB  . ARG   A 1 245 ? 21.139 -3.764  18.768  1.00 11.92 ? 245 ARG   A CB  1 
ATOM   2065 C  CG  . ARG   A 1 245 ? 22.294 -3.514  19.752  1.00 11.49 ? 245 ARG   A CG  1 
ATOM   2066 C  CD  . ARG   A 1 245 ? 22.171 -2.195  20.459  1.00 11.05 ? 245 ARG   A CD  1 
ATOM   2067 N  NE  . ARG   A 1 245 ? 23.420 -1.844  21.111  1.00 11.38 ? 245 ARG   A NE  1 
ATOM   2068 C  CZ  . ARG   A 1 245 ? 23.612 -0.825  21.913  1.00 11.54 ? 245 ARG   A CZ  1 
ATOM   2069 N  NH1 . ARG   A 1 245 ? 22.622 -0.021  22.286  1.00 12.32 ? 245 ARG   A NH1 1 
ATOM   2070 N  NH2 . ARG   A 1 245 ? 24.846 -0.571  22.356  1.00 12.57 ? 245 ARG   A NH2 1 
ATOM   2071 N  N   A PRO   A 1 246 ? 21.474 -6.947  20.004  0.50 11.71 ? 246 PRO   A N   1 
ATOM   2072 N  N   B PRO   A 1 246 ? 21.465 -6.912  20.054  0.50 12.00 ? 246 PRO   A N   1 
ATOM   2073 C  CA  A PRO   A 1 246 ? 21.109 -7.682  21.209  0.50 11.60 ? 246 PRO   A CA  1 
ATOM   2074 C  CA  B PRO   A 1 246 ? 20.995 -7.729  21.160  0.50 12.06 ? 246 PRO   A CA  1 
ATOM   2075 C  C   A PRO   A 1 246 ? 20.708 -6.834  22.418  0.50 11.31 ? 246 PRO   A C   1 
ATOM   2076 C  C   B PRO   A 1 246 ? 20.729 -6.880  22.403  0.50 11.85 ? 246 PRO   A C   1 
ATOM   2077 O  O   A PRO   A 1 246 ? 21.002 -5.649  22.509  0.50 11.68 ? 246 PRO   A O   1 
ATOM   2078 O  O   B PRO   A 1 246 ? 21.151 -5.737  22.492  0.50 12.30 ? 246 PRO   A O   1 
ATOM   2079 C  CB  A PRO   A 1 246 ? 22.385 -8.466  21.540  0.50 12.30 ? 246 PRO   A CB  1 
ATOM   2080 C  CB  B PRO   A 1 246 ? 22.145 -8.722  21.342  0.50 12.91 ? 246 PRO   A CB  1 
ATOM   2081 C  CG  A PRO   A 1 246 ? 23.041 -8.634  20.187  0.50 12.34 ? 246 PRO   A CG  1 
ATOM   2082 C  CG  B PRO   A 1 246 ? 23.353 -7.871  21.019  0.50 13.05 ? 246 PRO   A CG  1 
ATOM   2083 C  CD  A PRO   A 1 246 ? 22.821 -7.298  19.522  0.50 12.30 ? 246 PRO   A CD  1 
ATOM   2084 C  CD  B PRO   A 1 246 ? 22.913 -7.044  19.825  0.50 12.38 ? 246 PRO   A CD  1 
ATOM   2085 N  N   . ALA   A 1 247 ? 20.070 -7.508  23.381  1.00 12.04 ? 247 ALA   A N   1 
ATOM   2086 C  CA  . ALA   A 1 247 ? 19.736 -6.885  24.646  1.00 12.11 ? 247 ALA   A CA  1 
ATOM   2087 C  C   . ALA   A 1 247 ? 20.999 -6.357  25.334  1.00 11.59 ? 247 ALA   A C   1 
ATOM   2088 O  O   . ALA   A 1 247 ? 22.004 -7.074  25.406  1.00 13.52 ? 247 ALA   A O   1 
ATOM   2089 C  CB  . ALA   A 1 247 ? 18.955 -7.830  25.542  1.00 13.59 ? 247 ALA   A CB  1 
ATOM   2090 N  N   . GLN   A 1 248 ? 20.853 -5.197  25.928  1.00 11.71 ? 248 GLN   A N   1 
ATOM   2091 C  CA  . GLN   A 1 248 ? 21.888 -4.476  26.651  1.00 12.47 ? 248 GLN   A CA  1 
ATOM   2092 C  C   . GLN   A 1 248 ? 21.565 -4.458  28.126  1.00 13.17 ? 248 GLN   A C   1 
ATOM   2093 O  O   . GLN   A 1 248 ? 20.432 -4.674  28.573  1.00 13.33 ? 248 GLN   A O   1 
ATOM   2094 C  CB  . GLN   A 1 248 ? 21.965 -3.052  26.127  1.00 12.21 ? 248 GLN   A CB  1 
ATOM   2095 C  CG  . GLN   A 1 248 ? 22.302 -2.997  24.641  1.00 13.06 ? 248 GLN   A CG  1 
ATOM   2096 C  CD  . GLN   A 1 248 ? 23.606 -3.681  24.312  1.00 14.71 ? 248 GLN   A CD  1 
ATOM   2097 O  OE1 . GLN   A 1 248 ? 24.642 -3.381  24.898  1.00 16.04 ? 248 GLN   A OE1 1 
ATOM   2098 N  NE2 . GLN   A 1 248 ? 23.568 -4.593  23.362  1.00 14.71 ? 248 GLN   A NE2 1 
ATOM   2099 N  N   . PRO   A 1 249 ? 22.580 -4.186  28.985  1.00 13.93 ? 249 PRO   A N   1 
ATOM   2100 C  CA  . PRO   A 1 249 ? 22.337 -4.199  30.421  1.00 14.58 ? 249 PRO   A CA  1 
ATOM   2101 C  C   . PRO   A 1 249 ? 21.291 -3.203  30.881  1.00 13.72 ? 249 PRO   A C   1 
ATOM   2102 O  O   . PRO   A 1 249 ? 21.345 -2.047  30.529  1.00 13.57 ? 249 PRO   A O   1 
ATOM   2103 C  CB  . PRO   A 1 249 ? 23.730 -3.841  30.966  1.00 16.47 ? 249 PRO   A CB  1 
ATOM   2104 C  CG  . PRO   A 1 249 ? 24.667 -4.324  29.929  1.00 18.22 ? 249 PRO   A CG  1 
ATOM   2105 C  CD  . PRO   A 1 249 ? 24.005 -3.940  28.649  1.00 15.99 ? 249 PRO   A CD  1 
ATOM   2106 N  N   . LEU   A 1 250 ? 20.398 -3.664  31.761  1.00 13.92 ? 250 LEU   A N   1 
ATOM   2107 C  CA  . LEU   A 1 250 ? 19.338 -2.805  32.253  1.00 13.50 ? 250 LEU   A CA  1 
ATOM   2108 C  C   . LEU   A 1 250 ? 19.890 -1.704  33.164  1.00 13.06 ? 250 LEU   A C   1 
ATOM   2109 O  O   . LEU   A 1 250 ? 19.333 -0.607  33.271  1.00 13.73 ? 250 LEU   A O   1 
ATOM   2110 C  CB  . LEU   A 1 250 ? 18.282 -3.660  32.946  1.00 15.43 ? 250 LEU   A CB  1 
ATOM   2111 C  CG  . LEU   A 1 250 ? 17.009 -2.918  33.355  1.00 16.61 ? 250 LEU   A CG  1 
ATOM   2112 C  CD1 . LEU   A 1 250 ? 16.278 -2.306  32.152  1.00 16.62 ? 250 LEU   A CD1 1 
ATOM   2113 C  CD2 . LEU   A 1 250 ? 16.097 -3.876  34.117  1.00 19.89 ? 250 LEU   A CD2 1 
ATOM   2114 N  N   . LYS   A 1 251 ? 20.943 -2.031  33.937  1.00 14.34 ? 251 LYS   A N   1 
ATOM   2115 C  CA  . LYS   A 1 251 ? 21.570 -1.056  34.823  1.00 15.49 ? 251 LYS   A CA  1 
ATOM   2116 C  C   . LYS   A 1 251 ? 20.527 -0.506  35.808  1.00 16.74 ? 251 LYS   A C   1 
ATOM   2117 O  O   . LYS   A 1 251 ? 19.708 -1.254  36.296  1.00 20.45 ? 251 LYS   A O   1 
ATOM   2118 C  CB  . LYS   A 1 251 ? 22.374 -0.018  34.041  1.00 17.45 ? 251 LYS   A CB  1 
ATOM   2119 C  CG  . LYS   A 1 251 ? 23.464 -0.660  33.195  1.00 21.92 ? 251 LYS   A CG  1 
ATOM   2120 C  CD  . LYS   A 1 251 ? 24.560 0.224   32.658  1.00 26.18 ? 251 LYS   A CD  1 
ATOM   2121 C  CE  . LYS   A 1 251 ? 25.780 -0.566  32.233  1.00 29.94 ? 251 LYS   A CE  1 
ATOM   2122 N  N   . ASN   A 1 252 ? 20.536 0.778   36.089  1.00 17.64 ? 252 ASN   A N   1 
ATOM   2123 C  CA  . ASN   A 1 252 ? 19.672 1.287   37.141  1.00 23.05 ? 252 ASN   A CA  1 
ATOM   2124 C  C   . ASN   A 1 252 ? 18.373 1.748   36.491  1.00 24.65 ? 252 ASN   A C   1 
ATOM   2125 O  O   . ASN   A 1 252 ? 18.136 3.001   36.461  1.00 29.51 ? 252 ASN   A O   1 
ATOM   2126 C  CB  . ASN   A 1 252 ? 20.349 2.391   37.977  1.00 26.21 ? 252 ASN   A CB  1 
ATOM   2127 N  N   . ARG   A 1 253 ? 17.619 0.768   35.879  1.00 16.93 ? 253 ARG   A N   1 
ATOM   2128 C  CA  . ARG   A 1 253 ? 16.342 1.146   35.315  1.00 13.80 ? 253 ARG   A CA  1 
ATOM   2129 C  C   . ARG   A 1 253 ? 15.263 0.178   35.760  1.00 15.38 ? 253 ARG   A C   1 
ATOM   2130 O  O   . ARG   A 1 253 ? 15.529 -0.972  36.027  1.00 20.36 ? 253 ARG   A O   1 
ATOM   2131 C  CB  . ARG   A 1 253 ? 16.427 1.189   33.807  1.00 12.50 ? 253 ARG   A CB  1 
ATOM   2132 C  CG  . ARG   A 1 253 ? 17.316 2.312   33.286  1.00 12.13 ? 253 ARG   A CG  1 
ATOM   2133 C  CD  . ARG   A 1 253 ? 17.441 2.257   31.785  1.00 12.47 ? 253 ARG   A CD  1 
ATOM   2134 N  NE  . ARG   A 1 253 ? 18.228 1.116   31.348  1.00 11.52 ? 253 ARG   A NE  1 
ATOM   2135 C  CZ  . ARG   A 1 253 ? 18.479 0.840   30.070  1.00 10.82 ? 253 ARG   A CZ  1 
ATOM   2136 N  NH1 . ARG   A 1 253 ? 17.870 1.508   29.089  1.00 11.00 ? 253 ARG   A NH1 1 
ATOM   2137 N  NH2 . ARG   A 1 253 ? 19.295 -0.151  29.752  1.00 10.36 ? 253 ARG   A NH2 1 
ATOM   2138 N  N   . GLN   A 1 254 ? 14.057 0.705   35.850  1.00 16.59 ? 254 GLN   A N   1 
ATOM   2139 C  CA  . GLN   A 1 254 ? 12.858 -0.055  36.117  1.00 17.07 ? 254 GLN   A CA  1 
ATOM   2140 C  C   . GLN   A 1 254 ? 11.978 -0.047  34.860  1.00 15.08 ? 254 GLN   A C   1 
ATOM   2141 O  O   . GLN   A 1 254 ? 11.763 0.999   34.203  1.00 19.19 ? 254 GLN   A O   1 
ATOM   2142 C  CB  . GLN   A 1 254 ? 12.068 0.575   37.255  1.00 20.73 ? 254 GLN   A CB  1 
ATOM   2143 N  N   . ILE   A 1 255 ? 11.511 -1.220  34.507  1.00 13.70 ? 255 ILE   A N   1 
ATOM   2144 C  CA  . ILE   A 1 255 ? 10.527 -1.375  33.435  1.00 12.75 ? 255 ILE   A CA  1 
ATOM   2145 C  C   . ILE   A 1 255 ? 9.149  -1.418  34.078  1.00 13.02 ? 255 ILE   A C   1 
ATOM   2146 O  O   . ILE   A 1 255 ? 8.943  -2.096  35.098  1.00 14.52 ? 255 ILE   A O   1 
ATOM   2147 C  CB  . ILE   A 1 255 ? 10.773 -2.635  32.625  1.00 12.90 ? 255 ILE   A CB  1 
ATOM   2148 C  CG1 . ILE   A 1 255 ? 12.188 -2.664  32.051  1.00 13.91 ? 255 ILE   A CG1 1 
ATOM   2149 C  CG2 . ILE   A 1 255 ? 9.700  -2.761  31.520  1.00 14.51 ? 255 ILE   A CG2 1 
ATOM   2150 C  CD1 . ILE   A 1 255 ? 12.471 -3.855  31.175  1.00 14.63 ? 255 ILE   A CD1 1 
ATOM   2151 N  N   . LYS   A 1 256 ? 8.239  -0.568  33.594  1.00 12.35 ? 256 LYS   A N   1 
ATOM   2152 C  CA  . LYS   A 1 256 ? 6.897  -0.450  34.146  1.00 13.27 ? 256 LYS   A CA  1 
ATOM   2153 C  C   . LYS   A 1 256 ? 5.926  -1.101  33.167  1.00 13.24 ? 256 LYS   A C   1 
ATOM   2154 O  O   . LYS   A 1 256 ? 6.119  -1.053  31.961  1.00 14.56 ? 256 LYS   A O   1 
ATOM   2155 C  CB  . LYS   A 1 256 ? 6.524  1.013   34.384  1.00 15.54 ? 256 LYS   A CB  1 
ATOM   2156 C  CG  . LYS   A 1 256 ? 7.399  1.755   35.398  1.00 19.34 ? 256 LYS   A CG  1 
ATOM   2157 N  N   . ALA   A 1 257 ? 4.914  -1.757  33.707  1.00 12.84 ? 257 ALA   A N   1 
ATOM   2158 C  CA  . ALA   A 1 257 ? 3.833  -2.350  32.926  1.00 13.70 ? 257 ALA   A CA  1 
ATOM   2159 C  C   . ALA   A 1 257 ? 2.565  -1.511  33.055  1.00 13.02 ? 257 ALA   A C   1 
ATOM   2160 O  O   . ALA   A 1 257 ? 2.206  -1.077  34.135  1.00 15.41 ? 257 ALA   A O   1 
ATOM   2161 C  CB  . ALA   A 1 257 ? 3.578  -3.736  33.370  1.00 14.37 ? 257 ALA   A CB  1 
ATOM   2162 N  N   . SER   A 1 258 ? 1.819  -1.402  31.950  1.00 13.54 ? 258 SER   A N   1 
ATOM   2163 C  CA  . SER   A 1 258 ? 0.565  -0.667  31.947  1.00 14.75 ? 258 SER   A CA  1 
ATOM   2164 C  C   . SER   A 1 258 ? -0.605 -1.532  32.416  1.00 15.68 ? 258 SER   A C   1 
ATOM   2165 O  O   . SER   A 1 258 ? -1.723 -1.011  32.518  1.00 19.29 ? 258 SER   A O   1 
ATOM   2166 C  CB  . SER   A 1 258 ? 0.277  -0.178  30.568  1.00 14.33 ? 258 SER   A CB  1 
ATOM   2167 O  OG  . SER   A 1 258 ? -0.164 -1.199  29.672  1.00 13.93 ? 258 SER   A OG  1 
ATOM   2168 N  N   . PHE   A 1 259 ? -0.337 -2.811  32.661  1.00 16.73 ? 259 PHE   A N   1 
ATOM   2169 C  CA  . PHE   A 1 259 ? -1.369 -3.812  32.852  1.00 18.30 ? 259 PHE   A CA  1 
ATOM   2170 C  C   . PHE   A 1 259 ? -0.958 -4.751  33.976  1.00 22.15 ? 259 PHE   A C   1 
ATOM   2171 O  O   . PHE   A 1 259 ? 0.233  -4.884  34.288  1.00 24.28 ? 259 PHE   A O   1 
ATOM   2172 C  CB  . PHE   A 1 259 ? -1.564 -4.622  31.573  1.00 18.03 ? 259 PHE   A CB  1 
ATOM   2173 C  CG  . PHE   A 1 259 ? -0.306 -5.351  31.169  1.00 17.76 ? 259 PHE   A CG  1 
ATOM   2174 C  CD1 . PHE   A 1 259 ? 0.681  -4.704  30.453  1.00 15.32 ? 259 PHE   A CD1 1 
ATOM   2175 C  CD2 . PHE   A 1 259 ? -0.091 -6.648  31.607  1.00 20.14 ? 259 PHE   A CD2 1 
ATOM   2176 C  CE1 . PHE   A 1 259 ? 1.852  -5.373  30.118  1.00 18.00 ? 259 PHE   A CE1 1 
ATOM   2177 C  CE2 . PHE   A 1 259 ? 1.089  -7.307  31.297  1.00 21.54 ? 259 PHE   A CE2 1 
ATOM   2178 C  CZ  . PHE   A 1 259 ? 2.085  -6.654  30.588  1.00 20.52 ? 259 PHE   A CZ  1 
ATOM   2179 N  N   . LYS   A 1 260 ? -1.988 -5.410  34.534  1.00 27.98 ? 260 LYS   A N   1 
ATOM   2180 C  CA  . LYS   A 1 260 ? -1.818 -6.251  35.703  1.00 35.22 ? 260 LYS   A CA  1 
ATOM   2181 C  C   . LYS   A 1 260 ? -1.713 -7.707  35.229  1.00 40.12 ? 260 LYS   A C   1 
ATOM   2182 O  O   . LYS   A 1 260 ? -1.071 -8.484  35.965  1.00 54.30 ? 260 LYS   A O   1 
ATOM   2183 C  CB  . LYS   A 1 260 ? -2.944 -6.020  36.725  1.00 37.78 ? 260 LYS   A CB  1 
ATOM   2184 O  OXT . LYS   A 1 260 ? -2.254 -8.017  34.135  1.00 44.29 ? 260 LYS   A OXT 1 
HETATM 2185 ZN ZN  . ZN    B 2 .   ? 14.636 0.346   15.212  1.00 9.46  ? 301 ZN    A ZN  1 
HETATM 2186 C  C1  . A1H15 C 3 .   ? 17.664 7.837   14.334  1.00 20.32 ? 302 A1H15 A C1  1 
HETATM 2187 C  C2  . A1H15 C 3 .   ? 17.129 6.533   14.772  1.00 16.52 ? 302 A1H15 A C2  1 
HETATM 2188 C  C3  . A1H15 C 3 .   ? 17.968 5.481   15.076  1.00 14.88 ? 302 A1H15 A C3  1 
HETATM 2189 C  C4  . A1H15 C 3 .   ? 17.454 4.340   15.632  1.00 12.62 ? 302 A1H15 A C4  1 
HETATM 2190 C  C5  . A1H15 C 3 .   ? 16.092 4.257   15.878  1.00 11.59 ? 302 A1H15 A C5  1 
HETATM 2191 C  C6  . A1H15 C 3 .   ? 15.261 5.323   15.587  1.00 12.93 ? 302 A1H15 A C6  1 
HETATM 2192 C  C7  . A1H15 C 3 .   ? 15.782 6.432   14.994  1.00 15.92 ? 302 A1H15 A C7  1 
HETATM 2193 S  S8  . A1H15 C 3 .   ? 15.418 2.843   16.700  1.00 10.33 ? 302 A1H15 A S8  1 
HETATM 2194 N  N9  . A1H15 C 3 .   ? 15.972 1.555   15.958  1.00 10.14 ? 302 A1H15 A N9  1 
HETATM 2195 O  O10 . A1H15 C 3 .   ? 15.896 2.900   18.069  1.00 9.94  ? 302 A1H15 A O10 1 
HETATM 2196 O  O11 . A1H15 C 3 .   ? 13.968 2.917   16.514  1.00 10.61 ? 302 A1H15 A O11 1 
HETATM 2197 N  N12 . A1H15 C 3 .   ? 18.127 7.678   13.028  1.00 32.34 ? 302 A1H15 A N12 1 
HETATM 2198 C  C13 . A1H15 C 3 .   ? 19.369 7.888   12.987  1.00 34.65 ? 302 A1H15 A C13 1 
HETATM 2199 N  N14 . A1H15 C 3 .   ? 19.970 6.739   12.586  1.00 35.33 ? 302 A1H15 A N14 1 
HETATM 2200 C  C15 . A1H15 C 3 .   ? 20.994 6.678   11.696  1.00 42.02 ? 302 A1H15 A C15 1 
HETATM 2201 N  N16 . A1H15 C 3 .   ? 22.041 5.942   11.977  1.00 43.65 ? 302 A1H15 A N16 1 
HETATM 2202 N  N17 . A1H15 C 3 .   ? 19.874 9.079   13.236  1.00 38.72 ? 302 A1H15 A N17 1 
HETATM 2203 N  N18 . A1H15 C 3 .   ? 20.701 7.105   10.487  1.00 50.43 ? 302 A1H15 A N18 1 
HETATM 2204 O  O   . HOH   D 4 .   ? 23.574 1.629   7.507   0.50 41.79 ? 401 HOH   A O   1 
HETATM 2205 O  O   . HOH   D 4 .   ? 18.975 2.667   10.054  0.50 25.36 ? 402 HOH   A O   1 
HETATM 2206 O  O   . HOH   D 4 .   ? 24.592 0.231   8.228   0.50 37.35 ? 403 HOH   A O   1 
HETATM 2207 O  O   . HOH   D 4 .   ? 10.035 -13.034 34.311  0.50 19.55 ? 404 HOH   A O   1 
HETATM 2208 O  O   . HOH   D 4 .   ? 5.730  21.457  13.227  0.50 16.01 ? 405 HOH   A O   1 
HETATM 2209 O  O   . HOH   D 4 .   ? -5.996 8.526   20.904  0.50 75.39 ? 406 HOH   A O   1 
HETATM 2210 O  O   . HOH   D 4 .   ? 35.675 2.029   15.021  1.00 36.39 ? 407 HOH   A O   1 
HETATM 2211 O  O   . HOH   D 4 .   ? 12.591 -2.031  7.800   1.00 29.14 ? 408 HOH   A O   1 
HETATM 2212 O  O   . HOH   D 4 .   ? 2.319  19.576  18.799  1.00 30.79 ? 409 HOH   A O   1 
HETATM 2213 O  O   . HOH   D 4 .   ? 0.283  -5.114  -2.062  1.00 31.91 ? 410 HOH   A O   1 
HETATM 2214 O  O   . HOH   D 4 .   ? 3.373  -20.172 6.089   1.00 19.70 ? 411 HOH   A O   1 
HETATM 2215 O  O   . HOH   D 4 .   ? -4.166 11.498  13.217  1.00 31.08 ? 412 HOH   A O   1 
HETATM 2216 O  O   . HOH   D 4 .   ? 28.607 -6.323  -0.712  1.00 41.54 ? 413 HOH   A O   1 
HETATM 2217 O  O   . HOH   D 4 .   ? -6.201 5.021   23.717  0.50 21.56 ? 414 HOH   A O   1 
HETATM 2218 O  O   . HOH   D 4 .   ? 21.820 -7.653  -5.488  1.00 42.42 ? 415 HOH   A O   1 
HETATM 2219 O  O   . HOH   D 4 .   ? 7.068  16.647  27.106  1.00 30.36 ? 416 HOH   A O   1 
HETATM 2220 O  O   . HOH   D 4 .   ? -4.328 -3.072  13.391  0.50 16.99 ? 417 HOH   A O   1 
HETATM 2221 O  O   . HOH   D 4 .   ? 11.791 7.302   3.316   1.00 36.19 ? 418 HOH   A O   1 
HETATM 2222 O  O   . HOH   D 4 .   ? 26.527 -9.010  19.306  1.00 43.22 ? 419 HOH   A O   1 
HETATM 2223 O  O   . HOH   D 4 .   ? 8.207  -20.172 8.587   1.00 31.66 ? 420 HOH   A O   1 
HETATM 2224 O  O   . HOH   D 4 .   ? -1.562 -13.077 16.385  1.00 41.72 ? 421 HOH   A O   1 
HETATM 2225 O  O   . HOH   D 4 .   ? -0.504 -12.145 18.830  1.00 39.98 ? 422 HOH   A O   1 
HETATM 2226 O  O   . HOH   D 4 .   ? 0.722  10.504  30.006  1.00 32.12 ? 423 HOH   A O   1 
HETATM 2227 O  O   . HOH   D 4 .   ? 5.760  2.633   -4.899  1.00 44.62 ? 424 HOH   A O   1 
HETATM 2228 O  O   . HOH   D 4 .   ? -2.840 -1.478  29.647  0.50 21.09 ? 425 HOH   A O   1 
HETATM 2229 O  O   . HOH   D 4 .   ? 19.027 3.802   12.314  1.00 23.68 ? 426 HOH   A O   1 
HETATM 2230 O  O   . HOH   D 4 .   ? 16.155 4.425   37.411  1.00 27.80 ? 427 HOH   A O   1 
HETATM 2231 O  O   . HOH   D 4 .   ? 0.381  20.890  13.890  1.00 31.16 ? 428 HOH   A O   1 
HETATM 2232 O  O   . HOH   D 4 .   ? 19.989 -2.162  15.763  1.00 11.56 ? 429 HOH   A O   1 
HETATM 2233 O  O   . HOH   D 4 .   ? 4.766  -13.161 33.138  1.00 39.72 ? 430 HOH   A O   1 
HETATM 2234 O  O   . HOH   D 4 .   ? 15.881 2.426   9.193   1.00 31.50 ? 431 HOH   A O   1 
HETATM 2235 O  O   . HOH   D 4 .   ? 32.926 -4.961  22.419  1.00 27.76 ? 432 HOH   A O   1 
HETATM 2236 O  O   . HOH   D 4 .   ? -2.827 10.688  20.197  1.00 24.23 ? 433 HOH   A O   1 
HETATM 2237 O  O   . HOH   D 4 .   ? 1.651  19.411  6.207   1.00 28.23 ? 434 HOH   A O   1 
HETATM 2238 O  O   . HOH   D 4 .   ? 6.442  11.647  31.421  1.00 36.53 ? 435 HOH   A O   1 
HETATM 2239 O  O   . HOH   D 4 .   ? 32.861 1.577   15.793  0.50 18.73 ? 436 HOH   A O   1 
HETATM 2240 O  O   . HOH   D 4 .   ? 20.010 11.450  27.947  1.00 48.95 ? 437 HOH   A O   1 
HETATM 2241 O  O   . HOH   D 4 .   ? 31.056 -2.369  -7.456  1.00 32.42 ? 438 HOH   A O   1 
HETATM 2242 O  O   . HOH   D 4 .   ? 12.116 8.058   29.089  1.00 23.20 ? 439 HOH   A O   1 
HETATM 2243 O  O   . HOH   D 4 .   ? 24.917 6.889   29.982  1.00 21.08 ? 440 HOH   A O   1 
HETATM 2244 O  O   . HOH   D 4 .   ? 32.981 0.736   12.344  0.50 39.97 ? 441 HOH   A O   1 
HETATM 2245 O  O   . HOH   D 4 .   ? 10.781 -16.241 17.241  1.00 19.59 ? 442 HOH   A O   1 
HETATM 2246 O  O   . HOH   D 4 .   ? 25.531 -1.454  26.517  1.00 24.41 ? 443 HOH   A O   1 
HETATM 2247 O  O   . HOH   D 4 .   ? 11.460 17.942  29.907  1.00 32.47 ? 444 HOH   A O   1 
HETATM 2248 O  O   . HOH   D 4 .   ? 4.602  -9.313  36.611  1.00 45.03 ? 445 HOH   A O   1 
HETATM 2249 O  O   . HOH   D 4 .   ? 1.730  -18.834 5.285   1.00 27.76 ? 446 HOH   A O   1 
HETATM 2250 O  O   . HOH   D 4 .   ? 16.593 -9.860  32.091  1.00 23.95 ? 447 HOH   A O   1 
HETATM 2251 O  O   . HOH   D 4 .   ? 8.393  15.346  32.113  1.00 33.90 ? 448 HOH   A O   1 
HETATM 2252 O  O   . HOH   D 4 .   ? 23.469 9.960   27.705  1.00 46.26 ? 449 HOH   A O   1 
HETATM 2253 O  O   . HOH   D 4 .   ? 21.380 0.546   -4.810  1.00 23.32 ? 450 HOH   A O   1 
HETATM 2254 O  O   . HOH   D 4 .   ? 11.063 -10.503 40.006  1.00 35.62 ? 451 HOH   A O   1 
HETATM 2255 O  O   . HOH   D 4 .   ? 18.687 -6.633  29.155  1.00 13.75 ? 452 HOH   A O   1 
HETATM 2256 O  O   . HOH   D 4 .   ? 22.575 10.495  24.230  1.00 55.45 ? 453 HOH   A O   1 
HETATM 2257 O  O   . HOH   D 4 .   ? 8.282  -7.201  -3.205  1.00 29.62 ? 454 HOH   A O   1 
HETATM 2258 O  O   . HOH   D 4 .   ? 14.225 -12.764 31.692  1.00 22.89 ? 455 HOH   A O   1 
HETATM 2259 O  O   . HOH   D 4 .   ? 7.451  12.586  27.887  1.00 20.04 ? 456 HOH   A O   1 
HETATM 2260 O  O   . HOH   D 4 .   ? -4.464 9.882   6.301   1.00 30.83 ? 457 HOH   A O   1 
HETATM 2261 O  O   . HOH   D 4 .   ? 0.931  -14.539 3.141   1.00 19.89 ? 458 HOH   A O   1 
HETATM 2262 O  O   . HOH   D 4 .   ? 13.210 -13.516 11.417  1.00 12.87 ? 459 HOH   A O   1 
HETATM 2263 O  O   . HOH   D 4 .   ? 2.404  -19.012 14.968  1.00 29.96 ? 460 HOH   A O   1 
HETATM 2264 O  O   . HOH   D 4 .   ? 1.527  -1.883  41.345  1.00 39.16 ? 461 HOH   A O   1 
HETATM 2265 O  O   . HOH   D 4 .   ? -2.056 -9.224  17.139  1.00 26.24 ? 462 HOH   A O   1 
HETATM 2266 O  O   . HOH   D 4 .   ? 12.731 2.299   -6.554  1.00 37.87 ? 463 HOH   A O   1 
HETATM 2267 O  O   . HOH   D 4 .   ? -4.916 -5.495  30.264  1.00 51.25 ? 464 HOH   A O   1 
HETATM 2268 O  O   . HOH   D 4 .   ? 15.056 -2.921  -6.448  1.00 29.83 ? 465 HOH   A O   1 
HETATM 2269 O  O   . HOH   D 4 .   ? 10.695 10.828  25.510  1.00 14.11 ? 466 HOH   A O   1 
HETATM 2270 O  O   . HOH   D 4 .   ? 23.775 -11.585 5.251   1.00 23.86 ? 467 HOH   A O   1 
HETATM 2271 O  O   . HOH   D 4 .   ? 16.671 -11.528 18.056  1.00 11.92 ? 468 HOH   A O   1 
HETATM 2272 O  O   . HOH   D 4 .   ? 21.147 -17.919 11.100  1.00 36.83 ? 469 HOH   A O   1 
HETATM 2273 O  O   . HOH   D 4 .   ? 18.689 -1.700  11.493  1.00 15.85 ? 470 HOH   A O   1 
HETATM 2274 O  O   . HOH   D 4 .   ? 26.379 9.170   20.543  1.00 22.48 ? 471 HOH   A O   1 
HETATM 2275 O  O   . HOH   D 4 .   ? 6.553  -16.543 18.890  1.00 22.06 ? 472 HOH   A O   1 
HETATM 2276 O  O   . HOH   D 4 .   ? 17.746 7.622   -2.200  1.00 34.95 ? 473 HOH   A O   1 
HETATM 2277 O  O   . HOH   D 4 .   ? 17.685 -9.178  20.890  1.00 12.46 ? 474 HOH   A O   1 
HETATM 2278 O  O   . HOH   D 4 .   ? 8.692  14.663  29.283  1.00 38.94 ? 475 HOH   A O   1 
HETATM 2279 O  O   . HOH   D 4 .   ? 0.229  9.730   1.794   1.00 15.51 ? 476 HOH   A O   1 
HETATM 2280 O  O   . HOH   D 4 .   ? 5.124  -10.252 24.519  1.00 18.06 ? 477 HOH   A O   1 
HETATM 2281 O  O   . HOH   D 4 .   ? 20.997 3.164   34.533  1.00 29.99 ? 478 HOH   A O   1 
HETATM 2282 O  O   . HOH   D 4 .   ? 17.415 -11.199 -2.877  1.00 29.59 ? 479 HOH   A O   1 
HETATM 2283 O  O   . HOH   D 4 .   ? 2.937  -1.927  -2.677  1.00 26.76 ? 480 HOH   A O   1 
HETATM 2284 O  O   . HOH   D 4 .   ? -1.112 -16.381 13.699  1.00 26.20 ? 481 HOH   A O   1 
HETATM 2285 O  O   . HOH   D 4 .   ? 10.091 -17.705 7.311   1.00 28.38 ? 482 HOH   A O   1 
HETATM 2286 O  O   . HOH   D 4 .   ? 16.993 -6.539  31.226  1.00 25.63 ? 483 HOH   A O   1 
HETATM 2287 O  O   . HOH   D 4 .   ? 29.781 -1.772  21.135  1.00 15.21 ? 484 HOH   A O   1 
HETATM 2288 O  O   . HOH   D 4 .   ? 23.118 -13.680 9.432   1.00 30.11 ? 485 HOH   A O   1 
HETATM 2289 O  O   . HOH   D 4 .   ? 31.822 -7.179  9.011   1.00 37.13 ? 486 HOH   A O   1 
HETATM 2290 O  O   . HOH   D 4 .   ? 4.236  -6.326  20.338  1.00 11.59 ? 487 HOH   A O   1 
HETATM 2291 O  O   . HOH   D 4 .   ? 31.591 -8.779  16.179  1.00 24.66 ? 488 HOH   A O   1 
HETATM 2292 O  O   . HOH   D 4 .   ? 17.403 -13.812 24.481  1.00 16.37 ? 489 HOH   A O   1 
HETATM 2293 O  O   . HOH   D 4 .   ? 24.871 -1.461  4.231   1.00 32.96 ? 490 HOH   A O   1 
HETATM 2294 O  O   . HOH   D 4 .   ? -1.524 -3.930  2.814   1.00 22.56 ? 491 HOH   A O   1 
HETATM 2295 O  O   . HOH   D 4 .   ? -3.576 6.692   8.466   1.00 32.67 ? 492 HOH   A O   1 
HETATM 2296 O  O   . HOH   D 4 .   ? -3.569 -5.710  9.107   1.00 18.64 ? 493 HOH   A O   1 
HETATM 2297 O  O   . HOH   D 4 .   ? 22.891 -9.189  16.213  0.50 25.08 ? 494 HOH   A O   1 
HETATM 2298 O  O   . HOH   D 4 .   ? 10.347 3.323   33.733  0.50 26.21 ? 495 HOH   A O   1 
HETATM 2299 O  O   . HOH   D 4 .   ? -1.832 -0.980  6.702   1.00 20.35 ? 496 HOH   A O   1 
HETATM 2300 O  O   . HOH   D 4 .   ? 0.955  12.893  26.646  1.00 22.91 ? 497 HOH   A O   1 
HETATM 2301 O  O   . HOH   D 4 .   ? 34.594 2.364   24.481  1.00 20.69 ? 498 HOH   A O   1 
HETATM 2302 O  O   . HOH   D 4 .   ? 22.457 -9.785  25.119  1.00 30.27 ? 499 HOH   A O   1 
HETATM 2303 O  O   . HOH   D 4 .   ? 8.627  18.520  10.906  1.00 40.19 ? 500 HOH   A O   1 
HETATM 2304 O  O   . HOH   D 4 .   ? 13.880 -6.577  32.624  1.00 19.42 ? 501 HOH   A O   1 
HETATM 2305 O  O   . HOH   D 4 .   ? -0.569 7.665   4.727   1.00 15.53 ? 502 HOH   A O   1 
HETATM 2306 O  O   . HOH   D 4 .   ? 4.948  18.066  23.456  1.00 27.81 ? 503 HOH   A O   1 
HETATM 2307 O  O   . HOH   D 4 .   ? 3.136  12.603  11.386  1.00 19.49 ? 504 HOH   A O   1 
HETATM 2308 O  O   . HOH   D 4 .   ? 22.627 -8.957  14.701  0.50 19.35 ? 505 HOH   A O   1 
HETATM 2309 O  O   . HOH   D 4 .   ? 13.205 -17.099 30.577  1.00 42.54 ? 506 HOH   A O   1 
HETATM 2310 O  O   . HOH   D 4 .   ? -2.175 -11.338 11.379  1.00 22.97 ? 507 HOH   A O   1 
HETATM 2311 O  O   . HOH   D 4 .   ? 26.340 -5.391  22.324  1.00 31.00 ? 508 HOH   A O   1 
HETATM 2312 O  O   . HOH   D 4 .   ? 1.984  11.988  8.877   1.00 14.88 ? 509 HOH   A O   1 
HETATM 2313 O  O   . HOH   D 4 .   ? -0.332 -5.024  23.505  1.00 14.03 ? 510 HOH   A O   1 
HETATM 2314 O  O   . HOH   D 4 .   ? -3.782 -7.774  15.258  1.00 35.49 ? 511 HOH   A O   1 
HETATM 2315 O  O   . HOH   D 4 .   ? 23.882 -2.597  7.839   1.00 21.90 ? 512 HOH   A O   1 
HETATM 2316 O  O   . HOH   D 4 .   ? 6.075  22.290  17.742  1.00 21.50 ? 513 HOH   A O   1 
HETATM 2317 O  O   . HOH   D 4 .   ? -4.859 5.350   15.477  1.00 21.66 ? 514 HOH   A O   1 
HETATM 2318 O  O   . HOH   D 4 .   ? 2.131  -10.461 -3.423  1.00 20.41 ? 515 HOH   A O   1 
HETATM 2319 O  O   . HOH   D 4 .   ? 8.203  -14.831 26.735  1.00 18.46 ? 516 HOH   A O   1 
HETATM 2320 O  O   . HOH   D 4 .   ? -4.766 8.528   27.134  1.00 32.17 ? 517 HOH   A O   1 
HETATM 2321 O  O   . HOH   D 4 .   ? 3.218  -18.594 8.132   1.00 18.40 ? 518 HOH   A O   1 
HETATM 2322 O  O   . HOH   D 4 .   ? 24.271 12.087  18.497  1.00 36.28 ? 519 HOH   A O   1 
HETATM 2323 O  O   . HOH   D 4 .   ? -5.172 4.972   20.901  1.00 25.96 ? 520 HOH   A O   1 
HETATM 2324 O  O   . HOH   D 4 .   ? 17.798 -11.195 25.238  1.00 14.47 ? 521 HOH   A O   1 
HETATM 2325 O  O   . HOH   D 4 .   ? 12.910 11.832  11.167  1.00 46.83 ? 522 HOH   A O   1 
HETATM 2326 O  O   . HOH   D 4 .   ? 26.134 -2.899  21.034  1.00 15.20 ? 523 HOH   A O   1 
HETATM 2327 O  O   . HOH   D 4 .   ? 31.466 8.571   15.256  1.00 39.48 ? 524 HOH   A O   1 
HETATM 2328 O  O   . HOH   D 4 .   ? 11.859 -8.337  -1.127  1.00 25.09 ? 525 HOH   A O   1 
HETATM 2329 O  O   . HOH   D 4 .   ? 35.076 4.174   22.748  0.50 19.94 ? 526 HOH   A O   1 
HETATM 2330 O  O   . HOH   D 4 .   ? 14.535 -3.211  37.410  1.00 22.59 ? 527 HOH   A O   1 
HETATM 2331 O  O   . HOH   D 4 .   ? 17.427 0.569   11.173  1.00 24.80 ? 528 HOH   A O   1 
HETATM 2332 O  O   . HOH   D 4 .   ? 5.896  13.995  34.674  1.00 49.76 ? 529 HOH   A O   1 
HETATM 2333 O  O   . HOH   D 4 .   ? -5.346 -0.331  14.405  1.00 22.10 ? 530 HOH   A O   1 
HETATM 2334 O  O   . HOH   D 4 .   ? 9.253  4.880   30.792  0.50 15.99 ? 531 HOH   A O   1 
HETATM 2335 O  O   . HOH   D 4 .   ? 16.405 -14.261 0.957   1.00 32.97 ? 532 HOH   A O   1 
HETATM 2336 O  O   . HOH   D 4 .   ? 32.428 3.354   25.937  1.00 25.11 ? 533 HOH   A O   1 
HETATM 2337 O  O   . HOH   D 4 .   ? 25.769 -0.657  29.077  1.00 26.61 ? 534 HOH   A O   1 
HETATM 2338 O  O   . HOH   D 4 .   ? 34.268 -3.700  24.533  1.00 26.22 ? 535 HOH   A O   1 
HETATM 2339 O  O   . HOH   D 4 .   ? -3.343 13.964  6.258   1.00 29.33 ? 536 HOH   A O   1 
HETATM 2340 O  O   . HOH   D 4 .   ? 7.791  -14.630 -0.026  1.00 34.65 ? 537 HOH   A O   1 
HETATM 2341 O  O   . HOH   D 4 .   ? 13.859 -15.066 1.498   1.00 27.07 ? 538 HOH   A O   1 
HETATM 2342 O  O   . HOH   D 4 .   ? 7.293  22.156  15.232  1.00 25.59 ? 539 HOH   A O   1 
HETATM 2343 O  O   . HOH   D 4 .   ? -6.002 -8.835  22.339  1.00 41.29 ? 540 HOH   A O   1 
HETATM 2344 O  O   . HOH   D 4 .   ? 9.770  12.024  8.033   1.00 21.50 ? 541 HOH   A O   1 
HETATM 2345 O  O   . HOH   D 4 .   ? 23.805 -9.654  9.607   1.00 30.89 ? 542 HOH   A O   1 
HETATM 2346 O  O   . HOH   D 4 .   ? 7.771  -16.538 14.756  1.00 22.38 ? 543 HOH   A O   1 
HETATM 2347 O  O   . HOH   D 4 .   ? 22.689 -15.487 14.280  1.00 50.98 ? 544 HOH   A O   1 
HETATM 2348 O  O   . HOH   D 4 .   ? 8.470  10.047  28.699  1.00 28.20 ? 545 HOH   A O   1 
HETATM 2349 O  O   . HOH   D 4 .   ? 30.574 4.116   11.921  1.00 26.93 ? 546 HOH   A O   1 
HETATM 2350 O  O   . HOH   D 4 .   ? -2.095 2.036   34.583  1.00 35.29 ? 547 HOH   A O   1 
HETATM 2351 O  O   . HOH   D 4 .   ? -2.705 1.355   26.553  1.00 22.20 ? 548 HOH   A O   1 
HETATM 2352 O  O   . HOH   D 4 .   ? 25.582 -4.925  8.004   1.00 24.87 ? 549 HOH   A O   1 
HETATM 2353 O  O   . HOH   D 4 .   ? 7.781  1.015   -6.114  1.00 33.85 ? 550 HOH   A O   1 
HETATM 2354 O  O   . HOH   D 4 .   ? 12.803 -20.149 10.358  1.00 22.93 ? 551 HOH   A O   1 
HETATM 2355 O  O   . HOH   D 4 .   ? -3.143 -15.760 6.822   0.50 24.11 ? 552 HOH   A O   1 
HETATM 2356 O  O   . HOH   D 4 .   ? 5.619  10.994  -1.950  1.00 33.37 ? 553 HOH   A O   1 
HETATM 2357 O  O   . HOH   D 4 .   ? 3.794  -14.211 21.987  1.00 30.84 ? 554 HOH   A O   1 
HETATM 2358 O  O   . HOH   D 4 .   ? 22.464 0.373   29.426  1.00 16.36 ? 555 HOH   A O   1 
HETATM 2359 O  O   . HOH   D 4 .   ? 19.885 -4.135  36.345  1.00 41.98 ? 556 HOH   A O   1 
HETATM 2360 O  O   . HOH   D 4 .   ? 29.376 5.135   27.821  1.00 36.18 ? 557 HOH   A O   1 
HETATM 2361 O  O   . HOH   D 4 .   ? -4.461 1.285   35.127  1.00 37.72 ? 558 HOH   A O   1 
HETATM 2362 O  O   . HOH   D 4 .   ? 22.509 -4.402  34.485  1.00 27.51 ? 559 HOH   A O   1 
HETATM 2363 O  O   . HOH   D 4 .   ? 31.204 2.213   13.916  0.50 17.28 ? 560 HOH   A O   1 
HETATM 2364 O  O   . HOH   D 4 .   ? -4.771 -4.246  12.939  0.50 21.01 ? 561 HOH   A O   1 
HETATM 2365 O  O   . HOH   D 4 .   ? -2.806 -0.309  28.867  0.50 24.39 ? 562 HOH   A O   1 
HETATM 2366 O  O   . HOH   D 4 .   ? 4.876  -7.779  33.047  1.00 20.56 ? 563 HOH   A O   1 
HETATM 2367 O  O   . HOH   D 4 .   ? -1.138 21.847  12.183  1.00 38.69 ? 564 HOH   A O   1 
HETATM 2368 O  O   . HOH   D 4 .   ? 29.313 -7.344  16.499  1.00 23.75 ? 565 HOH   A O   1 
HETATM 2369 O  O   . HOH   D 4 .   ? 20.522 -6.434  32.695  1.00 26.66 ? 566 HOH   A O   1 
HETATM 2370 O  O   . HOH   D 4 .   ? -0.096 -17.779 6.836   1.00 30.94 ? 567 HOH   A O   1 
HETATM 2371 O  O   . HOH   D 4 .   ? 12.137 -3.719  35.904  1.00 20.58 ? 568 HOH   A O   1 
HETATM 2372 O  O   . HOH   D 4 .   ? -2.570 1.137   3.969   1.00 22.21 ? 569 HOH   A O   1 
HETATM 2373 O  O   . HOH   D 4 .   ? 0.665  2.529   0.120   1.00 39.41 ? 570 HOH   A O   1 
HETATM 2374 O  O   . HOH   D 4 .   ? -2.170 -16.433 6.419   0.50 22.99 ? 571 HOH   A O   1 
HETATM 2375 O  O   . HOH   D 4 .   ? 15.015 8.661   11.756  0.50 24.64 ? 572 HOH   A O   1 
HETATM 2376 O  O   . HOH   D 4 .   ? 15.750 4.168   11.610  1.00 22.72 ? 573 HOH   A O   1 
HETATM 2377 O  O   . HOH   D 4 .   ? 21.056 -12.204 22.237  1.00 26.68 ? 574 HOH   A O   1 
HETATM 2378 O  O   . HOH   D 4 .   ? 11.689 -5.861  34.137  1.00 22.85 ? 575 HOH   A O   1 
HETATM 2379 O  O   . HOH   D 4 .   ? 19.080 -10.263 22.920  1.00 13.26 ? 576 HOH   A O   1 
HETATM 2380 O  O   . HOH   D 4 .   ? 26.952 2.875   8.406   1.00 34.99 ? 577 HOH   A O   1 
HETATM 2381 O  O   . HOH   D 4 .   ? 8.072  20.913  12.289  1.00 30.32 ? 578 HOH   A O   1 
HETATM 2382 O  O   . HOH   D 4 .   ? 17.012 2.223   13.244  1.00 15.71 ? 579 HOH   A O   1 
HETATM 2383 O  O   . HOH   D 4 .   ? 0.824  15.903  28.847  1.00 43.43 ? 580 HOH   A O   1 
HETATM 2384 O  O   . HOH   D 4 .   ? 13.776 -6.891  -2.321  1.00 26.41 ? 581 HOH   A O   1 
HETATM 2385 O  O   . HOH   D 4 .   ? 10.815 16.806  12.013  1.00 29.50 ? 582 HOH   A O   1 
HETATM 2386 O  O   . HOH   D 4 .   ? 28.695 -11.809 -0.905  1.00 32.27 ? 583 HOH   A O   1 
HETATM 2387 O  O   . HOH   D 4 .   ? 27.676 -3.857  6.702   1.00 34.86 ? 584 HOH   A O   1 
HETATM 2388 O  O   . HOH   D 4 .   ? 35.975 -8.377  14.457  1.00 32.77 ? 585 HOH   A O   1 
HETATM 2389 O  O   . HOH   D 4 .   ? 14.219 3.669   35.303  1.00 25.34 ? 586 HOH   A O   1 
HETATM 2390 O  O   . HOH   D 4 .   ? -6.902 7.858   18.936  0.50 24.45 ? 587 HOH   A O   1 
HETATM 2391 O  O   . HOH   D 4 .   ? -1.810 -9.629  14.040  1.00 24.17 ? 588 HOH   A O   1 
HETATM 2392 O  O   . HOH   D 4 .   ? -2.235 1.935   32.024  1.00 33.61 ? 589 HOH   A O   1 
HETATM 2393 O  O   . HOH   D 4 .   ? 15.903 5.080   -5.932  1.00 42.83 ? 590 HOH   A O   1 
HETATM 2394 O  O   . HOH   D 4 .   ? 28.708 8.177   21.750  1.00 17.98 ? 591 HOH   A O   1 
HETATM 2395 O  O   . HOH   D 4 .   ? 13.504 -17.310 21.862  1.00 29.87 ? 592 HOH   A O   1 
HETATM 2396 O  O   . HOH   D 4 .   ? 2.472  -6.994  34.375  1.00 35.57 ? 593 HOH   A O   1 
HETATM 2397 O  O   . HOH   D 4 .   ? 26.830 -11.413 -5.631  1.00 39.77 ? 594 HOH   A O   1 
HETATM 2398 O  O   . HOH   D 4 .   ? 12.596 -17.940 26.673  1.00 32.18 ? 595 HOH   A O   1 
HETATM 2399 O  O   . HOH   D 4 .   ? -3.695 -7.538  2.025   1.00 29.63 ? 596 HOH   A O   1 
HETATM 2400 O  O   . HOH   D 4 .   ? 14.258 9.071   12.693  0.50 21.41 ? 597 HOH   A O   1 
HETATM 2401 O  O   . HOH   D 4 .   ? 31.450 7.347   12.864  1.00 43.35 ? 598 HOH   A O   1 
HETATM 2402 O  O   . HOH   D 4 .   ? 34.071 -1.467  13.362  1.00 44.76 ? 599 HOH   A O   1 
HETATM 2403 O  O   . HOH   D 4 .   ? 21.352 2.436   -6.808  1.00 37.41 ? 600 HOH   A O   1 
HETATM 2404 O  O   . HOH   D 4 .   ? 29.586 -2.538  23.699  1.00 31.93 ? 601 HOH   A O   1 
HETATM 2405 O  O   . HOH   D 4 .   ? -1.485 -7.415  25.403  1.00 30.48 ? 602 HOH   A O   1 
HETATM 2406 O  O   . HOH   D 4 .   ? 8.296  -15.222 16.985  1.00 19.03 ? 603 HOH   A O   1 
HETATM 2407 O  O   . HOH   D 4 .   ? 31.237 -0.263  14.072  0.50 18.07 ? 604 HOH   A O   1 
HETATM 2408 O  O   . HOH   D 4 .   ? 5.864  -14.291 25.527  1.00 37.55 ? 605 HOH   A O   1 
HETATM 2409 O  O   . HOH   D 4 .   ? 31.858 1.071   13.952  0.50 12.65 ? 606 HOH   A O   1 
HETATM 2410 O  O   . HOH   D 4 .   ? 3.339  21.964  17.658  1.00 29.60 ? 607 HOH   A O   1 
HETATM 2411 O  O   . HOH   D 4 .   ? -3.893 10.892  26.134  1.00 38.99 ? 608 HOH   A O   1 
HETATM 2412 O  O   . HOH   D 4 .   ? 19.733 -11.003 27.163  1.00 29.09 ? 609 HOH   A O   1 
HETATM 2413 O  O   . HOH   D 4 .   ? 19.312 -15.347 25.664  1.00 34.66 ? 610 HOH   A O   1 
HETATM 2414 O  O   . HOH   D 4 .   ? 10.671 6.964   31.054  1.00 49.58 ? 611 HOH   A O   1 
HETATM 2415 O  O   . HOH   D 4 .   ? 36.447 -1.838  25.157  1.00 22.29 ? 612 HOH   A O   1 
HETATM 2416 O  O   . HOH   D 4 .   ? 25.178 10.549  22.720  1.00 33.64 ? 613 HOH   A O   1 
HETATM 2417 O  O   . HOH   D 4 .   ? 5.075  18.912  26.499  1.00 39.58 ? 614 HOH   A O   1 
HETATM 2418 O  O   . HOH   D 4 .   ? 9.369  5.390   31.992  0.50 15.74 ? 615 HOH   A O   1 
HETATM 2419 O  O   . HOH   D 4 .   ? 4.384  -15.951 20.430  1.00 35.64 ? 616 HOH   A O   1 
HETATM 2420 O  O   . HOH   D 4 .   ? 36.435 0.845   26.018  1.00 24.08 ? 617 HOH   A O   1 
HETATM 2421 O  O   . HOH   D 4 .   ? 4.272  -11.851 26.463  1.00 27.75 ? 618 HOH   A O   1 
HETATM 2422 O  O   . HOH   D 4 .   ? 11.093 -18.364 24.831  1.00 37.74 ? 619 HOH   A O   1 
HETATM 2423 O  O   . HOH   D 4 .   ? 0.902  -3.100  -3.759  1.00 41.63 ? 620 HOH   A O   1 
HETATM 2424 O  O   . HOH   D 4 .   ? 13.861 -8.351  -4.637  1.00 37.11 ? 621 HOH   A O   1 
HETATM 2425 O  O   . HOH   D 4 .   ? 11.932 5.259   34.812  1.00 25.03 ? 622 HOH   A O   1 
HETATM 2426 O  O   . HOH   D 4 .   ? 27.339 7.081   29.119  1.00 57.67 ? 623 HOH   A O   1 
HETATM 2427 O  O   . HOH   D 4 .   ? 23.168 -12.137 20.596  1.00 30.67 ? 624 HOH   A O   1 
HETATM 2428 O  O   . HOH   D 4 .   ? 16.114 -7.631  33.950  1.00 46.56 ? 625 HOH   A O   1 
HETATM 2429 O  O   . HOH   D 4 .   ? -2.690 -5.297  -0.364  1.00 44.51 ? 626 HOH   A O   1 
HETATM 2430 O  O   . HOH   D 4 .   ? 3.357  -9.946  31.747  1.00 35.85 ? 627 HOH   A O   1 
HETATM 2431 O  O   . HOH   D 4 .   ? 33.165 6.389   27.426  1.00 45.04 ? 628 HOH   A O   1 
HETATM 2432 O  O   . HOH   D 4 .   ? 27.399 10.732  18.660  1.00 56.58 ? 629 HOH   A O   1 
HETATM 2433 O  O   . HOH   D 4 .   ? 12.176 7.266   33.032  1.00 30.93 ? 630 HOH   A O   1 
HETATM 2434 O  O   . HOH   D 4 .   ? 20.033 -9.103  29.052  1.00 21.01 ? 631 HOH   A O   1 
HETATM 2435 O  O   . HOH   D 4 .   ? -5.193 2.758   15.359  0.50 24.81 ? 632 HOH   A O   1 
HETATM 2436 O  O   . HOH   D 4 .   ? 8.335  12.668  -0.947  1.00 53.73 ? 633 HOH   A O   1 
HETATM 2437 O  O   . HOH   D 4 .   ? 7.274  5.618   33.179  1.00 36.07 ? 634 HOH   A O   1 
HETATM 2438 O  O   . HOH   D 4 .   ? 8.409  -17.588 26.304  1.00 32.94 ? 635 HOH   A O   1 
HETATM 2439 O  O   . HOH   D 4 .   ? 33.005 2.820   28.578  1.00 42.15 ? 636 HOH   A O   1 
HETATM 2440 O  O   . HOH   D 4 .   ? 35.942 -5.644  26.148  1.00 53.00 ? 637 HOH   A O   1 
HETATM 2441 O  O   . HOH   D 4 .   ? 17.864 6.190   40.605  1.00 22.92 ? 638 HOH   A O   1 
HETATM 2442 O  O   . HOH   D 4 .   ? -6.651 0.738   28.604  1.00 35.43 ? 639 HOH   A O   1 
HETATM 2443 O  O   . HOH   D 4 .   ? 10.683 5.370   37.635  1.00 37.19 ? 640 HOH   A O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N  N   . HIS   A 3   ? 0.2650 0.4779 0.4272 -0.0268 0.0365  0.0034  3   HIS   A N   
2    C  CA  . HIS   A 3   ? 0.4524 0.4340 0.4239 -0.0308 0.1229  0.0193  3   HIS   A CA  
3    C  C   . HIS   A 3   ? 0.3137 0.4847 0.4200 -0.0151 0.0486  0.0418  3   HIS   A C   
4    O  O   . HIS   A 3   ? 0.5066 0.5060 0.4126 -0.0986 0.0591  -0.0142 3   HIS   A O   
5    C  CB  . HIS   A 3   ? 0.5452 0.3806 0.3494 0.0032  0.0903  0.1021  3   HIS   A CB  
6    C  CG  . HIS   A 3   ? 0.5089 0.2810 0.4275 0.0386  0.1893  0.1171  3   HIS   A CG  
7    N  ND1 . HIS   A 3   ? 0.5387 0.2960 0.4851 0.0763  0.1458  0.1690  3   HIS   A ND1 
8    C  CD2 . HIS   A 3   ? 0.6499 0.3854 0.3312 -0.0309 0.1875  0.1095  3   HIS   A CD2 
9    C  CE1 . HIS   A 3   ? 0.6690 0.3002 0.5059 -0.0385 0.2013  0.1893  3   HIS   A CE1 
10   N  NE2 . HIS   A 3   ? 0.7205 0.3826 0.3950 -0.0580 0.2331  0.1885  3   HIS   A NE2 
11   N  N   . HIS   A 4   ? 0.2033 0.4225 0.3900 -0.0355 0.0528  -0.0015 4   HIS   A N   
12   C  CA  . HIS   A 4   ? 0.2228 0.3959 0.3515 -0.0302 0.0747  0.0403  4   HIS   A CA  
13   C  C   . HIS   A 4   ? 0.1462 0.3268 0.2919 -0.0249 0.0505  0.0013  4   HIS   A C   
14   O  O   . HIS   A 4   ? 0.1973 0.3139 0.2745 0.0064  0.0480  0.0089  4   HIS   A O   
15   C  CB  . HIS   A 4   ? 0.2528 0.4335 0.4455 -0.0072 0.0581  0.0918  4   HIS   A CB  
16   N  N   . TRP   A 5   ? 0.1504 0.2686 0.2640 -0.0017 0.0359  0.0088  5   TRP   A N   
17   C  CA  . TRP   A 5   ? 0.1160 0.2368 0.2241 -0.0181 0.0163  0.0043  5   TRP   A CA  
18   C  C   . TRP   A 5   ? 0.1358 0.2313 0.2274 0.0015  0.0095  -0.0016 5   TRP   A C   
19   O  O   . TRP   A 5   ? 0.1415 0.2943 0.2187 0.0135  0.0119  -0.0013 5   TRP   A O   
20   C  CB  . TRP   A 5   ? 0.1121 0.2413 0.2327 -0.0187 0.0062  0.0048  5   TRP   A CB  
21   C  CG  . TRP   A 5   ? 0.1381 0.2572 0.1871 -0.0045 0.0231  0.0137  5   TRP   A CG  
22   C  CD1 . TRP   A 5   ? 0.1705 0.2673 0.2249 0.0121  0.0248  0.0320  5   TRP   A CD1 
23   C  CD2 . TRP   A 5   ? 0.1312 0.2403 0.1843 0.0015  0.0026  -0.0015 5   TRP   A CD2 
24   N  NE1 . TRP   A 5   ? 0.1752 0.2699 0.2183 0.0303  0.0233  0.0369  5   TRP   A NE1 
25   C  CE2 . TRP   A 5   ? 0.1465 0.2673 0.1725 0.0242  0.0046  0.0137  5   TRP   A CE2 
26   C  CE3 . TRP   A 5   ? 0.1310 0.2439 0.1712 0.0109  -0.0100 -0.0116 5   TRP   A CE3 
27   C  CZ2 . TRP   A 5   ? 0.1490 0.2792 0.2010 0.0285  -0.0185 0.0060  5   TRP   A CZ2 
28   C  CZ3 . TRP   A 5   ? 0.1467 0.2644 0.1837 -0.0044 0.0032  -0.0284 5   TRP   A CZ3 
29   C  CH2 . TRP   A 5   ? 0.1465 0.2888 0.1734 0.0281  -0.0051 -0.0331 5   TRP   A CH2 
30   N  N   . GLY   A 6   ? 0.1306 0.2212 0.1873 0.0060  -0.0024 -0.0100 6   GLY   A N   
31   C  CA  . GLY   A 6   ? 0.1175 0.2465 0.2116 0.0097  0.0033  -0.0150 6   GLY   A CA  
32   C  C   . GLY   A 6   ? 0.1126 0.2586 0.2130 0.0137  0.0104  -0.0183 6   GLY   A C   
33   O  O   . GLY   A 6   ? 0.1150 0.2581 0.1857 0.0001  0.0018  -0.0057 6   GLY   A O   
34   N  N   . TYR   A 7   ? 0.1374 0.2519 0.2020 0.0109  0.0082  -0.0333 7   TYR   A N   
35   C  CA  . TYR   A 7   ? 0.1312 0.2678 0.2297 0.0070  0.0147  -0.0196 7   TYR   A CA  
36   C  C   . TYR   A 7   ? 0.1693 0.2616 0.2944 0.0230  0.0189  -0.0036 7   TYR   A C   
37   O  O   . TYR   A 7   ? 0.2146 0.2825 0.4533 0.0425  0.0863  0.0074  7   TYR   A O   
38   C  CB  . TYR   A 7   ? 0.1361 0.2503 0.2119 -0.0048 0.0064  -0.0317 7   TYR   A CB  
39   C  CG  . TYR   A 7   ? 0.1195 0.2205 0.1908 -0.0123 -0.0057 -0.0159 7   TYR   A CG  
40   C  CD1 . TYR   A 7   ? 0.0965 0.2079 0.1750 -0.0231 -0.0227 -0.0173 7   TYR   A CD1 
41   C  CD2 . TYR   A 7   ? 0.1077 0.2227 0.1717 -0.0212 -0.0120 -0.0173 7   TYR   A CD2 
42   C  CE1 . TYR   A 7   ? 0.1045 0.2038 0.1676 -0.0284 -0.0159 -0.0105 7   TYR   A CE1 
43   C  CE2 . TYR   A 7   ? 0.1299 0.2221 0.1407 -0.0259 -0.0082 -0.0163 7   TYR   A CE2 
44   C  CZ  . TYR   A 7   ? 0.1114 0.2109 0.1438 -0.0266 -0.0107 -0.0122 7   TYR   A CZ  
45   O  OH  . TYR   A 7   ? 0.1400 0.2022 0.1664 0.0021  -0.0074 -0.0073 7   TYR   A OH  
46   N  N   . GLY   A 8   ? 0.1770 0.2792 0.3287 0.0369  0.0382  -0.0231 8   GLY   A N   
47   C  CA  . GLY   A 8   ? 0.2047 0.3023 0.3801 0.0720  0.0367  -0.0158 8   GLY   A CA  
48   C  C   . GLY   A 8   ? 0.1982 0.3245 0.3850 0.0622  0.0422  -0.0140 8   GLY   A C   
49   O  O   . GLY   A 8   ? 0.1837 0.3391 0.3627 0.0392  0.0713  0.0148  8   GLY   A O   
50   N  N   . LYS   A 9   ? 0.2127 0.2941 0.3988 0.0614  0.0292  -0.0306 9   LYS   A N   
51   C  CA  . LYS   A 9   ? 0.2349 0.3189 0.3994 0.0721  0.0237  -0.0065 9   LYS   A CA  
52   C  C   . LYS   A 9   ? 0.2208 0.3206 0.3793 0.0642  0.0371  0.0203  9   LYS   A C   
53   O  O   . LYS   A 9   ? 0.2407 0.3091 0.3559 0.0218  0.0264  0.0297  9   LYS   A O   
54   C  CB  . LYS   A 9   ? 0.2295 0.3411 0.4492 0.0991  0.0152  -0.0201 9   LYS   A CB  
55   N  N   . HIS   A 10  ? 0.1932 0.2990 0.3662 0.0856  0.0531  0.0469  10  HIS   A N   
56   C  CA  . HIS   A 10  ? 0.1969 0.3123 0.3709 0.0754  0.0881  0.0603  10  HIS   A CA  
57   C  C   . HIS   A 10  ? 0.1706 0.3007 0.3230 0.0652  0.0710  0.0237  10  HIS   A C   
58   O  O   . HIS   A 10  ? 0.1948 0.3216 0.3670 0.0633  0.0805  0.0155  10  HIS   A O   
59   C  CB  . HIS   A 10  ? 0.2505 0.3442 0.3596 0.1075  0.1303  0.0615  10  HIS   A CB  
60   C  CG  . HIS   A 10  ? 0.2516 0.3712 0.3532 0.1168  0.0680  0.0638  10  HIS   A CG  
61   N  ND1 . HIS   A 10  ? 0.2606 0.3982 0.3576 0.1327  0.0748  0.0444  10  HIS   A ND1 
62   C  CD2 . HIS   A 10  ? 0.2495 0.4026 0.3820 0.0932  0.1221  0.0775  10  HIS   A CD2 
63   C  CE1 . HIS   A 10  ? 0.2700 0.4026 0.3623 0.1313  0.0822  0.0592  10  HIS   A CE1 
64   N  NE2 . HIS   A 10  ? 0.2443 0.3581 0.3880 0.0793  0.1263  0.0624  10  HIS   A NE2 
65   N  N   . ASN   A 11  ? 0.1501 0.2812 0.2909 0.0309  0.0319  0.0028  11  ASN   A N   
66   C  CA  . ASN   A 11  ? 0.1552 0.2849 0.2408 0.0269  0.0467  -0.0004 11  ASN   A CA  
67   C  C   . ASN   A 11  ? 0.1413 0.2706 0.1975 0.0426  0.0269  0.0040  11  ASN   A C   
68   O  O   . ASN   A 11  ? 0.1453 0.2493 0.2145 0.0406  0.0183  0.0163  11  ASN   A O   
69   C  CB  . ASN   A 11  ? 0.1755 0.3100 0.2408 0.0360  0.0533  0.0070  11  ASN   A CB  
70   C  CG  . ASN   A 11  ? 0.2124 0.3299 0.2195 0.0386  0.0569  0.0126  11  ASN   A CG  
71   O  OD1 . ASN   A 11  ? 0.2110 0.3067 0.2420 0.0539  0.0359  0.0143  11  ASN   A OD1 
72   N  ND2 . ASN   A 11  ? 0.2229 0.3868 0.2667 0.0396  0.0429  0.0393  11  ASN   A ND2 
73   N  N   . GLY   A 12  ? 0.1256 0.2687 0.2352 0.0346  0.0163  -0.0022 12  GLY   A N   
74   C  CA  . GLY   A 12  ? 0.1346 0.2684 0.2102 0.0241  0.0082  -0.0069 12  GLY   A CA  
75   C  C   . GLY   A 12  ? 0.1089 0.2217 0.2059 0.0151  0.0012  0.0025  12  GLY   A C   
76   O  O   . GLY   A 12  ? 0.1148 0.2280 0.2049 0.0128  -0.0188 0.0134  12  GLY   A O   
77   N  N   . PRO   A 13  ? 0.1326 0.2063 0.1783 -0.0126 -0.0072 0.0017  13  PRO   A N   
78   C  CA  . PRO   A 13  ? 0.1315 0.2036 0.1849 -0.0015 -0.0031 -0.0006 13  PRO   A CA  
79   C  C   . PRO   A 13  ? 0.1286 0.2072 0.1979 0.0048  0.0069  0.0074  13  PRO   A C   
80   O  O   . PRO   A 13  ? 0.1040 0.2210 0.1979 0.0031  -0.0069 0.0053  13  PRO   A O   
81   C  CB  . PRO   A 13  ? 0.1209 0.2336 0.1912 -0.0068 -0.0021 -0.0146 13  PRO   A CB  
82   C  CG  . PRO   A 13  ? 0.1515 0.2180 0.1857 -0.0048 0.0015  -0.0127 13  PRO   A CG  
83   C  CD  . PRO   A 13  ? 0.1258 0.2236 0.2002 -0.0102 -0.0024 -0.0124 13  PRO   A CD  
84   N  N   . GLU   A 14  ? 0.1335 0.2018 0.2178 -0.0004 -0.0117 0.0142  14  GLU   A N   
85   C  CA  . GLU   A 14  ? 0.1607 0.2306 0.2148 0.0196  -0.0261 0.0271  14  GLU   A CA  
86   C  C   . GLU   A 14  ? 0.1221 0.2173 0.2334 0.0429  -0.0334 0.0272  14  GLU   A C   
87   O  O   . GLU   A 14  ? 0.1380 0.2682 0.2286 0.0316  -0.0544 0.0303  14  GLU   A O   
88   C  CB  . GLU   A 14  ? 0.2011 0.2437 0.3039 0.0204  -0.0473 0.0544  14  GLU   A CB  
89   C  CG  . GLU   A 14  ? 0.2733 0.2751 0.3630 -0.0095 -0.0403 0.0599  14  GLU   A CG  
90   C  CD  . GLU   A 14  ? 0.3618 0.4040 0.4231 -0.0193 -0.0207 0.0058  14  GLU   A CD  
91   O  OE1 . GLU   A 14  ? 0.4973 0.4843 0.4108 -0.0350 -0.0311 0.0171  14  GLU   A OE1 
92   O  OE2 . GLU   A 14  ? 0.4142 0.4680 0.4709 0.0437  0.0552  -0.0267 14  GLU   A OE2 
93   N  N   . HIS   A 15  ? 0.1088 0.2160 0.2190 0.0345  -0.0282 0.0196  15  HIS   A N   
94   C  CA  . HIS   A 15  ? 0.0876 0.2257 0.2266 0.0349  -0.0151 0.0165  15  HIS   A CA  
95   C  C   . HIS   A 15  ? 0.0915 0.2191 0.1986 0.0263  -0.0177 0.0148  15  HIS   A C   
96   O  O   . HIS   A 15  ? 0.0865 0.2303 0.2011 0.0123  -0.0204 0.0135  15  HIS   A O   
97   C  CB  . HIS   A 15  ? 0.0889 0.2289 0.2367 0.0287  -0.0217 0.0138  15  HIS   A CB  
98   C  CG  . HIS   A 15  ? 0.1200 0.2529 0.2538 0.0404  -0.0131 -0.0018 15  HIS   A CG  
99   N  ND1 . HIS   A 15  ? 0.1186 0.2825 0.2771 0.0574  -0.0242 0.0028  15  HIS   A ND1 
100  C  CD2 . HIS   A 15  ? 0.1518 0.2526 0.2921 0.0585  -0.0188 -0.0098 15  HIS   A CD2 
101  C  CE1 . HIS   A 15  ? 0.1868 0.3046 0.3150 0.0946  -0.0706 -0.0145 15  HIS   A CE1 
102  N  NE2 . HIS   A 15  ? 0.1755 0.2847 0.3319 0.0791  -0.0205 -0.0205 15  HIS   A NE2 
103  N  N   . TRP   A 16  ? 0.0807 0.2119 0.1936 0.0157  -0.0085 0.0095  16  TRP   A N   
104  C  CA  . TRP   A 16  ? 0.0689 0.2044 0.1976 0.0049  -0.0276 0.0051  16  TRP   A CA  
105  C  C   . TRP   A 16  ? 0.0806 0.2107 0.1877 0.0047  -0.0173 0.0073  16  TRP   A C   
106  O  O   . TRP   A 16  ? 0.0780 0.2176 0.1948 -0.0060 -0.0475 0.0048  16  TRP   A O   
107  C  CB  . TRP   A 16  ? 0.0728 0.2083 0.1756 -0.0102 -0.0154 0.0054  16  TRP   A CB  
108  C  CG  . TRP   A 16  ? 0.0850 0.2018 0.1756 -0.0074 -0.0213 -0.0060 16  TRP   A CG  
109  C  CD1 . TRP   A 16  ? 0.0838 0.2140 0.1845 -0.0032 -0.0058 -0.0096 16  TRP   A CD1 
110  C  CD2 . TRP   A 16  ? 0.0740 0.1956 0.1784 0.0090  -0.0204 -0.0019 16  TRP   A CD2 
111  N  NE1 . TRP   A 16  ? 0.0931 0.2215 0.1884 -0.0040 -0.0097 -0.0254 16  TRP   A NE1 
112  C  CE2 . TRP   A 16  ? 0.0783 0.2023 0.1686 0.0029  -0.0196 -0.0113 16  TRP   A CE2 
113  C  CE3 . TRP   A 16  ? 0.0868 0.2068 0.1636 -0.0086 -0.0215 0.0028  16  TRP   A CE3 
114  C  CZ2 . TRP   A 16  ? 0.0904 0.2010 0.1597 0.0001  -0.0291 -0.0144 16  TRP   A CZ2 
115  C  CZ3 . TRP   A 16  ? 0.0905 0.2116 0.1690 0.0065  -0.0222 -0.0108 16  TRP   A CZ3 
116  C  CH2 . TRP   A 16  ? 0.0914 0.2113 0.1569 0.0040  -0.0280 0.0031  16  TRP   A CH2 
117  N  N   . HIS   A 17  ? 0.0798 0.2002 0.1953 0.0086  -0.0242 0.0122  17  HIS   A N   
118  C  CA  . HIS   A 17  ? 0.0831 0.2274 0.1873 -0.0058 -0.0243 0.0129  17  HIS   A CA  
119  C  C   . HIS   A 17  ? 0.0881 0.2241 0.1936 0.0005  -0.0351 0.0090  17  HIS   A C   
120  O  O   . HIS   A 17  ? 0.0767 0.2331 0.2246 -0.0008 -0.0390 0.0002  17  HIS   A O   
121  C  CB  . HIS   A 17  ? 0.0844 0.2495 0.1896 -0.0211 -0.0284 0.0157  17  HIS   A CB  
122  C  CG  . HIS   A 17  ? 0.0945 0.2593 0.1876 -0.0018 -0.0263 0.0387  17  HIS   A CG  
123  N  ND1 . HIS   A 17  ? 0.1067 0.2975 0.2123 0.0033  -0.0345 0.0492  17  HIS   A ND1 
124  C  CD2 . HIS   A 17  ? 0.0894 0.2759 0.2133 0.0019  -0.0244 0.0350  17  HIS   A CD2 
125  C  CE1 . HIS   A 17  ? 0.0876 0.3011 0.2209 0.0193  -0.0368 0.0395  17  HIS   A CE1 
126  N  NE2 . HIS   A 17  ? 0.1077 0.2848 0.2408 0.0240  -0.0349 0.0479  17  HIS   A NE2 
127  N  N   . LYS   A 18  ? 0.0726 0.2374 0.2007 -0.0069 -0.0309 0.0064  18  LYS   A N   
128  C  CA  . LYS   A 18  ? 0.0673 0.2719 0.2199 -0.0104 -0.0322 0.0333  18  LYS   A CA  
129  C  C   . LYS   A 18  ? 0.0693 0.2770 0.2367 -0.0291 -0.0358 0.0375  18  LYS   A C   
130  O  O   . LYS   A 18  ? 0.1480 0.2758 0.3439 -0.0637 -0.1063 0.0889  18  LYS   A O   
131  C  CB  . LYS   A 18  ? 0.0680 0.2864 0.2168 0.0200  -0.0334 0.0358  18  LYS   A CB  
132  C  CG  . LYS   A 18  ? 0.0713 0.2802 0.2336 0.0299  -0.0291 0.0403  18  LYS   A CG  
133  C  CD  . LYS   A 18  ? 0.0638 0.3056 0.2534 0.0370  -0.0228 0.0498  18  LYS   A CD  
134  C  CE  . LYS   A 18  ? 0.0779 0.2829 0.2528 0.0458  -0.0225 0.0605  18  LYS   A CE  
135  N  NZ  . LYS   A 18  ? 0.0647 0.3299 0.2497 0.0556  -0.0339 0.0669  18  LYS   A NZ  
136  N  N   A ASP   A 19  ? 0.0813 0.2527 0.2210 -0.0141 -0.0423 0.0295  19  ASP   A N   
137  N  N   B ASP   A 19  ? 0.0824 0.2766 0.2221 -0.0237 -0.0425 0.0315  19  ASP   A N   
138  C  CA  A ASP   A 19  ? 0.0942 0.2395 0.2168 -0.0220 -0.0278 0.0249  19  ASP   A CA  
139  C  CA  B ASP   A 19  ? 0.0943 0.2724 0.2244 -0.0298 -0.0228 0.0308  19  ASP   A CA  
140  C  C   A ASP   A 19  ? 0.0921 0.2267 0.2333 -0.0255 -0.0310 0.0192  19  ASP   A C   
141  C  C   B ASP   A 19  ? 0.0978 0.2496 0.2362 -0.0281 -0.0251 0.0262  19  ASP   A C   
142  O  O   A ASP   A 19  ? 0.0893 0.2285 0.2365 -0.0309 -0.0432 0.0302  19  ASP   A O   
143  O  O   B ASP   A 19  ? 0.0988 0.2545 0.2465 -0.0427 -0.0245 0.0252  19  ASP   A O   
144  C  CB  A ASP   A 19  ? 0.1125 0.2564 0.2097 -0.0120 -0.0219 0.0244  19  ASP   A CB  
145  C  CB  B ASP   A 19  ? 0.1236 0.3221 0.2158 -0.0188 -0.0189 0.0337  19  ASP   A CB  
146  C  CG  A ASP   A 19  ? 0.1424 0.2607 0.2313 -0.0059 0.0010  0.0246  19  ASP   A CG  
147  C  CG  B ASP   A 19  ? 0.1089 0.3609 0.2546 -0.0206 -0.0014 0.0334  19  ASP   A CG  
148  O  OD1 A ASP   A 19  ? 0.1650 0.2563 0.2597 0.0140  0.0051  0.0602  19  ASP   A OD1 
149  O  OD1 B ASP   A 19  ? 0.1033 0.3825 0.3148 -0.0113 0.0139  0.0491  19  ASP   A OD1 
150  O  OD2 A ASP   A 19  ? 0.2093 0.2618 0.2169 -0.0155 0.0091  0.0290  19  ASP   A OD2 
151  O  OD2 B ASP   A 19  ? 0.2248 0.3932 0.2870 0.0038  0.0010  0.0250  19  ASP   A OD2 
152  N  N   . PHE   A 20  ? 0.0823 0.2071 0.2265 -0.0120 -0.0278 0.0244  20  PHE   A N   
153  C  CA  . PHE   A 20  ? 0.0811 0.2178 0.2317 -0.0246 -0.0180 0.0138  20  PHE   A CA  
154  C  C   . PHE   A 20  ? 0.0903 0.2220 0.2230 -0.0207 -0.0168 0.0006  20  PHE   A C   
155  O  O   . PHE   A 20  ? 0.0915 0.2042 0.2128 -0.0003 -0.0039 0.0070  20  PHE   A O   
156  C  CB  . PHE   A 20  ? 0.0960 0.2343 0.2309 -0.0370 -0.0265 0.0299  20  PHE   A CB  
157  C  CG  . PHE   A 20  ? 0.0710 0.2656 0.2403 -0.0343 -0.0447 0.0542  20  PHE   A CG  
158  C  CD1 . PHE   A 20  ? 0.1155 0.2902 0.2551 -0.0423 -0.0386 0.0784  20  PHE   A CD1 
159  C  CD2 . PHE   A 20  ? 0.0957 0.2792 0.2388 -0.0274 -0.0422 0.0585  20  PHE   A CD2 
160  C  CE1 . PHE   A 20  ? 0.1187 0.3094 0.2534 -0.0351 -0.0552 0.0779  20  PHE   A CE1 
161  C  CE2 . PHE   A 20  ? 0.1061 0.3217 0.2514 -0.0402 -0.0411 0.0498  20  PHE   A CE2 
162  C  CZ  . PHE   A 20  ? 0.1194 0.3254 0.2528 -0.0545 -0.0516 0.0761  20  PHE   A CZ  
163  N  N   . PRO   A 21  ? 0.0993 0.2385 0.2338 -0.0329 -0.0160 -0.0037 21  PRO   A N   
164  C  CA  . PRO   A 21  ? 0.1157 0.2651 0.2287 -0.0459 -0.0292 -0.0058 21  PRO   A CA  
165  C  C   . PRO   A 21  ? 0.0981 0.2283 0.2173 -0.0300 -0.0385 -0.0032 21  PRO   A C   
166  O  O   . PRO   A 21  ? 0.0887 0.2762 0.2359 -0.0273 -0.0494 0.0094  21  PRO   A O   
167  C  CB  . PRO   A 21  ? 0.1184 0.3072 0.2613 -0.0668 -0.0343 -0.0168 21  PRO   A CB  
168  C  CG  . PRO   A 21  ? 0.2185 0.3011 0.2925 -0.0878 -0.0486 -0.0038 21  PRO   A CG  
169  C  CD  . PRO   A 21  ? 0.1137 0.2699 0.2668 -0.0539 -0.0233 0.0030  21  PRO   A CD  
170  N  N   A ILE   A 22  ? 0.0901 0.2234 0.2119 -0.0170 -0.0375 -0.0091 22  ILE   A N   
171  N  N   B ILE   A 22  ? 0.0858 0.2215 0.2064 -0.0195 -0.0328 -0.0139 22  ILE   A N   
172  C  CA  A ILE   A 22  ? 0.0984 0.2178 0.1934 -0.0239 -0.0444 -0.0086 22  ILE   A CA  
173  C  CA  B ILE   A 22  ? 0.1001 0.2223 0.1834 -0.0267 -0.0347 -0.0174 22  ILE   A CA  
174  C  C   A ILE   A 22  ? 0.0858 0.2200 0.1880 -0.0130 -0.0441 -0.0090 22  ILE   A C   
175  C  C   B ILE   A 22  ? 0.0794 0.2194 0.1803 -0.0149 -0.0368 -0.0110 22  ILE   A C   
176  O  O   A ILE   A 22  ? 0.0980 0.2169 0.1825 -0.0006 -0.0427 0.0093  22  ILE   A O   
177  O  O   B ILE   A 22  ? 0.0810 0.2270 0.1901 -0.0136 -0.0241 -0.0105 22  ILE   A O   
178  C  CB  A ILE   A 22  ? 0.1134 0.1941 0.2035 -0.0309 -0.0457 -0.0158 22  ILE   A CB  
179  C  CB  B ILE   A 22  ? 0.1244 0.2026 0.1892 -0.0266 -0.0279 -0.0300 22  ILE   A CB  
180  C  CG1 A ILE   A 22  ? 0.1000 0.2077 0.2184 -0.0300 -0.0485 -0.0198 22  ILE   A CG1 
181  C  CG1 B ILE   A 22  ? 0.1461 0.2193 0.2070 -0.0193 -0.0128 -0.0452 22  ILE   A CG1 
182  C  CG2 A ILE   A 22  ? 0.1020 0.2034 0.2117 -0.0301 -0.0575 -0.0076 22  ILE   A CG2 
183  C  CG2 B ILE   A 22  ? 0.1053 0.2119 0.1980 -0.0212 -0.0461 -0.0164 22  ILE   A CG2 
184  C  CD1 A ILE   A 22  ? 0.1152 0.2206 0.2053 -0.0199 -0.0402 -0.0190 22  ILE   A CD1 
185  C  CD1 B ILE   A 22  ? 0.1881 0.2462 0.1993 -0.0133 0.0038  -0.0548 22  ILE   A CD1 
186  N  N   . ALA   A 23  ? 0.0926 0.2084 0.1846 -0.0176 -0.0283 -0.0107 23  ALA   A N   
187  C  CA  . ALA   A 23  ? 0.0736 0.2111 0.1939 -0.0019 -0.0382 -0.0015 23  ALA   A CA  
188  C  C   . ALA   A 23  ? 0.0849 0.2068 0.1960 -0.0107 -0.0280 -0.0044 23  ALA   A C   
189  O  O   . ALA   A 23  ? 0.1041 0.2121 0.2308 -0.0158 -0.0293 0.0092  23  ALA   A O   
190  C  CB  . ALA   A 23  ? 0.0807 0.2234 0.1952 -0.0006 -0.0422 -0.0055 23  ALA   A CB  
191  N  N   . LYS   A 24  ? 0.0993 0.2242 0.1998 -0.0169 -0.0439 -0.0050 24  LYS   A N   
192  C  CA  . LYS   A 24  ? 0.1070 0.2778 0.2022 0.0019  -0.0422 0.0152  24  LYS   A CA  
193  C  C   . LYS   A 24  ? 0.1171 0.2925 0.1821 -0.0009 -0.0516 0.0012  24  LYS   A C   
194  O  O   . LYS   A 24  ? 0.1420 0.3539 0.2052 -0.0094 -0.0629 0.0156  24  LYS   A O   
195  C  CB  . LYS   A 24  ? 0.1280 0.3190 0.2452 0.0240  -0.0408 0.0215  24  LYS   A CB  
196  C  CG  . LYS   A 24  ? 0.1590 0.3384 0.2446 0.0223  -0.0313 0.0258  24  LYS   A CG  
197  C  CD  . LYS   A 24  ? 0.1824 0.3771 0.3104 0.0363  -0.0342 0.0429  24  LYS   A CD  
198  C  CE  . LYS   A 24  ? 0.2392 0.3831 0.3256 0.0450  -0.0151 0.0448  24  LYS   A CE  
199  N  NZ  . LYS   A 24  ? 0.2679 0.4080 0.4252 0.0517  0.0346  0.0324  24  LYS   A NZ  
200  N  N   . GLY   A 25  ? 0.1187 0.2686 0.2003 -0.0037 -0.0444 -0.0126 25  GLY   A N   
201  C  CA  . GLY   A 25  ? 0.1070 0.3055 0.1943 -0.0230 -0.0471 -0.0249 25  GLY   A CA  
202  C  C   . GLY   A 25  ? 0.1174 0.2926 0.1618 0.0055  -0.0542 -0.0194 25  GLY   A C   
203  O  O   . GLY   A 25  ? 0.1257 0.3119 0.1957 -0.0027 -0.0550 -0.0081 25  GLY   A O   
204  N  N   . GLU   A 26  ? 0.1187 0.3414 0.1546 -0.0149 -0.0672 -0.0312 26  GLU   A N   
205  C  CA  . GLU   A 26  ? 0.1298 0.3424 0.1369 -0.0070 -0.0524 -0.0220 26  GLU   A CA  
206  C  C   . GLU   A 26  ? 0.1188 0.2964 0.1510 -0.0096 -0.0409 -0.0049 26  GLU   A C   
207  O  O   . GLU   A 26  ? 0.1522 0.3133 0.1334 -0.0123 -0.0464 0.0048  26  GLU   A O   
208  C  CB  . GLU   A 26  ? 0.1739 0.4351 0.1510 -0.0418 -0.0711 -0.0638 26  GLU   A CB  
209  C  CG  . GLU   A 26  ? 0.2105 0.4924 0.1757 -0.0543 -0.0986 -0.0489 26  GLU   A CG  
210  C  CD  . GLU   A 26  ? 0.3044 0.5489 0.2804 -0.0308 -0.0690 -0.0023 26  GLU   A CD  
211  O  OE1 . GLU   A 26  ? 0.3572 0.6173 0.3496 -0.0490 -0.0929 0.0241  26  GLU   A OE1 
212  O  OE2 . GLU   A 26  ? 0.3447 0.6426 0.4283 0.0378  -0.1177 -0.0005 26  GLU   A OE2 
213  N  N   A ARG   A 27  ? 0.1112 0.2248 0.1377 -0.0122 -0.0358 -0.0150 27  ARG   A N   
214  N  N   B ARG   A 27  ? 0.1153 0.2233 0.1348 -0.0207 -0.0395 -0.0194 27  ARG   A N   
215  C  CA  A ARG   A 27  ? 0.1050 0.2132 0.1431 -0.0096 -0.0351 -0.0129 27  ARG   A CA  
216  C  CA  B ARG   A 27  ? 0.1011 0.2151 0.1393 -0.0137 -0.0350 -0.0141 27  ARG   A CA  
217  C  C   A ARG   A 27  ? 0.0891 0.1879 0.1472 -0.0162 -0.0404 -0.0098 27  ARG   A C   
218  C  C   B ARG   A 27  ? 0.0865 0.1884 0.1415 -0.0150 -0.0403 -0.0092 27  ARG   A C   
219  O  O   A ARG   A 27  ? 0.1021 0.1959 0.1448 -0.0112 -0.0411 -0.0077 27  ARG   A O   
220  O  O   B ARG   A 27  ? 0.1083 0.2047 0.1412 0.0000  -0.0414 0.0023  27  ARG   A O   
221  C  CB  A ARG   A 27  ? 0.1448 0.2175 0.1509 -0.0103 -0.0386 -0.0158 27  ARG   A CB  
222  C  CB  B ARG   A 27  ? 0.1159 0.2243 0.1369 -0.0204 -0.0193 -0.0250 27  ARG   A CB  
223  C  CG  A ARG   A 27  ? 0.1401 0.2296 0.1790 -0.0163 -0.0255 -0.0205 27  ARG   A CG  
224  C  CG  B ARG   A 27  ? 0.1668 0.2464 0.1554 -0.0217 -0.0086 -0.0164 27  ARG   A CG  
225  C  CD  A ARG   A 27  ? 0.1072 0.2360 0.1873 -0.0110 -0.0314 -0.0209 27  ARG   A CD  
226  C  CD  B ARG   A 27  ? 0.1987 0.2698 0.1744 -0.0191 0.0015  -0.0171 27  ARG   A CD  
227  N  NE  A ARG   A 27  ? 0.1293 0.2113 0.2022 -0.0183 -0.0510 -0.0351 27  ARG   A NE  
228  N  NE  B ARG   A 27  ? 0.1562 0.2569 0.1910 -0.0048 0.0221  0.0073  27  ARG   A NE  
229  C  CZ  A ARG   A 27  ? 0.1099 0.2072 0.2181 -0.0016 -0.0390 -0.0205 27  ARG   A CZ  
230  C  CZ  B ARG   A 27  ? 0.1585 0.2273 0.1382 0.0076  0.0172  -0.0202 27  ARG   A CZ  
231  N  NH1 A ARG   A 27  ? 0.1504 0.2138 0.2207 -0.0162 -0.0640 -0.0412 27  ARG   A NH1 
232  N  NH1 B ARG   A 27  ? 0.1649 0.2034 0.1545 0.0014  0.0059  -0.0338 27  ARG   A NH1 
233  N  NH2 A ARG   A 27  ? 0.1427 0.2331 0.2357 0.0030  -0.0072 -0.0386 27  ARG   A NH2 
234  N  NH2 B ARG   A 27  ? 0.1407 0.2424 0.1380 0.0020  0.0266  -0.0269 27  ARG   A NH2 
235  N  N   . GLN   A 28  ? 0.0834 0.1904 0.1314 -0.0072 -0.0368 -0.0143 28  GLN   A N   
236  C  CA  . GLN   A 28  ? 0.0925 0.1638 0.1288 -0.0033 -0.0289 -0.0137 28  GLN   A CA  
237  C  C   . GLN   A 28  ? 0.0824 0.1730 0.1128 -0.0041 -0.0216 -0.0106 28  GLN   A C   
238  O  O   . GLN   A 28  ? 0.0977 0.1930 0.1195 -0.0141 -0.0361 -0.0153 28  GLN   A O   
239  C  CB  . GLN   A 28  ? 0.0954 0.1765 0.1411 -0.0012 -0.0262 -0.0075 28  GLN   A CB  
240  C  CG  . GLN   A 28  ? 0.0930 0.1872 0.1480 -0.0064 -0.0275 -0.0108 28  GLN   A CG  
241  C  CD  . GLN   A 28  ? 0.0917 0.1986 0.1420 -0.0140 -0.0350 -0.0156 28  GLN   A CD  
242  O  OE1 . GLN   A 28  ? 0.0820 0.1864 0.1576 -0.0161 -0.0295 -0.0194 28  GLN   A OE1 
243  N  NE2 . GLN   A 28  ? 0.0861 0.2078 0.1251 -0.0048 -0.0328 0.0012  28  GLN   A NE2 
244  N  N   . SER   A 29  ? 0.0886 0.1777 0.1239 -0.0021 -0.0308 -0.0169 29  SER   A N   
245  C  CA  . SER   A 29  ? 0.0858 0.1581 0.1096 -0.0054 -0.0251 0.0000  29  SER   A CA  
246  C  C   . SER   A 29  ? 0.1001 0.1654 0.1212 0.0050  -0.0289 0.0106  29  SER   A C   
247  O  O   . SER   A 29  ? 0.1042 0.1781 0.1223 0.0006  -0.0170 -0.0008 29  SER   A O   
248  C  CB  . SER   A 29  ? 0.0903 0.1627 0.1146 -0.0045 -0.0221 -0.0049 29  SER   A CB  
249  O  OG  . SER   A 29  ? 0.0861 0.1687 0.1093 -0.0111 -0.0165 -0.0119 29  SER   A OG  
250  N  N   . PRO   A 30  ? 0.0827 0.1598 0.1183 0.0089  -0.0218 0.0036  30  PRO   A N   
251  C  CA  . PRO   A 30  ? 0.0855 0.1622 0.1120 0.0060  -0.0250 0.0016  30  PRO   A CA  
252  C  C   . PRO   A 30  ? 0.1006 0.1596 0.1146 0.0116  -0.0267 0.0092  30  PRO   A C   
253  O  O   . PRO   A 30  ? 0.0929 0.1899 0.1279 0.0122  -0.0360 -0.0042 30  PRO   A O   
254  C  CB  . PRO   A 30  ? 0.1060 0.1578 0.1126 0.0216  -0.0296 -0.0046 30  PRO   A CB  
255  C  CG  . PRO   A 30  ? 0.0934 0.1545 0.1161 0.0149  -0.0233 -0.0087 30  PRO   A CG  
256  C  CD  . PRO   A 30  ? 0.0923 0.1620 0.1278 0.0110  -0.0230 -0.0092 30  PRO   A CD  
257  N  N   . VAL   A 31  ? 0.0943 0.1634 0.1206 0.0133  -0.0399 0.0149  31  VAL   A N   
258  C  CA  . VAL   A 31  ? 0.0920 0.1620 0.1185 0.0045  -0.0271 0.0130  31  VAL   A CA  
259  C  C   . VAL   A 31  ? 0.1183 0.1787 0.1280 0.0032  -0.0205 0.0208  31  VAL   A C   
260  O  O   . VAL   A 31  ? 0.1146 0.1871 0.1315 -0.0028 -0.0358 0.0224  31  VAL   A O   
261  C  CB  . VAL   A 31  ? 0.1155 0.1672 0.1377 0.0154  -0.0240 0.0024  31  VAL   A CB  
262  C  CG1 . VAL   A 31  ? 0.1258 0.1827 0.1447 0.0083  -0.0199 -0.0144 31  VAL   A CG1 
263  C  CG2 . VAL   A 31  ? 0.1138 0.1705 0.1425 0.0122  -0.0077 -0.0002 31  VAL   A CG2 
264  N  N   . ASP   A 32  ? 0.1052 0.1693 0.1265 0.0013  -0.0383 0.0183  32  ASP   A N   
265  C  CA  . ASP   A 32  ? 0.1057 0.1581 0.1223 0.0096  -0.0250 0.0044  32  ASP   A CA  
266  C  C   . ASP   A 32  ? 0.1285 0.1749 0.0989 0.0119  -0.0268 -0.0010 32  ASP   A C   
267  O  O   . ASP   A 32  ? 0.1424 0.2194 0.1290 0.0044  -0.0415 -0.0250 32  ASP   A O   
268  C  CB  . ASP   A 32  ? 0.1249 0.1772 0.1194 0.0098  -0.0180 0.0161  32  ASP   A CB  
269  C  CG  . ASP   A 32  ? 0.1257 0.1858 0.1358 0.0083  -0.0226 0.0253  32  ASP   A CG  
270  O  OD1 . ASP   A 32  ? 0.1375 0.1860 0.1335 0.0073  -0.0378 0.0143  32  ASP   A OD1 
271  O  OD2 . ASP   A 32  ? 0.2029 0.2287 0.1396 -0.0219 -0.0359 0.0374  32  ASP   A OD2 
272  N  N   . ILE   A 33  ? 0.1251 0.1843 0.1246 0.0041  -0.0276 -0.0169 33  ILE   A N   
273  C  CA  . ILE   A 33  ? 0.1442 0.1745 0.1424 0.0172  -0.0309 0.0010  33  ILE   A CA  
274  C  C   . ILE   A 33  ? 0.1492 0.1886 0.1387 0.0290  -0.0146 0.0212  33  ILE   A C   
275  O  O   . ILE   A 33  ? 0.1591 0.1955 0.1611 0.0054  -0.0193 0.0198  33  ILE   A O   
276  C  CB  . ILE   A 33  ? 0.1371 0.2031 0.1458 0.0065  -0.0304 0.0115  33  ILE   A CB  
277  C  CG1 . ILE   A 33  ? 0.1189 0.2053 0.1608 0.0150  -0.0269 0.0256  33  ILE   A CG1 
278  C  CG2 . ILE   A 33  ? 0.1391 0.2182 0.1693 0.0140  -0.0275 0.0070  33  ILE   A CG2 
279  C  CD1 . ILE   A 33  ? 0.1412 0.2009 0.1611 0.0266  -0.0310 0.0256  33  ILE   A CD1 
280  N  N   A ASP   A 34  ? 0.1702 0.2115 0.1362 0.0201  -0.0294 0.0270  34  ASP   A N   
281  N  N   B ASP   A 34  ? 0.1627 0.2153 0.1420 0.0192  -0.0272 0.0257  34  ASP   A N   
282  C  CA  A ASP   A 34  ? 0.1968 0.2095 0.1495 0.0280  -0.0289 0.0349  34  ASP   A CA  
283  C  CA  B ASP   A 34  ? 0.1826 0.2128 0.1665 0.0321  -0.0202 0.0348  34  ASP   A CA  
284  C  C   A ASP   A 34  ? 0.2193 0.2154 0.1466 0.0453  -0.0135 0.0443  34  ASP   A C   
285  C  C   B ASP   A 34  ? 0.2074 0.2147 0.1572 0.0484  -0.0066 0.0418  34  ASP   A C   
286  O  O   A ASP   A 34  ? 0.2428 0.2406 0.1532 0.0396  0.0069  0.0291  34  ASP   A O   
287  O  O   B ASP   A 34  ? 0.2074 0.2334 0.1639 0.0434  0.0173  0.0286  34  ASP   A O   
288  C  CB  A ASP   A 34  ? 0.2156 0.2383 0.1441 0.0204  -0.0376 0.0394  34  ASP   A CB  
289  C  CB  B ASP   A 34  ? 0.1888 0.2502 0.1850 0.0357  -0.0269 0.0399  34  ASP   A CB  
290  C  CG  A ASP   A 34  ? 0.2331 0.2577 0.1563 0.0278  -0.0373 0.0586  34  ASP   A CG  
291  C  CG  B ASP   A 34  ? 0.1892 0.2831 0.2061 0.0341  -0.0147 0.0569  34  ASP   A CG  
292  O  OD1 A ASP   A 34  ? 0.2479 0.2464 0.1733 0.0319  -0.0495 0.0865  34  ASP   A OD1 
293  O  OD1 B ASP   A 34  ? 0.2184 0.2740 0.2583 0.0486  0.0056  0.0935  34  ASP   A OD1 
294  O  OD2 A ASP   A 34  ? 0.2411 0.3402 0.1854 0.0063  -0.0430 0.0858  34  ASP   A OD2 
295  O  OD2 B ASP   A 34  ? 0.2275 0.3267 0.2599 0.0322  0.0210  0.0594  34  ASP   A OD2 
296  N  N   . THR   A 35  ? 0.2049 0.2242 0.1685 0.0489  0.0056  0.0326  35  THR   A N   
297  C  CA  . THR   A 35  ? 0.2284 0.2210 0.1804 0.0687  0.0214  0.0409  35  THR   A CA  
298  C  C   . THR   A 35  ? 0.2604 0.2364 0.1846 0.0687  0.0283  0.0648  35  THR   A C   
299  O  O   . THR   A 35  ? 0.2780 0.2772 0.2268 0.0745  0.0554  0.0570  35  THR   A O   
300  C  CB  . THR   A 35  ? 0.2219 0.2790 0.2014 0.0363  0.0130  0.0550  35  THR   A CB  
301  O  OG1 . THR   A 35  ? 0.1952 0.2589 0.2093 0.0134  0.0116  0.0450  35  THR   A OG1 
302  C  CG2 . THR   A 35  ? 0.2199 0.2979 0.1960 0.0402  0.0027  0.0275  35  THR   A CG2 
303  N  N   A HIS   A 36  ? 0.3044 0.2519 0.1647 0.0728  0.0317  0.0783  36  HIS   A N   
304  N  N   B HIS   A 36  ? 0.2879 0.2388 0.1719 0.0878  0.0326  0.0574  36  HIS   A N   
305  C  CA  A HIS   A 36  ? 0.3603 0.2571 0.1638 0.0786  0.0364  0.0800  36  HIS   A CA  
306  C  CA  B HIS   A 36  ? 0.3306 0.2352 0.1644 0.1007  0.0321  0.0430  36  HIS   A CA  
307  C  C   A HIS   A 36  ? 0.4349 0.3023 0.1785 0.0528  0.0246  0.0579  36  HIS   A C   
308  C  C   B HIS   A 36  ? 0.3553 0.2410 0.1222 0.0945  0.0103  0.0477  36  HIS   A C   
309  O  O   A HIS   A 36  ? 0.5857 0.3160 0.1854 0.0398  0.0342  0.1097  36  HIS   A O   
310  O  O   B HIS   A 36  ? 0.2848 0.2472 0.1067 0.1212  -0.0207 0.0480  36  HIS   A O   
311  C  CB  A HIS   A 36  ? 0.3451 0.2569 0.1423 0.0533  0.0440  0.0903  36  HIS   A CB  
312  C  CB  B HIS   A 36  ? 0.3325 0.2400 0.1740 0.0907  0.0328  0.0398  36  HIS   A CB  
313  C  CG  A HIS   A 36  ? 0.3378 0.2707 0.1509 0.0495  0.0079  0.0962  36  HIS   A CG  
314  C  CG  B HIS   A 36  ? 0.3382 0.2428 0.1851 0.0850  -0.0125 0.0369  36  HIS   A CG  
315  N  ND1 A HIS   A 36  ? 0.3373 0.2704 0.1685 0.0260  -0.0158 0.1010  36  HIS   A ND1 
316  N  ND1 B HIS   A 36  ? 0.3505 0.2482 0.1707 0.0889  -0.0239 0.0627  36  HIS   A ND1 
317  C  CD2 A HIS   A 36  ? 0.3278 0.3042 0.1608 0.0272  -0.0206 0.0824  36  HIS   A CD2 
318  C  CD2 B HIS   A 36  ? 0.3466 0.2518 0.1847 0.0767  0.0069  0.0134  36  HIS   A CD2 
319  C  CE1 A HIS   A 36  ? 0.3204 0.3059 0.2054 0.0584  -0.0400 0.0969  36  HIS   A CE1 
320  C  CE1 B HIS   A 36  ? 0.3581 0.2342 0.1581 0.0797  -0.0203 0.0124  36  HIS   A CE1 
321  N  NE2 A HIS   A 36  ? 0.3524 0.3219 0.1969 0.0209  -0.0228 0.0861  36  HIS   A NE2 
322  N  NE2 B HIS   A 36  ? 0.3903 0.2671 0.1929 0.0815  -0.0196 0.0122  36  HIS   A NE2 
323  N  N   . THR   A 37  ? 0.3987 0.2493 0.1825 0.0773  -0.0119 0.0401  37  THR   A N   
324  C  CA  . THR   A 37  ? 0.4157 0.2888 0.2000 0.0755  -0.0174 0.0321  37  THR   A CA  
325  C  C   . THR   A 37  ? 0.3173 0.2787 0.1585 0.0785  -0.0116 -0.0031 37  THR   A C   
326  O  O   . THR   A 37  ? 0.3895 0.2799 0.2209 0.0780  -0.0645 -0.0136 37  THR   A O   
327  C  CB  . THR   A 37  ? 0.3711 0.3003 0.3275 0.0923  -0.1002 0.0362  37  THR   A CB  
328  O  OG1 . THR   A 37  ? 0.4896 0.3620 0.5208 0.1174  -0.1226 0.0791  37  THR   A OG1 
329  C  CG2 . THR   A 37  ? 0.3989 0.4150 0.3186 0.0744  -0.0933 0.0189  37  THR   A CG2 
330  N  N   . ALA   A 38  ? 0.3026 0.2646 0.1529 0.0618  0.0052  0.0063  38  ALA   A N   
331  C  CA  . ALA   A 38  ? 0.2575 0.2497 0.1734 0.0404  0.0245  0.0145  38  ALA   A CA  
332  C  C   . ALA   A 38  ? 0.2503 0.2827 0.2173 0.0427  0.0264  0.0311  38  ALA   A C   
333  O  O   . ALA   A 38  ? 0.3337 0.3140 0.3343 0.0023  0.1031  0.0248  38  ALA   A O   
334  C  CB  . ALA   A 38  ? 0.2327 0.2298 0.1924 0.0405  0.0117  0.0334  38  ALA   A CB  
335  N  N   . LYS   A 39  ? 0.2537 0.3006 0.1821 0.0595  0.0128  0.0193  39  LYS   A N   
336  C  CA  . LYS   A 39  ? 0.2610 0.3408 0.1909 0.0982  -0.0188 0.0240  39  LYS   A CA  
337  C  C   . LYS   A 39  ? 0.2232 0.3502 0.1378 0.0463  -0.0120 0.0290  39  LYS   A C   
338  O  O   . LYS   A 39  ? 0.1685 0.3220 0.1451 0.0515  0.0005  0.0361  39  LYS   A O   
339  C  CB  . LYS   A 39  ? 0.2837 0.4255 0.2728 0.1328  -0.0803 0.0096  39  LYS   A CB  
340  C  CG  . LYS   A 39  ? 0.3390 0.5451 0.3401 0.1333  -0.0853 -0.0091 39  LYS   A CG  
341  C  CD  . LYS   A 39  ? 0.2423 0.5388 0.3785 0.1833  -0.0777 0.0366  39  LYS   A CD  
342  C  CE  . LYS   A 39  ? 0.2745 0.5836 0.4213 0.1567  -0.0513 -0.0061 39  LYS   A CE  
343  N  NZ  . LYS   A 39  ? 0.2901 0.6704 0.4909 0.1456  -0.0292 0.0365  39  LYS   A NZ  
344  N  N   . TYR   A 40  ? 0.2673 0.3777 0.1600 0.0314  0.0125  0.0491  40  TYR   A N   
345  C  CA  . TYR   A 40  ? 0.1972 0.3960 0.1540 0.0040  0.0067  0.0163  40  TYR   A CA  
346  C  C   . TYR   A 40  ? 0.1945 0.4057 0.1429 0.0385  -0.0117 -0.0090 40  TYR   A C   
347  O  O   . TYR   A 40  ? 0.1930 0.4544 0.1505 0.0658  -0.0070 -0.0232 40  TYR   A O   
348  C  CB  . TYR   A 40  ? 0.2628 0.4192 0.1912 -0.0221 0.0325  0.0271  40  TYR   A CB  
349  C  CG  . TYR   A 40  ? 0.2449 0.5280 0.1865 -0.0346 0.0327  -0.0001 40  TYR   A CG  
350  C  CD1 . TYR   A 40  ? 0.2115 0.5421 0.1829 -0.0457 0.0052  -0.0266 40  TYR   A CD1 
351  C  CD2 . TYR   A 40  ? 0.2514 0.6340 0.1853 0.0110  0.0336  0.0080  40  TYR   A CD2 
352  C  CE1 . TYR   A 40  ? 0.2070 0.6410 0.2079 -0.0010 -0.0342 -0.0234 40  TYR   A CE1 
353  C  CE2 . TYR   A 40  ? 0.2455 0.7202 0.1920 0.0196  0.0527  -0.0195 40  TYR   A CE2 
354  C  CZ  . TYR   A 40  ? 0.2019 0.7044 0.2321 -0.0079 -0.0099 0.0008  40  TYR   A CZ  
355  O  OH  . TYR   A 40  ? 0.2104 0.8896 0.4163 0.0593  0.0022  -0.0429 40  TYR   A OH  
356  N  N   . ASP   A 41  ? 0.1705 0.3966 0.1637 0.0234  -0.0087 -0.0303 41  ASP   A N   
357  C  CA  . ASP   A 41  ? 0.1684 0.4254 0.1784 0.0368  -0.0178 -0.0396 41  ASP   A CA  
358  C  C   . ASP   A 41  ? 0.2020 0.4662 0.1827 0.0901  -0.0101 -0.0363 41  ASP   A C   
359  O  O   . ASP   A 41  ? 0.1787 0.4614 0.2168 0.0363  -0.0240 -0.0167 41  ASP   A O   
360  C  CB  . ASP   A 41  ? 0.2049 0.4215 0.2095 0.0220  -0.0175 -0.0505 41  ASP   A CB  
361  C  CG  . ASP   A 41  ? 0.2615 0.4198 0.2934 -0.0046 -0.0374 -0.0684 41  ASP   A CG  
362  O  OD1 . ASP   A 41  ? 0.2914 0.4074 0.2986 0.0308  -0.0742 -0.0915 41  ASP   A OD1 
363  O  OD2 . ASP   A 41  ? 0.3518 0.4418 0.4068 -0.0764 -0.0724 -0.0696 41  ASP   A OD2 
364  N  N   . PRO   A 42  ? 0.2421 0.5586 0.2012 0.1253  0.0037  0.0050  42  PRO   A N   
365  C  CA  . PRO   A 42  ? 0.2650 0.6003 0.2501 0.1504  0.0373  0.0106  42  PRO   A CA  
366  C  C   . PRO   A 42  ? 0.3045 0.5664 0.2561 0.1728  0.0262  -0.0035 42  PRO   A C   
367  O  O   . PRO   A 42  ? 0.2799 0.6028 0.3431 0.2150  0.0311  -0.0052 42  PRO   A O   
368  C  CB  . PRO   A 42  ? 0.3313 0.6314 0.2675 0.1558  0.0648  0.0187  42  PRO   A CB  
369  C  CG  . PRO   A 42  ? 0.3135 0.6417 0.2429 0.1243  0.0828  0.0033  42  PRO   A CG  
370  C  CD  . PRO   A 42  ? 0.2971 0.5849 0.2053 0.1477  0.0486  0.0101  42  PRO   A CD  
371  N  N   . SER   A 43  ? 0.3037 0.5236 0.2372 0.1468  0.0080  -0.0143 43  SER   A N   
372  C  CA  . SER   A 43  ? 0.3905 0.4751 0.2522 0.1422  -0.0461 -0.0120 43  SER   A CA  
373  C  C   . SER   A 43  ? 0.3782 0.4855 0.2751 0.0751  -0.0503 0.0122  43  SER   A C   
374  O  O   . SER   A 43  ? 0.4200 0.4669 0.3668 0.0771  -0.1037 0.0090  43  SER   A O   
375  C  CB  . SER   A 43  ? 0.4557 0.4852 0.2697 0.1058  -0.0443 -0.0445 43  SER   A CB  
376  O  OG  . SER   A 43  ? 0.5020 0.5038 0.3021 0.0873  -0.0639 -0.0864 43  SER   A OG  
377  N  N   . LEU   A 44  ? 0.2999 0.5197 0.2431 0.0371  -0.0583 0.0203  44  LEU   A N   
378  C  CA  . LEU   A 44  ? 0.2802 0.5153 0.2530 -0.0071 -0.0731 0.0451  44  LEU   A CA  
379  C  C   . LEU   A 44  ? 0.2471 0.5881 0.3768 -0.0759 -0.0731 0.1045  44  LEU   A C   
380  O  O   . LEU   A 44  ? 0.2844 0.6451 0.3697 -0.0899 -0.0389 0.1537  44  LEU   A O   
381  C  CB  . LEU   A 44  ? 0.2696 0.5177 0.2449 -0.0447 -0.0338 0.0007  44  LEU   A CB  
382  C  CG  . LEU   A 44  ? 0.2672 0.4096 0.2070 -0.0635 -0.0240 0.0095  44  LEU   A CG  
383  C  CD1 . LEU   A 44  ? 0.3073 0.3643 0.2197 -0.0985 -0.0095 0.0148  44  LEU   A CD1 
384  C  CD2 . LEU   A 44  ? 0.2586 0.3463 0.2601 -0.0838 -0.0299 -0.0158 44  LEU   A CD2 
385  N  N   . LYS   A 45  ? 0.4154 0.6100 0.4598 -0.0788 -0.0886 0.1635  45  LYS   A N   
386  C  CA  . LYS   A 45  ? 0.4020 0.5591 0.5561 -0.0539 -0.1137 0.0896  45  LYS   A CA  
387  C  C   . LYS   A 45  ? 0.3671 0.5334 0.5017 -0.0996 -0.1505 0.0967  45  LYS   A C   
388  O  O   . LYS   A 45  ? 0.3783 0.4263 0.4818 0.1265  -0.2032 0.0928  45  LYS   A O   
389  C  CB  . LYS   A 45  ? 0.3695 0.6116 0.4245 0.0281  -0.1221 0.0956  45  LYS   A CB  
390  C  CG  . LYS   A 45  ? 0.3200 0.6391 0.4419 0.0174  -0.1098 0.0325  45  LYS   A CG  
391  N  N   . PRO   A 46  ? 0.2438 0.5873 0.3846 -0.1536 -0.0390 0.0668  46  PRO   A N   
392  C  CA  . PRO   A 46  ? 0.3521 0.5626 0.3352 -0.1055 -0.0132 0.1055  46  PRO   A CA  
393  C  C   . PRO   A 46  ? 0.1540 0.4754 0.2779 -0.0520 -0.0391 0.0627  46  PRO   A C   
394  O  O   . PRO   A 46  ? 0.1786 0.4852 0.2776 -0.0697 -0.0596 0.0892  46  PRO   A O   
395  C  CB  . PRO   A 46  ? 0.3215 0.5642 0.3446 -0.1095 -0.0128 0.0805  46  PRO   A CB  
396  C  CG  . PRO   A 46  ? 0.3265 0.6461 0.3867 -0.0665 -0.0265 0.0510  46  PRO   A CG  
397  C  CD  . PRO   A 46  ? 0.3546 0.6134 0.3490 -0.0715 -0.0337 0.0505  46  PRO   A CD  
398  N  N   . LEU   A 47  ? 0.1735 0.4256 0.3682 -0.0622 -0.0621 0.0651  47  LEU   A N   
399  C  CA  . LEU   A 47  ? 0.1190 0.3567 0.3243 -0.0584 -0.0475 0.0504  47  LEU   A CA  
400  C  C   . LEU   A 47  ? 0.1333 0.3057 0.3165 -0.0580 -0.0621 0.0194  47  LEU   A C   
401  O  O   . LEU   A 47  ? 0.1224 0.3451 0.3896 -0.0580 -0.0766 0.0638  47  LEU   A O   
402  C  CB  . LEU   A 47  ? 0.2076 0.3478 0.4546 -0.0383 -0.0943 0.0531  47  LEU   A CB  
403  C  CG  . LEU   A 47  ? 0.1808 0.3444 0.4993 -0.0578 -0.1062 0.0132  47  LEU   A CG  
404  C  CD1 . LEU   A 47  ? 0.1057 0.3691 0.5133 -0.0620 -0.0998 0.0139  47  LEU   A CD1 
405  C  CD2 . LEU   A 47  ? 0.1432 0.3463 0.5859 -0.0200 -0.1252 -0.0096 47  LEU   A CD2 
406  N  N   . SER   A 48  ? 0.0992 0.2703 0.2243 -0.0248 -0.0550 0.0056  48  SER   A N   
407  C  CA  . SER   A 48  ? 0.1143 0.2780 0.2354 -0.0182 -0.0273 0.0057  48  SER   A CA  
408  C  C   . SER   A 48  ? 0.1037 0.2565 0.2239 -0.0200 -0.0185 -0.0101 48  SER   A C   
409  O  O   . SER   A 48  ? 0.1270 0.2509 0.2472 -0.0417 -0.0154 -0.0336 48  SER   A O   
410  C  CB  . SER   A 48  ? 0.1340 0.2894 0.2715 0.0042  -0.0284 0.0284  48  SER   A CB  
411  O  OG  . SER   A 48  ? 0.2114 0.3352 0.2996 0.0473  -0.0270 0.0270  48  SER   A OG  
412  N  N   . VAL   A 49  ? 0.1156 0.2685 0.2193 -0.0572 -0.0162 -0.0091 49  VAL   A N   
413  C  CA  . VAL   A 49  ? 0.1482 0.2875 0.2316 -0.0734 -0.0096 -0.0049 49  VAL   A CA  
414  C  C   . VAL   A 49  ? 0.1625 0.3127 0.2262 -0.0780 -0.0280 -0.0221 49  VAL   A C   
415  O  O   . VAL   A 49  ? 0.1956 0.4056 0.2553 -0.1330 -0.0363 -0.0195 49  VAL   A O   
416  C  CB  . VAL   A 49  ? 0.2092 0.2777 0.2476 -0.1004 0.0228  -0.0215 49  VAL   A CB  
417  C  CG1 . VAL   A 49  ? 0.2906 0.2927 0.2635 -0.1084 0.0501  -0.0309 49  VAL   A CG1 
418  C  CG2 . VAL   A 49  ? 0.2330 0.2658 0.3312 -0.0841 0.0093  -0.0306 49  VAL   A CG2 
419  N  N   . SER   A 50  ? 0.1429 0.2896 0.2425 -0.0599 -0.0399 -0.0184 50  SER   A N   
420  C  CA  . SER   A 50  ? 0.1383 0.3072 0.2714 -0.0407 -0.0597 -0.0095 50  SER   A CA  
421  C  C   . SER   A 50  ? 0.1429 0.3098 0.2367 -0.0255 -0.0894 -0.0019 50  SER   A C   
422  O  O   . SER   A 50  ? 0.1905 0.2802 0.2562 -0.0090 -0.0759 0.0169  50  SER   A O   
423  C  CB  . SER   A 50  ? 0.2250 0.3623 0.2837 -0.0257 -0.0282 0.0045  50  SER   A CB  
424  O  OG  . SER   A 50  ? 0.3047 0.4898 0.3805 -0.0096 -0.0002 -0.0532 50  SER   A OG  
425  N  N   . TYR   A 51  ? 0.1225 0.3002 0.2357 -0.0135 -0.0636 -0.0015 51  TYR   A N   
426  C  CA  . TYR   A 51  ? 0.1284 0.2783 0.2171 -0.0075 -0.0560 0.0190  51  TYR   A CA  
427  C  C   . TYR   A 51  ? 0.1513 0.3309 0.2319 0.0085  -0.0629 0.0247  51  TYR   A C   
428  O  O   . TYR   A 51  ? 0.1493 0.2993 0.2128 -0.0071 -0.0733 0.0163  51  TYR   A O   
429  C  CB  . TYR   A 51  ? 0.1155 0.2785 0.2228 -0.0096 -0.0691 0.0018  51  TYR   A CB  
430  C  CG  . TYR   A 51  ? 0.1147 0.2275 0.1777 -0.0149 -0.0445 0.0194  51  TYR   A CG  
431  C  CD1 . TYR   A 51  ? 0.1258 0.2137 0.2083 -0.0017 -0.0443 0.0051  51  TYR   A CD1 
432  C  CD2 . TYR   A 51  ? 0.1100 0.1961 0.1853 -0.0223 -0.0410 0.0076  51  TYR   A CD2 
433  C  CE1 . TYR   A 51  ? 0.1093 0.1938 0.1931 -0.0068 -0.0422 0.0033  51  TYR   A CE1 
434  C  CE2 . TYR   A 51  ? 0.1193 0.1806 0.1991 -0.0124 -0.0385 -0.0006 51  TYR   A CE2 
435  C  CZ  . TYR   A 51  ? 0.1177 0.1909 0.1752 -0.0135 -0.0325 0.0069  51  TYR   A CZ  
436  O  OH  . TYR   A 51  ? 0.1121 0.2004 0.1946 -0.0079 -0.0497 -0.0085 51  TYR   A OH  
437  N  N   . ASP   A 52  ? 0.1520 0.3921 0.2531 -0.0099 -0.0687 0.0233  52  ASP   A N   
438  C  CA  . ASP   A 52  ? 0.1778 0.4038 0.2623 0.0119  -0.0752 0.0572  52  ASP   A CA  
439  C  C   . ASP   A 52  ? 0.1609 0.3272 0.2796 0.0228  -0.1037 0.0439  52  ASP   A C   
440  O  O   . ASP   A 52  ? 0.2156 0.3738 0.2652 -0.0087 -0.0899 0.0691  52  ASP   A O   
441  C  CB  . ASP   A 52  ? 0.1767 0.4508 0.2930 0.0132  -0.0891 0.0772  52  ASP   A CB  
442  C  CG  . ASP   A 52  ? 0.2666 0.5186 0.4560 0.0657  -0.0238 0.0439  52  ASP   A CG  
443  O  OD1 . ASP   A 52  ? 0.4528 0.5727 0.5514 0.0448  0.0830  0.0759  52  ASP   A OD1 
444  O  OD2 . ASP   A 52  ? 0.5169 0.5917 0.6047 0.0792  0.0022  0.1551  52  ASP   A OD2 
445  N  N   . GLN   A 53  ? 0.1508 0.3093 0.3010 0.0101  -0.0728 0.0155  53  GLN   A N   
446  C  CA  . GLN   A 53  ? 0.1702 0.3059 0.3195 0.0283  -0.0577 0.0309  53  GLN   A CA  
447  C  C   . GLN   A 53  ? 0.1528 0.2483 0.2703 0.0094  -0.0673 0.0060  53  GLN   A C   
448  O  O   . GLN   A 53  ? 0.1782 0.2589 0.2853 0.0085  -0.0537 0.0076  53  GLN   A O   
449  C  CB  . GLN   A 53  ? 0.2109 0.3445 0.3457 0.0356  -0.0411 0.0110  53  GLN   A CB  
450  C  CG  . GLN   A 53  ? 0.2283 0.4346 0.4411 0.0286  -0.0130 0.0595  53  GLN   A CG  
451  C  CD  . GLN   A 53  ? 0.2900 0.4742 0.4928 0.0282  -0.0209 0.0771  53  GLN   A CD  
452  O  OE1 . GLN   A 53  ? 0.3625 0.5491 0.6302 -0.0292 0.0493  0.0862  53  GLN   A OE1 
453  N  NE2 . GLN   A 53  ? 0.2800 0.5178 0.5525 0.0110  -0.0516 0.1263  53  GLN   A NE2 
454  N  N   . ALA   A 54  ? 0.1482 0.2331 0.2584 -0.0058 -0.0436 -0.0054 54  ALA   A N   
455  C  CA  . ALA   A 54  ? 0.1382 0.2413 0.2416 0.0075  -0.0439 -0.0202 54  ALA   A CA  
456  C  C   . ALA   A 54  ? 0.1473 0.2466 0.2411 -0.0032 -0.0511 -0.0273 54  ALA   A C   
457  O  O   . ALA   A 54  ? 0.1627 0.3261 0.2649 -0.0270 -0.0606 -0.0662 54  ALA   A O   
458  C  CB  . ALA   A 54  ? 0.1568 0.2541 0.2915 0.0037  -0.0302 -0.0288 54  ALA   A CB  
459  N  N   . THR   A 55  ? 0.1438 0.2167 0.2053 0.0142  -0.0577 0.0006  55  THR   A N   
460  C  CA  . THR   A 55  ? 0.1636 0.1993 0.1837 0.0155  -0.0895 0.0154  55  THR   A CA  
461  C  C   . THR   A 55  ? 0.1606 0.1717 0.1704 -0.0040 -0.0683 0.0254  55  THR   A C   
462  O  O   . THR   A 55  ? 0.1684 0.1776 0.1936 -0.0118 -0.0632 0.0124  55  THR   A O   
463  C  CB  . THR   A 55  ? 0.1967 0.2324 0.2455 0.0297  -0.0904 0.0391  55  THR   A CB  
464  O  OG1 . THR   A 55  ? 0.2000 0.2641 0.3292 0.0375  -0.0740 0.0219  55  THR   A OG1 
465  C  CG2 . THR   A 55  ? 0.2583 0.2368 0.2626 0.0322  -0.0970 0.0561  55  THR   A CG2 
466  N  N   . SER   A 56  ? 0.1345 0.1836 0.1580 -0.0075 -0.0594 0.0196  56  SER   A N   
467  C  CA  . SER   A 56  ? 0.1374 0.1835 0.1508 -0.0039 -0.0592 0.0085  56  SER   A CA  
468  C  C   . SER   A 56  ? 0.1529 0.1991 0.1551 0.0056  -0.0513 0.0310  56  SER   A C   
469  O  O   . SER   A 56  ? 0.1424 0.2178 0.1875 0.0097  -0.0761 0.0269  56  SER   A O   
470  C  CB  . SER   A 56  ? 0.1411 0.1909 0.1521 0.0002  -0.0568 0.0202  56  SER   A CB  
471  O  OG  . SER   A 56  ? 0.1575 0.2004 0.1908 -0.0232 -0.0849 0.0162  56  SER   A OG  
472  N  N   . LEU   A 57  ? 0.1448 0.2092 0.1601 0.0230  -0.0319 0.0345  57  LEU   A N   
473  C  CA  . LEU   A 57  ? 0.1716 0.2061 0.1582 0.0134  -0.0416 0.0357  57  LEU   A CA  
474  C  C   . LEU   A 57  ? 0.1503 0.2233 0.1579 0.0070  -0.0391 0.0316  57  LEU   A C   
475  O  O   . LEU   A 57  ? 0.2245 0.3057 0.1662 0.0691  -0.0659 0.0312  57  LEU   A O   
476  C  CB  . LEU   A 57  ? 0.1846 0.1999 0.1773 0.0003  -0.0312 0.0426  57  LEU   A CB  
477  C  CG  . LEU   A 57  ? 0.2106 0.2254 0.2312 -0.0027 -0.0210 0.0113  57  LEU   A CG  
478  C  CD1 . LEU   A 57  ? 0.2412 0.2264 0.2772 -0.0252 0.0107  -0.0019 57  LEU   A CD1 
479  C  CD2 . LEU   A 57  ? 0.2860 0.2559 0.3013 0.0286  -0.0214 0.0144  57  LEU   A CD2 
480  N  N   . ARG   A 58  ? 0.1637 0.2265 0.1414 0.0149  -0.0406 0.0266  58  ARG   A N   
481  C  CA  . ARG   A 58  ? 0.1558 0.2257 0.1407 0.0064  -0.0317 0.0444  58  ARG   A CA  
482  C  C   . ARG   A 58  ? 0.1278 0.2340 0.1350 0.0159  -0.0413 0.0379  58  ARG   A C   
483  O  O   . ARG   A 58  ? 0.1636 0.2443 0.1342 0.0248  -0.0407 0.0424  58  ARG   A O   
484  C  CB  . ARG   A 58  ? 0.1984 0.2674 0.2323 0.0089  0.0065  0.0821  58  ARG   A CB  
485  C  CG  . ARG   A 58  ? 0.3016 0.3317 0.3394 0.0323  0.0457  0.1159  58  ARG   A CG  
486  C  CD  . ARG   A 58  ? 0.4014 0.4564 0.4102 0.0339  0.1076  0.1330  58  ARG   A CD  
487  N  NE  . ARG   A 58  ? 0.4192 0.5668 0.4266 0.0699  0.1297  0.1098  58  ARG   A NE  
488  C  CZ  . ARG   A 58  ? 0.3628 0.6755 0.3647 0.0802  0.1173  0.1718  58  ARG   A CZ  
489  N  NH1 . ARG   A 58  ? 0.5118 0.6644 0.3805 0.1809  0.1179  0.2207  58  ARG   A NH1 
490  N  NH2 . ARG   A 58  ? 0.4776 0.5563 0.3549 0.1193  0.0639  0.2012  58  ARG   A NH2 
491  N  N   . ILE   A 59  ? 0.1438 0.2238 0.1268 0.0112  -0.0285 0.0334  59  ILE   A N   
492  C  CA  . ILE   A 59  ? 0.1559 0.2242 0.1215 0.0087  -0.0406 0.0356  59  ILE   A CA  
493  C  C   . ILE   A 59  ? 0.1487 0.2298 0.1339 0.0057  -0.0345 0.0385  59  ILE   A C   
494  O  O   . ILE   A 59  ? 0.1582 0.2633 0.1333 0.0105  -0.0319 0.0371  59  ILE   A O   
495  C  CB  . ILE   A 59  ? 0.1542 0.2095 0.1349 0.0112  -0.0373 0.0284  59  ILE   A CB  
496  C  CG1 . ILE   A 59  ? 0.1415 0.2187 0.1505 0.0090  -0.0357 0.0298  59  ILE   A CG1 
497  C  CG2 . ILE   A 59  ? 0.1773 0.2310 0.1465 0.0054  -0.0410 0.0256  59  ILE   A CG2 
498  C  CD1 . ILE   A 59  ? 0.1752 0.2136 0.1819 0.0120  -0.0510 0.0147  59  ILE   A CD1 
499  N  N   A LEU   A 60  ? 0.1410 0.2355 0.1405 0.0085  -0.0355 0.0429  60  LEU   A N   
500  N  N   B LEU   A 60  ? 0.1403 0.2359 0.1377 0.0085  -0.0334 0.0444  60  LEU   A N   
501  C  CA  A LEU   A 60  ? 0.1457 0.2404 0.1712 -0.0049 -0.0255 0.0377  60  LEU   A CA  
502  C  CA  B LEU   A 60  ? 0.1450 0.2402 0.1648 -0.0046 -0.0226 0.0402  60  LEU   A CA  
503  C  C   A LEU   A 60  ? 0.1283 0.2174 0.1561 -0.0108 -0.0303 0.0222  60  LEU   A C   
504  C  C   B LEU   A 60  ? 0.1258 0.2186 0.1496 -0.0089 -0.0251 0.0276  60  LEU   A C   
505  O  O   A LEU   A 60  ? 0.1312 0.2138 0.1690 -0.0031 -0.0257 0.0405  60  LEU   A O   
506  O  O   B LEU   A 60  ? 0.1244 0.2096 0.1556 -0.0032 -0.0087 0.0399  60  LEU   A O   
507  C  CB  A LEU   A 60  ? 0.1626 0.2249 0.2350 -0.0078 -0.0308 0.0501  60  LEU   A CB  
508  C  CB  B LEU   A 60  ? 0.1642 0.2271 0.2288 -0.0118 -0.0265 0.0530  60  LEU   A CB  
509  C  CG  A LEU   A 60  ? 0.2040 0.2818 0.2518 -0.0188 -0.0370 0.0405  60  LEU   A CG  
510  C  CG  B LEU   A 60  ? 0.2053 0.2824 0.2501 -0.0193 -0.0363 0.0412  60  LEU   A CG  
511  C  CD1 . LEU   A 60  ? 0.2046 0.3049 0.2546 -0.0283 -0.0182 0.0467  60  LEU   A CD1 
512  C  CD2 . LEU   A 60  ? 0.2203 0.2996 0.2576 -0.0350 -0.0527 0.0489  60  LEU   A CD2 
513  N  N   . ASN   A 61  ? 0.1561 0.2343 0.1313 -0.0113 -0.0263 0.0177  61  ASN   A N   
514  C  CA  . ASN   A 61  ? 0.1529 0.2218 0.1575 -0.0196 -0.0306 0.0294  61  ASN   A CA  
515  C  C   . ASN   A 61  ? 0.1466 0.2205 0.1624 -0.0197 -0.0222 0.0298  61  ASN   A C   
516  O  O   . ASN   A 61  ? 0.1568 0.2478 0.1685 -0.0228 -0.0178 0.0290  61  ASN   A O   
517  C  CB  . ASN   A 61  ? 0.1559 0.2261 0.1851 -0.0156 -0.0169 0.0257  61  ASN   A CB  
518  C  CG  . ASN   A 61  ? 0.1364 0.2286 0.1698 -0.0200 -0.0147 0.0097  61  ASN   A CG  
519  O  OD1 . ASN   A 61  ? 0.1521 0.2448 0.1725 -0.0033 -0.0240 0.0012  61  ASN   A OD1 
520  N  ND2 . ASN   A 61  ? 0.1475 0.2440 0.1907 -0.0104 -0.0219 0.0051  61  ASN   A ND2 
521  N  N   A ASN   A 62  ? 0.1655 0.2344 0.1568 -0.0323 -0.0236 0.0272  62  ASN   A N   
522  N  N   B ASN   A 62  ? 0.1486 0.2274 0.1601 -0.0364 -0.0214 0.0288  62  ASN   A N   
523  C  CA  A ASN   A 62  ? 0.1901 0.2383 0.1740 -0.0424 -0.0290 0.0254  62  ASN   A CA  
524  C  CA  B ASN   A 62  ? 0.1634 0.2302 0.1805 -0.0456 -0.0210 0.0313  62  ASN   A CA  
525  C  C   A ASN   A 62  ? 0.1693 0.2564 0.1742 -0.0463 -0.0199 0.0237  62  ASN   A C   
526  C  C   B ASN   A 62  ? 0.1500 0.2532 0.1898 -0.0528 -0.0286 0.0289  62  ASN   A C   
527  O  O   A ASN   A 62  ? 0.1649 0.2848 0.2058 -0.0602 -0.0017 0.0146  62  ASN   A O   
528  O  O   B ASN   A 62  ? 0.1698 0.2926 0.2183 -0.0816 -0.0412 0.0278  62  ASN   A O   
529  C  CB  A ASN   A 62  ? 0.2191 0.2696 0.1740 -0.0437 -0.0381 0.0112  62  ASN   A CB  
530  C  CB  B ASN   A 62  ? 0.1685 0.2550 0.1937 -0.0430 -0.0222 0.0209  62  ASN   A CB  
531  C  CG  A ASN   A 62  ? 0.2629 0.2578 0.1517 -0.0297 -0.0568 -0.0006 62  ASN   A CG  
532  C  CG  B ASN   A 62  ? 0.1610 0.2433 0.1790 -0.0377 -0.0184 0.0172  62  ASN   A CG  
533  O  OD1 A ASN   A 62  ? 0.2155 0.2509 0.1669 -0.0209 -0.0615 0.0026  62  ASN   A OD1 
534  O  OD1 B ASN   A 62  ? 0.1674 0.2532 0.1628 -0.0286 -0.0111 0.0467  62  ASN   A OD1 
535  N  ND2 A ASN   A 62  ? 0.3189 0.2686 0.1983 -0.0419 -0.0667 -0.0345 62  ASN   A ND2 
536  N  ND2 B ASN   A 62  ? 0.1865 0.2381 0.1868 -0.0219 -0.0082 0.0270  62  ASN   A ND2 
537  N  N   . GLY   A 63  ? 0.1374 0.2445 0.1802 -0.0298 -0.0232 0.0530  63  GLY   A N   
538  C  CA  . GLY   A 63  ? 0.1467 0.2428 0.1994 -0.0209 -0.0276 0.0196  63  GLY   A CA  
539  C  C   . GLY   A 63  ? 0.1410 0.2326 0.1755 -0.0130 -0.0288 0.0034  63  GLY   A C   
540  O  O   . GLY   A 63  ? 0.1911 0.2550 0.1924 0.0187  -0.0239 -0.0114 63  GLY   A O   
541  N  N   A HIS   A 64  ? 0.1255 0.2203 0.1390 -0.0137 -0.0351 0.0183  64  HIS   A N   
542  N  N   B HIS   A 64  ? 0.1342 0.2677 0.1857 -0.0136 -0.0389 0.0150  64  HIS   A N   
543  C  CA  A HIS   A 64  ? 0.1243 0.1992 0.1338 -0.0095 -0.0205 0.0128  64  HIS   A CA  
544  C  CA  B HIS   A 64  ? 0.1643 0.2718 0.2151 -0.0226 -0.0231 0.0257  64  HIS   A CA  
545  C  C   A HIS   A 64  ? 0.1201 0.1962 0.1283 -0.0166 -0.0230 0.0035  64  HIS   A C   
546  C  C   B HIS   A 64  ? 0.1549 0.2485 0.2023 -0.0180 -0.0090 0.0259  64  HIS   A C   
547  O  O   A HIS   A 64  ? 0.1282 0.1990 0.1273 -0.0184 -0.0138 0.0010  64  HIS   A O   
548  O  O   B HIS   A 64  ? 0.1603 0.2588 0.2196 -0.0034 -0.0140 0.0472  64  HIS   A O   
549  C  CB  A HIS   A 64  ? 0.1163 0.2082 0.1230 -0.0078 -0.0238 0.0132  64  HIS   A CB  
550  C  CB  B HIS   A 64  ? 0.1778 0.3018 0.2404 -0.0403 -0.0296 0.0189  64  HIS   A CB  
551  C  CG  A HIS   A 64  ? 0.1302 0.2455 0.1161 -0.0250 -0.0240 -0.0060 64  HIS   A CG  
552  C  CG  B HIS   A 64  ? 0.2463 0.3360 0.2933 -0.0380 -0.0390 0.0129  64  HIS   A CG  
553  N  ND1 A HIS   A 64  ? 0.1075 0.2618 0.1321 -0.0300 -0.0090 -0.0245 64  HIS   A ND1 
554  N  ND1 B HIS   A 64  ? 0.2574 0.3680 0.3590 -0.0957 -0.0553 0.0124  64  HIS   A ND1 
555  C  CD2 A HIS   A 64  ? 0.1208 0.2690 0.1464 -0.0381 -0.0202 -0.0032 64  HIS   A CD2 
556  C  CD2 B HIS   A 64  ? 0.2431 0.3802 0.2801 -0.0476 -0.0462 0.0025  64  HIS   A CD2 
557  C  CE1 A HIS   A 64  ? 0.1311 0.2699 0.1427 -0.0424 -0.0055 -0.0157 64  HIS   A CE1 
558  C  CE1 B HIS   A 64  ? 0.2590 0.3869 0.3401 -0.0671 -0.0550 -0.0040 64  HIS   A CE1 
559  N  NE2 A HIS   A 64  ? 0.1215 0.2645 0.1616 -0.0590 -0.0133 -0.0288 64  HIS   A NE2 
560  N  NE2 B HIS   A 64  ? 0.2722 0.3807 0.3082 -0.0515 -0.0710 -0.0007 64  HIS   A NE2 
561  N  N   A SER   A 65  ? 0.1188 0.1944 0.1338 -0.0222 -0.0213 0.0063  65  SER   A N   
562  N  N   B SER   A 65  ? 0.1525 0.2376 0.1921 -0.0230 -0.0183 0.0233  65  SER   A N   
563  C  CA  A SER   A 65  ? 0.1263 0.1839 0.1407 -0.0229 -0.0175 0.0205  65  SER   A CA  
564  C  CA  B SER   A 65  ? 0.1551 0.2168 0.1829 -0.0188 -0.0222 0.0254  65  SER   A CA  
565  C  C   A SER   A 65  ? 0.1385 0.1910 0.1402 -0.0072 -0.0151 0.0150  65  SER   A C   
566  C  C   B SER   A 65  ? 0.1485 0.2146 0.1712 0.0025  -0.0134 0.0125  65  SER   A C   
567  O  O   A SER   A 65  ? 0.1514 0.1945 0.1357 -0.0230 -0.0277 0.0122  65  SER   A O   
568  O  O   B SER   A 65  ? 0.1638 0.2151 0.1649 0.0198  -0.0150 0.0036  65  SER   A O   
569  C  CB  A SER   A 65  ? 0.1273 0.1740 0.1497 -0.0129 -0.0211 0.0161  65  SER   A CB  
570  C  CB  B SER   A 65  ? 0.1509 0.2205 0.1962 -0.0161 -0.0167 0.0238  65  SER   A CB  
571  O  OG  A SER   A 65  ? 0.1304 0.2120 0.1508 -0.0029 -0.0125 0.0410  65  SER   A OG  
572  O  OG  B SER   A 65  ? 0.1741 0.2288 0.2048 -0.0077 -0.0046 0.0202  65  SER   A OG  
573  N  N   . PHE   A 66  ? 0.1445 0.2033 0.1526 -0.0073 -0.0269 0.0146  66  PHE   A N   
574  C  CA  . PHE   A 66  ? 0.1398 0.2187 0.1376 0.0133  -0.0206 0.0124  66  PHE   A CA  
575  C  C   . PHE   A 66  ? 0.1406 0.2119 0.1290 0.0052  -0.0159 0.0135  66  PHE   A C   
576  O  O   . PHE   A 66  ? 0.1590 0.2053 0.1265 -0.0058 -0.0167 0.0069  66  PHE   A O   
577  C  CB  . PHE   A 66  ? 0.1626 0.2140 0.1519 0.0222  -0.0147 0.0091  66  PHE   A CB  
578  C  CG  . PHE   A 66  ? 0.1489 0.2222 0.1464 0.0108  -0.0465 0.0022  66  PHE   A CG  
579  C  CD1 . PHE   A 66  ? 0.1564 0.2410 0.1648 0.0136  -0.0601 -0.0129 66  PHE   A CD1 
580  C  CD2 . PHE   A 66  ? 0.1482 0.2420 0.1745 0.0139  -0.0621 -0.0088 66  PHE   A CD2 
581  C  CE1 . PHE   A 66  ? 0.1413 0.2348 0.1895 0.0087  -0.0713 -0.0172 66  PHE   A CE1 
582  C  CE2 . PHE   A 66  ? 0.1776 0.2153 0.2039 -0.0041 -0.0683 -0.0138 66  PHE   A CE2 
583  C  CZ  . PHE   A 66  ? 0.1542 0.2144 0.1952 -0.0150 -0.0500 -0.0300 66  PHE   A CZ  
584  N  N   . LYS   A 67  ? 0.1569 0.2124 0.1392 0.0090  -0.0304 0.0251  67  LYS   A N   
585  C  CA  . LYS   A 67  ? 0.1549 0.2052 0.1483 0.0249  -0.0429 0.0137  67  LYS   A CA  
586  C  C   . LYS   A 67  ? 0.1481 0.2130 0.1249 0.0096  -0.0240 0.0266  67  LYS   A C   
587  O  O   . LYS   A 67  ? 0.1536 0.2310 0.1347 0.0245  -0.0212 0.0358  67  LYS   A O   
588  C  CB  . LYS   A 67  ? 0.1942 0.2505 0.2087 0.0252  -0.0994 0.0088  67  LYS   A CB  
589  C  CG  . LYS   A 67  ? 0.2287 0.3068 0.2373 -0.0013 -0.0826 -0.0099 67  LYS   A CG  
590  C  CD  . LYS   A 67  ? 0.2763 0.3288 0.3309 -0.0209 -0.0636 -0.0558 67  LYS   A CD  
591  C  CE  . LYS   A 67  ? 0.3400 0.4363 0.3861 -0.0431 -0.0384 -0.0906 67  LYS   A CE  
592  N  NZ  . LYS   A 67  ? 0.4195 0.4733 0.4902 -0.0661 -0.0324 -0.1399 67  LYS   A NZ  
593  N  N   . VAL   A 68  ? 0.1485 0.1818 0.1078 -0.0090 -0.0234 0.0285  68  VAL   A N   
594  C  CA  . VAL   A 68  ? 0.1392 0.1662 0.1133 -0.0050 -0.0244 0.0276  68  VAL   A CA  
595  C  C   . VAL   A 68  ? 0.1273 0.1804 0.1365 -0.0119 -0.0259 0.0298  68  VAL   A C   
596  O  O   . VAL   A 68  ? 0.1400 0.1820 0.1246 -0.0077 -0.0315 0.0321  68  VAL   A O   
597  C  CB  . VAL   A 68  ? 0.1456 0.1792 0.1242 -0.0130 -0.0284 0.0286  68  VAL   A CB  
598  C  CG1 . VAL   A 68  ? 0.1472 0.1917 0.1261 -0.0049 -0.0460 0.0219  68  VAL   A CG1 
599  C  CG2 . VAL   A 68  ? 0.1408 0.1972 0.1610 -0.0085 -0.0332 0.0153  68  VAL   A CG2 
600  N  N   A ASN   A 69  ? 0.1395 0.1763 0.1251 0.0105  -0.0345 0.0300  69  ASN   A N   
601  N  N   B ASN   A 69  ? 0.1530 0.1822 0.1360 0.0126  -0.0304 0.0319  69  ASN   A N   
602  C  CA  A ASN   A 69  ? 0.1247 0.1790 0.1275 -0.0016 -0.0498 0.0292  69  ASN   A CA  
603  C  CA  B ASN   A 69  ? 0.1552 0.1949 0.1480 0.0062  -0.0404 0.0250  69  ASN   A CA  
604  C  C   A ASN   A 69  ? 0.1272 0.1777 0.1461 0.0016  -0.0528 0.0220  69  ASN   A C   
605  C  C   B ASN   A 69  ? 0.1473 0.1800 0.1562 -0.0008 -0.0462 0.0200  69  ASN   A C   
606  O  O   A ASN   A 69  ? 0.1163 0.1745 0.1608 0.0111  -0.0648 0.0222  69  ASN   A O   
607  O  O   B ASN   A 69  ? 0.1468 0.1744 0.1583 -0.0003 -0.0495 0.0249  69  ASN   A O   
608  C  CB  A ASN   A 69  ? 0.1293 0.1850 0.1728 -0.0151 -0.0523 0.0293  69  ASN   A CB  
609  C  CB  B ASN   A 69  ? 0.1737 0.2089 0.2115 -0.0076 -0.0372 0.0151  69  ASN   A CB  
610  C  CG  A ASN   A 69  ? 0.1460 0.2101 0.1855 -0.0203 -0.0628 0.0118  69  ASN   A CG  
611  C  CG  B ASN   A 69  ? 0.2372 0.2399 0.2324 -0.0060 -0.0245 0.0241  69  ASN   A CG  
612  O  OD1 A ASN   A 69  ? 0.1820 0.2376 0.2028 -0.0312 -0.0599 0.0023  69  ASN   A OD1 
613  O  OD1 B ASN   A 69  ? 0.2370 0.2183 0.2465 -0.0042 -0.0279 0.0213  69  ASN   A OD1 
614  N  ND2 A ASN   A 69  ? 0.1330 0.2303 0.2102 -0.0380 -0.0611 0.0150  69  ASN   A ND2 
615  N  ND2 B ASN   A 69  ? 0.3002 0.2666 0.2757 0.0098  -0.0384 0.0407  69  ASN   A ND2 
616  N  N   . PHE   A 70  ? 0.1230 0.1727 0.1547 -0.0069 -0.0528 0.0194  70  PHE   A N   
617  C  CA  . PHE   A 70  ? 0.1380 0.1674 0.1547 -0.0070 -0.0547 0.0125  70  PHE   A CA  
618  C  C   . PHE   A 70  ? 0.1401 0.1603 0.1936 -0.0152 -0.0485 0.0229  70  PHE   A C   
619  O  O   . PHE   A 70  ? 0.1597 0.1930 0.2182 -0.0246 -0.0773 0.0205  70  PHE   A O   
620  C  CB  . PHE   A 70  ? 0.1272 0.1758 0.1599 -0.0046 -0.0457 0.0166  70  PHE   A CB  
621  C  CG  . PHE   A 70  ? 0.1304 0.1778 0.1571 -0.0082 -0.0339 0.0210  70  PHE   A CG  
622  C  CD1 . PHE   A 70  ? 0.1322 0.1811 0.1783 -0.0062 -0.0307 0.0380  70  PHE   A CD1 
623  C  CD2 . PHE   A 70  ? 0.1342 0.1841 0.1654 -0.0100 -0.0387 0.0321  70  PHE   A CD2 
624  C  CE1 . PHE   A 70  ? 0.1573 0.1667 0.1806 0.0017  -0.0094 0.0422  70  PHE   A CE1 
625  C  CE2 . PHE   A 70  ? 0.1370 0.1875 0.1615 -0.0203 -0.0465 0.0229  70  PHE   A CE2 
626  C  CZ  . PHE   A 70  ? 0.1659 0.1766 0.1662 -0.0141 -0.0130 0.0304  70  PHE   A CZ  
627  N  N   . ASP   A 71  ? 0.1495 0.1712 0.2160 -0.0025 -0.0648 0.0250  71  ASP   A N   
628  C  CA  . ASP   A 71  ? 0.1753 0.1733 0.2515 -0.0014 -0.0609 0.0307  71  ASP   A CA  
629  C  C   . ASP   A 71  ? 0.1844 0.1614 0.2544 0.0035  -0.0512 0.0037  71  ASP   A C   
630  O  O   . ASP   A 71  ? 0.2140 0.2279 0.3229 -0.0293 -0.0014 -0.0312 71  ASP   A O   
631  C  CB  . ASP   A 71  ? 0.2051 0.1779 0.3066 0.0125  -0.1046 0.0463  71  ASP   A CB  
632  C  CG  . ASP   A 71  ? 0.2526 0.1925 0.3319 0.0226  -0.1707 0.0428  71  ASP   A CG  
633  O  OD1 . ASP   A 71  ? 0.2676 0.1833 0.3702 0.0009  -0.1555 0.0393  71  ASP   A OD1 
634  O  OD2 . ASP   A 71  ? 0.2891 0.2154 0.5291 0.0130  -0.2056 0.0368  71  ASP   A OD2 
635  N  N   . ASP   A 72  ? 0.2099 0.1524 0.2410 -0.0299 -0.0301 0.0050  72  ASP   A N   
636  C  CA  . ASP   A 72  ? 0.2380 0.1610 0.2261 -0.0182 -0.0348 0.0103  72  ASP   A CA  
637  C  C   . ASP   A 72  ? 0.2627 0.1752 0.2658 -0.0279 -0.0466 0.0035  72  ASP   A C   
638  O  O   . ASP   A 72  ? 0.3294 0.1816 0.2708 -0.0164 -0.0548 -0.0019 72  ASP   A O   
639  C  CB  . ASP   A 72  ? 0.2556 0.1692 0.2339 -0.0192 -0.0610 0.0189  72  ASP   A CB  
640  C  CG  . ASP   A 72  ? 0.2541 0.1860 0.2266 -0.0368 -0.0790 0.0220  72  ASP   A CG  
641  O  OD1 . ASP   A 72  ? 0.2491 0.2267 0.2207 -0.0562 -0.0867 0.0348  72  ASP   A OD1 
642  O  OD2 . ASP   A 72  ? 0.2811 0.2165 0.1998 -0.0156 -0.0877 0.0294  72  ASP   A OD2 
643  N  N   . SER   A 73  ? 0.2979 0.1830 0.2608 -0.0426 -0.0329 0.0131  73  SER   A N   
644  C  CA  . SER   A 73  ? 0.3232 0.1925 0.2918 -0.0388 -0.0402 -0.0042 73  SER   A CA  
645  C  C   . SER   A 73  ? 0.3677 0.1950 0.2912 -0.0149 -0.0592 -0.0312 73  SER   A C   
646  O  O   . SER   A 73  ? 0.4233 0.1868 0.3217 -0.0125 -0.0610 -0.0277 73  SER   A O   
647  C  CB  . SER   A 73  ? 0.3653 0.2132 0.3101 -0.0036 -0.0375 0.0056  73  SER   A CB  
648  O  OG  . SER   A 73  ? 0.3463 0.2379 0.3100 0.0201  -0.0384 0.0470  73  SER   A OG  
649  N  N   . GLN   A 74  ? 0.3789 0.2059 0.3351 -0.0166 -0.0602 -0.0215 74  GLN   A N   
650  C  CA  . GLN   A 74  ? 0.3799 0.2851 0.3415 0.0043  -0.0803 -0.0344 74  GLN   A CA  
651  C  C   . GLN   A 74  ? 0.3415 0.2858 0.3172 -0.0316 -0.1032 -0.0651 74  GLN   A C   
652  O  O   . GLN   A 74  ? 0.2858 0.2364 0.3167 -0.0292 -0.0966 -0.0327 74  GLN   A O   
653  C  CB  . GLN   A 74  ? 0.4296 0.4058 0.4379 0.0367  -0.0585 -0.0228 74  GLN   A CB  
654  C  CG  . GLN   A 74  ? 0.4370 0.3986 0.4577 0.0511  -0.0793 0.0124  74  GLN   A CG  
655  C  CD  . GLN   A 74  ? 0.5185 0.4275 0.4798 0.0511  -0.1222 0.0587  74  GLN   A CD  
656  O  OE1 . GLN   A 74  ? 0.5021 0.4029 0.5193 -0.0619 -0.1525 0.1142  74  GLN   A OE1 
657  N  NE2 . GLN   A 74  ? 0.5017 0.3765 0.4484 0.0703  -0.0743 0.0572  74  GLN   A NE2 
658  N  N   A ASP   A 75  ? 0.3777 0.2902 0.3416 -0.0286 -0.1109 -0.0654 75  ASP   A N   
659  N  N   B ASP   A 75  ? 0.3803 0.2981 0.3371 -0.0241 -0.0986 -0.0571 75  ASP   A N   
660  C  CA  A ASP   A 75  ? 0.3504 0.3150 0.3561 -0.0019 -0.1279 -0.0351 75  ASP   A CA  
661  C  CA  B ASP   A 75  ? 0.3547 0.3033 0.3505 -0.0380 -0.1224 -0.0478 75  ASP   A CA  
662  C  C   A ASP   A 75  ? 0.2781 0.3001 0.3507 0.0212  -0.1320 -0.0183 75  ASP   A C   
663  C  C   B ASP   A 75  ? 0.3076 0.2462 0.3131 -0.0172 -0.1292 -0.0057 75  ASP   A C   
664  O  O   A ASP   A 75  ? 0.3161 0.3407 0.4045 0.0383  -0.0996 0.0023  75  ASP   A O   
665  O  O   B ASP   A 75  ? 0.3573 0.2354 0.3314 0.0020  -0.1618 -0.0037 75  ASP   A O   
666  C  CB  A ASP   A 75  ? 0.3621 0.2925 0.3237 0.0471  -0.1547 -0.0154 75  ASP   A CB  
667  C  CB  B ASP   A 75  ? 0.3897 0.3493 0.3843 -0.0046 -0.1120 -0.0416 75  ASP   A CB  
668  C  CG  A ASP   A 75  ? 0.3359 0.3092 0.3084 0.0166  -0.1169 -0.0327 75  ASP   A CG  
669  C  CG  B ASP   A 75  ? 0.3568 0.3344 0.3720 -0.0059 -0.0896 -0.0266 75  ASP   A CG  
670  O  OD1 A ASP   A 75  ? 0.3045 0.3467 0.2354 0.0388  -0.1307 -0.0138 75  ASP   A OD1 
671  O  OD1 B ASP   A 75  ? 0.3314 0.3106 0.3174 -0.0135 -0.0660 0.0376  75  ASP   A OD1 
672  O  OD2 A ASP   A 75  ? 0.4138 0.3201 0.2904 0.0089  -0.0843 0.0104  75  ASP   A OD2 
673  O  OD2 B ASP   A 75  ? 0.4554 0.3625 0.4013 0.0398  -0.0130 -0.0182 75  ASP   A OD2 
674  N  N   A LYS   A 76  ? 0.2630 0.2897 0.2914 0.0320  -0.1452 0.0257  76  LYS   A N   
675  N  N   B LYS   A 76  ? 0.2692 0.2467 0.2559 0.0074  -0.1274 0.0097  76  LYS   A N   
676  C  CA  A LYS   A 76  ? 0.2503 0.2617 0.3036 0.0259  -0.1074 0.0083  76  LYS   A CA  
677  C  CA  B LYS   A 76  ? 0.2858 0.2403 0.3221 -0.0197 -0.0975 0.0028  76  LYS   A CA  
678  C  C   A LYS   A 76  ? 0.2321 0.2868 0.2707 0.0074  -0.1062 0.0243  76  LYS   A C   
679  C  C   B LYS   A 76  ? 0.2876 0.2810 0.3249 0.0057  -0.0810 0.0197  76  LYS   A C   
680  O  O   A LYS   A 76  ? 0.1802 0.3371 0.3074 -0.0014 -0.1020 -0.0002 76  LYS   A O   
681  O  O   B LYS   A 76  ? 0.3490 0.3089 0.3318 -0.0052 -0.0636 0.0165  76  LYS   A O   
682  C  CB  A LYS   A 76  ? 0.2572 0.2943 0.2959 0.0500  -0.1225 0.0230  76  LYS   A CB  
683  C  CB  B LYS   A 76  ? 0.2878 0.2568 0.3234 -0.0420 -0.1127 -0.0028 76  LYS   A CB  
684  C  CG  A LYS   A 76  ? 0.2972 0.2823 0.3358 0.0516  -0.0929 0.0133  76  LYS   A CG  
685  C  CG  B LYS   A 76  ? 0.3074 0.2705 0.3388 -0.0428 -0.1046 -0.0038 76  LYS   A CG  
686  C  CD  A LYS   A 76  ? 0.2768 0.3379 0.3368 0.0655  -0.1006 0.0119  76  LYS   A CD  
687  C  CD  B LYS   A 76  ? 0.3133 0.2732 0.3127 -0.0633 -0.1235 -0.0340 76  LYS   A CD  
688  C  CE  A LYS   A 76  ? 0.2728 0.3612 0.3618 0.1080  -0.1145 0.0054  76  LYS   A CE  
689  C  CE  B LYS   A 76  ? 0.3069 0.2940 0.3168 -0.0628 -0.0956 -0.0286 76  LYS   A CE  
690  N  NZ  A LYS   A 76  ? 0.3028 0.3822 0.3858 0.1028  -0.1079 -0.0069 76  LYS   A NZ  
691  N  NZ  B LYS   A 76  ? 0.3323 0.2631 0.2875 -0.0604 -0.0982 -0.0353 76  LYS   A NZ  
692  N  N   . ALA   A 77  ? 0.2318 0.3238 0.3211 0.0221  -0.1110 0.0503  77  ALA   A N   
693  C  CA  . ALA   A 77  ? 0.1987 0.2570 0.2771 0.0064  -0.0904 0.0009  77  ALA   A CA  
694  C  C   . ALA   A 77  ? 0.1629 0.2369 0.2809 0.0167  -0.0835 0.0167  77  ALA   A C   
695  O  O   . ALA   A 77  ? 0.1552 0.3172 0.3627 0.0338  -0.0646 -0.0450 77  ALA   A O   
696  C  CB  . ALA   A 77  ? 0.2128 0.3465 0.2600 0.0454  -0.0789 0.0082  77  ALA   A CB  
697  N  N   . VAL   A 78  ? 0.1625 0.2357 0.2628 -0.0033 -0.1036 0.0054  78  VAL   A N   
698  C  CA  . VAL   A 78  ? 0.1886 0.2325 0.2538 -0.0039 -0.0939 0.0026  78  VAL   A CA  
699  C  C   . VAL   A 78  ? 0.1635 0.2285 0.2383 -0.0244 -0.0916 -0.0070 78  VAL   A C   
700  O  O   . VAL   A 78  ? 0.1670 0.2406 0.3122 -0.0250 -0.1340 0.0187  78  VAL   A O   
701  C  CB  . VAL   A 78  ? 0.2570 0.2656 0.2602 0.0385  -0.0958 0.0065  78  VAL   A CB  
702  C  CG1 . VAL   A 78  ? 0.2575 0.2607 0.3156 0.0258  -0.0578 0.0319  78  VAL   A CG1 
703  C  CG2 . VAL   A 78  ? 0.2816 0.2634 0.2623 0.0570  -0.0872 -0.0023 78  VAL   A CG2 
704  N  N   . LEU   A 79  ? 0.1408 0.1877 0.2216 -0.0159 -0.0665 -0.0014 79  LEU   A N   
705  C  CA  . LEU   A 79  ? 0.1302 0.1918 0.2441 -0.0080 -0.0549 -0.0076 79  LEU   A CA  
706  C  C   . LEU   A 79  ? 0.1552 0.2005 0.2328 -0.0040 -0.0560 -0.0026 79  LEU   A C   
707  O  O   . LEU   A 79  ? 0.1870 0.2135 0.2340 -0.0309 -0.0396 -0.0236 79  LEU   A O   
708  C  CB  . LEU   A 79  ? 0.1081 0.2042 0.2496 -0.0138 -0.0592 0.0120  79  LEU   A CB  
709  C  CG  . LEU   A 79  ? 0.1575 0.2221 0.2684 0.0139  -0.0213 0.0100  79  LEU   A CG  
710  C  CD1 . LEU   A 79  ? 0.1700 0.2377 0.3311 0.0005  0.0120  0.0154  79  LEU   A CD1 
711  C  CD2 . LEU   A 79  ? 0.1511 0.2231 0.2360 0.0374  -0.0055 0.0340  79  LEU   A CD2 
712  N  N   A LYS   A 80  ? 0.1471 0.2154 0.2456 -0.0226 -0.0586 -0.0218 80  LYS   A N   
713  N  N   B LYS   A 80  ? 0.1418 0.2270 0.2551 -0.0160 -0.0541 -0.0139 80  LYS   A N   
714  C  CA  A LYS   A 80  ? 0.1687 0.2199 0.2437 -0.0169 -0.0525 -0.0301 80  LYS   A CA  
715  C  CA  B LYS   A 80  ? 0.1620 0.2372 0.2514 -0.0010 -0.0446 -0.0190 80  LYS   A CA  
716  C  C   A LYS   A 80  ? 0.1661 0.2337 0.2443 -0.0088 -0.0385 -0.0282 80  LYS   A C   
717  C  C   B LYS   A 80  ? 0.1605 0.2375 0.2472 -0.0020 -0.0363 -0.0238 80  LYS   A C   
718  O  O   A LYS   A 80  ? 0.1612 0.2337 0.2485 -0.0198 -0.0525 -0.0090 80  LYS   A O   
719  O  O   B LYS   A 80  ? 0.1564 0.2385 0.2542 -0.0215 -0.0527 -0.0026 80  LYS   A O   
720  C  CB  A LYS   A 80  ? 0.1699 0.2199 0.2766 -0.0201 -0.0464 -0.0238 80  LYS   A CB  
721  C  CB  B LYS   A 80  ? 0.1755 0.2550 0.2824 0.0056  -0.0454 -0.0010 80  LYS   A CB  
722  C  CG  A LYS   A 80  ? 0.1752 0.2227 0.2803 0.0109  -0.0553 -0.0093 80  LYS   A CG  
723  C  CG  B LYS   A 80  ? 0.1724 0.2378 0.3090 0.0329  -0.0470 0.0246  80  LYS   A CG  
724  N  N   . GLY   A 81  ? 0.1817 0.2434 0.2388 0.0038  -0.0168 -0.0202 81  GLY   A N   
725  C  CA  . GLY   A 81  ? 0.1711 0.2470 0.2739 0.0269  0.0141  -0.0010 81  GLY   A CA  
726  C  C   . GLY   A 81  ? 0.1557 0.2331 0.2771 0.0217  0.0191  0.0014  81  GLY   A C   
727  O  O   . GLY   A 81  ? 0.1405 0.2512 0.2328 0.0053  0.0014  -0.0327 81  GLY   A O   
728  N  N   . GLY   A 82  ? 0.1737 0.2524 0.3572 0.0341  0.0101  0.0381  82  GLY   A N   
729  C  CA  . GLY   A 82  ? 0.1949 0.2591 0.3921 0.0308  0.0307  0.0524  82  GLY   A CA  
730  C  C   . GLY   A 82  ? 0.2007 0.2966 0.3246 0.0711  0.0388  0.0183  82  GLY   A C   
731  O  O   . GLY   A 82  ? 0.2500 0.3744 0.3203 0.1258  0.0766  0.0311  82  GLY   A O   
732  N  N   . PRO   A 83  ? 0.1631 0.2471 0.2795 0.0365  0.0238  -0.0086 83  PRO   A N   
733  C  CA  . PRO   A 83  ? 0.2062 0.2438 0.2397 0.0480  0.0019  -0.0039 83  PRO   A CA  
734  C  C   . PRO   A 83  ? 0.2043 0.2397 0.2027 0.0232  -0.0191 -0.0170 83  PRO   A C   
735  O  O   . PRO   A 83  ? 0.2729 0.3161 0.2884 0.0075  -0.1095 -0.0028 83  PRO   A O   
736  C  CB  . PRO   A 83  ? 0.1859 0.2401 0.2220 0.0535  -0.0170 0.0162  83  PRO   A CB  
737  C  CG  . PRO   A 83  ? 0.1548 0.2470 0.2246 0.0421  -0.0132 0.0087  83  PRO   A CG  
738  C  CD  . PRO   A 83  ? 0.1499 0.2341 0.2573 0.0098  0.0000  -0.0081 83  PRO   A CD  
739  N  N   . LEU   A 84  ? 0.1778 0.2319 0.1789 0.0290  -0.0020 -0.0166 84  LEU   A N   
740  C  CA  . LEU   A 84  ? 0.1378 0.2092 0.2153 0.0230  0.0008  -0.0305 84  LEU   A CA  
741  C  C   . LEU   A 84  ? 0.1773 0.2466 0.2356 0.0367  -0.0007 -0.0409 84  LEU   A C   
742  O  O   . LEU   A 84  ? 0.1872 0.2714 0.3195 0.0354  0.0236  -0.0679 84  LEU   A O   
743  C  CB  . LEU   A 84  ? 0.1469 0.1958 0.2107 0.0255  0.0054  -0.0352 84  LEU   A CB  
744  C  CG  . LEU   A 84  ? 0.1339 0.2001 0.1899 0.0069  0.0010  -0.0261 84  LEU   A CG  
745  C  CD1 . LEU   A 84  ? 0.1760 0.1976 0.1954 0.0114  -0.0170 -0.0301 84  LEU   A CD1 
746  C  CD2 . LEU   A 84  ? 0.1208 0.2198 0.1994 -0.0112 0.0057  -0.0305 84  LEU   A CD2 
747  N  N   . ASP   A 85  ? 0.1631 0.2289 0.2708 0.0310  0.0066  -0.0573 85  ASP   A N   
748  C  CA  . ASP   A 85  ? 0.2093 0.2480 0.3318 0.0182  0.0303  -0.0831 85  ASP   A CA  
749  C  C   . ASP   A 85  ? 0.2481 0.2096 0.4323 0.0175  0.0252  -0.0350 85  ASP   A C   
750  O  O   . ASP   A 85  ? 0.2799 0.3572 0.4653 0.0470  0.0557  -0.0815 85  ASP   A O   
751  C  CB  . ASP   A 85  ? 0.3389 0.2762 0.3646 0.0387  -0.0145 -0.1146 85  ASP   A CB  
752  C  CG  . ASP   A 85  ? 0.4293 0.4283 0.4840 0.0127  -0.0616 -0.0802 85  ASP   A CG  
753  O  OD1 . ASP   A 85  ? 0.4735 0.5913 0.5606 -0.0085 -0.0606 -0.1429 85  ASP   A OD1 
754  O  OD2 . ASP   A 85  ? 0.5435 0.6134 0.5553 0.0384  -0.1596 -0.1056 85  ASP   A OD2 
755  N  N   . GLY   A 86  ? 0.2723 0.2852 0.4120 -0.0677 -0.0237 -0.0502 86  GLY   A N   
756  C  CA  . GLY   A 86  ? 0.3250 0.2597 0.3878 -0.0704 -0.0174 -0.0528 86  GLY   A CA  
757  C  C   . GLY   A 86  ? 0.2647 0.2607 0.3381 -0.0766 -0.0540 -0.0355 86  GLY   A C   
758  O  O   . GLY   A 86  ? 0.3660 0.3057 0.3314 -0.1248 -0.0214 -0.0178 86  GLY   A O   
759  N  N   . THR   A 87  ? 0.1932 0.2182 0.3161 -0.0088 -0.0207 -0.0465 87  THR   A N   
760  C  CA  . THR   A 87  ? 0.1717 0.2116 0.3107 0.0235  -0.0391 -0.0473 87  THR   A CA  
761  C  C   . THR   A 87  ? 0.1382 0.1955 0.2783 0.0099  -0.0558 -0.0389 87  THR   A C   
762  O  O   . THR   A 87  ? 0.1672 0.1805 0.2935 -0.0064 -0.0467 -0.0205 87  THR   A O   
763  C  CB  . THR   A 87  ? 0.1841 0.3203 0.3253 0.0955  -0.0650 -0.0443 87  THR   A CB  
764  O  OG1 . THR   A 87  ? 0.2664 0.3814 0.4125 0.1144  -0.0384 -0.0886 87  THR   A OG1 
765  C  CG2 . THR   A 87  ? 0.2018 0.2961 0.3452 0.0892  -0.0705 -0.0253 87  THR   A CG2 
766  N  N   . TYR   A 88  ? 0.1170 0.1925 0.2646 0.0032  -0.0585 -0.0290 88  TYR   A N   
767  C  CA  . TYR   A 88  ? 0.1190 0.1710 0.2425 -0.0061 -0.0531 -0.0298 88  TYR   A CA  
768  C  C   . TYR   A 88  ? 0.1315 0.1742 0.2475 0.0110  -0.0665 -0.0171 88  TYR   A C   
769  O  O   . TYR   A 88  ? 0.1660 0.2648 0.2955 -0.0615 -0.0951 0.0216  88  TYR   A O   
770  C  CB  . TYR   A 88  ? 0.1276 0.1787 0.2373 0.0203  -0.0637 -0.0377 88  TYR   A CB  
771  C  CG  . TYR   A 88  ? 0.1220 0.1871 0.2016 0.0111  -0.0338 -0.0327 88  TYR   A CG  
772  C  CD1 . TYR   A 88  ? 0.1255 0.1936 0.2059 0.0069  -0.0335 -0.0503 88  TYR   A CD1 
773  C  CD2 . TYR   A 88  ? 0.1247 0.1818 0.1916 0.0182  -0.0247 -0.0314 88  TYR   A CD2 
774  C  CE1 . TYR   A 88  ? 0.1444 0.1982 0.1890 0.0356  -0.0196 -0.0520 88  TYR   A CE1 
775  C  CE2 . TYR   A 88  ? 0.1231 0.1824 0.1908 -0.0092 -0.0296 -0.0201 88  TYR   A CE2 
776  C  CZ  . TYR   A 88  ? 0.1369 0.1820 0.1911 0.0030  -0.0237 -0.0423 88  TYR   A CZ  
777  O  OH  . TYR   A 88  ? 0.1482 0.1964 0.1834 -0.0109 -0.0236 -0.0235 88  TYR   A OH  
778  N  N   A ARG   A 89  ? 0.1109 0.1654 0.2385 0.0211  -0.0579 -0.0239 89  ARG   A N   
779  N  N   B ARG   A 89  ? 0.1192 0.1693 0.2207 0.0048  -0.0642 -0.0109 89  ARG   A N   
780  C  CA  A ARG   A 89  ? 0.1357 0.1789 0.2387 0.0183  -0.0698 -0.0080 89  ARG   A CA  
781  C  CA  B ARG   A 89  ? 0.1459 0.1759 0.2059 0.0068  -0.0646 0.0101  89  ARG   A CA  
782  C  C   A ARG   A 89  ? 0.1209 0.1587 0.1954 0.0074  -0.0589 0.0060  89  ARG   A C   
783  C  C   B ARG   A 89  ? 0.1311 0.1543 0.1820 0.0035  -0.0589 0.0189  89  ARG   A C   
784  O  O   A ARG   A 89  ? 0.1128 0.1723 0.1600 -0.0010 -0.0458 -0.0025 89  ARG   A O   
785  O  O   B ARG   A 89  ? 0.1306 0.1814 0.1655 0.0023  -0.0363 0.0154  89  ARG   A O   
786  C  CB  A ARG   A 89  ? 0.1643 0.1853 0.2689 0.0293  -0.0683 -0.0006 89  ARG   A CB  
787  C  CB  B ARG   A 89  ? 0.1753 0.1903 0.2043 0.0061  -0.0621 0.0237  89  ARG   A CB  
788  C  CG  A ARG   A 89  ? 0.1955 0.1723 0.2773 0.0289  -0.0915 -0.0062 89  ARG   A CG  
789  C  CG  B ARG   A 89  ? 0.2161 0.1909 0.1661 -0.0050 -0.0541 0.0132  89  ARG   A CG  
790  C  CD  A ARG   A 89  ? 0.1955 0.2086 0.2808 0.0275  -0.1101 0.0052  89  ARG   A CD  
791  C  CD  B ARG   A 89  ? 0.2322 0.1920 0.1692 0.0044  -0.0637 0.0229  89  ARG   A CD  
792  N  NE  A ARG   A 89  ? 0.2506 0.2237 0.2822 0.0320  -0.1174 -0.0247 89  ARG   A NE  
793  N  NE  B ARG   A 89  ? 0.2497 0.1978 0.1746 -0.0063 -0.0497 0.0309  89  ARG   A NE  
794  C  CZ  A ARG   A 89  ? 0.2621 0.2301 0.2886 0.0392  -0.1208 -0.0217 89  ARG   A CZ  
795  C  CZ  B ARG   A 89  ? 0.2849 0.2116 0.2117 0.0092  -0.0366 0.0342  89  ARG   A CZ  
796  N  NH1 A ARG   A 89  ? 0.2577 0.2163 0.2763 0.0374  -0.1223 -0.0426 89  ARG   A NH1 
797  N  NH1 B ARG   A 89  ? 0.2940 0.2267 0.1925 0.0033  -0.0179 0.0442  89  ARG   A NH1 
798  N  NH2 A ARG   A 89  ? 0.3239 0.2660 0.3443 0.0420  -0.0808 -0.0425 89  ARG   A NH2 
799  N  NH2 B ARG   A 89  ? 0.2925 0.1916 0.2163 0.0261  -0.0218 0.0382  89  ARG   A NH2 
800  N  N   . LEU   A 90  ? 0.1123 0.1694 0.1816 0.0058  -0.0505 0.0044  90  LEU   A N   
801  C  CA  . LEU   A 90  ? 0.1293 0.1425 0.1677 -0.0069 -0.0542 0.0230  90  LEU   A CA  
802  C  C   . LEU   A 90  ? 0.1399 0.1514 0.1535 -0.0130 -0.0475 0.0217  90  LEU   A C   
803  O  O   . LEU   A 90  ? 0.1459 0.1902 0.1850 -0.0107 -0.0618 0.0511  90  LEU   A O   
804  C  CB  . LEU   A 90  ? 0.1202 0.1544 0.1724 -0.0172 -0.0558 0.0184  90  LEU   A CB  
805  C  CG  . LEU   A 90  ? 0.1276 0.1691 0.1790 -0.0273 -0.0419 0.0051  90  LEU   A CG  
806  C  CD1 . LEU   A 90  ? 0.1422 0.1674 0.1753 -0.0126 -0.0384 -0.0056 90  LEU   A CD1 
807  C  CD2 . LEU   A 90  ? 0.1523 0.1851 0.1772 -0.0303 -0.0382 -0.0176 90  LEU   A CD2 
808  N  N   . THR   A 91  ? 0.1291 0.1557 0.1480 -0.0056 -0.0428 0.0192  91  THR   A N   
809  C  CA  . THR   A 91  ? 0.1411 0.1482 0.1342 -0.0072 -0.0455 0.0243  91  THR   A CA  
810  C  C   . THR   A 91  ? 0.1165 0.1501 0.1359 -0.0182 -0.0288 0.0289  91  THR   A C   
811  O  O   . THR   A 91  ? 0.1323 0.1592 0.1334 -0.0114 -0.0298 0.0216  91  THR   A O   
812  C  CB  . THR   A 91  ? 0.1693 0.1694 0.1535 -0.0304 -0.0374 0.0089  91  THR   A CB  
813  O  OG1 . THR   A 91  ? 0.2015 0.2532 0.1712 -0.0937 -0.0553 0.0325  91  THR   A OG1 
814  C  CG2 . THR   A 91  ? 0.1482 0.1628 0.1779 -0.0307 -0.0350 -0.0021 91  THR   A CG2 
815  N  N   . GLN   A 92  ? 0.1188 0.1451 0.1258 -0.0093 -0.0357 0.0247  92  GLN   A N   
816  C  CA  . GLN   A 92  ? 0.1099 0.1530 0.1218 -0.0115 -0.0252 0.0151  92  GLN   A CA  
817  C  C   . GLN   A 92  ? 0.1016 0.1419 0.1213 -0.0036 -0.0247 0.0130  92  GLN   A C   
818  O  O   . GLN   A 92  ? 0.1299 0.1421 0.1291 -0.0077 -0.0320 0.0163  92  GLN   A O   
819  C  CB  . GLN   A 92  ? 0.1149 0.1801 0.1448 -0.0142 -0.0248 0.0157  92  GLN   A CB  
820  C  CG  . GLN   A 92  ? 0.1217 0.1657 0.1535 -0.0148 -0.0413 0.0209  92  GLN   A CG  
821  C  CD  . GLN   A 92  ? 0.1200 0.1788 0.1541 -0.0215 -0.0389 0.0263  92  GLN   A CD  
822  O  OE1 . GLN   A 92  ? 0.1215 0.1675 0.1779 -0.0058 -0.0520 0.0245  92  GLN   A OE1 
823  N  NE2 . GLN   A 92  ? 0.1228 0.2066 0.2117 -0.0172 -0.0516 0.0382  92  GLN   A NE2 
824  N  N   . PHE   A 93  ? 0.1118 0.1380 0.1294 -0.0018 -0.0423 0.0171  93  PHE   A N   
825  C  CA  . PHE   A 93  ? 0.1161 0.1450 0.1277 -0.0094 -0.0363 0.0140  93  PHE   A CA  
826  C  C   . PHE   A 93  ? 0.1150 0.1355 0.1178 -0.0162 -0.0392 0.0058  93  PHE   A C   
827  O  O   . PHE   A 93  ? 0.1323 0.1560 0.1129 -0.0069 -0.0432 0.0093  93  PHE   A O   
828  C  CB  . PHE   A 93  ? 0.1009 0.1426 0.1213 -0.0013 -0.0279 0.0088  93  PHE   A CB  
829  C  CG  . PHE   A 93  ? 0.1016 0.1543 0.1318 0.0017  -0.0329 0.0107  93  PHE   A CG  
830  C  CD1 . PHE   A 93  ? 0.1041 0.1676 0.1386 0.0065  -0.0394 -0.0013 93  PHE   A CD1 
831  C  CD2 . PHE   A 93  ? 0.1212 0.1559 0.1318 0.0061  -0.0429 0.0156  93  PHE   A CD2 
832  C  CE1 . PHE   A 93  ? 0.1278 0.1538 0.1400 0.0023  -0.0417 0.0107  93  PHE   A CE1 
833  C  CE2 . PHE   A 93  ? 0.1178 0.1708 0.1303 -0.0018 -0.0424 0.0159  93  PHE   A CE2 
834  C  CZ  . PHE   A 93  ? 0.1157 0.1674 0.1333 -0.0062 -0.0410 0.0146  93  PHE   A CZ  
835  N  N   . HIS   A 94  ? 0.1109 0.1502 0.1151 0.0032  -0.0263 0.0128  94  HIS   A N   
836  C  CA  . HIS   A 94  ? 0.1127 0.1507 0.1137 -0.0074 -0.0366 0.0069  94  HIS   A CA  
837  C  C   . HIS   A 94  ? 0.1090 0.1465 0.0978 -0.0054 -0.0411 0.0071  94  HIS   A C   
838  O  O   . HIS   A 94  ? 0.1175 0.1538 0.1120 0.0002  -0.0243 0.0209  94  HIS   A O   
839  C  CB  . HIS   A 94  ? 0.1063 0.1691 0.1172 -0.0080 -0.0359 0.0094  94  HIS   A CB  
840  C  CG  . HIS   A 94  ? 0.0939 0.1725 0.1248 -0.0030 -0.0389 0.0048  94  HIS   A CG  
841  N  ND1 . HIS   A 94  ? 0.1059 0.1759 0.1104 0.0004  -0.0280 0.0081  94  HIS   A ND1 
842  C  CD2 . HIS   A 94  ? 0.0864 0.1637 0.1200 0.0086  -0.0285 0.0010  94  HIS   A CD2 
843  C  CE1 . HIS   A 94  ? 0.0981 0.1578 0.1064 -0.0024 -0.0309 0.0036  94  HIS   A CE1 
844  N  NE2 . HIS   A 94  ? 0.0920 0.1636 0.1206 0.0027  -0.0256 -0.0030 94  HIS   A NE2 
845  N  N   . PHE   A 95  ? 0.1193 0.1595 0.1187 0.0025  -0.0224 0.0051  95  PHE   A N   
846  C  CA  . PHE   A 95  ? 0.1153 0.1439 0.1148 0.0077  -0.0340 -0.0003 95  PHE   A CA  
847  C  C   . PHE   A 95  ? 0.1035 0.1493 0.1147 -0.0038 -0.0259 0.0042  95  PHE   A C   
848  O  O   . PHE   A 95  ? 0.1151 0.1801 0.1303 -0.0121 -0.0240 0.0224  95  PHE   A O   
849  C  CB  . PHE   A 95  ? 0.1255 0.1421 0.1219 0.0108  -0.0281 0.0003  95  PHE   A CB  
850  C  CG  . PHE   A 95  ? 0.1205 0.1463 0.1236 0.0025  -0.0388 0.0006  95  PHE   A CG  
851  C  CD1 . PHE   A 95  ? 0.1309 0.1630 0.1418 -0.0134 -0.0537 0.0127  95  PHE   A CD1 
852  C  CD2 . PHE   A 95  ? 0.1230 0.1546 0.1245 -0.0028 -0.0432 -0.0049 95  PHE   A CD2 
853  C  CE1 . PHE   A 95  ? 0.1309 0.1702 0.1630 -0.0026 -0.0618 0.0029  95  PHE   A CE1 
854  C  CE2 . PHE   A 95  ? 0.1217 0.1676 0.1438 -0.0080 -0.0426 -0.0095 95  PHE   A CE2 
855  C  CZ  . PHE   A 95  ? 0.1149 0.1765 0.1686 -0.0075 -0.0612 -0.0120 95  PHE   A CZ  
856  N  N   . HIS   A 96  ? 0.1025 0.1468 0.1110 -0.0068 -0.0243 0.0016  96  HIS   A N   
857  C  CA  . HIS   A 96  ? 0.0999 0.1665 0.1103 0.0036  -0.0238 -0.0003 96  HIS   A CA  
858  C  C   . HIS   A 96  ? 0.1172 0.1778 0.1117 -0.0082 -0.0190 -0.0001 96  HIS   A C   
859  O  O   . HIS   A 96  ? 0.1113 0.1656 0.1219 -0.0058 -0.0151 0.0004  96  HIS   A O   
860  C  CB  . HIS   A 96  ? 0.1064 0.1761 0.1132 0.0010  -0.0210 -0.0070 96  HIS   A CB  
861  C  CG  . HIS   A 96  ? 0.0886 0.1666 0.1336 -0.0041 -0.0251 0.0066  96  HIS   A CG  
862  N  ND1 . HIS   A 96  ? 0.1010 0.1668 0.1412 -0.0056 -0.0306 -0.0037 96  HIS   A ND1 
863  C  CD2 . HIS   A 96  ? 0.0674 0.1635 0.1409 -0.0105 -0.0221 -0.0041 96  HIS   A CD2 
864  C  CE1 . HIS   A 96  ? 0.0863 0.1636 0.1429 0.0000  -0.0244 -0.0052 96  HIS   A CE1 
865  N  NE2 . HIS   A 96  ? 0.0743 0.1604 0.1299 -0.0007 -0.0196 0.0021  96  HIS   A NE2 
866  N  N   . TRP   A 97  ? 0.0932 0.1615 0.1195 -0.0090 -0.0256 -0.0040 97  TRP   A N   
867  C  CA  . TRP   A 97  ? 0.1111 0.1619 0.1248 -0.0046 -0.0280 -0.0091 97  TRP   A CA  
868  C  C   . TRP   A 97  ? 0.1098 0.1496 0.1300 -0.0082 -0.0248 -0.0086 97  TRP   A C   
869  O  O   . TRP   A 97  ? 0.1150 0.1651 0.1426 -0.0020 -0.0136 -0.0054 97  TRP   A O   
870  C  CB  . TRP   A 97  ? 0.1143 0.1568 0.1241 0.0026  -0.0319 -0.0165 97  TRP   A CB  
871  C  CG  . TRP   A 97  ? 0.1217 0.1643 0.1132 -0.0055 -0.0304 -0.0168 97  TRP   A CG  
872  C  CD1 . TRP   A 97  ? 0.1315 0.1691 0.1227 0.0003  -0.0153 -0.0080 97  TRP   A CD1 
873  C  CD2 . TRP   A 97  ? 0.1025 0.1721 0.1167 -0.0079 -0.0215 -0.0101 97  TRP   A CD2 
874  N  NE1 . TRP   A 97  ? 0.1368 0.1847 0.1113 0.0039  -0.0036 -0.0107 97  TRP   A NE1 
875  C  CE2 . TRP   A 97  ? 0.1293 0.1775 0.1245 -0.0045 -0.0115 -0.0146 97  TRP   A CE2 
876  C  CE3 . TRP   A 97  ? 0.0936 0.1845 0.1247 0.0012  -0.0196 -0.0041 97  TRP   A CE3 
877  C  CZ2 . TRP   A 97  ? 0.1312 0.1929 0.1330 0.0042  -0.0254 -0.0012 97  TRP   A CZ2 
878  C  CZ3 . TRP   A 97  ? 0.1187 0.1707 0.1356 -0.0064 -0.0281 -0.0138 97  TRP   A CZ3 
879  C  CH2 . TRP   A 97  ? 0.1216 0.1913 0.1343 -0.0058 -0.0228 -0.0116 97  TRP   A CH2 
880  N  N   . GLY   A 98  ? 0.1144 0.1447 0.1375 0.0005  -0.0246 -0.0195 98  GLY   A N   
881  C  CA  . GLY   A 98  ? 0.1195 0.1555 0.1461 0.0082  -0.0123 -0.0147 98  GLY   A CA  
882  C  C   . GLY   A 98  ? 0.1445 0.1540 0.1470 -0.0016 -0.0081 -0.0099 98  GLY   A C   
883  O  O   . GLY   A 98  ? 0.1558 0.1760 0.1387 0.0059  -0.0184 -0.0030 98  GLY   A O   
884  N  N   . SER   A 99  ? 0.1542 0.1657 0.1556 0.0184  -0.0158 -0.0227 99  SER   A N   
885  C  CA  . SER   A 99  ? 0.1702 0.1835 0.1660 0.0223  -0.0007 -0.0288 99  SER   A CA  
886  C  C   . SER   A 99  ? 0.1668 0.1703 0.1849 0.0224  -0.0205 -0.0317 99  SER   A C   
887  O  O   . SER   A 99  ? 0.2278 0.2052 0.2043 -0.0036 -0.0238 -0.0536 99  SER   A O   
888  C  CB  . SER   A 99  ? 0.1716 0.1970 0.1923 0.0190  0.0140  -0.0334 99  SER   A CB  
889  O  OG  . SER   A 99  ? 0.1616 0.2179 0.2067 0.0271  0.0038  -0.0023 99  SER   A OG  
890  N  N   . LEU   A 100 ? 0.1472 0.1587 0.2015 0.0106  -0.0070 -0.0288 100 LEU   A N   
891  C  CA  . LEU   A 100 ? 0.1799 0.1543 0.2662 0.0036  0.0138  -0.0378 100 LEU   A CA  
892  C  C   . LEU   A 100 ? 0.1729 0.1440 0.2158 0.0046  -0.0025 0.0000  100 LEU   A C   
893  O  O   . LEU   A 100 ? 0.1776 0.1544 0.2059 0.0025  -0.0168 -0.0080 100 LEU   A O   
894  C  CB  . LEU   A 100 ? 0.2458 0.1802 0.3300 0.0018  0.0398  -0.0085 100 LEU   A CB  
895  C  CG  . LEU   A 100 ? 0.2875 0.2549 0.3591 0.0314  0.0411  -0.0114 100 LEU   A CG  
896  C  CD1 . LEU   A 100 ? 0.3174 0.2629 0.4184 0.0847  0.0344  0.0087  100 LEU   A CD1 
897  C  CD2 . LEU   A 100 ? 0.3389 0.3136 0.3942 0.0337  0.0731  -0.0922 100 LEU   A CD2 
898  N  N   . ASP   A 101 ? 0.1800 0.1469 0.2412 -0.0126 -0.0118 -0.0080 101 ASP   A N   
899  C  CA  . ASP   A 101 ? 0.1763 0.1443 0.2139 0.0064  -0.0065 0.0042  101 ASP   A CA  
900  C  C   . ASP   A 101 ? 0.1689 0.1483 0.2296 0.0101  -0.0119 0.0197  101 ASP   A C   
901  O  O   . ASP   A 101 ? 0.2211 0.1778 0.2316 0.0068  -0.0038 0.0121  101 ASP   A O   
902  C  CB  . ASP   A 101 ? 0.1805 0.1859 0.2158 -0.0080 -0.0172 0.0229  101 ASP   A CB  
903  C  CG  . ASP   A 101 ? 0.1975 0.2010 0.2105 -0.0101 -0.0167 0.0119  101 ASP   A CG  
904  O  OD1 . ASP   A 101 ? 0.2078 0.2377 0.1934 -0.0446 -0.0106 0.0106  101 ASP   A OD1 
905  O  OD2 . ASP   A 101 ? 0.2350 0.2391 0.2374 -0.0425 -0.0372 0.0033  101 ASP   A OD2 
906  N  N   . GLY   A 102 ? 0.1881 0.1921 0.2255 -0.0018 -0.0318 0.0296  102 GLY   A N   
907  C  CA  . GLY   A 102 ? 0.2201 0.2058 0.2385 -0.0123 -0.0238 0.0543  102 GLY   A CA  
908  C  C   . GLY   A 102 ? 0.1966 0.2094 0.2005 -0.0024 -0.0166 0.0210  102 GLY   A C   
909  O  O   . GLY   A 102 ? 0.2283 0.2580 0.1908 -0.0050 -0.0214 0.0484  102 GLY   A O   
910  N  N   A GLN   A 103 ? 0.1532 0.1959 0.1861 -0.0037 -0.0262 0.0036  103 GLN   A N   
911  N  N   B GLN   A 103 ? 0.1659 0.2045 0.1983 -0.0084 -0.0254 0.0108  103 GLN   A N   
912  C  CA  A GLN   A 103 ? 0.1421 0.1705 0.1509 0.0164  -0.0232 -0.0089 103 GLN   A CA  
913  C  CA  B GLN   A 103 ? 0.1594 0.1822 0.1718 0.0088  -0.0217 -0.0002 103 GLN   A CA  
914  C  C   A GLN   A 103 ? 0.1274 0.1652 0.1455 0.0155  -0.0125 -0.0095 103 GLN   A C   
915  C  C   B GLN   A 103 ? 0.1393 0.1735 0.1629 0.0032  -0.0132 -0.0064 103 GLN   A C   
916  O  O   A GLN   A 103 ? 0.1258 0.1761 0.1362 0.0222  -0.0059 -0.0117 103 GLN   A O   
917  O  O   B GLN   A 103 ? 0.1420 0.1846 0.1703 -0.0160 -0.0135 -0.0192 103 GLN   A O   
918  C  CB  A GLN   A 103 ? 0.1440 0.1628 0.1564 0.0197  -0.0284 -0.0029 103 GLN   A CB  
919  C  CB  B GLN   A 103 ? 0.1669 0.1756 0.1771 0.0174  -0.0231 0.0176  103 GLN   A CB  
920  C  CG  A GLN   A 103 ? 0.1404 0.1625 0.1604 0.0198  -0.0234 0.0079  103 GLN   A CG  
921  C  CG  B GLN   A 103 ? 0.1715 0.1836 0.1922 0.0131  -0.0109 0.0305  103 GLN   A CG  
922  C  CD  A GLN   A 103 ? 0.1421 0.1744 0.2069 0.0146  -0.0213 0.0078  103 GLN   A CD  
923  C  CD  B GLN   A 103 ? 0.2030 0.2117 0.2205 0.0403  -0.0045 0.0389  103 GLN   A CD  
924  O  OE1 A GLN   A 103 ? 0.1433 0.2145 0.2353 0.0113  -0.0097 0.0224  103 GLN   A OE1 
925  O  OE1 B GLN   A 103 ? 0.2140 0.2135 0.2425 0.0617  0.0292  0.0507  103 GLN   A OE1 
926  N  NE2 A GLN   A 103 ? 0.1284 0.1612 0.2343 0.0225  -0.0082 -0.0018 103 GLN   A NE2 
927  N  NE2 B GLN   A 103 ? 0.1918 0.2315 0.2470 0.0357  0.0004  0.0464  103 GLN   A NE2 
928  N  N   . GLY   A 104 ? 0.1207 0.1651 0.1541 0.0110  -0.0166 -0.0087 104 GLY   A N   
929  C  CA  . GLY   A 104 ? 0.1039 0.1643 0.1563 0.0000  -0.0194 -0.0051 104 GLY   A CA  
930  C  C   . GLY   A 104 ? 0.1044 0.1566 0.1272 -0.0002 -0.0240 0.0069  104 GLY   A C   
931  O  O   . GLY   A 104 ? 0.1235 0.1681 0.1543 0.0056  -0.0232 0.0073  104 GLY   A O   
932  N  N   . SER   A 105 ? 0.1120 0.1582 0.1216 0.0053  -0.0236 0.0074  105 SER   A N   
933  C  CA  . SER   A 105 ? 0.1157 0.1567 0.1211 -0.0003 -0.0278 0.0039  105 SER   A CA  
934  C  C   . SER   A 105 ? 0.1137 0.1434 0.1285 -0.0064 -0.0205 0.0026  105 SER   A C   
935  O  O   . SER   A 105 ? 0.1167 0.1644 0.1355 0.0115  -0.0298 -0.0104 105 SER   A O   
936  C  CB  . SER   A 105 ? 0.1013 0.1514 0.1275 -0.0092 -0.0259 0.0007  105 SER   A CB  
937  O  OG  . SER   A 105 ? 0.1181 0.1431 0.1355 -0.0031 -0.0067 0.0038  105 SER   A OG  
938  N  N   . GLU   A 106 ? 0.0906 0.1480 0.1270 -0.0013 -0.0190 -0.0032 106 GLU   A N   
939  C  CA  . GLU   A 106 ? 0.0998 0.1498 0.1230 -0.0032 -0.0224 -0.0070 106 GLU   A CA  
940  C  C   . GLU   A 106 ? 0.0979 0.1408 0.1223 0.0043  -0.0253 0.0049  106 GLU   A C   
941  O  O   . GLU   A 106 ? 0.1021 0.1591 0.1307 0.0088  -0.0324 -0.0043 106 GLU   A O   
942  C  CB  . GLU   A 106 ? 0.0932 0.1576 0.1195 -0.0106 -0.0186 -0.0083 106 GLU   A CB  
943  C  CG  . GLU   A 106 ? 0.1248 0.1551 0.1155 -0.0068 -0.0188 0.0008  106 GLU   A CG  
944  C  CD  . GLU   A 106 ? 0.0925 0.1652 0.1126 -0.0078 -0.0124 -0.0174 106 GLU   A CD  
945  O  OE1 . GLU   A 106 ? 0.0893 0.1501 0.1342 -0.0062 -0.0268 -0.0091 106 GLU   A OE1 
946  O  OE2 . GLU   A 106 ? 0.0979 0.1940 0.1415 -0.0050 -0.0064 -0.0109 106 GLU   A OE2 
947  N  N   . HIS   A 107 ? 0.1004 0.1377 0.1167 0.0042  -0.0207 0.0084  107 HIS   A N   
948  C  CA  . HIS   A 107 ? 0.0915 0.1481 0.1196 -0.0049 -0.0249 0.0005  107 HIS   A CA  
949  C  C   . HIS   A 107 ? 0.1080 0.1403 0.1243 0.0018  -0.0122 -0.0020 107 HIS   A C   
950  O  O   . HIS   A 107 ? 0.1080 0.1386 0.1368 0.0070  -0.0269 -0.0035 107 HIS   A O   
951  C  CB  . HIS   A 107 ? 0.0952 0.1605 0.1137 0.0026  -0.0197 0.0094  107 HIS   A CB  
952  C  CG  . HIS   A 107 ? 0.0969 0.1522 0.1128 0.0043  -0.0187 0.0048  107 HIS   A CG  
953  N  ND1 . HIS   A 107 ? 0.0963 0.1410 0.1314 0.0020  -0.0316 0.0214  107 HIS   A ND1 
954  C  CD2 . HIS   A 107 ? 0.1103 0.1504 0.1083 0.0121  -0.0246 0.0042  107 HIS   A CD2 
955  C  CE1 . HIS   A 107 ? 0.0967 0.1377 0.1153 0.0062  -0.0137 0.0325  107 HIS   A CE1 
956  N  NE2 . HIS   A 107 ? 0.1088 0.1432 0.1135 0.0043  -0.0245 0.0021  107 HIS   A NE2 
957  N  N   . THR   A 108 ? 0.1139 0.1438 0.1332 -0.0099 -0.0294 0.0024  108 THR   A N   
958  C  CA  . THR   A 108 ? 0.1094 0.1355 0.1284 0.0023  -0.0316 -0.0022 108 THR   A CA  
959  C  C   . THR   A 108 ? 0.1113 0.1436 0.1296 0.0080  -0.0286 0.0113  108 THR   A C   
960  O  O   . THR   A 108 ? 0.1208 0.1665 0.1362 0.0110  -0.0240 0.0040  108 THR   A O   
961  C  CB  . THR   A 108 ? 0.1376 0.1346 0.1380 0.0188  -0.0319 -0.0022 108 THR   A CB  
962  O  OG1 . THR   A 108 ? 0.1315 0.1743 0.1302 0.0122  -0.0297 0.0043  108 THR   A OG1 
963  C  CG2 . THR   A 108 ? 0.1304 0.1474 0.1365 0.0176  -0.0409 -0.0069 108 THR   A CG2 
964  N  N   . VAL   A 109 ? 0.1255 0.1563 0.1307 0.0025  -0.0195 -0.0016 109 VAL   A N   
965  C  CA  . VAL   A 109 ? 0.1330 0.1784 0.1373 0.0042  -0.0213 0.0136  109 VAL   A CA  
966  C  C   . VAL   A 109 ? 0.1525 0.1753 0.1388 0.0053  -0.0230 0.0199  109 VAL   A C   
967  O  O   . VAL   A 109 ? 0.1510 0.1641 0.1624 0.0053  -0.0273 0.0180  109 VAL   A O   
968  C  CB  . VAL   A 109 ? 0.1309 0.1801 0.1413 -0.0006 -0.0325 0.0159  109 VAL   A CB  
969  C  CG1 . VAL   A 109 ? 0.1321 0.2077 0.1570 -0.0076 -0.0291 0.0268  109 VAL   A CG1 
970  C  CG2 . VAL   A 109 ? 0.1413 0.1939 0.1493 0.0137  -0.0387 0.0188  109 VAL   A CG2 
971  N  N   . ASP   A 110 ? 0.1550 0.1716 0.1255 0.0082  -0.0063 0.0179  110 ASP   A N   
972  C  CA  . ASP   A 110 ? 0.1563 0.1859 0.1589 0.0169  -0.0191 0.0426  110 ASP   A CA  
973  C  C   . ASP   A 110 ? 0.1624 0.1854 0.1554 0.0146  -0.0308 0.0294  110 ASP   A C   
974  O  O   . ASP   A 110 ? 0.1988 0.1815 0.1829 0.0135  -0.0114 0.0453  110 ASP   A O   
975  C  CB  . ASP   A 110 ? 0.2027 0.1850 0.1814 0.0100  0.0035  0.0507  110 ASP   A CB  
976  C  CG  . ASP   A 110 ? 0.1960 0.1891 0.1860 0.0029  0.0144  0.0474  110 ASP   A CG  
977  O  OD1 . ASP   A 110 ? 0.2125 0.2058 0.2188 0.0038  0.0193  0.0427  110 ASP   A OD1 
978  O  OD2 . ASP   A 110 ? 0.1933 0.2464 0.2354 -0.0141 -0.0067 0.0466  110 ASP   A OD2 
979  N  N   . LYS   A 111 ? 0.1546 0.1631 0.1538 0.0209  -0.0192 0.0242  111 LYS   A N   
980  C  CA  . LYS   A 111 ? 0.1682 0.1878 0.1564 0.0245  -0.0171 0.0136  111 LYS   A CA  
981  C  C   . LYS   A 111 ? 0.1791 0.1791 0.1400 0.0187  -0.0028 0.0030  111 LYS   A C   
982  O  O   . LYS   A 111 ? 0.1973 0.1911 0.1768 0.0060  0.0116  0.0004  111 LYS   A O   
983  C  CB  . LYS   A 111 ? 0.1832 0.2132 0.2012 0.0426  -0.0276 0.0299  111 LYS   A CB  
984  C  CG  . LYS   A 111 ? 0.2197 0.2700 0.2107 0.0702  -0.0663 0.0401  111 LYS   A CG  
985  C  CD  . LYS   A 111 ? 0.2627 0.3420 0.2539 0.0128  -0.0884 0.0120  111 LYS   A CD  
986  C  CE  . LYS   A 111 ? 0.3374 0.3954 0.2388 0.0670  -0.1007 0.0305  111 LYS   A CE  
987  N  NZ  . LYS   A 111 ? 0.3556 0.4279 0.3679 0.0600  -0.0735 0.0509  111 LYS   A NZ  
988  N  N   . LYS   A 112 ? 0.1809 0.1764 0.1284 0.0062  -0.0014 0.0201  112 LYS   A N   
989  C  CA  . LYS   A 112 ? 0.1758 0.1753 0.1477 0.0023  0.0024  -0.0033 112 LYS   A CA  
990  C  C   . LYS   A 112 ? 0.1508 0.1690 0.1328 0.0066  -0.0261 0.0010  112 LYS   A C   
991  O  O   . LYS   A 112 ? 0.1460 0.1624 0.1548 0.0002  -0.0198 -0.0023 112 LYS   A O   
992  C  CB  . LYS   A 112 ? 0.1775 0.1819 0.1914 -0.0294 -0.0006 -0.0183 112 LYS   A CB  
993  C  CG  . LYS   A 112 ? 0.2062 0.2416 0.2019 -0.0420 -0.0076 -0.0487 112 LYS   A CG  
994  C  CD  . LYS   A 112 ? 0.2299 0.2809 0.2823 -0.0177 -0.0214 -0.0098 112 LYS   A CD  
995  C  CE  . LYS   A 112 ? 0.2888 0.3150 0.3107 -0.0010 -0.0491 0.0061  112 LYS   A CE  
996  N  NZ  . LYS   A 112 ? 0.3156 0.3575 0.3531 0.0344  -0.1016 0.0165  112 LYS   A NZ  
997  N  N   A LYS   A 113 ? 0.1650 0.1648 0.1300 0.0147  -0.0223 0.0022  113 LYS   A N   
998  N  N   B LYS   A 113 ? 0.1648 0.1590 0.1330 0.0132  -0.0256 -0.0011 113 LYS   A N   
999  C  CA  A LYS   A 113 ? 0.1732 0.1790 0.1290 0.0137  -0.0137 -0.0010 113 LYS   A CA  
1000 C  CA  B LYS   A 113 ? 0.1741 0.1694 0.1338 0.0110  -0.0200 -0.0064 113 LYS   A CA  
1001 C  C   A LYS   A 113 ? 0.1615 0.1525 0.1494 0.0089  -0.0165 0.0000  113 LYS   A C   
1002 C  C   B LYS   A 113 ? 0.1547 0.1480 0.1494 0.0065  -0.0196 -0.0039 113 LYS   A C   
1003 O  O   A LYS   A 113 ? 0.1711 0.1498 0.1588 0.0060  -0.0093 0.0099  113 LYS   A O   
1004 O  O   B LYS   A 113 ? 0.1568 0.1585 0.1445 0.0093  -0.0281 -0.0137 113 LYS   A O   
1005 C  CB  A LYS   A 113 ? 0.1711 0.1885 0.1468 0.0337  -0.0186 0.0004  113 LYS   A CB  
1006 C  CB  B LYS   A 113 ? 0.1748 0.1724 0.1562 0.0291  -0.0263 -0.0073 113 LYS   A CB  
1007 C  CG  A LYS   A 113 ? 0.1786 0.2112 0.1299 0.0350  -0.0186 -0.0083 113 LYS   A CG  
1008 C  CG  B LYS   A 113 ? 0.1860 0.1749 0.1594 0.0276  -0.0299 -0.0199 113 LYS   A CG  
1009 C  CD  A LYS   A 113 ? 0.1683 0.2265 0.1514 0.0449  -0.0200 -0.0123 113 LYS   A CD  
1010 C  CD  B LYS   A 113 ? 0.1771 0.2045 0.1928 0.0259  -0.0257 -0.0260 113 LYS   A CD  
1011 C  CE  A LYS   A 113 ? 0.1710 0.2602 0.1456 0.0453  -0.0154 -0.0333 113 LYS   A CE  
1012 C  CE  B LYS   A 113 ? 0.1868 0.2256 0.2227 0.0229  -0.0306 -0.0202 113 LYS   A CE  
1013 N  NZ  A LYS   A 113 ? 0.1597 0.2659 0.1580 0.0578  -0.0044 -0.0208 113 LYS   A NZ  
1014 N  NZ  B LYS   A 113 ? 0.1863 0.2632 0.2206 0.0267  -0.0223 -0.0115 113 LYS   A NZ  
1015 N  N   . TYR   A 114 ? 0.1353 0.1397 0.1489 0.0127  -0.0272 -0.0085 114 TYR   A N   
1016 C  CA  . TYR   A 114 ? 0.1331 0.1372 0.1520 -0.0010 -0.0316 -0.0020 114 TYR   A CA  
1017 C  C   . TYR   A 114 ? 0.1315 0.1476 0.1578 0.0017  -0.0286 -0.0041 114 TYR   A C   
1018 O  O   . TYR   A 114 ? 0.1369 0.1559 0.1549 -0.0127 -0.0259 -0.0071 114 TYR   A O   
1019 C  CB  . TYR   A 114 ? 0.1364 0.1420 0.1526 -0.0012 -0.0197 0.0008  114 TYR   A CB  
1020 C  CG  . TYR   A 114 ? 0.1380 0.1319 0.1512 0.0109  -0.0151 0.0052  114 TYR   A CG  
1021 C  CD1 . TYR   A 114 ? 0.1710 0.1585 0.1591 0.0315  -0.0081 0.0151  114 TYR   A CD1 
1022 C  CD2 . TYR   A 114 ? 0.1601 0.1632 0.1707 -0.0126 -0.0123 0.0101  114 TYR   A CD2 
1023 C  CE1 . TYR   A 114 ? 0.2164 0.1940 0.1471 0.0366  -0.0034 0.0146  114 TYR   A CE1 
1024 C  CE2 . TYR   A 114 ? 0.1851 0.1819 0.1879 0.0123  0.0123  0.0265  114 TYR   A CE2 
1025 C  CZ  . TYR   A 114 ? 0.2174 0.1991 0.1718 0.0238  0.0271  0.0367  114 TYR   A CZ  
1026 O  OH  . TYR   A 114 ? 0.2741 0.2753 0.2116 0.0462  0.0506  0.0533  114 TYR   A OH  
1027 N  N   . ALA   A 115 ? 0.1191 0.1523 0.1519 -0.0002 -0.0229 -0.0123 115 ALA   A N   
1028 C  CA  . ALA   A 115 ? 0.1222 0.1679 0.1512 -0.0063 -0.0336 -0.0174 115 ALA   A CA  
1029 C  C   . ALA   A 115 ? 0.1071 0.1651 0.1500 -0.0113 -0.0254 -0.0081 115 ALA   A C   
1030 O  O   . ALA   A 115 ? 0.1304 0.1544 0.1551 0.0020  -0.0197 0.0033  115 ALA   A O   
1031 C  CB  . ALA   A 115 ? 0.1368 0.1721 0.1604 -0.0073 -0.0373 -0.0185 115 ALA   A CB  
1032 N  N   . ALA   A 116 ? 0.1127 0.1540 0.1214 -0.0176 -0.0090 -0.0106 116 ALA   A N   
1033 C  CA  . ALA   A 116 ? 0.1099 0.1639 0.1147 -0.0086 -0.0020 0.0029  116 ALA   A CA  
1034 C  C   . ALA   A 116 ? 0.0937 0.1613 0.1126 0.0002  -0.0186 0.0060  116 ALA   A C   
1035 O  O   . ALA   A 116 ? 0.1130 0.1485 0.1228 -0.0063 -0.0142 0.0046  116 ALA   A O   
1036 C  CB  . ALA   A 116 ? 0.1205 0.1565 0.1108 -0.0153 -0.0118 -0.0041 116 ALA   A CB  
1037 N  N   . GLU   A 117 ? 0.0938 0.1520 0.1084 -0.0034 -0.0138 0.0026  117 GLU   A N   
1038 C  CA  . GLU   A 117 ? 0.1010 0.1466 0.1120 -0.0055 -0.0189 0.0055  117 GLU   A CA  
1039 C  C   . GLU   A 117 ? 0.0953 0.1446 0.1125 0.0004  -0.0209 0.0026  117 GLU   A C   
1040 O  O   . GLU   A 117 ? 0.1015 0.1647 0.1353 0.0066  -0.0104 0.0225  117 GLU   A O   
1041 C  CB  . GLU   A 117 ? 0.1138 0.1451 0.1104 -0.0061 -0.0228 0.0111  117 GLU   A CB  
1042 C  CG  . GLU   A 117 ? 0.1062 0.1456 0.1059 -0.0007 -0.0251 0.0061  117 GLU   A CG  
1043 C  CD  . GLU   A 117 ? 0.0953 0.1473 0.1282 -0.0020 -0.0294 -0.0122 117 GLU   A CD  
1044 O  OE1 . GLU   A 117 ? 0.0958 0.1628 0.1347 0.0027  -0.0240 -0.0022 117 GLU   A OE1 
1045 O  OE2 . GLU   A 117 ? 0.1284 0.1477 0.1213 -0.0049 -0.0478 -0.0004 117 GLU   A OE2 
1046 N  N   . LEU   A 118 ? 0.0924 0.1361 0.1173 0.0002  -0.0311 0.0004  118 LEU   A N   
1047 C  CA  . LEU   A 118 ? 0.0911 0.1475 0.1061 -0.0084 -0.0320 0.0046  118 LEU   A CA  
1048 C  C   . LEU   A 118 ? 0.0886 0.1401 0.1059 -0.0059 -0.0264 0.0051  118 LEU   A C   
1049 O  O   . LEU   A 118 ? 0.0892 0.1457 0.1112 -0.0120 -0.0245 0.0110  118 LEU   A O   
1050 C  CB  . LEU   A 118 ? 0.0964 0.1519 0.1351 -0.0151 -0.0360 0.0108  118 LEU   A CB  
1051 C  CG  . LEU   A 118 ? 0.1007 0.1603 0.1189 -0.0004 -0.0448 0.0126  118 LEU   A CG  
1052 C  CD1 . LEU   A 118 ? 0.0894 0.1638 0.1296 -0.0011 -0.0496 0.0204  118 LEU   A CD1 
1053 C  CD2 . LEU   A 118 ? 0.1131 0.1741 0.1321 -0.0057 -0.0538 0.0069  118 LEU   A CD2 
1054 N  N   . HIS   A 119 ? 0.0872 0.1395 0.0951 -0.0114 -0.0309 0.0066  119 HIS   A N   
1055 C  CA  . HIS   A 119 ? 0.0840 0.1543 0.1122 -0.0165 -0.0269 0.0038  119 HIS   A CA  
1056 C  C   . HIS   A 119 ? 0.0800 0.1294 0.1226 -0.0153 -0.0288 -0.0016 119 HIS   A C   
1057 O  O   . HIS   A 119 ? 0.0909 0.1552 0.1279 -0.0009 -0.0237 0.0089  119 HIS   A O   
1058 C  CB  . HIS   A 119 ? 0.0778 0.1492 0.1189 -0.0168 -0.0266 0.0062  119 HIS   A CB  
1059 C  CG  . HIS   A 119 ? 0.0750 0.1583 0.1100 0.0021  -0.0335 0.0054  119 HIS   A CG  
1060 N  ND1 . HIS   A 119 ? 0.0875 0.1427 0.1091 -0.0120 -0.0321 0.0181  119 HIS   A ND1 
1061 C  CD2 . HIS   A 119 ? 0.0846 0.1411 0.1274 0.0019  -0.0345 0.0067  119 HIS   A CD2 
1062 C  CE1 . HIS   A 119 ? 0.0891 0.1459 0.1122 -0.0070 -0.0339 0.0198  119 HIS   A CE1 
1063 N  NE2 . HIS   A 119 ? 0.0894 0.1513 0.1245 0.0055  -0.0266 0.0077  119 HIS   A NE2 
1064 N  N   . LEU   A 120 ? 0.0906 0.1336 0.1164 -0.0075 -0.0332 0.0040  120 LEU   A N   
1065 C  CA  . LEU   A 120 ? 0.0874 0.1482 0.1198 -0.0021 -0.0300 0.0045  120 LEU   A CA  
1066 C  C   . LEU   A 120 ? 0.0864 0.1219 0.1175 0.0048  -0.0188 0.0075  120 LEU   A C   
1067 O  O   . LEU   A 120 ? 0.0909 0.1405 0.1210 -0.0105 -0.0277 0.0023  120 LEU   A O   
1068 C  CB  . LEU   A 120 ? 0.0929 0.1434 0.1534 -0.0033 -0.0336 0.0047  120 LEU   A CB  
1069 C  CG  . LEU   A 120 ? 0.0926 0.1496 0.1709 -0.0156 -0.0455 0.0053  120 LEU   A CG  
1070 C  CD1 . LEU   A 120 ? 0.1512 0.1710 0.1777 -0.0367 -0.0556 0.0023  120 LEU   A CD1 
1071 C  CD2 . LEU   A 120 ? 0.1153 0.1677 0.1440 -0.0242 -0.0544 -0.0016 120 LEU   A CD2 
1072 N  N   . VAL   A 121 ? 0.0881 0.1437 0.1140 -0.0128 -0.0269 0.0054  121 VAL   A N   
1073 C  CA  . VAL   A 121 ? 0.1017 0.1494 0.1280 -0.0071 -0.0338 0.0026  121 VAL   A CA  
1074 C  C   . VAL   A 121 ? 0.1094 0.1352 0.1238 -0.0153 -0.0265 0.0108  121 VAL   A C   
1075 O  O   . VAL   A 121 ? 0.1331 0.1459 0.1340 -0.0086 -0.0381 0.0173  121 VAL   A O   
1076 C  CB  . VAL   A 121 ? 0.0923 0.1568 0.1400 -0.0132 -0.0396 0.0214  121 VAL   A CB  
1077 C  CG1 . VAL   A 121 ? 0.0977 0.1568 0.1612 -0.0195 -0.0266 0.0256  121 VAL   A CG1 
1078 C  CG2 . VAL   A 121 ? 0.1087 0.1707 0.1525 -0.0015 -0.0421 0.0188  121 VAL   A CG2 
1079 N  N   . HIS   A 122 ? 0.1056 0.1322 0.1282 -0.0068 -0.0425 0.0014  122 HIS   A N   
1080 C  CA  . HIS   A 122 ? 0.1193 0.1346 0.1374 -0.0117 -0.0416 -0.0008 122 HIS   A CA  
1081 C  C   . HIS   A 122 ? 0.1300 0.1338 0.1534 -0.0120 -0.0454 -0.0028 122 HIS   A C   
1082 O  O   . HIS   A 122 ? 0.1547 0.1647 0.1556 -0.0060 -0.0745 -0.0034 122 HIS   A O   
1083 C  CB  . HIS   A 122 ? 0.1193 0.1364 0.1641 -0.0020 -0.0429 0.0091  122 HIS   A CB  
1084 C  CG  . HIS   A 122 ? 0.1165 0.1322 0.1588 -0.0087 -0.0374 0.0030  122 HIS   A CG  
1085 N  ND1 . HIS   A 122 ? 0.1077 0.1201 0.1761 -0.0077 -0.0318 -0.0036 122 HIS   A ND1 
1086 C  CD2 . HIS   A 122 ? 0.1243 0.1507 0.1552 0.0029  -0.0406 0.0044  122 HIS   A CD2 
1087 C  CE1 . HIS   A 122 ? 0.1090 0.0992 0.1838 0.0007  -0.0321 -0.0015 122 HIS   A CE1 
1088 N  NE2 . HIS   A 122 ? 0.1079 0.1543 0.1681 0.0042  -0.0412 -0.0005 122 HIS   A NE2 
1089 N  N   . TRP   A 123 ? 0.1347 0.1344 0.1456 -0.0005 -0.0548 -0.0048 123 TRP   A N   
1090 C  CA  . TRP   A 123 ? 0.1414 0.1371 0.1440 -0.0075 -0.0496 -0.0135 123 TRP   A CA  
1091 C  C   . TRP   A 123 ? 0.1507 0.1517 0.1668 0.0084  -0.0539 -0.0106 123 TRP   A C   
1092 O  O   . TRP   A 123 ? 0.1438 0.1489 0.2114 -0.0010 -0.0745 -0.0029 123 TRP   A O   
1093 C  CB  . TRP   A 123 ? 0.1641 0.1832 0.1751 -0.0195 -0.0447 0.0078  123 TRP   A CB  
1094 C  CG  . TRP   A 123 ? 0.2315 0.1655 0.1783 -0.0338 -0.0520 0.0116  123 TRP   A CG  
1095 C  CD1 . TRP   A 123 ? 0.2530 0.1678 0.1875 -0.0270 -0.0925 0.0017  123 TRP   A CD1 
1096 C  CD2 . TRP   A 123 ? 0.2959 0.1629 0.1694 -0.0241 -0.0683 0.0170  123 TRP   A CD2 
1097 N  NE1 . TRP   A 123 ? 0.3088 0.1570 0.1887 -0.0307 -0.1088 0.0078  123 TRP   A NE1 
1098 C  CE2 . TRP   A 123 ? 0.3154 0.1544 0.1879 -0.0331 -0.0990 0.0082  123 TRP   A CE2 
1099 C  CE3 . TRP   A 123 ? 0.3357 0.1719 0.1961 -0.0597 -0.0767 -0.0055 123 TRP   A CE3 
1100 C  CZ2 . TRP   A 123 ? 0.4066 0.1623 0.1831 -0.0138 -0.1104 0.0039  123 TRP   A CZ2 
1101 C  CZ3 . TRP   A 123 ? 0.3977 0.1655 0.1932 -0.0672 -0.0844 -0.0050 123 TRP   A CZ3 
1102 C  CH2 . TRP   A 123 ? 0.4243 0.1606 0.2174 -0.0138 -0.1022 0.0137  123 TRP   A CH2 
1103 N  N   . ASN   A 124 ? 0.1370 0.1584 0.1773 0.0061  -0.0455 -0.0295 124 ASN   A N   
1104 C  CA  . ASN   A 124 ? 0.1507 0.1423 0.1724 -0.0030 -0.0464 -0.0261 124 ASN   A CA  
1105 C  C   . ASN   A 124 ? 0.1681 0.1545 0.1800 0.0087  -0.0395 -0.0335 124 ASN   A C   
1106 O  O   . ASN   A 124 ? 0.1646 0.1454 0.2018 -0.0089 -0.0389 -0.0221 124 ASN   A O   
1107 C  CB  . ASN   A 124 ? 0.1446 0.1634 0.1790 -0.0250 -0.0403 -0.0243 124 ASN   A CB  
1108 C  CG  . ASN   A 124 ? 0.1733 0.1679 0.1876 -0.0239 -0.0111 -0.0135 124 ASN   A CG  
1109 O  OD1 . ASN   A 124 ? 0.1721 0.1846 0.2153 -0.0065 -0.0178 -0.0302 124 ASN   A OD1 
1110 N  ND2 . ASN   A 124 ? 0.1903 0.1946 0.1879 0.0191  0.0089  -0.0250 124 ASN   A ND2 
1111 N  N   . THR   A 125 ? 0.1575 0.1570 0.2124 0.0156  -0.0482 -0.0232 125 THR   A N   
1112 C  CA  . THR   A 125 ? 0.1801 0.1694 0.2545 0.0310  -0.0664 -0.0149 125 THR   A CA  
1113 C  C   . THR   A 125 ? 0.1807 0.1603 0.2533 0.0341  -0.0400 -0.0144 125 THR   A C   
1114 O  O   . THR   A 125 ? 0.2112 0.1553 0.3041 0.0246  -0.0437 -0.0080 125 THR   A O   
1115 C  CB  . THR   A 125 ? 0.1880 0.2236 0.3071 0.0294  -0.1107 -0.0161 125 THR   A CB  
1116 O  OG1 . THR   A 125 ? 0.1795 0.2258 0.3746 0.0501  -0.0764 -0.0341 125 THR   A OG1 
1117 C  CG2 . THR   A 125 ? 0.2224 0.2175 0.3272 0.0268  -0.1330 -0.0127 125 THR   A CG2 
1118 N  N   . LYS   A 126 ? 0.1670 0.1570 0.2273 0.0094  -0.0250 -0.0173 126 LYS   A N   
1119 C  CA  . LYS   A 126 ? 0.2078 0.1651 0.2514 -0.0065 -0.0047 -0.0333 126 LYS   A CA  
1120 C  C   . LYS   A 126 ? 0.1947 0.1575 0.2349 -0.0162 -0.0301 -0.0233 126 LYS   A C   
1121 O  O   . LYS   A 126 ? 0.2201 0.1627 0.3013 -0.0227 0.0114  -0.0534 126 LYS   A O   
1122 C  CB  . LYS   A 126 ? 0.2469 0.2065 0.2658 -0.0580 -0.0268 -0.0432 126 LYS   A CB  
1123 C  CG  . LYS   A 126 ? 0.2637 0.2356 0.2566 -0.0521 -0.0471 -0.0403 126 LYS   A CG  
1124 C  CD  . LYS   A 126 ? 0.3220 0.2712 0.2977 -0.0345 -0.0148 -0.0358 126 LYS   A CD  
1125 C  CE  . LYS   A 126 ? 0.2276 0.3432 0.4314 -0.0074 -0.1125 -0.0564 126 LYS   A CE  
1126 N  N   . TYR   A 127 ? 0.1701 0.1419 0.2011 -0.0237 -0.0347 -0.0241 127 TYR   A N   
1127 C  CA  . TYR   A 127 ? 0.1725 0.1656 0.1949 -0.0066 -0.0297 -0.0177 127 TYR   A CA  
1128 C  C   . TYR   A 127 ? 0.1944 0.1812 0.2054 0.0028  -0.0140 -0.0183 127 TYR   A C   
1129 O  O   . TYR   A 127 ? 0.1966 0.2122 0.2175 -0.0035 0.0001  0.0065  127 TYR   A O   
1130 C  CB  . TYR   A 127 ? 0.1705 0.1635 0.1964 -0.0043 -0.0119 -0.0237 127 TYR   A CB  
1131 C  CG  . TYR   A 127 ? 0.1604 0.1661 0.1913 0.0024  -0.0185 -0.0298 127 TYR   A CG  
1132 C  CD1 . TYR   A 127 ? 0.1886 0.1687 0.2049 -0.0117 -0.0337 -0.0265 127 TYR   A CD1 
1133 C  CD2 . TYR   A 127 ? 0.1636 0.1543 0.1856 0.0110  -0.0190 -0.0295 127 TYR   A CD2 
1134 C  CE1 . TYR   A 127 ? 0.2046 0.1926 0.1915 -0.0113 -0.0433 -0.0358 127 TYR   A CE1 
1135 C  CE2 . TYR   A 127 ? 0.1576 0.1662 0.1821 0.0009  -0.0136 -0.0241 127 TYR   A CE2 
1136 C  CZ  . TYR   A 127 ? 0.1683 0.1955 0.1822 -0.0002 -0.0082 -0.0403 127 TYR   A CZ  
1137 O  OH  . TYR   A 127 ? 0.2268 0.2119 0.1915 0.0047  -0.0227 -0.0443 127 TYR   A OH  
1138 N  N   . GLY   A 128 ? 0.1901 0.1824 0.2157 -0.0007 -0.0181 -0.0116 128 GLY   A N   
1139 C  CA  . GLY   A 128 ? 0.1956 0.1746 0.2062 -0.0132 0.0103  0.0099  128 GLY   A CA  
1140 C  C   . GLY   A 128 ? 0.2439 0.1883 0.1770 0.0253  -0.0014 0.0351  128 GLY   A C   
1141 O  O   . GLY   A 128 ? 0.3449 0.2006 0.1899 0.0217  -0.0362 0.0340  128 GLY   A O   
1142 N  N   . ASP   A 129 ? 0.3051 0.2007 0.1747 0.0530  -0.0250 0.0100  129 ASP   A N   
1143 C  CA  . ASP   A 129 ? 0.3528 0.2305 0.1822 0.0790  0.0119  0.0304  129 ASP   A CA  
1144 C  C   . ASP   A 129 ? 0.3388 0.2153 0.1852 0.0748  0.0154  0.0130  129 ASP   A C   
1145 O  O   . ASP   A 129 ? 0.3082 0.2335 0.1569 0.0708  0.0121  0.0166  129 ASP   A O   
1146 C  CB  . ASP   A 129 ? 0.3451 0.1964 0.1910 0.0926  0.0228  0.0114  129 ASP   A CB  
1147 C  CG  . ASP   A 129 ? 0.3709 0.2428 0.2946 0.1218  0.0100  -0.0239 129 ASP   A CG  
1148 O  OD1 . ASP   A 129 ? 0.3785 0.3023 0.2951 0.0849  -0.0076 0.0738  129 ASP   A OD1 
1149 O  OD2 . ASP   A 129 ? 0.2903 0.3174 0.3633 0.0758  -0.0463 0.0116  129 ASP   A OD2 
1150 N  N   . ALA   A 130 ? 0.3692 0.2119 0.1741 0.0927  0.0287  0.0201  130 ALA   A N   
1151 C  CA  . ALA   A 130 ? 0.3228 0.2176 0.1602 0.0852  0.0120  0.0191  130 ALA   A CA  
1152 C  C   . ALA   A 130 ? 0.2906 0.1957 0.2117 0.0326  0.0368  0.0001  130 ALA   A C   
1153 O  O   . ALA   A 130 ? 0.2501 0.1936 0.2226 0.0033  -0.0006 -0.0066 130 ALA   A O   
1154 C  CB  . ALA   A 130 ? 0.3059 0.2117 0.1807 0.0801  0.0036  0.0059  130 ALA   A CB  
1155 N  N   . SER   A 131 ? 0.3362 0.2330 0.2451 0.0381  0.0585  0.0170  131 SER   A N   
1156 C  CA  . SER   A 131 ? 0.3395 0.2802 0.2919 0.0137  0.0987  0.0089  131 SER   A CA  
1157 C  C   . SER   A 131 ? 0.2554 0.2262 0.2479 0.0061  0.0963  0.0144  131 SER   A C   
1158 O  O   . SER   A 131 ? 0.2682 0.2568 0.3473 -0.0023 0.0705  -0.0024 131 SER   A O   
1159 C  CB  . SER   A 131 ? 0.3910 0.3943 0.3048 0.0146  0.1516  0.0141  131 SER   A CB  
1160 O  OG  . SER   A 131 ? 0.5751 0.4814 0.3614 -0.0305 0.1617  -0.0157 131 SER   A OG  
1161 N  N   . LYS   A 132 ? 0.2410 0.2255 0.2837 -0.0020 0.0705  0.0225  132 LYS   A N   
1162 C  CA  . LYS   A 132 ? 0.2141 0.2005 0.3154 -0.0147 0.0471  0.0000  132 LYS   A CA  
1163 C  C   . LYS   A 132 ? 0.1609 0.2045 0.2580 -0.0489 0.0360  -0.0219 132 LYS   A C   
1164 O  O   . LYS   A 132 ? 0.1829 0.2600 0.2704 -0.0527 0.0139  -0.0321 132 LYS   A O   
1165 C  CB  . LYS   A 132 ? 0.2012 0.2041 0.3751 -0.0235 0.0449  -0.0208 132 LYS   A CB  
1166 C  CG  . LYS   A 132 ? 0.2847 0.2892 0.4477 0.0031  0.0427  0.0166  132 LYS   A CG  
1167 C  CD  . LYS   A 132 ? 0.2990 0.3755 0.5002 0.0055  0.0396  0.0431  132 LYS   A CD  
1168 N  N   . ALA   A 133 ? 0.1649 0.1852 0.2239 -0.0343 0.0106  -0.0221 133 ALA   A N   
1169 C  CA  . ALA   A 133 ? 0.1647 0.1870 0.1721 -0.0271 -0.0071 -0.0106 133 ALA   A CA  
1170 C  C   . ALA   A 133 ? 0.1581 0.1979 0.1794 -0.0196 0.0011  -0.0134 133 ALA   A C   
1171 O  O   . ALA   A 133 ? 0.1412 0.2048 0.1810 -0.0146 -0.0189 -0.0173 133 ALA   A O   
1172 C  CB  . ALA   A 133 ? 0.1569 0.1761 0.1719 -0.0245 -0.0156 -0.0056 133 ALA   A CB  
1173 N  N   A SER   A 134 ? 0.1656 0.1911 0.1748 -0.0011 0.0049  0.0094  134 SER   A N   
1174 N  N   B SER   A 134 ? 0.1787 0.2095 0.1877 -0.0016 0.0014  -0.0017 134 SER   A N   
1175 C  CA  A SER   A 134 ? 0.1692 0.1961 0.1943 0.0045  0.0036  -0.0027 134 SER   A CA  
1176 C  CA  B SER   A 134 ? 0.1933 0.2243 0.2298 0.0060  -0.0102 -0.0209 134 SER   A CA  
1177 C  C   A SER   A 134 ? 0.1713 0.2053 0.1916 0.0073  0.0046  0.0095  134 SER   A C   
1178 C  C   B SER   A 134 ? 0.1929 0.2330 0.2191 -0.0005 -0.0072 -0.0116 134 SER   A C   
1179 O  O   A SER   A 134 ? 0.1642 0.1987 0.2299 -0.0008 0.0181  0.0333  134 SER   A O   
1180 O  O   B SER   A 134 ? 0.1686 0.2376 0.2448 -0.0227 -0.0213 -0.0118 134 SER   A O   
1181 C  CB  A SER   A 134 ? 0.1695 0.2098 0.2043 0.0043  0.0251  -0.0025 134 SER   A CB  
1182 C  CB  B SER   A 134 ? 0.2228 0.2598 0.2611 0.0181  0.0163  -0.0326 134 SER   A CB  
1183 O  OG  A SER   A 134 ? 0.1465 0.2055 0.1752 0.0053  0.0246  0.0003  134 SER   A OG  
1184 O  OG  B SER   A 134 ? 0.2359 0.3064 0.3148 0.0339  0.0048  -0.0406 134 SER   A OG  
1185 N  N   . GLN   A 135 ? 0.1533 0.2268 0.2429 -0.0024 -0.0059 0.0024  135 GLN   A N   
1186 C  CA  . GLN   A 135 ? 0.1583 0.2690 0.2648 -0.0289 -0.0070 -0.0121 135 GLN   A CA  
1187 C  C   . GLN   A 135 ? 0.1448 0.2912 0.2272 -0.0252 -0.0301 -0.0002 135 GLN   A C   
1188 O  O   . GLN   A 135 ? 0.1639 0.4014 0.2592 -0.0403 -0.0467 -0.0018 135 GLN   A O   
1189 C  CB  . GLN   A 135 ? 0.2118 0.3056 0.3243 -0.0511 -0.0152 0.0165  135 GLN   A CB  
1190 C  CG  . GLN   A 135 ? 0.2559 0.3612 0.3602 -0.0724 0.0183  0.0269  135 GLN   A CG  
1191 C  CD  . GLN   A 135 ? 0.3423 0.4409 0.3772 -0.0281 0.0298  0.0283  135 GLN   A CD  
1192 O  OE1 . GLN   A 135 ? 0.4169 0.6327 0.4942 0.0276  -0.0241 -0.0092 135 GLN   A OE1 
1193 N  NE2 . GLN   A 135 ? 0.5365 0.4996 0.4517 -0.0010 0.0677  0.0466  135 GLN   A NE2 
1194 N  N   . GLN   A 136 ? 0.1381 0.2215 0.1899 -0.0230 -0.0141 -0.0226 136 GLN   A N   
1195 C  CA  . GLN   A 136 ? 0.1409 0.2029 0.1796 -0.0038 -0.0452 -0.0336 136 GLN   A CA  
1196 C  C   . GLN   A 136 ? 0.1259 0.2230 0.1803 -0.0131 -0.0383 -0.0463 136 GLN   A C   
1197 O  O   . GLN   A 136 ? 0.1451 0.2121 0.1790 -0.0199 -0.0444 -0.0459 136 GLN   A O   
1198 C  CB  . GLN   A 136 ? 0.1621 0.1909 0.2022 -0.0012 -0.0280 -0.0255 136 GLN   A CB  
1199 C  CG  . GLN   A 136 ? 0.2182 0.2220 0.2155 0.0080  -0.0245 -0.0219 136 GLN   A CG  
1200 C  CD  . GLN   A 136 ? 0.2375 0.2839 0.2673 -0.0316 -0.0381 0.0475  136 GLN   A CD  
1201 O  OE1 . GLN   A 136 ? 0.3056 0.2603 0.2809 -0.0532 -0.0648 -0.0396 136 GLN   A OE1 
1202 N  NE2 . GLN   A 136 ? 0.3053 0.3939 0.3896 -0.0186 0.0088  0.0733  136 GLN   A NE2 
1203 N  N   . PRO   A 137 ? 0.1622 0.2515 0.1741 -0.0295 -0.0524 -0.0402 137 PRO   A N   
1204 C  CA  . PRO   A 137 ? 0.1830 0.2541 0.1743 -0.0028 -0.0710 -0.0125 137 PRO   A CA  
1205 C  C   . PRO   A 137 ? 0.1805 0.2221 0.1626 -0.0038 -0.0461 -0.0152 137 PRO   A C   
1206 O  O   . PRO   A 137 ? 0.2066 0.2325 0.2525 -0.0002 -0.0448 0.0056  137 PRO   A O   
1207 C  CB  . PRO   A 137 ? 0.2244 0.3120 0.1813 -0.0125 -0.0668 -0.0154 137 PRO   A CB  
1208 C  CG  . PRO   A 137 ? 0.2928 0.3268 0.2030 -0.0315 -0.0610 -0.0475 137 PRO   A CG  
1209 C  CD  . PRO   A 137 ? 0.2046 0.2719 0.2142 -0.0343 -0.0679 -0.0403 137 PRO   A CD  
1210 N  N   . ASP   A 138 ? 0.1653 0.1926 0.1518 -0.0079 -0.0443 -0.0039 138 ASP   A N   
1211 C  CA  . ASP   A 138 ? 0.1537 0.2031 0.1491 -0.0072 -0.0324 -0.0114 138 ASP   A CA  
1212 C  C   . ASP   A 138 ? 0.1501 0.1813 0.1548 -0.0090 -0.0279 -0.0161 138 ASP   A C   
1213 O  O   . ASP   A 138 ? 0.1369 0.2002 0.1688 -0.0006 -0.0224 0.0023  138 ASP   A O   
1214 C  CB  . ASP   A 138 ? 0.1818 0.2595 0.1485 -0.0054 -0.0240 -0.0095 138 ASP   A CB  
1215 C  CG  . ASP   A 138 ? 0.1808 0.2654 0.1538 0.0269  -0.0229 -0.0426 138 ASP   A CG  
1216 O  OD1 . ASP   A 138 ? 0.2164 0.2352 0.1853 0.0189  -0.0112 -0.0530 138 ASP   A OD1 
1217 O  OD2 . ASP   A 138 ? 0.2001 0.3076 0.2379 0.0079  0.0074  -0.0854 138 ASP   A OD2 
1218 N  N   . GLY   A 139 ? 0.1348 0.1702 0.1420 0.0070  -0.0386 -0.0173 139 GLY   A N   
1219 C  CA  . GLY   A 139 ? 0.1292 0.1490 0.1415 -0.0041 -0.0363 -0.0141 139 GLY   A CA  
1220 C  C   . GLY   A 139 ? 0.1186 0.1427 0.1467 -0.0092 -0.0428 -0.0045 139 GLY   A C   
1221 O  O   . GLY   A 139 ? 0.1304 0.1472 0.1429 0.0018  -0.0372 -0.0066 139 GLY   A O   
1222 N  N   . LEU   A 140 ? 0.1080 0.1377 0.1378 -0.0004 -0.0350 -0.0087 140 LEU   A N   
1223 C  CA  . LEU   A 140 ? 0.1123 0.1311 0.1258 0.0118  -0.0385 -0.0072 140 LEU   A CA  
1224 C  C   . LEU   A 140 ? 0.1131 0.1324 0.1276 0.0002  -0.0288 -0.0103 140 LEU   A C   
1225 O  O   . LEU   A 140 ? 0.1077 0.1536 0.1377 0.0032  -0.0258 -0.0014 140 LEU   A O   
1226 C  CB  . LEU   A 140 ? 0.1162 0.1359 0.1391 -0.0016 -0.0239 -0.0214 140 LEU   A CB  
1227 C  CG  . LEU   A 140 ? 0.1497 0.1552 0.1607 0.0069  -0.0064 -0.0053 140 LEU   A CG  
1228 C  CD1 . LEU   A 140 ? 0.1571 0.1830 0.1681 0.0055  0.0115  0.0089  140 LEU   A CD1 
1229 C  CD2 . LEU   A 140 ? 0.1604 0.1725 0.1828 0.0026  0.0009  0.0099  140 LEU   A CD2 
1230 N  N   . ALA   A 141 ? 0.1123 0.1331 0.1482 0.0034  -0.0376 -0.0062 141 ALA   A N   
1231 C  CA  . ALA   A 141 ? 0.1105 0.1450 0.1472 0.0066  -0.0329 -0.0047 141 ALA   A CA  
1232 C  C   . ALA   A 141 ? 0.1042 0.1416 0.1208 -0.0101 -0.0318 0.0033  141 ALA   A C   
1233 O  O   . ALA   A 141 ? 0.1388 0.1537 0.1204 -0.0117 -0.0401 0.0080  141 ALA   A O   
1234 C  CB  . ALA   A 141 ? 0.1121 0.1606 0.1713 -0.0063 -0.0295 -0.0091 141 ALA   A CB  
1235 N  N   . VAL   A 142 ? 0.1046 0.1428 0.1126 0.0023  -0.0309 -0.0039 142 VAL   A N   
1236 C  CA  . VAL   A 142 ? 0.1067 0.1418 0.1203 0.0097  -0.0250 -0.0052 142 VAL   A CA  
1237 C  C   . VAL   A 142 ? 0.1050 0.1382 0.1217 -0.0012 -0.0268 0.0007  142 VAL   A C   
1238 O  O   . VAL   A 142 ? 0.1038 0.1619 0.1054 -0.0044 -0.0298 -0.0004 142 VAL   A O   
1239 C  CB  . VAL   A 142 ? 0.0951 0.1525 0.1199 0.0110  -0.0239 0.0079  142 VAL   A CB  
1240 C  CG1 . VAL   A 142 ? 0.1028 0.1661 0.1307 0.0193  -0.0292 -0.0009 142 VAL   A CG1 
1241 C  CG2 . VAL   A 142 ? 0.0936 0.1821 0.1296 0.0007  -0.0226 0.0246  142 VAL   A CG2 
1242 N  N   . LEU   A 143 ? 0.1018 0.1273 0.1228 0.0011  -0.0321 0.0098  143 LEU   A N   
1243 C  CA  . LEU   A 143 ? 0.0991 0.1383 0.1373 -0.0027 -0.0271 0.0139  143 LEU   A CA  
1244 C  C   . LEU   A 143 ? 0.0932 0.1347 0.1082 -0.0214 -0.0144 0.0125  143 LEU   A C   
1245 O  O   . LEU   A 143 ? 0.1088 0.1512 0.1196 -0.0145 -0.0171 0.0070  143 LEU   A O   
1246 C  CB  . LEU   A 143 ? 0.1084 0.1591 0.1315 -0.0058 -0.0247 0.0049  143 LEU   A CB  
1247 C  CG  . LEU   A 143 ? 0.1055 0.1704 0.1672 -0.0050 -0.0176 0.0048  143 LEU   A CG  
1248 C  CD1 . LEU   A 143 ? 0.1249 0.2118 0.1900 -0.0182 -0.0224 0.0270  143 LEU   A CD1 
1249 C  CD2 . LEU   A 143 ? 0.1137 0.1912 0.1815 0.0000  -0.0346 0.0158  143 LEU   A CD2 
1250 N  N   . GLY   A 144 ? 0.0925 0.1427 0.1125 -0.0114 -0.0194 -0.0035 144 GLY   A N   
1251 C  CA  . GLY   A 144 ? 0.0788 0.1418 0.1273 0.0033  -0.0192 0.0048  144 GLY   A CA  
1252 C  C   . GLY   A 144 ? 0.0977 0.1393 0.1020 0.0062  -0.0231 0.0068  144 GLY   A C   
1253 O  O   . GLY   A 144 ? 0.1076 0.1479 0.1132 -0.0154 -0.0154 -0.0005 144 GLY   A O   
1254 N  N   . ILE   A 145 ? 0.0903 0.1413 0.1032 -0.0038 -0.0136 0.0088  145 ILE   A N   
1255 C  CA  . ILE   A 145 ? 0.0881 0.1416 0.1190 -0.0096 -0.0267 0.0234  145 ILE   A CA  
1256 C  C   . ILE   A 145 ? 0.0879 0.1478 0.1076 -0.0078 -0.0255 0.0086  145 ILE   A C   
1257 O  O   . ILE   A 145 ? 0.1121 0.1551 0.1196 -0.0097 -0.0134 0.0035  145 ILE   A O   
1258 C  CB  . ILE   A 145 ? 0.0892 0.1564 0.1394 -0.0087 -0.0408 0.0228  145 ILE   A CB  
1259 C  CG1 . ILE   A 145 ? 0.0967 0.1820 0.1585 0.0030  -0.0342 0.0139  145 ILE   A CG1 
1260 C  CG2 . ILE   A 145 ? 0.1002 0.1677 0.1746 -0.0111 -0.0573 0.0149  145 ILE   A CG2 
1261 C  CD1 . ILE   A 145 ? 0.1096 0.1604 0.1576 -0.0052 -0.0287 0.0326  145 ILE   A CD1 
1262 N  N   . PHE   A 146 ? 0.1030 0.1433 0.1109 -0.0158 -0.0107 -0.0013 146 PHE   A N   
1263 C  CA  . PHE   A 146 ? 0.0967 0.1499 0.1264 -0.0021 -0.0125 -0.0078 146 PHE   A CA  
1264 C  C   . PHE   A 146 ? 0.1128 0.1482 0.1400 -0.0026 -0.0223 -0.0088 146 PHE   A C   
1265 O  O   . PHE   A 146 ? 0.1067 0.1708 0.1320 -0.0024 -0.0228 -0.0060 146 PHE   A O   
1266 C  CB  . PHE   A 146 ? 0.1027 0.1465 0.1280 -0.0064 -0.0167 -0.0061 146 PHE   A CB  
1267 C  CG  . PHE   A 146 ? 0.1118 0.1524 0.1132 -0.0002 -0.0140 0.0000  146 PHE   A CG  
1268 C  CD1 . PHE   A 146 ? 0.1065 0.1747 0.1043 0.0008  -0.0251 -0.0097 146 PHE   A CD1 
1269 C  CD2 . PHE   A 146 ? 0.1236 0.1530 0.1082 -0.0022 -0.0168 0.0099  146 PHE   A CD2 
1270 C  CE1 . PHE   A 146 ? 0.1200 0.1538 0.1189 0.0011  -0.0398 -0.0036 146 PHE   A CE1 
1271 C  CE2 . PHE   A 146 ? 0.1298 0.1778 0.1111 -0.0014 -0.0062 -0.0070 146 PHE   A CE2 
1272 C  CZ  . PHE   A 146 ? 0.1218 0.1717 0.1177 -0.0019 -0.0252 0.0112  146 PHE   A CZ  
1273 N  N   . LEU   A 147 ? 0.1087 0.1453 0.1386 -0.0020 -0.0320 -0.0117 147 LEU   A N   
1274 C  CA  . LEU   A 147 ? 0.1123 0.1540 0.1327 -0.0038 -0.0397 -0.0149 147 LEU   A CA  
1275 C  C   . LEU   A 147 ? 0.1374 0.1540 0.1365 -0.0077 -0.0405 -0.0159 147 LEU   A C   
1276 O  O   . LEU   A 147 ? 0.1280 0.1721 0.1432 -0.0153 -0.0294 -0.0073 147 LEU   A O   
1277 C  CB  . LEU   A 147 ? 0.1289 0.1411 0.1494 -0.0180 -0.0318 -0.0137 147 LEU   A CB  
1278 C  CG  . LEU   A 147 ? 0.1285 0.1556 0.1235 -0.0281 -0.0419 -0.0048 147 LEU   A CG  
1279 C  CD1 . LEU   A 147 ? 0.1695 0.1727 0.1382 -0.0167 -0.0514 -0.0052 147 LEU   A CD1 
1280 C  CD2 . LEU   A 147 ? 0.1422 0.1731 0.1378 -0.0194 -0.0366 -0.0003 147 LEU   A CD2 
1281 N  N   . LYS   A 148 ? 0.1301 0.1541 0.1556 -0.0169 -0.0405 0.0003  148 LYS   A N   
1282 C  CA  . LYS   A 148 ? 0.1546 0.1560 0.1687 -0.0223 -0.0591 0.0056  148 LYS   A CA  
1283 C  C   . LYS   A 148 ? 0.1658 0.1510 0.1857 -0.0106 -0.0650 0.0048  148 LYS   A C   
1284 O  O   . LYS   A 148 ? 0.1871 0.1770 0.1809 0.0112  -0.0845 -0.0029 148 LYS   A O   
1285 C  CB  . LYS   A 148 ? 0.1883 0.1920 0.1807 -0.0331 -0.0519 0.0178  148 LYS   A CB  
1286 C  CG  . LYS   A 148 ? 0.2172 0.2280 0.2167 -0.0533 -0.0459 0.0258  148 LYS   A CG  
1287 C  CD  . LYS   A 148 ? 0.3404 0.2549 0.2690 -0.0470 -0.0071 0.0494  148 LYS   A CD  
1288 N  N   . VAL   A 149 ? 0.1807 0.1486 0.2009 -0.0001 -0.0842 -0.0006 149 VAL   A N   
1289 C  CA  . VAL   A 149 ? 0.1831 0.1302 0.2111 0.0023  -0.0840 -0.0082 149 VAL   A CA  
1290 C  C   . VAL   A 149 ? 0.2086 0.1707 0.2092 -0.0133 -0.0702 0.0104  149 VAL   A C   
1291 O  O   . VAL   A 149 ? 0.2366 0.1964 0.2065 -0.0144 -0.0768 0.0238  149 VAL   A O   
1292 C  CB  . VAL   A 149 ? 0.2026 0.1487 0.2020 0.0207  -0.0912 0.0063  149 VAL   A CB  
1293 C  CG1 . VAL   A 149 ? 0.2226 0.2103 0.1957 0.0190  -0.0992 -0.0055 149 VAL   A CG1 
1294 C  CG2 . VAL   A 149 ? 0.1888 0.1804 0.2243 0.0103  -0.0671 0.0182  149 VAL   A CG2 
1295 N  N   . GLY   A 150 ? 0.2125 0.1572 0.1986 -0.0314 -0.0812 0.0191  150 GLY   A N   
1296 C  CA  . GLY   A 150 ? 0.2127 0.1862 0.2224 -0.0481 -0.0772 0.0342  150 GLY   A CA  
1297 C  C   . GLY   A 150 ? 0.2201 0.1897 0.1831 -0.0511 -0.0682 0.0175  150 GLY   A C   
1298 O  O   . GLY   A 150 ? 0.2127 0.2153 0.1867 -0.0659 -0.0689 0.0047  150 GLY   A O   
1299 N  N   A SER   A 151 ? 0.2176 0.1977 0.1969 -0.0562 -0.0814 0.0123  151 SER   A N   
1300 N  N   B SER   A 151 ? 0.2132 0.2012 0.1980 -0.0550 -0.0773 0.0135  151 SER   A N   
1301 C  CA  A SER   A 151 ? 0.2033 0.2192 0.2026 -0.0486 -0.0674 0.0076  151 SER   A CA  
1302 C  CA  B SER   A 151 ? 0.1983 0.2270 0.1949 -0.0456 -0.0621 0.0076  151 SER   A CA  
1303 C  C   A SER   A 151 ? 0.1831 0.2082 0.1812 -0.0419 -0.0705 0.0046  151 SER   A C   
1304 C  C   B SER   A 151 ? 0.1730 0.2015 0.1753 -0.0321 -0.0648 -0.0048 151 SER   A C   
1305 O  O   A SER   A 151 ? 0.1690 0.2093 0.1760 -0.0412 -0.0688 0.0065  151 SER   A O   
1306 O  O   B SER   A 151 ? 0.1763 0.2033 0.1564 -0.0218 -0.0504 -0.0303 151 SER   A O   
1307 C  CB  A SER   A 151 ? 0.2161 0.2394 0.2328 -0.0492 -0.0471 0.0043  151 SER   A CB  
1308 C  CB  B SER   A 151 ? 0.1966 0.2617 0.2394 -0.0503 -0.0532 0.0260  151 SER   A CB  
1309 O  OG  A SER   A 151 ? 0.2232 0.2769 0.2790 -0.0535 -0.0315 0.0222  151 SER   A OG  
1310 O  OG  B SER   A 151 ? 0.2273 0.3016 0.2777 -0.0397 -0.0536 0.0180  151 SER   A OG  
1311 N  N   . ALA   A 152 ? 0.1849 0.2067 0.1773 -0.0420 -0.0721 -0.0066 152 ALA   A N   
1312 C  CA  . ALA   A 152 ? 0.1840 0.2084 0.1665 -0.0265 -0.0662 0.0054  152 ALA   A CA  
1313 C  C   . ALA   A 152 ? 0.1574 0.2076 0.1571 -0.0294 -0.0460 0.0090  152 ALA   A C   
1314 O  O   . ALA   A 152 ? 0.1786 0.2032 0.2009 -0.0325 -0.0352 -0.0069 152 ALA   A O   
1315 C  CB  . ALA   A 152 ? 0.2412 0.2262 0.1771 -0.0153 -0.0819 0.0099  152 ALA   A CB  
1316 N  N   . LYS   A 153 ? 0.1532 0.1819 0.1604 -0.0148 -0.0452 0.0022  153 LYS   A N   
1317 C  CA  . LYS   A 153 ? 0.1654 0.1847 0.1550 -0.0204 -0.0437 0.0135  153 LYS   A CA  
1318 C  C   . LYS   A 153 ? 0.1431 0.1924 0.1589 -0.0215 -0.0578 0.0106  153 LYS   A C   
1319 O  O   . LYS   A 153 ? 0.1534 0.1943 0.1591 -0.0173 -0.0446 0.0136  153 LYS   A O   
1320 C  CB  . LYS   A 153 ? 0.1639 0.1885 0.1836 -0.0148 -0.0532 -0.0012 153 LYS   A CB  
1321 C  CG  . LYS   A 153 ? 0.2303 0.1968 0.1608 -0.0159 -0.0643 0.0070  153 LYS   A CG  
1322 C  CD  . LYS   A 153 ? 0.2734 0.2038 0.1621 -0.0102 -0.0595 0.0030  153 LYS   A CD  
1323 C  CE  . LYS   A 153 ? 0.3457 0.2316 0.1907 0.0118  -0.0239 -0.0079 153 LYS   A CE  
1324 N  NZ  . LYS   A 153 ? 0.4127 0.2453 0.2178 -0.0147 -0.0070 -0.0195 153 LYS   A NZ  
1325 N  N   . PRO   A 154 ? 0.1316 0.2153 0.1875 -0.0233 -0.0555 0.0164  154 PRO   A N   
1326 C  CA  . PRO   A 154 ? 0.1281 0.2296 0.2039 -0.0196 -0.0491 0.0319  154 PRO   A CA  
1327 C  C   . PRO   A 154 ? 0.1137 0.2263 0.2110 -0.0011 -0.0286 0.0273  154 PRO   A C   
1328 O  O   . PRO   A 154 ? 0.1407 0.2274 0.1999 -0.0042 -0.0301 0.0251  154 PRO   A O   
1329 C  CB  . PRO   A 154 ? 0.1333 0.2672 0.2713 -0.0071 -0.0572 0.0555  154 PRO   A CB  
1330 C  CG  . PRO   A 154 ? 0.1762 0.3061 0.2939 -0.0158 -0.0588 0.0624  154 PRO   A CG  
1331 C  CD  . PRO   A 154 ? 0.1547 0.2621 0.2418 -0.0272 -0.0484 0.0473  154 PRO   A CD  
1332 N  N   . GLY   A 155 ? 0.1482 0.2209 0.2048 -0.0002 -0.0356 0.0292  155 GLY   A N   
1333 C  CA  . GLY   A 155 ? 0.1478 0.2137 0.2361 0.0063  -0.0144 0.0461  155 GLY   A CA  
1334 C  C   . GLY   A 155 ? 0.1530 0.1758 0.2267 -0.0134 -0.0196 0.0371  155 GLY   A C   
1335 O  O   . GLY   A 155 ? 0.1809 0.1728 0.2982 -0.0193 -0.0316 0.0267  155 GLY   A O   
1336 N  N   . LEU   A 156 ? 0.1427 0.1681 0.1876 -0.0165 -0.0384 0.0192  156 LEU   A N   
1337 C  CA  . LEU   A 156 ? 0.1321 0.1717 0.1779 -0.0220 -0.0532 0.0041  156 LEU   A CA  
1338 C  C   . LEU   A 156 ? 0.1448 0.1735 0.1657 -0.0313 -0.0558 0.0138  156 LEU   A C   
1339 O  O   . LEU   A 156 ? 0.1316 0.1925 0.1633 -0.0311 -0.0569 0.0153  156 LEU   A O   
1340 C  CB  . LEU   A 156 ? 0.1415 0.1684 0.1629 -0.0271 -0.0546 0.0013  156 LEU   A CB  
1341 C  CG  . LEU   A 156 ? 0.1344 0.1850 0.1594 -0.0135 -0.0588 0.0036  156 LEU   A CG  
1342 C  CD1 . LEU   A 156 ? 0.1144 0.1930 0.1876 -0.0037 -0.0717 -0.0041 156 LEU   A CD1 
1343 C  CD2 . LEU   A 156 ? 0.1391 0.1950 0.1799 -0.0038 -0.0586 -0.0007 156 LEU   A CD2 
1344 N  N   . GLN   A 157 ? 0.1252 0.1928 0.1732 -0.0251 -0.0481 -0.0023 157 GLN   A N   
1345 C  CA  . GLN   A 157 ? 0.1241 0.1979 0.1624 -0.0276 -0.0588 -0.0099 157 GLN   A CA  
1346 C  C   . GLN   A 157 ? 0.1242 0.2172 0.1487 -0.0212 -0.0510 -0.0158 157 GLN   A C   
1347 O  O   . GLN   A 157 ? 0.1325 0.2264 0.1564 -0.0307 -0.0555 0.0056  157 GLN   A O   
1348 C  CB  . GLN   A 157 ? 0.1572 0.2027 0.1868 -0.0354 -0.0665 -0.0069 157 GLN   A CB  
1349 C  CG  . GLN   A 157 ? 0.2081 0.2226 0.1727 -0.0426 -0.0656 -0.0109 157 GLN   A CG  
1350 C  CD  . GLN   A 157 ? 0.2166 0.1850 0.1492 -0.0546 -0.0479 -0.0117 157 GLN   A CD  
1351 O  OE1 . GLN   A 157 ? 0.2277 0.2088 0.1550 -0.0204 -0.0447 0.0021  157 GLN   A OE1 
1352 N  NE2 . GLN   A 157 ? 0.2283 0.2240 0.1598 -0.0369 -0.0537 -0.0223 157 GLN   A NE2 
1353 N  N   . LYS   A 158 ? 0.1309 0.2251 0.1723 -0.0258 -0.0483 0.0053  158 LYS   A N   
1354 C  CA  . LYS   A 158 ? 0.1488 0.2320 0.1557 -0.0280 -0.0473 -0.0078 158 LYS   A CA  
1355 C  C   . LYS   A 158 ? 0.1463 0.2174 0.1445 -0.0270 -0.0445 -0.0005 158 LYS   A C   
1356 O  O   . LYS   A 158 ? 0.1534 0.2228 0.1690 -0.0267 -0.0527 0.0107  158 LYS   A O   
1357 C  CB  . LYS   A 158 ? 0.1800 0.2363 0.2248 -0.0292 -0.0728 0.0172  158 LYS   A CB  
1358 C  CG  . LYS   A 158 ? 0.2357 0.2991 0.2450 -0.0266 -0.0539 0.0230  158 LYS   A CG  
1359 N  N   . VAL   A 159 ? 0.1342 0.2056 0.1467 -0.0216 -0.0378 -0.0076 159 VAL   A N   
1360 C  CA  . VAL   A 159 ? 0.1285 0.2026 0.1623 -0.0330 -0.0417 -0.0100 159 VAL   A CA  
1361 C  C   . VAL   A 159 ? 0.1280 0.2136 0.1366 -0.0110 -0.0388 -0.0036 159 VAL   A C   
1362 O  O   . VAL   A 159 ? 0.1383 0.2266 0.1729 -0.0217 -0.0367 0.0065  159 VAL   A O   
1363 C  CB  . VAL   A 159 ? 0.1461 0.2345 0.1548 -0.0309 -0.0483 -0.0112 159 VAL   A CB  
1364 C  CG1 . VAL   A 159 ? 0.1680 0.2712 0.1776 -0.0358 -0.0704 0.0015  159 VAL   A CG1 
1365 C  CG2 . VAL   A 159 ? 0.1831 0.2397 0.1673 -0.0046 -0.0632 -0.0093 159 VAL   A CG2 
1366 N  N   A VAL   A 160 ? 0.1293 0.2129 0.1650 -0.0120 -0.0448 0.0006  160 VAL   A N   
1367 N  N   B VAL   A 160 ? 0.1227 0.1994 0.1513 -0.0102 -0.0490 -0.0011 160 VAL   A N   
1368 C  CA  A VAL   A 160 ? 0.1613 0.2018 0.1717 -0.0230 -0.0352 -0.0112 160 VAL   A CA  
1369 C  CA  B VAL   A 160 ? 0.1443 0.1781 0.1566 -0.0271 -0.0407 -0.0070 160 VAL   A CA  
1370 C  C   A VAL   A 160 ? 0.1731 0.2226 0.1814 -0.0180 -0.0437 -0.0062 160 VAL   A C   
1371 C  C   B VAL   A 160 ? 0.1659 0.2039 0.1658 -0.0249 -0.0444 -0.0089 160 VAL   A C   
1372 O  O   A VAL   A 160 ? 0.1785 0.2222 0.1969 -0.0103 -0.0323 -0.0179 160 VAL   A O   
1373 O  O   B VAL   A 160 ? 0.1868 0.2085 0.1720 -0.0243 -0.0183 -0.0208 160 VAL   A O   
1374 C  CB  A VAL   A 160 ? 0.1774 0.2085 0.1994 -0.0056 -0.0271 -0.0075 160 VAL   A CB  
1375 C  CB  B VAL   A 160 ? 0.1327 0.1735 0.1654 -0.0225 -0.0507 0.0009  160 VAL   A CB  
1376 C  CG1 A VAL   A 160 ? 0.2033 0.2128 0.2031 0.0000  -0.0115 0.0006  160 VAL   A CG1 
1377 C  CG1 B VAL   A 160 ? 0.1571 0.1635 0.1499 -0.0174 -0.0622 0.0141  160 VAL   A CG1 
1378 C  CG2 A VAL   A 160 ? 0.1651 0.2119 0.2027 -0.0114 -0.0279 -0.0032 160 VAL   A CG2 
1379 C  CG2 B VAL   A 160 ? 0.1438 0.1706 0.1670 -0.0270 -0.0414 0.0086  160 VAL   A CG2 
1380 N  N   . ASP   A 161 ? 0.1823 0.2277 0.1513 -0.0393 -0.0613 -0.0107 161 ASP   A N   
1381 C  CA  . ASP   A 161 ? 0.1947 0.2471 0.1651 -0.0417 -0.0493 -0.0191 161 ASP   A CA  
1382 C  C   . ASP   A 161 ? 0.2047 0.2649 0.1643 -0.0342 -0.0394 -0.0054 161 ASP   A C   
1383 O  O   . ASP   A 161 ? 0.3182 0.3715 0.1900 -0.1008 0.0144  -0.0233 161 ASP   A O   
1384 C  CB  . ASP   A 161 ? 0.2151 0.3272 0.1694 -0.0506 -0.0712 -0.0237 161 ASP   A CB  
1385 C  CG  . ASP   A 161 ? 0.2066 0.3291 0.2075 -0.0674 -0.0567 -0.0409 161 ASP   A CG  
1386 O  OD1 . ASP   A 161 ? 0.3010 0.3252 0.2709 -0.0889 -0.0569 -0.0077 161 ASP   A OD1 
1387 O  OD2 . ASP   A 161 ? 0.2064 0.3810 0.2267 -0.0593 -0.0408 -0.0133 161 ASP   A OD2 
1388 N  N   . VAL   A 162 ? 0.1819 0.2386 0.1543 -0.0368 -0.0566 0.0092  162 VAL   A N   
1389 C  CA  . VAL   A 162 ? 0.1815 0.2675 0.1771 -0.0224 -0.0483 0.0288  162 VAL   A CA  
1390 C  C   . VAL   A 162 ? 0.1802 0.2503 0.1439 -0.0205 -0.0377 0.0293  162 VAL   A C   
1391 O  O   . VAL   A 162 ? 0.1849 0.2739 0.1528 -0.0459 -0.0295 0.0209  162 VAL   A O   
1392 C  CB  . VAL   A 162 ? 0.1888 0.2697 0.2249 0.0007  -0.0342 0.0262  162 VAL   A CB  
1393 C  CG1 . VAL   A 162 ? 0.2197 0.2483 0.2312 -0.0184 -0.0077 0.0098  162 VAL   A CG1 
1394 C  CG2 . VAL   A 162 ? 0.2278 0.3252 0.2636 0.0030  -0.0260 0.0251  162 VAL   A CG2 
1395 N  N   . LEU   A 163 ? 0.1599 0.2377 0.1643 -0.0247 -0.0465 0.0187  163 LEU   A N   
1396 C  CA  . LEU   A 163 ? 0.1622 0.2364 0.1555 -0.0242 -0.0389 -0.0067 163 LEU   A CA  
1397 C  C   . LEU   A 163 ? 0.1839 0.2753 0.1473 -0.0397 -0.0149 -0.0132 163 LEU   A C   
1398 O  O   . LEU   A 163 ? 0.1672 0.2587 0.1967 -0.0157 -0.0144 -0.0077 163 LEU   A O   
1399 C  CB  . LEU   A 163 ? 0.1516 0.2382 0.1466 -0.0354 -0.0445 0.0078  163 LEU   A CB  
1400 C  CG  . LEU   A 163 ? 0.1457 0.2366 0.1457 -0.0177 -0.0369 0.0227  163 LEU   A CG  
1401 C  CD1 . LEU   A 163 ? 0.1278 0.2457 0.1810 -0.0191 -0.0222 0.0335  163 LEU   A CD1 
1402 C  CD2 . LEU   A 163 ? 0.1492 0.2520 0.1574 -0.0377 -0.0543 0.0124  163 LEU   A CD2 
1403 N  N   . ASP   A 164 ? 0.2422 0.2955 0.1526 -0.0476 -0.0157 -0.0208 164 ASP   A N   
1404 C  CA  . ASP   A 164 ? 0.2939 0.3345 0.1915 -0.0299 0.0222  -0.0428 164 ASP   A CA  
1405 C  C   . ASP   A 164 ? 0.2310 0.3540 0.1572 -0.0375 -0.0007 -0.0318 164 ASP   A C   
1406 O  O   . ASP   A 164 ? 0.3461 0.4636 0.2600 0.0043  0.0893  -0.0137 164 ASP   A O   
1407 C  CB  . ASP   A 164 ? 0.4035 0.3984 0.1831 -0.0544 0.0290  -0.1000 164 ASP   A CB  
1408 N  N   . SER   A 165 ? 0.2029 0.3449 0.1320 -0.0386 -0.0212 -0.0020 165 SER   A N   
1409 C  CA  . SER   A 165 ? 0.2238 0.3388 0.1417 -0.0339 -0.0232 0.0156  165 SER   A CA  
1410 C  C   . SER   A 165 ? 0.1928 0.3330 0.1543 -0.0381 -0.0233 0.0404  165 SER   A C   
1411 O  O   . SER   A 165 ? 0.2397 0.3551 0.1664 -0.0227 -0.0109 0.0564  165 SER   A O   
1412 C  CB  . SER   A 165 ? 0.2483 0.3324 0.1716 -0.0209 -0.0272 0.0461  165 SER   A CB  
1413 O  OG  . SER   A 165 ? 0.2469 0.3376 0.2282 -0.0064 -0.0370 0.0443  165 SER   A OG  
1414 N  N   . ILE   A 166 ? 0.1916 0.2726 0.1316 -0.0392 -0.0198 0.0250  166 ILE   A N   
1415 C  CA  . ILE   A 166 ? 0.1857 0.2746 0.1699 -0.0313 -0.0180 0.0134  166 ILE   A CA  
1416 C  C   . ILE   A 166 ? 0.1731 0.2581 0.1294 -0.0306 -0.0062 0.0062  166 ILE   A C   
1417 O  O   . ILE   A 166 ? 0.1725 0.2699 0.1384 -0.0398 -0.0062 0.0171  166 ILE   A O   
1418 C  CB  . ILE   A 166 ? 0.1658 0.2849 0.1676 -0.0216 -0.0311 0.0222  166 ILE   A CB  
1419 C  CG1 . ILE   A 166 ? 0.1417 0.2674 0.1641 -0.0260 -0.0300 0.0054  166 ILE   A CG1 
1420 C  CG2 . ILE   A 166 ? 0.1757 0.2934 0.1942 -0.0192 -0.0387 0.0212  166 ILE   A CG2 
1421 C  CD1 . ILE   A 166 ? 0.1626 0.2738 0.1776 -0.0081 -0.0226 -0.0044 166 ILE   A CD1 
1422 N  N   . LYS   A 167 ? 0.2182 0.2764 0.1318 -0.0214 -0.0040 0.0013  167 LYS   A N   
1423 C  CA  . LYS   A 167 ? 0.1904 0.2594 0.1775 -0.0335 -0.0079 -0.0094 167 LYS   A CA  
1424 C  C   . LYS   A 167 ? 0.2000 0.2640 0.1645 -0.0261 -0.0069 0.0123  167 LYS   A C   
1425 O  O   . LYS   A 167 ? 0.1866 0.2643 0.1693 -0.0218 0.0024  0.0071  167 LYS   A O   
1426 C  CB  . LYS   A 167 ? 0.2375 0.3175 0.2104 -0.0243 0.0164  -0.0240 167 LYS   A CB  
1427 C  CG  . LYS   A 167 ? 0.2860 0.3434 0.2511 -0.0180 -0.0267 -0.0427 167 LYS   A CG  
1428 C  CD  . LYS   A 167 ? 0.3752 0.4093 0.2872 -0.0018 -0.0593 -0.0749 167 LYS   A CD  
1429 C  CE  . LYS   A 167 ? 0.4789 0.4652 0.3989 -0.0007 -0.0481 -0.0704 167 LYS   A CE  
1430 N  NZ  . LYS   A 167 ? 0.5699 0.5794 0.4962 -0.0018 -0.0492 -0.0943 167 LYS   A NZ  
1431 N  N   . THR   A 168 ? 0.1947 0.2604 0.1603 -0.0439 -0.0051 0.0180  168 THR   A N   
1432 C  CA  . THR   A 168 ? 0.1982 0.2692 0.1927 -0.0278 0.0186  0.0152  168 THR   A CA  
1433 C  C   . THR   A 168 ? 0.1650 0.2526 0.1878 -0.0426 0.0055  0.0141  168 THR   A C   
1434 O  O   . THR   A 168 ? 0.1879 0.2491 0.1973 -0.0301 -0.0054 0.0142  168 THR   A O   
1435 C  CB  . THR   A 168 ? 0.2313 0.2959 0.1896 -0.0453 0.0374  0.0154  168 THR   A CB  
1436 O  OG1 . THR   A 168 ? 0.2413 0.3693 0.1713 -0.0403 0.0296  0.0287  168 THR   A OG1 
1437 C  CG2 . THR   A 168 ? 0.2621 0.2984 0.2069 -0.0312 0.0406  -0.0005 168 THR   A CG2 
1438 N  N   . LYS   A 169 ? 0.1781 0.2622 0.2168 -0.0339 0.0054  -0.0010 169 LYS   A N   
1439 C  CA  . LYS   A 169 ? 0.1682 0.2674 0.1966 -0.0165 0.0150  0.0214  169 LYS   A CA  
1440 C  C   . LYS   A 169 ? 0.1967 0.2824 0.2158 -0.0456 0.0028  0.0335  169 LYS   A C   
1441 O  O   . LYS   A 169 ? 0.2200 0.3107 0.1988 -0.0569 0.0028  0.0352  169 LYS   A O   
1442 C  CB  . LYS   A 169 ? 0.1544 0.2793 0.2272 -0.0155 0.0227  0.0207  169 LYS   A CB  
1443 C  CG  . LYS   A 169 ? 0.1775 0.2920 0.2627 -0.0302 -0.0106 0.0338  169 LYS   A CG  
1444 C  CD  . LYS   A 169 ? 0.2386 0.3743 0.3064 -0.0300 -0.0470 0.0290  169 LYS   A CD  
1445 C  CE  . LYS   A 169 ? 0.2863 0.4493 0.4304 -0.0504 -0.0693 -0.0052 169 LYS   A CE  
1446 N  NZ  . LYS   A 169 ? 0.3119 0.5443 0.4904 0.0079  -0.0721 -0.0328 169 LYS   A NZ  
1447 N  N   . GLY   A 170 ? 0.1867 0.2556 0.2181 -0.0603 0.0093  0.0298  170 GLY   A N   
1448 C  CA  . GLY   A 170 ? 0.1925 0.2738 0.2554 -0.0609 -0.0208 0.0464  170 GLY   A CA  
1449 C  C   . GLY   A 170 ? 0.2036 0.2741 0.2277 -0.0579 -0.0006 0.0447  170 GLY   A C   
1450 O  O   . GLY   A 170 ? 0.3171 0.2798 0.3302 -0.0932 -0.0406 0.0748  170 GLY   A O   
1451 N  N   . LYS   A 171 ? 0.1886 0.2568 0.1981 -0.0384 -0.0085 0.0424  171 LYS   A N   
1452 C  CA  . LYS   A 171 ? 0.1945 0.2792 0.1854 -0.0002 0.0000  0.0477  171 LYS   A CA  
1453 C  C   . LYS   A 171 ? 0.2030 0.2660 0.1643 -0.0043 -0.0015 0.0518  171 LYS   A C   
1454 O  O   . LYS   A 171 ? 0.2019 0.2829 0.1560 -0.0055 0.0023  0.0471  171 LYS   A O   
1455 C  CB  . LYS   A 171 ? 0.1848 0.2918 0.2306 -0.0033 -0.0121 0.0181  171 LYS   A CB  
1456 C  CG  . LYS   A 171 ? 0.1904 0.3283 0.2777 -0.0263 0.0080  -0.0201 171 LYS   A CG  
1457 C  CD  . LYS   A 171 ? 0.2848 0.3516 0.3654 -0.0364 0.0151  -0.0289 171 LYS   A CD  
1458 N  N   . SER   A 172 ? 0.2224 0.2911 0.1485 0.0168  -0.0077 0.0354  172 SER   A N   
1459 C  CA  . SER   A 172 ? 0.2218 0.3144 0.1622 0.0191  0.0111  0.0448  172 SER   A CA  
1460 C  C   . SER   A 172 ? 0.2260 0.3356 0.1437 0.0405  0.0108  0.0370  172 SER   A C   
1461 O  O   . SER   A 172 ? 0.2346 0.3915 0.1396 0.0243  0.0034  0.0317  172 SER   A O   
1462 C  CB  . SER   A 172 ? 0.2733 0.3259 0.1900 0.0048  -0.0018 0.0555  172 SER   A CB  
1463 O  OG  . SER   A 172 ? 0.3448 0.3289 0.2762 0.0108  0.0169  0.0959  172 SER   A OG  
1464 N  N   . ALA   A 173 ? 0.2096 0.3541 0.1321 0.0525  -0.0251 0.0598  173 ALA   A N   
1465 C  CA  . ALA   A 173 ? 0.2260 0.3586 0.1407 0.0574  -0.0306 0.0499  173 ALA   A CA  
1466 C  C   . ALA   A 173 ? 0.2498 0.2991 0.1432 0.0573  -0.0163 0.0520  173 ALA   A C   
1467 O  O   . ALA   A 173 ? 0.1899 0.3051 0.1354 0.0361  -0.0298 0.0395  173 ALA   A O   
1468 C  CB  . ALA   A 173 ? 0.2363 0.3785 0.1931 0.0734  -0.0454 0.0374  173 ALA   A CB  
1469 N  N   . ASP   A 174 ? 0.2784 0.3651 0.1489 0.1017  -0.0287 0.0575  174 ASP   A N   
1470 C  CA  . ASP   A 174 ? 0.2599 0.3916 0.1714 0.1005  -0.0475 0.0289  174 ASP   A CA  
1471 C  C   . ASP   A 174 ? 0.2155 0.3479 0.1691 0.0671  -0.0802 -0.0036 174 ASP   A C   
1472 O  O   . ASP   A 174 ? 0.2380 0.3988 0.2230 0.0694  -0.0501 -0.0711 174 ASP   A O   
1473 C  CB  . ASP   A 174 ? 0.3066 0.4561 0.1800 0.1303  -0.0360 0.0458  174 ASP   A CB  
1474 C  CG  . ASP   A 174 ? 0.3999 0.4894 0.3062 0.1633  -0.0231 0.0567  174 ASP   A CG  
1475 O  OD1 . ASP   A 174 ? 0.3517 0.6505 0.2009 0.2001  -0.0455 0.1349  174 ASP   A OD1 
1476 O  OD2 . ASP   A 174 ? 0.5639 0.4650 0.4740 0.0627  0.0443  0.1438  174 ASP   A OD2 
1477 N  N   . PHE   A 175 ? 0.1782 0.2799 0.1558 0.0382  -0.0481 -0.0075 175 PHE   A N   
1478 C  CA  . PHE   A 175 ? 0.1399 0.2402 0.1844 0.0205  -0.0665 0.0005  175 PHE   A CA  
1479 C  C   . PHE   A 175 ? 0.1539 0.2362 0.1579 0.0228  -0.0629 0.0127  175 PHE   A C   
1480 O  O   . PHE   A 175 ? 0.2249 0.3324 0.1768 0.1075  -0.1008 -0.0040 175 PHE   A O   
1481 C  CB  . PHE   A 175 ? 0.1429 0.2201 0.2030 0.0237  -0.0674 -0.0097 175 PHE   A CB  
1482 C  CG  . PHE   A 175 ? 0.1546 0.2286 0.1906 0.0145  -0.0571 -0.0083 175 PHE   A CG  
1483 C  CD1 . PHE   A 175 ? 0.1755 0.2494 0.1695 -0.0096 -0.0335 -0.0076 175 PHE   A CD1 
1484 C  CD2 . PHE   A 175 ? 0.1546 0.2287 0.2051 0.0207  -0.0734 -0.0142 175 PHE   A CD2 
1485 C  CE1 . PHE   A 175 ? 0.1801 0.2367 0.2163 -0.0034 -0.0326 -0.0143 175 PHE   A CE1 
1486 C  CE2 . PHE   A 175 ? 0.1698 0.2466 0.2074 0.0177  -0.0649 0.0022  175 PHE   A CE2 
1487 C  CZ  . PHE   A 175 ? 0.1600 0.2671 0.2160 -0.0020 -0.0448 -0.0112 175 PHE   A CZ  
1488 N  N   . THR   A 176 ? 0.1542 0.2066 0.1303 0.0172  -0.0513 0.0274  176 THR   A N   
1489 C  CA  . THR   A 176 ? 0.1591 0.1924 0.1687 0.0051  -0.0570 0.0401  176 THR   A CA  
1490 C  C   . THR   A 176 ? 0.1414 0.1642 0.1364 -0.0037 -0.0655 0.0316  176 THR   A C   
1491 O  O   . THR   A 176 ? 0.1524 0.2005 0.1375 -0.0095 -0.0423 0.0227  176 THR   A O   
1492 C  CB  . THR   A 176 ? 0.1531 0.2325 0.1480 -0.0054 -0.0398 0.0622  176 THR   A CB  
1493 O  OG1 . THR   A 176 ? 0.2196 0.2608 0.1612 0.0336  -0.0437 0.0566  176 THR   A OG1 
1494 C  CG2 . THR   A 176 ? 0.1750 0.2401 0.2252 -0.0058 -0.0408 0.0758  176 THR   A CG2 
1495 N  N   . ASN   A 177 ? 0.1474 0.1804 0.1503 -0.0140 -0.0599 0.0308  177 ASN   A N   
1496 C  CA  . ASN   A 177 ? 0.1466 0.2001 0.1727 -0.0082 -0.0516 0.0383  177 ASN   A CA  
1497 C  C   . ASN   A 177 ? 0.1468 0.1970 0.1660 -0.0158 -0.0539 0.0302  177 ASN   A C   
1498 O  O   . ASN   A 177 ? 0.1731 0.2157 0.2421 -0.0395 -0.0650 0.0775  177 ASN   A O   
1499 C  CB  . ASN   A 177 ? 0.1438 0.2145 0.1853 -0.0012 -0.0582 0.0463  177 ASN   A CB  
1500 C  CG  . ASN   A 177 ? 0.1650 0.2306 0.1618 0.0123  -0.0680 0.0333  177 ASN   A CG  
1501 O  OD1 . ASN   A 177 ? 0.1796 0.2521 0.2320 0.0292  -0.0228 0.0293  177 ASN   A OD1 
1502 N  ND2 . ASN   A 177 ? 0.1737 0.2175 0.1621 0.0111  -0.0608 0.0471  177 ASN   A ND2 
1503 N  N   . PHE   A 178 ? 0.1408 0.1935 0.1403 -0.0134 -0.0466 0.0382  178 PHE   A N   
1504 C  CA  . PHE   A 178 ? 0.1510 0.1976 0.1235 -0.0158 -0.0439 0.0230  178 PHE   A CA  
1505 C  C   . PHE   A 178 ? 0.1572 0.1630 0.1342 -0.0023 -0.0349 0.0284  178 PHE   A C   
1506 O  O   . PHE   A 178 ? 0.1764 0.1783 0.1594 -0.0173 -0.0301 0.0214  178 PHE   A O   
1507 C  CB  . PHE   A 178 ? 0.1631 0.1954 0.1335 -0.0099 -0.0419 0.0216  178 PHE   A CB  
1508 C  CG  . PHE   A 178 ? 0.1485 0.1917 0.1434 -0.0228 -0.0446 0.0392  178 PHE   A CG  
1509 C  CD1 . PHE   A 178 ? 0.1833 0.2069 0.1299 -0.0058 -0.0355 0.0321  178 PHE   A CD1 
1510 C  CD2 . PHE   A 178 ? 0.1306 0.1919 0.1576 -0.0213 -0.0413 0.0365  178 PHE   A CD2 
1511 C  CE1 . PHE   A 178 ? 0.1988 0.1923 0.1653 -0.0242 -0.0449 0.0268  178 PHE   A CE1 
1512 C  CE2 . PHE   A 178 ? 0.1320 0.1956 0.1449 -0.0155 -0.0552 0.0429  178 PHE   A CE2 
1513 C  CZ  . PHE   A 178 ? 0.1472 0.1896 0.1641 -0.0069 -0.0524 0.0444  178 PHE   A CZ  
1514 N  N   . ASP   A 179 ? 0.1353 0.1896 0.1378 -0.0209 -0.0433 0.0055  179 ASP   A N   
1515 C  CA  . ASP   A 179 ? 0.1275 0.1944 0.1545 -0.0051 -0.0334 0.0195  179 ASP   A CA  
1516 C  C   . ASP   A 179 ? 0.1377 0.1942 0.1553 -0.0055 -0.0303 0.0253  179 ASP   A C   
1517 O  O   . ASP   A 179 ? 0.1486 0.1969 0.1601 -0.0026 -0.0299 0.0141  179 ASP   A O   
1518 C  CB  . ASP   A 179 ? 0.1395 0.2431 0.1754 -0.0120 -0.0381 0.0339  179 ASP   A CB  
1519 C  CG  . ASP   A 179 ? 0.1555 0.3007 0.1955 -0.0014 -0.0183 0.0200  179 ASP   A CG  
1520 O  OD1 . ASP   A 179 ? 0.1637 0.2587 0.1963 0.0457  -0.0167 0.0342  179 ASP   A OD1 
1521 O  OD2 . ASP   A 179 ? 0.1727 0.5046 0.2885 0.0021  -0.0079 -0.0198 179 ASP   A OD2 
1522 N  N   . PRO   A 180 ? 0.1229 0.1800 0.1495 -0.0140 -0.0198 0.0297  180 PRO   A N   
1523 C  CA  . PRO   A 180 ? 0.1195 0.1677 0.1526 -0.0008 -0.0232 0.0284  180 PRO   A CA  
1524 C  C   . PRO   A 180 ? 0.1373 0.1835 0.1635 -0.0181 -0.0380 0.0334  180 PRO   A C   
1525 O  O   . PRO   A 180 ? 0.1461 0.1878 0.1473 -0.0113 -0.0444 0.0300  180 PRO   A O   
1526 C  CB  . PRO   A 180 ? 0.1176 0.2017 0.1721 -0.0089 -0.0240 0.0313  180 PRO   A CB  
1527 C  CG  . PRO   A 180 ? 0.1403 0.1921 0.1865 -0.0160 -0.0276 0.0227  180 PRO   A CG  
1528 C  CD  . PRO   A 180 ? 0.1568 0.1959 0.1630 -0.0031 -0.0267 0.0353  180 PRO   A CD  
1529 N  N   . ARG   A 181 ? 0.1442 0.1934 0.1527 -0.0131 -0.0358 0.0353  181 ARG   A N   
1530 C  CA  . ARG   A 181 ? 0.1374 0.1931 0.1550 -0.0051 -0.0347 0.0219  181 ARG   A CA  
1531 C  C   . ARG   A 181 ? 0.1214 0.1912 0.1681 0.0122  -0.0377 0.0320  181 ARG   A C   
1532 O  O   . ARG   A 181 ? 0.1378 0.2010 0.1890 -0.0009 -0.0303 0.0383  181 ARG   A O   
1533 C  CB  . ARG   A 181 ? 0.1557 0.1968 0.1690 0.0058  0.0030  0.0259  181 ARG   A CB  
1534 C  CG  . ARG   A 181 ? 0.2300 0.2121 0.1700 0.0133  0.0157  0.0303  181 ARG   A CG  
1535 C  CD  . ARG   A 181 ? 0.2528 0.2332 0.2059 0.0378  0.0275  0.0447  181 ARG   A CD  
1536 N  NE  . ARG   A 181 ? 0.2485 0.2364 0.2331 0.0767  0.0206  0.0526  181 ARG   A NE  
1537 C  CZ  . ARG   A 181 ? 0.2439 0.3043 0.2280 0.0811  0.0212  0.0590  181 ARG   A CZ  
1538 N  NH1 . ARG   A 181 ? 0.2732 0.3477 0.2700 0.1107  0.0074  0.0373  181 ARG   A NH1 
1539 N  NH2 . ARG   A 181 ? 0.2560 0.3785 0.2437 0.0754  -0.0035 0.0474  181 ARG   A NH2 
1540 N  N   . GLY   A 182 ? 0.1417 0.1929 0.1626 -0.0047 -0.0473 0.0303  182 GLY   A N   
1541 C  CA  . GLY   A 182 ? 0.1453 0.1987 0.1843 -0.0015 -0.0551 0.0358  182 GLY   A CA  
1542 C  C   . GLY   A 182 ? 0.1407 0.1779 0.1679 -0.0086 -0.0438 0.0168  182 GLY   A C   
1543 O  O   . GLY   A 182 ? 0.1642 0.1960 0.1832 -0.0110 -0.0675 0.0099  182 GLY   A O   
1544 N  N   . LEU   A 183 ? 0.1471 0.1930 0.1511 -0.0019 -0.0532 0.0231  183 LEU   A N   
1545 C  CA  . LEU   A 183 ? 0.1337 0.1613 0.1651 0.0068  -0.0448 0.0099  183 LEU   A CA  
1546 C  C   . LEU   A 183 ? 0.1446 0.1772 0.1672 -0.0047 -0.0359 0.0211  183 LEU   A C   
1547 O  O   . LEU   A 183 ? 0.1623 0.2131 0.1901 0.0145  -0.0365 0.0440  183 LEU   A O   
1548 C  CB  . LEU   A 183 ? 0.1495 0.1691 0.1704 0.0077  -0.0472 0.0226  183 LEU   A CB  
1549 C  CG  . LEU   A 183 ? 0.1607 0.1965 0.1546 0.0072  -0.0529 0.0308  183 LEU   A CG  
1550 C  CD1 . LEU   A 183 ? 0.1573 0.2189 0.1700 -0.0058 -0.0737 0.0491  183 LEU   A CD1 
1551 C  CD2 . LEU   A 183 ? 0.1993 0.2295 0.1671 0.0292  -0.0516 0.0117  183 LEU   A CD2 
1552 N  N   . LEU   A 184 ? 0.1443 0.1888 0.1574 -0.0138 -0.0387 0.0200  184 LEU   A N   
1553 C  CA  . LEU   A 184 ? 0.1324 0.1915 0.1554 -0.0266 -0.0446 0.0369  184 LEU   A CA  
1554 C  C   . LEU   A 184 ? 0.1543 0.2098 0.1750 -0.0557 -0.0590 0.0438  184 LEU   A C   
1555 O  O   . LEU   A 184 ? 0.2749 0.2719 0.2368 -0.1231 -0.1443 0.0655  184 LEU   A O   
1556 C  CB  . LEU   A 184 ? 0.1253 0.1948 0.1867 -0.0379 -0.0429 0.0219  184 LEU   A CB  
1557 C  CG  . LEU   A 184 ? 0.1200 0.2248 0.2122 -0.0240 -0.0437 0.0244  184 LEU   A CG  
1558 C  CD1 . LEU   A 184 ? 0.1707 0.2281 0.2028 -0.0182 -0.0379 0.0205  184 LEU   A CD1 
1559 C  CD2 . LEU   A 184 ? 0.1295 0.2287 0.2573 0.0046  -0.0581 0.0243  184 LEU   A CD2 
1560 N  N   . PRO   A 185 ? 0.1452 0.1931 0.1543 -0.0271 -0.0382 0.0270  185 PRO   A N   
1561 C  CA  . PRO   A 185 ? 0.1612 0.1772 0.1887 -0.0265 -0.0424 0.0291  185 PRO   A CA  
1562 C  C   . PRO   A 185 ? 0.1475 0.1865 0.1779 -0.0325 -0.0647 0.0212  185 PRO   A C   
1563 O  O   . PRO   A 185 ? 0.1086 0.2002 0.2611 -0.0197 -0.0668 0.0397  185 PRO   A O   
1564 C  CB  . PRO   A 185 ? 0.1359 0.1971 0.1850 -0.0027 -0.0185 0.0356  185 PRO   A CB  
1565 C  CG  . PRO   A 185 ? 0.1147 0.1996 0.1697 0.0093  -0.0234 0.0202  185 PRO   A CG  
1566 C  CD  . PRO   A 185 ? 0.1091 0.1983 0.1602 -0.0127 -0.0229 0.0123  185 PRO   A CD  
1567 N  N   . GLU   A 186 ? 0.1530 0.1960 0.1902 -0.0323 -0.0478 0.0320  186 GLU   A N   
1568 C  CA  . GLU   A 186 ? 0.1199 0.2354 0.2062 -0.0284 -0.0571 0.0319  186 GLU   A CA  
1569 C  C   . GLU   A 186 ? 0.0904 0.2227 0.2148 -0.0287 -0.0409 0.0397  186 GLU   A C   
1570 O  O   . GLU   A 186 ? 0.1132 0.2532 0.2614 0.0180  -0.0460 0.0312  186 GLU   A O   
1571 C  CB  . GLU   A 186 ? 0.1709 0.2723 0.2885 -0.0517 -0.0729 0.0410  186 GLU   A CB  
1572 C  CG  . GLU   A 186 ? 0.1820 0.2915 0.3662 -0.0387 -0.0908 0.0456  186 GLU   A CG  
1573 C  CD  . GLU   A 186 ? 0.1908 0.2829 0.3990 -0.0244 -0.0872 0.0604  186 GLU   A CD  
1574 O  OE1 . GLU   A 186 ? 0.1787 0.3098 0.4320 -0.0569 -0.0818 0.0963  186 GLU   A OE1 
1575 O  OE2 . GLU   A 186 ? 0.2539 0.3646 0.4375 0.0074  -0.1209 0.0151  186 GLU   A OE2 
1576 N  N   . SER   A 187 ? 0.0876 0.2281 0.2003 -0.0173 -0.0402 0.0322  187 SER   A N   
1577 C  CA  . SER   A 187 ? 0.1107 0.2239 0.2133 -0.0164 -0.0274 0.0178  187 SER   A CA  
1578 C  C   . SER   A 187 ? 0.0980 0.2338 0.1957 -0.0176 -0.0335 0.0300  187 SER   A C   
1579 O  O   . SER   A 187 ? 0.0956 0.2510 0.2147 -0.0212 -0.0242 -0.0065 187 SER   A O   
1580 C  CB  . SER   A 187 ? 0.1310 0.2458 0.2028 -0.0171 -0.0301 0.0381  187 SER   A CB  
1581 O  OG  . SER   A 187 ? 0.1656 0.2579 0.1982 -0.0281 -0.0277 0.0289  187 SER   A OG  
1582 N  N   . LEU   A 188 ? 0.0849 0.2355 0.2124 -0.0155 -0.0329 0.0142  188 LEU   A N   
1583 C  CA  . LEU   A 188 ? 0.0904 0.2331 0.2291 -0.0119 -0.0333 0.0004  188 LEU   A CA  
1584 C  C   . LEU   A 188 ? 0.1089 0.2373 0.2025 -0.0035 -0.0212 -0.0151 188 LEU   A C   
1585 O  O   . LEU   A 188 ? 0.1392 0.2569 0.2201 -0.0318 -0.0261 0.0066  188 LEU   A O   
1586 C  CB  . LEU   A 188 ? 0.1128 0.2364 0.2657 -0.0159 -0.0305 -0.0060 188 LEU   A CB  
1587 C  CG  . LEU   A 188 ? 0.1005 0.2676 0.2887 0.0004  -0.0404 0.0183  188 LEU   A CG  
1588 C  CD1 . LEU   A 188 ? 0.1237 0.2605 0.3137 -0.0074 -0.0554 0.0324  188 LEU   A CD1 
1589 C  CD2 . LEU   A 188 ? 0.1159 0.3003 0.2523 -0.0147 -0.0561 0.0209  188 LEU   A CD2 
1590 N  N   . ASP   A 189 ? 0.1048 0.2533 0.1821 -0.0124 -0.0231 -0.0114 189 ASP   A N   
1591 C  CA  . ASP   A 189 ? 0.1111 0.2746 0.1851 -0.0281 -0.0190 -0.0150 189 ASP   A CA  
1592 C  C   . ASP   A 189 ? 0.0995 0.2192 0.1577 -0.0131 -0.0207 -0.0120 189 ASP   A C   
1593 O  O   . ASP   A 189 ? 0.0920 0.2229 0.1606 -0.0064 -0.0211 -0.0031 189 ASP   A O   
1594 C  CB  . ASP   A 189 ? 0.1328 0.3262 0.1767 -0.0653 -0.0320 0.0039  189 ASP   A CB  
1595 C  CG  . ASP   A 189 ? 0.1567 0.3887 0.2579 -0.0909 -0.0110 -0.0002 189 ASP   A CG  
1596 O  OD1 . ASP   A 189 ? 0.1605 0.4946 0.2944 -0.0635 0.0402  -0.0526 189 ASP   A OD1 
1597 O  OD2 . ASP   A 189 ? 0.2166 0.4864 0.3088 -0.1523 -0.0243 0.0626  189 ASP   A OD2 
1598 N  N   . TYR   A 190 ? 0.1011 0.2266 0.1290 -0.0171 0.0027  -0.0043 190 TYR   A N   
1599 C  CA  . TYR   A 190 ? 0.0978 0.2063 0.1239 -0.0121 0.0004  0.0045  190 TYR   A CA  
1600 C  C   . TYR   A 190 ? 0.1027 0.2059 0.1279 0.0017  0.0037  0.0005  190 TYR   A C   
1601 O  O   . TYR   A 190 ? 0.1088 0.2114 0.1365 -0.0001 0.0063  -0.0013 190 TYR   A O   
1602 C  CB  . TYR   A 190 ? 0.1188 0.2062 0.1303 -0.0095 -0.0183 0.0079  190 TYR   A CB  
1603 C  CG  . TYR   A 190 ? 0.1036 0.1992 0.1419 -0.0071 -0.0244 0.0146  190 TYR   A CG  
1604 C  CD1 . TYR   A 190 ? 0.1022 0.2208 0.1616 -0.0190 -0.0267 0.0031  190 TYR   A CD1 
1605 C  CD2 . TYR   A 190 ? 0.1051 0.2138 0.1704 0.0085  -0.0204 0.0070  190 TYR   A CD2 
1606 C  CE1 . TYR   A 190 ? 0.1169 0.2184 0.1701 -0.0147 -0.0173 -0.0002 190 TYR   A CE1 
1607 C  CE2 . TYR   A 190 ? 0.1358 0.2143 0.1661 0.0009  -0.0079 0.0133  190 TYR   A CE2 
1608 C  CZ  . TYR   A 190 ? 0.1423 0.2063 0.1797 -0.0046 -0.0120 0.0004  190 TYR   A CZ  
1609 O  OH  . TYR   A 190 ? 0.1655 0.2337 0.1930 -0.0001 -0.0198 -0.0060 190 TYR   A OH  
1610 N  N   . TRP   A 191 ? 0.0978 0.1810 0.1147 -0.0078 -0.0098 -0.0118 191 TRP   A N   
1611 C  CA  . TRP   A 191 ? 0.1106 0.1702 0.1267 -0.0087 -0.0289 -0.0001 191 TRP   A CA  
1612 C  C   . TRP   A 191 ? 0.1082 0.1721 0.1149 0.0037  -0.0119 0.0022  191 TRP   A C   
1613 O  O   . TRP   A 191 ? 0.1255 0.1926 0.1378 -0.0290 -0.0234 0.0154  191 TRP   A O   
1614 C  CB  . TRP   A 191 ? 0.1083 0.1822 0.1323 -0.0058 -0.0262 0.0028  191 TRP   A CB  
1615 C  CG  . TRP   A 191 ? 0.1087 0.1766 0.1483 0.0019  -0.0200 0.0080  191 TRP   A CG  
1616 C  CD1 . TRP   A 191 ? 0.1385 0.1961 0.1574 -0.0041 -0.0181 0.0148  191 TRP   A CD1 
1617 C  CD2 . TRP   A 191 ? 0.1145 0.1854 0.1505 0.0070  -0.0294 0.0086  191 TRP   A CD2 
1618 N  NE1 . TRP   A 191 ? 0.1581 0.1992 0.1620 -0.0021 -0.0192 0.0251  191 TRP   A NE1 
1619 C  CE2 . TRP   A 191 ? 0.1230 0.1936 0.1633 -0.0002 -0.0335 0.0091  191 TRP   A CE2 
1620 C  CE3 . TRP   A 191 ? 0.0981 0.1894 0.1575 -0.0048 -0.0222 -0.0026 191 TRP   A CE3 
1621 C  CZ2 . TRP   A 191 ? 0.1286 0.1852 0.2067 0.0023  -0.0293 0.0159  191 TRP   A CZ2 
1622 C  CZ3 . TRP   A 191 ? 0.1186 0.2202 0.1812 -0.0035 -0.0456 -0.0167 191 TRP   A CZ3 
1623 C  CH2 . TRP   A 191 ? 0.1271 0.1840 0.2187 -0.0068 -0.0333 -0.0255 191 TRP   A CH2 
1624 N  N   . THR   A 192 ? 0.1100 0.1651 0.1082 -0.0051 -0.0232 0.0038  192 THR   A N   
1625 C  CA  . THR   A 192 ? 0.1085 0.1617 0.1158 -0.0042 -0.0175 -0.0071 192 THR   A CA  
1626 C  C   . THR   A 192 ? 0.1015 0.1688 0.1195 -0.0081 -0.0146 -0.0041 192 THR   A C   
1627 O  O   . THR   A 192 ? 0.1096 0.1942 0.1197 -0.0034 -0.0097 0.0013  192 THR   A O   
1628 C  CB  . THR   A 192 ? 0.0993 0.1650 0.1299 0.0028  -0.0151 -0.0065 192 THR   A CB  
1629 O  OG1 . THR   A 192 ? 0.1066 0.1610 0.1535 0.0096  -0.0197 -0.0070 192 THR   A OG1 
1630 C  CG2 . THR   A 192 ? 0.1174 0.1611 0.1411 0.0088  -0.0140 -0.0100 192 THR   A CG2 
1631 N  N   . TYR   A 193 ? 0.0849 0.1770 0.1154 0.0053  -0.0223 -0.0001 193 TYR   A N   
1632 C  CA  . TYR   A 193 ? 0.0888 0.1912 0.1201 -0.0013 -0.0290 -0.0051 193 TYR   A CA  
1633 C  C   . TYR   A 193 ? 0.1031 0.1624 0.1029 0.0095  -0.0261 -0.0089 193 TYR   A C   
1634 O  O   . TYR   A 193 ? 0.1004 0.1778 0.1003 0.0067  -0.0352 -0.0031 193 TYR   A O   
1635 C  CB  . TYR   A 193 ? 0.0906 0.1684 0.1118 -0.0052 -0.0338 -0.0056 193 TYR   A CB  
1636 C  CG  . TYR   A 193 ? 0.0981 0.1777 0.1216 0.0032  -0.0286 -0.0143 193 TYR   A CG  
1637 C  CD1 . TYR   A 193 ? 0.1024 0.1574 0.1335 0.0100  -0.0402 -0.0087 193 TYR   A CD1 
1638 C  CD2 . TYR   A 193 ? 0.1035 0.1664 0.1230 0.0048  -0.0340 -0.0188 193 TYR   A CD2 
1639 C  CE1 . TYR   A 193 ? 0.0960 0.1680 0.1252 -0.0030 -0.0338 -0.0116 193 TYR   A CE1 
1640 C  CE2 . TYR   A 193 ? 0.0847 0.1721 0.1220 -0.0018 -0.0374 -0.0125 193 TYR   A CE2 
1641 C  CZ  . TYR   A 193 ? 0.0946 0.1517 0.1200 0.0001  -0.0339 -0.0142 193 TYR   A CZ  
1642 O  OH  . TYR   A 193 ? 0.1042 0.1562 0.1143 0.0001  -0.0298 -0.0090 193 TYR   A OH  
1643 N  N   . PRO   A 194 ? 0.0959 0.1794 0.1085 0.0014  -0.0267 -0.0164 194 PRO   A N   
1644 C  CA  . PRO   A 194 ? 0.0999 0.1703 0.1242 0.0051  -0.0279 -0.0186 194 PRO   A CA  
1645 C  C   . PRO   A 194 ? 0.0968 0.1561 0.1235 -0.0015 -0.0326 -0.0146 194 PRO   A C   
1646 O  O   . PRO   A 194 ? 0.1071 0.1759 0.1273 0.0232  -0.0274 -0.0100 194 PRO   A O   
1647 C  CB  . PRO   A 194 ? 0.1100 0.1899 0.1379 -0.0016 -0.0205 -0.0315 194 PRO   A CB  
1648 C  CG  . PRO   A 194 ? 0.1300 0.2059 0.1304 -0.0068 -0.0331 -0.0282 194 PRO   A CG  
1649 C  CD  . PRO   A 194 ? 0.1241 0.1831 0.1131 -0.0071 -0.0182 -0.0153 194 PRO   A CD  
1650 N  N   . GLY   A 195 ? 0.0826 0.1595 0.1252 0.0127  -0.0223 -0.0073 195 GLY   A N   
1651 C  CA  . GLY   A 195 ? 0.0926 0.1709 0.1209 -0.0055 -0.0184 -0.0117 195 GLY   A CA  
1652 C  C   . GLY   A 195 ? 0.0933 0.1635 0.1191 0.0011  -0.0262 -0.0065 195 GLY   A C   
1653 O  O   . GLY   A 195 ? 0.0959 0.1564 0.1264 -0.0018 -0.0181 -0.0164 195 GLY   A O   
1654 N  N   . SER   A 196 ? 0.0954 0.1586 0.1085 -0.0035 -0.0214 -0.0048 196 SER   A N   
1655 C  CA  . SER   A 196 ? 0.0909 0.1634 0.1029 0.0155  -0.0243 -0.0051 196 SER   A CA  
1656 C  C   . SER   A 196 ? 0.0673 0.1475 0.1031 0.0080  -0.0276 -0.0017 196 SER   A C   
1657 O  O   . SER   A 196 ? 0.0905 0.1597 0.1184 -0.0005 -0.0329 -0.0050 196 SER   A O   
1658 C  CB  . SER   A 196 ? 0.0894 0.1793 0.1310 0.0030  -0.0290 -0.0029 196 SER   A CB  
1659 O  OG  . SER   A 196 ? 0.0815 0.1801 0.1381 -0.0062 -0.0277 -0.0102 196 SER   A OG  
1660 N  N   . LEU   A 197 ? 0.0821 0.1622 0.1123 -0.0026 -0.0154 -0.0055 197 LEU   A N   
1661 C  CA  . LEU   A 197 ? 0.0830 0.1645 0.1233 -0.0060 -0.0137 -0.0095 197 LEU   A CA  
1662 C  C   . LEU   A 197 ? 0.0707 0.1723 0.1227 -0.0070 -0.0212 -0.0103 197 LEU   A C   
1663 O  O   . LEU   A 197 ? 0.0784 0.1794 0.1214 -0.0052 -0.0316 -0.0079 197 LEU   A O   
1664 C  CB  . LEU   A 197 ? 0.0917 0.1671 0.1309 -0.0062 -0.0304 -0.0121 197 LEU   A CB  
1665 C  CG  . LEU   A 197 ? 0.1197 0.1783 0.1444 -0.0123 -0.0159 -0.0089 197 LEU   A CG  
1666 C  CD1 . LEU   A 197 ? 0.1486 0.1683 0.1636 -0.0214 -0.0201 0.0005  197 LEU   A CD1 
1667 C  CD2 . LEU   A 197 ? 0.1166 0.1975 0.1824 -0.0021 -0.0093 0.0041  197 LEU   A CD2 
1668 N  N   . THR   A 198 ? 0.0734 0.1574 0.1258 -0.0022 -0.0346 -0.0068 198 THR   A N   
1669 C  CA  . THR   A 198 ? 0.0792 0.1633 0.1274 0.0030  -0.0296 -0.0124 198 THR   A CA  
1670 C  C   . THR   A 198 ? 0.0771 0.1679 0.1356 -0.0001 -0.0322 -0.0088 198 THR   A C   
1671 O  O   . THR   A 198 ? 0.0772 0.1684 0.1541 0.0075  -0.0248 -0.0066 198 THR   A O   
1672 C  CB  . THR   A 198 ? 0.0978 0.1478 0.1064 0.0048  -0.0308 -0.0075 198 THR   A CB  
1673 O  OG1 . THR   A 198 ? 0.0828 0.1697 0.1029 0.0019  -0.0183 -0.0008 198 THR   A OG1 
1674 C  CG2 . THR   A 198 ? 0.1031 0.1549 0.1169 0.0006  -0.0261 -0.0044 198 THR   A CG2 
1675 N  N   . THR   A 199 ? 0.0815 0.1825 0.1471 0.0019  -0.0251 -0.0026 199 THR   A N   
1676 C  CA  . THR   A 199 ? 0.0842 0.1930 0.1537 -0.0098 -0.0194 -0.0100 199 THR   A CA  
1677 C  C   . THR   A 199 ? 0.0886 0.1984 0.1573 -0.0161 -0.0192 -0.0129 199 THR   A C   
1678 O  O   . THR   A 199 ? 0.1033 0.2021 0.1777 -0.0264 -0.0096 -0.0299 199 THR   A O   
1679 C  CB  . THR   A 199 ? 0.0956 0.1991 0.1541 0.0013  -0.0171 -0.0032 199 THR   A CB  
1680 O  OG1 . THR   A 199 ? 0.2383 0.2290 0.1713 0.0420  -0.0087 0.0116  199 THR   A OG1 
1681 C  CG2 . THR   A 199 ? 0.1108 0.1964 0.1626 -0.0069 -0.0366 0.0074  199 THR   A CG2 
1682 N  N   . PRO   A 200 ? 0.0823 0.2089 0.1728 -0.0254 -0.0139 -0.0181 200 PRO   A N   
1683 C  CA  . PRO   A 200 ? 0.0973 0.2056 0.1638 -0.0355 -0.0100 -0.0017 200 PRO   A CA  
1684 C  C   . PRO   A 200 ? 0.1210 0.2042 0.1670 -0.0242 -0.0192 -0.0149 200 PRO   A C   
1685 O  O   . PRO   A 200 ? 0.1297 0.2404 0.1770 -0.0130 -0.0205 -0.0185 200 PRO   A O   
1686 C  CB  . PRO   A 200 ? 0.0873 0.2325 0.1883 -0.0342 -0.0014 0.0072  200 PRO   A CB  
1687 C  CG  . PRO   A 200 ? 0.0948 0.2403 0.1890 -0.0263 -0.0138 -0.0127 200 PRO   A CG  
1688 C  CD  . PRO   A 200 ? 0.0926 0.2196 0.1595 -0.0248 -0.0104 -0.0182 200 PRO   A CD  
1689 N  N   . PRO   A 201 ? 0.1128 0.2125 0.1609 -0.0279 -0.0091 0.0074  201 PRO   A N   
1690 C  CA  . PRO   A 201 ? 0.1285 0.2107 0.1687 -0.0348 -0.0115 -0.0021 201 PRO   A CA  
1691 C  C   . PRO   A 201 ? 0.0939 0.1749 0.1673 -0.0330 -0.0256 -0.0147 201 PRO   A C   
1692 O  O   . PRO   A 201 ? 0.1009 0.2165 0.1836 -0.0386 -0.0171 -0.0194 201 PRO   A O   
1693 C  CB  . PRO   A 201 ? 0.1393 0.2239 0.2057 -0.0454 -0.0082 0.0078  201 PRO   A CB  
1694 C  CG  . PRO   A 201 ? 0.1680 0.2193 0.2059 -0.0047 -0.0160 0.0110  201 PRO   A CG  
1695 C  CD  . PRO   A 201 ? 0.1541 0.2103 0.1948 -0.0074 -0.0097 0.0057  201 PRO   A CD  
1696 N  N   . LEU   A 202 ? 0.0818 0.1840 0.1652 -0.0228 -0.0247 -0.0015 202 LEU   A N   
1697 C  CA  . LEU   A 202 ? 0.0766 0.1901 0.1464 -0.0142 -0.0179 -0.0100 202 LEU   A CA  
1698 C  C   . LEU   A 202 ? 0.0750 0.1711 0.1507 -0.0131 -0.0201 -0.0168 202 LEU   A C   
1699 O  O   . LEU   A 202 ? 0.0888 0.1876 0.1645 -0.0085 -0.0330 -0.0092 202 LEU   A O   
1700 C  CB  . LEU   A 202 ? 0.0838 0.2096 0.1681 -0.0017 -0.0314 -0.0057 202 LEU   A CB  
1701 C  CG  . LEU   A 202 ? 0.0812 0.1959 0.1684 0.0010  -0.0295 -0.0052 202 LEU   A CG  
1702 C  CD1 . LEU   A 202 ? 0.0895 0.2286 0.1813 0.0092  -0.0240 -0.0043 202 LEU   A CD1 
1703 C  CD2 . LEU   A 202 ? 0.0973 0.1816 0.1914 0.0011  -0.0155 -0.0147 202 LEU   A CD2 
1704 N  N   . ASN   A 203 ? 0.0958 0.1755 0.1734 -0.0127 -0.0239 -0.0221 203 ASN   A N   
1705 C  CA  . ASN   A 203 ? 0.1038 0.1522 0.1863 -0.0199 -0.0162 -0.0141 203 ASN   A CA  
1706 C  C   . ASN   A 203 ? 0.1025 0.1529 0.1475 -0.0124 -0.0215 -0.0183 203 ASN   A C   
1707 O  O   . ASN   A 203 ? 0.0904 0.1643 0.1644 -0.0116 -0.0261 -0.0215 203 ASN   A O   
1708 C  CB  . ASN   A 203 ? 0.1234 0.1727 0.1975 -0.0126 -0.0274 0.0051  203 ASN   A CB  
1709 C  CG  . ASN   A 203 ? 0.1720 0.1926 0.2482 0.0010  0.0005  0.0178  203 ASN   A CG  
1710 O  OD1 . ASN   A 203 ? 0.1943 0.2320 0.2893 0.0135  0.0511  0.0403  203 ASN   A OD1 
1711 N  ND2 . ASN   A 203 ? 0.2281 0.2356 0.2586 -0.0009 0.0246  0.0472  203 ASN   A ND2 
1712 N  N   . GLU   A 204 ? 0.1014 0.1802 0.1453 -0.0065 -0.0328 -0.0293 204 GLU   A N   
1713 C  CA  . GLU   A 204 ? 0.1123 0.1864 0.1375 -0.0123 -0.0355 -0.0371 204 GLU   A CA  
1714 C  C   . GLU   A 204 ? 0.1111 0.1876 0.1546 -0.0126 -0.0342 -0.0471 204 GLU   A C   
1715 O  O   . GLU   A 204 ? 0.1140 0.2510 0.1795 -0.0167 -0.0325 -0.0633 204 GLU   A O   
1716 C  CB  . GLU   A 204 ? 0.1193 0.2123 0.1516 -0.0177 -0.0412 -0.0329 204 GLU   A CB  
1717 C  CG  . GLU   A 204 ? 0.1163 0.2138 0.1565 -0.0260 -0.0527 -0.0327 204 GLU   A CG  
1718 C  CD  . GLU   A 204 ? 0.1180 0.2193 0.1546 -0.0128 -0.0471 -0.0246 204 GLU   A CD  
1719 O  OE1 . GLU   A 204 ? 0.1362 0.2467 0.1900 -0.0010 -0.0908 -0.0453 204 GLU   A OE1 
1720 O  OE2 . GLU   A 204 ? 0.1190 0.2258 0.1549 -0.0212 -0.0492 -0.0142 204 GLU   A OE2 
1721 N  N   . THR   A 205 ? 0.1057 0.1608 0.1551 -0.0143 -0.0325 -0.0415 205 THR   A N   
1722 C  CA  . THR   A 205 ? 0.0964 0.1547 0.1740 -0.0075 -0.0116 -0.0278 205 THR   A CA  
1723 C  C   . THR   A 205 ? 0.1065 0.1455 0.1429 -0.0103 -0.0194 -0.0177 205 THR   A C   
1724 O  O   . THR   A 205 ? 0.1172 0.1556 0.1817 0.0047  -0.0381 -0.0054 205 THR   A O   
1725 C  CB  . THR   A 205 ? 0.1289 0.1664 0.1945 -0.0130 -0.0211 -0.0173 205 THR   A CB  
1726 O  OG1 . THR   A 205 ? 0.1151 0.1896 0.1878 -0.0089 -0.0236 -0.0014 205 THR   A OG1 
1727 C  CG2 . THR   A 205 ? 0.1247 0.1841 0.2191 -0.0211 -0.0150 -0.0015 205 THR   A CG2 
1728 N  N   . VAL   A 206 ? 0.0805 0.1513 0.1507 -0.0020 -0.0337 0.0032  206 VAL   A N   
1729 C  CA  . VAL   A 206 ? 0.0771 0.1569 0.1427 -0.0017 -0.0344 0.0004  206 VAL   A CA  
1730 C  C   . VAL   A 206 ? 0.0912 0.1499 0.1346 0.0026  -0.0368 0.0032  206 VAL   A C   
1731 O  O   . VAL   A 206 ? 0.0885 0.1749 0.1617 0.0030  -0.0249 0.0237  206 VAL   A O   
1732 C  CB  . VAL   A 206 ? 0.0970 0.1545 0.1451 -0.0041 -0.0372 0.0018  206 VAL   A CB  
1733 C  CG1 . VAL   A 206 ? 0.1090 0.1445 0.1362 0.0030  -0.0498 -0.0048 206 VAL   A CG1 
1734 C  CG2 . VAL   A 206 ? 0.1002 0.1761 0.1446 0.0006  -0.0390 -0.0052 206 VAL   A CG2 
1735 N  N   . THR   A 207 ? 0.0852 0.1577 0.1424 0.0034  -0.0271 0.0003  207 THR   A N   
1736 C  CA  . THR   A 207 ? 0.1100 0.1374 0.1458 0.0018  -0.0328 -0.0027 207 THR   A CA  
1737 C  C   . THR   A 207 ? 0.0783 0.1542 0.1323 -0.0090 -0.0264 -0.0002 207 THR   A C   
1738 O  O   . THR   A 207 ? 0.1027 0.1604 0.1375 0.0007  -0.0419 -0.0028 207 THR   A O   
1739 C  CB  . THR   A 207 ? 0.1046 0.1535 0.1550 0.0065  -0.0218 -0.0027 207 THR   A CB  
1740 O  OG1 . THR   A 207 ? 0.1291 0.1555 0.1692 -0.0050 -0.0067 -0.0205 207 THR   A OG1 
1741 C  CG2 . THR   A 207 ? 0.1150 0.1639 0.1744 0.0065  -0.0097 -0.0014 207 THR   A CG2 
1742 N  N   . TRP   A 208 ? 0.0857 0.1348 0.1242 -0.0044 -0.0288 -0.0054 208 TRP   A N   
1743 C  CA  . TRP   A 208 ? 0.0826 0.1329 0.1263 -0.0060 -0.0284 0.0108  208 TRP   A CA  
1744 C  C   . TRP   A 208 ? 0.0837 0.1388 0.1252 0.0000  -0.0244 0.0012  208 TRP   A C   
1745 O  O   . TRP   A 208 ? 0.0971 0.1619 0.1186 0.0040  -0.0218 -0.0062 208 TRP   A O   
1746 C  CB  . TRP   A 208 ? 0.0873 0.1406 0.1117 -0.0083 -0.0329 0.0000  208 TRP   A CB  
1747 C  CG  . TRP   A 208 ? 0.0846 0.1399 0.1190 -0.0010 -0.0355 -0.0044 208 TRP   A CG  
1748 C  CD1 . TRP   A 208 ? 0.0774 0.1641 0.1036 -0.0035 -0.0368 -0.0140 208 TRP   A CD1 
1749 C  CD2 . TRP   A 208 ? 0.0857 0.1459 0.1224 0.0072  -0.0275 -0.0073 208 TRP   A CD2 
1750 N  NE1 . TRP   A 208 ? 0.0925 0.1628 0.1201 0.0046  -0.0221 -0.0109 208 TRP   A NE1 
1751 C  CE2 . TRP   A 208 ? 0.0841 0.1526 0.1277 0.0213  -0.0272 -0.0083 208 TRP   A CE2 
1752 C  CE3 . TRP   A 208 ? 0.0878 0.1573 0.1218 0.0120  -0.0386 -0.0047 208 TRP   A CE3 
1753 C  CZ2 . TRP   A 208 ? 0.0940 0.1576 0.1418 0.0243  -0.0167 -0.0064 208 TRP   A CZ2 
1754 C  CZ3 . TRP   A 208 ? 0.0973 0.1588 0.1260 0.0137  -0.0310 -0.0008 208 TRP   A CZ3 
1755 C  CH2 . TRP   A 208 ? 0.1051 0.1688 0.1218 0.0155  -0.0131 -0.0139 208 TRP   A CH2 
1756 N  N   . ILE   A 209 ? 0.0866 0.1509 0.1216 -0.0150 -0.0283 -0.0005 209 ILE   A N   
1757 C  CA  . ILE   A 209 ? 0.0900 0.1388 0.1200 -0.0021 -0.0265 0.0066  209 ILE   A CA  
1758 C  C   . ILE   A 209 ? 0.0854 0.1516 0.1215 0.0001  -0.0124 -0.0022 209 ILE   A C   
1759 O  O   . ILE   A 209 ? 0.1142 0.1538 0.1202 -0.0060 -0.0277 0.0035  209 ILE   A O   
1760 C  CB  . ILE   A 209 ? 0.0914 0.1576 0.1398 -0.0045 -0.0247 0.0104  209 ILE   A CB  
1761 C  CG1 . ILE   A 209 ? 0.1043 0.1650 0.1835 0.0141  -0.0293 -0.0041 209 ILE   A CG1 
1762 C  CG2 . ILE   A 209 ? 0.1009 0.1839 0.1628 0.0023  -0.0292 0.0179  209 ILE   A CG2 
1763 C  CD1 . ILE   A 209 ? 0.1212 0.1658 0.2061 0.0051  -0.0305 -0.0059 209 ILE   A CD1 
1764 N  N   . VAL   A 210 ? 0.0951 0.1476 0.1226 0.0047  -0.0163 -0.0075 210 VAL   A N   
1765 C  CA  . VAL   A 210 ? 0.0935 0.1284 0.1375 -0.0031 -0.0206 0.0030  210 VAL   A CA  
1766 C  C   . VAL   A 210 ? 0.0933 0.1573 0.1156 -0.0092 -0.0156 0.0043  210 VAL   A C   
1767 O  O   . VAL   A 210 ? 0.1005 0.1757 0.1213 -0.0070 -0.0117 0.0120  210 VAL   A O   
1768 C  CB  . VAL   A 210 ? 0.0962 0.1420 0.1372 0.0010  -0.0164 0.0103  210 VAL   A CB  
1769 C  CG1 . VAL   A 210 ? 0.0959 0.1545 0.1456 -0.0036 -0.0219 0.0017  210 VAL   A CG1 
1770 C  CG2 . VAL   A 210 ? 0.1119 0.1413 0.1497 -0.0087 -0.0331 0.0105  210 VAL   A CG2 
1771 N  N   . LEU   A 211 ? 0.0930 0.1605 0.1261 -0.0051 -0.0153 0.0038  211 LEU   A N   
1772 C  CA  . LEU   A 211 ? 0.0847 0.1698 0.1302 -0.0119 -0.0139 -0.0063 211 LEU   A CA  
1773 C  C   . LEU   A 211 ? 0.1076 0.1733 0.1297 -0.0170 -0.0292 0.0048  211 LEU   A C   
1774 O  O   . LEU   A 211 ? 0.1009 0.1775 0.1477 -0.0125 -0.0232 0.0157  211 LEU   A O   
1775 C  CB  . LEU   A 211 ? 0.0761 0.1799 0.1338 -0.0105 -0.0147 0.0047  211 LEU   A CB  
1776 C  CG  . LEU   A 211 ? 0.0891 0.1998 0.1603 -0.0075 -0.0363 0.0096  211 LEU   A CG  
1777 C  CD1 . LEU   A 211 ? 0.0981 0.2214 0.1813 -0.0063 -0.0432 0.0165  211 LEU   A CD1 
1778 C  CD2 . LEU   A 211 ? 0.1096 0.1956 0.1837 -0.0073 -0.0220 0.0115  211 LEU   A CD2 
1779 N  N   . LYS   A 212 ? 0.0925 0.1829 0.1506 -0.0119 -0.0280 0.0128  212 LYS   A N   
1780 C  CA  . LYS   A 212 ? 0.1259 0.1912 0.1426 -0.0179 -0.0428 0.0131  212 LYS   A CA  
1781 C  C   . LYS   A 212 ? 0.1071 0.1787 0.1531 -0.0236 -0.0300 0.0176  212 LYS   A C   
1782 O  O   . LYS   A 212 ? 0.1359 0.2032 0.1799 -0.0016 -0.0446 0.0277  212 LYS   A O   
1783 C  CB  . LYS   A 212 ? 0.1801 0.2385 0.1605 -0.0469 -0.0335 0.0024  212 LYS   A CB  
1784 C  CG  . LYS   A 212 ? 0.2565 0.2843 0.1799 -0.0474 -0.0542 0.0254  212 LYS   A CG  
1785 C  CD  . LYS   A 212 ? 0.3504 0.3358 0.2511 -0.0434 -0.0049 0.0309  212 LYS   A CD  
1786 C  CE  . LYS   A 212 ? 0.3730 0.3486 0.3544 -0.0308 -0.0033 0.0819  212 LYS   A CE  
1787 N  N   . GLU   A 213 ? 0.1155 0.1605 0.1422 -0.0176 -0.0344 0.0140  213 GLU   A N   
1788 C  CA  . GLU   A 213 ? 0.1249 0.1632 0.1394 -0.0221 -0.0327 0.0166  213 GLU   A CA  
1789 C  C   . GLU   A 213 ? 0.1119 0.1709 0.1339 -0.0208 -0.0329 0.0098  213 GLU   A C   
1790 O  O   . GLU   A 213 ? 0.1008 0.1743 0.1561 -0.0223 -0.0280 0.0115  213 GLU   A O   
1791 C  CB  . GLU   A 213 ? 0.1233 0.1917 0.1650 -0.0228 -0.0255 0.0165  213 GLU   A CB  
1792 C  CG  . GLU   A 213 ? 0.1511 0.2201 0.2121 -0.0385 -0.0426 0.0070  213 GLU   A CG  
1793 C  CD  . GLU   A 213 ? 0.1531 0.2627 0.2270 -0.0743 -0.0528 -0.0147 213 GLU   A CD  
1794 O  OE1 . GLU   A 213 ? 0.1248 0.2597 0.2817 -0.0358 -0.0439 -0.0074 213 GLU   A OE1 
1795 O  OE2 . GLU   A 213 ? 0.2412 0.3890 0.2682 -0.0372 -0.1051 0.0001  213 GLU   A OE2 
1796 N  N   A PRO   A 214 ? 0.1280 0.1685 0.1318 -0.0165 -0.0325 0.0116  214 PRO   A N   
1797 N  N   B PRO   A 214 ? 0.1256 0.1779 0.1391 -0.0174 -0.0318 0.0145  214 PRO   A N   
1798 C  CA  A PRO   A 214 ? 0.1334 0.1591 0.1328 -0.0244 -0.0366 -0.0019 214 PRO   A CA  
1799 C  CA  B PRO   A 214 ? 0.1269 0.1697 0.1467 -0.0243 -0.0294 0.0068  214 PRO   A CA  
1800 C  C   A PRO   A 214 ? 0.1283 0.1781 0.1483 -0.0348 -0.0374 0.0023  214 PRO   A C   
1801 C  C   B PRO   A 214 ? 0.1176 0.1678 0.1585 -0.0315 -0.0291 0.0147  214 PRO   A C   
1802 O  O   A PRO   A 214 ? 0.1330 0.1753 0.1590 -0.0332 -0.0274 -0.0149 214 PRO   A O   
1803 O  O   B PRO   A 214 ? 0.1153 0.1643 0.1715 -0.0280 -0.0309 0.0150  214 PRO   A O   
1804 C  CB  A PRO   A 214 ? 0.1255 0.1668 0.1341 -0.0209 -0.0421 -0.0002 214 PRO   A CB  
1805 C  CB  B PRO   A 214 ? 0.1222 0.1792 0.1627 -0.0210 -0.0228 0.0080  214 PRO   A CB  
1806 C  CG  A PRO   A 214 ? 0.1389 0.1540 0.1417 -0.0253 -0.0484 0.0048  214 PRO   A CG  
1807 C  CG  B PRO   A 214 ? 0.1395 0.1945 0.1717 -0.0319 -0.0307 0.0134  214 PRO   A CG  
1808 C  CD  A PRO   A 214 ? 0.1429 0.1613 0.1515 -0.0260 -0.0342 0.0009  214 PRO   A CD  
1809 C  CD  B PRO   A 214 ? 0.1344 0.1829 0.1525 -0.0259 -0.0402 0.0173  214 PRO   A CD  
1810 N  N   . ILE   A 215 ? 0.1247 0.1696 0.1521 -0.0468 -0.0307 -0.0054 215 ILE   A N   
1811 C  CA  . ILE   A 215 ? 0.1211 0.1989 0.1564 -0.0285 -0.0393 0.0019  215 ILE   A CA  
1812 C  C   . ILE   A 215 ? 0.1333 0.1893 0.1478 -0.0323 -0.0417 0.0038  215 ILE   A C   
1813 O  O   . ILE   A 215 ? 0.1273 0.1853 0.1987 -0.0307 -0.0414 -0.0076 215 ILE   A O   
1814 C  CB  . ILE   A 215 ? 0.1425 0.1984 0.1555 -0.0115 -0.0237 -0.0028 215 ILE   A CB  
1815 C  CG1 . ILE   A 215 ? 0.1431 0.1890 0.1262 -0.0118 -0.0315 0.0099  215 ILE   A CG1 
1816 C  CG2 . ILE   A 215 ? 0.1313 0.1890 0.1863 -0.0123 -0.0421 0.0012  215 ILE   A CG2 
1817 C  CD1 . ILE   A 215 ? 0.1623 0.1909 0.1571 0.0032  -0.0180 0.0174  215 ILE   A CD1 
1818 N  N   A SER   A 216 ? 0.1393 0.1662 0.1797 -0.0294 -0.0540 0.0062  216 SER   A N   
1819 N  N   B SER   A 216 ? 0.1412 0.1810 0.1889 -0.0338 -0.0584 0.0059  216 SER   A N   
1820 C  CA  A SER   A 216 ? 0.1548 0.1679 0.1666 -0.0307 -0.0725 -0.0009 216 SER   A CA  
1821 C  CA  B SER   A 216 ? 0.1642 0.1890 0.1850 -0.0318 -0.0752 0.0006  216 SER   A CA  
1822 C  C   A SER   A 216 ? 0.1613 0.1445 0.1677 -0.0220 -0.0728 -0.0039 216 SER   A C   
1823 C  C   B SER   A 216 ? 0.1641 0.1571 0.1830 -0.0198 -0.0740 -0.0007 216 SER   A C   
1824 O  O   A SER   A 216 ? 0.1718 0.1752 0.1662 -0.0152 -0.0718 0.0207  216 SER   A O   
1825 O  O   B SER   A 216 ? 0.1669 0.2010 0.1907 -0.0146 -0.0809 0.0252  216 SER   A O   
1826 C  CB  A SER   A 216 ? 0.1992 0.1586 0.1985 -0.0340 -0.0387 0.0118  216 SER   A CB  
1827 C  CB  B SER   A 216 ? 0.2233 0.1941 0.2341 -0.0419 -0.0302 0.0231  216 SER   A CB  
1828 O  OG  A SER   A 216 ? 0.1949 0.1775 0.1894 -0.0278 -0.0596 0.0113  216 SER   A OG  
1829 O  OG  B SER   A 216 ? 0.2731 0.2420 0.2644 -0.0159 -0.0439 0.0154  216 SER   A OG  
1830 N  N   . VAL   A 217 ? 0.1661 0.1553 0.1687 -0.0305 -0.0707 0.0044  217 VAL   A N   
1831 C  CA  . VAL   A 217 ? 0.1683 0.1300 0.1698 -0.0239 -0.0656 0.0037  217 VAL   A CA  
1832 C  C   . VAL   A 217 ? 0.1765 0.1606 0.1664 -0.0224 -0.0627 -0.0128 217 VAL   A C   
1833 O  O   . VAL   A 217 ? 0.1846 0.1627 0.1819 -0.0369 -0.0711 -0.0047 217 VAL   A O   
1834 C  CB  . VAL   A 217 ? 0.1730 0.1403 0.1838 -0.0199 -0.0631 0.0047  217 VAL   A CB  
1835 C  CG1 . VAL   A 217 ? 0.1621 0.1618 0.1897 -0.0144 -0.0638 0.0131  217 VAL   A CG1 
1836 C  CG2 . VAL   A 217 ? 0.1678 0.1618 0.2195 -0.0179 -0.0523 -0.0142 217 VAL   A CG2 
1837 N  N   . SER   A 218 ? 0.1719 0.1582 0.1577 -0.0295 -0.0689 -0.0018 218 SER   A N   
1838 C  CA  . SER   A 218 ? 0.1876 0.1709 0.1614 -0.0191 -0.0566 -0.0093 218 SER   A CA  
1839 C  C   . SER   A 218 ? 0.1778 0.1716 0.1933 -0.0178 -0.0785 0.0013  218 SER   A C   
1840 O  O   . SER   A 218 ? 0.1777 0.1618 0.1936 -0.0319 -0.0794 0.0089  218 SER   A O   
1841 C  CB  . SER   A 218 ? 0.1656 0.1852 0.1670 -0.0369 -0.0478 -0.0239 218 SER   A CB  
1842 O  OG  . SER   A 218 ? 0.1579 0.2038 0.1751 -0.0325 -0.0558 -0.0107 218 SER   A OG  
1843 N  N   A SER   A 219 ? 0.1740 0.1719 0.2118 -0.0059 -0.0835 0.0095  219 SER   A N   
1844 N  N   B SER   A 219 ? 0.1863 0.1677 0.2105 -0.0081 -0.0713 0.0144  219 SER   A N   
1845 C  CA  A SER   A 219 ? 0.1720 0.1752 0.2602 -0.0009 -0.0862 0.0012  219 SER   A CA  
1846 C  CA  B SER   A 219 ? 0.1922 0.1719 0.2575 -0.0027 -0.0660 0.0093  219 SER   A CA  
1847 C  C   A SER   A 219 ? 0.1630 0.1654 0.2670 -0.0205 -0.0718 -0.0048 219 SER   A C   
1848 C  C   B SER   A 219 ? 0.1584 0.1644 0.2714 -0.0156 -0.0621 0.0074  219 SER   A C   
1849 O  O   A SER   A 219 ? 0.1460 0.1651 0.2787 -0.0107 -0.0563 -0.0090 219 SER   A O   
1850 O  O   B SER   A 219 ? 0.1460 0.1743 0.3019 -0.0046 -0.0401 0.0054  219 SER   A O   
1851 C  CB  A SER   A 219 ? 0.1842 0.1851 0.2772 0.0033  -0.0889 -0.0101 219 SER   A CB  
1852 C  CB  B SER   A 219 ? 0.2257 0.1820 0.2724 -0.0004 -0.0473 0.0135  219 SER   A CB  
1853 O  OG  A SER   A 219 ? 0.1653 0.1765 0.2871 0.0139  -0.0986 -0.0089 219 SER   A OG  
1854 O  OG  B SER   A 219 ? 0.2541 0.2151 0.2587 0.0174  -0.0234 0.0313  219 SER   A OG  
1855 N  N   . GLU   A 220 ? 0.1548 0.1881 0.2413 -0.0207 -0.0523 0.0002  220 GLU   A N   
1856 C  CA  . GLU   A 220 ? 0.1970 0.1897 0.2168 -0.0040 -0.0616 -0.0111 220 GLU   A CA  
1857 C  C   . GLU   A 220 ? 0.1781 0.1920 0.1602 -0.0239 -0.0454 -0.0001 220 GLU   A C   
1858 O  O   . GLU   A 220 ? 0.1773 0.2164 0.2025 0.0084  -0.0239 0.0055  220 GLU   A O   
1859 C  CB  . GLU   A 220 ? 0.2026 0.2082 0.2036 -0.0076 -0.0534 -0.0432 220 GLU   A CB  
1860 C  CG  . GLU   A 220 ? 0.2112 0.2290 0.2708 0.0015  -0.0634 -0.0571 220 GLU   A CG  
1861 C  CD  . GLU   A 220 ? 0.2768 0.2198 0.3089 -0.0576 -0.0394 -0.0624 220 GLU   A CD  
1862 O  OE1 . GLU   A 220 ? 0.2530 0.2437 0.3020 -0.0535 -0.0287 -0.0799 220 GLU   A OE1 
1863 O  OE2 . GLU   A 220 ? 0.4221 0.3000 0.4362 -0.0935 -0.0525 -0.1229 220 GLU   A OE2 
1864 N  N   . GLN   A 221 ? 0.1826 0.1866 0.1577 -0.0197 -0.0543 -0.0146 221 GLN   A N   
1865 C  CA  . GLN   A 221 ? 0.1790 0.1910 0.1535 -0.0162 -0.0604 -0.0066 221 GLN   A CA  
1866 C  C   . GLN   A 221 ? 0.1675 0.1607 0.1705 -0.0134 -0.0510 0.0109  221 GLN   A C   
1867 O  O   . GLN   A 221 ? 0.1543 0.1896 0.1763 -0.0162 -0.0400 0.0071  221 GLN   A O   
1868 C  CB  . GLN   A 221 ? 0.1750 0.1638 0.1427 -0.0184 -0.0633 -0.0060 221 GLN   A CB  
1869 C  CG  . GLN   A 221 ? 0.1752 0.1722 0.1388 -0.0185 -0.0566 0.0019  221 GLN   A CG  
1870 C  CD  . GLN   A 221 ? 0.1681 0.1432 0.1584 -0.0246 -0.0526 -0.0009 221 GLN   A CD  
1871 O  OE1 . GLN   A 221 ? 0.1569 0.1780 0.1507 -0.0071 -0.0483 0.0068  221 GLN   A OE1 
1872 N  NE2 . GLN   A 221 ? 0.1584 0.1891 0.1601 0.0042  -0.0481 0.0028  221 GLN   A NE2 
1873 N  N   . VAL   A 222 ? 0.1568 0.1882 0.1774 -0.0344 -0.0525 0.0193  222 VAL   A N   
1874 C  CA  . VAL   A 222 ? 0.1585 0.2085 0.1826 -0.0305 -0.0545 0.0071  222 VAL   A CA  
1875 C  C   . VAL   A 222 ? 0.1771 0.2031 0.1845 -0.0163 -0.0461 0.0174  222 VAL   A C   
1876 O  O   . VAL   A 222 ? 0.1549 0.2135 0.2074 -0.0246 -0.0429 0.0077  222 VAL   A O   
1877 C  CB  . VAL   A 222 ? 0.1714 0.2674 0.2183 -0.0317 -0.0779 0.0365  222 VAL   A CB  
1878 C  CG1 . VAL   A 222 ? 0.2113 0.3100 0.2431 -0.0621 -0.0664 0.0410  222 VAL   A CG1 
1879 C  CG2 . VAL   A 222 ? 0.1982 0.2929 0.2199 -0.0554 -0.0734 0.0241  222 VAL   A CG2 
1880 N  N   . LEU   A 223 ? 0.1827 0.2008 0.2090 -0.0223 -0.0283 0.0064  223 LEU   A N   
1881 C  CA  . LEU   A 223 ? 0.1707 0.2265 0.2439 -0.0115 -0.0288 -0.0178 223 LEU   A CA  
1882 C  C   . LEU   A 223 ? 0.1752 0.2279 0.2249 -0.0190 -0.0240 -0.0218 223 LEU   A C   
1883 O  O   . LEU   A 223 ? 0.1769 0.2897 0.2212 -0.0145 0.0006  -0.0081 223 LEU   A O   
1884 C  CB  . LEU   A 223 ? 0.2268 0.2507 0.2845 -0.0255 -0.0145 -0.0362 223 LEU   A CB  
1885 C  CG  . LEU   A 223 ? 0.2677 0.2945 0.3362 -0.0347 -0.0340 -0.0304 223 LEU   A CG  
1886 C  CD1 . LEU   A 223 ? 0.3131 0.3406 0.3345 -0.0598 -0.0506 -0.0377 223 LEU   A CD1 
1887 C  CD2 . LEU   A 223 ? 0.2815 0.3185 0.3748 -0.0383 -0.0342 -0.0714 223 LEU   A CD2 
1888 N  N   . LYS   A 224 ? 0.1740 0.2298 0.1860 -0.0234 -0.0299 -0.0189 224 LYS   A N   
1889 C  CA  . LYS   A 224 ? 0.1762 0.2664 0.1840 -0.0197 -0.0430 -0.0072 224 LYS   A CA  
1890 C  C   . LYS   A 224 ? 0.1661 0.2365 0.1453 -0.0075 -0.0340 0.0047  224 LYS   A C   
1891 O  O   . LYS   A 224 ? 0.1799 0.2662 0.1461 -0.0109 -0.0313 0.0056  224 LYS   A O   
1892 C  CB  . LYS   A 224 ? 0.2030 0.3064 0.2052 -0.0141 -0.0561 0.0182  224 LYS   A CB  
1893 C  CG  . LYS   A 224 ? 0.2185 0.3611 0.2821 -0.0174 -0.0757 0.0056  224 LYS   A CG  
1894 N  N   . PHE   A 225 ? 0.1692 0.1903 0.1446 -0.0142 -0.0266 0.0009  225 PHE   A N   
1895 C  CA  . PHE   A 225 ? 0.1524 0.1744 0.1512 -0.0030 -0.0118 0.0000  225 PHE   A CA  
1896 C  C   . PHE   A 225 ? 0.1655 0.1951 0.1354 0.0013  -0.0057 0.0072  225 PHE   A C   
1897 O  O   . PHE   A 225 ? 0.1722 0.1910 0.1500 -0.0171 -0.0137 -0.0019 225 PHE   A O   
1898 C  CB  . PHE   A 225 ? 0.1572 0.1677 0.1523 -0.0098 -0.0203 -0.0042 225 PHE   A CB  
1899 C  CG  . PHE   A 225 ? 0.1460 0.1876 0.1675 -0.0070 -0.0214 -0.0039 225 PHE   A CG  
1900 C  CD1 . PHE   A 225 ? 0.1568 0.2336 0.1516 0.0139  -0.0178 -0.0143 225 PHE   A CD1 
1901 C  CD2 . PHE   A 225 ? 0.1401 0.2137 0.1839 0.0121  -0.0275 -0.0252 225 PHE   A CD2 
1902 C  CE1 . PHE   A 225 ? 0.1531 0.2486 0.1976 0.0137  -0.0134 0.0080  225 PHE   A CE1 
1903 C  CE2 . PHE   A 225 ? 0.1568 0.2516 0.2077 0.0194  -0.0283 -0.0394 225 PHE   A CE2 
1904 C  CZ  . PHE   A 225 ? 0.1319 0.2493 0.2228 0.0085  -0.0297 -0.0406 225 PHE   A CZ  
1905 N  N   . ARG   A 226 ? 0.1424 0.1893 0.1524 0.0000  -0.0034 0.0014  226 ARG   A N   
1906 C  CA  . ARG   A 226 ? 0.1545 0.2093 0.1535 0.0173  -0.0070 -0.0007 226 ARG   A CA  
1907 C  C   . ARG   A 226 ? 0.1748 0.2253 0.1560 0.0072  -0.0029 -0.0145 226 ARG   A C   
1908 O  O   . ARG   A 226 ? 0.1981 0.2446 0.2126 0.0237  0.0128  -0.0078 226 ARG   A O   
1909 C  CB  . ARG   A 226 ? 0.1843 0.2101 0.1714 0.0135  -0.0265 -0.0084 226 ARG   A CB  
1910 C  CG  . ARG   A 226 ? 0.1587 0.1965 0.1658 0.0137  -0.0280 0.0162  226 ARG   A CG  
1911 C  CD  . ARG   A 226 ? 0.1981 0.1978 0.1816 0.0162  -0.0245 -0.0026 226 ARG   A CD  
1912 N  NE  . ARG   A 226 ? 0.1867 0.1996 0.1668 -0.0226 -0.0395 -0.0164 226 ARG   A NE  
1913 C  CZ  . ARG   A 226 ? 0.2175 0.2084 0.1570 -0.0393 -0.0485 -0.0278 226 ARG   A CZ  
1914 N  NH1 . ARG   A 226 ? 0.2626 0.2691 0.1777 -0.0731 -0.0383 -0.0679 226 ARG   A NH1 
1915 N  NH2 . ARG   A 226 ? 0.2462 0.2182 0.1846 -0.0690 -0.0252 -0.0198 226 ARG   A NH2 
1916 N  N   . LYS   A 227 ? 0.1770 0.2183 0.1465 0.0064  -0.0125 -0.0149 227 LYS   A N   
1917 C  CA  . LYS   A 227 ? 0.2172 0.2481 0.1505 -0.0073 -0.0169 -0.0442 227 LYS   A CA  
1918 C  C   . LYS   A 227 ? 0.2129 0.2299 0.1503 0.0052  -0.0040 -0.0079 227 LYS   A C   
1919 O  O   . LYS   A 227 ? 0.2362 0.2743 0.1523 0.0005  0.0056  -0.0190 227 LYS   A O   
1920 C  CB  . LYS   A 227 ? 0.2300 0.3188 0.1790 -0.0246 -0.0351 -0.0475 227 LYS   A CB  
1921 C  CG  . LYS   A 227 ? 0.3078 0.3597 0.2742 -0.0474 -0.0414 -0.0567 227 LYS   A CG  
1922 C  CD  . LYS   A 227 ? 0.3889 0.4674 0.3627 -0.0498 -0.0644 -0.0817 227 LYS   A CD  
1923 C  CE  . LYS   A 227 ? 0.5794 0.5085 0.4839 -0.0242 -0.0588 -0.0613 227 LYS   A CE  
1924 N  NZ  . LYS   A 227 ? 0.6603 0.5856 0.5108 -0.0478 -0.0800 -0.0536 227 LYS   A NZ  
1925 N  N   . LEU   A 228 ? 0.1940 0.2268 0.1504 -0.0107 0.0023  0.0054  228 LEU   A N   
1926 C  CA  . LEU   A 228 ? 0.1889 0.2237 0.1390 -0.0107 -0.0005 -0.0001 228 LEU   A CA  
1927 C  C   . LEU   A 228 ? 0.2012 0.2366 0.1532 0.0084  0.0064  -0.0205 228 LEU   A C   
1928 O  O   . LEU   A 228 ? 0.1813 0.2437 0.1605 0.0040  0.0110  -0.0074 228 LEU   A O   
1929 C  CB  . LEU   A 228 ? 0.1742 0.2384 0.1304 -0.0122 -0.0089 0.0004  228 LEU   A CB  
1930 C  CG  . LEU   A 228 ? 0.1690 0.2460 0.1519 -0.0140 -0.0334 0.0107  228 LEU   A CG  
1931 C  CD1 . LEU   A 228 ? 0.1688 0.2425 0.1661 -0.0238 -0.0284 0.0033  228 LEU   A CD1 
1932 C  CD2 . LEU   A 228 ? 0.1921 0.2828 0.1647 0.0029  -0.0159 0.0262  228 LEU   A CD2 
1933 N  N   . ASN   A 229 ? 0.1782 0.2723 0.1738 0.0048  0.0178  0.0029  229 ASN   A N   
1934 C  CA  . ASN   A 229 ? 0.1876 0.2677 0.1972 -0.0042 0.0249  0.0049  229 ASN   A CA  
1935 C  C   . ASN   A 229 ? 0.1505 0.2613 0.1963 0.0038  0.0101  0.0051  229 ASN   A C   
1936 O  O   . ASN   A 229 ? 0.1814 0.2428 0.1747 0.0175  0.0157  0.0006  229 ASN   A O   
1937 C  CB  . ASN   A 229 ? 0.2020 0.3189 0.1842 -0.0055 0.0317  -0.0175 229 ASN   A CB  
1938 C  CG  . ASN   A 229 ? 0.2565 0.3374 0.1986 -0.0252 0.0433  -0.0336 229 ASN   A CG  
1939 O  OD1 . ASN   A 229 ? 0.3867 0.3791 0.2055 -0.0260 0.0595  -0.0264 229 ASN   A OD1 
1940 N  ND2 . ASN   A 229 ? 0.2847 0.3442 0.2018 -0.0454 0.0303  -0.0716 229 ASN   A ND2 
1941 N  N   . PHE   A 230 ? 0.1694 0.2544 0.1846 0.0097  0.0237  0.0001  230 PHE   A N   
1942 C  CA  . PHE   A 230 ? 0.1691 0.2623 0.1917 -0.0135 0.0083  -0.0010 230 PHE   A CA  
1943 C  C   . PHE   A 230 ? 0.1709 0.2713 0.2017 -0.0113 0.0118  -0.0094 230 PHE   A C   
1944 O  O   . PHE   A 230 ? 0.1930 0.2601 0.1996 -0.0333 0.0175  0.0216  230 PHE   A O   
1945 C  CB  . PHE   A 230 ? 0.1850 0.2639 0.1887 -0.0051 0.0047  -0.0076 230 PHE   A CB  
1946 C  CG  . PHE   A 230 ? 0.1725 0.2581 0.1742 -0.0123 -0.0166 -0.0058 230 PHE   A CG  
1947 C  CD1 . PHE   A 230 ? 0.1628 0.2785 0.1952 -0.0110 -0.0025 -0.0066 230 PHE   A CD1 
1948 C  CD2 . PHE   A 230 ? 0.1694 0.2721 0.2237 -0.0054 0.0120  -0.0138 230 PHE   A CD2 
1949 C  CE1 . PHE   A 230 ? 0.1813 0.2560 0.1813 -0.0183 -0.0143 -0.0247 230 PHE   A CE1 
1950 C  CE2 . PHE   A 230 ? 0.1719 0.2497 0.2087 -0.0103 0.0027  0.0001  230 PHE   A CE2 
1951 C  CZ  . PHE   A 230 ? 0.1680 0.2568 0.1756 0.0004  -0.0191 -0.0074 230 PHE   A CZ  
1952 N  N   . ASN   A 231 ? 0.1757 0.2694 0.1980 -0.0256 0.0200  -0.0231 231 ASN   A N   
1953 C  CA  . ASN   A 231 ? 0.1854 0.2718 0.2272 -0.0250 0.0301  -0.0131 231 ASN   A CA  
1954 C  C   . ASN   A 231 ? 0.2172 0.3047 0.2087 -0.0290 0.0541  0.0209  231 ASN   A C   
1955 O  O   . ASN   A 231 ? 0.2299 0.2897 0.1950 -0.0109 0.0386  -0.0201 231 ASN   A O   
1956 C  CB  . ASN   A 231 ? 0.2376 0.3013 0.2464 -0.0049 0.0508  -0.0264 231 ASN   A CB  
1957 C  CG  . ASN   A 231 ? 0.2391 0.3086 0.2030 -0.0030 0.0459  -0.0319 231 ASN   A CG  
1958 O  OD1 . ASN   A 231 ? 0.2424 0.3241 0.2327 -0.0018 0.0602  -0.0342 231 ASN   A OD1 
1959 N  ND2 . ASN   A 231 ? 0.3470 0.3902 0.1996 -0.0033 0.0402  -0.0209 231 ASN   A ND2 
1960 N  N   . GLY   A 232 ? 0.2132 0.3290 0.2293 -0.0419 0.0411  0.0307  232 GLY   A N   
1961 C  CA  . GLY   A 232 ? 0.2544 0.3413 0.2311 -0.0494 0.0584  0.0268  232 GLY   A CA  
1962 C  C   . GLY   A 232 ? 0.2997 0.3783 0.2098 -0.0766 0.0689  0.0287  232 GLY   A C   
1963 O  O   . GLY   A 232 ? 0.3236 0.4176 0.2415 -0.0541 0.0558  -0.0162 232 GLY   A O   
1964 N  N   . GLU   A 233 ? 0.3328 0.4428 0.2103 -0.1047 0.0524  0.0302  233 GLU   A N   
1965 C  CA  . GLU   A 233 ? 0.3937 0.5142 0.2361 -0.1238 0.0817  0.0235  233 GLU   A CA  
1966 C  C   . GLU   A 233 ? 0.4219 0.5196 0.2411 -0.0832 0.0820  0.0175  233 GLU   A C   
1967 O  O   . GLU   A 233 ? 0.3945 0.5119 0.2844 -0.0792 0.1298  0.0428  233 GLU   A O   
1968 C  CB  . GLU   A 233 ? 0.4086 0.5626 0.2922 -0.1314 0.0884  0.0492  233 GLU   A CB  
1969 C  CG  . GLU   A 233 ? 0.4275 0.6157 0.3095 -0.1851 0.0904  0.1030  233 GLU   A CG  
1970 C  CD  . GLU   A 233 ? 0.4296 0.7269 0.3548 -0.1019 0.0308  0.0519  233 GLU   A CD  
1971 O  OE1 . GLU   A 233 ? 0.4166 0.8285 0.3281 -0.0625 0.0721  0.1015  233 GLU   A OE1 
1972 O  OE2 . GLU   A 233 ? 0.4842 0.7942 0.4671 -0.1245 -0.0136 0.0269  233 GLU   A OE2 
1973 N  N   . GLY   A 234 ? 0.4709 0.5982 0.2896 -0.0206 0.1151  -0.0240 234 GLY   A N   
1974 C  CA  . GLY   A 234 ? 0.4755 0.6749 0.3454 -0.0280 0.1117  0.0000  234 GLY   A CA  
1975 C  C   . GLY   A 234 ? 0.4546 0.7247 0.3370 -0.0208 0.1516  0.0181  234 GLY   A C   
1976 O  O   . GLY   A 234 ? 0.4439 0.8191 0.3909 0.0210  0.1823  0.0005  234 GLY   A O   
1977 N  N   . GLU   A 235 ? 0.4568 0.6565 0.3282 -0.0261 0.2112  -0.0136 235 GLU   A N   
1978 C  CA  . GLU   A 235 ? 0.4585 0.5291 0.3715 0.0063  0.1963  -0.0388 235 GLU   A CA  
1979 C  C   . GLU   A 235 ? 0.4223 0.5595 0.3458 -0.0283 0.2030  -0.0567 235 GLU   A C   
1980 O  O   . GLU   A 235 ? 0.4790 0.5176 0.3356 -0.0763 0.1397  -0.0909 235 GLU   A O   
1981 C  CB  . GLU   A 235 ? 0.4341 0.4705 0.4137 -0.0349 0.2020  -0.0275 235 GLU   A CB  
1982 C  CG  . GLU   A 235 ? 0.4313 0.4361 0.4759 -0.0546 0.2160  0.0008  235 GLU   A CG  
1983 C  CD  . GLU   A 235 ? 0.4666 0.4733 0.5354 -0.0773 0.1905  -0.0204 235 GLU   A CD  
1984 O  OE1 . GLU   A 235 ? 0.2829 0.4853 0.5711 -0.0559 0.1242  0.0023  235 GLU   A OE1 
1985 O  OE2 . GLU   A 235 ? 0.5562 0.4915 0.5618 -0.0403 0.2121  0.0440  235 GLU   A OE2 
1986 N  N   . PRO   A 236 ? 0.4180 0.4912 0.4373 -0.0099 0.2212  -0.0803 236 PRO   A N   
1987 C  CA  . PRO   A 236 ? 0.4123 0.4821 0.4186 -0.0213 0.2338  -0.0795 236 PRO   A CA  
1988 C  C   . PRO   A 236 ? 0.4173 0.4088 0.3416 -0.0374 0.2202  -0.1062 236 PRO   A C   
1989 O  O   . PRO   A 236 ? 0.4588 0.4317 0.3748 -0.0196 0.1840  -0.1323 236 PRO   A O   
1990 C  CB  . PRO   A 236 ? 0.4282 0.4527 0.5075 -0.0100 0.2252  -0.1071 236 PRO   A CB  
1991 C  CG  . PRO   A 236 ? 0.4274 0.4868 0.5008 -0.0079 0.2177  -0.1040 236 PRO   A CG  
1992 C  CD  . PRO   A 236 ? 0.4245 0.4520 0.4936 0.0006  0.1929  -0.1084 236 PRO   A CD  
1993 N  N   . GLU   A 237 ? 0.4464 0.3885 0.3309 -0.0338 0.2047  -0.1050 237 GLU   A N   
1994 C  CA  . GLU   A 237 ? 0.4445 0.3751 0.2747 -0.0387 0.1881  -0.1007 237 GLU   A CA  
1995 C  C   . GLU   A 237 ? 0.3817 0.3098 0.3188 0.0038  0.1271  -0.0849 237 GLU   A C   
1996 O  O   . GLU   A 237 ? 0.4686 0.3414 0.3347 0.0438  0.1517  -0.0633 237 GLU   A O   
1997 C  CB  . GLU   A 237 ? 0.5144 0.3927 0.3711 -0.0764 0.1260  -0.1204 237 GLU   A CB  
1998 C  CG  . GLU   A 237 ? 0.5757 0.4484 0.3736 -0.1042 0.1325  -0.1803 237 GLU   A CG  
1999 C  CD  . GLU   A 237 ? 0.5826 0.5367 0.4208 -0.1299 0.1300  -0.2301 237 GLU   A CD  
2000 O  OE1 . GLU   A 237 ? 0.7419 0.5346 0.5728 -0.1275 0.1698  -0.2998 237 GLU   A OE1 
2001 O  OE2 . GLU   A 237 ? 0.4501 0.4878 0.3778 -0.2015 0.0972  -0.1931 237 GLU   A OE2 
2002 N  N   . GLU   A 238 ? 0.2798 0.2640 0.2682 -0.0216 0.1077  -0.0509 238 GLU   A N   
2003 C  CA  . GLU   A 238 ? 0.2239 0.2511 0.2902 -0.0007 0.0835  -0.0323 238 GLU   A CA  
2004 C  C   . GLU   A 238 ? 0.2219 0.2479 0.2698 0.0045  0.0759  -0.0301 238 GLU   A C   
2005 O  O   . GLU   A 238 ? 0.2345 0.2624 0.3135 -0.0101 0.0816  -0.0092 238 GLU   A O   
2006 C  CB  . GLU   A 238 ? 0.1980 0.2445 0.3757 -0.0153 0.0866  -0.0678 238 GLU   A CB  
2007 N  N   . LEU   A 239 ? 0.1961 0.2238 0.2260 0.0307  0.0452  -0.0187 239 LEU   A N   
2008 C  CA  . LEU   A 239 ? 0.1887 0.2410 0.1912 0.0402  0.0150  -0.0064 239 LEU   A CA  
2009 C  C   . LEU   A 239 ? 0.1646 0.2394 0.1491 0.0201  0.0247  0.0109  239 LEU   A C   
2010 O  O   . LEU   A 239 ? 0.1670 0.2784 0.1772 0.0426  0.0144  0.0222  239 LEU   A O   
2011 C  CB  . LEU   A 239 ? 0.2077 0.2423 0.2405 0.0277  0.0199  -0.0106 239 LEU   A CB  
2012 C  CG  . LEU   A 239 ? 0.2007 0.2840 0.2959 0.0463  0.0142  -0.0255 239 LEU   A CG  
2013 C  CD1 . LEU   A 239 ? 0.1948 0.2801 0.4011 0.0654  -0.0074 -0.0340 239 LEU   A CD1 
2014 C  CD2 . LEU   A 239 ? 0.2375 0.2781 0.2547 0.0578  -0.0024 -0.0584 239 LEU   A CD2 
2015 N  N   . MET   A 240 ? 0.1589 0.2207 0.1436 0.0120  0.0070  -0.0100 240 MET   A N   
2016 C  CA  . MET   A 240 ? 0.1530 0.2156 0.1482 0.0185  0.0049  -0.0014 240 MET   A CA  
2017 C  C   . MET   A 240 ? 0.1506 0.2162 0.1327 0.0072  0.0037  -0.0075 240 MET   A C   
2018 O  O   . MET   A 240 ? 0.1386 0.2436 0.1358 0.0170  -0.0047 0.0039  240 MET   A O   
2019 C  CB  . MET   A 240 ? 0.1425 0.2086 0.1741 0.0065  -0.0069 0.0037  240 MET   A CB  
2020 C  CG  . MET   A 240 ? 0.1449 0.2100 0.1721 -0.0032 0.0008  -0.0070 240 MET   A CG  
2021 S  SD  . MET   A 240 ? 0.1629 0.2167 0.1907 -0.0052 0.0207  0.0036  240 MET   A SD  
2022 C  CE  . MET   A 240 ? 0.1748 0.1982 0.1882 -0.0001 0.0094  0.0117  240 MET   A CE  
2023 N  N   . VAL   A 241 ? 0.1395 0.2107 0.1458 0.0093  -0.0156 -0.0010 241 VAL   A N   
2024 C  CA  . VAL   A 241 ? 0.1536 0.1959 0.1438 0.0153  -0.0065 -0.0094 241 VAL   A CA  
2025 C  C   . VAL   A 241 ? 0.1406 0.1868 0.1414 0.0105  -0.0164 -0.0082 241 VAL   A C   
2026 O  O   . VAL   A 241 ? 0.1345 0.2254 0.1470 0.0131  -0.0039 -0.0170 241 VAL   A O   
2027 C  CB  . VAL   A 241 ? 0.1747 0.2074 0.1470 0.0028  -0.0057 -0.0284 241 VAL   A CB  
2028 C  CG1 . VAL   A 241 ? 0.2015 0.2324 0.1489 -0.0070 -0.0041 -0.0328 241 VAL   A CG1 
2029 C  CG2 . VAL   A 241 ? 0.1831 0.2005 0.1546 0.0055  0.0102  -0.0343 241 VAL   A CG2 
2030 N  N   . ASP   A 242 ? 0.1192 0.1795 0.1377 0.0072  -0.0255 -0.0182 242 ASP   A N   
2031 C  CA  . ASP   A 242 ? 0.1187 0.1829 0.1323 0.0115  -0.0194 -0.0200 242 ASP   A CA  
2032 C  C   . ASP   A 242 ? 0.1145 0.1777 0.1437 0.0051  -0.0213 -0.0174 242 ASP   A C   
2033 O  O   . ASP   A 242 ? 0.1179 0.2134 0.1730 0.0146  -0.0455 -0.0173 242 ASP   A O   
2034 C  CB  . ASP   A 242 ? 0.1323 0.1863 0.1437 0.0207  -0.0258 -0.0142 242 ASP   A CB  
2035 C  CG  . ASP   A 242 ? 0.1300 0.1977 0.1518 0.0248  -0.0203 -0.0050 242 ASP   A CG  
2036 O  OD1 . ASP   A 242 ? 0.1484 0.1976 0.1516 0.0266  -0.0142 0.0021  242 ASP   A OD1 
2037 O  OD2 . ASP   A 242 ? 0.1513 0.2082 0.2190 0.0306  -0.0019 -0.0315 242 ASP   A OD2 
2038 N  N   . ASN   A 243 ? 0.1211 0.1633 0.1329 0.0036  -0.0171 -0.0150 243 ASN   A N   
2039 C  CA  . ASN   A 243 ? 0.1007 0.1665 0.1280 -0.0129 -0.0096 -0.0003 243 ASN   A CA  
2040 C  C   . ASN   A 243 ? 0.0941 0.1524 0.1339 -0.0140 -0.0213 -0.0042 243 ASN   A C   
2041 O  O   . ASN   A 243 ? 0.1382 0.1789 0.1483 0.0295  -0.0185 -0.0046 243 ASN   A O   
2042 C  CB  . ASN   A 243 ? 0.1159 0.1906 0.1290 -0.0148 -0.0124 0.0050  243 ASN   A CB  
2043 C  CG  . ASN   A 243 ? 0.1110 0.1870 0.1373 -0.0034 -0.0197 0.0103  243 ASN   A CG  
2044 O  OD1 . ASN   A 243 ? 0.1093 0.2046 0.1716 -0.0028 -0.0217 0.0232  243 ASN   A OD1 
2045 N  ND2 . ASN   A 243 ? 0.0944 0.2067 0.1745 -0.0147 -0.0347 0.0246  243 ASN   A ND2 
2046 N  N   . TRP   A 244 ? 0.0975 0.1537 0.1339 0.0047  -0.0143 0.0014  244 TRP   A N   
2047 C  CA  . TRP   A 244 ? 0.1051 0.1561 0.1194 0.0047  -0.0149 -0.0013 244 TRP   A CA  
2048 C  C   . TRP   A 244 ? 0.1034 0.1699 0.1347 0.0133  -0.0215 0.0023  244 TRP   A C   
2049 O  O   . TRP   A 244 ? 0.1117 0.1843 0.1513 0.0186  -0.0290 -0.0124 244 TRP   A O   
2050 C  CB  . TRP   A 244 ? 0.1084 0.1671 0.1334 0.0106  -0.0130 -0.0085 244 TRP   A CB  
2051 C  CG  . TRP   A 244 ? 0.1071 0.1710 0.1314 0.0219  -0.0079 -0.0071 244 TRP   A CG  
2052 C  CD1 . TRP   A 244 ? 0.1280 0.1791 0.1305 0.0169  -0.0133 -0.0133 244 TRP   A CD1 
2053 C  CD2 . TRP   A 244 ? 0.1259 0.1667 0.1354 0.0076  -0.0056 -0.0003 244 TRP   A CD2 
2054 N  NE1 . TRP   A 244 ? 0.1339 0.1807 0.1341 0.0132  -0.0151 -0.0203 244 TRP   A NE1 
2055 C  CE2 . TRP   A 244 ? 0.1389 0.1810 0.1462 0.0082  -0.0089 -0.0095 244 TRP   A CE2 
2056 C  CE3 . TRP   A 244 ? 0.1317 0.1858 0.1498 0.0190  -0.0144 -0.0095 244 TRP   A CE3 
2057 C  CZ2 . TRP   A 244 ? 0.1707 0.1804 0.1682 0.0193  -0.0241 -0.0157 244 TRP   A CZ2 
2058 C  CZ3 . TRP   A 244 ? 0.1585 0.1951 0.1383 0.0121  -0.0264 -0.0029 244 TRP   A CZ3 
2059 C  CH2 . TRP   A 244 ? 0.1557 0.1901 0.1586 0.0380  -0.0092 0.0009  244 TRP   A CH2 
2060 N  N   . ARG   A 245 ? 0.0974 0.1884 0.1435 0.0109  -0.0236 -0.0211 245 ARG   A N   
2061 C  CA  . ARG   A 245 ? 0.0890 0.1901 0.1369 0.0022  -0.0243 -0.0189 245 ARG   A CA  
2062 C  C   . ARG   A 245 ? 0.1136 0.1805 0.1436 0.0059  -0.0183 -0.0215 245 ARG   A C   
2063 O  O   . ARG   A 245 ? 0.1169 0.2090 0.1485 -0.0052 -0.0103 -0.0174 245 ARG   A O   
2064 C  CB  . ARG   A 245 ? 0.1029 0.2002 0.1498 -0.0154 -0.0233 -0.0209 245 ARG   A CB  
2065 C  CG  . ARG   A 245 ? 0.0987 0.1817 0.1561 -0.0015 -0.0312 -0.0104 245 ARG   A CG  
2066 C  CD  . ARG   A 245 ? 0.1003 0.1884 0.1311 -0.0041 -0.0302 -0.0112 245 ARG   A CD  
2067 N  NE  . ARG   A 245 ? 0.0886 0.1902 0.1533 -0.0051 -0.0364 -0.0208 245 ARG   A NE  
2068 C  CZ  . ARG   A 245 ? 0.0956 0.1987 0.1440 -0.0246 -0.0304 -0.0137 245 ARG   A CZ  
2069 N  NH1 . ARG   A 245 ? 0.1147 0.1969 0.1564 -0.0222 -0.0269 -0.0186 245 ARG   A NH1 
2070 N  NH2 . ARG   A 245 ? 0.0913 0.2130 0.1732 -0.0293 -0.0301 -0.0336 245 ARG   A NH2 
2071 N  N   A PRO   A 246 ? 0.1163 0.1823 0.1460 0.0066  -0.0093 -0.0188 246 PRO   A N   
2072 N  N   B PRO   A 246 ? 0.1133 0.1956 0.1468 0.0130  -0.0076 -0.0108 246 PRO   A N   
2073 C  CA  A PRO   A 246 ? 0.1169 0.1747 0.1490 0.0067  -0.0158 -0.0099 246 PRO   A CA  
2074 C  CA  B PRO   A 246 ? 0.1215 0.1888 0.1476 0.0165  -0.0177 0.0023  246 PRO   A CA  
2075 C  C   A PRO   A 246 ? 0.1128 0.1764 0.1404 0.0179  -0.0169 -0.0037 246 PRO   A C   
2076 C  C   B PRO   A 246 ? 0.1218 0.1910 0.1372 0.0240  -0.0180 0.0057  246 PRO   A C   
2077 O  O   A PRO   A 246 ? 0.1084 0.1840 0.1512 0.0076  -0.0249 -0.0173 246 PRO   A O   
2078 O  O   B PRO   A 246 ? 0.1427 0.1940 0.1303 0.0212  -0.0296 0.0033  246 PRO   A O   
2079 C  CB  A PRO   A 246 ? 0.1303 0.1774 0.1595 0.0163  -0.0160 -0.0074 246 PRO   A CB  
2080 C  CB  B PRO   A 246 ? 0.1268 0.1996 0.1638 0.0252  -0.0157 0.0076  246 PRO   A CB  
2081 C  CG  A PRO   A 246 ? 0.1273 0.1858 0.1555 0.0203  -0.0144 -0.0147 246 PRO   A CG  
2082 C  CG  B PRO   A 246 ? 0.1214 0.2040 0.1702 0.0334  -0.0114 0.0036  246 PRO   A CG  
2083 C  CD  A PRO   A 246 ? 0.1206 0.1880 0.1587 0.0206  -0.0173 -0.0156 246 PRO   A CD  
2084 C  CD  B PRO   A 246 ? 0.1133 0.2073 0.1495 0.0299  -0.0167 -0.0108 246 PRO   A CD  
2085 N  N   . ALA   A 247 ? 0.1322 0.1775 0.1475 0.0191  -0.0100 0.0086  247 ALA   A N   
2086 C  CA  . ALA   A 247 ? 0.1322 0.1976 0.1300 0.0049  -0.0242 -0.0011 247 ALA   A CA  
2087 C  C   . ALA   A 247 ? 0.1224 0.1720 0.1460 0.0226  -0.0361 0.0055  247 ALA   A C   
2088 O  O   . ALA   A 247 ? 0.1359 0.1893 0.1883 0.0417  -0.0264 0.0060  247 ALA   A O   
2089 C  CB  . ALA   A 247 ? 0.1606 0.2140 0.1415 0.0015  -0.0258 0.0074  247 ALA   A CB  
2090 N  N   . GLN   A 248 ? 0.1086 0.1914 0.1449 0.0267  -0.0316 -0.0041 248 GLN   A N   
2091 C  CA  . GLN   A 248 ? 0.1109 0.2056 0.1571 0.0174  -0.0383 -0.0004 248 GLN   A CA  
2092 C  C   . GLN   A 248 ? 0.1244 0.2195 0.1565 0.0338  -0.0379 0.0031  248 GLN   A C   
2093 O  O   . GLN   A 248 ? 0.1367 0.2173 0.1525 0.0205  -0.0297 0.0202  248 GLN   A O   
2094 C  CB  . GLN   A 248 ? 0.1057 0.2026 0.1554 0.0061  -0.0416 -0.0174 248 GLN   A CB  
2095 C  CG  . GLN   A 248 ? 0.1389 0.2067 0.1505 -0.0034 -0.0426 -0.0127 248 GLN   A CG  
2096 C  CD  . GLN   A 248 ? 0.1448 0.2372 0.1770 -0.0134 -0.0336 0.0008  248 GLN   A CD  
2097 O  OE1 . GLN   A 248 ? 0.1273 0.2737 0.2084 -0.0119 -0.0254 -0.0187 248 GLN   A OE1 
2098 N  NE2 . GLN   A 248 ? 0.1236 0.2559 0.1792 0.0071  -0.0337 -0.0002 248 GLN   A NE2 
2099 N  N   . PRO   A 249 ? 0.1308 0.2466 0.1516 0.0508  -0.0445 -0.0055 249 PRO   A N   
2100 C  CA  . PRO   A 249 ? 0.1554 0.2382 0.1602 0.0583  -0.0498 -0.0010 249 PRO   A CA  
2101 C  C   . PRO   A 249 ? 0.1632 0.2052 0.1527 0.0421  -0.0480 -0.0047 249 PRO   A C   
2102 O  O   . PRO   A 249 ? 0.1362 0.2309 0.1484 0.0205  -0.0458 0.0109  249 PRO   A O   
2103 C  CB  . PRO   A 249 ? 0.1560 0.2806 0.1891 0.0801  -0.0740 -0.0138 249 PRO   A CB  
2104 C  CG  . PRO   A 249 ? 0.1605 0.3297 0.2018 0.0447  -0.0657 -0.0115 249 PRO   A CG  
2105 C  CD  . PRO   A 249 ? 0.1278 0.2814 0.1982 0.0317  -0.0636 -0.0172 249 PRO   A CD  
2106 N  N   . LEU   A 250 ? 0.1799 0.1967 0.1522 0.0374  -0.0442 0.0031  250 LEU   A N   
2107 C  CA  . LEU   A 250 ? 0.1602 0.1850 0.1675 0.0337  -0.0329 -0.0008 250 LEU   A CA  
2108 C  C   . LEU   A 250 ? 0.1429 0.2043 0.1488 0.0281  -0.0455 -0.0032 250 LEU   A C   
2109 O  O   . LEU   A 250 ? 0.1613 0.2005 0.1597 0.0333  -0.0535 -0.0211 250 LEU   A O   
2110 C  CB  . LEU   A 250 ? 0.1904 0.2074 0.1882 0.0126  -0.0187 -0.0023 250 LEU   A CB  
2111 C  CG  . LEU   A 250 ? 0.2008 0.2411 0.1891 -0.0010 0.0040  -0.0179 250 LEU   A CG  
2112 C  CD1 . LEU   A 250 ? 0.1731 0.2676 0.1906 -0.0097 -0.0241 -0.0430 250 LEU   A CD1 
2113 C  CD2 . LEU   A 250 ? 0.2574 0.2766 0.2216 -0.0316 0.0156  -0.0145 250 LEU   A CD2 
2114 N  N   . LYS   A 251 ? 0.1561 0.2371 0.1515 0.0440  -0.0584 -0.0180 251 LYS   A N   
2115 C  CA  . LYS   A 251 ? 0.1753 0.2662 0.1470 0.0429  -0.0706 -0.0324 251 LYS   A CA  
2116 C  C   . LYS   A 251 ? 0.1639 0.2878 0.1842 0.0532  -0.0669 -0.0209 251 LYS   A C   
2117 O  O   . LYS   A 251 ? 0.2393 0.3342 0.2032 0.0132  -0.0298 0.0163  251 LYS   A O   
2118 C  CB  . LYS   A 251 ? 0.2026 0.2754 0.1849 0.0162  -0.0904 -0.0466 251 LYS   A CB  
2119 C  CG  . LYS   A 251 ? 0.2747 0.3258 0.2324 -0.0045 -0.0384 -0.0601 251 LYS   A CG  
2120 C  CD  . LYS   A 251 ? 0.2794 0.4065 0.3086 -0.0006 -0.0490 -0.0775 251 LYS   A CD  
2121 C  CE  . LYS   A 251 ? 0.3376 0.4120 0.3879 0.0478  -0.0052 -0.1116 251 LYS   A CE  
2122 N  N   . ASN   A 252 ? 0.1819 0.3138 0.1743 0.0311  -0.0604 -0.0415 252 ASN   A N   
2123 C  CA  . ASN   A 252 ? 0.2364 0.4008 0.2384 0.0270  -0.0541 -0.0626 252 ASN   A CA  
2124 C  C   . ASN   A 252 ? 0.2641 0.3686 0.3038 0.0741  -0.0473 -0.0656 252 ASN   A C   
2125 O  O   . ASN   A 252 ? 0.3559 0.4118 0.3533 0.1176  -0.0494 -0.0441 252 ASN   A O   
2126 C  CB  . ASN   A 252 ? 0.2777 0.4387 0.2795 -0.0021 -0.0468 -0.0817 252 ASN   A CB  
2127 N  N   . ARG   A 253 ? 0.1623 0.3130 0.1679 0.0431  -0.0174 -0.0106 253 ARG   A N   
2128 C  CA  . ARG   A 253 ? 0.1335 0.2350 0.1557 0.0230  -0.0129 -0.0155 253 ARG   A CA  
2129 C  C   . ARG   A 253 ? 0.1808 0.2307 0.1727 0.0145  -0.0160 -0.0020 253 ARG   A C   
2130 O  O   . ARG   A 253 ? 0.2472 0.2601 0.2661 0.0194  0.0640  0.0339  253 ARG   A O   
2131 C  CB  . ARG   A 253 ? 0.1436 0.1952 0.1359 0.0116  -0.0205 -0.0185 253 ARG   A CB  
2132 C  CG  . ARG   A 253 ? 0.1502 0.1903 0.1203 0.0105  -0.0298 -0.0120 253 ARG   A CG  
2133 C  CD  . ARG   A 253 ? 0.1529 0.1998 0.1209 0.0290  -0.0303 -0.0040 253 ARG   A CD  
2134 N  NE  . ARG   A 253 ? 0.1237 0.1830 0.1307 0.0358  -0.0372 0.0041  253 ARG   A NE  
2135 C  CZ  . ARG   A 253 ? 0.1079 0.1802 0.1230 0.0124  -0.0371 -0.0005 253 ARG   A CZ  
2136 N  NH1 . ARG   A 253 ? 0.1029 0.1863 0.1288 0.0193  -0.0390 0.0005  253 ARG   A NH1 
2137 N  NH2 . ARG   A 253 ? 0.1070 0.1778 0.1086 0.0116  -0.0439 -0.0019 253 ARG   A NH2 
2138 N  N   . GLN   A 254 ? 0.1741 0.2646 0.1915 0.0005  -0.0175 -0.0359 254 GLN   A N   
2139 C  CA  . GLN   A 254 ? 0.1691 0.2871 0.1922 -0.0153 -0.0400 -0.0412 254 GLN   A CA  
2140 C  C   . GLN   A 254 ? 0.1533 0.2356 0.1839 0.0182  -0.0417 -0.0127 254 GLN   A C   
2141 O  O   . GLN   A 254 ? 0.2305 0.2102 0.2881 0.0010  -0.0875 -0.0250 254 GLN   A O   
2142 C  CB  . GLN   A 254 ? 0.2097 0.3548 0.2231 -0.0144 -0.0136 -0.0594 254 GLN   A CB  
2143 N  N   . ILE   A 255 ? 0.1390 0.2307 0.1505 0.0082  -0.0303 0.0031  255 ILE   A N   
2144 C  CA  . ILE   A 255 ? 0.1321 0.2182 0.1340 0.0190  -0.0268 0.0092  255 ILE   A CA  
2145 C  C   . ILE   A 255 ? 0.1406 0.2021 0.1518 0.0107  -0.0087 0.0085  255 ILE   A C   
2146 O  O   . ILE   A 255 ? 0.1671 0.2251 0.1592 0.0198  -0.0165 0.0245  255 ILE   A O   
2147 C  CB  . ILE   A 255 ? 0.1347 0.2063 0.1490 0.0005  -0.0294 0.0022  255 ILE   A CB  
2148 C  CG1 . ILE   A 255 ? 0.1435 0.2286 0.1562 0.0172  -0.0188 -0.0037 255 ILE   A CG1 
2149 C  CG2 . ILE   A 255 ? 0.1616 0.2389 0.1506 -0.0021 -0.0216 -0.0254 255 ILE   A CG2 
2150 C  CD1 . ILE   A 255 ? 0.1490 0.2436 0.1632 0.0084  -0.0155 -0.0138 255 ILE   A CD1 
2151 N  N   . LYS   A 256 ? 0.1272 0.2093 0.1327 -0.0028 -0.0103 0.0127  256 LYS   A N   
2152 C  CA  . LYS   A 256 ? 0.1265 0.2323 0.1453 -0.0032 -0.0049 0.0154  256 LYS   A CA  
2153 C  C   . LYS   A 256 ? 0.1359 0.2334 0.1337 -0.0108 -0.0018 0.0068  256 LYS   A C   
2154 O  O   . LYS   A 256 ? 0.1668 0.2555 0.1310 -0.0425 -0.0036 0.0112  256 LYS   A O   
2155 C  CB  . LYS   A 256 ? 0.1531 0.2573 0.1798 0.0207  -0.0149 -0.0056 256 LYS   A CB  
2156 C  CG  . LYS   A 256 ? 0.1905 0.2900 0.2544 -0.0116 -0.0180 -0.0223 256 LYS   A CG  
2157 N  N   . ALA   A 257 ? 0.1299 0.2443 0.1135 -0.0138 -0.0020 0.0183  257 ALA   A N   
2158 C  CA  . ALA   A 257 ? 0.1331 0.2422 0.1450 -0.0121 -0.0061 -0.0009 257 ALA   A CA  
2159 C  C   . ALA   A 257 ? 0.1395 0.2361 0.1188 -0.0169 0.0156  -0.0044 257 ALA   A C   
2160 O  O   . ALA   A 257 ? 0.1415 0.2935 0.1502 0.0038  0.0108  -0.0277 257 ALA   A O   
2161 C  CB  . ALA   A 257 ? 0.1385 0.2541 0.1532 -0.0126 -0.0116 0.0102  257 ALA   A CB  
2162 N  N   . SER   A 258 ? 0.1274 0.2498 0.1371 -0.0005 0.0027  -0.0165 258 SER   A N   
2163 C  CA  . SER   A 258 ? 0.1490 0.2552 0.1563 0.0003  0.0073  0.0002  258 SER   A CA  
2164 C  C   . SER   A 258 ? 0.1449 0.2778 0.1728 -0.0030 0.0113  0.0011  258 SER   A C   
2165 O  O   . SER   A 258 ? 0.1428 0.3375 0.2526 0.0247  0.0319  0.0034  258 SER   A O   
2166 C  CB  . SER   A 258 ? 0.1378 0.2380 0.1685 0.0039  0.0143  0.0051  258 SER   A CB  
2167 O  OG  . SER   A 258 ? 0.1160 0.2595 0.1536 0.0010  -0.0050 0.0054  258 SER   A OG  
2168 N  N   . PHE   A 259 ? 0.1375 0.3007 0.1973 -0.0269 0.0032  0.0096  259 PHE   A N   
2169 C  CA  . PHE   A 259 ? 0.1714 0.2997 0.2240 -0.0522 0.0028  0.0232  259 PHE   A CA  
2170 C  C   . PHE   A 259 ? 0.2271 0.3728 0.2416 -0.0789 0.0107  0.0618  259 PHE   A C   
2171 O  O   . PHE   A 259 ? 0.2734 0.3958 0.2533 -0.1003 -0.0681 0.0807  259 PHE   A O   
2172 C  CB  . PHE   A 259 ? 0.1656 0.2593 0.2601 -0.0562 -0.0101 0.0089  259 PHE   A CB  
2173 C  CG  . PHE   A 259 ? 0.1714 0.2306 0.2727 -0.0408 -0.0250 0.0200  259 PHE   A CG  
2174 C  CD1 . PHE   A 259 ? 0.1466 0.2282 0.2072 -0.0253 -0.0341 0.0148  259 PHE   A CD1 
2175 C  CD2 . PHE   A 259 ? 0.1887 0.2447 0.3317 -0.0265 -0.0308 0.0489  259 PHE   A CD2 
2176 C  CE1 . PHE   A 259 ? 0.1497 0.2621 0.2722 -0.0344 -0.0335 0.0158  259 PHE   A CE1 
2177 C  CE2 . PHE   A 259 ? 0.2134 0.2401 0.3648 0.0100  -0.0275 0.0672  259 PHE   A CE2 
2178 C  CZ  . PHE   A 259 ? 0.1707 0.2673 0.3414 -0.0070 -0.0284 0.0230  259 PHE   A CZ  
2179 N  N   . LYS   A 260 ? 0.2965 0.4623 0.3040 -0.1282 0.0005  0.0944  260 LYS   A N   
2180 C  CA  . LYS   A 260 ? 0.4426 0.5156 0.3800 -0.1249 -0.0151 0.1614  260 LYS   A CA  
2181 C  C   . LYS   A 260 ? 0.5553 0.5384 0.4306 -0.0881 -0.0555 0.2207  260 LYS   A C   
2182 O  O   . LYS   A 260 ? 0.7197 0.7212 0.6222 0.0011  -0.1649 0.2535  260 LYS   A O   
2183 C  CB  . LYS   A 260 ? 0.4582 0.5529 0.4242 -0.1664 0.0177  0.1543  260 LYS   A CB  
2184 O  OXT . LYS   A 260 ? 0.5567 0.5814 0.5445 -0.1227 -0.1079 0.1636  260 LYS   A OXT 
2185 ZN ZN  . ZN    B .   ? 0.0860 0.1568 0.1165 -0.0029 -0.0302 0.0012  301 ZN    A ZN  
2186 C  C1  . A1H15 C .   ? 0.2627 0.2557 0.2536 -0.0519 -0.0509 0.0438  302 A1H15 A C1  
2187 C  C2  . A1H15 C .   ? 0.2171 0.2005 0.2102 -0.0314 -0.0451 0.0337  302 A1H15 A C2  
2188 C  C3  . A1H15 C .   ? 0.1580 0.1858 0.2214 -0.0474 -0.0064 0.0020  302 A1H15 A C3  
2189 C  C4  . A1H15 C .   ? 0.1349 0.1790 0.1654 -0.0251 -0.0095 -0.0009 302 A1H15 A C4  
2190 C  C5  . A1H15 C .   ? 0.1102 0.1605 0.1694 -0.0245 -0.0391 0.0002  302 A1H15 A C5  
2191 C  C6  . A1H15 C .   ? 0.1260 0.1595 0.2056 -0.0097 -0.0406 0.0034  302 A1H15 A C6  
2192 C  C7  . A1H15 C .   ? 0.1737 0.1987 0.2323 -0.0037 -0.0622 0.0293  302 A1H15 A C7  
2193 S  S8  . A1H15 C .   ? 0.0884 0.1675 0.1365 -0.0065 -0.0359 -0.0042 302 A1H15 A S8  
2194 N  N9  . A1H15 C .   ? 0.0807 0.1768 0.1275 -0.0045 -0.0109 0.0030  302 A1H15 A N9  
2195 O  O10 . A1H15 C .   ? 0.0901 0.1687 0.1187 0.0012  -0.0356 -0.0064 302 A1H15 A O10 
2196 O  O11 . A1H15 C .   ? 0.0728 0.1866 0.1438 0.0047  -0.0370 0.0046  302 A1H15 A O11 
2197 N  N12 . A1H15 C .   ? 0.4195 0.4078 0.4011 -0.0243 0.0144  0.0802  302 A1H15 A N12 
2198 C  C13 . A1H15 C .   ? 0.3766 0.4750 0.4648 -0.1076 -0.1218 0.0742  302 A1H15 A C13 
2199 N  N14 . A1H15 C .   ? 0.4338 0.4585 0.4501 -0.0179 -0.1092 0.2262  302 A1H15 A N14 
2200 C  C15 . A1H15 C .   ? 0.4961 0.6664 0.4339 -0.1039 0.0382  0.2267  302 A1H15 A C15 
2201 N  N16 . A1H15 C .   ? 0.5029 0.7449 0.4104 -0.0727 -0.0835 0.1808  302 A1H15 A N16 
2202 N  N17 . A1H15 C .   ? 0.5726 0.3586 0.5400 -0.1569 -0.0497 0.1656  302 A1H15 A N17 
2203 N  N18 . A1H15 C .   ? 0.6151 0.8900 0.4108 -0.0570 -0.0585 0.1637  302 A1H15 A N18 
2204 O  O   . HOH   D .   ? 0.6421 0.5703 0.3753 0.0307  -0.1459 -0.0835 401 HOH   A O   
2205 O  O   . HOH   D .   ? 0.3358 0.4583 0.1691 0.1194  0.0674  0.0230  402 HOH   A O   
2206 O  O   . HOH   D .   ? 0.4087 0.6635 0.3469 0.2251  0.0792  0.0232  403 HOH   A O   
2207 O  O   . HOH   D .   ? 0.2090 0.2939 0.2396 0.0087  -0.0279 0.0547  404 HOH   A O   
2208 O  O   . HOH   D .   ? 0.2166 0.1765 0.2151 0.0316  -0.0773 0.0164  405 HOH   A O   
2209 O  O   . HOH   D .   ? 1.2040 0.8088 0.8515 0.1970  -0.0119 0.0204  406 HOH   A O   
2210 O  O   . HOH   D .   ? 0.4906 0.5891 0.3027 0.1602  0.0100  0.1038  407 HOH   A O   
2211 O  O   . HOH   D .   ? 0.3098 0.4486 0.3486 0.0357  -0.1237 -0.0002 408 HOH   A O   
2212 O  O   . HOH   D .   ? 0.3676 0.3666 0.4357 0.0360  -0.1211 -0.0161 409 HOH   A O   
2213 O  O   . HOH   D .   ? 0.3523 0.3719 0.4881 -0.0218 -0.2210 -0.1325 410 HOH   A O   
2214 O  O   . HOH   D .   ? 0.2483 0.1929 0.3069 -0.0381 -0.0875 -0.0286 411 HOH   A O   
2215 O  O   . HOH   D .   ? 0.3302 0.3833 0.4674 0.0489  -0.1527 0.0542  412 HOH   A O   
2216 O  O   . HOH   D .   ? 0.3944 0.5146 0.6691 -0.0817 0.1066  -0.1830 413 HOH   A O   
2217 O  O   . HOH   D .   ? 0.1231 0.3588 0.3372 -0.0691 -0.0601 0.1057  414 HOH   A O   
2218 O  O   . HOH   D .   ? 0.5743 0.7180 0.3196 0.1038  0.0825  0.0250  415 HOH   A O   
2219 O  O   . HOH   D .   ? 0.4490 0.4180 0.2863 -0.1329 0.1455  -0.1215 416 HOH   A O   
2220 O  O   . HOH   D .   ? 0.1702 0.2118 0.2635 -0.0222 -0.0408 0.0142  417 HOH   A O   
2221 O  O   . HOH   D .   ? 0.3276 0.6048 0.4426 0.1051  -0.0678 -0.1781 418 HOH   A O   
2222 O  O   . HOH   D .   ? 0.3922 0.5318 0.7182 -0.1051 0.1597  -0.0133 419 HOH   A O   
2223 O  O   . HOH   D .   ? 0.4679 0.4101 0.3246 -0.0324 -0.1244 0.0224  420 HOH   A O   
2224 O  O   . HOH   D .   ? 0.4951 0.5845 0.5055 -0.0844 0.1171  -0.1475 421 HOH   A O   
2225 O  O   . HOH   D .   ? 0.4312 0.3825 0.7051 -0.2057 -0.0918 0.1626  422 HOH   A O   
2226 O  O   . HOH   D .   ? 0.3195 0.4958 0.4051 -0.0207 0.0664  -0.0406 423 HOH   A O   
2227 O  O   . HOH   D .   ? 0.6644 0.3933 0.6376 0.0976  -0.1371 -0.1156 424 HOH   A O   
2228 O  O   . HOH   D .   ? 0.1082 0.4076 0.2852 0.0735  -0.0297 -0.0055 425 HOH   A O   
2229 O  O   . HOH   D .   ? 0.2091 0.4067 0.2838 -0.0380 -0.0341 0.0578  426 HOH   A O   
2230 O  O   . HOH   D .   ? 0.2549 0.3620 0.4390 0.0887  -0.0668 -0.1273 427 HOH   A O   
2231 O  O   . HOH   D .   ? 0.3640 0.3699 0.4500 0.0673  -0.0513 -0.0683 428 HOH   A O   
2232 O  O   . HOH   D .   ? 0.1097 0.1731 0.1565 -0.0009 -0.0205 -0.0140 429 HOH   A O   
2233 O  O   . HOH   D .   ? 0.2089 0.7649 0.5354 -0.0046 0.0169  0.2924  430 HOH   A O   
2234 O  O   . HOH   D .   ? 0.2944 0.2975 0.6049 0.0079  0.0614  0.0323  431 HOH   A O   
2235 O  O   . HOH   D .   ? 0.3809 0.3900 0.2838 0.0483  -0.1085 0.0427  432 HOH   A O   
2236 O  O   . HOH   D .   ? 0.2400 0.3542 0.3262 -0.0132 -0.0527 0.0394  433 HOH   A O   
2237 O  O   . HOH   D .   ? 0.2951 0.3985 0.3790 -0.0358 -0.1151 0.0876  434 HOH   A O   
2238 O  O   . HOH   D .   ? 0.5479 0.4257 0.4142 -0.0434 0.0213  -0.0117 435 HOH   A O   
2239 O  O   . HOH   D .   ? 0.1466 0.2605 0.3042 0.0412  0.0445  0.0992  436 HOH   A O   
2240 O  O   . HOH   D .   ? 0.3802 0.7634 0.7160 0.2559  0.3713  -0.0624 437 HOH   A O   
2241 O  O   . HOH   D .   ? 0.3870 0.3653 0.4793 -0.0181 0.0829  -0.0236 438 HOH   A O   
2242 O  O   . HOH   D .   ? 0.2560 0.3170 0.3083 0.0409  -0.0920 -0.0410 439 HOH   A O   
2243 O  O   . HOH   D .   ? 0.2122 0.3213 0.2673 -0.0107 -0.1402 -0.0504 440 HOH   A O   
2244 O  O   . HOH   D .   ? 0.3326 0.6570 0.5290 0.1317  -0.1041 0.0562  441 HOH   A O   
2245 O  O   . HOH   D .   ? 0.2712 0.2171 0.2561 -0.0213 -0.0503 0.0121  442 HOH   A O   
2246 O  O   . HOH   D .   ? 0.3647 0.3163 0.2465 -0.1421 -0.0628 0.0112  443 HOH   A O   
2247 O  O   . HOH   D .   ? 0.4781 0.3958 0.3596 -0.0955 0.1275  -0.0638 444 HOH   A O   
2248 O  O   . HOH   D .   ? 0.4856 0.6858 0.5394 0.2383  0.0860  0.1084  445 HOH   A O   
2249 O  O   . HOH   D .   ? 0.2953 0.3207 0.4387 -0.0821 0.0104  -0.0714 446 HOH   A O   
2250 O  O   . HOH   D .   ? 0.2928 0.3626 0.2544 -0.0429 -0.0926 0.0615  447 HOH   A O   
2251 O  O   . HOH   D .   ? 0.3640 0.3476 0.5762 -0.1092 0.0017  -0.0971 448 HOH   A O   
2252 O  O   . HOH   D .   ? 0.6201 0.4224 0.7151 0.1180  -0.0875 0.0348  449 HOH   A O   
2253 O  O   . HOH   D .   ? 0.3187 0.3433 0.2237 -0.0719 0.0503  0.0310  450 HOH   A O   
2254 O  O   . HOH   D .   ? 0.4603 0.4894 0.4035 -0.0407 0.0123  0.1069  451 HOH   A O   
2255 O  O   . HOH   D .   ? 0.1310 0.2098 0.1817 -0.0024 -0.0710 0.0160  452 HOH   A O   
2256 O  O   . HOH   D .   ? 1.1025 0.3263 0.6778 -0.3706 -0.0702 -0.2073 453 HOH   A O   
2257 O  O   . HOH   D .   ? 0.2690 0.5060 0.3503 -0.0129 0.0154  -0.1589 454 HOH   A O   
2258 O  O   . HOH   D .   ? 0.3538 0.3044 0.2112 -0.0758 -0.0385 0.0510  455 HOH   A O   
2259 O  O   . HOH   D .   ? 0.1854 0.3326 0.2432 0.0152  0.0220  -0.0345 456 HOH   A O   
2260 O  O   . HOH   D .   ? 0.2648 0.5034 0.4030 -0.0289 -0.1131 -0.0355 457 HOH   A O   
2261 O  O   . HOH   D .   ? 0.1893 0.3944 0.1719 -0.0659 -0.0786 0.0008  458 HOH   A O   
2262 O  O   . HOH   D .   ? 0.1569 0.1713 0.1607 -0.0086 -0.0099 -0.0224 459 HOH   A O   
2263 O  O   . HOH   D .   ? 0.2906 0.4828 0.3649 -0.0092 -0.0431 0.1257  460 HOH   A O   
2264 O  O   . HOH   D .   ? 0.4118 0.7972 0.2789 0.0642  0.0060  0.0028  461 HOH   A O   
2265 O  O   . HOH   D .   ? 0.1913 0.4776 0.3278 -0.0503 -0.0879 0.0673  462 HOH   A O   
2266 O  O   . HOH   D .   ? 0.6316 0.4248 0.3823 -0.0441 0.0440  0.0902  463 HOH   A O   
2267 O  O   . HOH   D .   ? 0.6004 0.8507 0.4961 0.0085  0.0613  0.0973  464 HOH   A O   
2268 O  O   . HOH   D .   ? 0.4087 0.5413 0.1832 -0.0108 -0.0074 0.0197  465 HOH   A O   
2269 O  O   . HOH   D .   ? 0.1586 0.1925 0.1847 -0.0068 -0.0212 -0.0209 466 HOH   A O   
2270 O  O   . HOH   D .   ? 0.3069 0.3510 0.2485 0.1008  -0.0199 0.0206  467 HOH   A O   
2271 O  O   . HOH   D .   ? 0.1290 0.1869 0.1367 0.0075  -0.0300 -0.0138 468 HOH   A O   
2272 O  O   . HOH   D .   ? 0.5270 0.3672 0.5052 0.1992  -0.2515 -0.0827 469 HOH   A O   
2273 O  O   . HOH   D .   ? 0.1449 0.2808 0.1764 0.0010  -0.0008 -0.0153 470 HOH   A O   
2274 O  O   . HOH   D .   ? 0.1987 0.2710 0.3842 -0.0884 -0.1238 0.0091  471 HOH   A O   
2275 O  O   . HOH   D .   ? 0.3232 0.2628 0.2520 -0.0020 -0.0366 -0.0013 472 HOH   A O   
2276 O  O   . HOH   D .   ? 0.3739 0.2761 0.6780 -0.0536 0.2279  0.0447  473 HOH   A O   
2277 O  O   . HOH   D .   ? 0.1153 0.1975 0.1604 0.0267  -0.0286 0.0073  474 HOH   A O   
2278 O  O   . HOH   D .   ? 0.3936 0.6220 0.4637 -0.1260 0.1210  -0.2621 475 HOH   A O   
2279 O  O   . HOH   D .   ? 0.1724 0.2133 0.2037 0.0148  -0.0743 0.0093  476 HOH   A O   
2280 O  O   . HOH   D .   ? 0.1888 0.2515 0.2459 0.0320  -0.0602 0.0181  477 HOH   A O   
2281 O  O   . HOH   D .   ? 0.5330 0.4135 0.1927 -0.0588 0.0314  -0.0312 478 HOH   A O   
2282 O  O   . HOH   D .   ? 0.3053 0.5029 0.3159 -0.0729 0.0540  -0.1079 479 HOH   A O   
2283 O  O   . HOH   D .   ? 0.3475 0.4451 0.2239 0.0029  -0.1221 0.0910  480 HOH   A O   
2284 O  O   . HOH   D .   ? 0.3846 0.2888 0.3222 -0.0395 0.0380  0.0074  481 HOH   A O   
2285 O  O   . HOH   D .   ? 0.3067 0.4472 0.3243 -0.0843 -0.0666 -0.0254 482 HOH   A O   
2286 O  O   . HOH   D .   ? 0.2324 0.4787 0.2625 0.0333  -0.0785 -0.0802 483 HOH   A O   
2287 O  O   . HOH   D .   ? 0.1194 0.2436 0.2147 -0.0053 -0.0268 0.0157  484 HOH   A O   
2288 O  O   . HOH   D .   ? 0.2191 0.4977 0.4273 0.0974  0.0471  -0.0053 485 HOH   A O   
2289 O  O   . HOH   D .   ? 0.3907 0.6156 0.4042 0.0895  -0.0577 0.0385  486 HOH   A O   
2290 O  O   . HOH   D .   ? 0.1140 0.1713 0.1549 -0.0108 -0.0026 0.0005  487 HOH   A O   
2291 O  O   . HOH   D .   ? 0.1996 0.2844 0.4528 0.0150  -0.0262 0.0060  488 HOH   A O   
2292 O  O   . HOH   D .   ? 0.1689 0.2515 0.2013 0.0466  -0.0204 0.0249  489 HOH   A O   
2293 O  O   . HOH   D .   ? 0.3060 0.5550 0.3911 0.0646  -0.0585 -0.0494 490 HOH   A O   
2294 O  O   . HOH   D .   ? 0.1985 0.3166 0.3419 0.0572  0.0614  0.1151  491 HOH   A O   
2295 O  O   . HOH   D .   ? 0.4305 0.3205 0.4902 -0.0308 -0.1262 -0.0977 492 HOH   A O   
2296 O  O   . HOH   D .   ? 0.2333 0.2336 0.2410 -0.0153 -0.0559 0.0092  493 HOH   A O   
2297 O  O   . HOH   D .   ? 0.2196 0.2844 0.4487 0.0979  0.0096  -0.0377 494 HOH   A O   
2298 O  O   . HOH   D .   ? 0.2497 0.2148 0.5311 0.0014  0.1892  0.0092  495 HOH   A O   
2299 O  O   . HOH   D .   ? 0.2664 0.2392 0.2673 -0.0220 0.0227  -0.0321 496 HOH   A O   
2300 O  O   . HOH   D .   ? 0.2351 0.2577 0.3775 0.0222  -0.0113 -0.0371 497 HOH   A O   
2301 O  O   . HOH   D .   ? 0.1511 0.3497 0.2850 -0.0127 -0.0350 -0.0099 498 HOH   A O   
2302 O  O   . HOH   D .   ? 0.4915 0.3344 0.3242 0.1956  -0.1580 -0.0645 499 HOH   A O   
2303 O  O   . HOH   D .   ? 0.3597 0.3200 0.8472 -0.0258 -0.1543 0.0477  500 HOH   A O   
2304 O  O   . HOH   D .   ? 0.2187 0.2995 0.2195 0.0212  -0.0361 -0.0358 501 HOH   A O   
2305 O  O   . HOH   D .   ? 0.1562 0.2204 0.2133 -0.0152 -0.0476 0.0083  502 HOH   A O   
2306 O  O   . HOH   D .   ? 0.2249 0.2328 0.5990 -0.0153 0.0544  -0.0436 503 HOH   A O   
2307 O  O   . HOH   D .   ? 0.2174 0.3205 0.2026 0.0011  -0.0608 -0.0120 504 HOH   A O   
2308 O  O   . HOH   D .   ? 0.2274 0.2881 0.2197 0.0238  -0.0498 -0.0645 505 HOH   A O   
2309 O  O   . HOH   D .   ? 0.6201 0.5214 0.4747 0.0617  0.0274  -0.0727 506 HOH   A O   
2310 O  O   . HOH   D .   ? 0.2458 0.4248 0.2019 -0.0042 -0.0626 0.0060  507 HOH   A O   
2311 O  O   . HOH   D .   ? 0.2600 0.4522 0.4653 0.1342  0.1061  0.1128  508 HOH   A O   
2312 O  O   . HOH   D .   ? 0.1523 0.2120 0.2010 -0.0032 -0.0572 0.0129  509 HOH   A O   
2313 O  O   . HOH   D .   ? 0.1077 0.2224 0.2028 -0.0098 -0.0327 -0.0197 510 HOH   A O   
2314 O  O   . HOH   D .   ? 0.5618 0.4833 0.3031 -0.1832 -0.0268 0.0181  511 HOH   A O   
2315 O  O   . HOH   D .   ? 0.2356 0.3285 0.2680 -0.0204 -0.0761 -0.0163 512 HOH   A O   
2316 O  O   . HOH   D .   ? 0.2782 0.2708 0.2677 -0.0103 -0.0600 0.0001  513 HOH   A O   
2317 O  O   . HOH   D .   ? 0.1655 0.4315 0.2259 0.0023  -0.0379 -0.0097 514 HOH   A O   
2318 O  O   . HOH   D .   ? 0.2080 0.3303 0.2371 -0.0530 -0.0581 0.0234  515 HOH   A O   
2319 O  O   . HOH   D .   ? 0.2106 0.2336 0.2571 -0.0183 -0.0065 0.0206  516 HOH   A O   
2320 O  O   . HOH   D .   ? 0.2629 0.4414 0.5177 0.0100  -0.0847 -0.1004 517 HOH   A O   
2321 O  O   . HOH   D .   ? 0.2234 0.2075 0.2680 -0.0688 -0.0711 0.0134  518 HOH   A O   
2322 O  O   . HOH   D .   ? 0.4756 0.3684 0.5342 -0.0365 0.1509  0.0255  519 HOH   A O   
2323 O  O   . HOH   D .   ? 0.2710 0.4163 0.2990 -0.2032 -0.1063 0.0674  520 HOH   A O   
2324 O  O   . HOH   D .   ? 0.1421 0.2182 0.1894 0.0323  -0.0319 0.0255  521 HOH   A O   
2325 O  O   . HOH   D .   ? 0.5041 0.7709 0.5041 -0.0142 -0.0772 -0.0021 522 HOH   A O   
2326 O  O   . HOH   D .   ? 0.1012 0.2583 0.2180 0.0182  -0.0203 -0.0118 523 HOH   A O   
2327 O  O   . HOH   D .   ? 0.3190 0.5267 0.6543 -0.1250 -0.0988 0.1269  524 HOH   A O   
2328 O  O   . HOH   D .   ? 0.4351 0.3287 0.1895 0.0979  -0.0114 0.0087  525 HOH   A O   
2329 O  O   . HOH   D .   ? 0.0932 0.3496 0.3147 -0.0094 -0.0066 -0.0061 526 HOH   A O   
2330 O  O   . HOH   D .   ? 0.2446 0.3655 0.2481 0.0467  -0.0214 0.0522  527 HOH   A O   
2331 O  O   . HOH   D .   ? 0.3104 0.4432 0.1884 0.1020  -0.0891 -0.0298 528 HOH   A O   
2332 O  O   . HOH   D .   ? 0.7125 0.5176 0.6603 -0.2446 0.0421  -0.2225 529 HOH   A O   
2333 O  O   . HOH   D .   ? 0.1974 0.4116 0.2307 0.0385  -0.0034 0.1070  530 HOH   A O   
2334 O  O   . HOH   D .   ? 0.1523 0.3160 0.1391 0.0030  -0.0546 -0.1230 531 HOH   A O   
2335 O  O   . HOH   D .   ? 0.3607 0.3444 0.5476 -0.0160 -0.0505 -0.1492 532 HOH   A O   
2336 O  O   . HOH   D .   ? 0.1128 0.5205 0.3206 0.0624  -0.0167 0.0982  533 HOH   A O   
2337 O  O   . HOH   D .   ? 0.3736 0.3132 0.3240 -0.1205 0.0242  -0.0719 534 HOH   A O   
2338 O  O   . HOH   D .   ? 0.2452 0.4303 0.3204 0.0147  0.0114  0.0982  535 HOH   A O   
2339 O  O   . HOH   D .   ? 0.3718 0.4313 0.3112 0.0031  -0.0615 0.0442  536 HOH   A O   
2340 O  O   . HOH   D .   ? 0.4692 0.5228 0.3244 -0.1495 0.1468  -0.1454 537 HOH   A O   
2341 O  O   . HOH   D .   ? 0.3075 0.3335 0.3875 0.0157  0.0322  -0.0473 538 HOH   A O   
2342 O  O   . HOH   D .   ? 0.3749 0.2246 0.3728 0.0544  -0.1768 -0.0269 539 HOH   A O   
2343 O  O   . HOH   D .   ? 0.4016 0.5928 0.5741 -0.0603 -0.0071 0.2716  540 HOH   A O   
2344 O  O   . HOH   D .   ? 0.2250 0.3066 0.2852 -0.0542 -0.0258 0.0409  541 HOH   A O   
2345 O  O   . HOH   D .   ? 0.2384 0.5350 0.4003 0.0866  -0.0445 0.0097  542 HOH   A O   
2346 O  O   . HOH   D .   ? 0.2607 0.2944 0.2953 0.0498  -0.0523 0.0243  543 HOH   A O   
2347 O  O   . HOH   D .   ? 0.8452 0.3972 0.6946 0.1304  -0.0746 -0.2496 544 HOH   A O   
2348 O  O   . HOH   D .   ? 0.3275 0.3868 0.3569 0.0789  0.0913  0.0221  545 HOH   A O   
2349 O  O   . HOH   D .   ? 0.2762 0.3596 0.3871 0.0319  0.0132  0.0233  546 HOH   A O   
2350 O  O   . HOH   D .   ? 0.2601 0.8100 0.2705 -0.0910 -0.0715 0.0829  547 HOH   A O   
2351 O  O   . HOH   D .   ? 0.1633 0.3670 0.3131 0.0100  -0.0415 -0.0464 548 HOH   A O   
2352 O  O   . HOH   D .   ? 0.2926 0.4323 0.2200 0.0157  -0.0194 -0.0318 549 HOH   A O   
2353 O  O   . HOH   D .   ? 0.3990 0.4517 0.4354 0.1123  0.0526  0.0544  550 HOH   A O   
2354 O  O   . HOH   D .   ? 0.3558 0.2475 0.2679 -0.0283 -0.0031 -0.0665 551 HOH   A O   
2355 O  O   . HOH   D .   ? 0.2495 0.4620 0.2044 -0.0960 -0.0541 -0.1051 552 HOH   A O   
2356 O  O   . HOH   D .   ? 0.4027 0.4248 0.4402 0.0075  -0.0147 0.1937  553 HOH   A O   
2357 O  O   . HOH   D .   ? 0.3572 0.3324 0.4819 -0.0243 0.0947  0.0549  554 HOH   A O   
2358 O  O   . HOH   D .   ? 0.1251 0.2955 0.2008 0.0092  -0.0569 0.0408  555 HOH   A O   
2359 O  O   . HOH   D .   ? 0.7652 0.5108 0.3188 0.0360  -0.0179 0.1196  556 HOH   A O   
2360 O  O   . HOH   D .   ? 0.3298 0.6885 0.3562 -0.1051 -0.0245 0.0007  557 HOH   A O   
2361 O  O   . HOH   D .   ? 0.2353 0.8200 0.3777 -0.0155 -0.0183 0.0278  558 HOH   A O   
2362 O  O   . HOH   D .   ? 0.4128 0.3677 0.2645 0.1898  -0.1072 0.0210  559 HOH   A O   
2363 O  O   . HOH   D .   ? 0.1201 0.2730 0.2635 0.0160  -0.0876 0.0044  560 HOH   A O   
2364 O  O   . HOH   D .   ? 0.2823 0.3201 0.1957 0.0334  -0.0472 -0.0513 561 HOH   A O   
2365 O  O   . HOH   D .   ? 0.2292 0.4317 0.2658 0.0287  -0.0906 0.0372  562 HOH   A O   
2366 O  O   . HOH   D .   ? 0.2890 0.2669 0.2250 0.0284  0.0313  0.0800  563 HOH   A O   
2367 O  O   . HOH   D .   ? 0.7022 0.4237 0.3439 -0.2221 -0.0926 0.0771  564 HOH   A O   
2368 O  O   . HOH   D .   ? 0.2457 0.3140 0.3426 0.0660  -0.0792 -0.0462 565 HOH   A O   
2369 O  O   . HOH   D .   ? 0.3893 0.2890 0.3344 0.0514  -0.0509 0.0355  566 HOH   A O   
2370 O  O   . HOH   D .   ? 0.4212 0.3725 0.3819 -0.0195 -0.1270 -0.0704 567 HOH   A O   
2371 O  O   . HOH   D .   ? 0.2734 0.2885 0.2198 0.0446  -0.0286 0.0151  568 HOH   A O   
2372 O  O   . HOH   D .   ? 0.2459 0.3210 0.2769 -0.0828 -0.0525 -0.0386 569 HOH   A O   
2373 O  O   . HOH   D .   ? 0.7069 0.3927 0.3977 0.1079  -0.1687 0.0401  570 HOH   A O   
2374 O  O   . HOH   D .   ? 0.2597 0.3146 0.2991 -0.0453 -0.0879 -0.1062 571 HOH   A O   
2375 O  O   . HOH   D .   ? 0.2532 0.2799 0.4029 -0.1198 -0.0580 0.0364  572 HOH   A O   
2376 O  O   . HOH   D .   ? 0.1606 0.3036 0.3988 0.0458  0.0476  0.1357  573 HOH   A O   
2377 O  O   . HOH   D .   ? 0.2465 0.3294 0.4379 0.1041  -0.0504 0.0125  574 HOH   A O   
2378 O  O   . HOH   D .   ? 0.3110 0.2858 0.2714 0.0428  0.0281  0.0462  575 HOH   A O   
2379 O  O   . HOH   D .   ? 0.1273 0.1957 0.1806 0.0155  -0.0439 0.0057  576 HOH   A O   
2380 O  O   . HOH   D .   ? 0.3686 0.6498 0.3109 -0.0151 -0.0420 -0.0444 577 HOH   A O   
2381 O  O   . HOH   D .   ? 0.3898 0.3197 0.4425 -0.0714 0.0303  0.1005  578 HOH   A O   
2382 O  O   . HOH   D .   ? 0.1661 0.2167 0.2139 0.0038  0.0150  0.0059  579 HOH   A O   
2383 O  O   . HOH   D .   ? 0.4342 0.7221 0.4936 0.1449  0.0526  -0.0885 580 HOH   A O   
2384 O  O   . HOH   D .   ? 0.3178 0.3966 0.2889 -0.0233 -0.0089 0.0439  581 HOH   A O   
2385 O  O   . HOH   D .   ? 0.5149 0.4108 0.1951 0.2146  -0.0175 0.0368  582 HOH   A O   
2386 O  O   . HOH   D .   ? 0.4344 0.3922 0.3995 0.0639  -0.0406 -0.0455 583 HOH   A O   
2387 O  O   . HOH   D .   ? 0.3824 0.4956 0.4464 0.0349  -0.0492 0.0485  584 HOH   A O   
2388 O  O   . HOH   D .   ? 0.2893 0.4121 0.5436 0.1775  -0.1150 -0.0915 585 HOH   A O   
2389 O  O   . HOH   D .   ? 0.2918 0.2411 0.4297 0.0002  0.0164  -0.0114 586 HOH   A O   
2390 O  O   . HOH   D .   ? 0.1875 0.2021 0.5394 -0.0401 0.1235  0.0038  587 HOH   A O   
2391 O  O   . HOH   D .   ? 0.1721 0.3678 0.3783 0.0205  -0.1129 0.0701  588 HOH   A O   
2392 O  O   . HOH   D .   ? 0.4130 0.4297 0.4340 -0.0029 0.1998  0.0291  589 HOH   A O   
2393 O  O   . HOH   D .   ? 0.4936 0.6293 0.5043 0.1381  0.0758  0.1196  590 HOH   A O   
2394 O  O   . HOH   D .   ? 0.1282 0.2923 0.2626 -0.0271 -0.0111 -0.0100 591 HOH   A O   
2395 O  O   . HOH   D .   ? 0.5645 0.2587 0.3116 0.1375  0.0089  -0.0083 592 HOH   A O   
2396 O  O   . HOH   D .   ? 0.5029 0.3742 0.4744 0.1110  0.1176  0.1174  593 HOH   A O   
2397 O  O   . HOH   D .   ? 0.5302 0.6658 0.3150 0.3068  -0.0291 0.0006  594 HOH   A O   
2398 O  O   . HOH   D .   ? 0.6093 0.3484 0.2649 0.1085  0.0328  0.0425  595 HOH   A O   
2399 O  O   . HOH   D .   ? 0.3662 0.3994 0.3601 -0.0752 -0.0821 -0.0428 596 HOH   A O   
2400 O  O   . HOH   D .   ? 0.2073 0.3033 0.3026 -0.0796 -0.0893 0.0106  597 HOH   A O   
2401 O  O   . HOH   D .   ? 0.4015 0.7740 0.4714 -0.0437 -0.0253 0.2392  598 HOH   A O   
2402 O  O   . HOH   D .   ? 0.4753 0.6823 0.5430 -0.0716 0.0828  -0.0699 599 HOH   A O   
2403 O  O   . HOH   D .   ? 0.4639 0.5684 0.3890 -0.0885 0.0684  0.1727  600 HOH   A O   
2404 O  O   . HOH   D .   ? 0.4240 0.5740 0.2151 -0.2064 -0.0083 -0.0012 601 HOH   A O   
2405 O  O   . HOH   D .   ? 0.2288 0.5654 0.3637 -0.0359 -0.0502 -0.0197 602 HOH   A O   
2406 O  O   . HOH   D .   ? 0.2396 0.2129 0.2705 -0.0161 -0.0973 0.0183  603 HOH   A O   
2407 O  O   . HOH   D .   ? 0.1241 0.2990 0.2632 -0.0482 -0.0512 0.0361  604 HOH   A O   
2408 O  O   . HOH   D .   ? 0.4979 0.4258 0.5029 0.0497  -0.0914 -0.0806 605 HOH   A O   
2409 O  O   . HOH   D .   ? 0.0686 0.2037 0.2083 -0.0349 -0.0262 0.0096  606 HOH   A O   
2410 O  O   . HOH   D .   ? 0.2844 0.3926 0.4473 -0.0015 -0.1054 0.0628  607 HOH   A O   
2411 O  O   . HOH   D .   ? 0.2730 0.4936 0.7149 0.0401  0.0379  -0.0085 608 HOH   A O   
2412 O  O   . HOH   D .   ? 0.4112 0.3086 0.3855 0.0365  -0.0736 -0.0485 609 HOH   A O   
2413 O  O   . HOH   D .   ? 0.3711 0.5137 0.4320 0.1821  -0.0711 0.0872  610 HOH   A O   
2414 O  O   . HOH   D .   ? 0.5910 0.6593 0.6335 0.2400  0.2459  0.0538  611 HOH   A O   
2415 O  O   . HOH   D .   ? 0.1629 0.3852 0.2984 0.0697  0.0088  0.0082  612 HOH   A O   
2416 O  O   . HOH   D .   ? 0.2656 0.4126 0.5998 -0.0554 0.0667  -0.1046 613 HOH   A O   
2417 O  O   . HOH   D .   ? 0.4349 0.5147 0.5540 0.0762  0.0581  -0.1860 614 HOH   A O   
2418 O  O   . HOH   D .   ? 0.1506 0.2689 0.1783 0.0429  0.0091  -0.0202 615 HOH   A O   
2419 O  O   . HOH   D .   ? 0.3492 0.5077 0.4973 -0.0415 0.0410  0.0181  616 HOH   A O   
2420 O  O   . HOH   D .   ? 0.2269 0.3689 0.3190 0.0194  -0.0739 -0.0321 617 HOH   A O   
2421 O  O   . HOH   D .   ? 0.2562 0.3988 0.3993 -0.0715 -0.0855 0.1364  618 HOH   A O   
2422 O  O   . HOH   D .   ? 0.7560 0.2521 0.4257 0.0015  -0.2161 -0.0238 619 HOH   A O   
2423 O  O   . HOH   D .   ? 0.4354 0.6237 0.5224 0.0415  -0.2645 -0.2612 620 HOH   A O   
2424 O  O   . HOH   D .   ? 0.5249 0.4921 0.3928 -0.0575 0.0093  -0.0264 621 HOH   A O   
2425 O  O   . HOH   D .   ? 0.3061 0.3550 0.2899 0.0816  -0.0269 -0.0629 622 HOH   A O   
2426 O  O   . HOH   D .   ? 0.6779 0.3150 1.1982 0.2297  -0.0088 0.1564  623 HOH   A O   
2427 O  O   . HOH   D .   ? 0.3634 0.4152 0.3867 0.1214  0.0128  0.0584  624 HOH   A O   
2428 O  O   . HOH   D .   ? 0.4173 0.7205 0.6311 -0.1050 0.2826  -0.0179 625 HOH   A O   
2429 O  O   . HOH   D .   ? 0.4046 0.4614 0.8248 -0.0945 -0.2192 0.0009  626 HOH   A O   
2430 O  O   . HOH   D .   ? 0.2235 0.3424 0.7960 0.0133  0.0601  0.1034  627 HOH   A O   
2431 O  O   . HOH   D .   ? 0.4147 0.8183 0.4783 -0.2502 -0.0473 -0.1851 628 HOH   A O   
2432 O  O   . HOH   D .   ? 0.9615 0.7313 0.4569 -0.0168 -0.3892 -0.2526 629 HOH   A O   
2433 O  O   . HOH   D .   ? 0.2965 0.3954 0.4829 0.0127  -0.0542 -0.1709 630 HOH   A O   
2434 O  O   . HOH   D .   ? 0.2528 0.2789 0.2664 0.0593  -0.0899 0.0251  631 HOH   A O   
2435 O  O   . HOH   D .   ? 0.2515 0.3574 0.3335 0.0889  0.0808  0.1379  632 HOH   A O   
2436 O  O   . HOH   D .   ? 1.0138 0.4993 0.5284 -0.0200 0.2175  0.0000  633 HOH   A O   
2437 O  O   . HOH   D .   ? 0.5964 0.4161 0.3579 0.1436  -0.1427 -0.1253 634 HOH   A O   
2438 O  O   . HOH   D .   ? 0.3874 0.3047 0.5593 0.0112  0.1652  -0.0233 635 HOH   A O   
2439 O  O   . HOH   D .   ? 0.3360 0.8058 0.4597 -0.0763 -0.0848 -0.1444 636 HOH   A O   
2440 O  O   . HOH   D .   ? 0.5858 0.6556 0.7720 0.1457  0.0149  0.0561  637 HOH   A O   
2441 O  O   . HOH   D .   ? 0.2536 0.3891 0.2280 0.1024  -0.0011 0.0278  638 HOH   A O   
2442 O  O   . HOH   D .   ? 0.3031 0.7451 0.2977 0.0190  0.0407  0.0829  639 HOH   A O   
2443 O  O   . HOH   D .   ? 0.5419 0.4409 0.4300 -0.0333 0.0479  -0.1140 640 HOH   A O   
# 
