data_9G38
# 
_entry.id   9G38 
# 
_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   9G38         pdb_00009g38 10.2210/pdb9g38/pdb 
WWPDB D_1292139655 ?            ?                   
# 
_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       2025-01-22 
# 
_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                        9G38 
_pdbx_database_status.recvd_initial_deposition_date   2024-07-11 
_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              giuseppina.desimone@cnr.it 
_pdbx_contact_author.name_first         GIUSEPPINA 
_pdbx_contact_author.name_last          'De Simone' 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-9783-5431 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Alterio, V.'   1 ? 
'De Simone, G.' 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                   DE 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Arch Pharm' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1521-4184 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            358 
_citation.language                  ? 
_citation.page_first                e2400823 
_citation.page_last                 e2400823 
_citation.title                     
;Depsides from Origanum dictamnus and Satureja pilosa as selective inhibitors of carbonic anhydrases: Isolation, structure elucidation, X-ray crystallography.
;
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1002/ardp.202400823 
_citation.pdbx_database_id_PubMed   39711099 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Paloukopoulou, C.' 1  ?                   
primary 'Ntagli, O.S.'      2  ?                   
primary 'Gherardi, L.'      3  ?                   
primary 'Dourdouni, V.'     4  ?                   
primary 'Filippou, G.'      5  ?                   
primary 'Alterio, V.'       6  ?                   
primary 'Giovannuzzi, S.'   7  0000-0002-0669-7481 
primary 'Massardi, M.L.'    8  ?                   
primary 'De Simone, G.'     9  0000-0001-9783-5431 
primary 'Ronca, R.'         10 ?                   
primary 'Supuran, C.T.'     11 ?                   
primary 'Pescitelli, G.'    12 ?                   
primary 'Karioti, A.'       13 0000-0002-5249-6808 
# 
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' 29477.307 1   4.2.1.1 ? ? ? 
2 non-polymer man 'Salvianolic acid P'   538.456   1   ?       ? ? ? 
3 non-polymer syn 'ZINC ION'             65.409    1   ?       ? ? ? 
4 non-polymer syn GLYCEROL               92.094    1   ?       ? ? ? 
5 water       nat water                  18.015    258 ?       ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Carbonate dehydratase II,Carbonic anhydrase C,CAC,Carbonic anhydrase II,CA-II' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MGMSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAV
LKGGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQK
VVDVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEE
LMVDNWRPAQPLKNRQIKASFK
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MGMSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAV
LKGGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQK
VVDVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEE
LMVDNWRPAQPLKNRQIKASFK
;
_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 'Salvianolic acid P' A1IH2 
3 'ZINC ION'           ZN    
4 GLYCEROL             GOL   
5 water                HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   GLY n 
1 3   MET n 
1 4   SER n 
1 5   HIS n 
1 6   HIS n 
1 7   TRP n 
1 8   GLY n 
1 9   TYR n 
1 10  GLY n 
1 11  LYS n 
1 12  HIS n 
1 13  ASN n 
1 14  GLY n 
1 15  PRO n 
1 16  GLU n 
1 17  HIS n 
1 18  TRP n 
1 19  HIS n 
1 20  LYS n 
1 21  ASP n 
1 22  PHE n 
1 23  PRO n 
1 24  ILE n 
1 25  ALA n 
1 26  LYS n 
1 27  GLY n 
1 28  GLU n 
1 29  ARG n 
1 30  GLN n 
1 31  SER n 
1 32  PRO n 
1 33  VAL n 
1 34  ASP n 
1 35  ILE n 
1 36  ASP n 
1 37  THR n 
1 38  HIS n 
1 39  THR n 
1 40  ALA n 
1 41  LYS n 
1 42  TYR n 
1 43  ASP n 
1 44  PRO n 
1 45  SER n 
1 46  LEU n 
1 47  LYS n 
1 48  PRO n 
1 49  LEU n 
1 50  SER n 
1 51  VAL n 
1 52  SER n 
1 53  TYR n 
1 54  ASP n 
1 55  GLN n 
1 56  ALA n 
1 57  THR n 
1 58  SER n 
1 59  LEU n 
1 60  ARG n 
1 61  ILE n 
1 62  LEU n 
1 63  ASN n 
1 64  ASN n 
1 65  GLY n 
1 66  HIS n 
1 67  ALA n 
1 68  PHE n 
1 69  ASN n 
1 70  VAL n 
1 71  GLU n 
1 72  PHE n 
1 73  ASP n 
1 74  ASP n 
1 75  SER n 
1 76  GLN n 
1 77  ASP n 
1 78  LYS n 
1 79  ALA n 
1 80  VAL n 
1 81  LEU n 
1 82  LYS n 
1 83  GLY n 
1 84  GLY n 
1 85  PRO n 
1 86  LEU n 
1 87  ASP n 
1 88  GLY n 
1 89  THR n 
1 90  TYR n 
1 91  ARG n 
1 92  LEU n 
1 93  ILE n 
1 94  GLN n 
1 95  PHE n 
1 96  HIS n 
1 97  PHE n 
1 98  HIS n 
1 99  TRP n 
1 100 GLY n 
1 101 SER n 
1 102 LEU n 
1 103 ASP n 
1 104 GLY n 
1 105 GLN n 
1 106 GLY n 
1 107 SER n 
1 108 GLU n 
1 109 HIS n 
1 110 THR n 
1 111 VAL n 
1 112 ASP n 
1 113 LYS n 
1 114 LYS n 
1 115 LYS n 
1 116 TYR n 
1 117 ALA n 
1 118 ALA n 
1 119 GLU n 
1 120 LEU n 
1 121 HIS n 
1 122 LEU n 
1 123 VAL n 
1 124 HIS n 
1 125 TRP n 
1 126 ASN n 
1 127 THR n 
1 128 LYS n 
1 129 TYR n 
1 130 GLY n 
1 131 ASP n 
1 132 PHE n 
1 133 GLY n 
1 134 LYS n 
1 135 ALA n 
1 136 VAL n 
1 137 GLN n 
1 138 GLN n 
1 139 PRO n 
1 140 ASP n 
1 141 GLY n 
1 142 LEU n 
1 143 ALA n 
1 144 VAL n 
1 145 LEU n 
1 146 GLY n 
1 147 ILE n 
1 148 PHE n 
1 149 LEU n 
1 150 LYS n 
1 151 VAL n 
1 152 GLY n 
1 153 SER n 
1 154 ALA n 
1 155 LYS n 
1 156 PRO n 
1 157 GLY n 
1 158 LEU n 
1 159 GLN n 
1 160 LYS n 
1 161 VAL n 
1 162 VAL n 
1 163 ASP n 
1 164 VAL n 
1 165 LEU n 
1 166 ASP n 
1 167 SER n 
1 168 ILE n 
1 169 LYS n 
1 170 THR n 
1 171 LYS n 
1 172 GLY n 
1 173 LYS n 
1 174 SER n 
1 175 ALA n 
1 176 ASP n 
1 177 PHE n 
1 178 THR n 
1 179 ASN n 
1 180 PHE n 
1 181 ASP n 
1 182 PRO n 
1 183 ARG n 
1 184 GLY n 
1 185 LEU n 
1 186 LEU n 
1 187 PRO n 
1 188 GLU n 
1 189 SER n 
1 190 LEU n 
1 191 ASP n 
1 192 TYR n 
1 193 TRP n 
1 194 THR n 
1 195 TYR n 
1 196 PRO n 
1 197 GLY n 
1 198 SER n 
1 199 LEU n 
1 200 THR n 
1 201 THR n 
1 202 PRO n 
1 203 PRO n 
1 204 LEU n 
1 205 LEU n 
1 206 GLU n 
1 207 CYS n 
1 208 VAL n 
1 209 THR n 
1 210 TRP n 
1 211 ILE n 
1 212 VAL n 
1 213 LEU n 
1 214 LYS n 
1 215 GLU n 
1 216 PRO n 
1 217 ILE n 
1 218 SER n 
1 219 VAL n 
1 220 SER n 
1 221 SER n 
1 222 GLU n 
1 223 GLN n 
1 224 VAL n 
1 225 LEU n 
1 226 LYS n 
1 227 PHE n 
1 228 ARG n 
1 229 LYS n 
1 230 LEU n 
1 231 ASN n 
1 232 PHE n 
1 233 ASN n 
1 234 GLY n 
1 235 GLU n 
1 236 GLY n 
1 237 GLU n 
1 238 PRO n 
1 239 GLU n 
1 240 GLU n 
1 241 LEU n 
1 242 MET n 
1 243 VAL n 
1 244 ASP n 
1 245 ASN n 
1 246 TRP n 
1 247 ARG n 
1 248 PRO n 
1 249 ALA n 
1 250 GLN n 
1 251 PRO n 
1 252 LEU n 
1 253 LYS n 
1 254 ASN n 
1 255 ARG n 
1 256 GLN n 
1 257 ILE n 
1 258 LYS n 
1 259 ALA n 
1 260 SER n 
1 261 PHE n 
1 262 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                   262 
_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 
A1IH2 non-polymer         . 'Salvianolic acid P' 
;(2~{S},3~{S})-3-[3,4-bis(oxidanyl)phenyl]-6-[(~{E})-3-[(2~{R})-3-[3,4-bis(oxidanyl)phenyl]-1-oxidanyl-1-oxidanylidene-propan-2-yl]oxy-3-oxidanylidene-prop-1-enyl]-2,3-dihydro-1,4-benzodioxine-2-carboxylic acid
;
'C27 H22 O12'    538.456 
ALA   'L-peptide linking' y ALANINE              ? 'C3 H7 N O2'     89.093  
ARG   'L-peptide linking' y ARGININE             ? 'C6 H15 N4 O2 1' 175.209 
ASN   'L-peptide linking' y ASPARAGINE           ? 'C4 H8 N2 O3'    132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'      ? 'C4 H7 N O4'     133.103 
CYS   'L-peptide linking' y CYSTEINE             ? 'C3 H7 N O2 S'   121.158 
GLN   'L-peptide linking' y GLUTAMINE            ? 'C5 H10 N2 O3'   146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'      ? 'C5 H9 N O4'     147.129 
GLY   'peptide linking'   y GLYCINE              ? 'C2 H5 N O2'     75.067  
GOL   non-polymer         . GLYCEROL             'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'       92.094  
HIS   'L-peptide linking' y HISTIDINE            ? 'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer         . WATER                ? 'H2 O'           18.015  
ILE   'L-peptide linking' y ISOLEUCINE           ? 'C6 H13 N O2'    131.173 
LEU   'L-peptide linking' y LEUCINE              ? 'C6 H13 N O2'    131.173 
LYS   'L-peptide linking' y LYSINE               ? 'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking' y METHIONINE           ? 'C5 H11 N O2 S'  149.211 
PHE   'L-peptide linking' y PHENYLALANINE        ? 'C9 H11 N O2'    165.189 
PRO   'L-peptide linking' y PROLINE              ? 'C5 H9 N O2'     115.130 
SER   'L-peptide linking' y SERINE               ? 'C3 H7 N O3'     105.093 
THR   'L-peptide linking' y THREONINE            ? 'C4 H9 N O3'     119.119 
TRP   'L-peptide linking' y TRYPTOPHAN           ? 'C11 H12 N2 O2'  204.225 
TYR   'L-peptide linking' y TYROSINE             ? 'C9 H11 N O3'    181.189 
VAL   'L-peptide linking' y VALINE               ? 'C5 H11 N O2'    117.146 
ZN    non-polymer         . 'ZINC ION'           ? 'Zn 2'           65.409  
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   -1  ?   ?   ?   A . n 
A 1 2   GLY 2   0   ?   ?   ?   A . n 
A 1 3   MET 3   1   ?   ?   ?   A . n 
A 1 4   SER 4   2   ?   ?   ?   A . n 
A 1 5   HIS 5   3   ?   ?   ?   A . n 
A 1 6   HIS 6   4   4   HIS HIS A . n 
A 1 7   TRP 7   5   5   TRP TRP A . n 
A 1 8   GLY 8   6   6   GLY GLY A . n 
A 1 9   TYR 9   7   7   TYR TYR A . n 
A 1 10  GLY 10  8   8   GLY GLY A . n 
A 1 11  LYS 11  9   9   LYS LYS A . n 
A 1 12  HIS 12  10  10  HIS HIS A . n 
A 1 13  ASN 13  11  11  ASN ASN A . n 
A 1 14  GLY 14  12  12  GLY GLY A . n 
A 1 15  PRO 15  13  13  PRO PRO A . n 
A 1 16  GLU 16  14  14  GLU GLU A . n 
A 1 17  HIS 17  15  15  HIS HIS A . n 
A 1 18  TRP 18  16  16  TRP TRP A . n 
A 1 19  HIS 19  17  17  HIS HIS A . n 
A 1 20  LYS 20  18  18  LYS LYS A . n 
A 1 21  ASP 21  19  19  ASP ASP A . n 
A 1 22  PHE 22  20  20  PHE PHE A . n 
A 1 23  PRO 23  21  21  PRO PRO A . n 
A 1 24  ILE 24  22  22  ILE ILE A . n 
A 1 25  ALA 25  23  23  ALA ALA A . n 
A 1 26  LYS 26  24  24  LYS LYS A . n 
A 1 27  GLY 27  25  25  GLY GLY A . n 
A 1 28  GLU 28  26  26  GLU GLU A . n 
A 1 29  ARG 29  27  27  ARG ARG A . n 
A 1 30  GLN 30  28  28  GLN GLN A . n 
A 1 31  SER 31  29  29  SER SER A . n 
A 1 32  PRO 32  30  30  PRO PRO A . n 
A 1 33  VAL 33  31  31  VAL VAL A . n 
A 1 34  ASP 34  32  32  ASP ASP A . n 
A 1 35  ILE 35  33  33  ILE ILE A . n 
A 1 36  ASP 36  34  34  ASP ASP A . n 
A 1 37  THR 37  35  35  THR THR A . n 
A 1 38  HIS 38  36  36  HIS HIS A . n 
A 1 39  THR 39  37  37  THR THR A . n 
A 1 40  ALA 40  38  38  ALA ALA A . n 
A 1 41  LYS 41  39  39  LYS LYS A . n 
A 1 42  TYR 42  40  40  TYR TYR A . n 
A 1 43  ASP 43  41  41  ASP ASP A . n 
A 1 44  PRO 44  42  42  PRO PRO A . n 
A 1 45  SER 45  43  43  SER SER A . n 
A 1 46  LEU 46  44  44  LEU LEU A . n 
A 1 47  LYS 47  45  45  LYS LYS A . n 
A 1 48  PRO 48  46  46  PRO PRO A . n 
A 1 49  LEU 49  47  47  LEU LEU A . n 
A 1 50  SER 50  48  48  SER SER A . n 
A 1 51  VAL 51  49  49  VAL VAL A . n 
A 1 52  SER 52  50  50  SER SER A . n 
A 1 53  TYR 53  51  51  TYR TYR A . n 
A 1 54  ASP 54  52  52  ASP ASP A . n 
A 1 55  GLN 55  53  53  GLN GLN A . n 
A 1 56  ALA 56  54  54  ALA ALA A . n 
A 1 57  THR 57  55  55  THR THR A . n 
A 1 58  SER 58  56  56  SER SER A . n 
A 1 59  LEU 59  57  57  LEU LEU A . n 
A 1 60  ARG 60  58  58  ARG ARG A . n 
A 1 61  ILE 61  59  59  ILE ILE A . n 
A 1 62  LEU 62  60  60  LEU LEU A . n 
A 1 63  ASN 63  61  61  ASN ASN A . n 
A 1 64  ASN 64  62  62  ASN ASN A . n 
A 1 65  GLY 65  63  63  GLY GLY A . n 
A 1 66  HIS 66  64  64  HIS HIS A . n 
A 1 67  ALA 67  65  65  ALA ALA A . n 
A 1 68  PHE 68  66  66  PHE PHE A . n 
A 1 69  ASN 69  67  67  ASN ASN A . n 
A 1 70  VAL 70  68  68  VAL VAL A . n 
A 1 71  GLU 71  69  69  GLU GLU A . n 
A 1 72  PHE 72  70  70  PHE PHE A . n 
A 1 73  ASP 73  71  71  ASP ASP A . n 
A 1 74  ASP 74  72  72  ASP ASP A . n 
A 1 75  SER 75  73  73  SER SER A . n 
A 1 76  GLN 76  74  74  GLN GLN A . n 
A 1 77  ASP 77  75  75  ASP ASP A . n 
A 1 78  LYS 78  76  76  LYS LYS A . n 
A 1 79  ALA 79  77  77  ALA ALA A . n 
A 1 80  VAL 80  78  78  VAL VAL A . n 
A 1 81  LEU 81  79  79  LEU LEU A . n 
A 1 82  LYS 82  80  80  LYS LYS A . n 
A 1 83  GLY 83  81  81  GLY GLY A . n 
A 1 84  GLY 84  82  82  GLY GLY A . n 
A 1 85  PRO 85  83  83  PRO PRO A . n 
A 1 86  LEU 86  84  84  LEU LEU A . n 
A 1 87  ASP 87  85  85  ASP ASP A . n 
A 1 88  GLY 88  86  86  GLY GLY A . n 
A 1 89  THR 89  87  87  THR THR A . n 
A 1 90  TYR 90  88  88  TYR TYR A . n 
A 1 91  ARG 91  89  89  ARG ARG A . n 
A 1 92  LEU 92  90  90  LEU LEU A . n 
A 1 93  ILE 93  91  91  ILE ILE A . n 
A 1 94  GLN 94  92  92  GLN GLN A . n 
A 1 95  PHE 95  93  93  PHE PHE A . n 
A 1 96  HIS 96  94  94  HIS HIS A . n 
A 1 97  PHE 97  95  95  PHE PHE A . n 
A 1 98  HIS 98  96  96  HIS HIS A . n 
A 1 99  TRP 99  97  97  TRP TRP A . n 
A 1 100 GLY 100 98  98  GLY GLY A . n 
A 1 101 SER 101 99  99  SER SER A . n 
A 1 102 LEU 102 100 100 LEU LEU A . n 
A 1 103 ASP 103 101 101 ASP ASP A . n 
A 1 104 GLY 104 102 102 GLY GLY A . n 
A 1 105 GLN 105 103 103 GLN GLN A . n 
A 1 106 GLY 106 104 104 GLY GLY A . n 
A 1 107 SER 107 105 105 SER SER A . n 
A 1 108 GLU 108 106 106 GLU GLU A . n 
A 1 109 HIS 109 107 107 HIS HIS A . n 
A 1 110 THR 110 108 108 THR THR A . n 
A 1 111 VAL 111 109 109 VAL VAL A . n 
A 1 112 ASP 112 110 110 ASP ASP A . n 
A 1 113 LYS 113 111 111 LYS LYS A . n 
A 1 114 LYS 114 112 112 LYS LYS A . n 
A 1 115 LYS 115 113 113 LYS LYS A . n 
A 1 116 TYR 116 114 114 TYR TYR A . n 
A 1 117 ALA 117 115 115 ALA ALA A . n 
A 1 118 ALA 118 116 116 ALA ALA A . n 
A 1 119 GLU 119 117 117 GLU GLU A . n 
A 1 120 LEU 120 118 118 LEU LEU A . n 
A 1 121 HIS 121 119 119 HIS HIS A . n 
A 1 122 LEU 122 120 120 LEU LEU A . n 
A 1 123 VAL 123 121 121 VAL VAL A . n 
A 1 124 HIS 124 122 122 HIS HIS A . n 
A 1 125 TRP 125 123 123 TRP TRP A . n 
A 1 126 ASN 126 124 124 ASN ASN A . n 
A 1 127 THR 127 125 125 THR THR A . n 
A 1 128 LYS 128 127 127 LYS LYS A . n 
A 1 129 TYR 129 128 128 TYR TYR A . n 
A 1 130 GLY 130 129 129 GLY GLY A . n 
A 1 131 ASP 131 130 130 ASP ASP A . n 
A 1 132 PHE 132 131 131 PHE PHE A . n 
A 1 133 GLY 133 132 132 GLY GLY A . n 
A 1 134 LYS 134 133 133 LYS LYS A . n 
A 1 135 ALA 135 134 134 ALA ALA A . n 
A 1 136 VAL 136 135 135 VAL VAL A . n 
A 1 137 GLN 137 136 136 GLN GLN A . n 
A 1 138 GLN 138 137 137 GLN GLN A . n 
A 1 139 PRO 139 138 138 PRO PRO A . n 
A 1 140 ASP 140 139 139 ASP ASP A . n 
A 1 141 GLY 141 140 140 GLY GLY A . n 
A 1 142 LEU 142 141 141 LEU LEU A . n 
A 1 143 ALA 143 142 142 ALA ALA A . n 
A 1 144 VAL 144 143 143 VAL VAL A . n 
A 1 145 LEU 145 144 144 LEU LEU A . n 
A 1 146 GLY 146 145 145 GLY GLY A . n 
A 1 147 ILE 147 146 146 ILE ILE A . n 
A 1 148 PHE 148 147 147 PHE PHE A . n 
A 1 149 LEU 149 148 148 LEU LEU A . n 
A 1 150 LYS 150 149 149 LYS LYS A . n 
A 1 151 VAL 151 150 150 VAL VAL A . n 
A 1 152 GLY 152 151 151 GLY GLY A . n 
A 1 153 SER 153 152 152 SER SER A . n 
A 1 154 ALA 154 153 153 ALA ALA A . n 
A 1 155 LYS 155 154 154 LYS LYS A . n 
A 1 156 PRO 156 155 155 PRO PRO A . n 
A 1 157 GLY 157 156 156 GLY GLY A . n 
A 1 158 LEU 158 157 157 LEU LEU A . n 
A 1 159 GLN 159 158 158 GLN GLN A . n 
A 1 160 LYS 160 159 159 LYS LYS A . n 
A 1 161 VAL 161 160 160 VAL VAL A . n 
A 1 162 VAL 162 161 161 VAL VAL A . n 
A 1 163 ASP 163 162 162 ASP ASP A . n 
A 1 164 VAL 164 163 163 VAL VAL A . n 
A 1 165 LEU 165 164 164 LEU LEU A . n 
A 1 166 ASP 166 165 165 ASP ASP A . n 
A 1 167 SER 167 166 166 SER SER A . n 
A 1 168 ILE 168 167 167 ILE ILE A . n 
A 1 169 LYS 169 168 168 LYS LYS A . n 
A 1 170 THR 170 169 169 THR THR A . n 
A 1 171 LYS 171 170 170 LYS LYS A . n 
A 1 172 GLY 172 171 171 GLY GLY A . n 
A 1 173 LYS 173 172 172 LYS LYS A . n 
A 1 174 SER 174 173 173 SER SER A . n 
A 1 175 ALA 175 174 174 ALA ALA A . n 
A 1 176 ASP 176 175 175 ASP ASP A . n 
A 1 177 PHE 177 176 176 PHE PHE A . n 
A 1 178 THR 178 177 177 THR THR A . n 
A 1 179 ASN 179 178 178 ASN ASN A . n 
A 1 180 PHE 180 179 179 PHE PHE A . n 
A 1 181 ASP 181 180 180 ASP ASP A . n 
A 1 182 PRO 182 181 181 PRO PRO A . n 
A 1 183 ARG 183 182 182 ARG ARG A . n 
A 1 184 GLY 184 183 183 GLY GLY A . n 
A 1 185 LEU 185 184 184 LEU LEU A . n 
A 1 186 LEU 186 185 185 LEU LEU A . n 
A 1 187 PRO 187 186 186 PRO PRO A . n 
A 1 188 GLU 188 187 187 GLU GLU A . n 
A 1 189 SER 189 188 188 SER SER A . n 
A 1 190 LEU 190 189 189 LEU LEU A . n 
A 1 191 ASP 191 190 190 ASP ASP A . n 
A 1 192 TYR 192 191 191 TYR TYR A . n 
A 1 193 TRP 193 192 192 TRP TRP A . n 
A 1 194 THR 194 193 193 THR THR A . n 
A 1 195 TYR 195 194 194 TYR TYR A . n 
A 1 196 PRO 196 195 195 PRO PRO A . n 
A 1 197 GLY 197 196 196 GLY GLY A . n 
A 1 198 SER 198 197 197 SER SER A . n 
A 1 199 LEU 199 198 198 LEU LEU A . n 
A 1 200 THR 200 199 199 THR THR A . n 
A 1 201 THR 201 200 200 THR THR A . n 
A 1 202 PRO 202 201 201 PRO PRO A . n 
A 1 203 PRO 203 202 202 PRO PRO A . n 
A 1 204 LEU 204 203 203 LEU LEU A . n 
A 1 205 LEU 205 204 204 LEU LEU A . n 
A 1 206 GLU 206 205 205 GLU GLU A . n 
A 1 207 CYS 207 206 206 CYS CYS A . n 
A 1 208 VAL 208 207 207 VAL VAL A . n 
A 1 209 THR 209 208 208 THR THR A . n 
A 1 210 TRP 210 209 209 TRP TRP A . n 
A 1 211 ILE 211 210 210 ILE ILE A . n 
A 1 212 VAL 212 211 211 VAL VAL A . n 
A 1 213 LEU 213 212 212 LEU LEU A . n 
A 1 214 LYS 214 213 213 LYS LYS A . n 
A 1 215 GLU 215 214 214 GLU GLU A . n 
A 1 216 PRO 216 215 215 PRO PRO A . n 
A 1 217 ILE 217 216 216 ILE ILE A . n 
A 1 218 SER 218 217 217 SER SER A . n 
A 1 219 VAL 219 218 218 VAL VAL A . n 
A 1 220 SER 220 219 219 SER SER A . n 
A 1 221 SER 221 220 220 SER SER A . n 
A 1 222 GLU 222 221 221 GLU GLU A . n 
A 1 223 GLN 223 222 222 GLN GLN A . n 
A 1 224 VAL 224 223 223 VAL VAL A . n 
A 1 225 LEU 225 224 224 LEU LEU A . n 
A 1 226 LYS 226 225 225 LYS LYS A . n 
A 1 227 PHE 227 226 226 PHE PHE A . n 
A 1 228 ARG 228 227 227 ARG ARG A . n 
A 1 229 LYS 229 228 228 LYS LYS A . n 
A 1 230 LEU 230 229 229 LEU LEU A . n 
A 1 231 ASN 231 230 230 ASN ASN A . n 
A 1 232 PHE 232 231 231 PHE PHE A . n 
A 1 233 ASN 233 232 232 ASN ASN A . n 
A 1 234 GLY 234 233 233 GLY GLY A . n 
A 1 235 GLU 235 234 234 GLU GLU A . n 
A 1 236 GLY 236 235 235 GLY GLY A . n 
A 1 237 GLU 237 236 236 GLU GLU A . n 
A 1 238 PRO 238 237 237 PRO PRO A . n 
A 1 239 GLU 239 238 238 GLU GLU A . n 
A 1 240 GLU 240 239 239 GLU GLU A . n 
A 1 241 LEU 241 240 240 LEU LEU A . n 
A 1 242 MET 242 241 241 MET MET A . n 
A 1 243 VAL 243 242 242 VAL VAL A . n 
A 1 244 ASP 244 243 243 ASP ASP A . n 
A 1 245 ASN 245 244 244 ASN ASN A . n 
A 1 246 TRP 246 245 245 TRP TRP A . n 
A 1 247 ARG 247 246 246 ARG ARG A . n 
A 1 248 PRO 248 247 247 PRO PRO A . n 
A 1 249 ALA 249 248 248 ALA ALA A . n 
A 1 250 GLN 250 249 249 GLN GLN A . n 
A 1 251 PRO 251 250 250 PRO PRO A . n 
A 1 252 LEU 252 251 251 LEU LEU A . n 
A 1 253 LYS 253 252 252 LYS LYS A . n 
A 1 254 ASN 254 253 253 ASN ASN A . n 
A 1 255 ARG 255 254 254 ARG ARG A . n 
A 1 256 GLN 256 255 255 GLN GLN A . n 
A 1 257 ILE 257 256 256 ILE ILE A . n 
A 1 258 LYS 258 257 257 LYS LYS A . n 
A 1 259 ALA 259 258 258 ALA ALA A . n 
A 1 260 SER 260 259 259 SER SER A . n 
A 1 261 PHE 261 260 260 PHE PHE A . n 
A 1 262 LYS 262 261 261 LYS LYS A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1IH2 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1IH2 
_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 A1IH2 1   301 300 A1IH2 GL1 A . 
C 3 ZN    1   302 262 ZN    ZN  A . 
D 4 GOL   1   303 270 GOL   GOL A . 
E 5 HOH   1   401 203 HOH   HOH A . 
E 5 HOH   2   402 73  HOH   HOH A . 
E 5 HOH   3   403 144 HOH   HOH A . 
E 5 HOH   4   404 4   HOH   HOH A . 
E 5 HOH   5   405 127 HOH   HOH A . 
E 5 HOH   6   406 156 HOH   HOH A . 
E 5 HOH   7   407 75  HOH   HOH A . 
E 5 HOH   8   408 177 HOH   HOH A . 
E 5 HOH   9   409 97  HOH   HOH A . 
E 5 HOH   10  410 193 HOH   HOH A . 
E 5 HOH   11  411 246 HOH   HOH A . 
E 5 HOH   12  412 153 HOH   HOH A . 
E 5 HOH   13  413 118 HOH   HOH A . 
E 5 HOH   14  414 145 HOH   HOH A . 
E 5 HOH   15  415 77  HOH   HOH A . 
E 5 HOH   16  416 152 HOH   HOH A . 
E 5 HOH   17  417 209 HOH   HOH A . 
E 5 HOH   18  418 111 HOH   HOH A . 
E 5 HOH   19  419 95  HOH   HOH A . 
E 5 HOH   20  420 121 HOH   HOH A . 
E 5 HOH   21  421 125 HOH   HOH A . 
E 5 HOH   22  422 116 HOH   HOH A . 
E 5 HOH   23  423 99  HOH   HOH A . 
E 5 HOH   24  424 33  HOH   HOH A . 
E 5 HOH   25  425 76  HOH   HOH A . 
E 5 HOH   26  426 230 HOH   HOH A . 
E 5 HOH   27  427 3   HOH   HOH A . 
E 5 HOH   28  428 163 HOH   HOH A . 
E 5 HOH   29  429 114 HOH   HOH A . 
E 5 HOH   30  430 149 HOH   HOH A . 
E 5 HOH   31  431 186 HOH   HOH A . 
E 5 HOH   32  432 31  HOH   HOH A . 
E 5 HOH   33  433 49  HOH   HOH A . 
E 5 HOH   34  434 245 HOH   HOH A . 
E 5 HOH   35  435 175 HOH   HOH A . 
E 5 HOH   36  436 18  HOH   HOH A . 
E 5 HOH   37  437 134 HOH   HOH A . 
E 5 HOH   38  438 45  HOH   HOH A . 
E 5 HOH   39  439 133 HOH   HOH A . 
E 5 HOH   40  440 255 HOH   HOH A . 
E 5 HOH   41  441 242 HOH   HOH A . 
E 5 HOH   42  442 68  HOH   HOH A . 
E 5 HOH   43  443 35  HOH   HOH A . 
E 5 HOH   44  444 192 HOH   HOH A . 
E 5 HOH   45  445 25  HOH   HOH A . 
E 5 HOH   46  446 130 HOH   HOH A . 
E 5 HOH   47  447 183 HOH   HOH A . 
E 5 HOH   48  448 258 HOH   HOH A . 
E 5 HOH   49  449 16  HOH   HOH A . 
E 5 HOH   50  450 206 HOH   HOH A . 
E 5 HOH   51  451 57  HOH   HOH A . 
E 5 HOH   52  452 176 HOH   HOH A . 
E 5 HOH   53  453 103 HOH   HOH A . 
E 5 HOH   54  454 195 HOH   HOH A . 
E 5 HOH   55  455 14  HOH   HOH A . 
E 5 HOH   56  456 166 HOH   HOH A . 
E 5 HOH   57  457 105 HOH   HOH A . 
E 5 HOH   58  458 80  HOH   HOH A . 
E 5 HOH   59  459 8   HOH   HOH A . 
E 5 HOH   60  460 42  HOH   HOH A . 
E 5 HOH   61  461 47  HOH   HOH A . 
E 5 HOH   62  462 26  HOH   HOH A . 
E 5 HOH   63  463 140 HOH   HOH A . 
E 5 HOH   64  464 30  HOH   HOH A . 
E 5 HOH   65  465 220 HOH   HOH A . 
E 5 HOH   66  466 90  HOH   HOH A . 
E 5 HOH   67  467 120 HOH   HOH A . 
E 5 HOH   68  468 23  HOH   HOH A . 
E 5 HOH   69  469 13  HOH   HOH A . 
E 5 HOH   70  470 173 HOH   HOH A . 
E 5 HOH   71  471 243 HOH   HOH A . 
E 5 HOH   72  472 46  HOH   HOH A . 
E 5 HOH   73  473 240 HOH   HOH A . 
E 5 HOH   74  474 179 HOH   HOH A . 
E 5 HOH   75  475 6   HOH   HOH A . 
E 5 HOH   76  476 7   HOH   HOH A . 
E 5 HOH   77  477 29  HOH   HOH A . 
E 5 HOH   78  478 257 HOH   HOH A . 
E 5 HOH   79  479 112 HOH   HOH A . 
E 5 HOH   80  480 19  HOH   HOH A . 
E 5 HOH   81  481 110 HOH   HOH A . 
E 5 HOH   82  482 63  HOH   HOH A . 
E 5 HOH   83  483 185 HOH   HOH A . 
E 5 HOH   84  484 40  HOH   HOH A . 
E 5 HOH   85  485 5   HOH   HOH A . 
E 5 HOH   86  486 191 HOH   HOH A . 
E 5 HOH   87  487 189 HOH   HOH A . 
E 5 HOH   88  488 38  HOH   HOH A . 
E 5 HOH   89  489 86  HOH   HOH A . 
E 5 HOH   90  490 159 HOH   HOH A . 
E 5 HOH   91  491 67  HOH   HOH A . 
E 5 HOH   92  492 56  HOH   HOH A . 
E 5 HOH   93  493 71  HOH   HOH A . 
E 5 HOH   94  494 21  HOH   HOH A . 
E 5 HOH   95  495 64  HOH   HOH A . 
E 5 HOH   96  496 170 HOH   HOH A . 
E 5 HOH   97  497 1   HOH   HOH A . 
E 5 HOH   98  498 164 HOH   HOH A . 
E 5 HOH   99  499 131 HOH   HOH A . 
E 5 HOH   100 500 9   HOH   HOH A . 
E 5 HOH   101 501 74  HOH   HOH A . 
E 5 HOH   102 502 129 HOH   HOH A . 
E 5 HOH   103 503 50  HOH   HOH A . 
E 5 HOH   104 504 190 HOH   HOH A . 
E 5 HOH   105 505 10  HOH   HOH A . 
E 5 HOH   106 506 37  HOH   HOH A . 
E 5 HOH   107 507 168 HOH   HOH A . 
E 5 HOH   108 508 93  HOH   HOH A . 
E 5 HOH   109 509 256 HOH   HOH A . 
E 5 HOH   110 510 222 HOH   HOH A . 
E 5 HOH   111 511 126 HOH   HOH A . 
E 5 HOH   112 512 180 HOH   HOH A . 
E 5 HOH   113 513 15  HOH   HOH A . 
E 5 HOH   114 514 44  HOH   HOH A . 
E 5 HOH   115 515 109 HOH   HOH A . 
E 5 HOH   116 516 96  HOH   HOH A . 
E 5 HOH   117 517 91  HOH   HOH A . 
E 5 HOH   118 518 52  HOH   HOH A . 
E 5 HOH   119 519 32  HOH   HOH A . 
E 5 HOH   120 520 28  HOH   HOH A . 
E 5 HOH   121 521 102 HOH   HOH A . 
E 5 HOH   122 522 70  HOH   HOH A . 
E 5 HOH   123 523 55  HOH   HOH A . 
E 5 HOH   124 524 167 HOH   HOH A . 
E 5 HOH   125 525 48  HOH   HOH A . 
E 5 HOH   126 526 150 HOH   HOH A . 
E 5 HOH   127 527 137 HOH   HOH A . 
E 5 HOH   128 528 2   HOH   HOH A . 
E 5 HOH   129 529 92  HOH   HOH A . 
E 5 HOH   130 530 172 HOH   HOH A . 
E 5 HOH   131 531 20  HOH   HOH A . 
E 5 HOH   132 532 65  HOH   HOH A . 
E 5 HOH   133 533 124 HOH   HOH A . 
E 5 HOH   134 534 24  HOH   HOH A . 
E 5 HOH   135 535 78  HOH   HOH A . 
E 5 HOH   136 536 169 HOH   HOH A . 
E 5 HOH   137 537 119 HOH   HOH A . 
E 5 HOH   138 538 197 HOH   HOH A . 
E 5 HOH   139 539 106 HOH   HOH A . 
E 5 HOH   140 540 155 HOH   HOH A . 
E 5 HOH   141 541 41  HOH   HOH A . 
E 5 HOH   142 542 54  HOH   HOH A . 
E 5 HOH   143 543 113 HOH   HOH A . 
E 5 HOH   144 544 196 HOH   HOH A . 
E 5 HOH   145 545 11  HOH   HOH A . 
E 5 HOH   146 546 135 HOH   HOH A . 
E 5 HOH   147 547 88  HOH   HOH A . 
E 5 HOH   148 548 79  HOH   HOH A . 
E 5 HOH   149 549 17  HOH   HOH A . 
E 5 HOH   150 550 43  HOH   HOH A . 
E 5 HOH   151 551 94  HOH   HOH A . 
E 5 HOH   152 552 253 HOH   HOH A . 
E 5 HOH   153 553 108 HOH   HOH A . 
E 5 HOH   154 554 87  HOH   HOH A . 
E 5 HOH   155 555 22  HOH   HOH A . 
E 5 HOH   156 556 81  HOH   HOH A . 
E 5 HOH   157 557 122 HOH   HOH A . 
E 5 HOH   158 558 36  HOH   HOH A . 
E 5 HOH   159 559 202 HOH   HOH A . 
E 5 HOH   160 560 141 HOH   HOH A . 
E 5 HOH   161 561 128 HOH   HOH A . 
E 5 HOH   162 562 181 HOH   HOH A . 
E 5 HOH   163 563 227 HOH   HOH A . 
E 5 HOH   164 564 194 HOH   HOH A . 
E 5 HOH   165 565 217 HOH   HOH A . 
E 5 HOH   166 566 138 HOH   HOH A . 
E 5 HOH   167 567 188 HOH   HOH A . 
E 5 HOH   168 568 199 HOH   HOH A . 
E 5 HOH   169 569 61  HOH   HOH A . 
E 5 HOH   170 570 184 HOH   HOH A . 
E 5 HOH   171 571 143 HOH   HOH A . 
E 5 HOH   172 572 147 HOH   HOH A . 
E 5 HOH   173 573 171 HOH   HOH A . 
E 5 HOH   174 574 219 HOH   HOH A . 
E 5 HOH   175 575 151 HOH   HOH A . 
E 5 HOH   176 576 178 HOH   HOH A . 
E 5 HOH   177 577 224 HOH   HOH A . 
E 5 HOH   178 578 34  HOH   HOH A . 
E 5 HOH   179 579 39  HOH   HOH A . 
E 5 HOH   180 580 132 HOH   HOH A . 
E 5 HOH   181 581 12  HOH   HOH A . 
E 5 HOH   182 582 225 HOH   HOH A . 
E 5 HOH   183 583 101 HOH   HOH A . 
E 5 HOH   184 584 107 HOH   HOH A . 
E 5 HOH   185 585 117 HOH   HOH A . 
E 5 HOH   186 586 66  HOH   HOH A . 
E 5 HOH   187 587 182 HOH   HOH A . 
E 5 HOH   188 588 165 HOH   HOH A . 
E 5 HOH   189 589 215 HOH   HOH A . 
E 5 HOH   190 590 59  HOH   HOH A . 
E 5 HOH   191 591 198 HOH   HOH A . 
E 5 HOH   192 592 62  HOH   HOH A . 
E 5 HOH   193 593 211 HOH   HOH A . 
E 5 HOH   194 594 157 HOH   HOH A . 
E 5 HOH   195 595 174 HOH   HOH A . 
E 5 HOH   196 596 98  HOH   HOH A . 
E 5 HOH   197 597 27  HOH   HOH A . 
E 5 HOH   198 598 142 HOH   HOH A . 
E 5 HOH   199 599 249 HOH   HOH A . 
E 5 HOH   200 600 244 HOH   HOH A . 
E 5 HOH   201 601 53  HOH   HOH A . 
E 5 HOH   202 602 216 HOH   HOH A . 
E 5 HOH   203 603 160 HOH   HOH A . 
E 5 HOH   204 604 221 HOH   HOH A . 
E 5 HOH   205 605 60  HOH   HOH A . 
E 5 HOH   206 606 82  HOH   HOH A . 
E 5 HOH   207 607 123 HOH   HOH A . 
E 5 HOH   208 608 100 HOH   HOH A . 
E 5 HOH   209 609 154 HOH   HOH A . 
E 5 HOH   210 610 84  HOH   HOH A . 
E 5 HOH   211 611 83  HOH   HOH A . 
E 5 HOH   212 612 146 HOH   HOH A . 
E 5 HOH   213 613 226 HOH   HOH A . 
E 5 HOH   214 614 234 HOH   HOH A . 
E 5 HOH   215 615 58  HOH   HOH A . 
E 5 HOH   216 616 218 HOH   HOH A . 
E 5 HOH   217 617 223 HOH   HOH A . 
E 5 HOH   218 618 208 HOH   HOH A . 
E 5 HOH   219 619 104 HOH   HOH A . 
E 5 HOH   220 620 89  HOH   HOH A . 
E 5 HOH   221 621 238 HOH   HOH A . 
E 5 HOH   222 622 69  HOH   HOH A . 
E 5 HOH   223 623 162 HOH   HOH A . 
E 5 HOH   224 624 51  HOH   HOH A . 
E 5 HOH   225 625 148 HOH   HOH A . 
E 5 HOH   226 626 85  HOH   HOH A . 
E 5 HOH   227 627 239 HOH   HOH A . 
E 5 HOH   228 628 115 HOH   HOH A . 
E 5 HOH   229 629 231 HOH   HOH A . 
E 5 HOH   230 630 237 HOH   HOH A . 
E 5 HOH   231 631 247 HOH   HOH A . 
E 5 HOH   232 632 161 HOH   HOH A . 
E 5 HOH   233 633 233 HOH   HOH A . 
E 5 HOH   234 634 136 HOH   HOH A . 
E 5 HOH   235 635 72  HOH   HOH A . 
E 5 HOH   236 636 251 HOH   HOH A . 
E 5 HOH   237 637 205 HOH   HOH A . 
E 5 HOH   238 638 232 HOH   HOH A . 
E 5 HOH   239 639 158 HOH   HOH A . 
E 5 HOH   240 640 254 HOH   HOH A . 
E 5 HOH   241 641 235 HOH   HOH A . 
E 5 HOH   242 642 213 HOH   HOH A . 
E 5 HOH   243 643 139 HOH   HOH A . 
E 5 HOH   244 644 228 HOH   HOH A . 
E 5 HOH   245 645 236 HOH   HOH A . 
E 5 HOH   246 646 204 HOH   HOH A . 
E 5 HOH   247 647 241 HOH   HOH A . 
E 5 HOH   248 648 212 HOH   HOH A . 
E 5 HOH   249 649 207 HOH   HOH A . 
E 5 HOH   250 650 200 HOH   HOH A . 
E 5 HOH   251 651 248 HOH   HOH A . 
E 5 HOH   252 652 252 HOH   HOH A . 
E 5 HOH   253 653 210 HOH   HOH A . 
E 5 HOH   254 654 187 HOH   HOH A . 
E 5 HOH   255 655 250 HOH   HOH A . 
E 5 HOH   256 656 214 HOH   HOH A . 
E 5 HOH   257 657 229 HOH   HOH A . 
E 5 HOH   258 658 201 HOH   HOH A . 
# 
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    ? ? ? 5.8.0425 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? SCALEPACK ? ? ? .        2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? HKL-3000  ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? REFMAC    ? ? ? .        4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   104.37 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9G38 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     42.222 
_cell.length_a_esd                 ? 
_cell.length_b                     41.268 
_cell.length_b_esd                 ? 
_cell.length_c                     72.101 
_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                         9G38 
_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                   9G38 
_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          40.42 
_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              8 
_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    '1.3 M sodium citrate, 60 mM Tris-HCl' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_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                         'RIGAKU HyPix-6000HE' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-05-10 
_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   1.54178 
_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                      'ROTATING ANODE' 
_diffrn_source.target                      ? 
_diffrn_source.type                        'RIGAKU PhotonJet-R' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.54178 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   ? 
_diffrn_source.pdbx_synchrotron_site       ? 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9G38 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.20 
_reflns.d_resolution_low                               34.95 
_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                                     68762 
_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                           91.3 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                2.7 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          24.1 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               1.010 
_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                                0.063 
_reflns.pdbx_Rpim_I_all                                0.033 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.998 
_reflns.pdbx_CC_star                                   0.999 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.053 
_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                                    1.20 
_reflns_shell.d_res_low                                     1.22 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             3236 
_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                               2.0 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               0.258 
_reflns_shell.pdbx_Rpim_I_all                               0.160 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.914 
_reflns_shell.pdbx_CC_star                                  0.977 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          86.7 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.201 
_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]                            -0.05 
_refine.aniso_B[1][2]                            -0.00 
_refine.aniso_B[1][3]                            -0.09 
_refine.aniso_B[2][2]                            0.14 
_refine.aniso_B[2][3]                            0.00 
_refine.aniso_B[3][3]                            -0.04 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               9.926 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.975 
_refine.correlation_coeff_Fo_to_Fc_free          0.967 
_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                                 9G38 
_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                            1.20 
_refine.ls_d_res_low                             34.95 
_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                     66677 
_refine.ls_number_reflns_R_free                  2070 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    91.24 
_refine.ls_percent_reflns_R_free                 3.0 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.13588 
_refine.ls_R_factor_R_free                       0.15671 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.13525 
_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               'FREE R-VALUE' 
_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                       0.039 
_refine.pdbx_overall_ESU_R_Free                  0.038 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             0.843 
_refine.overall_SU_ML                            0.019 
_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                       1.20 
_refine_hist.d_res_low                        34.95 
_refine_hist.number_atoms_solvent             258 
_refine_hist.number_atoms_total               2352 
_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        2048 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         46 
_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' ? 0.013  0.012  2275 ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.002  0.016  2083 ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 2.009  1.838  3107 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 0.760  1.792  4848 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 6.938  5.000  281  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 6.103  5.000  7    ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 11.827 10.000 373  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.114  0.200  321  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.011  0.020  2692 ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  507  ? 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' ? 2.332  0.920  1094 ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 2.313  0.920  1094 ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 3.694  1.655  1385 ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 3.698  1.657  1386 ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 2.882  1.123  1181 ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 2.881  1.124  1182 ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 4.524  1.968  1723 ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 6.038  495.81 2549 ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 5.996  507.76 2485 ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? 3.748  3.000  4289 ? 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                       1.200 
_refine_ls_shell.d_res_low                        1.231 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             167 
_refine_ls_shell.number_reflns_R_work             4628 
_refine_ls_shell.percent_reflns_obs               86.85 
_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                  0.173 
_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                  0.203 
# 
_struct.entry_id                     9G38 
_struct.title                        'CRYSTAL STRUCTURE OF HUMAN CARBONIC ANHYDRASE II IN COMPLEX WITH SALVIANOLIC ACID P' 
_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        9G38 
_struct_keywords.text            'CARBONIC ANHYDRASE II, SALVIANOLIC ACID P, COMPLEX, INHIBITOR, LYASE' 
_struct_keywords.pdbx_keywords   LYASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    CAH2_HUMAN 
_struct_ref.pdbx_db_accession          P00918 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLK
GGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9G38 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 3 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 262 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P00918 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  260 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       261 
# 
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 9G38 MET A 1 ? UNP P00918 ? ? 'initiating methionine' -1 1 
1 9G38 GLY A 2 ? UNP P00918 ? ? 'expression tag'        0  2 
# 
_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)' 1180  ? 
1 MORE         -43   ? 
1 'SSA (A^2)'  11710 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_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 14  ? ASP A 21  ? GLY A 12  ASP A 19  5 ? 8 
HELX_P HELX_P2 AA2 PHE A 22  ? GLY A 27  ? PHE A 20  GLY A 25  5 ? 6 
HELX_P HELX_P3 AA3 LYS A 128 ? GLY A 130 ? LYS A 127 GLY A 129 5 ? 3 
HELX_P HELX_P4 AA4 ASP A 131 ? VAL A 136 ? ASP A 130 VAL A 135 1 ? 6 
HELX_P HELX_P5 AA5 LYS A 155 ? GLY A 157 ? LYS A 154 GLY A 156 5 ? 3 
HELX_P HELX_P6 AA6 LEU A 158 ? LEU A 165 ? LEU A 157 LEU A 164 1 ? 8 
HELX_P HELX_P7 AA7 ASP A 166 ? LYS A 169 ? ASP A 165 LYS A 168 5 ? 4 
HELX_P HELX_P8 AA8 ASP A 181 ? LEU A 186 ? ASP A 180 LEU A 185 5 ? 6 
HELX_P HELX_P9 AA9 SER A 220 ? ARG A 228 ? SER A 219 ARG A 227 1 ? 9 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A HIS 96  NE2 ? ? ? 1_555 C ZN  . ZN ? ? A HIS 94  A ZN  302 1_555 ? ? ? ? ? ? ? 1.991 ? ? 
metalc2 metalc ? ? A HIS 98  NE2 ? ? ? 1_555 C ZN  . ZN ? ? A HIS 96  A ZN  302 1_555 ? ? ? ? ? ? ? 2.013 ? ? 
metalc3 metalc ? ? A HIS 121 ND1 ? ? ? 1_555 C ZN  . ZN ? ? A HIS 119 A ZN  302 1_555 ? ? ? ? ? ? ? 2.016 ? ? 
metalc4 metalc ? ? C ZN  .   ZN  ? ? ? 1_555 E HOH . O  ? ? A ZN  302 A HOH 408 1_555 ? ? ? ? ? ? ? 1.923 ? ? 
# 
_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 96  ? A HIS 94  ? 1_555 ZN ? C ZN . ? A ZN 302 ? 1_555 NE2 ? A HIS 98  ? A HIS 96  ? 1_555 105.4 ? 
2 NE2 ? A HIS 96  ? A HIS 94  ? 1_555 ZN ? C ZN . ? A ZN 302 ? 1_555 ND1 ? A HIS 121 ? A HIS 119 ? 1_555 113.4 ? 
3 NE2 ? A HIS 98  ? A HIS 96  ? 1_555 ZN ? C ZN . ? A ZN 302 ? 1_555 ND1 ? A HIS 121 ? A HIS 119 ? 1_555 99.9  ? 
4 NE2 ? A HIS 96  ? A HIS 94  ? 1_555 ZN ? C ZN . ? A ZN 302 ? 1_555 O   ? E HOH .   ? A HOH 408 ? 1_555 113.8 ? 
5 NE2 ? A HIS 98  ? A HIS 96  ? 1_555 ZN ? C ZN . ? A ZN 302 ? 1_555 O   ? E HOH .   ? A HOH 408 ? 1_555 107.7 ? 
6 ND1 ? A HIS 121 ? A HIS 119 ? 1_555 ZN ? C ZN . ? A ZN 302 ? 1_555 O   ? E HOH .   ? A HOH 408 ? 1_555 115.0 ? 
# 
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 31  A . ? SER 29  A PRO 32  A ? PRO 30  A 1 -5.27 
2 PRO 202 A . ? PRO 201 A PRO 203 A ? PRO 202 A 1 14.84 
# 
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 34  ? ILE A 35  ? ASP A 32  ILE A 33  
AA1 2  THR A 110 ? VAL A 111 ? THR A 108 VAL A 109 
AA2 1  LYS A 41  ? TYR A 42  ? LYS A 39  TYR A 40  
AA2 2  LYS A 258 ? ALA A 259 ? LYS A 257 ALA A 258 
AA2 3  TYR A 192 ? GLY A 197 ? TYR A 191 GLY A 196 
AA2 4  VAL A 208 ? LEU A 213 ? VAL A 207 LEU A 212 
AA2 5  LEU A 142 ? VAL A 151 ? LEU A 141 VAL A 150 
AA2 6  ALA A 118 ? ASN A 126 ? ALA A 116 ASN A 124 
AA2 7  TYR A 90  ? TRP A 99  ? TYR A 88  TRP A 97  
AA2 8  PHE A 68  ? PHE A 72  ? PHE A 66  PHE A 70  
AA2 9  SER A 58  ? ASN A 63  ? SER A 56  ASN A 61  
AA2 10 SER A 174 ? ASP A 176 ? SER A 173 ASP A 175 
AA3 1  LYS A 47  ? SER A 52  ? LYS A 45  SER A 50  
AA3 2  VAL A 80  ? GLY A 84  ? VAL A 78  GLY A 82  
AA3 3  TYR A 90  ? TRP A 99  ? TYR A 88  TRP A 97  
AA3 4  ALA A 118 ? ASN A 126 ? ALA A 116 ASN A 124 
AA3 5  LEU A 142 ? VAL A 151 ? LEU A 141 VAL A 150 
AA3 6  ILE A 217 ? VAL A 219 ? ILE A 216 VAL A 218 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2  N ILE A 35  ? N ILE A 33  O THR A 110 ? O THR A 108 
AA2 1 2  N LYS A 41  ? N LYS A 39  O ALA A 259 ? O ALA A 258 
AA2 2 3  O LYS A 258 ? O LYS A 257 N THR A 194 ? N THR A 193 
AA2 3 4  N GLY A 197 ? N GLY A 196 O VAL A 208 ? O VAL A 207 
AA2 4 5  O LEU A 213 ? O LEU A 212 N GLY A 146 ? N GLY A 145 
AA2 5 6  O ILE A 147 ? O ILE A 146 N LEU A 120 ? N LEU A 118 
AA2 6 7  O HIS A 121 ? O HIS A 119 N HIS A 96  ? N HIS A 94  
AA2 7 8  O PHE A 95  ? O PHE A 93  N VAL A 70  ? N VAL A 68  
AA2 8 9  O GLU A 71  ? O GLU A 69  N LEU A 59  ? N LEU A 57  
AA2 9 10 N ILE A 61  ? N ILE A 59  O ALA A 175 ? O ALA A 174 
AA3 1 2  N SER A 52  ? N SER A 50  O VAL A 80  ? O VAL A 78  
AA3 2 3  N LEU A 81  ? N LEU A 79  O TYR A 90  ? O TYR A 88  
AA3 3 4  N HIS A 96  ? N HIS A 94  O HIS A 121 ? O HIS A 119 
AA3 4 5  N LEU A 120 ? N LEU A 118 O ILE A 147 ? O ILE A 146 
AA3 5 6  N PHE A 148 ? N PHE A 147 O ILE A 217 ? O ILE A 216 
# 
_pdbx_entry_details.entry_id                   9G38 
_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_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             NE 
_pdbx_validate_rmsd_angle.auth_asym_id_1             A 
_pdbx_validate_rmsd_angle.auth_comp_id_1             ARG 
_pdbx_validate_rmsd_angle.auth_seq_id_1              27 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             CZ 
_pdbx_validate_rmsd_angle.auth_asym_id_2             A 
_pdbx_validate_rmsd_angle.auth_comp_id_2             ARG 
_pdbx_validate_rmsd_angle.auth_seq_id_2              27 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             NH2 
_pdbx_validate_rmsd_angle.auth_asym_id_3             A 
_pdbx_validate_rmsd_angle.auth_comp_id_3             ARG 
_pdbx_validate_rmsd_angle.auth_seq_id_3              27 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                116.43 
_pdbx_validate_rmsd_angle.angle_target_value         120.30 
_pdbx_validate_rmsd_angle.angle_deviation            -3.87 
_pdbx_validate_rmsd_angle.angle_standard_deviation   0.50 
_pdbx_validate_rmsd_angle.linker_flag                N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ARG A 27  ? ? -141.89 57.66   
2 1 LEU A 44  ? A -33.06  141.49  
3 1 ALA A 65  ? ? -163.01 -168.12 
4 1 GLU A 106 ? ? -94.51  -60.18  
5 1 LYS A 111 ? ? 74.91   -0.95   
6 1 PHE A 176 ? ? -151.72 65.83   
7 1 ASN A 244 ? ? -95.30  47.83   
8 1 LYS A 252 ? ? 56.33   -141.26 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A MET -1 ? A MET 1 
2 1 Y 1 A GLY 0  ? A GLY 2 
3 1 Y 1 A MET 1  ? A MET 3 
4 1 Y 1 A SER 2  ? A SER 4 
5 1 Y 1 A HIS 3  ? A HIS 5 
# 
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 
A1IH2 C1   C  Y N 1   
A1IH2 C2   C  Y N 2   
A1IH2 C3   C  Y N 3   
A1IH2 C4   C  Y N 4   
A1IH2 C5   C  Y N 5   
A1IH2 C6   C  Y N 6   
A1IH2 O3   O  N N 7   
A1IH2 O4   O  N N 8   
A1IH2 C20  C  Y N 9   
A1IH2 C21  C  Y N 10  
A1IH2 O21  O  N N 11  
A1IH2 C22  C  Y N 12  
A1IH2 O22  O  N N 13  
A1IH2 C23  C  Y N 14  
A1IH2 C24  C  Y N 15  
A1IH2 C19  C  Y N 16  
A1IH2 C25  C  N S 17  
A1IH2 C26  C  N S 18  
A1IH2 O13  O  N N 19  
A1IH2 C27  C  N N 20  
A1IH2 O29  O  N N 21  
A1IH2 O28  O  N N 22  
A1IH2 O12  O  N N 23  
A1IH2 C12  C  Y N 24  
A1IH2 C11  C  Y N 25  
A1IH2 C13  C  Y N 26  
A1IH2 C14  C  Y N 27  
A1IH2 C15  C  Y N 28  
A1IH2 C10  C  Y N 29  
A1IH2 C16  C  N N 30  
A1IH2 C17  C  N N 31  
A1IH2 C18  C  N N 32  
A1IH2 O20  O  N N 33  
A1IH2 O19  O  N N 34  
A1IH2 C8   C  N R 35  
A1IH2 C9   C  N N 36  
A1IH2 O11  O  N N 37  
A1IH2 O10  O  N N 38  
A1IH2 C7   C  N N 39  
A1IH2 H1   H  N N 40  
A1IH2 H2   H  N N 41  
A1IH2 H3   H  N N 42  
A1IH2 H4   H  N N 43  
A1IH2 H5   H  N N 44  
A1IH2 H6   H  N N 45  
A1IH2 H7   H  N N 46  
A1IH2 H8   H  N N 47  
A1IH2 H9   H  N N 48  
A1IH2 H10  H  N N 49  
A1IH2 H11  H  N N 50  
A1IH2 H12  H  N N 51  
A1IH2 H13  H  N N 52  
A1IH2 H14  H  N N 53  
A1IH2 H15  H  N N 54  
A1IH2 H16  H  N N 55  
A1IH2 H17  H  N N 56  
A1IH2 H18  H  N N 57  
A1IH2 H19  H  N N 58  
A1IH2 H20  H  N N 59  
A1IH2 H21  H  N N 60  
A1IH2 H22  H  N N 61  
ALA   N    N  N N 62  
ALA   CA   C  N S 63  
ALA   C    C  N N 64  
ALA   O    O  N N 65  
ALA   CB   C  N N 66  
ALA   OXT  O  N N 67  
ALA   H    H  N N 68  
ALA   H2   H  N N 69  
ALA   HA   H  N N 70  
ALA   HB1  H  N N 71  
ALA   HB2  H  N N 72  
ALA   HB3  H  N N 73  
ALA   HXT  H  N N 74  
ARG   N    N  N N 75  
ARG   CA   C  N S 76  
ARG   C    C  N N 77  
ARG   O    O  N N 78  
ARG   CB   C  N N 79  
ARG   CG   C  N N 80  
ARG   CD   C  N N 81  
ARG   NE   N  N N 82  
ARG   CZ   C  N N 83  
ARG   NH1  N  N N 84  
ARG   NH2  N  N N 85  
ARG   OXT  O  N N 86  
ARG   H    H  N N 87  
ARG   H2   H  N N 88  
ARG   HA   H  N N 89  
ARG   HB2  H  N N 90  
ARG   HB3  H  N N 91  
ARG   HG2  H  N N 92  
ARG   HG3  H  N N 93  
ARG   HD2  H  N N 94  
ARG   HD3  H  N N 95  
ARG   HE   H  N N 96  
ARG   HH11 H  N N 97  
ARG   HH12 H  N N 98  
ARG   HH21 H  N N 99  
ARG   HH22 H  N N 100 
ARG   HXT  H  N N 101 
ASN   N    N  N N 102 
ASN   CA   C  N S 103 
ASN   C    C  N N 104 
ASN   O    O  N N 105 
ASN   CB   C  N N 106 
ASN   CG   C  N N 107 
ASN   OD1  O  N N 108 
ASN   ND2  N  N N 109 
ASN   OXT  O  N N 110 
ASN   H    H  N N 111 
ASN   H2   H  N N 112 
ASN   HA   H  N N 113 
ASN   HB2  H  N N 114 
ASN   HB3  H  N N 115 
ASN   HD21 H  N N 116 
ASN   HD22 H  N N 117 
ASN   HXT  H  N N 118 
ASP   N    N  N N 119 
ASP   CA   C  N S 120 
ASP   C    C  N N 121 
ASP   O    O  N N 122 
ASP   CB   C  N N 123 
ASP   CG   C  N N 124 
ASP   OD1  O  N N 125 
ASP   OD2  O  N N 126 
ASP   OXT  O  N N 127 
ASP   H    H  N N 128 
ASP   H2   H  N N 129 
ASP   HA   H  N N 130 
ASP   HB2  H  N N 131 
ASP   HB3  H  N N 132 
ASP   HD2  H  N N 133 
ASP   HXT  H  N N 134 
CYS   N    N  N N 135 
CYS   CA   C  N R 136 
CYS   C    C  N N 137 
CYS   O    O  N N 138 
CYS   CB   C  N N 139 
CYS   SG   S  N N 140 
CYS   OXT  O  N N 141 
CYS   H    H  N N 142 
CYS   H2   H  N N 143 
CYS   HA   H  N N 144 
CYS   HB2  H  N N 145 
CYS   HB3  H  N N 146 
CYS   HG   H  N N 147 
CYS   HXT  H  N N 148 
GLN   N    N  N N 149 
GLN   CA   C  N S 150 
GLN   C    C  N N 151 
GLN   O    O  N N 152 
GLN   CB   C  N N 153 
GLN   CG   C  N N 154 
GLN   CD   C  N N 155 
GLN   OE1  O  N N 156 
GLN   NE2  N  N N 157 
GLN   OXT  O  N N 158 
GLN   H    H  N N 159 
GLN   H2   H  N N 160 
GLN   HA   H  N N 161 
GLN   HB2  H  N N 162 
GLN   HB3  H  N N 163 
GLN   HG2  H  N N 164 
GLN   HG3  H  N N 165 
GLN   HE21 H  N N 166 
GLN   HE22 H  N N 167 
GLN   HXT  H  N N 168 
GLU   N    N  N N 169 
GLU   CA   C  N S 170 
GLU   C    C  N N 171 
GLU   O    O  N N 172 
GLU   CB   C  N N 173 
GLU   CG   C  N N 174 
GLU   CD   C  N N 175 
GLU   OE1  O  N N 176 
GLU   OE2  O  N N 177 
GLU   OXT  O  N N 178 
GLU   H    H  N N 179 
GLU   H2   H  N N 180 
GLU   HA   H  N N 181 
GLU   HB2  H  N N 182 
GLU   HB3  H  N N 183 
GLU   HG2  H  N N 184 
GLU   HG3  H  N N 185 
GLU   HE2  H  N N 186 
GLU   HXT  H  N N 187 
GLY   N    N  N N 188 
GLY   CA   C  N N 189 
GLY   C    C  N N 190 
GLY   O    O  N N 191 
GLY   OXT  O  N N 192 
GLY   H    H  N N 193 
GLY   H2   H  N N 194 
GLY   HA2  H  N N 195 
GLY   HA3  H  N N 196 
GLY   HXT  H  N N 197 
GOL   C1   C  N N 198 
GOL   O1   O  N N 199 
GOL   C2   C  N N 200 
GOL   O2   O  N N 201 
GOL   C3   C  N N 202 
GOL   O3   O  N N 203 
GOL   H11  H  N N 204 
GOL   H12  H  N N 205 
GOL   HO1  H  N N 206 
GOL   H2   H  N N 207 
GOL   HO2  H  N N 208 
GOL   H31  H  N N 209 
GOL   H32  H  N N 210 
GOL   HO3  H  N N 211 
HIS   N    N  N N 212 
HIS   CA   C  N S 213 
HIS   C    C  N N 214 
HIS   O    O  N N 215 
HIS   CB   C  N N 216 
HIS   CG   C  Y N 217 
HIS   ND1  N  Y N 218 
HIS   CD2  C  Y N 219 
HIS   CE1  C  Y N 220 
HIS   NE2  N  Y N 221 
HIS   OXT  O  N N 222 
HIS   H    H  N N 223 
HIS   H2   H  N N 224 
HIS   HA   H  N N 225 
HIS   HB2  H  N N 226 
HIS   HB3  H  N N 227 
HIS   HD1  H  N N 228 
HIS   HD2  H  N N 229 
HIS   HE1  H  N N 230 
HIS   HE2  H  N N 231 
HIS   HXT  H  N N 232 
HOH   O    O  N N 233 
HOH   H1   H  N N 234 
HOH   H2   H  N N 235 
ILE   N    N  N N 236 
ILE   CA   C  N S 237 
ILE   C    C  N N 238 
ILE   O    O  N N 239 
ILE   CB   C  N S 240 
ILE   CG1  C  N N 241 
ILE   CG2  C  N N 242 
ILE   CD1  C  N N 243 
ILE   OXT  O  N N 244 
ILE   H    H  N N 245 
ILE   H2   H  N N 246 
ILE   HA   H  N N 247 
ILE   HB   H  N N 248 
ILE   HG12 H  N N 249 
ILE   HG13 H  N N 250 
ILE   HG21 H  N N 251 
ILE   HG22 H  N N 252 
ILE   HG23 H  N N 253 
ILE   HD11 H  N N 254 
ILE   HD12 H  N N 255 
ILE   HD13 H  N N 256 
ILE   HXT  H  N N 257 
LEU   N    N  N N 258 
LEU   CA   C  N S 259 
LEU   C    C  N N 260 
LEU   O    O  N N 261 
LEU   CB   C  N N 262 
LEU   CG   C  N N 263 
LEU   CD1  C  N N 264 
LEU   CD2  C  N N 265 
LEU   OXT  O  N N 266 
LEU   H    H  N N 267 
LEU   H2   H  N N 268 
LEU   HA   H  N N 269 
LEU   HB2  H  N N 270 
LEU   HB3  H  N N 271 
LEU   HG   H  N N 272 
LEU   HD11 H  N N 273 
LEU   HD12 H  N N 274 
LEU   HD13 H  N N 275 
LEU   HD21 H  N N 276 
LEU   HD22 H  N N 277 
LEU   HD23 H  N N 278 
LEU   HXT  H  N N 279 
LYS   N    N  N N 280 
LYS   CA   C  N S 281 
LYS   C    C  N N 282 
LYS   O    O  N N 283 
LYS   CB   C  N N 284 
LYS   CG   C  N N 285 
LYS   CD   C  N N 286 
LYS   CE   C  N N 287 
LYS   NZ   N  N N 288 
LYS   OXT  O  N N 289 
LYS   H    H  N N 290 
LYS   H2   H  N N 291 
LYS   HA   H  N N 292 
LYS   HB2  H  N N 293 
LYS   HB3  H  N N 294 
LYS   HG2  H  N N 295 
LYS   HG3  H  N N 296 
LYS   HD2  H  N N 297 
LYS   HD3  H  N N 298 
LYS   HE2  H  N N 299 
LYS   HE3  H  N N 300 
LYS   HZ1  H  N N 301 
LYS   HZ2  H  N N 302 
LYS   HZ3  H  N N 303 
LYS   HXT  H  N N 304 
MET   N    N  N N 305 
MET   CA   C  N S 306 
MET   C    C  N N 307 
MET   O    O  N N 308 
MET   CB   C  N N 309 
MET   CG   C  N N 310 
MET   SD   S  N N 311 
MET   CE   C  N N 312 
MET   OXT  O  N N 313 
MET   H    H  N N 314 
MET   H2   H  N N 315 
MET   HA   H  N N 316 
MET   HB2  H  N N 317 
MET   HB3  H  N N 318 
MET   HG2  H  N N 319 
MET   HG3  H  N N 320 
MET   HE1  H  N N 321 
MET   HE2  H  N N 322 
MET   HE3  H  N N 323 
MET   HXT  H  N N 324 
PHE   N    N  N N 325 
PHE   CA   C  N S 326 
PHE   C    C  N N 327 
PHE   O    O  N N 328 
PHE   CB   C  N N 329 
PHE   CG   C  Y N 330 
PHE   CD1  C  Y N 331 
PHE   CD2  C  Y N 332 
PHE   CE1  C  Y N 333 
PHE   CE2  C  Y N 334 
PHE   CZ   C  Y N 335 
PHE   OXT  O  N N 336 
PHE   H    H  N N 337 
PHE   H2   H  N N 338 
PHE   HA   H  N N 339 
PHE   HB2  H  N N 340 
PHE   HB3  H  N N 341 
PHE   HD1  H  N N 342 
PHE   HD2  H  N N 343 
PHE   HE1  H  N N 344 
PHE   HE2  H  N N 345 
PHE   HZ   H  N N 346 
PHE   HXT  H  N N 347 
PRO   N    N  N N 348 
PRO   CA   C  N S 349 
PRO   C    C  N N 350 
PRO   O    O  N N 351 
PRO   CB   C  N N 352 
PRO   CG   C  N N 353 
PRO   CD   C  N N 354 
PRO   OXT  O  N N 355 
PRO   H    H  N N 356 
PRO   HA   H  N N 357 
PRO   HB2  H  N N 358 
PRO   HB3  H  N N 359 
PRO   HG2  H  N N 360 
PRO   HG3  H  N N 361 
PRO   HD2  H  N N 362 
PRO   HD3  H  N N 363 
PRO   HXT  H  N N 364 
SER   N    N  N N 365 
SER   CA   C  N S 366 
SER   C    C  N N 367 
SER   O    O  N N 368 
SER   CB   C  N N 369 
SER   OG   O  N N 370 
SER   OXT  O  N N 371 
SER   H    H  N N 372 
SER   H2   H  N N 373 
SER   HA   H  N N 374 
SER   HB2  H  N N 375 
SER   HB3  H  N N 376 
SER   HG   H  N N 377 
SER   HXT  H  N N 378 
THR   N    N  N N 379 
THR   CA   C  N S 380 
THR   C    C  N N 381 
THR   O    O  N N 382 
THR   CB   C  N R 383 
THR   OG1  O  N N 384 
THR   CG2  C  N N 385 
THR   OXT  O  N N 386 
THR   H    H  N N 387 
THR   H2   H  N N 388 
THR   HA   H  N N 389 
THR   HB   H  N N 390 
THR   HG1  H  N N 391 
THR   HG21 H  N N 392 
THR   HG22 H  N N 393 
THR   HG23 H  N N 394 
THR   HXT  H  N N 395 
TRP   N    N  N N 396 
TRP   CA   C  N S 397 
TRP   C    C  N N 398 
TRP   O    O  N N 399 
TRP   CB   C  N N 400 
TRP   CG   C  Y N 401 
TRP   CD1  C  Y N 402 
TRP   CD2  C  Y N 403 
TRP   NE1  N  Y N 404 
TRP   CE2  C  Y N 405 
TRP   CE3  C  Y N 406 
TRP   CZ2  C  Y N 407 
TRP   CZ3  C  Y N 408 
TRP   CH2  C  Y N 409 
TRP   OXT  O  N N 410 
TRP   H    H  N N 411 
TRP   H2   H  N N 412 
TRP   HA   H  N N 413 
TRP   HB2  H  N N 414 
TRP   HB3  H  N N 415 
TRP   HD1  H  N N 416 
TRP   HE1  H  N N 417 
TRP   HE3  H  N N 418 
TRP   HZ2  H  N N 419 
TRP   HZ3  H  N N 420 
TRP   HH2  H  N N 421 
TRP   HXT  H  N N 422 
TYR   N    N  N N 423 
TYR   CA   C  N S 424 
TYR   C    C  N N 425 
TYR   O    O  N N 426 
TYR   CB   C  N N 427 
TYR   CG   C  Y N 428 
TYR   CD1  C  Y N 429 
TYR   CD2  C  Y N 430 
TYR   CE1  C  Y N 431 
TYR   CE2  C  Y N 432 
TYR   CZ   C  Y N 433 
TYR   OH   O  N N 434 
TYR   OXT  O  N N 435 
TYR   H    H  N N 436 
TYR   H2   H  N N 437 
TYR   HA   H  N N 438 
TYR   HB2  H  N N 439 
TYR   HB3  H  N N 440 
TYR   HD1  H  N N 441 
TYR   HD2  H  N N 442 
TYR   HE1  H  N N 443 
TYR   HE2  H  N N 444 
TYR   HH   H  N N 445 
TYR   HXT  H  N N 446 
VAL   N    N  N N 447 
VAL   CA   C  N S 448 
VAL   C    C  N N 449 
VAL   O    O  N N 450 
VAL   CB   C  N N 451 
VAL   CG1  C  N N 452 
VAL   CG2  C  N N 453 
VAL   OXT  O  N N 454 
VAL   H    H  N N 455 
VAL   H2   H  N N 456 
VAL   HA   H  N N 457 
VAL   HB   H  N N 458 
VAL   HG11 H  N N 459 
VAL   HG12 H  N N 460 
VAL   HG13 H  N N 461 
VAL   HG21 H  N N 462 
VAL   HG22 H  N N 463 
VAL   HG23 H  N N 464 
VAL   HXT  H  N N 465 
ZN    ZN   ZN N N 466 
# 
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 
A1IH2 O29 C27  doub N N 1   
A1IH2 O28 C27  sing N N 2   
A1IH2 C27 C26  sing N N 3   
A1IH2 O13 C26  sing N N 4   
A1IH2 O13 C13  sing N N 5   
A1IH2 C14 C13  doub Y N 6   
A1IH2 C14 C15  sing Y N 7   
A1IH2 O4  C4   sing N N 8   
A1IH2 C5  C4   doub Y N 9   
A1IH2 C5  C6   sing Y N 10  
A1IH2 C26 C25  sing N N 11  
A1IH2 C13 C12  sing Y N 12  
A1IH2 C4  C3   sing Y N 13  
A1IH2 C15 C10  doub Y N 14  
A1IH2 C6  C1   doub Y N 15  
A1IH2 C25 C19  sing N N 16  
A1IH2 C25 O12  sing N N 17  
A1IH2 C12 O12  sing N N 18  
A1IH2 C12 C11  doub Y N 19  
A1IH2 C3  C2   doub Y N 20  
A1IH2 C3  O3   sing N N 21  
A1IH2 C1  C2   sing Y N 22  
A1IH2 C1  C7   sing N N 23  
A1IH2 C24 C19  doub Y N 24  
A1IH2 C24 C23  sing Y N 25  
A1IH2 C10 C11  sing Y N 26  
A1IH2 C10 C16  sing N N 27  
A1IH2 C19 C20  sing Y N 28  
A1IH2 C17 C16  doub N E 29  
A1IH2 C17 C18  sing N N 30  
A1IH2 C23 C22  doub Y N 31  
A1IH2 C7  C8   sing N N 32  
A1IH2 O19 C18  sing N N 33  
A1IH2 O19 C8   sing N N 34  
A1IH2 C20 C21  doub Y N 35  
A1IH2 C22 C21  sing Y N 36  
A1IH2 C22 O22  sing N N 37  
A1IH2 C18 O20  doub N N 38  
A1IH2 C21 O21  sing N N 39  
A1IH2 C8  C9   sing N N 40  
A1IH2 O10 C9   doub N N 41  
A1IH2 C9  O11  sing N N 42  
A1IH2 C2  H1   sing N N 43  
A1IH2 C5  H2   sing N N 44  
A1IH2 C6  H3   sing N N 45  
A1IH2 O3  H4   sing N N 46  
A1IH2 O4  H5   sing N N 47  
A1IH2 C20 H6   sing N N 48  
A1IH2 O21 H7   sing N N 49  
A1IH2 O22 H8   sing N N 50  
A1IH2 C23 H9   sing N N 51  
A1IH2 C24 H10  sing N N 52  
A1IH2 C25 H11  sing N N 53  
A1IH2 C26 H12  sing N N 54  
A1IH2 O28 H13  sing N N 55  
A1IH2 C11 H14  sing N N 56  
A1IH2 C14 H15  sing N N 57  
A1IH2 C15 H16  sing N N 58  
A1IH2 C16 H17  sing N N 59  
A1IH2 C17 H18  sing N N 60  
A1IH2 C8  H19  sing N N 61  
A1IH2 O11 H20  sing N N 62  
A1IH2 C7  H21  sing N N 63  
A1IH2 C7  H22  sing N N 64  
ALA   N   CA   sing N N 65  
ALA   N   H    sing N N 66  
ALA   N   H2   sing N N 67  
ALA   CA  C    sing N N 68  
ALA   CA  CB   sing N N 69  
ALA   CA  HA   sing N N 70  
ALA   C   O    doub N N 71  
ALA   C   OXT  sing N N 72  
ALA   CB  HB1  sing N N 73  
ALA   CB  HB2  sing N N 74  
ALA   CB  HB3  sing N N 75  
ALA   OXT HXT  sing N N 76  
ARG   N   CA   sing N N 77  
ARG   N   H    sing N N 78  
ARG   N   H2   sing N N 79  
ARG   CA  C    sing N N 80  
ARG   CA  CB   sing N N 81  
ARG   CA  HA   sing N N 82  
ARG   C   O    doub N N 83  
ARG   C   OXT  sing N N 84  
ARG   CB  CG   sing N N 85  
ARG   CB  HB2  sing N N 86  
ARG   CB  HB3  sing N N 87  
ARG   CG  CD   sing N N 88  
ARG   CG  HG2  sing N N 89  
ARG   CG  HG3  sing N N 90  
ARG   CD  NE   sing N N 91  
ARG   CD  HD2  sing N N 92  
ARG   CD  HD3  sing N N 93  
ARG   NE  CZ   sing N N 94  
ARG   NE  HE   sing N N 95  
ARG   CZ  NH1  sing N N 96  
ARG   CZ  NH2  doub N N 97  
ARG   NH1 HH11 sing N N 98  
ARG   NH1 HH12 sing N N 99  
ARG   NH2 HH21 sing N N 100 
ARG   NH2 HH22 sing N N 101 
ARG   OXT HXT  sing N N 102 
ASN   N   CA   sing N N 103 
ASN   N   H    sing N N 104 
ASN   N   H2   sing N N 105 
ASN   CA  C    sing N N 106 
ASN   CA  CB   sing N N 107 
ASN   CA  HA   sing N N 108 
ASN   C   O    doub N N 109 
ASN   C   OXT  sing N N 110 
ASN   CB  CG   sing N N 111 
ASN   CB  HB2  sing N N 112 
ASN   CB  HB3  sing N N 113 
ASN   CG  OD1  doub N N 114 
ASN   CG  ND2  sing N N 115 
ASN   ND2 HD21 sing N N 116 
ASN   ND2 HD22 sing N N 117 
ASN   OXT HXT  sing N N 118 
ASP   N   CA   sing N N 119 
ASP   N   H    sing N N 120 
ASP   N   H2   sing N N 121 
ASP   CA  C    sing N N 122 
ASP   CA  CB   sing N N 123 
ASP   CA  HA   sing N N 124 
ASP   C   O    doub N N 125 
ASP   C   OXT  sing N N 126 
ASP   CB  CG   sing N N 127 
ASP   CB  HB2  sing N N 128 
ASP   CB  HB3  sing N N 129 
ASP   CG  OD1  doub N N 130 
ASP   CG  OD2  sing N N 131 
ASP   OD2 HD2  sing N N 132 
ASP   OXT HXT  sing N N 133 
CYS   N   CA   sing N N 134 
CYS   N   H    sing N N 135 
CYS   N   H2   sing N N 136 
CYS   CA  C    sing N N 137 
CYS   CA  CB   sing N N 138 
CYS   CA  HA   sing N N 139 
CYS   C   O    doub N N 140 
CYS   C   OXT  sing N N 141 
CYS   CB  SG   sing N N 142 
CYS   CB  HB2  sing N N 143 
CYS   CB  HB3  sing N N 144 
CYS   SG  HG   sing N N 145 
CYS   OXT HXT  sing N N 146 
GLN   N   CA   sing N N 147 
GLN   N   H    sing N N 148 
GLN   N   H2   sing N N 149 
GLN   CA  C    sing N N 150 
GLN   CA  CB   sing N N 151 
GLN   CA  HA   sing N N 152 
GLN   C   O    doub N N 153 
GLN   C   OXT  sing N N 154 
GLN   CB  CG   sing N N 155 
GLN   CB  HB2  sing N N 156 
GLN   CB  HB3  sing N N 157 
GLN   CG  CD   sing N N 158 
GLN   CG  HG2  sing N N 159 
GLN   CG  HG3  sing N N 160 
GLN   CD  OE1  doub N N 161 
GLN   CD  NE2  sing N N 162 
GLN   NE2 HE21 sing N N 163 
GLN   NE2 HE22 sing N N 164 
GLN   OXT HXT  sing N N 165 
GLU   N   CA   sing N N 166 
GLU   N   H    sing N N 167 
GLU   N   H2   sing N N 168 
GLU   CA  C    sing N N 169 
GLU   CA  CB   sing N N 170 
GLU   CA  HA   sing N N 171 
GLU   C   O    doub N N 172 
GLU   C   OXT  sing N N 173 
GLU   CB  CG   sing N N 174 
GLU   CB  HB2  sing N N 175 
GLU   CB  HB3  sing N N 176 
GLU   CG  CD   sing N N 177 
GLU   CG  HG2  sing N N 178 
GLU   CG  HG3  sing N N 179 
GLU   CD  OE1  doub N N 180 
GLU   CD  OE2  sing N N 181 
GLU   OE2 HE2  sing N N 182 
GLU   OXT HXT  sing N N 183 
GLY   N   CA   sing N N 184 
GLY   N   H    sing N N 185 
GLY   N   H2   sing N N 186 
GLY   CA  C    sing N N 187 
GLY   CA  HA2  sing N N 188 
GLY   CA  HA3  sing N N 189 
GLY   C   O    doub N N 190 
GLY   C   OXT  sing N N 191 
GLY   OXT HXT  sing N N 192 
GOL   C1  O1   sing N N 193 
GOL   C1  C2   sing N N 194 
GOL   C1  H11  sing N N 195 
GOL   C1  H12  sing N N 196 
GOL   O1  HO1  sing N N 197 
GOL   C2  O2   sing N N 198 
GOL   C2  C3   sing N N 199 
GOL   C2  H2   sing N N 200 
GOL   O2  HO2  sing N N 201 
GOL   C3  O3   sing N N 202 
GOL   C3  H31  sing N N 203 
GOL   C3  H32  sing N N 204 
GOL   O3  HO3  sing N N 205 
HIS   N   CA   sing N N 206 
HIS   N   H    sing N N 207 
HIS   N   H2   sing N N 208 
HIS   CA  C    sing N N 209 
HIS   CA  CB   sing N N 210 
HIS   CA  HA   sing N N 211 
HIS   C   O    doub N N 212 
HIS   C   OXT  sing N N 213 
HIS   CB  CG   sing N N 214 
HIS   CB  HB2  sing N N 215 
HIS   CB  HB3  sing N N 216 
HIS   CG  ND1  sing Y N 217 
HIS   CG  CD2  doub Y N 218 
HIS   ND1 CE1  doub Y N 219 
HIS   ND1 HD1  sing N N 220 
HIS   CD2 NE2  sing Y N 221 
HIS   CD2 HD2  sing N N 222 
HIS   CE1 NE2  sing Y N 223 
HIS   CE1 HE1  sing N N 224 
HIS   NE2 HE2  sing N N 225 
HIS   OXT HXT  sing N N 226 
HOH   O   H1   sing N N 227 
HOH   O   H2   sing N N 228 
ILE   N   CA   sing N N 229 
ILE   N   H    sing N N 230 
ILE   N   H2   sing N N 231 
ILE   CA  C    sing N N 232 
ILE   CA  CB   sing N N 233 
ILE   CA  HA   sing N N 234 
ILE   C   O    doub N N 235 
ILE   C   OXT  sing N N 236 
ILE   CB  CG1  sing N N 237 
ILE   CB  CG2  sing N N 238 
ILE   CB  HB   sing N N 239 
ILE   CG1 CD1  sing N N 240 
ILE   CG1 HG12 sing N N 241 
ILE   CG1 HG13 sing N N 242 
ILE   CG2 HG21 sing N N 243 
ILE   CG2 HG22 sing N N 244 
ILE   CG2 HG23 sing N N 245 
ILE   CD1 HD11 sing N N 246 
ILE   CD1 HD12 sing N N 247 
ILE   CD1 HD13 sing N N 248 
ILE   OXT HXT  sing N N 249 
LEU   N   CA   sing N N 250 
LEU   N   H    sing N N 251 
LEU   N   H2   sing N N 252 
LEU   CA  C    sing N N 253 
LEU   CA  CB   sing N N 254 
LEU   CA  HA   sing N N 255 
LEU   C   O    doub N N 256 
LEU   C   OXT  sing N N 257 
LEU   CB  CG   sing N N 258 
LEU   CB  HB2  sing N N 259 
LEU   CB  HB3  sing N N 260 
LEU   CG  CD1  sing N N 261 
LEU   CG  CD2  sing N N 262 
LEU   CG  HG   sing N N 263 
LEU   CD1 HD11 sing N N 264 
LEU   CD1 HD12 sing N N 265 
LEU   CD1 HD13 sing N N 266 
LEU   CD2 HD21 sing N N 267 
LEU   CD2 HD22 sing N N 268 
LEU   CD2 HD23 sing N N 269 
LEU   OXT HXT  sing N N 270 
LYS   N   CA   sing N N 271 
LYS   N   H    sing N N 272 
LYS   N   H2   sing N N 273 
LYS   CA  C    sing N N 274 
LYS   CA  CB   sing N N 275 
LYS   CA  HA   sing N N 276 
LYS   C   O    doub N N 277 
LYS   C   OXT  sing N N 278 
LYS   CB  CG   sing N N 279 
LYS   CB  HB2  sing N N 280 
LYS   CB  HB3  sing N N 281 
LYS   CG  CD   sing N N 282 
LYS   CG  HG2  sing N N 283 
LYS   CG  HG3  sing N N 284 
LYS   CD  CE   sing N N 285 
LYS   CD  HD2  sing N N 286 
LYS   CD  HD3  sing N N 287 
LYS   CE  NZ   sing N N 288 
LYS   CE  HE2  sing N N 289 
LYS   CE  HE3  sing N N 290 
LYS   NZ  HZ1  sing N N 291 
LYS   NZ  HZ2  sing N N 292 
LYS   NZ  HZ3  sing N N 293 
LYS   OXT HXT  sing N N 294 
MET   N   CA   sing N N 295 
MET   N   H    sing N N 296 
MET   N   H2   sing N N 297 
MET   CA  C    sing N N 298 
MET   CA  CB   sing N N 299 
MET   CA  HA   sing N N 300 
MET   C   O    doub N N 301 
MET   C   OXT  sing N N 302 
MET   CB  CG   sing N N 303 
MET   CB  HB2  sing N N 304 
MET   CB  HB3  sing N N 305 
MET   CG  SD   sing N N 306 
MET   CG  HG2  sing N N 307 
MET   CG  HG3  sing N N 308 
MET   SD  CE   sing N N 309 
MET   CE  HE1  sing N N 310 
MET   CE  HE2  sing N N 311 
MET   CE  HE3  sing N N 312 
MET   OXT HXT  sing N N 313 
PHE   N   CA   sing N N 314 
PHE   N   H    sing N N 315 
PHE   N   H2   sing N N 316 
PHE   CA  C    sing N N 317 
PHE   CA  CB   sing N N 318 
PHE   CA  HA   sing N N 319 
PHE   C   O    doub N N 320 
PHE   C   OXT  sing N N 321 
PHE   CB  CG   sing N N 322 
PHE   CB  HB2  sing N N 323 
PHE   CB  HB3  sing N N 324 
PHE   CG  CD1  doub Y N 325 
PHE   CG  CD2  sing Y N 326 
PHE   CD1 CE1  sing Y N 327 
PHE   CD1 HD1  sing N N 328 
PHE   CD2 CE2  doub Y N 329 
PHE   CD2 HD2  sing N N 330 
PHE   CE1 CZ   doub Y N 331 
PHE   CE1 HE1  sing N N 332 
PHE   CE2 CZ   sing Y N 333 
PHE   CE2 HE2  sing N N 334 
PHE   CZ  HZ   sing N N 335 
PHE   OXT HXT  sing N N 336 
PRO   N   CA   sing N N 337 
PRO   N   CD   sing N N 338 
PRO   N   H    sing N N 339 
PRO   CA  C    sing N N 340 
PRO   CA  CB   sing N N 341 
PRO   CA  HA   sing N N 342 
PRO   C   O    doub N N 343 
PRO   C   OXT  sing N N 344 
PRO   CB  CG   sing N N 345 
PRO   CB  HB2  sing N N 346 
PRO   CB  HB3  sing N N 347 
PRO   CG  CD   sing N N 348 
PRO   CG  HG2  sing N N 349 
PRO   CG  HG3  sing N N 350 
PRO   CD  HD2  sing N N 351 
PRO   CD  HD3  sing N N 352 
PRO   OXT HXT  sing N N 353 
SER   N   CA   sing N N 354 
SER   N   H    sing N N 355 
SER   N   H2   sing N N 356 
SER   CA  C    sing N N 357 
SER   CA  CB   sing N N 358 
SER   CA  HA   sing N N 359 
SER   C   O    doub N N 360 
SER   C   OXT  sing N N 361 
SER   CB  OG   sing N N 362 
SER   CB  HB2  sing N N 363 
SER   CB  HB3  sing N N 364 
SER   OG  HG   sing N N 365 
SER   OXT HXT  sing N N 366 
THR   N   CA   sing N N 367 
THR   N   H    sing N N 368 
THR   N   H2   sing N N 369 
THR   CA  C    sing N N 370 
THR   CA  CB   sing N N 371 
THR   CA  HA   sing N N 372 
THR   C   O    doub N N 373 
THR   C   OXT  sing N N 374 
THR   CB  OG1  sing N N 375 
THR   CB  CG2  sing N N 376 
THR   CB  HB   sing N N 377 
THR   OG1 HG1  sing N N 378 
THR   CG2 HG21 sing N N 379 
THR   CG2 HG22 sing N N 380 
THR   CG2 HG23 sing N N 381 
THR   OXT HXT  sing N N 382 
TRP   N   CA   sing N N 383 
TRP   N   H    sing N N 384 
TRP   N   H2   sing N N 385 
TRP   CA  C    sing N N 386 
TRP   CA  CB   sing N N 387 
TRP   CA  HA   sing N N 388 
TRP   C   O    doub N N 389 
TRP   C   OXT  sing N N 390 
TRP   CB  CG   sing N N 391 
TRP   CB  HB2  sing N N 392 
TRP   CB  HB3  sing N N 393 
TRP   CG  CD1  doub Y N 394 
TRP   CG  CD2  sing Y N 395 
TRP   CD1 NE1  sing Y N 396 
TRP   CD1 HD1  sing N N 397 
TRP   CD2 CE2  doub Y N 398 
TRP   CD2 CE3  sing Y N 399 
TRP   NE1 CE2  sing Y N 400 
TRP   NE1 HE1  sing N N 401 
TRP   CE2 CZ2  sing Y N 402 
TRP   CE3 CZ3  doub Y N 403 
TRP   CE3 HE3  sing N N 404 
TRP   CZ2 CH2  doub Y N 405 
TRP   CZ2 HZ2  sing N N 406 
TRP   CZ3 CH2  sing Y N 407 
TRP   CZ3 HZ3  sing N N 408 
TRP   CH2 HH2  sing N N 409 
TRP   OXT HXT  sing N N 410 
TYR   N   CA   sing N N 411 
TYR   N   H    sing N N 412 
TYR   N   H2   sing N N 413 
TYR   CA  C    sing N N 414 
TYR   CA  CB   sing N N 415 
TYR   CA  HA   sing N N 416 
TYR   C   O    doub N N 417 
TYR   C   OXT  sing N N 418 
TYR   CB  CG   sing N N 419 
TYR   CB  HB2  sing N N 420 
TYR   CB  HB3  sing N N 421 
TYR   CG  CD1  doub Y N 422 
TYR   CG  CD2  sing Y N 423 
TYR   CD1 CE1  sing Y N 424 
TYR   CD1 HD1  sing N N 425 
TYR   CD2 CE2  doub Y N 426 
TYR   CD2 HD2  sing N N 427 
TYR   CE1 CZ   doub Y N 428 
TYR   CE1 HE1  sing N N 429 
TYR   CE2 CZ   sing Y N 430 
TYR   CE2 HE2  sing N N 431 
TYR   CZ  OH   sing N N 432 
TYR   OH  HH   sing N N 433 
TYR   OXT HXT  sing N N 434 
VAL   N   CA   sing N N 435 
VAL   N   H    sing N N 436 
VAL   N   H2   sing N N 437 
VAL   CA  C    sing N N 438 
VAL   CA  CB   sing N N 439 
VAL   CA  HA   sing N N 440 
VAL   C   O    doub N N 441 
VAL   C   OXT  sing N N 442 
VAL   CB  CG1  sing N N 443 
VAL   CB  CG2  sing N N 444 
VAL   CB  HB   sing N N 445 
VAL   CG1 HG11 sing N N 446 
VAL   CG1 HG12 sing N N 447 
VAL   CG1 HG13 sing N N 448 
VAL   CG2 HG21 sing N N 449 
VAL   CG2 HG22 sing N N 450 
VAL   CG2 HG23 sing N N 451 
VAL   OXT HXT  sing N N 452 
# 
_pdbx_audit_support.funding_organization   'Ministero dell Universita e della Ricerca' 
_pdbx_audit_support.country                Italy 
_pdbx_audit_support.grant_number           PRIN201744BN5T 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   4XE1 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9G38 
_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]   0.023684 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.006067 
_atom_sites.fract_transf_matrix[2][1]   -0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.024232 
_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]   0.014317 
_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 6   ? 9.695   2.085   9.134   1.00 24.40 ? 4   HIS   A N   1 
ATOM   2    C  CA  . HIS   A 1 6   ? 9.657   0.706   8.588   1.00 22.64 ? 4   HIS   A CA  1 
ATOM   3    C  C   . HIS   A 1 6   ? 9.132   -0.361  9.552   1.00 18.70 ? 4   HIS   A C   1 
ATOM   4    O  O   . HIS   A 1 6   ? 9.386   -1.555  9.363   1.00 20.28 ? 4   HIS   A O   1 
ATOM   5    C  CB  . HIS   A 1 6   ? 11.045  0.241   8.154   1.00 24.43 ? 4   HIS   A CB  1 
ATOM   6    C  CG  . HIS   A 1 6   ? 11.479  1.013   6.965   1.00 29.29 ? 4   HIS   A CG  1 
ATOM   7    N  ND1 . HIS   A 1 6   ? 10.822  0.839   5.766   1.00 33.03 ? 4   HIS   A ND1 1 
ATOM   8    C  CD2 . HIS   A 1 6   ? 12.384  1.966   6.757   1.00 32.31 ? 4   HIS   A CD2 1 
ATOM   9    C  CE1 . HIS   A 1 6   ? 11.342  1.651   4.866   1.00 33.51 ? 4   HIS   A CE1 1 
ATOM   10   N  NE2 . HIS   A 1 6   ? 12.290  2.352   5.446   1.00 33.77 ? 4   HIS   A NE2 1 
ATOM   11   N  N   . TRP   A 1 7   ? 8.383   0.025   10.580  1.00 15.28 ? 5   TRP   A N   1 
ATOM   12   C  CA  . TRP   A 1 7   ? 7.682   -0.938  11.395  1.00 13.09 ? 5   TRP   A CA  1 
ATOM   13   C  C   . TRP   A 1 7   ? 6.677   -1.734  10.562  1.00 12.03 ? 5   TRP   A C   1 
ATOM   14   O  O   . TRP   A 1 7   ? 6.129   -1.273  9.569   1.00 13.18 ? 5   TRP   A O   1 
ATOM   15   C  CB  . TRP   A 1 7   ? 6.996   -0.229  12.569  1.00 11.85 ? 5   TRP   A CB  1 
ATOM   16   C  CG  . TRP   A 1 7   ? 5.834   0.622   12.167  1.00 11.39 ? 5   TRP   A CG  1 
ATOM   17   C  CD1 . TRP   A 1 7   ? 5.832   1.948   11.833  1.00 12.06 ? 5   TRP   A CD1 1 
ATOM   18   C  CD2 . TRP   A 1 7   ? 4.469   0.157   12.057  1.00 10.84 ? 5   TRP   A CD2 1 
ATOM   19   N  NE1 . TRP   A 1 7   ? 4.560   2.336   11.537  1.00 12.24 ? 5   TRP   A NE1 1 
ATOM   20   C  CE2 . TRP   A 1 7   ? 3.702   1.271   11.652  1.00 11.34 ? 5   TRP   A CE2 1 
ATOM   21   C  CE3 . TRP   A 1 7   ? 3.818   -1.064  12.280  1.00 10.70 ? 5   TRP   A CE3 1 
ATOM   22   C  CZ2 . TRP   A 1 7   ? 2.332   1.192   11.467  1.00 11.91 ? 5   TRP   A CZ2 1 
ATOM   23   C  CZ3 . TRP   A 1 7   ? 2.450   -1.128  12.080  1.00 11.43 ? 5   TRP   A CZ3 1 
ATOM   24   C  CH2 . TRP   A 1 7   ? 1.720   -0.003  11.688  1.00 11.81 ? 5   TRP   A CH2 1 
ATOM   25   N  N   . GLY   A 1 8   ? 6.401   -2.940  11.016  1.00 10.38 ? 6   GLY   A N   1 
ATOM   26   C  CA  . GLY   A 1 8   ? 5.373   -3.771  10.428  1.00 9.97  ? 6   GLY   A CA  1 
ATOM   27   C  C   . GLY   A 1 8   ? 5.066   -4.949  11.338  1.00 9.43  ? 6   GLY   A C   1 
ATOM   28   O  O   . GLY   A 1 8   ? 5.079   -4.822  12.555  1.00 9.47  ? 6   GLY   A O   1 
ATOM   29   N  N   . TYR   A 1 9   ? 4.735   -6.091  10.726  1.00 9.50  ? 7   TYR   A N   1 
ATOM   30   C  CA  . TYR   A 1 9   ? 4.329   -7.293  11.457  1.00 10.02 ? 7   TYR   A CA  1 
ATOM   31   C  C   . TYR   A 1 9   ? 5.220   -8.477  11.098  1.00 12.62 ? 7   TYR   A C   1 
ATOM   32   O  O   . TYR   A 1 9   ? 4.836   -9.618  11.304  1.00 15.90 ? 7   TYR   A O   1 
ATOM   33   C  CB  . TYR   A 1 9   ? 2.856   -7.553  11.161  1.00 9.14  ? 7   TYR   A CB  1 
ATOM   34   C  CG  . TYR   A 1 9   ? 1.960   -6.488  11.764  1.00 7.72  ? 7   TYR   A CG  1 
ATOM   35   C  CD1 . TYR   A 1 9   ? 1.578   -6.495  13.089  1.00 7.31  ? 7   TYR   A CD1 1 
ATOM   36   C  CD2 . TYR   A 1 9   ? 1.526   -5.463  10.984  1.00 7.64  ? 7   TYR   A CD2 1 
ATOM   37   C  CE1 . TYR   A 1 9   ? 0.761   -5.510  13.604  1.00 6.91  ? 7   TYR   A CE1 1 
ATOM   38   C  CE2 . TYR   A 1 9   ? 0.674   -4.491  11.461  1.00 7.22  ? 7   TYR   A CE2 1 
ATOM   39   C  CZ  . TYR   A 1 9   ? 0.282   -4.523  12.784  1.00 6.89  ? 7   TYR   A CZ  1 
ATOM   40   O  OH  . TYR   A 1 9   ? -0.529  -3.539  13.240  1.00 7.24  ? 7   TYR   A OH  1 
ATOM   41   N  N   . GLY   A 1 10  ? 6.355   -8.245  10.440  1.00 14.15 ? 8   GLY   A N   1 
ATOM   42   C  CA  . GLY   A 1 10  ? 7.292   -9.324  10.103  1.00 16.10 ? 8   GLY   A CA  1 
ATOM   43   C  C   . GLY   A 1 10  ? 8.202   -9.678  11.289  1.00 18.00 ? 8   GLY   A C   1 
ATOM   44   O  O   . GLY   A 1 10  ? 8.290   -8.994  12.324  1.00 19.84 ? 8   GLY   A O   1 
ATOM   45   N  N   . LYS   A 1 11  ? 9.121   -10.611 11.051  1.00 20.45 ? 9   LYS   A N   1 
ATOM   46   C  CA  . LYS   A 1 11  ? 10.032  -11.063 12.093  1.00 23.04 ? 9   LYS   A CA  1 
ATOM   47   C  C   . LYS   A 1 11  ? 11.025  -9.961  12.421  1.00 21.67 ? 9   LYS   A C   1 
ATOM   48   O  O   . LYS   A 1 11  ? 11.494  -9.807  13.564  1.00 21.99 ? 9   LYS   A O   1 
ATOM   49   C  CB  . LYS   A 1 11  ? 10.894  -12.236 11.632  1.00 25.68 ? 9   LYS   A CB  1 
ATOM   50   C  CG  . LYS   A 1 11  ? 10.107  -13.529 11.459  1.00 29.66 ? 9   LYS   A CG  1 
ATOM   51   C  CD  . LYS   A 1 11  ? 11.061  -14.683 11.193  1.00 32.40 ? 9   LYS   A CD  1 
ATOM   52   C  CE  . LYS   A 1 11  ? 10.470  -16.042 11.343  1.00 34.65 ? 9   LYS   A CE  1 
ATOM   53   N  NZ  . LYS   A 1 11  ? 11.503  -17.009 10.949  1.00 36.34 ? 9   LYS   A NZ  1 
ATOM   54   N  N   . HIS   A 1 12  ? 11.410  -9.217  11.396  1.00 18.86 ? 10  HIS   A N   1 
ATOM   55   C  CA  . HIS   A 1 12  ? 12.460  -8.296  11.679  1.00 18.42 ? 10  HIS   A CA  1 
ATOM   56   C  C   . HIS   A 1 12  ? 11.927  -6.923  12.010  1.00 16.05 ? 10  HIS   A C   1 
ATOM   57   O  O   . HIS   A 1 12  ? 12.731  -6.042  12.326  1.00 17.53 ? 10  HIS   A O   1 
ATOM   58   C  CB  . HIS   A 1 12  ? 13.426  -8.272  10.511  1.00 19.42 ? 10  HIS   A CB  1 
ATOM   59   C  CG  . HIS   A 1 12  ? 14.195  -9.561  10.449  1.00 22.41 ? 10  HIS   A CG  1 
ATOM   60   N  ND1 . HIS   A 1 12  ? 13.829  -10.524 9.537   1.00 24.32 ? 10  HIS   A ND1 1 
ATOM   61   C  CD2 . HIS   A 1 12  ? 15.209  -10.097 11.172  1.00 23.62 ? 10  HIS   A CD2 1 
ATOM   62   C  CE1 . HIS   A 1 12  ? 14.608  -11.592 9.676   1.00 23.73 ? 10  HIS   A CE1 1 
ATOM   63   N  NE2 . HIS   A 1 12  ? 15.423  -11.364 10.693  1.00 24.92 ? 10  HIS   A NE2 1 
ATOM   64   N  N   . ASN   A 1 13  ? 10.607  -6.670  11.841  1.00 13.97 ? 11  ASN   A N   1 
ATOM   65   C  CA  . ASN   A 1 13  ? 10.076  -5.336  12.094  1.00 12.59 ? 11  ASN   A CA  1 
ATOM   66   C  C   . ASN   A 1 13  ? 8.772   -5.317  12.912  1.00 11.65 ? 11  ASN   A C   1 
ATOM   67   O  O   . ASN   A 1 13  ? 8.128   -4.279  12.985  1.00 11.98 ? 11  ASN   A O   1 
ATOM   68   C  CB  . ASN   A 1 13  ? 9.930   -4.573  10.780  1.00 12.72 ? 11  ASN   A CB  1 
ATOM   69   C  CG  . ASN   A 1 13  ? 8.841   -5.141  9.914   1.00 13.51 ? 11  ASN   A CG  1 
ATOM   70   O  OD1 . ASN   A 1 13  ? 8.254   -6.174  10.236  1.00 13.71 ? 11  ASN   A OD1 1 
ATOM   71   N  ND2 . ASN   A 1 13  ? 8.526   -4.459  8.826   1.00 15.05 ? 11  ASN   A ND2 1 
ATOM   72   N  N   . GLY   A 1 14  ? 8.453   -6.452  13.524  1.00 10.96 ? 12  GLY   A N   1 
ATOM   73   C  CA  . GLY   A 1 14  ? 7.182   -6.657  14.185  1.00 10.64 ? 12  GLY   A CA  1 
ATOM   74   C  C   . GLY   A 1 14  ? 7.141   -6.042  15.572  1.00 9.66  ? 12  GLY   A C   1 
ATOM   75   O  O   . GLY   A 1 14  ? 8.049   -5.351  16.018  1.00 9.79  ? 12  GLY   A O   1 
ATOM   76   N  N   . PRO   A 1 15  ? 6.052   -6.351  16.309  1.00 8.75  ? 13  PRO   A N   1 
ATOM   77   C  CA  . PRO   A 1 15  ? 5.779   -5.740  17.604  1.00 8.86  ? 13  PRO   A CA  1 
ATOM   78   C  C   . PRO   A 1 15  ? 6.909   -5.755  18.602  1.00 8.90  ? 13  PRO   A C   1 
ATOM   79   O  O   . PRO   A 1 15  ? 7.026   -4.813  19.367  1.00 8.26  ? 13  PRO   A O   1 
ATOM   80   C  CB  . PRO   A 1 15  ? 4.558   -6.518  18.101  1.00 9.29  ? 13  PRO   A CB  1 
ATOM   81   C  CG  . PRO   A 1 15  ? 3.793   -6.828  16.833  1.00 9.34  ? 13  PRO   A CG  1 
ATOM   82   C  CD  . PRO   A 1 15  ? 4.885   -7.136  15.842  1.00 9.53  ? 13  PRO   A CD  1 
ATOM   83   N  N   . GLU   A 1 16  ? 7.775   -6.769  18.602  1.00 10.11 ? 14  GLU   A N   1 
ATOM   84   C  CA  . GLU   A 1 16  ? 8.850   -6.853  19.574  1.00 11.45 ? 14  GLU   A CA  1 
ATOM   85   C  C   . GLU   A 1 16  ? 9.972   -5.874  19.267  1.00 10.69 ? 14  GLU   A C   1 
ATOM   86   O  O   . GLU   A 1 16  ? 10.839  -5.651  20.109  1.00 11.39 ? 14  GLU   A O   1 
ATOM   87   C  CB  . GLU   A 1 16  ? 9.421   -8.241  19.717  1.00 13.92 ? 14  GLU   A CB  1 
ATOM   88   C  CG  . GLU   A 1 16  ? 8.343   -9.263  20.079  1.00 16.49 ? 14  GLU   A CG  1 
ATOM   89   C  CD  . GLU   A 1 16  ? 7.308   -8.875  21.150  1.00 18.66 ? 14  GLU   A CD  1 
ATOM   90   O  OE1 . GLU   A 1 16  ? 7.861   -8.473  22.198  1.00 22.38 ? 14  GLU   A OE1 1 
ATOM   91   O  OE2 . GLU   A 1 16  ? 6.023   -8.967  21.032  1.00 21.55 ? 14  GLU   A OE2 1 
ATOM   92   N  N   . HIS   A 1 17  ? 9.956   -5.279  18.068  1.00 9.55  ? 15  HIS   A N   1 
ATOM   93   C  CA  . HIS   A 1 17  ? 10.928  -4.303  17.635  1.00 9.33  ? 15  HIS   A CA  1 
ATOM   94   C  C   . HIS   A 1 17  ? 10.474  -2.866  17.798  1.00 8.39  ? 15  HIS   A C   1 
ATOM   95   O  O   . HIS   A 1 17  ? 11.299  -1.955  17.714  1.00 8.94  ? 15  HIS   A O   1 
ATOM   96   C  CB  . HIS   A 1 17  ? 11.304  -4.513  16.170  1.00 10.17 ? 15  HIS   A CB  1 
ATOM   97   C  CG  . HIS   A 1 17  ? 12.051  -5.746  15.874  1.00 11.89 ? 15  HIS   A CG  1 
ATOM   98   N  ND1 . HIS   A 1 17  ? 13.426  -5.818  15.966  1.00 13.37 ? 15  HIS   A ND1 1 
ATOM   99   C  CD2 . HIS   A 1 17  ? 11.614  -6.956  15.554  1.00 12.94 ? 15  HIS   A CD2 1 
ATOM   100  C  CE1 . HIS   A 1 17  ? 13.784  -7.049  15.682  1.00 14.52 ? 15  HIS   A CE1 1 
ATOM   101  N  NE2 . HIS   A 1 17  ? 12.721  -7.753  15.416  1.00 14.54 ? 15  HIS   A NE2 1 
ATOM   102  N  N   . TRP   A 1 18  ? 9.157   -2.634  17.929  1.00 7.84  ? 16  TRP   A N   1 
ATOM   103  C  CA  . TRP   A 1 18  ? 8.616   -1.284  17.812  1.00 7.27  ? 16  TRP   A CA  1 
ATOM   104  C  C   . TRP   A 1 18  ? 9.192   -0.319  18.840  1.00 7.59  ? 16  TRP   A C   1 
ATOM   105  O  O   . TRP   A 1 18  ? 9.292   0.871   18.573  1.00 8.26  ? 16  TRP   A O   1 
ATOM   106  C  CB  . TRP   A 1 18  ? 7.092   -1.332  17.935  1.00 6.94  ? 16  TRP   A CB  1 
ATOM   107  C  CG  . TRP   A 1 18  ? 6.402   -2.025  16.795  1.00 6.94  ? 16  TRP   A CG  1 
ATOM   108  C  CD1 . TRP   A 1 18  ? 6.931   -2.489  15.637  1.00 7.11  ? 16  TRP   A CD1 1 
ATOM   109  C  CD2 . TRP   A 1 18  ? 4.989   -2.318  16.745  1.00 6.57  ? 16  TRP   A CD2 1 
ATOM   110  N  NE1 . TRP   A 1 18  ? 5.968   -3.062  14.866  1.00 7.00  ? 16  TRP   A NE1 1 
ATOM   111  C  CE2 . TRP   A 1 18  ? 4.753   -2.958  15.511  1.00 6.73  ? 16  TRP   A CE2 1 
ATOM   112  C  CE3 . TRP   A 1 18  ? 3.929   -2.124  17.609  1.00 6.42  ? 16  TRP   A CE3 1 
ATOM   113  C  CZ2 . TRP   A 1 18  ? 3.478   -3.401  15.124  1.00 6.70  ? 16  TRP   A CZ2 1 
ATOM   114  C  CZ3 . TRP   A 1 18  ? 2.678   -2.536  17.214  1.00 6.31  ? 16  TRP   A CZ3 1 
ATOM   115  C  CH2 . TRP   A 1 18  ? 2.457   -3.181  16.019  1.00 6.51  ? 16  TRP   A CH2 1 
ATOM   116  N  N   . HIS   A 1 19  ? 9.544   -0.825  20.019  1.00 7.91  ? 17  HIS   A N   1 
ATOM   117  C  CA  . HIS   A 1 19  ? 10.069  0.023   21.086  1.00 8.35  ? 17  HIS   A CA  1 
ATOM   118  C  C   . HIS   A 1 19  ? 11.297  0.820   20.706  1.00 8.85  ? 17  HIS   A C   1 
ATOM   119  O  O   . HIS   A 1 19  ? 11.551  1.872   21.292  1.00 9.47  ? 17  HIS   A O   1 
ATOM   120  C  CB  . HIS   A 1 19  ? 10.344  -0.771  22.361  1.00 9.09  ? 17  HIS   A CB  1 
ATOM   121  C  CG  . HIS   A 1 19  ? 11.526  -1.636  22.257  1.00 9.88  ? 17  HIS   A CG  1 
ATOM   122  N  ND1 . HIS   A 1 19  ? 12.738  -1.290  22.829  1.00 11.42 ? 17  HIS   A ND1 1 
ATOM   123  C  CD2 . HIS   A 1 19  ? 11.675  -2.834  21.679  1.00 10.28 ? 17  HIS   A CD2 1 
ATOM   124  C  CE1 . HIS   A 1 19  ? 13.591  -2.262  22.535  1.00 11.57 ? 17  HIS   A CE1 1 
ATOM   125  N  NE2 . HIS   A 1 19  ? 12.996  -3.194  21.863  1.00 11.25 ? 17  HIS   A NE2 1 
ATOM   126  N  N   . LYS   A 1 20  ? 12.076  0.339   19.733  1.00 9.32  ? 18  LYS   A N   1 
ATOM   127  C  CA  . LYS   A 1 20  ? 13.305  1.047   19.371  1.00 10.45 ? 18  LYS   A CA  1 
ATOM   128  C  C   . LYS   A 1 20  ? 12.971  2.390   18.722  1.00 10.88 ? 18  LYS   A C   1 
ATOM   129  O  O   . LYS   A 1 20  ? 13.668  3.351   18.916  1.00 13.91 ? 18  LYS   A O   1 
ATOM   130  C  CB  . LYS   A 1 20  ? 14.160  0.160   18.465  1.00 10.74 ? 18  LYS   A CB  1 
ATOM   131  C  CG  . LYS   A 1 20  ? 14.788  -1.004  19.192  1.00 11.12 ? 18  LYS   A CG  1 
ATOM   132  C  CD  . LYS   A 1 20  ? 15.496  -1.998  18.275  1.00 11.42 ? 18  LYS   A CD  1 
ATOM   133  C  CE  . LYS   A 1 20  ? 14.550  -2.956  17.626  1.00 11.45 ? 18  LYS   A CE  1 
ATOM   134  N  NZ  . LYS   A 1 20  ? 15.225  -3.812  16.649  1.00 11.63 ? 18  LYS   A NZ  1 
ATOM   135  N  N   . ASP   A 1 21  ? 11.974  2.471   17.878  1.00 10.88 ? 19  ASP   A N   1 
ATOM   136  C  CA  . ASP   A 1 21  ? 11.554  3.724   17.277  1.00 11.30 ? 19  ASP   A CA  1 
ATOM   137  C  C   . ASP   A 1 21  ? 10.483  4.435   18.093  1.00 10.53 ? 19  ASP   A C   1 
ATOM   138  O  O   . ASP   A 1 21  ? 10.369  5.648   17.985  1.00 11.45 ? 19  ASP   A O   1 
ATOM   139  C  CB  . ASP   A 1 21  ? 11.039  3.520   15.863  1.00 13.65 ? 19  ASP   A CB  1 
ATOM   140  C  CG  . ASP   A 1 21  ? 12.063  3.507   14.742  1.00 16.46 ? 19  ASP   A CG  1 
ATOM   141  O  OD1 . ASP   A 1 21  ? 13.120  4.028   14.931  1.00 18.64 ? 19  ASP   A OD1 1 
ATOM   142  O  OD2 . ASP   A 1 21  ? 11.731  3.002   13.660  1.00 21.52 ? 19  ASP   A OD2 1 
ATOM   143  N  N   . PHE   A 1 22  ? 9.723   3.694   18.924  1.00 9.74  ? 20  PHE   A N   1 
ATOM   144  C  CA  . PHE   A 1 22  ? 8.586   4.207   19.648  1.00 9.57  ? 20  PHE   A CA  1 
ATOM   145  C  C   . PHE   A 1 22  ? 8.714   3.740   21.084  1.00 9.46  ? 20  PHE   A C   1 
ATOM   146  O  O   . PHE   A 1 22  ? 8.080   2.755   21.488  1.00 8.89  ? 20  PHE   A O   1 
ATOM   147  C  CB  . PHE   A 1 22  ? 7.271   3.760   19.015  1.00 9.51  ? 20  PHE   A CB  1 
ATOM   148  C  CG  . PHE   A 1 22  ? 7.165   4.123   17.559  1.00 9.95  ? 20  PHE   A CG  1 
ATOM   149  C  CD1 . PHE   A 1 22  ? 6.743   5.389   17.182  1.00 11.43 ? 20  PHE   A CD1 1 
ATOM   150  C  CD2 . PHE   A 1 22  ? 7.539   3.213   16.580  1.00 10.71 ? 20  PHE   A CD2 1 
ATOM   151  C  CE1 . PHE   A 1 22  ? 6.694   5.722   15.848  1.00 12.34 ? 20  PHE   A CE1 1 
ATOM   152  C  CE2 . PHE   A 1 22  ? 7.511   3.601   15.242  1.00 11.60 ? 20  PHE   A CE2 1 
ATOM   153  C  CZ  . PHE   A 1 22  ? 7.077   4.832   14.896  1.00 12.07 ? 20  PHE   A CZ  1 
ATOM   154  N  N   . PRO   A 1 23  ? 9.542   4.406   21.902  1.00 10.10 ? 21  PRO   A N   1 
ATOM   155  C  CA  . PRO   A 1 23  ? 9.798   3.931   23.255  1.00 10.24 ? 21  PRO   A CA  1 
ATOM   156  C  C   . PRO   A 1 23  ? 8.558   3.788   24.150  1.00 9.37  ? 21  PRO   A C   1 
ATOM   157  O  O   . PRO   A 1 23  ? 8.569   3.037   25.123  1.00 9.99  ? 21  PRO   A O   1 
ATOM   158  C  CB  . PRO   A 1 23  ? 10.822  4.936   23.854  1.00 11.82 ? 21  PRO   A CB  1 
ATOM   159  C  CG  . PRO   A 1 23  ? 10.744  6.106   22.916  1.00 13.33 ? 21  PRO   A CG  1 
ATOM   160  C  CD  . PRO   A 1 23  ? 10.459  5.501   21.542  1.00 11.41 ? 21  PRO   A CD  1 
ATOM   161  N  N   A ILE   A 1 24  ? 7.486   4.532   23.839  0.50 8.61  ? 22  ILE   A N   1 
ATOM   162  N  N   B ILE   A 1 24  ? 7.500   4.537   23.815  0.50 8.97  ? 22  ILE   A N   1 
ATOM   163  C  CA  A ILE   A 1 24  ? 6.248   4.417   24.600  0.50 8.25  ? 22  ILE   A CA  1 
ATOM   164  C  CA  B ILE   A 1 24  ? 6.231   4.454   24.521  0.50 8.81  ? 22  ILE   A CA  1 
ATOM   165  C  C   A ILE   A 1 24  ? 5.663   3.007   24.458  0.50 8.06  ? 22  ILE   A C   1 
ATOM   166  C  C   B ILE   A 1 24  ? 5.631   3.045   24.406  0.50 8.32  ? 22  ILE   A C   1 
ATOM   167  O  O   A ILE   A 1 24  ? 4.830   2.616   25.259  0.50 7.93  ? 22  ILE   A O   1 
ATOM   168  O  O   B ILE   A 1 24  ? 4.688   2.727   25.119  0.50 8.16  ? 22  ILE   A O   1 
ATOM   169  C  CB  A ILE   A 1 24  ? 5.231   5.497   24.171  0.50 8.22  ? 22  ILE   A CB  1 
ATOM   170  C  CB  B ILE   A 1 24  ? 5.271   5.521   23.957  0.50 9.25  ? 22  ILE   A CB  1 
ATOM   171  C  CG1 A ILE   A 1 24  ? 4.186   5.806   25.220  0.50 8.24  ? 22  ILE   A CG1 1 
ATOM   172  C  CG1 B ILE   A 1 24  ? 4.175   5.893   24.937  0.50 9.73  ? 22  ILE   A CG1 1 
ATOM   173  C  CG2 A ILE   A 1 24  ? 4.550   5.130   22.859  0.50 8.30  ? 22  ILE   A CG2 1 
ATOM   174  C  CG2 B ILE   A 1 24  ? 4.733   5.068   22.604  0.50 9.31  ? 22  ILE   A CG2 1 
ATOM   175  C  CD1 A ILE   A 1 24  ? 3.267   6.927   24.774  0.50 8.20  ? 22  ILE   A CD1 1 
ATOM   176  C  CD1 B ILE   A 1 24  ? 4.701   6.397   26.267  0.50 10.38 ? 22  ILE   A CD1 1 
ATOM   177  N  N   . ALA   A 1 25  ? 6.167   2.192   23.528  1.00 8.04  ? 23  ALA   A N   1 
ATOM   178  C  CA  . ALA   A 1 25  ? 5.734   0.803   23.438  1.00 7.97  ? 23  ALA   A CA  1 
ATOM   179  C  C   . ALA   A 1 25  ? 5.860   0.062   24.770  1.00 8.27  ? 23  ALA   A C   1 
ATOM   180  O  O   . ALA   A 1 25  ? 5.139   -0.922  24.949  1.00 8.73  ? 23  ALA   A O   1 
ATOM   181  C  CB  . ALA   A 1 25  ? 6.554   0.046   22.427  1.00 8.12  ? 23  ALA   A CB  1 
ATOM   182  N  N   . LYS   A 1 26  ? 6.766   0.489   25.648  1.00 8.69  ? 24  LYS   A N   1 
ATOM   183  C  CA  . LYS   A 1 26  ? 6.960   -0.085  26.971  1.00 10.07 ? 24  LYS   A CA  1 
ATOM   184  C  C   . LYS   A 1 26  ? 6.337   0.814   28.055  1.00 10.98 ? 24  LYS   A C   1 
ATOM   185  O  O   . LYS   A 1 26  ? 6.723   0.753   29.219  1.00 12.39 ? 24  LYS   A O   1 
ATOM   186  C  CB  . LYS   A 1 26  ? 8.445   -0.367  27.235  1.00 11.45 ? 24  LYS   A CB  1 
ATOM   187  C  CG  . LYS   A 1 26  ? 9.045   -1.396  26.321  1.00 12.80 ? 24  LYS   A CG  1 
ATOM   188  C  CD  . LYS   A 1 26  ? 10.515  -1.637  26.605  1.00 14.60 ? 24  LYS   A CD  1 
ATOM   189  C  CE  . LYS   A 1 26  ? 11.187  -2.515  25.687  1.00 16.05 ? 24  LYS   A CE  1 
ATOM   190  N  NZ  . LYS   A 1 26  ? 10.903  -3.866  26.111  1.00 18.09 ? 24  LYS   A NZ  1 
ATOM   191  N  N   . GLY   A 1 27  ? 5.350   1.625   27.698  1.00 10.24 ? 25  GLY   A N   1 
ATOM   192  C  CA  . GLY   A 1 27  ? 4.756   2.599   28.617  1.00 10.47 ? 25  GLY   A CA  1 
ATOM   193  C  C   . GLY   A 1 27  ? 3.774   1.969   29.598  1.00 10.11 ? 25  GLY   A C   1 
ATOM   194  O  O   . GLY   A 1 27  ? 3.601   0.754   29.718  1.00 10.23 ? 25  GLY   A O   1 
ATOM   195  N  N   . GLU   A 1 28  ? 3.114   2.877   30.319  1.00 9.80  ? 26  GLU   A N   1 
ATOM   196  C  CA  . GLU   A 1 28  ? 2.289   2.531   31.456  1.00 10.37 ? 26  GLU   A CA  1 
ATOM   197  C  C   . GLU   A 1 28  ? 0.843   2.217   31.077  1.00 9.26  ? 26  GLU   A C   1 
ATOM   198  O  O   . GLU   A 1 28  ? 0.086   1.717   31.911  1.00 9.97  ? 26  GLU   A O   1 
ATOM   199  C  CB  . GLU   A 1 28  ? 2.319   3.670   32.489  1.00 12.25 ? 26  GLU   A CB  1 
ATOM   200  C  CG  . GLU   A 1 28  ? 3.712   3.898   33.063  1.00 14.25 ? 26  GLU   A CG  1 
ATOM   201  C  CD  . GLU   A 1 28  ? 4.305   2.638   33.659  1.00 17.53 ? 26  GLU   A CD  1 
ATOM   202  O  OE1 . GLU   A 1 28  ? 3.602   2.047   34.523  1.00 21.12 ? 26  GLU   A OE1 1 
ATOM   203  O  OE2 . GLU   A 1 28  ? 5.410   2.202   33.230  1.00 22.87 ? 26  GLU   A OE2 1 
ATOM   204  N  N   . ARG   A 1 29  ? 0.415   2.547   29.861  1.00 8.14  ? 27  ARG   A N   1 
ATOM   205  C  CA  . ARG   A 1 29  ? -0.963  2.275   29.466  1.00 7.71  ? 27  ARG   A CA  1 
ATOM   206  C  C   . ARG   A 1 29  ? -1.033  1.825   28.002  1.00 6.74  ? 27  ARG   A C   1 
ATOM   207  O  O   . ARG   A 1 29  ? -1.774  2.416   27.199  1.00 6.80  ? 27  ARG   A O   1 
ATOM   208  C  CB  . ARG   A 1 29  ? -1.898  3.458   29.801  1.00 9.34  ? 27  ARG   A CB  1 
ATOM   209  C  CG  . ARG   A 1 29  ? -1.588  4.819   29.232  1.00 10.47 ? 27  ARG   A CG  1 
ATOM   210  C  CD  . ARG   A 1 29  ? -2.571  5.984   29.416  1.00 11.74 ? 27  ARG   A CD  1 
ATOM   211  N  NE  . ARG   A 1 29  ? -3.710  5.892   28.490  1.00 11.71 ? 27  ARG   A NE  1 
ATOM   212  C  CZ  . ARG   A 1 29  ? -4.681  6.793   28.451  1.00 10.82 ? 27  ARG   A CZ  1 
ATOM   213  N  NH1 . ARG   A 1 29  ? -4.646  7.929   29.157  1.00 11.84 ? 27  ARG   A NH1 1 
ATOM   214  N  NH2 . ARG   A 1 29  ? -5.599  6.592   27.612  1.00 10.69 ? 27  ARG   A NH2 1 
ATOM   215  N  N   . GLN   A 1 30  ? -0.325  0.754   27.677  1.00 6.04  ? 28  GLN   A N   1 
ATOM   216  C  CA  . GLN   A 1 30  ? -0.320  0.242   26.305  1.00 5.71  ? 28  GLN   A CA  1 
ATOM   217  C  C   . GLN   A 1 30  ? -1.474  -0.733  26.094  1.00 5.59  ? 28  GLN   A C   1 
ATOM   218  O  O   . GLN   A 1 30  ? -1.965  -1.410  26.980  1.00 6.22  ? 28  GLN   A O   1 
ATOM   219  C  CB  . GLN   A 1 30  ? 1.031   -0.420  26.041  1.00 6.24  ? 28  GLN   A CB  1 
ATOM   220  C  CG  . GLN   A 1 30  ? 2.145   0.614   25.957  1.00 6.41  ? 28  GLN   A CG  1 
ATOM   221  C  CD  . GLN   A 1 30  ? 2.034   1.420   24.669  1.00 6.20  ? 28  GLN   A CD  1 
ATOM   222  O  OE1 . GLN   A 1 30  ? 2.220   0.868   23.572  1.00 6.63  ? 28  GLN   A OE1 1 
ATOM   223  N  NE2 . GLN   A 1 30  ? 1.663   2.686   24.773  1.00 6.07  ? 28  GLN   A NE2 1 
ATOM   224  N  N   . SER   A 1 31  ? -1.838  -0.836  24.809  1.00 5.19  ? 29  SER   A N   1 
ATOM   225  C  CA  . SER   A 1 31  ? -2.883  -1.704  24.341  1.00 4.98  ? 29  SER   A CA  1 
ATOM   226  C  C   . SER   A 1 31  ? -2.337  -2.582  23.223  1.00 5.10  ? 29  SER   A C   1 
ATOM   227  O  O   . SER   A 1 31  ? -1.415  -2.198  22.506  1.00 5.37  ? 29  SER   A O   1 
ATOM   228  C  CB  . SER   A 1 31  ? -4.059  -0.876  23.824  1.00 5.03  ? 29  SER   A CB  1 
ATOM   229  O  OG  . SER   A 1 31  ? -4.634  -0.145  24.902  1.00 5.30  ? 29  SER   A OG  1 
ATOM   230  N  N   . PRO   A 1 32  ? -2.992  -3.721  22.954  1.00 4.99  ? 30  PRO   A N   1 
ATOM   231  C  CA  . PRO   A 1 32  ? -4.131  -4.289  23.686  1.00 4.94  ? 30  PRO   A CA  1 
ATOM   232  C  C   . PRO   A 1 32  ? -3.695  -4.923  24.973  1.00 5.03  ? 30  PRO   A C   1 
ATOM   233  O  O   . PRO   A 1 32  ? -2.521  -4.953  25.313  1.00 5.36  ? 30  PRO   A O   1 
ATOM   234  C  CB  . PRO   A 1 32  ? -4.652  -5.323  22.671  1.00 5.05  ? 30  PRO   A CB  1 
ATOM   235  C  CG  . PRO   A 1 32  ? -3.356  -5.866  22.067  1.00 5.24  ? 30  PRO   A CG  1 
ATOM   236  C  CD  . PRO   A 1 32  ? -2.512  -4.634  21.912  1.00 5.18  ? 30  PRO   A CD  1 
ATOM   237  N  N   . VAL   A 1 33  ? -4.701  -5.481  25.691  1.00 5.18  ? 31  VAL   A N   1 
ATOM   238  C  CA  . VAL   A 1 33  ? -4.514  -6.221  26.927  1.00 5.50  ? 31  VAL   A CA  1 
ATOM   239  C  C   . VAL   A 1 33  ? -5.392  -7.457  26.865  1.00 5.54  ? 31  VAL   A C   1 
ATOM   240  O  O   . VAL   A 1 33  ? -6.373  -7.543  26.116  1.00 5.83  ? 31  VAL   A O   1 
ATOM   241  C  CB  . VAL   A 1 33  ? -4.846  -5.366  28.182  1.00 6.08  ? 31  VAL   A CB  1 
ATOM   242  C  CG1 . VAL   A 1 33  ? -3.936  -4.162  28.239  1.00 6.68  ? 31  VAL   A CG1 1 
ATOM   243  C  CG2 . VAL   A 1 33  ? -6.311  -4.951  28.226  1.00 6.33  ? 31  VAL   A CG2 1 
ATOM   244  N  N   . ASP   A 1 34  ? -5.053  -8.416  27.746  1.00 5.76  ? 32  ASP   A N   1 
ATOM   245  C  CA  . ASP   A 1 34  ? -5.961  -9.504  28.037  1.00 6.16  ? 32  ASP   A CA  1 
ATOM   246  C  C   . ASP   A 1 34  ? -7.020  -8.986  28.999  1.00 6.27  ? 32  ASP   A C   1 
ATOM   247  O  O   . ASP   A 1 34  ? -6.720  -8.316  29.992  1.00 7.19  ? 32  ASP   A O   1 
ATOM   248  C  CB  . ASP   A 1 34  ? -5.228  -10.673 28.633  1.00 6.81  ? 32  ASP   A CB  1 
ATOM   249  C  CG  . ASP   A 1 34  ? -6.143  -11.838 28.929  1.00 7.29  ? 32  ASP   A CG  1 
ATOM   250  O  OD1 . ASP   A 1 34  ? -6.829  -12.328 27.991  1.00 7.27  ? 32  ASP   A OD1 1 
ATOM   251  O  OD2 . ASP   A 1 34  ? -6.193  -12.279 30.120  1.00 9.39  ? 32  ASP   A OD2 1 
ATOM   252  N  N   . ILE   A 1 35  ? -8.284  -9.315  28.693  1.00 6.57  ? 33  ILE   A N   1 
ATOM   253  C  CA  . ILE   A 1 35  ? -9.425  -8.993  29.547  1.00 7.04  ? 33  ILE   A CA  1 
ATOM   254  C  C   . ILE   A 1 35  ? -9.720  -10.249 30.350  1.00 7.66  ? 33  ILE   A C   1 
ATOM   255  O  O   . ILE   A 1 35  ? -10.263 -11.236 29.879  1.00 7.76  ? 33  ILE   A O   1 
ATOM   256  C  CB  . ILE   A 1 35  ? -10.613 -8.523  28.687  1.00 7.30  ? 33  ILE   A CB  1 
ATOM   257  C  CG1 . ILE   A 1 35  ? -10.261 -7.343  27.838  1.00 7.92  ? 33  ILE   A CG1 1 
ATOM   258  C  CG2 . ILE   A 1 35  ? -11.820 -8.291  29.580  1.00 7.92  ? 33  ILE   A CG2 1 
ATOM   259  C  CD1 . ILE   A 1 35  ? -11.270 -7.022  26.752  1.00 8.43  ? 33  ILE   A CD1 1 
ATOM   260  N  N   A ASP   A 1 36  ? -9.377  -10.171 31.633  0.50 8.30  ? 34  ASP   A N   1 
ATOM   261  N  N   B ASP   A 1 36  ? -9.323  -10.200 31.611  0.50 8.17  ? 34  ASP   A N   1 
ATOM   262  C  CA  A ASP   A 1 36  ? -9.661  -11.228 32.596  0.50 8.96  ? 34  ASP   A CA  1 
ATOM   263  C  CA  B ASP   A 1 36  ? -9.635  -11.267 32.544  0.50 8.68  ? 34  ASP   A CA  1 
ATOM   264  C  C   A ASP   A 1 36  ? -11.089 -10.971 33.085  0.50 9.23  ? 34  ASP   A C   1 
ATOM   265  C  C   B ASP   A 1 36  ? -11.046 -10.992 33.068  0.50 9.10  ? 34  ASP   A C   1 
ATOM   266  O  O   A ASP   A 1 36  ? -11.355 -10.031 33.842  0.50 10.02 ? 34  ASP   A O   1 
ATOM   267  O  O   B ASP   A 1 36  ? -11.216 -10.079 33.879  0.50 9.94  ? 34  ASP   A O   1 
ATOM   268  C  CB  A ASP   A 1 36  ? -8.595  -11.273 33.690  0.50 10.06 ? 34  ASP   A CB  1 
ATOM   269  C  CB  B ASP   A 1 36  ? -8.601  -11.321 33.658  0.50 9.45  ? 34  ASP   A CB  1 
ATOM   270  C  CG  A ASP   A 1 36  ? -8.854  -12.226 34.846  0.50 10.93 ? 34  ASP   A CG  1 
ATOM   271  C  CG  B ASP   A 1 36  ? -8.748  -12.548 34.526  0.50 9.93  ? 34  ASP   A CG  1 
ATOM   272  O  OD1 A ASP   A 1 36  ? -9.994  -12.690 34.989  0.50 11.36 ? 34  ASP   A OD1 1 
ATOM   273  O  OD1 B ASP   A 1 36  ? -8.286  -13.604 34.069  0.50 10.40 ? 34  ASP   A OD1 1 
ATOM   274  O  OD2 A ASP   A 1 36  ? -7.893  -12.509 35.594  0.50 13.20 ? 34  ASP   A OD2 1 
ATOM   275  O  OD2 B ASP   A 1 36  ? -9.338  -12.392 35.609  0.50 10.83 ? 34  ASP   A OD2 1 
ATOM   276  N  N   . THR   A 1 37  ? -12.016 -11.778 32.597  1.00 9.72  ? 35  THR   A N   1 
ATOM   277  C  CA  . THR   A 1 37  ? -13.420 -11.480 32.825  1.00 10.46 ? 35  THR   A CA  1 
ATOM   278  C  C   . THR   A 1 37  ? -13.801 -11.600 34.280  1.00 10.96 ? 35  THR   A C   1 
ATOM   279  O  O   . THR   A 1 37  ? -14.678 -10.890 34.750  1.00 12.65 ? 35  THR   A O   1 
ATOM   280  C  CB  . THR   A 1 37  ? -14.282 -12.400 31.977  1.00 11.67 ? 35  THR   A CB  1 
ATOM   281  O  OG1 . THR   A 1 37  ? -14.179 -13.737 32.465  1.00 12.34 ? 35  THR   A OG1 1 
ATOM   282  C  CG2 . THR   A 1 37  ? -14.014 -12.292 30.497  1.00 12.21 ? 35  THR   A CG2 1 
ATOM   283  N  N   . HIS   A 1 38  ? -13.089 -12.428 35.049  1.00 11.17 ? 36  HIS   A N   1 
ATOM   284  C  CA  . HIS   A 1 38  ? -13.429 -12.610 36.437  1.00 12.45 ? 36  HIS   A CA  1 
ATOM   285  C  C   . HIS   A 1 38  ? -12.912 -11.462 37.285  1.00 13.44 ? 36  HIS   A C   1 
ATOM   286  O  O   . HIS   A 1 38  ? -13.570 -11.220 38.286  1.00 15.35 ? 36  HIS   A O   1 
ATOM   287  C  CB  . HIS   A 1 38  ? -12.992 -14.000 36.894  1.00 13.72 ? 36  HIS   A CB  1 
ATOM   288  C  CG  . HIS   A 1 38  ? -13.860 -15.132 36.348  1.00 14.91 ? 36  HIS   A CG  1 
ATOM   289  N  ND1 . HIS   A 1 38  ? -15.193 -15.195 36.734  1.00 16.89 ? 36  HIS   A ND1 1 
ATOM   290  C  CD2 . HIS   A 1 38  ? -13.676 -16.089 35.390  1.00 15.52 ? 36  HIS   A CD2 1 
ATOM   291  C  CE1 . HIS   A 1 38  ? -15.767 -16.208 36.107  1.00 17.59 ? 36  HIS   A CE1 1 
ATOM   292  N  NE2 . HIS   A 1 38  ? -14.877 -16.773 35.301  1.00 16.97 ? 36  HIS   A NE2 1 
ATOM   293  N  N   . THR   A 1 39  ? -11.813 -10.793 36.871  1.00 13.91 ? 37  THR   A N   1 
ATOM   294  C  CA  . THR   A 1 39  ? -11.207 -9.674  37.590  1.00 15.33 ? 37  THR   A CA  1 
ATOM   295  C  C   . THR   A 1 39  ? -11.799 -8.308  37.203  1.00 14.36 ? 37  THR   A C   1 
ATOM   296  O  O   . THR   A 1 39  ? -11.612 -7.347  37.930  1.00 15.59 ? 37  THR   A O   1 
ATOM   297  C  CB  . THR   A 1 39  ? -9.698  -9.700  37.319  1.00 18.22 ? 37  THR   A CB  1 
ATOM   298  O  OG1 . THR   A 1 39  ? -9.183  -10.901 37.856  1.00 21.67 ? 37  THR   A OG1 1 
ATOM   299  C  CG2 . THR   A 1 39  ? -8.958  -8.559  37.989  1.00 19.51 ? 37  THR   A CG2 1 
ATOM   300  N  N   . ALA   A 1 40  ? -12.438 -8.196  36.042  1.00 12.54 ? 38  ALA   A N   1 
ATOM   301  C  CA  . ALA   A 1 40  ? -13.080 -6.936  35.644  1.00 12.21 ? 38  ALA   A CA  1 
ATOM   302  C  C   . ALA   A 1 40  ? -14.157 -6.643  36.667  1.00 13.37 ? 38  ALA   A C   1 
ATOM   303  O  O   . ALA   A 1 40  ? -14.720 -7.545  37.262  1.00 16.75 ? 38  ALA   A O   1 
ATOM   304  C  CB  . ALA   A 1 40  ? -13.617 -7.042  34.234  1.00 11.79 ? 38  ALA   A CB  1 
ATOM   305  N  N   . LYS   A 1 41  ? -14.335 -5.406  37.039  1.00 13.57 ? 39  LYS   A N   1 
ATOM   306  C  CA  . LYS   A 1 41  ? -15.408 -5.187  38.001  1.00 14.05 ? 39  LYS   A CA  1 
ATOM   307  C  C   . LYS   A 1 41  ? -16.543 -4.395  37.388  1.00 12.08 ? 39  LYS   A C   1 
ATOM   308  O  O   . LYS   A 1 41  ? -16.373 -3.399  36.667  1.00 10.86 ? 39  LYS   A O   1 
ATOM   309  C  CB  . LYS   A 1 41  ? -14.992 -4.605  39.327  1.00 15.56 ? 39  LYS   A CB  1 
ATOM   310  C  CG  . LYS   A 1 41  ? -16.049 -4.571  40.407  1.00 16.85 ? 39  LYS   A CG  1 
ATOM   311  C  CD  . LYS   A 1 41  ? -15.535 -3.702  41.519  1.00 17.74 ? 39  LYS   A CD  1 
ATOM   312  C  CE  . LYS   A 1 41  ? -16.515 -3.676  42.688  1.00 19.42 ? 39  LYS   A CE  1 
ATOM   313  N  NZ  . LYS   A 1 41  ? -16.214 -2.846  43.828  1.00 21.64 ? 39  LYS   A NZ  1 
ATOM   314  N  N   . TYR   A 1 42  ? -17.745 -4.853  37.677  1.00 13.66 ? 40  TYR   A N   1 
ATOM   315  C  CA  . TYR   A 1 42  ? -18.939 -4.163  37.270  1.00 13.30 ? 40  TYR   A CA  1 
ATOM   316  C  C   . TYR   A 1 42  ? -18.964 -2.778  37.903  1.00 12.66 ? 40  TYR   A C   1 
ATOM   317  O  O   . TYR   A 1 42  ? -18.753 -2.596  39.117  1.00 13.38 ? 40  TYR   A O   1 
ATOM   318  C  CB  . TYR   A 1 42  ? -20.124 -4.985  37.782  1.00 15.06 ? 40  TYR   A CB  1 
ATOM   319  C  CG  . TYR   A 1 42  ? -21.440 -4.323  37.573  1.00 16.85 ? 40  TYR   A CG  1 
ATOM   320  C  CD1 . TYR   A 1 42  ? -21.840 -3.859  36.345  1.00 17.23 ? 40  TYR   A CD1 1 
ATOM   321  C  CD2 . TYR   A 1 42  ? -22.289 -4.196  38.656  1.00 18.44 ? 40  TYR   A CD2 1 
ATOM   322  C  CE1 . TYR   A 1 42  ? -23.058 -3.252  36.179  1.00 19.00 ? 40  TYR   A CE1 1 
ATOM   323  C  CE2 . TYR   A 1 42  ? -23.511 -3.582  38.502  1.00 19.39 ? 40  TYR   A CE2 1 
ATOM   324  C  CZ  . TYR   A 1 42  ? -23.889 -3.115  37.259  1.00 19.58 ? 40  TYR   A CZ  1 
ATOM   325  O  OH  . TYR   A 1 42  ? -25.109 -2.544  37.104  1.00 23.22 ? 40  TYR   A OH  1 
ATOM   326  N  N   . ASP   A 1 43  ? -19.204 -1.770  37.102  1.00 12.53 ? 41  ASP   A N   1 
ATOM   327  C  CA  . ASP   A 1 43  ? -19.291 -0.410  37.600  1.00 14.13 ? 41  ASP   A CA  1 
ATOM   328  C  C   . ASP   A 1 43  ? -20.701 0.101   37.330  1.00 15.62 ? 41  ASP   A C   1 
ATOM   329  O  O   . ASP   A 1 43  ? -21.029 0.505   36.221  1.00 15.48 ? 41  ASP   A O   1 
ATOM   330  C  CB  . ASP   A 1 43  ? -18.235 0.439   36.932  1.00 15.83 ? 41  ASP   A CB  1 
ATOM   331  C  CG  . ASP   A 1 43  ? -18.182 1.866   37.442  1.00 18.75 ? 41  ASP   A CG  1 
ATOM   332  O  OD1 . ASP   A 1 43  ? -19.114 2.250   38.170  1.00 20.08 ? 41  ASP   A OD1 1 
ATOM   333  O  OD2 . ASP   A 1 43  ? -17.205 2.519   37.079  1.00 22.78 ? 41  ASP   A OD2 1 
ATOM   334  N  N   . PRO   A 1 44  ? -21.610 0.078   38.344  1.00 18.11 ? 42  PRO   A N   1 
ATOM   335  C  CA  . PRO   A 1 44  ? -23.030 0.400   38.136  1.00 19.52 ? 42  PRO   A CA  1 
ATOM   336  C  C   . PRO   A 1 44  ? -23.174 1.872   37.796  1.00 21.07 ? 42  PRO   A C   1 
ATOM   337  O  O   . PRO   A 1 44  ? -24.255 2.316   37.425  1.00 24.78 ? 42  PRO   A O   1 
ATOM   338  C  CB  . PRO   A 1 44  ? -23.743 -0.021  39.437  1.00 21.15 ? 42  PRO   A CB  1 
ATOM   339  C  CG  . PRO   A 1 44  ? -22.652 0.083   40.474  1.00 21.61 ? 42  PRO   A CG  1 
ATOM   340  C  CD  . PRO   A 1 44  ? -21.372 -0.303  39.745  1.00 19.94 ? 42  PRO   A CD  1 
ATOM   341  N  N   . SER   A 1 45  ? -22.120 2.677   37.952  1.00 20.08 ? 43  SER   A N   1 
ATOM   342  C  CA  . SER   A 1 45  ? -22.289 4.070   37.579  1.00 23.06 ? 43  SER   A CA  1 
ATOM   343  C  C   . SER   A 1 45  ? -22.000 4.336   36.089  1.00 21.14 ? 43  SER   A C   1 
ATOM   344  O  O   . SER   A 1 45  ? -22.385 5.404   35.617  1.00 24.94 ? 43  SER   A O   1 
ATOM   345  C  CB  . SER   A 1 45  ? -21.445 4.925   38.434  1.00 24.90 ? 43  SER   A CB  1 
ATOM   346  O  OG  . SER   A 1 45  ? -20.115 4.902   37.970  1.00 25.28 ? 43  SER   A OG  1 
ATOM   347  N  N   A LEU   A 1 46  ? -21.131 3.636   35.371  0.50 18.27 ? 44  LEU   A N   1 
ATOM   348  N  N   B LEU   A 1 46  ? -21.557 3.267   35.370  0.50 19.03 ? 44  LEU   A N   1 
ATOM   349  C  CA  A LEU   A 1 46  ? -21.057 3.990   33.966  0.50 16.08 ? 44  LEU   A CA  1 
ATOM   350  C  CA  B LEU   A 1 46  ? -21.262 3.260   33.933  0.50 16.83 ? 44  LEU   A CA  1 
ATOM   351  C  C   A LEU   A 1 46  ? -22.452 4.424   33.520  0.50 15.50 ? 44  LEU   A C   1 
ATOM   352  C  C   B LEU   A 1 46  ? -22.574 3.333   33.164  0.50 17.18 ? 44  LEU   A C   1 
ATOM   353  O  O   A LEU   A 1 46  ? -23.445 3.819   33.905  0.50 15.04 ? 44  LEU   A O   1 
ATOM   354  O  O   B LEU   A 1 46  ? -23.538 2.624   33.481  0.50 18.35 ? 44  LEU   A O   1 
ATOM   355  C  CB  A LEU   A 1 46  ? -20.560 2.770   33.212  0.50 14.41 ? 44  LEU   A CB  1 
ATOM   356  C  CB  B LEU   A 1 46  ? -20.444 2.081   33.392  0.50 15.30 ? 44  LEU   A CB  1 
ATOM   357  C  CG  A LEU   A 1 46  ? -19.134 2.333   33.525  0.50 13.74 ? 44  LEU   A CG  1 
ATOM   358  C  CG  B LEU   A 1 46  ? -18.921 2.165   33.504  0.50 14.56 ? 44  LEU   A CG  1 
ATOM   359  C  CD1 A LEU   A 1 46  ? -18.896 0.954   32.952  0.50 13.45 ? 44  LEU   A CD1 1 
ATOM   360  C  CD1 B LEU   A 1 46  ? -18.393 0.748   33.267  0.50 14.27 ? 44  LEU   A CD1 1 
ATOM   361  C  CD2 A LEU   A 1 46  ? -18.151 3.344   32.958  0.50 13.72 ? 44  LEU   A CD2 1 
ATOM   362  C  CD2 B LEU   A 1 46  ? -18.216 3.143   32.538  0.50 14.37 ? 44  LEU   A CD2 1 
ATOM   363  N  N   A LYS   A 1 47  ? -22.517 5.450   32.668  0.50 14.53 ? 45  LYS   A N   1 
ATOM   364  N  N   B LYS   A 1 47  ? -22.594 4.228   32.180  0.50 16.59 ? 45  LYS   A N   1 
ATOM   365  C  CA  A LYS   A 1 47  ? -23.779 5.863   32.070  0.50 14.01 ? 45  LYS   A CA  1 
ATOM   366  C  CA  B LYS   A 1 47  ? -23.825 4.503   31.461  0.50 15.99 ? 45  LYS   A CA  1 
ATOM   367  C  C   A LYS   A 1 47  ? -24.077 5.036   30.832  0.50 12.58 ? 45  LYS   A C   1 
ATOM   368  C  C   B LYS   A 1 47  ? -23.875 3.660   30.194  0.50 14.78 ? 45  LYS   A C   1 
ATOM   369  O  O   A LYS   A 1 47  ? -23.171 4.433   30.297  0.50 10.96 ? 45  LYS   A O   1 
ATOM   370  O  O   B LYS   A 1 47  ? -22.861 3.210   29.662  0.50 13.89 ? 45  LYS   A O   1 
ATOM   371  C  CB  A LYS   A 1 47  ? -23.639 7.332   31.673  0.50 15.17 ? 45  LYS   A CB  1 
ATOM   372  C  CB  B LYS   A 1 47  ? -23.829 5.992   31.107  0.50 16.67 ? 45  LYS   A CB  1 
ATOM   373  C  CG  A LYS   A 1 47  ? -23.781 8.253   32.877  0.50 16.97 ? 45  LYS   A CG  1 
ATOM   374  C  CG  B LYS   A 1 47  ? -24.016 6.971   32.260  0.50 17.56 ? 45  LYS   A CG  1 
ATOM   375  C  CD  A LYS   A 1 47  ? -23.595 9.741   32.616  0.50 18.30 ? 45  LYS   A CD  1 
ATOM   376  C  CD  B LYS   A 1 47  ? -23.266 8.291   32.073  0.50 18.72 ? 45  LYS   A CD  1 
ATOM   377  C  CE  A LYS   A 1 47  ? -23.646 10.463  33.925  0.50 19.51 ? 45  LYS   A CE  1 
ATOM   378  C  CE  B LYS   A 1 47  ? -23.146 9.156   33.288  0.50 20.08 ? 45  LYS   A CE  1 
ATOM   379  N  NZ  A LYS   A 1 47  ? -23.122 11.823  33.806  0.50 20.41 ? 45  LYS   A NZ  1 
ATOM   380  N  NZ  B LYS   A 1 47  ? -22.618 10.482  32.954  0.50 20.87 ? 45  LYS   A NZ  1 
ATOM   381  N  N   A PRO   A 1 48  ? -25.318 4.983   30.328  0.50 11.98 ? 46  PRO   A N   1 
ATOM   382  N  N   B PRO   A 1 48  ? -25.083 3.471   29.632  0.50 14.11 ? 46  PRO   A N   1 
ATOM   383  C  CA  A PRO   A 1 48  ? -25.586 4.241   29.096  0.50 11.72 ? 46  PRO   A CA  1 
ATOM   384  C  CA  B PRO   A 1 48  ? -25.221 2.809   28.349  0.50 13.64 ? 46  PRO   A CA  1 
ATOM   385  C  C   A PRO   A 1 48  ? -24.724 4.699   27.930  0.50 11.30 ? 46  PRO   A C   1 
ATOM   386  C  C   B PRO   A 1 48  ? -24.379 3.590   27.363  0.50 12.61 ? 46  PRO   A C   1 
ATOM   387  O  O   A PRO   A 1 48  ? -24.460 5.881   27.789  0.50 11.52 ? 46  PRO   A O   1 
ATOM   388  O  O   B PRO   A 1 48  ? -24.304 4.826   27.399  0.50 11.66 ? 46  PRO   A O   1 
ATOM   389  C  CB  A PRO   A 1 48  ? -27.067 4.505   28.836  0.50 12.29 ? 46  PRO   A CB  1 
ATOM   390  C  CB  B PRO   A 1 48  ? -26.713 2.857   28.021  0.50 14.17 ? 46  PRO   A CB  1 
ATOM   391  C  CG  A PRO   A 1 48  ? -27.602 4.849   30.214  0.50 12.66 ? 46  PRO   A CG  1 
ATOM   392  C  CG  B PRO   A 1 48  ? -27.388 3.187   29.345  0.50 14.73 ? 46  PRO   A CG  1 
ATOM   393  C  CD  A PRO   A 1 48  ? -26.511 5.599   30.934  0.50 12.48 ? 46  PRO   A CD  1 
ATOM   394  C  CD  B PRO   A 1 48  ? -26.369 3.945   30.170  0.50 14.40 ? 46  PRO   A CD  1 
ATOM   395  N  N   A LEU   A 1 49  ? -24.309 3.726   27.109  0.50 10.68 ? 47  LEU   A N   1 
ATOM   396  N  N   B LEU   A 1 49  ? -23.781 2.837   26.457  0.50 12.59 ? 47  LEU   A N   1 
ATOM   397  C  CA  A LEU   A 1 49  ? -23.459 3.991   25.948  0.50 10.42 ? 47  LEU   A CA  1 
ATOM   398  C  CA  B LEU   A 1 49  ? -23.154 3.470   25.328  0.50 12.28 ? 47  LEU   A CA  1 
ATOM   399  C  C   A LEU   A 1 49  ? -24.286 4.244   24.675  0.50 10.97 ? 47  LEU   A C   1 
ATOM   400  C  C   B LEU   A 1 49  ? -24.273 4.189   24.584  0.50 11.75 ? 47  LEU   A C   1 
ATOM   401  O  O   A LEU   A 1 49  ? -25.126 3.428   24.273  0.50 11.56 ? 47  LEU   A O   1 
ATOM   402  O  O   B LEU   A 1 49  ? -25.446 3.819   24.717  0.50 11.45 ? 47  LEU   A O   1 
ATOM   403  C  CB  A LEU   A 1 49  ? -22.587 2.774   25.683  0.50 10.52 ? 47  LEU   A CB  1 
ATOM   404  C  CB  B LEU   A 1 49  ? -22.462 2.377   24.529  0.50 13.49 ? 47  LEU   A CB  1 
ATOM   405  C  CG  A LEU   A 1 49  ? -21.662 2.889   24.471  0.50 10.57 ? 47  LEU   A CG  1 
ATOM   406  C  CG  B LEU   A 1 49  ? -21.117 2.761   23.965  0.50 14.51 ? 47  LEU   A CG  1 
ATOM   407  C  CD1 A LEU   A 1 49  ? -20.460 3.844   24.640  0.50 11.08 ? 47  LEU   A CD1 1 
ATOM   408  C  CD1 B LEU   A 1 49  ? -20.253 3.334   25.117  0.50 14.48 ? 47  LEU   A CD1 1 
ATOM   409  C  CD2 A LEU   A 1 49  ? -21.152 1.502   24.130  0.50 10.84 ? 47  LEU   A CD2 1 
ATOM   410  C  CD2 B LEU   A 1 49  ? -20.571 1.501   23.323  0.50 14.70 ? 47  LEU   A CD2 1 
ATOM   411  N  N   . SER   A 1 50  ? -23.925 5.280   23.920  1.00 10.55 ? 48  SER   A N   1 
ATOM   412  C  CA  . SER   A 1 50  ? -24.760 5.827   22.855  1.00 11.06 ? 48  SER   A CA  1 
ATOM   413  C  C   . SER   A 1 50  ? -23.911 5.788   21.583  1.00 10.97 ? 48  SER   A C   1 
ATOM   414  O  O   . SER   A 1 50  ? -22.949 6.538   21.480  1.00 11.00 ? 48  SER   A O   1 
ATOM   415  C  CB  . SER   A 1 50  ? -25.153 7.272   23.237  1.00 12.30 ? 48  SER   A CB  1 
ATOM   416  O  OG  . SER   A 1 50  ? -25.732 7.986   22.170  1.00 14.83 ? 48  SER   A OG  1 
ATOM   417  N  N   . VAL   A 1 51  ? -24.329 4.978   20.637  1.00 12.00 ? 49  VAL   A N   1 
ATOM   418  C  CA  . VAL   A 1 51  ? -23.709 4.881   19.344  1.00 13.24 ? 49  VAL   A CA  1 
ATOM   419  C  C   . VAL   A 1 51  ? -24.681 5.461   18.319  1.00 13.79 ? 49  VAL   A C   1 
ATOM   420  O  O   . VAL   A 1 51  ? -25.706 4.830   18.106  1.00 16.42 ? 49  VAL   A O   1 
ATOM   421  C  CB  . VAL   A 1 51  ? -23.332 3.411   19.020  1.00 15.02 ? 49  VAL   A CB  1 
ATOM   422  C  CG1 . VAL   A 1 51  ? -22.494 3.309   17.754  1.00 16.07 ? 49  VAL   A CG1 1 
ATOM   423  C  CG2 . VAL   A 1 51  ? -22.603 2.726   20.177  1.00 15.52 ? 49  VAL   A CG2 1 
ATOM   424  N  N   . SER   A 1 52  ? -24.400 6.631   17.734  1.00 13.21 ? 50  SER   A N   1 
ATOM   425  C  CA  . SER   A 1 52  ? -25.348 7.314   16.881  1.00 14.23 ? 50  SER   A CA  1 
ATOM   426  C  C   . SER   A 1 52  ? -24.749 7.447   15.502  1.00 13.27 ? 50  SER   A C   1 
ATOM   427  O  O   . SER   A 1 52  ? -24.025 8.385   15.237  1.00 13.28 ? 50  SER   A O   1 
ATOM   428  C  CB  . SER   A 1 52  ? -25.721 8.641   17.454  1.00 16.15 ? 50  SER   A CB  1 
ATOM   429  O  OG  . SER   A 1 52  ? -26.373 8.461   18.706  1.00 19.92 ? 50  SER   A OG  1 
ATOM   430  N  N   . TYR   A 1 53  ? -25.008 6.442   14.650  1.00 12.79 ? 51  TYR   A N   1 
ATOM   431  C  CA  . TYR   A 1 53  ? -24.384 6.340   13.339  1.00 12.45 ? 51  TYR   A CA  1 
ATOM   432  C  C   . TYR   A 1 53  ? -25.369 6.622   12.205  1.00 12.88 ? 51  TYR   A C   1 
ATOM   433  O  O   . TYR   A 1 53  ? -24.991 6.473   11.043  1.00 13.18 ? 51  TYR   A O   1 
ATOM   434  C  CB  . TYR   A 1 53  ? -23.749 4.955   13.176  1.00 12.03 ? 51  TYR   A CB  1 
ATOM   435  C  CG  . TYR   A 1 53  ? -22.489 4.668   13.981  1.00 10.58 ? 51  TYR   A CG  1 
ATOM   436  C  CD1 . TYR   A 1 53  ? -21.775 5.662   14.639  1.00 10.15 ? 51  TYR   A CD1 1 
ATOM   437  C  CD2 . TYR   A 1 53  ? -21.970 3.390   14.016  1.00 9.80  ? 51  TYR   A CD2 1 
ATOM   438  C  CE1 . TYR   A 1 53  ? -20.565 5.395   15.283  1.00 9.06  ? 51  TYR   A CE1 1 
ATOM   439  C  CE2 . TYR   A 1 53  ? -20.794 3.105   14.682  1.00 9.26  ? 51  TYR   A CE2 1 
ATOM   440  C  CZ  . TYR   A 1 53  ? -20.073 4.097   15.321  1.00 8.84  ? 51  TYR   A CZ  1 
ATOM   441  O  OH  . TYR   A 1 53  ? -18.920 3.733   15.932  1.00 8.76  ? 51  TYR   A OH  1 
ATOM   442  N  N   . ASP   A 1 54  ? -26.611 7.053   12.478  1.00 14.50 ? 52  ASP   A N   1 
ATOM   443  C  CA  . ASP   A 1 54  ? -27.586 7.223   11.391  1.00 16.16 ? 52  ASP   A CA  1 
ATOM   444  C  C   . ASP   A 1 54  ? -27.130 8.226   10.319  1.00 16.20 ? 52  ASP   A C   1 
ATOM   445  O  O   . ASP   A 1 54  ? -27.511 8.086   9.156   1.00 17.60 ? 52  ASP   A O   1 
ATOM   446  C  CB  . ASP   A 1 54  ? -28.977 7.504   11.927  1.00 19.09 ? 52  ASP   A CB  1 
ATOM   447  C  CG  . ASP   A 1 54  ? -29.023 8.789   12.704  1.00 22.99 ? 52  ASP   A CG  1 
ATOM   448  O  OD1 . ASP   A 1 54  ? -28.384 8.829   13.770  1.00 27.80 ? 52  ASP   A OD1 1 
ATOM   449  O  OD2 . ASP   A 1 54  ? -29.731 9.703   12.239  1.00 28.81 ? 52  ASP   A OD2 1 
ATOM   450  N  N   . GLN   A 1 55  ? -26.391 9.280   10.650  1.00 15.63 ? 53  GLN   A N   1 
ATOM   451  C  CA  . GLN   A 1 55  ? -25.962 10.233  9.623   1.00 16.41 ? 53  GLN   A CA  1 
ATOM   452  C  C   . GLN   A 1 55  ? -24.532 9.990   9.141   1.00 14.30 ? 53  GLN   A C   1 
ATOM   453  O  O   . GLN   A 1 55  ? -23.952 10.877  8.546   1.00 14.66 ? 53  GLN   A O   1 
ATOM   454  C  CB  . GLN   A 1 55  ? -26.177 11.643  10.183  1.00 17.99 ? 53  GLN   A CB  1 
ATOM   455  C  CG  . GLN   A 1 55  ? -27.655 11.962  10.435  1.00 19.31 ? 53  GLN   A CG  1 
ATOM   456  C  CD  . GLN   A 1 55  ? -28.402 12.138  9.135   1.00 21.93 ? 53  GLN   A CD  1 
ATOM   457  O  OE1 . GLN   A 1 55  ? -28.012 12.961  8.296   1.00 26.08 ? 53  GLN   A OE1 1 
ATOM   458  N  NE2 . GLN   A 1 55  ? -29.437 11.335  8.927   1.00 23.14 ? 53  GLN   A NE2 1 
ATOM   459  N  N   . ALA   A 1 56  ? -23.949 8.831   9.434   1.00 12.61 ? 54  ALA   A N   1 
ATOM   460  C  CA  . ALA   A 1 56  ? -22.576 8.574   9.049   1.00 11.99 ? 54  ALA   A CA  1 
ATOM   461  C  C   . ALA   A 1 56  ? -22.402 8.716   7.542   1.00 12.30 ? 54  ALA   A C   1 
ATOM   462  O  O   . ALA   A 1 56  ? -23.256 8.263   6.753   1.00 14.45 ? 54  ALA   A O   1 
ATOM   463  C  CB  . ALA   A 1 56  ? -22.150 7.179   9.472   1.00 12.88 ? 54  ALA   A CB  1 
ATOM   464  N  N   . THR   A 1 57  ? -21.289 9.369   7.175   1.00 10.45 ? 55  THR   A N   1 
ATOM   465  C  CA  . THR   A 1 57  ? -20.925 9.585   5.773   1.00 10.72 ? 55  THR   A CA  1 
ATOM   466  C  C   . THR   A 1 57  ? -19.575 8.959   5.479   1.00 9.07  ? 55  THR   A C   1 
ATOM   467  O  O   . THR   A 1 57  ? -18.552 9.570   5.752   1.00 8.65  ? 55  THR   A O   1 
ATOM   468  C  CB  . THR   A 1 57  ? -20.832 11.084  5.419   1.00 13.39 ? 55  THR   A CB  1 
ATOM   469  O  OG1 . THR   A 1 57  ? -22.082 11.730  5.438   1.00 17.57 ? 55  THR   A OG1 1 
ATOM   470  C  CG2 . THR   A 1 57  ? -20.294 11.262  4.004   1.00 14.36 ? 55  THR   A CG2 1 
ATOM   471  N  N   . SER   A 1 58  ? -19.566 7.742   4.966   1.00 8.42  ? 56  SER   A N   1 
ATOM   472  C  CA  . SER   A 1 58  ? -18.326 7.121   4.539   1.00 8.27  ? 56  SER   A CA  1 
ATOM   473  C  C   . SER   A 1 58  ? -17.856 7.772   3.264   1.00 8.48  ? 56  SER   A C   1 
ATOM   474  O  O   . SER   A 1 58  ? -18.658 8.247   2.467   1.00 8.98  ? 56  SER   A O   1 
ATOM   475  C  CB  . SER   A 1 58  ? -18.444 5.653   4.377   1.00 8.55  ? 56  SER   A CB  1 
ATOM   476  O  OG  . SER   A 1 58  ? -19.298 5.269   3.300   1.00 9.06  ? 56  SER   A OG  1 
ATOM   477  N  N   . LEU   A 1 59  ? -16.537 7.806   3.075   1.00 8.30  ? 57  LEU   A N   1 
ATOM   478  C  CA  . LEU   A 1 59  ? -15.991 8.435   1.879   1.00 8.85  ? 57  LEU   A CA  1 
ATOM   479  C  C   . LEU   A 1 59  ? -15.150 7.497   1.032   1.00 8.41  ? 57  LEU   A C   1 
ATOM   480  O  O   . LEU   A 1 59  ? -15.245 7.522   -0.186  1.00 9.24  ? 57  LEU   A O   1 
ATOM   481  C  CB  . LEU   A 1 59  ? -15.146 9.628   2.311   1.00 10.74 ? 57  LEU   A CB  1 
ATOM   482  C  CG  . LEU   A 1 59  ? -15.965 10.806  2.885   1.00 12.67 ? 57  LEU   A CG  1 
ATOM   483  C  CD1 . LEU   A 1 59  ? -14.987 11.910  3.240   1.00 13.77 ? 57  LEU   A CD1 1 
ATOM   484  C  CD2 . LEU   A 1 59  ? -17.011 11.365  1.909   1.00 14.06 ? 57  LEU   A CD2 1 
ATOM   485  N  N   . ARG   A 1 60  ? -14.254 6.732   1.649   1.00 8.07  ? 58  ARG   A N   1 
ATOM   486  C  CA  . ARG   A 1 60  ? -13.153 6.104   0.909   1.00 7.92  ? 58  ARG   A CA  1 
ATOM   487  C  C   . ARG   A 1 60  ? -12.670 4.901   1.723   1.00 7.03  ? 58  ARG   A C   1 
ATOM   488  O  O   . ARG   A 1 60  ? -12.839 4.870   2.961   1.00 7.42  ? 58  ARG   A O   1 
ATOM   489  C  CB  . ARG   A 1 60  ? -12.013 7.102   0.709   1.00 9.43  ? 58  ARG   A CB  1 
ATOM   490  C  CG  . ARG   A 1 60  ? -10.945 6.763   -0.295  1.00 11.29 ? 58  ARG   A CG  1 
ATOM   491  C  CD  . ARG   A 1 60  ? -9.933  7.882   -0.353  1.00 12.43 ? 58  ARG   A CD  1 
ATOM   492  N  NE  . ARG   A 1 60  ? -9.086  7.937   0.825   1.00 12.68 ? 58  ARG   A NE  1 
ATOM   493  C  CZ  . ARG   A 1 60  ? -7.776  8.107   0.764   1.00 12.71 ? 58  ARG   A CZ  1 
ATOM   494  N  NH1 . ARG   A 1 60  ? -7.154  8.352   -0.362  1.00 13.56 ? 58  ARG   A NH1 1 
ATOM   495  N  NH2 . ARG   A 1 60  ? -7.119  8.043   1.867   1.00 12.58 ? 58  ARG   A NH2 1 
ATOM   496  N  N   . ILE   A 1 61  ? -12.038 3.965   1.017   1.00 6.68  ? 59  ILE   A N   1 
ATOM   497  C  CA  . ILE   A 1 61  ? -11.358 2.863   1.656   1.00 6.82  ? 59  ILE   A CA  1 
ATOM   498  C  C   . ILE   A 1 61  ? -9.928  2.860   1.148   1.00 7.04  ? 59  ILE   A C   1 
ATOM   499  O  O   . ILE   A 1 61  ? -9.687  3.057   -0.047  1.00 8.16  ? 59  ILE   A O   1 
ATOM   500  C  CB  . ILE   A 1 61  ? -12.134 1.551   1.438   1.00 6.96  ? 59  ILE   A CB  1 
ATOM   501  C  CG1 . ILE   A 1 61  ? -11.591 0.426   2.327   1.00 7.21  ? 59  ILE   A CG1 1 
ATOM   502  C  CG2 . ILE   A 1 61  ? -12.160 1.161   -0.054  1.00 7.42  ? 59  ILE   A CG2 1 
ATOM   503  C  CD1 . ILE   A 1 61  ? -12.397 -0.869  2.248   1.00 7.62  ? 59  ILE   A CD1 1 
ATOM   504  N  N   . LEU   A 1 62  ? -8.959  2.687   2.060   1.00 6.86  ? 60  LEU   A N   1 
ATOM   505  C  CA  . LEU   A 1 62  ? -7.543  2.824   1.802   1.00 7.07  ? 60  LEU   A CA  1 
ATOM   506  C  C   . LEU   A 1 62  ? -6.781  1.613   2.335   1.00 6.62  ? 60  LEU   A C   1 
ATOM   507  O  O   . LEU   A 1 62  ? -6.909  1.299   3.503   1.00 7.05  ? 60  LEU   A O   1 
ATOM   508  C  CB  . LEU   A 1 62  ? -7.009  4.108   2.477   1.00 7.97  ? 60  LEU   A CB  1 
ATOM   509  C  CG  . LEU   A 1 62  ? -5.485  4.276   2.461   1.00 8.65  ? 60  LEU   A CG  1 
ATOM   510  C  CD1 . LEU   A 1 62  ? -4.946  4.531   1.069   1.00 8.94  ? 60  LEU   A CD1 1 
ATOM   511  C  CD2 . LEU   A 1 62  ? -5.052  5.374   3.399   1.00 9.71  ? 60  LEU   A CD2 1 
ATOM   512  N  N   . ASN   A 1 63  ? -5.929  0.998   1.486   1.00 6.56  ? 61  ASN   A N   1 
ATOM   513  C  CA  . ASN   A 1 63  ? -4.926  0.069   1.981   1.00 6.72  ? 61  ASN   A CA  1 
ATOM   514  C  C   . ASN   A 1 63  ? -3.691  0.867   2.377   1.00 6.68  ? 61  ASN   A C   1 
ATOM   515  O  O   . ASN   A 1 63  ? -3.074  1.465   1.520   1.00 7.45  ? 61  ASN   A O   1 
ATOM   516  C  CB  . ASN   A 1 63  ? -4.617  -0.978  0.909   1.00 6.91  ? 61  ASN   A CB  1 
ATOM   517  C  CG  . ASN   A 1 63  ? -3.540  -1.962  1.301   1.00 6.93  ? 61  ASN   A CG  1 
ATOM   518  O  OD1 . ASN   A 1 63  ? -2.684  -1.685  2.147   1.00 7.11  ? 61  ASN   A OD1 1 
ATOM   519  N  ND2 . ASN   A 1 63  ? -3.573  -3.137  0.715   1.00 7.32  ? 61  ASN   A ND2 1 
ATOM   520  N  N   . ASN   A 1 64  ? -3.389  0.933   3.684   1.00 6.87  ? 62  ASN   A N   1 
ATOM   521  C  CA  . ASN   A 1 64  ? -2.288  1.764   4.125   1.00 7.76  ? 62  ASN   A CA  1 
ATOM   522  C  C   . ASN   A 1 64  ? -1.023  0.961   4.380   1.00 8.37  ? 62  ASN   A C   1 
ATOM   523  O  O   . ASN   A 1 64  ? -0.025  1.497   4.923   1.00 10.09 ? 62  ASN   A O   1 
ATOM   524  C  CB  . ASN   A 1 64  ? -2.664  2.598   5.347   1.00 8.23  ? 62  ASN   A CB  1 
ATOM   525  C  CG  . ASN   A 1 64  ? -3.041  1.711   6.513   1.00 8.65  ? 62  ASN   A CG  1 
ATOM   526  O  OD1 . ASN   A 1 64  ? -2.622  0.541   6.592   1.00 8.97  ? 62  ASN   A OD1 1 
ATOM   527  N  ND2 . ASN   A 1 64  ? -3.845  2.224   7.436   1.00 10.43 ? 62  ASN   A ND2 1 
ATOM   528  N  N   . GLY   A 1 65  ? -0.975  -0.304  3.927   1.00 7.94  ? 63  GLY   A N   1 
ATOM   529  C  CA  . GLY   A 1 65  ? 0.202   -1.121  4.112   1.00 8.56  ? 63  GLY   A CA  1 
ATOM   530  C  C   . GLY   A 1 65  ? 0.243   -1.874  5.432   1.00 8.60  ? 63  GLY   A C   1 
ATOM   531  O  O   . GLY   A 1 65  ? 1.114   -2.721  5.606   1.00 9.63  ? 63  GLY   A O   1 
ATOM   532  N  N   A HIS   A 1 66  ? -0.671  -1.576  6.359   0.50 8.34  ? 64  HIS   A N   1 
ATOM   533  N  N   B HIS   A 1 66  ? -0.735  -1.636  6.315   0.50 8.19  ? 64  HIS   A N   1 
ATOM   534  C  CA  A HIS   A 1 66  ? -0.796  -2.355  7.596   0.50 8.56  ? 64  HIS   A CA  1 
ATOM   535  C  CA  B HIS   A 1 66  ? -0.822  -2.274  7.641   0.50 8.28  ? 64  HIS   A CA  1 
ATOM   536  C  C   A HIS   A 1 66  ? -2.181  -2.983  7.723   0.50 7.99  ? 64  HIS   A C   1 
ATOM   537  C  C   B HIS   A 1 66  ? -2.208  -2.840  7.939   0.50 7.56  ? 64  HIS   A C   1 
ATOM   538  O  O   A HIS   A 1 66  ? -2.274  -4.179  8.037   0.50 8.23  ? 64  HIS   A O   1 
ATOM   539  O  O   B HIS   A 1 66  ? -2.360  -3.741  8.774   0.50 7.25  ? 64  HIS   A O   1 
ATOM   540  C  CB  A HIS   A 1 66  ? -0.309  -1.603  8.851   0.50 9.32  ? 64  HIS   A CB  1 
ATOM   541  C  CB  B HIS   A 1 66  ? -0.528  -1.275  8.775   0.50 9.04  ? 64  HIS   A CB  1 
ATOM   542  C  CG  A HIS   A 1 66  ? -0.693  -0.168  9.056   0.50 10.56 ? 64  HIS   A CG  1 
ATOM   543  C  CG  B HIS   A 1 66  ? 0.752   -0.538  8.573   0.50 10.41 ? 64  HIS   A CG  1 
ATOM   544  N  ND1 A HIS   A 1 66  ? 0.035   0.873   8.533   0.50 11.75 ? 64  HIS   A ND1 1 
ATOM   545  N  ND1 B HIS   A 1 66  ? 1.976   -1.160  8.683   0.50 11.70 ? 64  HIS   A ND1 1 
ATOM   546  C  CD2 A HIS   A 1 66  ? -1.639  0.424   9.839   0.50 11.13 ? 64  HIS   A CD2 1 
ATOM   547  C  CD2 B HIS   A 1 66  ? 1.007   0.730   8.266   0.50 11.36 ? 64  HIS   A CD2 1 
ATOM   548  C  CE1 A HIS   A 1 66  ? -0.533  2.034   8.894   0.50 11.91 ? 64  HIS   A CE1 1 
ATOM   549  C  CE1 B HIS   A 1 66  ? 2.949   -0.276  8.498   0.50 11.82 ? 64  HIS   A CE1 1 
ATOM   550  N  NE2 A HIS   A 1 66  ? -1.531  1.781   9.720   0.50 11.74 ? 64  HIS   A NE2 1 
ATOM   551  N  NE2 B HIS   A 1 66  ? 2.387   0.883   8.193   0.50 12.09 ? 64  HIS   A NE2 1 
ATOM   552  N  N   . ALA   A 1 67  ? -3.234  -2.238  7.351   1.00 7.43  ? 65  ALA   A N   1 
ATOM   553  C  CA  . ALA   A 1 67  ? -4.624  -2.696  7.372   1.00 7.11  ? 65  ALA   A CA  1 
ATOM   554  C  C   . ALA   A 1 67  ? -5.303  -1.938  6.232   1.00 6.76  ? 65  ALA   A C   1 
ATOM   555  O  O   . ALA   A 1 67  ? -4.648  -1.330  5.392   1.00 7.69  ? 65  ALA   A O   1 
ATOM   556  C  CB  . ALA   A 1 67  ? -5.267  -2.456  8.753   1.00 7.70  ? 65  ALA   A CB  1 
ATOM   557  N  N   . PHE   A 1 68  ? -6.619  -1.993  6.193   1.00 6.68  ? 66  PHE   A N   1 
ATOM   558  C  CA  . PHE   A 1 68  ? -7.398  -1.062  5.382   1.00 6.99  ? 66  PHE   A CA  1 
ATOM   559  C  C   . PHE   A 1 68  ? -8.295  -0.222  6.281   1.00 6.67  ? 66  PHE   A C   1 
ATOM   560  O  O   . PHE   A 1 68  ? -8.907  -0.710  7.224   1.00 7.07  ? 66  PHE   A O   1 
ATOM   561  C  CB  . PHE   A 1 68  ? -8.189  -1.747  4.265   1.00 7.38  ? 66  PHE   A CB  1 
ATOM   562  C  CG  . PHE   A 1 68  ? -9.250  -2.732  4.741   1.00 7.72  ? 66  PHE   A CG  1 
ATOM   563  C  CD1 . PHE   A 1 68  ? -10.504 -2.270  5.095   1.00 7.90  ? 66  PHE   A CD1 1 
ATOM   564  C  CD2 . PHE   A 1 68  ? -8.962  -4.061  4.880   1.00 8.18  ? 66  PHE   A CD2 1 
ATOM   565  C  CE1 . PHE   A 1 68  ? -11.456 -3.155  5.541   1.00 8.51  ? 66  PHE   A CE1 1 
ATOM   566  C  CE2 . PHE   A 1 68  ? -9.913  -4.945  5.346   1.00 8.75  ? 66  PHE   A CE2 1 
ATOM   567  C  CZ  . PHE   A 1 68  ? -11.167 -4.482  5.679   1.00 8.42  ? 66  PHE   A CZ  1 
ATOM   568  N  N   . ASN   A 1 69  ? -8.393  1.059   5.949   1.00 6.56  ? 67  ASN   A N   1 
ATOM   569  C  CA  . ASN   A 1 69  ? -9.248  1.984   6.671   1.00 6.60  ? 67  ASN   A CA  1 
ATOM   570  C  C   . ASN   A 1 69  ? -10.436 2.380   5.804   1.00 6.27  ? 67  ASN   A C   1 
ATOM   571  O  O   . ASN   A 1 69  ? -10.262 2.817   4.668   1.00 6.65  ? 67  ASN   A O   1 
ATOM   572  C  CB  . ASN   A 1 69  ? -8.517  3.255   7.050   1.00 7.82  ? 67  ASN   A CB  1 
ATOM   573  C  CG  . ASN   A 1 69  ? -7.408  3.123   8.060   1.00 8.73  ? 67  ASN   A CG  1 
ATOM   574  O  OD1 . ASN   A 1 69  ? -6.610  4.075   8.251   1.00 13.01 ? 67  ASN   A OD1 1 
ATOM   575  N  ND2 . ASN   A 1 69  ? -7.336  2.016   8.695   1.00 8.94  ? 67  ASN   A ND2 1 
ATOM   576  N  N   . VAL   A 1 70  ? -11.631 2.279   6.408   1.00 5.91  ? 68  VAL   A N   1 
ATOM   577  C  CA  . VAL   A 1 70  ? -12.829 2.909   5.862   1.00 6.19  ? 68  VAL   A CA  1 
ATOM   578  C  C   . VAL   A 1 70  ? -12.966 4.255   6.561   1.00 6.10  ? 68  VAL   A C   1 
ATOM   579  O  O   . VAL   A 1 70  ? -13.105 4.319   7.784   1.00 6.11  ? 68  VAL   A O   1 
ATOM   580  C  CB  . VAL   A 1 70  ? -14.084 2.035   6.019   1.00 6.72  ? 68  VAL   A CB  1 
ATOM   581  C  CG1 . VAL   A 1 70  ? -15.308 2.795   5.558   1.00 7.17  ? 68  VAL   A CG1 1 
ATOM   582  C  CG2 . VAL   A 1 70  ? -13.926 0.737   5.261   1.00 6.79  ? 68  VAL   A CG2 1 
ATOM   583  N  N   . GLU   A 1 71  ? -12.867 5.320   5.760   1.00 6.43  ? 69  GLU   A N   1 
ATOM   584  C  CA  . GLU   A 1 71  ? -12.767 6.680   6.250   1.00 6.87  ? 69  GLU   A CA  1 
ATOM   585  C  C   . GLU   A 1 71  ? -14.095 7.387   6.136   1.00 6.84  ? 69  GLU   A C   1 
ATOM   586  O  O   . GLU   A 1 71  ? -14.843 7.118   5.177   1.00 7.80  ? 69  GLU   A O   1 
ATOM   587  C  CB  . GLU   A 1 71  ? -11.774 7.444   5.396   1.00 7.62  ? 69  GLU   A CB  1 
ATOM   588  C  CG  . GLU   A 1 71  ? -10.367 6.867   5.454   1.00 8.68  ? 69  GLU   A CG  1 
ATOM   589  C  CD  . GLU   A 1 71  ? -9.510  7.379   4.304   1.00 10.55 ? 69  GLU   A CD  1 
ATOM   590  O  OE1 . GLU   A 1 71  ? -10.000 8.109   3.404   1.00 11.62 ? 69  GLU   A OE1 1 
ATOM   591  O  OE2 . GLU   A 1 71  ? -8.323  7.013   4.284   1.00 12.39 ? 69  GLU   A OE2 1 
ATOM   592  N  N   . PHE   A 1 72  ? -14.393 8.237   7.123   1.00 6.60  ? 70  PHE   A N   1 
ATOM   593  C  CA  . PHE   A 1 72  ? -15.628 8.981   7.209   1.00 7.02  ? 70  PHE   A CA  1 
ATOM   594  C  C   . PHE   A 1 72  ? -15.390 10.474  7.145   1.00 7.97  ? 70  PHE   A C   1 
ATOM   595  O  O   . PHE   A 1 72  ? -14.335 10.982  7.548   1.00 8.60  ? 70  PHE   A O   1 
ATOM   596  C  CB  . PHE   A 1 72  ? -16.370 8.658   8.512   1.00 6.68  ? 70  PHE   A CB  1 
ATOM   597  C  CG  . PHE   A 1 72  ? -16.906 7.247   8.502   1.00 6.35  ? 70  PHE   A CG  1 
ATOM   598  C  CD1 . PHE   A 1 72  ? -16.088 6.166   8.692   1.00 6.83  ? 70  PHE   A CD1 1 
ATOM   599  C  CD2 . PHE   A 1 72  ? -18.229 7.006   8.175   1.00 6.63  ? 70  PHE   A CD2 1 
ATOM   600  C  CE1 . PHE   A 1 72  ? -16.597 4.884   8.582   1.00 7.29  ? 70  PHE   A CE1 1 
ATOM   601  C  CE2 . PHE   A 1 72  ? -18.736 5.722   8.044   1.00 7.11  ? 70  PHE   A CE2 1 
ATOM   602  C  CZ  . PHE   A 1 72  ? -17.907 4.654   8.243   1.00 7.37  ? 70  PHE   A CZ  1 
ATOM   603  N  N   . ASP   A 1 73  ? -16.415 11.219  6.726   1.00 9.29  ? 71  ASP   A N   1 
ATOM   604  C  CA  . ASP   A 1 73  ? -16.424 12.665  6.870   1.00 10.30 ? 71  ASP   A CA  1 
ATOM   605  C  C   . ASP   A 1 73  ? -16.622 13.027  8.340   1.00 10.89 ? 71  ASP   A C   1 
ATOM   606  O  O   . ASP   A 1 73  ? -17.676 12.733  8.943   1.00 12.91 ? 71  ASP   A O   1 
ATOM   607  C  CB  . ASP   A 1 73  ? -17.534 13.295  6.067   1.00 11.83 ? 71  ASP   A CB  1 
ATOM   608  C  CG  . ASP   A 1 73  ? -17.705 14.787  6.261   1.00 13.45 ? 71  ASP   A CG  1 
ATOM   609  O  OD1 . ASP   A 1 73  ? -16.811 15.417  6.775   1.00 14.40 ? 71  ASP   A OD1 1 
ATOM   610  O  OD2 . ASP   A 1 73  ? -18.753 15.322  5.899   1.00 16.03 ? 71  ASP   A OD2 1 
ATOM   611  N  N   . ASP   A 1 74  ? -15.588 13.539  8.963   1.00 10.84 ? 72  ASP   A N   1 
ATOM   612  C  CA  . ASP   A 1 74  ? -15.621 13.938  10.361  1.00 11.68 ? 72  ASP   A CA  1 
ATOM   613  C  C   . ASP   A 1 74  ? -15.593 15.456  10.520  1.00 13.09 ? 72  ASP   A C   1 
ATOM   614  O  O   . ASP   A 1 74  ? -15.155 15.935  11.573  1.00 14.88 ? 72  ASP   A O   1 
ATOM   615  C  CB  . ASP   A 1 74  ? -14.511 13.259  11.151  1.00 11.41 ? 72  ASP   A CB  1 
ATOM   616  C  CG  . ASP   A 1 74  ? -13.120 13.698  10.751  1.00 11.32 ? 72  ASP   A CG  1 
ATOM   617  O  OD1 . ASP   A 1 74  ? -13.030 14.386  9.684   1.00 12.20 ? 72  ASP   A OD1 1 
ATOM   618  O  OD2 . ASP   A 1 74  ? -12.157 13.387  11.441  1.00 12.33 ? 72  ASP   A OD2 1 
ATOM   619  N  N   . SER   A 1 75  ? -16.055 16.189  9.499   1.00 12.91 ? 73  SER   A N   1 
ATOM   620  C  CA  . SER   A 1 75  ? -16.048 17.649  9.584   1.00 14.01 ? 73  SER   A CA  1 
ATOM   621  C  C   . SER   A 1 75  ? -17.323 18.229  10.200  1.00 14.44 ? 73  SER   A C   1 
ATOM   622  O  O   . SER   A 1 75  ? -17.461 19.443  10.305  1.00 14.56 ? 73  SER   A O   1 
ATOM   623  C  CB  . SER   A 1 75  ? -15.776 18.239  8.231   1.00 15.85 ? 73  SER   A CB  1 
ATOM   624  O  OG  . SER   A 1 75  ? -16.894 18.080  7.374   1.00 15.88 ? 73  SER   A OG  1 
ATOM   625  N  N   . GLN   A 1 76  ? -18.258 17.366  10.578  1.00 15.54 ? 74  GLN   A N   1 
ATOM   626  C  CA  . GLN   A 1 76  ? -19.432 17.717  11.368  1.00 16.56 ? 74  GLN   A CA  1 
ATOM   627  C  C   . GLN   A 1 76  ? -19.821 16.572  12.290  1.00 16.74 ? 74  GLN   A C   1 
ATOM   628  O  O   . GLN   A 1 76  ? -19.329 15.514  12.065  1.00 15.31 ? 74  GLN   A O   1 
ATOM   629  C  CB  . GLN   A 1 76  ? -20.611 17.888  10.437  1.00 18.85 ? 74  GLN   A CB  1 
ATOM   630  C  CG  . GLN   A 1 76  ? -20.531 19.132  9.583   1.00 20.55 ? 74  GLN   A CG  1 
ATOM   631  C  CD  . GLN   A 1 76  ? -21.831 19.289  8.850   1.00 21.49 ? 74  GLN   A CD  1 
ATOM   632  O  OE1 . GLN   A 1 76  ? -22.776 19.889  9.383   1.00 24.36 ? 74  GLN   A OE1 1 
ATOM   633  N  NE2 . GLN   A 1 76  ? -21.890 18.700  7.660   1.00 21.55 ? 74  GLN   A NE2 1 
ATOM   634  N  N   . ASP   A 1 77  ? -20.676 16.780  13.321  1.00 19.76 ? 75  ASP   A N   1 
ATOM   635  C  CA  . ASP   A 1 77  ? -21.144 15.710  14.183  1.00 20.80 ? 75  ASP   A CA  1 
ATOM   636  C  C   . ASP   A 1 77  ? -22.227 14.991  13.399  1.00 19.66 ? 75  ASP   A C   1 
ATOM   637  O  O   . ASP   A 1 77  ? -23.367 15.506  13.250  1.00 22.02 ? 75  ASP   A O   1 
ATOM   638  C  CB  . ASP   A 1 77  ? -21.725 16.157  15.512  1.00 22.37 ? 75  ASP   A CB  1 
ATOM   639  C  CG  . ASP   A 1 77  ? -20.707 16.509  16.587  1.00 23.18 ? 75  ASP   A CG  1 
ATOM   640  O  OD1 . ASP   A 1 77  ? -19.680 15.806  16.643  1.00 24.58 ? 75  ASP   A OD1 1 
ATOM   641  O  OD2 . ASP   A 1 77  ? -21.030 17.356  17.442  1.00 26.26 ? 75  ASP   A OD2 1 
ATOM   642  N  N   . LYS   A 1 78  ? -21.770 13.918  12.774  1.00 17.86 ? 76  LYS   A N   1 
ATOM   643  C  CA  . LYS   A 1 78  ? -22.582 13.019  11.947  1.00 18.27 ? 76  LYS   A CA  1 
ATOM   644  C  C   . LYS   A 1 78  ? -22.708 11.555  12.410  1.00 18.50 ? 76  LYS   A C   1 
ATOM   645  O  O   . LYS   A 1 78  ? -23.603 10.830  12.016  1.00 20.76 ? 76  LYS   A O   1 
ATOM   646  C  CB  . LYS   A 1 78  ? -21.920 12.879  10.571  1.00 19.82 ? 76  LYS   A CB  1 
ATOM   647  C  CG  . LYS   A 1 78  ? -22.113 14.088  9.670   1.00 21.35 ? 76  LYS   A CG  1 
ATOM   648  C  CD  . LYS   A 1 78  ? -21.572 13.881  8.254   1.00 22.89 ? 76  LYS   A CD  1 
ATOM   649  C  CE  . LYS   A 1 78  ? -21.972 14.934  7.252   1.00 24.61 ? 76  LYS   A CE  1 
ATOM   650  N  NZ  . LYS   A 1 78  ? -23.424 15.165  7.226   1.00 26.47 ? 76  LYS   A NZ  1 
ATOM   651  N  N   . ALA   A 1 79  ? -21.691 11.044  13.062  1.00 16.62 ? 77  ALA   A N   1 
ATOM   652  C  CA  . ALA   A 1 79  ? -21.543 9.677   13.563  1.00 14.24 ? 77  ALA   A CA  1 
ATOM   653  C  C   . ALA   A 1 79  ? -20.742 9.791   14.841  1.00 12.93 ? 77  ALA   A C   1 
ATOM   654  O  O   . ALA   A 1 79  ? -19.524 10.011  14.767  1.00 14.77 ? 77  ALA   A O   1 
ATOM   655  C  CB  . ALA   A 1 79  ? -20.789 8.860   12.539  1.00 14.86 ? 77  ALA   A CB  1 
ATOM   656  N  N   . VAL   A 1 80  ? -21.428 9.700   15.978  1.00 11.99 ? 78  VAL   A N   1 
ATOM   657  C  CA  . VAL   A 1 80  ? -20.791 10.009  17.227  1.00 12.16 ? 78  VAL   A CA  1 
ATOM   658  C  C   . VAL   A 1 80  ? -21.043 8.908   18.232  1.00 10.75 ? 78  VAL   A C   1 
ATOM   659  O  O   . VAL   A 1 80  ? -22.081 8.252   18.244  1.00 11.87 ? 78  VAL   A O   1 
ATOM   660  C  CB  . VAL   A 1 80  ? -21.202 11.358  17.782  1.00 14.34 ? 78  VAL   A CB  1 
ATOM   661  C  CG1 . VAL   A 1 80  ? -20.911 12.480  16.792  1.00 14.34 ? 78  VAL   A CG1 1 
ATOM   662  C  CG2 . VAL   A 1 80  ? -22.622 11.322  18.176  1.00 15.19 ? 78  VAL   A CG2 1 
ATOM   663  N  N   . LEU   A 1 81  ? -20.076 8.805   19.121  1.00 9.73  ? 79  LEU   A N   1 
ATOM   664  C  CA  . LEU   A 1 81  ? -20.083 7.952   20.288  1.00 9.39  ? 79  LEU   A CA  1 
ATOM   665  C  C   . LEU   A 1 81  ? -20.075 8.816   21.538  1.00 9.62  ? 79  LEU   A C   1 
ATOM   666  O  O   . LEU   A 1 81  ? -19.288 9.753   21.656  1.00 10.30 ? 79  LEU   A O   1 
ATOM   667  C  CB  . LEU   A 1 81  ? -18.847 7.065   20.178  1.00 9.99  ? 79  LEU   A CB  1 
ATOM   668  C  CG  . LEU   A 1 81  ? -18.683 5.988   21.238  1.00 10.45 ? 79  LEU   A CG  1 
ATOM   669  C  CD1 . LEU   A 1 81  ? -19.751 4.940   21.126  1.00 11.55 ? 79  LEU   A CD1 1 
ATOM   670  C  CD2 . LEU   A 1 81  ? -17.344 5.357   21.080  1.00 10.71 ? 79  LEU   A CD2 1 
ATOM   671  N  N   . LYS   A 1 82  ? -20.964 8.507   22.461  1.00 10.28 ? 80  LYS   A N   1 
ATOM   672  C  CA  . LYS   A 1 82  ? -21.017 9.204   23.737  1.00 11.30 ? 80  LYS   A CA  1 
ATOM   673  C  C   . LYS   A 1 82  ? -21.492 8.249   24.801  1.00 10.82 ? 80  LYS   A C   1 
ATOM   674  O  O   . LYS   A 1 82  ? -21.833 7.116   24.525  1.00 10.56 ? 80  LYS   A O   1 
ATOM   675  C  CB  . LYS   A 1 82  ? -21.846 10.470  23.712  1.00 14.23 ? 80  LYS   A CB  1 
ATOM   676  C  CG  . LYS   A 1 82  ? -23.220 10.333  23.394  1.00 16.16 ? 80  LYS   A CG  1 
ATOM   677  C  CD  . LYS   A 1 82  ? -23.812 11.710  23.076  1.00 18.93 ? 80  LYS   A CD  1 
ATOM   678  C  CE  . LYS   A 1 82  ? -23.193 12.263  21.868  1.00 21.57 ? 80  LYS   A CE  1 
ATOM   679  N  NZ  . LYS   A 1 82  ? -23.833 13.430  21.269  1.00 24.47 ? 80  LYS   A NZ  1 
ATOM   680  N  N   . GLY   A 1 83  ? -21.578 8.733   26.036  1.00 11.44 ? 81  GLY   A N   1 
ATOM   681  C  CA  . GLY   A 1 83  ? -22.039 7.896   27.103  1.00 11.16 ? 81  GLY   A CA  1 
ATOM   682  C  C   . GLY   A 1 83  ? -20.999 6.882   27.521  1.00 11.03 ? 81  GLY   A C   1 
ATOM   683  O  O   . GLY   A 1 83  ? -19.808 7.040   27.286  1.00 10.65 ? 81  GLY   A O   1 
ATOM   684  N  N   . GLY   A 1 84  ? -21.462 5.869   28.262  1.00 11.80 ? 82  GLY   A N   1 
ATOM   685  C  CA  . GLY   A 1 84  ? -20.529 4.917   28.824  1.00 12.54 ? 82  GLY   A CA  1 
ATOM   686  C  C   . GLY   A 1 84  ? -19.536 5.587   29.764  1.00 12.49 ? 82  GLY   A C   1 
ATOM   687  O  O   . GLY   A 1 84  ? -19.909 6.388   30.649  1.00 14.84 ? 82  GLY   A O   1 
ATOM   688  N  N   . PRO   A 1 85  ? -18.238 5.323   29.558  1.00 11.32 ? 83  PRO   A N   1 
ATOM   689  C  CA  . PRO   A 1 85  ? -17.222 5.970   30.355  1.00 12.13 ? 83  PRO   A CA  1 
ATOM   690  C  C   . PRO   A 1 85  ? -16.895 7.374   29.895  1.00 11.79 ? 83  PRO   A C   1 
ATOM   691  O  O   . PRO   A 1 85  ? -16.095 8.020   30.554  1.00 14.22 ? 83  PRO   A O   1 
ATOM   692  C  CB  . PRO   A 1 85  ? -16.030 5.052   30.182  1.00 12.01 ? 83  PRO   A CB  1 
ATOM   693  C  CG  . PRO   A 1 85  ? -16.180 4.556   28.750  1.00 11.39 ? 83  PRO   A CG  1 
ATOM   694  C  CD  . PRO   A 1 85  ? -17.670 4.404   28.550  1.00 11.56 ? 83  PRO   A CD  1 
ATOM   695  N  N   . LEU   A 1 86  ? -17.461 7.826   28.758  1.00 10.09 ? 84  LEU   A N   1 
ATOM   696  C  CA  . LEU   A 1 86  ? -16.979 9.006   28.052  1.00 9.83  ? 84  LEU   A CA  1 
ATOM   697  C  C   . LEU   A 1 86  ? -17.607 10.257  28.631  1.00 11.04 ? 84  LEU   A C   1 
ATOM   698  O  O   . LEU   A 1 86  ? -18.802 10.288  28.891  1.00 12.46 ? 84  LEU   A O   1 
ATOM   699  C  CB  . LEU   A 1 86  ? -17.265 8.899   26.560  1.00 8.83  ? 84  LEU   A CB  1 
ATOM   700  C  CG  . LEU   A 1 86  ? -16.714 7.646   25.917  1.00 8.57  ? 84  LEU   A CG  1 
ATOM   701  C  CD1 . LEU   A 1 86  ? -17.216 7.570   24.496  1.00 9.22  ? 84  LEU   A CD1 1 
ATOM   702  C  CD2 . LEU   A 1 86  ? -15.168 7.641   25.949  1.00 8.58  ? 84  LEU   A CD2 1 
ATOM   703  N  N   . ASP   A 1 87  ? -16.808 11.306  28.667  1.00 12.43 ? 85  ASP   A N   1 
ATOM   704  C  CA  . ASP   A 1 87  ? -17.256 12.656  28.946  1.00 14.52 ? 85  ASP   A CA  1 
ATOM   705  C  C   . ASP   A 1 87  ? -17.262 13.334  27.574  1.00 14.69 ? 85  ASP   A C   1 
ATOM   706  O  O   . ASP   A 1 87  ? -16.255 13.309  26.858  1.00 16.59 ? 85  ASP   A O   1 
ATOM   707  C  CB  . ASP   A 1 87  ? -16.327 13.302  29.988  1.00 17.20 ? 85  ASP   A CB  1 
ATOM   708  C  CG  . ASP   A 1 87  ? -16.449 12.779  31.427  1.00 20.62 ? 85  ASP   A CG  1 
ATOM   709  O  OD1 . ASP   A 1 87  ? -17.475 12.123  31.718  1.00 23.99 ? 85  ASP   A OD1 1 
ATOM   710  O  OD2 . ASP   A 1 87  ? -15.547 13.093  32.297  1.00 25.25 ? 85  ASP   A OD2 1 
ATOM   711  N  N   . GLY   A 1 88  ? -18.364 13.930  27.171  1.00 15.63 ? 86  GLY   A N   1 
ATOM   712  C  CA  . GLY   A 1 88  ? -18.417 14.633  25.912  1.00 14.43 ? 86  GLY   A CA  1 
ATOM   713  C  C   . GLY   A 1 88  ? -18.715 13.741  24.702  1.00 13.64 ? 86  GLY   A C   1 
ATOM   714  O  O   . GLY   A 1 88  ? -19.255 12.656  24.823  1.00 16.29 ? 86  GLY   A O   1 
ATOM   715  N  N   A THR   A 1 89  ? -18.353 14.225  23.532  0.50 11.74 ? 87  THR   A N   1 
ATOM   716  N  N   B THR   A 1 89  ? -18.400 14.280  23.502  0.50 11.70 ? 87  THR   A N   1 
ATOM   717  C  CA  A THR   A 1 89  ? -18.774 13.547  22.328  0.50 11.21 ? 87  THR   A CA  1 
ATOM   718  C  CA  B THR   A 1 89  ? -18.794 13.751  22.190  0.50 11.18 ? 87  THR   A CA  1 
ATOM   719  C  C   A THR   A 1 89  ? -17.545 13.273  21.496  0.50 9.84  ? 87  THR   A C   1 
ATOM   720  C  C   B THR   A 1 89  ? -17.561 13.321  21.412  0.50 9.84  ? 87  THR   A C   1 
ATOM   721  O  O   A THR   A 1 89  ? -16.597 14.078  21.457  0.50 9.61  ? 87  THR   A O   1 
ATOM   722  O  O   B THR   A 1 89  ? -16.650 14.132  21.187  0.50 9.77  ? 87  THR   A O   1 
ATOM   723  C  CB  A THR   A 1 89  ? -19.776 14.443  21.625  0.50 12.02 ? 87  THR   A CB  1 
ATOM   724  C  CB  B THR   A 1 89  ? -19.502 14.803  21.324  0.50 11.58 ? 87  THR   A CB  1 
ATOM   725  O  OG1 A THR   A 1 89  ? -19.153 15.714  21.520  0.50 12.69 ? 87  THR   A OG1 1 
ATOM   726  O  OG1 B THR   A 1 89  ? -20.635 15.294  22.027  0.50 12.50 ? 87  THR   A OG1 1 
ATOM   727  C  CG2 A THR   A 1 89  ? -21.024 14.613  22.458  0.50 12.08 ? 87  THR   A CG2 1 
ATOM   728  C  CG2 B THR   A 1 89  ? -19.922 14.210  19.984  0.50 12.08 ? 87  THR   A CG2 1 
ATOM   729  N  N   . TYR   A 1 90  ? -17.582 12.092  20.887  1.00 8.65  ? 88  TYR   A N   1 
ATOM   730  C  CA  . TYR   A 1 90  ? -16.481 11.590  20.100  1.00 8.28  ? 88  TYR   A CA  1 
ATOM   731  C  C   . TYR   A 1 90  ? -16.970 11.249  18.682  1.00 8.43  ? 88  TYR   A C   1 
ATOM   732  O  O   . TYR   A 1 90  ? -17.953 10.542  18.501  1.00 10.49 ? 88  TYR   A O   1 
ATOM   733  C  CB  . TYR   A 1 90  ? -15.878 10.351  20.748  1.00 8.02  ? 88  TYR   A CB  1 
ATOM   734  C  CG  . TYR   A 1 90  ? -15.121 10.598  22.042  1.00 7.37  ? 88  TYR   A CG  1 
ATOM   735  C  CD1 . TYR   A 1 90  ? -15.743 10.991  23.233  1.00 7.41  ? 88  TYR   A CD1 1 
ATOM   736  C  CD2 . TYR   A 1 90  ? -13.740 10.436  22.063  1.00 7.08  ? 88  TYR   A CD2 1 
ATOM   737  C  CE1 . TYR   A 1 90  ? -15.002 11.177  24.378  1.00 7.25  ? 88  TYR   A CE1 1 
ATOM   738  C  CE2 . TYR   A 1 90  ? -12.993 10.588  23.209  1.00 7.01  ? 88  TYR   A CE2 1 
ATOM   739  C  CZ  . TYR   A 1 90  ? -13.633 10.943  24.372  1.00 7.28  ? 88  TYR   A CZ  1 
ATOM   740  O  OH  . TYR   A 1 90  ? -12.939 11.065  25.552  1.00 7.65  ? 88  TYR   A OH  1 
ATOM   741  N  N   . ARG   A 1 91  ? -16.277 11.773  17.668  1.00 7.35  ? 89  ARG   A N   1 
ATOM   742  C  CA  . ARG   A 1 91  ? -16.699 11.643  16.280  1.00 8.20  ? 89  ARG   A CA  1 
ATOM   743  C  C   . ARG   A 1 91  ? -15.947 10.527  15.575  1.00 7.00  ? 89  ARG   A C   1 
ATOM   744  O  O   . ARG   A 1 91  ? -14.719 10.482  15.640  1.00 6.92  ? 89  ARG   A O   1 
ATOM   745  C  CB  . ARG   A 1 91  ? -16.408 12.975  15.601  1.00 9.94  ? 89  ARG   A CB  1 
ATOM   746  C  CG  . ARG   A 1 91  ? -17.165 13.167  14.304  1.00 12.10 ? 89  ARG   A CG  1 
ATOM   747  C  CD  . ARG   A 1 91  ? -16.890 14.597  13.798  1.00 13.40 ? 89  ARG   A CD  1 
ATOM   748  N  NE  . ARG   A 1 91  ? -17.534 15.602  14.655  1.00 15.05 ? 89  ARG   A NE  1 
ATOM   749  C  CZ  . ARG   A 1 91  ? -17.357 16.922  14.507  1.00 15.57 ? 89  ARG   A CZ  1 
ATOM   750  N  NH1 . ARG   A 1 91  ? -16.573 17.447  13.590  1.00 16.27 ? 89  ARG   A NH1 1 
ATOM   751  N  NH2 . ARG   A 1 91  ? -18.031 17.804  15.198  1.00 16.29 ? 89  ARG   A NH2 1 
ATOM   752  N  N   . LEU   A 1 92  ? -16.690 9.729   14.801  1.00 6.89  ? 90  LEU   A N   1 
ATOM   753  C  CA  . LEU   A 1 92  ? -16.109 8.651   14.032  1.00 6.94  ? 90  LEU   A CA  1 
ATOM   754  C  C   . LEU   A 1 92  ? -15.284 9.213   12.886  1.00 6.71  ? 90  LEU   A C   1 
ATOM   755  O  O   . LEU   A 1 92  ? -15.771 10.017  12.094  1.00 7.71  ? 90  LEU   A O   1 
ATOM   756  C  CB  . LEU   A 1 92  ? -17.234 7.796   13.459  1.00 7.17  ? 90  LEU   A CB  1 
ATOM   757  C  CG  . LEU   A 1 92  ? -16.796 6.594   12.616  1.00 7.60  ? 90  LEU   A CG  1 
ATOM   758  C  CD1 . LEU   A 1 92  ? -16.013 5.535   13.408  1.00 7.77  ? 90  LEU   A CD1 1 
ATOM   759  C  CD2 . LEU   A 1 92  ? -18.019 5.989   11.933  1.00 8.27  ? 90  LEU   A CD2 1 
ATOM   760  N  N   . ILE   A 1 93  ? -14.029 8.748   12.808  1.00 6.35  ? 91  ILE   A N   1 
ATOM   761  C  CA  . ILE   A 1 93  ? -13.131 9.132   11.734  1.00 6.19  ? 91  ILE   A CA  1 
ATOM   762  C  C   . ILE   A 1 93  ? -12.866 7.970   10.782  1.00 5.69  ? 91  ILE   A C   1 
ATOM   763  O  O   . ILE   A 1 93  ? -12.774 8.142   9.576   1.00 5.73  ? 91  ILE   A O   1 
ATOM   764  C  CB  . ILE   A 1 93  ? -11.827 9.776   12.241  1.00 6.90  ? 91  ILE   A CB  1 
ATOM   765  C  CG1 . ILE   A 1 93  ? -10.889 10.150  11.096  1.00 7.88  ? 91  ILE   A CG1 1 
ATOM   766  C  CG2 . ILE   A 1 93  ? -11.131 8.945   13.278  1.00 6.90  ? 91  ILE   A CG2 1 
ATOM   767  C  CD1 . ILE   A 1 93  ? -9.742  11.049  11.510  1.00 8.65  ? 91  ILE   A CD1 1 
ATOM   768  N  N   . GLN   A 1 94  ? -12.712 6.746   11.288  1.00 5.67  ? 92  GLN   A N   1 
ATOM   769  C  CA  . GLN   A 1 94  ? -12.377 5.615   10.438  1.00 5.56  ? 92  GLN   A CA  1 
ATOM   770  C  C   . GLN   A 1 94  ? -12.627 4.344   11.223  1.00 5.34  ? 92  GLN   A C   1 
ATOM   771  O  O   . GLN   A 1 94  ? -12.675 4.348   12.449  1.00 5.58  ? 92  GLN   A O   1 
ATOM   772  C  CB  . GLN   A 1 94  ? -10.937 5.623   9.926   1.00 6.23  ? 92  GLN   A CB  1 
ATOM   773  C  CG  . GLN   A 1 94  ? -9.898  5.728   11.029  1.00 6.84  ? 92  GLN   A CG  1 
ATOM   774  C  CD  . GLN   A 1 94  ? -9.131  4.475   11.267  1.00 7.31  ? 92  GLN   A CD  1 
ATOM   775  O  OE1 . GLN   A 1 94  ? -9.673  3.359   11.285  1.00 7.52  ? 92  GLN   A OE1 1 
ATOM   776  N  NE2 . GLN   A 1 94  ? -7.884  4.646   11.626  1.00 9.71  ? 92  GLN   A NE2 1 
ATOM   777  N  N   . PHE   A 1 95  ? -12.830 3.242   10.488  1.00 5.10  ? 93  PHE   A N   1 
ATOM   778  C  CA  . PHE   A 1 95  ? -12.694 1.933   11.090  1.00 4.90  ? 93  PHE   A CA  1 
ATOM   779  C  C   . PHE   A 1 95  ? -11.727 1.087   10.281  1.00 4.76  ? 93  PHE   A C   1 
ATOM   780  O  O   . PHE   A 1 95  ? -11.507 1.274   9.080   1.00 5.22  ? 93  PHE   A O   1 
ATOM   781  C  CB  . PHE   A 1 95  ? -14.023 1.218   11.323  1.00 5.16  ? 93  PHE   A CB  1 
ATOM   782  C  CG  . PHE   A 1 95  ? -14.788 0.743   10.104  1.00 5.46  ? 93  PHE   A CG  1 
ATOM   783  C  CD1 . PHE   A 1 95  ? -14.398 -0.408  9.412   1.00 5.88  ? 93  PHE   A CD1 1 
ATOM   784  C  CD2 . PHE   A 1 95  ? -15.908 1.428   9.661   1.00 5.67  ? 93  PHE   A CD2 1 
ATOM   785  C  CE1 . PHE   A 1 95  ? -15.098 -0.835  8.307   1.00 6.00  ? 93  PHE   A CE1 1 
ATOM   786  C  CE2 . PHE   A 1 95  ? -16.609 0.980   8.561   1.00 5.94  ? 93  PHE   A CE2 1 
ATOM   787  C  CZ  . PHE   A 1 95  ? -16.194 -0.123  7.858   1.00 5.94  ? 93  PHE   A CZ  1 
ATOM   788  N  N   . HIS   A 1 96  ? -11.193 0.059   10.968  1.00 4.74  ? 94  HIS   A N   1 
ATOM   789  C  CA  . HIS   A 1 96  ? -10.298 -0.914  10.364  1.00 4.50  ? 94  HIS   A CA  1 
ATOM   790  C  C   . HIS   A 1 96  ? -10.371 -2.182  11.175  1.00 4.32  ? 94  HIS   A C   1 
ATOM   791  O  O   . HIS   A 1 96  ? -10.959 -2.219  12.241  1.00 4.79  ? 94  HIS   A O   1 
ATOM   792  C  CB  . HIS   A 1 96  ? -8.864  -0.380  10.302  1.00 4.84  ? 94  HIS   A CB  1 
ATOM   793  C  CG  . HIS   A 1 96  ? -8.307  -0.083  11.650  1.00 4.81  ? 94  HIS   A CG  1 
ATOM   794  N  ND1 . HIS   A 1 96  ? -8.440  1.117   12.309  1.00 5.11  ? 94  HIS   A ND1 1 
ATOM   795  C  CD2 . HIS   A 1 96  ? -7.654  -0.892  12.523  1.00 4.83  ? 94  HIS   A CD2 1 
ATOM   796  C  CE1 . HIS   A 1 96  ? -7.908  0.994   13.517  1.00 4.99  ? 94  HIS   A CE1 1 
ATOM   797  N  NE2 . HIS   A 1 96  ? -7.424  -0.225  13.685  1.00 4.68  ? 94  HIS   A NE2 1 
ATOM   798  N  N   . PHE   A 1 97  ? -9.679  -3.209  10.694  1.00 4.44  ? 95  PHE   A N   1 
ATOM   799  C  CA  . PHE   A 1 97  ? -9.639  -4.523  11.353  1.00 4.79  ? 95  PHE   A CA  1 
ATOM   800  C  C   . PHE   A 1 97  ? -8.188  -4.946  11.533  1.00 4.85  ? 95  PHE   A C   1 
ATOM   801  O  O   . PHE   A 1 97  ? -7.263  -4.481  10.855  1.00 5.40  ? 95  PHE   A O   1 
ATOM   802  C  CB  . PHE   A 1 97  ? -10.339 -5.599  10.511  1.00 5.16  ? 95  PHE   A CB  1 
ATOM   803  C  CG  . PHE   A 1 97  ? -11.785 -5.299  10.187  1.00 5.43  ? 95  PHE   A CG  1 
ATOM   804  C  CD1 . PHE   A 1 97  ? -12.131 -4.460  9.147   1.00 5.82  ? 95  PHE   A CD1 1 
ATOM   805  C  CD2 . PHE   A 1 97  ? -12.825 -5.960  10.858  1.00 5.64  ? 95  PHE   A CD2 1 
ATOM   806  C  CE1 . PHE   A 1 97  ? -13.461 -4.266  8.782   1.00 6.07  ? 95  PHE   A CE1 1 
ATOM   807  C  CE2 . PHE   A 1 97  ? -14.138 -5.737  10.506  1.00 6.17  ? 95  PHE   A CE2 1 
ATOM   808  C  CZ  . PHE   A 1 97  ? -14.433 -4.884  9.484   1.00 6.19  ? 95  PHE   A CZ  1 
ATOM   809  N  N   . HIS   A 1 98  ? -8.026  -5.926  12.461  1.00 4.66  ? 96  HIS   A N   1 
ATOM   810  C  CA  . HIS   A 1 98  ? -6.831  -6.725  12.601  1.00 4.77  ? 96  HIS   A CA  1 
ATOM   811  C  C   . HIS   A 1 98  ? -7.261  -8.175  12.491  1.00 4.90  ? 96  HIS   A C   1 
ATOM   812  O  O   . HIS   A 1 98  ? -8.321  -8.539  12.988  1.00 5.02  ? 96  HIS   A O   1 
ATOM   813  C  CB  . HIS   A 1 98  ? -6.166  -6.482  13.964  1.00 5.11  ? 96  HIS   A CB  1 
ATOM   814  C  CG  . HIS   A 1 98  ? -5.891  -5.059  14.264  1.00 5.12  ? 96  HIS   A CG  1 
ATOM   815  N  ND1 . HIS   A 1 98  ? -4.674  -4.465  14.017  1.00 5.72  ? 96  HIS   A ND1 1 
ATOM   816  C  CD2 . HIS   A 1 98  ? -6.681  -4.026  14.694  1.00 5.31  ? 96  HIS   A CD2 1 
ATOM   817  C  CE1 . HIS   A 1 98  ? -4.746  -3.178  14.331  1.00 5.42  ? 96  HIS   A CE1 1 
ATOM   818  N  NE2 . HIS   A 1 98  ? -5.963  -2.854  14.734  1.00 5.07  ? 96  HIS   A NE2 1 
ATOM   819  N  N   . TRP   A 1 99  ? -6.488  -9.010  11.804  1.00 4.82  ? 97  TRP   A N   1 
ATOM   820  C  CA  . TRP   A 1 99  ? -6.887  -10.381 11.591  1.00 5.22  ? 97  TRP   A CA  1 
ATOM   821  C  C   . TRP   A 1 99  ? -5.686  -11.304 11.446  1.00 5.16  ? 97  TRP   A C   1 
ATOM   822  O  O   . TRP   A 1 99  ? -4.542  -10.881 11.329  1.00 5.49  ? 97  TRP   A O   1 
ATOM   823  C  CB  . TRP   A 1 99  ? -7.784  -10.500 10.342  1.00 5.21  ? 97  TRP   A CB  1 
ATOM   824  C  CG  . TRP   A 1 99  ? -7.142  -10.094 9.051   1.00 5.33  ? 97  TRP   A CG  1 
ATOM   825  C  CD1 . TRP   A 1 99  ? -6.464  -10.878 8.181   1.00 5.75  ? 97  TRP   A CD1 1 
ATOM   826  C  CD2 . TRP   A 1 99  ? -7.072  -8.771  8.504   1.00 5.22  ? 97  TRP   A CD2 1 
ATOM   827  N  NE1 . TRP   A 1 99  ? -6.033  -10.170 7.120   1.00 5.64  ? 97  TRP   A NE1 1 
ATOM   828  C  CE2 . TRP   A 1 99  ? -6.387  -8.854  7.285   1.00 5.26  ? 97  TRP   A CE2 1 
ATOM   829  C  CE3 . TRP   A 1 99  ? -7.540  -7.507  8.900   1.00 5.12  ? 97  TRP   A CE3 1 
ATOM   830  C  CZ2 . TRP   A 1 99  ? -6.177  -7.756  6.465   1.00 5.58  ? 97  TRP   A CZ2 1 
ATOM   831  C  CZ3 . TRP   A 1 99  ? -7.326  -6.424  8.100   1.00 5.39  ? 97  TRP   A CZ3 1 
ATOM   832  C  CH2 . TRP   A 1 99  ? -6.672  -6.531  6.875   1.00 5.48  ? 97  TRP   A CH2 1 
ATOM   833  N  N   . GLY   A 1 100 ? -5.976  -12.593 11.493  1.00 5.57  ? 98  GLY   A N   1 
ATOM   834  C  CA  . GLY   A 1 100 ? -4.942  -13.590 11.497  1.00 5.70  ? 98  GLY   A CA  1 
ATOM   835  C  C   . GLY   A 1 100 ? -4.753  -14.257 10.143  1.00 6.09  ? 98  GLY   A C   1 
ATOM   836  O  O   . GLY   A 1 100 ? -5.550  -14.112 9.229   1.00 6.85  ? 98  GLY   A O   1 
ATOM   837  N  N   . SER   A 1 101 ? -3.718  -15.111 10.101  1.00 6.63  ? 99  SER   A N   1 
ATOM   838  C  CA  . SER   A 1 101 ? -3.533  -16.035 8.973   1.00 7.67  ? 99  SER   A CA  1 
ATOM   839  C  C   . SER   A 1 101 ? -4.370  -17.302 9.136   1.00 8.50  ? 99  SER   A C   1 
ATOM   840  O  O   . SER   A 1 101 ? -4.477  -18.064 8.168   1.00 9.69  ? 99  SER   A O   1 
ATOM   841  C  CB  . SER   A 1 101 ? -2.097  -16.387 8.861   1.00 8.25  ? 99  SER   A CB  1 
ATOM   842  O  OG  . SER   A 1 101 ? -1.571  -16.911 10.055  1.00 8.69  ? 99  SER   A OG  1 
ATOM   843  N  N   . LEU   A 1 102 ? -4.919  -17.538 10.338  1.00 8.79  ? 100 LEU   A N   1 
ATOM   844  C  CA  . LEU   A 1 102 ? -5.604  -18.747 10.774  1.00 9.69  ? 100 LEU   A CA  1 
ATOM   845  C  C   . LEU   A 1 102 ? -6.746  -18.300 11.635  1.00 9.24  ? 100 LEU   A C   1 
ATOM   846  O  O   . LEU   A 1 102 ? -6.602  -17.307 12.318  1.00 8.66  ? 100 LEU   A O   1 
ATOM   847  C  CB  . LEU   A 1 102 ? -4.631  -19.611 11.630  1.00 11.76 ? 100 LEU   A CB  1 
ATOM   848  C  CG  . LEU   A 1 102 ? -3.308  -19.945 10.954  1.00 12.61 ? 100 LEU   A CG  1 
ATOM   849  C  CD1 . LEU   A 1 102 ? -2.197  -20.412 11.924  1.00 13.69 ? 100 LEU   A CD1 1 
ATOM   850  C  CD2 . LEU   A 1 102 ? -3.538  -21.026 9.911   1.00 14.13 ? 100 LEU   A CD2 1 
ATOM   851  N  N   . ASP   A 1 103 ? -7.827  -19.053 11.664  1.00 8.69  ? 101 ASP   A N   1 
ATOM   852  C  CA  . ASP   A 1 103 ? -9.001  -18.640 12.426  1.00 8.98  ? 101 ASP   A CA  1 
ATOM   853  C  C   . ASP   A 1 103 ? -8.710  -18.594 13.929  1.00 9.11  ? 101 ASP   A C   1 
ATOM   854  O  O   . ASP   A 1 103 ? -9.377  -17.861 14.626  1.00 10.28 ? 101 ASP   A O   1 
ATOM   855  C  CB  . ASP   A 1 103 ? -10.168 -19.578 12.179  1.00 9.73  ? 101 ASP   A CB  1 
ATOM   856  C  CG  . ASP   A 1 103 ? -10.737 -19.565 10.769  1.00 10.94 ? 101 ASP   A CG  1 
ATOM   857  O  OD1 . ASP   A 1 103 ? -10.395 -18.712 9.931   1.00 11.59 ? 101 ASP   A OD1 1 
ATOM   858  O  OD2 . ASP   A 1 103 ? -11.584 -20.410 10.500  1.00 13.61 ? 101 ASP   A OD2 1 
ATOM   859  N  N   . GLY   A 1 104 ? -7.690  -19.334 14.393  1.00 9.14  ? 102 GLY   A N   1 
ATOM   860  C  CA  . GLY   A 1 104 ? -7.339  -19.403 15.800  1.00 9.62  ? 102 GLY   A CA  1 
ATOM   861  C  C   . GLY   A 1 104 ? -6.593  -18.191 16.347  1.00 8.82  ? 102 GLY   A C   1 
ATOM   862  O  O   . GLY   A 1 104 ? -6.320  -18.178 17.538  1.00 9.53  ? 102 GLY   A O   1 
ATOM   863  N  N   . GLN   A 1 105 ? -6.346  -17.162 15.540  1.00 7.90  ? 103 GLN   A N   1 
ATOM   864  C  CA  . GLN   A 1 105 ? -5.681  -15.974 16.013  1.00 7.24  ? 103 GLN   A CA  1 
ATOM   865  C  C   . GLN   A 1 105 ? -6.107  -14.794 15.132  1.00 6.39  ? 103 GLN   A C   1 
ATOM   866  O  O   . GLN   A 1 105 ? -6.675  -14.984 14.080  1.00 7.22  ? 103 GLN   A O   1 
ATOM   867  C  CB  . GLN   A 1 105 ? -4.161  -16.149 15.989  1.00 7.48  ? 103 GLN   A CB  1 
ATOM   868  C  CG  . GLN   A 1 105 ? -3.608  -16.337 14.593  1.00 8.19  ? 103 GLN   A CG  1 
ATOM   869  C  CD  . GLN   A 1 105 ? -2.238  -16.933 14.570  1.00 9.22  ? 103 GLN   A CD  1 
ATOM   870  O  OE1 . GLN   A 1 105 ? -1.966  -17.926 15.263  1.00 12.38 ? 103 GLN   A OE1 1 
ATOM   871  N  NE2 . GLN   A 1 105 ? -1.358  -16.448 13.732  1.00 9.35  ? 103 GLN   A NE2 1 
ATOM   872  N  N   . GLY   A 1 106 ? -5.794  -13.581 15.595  1.00 5.91  ? 104 GLY   A N   1 
ATOM   873  C  CA  . GLY   A 1 106 ? -6.089  -12.389 14.840  1.00 5.74  ? 104 GLY   A CA  1 
ATOM   874  C  C   . GLY   A 1 106 ? -6.527  -11.208 15.668  1.00 5.41  ? 104 GLY   A C   1 
ATOM   875  O  O   . GLY   A 1 106 ? -6.266  -10.077 15.278  1.00 6.16  ? 104 GLY   A O   1 
ATOM   876  N  N   . SER   A 1 107 ? -7.226  -11.453 16.789  1.00 5.07  ? 105 SER   A N   1 
ATOM   877  C  CA  . SER   A 1 107 ? -7.618  -10.347 17.624  1.00 5.06  ? 105 SER   A CA  1 
ATOM   878  C  C   . SER   A 1 107 ? -6.407  -9.801  18.377  1.00 4.96  ? 105 SER   A C   1 
ATOM   879  O  O   . SER   A 1 107 ? -5.375  -10.449 18.568  1.00 5.75  ? 105 SER   A O   1 
ATOM   880  C  CB  . SER   A 1 107 ? -8.747  -10.687 18.546  1.00 5.38  ? 105 SER   A CB  1 
ATOM   881  O  OG  . SER   A 1 107 ? -8.380  -11.630 19.548  1.00 5.82  ? 105 SER   A OG  1 
ATOM   882  N  N   . GLU   A 1 108 ? -6.562  -8.537  18.804  1.00 5.09  ? 106 GLU   A N   1 
ATOM   883  C  CA  . GLU   A 1 108 ? -5.537  -7.837  19.590  1.00 4.87  ? 106 GLU   A CA  1 
ATOM   884  C  C   . GLU   A 1 108 ? -5.871  -8.001  21.076  1.00 4.74  ? 106 GLU   A C   1 
ATOM   885  O  O   . GLU   A 1 108 ? -5.102  -8.581  21.847  1.00 5.42  ? 106 GLU   A O   1 
ATOM   886  C  CB  . GLU   A 1 108 ? -5.486  -6.376  19.163  1.00 4.99  ? 106 GLU   A CB  1 
ATOM   887  C  CG  . GLU   A 1 108 ? -4.967  -6.238  17.761  1.00 5.39  ? 106 GLU   A CG  1 
ATOM   888  C  CD  . GLU   A 1 108 ? -4.365  -4.941  17.418  1.00 5.09  ? 106 GLU   A CD  1 
ATOM   889  O  OE1 . GLU   A 1 108 ? -5.005  -3.909  17.678  1.00 5.26  ? 106 GLU   A OE1 1 
ATOM   890  O  OE2 . GLU   A 1 108 ? -3.227  -4.944  16.898  1.00 6.14  ? 106 GLU   A OE2 1 
ATOM   891  N  N   . HIS   A 1 109 ? -7.040  -7.523  21.485  1.00 4.86  ? 107 HIS   A N   1 
ATOM   892  C  CA  . HIS   A 1 109 ? -7.522  -7.915  22.796  1.00 4.95  ? 107 HIS   A CA  1 
ATOM   893  C  C   . HIS   A 1 109 ? -7.799  -9.416  22.815  1.00 5.51  ? 107 HIS   A C   1 
ATOM   894  O  O   . HIS   A 1 109 ? -8.160  -10.012 21.809  1.00 5.51  ? 107 HIS   A O   1 
ATOM   895  C  CB  . HIS   A 1 109 ? -8.767  -7.108  23.171  1.00 4.99  ? 107 HIS   A CB  1 
ATOM   896  C  CG  . HIS   A 1 109 ? -8.477  -5.662  23.342  1.00 4.98  ? 107 HIS   A CG  1 
ATOM   897  N  ND1 . HIS   A 1 109 ? -8.528  -4.767  22.312  1.00 4.98  ? 107 HIS   A ND1 1 
ATOM   898  C  CD2 . HIS   A 1 109 ? -8.026  -4.966  24.412  1.00 5.03  ? 107 HIS   A CD2 1 
ATOM   899  C  CE1 . HIS   A 1 109 ? -8.095  -3.581  22.765  1.00 5.07  ? 107 HIS   A CE1 1 
ATOM   900  N  NE2 . HIS   A 1 109 ? -7.796  -3.657  24.034  1.00 5.07  ? 107 HIS   A NE2 1 
ATOM   901  N  N   . THR   A 1 110 ? -7.671  -9.976  24.020  1.00 5.54  ? 108 THR   A N   1 
ATOM   902  C  CA  . THR   A 1 110 ? -8.038  -11.371 24.294  1.00 5.74  ? 108 THR   A CA  1 
ATOM   903  C  C   . THR   A 1 110 ? -9.012  -11.380 25.472  1.00 5.88  ? 108 THR   A C   1 
ATOM   904  O  O   . THR   A 1 110 ? -9.035  -10.432 26.252  1.00 5.78  ? 108 THR   A O   1 
ATOM   905  C  CB  . THR   A 1 110 ? -6.805  -12.282 24.467  1.00 6.08  ? 108 THR   A CB  1 
ATOM   906  O  OG1 . THR   A 1 110 ? -5.990  -11.768 25.525  1.00 6.30  ? 108 THR   A OG1 1 
ATOM   907  C  CG2 . THR   A 1 110 ? -5.963  -12.310 23.205  1.00 6.42  ? 108 THR   A CG2 1 
ATOM   908  N  N   . VAL   A 1 111 ? -9.776  -12.476 25.560  1.00 6.17  ? 109 VAL   A N   1 
ATOM   909  C  CA  . VAL   A 1 111 ? -10.755 -12.591 26.618  1.00 6.79  ? 109 VAL   A CA  1 
ATOM   910  C  C   . VAL   A 1 111 ? -10.433 -13.867 27.366  1.00 7.08  ? 109 VAL   A C   1 
ATOM   911  O  O   . VAL   A 1 111 ? -10.555 -14.952 26.816  1.00 7.42  ? 109 VAL   A O   1 
ATOM   912  C  CB  . VAL   A 1 111 ? -12.185 -12.595 26.088  1.00 7.27  ? 109 VAL   A CB  1 
ATOM   913  C  CG1 . VAL   A 1 111 ? -13.200 -12.780 27.224  1.00 7.71  ? 109 VAL   A CG1 1 
ATOM   914  C  CG2 . VAL   A 1 111 ? -12.499 -11.321 25.323  1.00 7.68  ? 109 VAL   A CG2 1 
ATOM   915  N  N   . ASP   A 1 112 ? -9.949  -13.767 28.601  1.00 7.52  ? 110 ASP   A N   1 
ATOM   916  C  CA  . ASP   A 1 112 ? -9.474  -14.945 29.323  1.00 8.30  ? 110 ASP   A CA  1 
ATOM   917  C  C   . ASP   A 1 112 ? -8.483  -15.747 28.481  1.00 8.27  ? 110 ASP   A C   1 
ATOM   918  O  O   . ASP   A 1 112 ? -8.546  -16.965 28.423  1.00 8.87  ? 110 ASP   A O   1 
ATOM   919  C  CB  . ASP   A 1 112 ? -10.659 -15.768 29.791  1.00 9.39  ? 110 ASP   A CB  1 
ATOM   920  C  CG  . ASP   A 1 112 ? -11.527 -15.055 30.806  1.00 10.09 ? 110 ASP   A CG  1 
ATOM   921  O  OD1 . ASP   A 1 112 ? -10.977 -14.182 31.519  1.00 10.14 ? 110 ASP   A OD1 1 
ATOM   922  O  OD2 . ASP   A 1 112 ? -12.733 -15.426 30.862  1.00 11.91 ? 110 ASP   A OD2 1 
ATOM   923  N  N   . LYS   A 1 113 ? -7.613  -14.993 27.804  1.00 8.34  ? 111 LYS   A N   1 
ATOM   924  C  CA  . LYS   A 1 113 ? -6.528  -15.468 26.963  1.00 8.86  ? 111 LYS   A CA  1 
ATOM   925  C  C   . LYS   A 1 113 ? -7.034  -16.005 25.628  1.00 8.58  ? 111 LYS   A C   1 
ATOM   926  O  O   . LYS   A 1 113 ? -6.204  -16.342 24.769  1.00 9.72  ? 111 LYS   A O   1 
ATOM   927  C  CB  . LYS   A 1 113 ? -5.596  -16.488 27.640  1.00 9.90  ? 111 LYS   A CB  1 
ATOM   928  C  CG  . LYS   A 1 113 ? -4.887  -15.929 28.847  1.00 11.97 ? 111 LYS   A CG  1 
ATOM   929  C  CD  . LYS   A 1 113 ? -3.963  -14.770 28.554  1.00 14.11 ? 111 LYS   A CD  1 
ATOM   930  C  CE  . LYS   A 1 113 ? -3.230  -14.079 29.704  1.00 16.36 ? 111 LYS   A CE  1 
ATOM   931  N  NZ  . LYS   A 1 113 ? -2.104  -14.844 30.224  1.00 19.18 ? 111 LYS   A NZ  1 
ATOM   932  N  N   . LYS   A 1 114 ? -8.338  -16.018 25.357  1.00 8.33  ? 112 LYS   A N   1 
ATOM   933  C  CA  . LYS   A 1 114 ? -8.858  -16.457 24.070  1.00 9.04  ? 112 LYS   A CA  1 
ATOM   934  C  C   . LYS   A 1 114 ? -8.615  -15.394 22.994  1.00 7.51  ? 112 LYS   A C   1 
ATOM   935  O  O   . LYS   A 1 114 ? -8.969  -14.229 23.188  1.00 7.36  ? 112 LYS   A O   1 
ATOM   936  C  CB  . LYS   A 1 114 ? -10.389 -16.656 24.147  1.00 11.15 ? 112 LYS   A CB  1 
ATOM   937  C  CG  . LYS   A 1 114 ? -11.170 -16.948 22.793  1.00 13.21 ? 112 LYS   A CG  1 
ATOM   938  C  CD  . LYS   A 1 114 ? -12.708 -16.910 22.925  1.00 15.36 ? 112 LYS   A CD  1 
ATOM   939  C  CE  . LYS   A 1 114 ? -13.529 -17.079 21.718  1.00 16.49 ? 112 LYS   A CE  1 
ATOM   940  N  NZ  . LYS   A 1 114 ? -13.165 -18.342 21.170  1.00 16.68 ? 112 LYS   A NZ  1 
ATOM   941  N  N   . LYS   A 1 115 ? -8.062  -15.826 21.876  1.00 7.48  ? 113 LYS   A N   1 
ATOM   942  C  CA  . LYS   A 1 115 ? -7.920  -15.012 20.676  1.00 7.56  ? 113 LYS   A CA  1 
ATOM   943  C  C   . LYS   A 1 115 ? -9.062  -15.287 19.703  1.00 7.59  ? 113 LYS   A C   1 
ATOM   944  O  O   . LYS   A 1 115 ? -9.399  -16.441 19.412  1.00 8.70  ? 113 LYS   A O   1 
ATOM   945  C  CB  . LYS   A 1 115 ? -6.624  -15.374 19.954  1.00 8.04  ? 113 LYS   A CB  1 
ATOM   946  C  CG  . LYS   A 1 115 ? -5.381  -15.060 20.764  1.00 8.70  ? 113 LYS   A CG  1 
ATOM   947  C  CD  . LYS   A 1 115 ? -4.135  -15.595 20.057  1.00 9.90  ? 113 LYS   A CD  1 
ATOM   948  C  CE  . LYS   A 1 115 ? -2.893  -15.027 20.636  1.00 11.85 ? 113 LYS   A CE  1 
ATOM   949  N  NZ  . LYS   A 1 115 ? -2.473  -15.720 21.831  1.00 14.73 ? 113 LYS   A NZ  1 
ATOM   950  N  N   . TYR   A 1 116 ? -9.680  -14.212 19.250  1.00 6.77  ? 114 TYR   A N   1 
ATOM   951  C  CA  . TYR   A 1 116 ? -10.672 -14.279 18.181  1.00 6.45  ? 114 TYR   A CA  1 
ATOM   952  C  C   . TYR   A 1 116 ? -10.001 -14.240 16.802  1.00 6.21  ? 114 TYR   A C   1 
ATOM   953  O  O   . TYR   A 1 116 ? -8.814  -13.932 16.709  1.00 6.49  ? 114 TYR   A O   1 
ATOM   954  C  CB  . TYR   A 1 116 ? -11.724 -13.173 18.347  1.00 6.52  ? 114 TYR   A CB  1 
ATOM   955  C  CG  . TYR   A 1 116 ? -12.683 -13.397 19.484  1.00 6.95  ? 114 TYR   A CG  1 
ATOM   956  C  CD1 . TYR   A 1 116 ? -12.440 -12.979 20.793  1.00 8.33  ? 114 TYR   A CD1 1 
ATOM   957  C  CD2 . TYR   A 1 116 ? -13.895 -14.034 19.242  1.00 8.13  ? 114 TYR   A CD2 1 
ATOM   958  C  CE1 . TYR   A 1 116 ? -13.366 -13.184 21.799  1.00 9.34  ? 114 TYR   A CE1 1 
ATOM   959  C  CE2 . TYR   A 1 116 ? -14.820 -14.251 20.270  1.00 9.42  ? 114 TYR   A CE2 1 
ATOM   960  C  CZ  . TYR   A 1 116 ? -14.538 -13.825 21.536  1.00 10.44 ? 114 TYR   A CZ  1 
ATOM   961  O  OH  . TYR   A 1 116 ? -15.401 -13.973 22.588  1.00 13.74 ? 114 TYR   A OH  1 
ATOM   962  N  N   . ALA   A 1 117 ? -10.786 -14.532 15.739  1.00 6.20  ? 115 ALA   A N   1 
ATOM   963  C  CA  . ALA   A 1 117 ? -10.242 -14.542 14.396  1.00 5.94  ? 115 ALA   A CA  1 
ATOM   964  C  C   . ALA   A 1 117 ? -9.867  -13.154 13.914  1.00 5.66  ? 115 ALA   A C   1 
ATOM   965  O  O   . ALA   A 1 117 ? -9.036  -12.998 12.993  1.00 6.25  ? 115 ALA   A O   1 
ATOM   966  C  CB  . ALA   A 1 117 ? -11.257 -15.196 13.459  1.00 6.35  ? 115 ALA   A CB  1 
ATOM   967  N  N   . ALA   A 1 118 ? -10.519 -12.108 14.429  1.00 5.57  ? 116 ALA   A N   1 
ATOM   968  C  CA  . ALA   A 1 118 ? -10.263 -10.754 13.992  1.00 5.29  ? 116 ALA   A CA  1 
ATOM   969  C  C   . ALA   A 1 118 ? -10.863 -9.809  15.011  1.00 4.84  ? 116 ALA   A C   1 
ATOM   970  O  O   . ALA   A 1 118 ? -11.577 -10.214 15.941  1.00 5.06  ? 116 ALA   A O   1 
ATOM   971  C  CB  . ALA   A 1 118 ? -10.792 -10.520 12.588  1.00 5.22  ? 116 ALA   A CB  1 
ATOM   972  N  N   . GLU   A 1 119 ? -10.541 -8.516  14.856  1.00 4.82  ? 117 GLU   A N   1 
ATOM   973  C  CA  . GLU   A 1 119 ? -11.060 -7.481  15.733  1.00 4.91  ? 117 GLU   A CA  1 
ATOM   974  C  C   . GLU   A 1 119 ? -11.243 -6.205  14.903  1.00 4.94  ? 117 GLU   A C   1 
ATOM   975  O  O   . GLU   A 1 119 ? -10.352 -5.793  14.166  1.00 5.87  ? 117 GLU   A O   1 
ATOM   976  C  CB  . GLU   A 1 119 ? -10.063 -7.252  16.885  1.00 5.17  ? 117 GLU   A CB  1 
ATOM   977  C  CG  . GLU   A 1 119 ? -10.547 -6.265  17.948  1.00 5.52  ? 117 GLU   A CG  1 
ATOM   978  C  CD  . GLU   A 1 119 ? -9.623  -6.224  19.157  1.00 5.32  ? 117 GLU   A CD  1 
ATOM   979  O  OE1 . GLU   A 1 119 ? -8.985  -7.242  19.451  1.00 5.89  ? 117 GLU   A OE1 1 
ATOM   980  O  OE2 . GLU   A 1 119 ? -9.530  -5.118  19.759  1.00 5.76  ? 117 GLU   A OE2 1 
ATOM   981  N  N   . LEU   A 1 120 ? -12.419 -5.614  15.029  1.00 4.61  ? 118 LEU   A N   1 
ATOM   982  C  CA  . LEU   A 1 120 ? -12.815 -4.364  14.413  1.00 4.73  ? 118 LEU   A CA  1 
ATOM   983  C  C   . LEU   A 1 120 ? -12.594 -3.228  15.411  1.00 4.46  ? 118 LEU   A C   1 
ATOM   984  O  O   . LEU   A 1 120 ? -13.003 -3.303  16.565  1.00 4.52  ? 118 LEU   A O   1 
ATOM   985  C  CB  . LEU   A 1 120 ? -14.304 -4.464  14.044  1.00 5.26  ? 118 LEU   A CB  1 
ATOM   986  C  CG  . LEU   A 1 120 ? -15.052 -3.183  13.659  1.00 5.67  ? 118 LEU   A CG  1 
ATOM   987  C  CD1 . LEU   A 1 120 ? -14.472 -2.510  12.455  1.00 5.83  ? 118 LEU   A CD1 1 
ATOM   988  C  CD2 . LEU   A 1 120 ? -16.508 -3.543  13.412  1.00 6.29  ? 118 LEU   A CD2 1 
ATOM   989  N  N   . HIS   A 1 121 ? -11.966 -2.149  14.895  1.00 4.32  ? 119 HIS   A N   1 
ATOM   990  C  CA  . HIS   A 1 121 ? -11.746 -0.921  15.672  1.00 4.41  ? 119 HIS   A CA  1 
ATOM   991  C  C   . HIS   A 1 121 ? -12.459 0.233   14.974  1.00 4.33  ? 119 HIS   A C   1 
ATOM   992  O  O   . HIS   A 1 121 ? -12.070 0.601   13.857  1.00 4.96  ? 119 HIS   A O   1 
ATOM   993  C  CB  . HIS   A 1 121 ? -10.255 -0.614  15.739  1.00 4.56  ? 119 HIS   A CB  1 
ATOM   994  C  CG  . HIS   A 1 121 ? -9.511  -1.547  16.615  1.00 4.47  ? 119 HIS   A CG  1 
ATOM   995  N  ND1 . HIS   A 1 121 ? -8.140  -1.717  16.598  1.00 4.73  ? 119 HIS   A ND1 1 
ATOM   996  C  CD2 . HIS   A 1 121 ? -10.030 -2.415  17.531  1.00 4.80  ? 119 HIS   A CD2 1 
ATOM   997  C  CE1 . HIS   A 1 121 ? -7.868  -2.665  17.483  1.00 4.57  ? 119 HIS   A CE1 1 
ATOM   998  N  NE2 . HIS   A 1 121 ? -8.963  -3.110  18.075  1.00 4.98  ? 119 HIS   A NE2 1 
ATOM   999  N  N   . LEU   A 1 122 ? -13.468 0.806   15.635  1.00 4.54  ? 120 LEU   A N   1 
ATOM   1000 C  CA  . LEU   A 1 122 ? -14.145 2.030   15.203  1.00 4.82  ? 120 LEU   A CA  1 
ATOM   1001 C  C   . LEU   A 1 122 ? -13.537 3.176   16.010  1.00 4.49  ? 120 LEU   A C   1 
ATOM   1002 O  O   . LEU   A 1 122 ? -13.675 3.199   17.230  1.00 4.54  ? 120 LEU   A O   1 
ATOM   1003 C  CB  . LEU   A 1 122 ? -15.658 1.915   15.407  1.00 5.35  ? 120 LEU   A CB  1 
ATOM   1004 C  CG  . LEU   A 1 122 ? -16.346 0.859   14.526  1.00 6.19  ? 120 LEU   A CG  1 
ATOM   1005 C  CD1 . LEU   A 1 122 ? -17.232 -0.062  15.310  1.00 7.46  ? 120 LEU   A CD1 1 
ATOM   1006 C  CD2 . LEU   A 1 122 ? -17.155 1.518   13.441  1.00 7.05  ? 120 LEU   A CD2 1 
ATOM   1007 N  N   . VAL   A 1 123 ? -12.825 4.062   15.305  1.00 4.80  ? 121 VAL   A N   1 
ATOM   1008 C  CA  . VAL   A 1 123 ? -11.991 5.071   15.916  1.00 4.94  ? 121 VAL   A CA  1 
ATOM   1009 C  C   . VAL   A 1 123 ? -12.691 6.406   15.944  1.00 5.15  ? 121 VAL   A C   1 
ATOM   1010 O  O   . VAL   A 1 123 ? -13.163 6.883   14.886  1.00 5.57  ? 121 VAL   A O   1 
ATOM   1011 C  CB  . VAL   A 1 123 ? -10.666 5.195   15.138  1.00 5.39  ? 121 VAL   A CB  1 
ATOM   1012 C  CG1 . VAL   A 1 123 ? -9.760  6.236   15.762  1.00 5.69  ? 121 VAL   A CG1 1 
ATOM   1013 C  CG2 . VAL   A 1 123 ? -9.976  3.832   15.031  1.00 5.64  ? 121 VAL   A CG2 1 
ATOM   1014 N  N   . HIS   A 1 124 ? -12.783 7.007   17.119  1.00 5.10  ? 122 HIS   A N   1 
ATOM   1015 C  CA  . HIS   A 1 124 ? -13.487 8.268   17.304  1.00 5.23  ? 122 HIS   A CA  1 
ATOM   1016 C  C   . HIS   A 1 124 ? -12.594 9.258   18.055  1.00 5.53  ? 122 HIS   A C   1 
ATOM   1017 O  O   . HIS   A 1 124 ? -11.875 8.857   18.962  1.00 5.94  ? 122 HIS   A O   1 
ATOM   1018 C  CB  . HIS   A 1 124 ? -14.765 8.091   18.138  1.00 5.34  ? 122 HIS   A CB  1 
ATOM   1019 C  CG  . HIS   A 1 124 ? -15.665 6.969   17.735  1.00 5.62  ? 122 HIS   A CG  1 
ATOM   1020 N  ND1 . HIS   A 1 124 ? -15.316 5.657   17.966  1.00 5.62  ? 122 HIS   A ND1 1 
ATOM   1021 C  CD2 . HIS   A 1 124 ? -16.865 6.905   17.109  1.00 5.87  ? 122 HIS   A CD2 1 
ATOM   1022 C  CE1 . HIS   A 1 124 ? -16.327 4.895   17.526  1.00 5.75  ? 122 HIS   A CE1 1 
ATOM   1023 N  NE2 . HIS   A 1 124 ? -17.267 5.604   17.001  1.00 6.07  ? 122 HIS   A NE2 1 
ATOM   1024 N  N   . TRP   A 1 125 ? -12.695 10.554  17.746  1.00 5.61  ? 123 TRP   A N   1 
ATOM   1025 C  CA  . TRP   A 1 125 ? -11.904 11.584  18.436  1.00 5.91  ? 123 TRP   A CA  1 
ATOM   1026 C  C   . TRP   A 1 125 ? -12.806 12.565  19.155  1.00 5.97  ? 123 TRP   A C   1 
ATOM   1027 O  O   . TRP   A 1 125 ? -13.919 12.898  18.739  1.00 6.16  ? 123 TRP   A O   1 
ATOM   1028 C  CB  . TRP   A 1 125 ? -10.910 12.294  17.494  1.00 6.79  ? 123 TRP   A CB  1 
ATOM   1029 C  CG  . TRP   A 1 125 ? -11.553 12.925  16.299  1.00 7.42  ? 123 TRP   A CG  1 
ATOM   1030 C  CD1 . TRP   A 1 125 ? -11.748 12.342  15.092  1.00 7.78  ? 123 TRP   A CD1 1 
ATOM   1031 C  CD2 . TRP   A 1 125 ? -12.027 14.277  16.164  1.00 8.17  ? 123 TRP   A CD2 1 
ATOM   1032 N  NE1 . TRP   A 1 125 ? -12.339 13.208  14.229  1.00 8.14  ? 123 TRP   A NE1 1 
ATOM   1033 C  CE2 . TRP   A 1 125 ? -12.531 14.402  14.863  1.00 8.41  ? 123 TRP   A CE2 1 
ATOM   1034 C  CE3 . TRP   A 1 125 ? -12.093 15.393  17.021  1.00 8.74  ? 123 TRP   A CE3 1 
ATOM   1035 C  CZ2 . TRP   A 1 125 ? -13.068 15.584  14.380  1.00 9.38  ? 123 TRP   A CZ2 1 
ATOM   1036 C  CZ3 . TRP   A 1 125 ? -12.615 16.567  16.520  1.00 9.33  ? 123 TRP   A CZ3 1 
ATOM   1037 C  CH2 . TRP   A 1 125 ? -13.113 16.638  15.233  1.00 9.60  ? 123 TRP   A CH2 1 
ATOM   1038 N  N   . ASN   A 1 126 ? -12.275 13.035  20.308  1.00 6.33  ? 124 ASN   A N   1 
ATOM   1039 C  CA  . ASN   A 1 126 ? -12.997 13.923  21.225  1.00 6.73  ? 124 ASN   A CA  1 
ATOM   1040 C  C   . ASN   A 1 126 ? -13.127 15.297  20.587  1.00 6.81  ? 124 ASN   A C   1 
ATOM   1041 O  O   . ASN   A 1 126 ? -12.121 15.971  20.329  1.00 6.90  ? 124 ASN   A O   1 
ATOM   1042 C  CB  . ASN   A 1 126 ? -12.191 13.974  22.508  1.00 6.98  ? 124 ASN   A CB  1 
ATOM   1043 C  CG  . ASN   A 1 126 ? -12.942 14.621  23.623  1.00 7.41  ? 124 ASN   A CG  1 
ATOM   1044 O  OD1 . ASN   A 1 126 ? -13.782 15.507  23.418  1.00 8.05  ? 124 ASN   A OD1 1 
ATOM   1045 N  ND2 . ASN   A 1 126 ? -12.651 14.185  24.840  1.00 8.35  ? 124 ASN   A ND2 1 
ATOM   1046 N  N   . THR   A 1 127 ? -14.368 15.736  20.392  1.00 7.56  ? 125 THR   A N   1 
ATOM   1047 C  CA  . THR   A 1 127 ? -14.586 16.986  19.651  1.00 9.01  ? 125 THR   A CA  1 
ATOM   1048 C  C   . THR   A 1 127 ? -14.047 18.201  20.396  1.00 9.57  ? 125 THR   A C   1 
ATOM   1049 O  O   . THR   A 1 127 ? -13.812 19.221  19.725  1.00 10.80 ? 125 THR   A O   1 
ATOM   1050 C  CB  . THR   A 1 127 ? -16.065 17.120  19.246  1.00 10.44 ? 125 THR   A CB  1 
ATOM   1051 O  OG1 . THR   A 1 127 ? -16.869 17.217  20.408  1.00 12.46 ? 125 THR   A OG1 1 
ATOM   1052 C  CG2 . THR   A 1 127 ? -16.539 16.025  18.337  1.00 11.07 ? 125 THR   A CG2 1 
ATOM   1053 N  N   . LYS   A 1 128 ? -13.816 18.105  21.697  1.00 9.60  ? 127 LYS   A N   1 
ATOM   1054 C  CA  . LYS   A 1 128 ? -13.246 19.269  22.347  1.00 10.61 ? 127 LYS   A CA  1 
ATOM   1055 C  C   . LYS   A 1 128 ? -11.842 19.610  21.858  1.00 9.91  ? 127 LYS   A C   1 
ATOM   1056 O  O   . LYS   A 1 128 ? -11.390 20.730  22.119  1.00 11.53 ? 127 LYS   A O   1 
ATOM   1057 C  CB  . LYS   A 1 128 ? -13.333 19.056  23.837  1.00 12.15 ? 127 LYS   A CB  1 
ATOM   1058 C  CG  . LYS   A 1 128 ? -12.288 18.297  24.414  1.00 13.58 ? 127 LYS   A CG  1 
ATOM   1059 C  CD  . LYS   A 1 128 ? -12.800 18.014  25.818  1.00 16.65 ? 127 LYS   A CD  1 
ATOM   1060 C  CE  . LYS   A 1 128 ? -11.813 17.479  26.745  1.00 18.30 ? 127 LYS   A CE  1 
ATOM   1061 N  NZ  . LYS   A 1 128 ? -12.318 17.536  28.126  1.00 21.26 ? 127 LYS   A NZ  1 
ATOM   1062 N  N   . TYR   A 1 129 ? -11.169 18.703  21.149  1.00 9.18  ? 128 TYR   A N   1 
ATOM   1063 C  CA  . TYR   A 1 129 ? -9.808  18.955  20.684  1.00 9.26  ? 128 TYR   A CA  1 
ATOM   1064 C  C   . TYR   A 1 129 ? -9.721  19.367  19.217  1.00 9.02  ? 128 TYR   A C   1 
ATOM   1065 O  O   . TYR   A 1 129 ? -8.627  19.538  18.653  1.00 9.84  ? 128 TYR   A O   1 
ATOM   1066 C  CB  . TYR   A 1 129 ? -8.892  17.762  20.959  1.00 9.53  ? 128 TYR   A CB  1 
ATOM   1067 C  CG  . TYR   A 1 129 ? -8.833  17.483  22.432  1.00 9.59  ? 128 TYR   A CG  1 
ATOM   1068 C  CD1 . TYR   A 1 129 ? -8.428  18.439  23.354  1.00 10.33 ? 128 TYR   A CD1 1 
ATOM   1069 C  CD2 . TYR   A 1 129 ? -9.136  16.227  22.913  1.00 9.30  ? 128 TYR   A CD2 1 
ATOM   1070 C  CE1 . TYR   A 1 129 ? -8.409  18.177  24.714  1.00 10.57 ? 128 TYR   A CE1 1 
ATOM   1071 C  CE2 . TYR   A 1 129 ? -9.093  15.924  24.262  1.00 9.65  ? 128 TYR   A CE2 1 
ATOM   1072 C  CZ  . TYR   A 1 129 ? -8.726  16.909  25.173  1.00 10.39 ? 128 TYR   A CZ  1 
ATOM   1073 O  OH  . TYR   A 1 129 ? -8.689  16.663  26.495  1.00 12.10 ? 128 TYR   A OH  1 
ATOM   1074 N  N   . GLY   A 1 130 ? -10.868 19.499  18.554  1.00 8.95  ? 129 GLY   A N   1 
ATOM   1075 C  CA  . GLY   A 1 130 ? -10.888 20.168  17.236  1.00 9.41  ? 129 GLY   A CA  1 
ATOM   1076 C  C   . GLY   A 1 130 ? -10.607 19.278  16.015  1.00 9.08  ? 129 GLY   A C   1 
ATOM   1077 O  O   . GLY   A 1 130 ? -11.273 19.391  14.987  1.00 9.99  ? 129 GLY   A O   1 
ATOM   1078 N  N   . ASP   A 1 131 ? -9.609  18.400  16.089  1.00 9.20  ? 130 ASP   A N   1 
ATOM   1079 C  CA  . ASP   A 1 131 ? -9.410  17.398  15.072  1.00 9.71  ? 130 ASP   A CA  1 
ATOM   1080 C  C   . ASP   A 1 131 ? -8.608  16.234  15.632  1.00 8.75  ? 130 ASP   A C   1 
ATOM   1081 O  O   . ASP   A 1 131 ? -8.174  16.239  16.793  1.00 8.51  ? 130 ASP   A O   1 
ATOM   1082 C  CB  . ASP   A 1 131 ? -8.796  17.957  13.815  1.00 10.56 ? 130 ASP   A CB  1 
ATOM   1083 C  CG  . ASP   A 1 131 ? -7.423  18.507  13.970  1.00 10.81 ? 130 ASP   A CG  1 
ATOM   1084 O  OD1 . ASP   A 1 131 ? -6.732  18.158  14.936  1.00 13.12 ? 130 ASP   A OD1 1 
ATOM   1085 O  OD2 . ASP   A 1 131 ? -6.982  19.206  13.063  1.00 12.94 ? 130 ASP   A OD2 1 
ATOM   1086 N  N   . PHE   A 1 132 ? -8.444  15.204  14.806  1.00 9.03  ? 131 PHE   A N   1 
ATOM   1087 C  CA  . PHE   A 1 132 ? -7.821  13.957  15.234  1.00 8.29  ? 131 PHE   A CA  1 
ATOM   1088 C  C   . PHE   A 1 132 ? -6.365  14.177  15.659  1.00 7.97  ? 131 PHE   A C   1 
ATOM   1089 O  O   . PHE   A 1 132 ? -5.940  13.638  16.686  1.00 7.62  ? 131 PHE   A O   1 
ATOM   1090 C  CB  . PHE   A 1 132 ? -7.933  12.955  14.099  1.00 8.57  ? 131 PHE   A CB  1 
ATOM   1091 C  CG  . PHE   A 1 132 ? -7.193  11.665  14.353  1.00 8.76  ? 131 PHE   A CG  1 
ATOM   1092 C  CD1 . PHE   A 1 132 ? -7.838  10.616  15.014  1.00 8.82  ? 131 PHE   A CD1 1 
ATOM   1093 C  CD2 . PHE   A 1 132 ? -5.878  11.456  13.980  1.00 9.51  ? 131 PHE   A CD2 1 
ATOM   1094 C  CE1 . PHE   A 1 132 ? -7.189  9.406   15.236  1.00 9.70  ? 131 PHE   A CE1 1 
ATOM   1095 C  CE2 . PHE   A 1 132 ? -5.237  10.263  14.207  1.00 10.52 ? 131 PHE   A CE2 1 
ATOM   1096 C  CZ  . PHE   A 1 132 ? -5.894  9.247   14.827  1.00 10.36 ? 131 PHE   A CZ  1 
ATOM   1097 N  N   . GLY   A 1 133 ? -5.608  14.946  14.873  1.00 8.34  ? 132 GLY   A N   1 
ATOM   1098 C  CA  . GLY   A 1 133 ? -4.210  15.107  15.184  1.00 8.49  ? 132 GLY   A CA  1 
ATOM   1099 C  C   . GLY   A 1 133 ? -3.931  15.822  16.491  1.00 8.87  ? 132 GLY   A C   1 
ATOM   1100 O  O   . GLY   A 1 133 ? -2.957  15.505  17.174  1.00 9.54  ? 132 GLY   A O   1 
ATOM   1101 N  N   . LYS   A 1 134 ? -4.794  16.763  16.892  1.00 8.52  ? 133 LYS   A N   1 
ATOM   1102 C  CA  . LYS   A 1 134 ? -4.682  17.350  18.217  1.00 8.47  ? 133 LYS   A CA  1 
ATOM   1103 C  C   . LYS   A 1 134 ? -5.164  16.361  19.292  1.00 7.68  ? 133 LYS   A C   1 
ATOM   1104 O  O   . LYS   A 1 134 ? -4.597  16.281  20.385  1.00 7.59  ? 133 LYS   A O   1 
ATOM   1105 C  CB  . LYS   A 1 134 ? -5.475  18.648  18.307  1.00 9.63  ? 133 LYS   A CB  1 
ATOM   1106 C  CG  . LYS   A 1 134 ? -5.497  19.354  19.634  1.00 12.56 ? 133 LYS   A CG  1 
ATOM   1107 C  CD  . LYS   A 1 134 ? -4.118  19.763  20.100  1.00 14.50 ? 133 LYS   A CD  1 
ATOM   1108 C  CE  . LYS   A 1 134 ? -3.333  20.565  19.112  1.00 17.08 ? 133 LYS   A CE  1 
ATOM   1109 N  NZ  . LYS   A 1 134 ? -2.517  21.604  19.725  1.00 19.85 ? 133 LYS   A NZ  1 
ATOM   1110 N  N   . ALA   A 1 135 ? -6.259  15.643  19.028  1.00 7.39  ? 134 ALA   A N   1 
ATOM   1111 C  CA  . ALA   A 1 135 ? -6.829  14.705  19.982  1.00 7.12  ? 134 ALA   A CA  1 
ATOM   1112 C  C   . ALA   A 1 135 ? -5.835  13.641  20.407  1.00 7.18  ? 134 ALA   A C   1 
ATOM   1113 O  O   . ALA   A 1 135 ? -5.832  13.281  21.566  1.00 7.27  ? 134 ALA   A O   1 
ATOM   1114 C  CB  . ALA   A 1 135 ? -8.090  14.077  19.426  1.00 6.84  ? 134 ALA   A CB  1 
ATOM   1115 N  N   . VAL   A 1 136 ? -5.022  13.121  19.491  1.00 7.41  ? 135 VAL   A N   1 
ATOM   1116 C  CA  . VAL   A 1 136 ? -4.160  12.000  19.830  1.00 8.09  ? 135 VAL   A CA  1 
ATOM   1117 C  C   . VAL   A 1 136 ? -3.052  12.415  20.789  1.00 8.33  ? 135 VAL   A C   1 
ATOM   1118 O  O   . VAL   A 1 136 ? -2.360  11.557  21.320  1.00 8.86  ? 135 VAL   A O   1 
ATOM   1119 C  CB  . VAL   A 1 136 ? -3.547  11.253  18.646  1.00 8.86  ? 135 VAL   A CB  1 
ATOM   1120 C  CG1 . VAL   A 1 136 ? -4.634  10.619  17.840  1.00 9.80  ? 135 VAL   A CG1 1 
ATOM   1121 C  CG2 . VAL   A 1 136 ? -2.690  12.159  17.755  1.00 8.83  ? 135 VAL   A CG2 1 
ATOM   1122 N  N   . GLN   A 1 137 ? -2.856  13.716  20.978  1.00 7.98  ? 136 GLN   A N   1 
ATOM   1123 C  CA  . GLN   A 1 137 ? -1.873  14.207  21.941  1.00 8.98  ? 136 GLN   A CA  1 
ATOM   1124 C  C   . GLN   A 1 137 ? -2.455  14.406  23.342  1.00 8.69  ? 136 GLN   A C   1 
ATOM   1125 O  O   . GLN   A 1 137 ? -1.773  14.923  24.247  1.00 9.51  ? 136 GLN   A O   1 
ATOM   1126 C  CB  . GLN   A 1 137 ? -1.285  15.530  21.410  1.00 10.43 ? 136 GLN   A CB  1 
ATOM   1127 C  CG  . GLN   A 1 137 ? -0.507  15.344  20.099  1.00 12.52 ? 136 GLN   A CG  1 
ATOM   1128 C  CD  . GLN   A 1 137 ? 0.675   14.393  20.250  1.00 16.06 ? 136 GLN   A CD  1 
ATOM   1129 O  OE1 . GLN   A 1 137 ? 1.361   14.392  21.275  1.00 20.96 ? 136 GLN   A OE1 1 
ATOM   1130 N  NE2 . GLN   A 1 137 ? 1.037   13.602  19.248  1.00 18.23 ? 136 GLN   A NE2 1 
ATOM   1131 N  N   . GLN   A 1 138 ? -3.694  13.950  23.556  1.00 8.15  ? 137 GLN   A N   1 
ATOM   1132 C  CA  . GLN   A 1 138 ? -4.368  14.132  24.827  1.00 7.81  ? 137 GLN   A CA  1 
ATOM   1133 C  C   . GLN   A 1 138 ? -4.724  12.793  25.439  1.00 7.84  ? 137 GLN   A C   1 
ATOM   1134 O  O   . GLN   A 1 138 ? -5.061  11.838  24.700  1.00 7.12  ? 137 GLN   A O   1 
ATOM   1135 C  CB  . GLN   A 1 138 ? -5.687  14.888  24.672  1.00 8.16  ? 137 GLN   A CB  1 
ATOM   1136 C  CG  . GLN   A 1 138 ? -5.608  16.077  23.717  1.00 9.44  ? 137 GLN   A CG  1 
ATOM   1137 C  CD  . GLN   A 1 138 ? -4.501  17.013  24.071  1.00 11.04 ? 137 GLN   A CD  1 
ATOM   1138 O  OE1 . GLN   A 1 138 ? -4.213  17.276  25.245  1.00 11.58 ? 137 GLN   A OE1 1 
ATOM   1139 N  NE2 . GLN   A 1 138 ? -3.924  17.614  23.028  1.00 11.99 ? 137 GLN   A NE2 1 
ATOM   1140 N  N   A PRO   A 1 139 ? -4.697  12.663  26.782  0.50 7.95  ? 138 PRO   A N   1 
ATOM   1141 N  N   B PRO   A 1 139 ? -4.698  12.640  26.782  0.50 8.24  ? 138 PRO   A N   1 
ATOM   1142 C  CA  A PRO   A 1 139 ? -4.974  11.366  27.407  0.50 8.20  ? 138 PRO   A CA  1 
ATOM   1143 C  CA  B PRO   A 1 139 ? -5.009  11.338  27.393  0.50 8.54  ? 138 PRO   A CA  1 
ATOM   1144 C  C   A PRO   A 1 139 ? -6.410  10.865  27.303  0.50 8.16  ? 138 PRO   A C   1 
ATOM   1145 C  C   B PRO   A 1 139 ? -6.406  10.813  27.113  0.50 8.35  ? 138 PRO   A C   1 
ATOM   1146 O  O   A PRO   A 1 139 ? -6.664  9.703   27.600  0.50 8.61  ? 138 PRO   A O   1 
ATOM   1147 O  O   B PRO   A 1 139 ? -6.619  9.590   27.027  0.50 8.83  ? 138 PRO   A O   1 
ATOM   1148 C  CB  A PRO   A 1 139 ? -4.530  11.615  28.859  0.50 8.48  ? 138 PRO   A CB  1 
ATOM   1149 C  CB  B PRO   A 1 139 ? -4.831  11.584  28.871  0.50 9.04  ? 138 PRO   A CB  1 
ATOM   1150 C  CG  A PRO   A 1 139 ? -4.792  13.083  29.070  0.50 8.40  ? 138 PRO   A CG  1 
ATOM   1151 C  CG  B PRO   A 1 139 ? -3.806  12.692  28.929  0.50 9.22  ? 138 PRO   A CG  1 
ATOM   1152 C  CD  A PRO   A 1 139 ? -4.259  13.684  27.761  0.50 8.45  ? 138 PRO   A CD  1 
ATOM   1153 C  CD  B PRO   A 1 139 ? -4.177  13.613  27.765  0.50 8.97  ? 138 PRO   A CD  1 
ATOM   1154 N  N   . ASP   A 1 140 ? -7.353  11.762  26.952  1.00 8.10  ? 139 ASP   A N   1 
ATOM   1155 C  CA  . ASP   A 1 140 ? -8.728  11.406  26.650  1.00 7.98  ? 139 ASP   A CA  1 
ATOM   1156 C  C   . ASP   A 1 140 ? -9.082  11.836  25.240  1.00 6.92  ? 139 ASP   A C   1 
ATOM   1157 O  O   . ASP   A 1 140 ? -10.211 12.227  24.960  1.00 7.63  ? 139 ASP   A O   1 
ATOM   1158 C  CB  . ASP   A 1 140 ? -9.689  12.041  27.625  1.00 9.47  ? 139 ASP   A CB  1 
ATOM   1159 C  CG  . ASP   A 1 140 ? -9.606  13.540  27.674  1.00 10.21 ? 139 ASP   A CG  1 
ATOM   1160 O  OD1 . ASP   A 1 140 ? -8.690  14.136  27.052  1.00 10.67 ? 139 ASP   A OD1 1 
ATOM   1161 O  OD2 . ASP   A 1 140 ? -10.494 14.124  28.360  1.00 12.63 ? 139 ASP   A OD2 1 
ATOM   1162 N  N   . GLY   A 1 141 ? -8.144  11.729  24.291  1.00 5.75  ? 140 GLY   A N   1 
ATOM   1163 C  CA  . GLY   A 1 141 ? -8.384  12.209  22.951  1.00 5.92  ? 140 GLY   A CA  1 
ATOM   1164 C  C   . GLY   A 1 141 ? -9.234  11.299  22.082  1.00 5.55  ? 140 GLY   A C   1 
ATOM   1165 O  O   . GLY   A 1 141 ? -9.922  11.809  21.201  1.00 5.71  ? 140 GLY   A O   1 
ATOM   1166 N  N   . LEU   A 1 142 ? -9.101  9.973   22.251  1.00 5.55  ? 141 LEU   A N   1 
ATOM   1167 C  CA  . LEU   A 1 142 ? -9.799  9.033   21.389  1.00 5.66  ? 141 LEU   A CA  1 
ATOM   1168 C  C   . LEU   A 1 142 ? -10.657 8.085   22.193  1.00 5.51  ? 141 LEU   A C   1 
ATOM   1169 O  O   . LEU   A 1 142 ? -10.384 7.788   23.356  1.00 5.55  ? 141 LEU   A O   1 
ATOM   1170 C  CB  . LEU   A 1 142 ? -8.831  8.173   20.579  1.00 6.23  ? 141 LEU   A CB  1 
ATOM   1171 C  CG  . LEU   A 1 142 ? -7.924  8.835   19.574  1.00 7.43  ? 141 LEU   A CG  1 
ATOM   1172 C  CD1 . LEU   A 1 142 ? -7.158  7.813   18.782  1.00 7.11  ? 141 LEU   A CD1 1 
ATOM   1173 C  CD2 . LEU   A 1 142 ? -8.554  9.877   18.667  1.00 8.21  ? 141 LEU   A CD2 1 
ATOM   1174 N  N   . ALA   A 1 143 ? -11.721 7.579   21.530  1.00 5.37  ? 142 ALA   A N   1 
ATOM   1175 C  CA  . ALA   A 1 143 ? -12.512 6.459   22.038  1.00 5.32  ? 142 ALA   A CA  1 
ATOM   1176 C  C   . ALA   A 1 143 ? -12.569 5.452   20.917  1.00 5.26  ? 142 ALA   A C   1 
ATOM   1177 O  O   . ALA   A 1 143 ? -12.936 5.795   19.790  1.00 5.80  ? 142 ALA   A O   1 
ATOM   1178 C  CB  . ALA   A 1 143 ? -13.888 6.892   22.440  1.00 5.74  ? 142 ALA   A CB  1 
ATOM   1179 N  N   . VAL   A 1 144 ? -12.057 4.245   21.189  1.00 5.17  ? 143 VAL   A N   1 
ATOM   1180 C  CA  . VAL   A 1 144 ? -12.052 3.188   20.172  1.00 5.31  ? 143 VAL   A CA  1 
ATOM   1181 C  C   . VAL   A 1 144 ? -13.017 2.116   20.646  1.00 5.01  ? 143 VAL   A C   1 
ATOM   1182 O  O   . VAL   A 1 144 ? -12.871 1.582   21.741  1.00 5.36  ? 143 VAL   A O   1 
ATOM   1183 C  CB  . VAL   A 1 144 ? -10.666 2.621   19.811  1.00 5.70  ? 143 VAL   A CB  1 
ATOM   1184 C  CG1 . VAL   A 1 144 ? -10.801 1.608   18.709  1.00 5.83  ? 143 VAL   A CG1 1 
ATOM   1185 C  CG2 . VAL   A 1 144 ? -9.734  3.725   19.372  1.00 6.14  ? 143 VAL   A CG2 1 
ATOM   1186 N  N   . LEU   A 1 145 ? -14.018 1.836   19.804  1.00 5.03  ? 144 LEU   A N   1 
ATOM   1187 C  CA  . LEU   A 1 145 ? -14.944 0.724   20.011  1.00 5.35  ? 144 LEU   A CA  1 
ATOM   1188 C  C   . LEU   A 1 145 ? -14.376 -0.504  19.316  1.00 5.16  ? 144 LEU   A C   1 
ATOM   1189 O  O   . LEU   A 1 145 ? -14.197 -0.491  18.099  1.00 6.06  ? 144 LEU   A O   1 
ATOM   1190 C  CB  . LEU   A 1 145 ? -16.294 1.191   19.428  1.00 6.66  ? 144 LEU   A CB  1 
ATOM   1191 C  CG  . LEU   A 1 145 ? -17.489 0.255   19.621  1.00 7.77  ? 144 LEU   A CG  1 
ATOM   1192 C  CD1 . LEU   A 1 145 ? -17.798 0.009   21.052  1.00 8.83  ? 144 LEU   A CD1 1 
ATOM   1193 C  CD2 . LEU   A 1 145 ? -18.704 0.811   18.918  1.00 8.34  ? 144 LEU   A CD2 1 
ATOM   1194 N  N   . GLY   A 1 146 ? -14.079 -1.506  20.142  1.00 4.79  ? 145 GLY   A N   1 
ATOM   1195 C  CA  . GLY   A 1 146 ? -13.536 -2.759  19.647  1.00 5.01  ? 145 GLY   A CA  1 
ATOM   1196 C  C   . GLY   A 1 146 ? -14.590 -3.839  19.667  1.00 4.79  ? 145 GLY   A C   1 
ATOM   1197 O  O   . GLY   A 1 146 ? -15.297 -4.006  20.653  1.00 5.76  ? 145 GLY   A O   1 
ATOM   1198 N  N   . ILE   A 1 147 ? -14.641 -4.581  18.561  1.00 4.54  ? 146 ILE   A N   1 
ATOM   1199 C  CA  . ILE   A 1 147 ? -15.627 -5.626  18.358  1.00 4.87  ? 146 ILE   A CA  1 
ATOM   1200 C  C   . ILE   A 1 147 ? -14.901 -6.853  17.841  1.00 4.97  ? 146 ILE   A C   1 
ATOM   1201 O  O   . ILE   A 1 147 ? -14.169 -6.808  16.849  1.00 5.31  ? 146 ILE   A O   1 
ATOM   1202 C  CB  . ILE   A 1 147 ? -16.735 -5.134  17.406  1.00 5.63  ? 146 ILE   A CB  1 
ATOM   1203 C  CG1 . ILE   A 1 147 ? -17.400 -3.899  17.928  1.00 6.18  ? 146 ILE   A CG1 1 
ATOM   1204 C  CG2 . ILE   A 1 147 ? -17.756 -6.246  17.181  1.00 6.48  ? 146 ILE   A CG2 1 
ATOM   1205 C  CD1 . ILE   A 1 147 ? -18.446 -3.280  17.054  1.00 6.16  ? 146 ILE   A CD1 1 
ATOM   1206 N  N   . PHE   A 1 148 ? -15.099 -7.973  18.530  1.00 4.91  ? 147 PHE   A N   1 
ATOM   1207 C  CA  . PHE   A 1 148 ? -14.465 -9.232  18.107  1.00 5.13  ? 147 PHE   A CA  1 
ATOM   1208 C  C   . PHE   A 1 148 ? -15.242 -9.853  16.967  1.00 5.49  ? 147 PHE   A C   1 
ATOM   1209 O  O   . PHE   A 1 148 ? -16.460 -9.746  16.883  1.00 5.92  ? 147 PHE   A O   1 
ATOM   1210 C  CB  . PHE   A 1 148 ? -14.449 -10.208 19.281  1.00 5.18  ? 147 PHE   A CB  1 
ATOM   1211 C  CG  . PHE   A 1 148 ? -13.613 -9.737  20.454  1.00 5.19  ? 147 PHE   A CG  1 
ATOM   1212 C  CD1 . PHE   A 1 148 ? -12.257 -9.557  20.292  1.00 5.50  ? 147 PHE   A CD1 1 
ATOM   1213 C  CD2 . PHE   A 1 148 ? -14.155 -9.484  21.693  1.00 5.42  ? 147 PHE   A CD2 1 
ATOM   1214 C  CE1 . PHE   A 1 148 ? -11.446 -9.156  21.336  1.00 5.75  ? 147 PHE   A CE1 1 
ATOM   1215 C  CE2 . PHE   A 1 148 ? -13.358 -9.069  22.724  1.00 5.81  ? 147 PHE   A CE2 1 
ATOM   1216 C  CZ  . PHE   A 1 148 ? -12.012 -8.919  22.570  1.00 5.65  ? 147 PHE   A CZ  1 
ATOM   1217 N  N   . LEU   A 1 149 ? -14.519 -10.543 16.096  1.00 5.42  ? 148 LEU   A N   1 
ATOM   1218 C  CA  . LEU   A 1 149 ? -15.068 -11.346 15.003  1.00 5.80  ? 148 LEU   A CA  1 
ATOM   1219 C  C   . LEU   A 1 149 ? -14.729 -12.814 15.211  1.00 6.20  ? 148 LEU   A C   1 
ATOM   1220 O  O   . LEU   A 1 149 ? -13.567 -13.169 15.442  1.00 6.61  ? 148 LEU   A O   1 
ATOM   1221 C  CB  . LEU   A 1 149 ? -14.475 -10.937 13.649  1.00 6.07  ? 148 LEU   A CB  1 
ATOM   1222 C  CG  . LEU   A 1 149 ? -15.058 -9.681  12.997  1.00 6.31  ? 148 LEU   A CG  1 
ATOM   1223 C  CD1 . LEU   A 1 149 ? -14.822 -8.416  13.786  1.00 6.66  ? 148 LEU   A CD1 1 
ATOM   1224 C  CD2 . LEU   A 1 149 ? -14.423 -9.515  11.611  1.00 6.86  ? 148 LEU   A CD2 1 
ATOM   1225 N  N   . LYS   A 1 150 ? -15.760 -13.665 15.137  1.00 7.17  ? 149 LYS   A N   1 
ATOM   1226 C  CA  . LYS   A 1 150 ? -15.585 -15.113 15.088  1.00 8.09  ? 149 LYS   A CA  1 
ATOM   1227 C  C   . LYS   A 1 150 ? -16.081 -15.630 13.742  1.00 8.55  ? 149 LYS   A C   1 
ATOM   1228 O  O   . LYS   A 1 150 ? -16.883 -14.985 13.074  1.00 8.85  ? 149 LYS   A O   1 
ATOM   1229 C  CB  . LYS   A 1 150 ? -16.288 -15.777 16.251  1.00 9.75  ? 149 LYS   A CB  1 
ATOM   1230 C  CG  . LYS   A 1 150 ? -17.809 -15.657 16.212  1.00 11.39 ? 149 LYS   A CG  1 
ATOM   1231 C  CD  . LYS   A 1 150 ? -18.468 -16.271 17.440  1.00 14.05 ? 149 LYS   A CD  1 
ATOM   1232 C  CE  . LYS   A 1 150 ? -19.965 -16.294 17.398  1.00 16.83 ? 149 LYS   A CE  1 
ATOM   1233 N  NZ  . LYS   A 1 150 ? -20.631 -16.959 18.527  1.00 18.53 ? 149 LYS   A NZ  1 
ATOM   1234 N  N   . VAL   A 1 151 ? -15.557 -16.776 13.341  1.00 8.80  ? 150 VAL   A N   1 
ATOM   1235 C  CA  . VAL   A 1 151 ? -15.960 -17.352 12.067  1.00 8.72  ? 150 VAL   A CA  1 
ATOM   1236 C  C   . VAL   A 1 151 ? -17.162 -18.277 12.283  1.00 9.46  ? 150 VAL   A C   1 
ATOM   1237 O  O   . VAL   A 1 151 ? -17.143 -19.218 13.088  1.00 10.50 ? 150 VAL   A O   1 
ATOM   1238 C  CB  . VAL   A 1 151 ? -14.776 -18.114 11.458  1.00 9.33  ? 150 VAL   A CB  1 
ATOM   1239 C  CG1 . VAL   A 1 151 ? -15.217 -18.918 10.233  1.00 9.77  ? 150 VAL   A CG1 1 
ATOM   1240 C  CG2 . VAL   A 1 151 ? -13.652 -17.177 11.096  1.00 9.81  ? 150 VAL   A CG2 1 
ATOM   1241 N  N   . GLY   A 1 152 ? -18.234 -18.005 11.541  1.00 8.93  ? 151 GLY   A N   1 
ATOM   1242 C  CA  . GLY   A 1 152 ? -19.440 -18.822 11.563  1.00 9.31  ? 151 GLY   A CA  1 
ATOM   1243 C  C   . GLY   A 1 152 ? -20.309 -18.363 10.409  1.00 9.16  ? 151 GLY   A C   1 
ATOM   1244 O  O   . GLY   A 1 152 ? -19.954 -18.468 9.246   1.00 9.23  ? 151 GLY   A O   1 
ATOM   1245 N  N   A SER   A 1 153 ? -21.491 -17.864 10.751  0.50 9.83  ? 152 SER   A N   1 
ATOM   1246 N  N   B SER   A 1 153 ? -21.504 -17.878 10.719  0.50 10.03 ? 152 SER   A N   1 
ATOM   1247 C  CA  A SER   A 1 153 ? -22.400 -17.262 9.791   0.50 10.11 ? 152 SER   A CA  1 
ATOM   1248 C  CA  B SER   A 1 153 ? -22.380 -17.333 9.694   0.50 10.54 ? 152 SER   A CA  1 
ATOM   1249 C  C   A SER   A 1 153 ? -21.776 -16.009 9.176   0.50 9.68  ? 152 SER   A C   1 
ATOM   1250 C  C   B SER   A 1 153 ? -21.833 -16.005 9.188   0.50 9.91  ? 152 SER   A C   1 
ATOM   1251 O  O   A SER   A 1 153 ? -20.977 -15.331 9.799   0.50 9.43  ? 152 SER   A O   1 
ATOM   1252 O  O   B SER   A 1 153 ? -21.214 -15.255 9.928   0.50 9.62  ? 152 SER   A O   1 
ATOM   1253 C  CB  A SER   A 1 153 ? -23.730 -16.931 10.463  0.50 10.92 ? 152 SER   A CB  1 
ATOM   1254 C  CB  B SER   A 1 153 ? -23.773 -17.117 10.220  0.50 11.80 ? 152 SER   A CB  1 
ATOM   1255 O  OG  A SER   A 1 153 ? -24.364 -18.094 10.988  0.50 11.92 ? 152 SER   A OG  1 
ATOM   1256 O  OG  B SER   A 1 153 ? -23.779 -16.026 11.139  0.50 13.86 ? 152 SER   A OG  1 
ATOM   1257 N  N   . ALA   A 1 154 ? -22.127 -15.695 7.925   1.00 9.41  ? 153 ALA   A N   1 
ATOM   1258 C  CA  . ALA   A 1 154 ? -21.720 -14.466 7.267   1.00 9.38  ? 153 ALA   A CA  1 
ATOM   1259 C  C   . ALA   A 1 154 ? -22.363 -13.263 7.966   1.00 9.32  ? 153 ALA   A C   1 
ATOM   1260 O  O   . ALA   A 1 154 ? -23.460 -13.334 8.520   1.00 10.19 ? 153 ALA   A O   1 
ATOM   1261 C  CB  . ALA   A 1 154 ? -22.159 -14.480 5.813   1.00 9.82  ? 153 ALA   A CB  1 
ATOM   1262 N  N   . LYS   A 1 155 ? -21.670 -12.128 7.943   1.00 9.15  ? 154 LYS   A N   1 
ATOM   1263 C  CA  . LYS   A 1 155 ? -22.192 -10.851 8.393   1.00 9.60  ? 154 LYS   A CA  1 
ATOM   1264 C  C   . LYS   A 1 155 ? -22.626 -10.102 7.145   1.00 9.76  ? 154 LYS   A C   1 
ATOM   1265 O  O   . LYS   A 1 155 ? -21.784 -9.600  6.369   1.00 8.94  ? 154 LYS   A O   1 
ATOM   1266 C  CB  . LYS   A 1 155 ? -21.123 -10.065 9.147   1.00 10.06 ? 154 LYS   A CB  1 
ATOM   1267 C  CG  . LYS   A 1 155 ? -21.649 -8.864  9.908   1.00 11.04 ? 154 LYS   A CG  1 
ATOM   1268 C  CD  . LYS   A 1 155 ? -22.527 -9.212  11.108  1.00 12.43 ? 154 LYS   A CD  1 
ATOM   1269 C  CE  . LYS   A 1 155 ? -22.769 -8.037  12.006  1.00 13.84 ? 154 LYS   A CE  1 
ATOM   1270 N  NZ  . LYS   A 1 155 ? -23.536 -8.396  13.181  1.00 15.70 ? 154 LYS   A NZ  1 
ATOM   1271 N  N   . PRO   A 1 156 ? -23.942 -9.957  6.872   1.00 10.75 ? 155 PRO   A N   1 
ATOM   1272 C  CA  . PRO   A 1 156 ? -24.339 -9.308  5.623   1.00 11.19 ? 155 PRO   A CA  1 
ATOM   1273 C  C   . PRO   A 1 156 ? -23.801 -7.897  5.499   1.00 11.49 ? 155 PRO   A C   1 
ATOM   1274 O  O   . PRO   A 1 156 ? -23.421 -7.524  4.391   1.00 12.23 ? 155 PRO   A O   1 
ATOM   1275 C  CB  . PRO   A 1 156 ? -25.877 -9.389  5.706   1.00 12.59 ? 155 PRO   A CB  1 
ATOM   1276 C  CG  . PRO   A 1 156 ? -26.130 -10.583 6.548   1.00 13.63 ? 155 PRO   A CG  1 
ATOM   1277 C  CD  . PRO   A 1 156 ? -25.090 -10.499 7.631   1.00 12.14 ? 155 PRO   A CD  1 
ATOM   1278 N  N   . GLY   A 1 157 ? -23.751 -7.154  6.616   1.00 10.97 ? 156 GLY   A N   1 
ATOM   1279 C  CA  . GLY   A 1 157 ? -23.326 -5.771  6.600   1.00 10.99 ? 156 GLY   A CA  1 
ATOM   1280 C  C   . GLY   A 1 157 ? -21.838 -5.623  6.317   1.00 10.70 ? 156 GLY   A C   1 
ATOM   1281 O  O   . GLY   A 1 157 ? -21.418 -4.483  6.104   1.00 12.08 ? 156 GLY   A O   1 
ATOM   1282 N  N   . LEU   A 1 158 ? -21.062 -6.704  6.342   1.00 9.29  ? 157 LEU   A N   1 
ATOM   1283 C  CA  . LEU   A 1 158 ? -19.641 -6.655  5.998   1.00 8.87  ? 157 LEU   A CA  1 
ATOM   1284 C  C   . LEU   A 1 158 ? -19.394 -6.867  4.522   1.00 8.91  ? 157 LEU   A C   1 
ATOM   1285 O  O   . LEU   A 1 158 ? -18.334 -6.560  4.034   1.00 9.09  ? 157 LEU   A O   1 
ATOM   1286 C  CB  . LEU   A 1 158 ? -18.905 -7.682  6.846   1.00 9.33  ? 157 LEU   A CB  1 
ATOM   1287 C  CG  . LEU   A 1 158 ? -17.388 -7.782  6.691   1.00 9.35  ? 157 LEU   A CG  1 
ATOM   1288 C  CD1 . LEU   A 1 158 ? -16.707 -6.498  7.072   1.00 9.47  ? 157 LEU   A CD1 1 
ATOM   1289 C  CD2 . LEU   A 1 158 ? -16.852 -8.950  7.492   1.00 10.11 ? 157 LEU   A CD2 1 
ATOM   1290 N  N   . GLN   A 1 159 ? -20.352 -7.425  3.786   1.00 9.42  ? 158 GLN   A N   1 
ATOM   1291 C  CA  . GLN   A 1 159 ? -20.024 -7.908  2.463   1.00 9.96  ? 158 GLN   A CA  1 
ATOM   1292 C  C   . GLN   A 1 159 ? -19.587 -6.757  1.544   1.00 9.89  ? 158 GLN   A C   1 
ATOM   1293 O  O   . GLN   A 1 159 ? -18.757 -6.980  0.673   1.00 9.52  ? 158 GLN   A O   1 
ATOM   1294 C  CB  . GLN   A 1 159 ? -21.169 -8.748  1.877   1.00 10.57 ? 158 GLN   A CB  1 
ATOM   1295 C  CG  . GLN   A 1 159 ? -20.767 -9.448  0.591   1.00 11.12 ? 158 GLN   A CG  1 
ATOM   1296 C  CD  . GLN   A 1 159 ? -19.644 -10.433 0.804   1.00 10.84 ? 158 GLN   A CD  1 
ATOM   1297 O  OE1 . GLN   A 1 159 ? -19.510 -11.044 1.880   1.00 10.13 ? 158 GLN   A OE1 1 
ATOM   1298 N  NE2 . GLN   A 1 159 ? -18.858 -10.642 -0.239  1.00 11.76 ? 158 GLN   A NE2 1 
ATOM   1299 N  N   . LYS   A 1 160 ? -20.165 -5.559  1.633   1.00 10.16 ? 159 LYS   A N   1 
ATOM   1300 C  CA  . LYS   A 1 160 ? -19.754 -4.442  0.793   1.00 10.76 ? 159 LYS   A CA  1 
ATOM   1301 C  C   . LYS   A 1 160 ? -18.275 -4.143  0.956   1.00 10.03 ? 159 LYS   A C   1 
ATOM   1302 O  O   . LYS   A 1 160 ? -17.596 -3.766  0.003   1.00 10.61 ? 159 LYS   A O   1 
ATOM   1303 C  CB  . LYS   A 1 160 ? -20.632 -3.217  1.057   1.00 12.84 ? 159 LYS   A CB  1 
ATOM   1304 C  CG  . LYS   A 1 160 ? -21.970 -3.290  0.338   1.00 16.39 ? 159 LYS   A CG  1 
ATOM   1305 C  CD  . LYS   A 1 160 ? -22.069 -2.942  -1.138  1.00 20.61 ? 159 LYS   A CD  1 
ATOM   1306 C  CE  . LYS   A 1 160 ? -23.522 -2.964  -1.594  1.00 23.47 ? 159 LYS   A CE  1 
ATOM   1307 N  NZ  . LYS   A 1 160 ? -23.600 -3.255  -3.032  1.00 26.83 ? 159 LYS   A NZ  1 
ATOM   1308 N  N   . VAL   A 1 161 ? -17.784 -4.265  2.186   1.00 9.60  ? 160 VAL   A N   1 
ATOM   1309 C  CA  . VAL   A 1 161 ? -16.361 -4.088  2.425   1.00 9.15  ? 160 VAL   A CA  1 
ATOM   1310 C  C   . VAL   A 1 161 ? -15.557 -5.189  1.740   1.00 8.98  ? 160 VAL   A C   1 
ATOM   1311 O  O   . VAL   A 1 161 ? -14.599 -4.951  1.007   1.00 9.57  ? 160 VAL   A O   1 
ATOM   1312 C  CB  . VAL   A 1 161 ? -16.068 -4.078  3.926   1.00 9.38  ? 160 VAL   A CB  1 
ATOM   1313 C  CG1 . VAL   A 1 161 ? -14.556 -4.159  4.224   1.00 9.84  ? 160 VAL   A CG1 1 
ATOM   1314 C  CG2 . VAL   A 1 161 ? -16.750 -2.886  4.588   1.00 10.00 ? 160 VAL   A CG2 1 
ATOM   1315 N  N   . VAL   A 1 162 ? -15.966 -6.444  1.942   1.00 9.11  ? 161 VAL   A N   1 
ATOM   1316 C  CA  . VAL   A 1 162 ? -15.280 -7.593  1.356   1.00 10.38 ? 161 VAL   A CA  1 
ATOM   1317 C  C   . VAL   A 1 162 ? -15.159 -7.419  -0.149  1.00 10.86 ? 161 VAL   A C   1 
ATOM   1318 O  O   . VAL   A 1 162 ? -14.129 -7.717  -0.758  1.00 11.85 ? 161 VAL   A O   1 
ATOM   1319 C  CB  . VAL   A 1 162 ? -16.013 -8.917  1.712   1.00 11.28 ? 161 VAL   A CB  1 
ATOM   1320 C  CG1 . VAL   A 1 162 ? -15.542 -10.104 0.882   1.00 12.10 ? 161 VAL   A CG1 1 
ATOM   1321 C  CG2 . VAL   A 1 162 ? -15.848 -9.181  3.202   1.00 11.64 ? 161 VAL   A CG2 1 
ATOM   1322 N  N   . ASP   A 1 163 ? -16.262 -6.983  -0.783  1.00 11.19 ? 162 ASP   A N   1 
ATOM   1323 C  CA  . ASP   A 1 163 ? -16.306 -6.935  -2.240  1.00 12.61 ? 162 ASP   A CA  1 
ATOM   1324 C  C   . ASP   A 1 163 ? -15.432 -5.869  -2.868  1.00 12.99 ? 162 ASP   A C   1 
ATOM   1325 O  O   . ASP   A 1 163 ? -15.062 -6.012  -4.026  1.00 16.38 ? 162 ASP   A O   1 
ATOM   1326 C  CB  . ASP   A 1 163 ? -17.730 -6.929  -2.690  1.00 15.14 ? 162 ASP   A CB  1 
ATOM   1327 C  CG  . ASP   A 1 163 ? -18.326 -8.329  -2.618  1.00 16.58 ? 162 ASP   A CG  1 
ATOM   1328 O  OD1 . ASP   A 1 163 ? -17.586 -9.359  -2.723  1.00 18.90 ? 162 ASP   A OD1 1 
ATOM   1329 O  OD2 . ASP   A 1 163 ? -19.499 -8.400  -2.371  1.00 19.93 ? 162 ASP   A OD2 1 
ATOM   1330 N  N   . VAL   A 1 164 ? -15.024 -4.851  -2.134  1.00 10.64 ? 163 VAL   A N   1 
ATOM   1331 C  CA  . VAL   A 1 164 ? -14.192 -3.782  -2.660  1.00 11.19 ? 163 VAL   A CA  1 
ATOM   1332 C  C   . VAL   A 1 164 ? -12.699 -4.098  -2.485  1.00 10.27 ? 163 VAL   A C   1 
ATOM   1333 O  O   . VAL   A 1 164 ? -11.848 -3.382  -3.034  1.00 10.65 ? 163 VAL   A O   1 
ATOM   1334 C  CB  . VAL   A 1 164 ? -14.553 -2.415  -2.068  1.00 12.11 ? 163 VAL   A CB  1 
ATOM   1335 C  CG1 . VAL   A 1 164 ? -14.020 -2.217  -0.681  1.00 11.90 ? 163 VAL   A CG1 1 
ATOM   1336 C  CG2 . VAL   A 1 164 ? -14.173 -1.226  -2.930  1.00 12.93 ? 163 VAL   A CG2 1 
ATOM   1337 N  N   . LEU   A 1 165 ? -12.356 -5.113  -1.698  1.00 10.03 ? 164 LEU   A N   1 
ATOM   1338 C  CA  . LEU   A 1 165 ? -10.964 -5.341  -1.359  1.00 9.98  ? 164 LEU   A CA  1 
ATOM   1339 C  C   . LEU   A 1 165 ? -10.095 -5.630  -2.567  1.00 10.79 ? 164 LEU   A C   1 
ATOM   1340 O  O   . LEU   A 1 165 ? -8.928  -5.285  -2.567  1.00 10.69 ? 164 LEU   A O   1 
ATOM   1341 C  CB  . LEU   A 1 165 ? -10.812 -6.418  -0.313  1.00 10.17 ? 164 LEU   A CB  1 
ATOM   1342 C  CG  . LEU   A 1 165 ? -11.473 -6.115  1.044   1.00 9.98  ? 164 LEU   A CG  1 
ATOM   1343 C  CD1 . LEU   A 1 165 ? -11.220 -7.222  2.045   1.00 10.57 ? 164 LEU   A CD1 1 
ATOM   1344 C  CD2 . LEU   A 1 165 ? -11.007 -4.805  1.639   1.00 10.03 ? 164 LEU   A CD2 1 
ATOM   1345 N  N   . ASP   A 1 166 ? -10.642 -6.263  -3.592  1.00 12.82 ? 165 ASP   A N   1 
ATOM   1346 C  CA  . ASP   A 1 166 ? -9.915  -6.531  -4.828  1.00 14.79 ? 165 ASP   A CA  1 
ATOM   1347 C  C   . ASP   A 1 166 ? -9.362  -5.259  -5.445  1.00 14.41 ? 165 ASP   A C   1 
ATOM   1348 O  O   . ASP   A 1 166 ? -8.345  -5.274  -6.137  1.00 18.22 ? 165 ASP   A O   1 
ATOM   1349 C  CB  . ASP   A 1 166 ? -10.825 -7.247  -5.831  1.00 17.98 ? 165 ASP   A CB  1 
ATOM   1350 C  CG  . ASP   A 1 166 ? -10.826 -8.751  -5.698  1.00 21.98 ? 165 ASP   A CG  1 
ATOM   1351 O  OD1 . ASP   A 1 166 ? -9.888  -9.265  -5.011  1.00 26.44 ? 165 ASP   A OD1 1 
ATOM   1352 O  OD2 . ASP   A 1 166 ? -11.736 -9.377  -6.290  1.00 26.26 ? 165 ASP   A OD2 1 
ATOM   1353 N  N   . SER   A 1 167 ? -10.050 -4.150  -5.231  1.00 12.20 ? 166 SER   A N   1 
ATOM   1354 C  CA  . SER   A 1 167 ? -9.658  -2.905  -5.866  1.00 11.95 ? 166 SER   A CA  1 
ATOM   1355 C  C   . SER   A 1 167 ? -8.603  -2.160  -5.052  1.00 10.12 ? 166 SER   A C   1 
ATOM   1356 O  O   . SER   A 1 167 ? -8.051  -1.163  -5.495  1.00 11.56 ? 166 SER   A O   1 
ATOM   1357 C  CB  . SER   A 1 167 ? -10.812 -2.040  -6.079  1.00 13.04 ? 166 SER   A CB  1 
ATOM   1358 O  OG  . SER   A 1 167 ? -11.351 -1.498  -4.916  1.00 14.10 ? 166 SER   A OG  1 
ATOM   1359 N  N   . ILE   A 1 168 ? -8.315  -2.619  -3.819  1.00 8.84  ? 167 ILE   A N   1 
ATOM   1360 C  CA  . ILE   A 1 168 ? -7.311  -1.997  -2.961  1.00 8.66  ? 167 ILE   A CA  1 
ATOM   1361 C  C   . ILE   A 1 168 ? -6.325  -3.064  -2.469  1.00 7.94  ? 167 ILE   A C   1 
ATOM   1362 O  O   . ILE   A 1 168 ? -5.909  -3.057  -1.317  1.00 8.02  ? 167 ILE   A O   1 
ATOM   1363 C  CB  . ILE   A 1 168 ? -7.907  -1.176  -1.806  1.00 8.79  ? 167 ILE   A CB  1 
ATOM   1364 C  CG1 . ILE   A 1 168 ? -8.781  -2.043  -0.908  1.00 8.56  ? 167 ILE   A CG1 1 
ATOM   1365 C  CG2 . ILE   A 1 168 ? -8.677  0.033   -2.339  1.00 9.40  ? 167 ILE   A CG2 1 
ATOM   1366 C  CD1 . ILE   A 1 168 ? -8.845  -1.517  0.493   1.00 9.12  ? 167 ILE   A CD1 1 
ATOM   1367 N  N   . LYS   A 1 169 ? -5.915  -3.947  -3.369  1.00 8.19  ? 168 LYS   A N   1 
ATOM   1368 C  CA  . LYS   A 1 169 ? -5.133  -5.085  -2.941  1.00 8.49  ? 168 LYS   A CA  1 
ATOM   1369 C  C   . LYS   A 1 169 ? -3.816  -4.698  -2.308  1.00 8.12  ? 168 LYS   A C   1 
ATOM   1370 O  O   . LYS   A 1 169 ? -3.389  -5.372  -1.372  1.00 8.08  ? 168 LYS   A O   1 
ATOM   1371 C  CB  . LYS   A 1 169 ? -4.848  -6.005  -4.128  1.00 10.19 ? 168 LYS   A CB  1 
ATOM   1372 C  CG  . LYS   A 1 169 ? -4.114  -7.284  -3.758  1.00 11.72 ? 168 LYS   A CG  1 
ATOM   1373 C  CD  . LYS   A 1 169 ? -3.953  -8.207  -4.952  1.00 13.99 ? 168 LYS   A CD  1 
ATOM   1374 C  CE  . LYS   A 1 169 ? -3.051  -9.346  -4.742  1.00 16.61 ? 168 LYS   A CE  1 
ATOM   1375 N  NZ  . LYS   A 1 169 ? -3.046  -10.316 -5.815  1.00 19.56 ? 168 LYS   A NZ  1 
ATOM   1376 N  N   . THR   A 1 170 ? -3.176  -3.648  -2.818  1.00 7.76  ? 169 THR   A N   1 
ATOM   1377 C  CA  . THR   A 1 170 ? -1.816  -3.331  -2.441  1.00 7.81  ? 169 THR   A CA  1 
ATOM   1378 C  C   . THR   A 1 170 ? -1.726  -1.948  -1.779  1.00 7.81  ? 169 THR   A C   1 
ATOM   1379 O  O   . THR   A 1 170 ? -2.598  -1.081  -1.895  1.00 8.19  ? 169 THR   A O   1 
ATOM   1380 C  CB  . THR   A 1 170 ? -0.911  -3.352  -3.669  1.00 8.54  ? 169 THR   A CB  1 
ATOM   1381 O  OG1 . THR   A 1 170 ? -1.487  -2.570  -4.709  1.00 9.06  ? 169 THR   A OG1 1 
ATOM   1382 C  CG2 . THR   A 1 170 ? -0.695  -4.779  -4.145  1.00 8.83  ? 169 THR   A CG2 1 
ATOM   1383 N  N   . LYS   A 1 171 ? -0.644  -1.797  -1.025  1.00 8.18  ? 170 LYS   A N   1 
ATOM   1384 C  CA  . LYS   A 1 171 ? -0.371  -0.610  -0.246  1.00 8.54  ? 170 LYS   A CA  1 
ATOM   1385 C  C   . LYS   A 1 171 ? -0.451  0.658   -1.088  1.00 8.84  ? 170 LYS   A C   1 
ATOM   1386 O  O   . LYS   A 1 171 ? 0.128   0.762   -2.179  1.00 9.51  ? 170 LYS   A O   1 
ATOM   1387 C  CB  . LYS   A 1 171 ? 1.047   -0.741  0.325   1.00 9.65  ? 170 LYS   A CB  1 
ATOM   1388 C  CG  . LYS   A 1 171 ? 1.484   0.470   1.136   1.00 11.27 ? 170 LYS   A CG  1 
ATOM   1389 C  CD  . LYS   A 1 171 ? 2.836   0.308   1.793   1.00 13.45 ? 170 LYS   A CD  1 
ATOM   1390 C  CE  . LYS   A 1 171 ? 3.231   1.459   2.709   1.00 17.04 ? 170 LYS   A CE  1 
ATOM   1391 N  NZ  . LYS   A 1 171 ? 4.585   1.353   3.290   1.00 20.46 ? 170 LYS   A NZ  1 
ATOM   1392 N  N   . GLY   A 1 172 ? -1.194  1.643   -0.565  1.00 8.77  ? 171 GLY   A N   1 
ATOM   1393 C  CA  . GLY   A 1 172 ? -1.355  2.937   -1.181  1.00 9.61  ? 171 GLY   A CA  1 
ATOM   1394 C  C   . GLY   A 1 172 ? -2.548  3.024   -2.108  1.00 9.77  ? 171 GLY   A C   1 
ATOM   1395 O  O   . GLY   A 1 172 ? -2.847  4.111   -2.600  1.00 11.81 ? 171 GLY   A O   1 
ATOM   1396 N  N   . LYS   A 1 173 ? -3.232  1.933   -2.406  1.00 9.17  ? 172 LYS   A N   1 
ATOM   1397 C  CA  . LYS   A 1 173 ? -4.436  1.982   -3.211  1.00 9.75  ? 172 LYS   A CA  1 
ATOM   1398 C  C   . LYS   A 1 173 ? -5.615  2.409   -2.358  1.00 8.91  ? 172 LYS   A C   1 
ATOM   1399 O  O   . LYS   A 1 173 ? -5.806  1.933   -1.247  1.00 8.47  ? 172 LYS   A O   1 
ATOM   1400 C  CB  . LYS   A 1 173 ? -4.733  0.641   -3.890  1.00 11.15 ? 172 LYS   A CB  1 
ATOM   1401 C  CG  . LYS   A 1 173 ? -3.729  0.252   -4.960  1.00 13.46 ? 172 LYS   A CG  1 
ATOM   1402 C  CD  . LYS   A 1 173 ? -4.183  -0.768  -5.992  1.00 16.68 ? 172 LYS   A CD  1 
ATOM   1403 C  CE  . LYS   A 1 173 ? -3.373  -0.692  -7.245  1.00 18.67 ? 172 LYS   A CE  1 
ATOM   1404 N  NZ  . LYS   A 1 173 ? -2.763  0.602   -7.528  1.00 20.99 ? 172 LYS   A NZ  1 
ATOM   1405 N  N   . SER   A 1 174 ? -6.468  3.237   -2.921  1.00 9.66  ? 173 SER   A N   1 
ATOM   1406 C  CA  . SER   A 1 174 ? -7.743  3.642   -2.352  1.00 9.74  ? 173 SER   A CA  1 
ATOM   1407 C  C   . SER   A 1 174 ? -8.845  3.493   -3.387  1.00 10.16 ? 173 SER   A C   1 
ATOM   1408 O  O   . SER   A 1 174 ? -8.618  3.445   -4.594  1.00 11.05 ? 173 SER   A O   1 
ATOM   1409 C  CB  . SER   A 1 174 ? -7.662  5.053   -1.836  1.00 10.97 ? 173 SER   A CB  1 
ATOM   1410 O  OG  . SER   A 1 174 ? -7.549  5.996   -2.892  1.00 12.23 ? 173 SER   A OG  1 
ATOM   1411 N  N   . ALA   A 1 175 ? -10.080 3.501   -2.902  1.00 10.18 ? 174 ALA   A N   1 
ATOM   1412 C  CA  . ALA   A 1 175 ? -11.266 3.479   -3.741  1.00 10.48 ? 174 ALA   A CA  1 
ATOM   1413 C  C   . ALA   A 1 175 ? -12.370 4.256   -3.056  1.00 10.20 ? 174 ALA   A C   1 
ATOM   1414 O  O   . ALA   A 1 175 ? -12.469 4.318   -1.835  1.00 9.24  ? 174 ALA   A O   1 
ATOM   1415 C  CB  . ALA   A 1 175 ? -11.735 2.064   -3.977  1.00 10.93 ? 174 ALA   A CB  1 
ATOM   1416 N  N   . ASP   A 1 176 ? -13.253 4.830   -3.854  1.00 11.32 ? 175 ASP   A N   1 
ATOM   1417 C  CA  . ASP   A 1 176 ? -14.438 5.492   -3.330  1.00 12.22 ? 175 ASP   A CA  1 
ATOM   1418 C  C   . ASP   A 1 176 ? -15.225 4.454   -2.566  1.00 11.62 ? 175 ASP   A C   1 
ATOM   1419 O  O   . ASP   A 1 176 ? -15.304 3.272   -2.954  1.00 13.45 ? 175 ASP   A O   1 
ATOM   1420 C  CB  . ASP   A 1 176 ? -15.289 6.088   -4.464  1.00 14.75 ? 175 ASP   A CB  1 
ATOM   1421 C  CG  . ASP   A 1 176 ? -14.624 7.202   -5.274  1.00 18.91 ? 175 ASP   A CG  1 
ATOM   1422 O  OD1 . ASP   A 1 176 ? -13.980 8.096   -4.648  1.00 22.91 ? 175 ASP   A OD1 1 
ATOM   1423 O  OD2 . ASP   A 1 176 ? -14.787 7.248   -6.539  1.00 22.75 ? 175 ASP   A OD2 1 
ATOM   1424 N  N   . PHE   A 1 177 ? -15.799 4.893   -1.441  1.00 9.97  ? 176 PHE   A N   1 
ATOM   1425 C  CA  . PHE   A 1 177 ? -16.528 3.958   -0.608  1.00 9.58  ? 176 PHE   A CA  1 
ATOM   1426 C  C   . PHE   A 1 177 ? -17.596 4.750   0.120   1.00 9.22  ? 176 PHE   A C   1 
ATOM   1427 O  O   . PHE   A 1 177 ? -17.550 4.916   1.334   1.00 11.28 ? 176 PHE   A O   1 
ATOM   1428 C  CB  . PHE   A 1 177 ? -15.589 3.190   0.325   1.00 9.90  ? 176 PHE   A CB  1 
ATOM   1429 C  CG  . PHE   A 1 177 ? -16.212 1.921   0.858   1.00 10.12 ? 176 PHE   A CG  1 
ATOM   1430 C  CD1 . PHE   A 1 177 ? -16.452 0.875   -0.002  1.00 10.63 ? 176 PHE   A CD1 1 
ATOM   1431 C  CD2 . PHE   A 1 177 ? -16.590 1.771   2.180   1.00 10.07 ? 176 PHE   A CD2 1 
ATOM   1432 C  CE1 . PHE   A 1 177 ? -17.018 -0.299  0.440   1.00 11.28 ? 176 PHE   A CE1 1 
ATOM   1433 C  CE2 . PHE   A 1 177 ? -17.129 0.581   2.647   1.00 10.70 ? 176 PHE   A CE2 1 
ATOM   1434 C  CZ  . PHE   A 1 177 ? -17.376 -0.440  1.752   1.00 11.04 ? 176 PHE   A CZ  1 
ATOM   1435 N  N   . THR   A 1 178 ? -18.548 5.279   -0.609  1.00 8.92  ? 177 THR   A N   1 
ATOM   1436 C  CA  . THR   A 1 178 ? -19.639 6.093   -0.068  1.00 8.66  ? 177 THR   A CA  1 
ATOM   1437 C  C   . THR   A 1 178 ? -20.824 5.224   0.359   1.00 8.60  ? 177 THR   A C   1 
ATOM   1438 O  O   . THR   A 1 178 ? -21.024 4.104   -0.112  1.00 9.37  ? 177 THR   A O   1 
ATOM   1439 C  CB  . THR   A 1 178 ? -19.999 7.165   -1.102  1.00 9.87  ? 177 THR   A CB  1 
ATOM   1440 O  OG1 . THR   A 1 178 ? -20.372 6.556   -2.344  1.00 12.36 ? 177 THR   A OG1 1 
ATOM   1441 C  CG2 . THR   A 1 178 ? -18.936 8.246   -1.273  1.00 11.65 ? 177 THR   A CG2 1 
ATOM   1442 N  N   . ASN   A 1 179 ? -21.669 5.817   1.196   1.00 8.21  ? 178 ASN   A N   1 
ATOM   1443 C  CA  . ASN   A 1 179 ? -22.934 5.240   1.601   1.00 8.99  ? 178 ASN   A CA  1 
ATOM   1444 C  C   . ASN   A 1 179 ? -22.804 3.928   2.355   1.00 9.04  ? 178 ASN   A C   1 
ATOM   1445 O  O   . ASN   A 1 179 ? -23.747 3.163   2.324   1.00 12.00 ? 178 ASN   A O   1 
ATOM   1446 C  CB  . ASN   A 1 179 ? -23.889 5.157   0.412   1.00 9.18  ? 178 ASN   A CB  1 
ATOM   1447 C  CG  . ASN   A 1 179 ? -24.102 6.524   -0.180  1.00 10.05 ? 178 ASN   A CG  1 
ATOM   1448 O  OD1 . ASN   A 1 179 ? -24.697 7.396   0.452   1.00 11.74 ? 178 ASN   A OD1 1 
ATOM   1449 N  ND2 . ASN   A 1 179 ? -23.506 6.774   -1.326  1.00 10.20 ? 178 ASN   A ND2 1 
ATOM   1450 N  N   . PHE   A 1 180 ? -21.695 3.664   3.001   1.00 8.35  ? 179 PHE   A N   1 
ATOM   1451 C  CA  . PHE   A 1 180 ? -21.587 2.468   3.808   1.00 8.24  ? 179 PHE   A CA  1 
ATOM   1452 C  C   . PHE   A 1 180 ? -22.073 2.738   5.209   1.00 8.20  ? 179 PHE   A C   1 
ATOM   1453 O  O   . PHE   A 1 180 ? -21.685 3.726   5.814   1.00 9.05  ? 179 PHE   A O   1 
ATOM   1454 C  CB  . PHE   A 1 180 ? -20.132 1.997   3.887   1.00 8.20  ? 179 PHE   A CB  1 
ATOM   1455 C  CG  . PHE   A 1 180 ? -20.014 0.756   4.727   1.00 8.38  ? 179 PHE   A CG  1 
ATOM   1456 C  CD1 . PHE   A 1 180 ? -20.316 -0.484  4.187   1.00 9.22  ? 179 PHE   A CD1 1 
ATOM   1457 C  CD2 . PHE   A 1 180 ? -19.604 0.798   6.043   1.00 7.83  ? 179 PHE   A CD2 1 
ATOM   1458 C  CE1 . PHE   A 1 180 ? -20.329 -1.612  4.987   1.00 9.01  ? 179 PHE   A CE1 1 
ATOM   1459 C  CE2 . PHE   A 1 180 ? -19.581 -0.343  6.827   1.00 8.00  ? 179 PHE   A CE2 1 
ATOM   1460 C  CZ  . PHE   A 1 180 ? -19.913 -1.560  6.283   1.00 8.48  ? 179 PHE   A CZ  1 
ATOM   1461 N  N   . ASP   A 1 181 ? -22.914 1.849   5.741   1.00 8.48  ? 180 ASP   A N   1 
ATOM   1462 C  CA  . ASP   A 1 181 ? -23.583 1.998   7.022   1.00 8.70  ? 180 ASP   A CA  1 
ATOM   1463 C  C   . ASP   A 1 181 ? -22.887 1.159   8.078   1.00 8.18  ? 180 ASP   A C   1 
ATOM   1464 O  O   . ASP   A 1 181 ? -23.029 -0.060  8.131   1.00 8.40  ? 180 ASP   A O   1 
ATOM   1465 C  CB  . ASP   A 1 181 ? -25.027 1.602   6.900   1.00 9.76  ? 180 ASP   A CB  1 
ATOM   1466 C  CG  . ASP   A 1 181 ? -25.825 1.957   8.142   1.00 10.92 ? 180 ASP   A CG  1 
ATOM   1467 O  OD1 . ASP   A 1 181 ? -25.257 2.230   9.194   1.00 10.75 ? 180 ASP   A OD1 1 
ATOM   1468 O  OD2 . ASP   A 1 181 ? -27.053 1.885   8.038   1.00 15.30 ? 180 ASP   A OD2 1 
ATOM   1469 N  N   . PRO   A 1 182 ? -22.087 1.766   8.978   1.00 7.92  ? 181 PRO   A N   1 
ATOM   1470 C  CA  . PRO   A 1 182 ? -21.380 0.975   10.004  1.00 8.24  ? 181 PRO   A CA  1 
ATOM   1471 C  C   . PRO   A 1 182 ? -22.284 0.323   11.039  1.00 8.08  ? 181 PRO   A C   1 
ATOM   1472 O  O   . PRO   A 1 182 ? -21.812 -0.513  11.795  1.00 8.01  ? 181 PRO   A O   1 
ATOM   1473 C  CB  . PRO   A 1 182 ? -20.395 1.968   10.590  1.00 8.60  ? 181 PRO   A CB  1 
ATOM   1474 C  CG  . PRO   A 1 182 ? -21.057 3.303   10.434  1.00 8.57  ? 181 PRO   A CG  1 
ATOM   1475 C  CD  . PRO   A 1 182 ? -21.786 3.227   9.099   1.00 8.20  ? 181 PRO   A CD  1 
ATOM   1476 N  N   . ARG   A 1 183 ? -23.555 0.707   11.069  1.00 8.02  ? 182 ARG   A N   1 
ATOM   1477 C  CA  . ARG   A 1 183 ? -24.477 0.027   11.984  1.00 8.63  ? 182 ARG   A CA  1 
ATOM   1478 C  C   . ARG   A 1 183 ? -24.531 -1.459  11.646  1.00 8.66  ? 182 ARG   A C   1 
ATOM   1479 O  O   . ARG   A 1 183 ? -24.887 -2.259  12.523  1.00 9.15  ? 182 ARG   A O   1 
ATOM   1480 C  CB  . ARG   A 1 183 ? -25.885 0.629   11.910  1.00 9.50  ? 182 ARG   A CB  1 
ATOM   1481 C  CG  . ARG   A 1 183 ? -25.905 2.040   12.492  1.00 10.58 ? 182 ARG   A CG  1 
ATOM   1482 C  CD  . ARG   A 1 183 ? -27.198 2.736   12.420  1.00 12.32 ? 182 ARG   A CD  1 
ATOM   1483 N  NE  . ARG   A 1 183 ? -27.507 2.998   11.028  1.00 13.43 ? 182 ARG   A NE  1 
ATOM   1484 C  CZ  . ARG   A 1 183 ? -28.551 3.720   10.643  1.00 15.36 ? 182 ARG   A CZ  1 
ATOM   1485 N  NH1 . ARG   A 1 183 ? -29.360 4.216   11.538  1.00 17.40 ? 182 ARG   A NH1 1 
ATOM   1486 N  NH2 . ARG   A 1 183 ? -28.764 3.915   9.335   1.00 17.36 ? 182 ARG   A NH2 1 
ATOM   1487 N  N   . GLY   A 1 184 ? -24.277 -1.841  10.373  1.00 8.60  ? 183 GLY   A N   1 
ATOM   1488 C  CA  . GLY   A 1 184 ? -24.325 -3.240  9.998   1.00 9.29  ? 183 GLY   A CA  1 
ATOM   1489 C  C   . GLY   A 1 184 ? -23.174 -4.081  10.541  1.00 9.48  ? 183 GLY   A C   1 
ATOM   1490 O  O   . GLY   A 1 184 ? -23.140 -5.267  10.266  1.00 10.74 ? 183 GLY   A O   1 
ATOM   1491 N  N   . LEU   A 1 185 ? -22.234 -3.465  11.272  1.00 9.05  ? 184 LEU   A N   1 
ATOM   1492 C  CA  . LEU   A 1 185 ? -21.114 -4.177  11.869  1.00 8.94  ? 184 LEU   A CA  1 
ATOM   1493 C  C   . LEU   A 1 185 ? -21.271 -4.384  13.368  1.00 8.81  ? 184 LEU   A C   1 
ATOM   1494 O  O   . LEU   A 1 185 ? -20.372 -4.937  13.999  1.00 9.99  ? 184 LEU   A O   1 
ATOM   1495 C  CB  . LEU   A 1 185 ? -19.820 -3.430  11.594  1.00 9.13  ? 184 LEU   A CB  1 
ATOM   1496 C  CG  . LEU   A 1 185 ? -19.498 -3.328  10.107  1.00 10.15 ? 184 LEU   A CG  1 
ATOM   1497 C  CD1 . LEU   A 1 185 ? -18.253 -2.552  9.829   1.00 10.91 ? 184 LEU   A CD1 1 
ATOM   1498 C  CD2 . LEU   A 1 185 ? -19.410 -4.670  9.414   1.00 11.28 ? 184 LEU   A CD2 1 
ATOM   1499 N  N   . LEU   A 1 186 ? -22.375 -3.926  13.993  1.00 8.74  ? 185 LEU   A N   1 
ATOM   1500 C  CA  . LEU   A 1 186 ? -22.527 -3.956  15.439  1.00 9.27  ? 185 LEU   A CA  1 
ATOM   1501 C  C   . LEU   A 1 186 ? -23.283 -5.203  15.878  1.00 9.96  ? 185 LEU   A C   1 
ATOM   1502 O  O   . LEU   A 1 186 ? -24.327 -5.559  15.335  1.00 13.20 ? 185 LEU   A O   1 
ATOM   1503 C  CB  . LEU   A 1 186 ? -23.314 -2.723  15.939  1.00 9.27  ? 185 LEU   A CB  1 
ATOM   1504 C  CG  . LEU   A 1 186 ? -22.741 -1.361  15.548  1.00 9.42  ? 185 LEU   A CG  1 
ATOM   1505 C  CD1 . LEU   A 1 186 ? -23.630 -0.202  15.991  1.00 9.71  ? 185 LEU   A CD1 1 
ATOM   1506 C  CD2 . LEU   A 1 186 ? -21.329 -1.198  16.072  1.00 10.31 ? 185 LEU   A CD2 1 
ATOM   1507 N  N   . PRO   A 1 187 ? -22.901 -5.821  17.002  1.00 9.10  ? 186 PRO   A N   1 
ATOM   1508 C  CA  . PRO   A 1 187 ? -23.665 -6.936  17.566  1.00 9.43  ? 186 PRO   A CA  1 
ATOM   1509 C  C   . PRO   A 1 187 ? -24.944 -6.381  18.168  1.00 9.06  ? 186 PRO   A C   1 
ATOM   1510 O  O   . PRO   A 1 187 ? -25.150 -5.173  18.262  1.00 9.58  ? 186 PRO   A O   1 
ATOM   1511 C  CB  . PRO   A 1 187 ? -22.737 -7.533  18.557  1.00 9.23  ? 186 PRO   A CB  1 
ATOM   1512 C  CG  . PRO   A 1 187 ? -21.998 -6.342  19.041  1.00 8.63  ? 186 PRO   A CG  1 
ATOM   1513 C  CD  . PRO   A 1 187 ? -21.767 -5.430  17.832  1.00 8.54  ? 186 PRO   A CD  1 
ATOM   1514 N  N   . GLU   A 1 188 ? -25.788 -7.291  18.631  1.00 9.90  ? 187 GLU   A N   1 
ATOM   1515 C  CA  . GLU   A 1 188 ? -27.046 -6.926  19.265  1.00 10.24 ? 187 GLU   A CA  1 
ATOM   1516 C  C   . GLU   A 1 188 ? -26.844 -6.160  20.570  1.00 9.46  ? 187 GLU   A C   1 
ATOM   1517 O  O   . GLU   A 1 188 ? -27.490 -5.134  20.825  1.00 10.62 ? 187 GLU   A O   1 
ATOM   1518 C  CB  . GLU   A 1 188 ? -27.770 -8.243  19.581  1.00 12.79 ? 187 GLU   A CB  1 
ATOM   1519 C  CG  . GLU   A 1 188 ? -29.080 -8.156  20.315  1.00 16.23 ? 187 GLU   A CG  1 
ATOM   1520 C  CD  . GLU   A 1 188 ? -29.646 -9.499  20.723  1.00 18.16 ? 187 GLU   A CD  1 
ATOM   1521 O  OE1 . GLU   A 1 188 ? -29.473 -10.384 19.916  1.00 19.20 ? 187 GLU   A OE1 1 
ATOM   1522 O  OE2 . GLU   A 1 188 ? -30.329 -9.565  21.775  1.00 21.86 ? 187 GLU   A OE2 1 
ATOM   1523 N  N   . SER   A 1 189 ? -25.969 -6.679  21.434  1.00 8.51  ? 188 SER   A N   1 
ATOM   1524 C  CA  . SER   A 1 189 ? -25.734 -6.100  22.744  1.00 9.03  ? 188 SER   A CA  1 
ATOM   1525 C  C   . SER   A 1 189 ? -24.609 -5.089  22.685  1.00 8.94  ? 188 SER   A C   1 
ATOM   1526 O  O   . SER   A 1 189 ? -23.558 -5.348  22.101  1.00 9.35  ? 188 SER   A O   1 
ATOM   1527 C  CB  . SER   A 1 189 ? -25.339 -7.183  23.727  1.00 9.80  ? 188 SER   A CB  1 
ATOM   1528 O  OG  . SER   A 1 189 ? -25.080 -6.659  25.025  1.00 10.47 ? 188 SER   A OG  1 
ATOM   1529 N  N   . LEU   A 1 190 ? -24.738 -4.011  23.483  1.00 9.10  ? 189 LEU   A N   1 
ATOM   1530 C  CA  . LEU   A 1 190 ? -23.669 -3.039  23.693  1.00 9.75  ? 189 LEU   A CA  1 
ATOM   1531 C  C   . LEU   A 1 190 ? -22.976 -3.239  25.040  1.00 9.40  ? 189 LEU   A C   1 
ATOM   1532 O  O   . LEU   A 1 190 ? -22.268 -2.344  25.463  1.00 11.51 ? 189 LEU   A O   1 
ATOM   1533 C  CB  . LEU   A 1 190 ? -24.183 -1.606  23.530  1.00 10.96 ? 189 LEU   A CB  1 
ATOM   1534 C  CG  . LEU   A 1 190 ? -24.686 -1.192  22.142  1.00 11.53 ? 189 LEU   A CG  1 
ATOM   1535 C  CD1 . LEU   A 1 190 ? -25.200 0.251   22.169  1.00 12.58 ? 189 LEU   A CD1 1 
ATOM   1536 C  CD2 . LEU   A 1 190 ? -23.600 -1.395  21.083  1.00 12.54 ? 189 LEU   A CD2 1 
ATOM   1537 N  N   . ASP   A 1 191 ? -23.143 -4.356  25.708  1.00 8.75  ? 190 ASP   A N   1 
ATOM   1538 C  CA  . ASP   A 1 191 ? -22.384 -4.618  26.926  1.00 8.89  ? 190 ASP   A CA  1 
ATOM   1539 C  C   . ASP   A 1 191 ? -20.902 -4.565  26.615  1.00 7.83  ? 190 ASP   A C   1 
ATOM   1540 O  O   . ASP   A 1 191 ? -20.468 -5.077  25.580  1.00 7.58  ? 190 ASP   A O   1 
ATOM   1541 C  CB  . ASP   A 1 191 ? -22.755 -5.980  27.496  1.00 10.45 ? 190 ASP   A CB  1 
ATOM   1542 C  CG  . ASP   A 1 191 ? -24.141 -6.133  28.128  1.00 12.97 ? 190 ASP   A CG  1 
ATOM   1543 O  OD1 . ASP   A 1 191 ? -24.765 -5.108  28.384  1.00 15.16 ? 190 ASP   A OD1 1 
ATOM   1544 O  OD2 . ASP   A 1 191 ? -24.549 -7.276  28.350  1.00 16.54 ? 190 ASP   A OD2 1 
ATOM   1545 N  N   . TYR   A 1 192 ? -20.129 -3.976  27.532  1.00 6.89  ? 191 TYR   A N   1 
ATOM   1546 C  CA  . TYR   A 1 192 ? -18.731 -3.726  27.207  1.00 6.77  ? 191 TYR   A CA  1 
ATOM   1547 C  C   . TYR   A 1 192 ? -17.834 -3.773  28.442  1.00 6.26  ? 191 TYR   A C   1 
ATOM   1548 O  O   . TYR   A 1 192 ? -18.291 -3.650  29.576  1.00 6.74  ? 191 TYR   A O   1 
ATOM   1549 C  CB  . TYR   A 1 192 ? -18.603 -2.363  26.501  1.00 7.48  ? 191 TYR   A CB  1 
ATOM   1550 C  CG  . TYR   A 1 192 ? -18.973 -1.174  27.366  1.00 7.35  ? 191 TYR   A CG  1 
ATOM   1551 C  CD1 . TYR   A 1 192 ? -18.065 -0.565  28.211  1.00 7.97  ? 191 TYR   A CD1 1 
ATOM   1552 C  CD2 . TYR   A 1 192 ? -20.234 -0.640  27.323  1.00 7.76  ? 191 TYR   A CD2 1 
ATOM   1553 C  CE1 . TYR   A 1 192 ? -18.418 0.490   29.016  1.00 8.31  ? 191 TYR   A CE1 1 
ATOM   1554 C  CE2 . TYR   A 1 192 ? -20.620 0.450   28.093  1.00 8.27  ? 191 TYR   A CE2 1 
ATOM   1555 C  CZ  . TYR   A 1 192 ? -19.697 0.989   28.975  1.00 8.61  ? 191 TYR   A CZ  1 
ATOM   1556 O  OH  . TYR   A 1 192 ? -20.036 2.017   29.811  1.00 9.90  ? 191 TYR   A OH  1 
ATOM   1557 N  N   . TRP   A 1 193 ? -16.560 -3.883  28.156  1.00 5.92  ? 192 TRP   A N   1 
ATOM   1558 C  CA  . TRP   A 1 193 ? -15.480 -3.615  29.092  1.00 5.80  ? 192 TRP   A CA  1 
ATOM   1559 C  C   . TRP   A 1 193 ? -14.779 -2.318  28.673  1.00 5.71  ? 192 TRP   A C   1 
ATOM   1560 O  O   . TRP   A 1 193 ? -14.714 -1.993  27.490  1.00 6.74  ? 192 TRP   A O   1 
ATOM   1561 C  CB  . TRP   A 1 193 ? -14.437 -4.741  29.087  1.00 6.23  ? 192 TRP   A CB  1 
ATOM   1562 C  CG  . TRP   A 1 193 ? -14.970 -6.080  29.492  1.00 6.33  ? 192 TRP   A CG  1 
ATOM   1563 C  CD1 . TRP   A 1 193 ? -15.191 -6.510  30.751  1.00 6.84  ? 192 TRP   A CD1 1 
ATOM   1564 C  CD2 . TRP   A 1 193 ? -15.235 -7.199  28.618  1.00 6.77  ? 192 TRP   A CD2 1 
ATOM   1565 N  NE1 . TRP   A 1 193 ? -15.626 -7.815  30.754  1.00 7.43  ? 192 TRP   A NE1 1 
ATOM   1566 C  CE2 . TRP   A 1 193 ? -15.657 -8.258  29.452  1.00 7.33  ? 192 TRP   A CE2 1 
ATOM   1567 C  CE3 . TRP   A 1 193 ? -15.129 -7.399  27.237  1.00 7.18  ? 192 TRP   A CE3 1 
ATOM   1568 C  CZ2 . TRP   A 1 193 ? -15.956 -9.512  28.906  1.00 7.94  ? 192 TRP   A CZ2 1 
ATOM   1569 C  CZ3 . TRP   A 1 193 ? -15.415 -8.646  26.742  1.00 8.04  ? 192 TRP   A CZ3 1 
ATOM   1570 C  CH2 . TRP   A 1 193 ? -15.803 -9.669  27.562  1.00 8.50  ? 192 TRP   A CH2 1 
ATOM   1571 N  N   . THR   A 1 194 ? -14.223 -1.591  29.638  1.00 5.38  ? 193 THR   A N   1 
ATOM   1572 C  CA  . THR   A 1 194 ? -13.523 -0.353  29.302  1.00 5.61  ? 193 THR   A CA  1 
ATOM   1573 C  C   . THR   A 1 194 ? -12.278 -0.189  30.184  1.00 5.79  ? 193 THR   A C   1 
ATOM   1574 O  O   . THR   A 1 194 ? -12.247 -0.581  31.350  1.00 6.51  ? 193 THR   A O   1 
ATOM   1575 C  CB  . THR   A 1 194 ? -14.458 0.852   29.430  1.00 6.02  ? 193 THR   A CB  1 
ATOM   1576 O  OG1 . THR   A 1 194 ? -13.783 2.040   28.986  1.00 6.19  ? 193 THR   A OG1 1 
ATOM   1577 C  CG2 . THR   A 1 194 ? -15.004 1.092   30.818  1.00 6.43  ? 193 THR   A CG2 1 
ATOM   1578 N  N   . TYR   A 1 195 ? -11.249 0.416   29.590  1.00 5.56  ? 194 TYR   A N   1 
ATOM   1579 C  CA  . TYR   A 1 195 ? -10.002 0.714   30.288  1.00 5.53  ? 194 TYR   A CA  1 
ATOM   1580 C  C   . TYR   A 1 195 ? -9.261  1.770   29.502  1.00 5.38  ? 194 TYR   A C   1 
ATOM   1581 O  O   . TYR   A 1 195 ? -9.462  1.941   28.295  1.00 5.38  ? 194 TYR   A O   1 
ATOM   1582 C  CB  . TYR   A 1 195 ? -9.161  -0.561  30.478  1.00 5.33  ? 194 TYR   A CB  1 
ATOM   1583 C  CG  . TYR   A 1 195 ? -8.473  -1.047  29.213  1.00 5.34  ? 194 TYR   A CG  1 
ATOM   1584 C  CD1 . TYR   A 1 195 ? -9.139  -1.745  28.239  1.00 5.15  ? 194 TYR   A CD1 1 
ATOM   1585 C  CD2 . TYR   A 1 195 ? -7.169  -0.691  29.004  1.00 5.26  ? 194 TYR   A CD2 1 
ATOM   1586 C  CE1 . TYR   A 1 195 ? -8.530  -2.094  27.052  1.00 5.04  ? 194 TYR   A CE1 1 
ATOM   1587 C  CE2 . TYR   A 1 195 ? -6.535  -1.051  27.841  1.00 5.18  ? 194 TYR   A CE2 1 
ATOM   1588 C  CZ  . TYR   A 1 195 ? -7.200  -1.733  26.850  1.00 5.13  ? 194 TYR   A CZ  1 
ATOM   1589 O  OH  . TYR   A 1 195 ? -6.532  -2.030  25.677  1.00 5.23  ? 194 TYR   A OH  1 
ATOM   1590 N  N   . PRO   A 1 196 ? -8.316  2.470   30.175  1.00 5.76  ? 195 PRO   A N   1 
ATOM   1591 C  CA  . PRO   A 1 196 ? -7.489  3.471   29.473  1.00 5.84  ? 195 PRO   A CA  1 
ATOM   1592 C  C   . PRO   A 1 196 ? -6.285  2.813   28.828  1.00 5.36  ? 195 PRO   A C   1 
ATOM   1593 O  O   . PRO   A 1 196 ? -5.547  2.041   29.475  1.00 5.89  ? 195 PRO   A O   1 
ATOM   1594 C  CB  . PRO   A 1 196 ? -7.012  4.407   30.603  1.00 6.46  ? 195 PRO   A CB  1 
ATOM   1595 C  CG  . PRO   A 1 196 ? -6.967  3.494   31.808  1.00 6.68  ? 195 PRO   A CG  1 
ATOM   1596 C  CD  . PRO   A 1 196 ? -8.097  2.497   31.624  1.00 6.80  ? 195 PRO   A CD  1 
ATOM   1597 N  N   . GLY   A 1 197 ? -6.040  3.082   27.552  1.00 5.14  ? 196 GLY   A N   1 
ATOM   1598 C  CA  . GLY   A 1 197 ? -4.931  2.472   26.837  1.00 5.12  ? 196 GLY   A CA  1 
ATOM   1599 C  C   . GLY   A 1 197 ? -4.398  3.363   25.751  1.00 4.98  ? 196 GLY   A C   1 
ATOM   1600 O  O   . GLY   A 1 197 ? -4.324  4.592   25.854  1.00 5.25  ? 196 GLY   A O   1 
ATOM   1601 N  N   . SER   A 1 198 ? -3.978  2.702   24.678  1.00 5.09  ? 197 SER   A N   1 
ATOM   1602 C  CA  . SER   A 1 198 ? -3.167  3.324   23.628  1.00 5.02  ? 197 SER   A CA  1 
ATOM   1603 C  C   . SER   A 1 198 ? -3.667  2.923   22.237  1.00 4.96  ? 197 SER   A C   1 
ATOM   1604 O  O   . SER   A 1 198 ? -4.426  1.959   22.083  1.00 4.89  ? 197 SER   A O   1 
ATOM   1605 C  CB  . SER   A 1 198 ? -1.702  2.951   23.761  1.00 5.09  ? 197 SER   A CB  1 
ATOM   1606 O  OG  . SER   A 1 198 ? -1.436  1.599   23.332  1.00 5.31  ? 197 SER   A OG  1 
ATOM   1607 N  N   . LEU   A 1 199 ? -3.115  3.599   21.230  1.00 5.22  ? 198 LEU   A N   1 
ATOM   1608 C  CA  . LEU   A 1 199 ? -3.137  3.068   19.876  1.00 5.65  ? 198 LEU   A CA  1 
ATOM   1609 C  C   . LEU   A 1 199 ? -2.386  1.754   19.880  1.00 5.65  ? 198 LEU   A C   1 
ATOM   1610 O  O   . LEU   A 1 199 ? -1.374  1.585   20.589  1.00 5.58  ? 198 LEU   A O   1 
ATOM   1611 C  CB  . LEU   A 1 199 ? -2.434  4.029   18.922  1.00 6.48  ? 198 LEU   A CB  1 
ATOM   1612 C  CG  . LEU   A 1 199 ? -2.992  5.434   18.837  1.00 7.89  ? 198 LEU   A CG  1 
ATOM   1613 C  CD1 . LEU   A 1 199 ? -2.150  6.277   17.896  1.00 8.71  ? 198 LEU   A CD1 1 
ATOM   1614 C  CD2 . LEU   A 1 199 ? -4.436  5.462   18.430  1.00 8.61  ? 198 LEU   A CD2 1 
ATOM   1615 N  N   . THR   A 1 200 ? -2.816  0.787   19.061  1.00 5.56  ? 199 THR   A N   1 
ATOM   1616 C  CA  . THR   A 1 200 ? -2.166  -0.513  18.995  1.00 5.53  ? 199 THR   A CA  1 
ATOM   1617 C  C   . THR   A 1 200 ? -1.163  -0.598  17.877  1.00 5.74  ? 199 THR   A C   1 
ATOM   1618 O  O   . THR   A 1 200 ? -0.506  -1.638  17.713  1.00 5.93  ? 199 THR   A O   1 
ATOM   1619 C  CB  . THR   A 1 200 ? -3.135  -1.690  18.916  1.00 5.46  ? 199 THR   A CB  1 
ATOM   1620 O  OG1 . THR   A 1 200 ? -3.777  -1.651  17.646  1.00 5.89  ? 199 THR   A OG1 1 
ATOM   1621 C  CG2 . THR   A 1 200 ? -4.141  -1.678  20.071  1.00 5.93  ? 199 THR   A CG2 1 
ATOM   1622 N  N   . THR   A 1 201 ? -1.044  0.446   17.044  1.00 6.84  ? 200 THR   A N   1 
ATOM   1623 C  CA  . THR   A 1 201 ? 0.038   0.561   16.060  1.00 7.93  ? 200 THR   A CA  1 
ATOM   1624 C  C   . THR   A 1 201 ? 0.826   1.806   16.373  1.00 7.89  ? 200 THR   A C   1 
ATOM   1625 O  O   . THR   A 1 201 ? 0.291   2.762   16.964  1.00 7.75  ? 200 THR   A O   1 
ATOM   1626 C  CB  . THR   A 1 201 ? -0.417  0.680   14.624  1.00 9.49  ? 200 THR   A CB  1 
ATOM   1627 O  OG1 . THR   A 1 201 ? -1.241  1.813   14.462  1.00 11.77 ? 200 THR   A OG1 1 
ATOM   1628 C  CG2 . THR   A 1 201 ? -1.243  -0.501  14.197  1.00 10.97 ? 200 THR   A CG2 1 
ATOM   1629 N  N   . PRO   A 1 202 ? 2.104   1.867   15.943  1.00 8.30  ? 201 PRO   A N   1 
ATOM   1630 C  CA  . PRO   A 1 202 ? 2.849   3.119   15.966  1.00 8.87  ? 201 PRO   A CA  1 
ATOM   1631 C  C   . PRO   A 1 202 ? 1.989   4.261   15.451  1.00 9.61  ? 201 PRO   A C   1 
ATOM   1632 O  O   . PRO   A 1 202 ? 1.297   4.118   14.444  1.00 10.93 ? 201 PRO   A O   1 
ATOM   1633 C  CB  . PRO   A 1 202 ? 4.091   2.796   15.139  1.00 9.53  ? 201 PRO   A CB  1 
ATOM   1634 C  CG  . PRO   A 1 202 ? 4.316   1.348   15.402  1.00 9.35  ? 201 PRO   A CG  1 
ATOM   1635 C  CD  . PRO   A 1 202 ? 2.900   0.786   15.357  1.00 8.43  ? 201 PRO   A CD  1 
ATOM   1636 N  N   . PRO   A 1 203 ? 1.944   5.410   16.133  1.00 9.44  ? 202 PRO   A N   1 
ATOM   1637 C  CA  . PRO   A 1 203 ? 2.876   5.809   17.182  1.00 9.24  ? 202 PRO   A CA  1 
ATOM   1638 C  C   . PRO   A 1 203 ? 2.566   5.368   18.612  1.00 7.87  ? 202 PRO   A C   1 
ATOM   1639 O  O   . PRO   A 1 203 ? 3.227   5.838   19.531  1.00 8.62  ? 202 PRO   A O   1 
ATOM   1640 C  CB  . PRO   A 1 203 ? 2.895   7.344   17.009  1.00 9.93  ? 202 PRO   A CB  1 
ATOM   1641 C  CG  . PRO   A 1 203 ? 1.510   7.651   16.587  1.00 10.48 ? 202 PRO   A CG  1 
ATOM   1642 C  CD  . PRO   A 1 203 ? 1.155   6.534   15.630  1.00 10.14 ? 202 PRO   A CD  1 
ATOM   1643 N  N   . LEU   A 1 204 ? 1.556   4.500   18.813  1.00 7.07  ? 203 LEU   A N   1 
ATOM   1644 C  CA  . LEU   A 1 204 ? 1.342   3.839   20.111  1.00 6.19  ? 203 LEU   A CA  1 
ATOM   1645 C  C   . LEU   A 1 204 ? 0.984   4.864   21.208  1.00 6.22  ? 203 LEU   A C   1 
ATOM   1646 O  O   . LEU   A 1 204 ? 1.159   4.624   22.390  1.00 6.53  ? 203 LEU   A O   1 
ATOM   1647 C  CB  . LEU   A 1 204 ? 2.524   2.980   20.554  1.00 6.44  ? 203 LEU   A CB  1 
ATOM   1648 C  CG  . LEU   A 1 204 ? 2.883   1.845   19.615  1.00 6.66  ? 203 LEU   A CG  1 
ATOM   1649 C  CD1 . LEU   A 1 204 ? 4.174   1.174   20.061  1.00 7.16  ? 203 LEU   A CD1 1 
ATOM   1650 C  CD2 . LEU   A 1 204 ? 1.794   0.780   19.453  1.00 6.96  ? 203 LEU   A CD2 1 
ATOM   1651 N  N   . LEU   A 1 205 ? 0.377   5.971   20.803  1.00 6.39  ? 204 LEU   A N   1 
ATOM   1652 C  CA  . LEU   A 1 205 ? 0.118   7.058   21.707  1.00 6.92  ? 204 LEU   A CA  1 
ATOM   1653 C  C   . LEU   A 1 205 ? -0.921  6.660   22.734  1.00 6.44  ? 204 LEU   A C   1 
ATOM   1654 O  O   . LEU   A 1 205 ? -1.901  5.957   22.464  1.00 6.33  ? 204 LEU   A O   1 
ATOM   1655 C  CB  . LEU   A 1 205 ? -0.357  8.305   20.956  1.00 7.79  ? 204 LEU   A CB  1 
ATOM   1656 C  CG  . LEU   A 1 205 ? 0.679   8.906   20.001  1.00 8.80  ? 204 LEU   A CG  1 
ATOM   1657 C  CD1 . LEU   A 1 205 ? 0.090   9.922   19.090  1.00 9.49  ? 204 LEU   A CD1 1 
ATOM   1658 C  CD2 . LEU   A 1 205 ? 1.822   9.538   20.784  1.00 10.19 ? 204 LEU   A CD2 1 
ATOM   1659 N  N   . GLU   A 1 206 ? -0.731  7.131   23.964  1.00 6.48  ? 205 GLU   A N   1 
ATOM   1660 C  CA  . GLU   A 1 206 ? -1.552  6.757   25.116  1.00 6.53  ? 205 GLU   A CA  1 
ATOM   1661 C  C   . GLU   A 1 206 ? -2.722  7.729   25.282  1.00 6.44  ? 205 GLU   A C   1 
ATOM   1662 O  O   . GLU   A 1 206 ? -2.824  8.476   26.248  1.00 7.67  ? 205 GLU   A O   1 
ATOM   1663 C  CB  . GLU   A 1 206 ? -0.638  6.635   26.360  1.00 7.05  ? 205 GLU   A CB  1 
ATOM   1664 C  CG  . GLU   A 1 206 ? 0.258   5.409   26.231  1.00 7.29  ? 205 GLU   A CG  1 
ATOM   1665 C  CD  . GLU   A 1 206 ? 1.193   5.127   27.386  1.00 7.90  ? 205 GLU   A CD  1 
ATOM   1666 O  OE1 . GLU   A 1 206 ? 1.523   6.083   28.130  1.00 9.71  ? 205 GLU   A OE1 1 
ATOM   1667 O  OE2 . GLU   A 1 206 ? 1.610   3.959   27.536  1.00 8.12  ? 205 GLU   A OE2 1 
ATOM   1668 N  N   . CYS   A 1 207 ? -3.639  7.660   24.317  1.00 5.79  ? 206 CYS   A N   1 
ATOM   1669 C  CA  . CYS   A 1 207 ? -4.712  8.635   24.166  1.00 6.04  ? 206 CYS   A CA  1 
ATOM   1670 C  C   . CYS   A 1 207 ? -6.071  7.997   24.046  1.00 5.82  ? 206 CYS   A C   1 
ATOM   1671 O  O   . CYS   A 1 207 ? -7.021  8.703   23.728  1.00 6.99  ? 206 CYS   A O   1 
ATOM   1672 C  CB  . CYS   A 1 207 ? -4.432  9.479   22.907  1.00 6.79  ? 206 CYS   A CB  1 
ATOM   1673 S  SG  . CYS   A 1 207 ? -4.384  8.489   21.369  1.00 7.53  ? 206 CYS   A SG  1 
ATOM   1674 N  N   . VAL   A 1 208 ? -6.209  6.689   24.312  1.00 5.49  ? 207 VAL   A N   1 
ATOM   1675 C  CA  . VAL   A 1 208 ? -7.423  5.965   23.987  1.00 5.37  ? 207 VAL   A CA  1 
ATOM   1676 C  C   . VAL   A 1 208 ? -8.185  5.547   25.245  1.00 5.24  ? 207 VAL   A C   1 
ATOM   1677 O  O   . VAL   A 1 208 ? -7.644  4.856   26.111  1.00 6.30  ? 207 VAL   A O   1 
ATOM   1678 C  CB  . VAL   A 1 208 ? -7.129  4.713   23.141  1.00 5.47  ? 207 VAL   A CB  1 
ATOM   1679 C  CG1 . VAL   A 1 208 ? -8.429  3.997   22.797  1.00 5.46  ? 207 VAL   A CG1 1 
ATOM   1680 C  CG2 . VAL   A 1 208 ? -6.362  5.050   21.857  1.00 5.81  ? 207 VAL   A CG2 1 
ATOM   1681 N  N   . THR   A 1 209 ? -9.490  5.848   25.266  1.00 5.27  ? 208 THR   A N   1 
ATOM   1682 C  CA  . THR   A 1 209 ? -10.438 5.116   26.099  1.00 5.44  ? 208 THR   A CA  1 
ATOM   1683 C  C   . THR   A 1 209 ? -10.950 3.954   25.259  1.00 5.15  ? 208 THR   A C   1 
ATOM   1684 O  O   . THR   A 1 209 ? -11.645 4.147   24.262  1.00 5.42  ? 208 THR   A O   1 
ATOM   1685 C  CB  . THR   A 1 209 ? -11.572 6.006   26.570  1.00 5.94  ? 208 THR   A CB  1 
ATOM   1686 O  OG1 . THR   A 1 209 ? -11.060 7.101   27.313  1.00 6.62  ? 208 THR   A OG1 1 
ATOM   1687 C  CG2 . THR   A 1 209 ? -12.527 5.209   27.411  1.00 6.55  ? 208 THR   A CG2 1 
ATOM   1688 N  N   . TRP   A 1 210 ? -10.568 2.742   25.669  1.00 4.80  ? 209 TRP   A N   1 
ATOM   1689 C  CA  . TRP   A 1 210 ? -11.038 1.538   24.980  1.00 4.72  ? 209 TRP   A CA  1 
ATOM   1690 C  C   . TRP   A 1 210 ? -12.400 1.123   25.502  1.00 4.65  ? 209 TRP   A C   1 
ATOM   1691 O  O   . TRP   A 1 210 ? -12.624 1.071   26.708  1.00 5.08  ? 209 TRP   A O   1 
ATOM   1692 C  CB  . TRP   A 1 210 ? -10.044 0.386   25.200  1.00 4.73  ? 209 TRP   A CB  1 
ATOM   1693 C  CG  . TRP   A 1 210 ? -8.891  0.504   24.240  1.00 4.72  ? 209 TRP   A CG  1 
ATOM   1694 C  CD1 . TRP   A 1 210 ? -7.673  1.069   24.463  1.00 5.17  ? 209 TRP   A CD1 1 
ATOM   1695 C  CD2 . TRP   A 1 210 ? -8.912  0.093   22.873  1.00 4.98  ? 209 TRP   A CD2 1 
ATOM   1696 N  NE1 . TRP   A 1 210 ? -6.945  1.055   23.308  1.00 5.34  ? 209 TRP   A NE1 1 
ATOM   1697 C  CE2 . TRP   A 1 210 ? -7.676  0.452   22.323  1.00 5.19  ? 209 TRP   A CE2 1 
ATOM   1698 C  CE3 . TRP   A 1 210 ? -9.855  -0.519  22.055  1.00 4.90  ? 209 TRP   A CE3 1 
ATOM   1699 C  CZ2 . TRP   A 1 210 ? -7.374  0.232   20.995  1.00 5.45  ? 209 TRP   A CZ2 1 
ATOM   1700 C  CZ3 . TRP   A 1 210 ? -9.539  -0.802  20.763  1.00 5.29  ? 209 TRP   A CZ3 1 
ATOM   1701 C  CH2 . TRP   A 1 210 ? -8.316  -0.442  20.243  1.00 5.44  ? 209 TRP   A CH2 1 
ATOM   1702 N  N   . ILE   A 1 211 ? -13.282 0.767   24.572  1.00 4.79  ? 210 ILE   A N   1 
ATOM   1703 C  CA  . ILE   A 1 211 ? -14.616 0.233   24.853  1.00 5.11  ? 210 ILE   A CA  1 
ATOM   1704 C  C   . ILE   A 1 211 ? -14.732 -1.026  24.009  1.00 4.94  ? 210 ILE   A C   1 
ATOM   1705 O  O   . ILE   A 1 211 ? -14.828 -0.952  22.791  1.00 5.68  ? 210 ILE   A O   1 
ATOM   1706 C  CB  . ILE   A 1 211 ? -15.712 1.257   24.501  1.00 5.65  ? 210 ILE   A CB  1 
ATOM   1707 C  CG1 . ILE   A 1 211 ? -15.507 2.553   25.329  1.00 6.32  ? 210 ILE   A CG1 1 
ATOM   1708 C  CG2 . ILE   A 1 211 ? -17.074 0.637   24.712  1.00 5.83  ? 210 ILE   A CG2 1 
ATOM   1709 C  CD1 . ILE   A 1 211 ? -16.367 3.731   24.918  1.00 7.11  ? 210 ILE   A CD1 1 
ATOM   1710 N  N   . VAL   A 1 212 ? -14.599 -2.197  24.658  1.00 5.02  ? 211 VAL   A N   1 
ATOM   1711 C  CA  . VAL   A 1 212 ? -14.531 -3.477  23.949  1.00 5.16  ? 211 VAL   A CA  1 
ATOM   1712 C  C   . VAL   A 1 212 ? -15.844 -4.214  24.227  1.00 5.34  ? 211 VAL   A C   1 
ATOM   1713 O  O   . VAL   A 1 212 ? -16.166 -4.502  25.381  1.00 5.78  ? 211 VAL   A O   1 
ATOM   1714 C  CB  . VAL   A 1 212 ? -13.324 -4.302  24.409  1.00 5.67  ? 211 VAL   A CB  1 
ATOM   1715 C  CG1 . VAL   A 1 212 ? -13.318 -5.675  23.706  1.00 5.85  ? 211 VAL   A CG1 1 
ATOM   1716 C  CG2 . VAL   A 1 212 ? -12.038 -3.535  24.166  1.00 5.86  ? 211 VAL   A CG2 1 
ATOM   1717 N  N   . LEU   A 1 213 ? -16.603 -4.480  23.165  1.00 5.68  ? 212 LEU   A N   1 
ATOM   1718 C  CA  . LEU   A 1 213 ? -17.871 -5.144  23.304  1.00 6.21  ? 212 LEU   A CA  1 
ATOM   1719 C  C   . LEU   A 1 213 ? -17.684 -6.610  23.685  1.00 6.29  ? 212 LEU   A C   1 
ATOM   1720 O  O   . LEU   A 1 213 ? -16.843 -7.313  23.139  1.00 6.98  ? 212 LEU   A O   1 
ATOM   1721 C  CB  . LEU   A 1 213 ? -18.721 -5.008  22.057  1.00 6.54  ? 212 LEU   A CB  1 
ATOM   1722 C  CG  . LEU   A 1 213 ? -19.123 -3.594  21.636  1.00 7.18  ? 212 LEU   A CG  1 
ATOM   1723 C  CD1 . LEU   A 1 213 ? -20.149 -3.619  20.505  1.00 7.93  ? 212 LEU   A CD1 1 
ATOM   1724 C  CD2 . LEU   A 1 213 ? -19.663 -2.780  22.792  1.00 7.68  ? 212 LEU   A CD2 1 
ATOM   1725 N  N   . LYS   A 1 214 ? -18.538 -7.091  24.587  1.00 6.88  ? 213 LYS   A N   1 
ATOM   1726 C  CA  . LYS   A 1 214 ? -18.518 -8.493  24.983  1.00 7.77  ? 213 LYS   A CA  1 
ATOM   1727 C  C   . LYS   A 1 214 ? -18.987 -9.420  23.879  1.00 7.37  ? 213 LYS   A C   1 
ATOM   1728 O  O   . LYS   A 1 214 ? -18.457 -10.521 23.740  1.00 8.92  ? 213 LYS   A O   1 
ATOM   1729 C  CB  . LYS   A 1 214 ? -19.317 -8.695  26.254  1.00 9.51  ? 213 LYS   A CB  1 
ATOM   1730 C  CG  . LYS   A 1 214 ? -19.465 -10.157 26.644  1.00 12.07 ? 213 LYS   A CG  1 
ATOM   1731 C  CD  . LYS   A 1 214 ? -19.912 -10.476 28.049  1.00 14.99 ? 213 LYS   A CD  1 
ATOM   1732 C  CE  . LYS   A 1 214 ? -20.080 -11.953 28.185  1.00 17.83 ? 213 LYS   A CE  1 
ATOM   1733 N  NZ  . LYS   A 1 214 ? -20.521 -12.538 29.432  1.00 21.20 ? 213 LYS   A NZ  1 
ATOM   1734 N  N   . GLU   A 1 215 ? -20.040 -9.054  23.169  1.00 7.29  ? 214 GLU   A N   1 
ATOM   1735 C  CA  . GLU   A 1 215 ? -20.610 -9.920  22.145  1.00 7.21  ? 214 GLU   A CA  1 
ATOM   1736 C  C   . GLU   A 1 215 ? -19.857 -9.816  20.839  1.00 6.87  ? 214 GLU   A C   1 
ATOM   1737 O  O   . GLU   A 1 215 ? -19.779 -8.718  20.269  1.00 6.75  ? 214 GLU   A O   1 
ATOM   1738 C  CB  . GLU   A 1 215 ? -22.071 -9.583  21.924  1.00 7.99  ? 214 GLU   A CB  1 
ATOM   1739 C  CG  . GLU   A 1 215 ? -22.775 -10.528 20.968  1.00 9.75  ? 214 GLU   A CG  1 
ATOM   1740 C  CD  . GLU   A 1 215 ? -24.253 -10.329 20.746  1.00 12.02 ? 214 GLU   A CD  1 
ATOM   1741 O  OE1 . GLU   A 1 215 ? -24.819 -9.356  21.267  1.00 11.96 ? 214 GLU   A OE1 1 
ATOM   1742 O  OE2 . GLU   A 1 215 ? -24.914 -11.351 20.293  1.00 16.62 ? 214 GLU   A OE2 1 
ATOM   1743 N  N   . PRO   A 1 216 ? -19.266 -10.926 20.334  1.00 7.38  ? 215 PRO   A N   1 
ATOM   1744 C  CA  . PRO   A 1 216 ? -18.641 -10.876 19.011  1.00 7.39  ? 215 PRO   A CA  1 
ATOM   1745 C  C   . PRO   A 1 216 ? -19.682 -10.810 17.907  1.00 7.84  ? 215 PRO   A C   1 
ATOM   1746 O  O   . PRO   A 1 216 ? -20.833 -11.191 18.098  1.00 8.79  ? 215 PRO   A O   1 
ATOM   1747 C  CB  . PRO   A 1 216 ? -17.885 -12.186 18.947  1.00 8.08  ? 215 PRO   A CB  1 
ATOM   1748 C  CG  . PRO   A 1 216 ? -18.760 -13.107 19.688  1.00 9.97  ? 215 PRO   A CG  1 
ATOM   1749 C  CD  . PRO   A 1 216 ? -19.229 -12.280 20.911  1.00 8.27  ? 215 PRO   A CD  1 
ATOM   1750 N  N   . ILE   A 1 217 ? -19.267 -10.377 16.714  1.00 7.39  ? 216 ILE   A N   1 
ATOM   1751 C  CA  . ILE   A 1 217 ? -20.039 -10.602 15.513  1.00 7.60  ? 216 ILE   A CA  1 
ATOM   1752 C  C   . ILE   A 1 217 ? -19.469 -11.840 14.838  1.00 7.84  ? 216 ILE   A C   1 
ATOM   1753 O  O   . ILE   A 1 217 ? -18.311 -12.205 15.002  1.00 8.00  ? 216 ILE   A O   1 
ATOM   1754 C  CB  . ILE   A 1 217 ? -20.026 -9.369  14.602  1.00 7.64  ? 216 ILE   A CB  1 
ATOM   1755 C  CG1 . ILE   A 1 217 ? -18.622 -8.994  14.110  1.00 7.91  ? 216 ILE   A CG1 1 
ATOM   1756 C  CG2 . ILE   A 1 217 ? -20.698 -8.163  15.283  1.00 8.25  ? 216 ILE   A CG2 1 
ATOM   1757 C  CD1 . ILE   A 1 217 ? -18.624 -7.985  12.954  1.00 8.51  ? 216 ILE   A CD1 1 
ATOM   1758 N  N   A SER   A 1 218 ? -20.333 -12.477 14.050  0.35 8.01  ? 217 SER   A N   1 
ATOM   1759 N  N   B SER   A 1 218 ? -20.318 -12.569 14.119  0.35 8.27  ? 217 SER   A N   1 
ATOM   1760 N  N   C SER   A 1 218 ? -20.334 -12.484 14.056  0.30 8.12  ? 217 SER   A N   1 
ATOM   1761 C  CA  A SER   A 1 218 ? -19.987 -13.632 13.241  0.35 8.01  ? 217 SER   A CA  1 
ATOM   1762 C  CA  B SER   A 1 218 ? -19.831 -13.672 13.301  0.35 8.51  ? 217 SER   A CA  1 
ATOM   1763 C  CA  C SER   A 1 218 ? -19.978 -13.638 13.248  0.30 8.24  ? 217 SER   A CA  1 
ATOM   1764 C  C   A SER   A 1 218 ? -19.741 -13.180 11.807  0.35 8.05  ? 217 SER   A C   1 
ATOM   1765 C  C   B SER   A 1 218 ? -19.764 -13.267 11.836  0.35 8.29  ? 217 SER   A C   1 
ATOM   1766 C  C   C SER   A 1 218 ? -19.741 -13.185 11.814  0.30 8.18  ? 217 SER   A C   1 
ATOM   1767 O  O   A SER   A 1 218 ? -20.532 -12.399 11.252  0.35 8.47  ? 217 SER   A O   1 
ATOM   1768 O  O   B SER   A 1 218 ? -20.718 -12.689 11.293  0.35 8.59  ? 217 SER   A O   1 
ATOM   1769 O  O   C SER   A 1 218 ? -20.533 -12.402 11.268  0.30 8.54  ? 217 SER   A O   1 
ATOM   1770 C  CB  A SER   A 1 218 ? -21.078 -14.685 13.303  0.35 8.08  ? 217 SER   A CB  1 
ATOM   1771 C  CB  B SER   A 1 218 ? -20.631 -14.931 13.473  0.35 8.98  ? 217 SER   A CB  1 
ATOM   1772 C  CB  C SER   A 1 218 ? -21.054 -14.703 13.317  0.30 8.45  ? 217 SER   A CB  1 
ATOM   1773 O  OG  A SER   A 1 218 ? -21.093 -15.354 14.558  0.35 8.32  ? 217 SER   A OG  1 
ATOM   1774 O  OG  B SER   A 1 218 ? -22.003 -14.711 13.227  0.35 9.75  ? 217 SER   A OG  1 
ATOM   1775 O  OG  C SER   A 1 218 ? -20.669 -15.872 12.604  0.30 8.98  ? 217 SER   A OG  1 
ATOM   1776 N  N   . VAL   A 1 219 ? -18.652 -13.682 11.221  1.00 8.16  ? 218 VAL   A N   1 
ATOM   1777 C  CA  . VAL   A 1 219 ? -18.390 -13.480 9.800   1.00 8.17  ? 218 VAL   A CA  1 
ATOM   1778 C  C   . VAL   A 1 219 ? -18.114 -14.853 9.214   1.00 8.14  ? 218 VAL   A C   1 
ATOM   1779 O  O   . VAL   A 1 219 ? -17.772 -15.788 9.938   1.00 8.49  ? 218 VAL   A O   1 
ATOM   1780 C  CB  . VAL   A 1 219 ? -17.190 -12.547 9.594   1.00 8.67  ? 218 VAL   A CB  1 
ATOM   1781 C  CG1 . VAL   A 1 219 ? -17.432 -11.197 10.250  1.00 9.12  ? 218 VAL   A CG1 1 
ATOM   1782 C  CG2 . VAL   A 1 219 ? -15.884 -13.171 10.085  1.00 8.89  ? 218 VAL   A CG2 1 
ATOM   1783 N  N   . SER   A 1 220 ? -18.251 -14.993 7.895   1.00 7.86  ? 219 SER   A N   1 
ATOM   1784 C  CA  . SER   A 1 220 ? -18.082 -16.308 7.313   1.00 8.30  ? 219 SER   A CA  1 
ATOM   1785 C  C   . SER   A 1 220 ? -16.603 -16.558 7.020   1.00 8.37  ? 219 SER   A C   1 
ATOM   1786 O  O   . SER   A 1 220 ? -15.789 -15.634 6.921   1.00 8.47  ? 219 SER   A O   1 
ATOM   1787 C  CB  . SER   A 1 220 ? -18.888 -16.491 6.069   1.00 8.49  ? 219 SER   A CB  1 
ATOM   1788 O  OG  . SER   A 1 220 ? -18.423 -15.598 5.096   1.00 9.19  ? 219 SER   A OG  1 
ATOM   1789 N  N   A SER   A 1 221 ? -16.292 -17.826 6.887   0.50 8.95  ? 220 SER   A N   1 
ATOM   1790 N  N   B SER   A 1 221 ? -16.235 -17.825 6.841   0.50 8.63  ? 220 SER   A N   1 
ATOM   1791 C  CA  A SER   A 1 221 ? -14.961 -18.222 6.499   0.50 9.96  ? 220 SER   A CA  1 
ATOM   1792 C  CA  B SER   A 1 221 ? -14.886 -18.213 6.430   0.50 9.16  ? 220 SER   A CA  1 
ATOM   1793 C  C   A SER   A 1 221 ? -14.567 -17.492 5.214   0.50 9.64  ? 220 SER   A C   1 
ATOM   1794 C  C   B SER   A 1 221 ? -14.516 -17.538 5.108   0.50 9.25  ? 220 SER   A C   1 
ATOM   1795 O  O   A SER   A 1 221 ? -13.460 -16.966 5.166   0.50 9.96  ? 220 SER   A O   1 
ATOM   1796 O  O   B SER   A 1 221 ? -13.378 -17.190 4.820   0.50 9.39  ? 220 SER   A O   1 
ATOM   1797 C  CB  A SER   A 1 221 ? -14.886 -19.705 6.366   0.50 11.04 ? 220 SER   A CB  1 
ATOM   1798 C  CB  B SER   A 1 221 ? -14.766 -19.730 6.305   0.50 9.66  ? 220 SER   A CB  1 
ATOM   1799 O  OG  A SER   A 1 221 ? -13.525 -20.062 6.217   0.50 12.65 ? 220 SER   A OG  1 
ATOM   1800 O  OG  B SER   A 1 221 ? -15.809 -20.319 5.526   0.50 9.56  ? 220 SER   A OG  1 
ATOM   1801 N  N   . GLU   A 1 222 ? -15.478 -17.402 4.217   1.00 9.41  ? 221 GLU   A N   1 
ATOM   1802 C  CA  . GLU   A 1 222 ? -15.220 -16.774 2.936   1.00 10.22 ? 221 GLU   A CA  1 
ATOM   1803 C  C   . GLU   A 1 222 ? -14.891 -15.308 3.111   1.00 9.56  ? 221 GLU   A C   1 
ATOM   1804 O  O   . GLU   A 1 222 ? -14.064 -14.747 2.382   1.00 9.90  ? 221 GLU   A O   1 
ATOM   1805 C  CB  . GLU   A 1 222 ? -16.370 -16.985 1.972   1.00 11.78 ? 221 GLU   A CB  1 
ATOM   1806 C  CG  . GLU   A 1 222 ? -16.581 -18.425 1.563   1.00 13.72 ? 221 GLU   A CG  1 
ATOM   1807 C  CD  . GLU   A 1 222 ? -17.507 -19.165 2.496   1.00 15.09 ? 221 GLU   A CD  1 
ATOM   1808 O  OE1 . GLU   A 1 222 ? -18.070 -18.661 3.455   1.00 16.19 ? 221 GLU   A OE1 1 
ATOM   1809 O  OE2 . GLU   A 1 222 ? -17.697 -20.384 2.200   1.00 19.82 ? 221 GLU   A OE2 1 
ATOM   1810 N  N   . GLN   A 1 223 ? -15.588 -14.636 4.036   1.00 8.59  ? 222 GLN   A N   1 
ATOM   1811 C  CA  . GLN   A 1 223 ? -15.341 -13.217 4.262   1.00 8.23  ? 222 GLN   A CA  1 
ATOM   1812 C  C   . GLN   A 1 223 ? -13.916 -13.000 4.792   1.00 8.50  ? 222 GLN   A C   1 
ATOM   1813 O  O   . GLN   A 1 223 ? -13.188 -12.137 4.313   1.00 8.91  ? 222 GLN   A O   1 
ATOM   1814 C  CB  . GLN   A 1 223 ? -16.397 -12.635 5.204   1.00 7.86  ? 222 GLN   A CB  1 
ATOM   1815 C  CG  . GLN   A 1 223 ? -17.759 -12.533 4.539   1.00 7.73  ? 222 GLN   A CG  1 
ATOM   1816 C  CD  . GLN   A 1 223 ? -18.859 -11.974 5.406   1.00 7.83  ? 222 GLN   A CD  1 
ATOM   1817 O  OE1 . GLN   A 1 223 ? -18.996 -12.347 6.561   1.00 8.09  ? 222 GLN   A OE1 1 
ATOM   1818 N  NE2 . GLN   A 1 223 ? -19.687 -11.119 4.829   1.00 8.14  ? 222 GLN   A NE2 1 
ATOM   1819 N  N   . VAL   A 1 224 ? -13.522 -13.769 5.813   1.00 8.75  ? 223 VAL   A N   1 
ATOM   1820 C  CA  . VAL   A 1 224 ? -12.181 -13.571 6.369   1.00 9.90  ? 223 VAL   A CA  1 
ATOM   1821 C  C   . VAL   A 1 224 ? -11.101 -14.010 5.356   1.00 9.60  ? 223 VAL   A C   1 
ATOM   1822 O  O   . VAL   A 1 224 ? -10.019 -13.447 5.304   1.00 9.71  ? 223 VAL   A O   1 
ATOM   1823 C  CB  . VAL   A 1 224 ? -12.014 -14.200 7.767   1.00 11.75 ? 223 VAL   A CB  1 
ATOM   1824 C  CG1 . VAL   A 1 224 ? -12.055 -15.687 7.730   1.00 13.07 ? 223 VAL   A CG1 1 
ATOM   1825 C  CG2 . VAL   A 1 224 ? -10.766 -13.633 8.445   1.00 12.51 ? 223 VAL   A CG2 1 
ATOM   1826 N  N   . LEU   A 1 225 ? -11.396 -15.040 4.555   1.00 10.31 ? 224 LEU   A N   1 
ATOM   1827 C  CA  . LEU   A 1 225 ? -10.444 -15.450 3.523   1.00 11.42 ? 224 LEU   A CA  1 
ATOM   1828 C  C   . LEU   A 1 225 ? -10.127 -14.300 2.570   1.00 10.84 ? 224 LEU   A C   1 
ATOM   1829 O  O   . LEU   A 1 225 ? -8.990  -14.173 2.122   1.00 11.17 ? 224 LEU   A O   1 
ATOM   1830 C  CB  . LEU   A 1 225 ? -10.939 -16.691 2.780   1.00 13.37 ? 224 LEU   A CB  1 
ATOM   1831 C  CG  . LEU   A 1 225 ? -10.759 -18.004 3.558   1.00 15.83 ? 224 LEU   A CG  1 
ATOM   1832 C  CD1 . LEU   A 1 225 ? -11.645 -19.134 3.032   1.00 17.06 ? 224 LEU   A CD1 1 
ATOM   1833 C  CD2 . LEU   A 1 225 ? -9.292  -18.414 3.615   1.00 16.47 ? 224 LEU   A CD2 1 
ATOM   1834 N  N   . LYS   A 1 226 ? -11.115 -13.471 2.267   1.00 10.13 ? 225 LYS   A N   1 
ATOM   1835 C  CA  . LYS   A 1 226 ? -10.870 -12.330 1.410   1.00 10.36 ? 225 LYS   A CA  1 
ATOM   1836 C  C   . LYS   A 1 226 ? -9.984  -11.297 2.081   1.00 8.91  ? 225 LYS   A C   1 
ATOM   1837 O  O   . LYS   A 1 226 ? -9.209  -10.656 1.399   1.00 9.42  ? 225 LYS   A O   1 
ATOM   1838 C  CB  . LYS   A 1 226 ? -12.182 -11.818 0.832   1.00 11.95 ? 225 LYS   A CB  1 
ATOM   1839 C  CG  . LYS   A 1 226 ? -12.735 -12.920 -0.110  1.00 14.86 ? 225 LYS   A CG  1 
ATOM   1840 C  CD  . LYS   A 1 226 ? -14.018 -12.612 -0.846  1.00 16.99 ? 225 LYS   A CD  1 
ATOM   1841 C  CE  . LYS   A 1 226 ? -14.528 -13.694 -1.742  1.00 18.65 ? 225 LYS   A CE  1 
ATOM   1842 N  NZ  . LYS   A 1 226 ? -15.725 -13.283 -2.475  1.00 19.50 ? 225 LYS   A NZ  1 
ATOM   1843 N  N   . PHE   A 1 227 ? -10.137 -11.088 3.380   1.00 8.40  ? 226 PHE   A N   1 
ATOM   1844 C  CA  . PHE   A 1 227 ? -9.202  -10.227 4.060   1.00 8.09  ? 226 PHE   A CA  1 
ATOM   1845 C  C   . PHE   A 1 227 ? -7.757  -10.678 3.866   1.00 7.75  ? 226 PHE   A C   1 
ATOM   1846 O  O   . PHE   A 1 227 ? -6.850  -9.866  3.671   1.00 7.64  ? 226 PHE   A O   1 
ATOM   1847 C  CB  . PHE   A 1 227 ? -9.446  -10.176 5.559   1.00 8.59  ? 226 PHE   A CB  1 
ATOM   1848 C  CG  . PHE   A 1 227 ? -10.636 -9.384  6.112   1.00 9.19  ? 226 PHE   A CG  1 
ATOM   1849 C  CD1 . PHE   A 1 227 ? -11.749 -9.018  5.377   1.00 11.13 ? 226 PHE   A CD1 1 
ATOM   1850 C  CD2 . PHE   A 1 227 ? -10.695 -9.123  7.500   1.00 11.26 ? 226 PHE   A CD2 1 
ATOM   1851 C  CE1 . PHE   A 1 227 ? -12.789 -8.315  5.937   1.00 11.60 ? 226 PHE   A CE1 1 
ATOM   1852 C  CE2 . PHE   A 1 227 ? -11.753 -8.446  8.064   1.00 12.25 ? 226 PHE   A CE2 1 
ATOM   1853 C  CZ  . PHE   A 1 227 ? -12.755 -7.967  7.257   1.00 11.93 ? 226 PHE   A CZ  1 
ATOM   1854 N  N   . ARG   A 1 228 ? -7.554  -11.999 3.898   1.00 7.44  ? 227 ARG   A N   1 
ATOM   1855 C  CA  . ARG   A 1 228 ? -6.224  -12.583 3.842   1.00 7.96  ? 227 ARG   A CA  1 
ATOM   1856 C  C   . ARG   A 1 228 ? -5.637  -12.567 2.445   1.00 8.33  ? 227 ARG   A C   1 
ATOM   1857 O  O   . ARG   A 1 228 ? -4.485  -12.957 2.298   1.00 9.23  ? 227 ARG   A O   1 
ATOM   1858 C  CB  . ARG   A 1 228 ? -6.281  -14.020 4.367   1.00 8.16  ? 227 ARG   A CB  1 
ATOM   1859 C  CG  . ARG   A 1 228 ? -6.744  -14.145 5.819   1.00 7.98  ? 227 ARG   A CG  1 
ATOM   1860 C  CD  . ARG   A 1 228 ? -6.795  -15.597 6.258   1.00 8.89  ? 227 ARG   A CD  1 
ATOM   1861 N  NE  . ARG   A 1 228 ? -7.258  -15.753 7.621   1.00 9.10  ? 227 ARG   A NE  1 
ATOM   1862 C  CZ  . ARG   A 1 228 ? -8.134  -16.652 8.043   1.00 10.28 ? 227 ARG   A CZ  1 
ATOM   1863 N  NH1 . ARG   A 1 228 ? -8.590  -17.539 7.189   1.00 12.05 ? 227 ARG   A NH1 1 
ATOM   1864 N  NH2 . ARG   A 1 228 ? -8.569  -16.639 9.277   1.00 10.98 ? 227 ARG   A NH2 1 
ATOM   1865 N  N   . LYS   A 1 229 ? -6.366  -12.093 1.437   1.00 8.34  ? 228 LYS   A N   1 
ATOM   1866 C  CA  . LYS   A 1 229 ? -5.832  -11.917 0.099   1.00 9.14  ? 228 LYS   A CA  1 
ATOM   1867 C  C   . LYS   A 1 229 ? -5.250  -10.543 -0.147  1.00 8.17  ? 228 LYS   A C   1 
ATOM   1868 O  O   . LYS   A 1 229 ? -4.610  -10.338 -1.167  1.00 9.13  ? 228 LYS   A O   1 
ATOM   1869 C  CB  . LYS   A 1 229 ? -6.911  -12.194 -0.956  1.00 10.86 ? 228 LYS   A CB  1 
ATOM   1870 C  CG  . LYS   A 1 229 ? -7.385  -13.620 -1.005  1.00 13.94 ? 228 LYS   A CG  1 
ATOM   1871 C  CD  . LYS   A 1 229 ? -8.456  -13.958 -2.032  1.00 17.25 ? 228 LYS   A CD  1 
ATOM   1872 C  CE  . LYS   A 1 229 ? -8.951  -15.358 -1.786  1.00 20.41 ? 228 LYS   A CE  1 
ATOM   1873 N  NZ  . LYS   A 1 229 ? -9.585  -16.024 -2.917  1.00 23.29 ? 228 LYS   A NZ  1 
ATOM   1874 N  N   . LEU   A 1 230 ? -5.476  -9.633  0.794   1.00 7.65  ? 229 LEU   A N   1 
ATOM   1875 C  CA  . LEU   A 1 230 ? -4.837  -8.332  0.717   1.00 7.58  ? 229 LEU   A CA  1 
ATOM   1876 C  C   . LEU   A 1 230 ? -3.322  -8.485  0.810   1.00 7.14  ? 229 LEU   A C   1 
ATOM   1877 O  O   . LEU   A 1 230 ? -2.807  -9.515  1.221   1.00 7.58  ? 229 LEU   A O   1 
ATOM   1878 C  CB  . LEU   A 1 230 ? -5.338  -7.437  1.819   1.00 7.55  ? 229 LEU   A CB  1 
ATOM   1879 C  CG  . LEU   A 1 230 ? -6.774  -6.944  1.634   1.00 8.04  ? 229 LEU   A CG  1 
ATOM   1880 C  CD1 . LEU   A 1 230 ? -7.314  -6.380  2.907   1.00 8.44  ? 229 LEU   A CD1 1 
ATOM   1881 C  CD2 . LEU   A 1 230 ? -6.886  -5.889  0.526   1.00 8.89  ? 229 LEU   A CD2 1 
ATOM   1882 N  N   . ASN   A 1 231 ? -2.607  -7.424  0.423   1.00 7.42  ? 230 ASN   A N   1 
ATOM   1883 C  CA  . ASN   A 1 231 ? -1.150  -7.388  0.437   1.00 7.54  ? 230 ASN   A CA  1 
ATOM   1884 C  C   . ASN   A 1 231 ? -0.632  -6.239  1.299   1.00 7.34  ? 230 ASN   A C   1 
ATOM   1885 O  O   . ASN   A 1 231 ? -1.116  -5.130  1.248   1.00 7.88  ? 230 ASN   A O   1 
ATOM   1886 C  CB  . ASN   A 1 231 ? -0.600  -7.163  -0.971  1.00 8.25  ? 230 ASN   A CB  1 
ATOM   1887 C  CG  . ASN   A 1 231 ? -0.665  -8.317  -1.937  1.00 9.65  ? 230 ASN   A CG  1 
ATOM   1888 O  OD1 . ASN   A 1 231 ? -0.156  -8.172  -3.062  1.00 11.28 ? 230 ASN   A OD1 1 
ATOM   1889 N  ND2 . ASN   A 1 231 ? -1.217  -9.446  -1.559  1.00 9.72  ? 230 ASN   A ND2 1 
ATOM   1890 N  N   . PHE   A 1 232 ? 0.440   -6.537  2.045   1.00 7.69  ? 231 PHE   A N   1 
ATOM   1891 C  CA  . PHE   A 1 232 ? 1.198   -5.492  2.725   1.00 8.30  ? 231 PHE   A CA  1 
ATOM   1892 C  C   . PHE   A 1 232 ? 1.993   -4.640  1.734   1.00 8.93  ? 231 PHE   A C   1 
ATOM   1893 O  O   . PHE   A 1 232 ? 2.273   -3.473  1.990   1.00 9.67  ? 231 PHE   A O   1 
ATOM   1894 C  CB  . PHE   A 1 232 ? 2.172   -6.094  3.729   1.00 8.59  ? 231 PHE   A CB  1 
ATOM   1895 C  CG  . PHE   A 1 232 ? 1.625   -6.697  4.997   1.00 8.37  ? 231 PHE   A CG  1 
ATOM   1896 C  CD1 . PHE   A 1 232 ? 0.881   -5.922  5.860   1.00 8.40  ? 231 PHE   A CD1 1 
ATOM   1897 C  CD2 . PHE   A 1 232 ? 1.961   -7.993  5.381   1.00 8.47  ? 231 PHE   A CD2 1 
ATOM   1898 C  CE1 . PHE   A 1 232 ? 0.466   -6.430  7.086   1.00 8.77  ? 231 PHE   A CE1 1 
ATOM   1899 C  CE2 . PHE   A 1 232 ? 1.558   -8.485  6.601   1.00 8.39  ? 231 PHE   A CE2 1 
ATOM   1900 C  CZ  . PHE   A 1 232 ? 0.811   -7.714  7.467   1.00 8.53  ? 231 PHE   A CZ  1 
ATOM   1901 N  N   . ASN   A 1 233 ? 2.495   -5.282  0.688   1.00 9.37  ? 232 ASN   A N   1 
ATOM   1902 C  CA  . ASN   A 1 233 ? 3.342   -4.675  -0.330  1.00 10.14 ? 232 ASN   A CA  1 
ATOM   1903 C  C   . ASN   A 1 233 ? 2.573   -3.746  -1.268  1.00 9.63  ? 232 ASN   A C   1 
ATOM   1904 O  O   . ASN   A 1 233 ? 1.361   -3.859  -1.422  1.00 9.68  ? 232 ASN   A O   1 
ATOM   1905 C  CB  . ASN   A 1 233 ? 4.056   -5.755  -1.118  1.00 11.03 ? 232 ASN   A CB  1 
ATOM   1906 C  CG  . ASN   A 1 233 ? 3.037   -6.672  -1.716  1.00 10.69 ? 232 ASN   A CG  1 
ATOM   1907 O  OD1 . ASN   A 1 233 ? 2.541   -7.573  -1.042  1.00 11.39 ? 232 ASN   A OD1 1 
ATOM   1908 N  ND2 . ASN   A 1 233 ? 2.698   -6.538  -2.985  1.00 11.74 ? 232 ASN   A ND2 1 
ATOM   1909 N  N   . GLY   A 1 234 ? 3.348   -2.901  -1.951  1.00 10.46 ? 233 GLY   A N   1 
ATOM   1910 C  CA  . GLY   A 1 234 ? 2.835   -2.119  -3.049  1.00 10.59 ? 233 GLY   A CA  1 
ATOM   1911 C  C   . GLY   A 1 234 ? 2.776   -2.918  -4.353  1.00 10.81 ? 233 GLY   A C   1 
ATOM   1912 O  O   . GLY   A 1 234 ? 3.381   -3.992  -4.492  1.00 12.43 ? 233 GLY   A O   1 
ATOM   1913 N  N   . GLU   A 1 235 ? 2.004   -2.386  -5.300  1.00 10.73 ? 234 GLU   A N   1 
ATOM   1914 C  CA  . GLU   A 1 235 ? 1.920   -3.003  -6.617  1.00 11.58 ? 234 GLU   A CA  1 
ATOM   1915 C  C   . GLU   A 1 235 ? 3.310   -3.072  -7.238  1.00 12.82 ? 234 GLU   A C   1 
ATOM   1916 O  O   . GLU   A 1 235 ? 4.097   -2.138  -7.161  1.00 13.76 ? 234 GLU   A O   1 
ATOM   1917 C  CB  . GLU   A 1 235 ? 0.975   -2.186  -7.502  1.00 11.87 ? 234 GLU   A CB  1 
ATOM   1918 C  CG  . GLU   A 1 235 ? 0.681   -2.768  -8.892  1.00 12.62 ? 234 GLU   A CG  1 
ATOM   1919 C  CD  . GLU   A 1 235 ? -0.389  -2.026  -9.681  1.00 15.33 ? 234 GLU   A CD  1 
ATOM   1920 O  OE1 . GLU   A 1 235 ? -0.604  -0.801  -9.458  1.00 16.61 ? 234 GLU   A OE1 1 
ATOM   1921 O  OE2 . GLU   A 1 235 ? -1.009  -2.675  -10.561 1.00 19.53 ? 234 GLU   A OE2 1 
ATOM   1922 N  N   . GLY   A 1 236 ? 3.615   -4.189  -7.895  1.00 14.64 ? 235 GLY   A N   1 
ATOM   1923 C  CA  . GLY   A 1 236 ? 4.911   -4.355  -8.526  1.00 16.92 ? 235 GLY   A CA  1 
ATOM   1924 C  C   . GLY   A 1 236 ? 6.051   -4.747  -7.588  1.00 18.07 ? 235 GLY   A C   1 
ATOM   1925 O  O   . GLY   A 1 236 ? 7.193   -4.957  -8.033  1.00 21.77 ? 235 GLY   A O   1 
ATOM   1926 N  N   . GLU   A 1 237 ? 5.695   -5.010  -6.331  1.00 18.23 ? 236 GLU   A N   1 
ATOM   1927 C  CA  . GLU   A 1 237 ? 6.636   -5.557  -5.370  1.00 18.84 ? 236 GLU   A CA  1 
ATOM   1928 C  C   . GLU   A 1 237 ? 6.288   -7.000  -5.040  1.00 19.52 ? 236 GLU   A C   1 
ATOM   1929 O  O   . GLU   A 1 237 ? 5.164   -7.453  -5.304  1.00 20.81 ? 236 GLU   A O   1 
ATOM   1930 C  CB  . GLU   A 1 237 ? 6.575   -4.780  -4.065  1.00 20.70 ? 236 GLU   A CB  1 
ATOM   1931 C  CG  . GLU   A 1 237 ? 6.964   -3.318  -4.207  1.00 22.12 ? 236 GLU   A CG  1 
ATOM   1932 C  CD  . GLU   A 1 237 ? 6.815   -2.533  -2.924  1.00 24.61 ? 236 GLU   A CD  1 
ATOM   1933 O  OE1 . GLU   A 1 237 ? 6.213   -3.045  -1.957  1.00 23.66 ? 236 GLU   A OE1 1 
ATOM   1934 O  OE2 . GLU   A 1 237 ? 7.358   -1.410  -2.948  1.00 28.04 ? 236 GLU   A OE2 1 
ATOM   1935 N  N   . PRO   A 1 238 ? 7.249   -7.768  -4.465  1.00 20.54 ? 237 PRO   A N   1 
ATOM   1936 C  CA  . PRO   A 1 238 ? 6.980   -9.150  -4.080  1.00 19.88 ? 237 PRO   A CA  1 
ATOM   1937 C  C   . PRO   A 1 238 ? 5.769   -9.250  -3.156  1.00 17.47 ? 237 PRO   A C   1 
ATOM   1938 O  O   . PRO   A 1 238 ? 5.666   -8.491  -2.209  1.00 18.49 ? 237 PRO   A O   1 
ATOM   1939 C  CB  . PRO   A 1 238 ? 8.270   -9.577  -3.387  1.00 21.30 ? 237 PRO   A CB  1 
ATOM   1940 C  CG  . PRO   A 1 238 ? 9.336   -8.706  -4.021  1.00 21.99 ? 237 PRO   A CG  1 
ATOM   1941 C  CD  . PRO   A 1 238 ? 8.662   -7.393  -4.243  1.00 21.80 ? 237 PRO   A CD  1 
ATOM   1942 N  N   . GLU   A 1 239 ? 4.946   -10.253 -3.398  1.00 16.35 ? 238 GLU   A N   1 
ATOM   1943 C  CA  . GLU   A 1 239 ? 3.682   -10.343 -2.688  1.00 15.01 ? 238 GLU   A CA  1 
ATOM   1944 C  C   . GLU   A 1 239 ? 3.904   -10.870 -1.282  1.00 12.99 ? 238 GLU   A C   1 
ATOM   1945 O  O   . GLU   A 1 239 ? 4.466   -11.952 -1.085  1.00 13.32 ? 238 GLU   A O   1 
ATOM   1946 C  CB  . GLU   A 1 239 ? 2.704   -11.282 -3.389  1.00 17.05 ? 238 GLU   A CB  1 
ATOM   1947 C  CG  . GLU   A 1 239 ? 1.315   -11.267 -2.774  1.00 18.32 ? 238 GLU   A CG  1 
ATOM   1948 C  CD  . GLU   A 1 239 ? 0.226   -12.013 -3.529  1.00 19.95 ? 238 GLU   A CD  1 
ATOM   1949 O  OE1 . GLU   A 1 239 ? 0.570   -12.948 -4.291  1.00 23.63 ? 238 GLU   A OE1 1 
ATOM   1950 O  OE2 . GLU   A 1 239 ? -0.964  -11.715 -3.356  1.00 17.27 ? 238 GLU   A OE2 1 
ATOM   1951 N  N   . GLU   A 1 240 ? 3.388   -10.133 -0.318  1.00 11.01 ? 239 GLU   A N   1 
ATOM   1952 C  CA  . GLU   A 1 240 ? 3.378   -10.508 1.069   1.00 11.37 ? 239 GLU   A CA  1 
ATOM   1953 C  C   . GLU   A 1 240 ? 1.963   -10.333 1.577   1.00 9.49  ? 239 GLU   A C   1 
ATOM   1954 O  O   . GLU   A 1 240 ? 1.451   -9.218  1.668   1.00 10.73 ? 239 GLU   A O   1 
ATOM   1955 C  CB  . GLU   A 1 240 ? 4.354   -9.697  1.903   1.00 13.96 ? 239 GLU   A CB  1 
ATOM   1956 C  CG  . GLU   A 1 240 ? 4.588   -10.423 3.238   1.00 16.79 ? 239 GLU   A CG  1 
ATOM   1957 C  CD  . GLU   A 1 240 ? 4.980   -11.934 3.374   1.00 18.75 ? 239 GLU   A CD  1 
ATOM   1958 O  OE1 . GLU   A 1 240 ? 5.390   -12.757 2.468   1.00 21.56 ? 239 GLU   A OE1 1 
ATOM   1959 O  OE2 . GLU   A 1 240 ? 4.907   -12.344 4.553   1.00 23.21 ? 239 GLU   A OE2 1 
ATOM   1960 N  N   . LEU   A 1 241 ? 1.304   -11.448 1.872   1.00 8.34  ? 240 LEU   A N   1 
ATOM   1961 C  CA  . LEU   A 1 241 ? -0.095  -11.372 2.261   1.00 8.24  ? 240 LEU   A CA  1 
ATOM   1962 C  C   . LEU   A 1 241 ? -0.238  -10.567 3.551   1.00 7.64  ? 240 LEU   A C   1 
ATOM   1963 O  O   . LEU   A 1 241 ? 0.516   -10.743 4.513   1.00 8.00  ? 240 LEU   A O   1 
ATOM   1964 C  CB  . LEU   A 1 241 ? -0.649  -12.770 2.473   1.00 8.90  ? 240 LEU   A CB  1 
ATOM   1965 C  CG  . LEU   A 1 241 ? -0.677  -13.692 1.255   1.00 10.14 ? 240 LEU   A CG  1 
ATOM   1966 C  CD1 . LEU   A 1 241 ? -1.273  -15.040 1.645   1.00 11.07 ? 240 LEU   A CD1 1 
ATOM   1967 C  CD2 . LEU   A 1 241 ? -1.535  -13.082 0.156   1.00 10.31 ? 240 LEU   A CD2 1 
ATOM   1968 N  N   . MET   A 1 242 ? -1.284  -9.745  3.581   1.00 7.02  ? 241 MET   A N   1 
ATOM   1969 C  CA  . MET   A 1 242 ? -1.650  -8.955  4.741   1.00 7.07  ? 241 MET   A CA  1 
ATOM   1970 C  C   . MET   A 1 242 ? -2.433  -9.863  5.685   1.00 6.74  ? 241 MET   A C   1 
ATOM   1971 O  O   . MET   A 1 242 ? -3.646  -9.999  5.573   1.00 7.13  ? 241 MET   A O   1 
ATOM   1972 C  CB  . MET   A 1 242 ? -2.480  -7.744  4.328   1.00 7.24  ? 241 MET   A CB  1 
ATOM   1973 C  CG  . MET   A 1 242 ? -2.816  -6.818  5.470   1.00 7.43  ? 241 MET   A CG  1 
ATOM   1974 S  SD  . MET   A 1 242 ? -3.811  -5.403  4.997   1.00 8.10  ? 241 MET   A SD  1 
ATOM   1975 C  CE  . MET   A 1 242 ? -2.519  -4.348  4.323   1.00 8.40  ? 241 MET   A CE  1 
ATOM   1976 N  N   . VAL   A 1 243 ? -1.679  -10.508 6.576   1.00 6.38  ? 242 VAL   A N   1 
ATOM   1977 C  CA  . VAL   A 1 243 ? -2.225  -11.392 7.606   1.00 6.54  ? 242 VAL   A CA  1 
ATOM   1978 C  C   . VAL   A 1 243 ? -1.422  -11.167 8.863   1.00 6.18  ? 242 VAL   A C   1 
ATOM   1979 O  O   . VAL   A 1 243 ? -0.274  -10.743 8.846   1.00 6.67  ? 242 VAL   A O   1 
ATOM   1980 C  CB  . VAL   A 1 243 ? -2.151  -12.877 7.212   1.00 7.26  ? 242 VAL   A CB  1 
ATOM   1981 C  CG1 . VAL   A 1 243 ? -3.068  -13.160 6.042   1.00 7.96  ? 242 VAL   A CG1 1 
ATOM   1982 C  CG2 . VAL   A 1 243 ? -0.720  -13.345 6.894   1.00 7.65  ? 242 VAL   A CG2 1 
ATOM   1983 N  N   . ASP   A 1 244 ? -2.014  -11.506 10.021  1.00 6.05  ? 243 ASP   A N   1 
ATOM   1984 C  CA  . ASP   A 1 244 ? -1.351  -11.403 11.299  1.00 6.15  ? 243 ASP   A CA  1 
ATOM   1985 C  C   . ASP   A 1 244 ? -0.867  -9.982  11.557  1.00 5.68  ? 243 ASP   A C   1 
ATOM   1986 O  O   . ASP   A 1 244 ? 0.201   -9.743  12.096  1.00 6.38  ? 243 ASP   A O   1 
ATOM   1987 C  CB  . ASP   A 1 244 ? -0.280  -12.467 11.481  1.00 6.36  ? 243 ASP   A CB  1 
ATOM   1988 C  CG  . ASP   A 1 244 ? -0.855  -13.863 11.540  1.00 7.00  ? 243 ASP   A CG  1 
ATOM   1989 O  OD1 . ASP   A 1 244 ? -1.888  -14.063 12.223  1.00 6.88  ? 243 ASP   A OD1 1 
ATOM   1990 O  OD2 . ASP   A 1 244 ? -0.261  -14.762 10.908  1.00 8.10  ? 243 ASP   A OD2 1 
ATOM   1991 N  N   . ASN   A 1 245 ? -1.753  -9.022  11.287  1.00 5.29  ? 244 ASN   A N   1 
ATOM   1992 C  CA  . ASN   A 1 245 ? -1.500  -7.617  11.542  1.00 5.37  ? 244 ASN   A CA  1 
ATOM   1993 C  C   . ASN   A 1 245 ? -2.066  -7.181  12.893  1.00 5.17  ? 244 ASN   A C   1 
ATOM   1994 O  O   . ASN   A 1 245 ? -2.740  -6.146  13.033  1.00 5.97  ? 244 ASN   A O   1 
ATOM   1995 C  CB  . ASN   A 1 245 ? -2.030  -6.746  10.421  1.00 5.74  ? 244 ASN   A CB  1 
ATOM   1996 C  CG  . ASN   A 1 245 ? -3.513  -6.912  10.188  1.00 6.43  ? 244 ASN   A CG  1 
ATOM   1997 O  OD1 . ASN   A 1 245 ? -4.174  -7.793  10.735  1.00 6.48  ? 244 ASN   A OD1 1 
ATOM   1998 N  ND2 . ASN   A 1 245 ? -4.083  -6.022  9.410   1.00 7.91  ? 244 ASN   A ND2 1 
ATOM   1999 N  N   . TRP   A 1 246 ? -1.769  -7.991  13.932  1.00 4.94  ? 245 TRP   A N   1 
ATOM   2000 C  CA  . TRP   A 1 246 ? -2.214  -7.744  15.299  1.00 4.98  ? 245 TRP   A CA  1 
ATOM   2001 C  C   . TRP   A 1 246 ? -0.996  -7.637  16.221  1.00 5.08  ? 245 TRP   A C   1 
ATOM   2002 O  O   . TRP   A 1 246 ? -0.032  -8.383  16.085  1.00 5.81  ? 245 TRP   A O   1 
ATOM   2003 C  CB  . TRP   A 1 246 ? -3.163  -8.862  15.759  1.00 5.33  ? 245 TRP   A CB  1 
ATOM   2004 C  CG  . TRP   A 1 246 ? -2.674  -10.272 15.581  1.00 5.65  ? 245 TRP   A CG  1 
ATOM   2005 C  CD1 . TRP   A 1 246 ? -2.801  -11.028 14.450  1.00 5.65  ? 245 TRP   A CD1 1 
ATOM   2006 C  CD2 . TRP   A 1 246 ? -2.025  -11.124 16.538  1.00 6.10  ? 245 TRP   A CD2 1 
ATOM   2007 N  NE1 . TRP   A 1 246 ? -2.260  -12.258 14.608  1.00 5.97  ? 245 TRP   A NE1 1 
ATOM   2008 C  CE2 . TRP   A 1 246 ? -1.769  -12.353 15.884  1.00 6.34  ? 245 TRP   A CE2 1 
ATOM   2009 C  CE3 . TRP   A 1 246 ? -1.690  -10.965 17.876  1.00 6.68  ? 245 TRP   A CE3 1 
ATOM   2010 C  CZ2 . TRP   A 1 246 ? -1.163  -13.419 16.544  1.00 7.12  ? 245 TRP   A CZ2 1 
ATOM   2011 C  CZ3 . TRP   A 1 246 ? -1.101  -12.031 18.520  1.00 7.44  ? 245 TRP   A CZ3 1 
ATOM   2012 C  CH2 . TRP   A 1 246 ? -0.841  -13.244 17.862  1.00 7.56  ? 245 TRP   A CH2 1 
ATOM   2013 N  N   . ARG   A 1 247 ? -1.126  -6.765  17.193  1.00 5.11  ? 246 ARG   A N   1 
ATOM   2014 C  CA  . ARG   A 1 247 ? -0.198  -6.638  18.303  1.00 5.63  ? 246 ARG   A CA  1 
ATOM   2015 C  C   . ARG   A 1 247 ? -0.681  -7.545  19.427  1.00 5.92  ? 246 ARG   A C   1 
ATOM   2016 O  O   . ARG   A 1 247 ? -1.880  -7.550  19.716  1.00 6.14  ? 246 ARG   A O   1 
ATOM   2017 C  CB  . ARG   A 1 247 ? -0.144  -5.186  18.805  1.00 5.58  ? 246 ARG   A CB  1 
ATOM   2018 C  CG  . ARG   A 1 247 ? 0.966   -4.916  19.801  1.00 5.55  ? 246 ARG   A CG  1 
ATOM   2019 C  CD  . ARG   A 1 247 ? 0.888   -3.541  20.417  1.00 5.91  ? 246 ARG   A CD  1 
ATOM   2020 N  NE  . ARG   A 1 247 ? 2.113   -3.268  21.164  1.00 6.34  ? 246 ARG   A NE  1 
ATOM   2021 C  CZ  . ARG   A 1 247 ? 2.315   -2.251  21.975  1.00 6.47  ? 246 ARG   A CZ  1 
ATOM   2022 N  NH1 . ARG   A 1 247 ? 1.335   -1.447  22.318  1.00 6.82  ? 246 ARG   A NH1 1 
ATOM   2023 N  NH2 . ARG   A 1 247 ? 3.541   -1.992  22.415  1.00 7.18  ? 246 ARG   A NH2 1 
ATOM   2024 N  N   . PRO   A 1 248 ? 0.210   -8.302  20.089  1.00 6.47  ? 247 PRO   A N   1 
ATOM   2025 C  CA  . PRO   A 1 248 ? -0.225  -9.153  21.188  1.00 6.78  ? 247 PRO   A CA  1 
ATOM   2026 C  C   . PRO   A 1 248 ? -0.526  -8.320  22.436  1.00 6.32  ? 247 PRO   A C   1 
ATOM   2027 O  O   . PRO   A 1 248 ? -0.191  -7.142  22.558  1.00 6.38  ? 247 PRO   A O   1 
ATOM   2028 C  CB  . PRO   A 1 248 ? 0.946   -10.081 21.413  1.00 7.79  ? 247 PRO   A CB  1 
ATOM   2029 C  CG  . PRO   A 1 248 ? 2.135   -9.267  21.023  1.00 8.35  ? 247 PRO   A CG  1 
ATOM   2030 C  CD  . PRO   A 1 248 ? 1.645   -8.468  19.814  1.00 7.41  ? 247 PRO   A CD  1 
ATOM   2031 N  N   . ALA   A 1 249 ? -1.162  -8.970  23.404  1.00 6.74  ? 248 ALA   A N   1 
ATOM   2032 C  CA  . ALA   A 1 249 ? -1.489  -8.342  24.678  1.00 6.76  ? 248 ALA   A CA  1 
ATOM   2033 C  C   . ALA   A 1 249 ? -0.248  -7.831  25.389  1.00 6.81  ? 248 ALA   A C   1 
ATOM   2034 O  O   . ALA   A 1 249 ? 0.791   -8.477  25.433  1.00 7.32  ? 248 ALA   A O   1 
ATOM   2035 C  CB  . ALA   A 1 249 ? -2.245  -9.333  25.567  1.00 7.34  ? 248 ALA   A CB  1 
ATOM   2036 N  N   . GLN   A 1 250 ? -0.409  -6.637  25.967  1.00 6.61  ? 249 GLN   A N   1 
ATOM   2037 C  CA  . GLN   A 1 250 ? 0.619   -5.907  26.693  1.00 7.06  ? 249 GLN   A CA  1 
ATOM   2038 C  C   . GLN   A 1 250 ? 0.313   -5.944  28.183  1.00 7.58  ? 249 GLN   A C   1 
ATOM   2039 O  O   . GLN   A 1 250 ? -0.826  -6.169  28.593  1.00 7.94  ? 249 GLN   A O   1 
ATOM   2040 C  CB  . GLN   A 1 250 ? 0.650   -4.468  26.194  1.00 7.42  ? 249 GLN   A CB  1 
ATOM   2041 C  CG  . GLN   A 1 250 ? 0.948   -4.374  24.706  1.00 8.02  ? 249 GLN   A CG  1 
ATOM   2042 C  CD  . GLN   A 1 250 ? 2.255   -5.024  24.355  1.00 8.27  ? 249 GLN   A CD  1 
ATOM   2043 O  OE1 . GLN   A 1 250 ? 3.308   -4.710  24.923  1.00 9.97  ? 249 GLN   A OE1 1 
ATOM   2044 N  NE2 . GLN   A 1 250 ? 2.255   -5.952  23.432  1.00 8.32  ? 249 GLN   A NE2 1 
ATOM   2045 N  N   . PRO   A 1 251 ? 1.315   -5.646  29.054  1.00 8.62  ? 250 PRO   A N   1 
ATOM   2046 C  CA  . PRO   A 1 251 ? 1.067   -5.709  30.487  1.00 9.46  ? 250 PRO   A CA  1 
ATOM   2047 C  C   . PRO   A 1 251 ? 0.026   -4.708  30.955  1.00 8.90  ? 250 PRO   A C   1 
ATOM   2048 O  O   . PRO   A 1 251 ? 0.047   -3.533  30.575  1.00 8.83  ? 250 PRO   A O   1 
ATOM   2049 C  CB  . PRO   A 1 251 ? 2.460   -5.388  31.077  1.00 10.72 ? 250 PRO   A CB  1 
ATOM   2050 C  CG  . PRO   A 1 251 ? 3.448   -5.744  29.986  1.00 11.17 ? 250 PRO   A CG  1 
ATOM   2051 C  CD  . PRO   A 1 251 ? 2.721   -5.379  28.700  1.00 9.74  ? 250 PRO   A CD  1 
ATOM   2052 N  N   . LEU   A 1 252 ? -0.864  -5.170  31.813  1.00 9.15  ? 251 LEU   A N   1 
ATOM   2053 C  CA  . LEU   A 1 252 ? -1.912  -4.314  32.357  1.00 8.94  ? 251 LEU   A CA  1 
ATOM   2054 C  C   . LEU   A 1 252 ? -1.372  -3.193  33.228  1.00 8.54  ? 251 LEU   A C   1 
ATOM   2055 O  O   . LEU   A 1 252 ? -1.945  -2.111  33.277  1.00 8.30  ? 251 LEU   A O   1 
ATOM   2056 C  CB  . LEU   A 1 252 ? -2.945  -5.172  33.080  1.00 10.15 ? 251 LEU   A CB  1 
ATOM   2057 C  CG  . LEU   A 1 252 ? -4.240  -4.481  33.492  1.00 11.08 ? 251 LEU   A CG  1 
ATOM   2058 C  CD1 . LEU   A 1 252 ? -5.006  -3.934  32.306  1.00 11.56 ? 251 LEU   A CD1 1 
ATOM   2059 C  CD2 . LEU   A 1 252 ? -5.099  -5.405  34.313  1.00 12.06 ? 251 LEU   A CD2 1 
ATOM   2060 N  N   . LYS   A 1 253 ? -0.319  -3.479  33.991  1.00 9.24  ? 252 LYS   A N   1 
ATOM   2061 C  CA  . LYS   A 1 253 ? 0.263   -2.465  34.869  1.00 10.67 ? 252 LYS   A CA  1 
ATOM   2062 C  C   . LYS   A 1 253 ? -0.802  -1.921  35.814  1.00 10.74 ? 252 LYS   A C   1 
ATOM   2063 O  O   . LYS   A 1 253 ? -1.600  -2.683  36.317  1.00 12.52 ? 252 LYS   A O   1 
ATOM   2064 C  CB  . LYS   A 1 253 ? 1.053   -1.435  34.071  1.00 11.69 ? 252 LYS   A CB  1 
ATOM   2065 C  CG  . LYS   A 1 253 ? 2.210   -2.139  33.355  1.00 13.23 ? 252 LYS   A CG  1 
ATOM   2066 C  CD  . LYS   A 1 253 ? 3.135   -1.153  32.687  1.00 14.69 ? 252 LYS   A CD  1 
ATOM   2067 C  CE  . LYS   A 1 253 ? 4.337   -1.811  32.133  1.00 16.32 ? 252 LYS   A CE  1 
ATOM   2068 N  NZ  . LYS   A 1 253 ? 5.164   -0.997  31.230  1.00 17.78 ? 252 LYS   A NZ  1 
ATOM   2069 N  N   . ASN   A 1 254 ? -0.778  -0.627  36.082  1.00 10.53 ? 253 ASN   A N   1 
ATOM   2070 C  CA  . ASN   A 1 254 ? -1.625  -0.064  37.103  1.00 11.86 ? 253 ASN   A CA  1 
ATOM   2071 C  C   . ASN   A 1 254 ? -2.942  0.355   36.463  1.00 11.45 ? 253 ASN   A C   1 
ATOM   2072 O  O   . ASN   A 1 254 ? -3.209  1.577   36.436  1.00 13.24 ? 253 ASN   A O   1 
ATOM   2073 C  CB  . ASN   A 1 254 ? -0.929  1.099   37.788  1.00 13.48 ? 253 ASN   A CB  1 
ATOM   2074 C  CG  . ASN   A 1 254 ? -1.706  1.564   39.001  1.00 15.43 ? 253 ASN   A CG  1 
ATOM   2075 O  OD1 . ASN   A 1 254 ? -2.299  0.752   39.714  1.00 18.09 ? 253 ASN   A OD1 1 
ATOM   2076 N  ND2 . ASN   A 1 254 ? -1.829  2.855   39.186  1.00 16.65 ? 253 ASN   A ND2 1 
ATOM   2077 N  N   . ARG   A 1 255 ? -3.728  -0.644  35.996  1.00 9.71  ? 254 ARG   A N   1 
ATOM   2078 C  CA  . ARG   A 1 255 ? -5.027  -0.388  35.405  1.00 8.56  ? 254 ARG   A CA  1 
ATOM   2079 C  C   . ARG   A 1 255 ? -6.033  -1.389  35.940  1.00 9.80  ? 254 ARG   A C   1 
ATOM   2080 O  O   . ARG   A 1 255 ? -5.714  -2.532  36.199  1.00 11.42 ? 254 ARG   A O   1 
ATOM   2081 C  CB  . ARG   A 1 255 ? -4.930  -0.399  33.881  1.00 7.88  ? 254 ARG   A CB  1 
ATOM   2082 C  CG  . ARG   A 1 255 ? -4.085  0.736   33.348  1.00 7.10  ? 254 ARG   A CG  1 
ATOM   2083 C  CD  . ARG   A 1 255 ? -3.997  0.723   31.840  1.00 6.95  ? 254 ARG   A CD  1 
ATOM   2084 N  NE  . ARG   A 1 255 ? -3.188  -0.390  31.392  1.00 6.63  ? 254 ARG   A NE  1 
ATOM   2085 C  CZ  . ARG   A 1 255 ? -2.869  -0.638  30.132  1.00 6.20  ? 254 ARG   A CZ  1 
ATOM   2086 N  NH1 . ARG   A 1 255 ? -3.471  0.018   29.170  1.00 6.26  ? 254 ARG   A NH1 1 
ATOM   2087 N  NH2 . ARG   A 1 255 ? -2.028  -1.614  29.812  1.00 6.14  ? 254 ARG   A NH2 1 
ATOM   2088 N  N   . GLN   A 1 256 ? -7.270  -0.949  35.951  1.00 10.51 ? 255 GLN   A N   1 
ATOM   2089 C  CA  . GLN   A 1 256 ? -8.426  -1.789  36.184  1.00 12.04 ? 255 GLN   A CA  1 
ATOM   2090 C  C   . GLN   A 1 256 ? -9.346  -1.715  34.983  1.00 10.86 ? 255 GLN   A C   1 
ATOM   2091 O  O   . GLN   A 1 256 ? -9.557  -0.664  34.350  1.00 13.66 ? 255 GLN   A O   1 
ATOM   2092 C  CB  . GLN   A 1 256 ? -9.202  -1.356  37.413  1.00 14.45 ? 255 GLN   A CB  1 
ATOM   2093 C  CG  . GLN   A 1 256 ? -8.479  -1.647  38.701  1.00 17.24 ? 255 GLN   A CG  1 
ATOM   2094 C  CD  . GLN   A 1 256 ? -9.304  -1.293  39.908  1.00 19.75 ? 255 GLN   A CD  1 
ATOM   2095 O  OE1 . GLN   A 1 256 ? -10.066 -0.307  39.925  1.00 22.79 ? 255 GLN   A OE1 1 
ATOM   2096 N  NE2 . GLN   A 1 256 ? -9.126  -2.104  40.936  1.00 21.51 ? 255 GLN   A NE2 1 
ATOM   2097 N  N   . ILE   A 1 257 ? -9.797  -2.877  34.584  1.00 8.92  ? 256 ILE   A N   1 
ATOM   2098 C  CA  . ILE   A 1 257 ? -10.813 -2.998  33.553  1.00 8.55  ? 256 ILE   A CA  1 
ATOM   2099 C  C   . ILE   A 1 257 ? -12.182 -3.024  34.219  1.00 8.09  ? 256 ILE   A C   1 
ATOM   2100 O  O   . ILE   A 1 257 ? -12.402 -3.767  35.170  1.00 8.75  ? 256 ILE   A O   1 
ATOM   2101 C  CB  . ILE   A 1 257 ? -10.591 -4.230  32.720  1.00 8.45  ? 256 ILE   A CB  1 
ATOM   2102 C  CG1 . ILE   A 1 257 ? -9.152  -4.225  32.117  1.00 9.34  ? 256 ILE   A CG1 1 
ATOM   2103 C  CG2 . ILE   A 1 257 ? -11.634 -4.297  31.608  1.00 9.09  ? 256 ILE   A CG2 1 
ATOM   2104 C  CD1 . ILE   A 1 257 ? -8.828  -5.401  31.237  1.00 10.23 ? 256 ILE   A CD1 1 
ATOM   2105 N  N   A LYS   A 1 258 ? -13.087 -2.162  33.744  0.50 7.90  ? 257 LYS   A N   1 
ATOM   2106 N  N   B LYS   A 1 258 ? -13.089 -2.176  33.740  0.50 7.96  ? 257 LYS   A N   1 
ATOM   2107 C  CA  A LYS   A 1 258 ? -14.437 -2.040  34.264  0.50 8.28  ? 257 LYS   A CA  1 
ATOM   2108 C  CA  B LYS   A 1 258 ? -14.427 -2.082  34.285  0.50 8.39  ? 257 LYS   A CA  1 
ATOM   2109 C  C   A LYS   A 1 258 ? -15.415 -2.686  33.284  0.50 7.86  ? 257 LYS   A C   1 
ATOM   2110 C  C   B LYS   A 1 258 ? -15.409 -2.693  33.289  0.50 7.94  ? 257 LYS   A C   1 
ATOM   2111 O  O   A LYS   A 1 258 ? -15.252 -2.604  32.064  0.50 8.03  ? 257 LYS   A O   1 
ATOM   2112 O  O   B LYS   A 1 258 ? -15.210 -2.640  32.071  0.50 8.10  ? 257 LYS   A O   1 
ATOM   2113 C  CB  A LYS   A 1 258 ? -14.886 -0.585  34.431  0.50 9.14  ? 257 LYS   A CB  1 
ATOM   2114 C  CB  B LYS   A 1 258 ? -14.748 -0.625  34.605  0.50 9.36  ? 257 LYS   A CB  1 
ATOM   2115 C  CG  A LYS   A 1 258 ? -14.148 0.185   35.526  0.50 10.59 ? 257 LYS   A CG  1 
ATOM   2116 C  CG  B LYS   A 1 258 ? -13.753 -0.004  35.599  0.50 10.79 ? 257 LYS   A CG  1 
ATOM   2117 C  CD  A LYS   A 1 258 ? -13.858 -0.609  36.796  0.50 12.07 ? 257 LYS   A CD  1 
ATOM   2118 C  CD  B LYS   A 1 258 ? -14.245 1.395   35.937  0.50 12.45 ? 257 LYS   A CD  1 
ATOM   2119 C  CE  A LYS   A 1 258 ? -13.252 0.093   37.981  0.50 13.47 ? 257 LYS   A CE  1 
ATOM   2120 C  CE  B LYS   A 1 258 ? -13.277 2.440   36.271  0.50 13.70 ? 257 LYS   A CE  1 
ATOM   2121 N  NZ  A LYS   A 1 258 ? -13.653 -0.474  39.261  0.50 14.59 ? 257 LYS   A NZ  1 
ATOM   2122 N  NZ  B LYS   A 1 258 ? -13.716 3.117   37.491  0.50 15.31 ? 257 LYS   A NZ  1 
ATOM   2123 N  N   . ALA   A 1 259 ? -16.444 -3.327  33.830  1.00 7.90  ? 258 ALA   A N   1 
ATOM   2124 C  CA  . ALA   A 1 259 ? -17.520 -3.910  33.046  1.00 7.90  ? 258 ALA   A CA  1 
ATOM   2125 C  C   . ALA   A 1 259 ? -18.769 -3.062  33.188  1.00 7.69  ? 258 ALA   A C   1 
ATOM   2126 O  O   . ALA   A 1 259 ? -19.138 -2.629  34.293  1.00 8.45  ? 258 ALA   A O   1 
ATOM   2127 C  CB  . ALA   A 1 259 ? -17.803 -5.355  33.474  1.00 8.52  ? 258 ALA   A CB  1 
ATOM   2128 N  N   . SER   A 1 260 ? -19.528 -3.006  32.090  1.00 7.95  ? 259 SER   A N   1 
ATOM   2129 C  CA  . SER   A 1 260 ? -20.793 -2.275  32.052  1.00 8.70  ? 259 SER   A CA  1 
ATOM   2130 C  C   . SER   A 1 260 ? -21.973 -3.121  32.525  1.00 9.29  ? 259 SER   A C   1 
ATOM   2131 O  O   . SER   A 1 260 ? -23.092 -2.624  32.621  1.00 11.13 ? 259 SER   A O   1 
ATOM   2132 C  CB  . SER   A 1 260 ? -21.089 -1.763  30.672  1.00 8.76  ? 259 SER   A CB  1 
ATOM   2133 O  OG  . SER   A 1 260 ? -21.516 -2.791  29.812  1.00 8.71  ? 259 SER   A OG  1 
ATOM   2134 N  N   . PHE   A 1 261 ? -21.714 -4.402  32.762  1.00 9.96  ? 260 PHE   A N   1 
ATOM   2135 C  CA  . PHE   A 1 261 ? -22.725 -5.433  32.956  1.00 11.67 ? 260 PHE   A CA  1 
ATOM   2136 C  C   . PHE   A 1 261 ? -22.287 -6.362  34.087  1.00 14.57 ? 260 PHE   A C   1 
ATOM   2137 O  O   . PHE   A 1 261 ? -21.107 -6.491  34.396  1.00 15.68 ? 260 PHE   A O   1 
ATOM   2138 C  CB  . PHE   A 1 261 ? -22.917 -6.246  31.661  1.00 11.13 ? 260 PHE   A CB  1 
ATOM   2139 C  CG  . PHE   A 1 261 ? -21.634 -6.979  31.256  1.00 11.26 ? 260 PHE   A CG  1 
ATOM   2140 C  CD1 . PHE   A 1 261 ? -20.641 -6.317  30.535  1.00 11.11 ? 260 PHE   A CD1 1 
ATOM   2141 C  CD2 . PHE   A 1 261 ? -21.407 -8.301  31.627  1.00 13.06 ? 260 PHE   A CD2 1 
ATOM   2142 C  CE1 . PHE   A 1 261 ? -19.438 -6.976  30.230  1.00 11.46 ? 260 PHE   A CE1 1 
ATOM   2143 C  CE2 . PHE   A 1 261 ? -20.221 -8.923  31.314  1.00 13.65 ? 260 PHE   A CE2 1 
ATOM   2144 C  CZ  . PHE   A 1 261 ? -19.259 -8.284  30.610  1.00 13.12 ? 260 PHE   A CZ  1 
ATOM   2145 N  N   . LYS   A 1 262 ? -23.312 -7.068  34.582  1.00 18.72 ? 261 LYS   A N   1 
ATOM   2146 C  CA  . LYS   A 1 262 ? -23.274 -8.141  35.556  1.00 22.99 ? 261 LYS   A CA  1 
ATOM   2147 C  C   . LYS   A 1 262 ? -22.192 -7.931  36.608  1.00 26.63 ? 261 LYS   A C   1 
ATOM   2148 O  O   . LYS   A 1 262 ? -22.242 -8.784  37.516  1.00 31.71 ? 261 LYS   A O   1 
ATOM   2149 C  CB  . LYS   A 1 262 ? -23.171 -9.475  34.809  1.00 24.98 ? 261 LYS   A CB  1 
ATOM   2150 C  CG  . LYS   A 1 262 ? -24.241 -9.743  33.777  1.00 28.12 ? 261 LYS   A CG  1 
ATOM   2151 C  CD  . LYS   A 1 262 ? -24.205 -11.180 33.273  1.00 31.18 ? 261 LYS   A CD  1 
ATOM   2152 C  CE  . LYS   A 1 262 ? -24.153 -11.253 31.784  1.00 33.51 ? 261 LYS   A CE  1 
ATOM   2153 N  NZ  . LYS   A 1 262 ? -23.730 -12.603 31.417  1.00 35.47 ? 261 LYS   A NZ  1 
HETATM 2154 C  C1  . A1IH2 B 2 .   ? -1.309  17.381  14.014  1.00 18.24 ? 301 A1IH2 A C1  1 
HETATM 2155 C  C2  . A1IH2 B 2 .   ? -2.331  18.183  14.584  1.00 16.34 ? 301 A1IH2 A C2  1 
HETATM 2156 C  C3  . A1IH2 B 2 .   ? -3.543  18.362  13.987  1.00 16.02 ? 301 A1IH2 A C3  1 
HETATM 2157 C  C4  . A1IH2 B 2 .   ? -3.784  17.758  12.734  1.00 16.37 ? 301 A1IH2 A C4  1 
HETATM 2158 C  C5  . A1IH2 B 2 .   ? -2.762  16.944  12.168  1.00 16.81 ? 301 A1IH2 A C5  1 
HETATM 2159 C  C6  . A1IH2 B 2 .   ? -1.567  16.770  12.779  1.00 17.61 ? 301 A1IH2 A C6  1 
HETATM 2160 O  O3  . A1IH2 B 2 .   ? -4.471  19.189  14.603  1.00 16.89 ? 301 A1IH2 A O3  1 
HETATM 2161 O  O4  . A1IH2 B 2 .   ? -4.955  17.931  12.103  1.00 16.56 ? 301 A1IH2 A O4  1 
HETATM 2162 C  C20 . A1IH2 B 2 .   ? -3.247  3.839   15.099  1.00 15.99 ? 301 A1IH2 A C20 1 
HETATM 2163 C  C21 . A1IH2 B 2 .   ? -4.180  2.978   15.620  1.00 14.40 ? 301 A1IH2 A C21 1 
HETATM 2164 O  O21 . A1IH2 B 2 .   ? -3.871  1.900   16.411  1.00 13.31 ? 301 A1IH2 A O21 1 
HETATM 2165 C  C22 . A1IH2 B 2 .   ? -5.511  3.136   15.373  1.00 15.10 ? 301 A1IH2 A C22 1 
HETATM 2166 O  O22 . A1IH2 B 2 .   ? -6.290  2.205   15.907  1.00 14.19 ? 301 A1IH2 A O22 1 
HETATM 2167 C  C23 . A1IH2 B 2 .   ? -5.965  4.174   14.588  1.00 16.14 ? 301 A1IH2 A C23 1 
HETATM 2168 C  C24 . A1IH2 B 2 .   ? -5.037  5.097   14.065  1.00 17.33 ? 301 A1IH2 A C24 1 
HETATM 2169 C  C19 . A1IH2 B 2 .   ? -3.662  4.887   14.306  1.00 17.96 ? 301 A1IH2 A C19 1 
HETATM 2170 C  C25 . A1IH2 B 2 .   ? -2.550  5.777   13.804  1.00 22.27 ? 301 A1IH2 A C25 1 
HETATM 2171 C  C26 . A1IH2 B 2 .   ? -2.289  5.817   12.277  1.00 27.50 ? 301 A1IH2 A C26 1 
HETATM 2172 O  O13 . A1IH2 B 2 .   ? -2.296  7.168   11.801  1.00 28.96 ? 301 A1IH2 A O13 1 
HETATM 2173 C  C27 . A1IH2 B 2 .   ? -3.149  4.836   11.417  1.00 31.60 ? 301 A1IH2 A C27 1 
HETATM 2174 O  O29 . A1IH2 B 2 .   ? -4.194  5.286   10.834  1.00 34.48 ? 301 A1IH2 A O29 1 
HETATM 2175 O  O28 . A1IH2 B 2 .   ? -2.731  3.669   11.310  1.00 33.23 ? 301 A1IH2 A O28 1 
HETATM 2176 O  O12 . A1IH2 B 2 .   ? -2.680  7.103   14.331  1.00 20.42 ? 301 A1IH2 A O12 1 
HETATM 2177 C  C12 . A1IH2 B 2 .   ? -1.959  8.147   13.872  1.00 22.32 ? 301 A1IH2 A C12 1 
HETATM 2178 C  C11 . A1IH2 B 2 .   ? -1.505  9.101   14.714  1.00 21.61 ? 301 A1IH2 A C11 1 
HETATM 2179 C  C13 . A1IH2 B 2 .   ? -1.770  8.179   12.528  1.00 25.33 ? 301 A1IH2 A C13 1 
HETATM 2180 C  C14 . A1IH2 B 2 .   ? -1.055  9.181   11.914  1.00 26.11 ? 301 A1IH2 A C14 1 
HETATM 2181 C  C15 . A1IH2 B 2 .   ? -0.561  10.175  12.743  1.00 26.01 ? 301 A1IH2 A C15 1 
HETATM 2182 C  C10 . A1IH2 B 2 .   ? -0.774  10.142  14.143  1.00 22.72 ? 301 A1IH2 A C10 1 
HETATM 2183 C  C16 . A1IH2 B 2 .   ? -0.235  11.237  14.936  1.00 22.39 ? 301 A1IH2 A C16 1 
HETATM 2184 C  C17 . A1IH2 B 2 .   ? -0.340  12.552  14.566  1.00 22.31 ? 301 A1IH2 A C17 1 
HETATM 2185 C  C18 . A1IH2 B 2 .   ? -0.119  13.653  15.468  1.00 22.34 ? 301 A1IH2 A C18 1 
HETATM 2186 O  O20 . A1IH2 B 2 .   ? -0.022  13.581  16.652  1.00 20.95 ? 301 A1IH2 A O20 1 
HETATM 2187 O  O19 . A1IH2 B 2 .   ? 0.011   14.842  14.789  1.00 21.51 ? 301 A1IH2 A O19 1 
HETATM 2188 C  C8  . A1IH2 B 2 .   ? 0.085   16.024  15.637  1.00 22.19 ? 301 A1IH2 A C8  1 
HETATM 2189 C  C9  . A1IH2 B 2 .   ? 1.378   16.092  16.422  1.00 23.81 ? 301 A1IH2 A C9  1 
HETATM 2190 O  O11 . A1IH2 B 2 .   ? 1.455   16.686  17.502  1.00 24.92 ? 301 A1IH2 A O11 1 
HETATM 2191 O  O10 . A1IH2 B 2 .   ? 2.360   15.472  15.800  1.00 25.72 ? 301 A1IH2 A O10 1 
HETATM 2192 C  C7  . A1IH2 B 2 .   ? 0.012   17.226  14.737  1.00 20.30 ? 301 A1IH2 A C7  1 
HETATM 2193 ZN ZN  . ZN    C 3 .   ? -6.705  -1.081  15.333  1.00 5.61  ? 302 ZN    A ZN  1 
HETATM 2194 C  C1  . GOL   D 4 .   ? 2.386   -10.110 15.515  1.00 16.28 ? 303 GOL   A C1  1 
HETATM 2195 O  O1  . GOL   D 4 .   ? 1.653   -10.391 16.697  1.00 13.77 ? 303 GOL   A O1  1 
HETATM 2196 C  C2  . GOL   D 4 .   ? 1.903   -11.110 14.509  1.00 16.97 ? 303 GOL   A C2  1 
HETATM 2197 O  O2  . GOL   D 4 .   ? 2.405   -10.949 13.158  1.00 13.51 ? 303 GOL   A O2  1 
HETATM 2198 C  C3  . GOL   D 4 .   ? 2.193   -12.522 14.994  1.00 18.54 ? 303 GOL   A C3  1 
HETATM 2199 O  O3  . GOL   D 4 .   ? 1.575   -13.496 14.164  1.00 21.50 ? 303 GOL   A O3  1 
HETATM 2200 O  O   . HOH   E 5 .   ? -26.208 7.163   27.247  1.00 26.75 ? 401 HOH   A O   1 
HETATM 2201 O  O   . HOH   E 5 .   ? -17.853 19.687  6.136   1.00 11.41 ? 402 HOH   A O   1 
HETATM 2202 O  O   . HOH   E 5 .   ? 1.696   12.791  22.877  1.00 29.09 ? 403 HOH   A O   1 
HETATM 2203 O  O   . HOH   E 5 .   ? -5.504  1.348   18.070  1.00 12.60 ? 404 HOH   A O   1 
HETATM 2204 O  O   . HOH   E 5 .   ? -15.372 -9.899  37.417  1.00 23.02 ? 405 HOH   A O   1 
HETATM 2205 O  O   . HOH   E 5 .   ? -18.201 -2.339  45.124  1.00 32.46 ? 406 HOH   A O   1 
HETATM 2206 O  O   . HOH   E 5 .   ? -11.264 -14.630 34.224  1.00 16.57 ? 407 HOH   A O   1 
HETATM 2207 O  O   . HOH   E 5 .   ? -5.273  -0.097  16.158  1.00 8.88  ? 408 HOH   A O   1 
HETATM 2208 O  O   . HOH   E 5 .   ? -24.207 -3.092  29.666  1.00 18.66 ? 409 HOH   A O   1 
HETATM 2209 O  O   . HOH   E 5 .   ? 4.967   -9.949  13.739  1.00 23.13 ? 410 HOH   A O   1 
HETATM 2210 O  O   . HOH   E 5 .   ? -19.155 18.196  18.828  1.00 25.91 ? 411 HOH   A O   1 
HETATM 2211 O  O   . HOH   E 5 .   ? -20.953 -6.438  -1.933  1.00 27.14 ? 412 HOH   A O   1 
HETATM 2212 O  O   . HOH   E 5 .   ? -9.824  2.051   38.973  1.00 28.81 ? 413 HOH   A O   1 
HETATM 2213 O  O   . HOH   E 5 .   ? -25.618 10.147  13.442  1.00 28.19 ? 414 HOH   A O   1 
HETATM 2214 O  O   . HOH   E 5 .   ? 8.334   -5.290  -10.307 1.00 22.27 ? 415 HOH   A O   1 
HETATM 2215 O  O   . HOH   E 5 .   ? -6.840  -19.695 19.544  1.00 18.31 ? 416 HOH   A O   1 
HETATM 2216 O  O   . HOH   E 5 .   ? -15.924 -11.555 39.277  1.00 26.29 ? 417 HOH   A O   1 
HETATM 2217 O  O   . HOH   E 5 .   ? 0.104   1.608   -8.859  1.00 18.05 ? 418 HOH   A O   1 
HETATM 2218 O  O   . HOH   E 5 .   ? -12.750 13.192  29.210  1.00 20.74 ? 419 HOH   A O   1 
HETATM 2219 O  O   . HOH   E 5 .   ? -13.044 13.799  31.997  1.00 20.62 ? 420 HOH   A O   1 
HETATM 2220 O  O   . HOH   E 5 .   ? -9.289  6.467   29.134  1.00 17.26 ? 421 HOH   A O   1 
HETATM 2221 O  O   . HOH   E 5 .   ? -15.490 1.402   -4.781  1.00 24.38 ? 422 HOH   A O   1 
HETATM 2222 O  O   . HOH   E 5 .   ? -19.402 -20.219 5.090   1.00 18.94 ? 423 HOH   A O   1 
HETATM 2223 O  O   . HOH   E 5 .   ? -19.923 -16.137 3.010   1.00 19.05 ? 424 HOH   A O   1 
HETATM 2224 O  O   . HOH   E 5 .   ? -23.448 0.251   32.361  1.00 19.93 ? 425 HOH   A O   1 
HETATM 2225 O  O   . HOH   E 5 .   ? 2.791   -11.915 18.513  1.00 18.43 ? 426 HOH   A O   1 
HETATM 2226 O  O   . HOH   E 5 .   ? -8.789  -3.226  7.984   1.00 5.69  ? 427 HOH   A O   1 
HETATM 2227 O  O   . HOH   E 5 .   ? -1.260  -3.542  15.768  1.00 6.95  ? 428 HOH   A O   1 
HETATM 2228 O  O   . HOH   E 5 .   ? 1.445   8.716   28.162  1.00 23.58 ? 429 HOH   A O   1 
HETATM 2229 O  O   . HOH   E 5 .   ? 11.347  -6.395  22.585  1.00 20.53 ? 430 HOH   A O   1 
HETATM 2230 O  O   . HOH   E 5 .   ? 1.937   -14.828 9.454   1.00 17.81 ? 431 HOH   A O   1 
HETATM 2231 O  O   . HOH   E 5 .   ? -6.232  -3.714  -6.374  1.00 21.14 ? 432 HOH   A O   1 
HETATM 2232 O  O   . HOH   E 5 .   ? -14.139 14.805  27.359  1.00 20.50 ? 433 HOH   A O   1 
HETATM 2233 O  O   . HOH   E 5 .   ? -28.043 6.593   15.138  1.00 26.28 ? 434 HOH   A O   1 
HETATM 2234 O  O   . HOH   E 5 .   ? 2.355   -12.606 5.209   1.00 14.15 ? 435 HOH   A O   1 
HETATM 2235 O  O   . HOH   E 5 .   ? 3.468   5.648   29.874  1.00 13.99 ? 436 HOH   A O   1 
HETATM 2236 O  O   . HOH   E 5 .   ? -18.606 -20.658 14.766  1.00 19.49 ? 437 HOH   A O   1 
HETATM 2237 O  O   . HOH   E 5 .   ? -7.001  6.542   6.539   1.00 14.43 ? 438 HOH   A O   1 
HETATM 2238 O  O   . HOH   E 5 .   ? -18.360 -3.137  -2.467  1.00 22.29 ? 439 HOH   A O   1 
HETATM 2239 O  O   . HOH   E 5 .   ? -3.298  0.551   42.172  1.00 35.04 ? 440 HOH   A O   1 
HETATM 2240 O  O   . HOH   E 5 .   ? 5.781   -5.522  24.364  1.00 24.20 ? 441 HOH   A O   1 
HETATM 2241 O  O   . HOH   E 5 .   ? -3.788  21.318  16.055  1.00 21.58 ? 442 HOH   A O   1 
HETATM 2242 O  O   . HOH   E 5 .   ? -14.433 -16.099 28.919  1.00 16.30 ? 443 HOH   A O   1 
HETATM 2243 O  O   . HOH   E 5 .   ? 5.148   -10.128 18.794  1.00 25.46 ? 444 HOH   A O   1 
HETATM 2244 O  O   . HOH   E 5 .   ? -24.272 9.225   20.311  1.00 16.49 ? 445 HOH   A O   1 
HETATM 2245 O  O   . HOH   E 5 .   ? -16.565 5.782   -7.889  1.00 22.34 ? 446 HOH   A O   1 
HETATM 2246 O  O   . HOH   E 5 .   ? -4.711  -11.465 32.190  1.00 17.62 ? 447 HOH   A O   1 
HETATM 2247 O  O   . HOH   E 5 .   ? -1.019  17.384  18.244  1.00 22.55 ? 448 HOH   A O   1 
HETATM 2248 O  O   . HOH   E 5 .   ? -20.787 9.017   30.159  1.00 19.27 ? 449 HOH   A O   1 
HETATM 2249 O  O   . HOH   E 5 .   ? 4.086   -1.851  28.922  1.00 22.24 ? 450 HOH   A O   1 
HETATM 2250 O  O   . HOH   E 5 .   ? -23.403 -12.851 11.249  1.00 20.23 ? 451 HOH   A O   1 
HETATM 2251 O  O   . HOH   E 5 .   ? 4.209   -2.831  26.625  1.00 15.25 ? 452 HOH   A O   1 
HETATM 2252 O  O   . HOH   E 5 .   ? -2.643  -3.788  -6.814  1.00 25.19 ? 453 HOH   A O   1 
HETATM 2253 O  O   . HOH   E 5 .   ? 7.398   -7.148  -0.641  1.00 22.39 ? 454 HOH   A O   1 
HETATM 2254 O  O   . HOH   E 5 .   ? 0.027   -0.317  -4.647  1.00 10.00 ? 455 HOH   A O   1 
HETATM 2255 O  O   . HOH   E 5 .   ? -2.554  -8.143  29.214  1.00 8.94  ? 456 HOH   A O   1 
HETATM 2256 O  O   . HOH   E 5 .   ? -13.087 -21.666 8.646   1.00 22.60 ? 457 HOH   A O   1 
HETATM 2257 O  O   . HOH   E 5 .   ? -6.246  15.565  11.999  1.00 16.99 ? 458 HOH   A O   1 
HETATM 2258 O  O   . HOH   E 5 .   ? -10.821 9.262   25.712  1.00 8.13  ? 459 HOH   A O   1 
HETATM 2259 O  O   . HOH   E 5 .   ? -22.232 -17.825 13.623  1.00 19.42 ? 460 HOH   A O   1 
HETATM 2260 O  O   . HOH   E 5 .   ? -1.385  9.866   28.065  1.00 17.75 ? 461 HOH   A O   1 
HETATM 2261 O  O   . HOH   E 5 .   ? -5.085  1.106   9.884   1.00 15.33 ? 462 HOH   A O   1 
HETATM 2262 O  O   . HOH   E 5 .   ? -16.881 15.250  33.234  1.00 23.68 ? 463 HOH   A O   1 
HETATM 2263 O  O   . HOH   E 5 .   ? -20.472 11.304  26.825  1.00 14.50 ? 464 HOH   A O   1 
HETATM 2264 O  O   . HOH   E 5 .   ? -25.632 -5.411  12.969  1.00 31.20 ? 465 HOH   A O   1 
HETATM 2265 O  O   . HOH   E 5 .   ? -18.582 -11.723 -3.586  1.00 18.61 ? 466 HOH   A O   1 
HETATM 2266 O  O   . HOH   E 5 .   ? -5.329  2.767   37.646  1.00 20.59 ? 467 HOH   A O   1 
HETATM 2267 O  O   . HOH   E 5 .   ? -21.332 8.459   2.040   1.00 11.03 ? 468 HOH   A O   1 
HETATM 2268 O  O   . HOH   E 5 .   ? -13.924 10.866  28.078  1.00 12.56 ? 469 HOH   A O   1 
HETATM 2269 O  O   . HOH   E 5 .   ? 4.863   -6.839  22.269  1.00 15.67 ? 470 HOH   A O   1 
HETATM 2270 O  O   . HOH   E 5 .   ? -3.279  -19.951 6.615   1.00 26.87 ? 471 HOH   A O   1 
HETATM 2271 O  O   . HOH   E 5 .   ? -15.440 -21.342 13.173  1.00 13.49 ? 472 HOH   A O   1 
HETATM 2272 O  O   . HOH   E 5 .   ? 3.346   -13.603 12.096  1.00 26.59 ? 473 HOH   A O   1 
HETATM 2273 O  O   . HOH   E 5 .   ? 2.597   -3.670  7.820   1.00 15.96 ? 474 HOH   A O   1 
HETATM 2274 O  O   . HOH   E 5 .   ? -8.009  -14.994 11.445  1.00 8.24  ? 475 HOH   A O   1 
HETATM 2275 O  O   . HOH   E 5 .   ? -4.470  -12.973 18.043  1.00 6.83  ? 476 HOH   A O   1 
HETATM 2276 O  O   . HOH   E 5 .   ? 5.173   7.633   20.212  1.00 13.96 ? 477 HOH   A O   1 
HETATM 2277 O  O   . HOH   E 5 .   ? -7.189  -9.389  -4.581  1.00 29.12 ? 478 HOH   A O   1 
HETATM 2278 O  O   . HOH   E 5 .   ? 13.698  2.596   22.829  1.00 19.70 ? 479 HOH   A O   1 
HETATM 2279 O  O   . HOH   E 5 .   ? -0.029  1.694   34.647  1.00 16.74 ? 480 HOH   A O   1 
HETATM 2280 O  O   . HOH   E 5 .   ? -7.096  -7.555  -6.999  1.00 26.35 ? 481 HOH   A O   1 
HETATM 2281 O  O   . HOH   E 5 .   ? -19.848 -3.533  41.449  1.00 24.46 ? 482 HOH   A O   1 
HETATM 2282 O  O   . HOH   E 5 .   ? -7.138  -14.326 31.680  1.00 15.27 ? 483 HOH   A O   1 
HETATM 2283 O  O   . HOH   E 5 .   ? -3.645  -12.259 -2.869  1.00 18.29 ? 484 HOH   A O   1 
HETATM 2284 O  O   . HOH   E 5 .   ? -18.151 11.218  11.451  1.00 14.54 ? 485 HOH   A O   1 
HETATM 2285 O  O   . HOH   E 5 .   ? 1.235   -11.164 25.092  1.00 21.96 ? 486 HOH   A O   1 
HETATM 2286 O  O   . HOH   E 5 .   ? 3.553   -2.572  4.354   1.00 22.66 ? 487 HOH   A O   1 
HETATM 2287 O  O   . HOH   E 5 .   ? -15.013 20.731  17.770  1.00 14.37 ? 488 HOH   A O   1 
HETATM 2288 O  O   . HOH   E 5 .   ? 11.559  0.172   15.995  1.00 20.43 ? 489 HOH   A O   1 
HETATM 2289 O  O   . HOH   E 5 .   ? -11.075 -19.162 7.307   1.00 32.39 ? 490 HOH   A O   1 
HETATM 2290 O  O   . HOH   E 5 .   ? 15.795  3.924   15.555  1.00 18.67 ? 491 HOH   A O   1 
HETATM 2291 O  O   . HOH   E 5 .   ? -8.813  1.432   -6.456  1.00 19.65 ? 492 HOH   A O   1 
HETATM 2292 O  O   . HOH   E 5 .   ? -17.119 -13.492 37.711  1.00 24.63 ? 493 HOH   A O   1 
HETATM 2293 O  O   . HOH   E 5 .   ? -10.357 -17.783 17.196  1.00 9.55  ? 494 HOH   A O   1 
HETATM 2294 O  O   . HOH   E 5 .   ? -12.237 11.326  5.800   1.00 19.15 ? 495 HOH   A O   1 
HETATM 2295 O  O   . HOH   E 5 .   ? 8.467   -3.259  21.126  1.00 9.99  ? 496 HOH   A O   1 
HETATM 2296 O  O   . HOH   E 5 .   ? -17.116 -7.906  20.462  1.00 6.40  ? 497 HOH   A O   1 
HETATM 2297 O  O   . HOH   E 5 .   ? -3.531  -10.659 20.948  1.00 7.31  ? 498 HOH   A O   1 
HETATM 2298 O  O   . HOH   E 5 .   ? -10.669 22.313  19.980  1.00 20.78 ? 499 HOH   A O   1 
HETATM 2299 O  O   . HOH   E 5 .   ? -21.674 -6.689  23.696  1.00 9.37  ? 500 HOH   A O   1 
HETATM 2300 O  O   . HOH   E 5 .   ? -16.356 16.465  23.662  1.00 16.37 ? 501 HOH   A O   1 
HETATM 2301 O  O   . HOH   E 5 .   ? -24.976 5.102   8.650   1.00 24.42 ? 502 HOH   A O   1 
HETATM 2302 O  O   . HOH   E 5 .   ? -22.846 -5.327  2.825   1.00 18.26 ? 503 HOH   A O   1 
HETATM 2303 O  O   . HOH   E 5 .   ? -8.671  -14.868 36.803  1.00 21.56 ? 504 HOH   A O   1 
HETATM 2304 O  O   . HOH   E 5 .   ? -17.959 -20.002 8.105   1.00 10.90 ? 505 HOH   A O   1 
HETATM 2305 O  O   . HOH   E 5 .   ? -16.118 -11.811 24.456  1.00 12.61 ? 506 HOH   A O   1 
HETATM 2306 O  O   . HOH   E 5 .   ? -3.666  -15.301 24.413  1.00 10.20 ? 507 HOH   A O   1 
HETATM 2307 O  O   . HOH   E 5 .   ? -17.390 -15.781 21.933  1.00 21.72 ? 508 HOH   A O   1 
HETATM 2308 O  O   . HOH   E 5 .   ? -25.610 -10.139 17.900  1.00 19.91 ? 509 HOH   A O   1 
HETATM 2309 O  O   . HOH   E 5 .   ? -25.790 -3.051  32.153  1.00 29.04 ? 510 HOH   A O   1 
HETATM 2310 O  O   . HOH   E 5 .   ? -27.584 -7.016  26.163  1.00 25.49 ? 511 HOH   A O   1 
HETATM 2311 O  O   . HOH   E 5 .   ? -4.288  -7.892  31.257  1.00 15.02 ? 512 HOH   A O   1 
HETATM 2312 O  O   . HOH   E 5 .   ? -22.099 6.311   4.891   1.00 10.20 ? 513 HOH   A O   1 
HETATM 2313 O  O   . HOH   E 5 .   ? -26.495 3.259   20.909  1.00 16.45 ? 514 HOH   A O   1 
HETATM 2314 O  O   . HOH   E 5 .   ? -23.385 -10.595 17.171  1.00 27.14 ? 515 HOH   A O   1 
HETATM 2315 O  O   . HOH   E 5 .   ? -14.573 -17.999 18.796  1.00 12.75 ? 516 HOH   A O   1 
HETATM 2316 O  O   . HOH   E 5 .   ? -15.742 9.488   -2.090  1.00 18.91 ? 517 HOH   A O   1 
HETATM 2317 O  O   . HOH   E 5 .   ? -23.364 -2.494  6.819   1.00 14.88 ? 518 HOH   A O   1 
HETATM 2318 O  O   . HOH   E 5 .   ? -2.575  -2.815  11.491  1.00 12.04 ? 519 HOH   A O   1 
HETATM 2319 O  O   . HOH   E 5 .   ? -10.096 15.098  12.213  1.00 13.71 ? 520 HOH   A O   1 
HETATM 2320 O  O   . HOH   E 5 .   ? -9.510  -9.523  -1.131  1.00 18.99 ? 521 HOH   A O   1 
HETATM 2321 O  O   . HOH   E 5 .   ? -0.755  11.285  23.586  1.00 16.44 ? 522 HOH   A O   1 
HETATM 2322 O  O   . HOH   E 5 .   ? -13.814 20.519  15.244  1.00 12.83 ? 523 HOH   A O   1 
HETATM 2323 O  O   . HOH   E 5 .   ? -3.363  -12.691 25.269  1.00 8.31  ? 524 HOH   A O   1 
HETATM 2324 O  O   . HOH   E 5 .   ? -7.210  -16.254 1.542   1.00 16.65 ? 525 HOH   A O   1 
HETATM 2325 O  O   . HOH   E 5 .   ? -6.714  -4.776  37.542  1.00 15.98 ? 526 HOH   A O   1 
HETATM 2326 O  O   . HOH   E 5 .   ? -10.432 14.024  8.689   1.00 31.93 ? 527 HOH   A O   1 
HETATM 2327 O  O   . HOH   E 5 .   ? -19.458 10.567  9.047   1.00 9.83  ? 528 HOH   A O   1 
HETATM 2328 O  O   . HOH   E 5 .   ? -12.027 10.049  3.318   1.00 17.10 ? 529 HOH   A O   1 
HETATM 2329 O  O   . HOH   E 5 .   ? -7.515  -8.140  32.680  1.00 12.36 ? 530 HOH   A O   1 
HETATM 2330 O  O   . HOH   E 5 .   ? 13.258  0.868   24.550  1.00 15.82 ? 531 HOH   A O   1 
HETATM 2331 O  O   . HOH   E 5 .   ? 11.006  1.886   25.915  1.00 18.57 ? 532 HOH   A O   1 
HETATM 2332 O  O   . HOH   E 5 .   ? -13.537 -0.165  -6.073  1.00 20.53 ? 533 HOH   A O   1 
HETATM 2333 O  O   . HOH   E 5 .   ? -13.381 -17.993 14.638  1.00 12.32 ? 534 HOH   A O   1 
HETATM 2334 O  O   . HOH   E 5 .   ? -12.961 8.429   28.908  1.00 17.50 ? 535 HOH   A O   1 
HETATM 2335 O  O   . HOH   E 5 .   ? 4.774   -4.340  20.996  1.00 10.08 ? 536 HOH   A O   1 
HETATM 2336 O  O   . HOH   E 5 .   ? -6.439  6.989   10.696  1.00 22.21 ? 537 HOH   A O   1 
HETATM 2337 O  O   . HOH   E 5 .   ? 7.002   -2.870  30.192  1.00 26.38 ? 538 HOH   A O   1 
HETATM 2338 O  O   . HOH   E 5 .   ? -19.616 18.000  6.117   1.00 18.97 ? 539 HOH   A O   1 
HETATM 2339 O  O   . HOH   E 5 .   ? 9.313   2.594   12.261  1.00 21.05 ? 540 HOH   A O   1 
HETATM 2340 O  O   . HOH   E 5 .   ? -13.025 -16.310 26.620  1.00 13.83 ? 541 HOH   A O   1 
HETATM 2341 O  O   . HOH   E 5 .   ? -26.813 -1.911  14.563  1.00 16.17 ? 542 HOH   A O   1 
HETATM 2342 O  O   . HOH   E 5 .   ? -21.433 1.371   0.492   1.00 27.07 ? 543 HOH   A O   1 
HETATM 2343 O  O   . HOH   E 5 .   ? 2.858   -8.526  27.364  1.00 26.12 ? 544 HOH   A O   1 
HETATM 2344 O  O   . HOH   E 5 .   ? -16.466 -9.484  33.063  1.00 13.93 ? 545 HOH   A O   1 
HETATM 2345 O  O   . HOH   E 5 .   ? -11.183 1.558   33.674  1.00 20.73 ? 546 HOH   A O   1 
HETATM 2346 O  O   . HOH   E 5 .   ? -1.456  5.236   -4.800  1.00 18.63 ? 547 HOH   A O   1 
HETATM 2347 O  O   . HOH   E 5 .   ? -7.919  19.613  10.412  1.00 17.02 ? 548 HOH   A O   1 
HETATM 2348 O  O   . HOH   E 5 .   ? 1.013   9.340   24.361  1.00 12.89 ? 549 HOH   A O   1 
HETATM 2349 O  O   . HOH   E 5 .   ? -24.921 -7.215  9.210   1.00 14.76 ? 550 HOH   A O   1 
HETATM 2350 O  O   . HOH   E 5 .   ? -5.970  17.587  27.462  1.00 19.09 ? 551 HOH   A O   1 
HETATM 2351 O  O   . HOH   E 5 .   ? -15.041 -15.464 24.991  1.00 27.85 ? 552 HOH   A O   1 
HETATM 2352 O  O   . HOH   E 5 .   ? -4.655  -15.443 0.909   1.00 20.63 ? 553 HOH   A O   1 
HETATM 2353 O  O   . HOH   E 5 .   ? -21.130 -19.084 6.718   1.00 19.57 ? 554 HOH   A O   1 
HETATM 2354 O  O   . HOH   E 5 .   ? -12.114 3.297   30.937  1.00 15.38 ? 555 HOH   A O   1 
HETATM 2355 O  O   . HOH   E 5 .   ? -10.622 9.059   7.926   1.00 17.78 ? 556 HOH   A O   1 
HETATM 2356 O  O   . HOH   E 5 .   ? -16.466 -15.468 32.637  1.00 24.66 ? 557 HOH   A O   1 
HETATM 2357 O  O   . HOH   E 5 .   ? -2.911  6.733   -1.422  1.00 15.58 ? 558 HOH   A O   1 
HETATM 2358 O  O   . HOH   E 5 .   ? -23.393 -17.653 6.240   1.00 25.88 ? 559 HOH   A O   1 
HETATM 2359 O  O   . HOH   E 5 .   ? -11.372 18.076  12.426  1.00 24.15 ? 560 HOH   A O   1 
HETATM 2360 O  O   . HOH   E 5 .   ? 8.042   3.776   27.857  1.00 30.71 ? 561 HOH   A O   1 
HETATM 2361 O  O   . HOH   E 5 .   ? 2.540   -10.798 9.464   1.00 16.00 ? 562 HOH   A O   1 
HETATM 2362 O  O   . HOH   E 5 .   ? 9.147   8.165   18.694  1.00 31.86 ? 563 HOH   A O   1 
HETATM 2363 O  O   . HOH   E 5 .   ? -1.597  23.878  18.195  1.00 26.38 ? 564 HOH   A O   1 
HETATM 2364 O  O   . HOH   E 5 .   ? -27.217 -10.235 22.626  1.00 27.56 ? 565 HOH   A O   1 
HETATM 2365 O  O   . HOH   E 5 .   ? -10.098 6.794   -4.025  1.00 25.52 ? 566 HOH   A O   1 
HETATM 2366 O  O   . HOH   E 5 .   ? 1.381   -5.777  34.507  1.00 20.15 ? 567 HOH   A O   1 
HETATM 2367 O  O   . HOH   E 5 .   ? 10.334  -10.150 16.205  1.00 22.95 ? 568 HOH   A O   1 
HETATM 2368 O  O   . HOH   E 5 .   ? -27.024 -3.446  25.186  1.00 15.29 ? 569 HOH   A O   1 
HETATM 2369 O  O   . HOH   E 5 .   ? 8.187   -8.762  16.527  1.00 19.09 ? 570 HOH   A O   1 
HETATM 2370 O  O   . HOH   E 5 .   ? -24.683 12.661  6.364   1.00 28.81 ? 571 HOH   A O   1 
HETATM 2371 O  O   . HOH   E 5 .   ? 12.937  -5.250  24.553  1.00 18.86 ? 572 HOH   A O   1 
HETATM 2372 O  O   . HOH   E 5 .   ? 1.151   -0.996  29.478  1.00 11.08 ? 573 HOH   A O   1 
HETATM 2373 O  O   . HOH   E 5 .   ? 2.261   -13.855 -0.984  1.00 25.42 ? 574 HOH   A O   1 
HETATM 2374 O  O   . HOH   E 5 .   ? 9.917   -3.978  -7.681  1.00 26.08 ? 575 HOH   A O   1 
HETATM 2375 O  O   . HOH   E 5 .   ? 4.297   -5.987  7.845   1.00 17.57 ? 576 HOH   A O   1 
HETATM 2376 O  O   . HOH   E 5 .   ? -25.367 -9.233  15.301  1.00 29.03 ? 577 HOH   A O   1 
HETATM 2377 O  O   . HOH   E 5 .   ? -23.089 -11.109 14.181  1.00 15.88 ? 578 HOH   A O   1 
HETATM 2378 O  O   . HOH   E 5 .   ? -9.171  -5.351  36.020  1.00 15.31 ? 579 HOH   A O   1 
HETATM 2379 O  O   . HOH   E 5 .   ? 13.918  6.255   19.242  1.00 21.96 ? 580 HOH   A O   1 
HETATM 2380 O  O   . HOH   E 5 .   ? -23.996 -0.233  3.977   1.00 14.50 ? 581 HOH   A O   1 
HETATM 2381 O  O   . HOH   E 5 .   ? -13.888 15.174  6.645   1.00 30.64 ? 582 HOH   A O   1 
HETATM 2382 O  O   . HOH   E 5 .   ? -24.105 -0.082  26.626  1.00 21.53 ? 583 HOH   A O   1 
HETATM 2383 O  O   . HOH   E 5 .   ? -25.956 -6.105  33.716  1.00 32.09 ? 584 HOH   A O   1 
HETATM 2384 O  O   . HOH   E 5 .   ? -1.552  19.388  23.044  1.00 26.85 ? 585 HOH   A O   1 
HETATM 2385 O  O   . HOH   E 5 .   ? -8.440  -19.265 26.559  1.00 20.42 ? 586 HOH   A O   1 
HETATM 2386 O  O   . HOH   E 5 .   ? -0.643  -7.985  32.710  1.00 18.81 ? 587 HOH   A O   1 
HETATM 2387 O  O   . HOH   E 5 .   ? -2.086  -11.754 22.955  1.00 7.63  ? 588 HOH   A O   1 
HETATM 2388 O  O   . HOH   E 5 .   ? 6.662   -5.593  6.787   1.00 30.94 ? 589 HOH   A O   1 
HETATM 2389 O  O   . HOH   E 5 .   ? -12.792 4.245   -6.768  1.00 18.90 ? 590 HOH   A O   1 
HETATM 2390 O  O   . HOH   E 5 .   ? 10.724  -8.056  8.703   1.00 26.94 ? 591 HOH   A O   1 
HETATM 2391 O  O   . HOH   E 5 .   ? -5.455  4.446   -5.488  1.00 25.81 ? 592 HOH   A O   1 
HETATM 2392 O  O   . HOH   E 5 .   ? -10.750 21.362  25.010  1.00 19.91 ? 593 HOH   A O   1 
HETATM 2393 O  O   . HOH   E 5 .   ? 10.234  7.202   15.386  1.00 36.43 ? 594 HOH   A O   1 
HETATM 2394 O  O   . HOH   E 5 .   ? -0.232  -13.729 22.281  1.00 14.36 ? 595 HOH   A O   1 
HETATM 2395 O  O   . HOH   E 5 .   ? -8.186  -18.850 21.706  1.00 18.81 ? 596 HOH   A O   1 
HETATM 2396 O  O   . HOH   E 5 .   ? 7.400   6.664   21.652  1.00 12.53 ? 597 HOH   A O   1 
HETATM 2397 O  O   . HOH   E 5 .   ? -23.839 0.357   1.165   1.00 29.60 ? 598 HOH   A O   1 
HETATM 2398 O  O   . HOH   E 5 .   ? -16.488 -15.518 -4.390  1.00 36.74 ? 599 HOH   A O   1 
HETATM 2399 O  O   . HOH   E 5 .   ? 4.523   -10.811 22.950  1.00 37.25 ? 600 HOH   A O   1 
HETATM 2400 O  O   . HOH   E 5 .   ? -9.649  -7.479  34.235  1.00 16.13 ? 601 HOH   A O   1 
HETATM 2401 O  O   . HOH   E 5 .   ? 10.027  -2.046  13.854  1.00 23.05 ? 602 HOH   A O   1 
HETATM 2402 O  O   . HOH   E 5 .   ? -8.492  9.860   -2.669  1.00 28.69 ? 603 HOH   A O   1 
HETATM 2403 O  O   . HOH   E 5 .   ? -25.554 11.496  19.607  1.00 27.63 ? 604 HOH   A O   1 
HETATM 2404 O  O   . HOH   E 5 .   ? -19.133 3.912   -3.328  1.00 21.49 ? 605 HOH   A O   1 
HETATM 2405 O  O   . HOH   E 5 .   ? -7.352  2.050   35.234  1.00 22.63 ? 606 HOH   A O   1 
HETATM 2406 O  O   . HOH   E 5 .   ? -4.031  5.359   7.115   1.00 27.70 ? 607 HOH   A O   1 
HETATM 2407 O  O   . HOH   E 5 .   ? -7.502  -8.035  -2.323  1.00 21.88 ? 608 HOH   A O   1 
HETATM 2408 O  O   . HOH   E 5 .   ? -24.713 -9.012  1.922   1.00 20.98 ? 609 HOH   A O   1 
HETATM 2409 O  O   . HOH   E 5 .   ? 12.935  -3.063  13.524  1.00 23.55 ? 610 HOH   A O   1 
HETATM 2410 O  O   . HOH   E 5 .   ? -1.585  12.163  26.106  1.00 20.56 ? 611 HOH   A O   1 
HETATM 2411 O  O   . HOH   E 5 .   ? -12.839 -16.697 16.962  1.00 9.52  ? 612 HOH   A O   1 
HETATM 2412 O  O   . HOH   E 5 .   ? -20.043 -15.815 21.499  1.00 33.48 ? 613 HOH   A O   1 
HETATM 2413 O  O   . HOH   E 5 .   ? 8.667   -4.214  23.779  1.00 28.95 ? 614 HOH   A O   1 
HETATM 2414 O  O   . HOH   E 5 .   ? -17.967 -11.606 31.470  1.00 22.93 ? 615 HOH   A O   1 
HETATM 2415 O  O   . HOH   E 5 .   ? -0.529  14.341  27.403  1.00 24.32 ? 616 HOH   A O   1 
HETATM 2416 O  O   . HOH   E 5 .   ? -8.387  -16.955 34.926  1.00 24.88 ? 617 HOH   A O   1 
HETATM 2417 O  O   . HOH   E 5 .   ? -23.799 -2.858  4.152   1.00 32.37 ? 618 HOH   A O   1 
HETATM 2418 O  O   . HOH   E 5 .   ? -7.034  -19.732 24.099  1.00 21.37 ? 619 HOH   A O   1 
HETATM 2419 O  O   . HOH   E 5 .   ? -4.296  -0.435  11.942  1.00 20.85 ? 620 HOH   A O   1 
HETATM 2420 O  O   . HOH   E 5 .   ? 1.161   -15.850 -2.249  1.00 26.22 ? 621 HOH   A O   1 
HETATM 2421 O  O   . HOH   E 5 .   ? 0.711   1.479   -6.461  1.00 22.74 ? 622 HOH   A O   1 
HETATM 2422 O  O   . HOH   E 5 .   ? 11.399  -18.727 7.620   1.00 30.59 ? 623 HOH   A O   1 
HETATM 2423 O  O   . HOH   E 5 .   ? -17.816 20.600  17.695  1.00 20.23 ? 624 HOH   A O   1 
HETATM 2424 O  O   . HOH   E 5 .   ? 14.484  0.527   15.139  1.00 22.49 ? 625 HOH   A O   1 
HETATM 2425 O  O   . HOH   E 5 .   ? -10.599 5.435   31.062  1.00 22.23 ? 626 HOH   A O   1 
HETATM 2426 O  O   . HOH   E 5 .   ? 12.072  -6.059  8.253   1.00 25.60 ? 627 HOH   A O   1 
HETATM 2427 O  O   . HOH   E 5 .   ? -16.865 -17.383 20.277  1.00 24.96 ? 628 HOH   A O   1 
HETATM 2428 O  O   . HOH   E 5 .   ? -1.411  -12.463 27.180  1.00 17.68 ? 629 HOH   A O   1 
HETATM 2429 O  O   . HOH   E 5 .   ? 2.842   -12.995 7.872   1.00 21.76 ? 630 HOH   A O   1 
HETATM 2430 O  O   . HOH   E 5 .   ? -9.386  11.707  -0.439  1.00 27.91 ? 631 HOH   A O   1 
HETATM 2431 O  O   . HOH   E 5 .   ? -19.865 -1.398  43.100  1.00 36.52 ? 632 HOH   A O   1 
HETATM 2432 O  O   . HOH   E 5 .   ? -5.027  -9.114  33.529  1.00 21.60 ? 633 HOH   A O   1 
HETATM 2433 O  O   . HOH   E 5 .   ? 15.074  -0.720  26.040  1.00 24.55 ? 634 HOH   A O   1 
HETATM 2434 O  O   . HOH   E 5 .   ? -16.932 -13.541 26.274  1.00 18.62 ? 635 HOH   A O   1 
HETATM 2435 O  O   . HOH   E 5 .   ? 5.915   -6.795  2.195   1.00 39.20 ? 636 HOH   A O   1 
HETATM 2436 O  O   . HOH   E 5 .   ? -1.269  6.312   41.212  1.00 27.14 ? 637 HOH   A O   1 
HETATM 2437 O  O   . HOH   E 5 .   ? -1.797  -16.879 25.694  1.00 21.66 ? 638 HOH   A O   1 
HETATM 2438 O  O   . HOH   E 5 .   ? -24.039 -6.412  0.496   1.00 28.73 ? 639 HOH   A O   1 
HETATM 2439 O  O   . HOH   E 5 .   ? 7.812   8.622   23.740  1.00 31.50 ? 640 HOH   A O   1 
HETATM 2440 O  O   . HOH   E 5 .   ? 6.409   -4.499  27.734  1.00 28.86 ? 641 HOH   A O   1 
HETATM 2441 O  O   . HOH   E 5 .   ? 2.877   7.229   31.964  1.00 29.64 ? 642 HOH   A O   1 
HETATM 2442 O  O   . HOH   E 5 .   ? -8.209  8.041   8.570   1.00 24.63 ? 643 HOH   A O   1 
HETATM 2443 O  O   . HOH   E 5 .   ? -1.232  -10.508 29.102  1.00 15.22 ? 644 HOH   A O   1 
HETATM 2444 O  O   . HOH   E 5 .   ? 6.269   -10.722 15.843  1.00 28.34 ? 645 HOH   A O   1 
HETATM 2445 O  O   . HOH   E 5 .   ? 1.153   3.963   -5.084  1.00 23.75 ? 646 HOH   A O   1 
HETATM 2446 O  O   . HOH   E 5 .   ? -21.313 -19.926 14.707  1.00 26.24 ? 647 HOH   A O   1 
HETATM 2447 O  O   . HOH   E 5 .   ? 3.758   5.564   1.989   1.00 27.93 ? 648 HOH   A O   1 
HETATM 2448 O  O   . HOH   E 5 .   ? -11.851 11.492  0.901   1.00 22.08 ? 649 HOH   A O   1 
HETATM 2449 O  O   . HOH   E 5 .   ? -12.352 14.041  4.897   1.00 24.54 ? 650 HOH   A O   1 
HETATM 2450 O  O   . HOH   E 5 .   ? 6.309   5.900   28.777  1.00 29.62 ? 651 HOH   A O   1 
HETATM 2451 O  O   . HOH   E 5 .   ? 4.204   -13.029 22.015  1.00 28.77 ? 652 HOH   A O   1 
HETATM 2452 O  O   . HOH   E 5 .   ? 6.241   8.976   17.950  1.00 26.79 ? 653 HOH   A O   1 
HETATM 2453 O  O   . HOH   E 5 .   ? -12.834 -19.045 26.363  1.00 23.95 ? 654 HOH   A O   1 
HETATM 2454 O  O   . HOH   E 5 .   ? 1.741   -9.328  32.014  1.00 29.07 ? 655 HOH   A O   1 
HETATM 2455 O  O   . HOH   E 5 .   ? 5.213   9.649   21.951  1.00 24.01 ? 656 HOH   A O   1 
HETATM 2456 O  O   . HOH   E 5 .   ? 1.916   -13.494 20.530  1.00 17.79 ? 657 HOH   A O   1 
HETATM 2457 O  O   . HOH   E 5 .   ? 3.427   10.527  23.716  1.00 22.03 ? 658 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 6   ? 0.2840 0.3394 0.3036 -0.0684 0.1109  0.0078  4   HIS A N   
2    C  CA  . HIS A 6   ? 0.2670 0.3213 0.2719 -0.0584 0.1144  -0.0083 4   HIS A CA  
3    C  C   . HIS A 6   ? 0.2287 0.2459 0.2356 -0.0431 0.0952  -0.0191 4   HIS A C   
4    O  O   . HIS A 6   ? 0.2676 0.2437 0.2589 -0.0420 0.0984  -0.0222 4   HIS A O   
5    C  CB  . HIS A 6   ? 0.2784 0.3480 0.3015 -0.0539 0.0965  -0.0123 4   HIS A CB  
6    C  CG  . HIS A 6   ? 0.3617 0.4197 0.3315 -0.0584 0.0823  -0.0012 4   HIS A CG  
7    N  ND1 . HIS A 6   ? 0.4149 0.4800 0.3601 -0.0643 0.0709  0.0052  4   HIS A ND1 
8    C  CD2 . HIS A 6   ? 0.4053 0.4611 0.3611 -0.0647 0.0760  -0.0012 4   HIS A CD2 
9    C  CE1 . HIS A 6   ? 0.4236 0.4772 0.3723 -0.0696 0.0734  0.0195  4   HIS A CE1 
10   N  NE2 . HIS A 6   ? 0.4346 0.4827 0.3659 -0.0682 0.0564  0.0147  4   HIS A NE2 
11   N  N   . TRP A 7   ? 0.1897 0.1914 0.1994 -0.0438 0.0722  -0.0138 5   TRP A N   
12   C  CA  . TRP A 7   ? 0.1573 0.1594 0.1806 -0.0349 0.0473  -0.0111 5   TRP A CA  
13   C  C   . TRP A 7   ? 0.1531 0.1504 0.1536 -0.0270 0.0462  -0.0154 5   TRP A C   
14   O  O   . TRP A 7   ? 0.1705 0.1614 0.1688 -0.0384 0.0542  -0.0036 5   TRP A O   
15   C  CB  . TRP A 7   ? 0.1415 0.1454 0.1632 -0.0363 0.0390  -0.0058 5   TRP A CB  
16   C  CG  . TRP A 7   ? 0.1510 0.1381 0.1436 -0.0265 0.0404  -0.0047 5   TRP A CG  
17   C  CD1 . TRP A 7   ? 0.1664 0.1479 0.1439 -0.0326 0.0395  0.0048  5   TRP A CD1 
18   C  CD2 . TRP A 7   ? 0.1466 0.1440 0.1212 -0.0160 0.0235  -0.0054 5   TRP A CD2 
19   N  NE1 . TRP A 7   ? 0.1755 0.1467 0.1428 -0.0226 0.0320  0.0102  5   TRP A NE1 
20   C  CE2 . TRP A 7   ? 0.1512 0.1503 0.1293 -0.0140 0.0225  -0.0008 5   TRP A CE2 
21   C  CE3 . TRP A 7   ? 0.1390 0.1437 0.1236 -0.0146 0.0195  -0.0220 5   TRP A CE3 
22   C  CZ2 . TRP A 7   ? 0.1568 0.1728 0.1228 -0.0108 0.0112  -0.0020 5   TRP A CZ2 
23   C  CZ3 . TRP A 7   ? 0.1473 0.1556 0.1314 -0.0139 0.0126  -0.0225 5   TRP A CZ3 
24   C  CH2 . TRP A 7   ? 0.1483 0.1710 0.1291 -0.0112 0.0052  -0.0182 5   TRP A CH2 
25   N  N   . GLY A 8   ? 0.1282 0.1352 0.1307 -0.0251 0.0402  -0.0168 6   GLY A N   
26   C  CA  . GLY A 8   ? 0.1226 0.1329 0.1231 -0.0177 0.0335  -0.0156 6   GLY A CA  
27   C  C   . GLY A 8   ? 0.1106 0.1252 0.1223 -0.0118 0.0346  -0.0168 6   GLY A C   
28   O  O   . GLY A 8   ? 0.1084 0.1359 0.1153 -0.0055 0.0310  -0.0184 6   GLY A O   
29   N  N   . TYR A 9   ? 0.1166 0.1167 0.1276 -0.0072 0.0418  -0.0199 7   TYR A N   
30   C  CA  . TYR A 9   ? 0.1223 0.1127 0.1455 -0.0074 0.0449  -0.0172 7   TYR A CA  
31   C  C   . TYR A 9   ? 0.1484 0.1250 0.2061 -0.0015 0.0621  -0.0233 7   TYR A C   
32   O  O   . TYR A 9   ? 0.1854 0.1476 0.2709 -0.0055 0.0862  -0.0009 7   TYR A O   
33   C  CB  . TYR A 9   ? 0.1120 0.1066 0.1285 -0.0126 0.0369  -0.0106 7   TYR A CB  
34   C  CG  . TYR A 9   ? 0.0891 0.0990 0.1051 -0.0159 0.0260  -0.0079 7   TYR A CG  
35   C  CD1 . TYR A 9   ? 0.0888 0.0917 0.0972 -0.0135 0.0208  -0.0063 7   TYR A CD1 
36   C  CD2 . TYR A 9   ? 0.0928 0.1015 0.0958 -0.0165 0.0210  -0.0048 7   TYR A CD2 
37   C  CE1 . TYR A 9   ? 0.0813 0.0880 0.0930 -0.0135 0.0211  -0.0051 7   TYR A CE1 
38   C  CE2 . TYR A 9   ? 0.0886 0.0978 0.0878 -0.0143 0.0188  0.0000  7   TYR A CE2 
39   C  CZ  . TYR A 9   ? 0.0809 0.0923 0.0886 -0.0112 0.0189  -0.0077 7   TYR A CZ  
40   O  OH  . TYR A 9   ? 0.0903 0.0908 0.0937 -0.0005 0.0191  0.0014  7   TYR A OH  
41   N  N   . GLY A 10  ? 0.1602 0.1497 0.2275 0.0033  0.0844  -0.0403 8   GLY A N   
42   C  CA  . GLY A 10  ? 0.1795 0.1709 0.2613 0.0143  0.0847  -0.0438 8   GLY A CA  
43   C  C   . GLY A 10  ? 0.2018 0.1844 0.2975 0.0408  0.0786  -0.0342 8   GLY A C   
44   O  O   . GLY A 10  ? 0.2111 0.2445 0.2978 0.0291  0.0812  -0.0189 8   GLY A O   
45   N  N   . LYS A 11  ? 0.2026 0.2243 0.3498 0.0401  0.0787  -0.0104 9   LYS A N   
46   C  CA  . LYS A 11  ? 0.2519 0.2510 0.3722 0.0311  0.0702  0.0005  9   LYS A CA  
47   C  C   . LYS A 11  ? 0.2176 0.2629 0.3428 0.0236  0.0961  0.0083  9   LYS A C   
48   O  O   . LYS A 11  ? 0.2043 0.2759 0.3552 0.0092  0.0770  -0.0008 9   LYS A O   
49   C  CB  . LYS A 11  ? 0.2907 0.2822 0.4025 0.0324  0.0712  0.0149  9   LYS A CB  
50   C  CG  . LYS A 11  ? 0.3586 0.3197 0.4485 0.0161  0.0704  0.0209  9   LYS A CG  
51   C  CD  . LYS A 11  ? 0.4013 0.3506 0.4792 0.0208  0.0765  0.0166  9   LYS A CD  
52   C  CE  . LYS A 11  ? 0.4376 0.3748 0.5039 0.0211  0.0777  0.0184  9   LYS A CE  
53   N  NZ  . LYS A 11  ? 0.4512 0.4116 0.5179 0.0299  0.0776  0.0184  9   LYS A NZ  
54   N  N   . HIS A 12  ? 0.2062 0.2051 0.3051 0.0486  0.1158  -0.0077 10  HIS A N   
55   C  CA  . HIS A 12  ? 0.1911 0.2124 0.2963 0.0420  0.1154  -0.0004 10  HIS A CA  
56   C  C   . HIS A 12  ? 0.1619 0.1995 0.2484 0.0305  0.0991  -0.0031 10  HIS A C   
57   O  O   . HIS A 12  ? 0.1721 0.2354 0.2583 0.0409  0.0837  -0.0284 10  HIS A O   
58   C  CB  . HIS A 12  ? 0.2071 0.2129 0.3176 0.0370  0.1325  -0.0027 10  HIS A CB  
59   C  CG  . HIS A 12  ? 0.2550 0.2330 0.3632 0.0487  0.1266  0.0183  10  HIS A CG  
60   N  ND1 . HIS A 12  ? 0.2761 0.2548 0.3930 0.0384  0.1378  0.0295  10  HIS A ND1 
61   C  CD2 . HIS A 12  ? 0.2769 0.2401 0.3803 0.0558  0.1290  0.0274  10  HIS A CD2 
62   C  CE1 . HIS A 12  ? 0.2681 0.2381 0.3953 0.0472  0.1419  0.0250  10  HIS A CE1 
63   N  NE2 . HIS A 12  ? 0.2917 0.2559 0.3990 0.0572  0.1358  0.0331  10  HIS A NE2 
64   N  N   . ASN A 13  ? 0.1416 0.1856 0.2035 0.0231  0.0848  -0.0132 11  ASN A N   
65   C  CA  . ASN A 13  ? 0.1255 0.1794 0.1733 0.0128  0.0626  -0.0184 11  ASN A CA  
66   C  C   . ASN A 13  ? 0.1164 0.1724 0.1538 0.0166  0.0503  -0.0174 11  ASN A C   
67   O  O   . ASN A 13  ? 0.1284 0.1722 0.1544 0.0142  0.0582  -0.0168 11  ASN A O   
68   C  CB  . ASN A 13  ? 0.1358 0.1824 0.1650 0.0068  0.0711  -0.0159 11  ASN A CB  
69   C  CG  . ASN A 13  ? 0.1607 0.1931 0.1592 -0.0011 0.0708  -0.0127 11  ASN A CG  
70   O  OD1 . ASN A 13  ? 0.1594 0.2002 0.1611 -0.0003 0.0659  -0.0128 11  ASN A OD1 
71   N  ND2 . ASN A 13  ? 0.1820 0.2048 0.1848 -0.0211 0.0626  0.0022  11  ASN A ND2 
72   N  N   . GLY A 14  ? 0.1133 0.1637 0.1393 0.0249  0.0432  -0.0184 12  GLY A N   
73   C  CA  . GLY A 14  ? 0.1171 0.1543 0.1328 0.0211  0.0346  -0.0189 12  GLY A CA  
74   C  C   . GLY A 14  ? 0.1090 0.1351 0.1227 0.0131  0.0308  -0.0139 12  GLY A C   
75   O  O   . GLY A 14  ? 0.0971 0.1498 0.1249 0.0179  0.0171  -0.0105 12  GLY A O   
76   N  N   . PRO A 15  ? 0.1050 0.1075 0.1198 0.0005  0.0308  -0.0118 13  PRO A N   
77   C  CA  . PRO A 15  ? 0.1072 0.1025 0.1269 0.0003  0.0363  -0.0111 13  PRO A CA  
78   C  C   . PRO A 15  ? 0.1090 0.1016 0.1272 -0.0008 0.0276  -0.0102 13  PRO A C   
79   O  O   . PRO A 15  ? 0.0914 0.1114 0.1108 -0.0076 0.0308  -0.0185 13  PRO A O   
80   C  CB  . PRO A 15  ? 0.1129 0.1080 0.1319 -0.0052 0.0358  -0.0112 13  PRO A CB  
81   C  CG  . PRO A 15  ? 0.1153 0.1095 0.1300 -0.0073 0.0343  -0.0107 13  PRO A CG  
82   C  CD  . PRO A 15  ? 0.1200 0.1144 0.1277 -0.0024 0.0307  -0.0164 13  PRO A CD  
83   N  N   . GLU A 16  ? 0.1359 0.1047 0.1432 0.0060  0.0103  -0.0130 14  GLU A N   
84   C  CA  . GLU A 16  ? 0.1516 0.1289 0.1545 0.0196  -0.0017 -0.0043 14  GLU A CA  
85   C  C   . GLU A 16  ? 0.1234 0.1326 0.1501 0.0331  -0.0077 -0.0147 14  GLU A C   
86   O  O   . GLU A 16  ? 0.1389 0.1475 0.1462 0.0366  -0.0138 -0.0036 14  GLU A O   
87   C  CB  . GLU A 16  ? 0.1882 0.1534 0.1871 0.0207  -0.0091 0.0024  14  GLU A CB  
88   C  CG  . GLU A 16  ? 0.2155 0.1871 0.2237 0.0106  -0.0071 -0.0008 14  GLU A CG  
89   C  CD  . GLU A 16  ? 0.2323 0.2262 0.2505 0.0153  -0.0162 -0.0064 14  GLU A CD  
90   O  OE1 . GLU A 16  ? 0.2838 0.2809 0.2856 0.0050  -0.0323 -0.0024 14  GLU A OE1 
91   O  OE2 . GLU A 16  ? 0.2454 0.2728 0.3005 0.0411  -0.0278 -0.0238 14  GLU A OE2 
92   N  N   . HIS A 17  ? 0.0943 0.1284 0.1400 0.0330  -0.0051 -0.0162 15  HIS A N   
93   C  CA  . HIS A 17  ? 0.0845 0.1260 0.1439 0.0300  -0.0060 -0.0207 15  HIS A CA  
94   C  C   . HIS A 17  ? 0.0675 0.1196 0.1315 0.0183  0.0029  -0.0207 15  HIS A C   
95   O  O   . HIS A 17  ? 0.0677 0.1238 0.1483 0.0090  0.0014  -0.0230 15  HIS A O   
96   C  CB  . HIS A 17  ? 0.0891 0.1374 0.1597 0.0391  -0.0068 -0.0261 15  HIS A CB  
97   C  CG  . HIS A 17  ? 0.1105 0.1599 0.1813 0.0537  -0.0104 -0.0390 15  HIS A CG  
98   N  ND1 . HIS A 17  ? 0.1261 0.1909 0.1908 0.0628  -0.0166 -0.0535 15  HIS A ND1 
99   C  CD2 . HIS A 17  ? 0.1318 0.1624 0.1971 0.0676  -0.0060 -0.0466 15  HIS A CD2 
100  C  CE1 . HIS A 17  ? 0.1499 0.1940 0.2077 0.0743  -0.0180 -0.0579 15  HIS A CE1 
101  N  NE2 . HIS A 17  ? 0.1585 0.1749 0.2189 0.0790  -0.0033 -0.0630 15  HIS A NE2 
102  N  N   . TRP A 18  ? 0.0614 0.1080 0.1283 0.0128  0.0081  -0.0158 16  TRP A N   
103  C  CA  . TRP A 18  ? 0.0580 0.1031 0.1151 0.0088  0.0077  -0.0140 16  TRP A CA  
104  C  C   . TRP A 18  ? 0.0572 0.1077 0.1233 0.0054  0.0042  -0.0133 16  TRP A C   
105  O  O   . TRP A 18  ? 0.0646 0.1148 0.1345 0.0016  0.0026  -0.0123 16  TRP A O   
106  C  CB  . TRP A 18  ? 0.0578 0.0994 0.1064 0.0049  0.0092  -0.0125 16  TRP A CB  
107  C  CG  . TRP A 18  ? 0.0627 0.1021 0.0988 0.0027  0.0119  -0.0136 16  TRP A CG  
108  C  CD1 . TRP A 18  ? 0.0642 0.1090 0.0969 0.0020  0.0180  -0.0111 16  TRP A CD1 
109  C  CD2 . TRP A 18  ? 0.0643 0.0910 0.0943 -0.0004 0.0175  -0.0109 16  TRP A CD2 
110  N  NE1 . TRP A 18  ? 0.0690 0.1067 0.0900 0.0022  0.0203  -0.0176 16  TRP A NE1 
111  C  CE2 . TRP A 18  ? 0.0659 0.0963 0.0932 -0.0001 0.0199  -0.0117 16  TRP A CE2 
112  C  CE3 . TRP A 18  ? 0.0646 0.0840 0.0953 0.0002  0.0179  -0.0143 16  TRP A CE3 
113  C  CZ2 . TRP A 18  ? 0.0743 0.0873 0.0929 -0.0034 0.0196  -0.0129 16  TRP A CZ2 
114  C  CZ3 . TRP A 18  ? 0.0654 0.0835 0.0907 -0.0016 0.0223  -0.0120 16  TRP A CZ3 
115  C  CH2 . TRP A 18  ? 0.0696 0.0838 0.0940 -0.0019 0.0195  -0.0111 16  TRP A CH2 
116  N  N   . HIS A 19  ? 0.0587 0.1159 0.1257 0.0037  0.0074  -0.0109 17  HIS A N   
117  C  CA  . HIS A 19  ? 0.0598 0.1266 0.1309 0.0043  0.0085  -0.0098 17  HIS A CA  
118  C  C   . HIS A 19  ? 0.0621 0.1343 0.1398 0.0008  0.0100  -0.0093 17  HIS A C   
119  O  O   . HIS A 19  ? 0.0715 0.1450 0.1431 -0.0092 0.0087  -0.0105 17  HIS A O   
120  C  CB  . HIS A 19  ? 0.0715 0.1394 0.1343 0.0012  0.0031  -0.0040 17  HIS A CB  
121  C  CG  . HIS A 19  ? 0.0788 0.1563 0.1402 0.0067  0.0045  0.0082  17  HIS A CG  
122  N  ND1 . HIS A 19  ? 0.0862 0.1912 0.1562 0.0102  0.0055  0.0115  17  HIS A ND1 
123  C  CD2 . HIS A 19  ? 0.0849 0.1648 0.1407 0.0104  0.0075  0.0071  17  HIS A CD2 
124  C  CE1 . HIS A 19  ? 0.0930 0.1887 0.1576 0.0201  0.0079  0.0135  17  HIS A CE1 
125  N  NE2 . HIS A 19  ? 0.0967 0.1770 0.1537 0.0217  0.0118  0.0133  17  HIS A NE2 
126  N  N   . LYS A 20  ? 0.0588 0.1405 0.1546 0.0015  0.0140  -0.0094 18  LYS A N   
127  C  CA  . LYS A 20  ? 0.0645 0.1629 0.1696 -0.0025 0.0134  0.0031  18  LYS A CA  
128  C  C   . LYS A 20  ? 0.0695 0.1588 0.1849 -0.0173 0.0171  0.0053  18  LYS A C   
129  O  O   . LYS A 20  ? 0.1212 0.1729 0.2343 -0.0417 -0.0061 0.0201  18  LYS A O   
130  C  CB  . LYS A 20  ? 0.0641 0.1761 0.1675 0.0133  0.0144  0.0106  18  LYS A CB  
131  C  CG  . LYS A 20  ? 0.0651 0.1904 0.1670 0.0214  0.0167  0.0189  18  LYS A CG  
132  C  CD  . LYS A 20  ? 0.0674 0.1980 0.1684 0.0287  0.0155  0.0253  18  LYS A CD  
133  C  CE  . LYS A 20  ? 0.0712 0.2012 0.1625 0.0322  0.0207  0.0297  18  LYS A CE  
134  N  NZ  . LYS A 20  ? 0.0731 0.2077 0.1608 0.0439  0.0172  0.0297  18  LYS A NZ  
135  N  N   . ASP A 21  ? 0.0762 0.1571 0.1798 -0.0188 0.0178  0.0014  19  ASP A N   
136  C  CA  . ASP A 21  ? 0.0833 0.1654 0.1806 -0.0156 0.0229  0.0015  19  ASP A CA  
137  C  C   . ASP A 21  ? 0.0845 0.1373 0.1780 -0.0138 0.0252  -0.0018 19  ASP A C   
138  O  O   . ASP A 21  ? 0.1106 0.1343 0.1900 -0.0209 0.0396  0.0034  19  ASP A O   
139  C  CB  . ASP A 21  ? 0.1141 0.2079 0.1964 -0.0071 0.0219  0.0004  19  ASP A CB  
140  C  CG  . ASP A 21  ? 0.1544 0.2564 0.2146 -0.0074 0.0252  0.0018  19  ASP A CG  
141  O  OD1 . ASP A 21  ? 0.1623 0.3083 0.2374 -0.0106 0.0573  0.0158  19  ASP A OD1 
142  O  OD2 . ASP A 21  ? 0.2384 0.3304 0.2488 0.0020  0.0381  0.0007  19  ASP A OD2 
143  N  N   . PHE A 22  ? 0.0798 0.1233 0.1670 -0.0084 0.0255  -0.0088 20  PHE A N   
144  C  CA  . PHE A 22  ? 0.0818 0.1224 0.1592 -0.0118 0.0201  -0.0168 20  PHE A CA  
145  C  C   . PHE A 22  ? 0.0741 0.1274 0.1577 -0.0105 0.0204  -0.0216 20  PHE A C   
146  O  O   . PHE A 22  ? 0.0768 0.1259 0.1349 -0.0087 0.0215  -0.0149 20  PHE A O   
147  C  CB  . PHE A 22  ? 0.0830 0.1249 0.1533 -0.0107 0.0182  -0.0119 20  PHE A CB  
148  C  CG  . PHE A 22  ? 0.0907 0.1345 0.1526 -0.0136 0.0137  -0.0043 20  PHE A CG  
149  C  CD1 . PHE A 22  ? 0.1227 0.1491 0.1623 -0.0144 0.0096  -0.0008 20  PHE A CD1 
150  C  CD2 . PHE A 22  ? 0.1015 0.1554 0.1500 -0.0073 0.0213  0.0020  20  PHE A CD2 
151  C  CE1 . PHE A 22  ? 0.1344 0.1640 0.1703 -0.0114 0.0135  0.0132  20  PHE A CE1 
152  C  CE2 . PHE A 22  ? 0.1118 0.1748 0.1539 -0.0020 0.0234  0.0077  20  PHE A CE2 
153  C  CZ  . PHE A 22  ? 0.1233 0.1772 0.1578 -0.0100 0.0193  0.0151  20  PHE A CZ  
154  N  N   . PRO A 23  ? 0.0829 0.1331 0.1675 -0.0202 0.0219  -0.0230 21  PRO A N   
155  C  CA  . PRO A 23  ? 0.0811 0.1464 0.1612 -0.0180 0.0184  -0.0268 21  PRO A CA  
156  C  C   . PRO A 23  ? 0.0776 0.1289 0.1495 -0.0192 0.0116  -0.0255 21  PRO A C   
157  O  O   . PRO A 23  ? 0.0765 0.1446 0.1583 -0.0062 -0.0017 -0.0235 21  PRO A O   
158  C  CB  . PRO A 23  ? 0.0966 0.1735 0.1789 -0.0319 0.0171  -0.0262 21  PRO A CB  
159  C  CG  . PRO A 23  ? 0.1184 0.1808 0.2070 -0.0337 0.0129  -0.0242 21  PRO A CG  
160  C  CD  . PRO A 23  ? 0.0883 0.1586 0.1865 -0.0302 0.0203  -0.0203 21  PRO A CD  
161  N  N   A ILE A 24  ? 0.0684 0.1185 0.1401 -0.0187 0.0121  -0.0273 22  ILE A N   
162  N  N   B ILE A 24  ? 0.0770 0.1227 0.1410 -0.0195 0.0122  -0.0261 22  ILE A N   
163  C  CA  A ILE A 24  ? 0.0637 0.1144 0.1351 -0.0130 0.0115  -0.0251 22  ILE A CA  
164  C  CA  B ILE A 24  ? 0.0775 0.1213 0.1360 -0.0156 0.0129  -0.0234 22  ILE A CA  
165  C  C   A ILE A 24  ? 0.0621 0.1129 0.1311 -0.0090 0.0067  -0.0211 22  ILE A C   
166  C  C   B ILE A 24  ? 0.0690 0.1158 0.1310 -0.0101 0.0083  -0.0196 22  ILE A C   
167  O  O   A ILE A 24  ? 0.0674 0.1081 0.1257 -0.0094 0.0072  -0.0218 22  ILE A O   
168  O  O   B ILE A 24  ? 0.0752 0.1073 0.1276 -0.0126 0.0114  -0.0189 22  ILE A O   
169  C  CB  A ILE A 24  ? 0.0632 0.1101 0.1390 -0.0160 0.0102  -0.0270 22  ILE A CB  
170  C  CB  B ILE A 24  ? 0.0883 0.1222 0.1409 -0.0197 0.0125  -0.0235 22  ILE A CB  
171  C  CG1 A ILE A 24  ? 0.0634 0.1081 0.1415 -0.0124 0.0092  -0.0295 22  ILE A CG1 
172  C  CG1 B ILE A 24  ? 0.0990 0.1269 0.1438 -0.0158 0.0128  -0.0263 22  ILE A CG1 
173  C  CG2 A ILE A 24  ? 0.0651 0.1111 0.1388 -0.0152 0.0092  -0.0254 22  ILE A CG2 
174  C  CG2 B ILE A 24  ? 0.0900 0.1232 0.1406 -0.0214 0.0111  -0.0217 22  ILE A CG2 
175  C  CD1 A ILE A 24  ? 0.0622 0.1059 0.1432 -0.0114 0.0099  -0.0309 22  ILE A CD1 
176  C  CD1 B ILE A 24  ? 0.1086 0.1366 0.1490 -0.0147 0.0134  -0.0263 22  ILE A CD1 
177  N  N   . ALA A 25  ? 0.0654 0.1103 0.1297 -0.0133 0.0098  -0.0192 23  ALA A N   
178  C  CA  . ALA A 25  ? 0.0639 0.1096 0.1293 -0.0071 0.0065  -0.0194 23  ALA A CA  
179  C  C   . ALA A 25  ? 0.0645 0.1183 0.1313 -0.0045 0.0041  -0.0195 23  ALA A C   
180  O  O   . ALA A 25  ? 0.0762 0.1200 0.1353 -0.0071 -0.0003 -0.0131 23  ALA A O   
181  C  CB  . ALA A 25  ? 0.0659 0.1111 0.1313 -0.0038 0.0033  -0.0179 23  ALA A CB  
182  N  N   . LYS A 26  ? 0.0776 0.1283 0.1242 -0.0114 0.0038  -0.0156 24  LYS A N   
183  C  CA  . LYS A 26  ? 0.0959 0.1536 0.1331 -0.0031 -0.0054 -0.0143 24  LYS A CA  
184  C  C   . LYS A 26  ? 0.1079 0.1699 0.1394 -0.0063 -0.0037 -0.0214 24  LYS A C   
185  O  O   . LYS A 26  ? 0.1269 0.1958 0.1478 0.0027  -0.0111 -0.0193 24  LYS A O   
186  C  CB  . LYS A 26  ? 0.1132 0.1716 0.1499 0.0056  -0.0108 -0.0125 24  LYS A CB  
187  C  CG  . LYS A 26  ? 0.1307 0.1956 0.1601 0.0194  -0.0013 -0.0069 24  LYS A CG  
188  C  CD  . LYS A 26  ? 0.1526 0.2159 0.1859 0.0329  0.0053  -0.0085 24  LYS A CD  
189  C  CE  . LYS A 26  ? 0.1667 0.2333 0.2096 0.0409  0.0168  -0.0069 24  LYS A CE  
190  N  NZ  . LYS A 26  ? 0.2021 0.2485 0.2367 0.0363  0.0233  -0.0140 24  LYS A NZ  
191  N  N   . GLY A 27  ? 0.0987 0.1619 0.1285 -0.0056 -0.0013 -0.0339 25  GLY A N   
192  C  CA  . GLY A 27  ? 0.1016 0.1666 0.1296 -0.0050 -0.0007 -0.0363 25  GLY A CA  
193  C  C   . GLY A 27  ? 0.0968 0.1644 0.1227 -0.0013 -0.0072 -0.0314 25  GLY A C   
194  O  O   . GLY A 27  ? 0.1013 0.1617 0.1256 -0.0008 -0.0035 -0.0290 25  GLY A O   
195  N  N   . GLU A 28  ? 0.0994 0.1699 0.1031 -0.0023 -0.0096 -0.0343 26  GLU A N   
196  C  CA  . GLU A 28  ? 0.1061 0.1796 0.1080 -0.0003 -0.0081 -0.0287 26  GLU A CA  
197  C  C   . GLU A 28  ? 0.1010 0.1435 0.1071 -0.0005 -0.0034 -0.0203 26  GLU A C   
198  O  O   . GLU A 28  ? 0.1268 0.1615 0.0902 -0.0102 -0.0103 -0.0098 26  GLU A O   
199  C  CB  . GLU A 28  ? 0.1250 0.2103 0.1298 -0.0063 -0.0134 -0.0390 26  GLU A CB  
200  C  CG  . GLU A 28  ? 0.1417 0.2480 0.1516 -0.0099 -0.0162 -0.0402 26  GLU A CG  
201  C  CD  . GLU A 28  ? 0.1806 0.3018 0.1834 -0.0028 -0.0170 -0.0313 26  GLU A CD  
202  O  OE1 . GLU A 28  ? 0.2518 0.3405 0.2101 -0.0120 -0.0175 -0.0188 26  GLU A OE1 
203  O  OE2 . GLU A 28  ? 0.2392 0.3651 0.2645 0.0289  -0.0219 -0.0211 26  GLU A OE2 
204  N  N   . ARG A 29  ? 0.0902 0.1165 0.1025 -0.0050 -0.0013 -0.0171 27  ARG A N   
205  C  CA  . ARG A 29  ? 0.0863 0.1075 0.0990 -0.0004 0.0040  -0.0209 27  ARG A CA  
206  C  C   . ARG A 29  ? 0.0787 0.0862 0.0911 -0.0023 0.0033  -0.0131 27  ARG A C   
207  O  O   . ARG A 29  ? 0.0761 0.0893 0.0928 0.0012  0.0034  -0.0102 27  ARG A O   
208  C  CB  . ARG A 29  ? 0.1128 0.1319 0.1099 0.0030  0.0065  -0.0262 27  ARG A CB  
209  C  CG  . ARG A 29  ? 0.1276 0.1441 0.1261 -0.0032 0.0069  -0.0251 27  ARG A CG  
210  C  CD  . ARG A 29  ? 0.1598 0.1528 0.1333 -0.0033 0.0163  -0.0163 27  ARG A CD  
211  N  NE  . ARG A 29  ? 0.1566 0.1470 0.1414 -0.0009 0.0278  -0.0094 27  ARG A NE  
212  C  CZ  . ARG A 29  ? 0.1475 0.1351 0.1284 0.0002  0.0345  -0.0155 27  ARG A CZ  
213  N  NH1 . ARG A 29  ? 0.1617 0.1565 0.1314 0.0006  0.0311  -0.0347 27  ARG A NH1 
214  N  NH2 . ARG A 29  ? 0.1471 0.1292 0.1295 -0.0111 0.0415  -0.0096 27  ARG A NH2 
215  N  N   . GLN A 30  ? 0.0710 0.0772 0.0812 -0.0025 0.0045  -0.0076 28  GLN A N   
216  C  CA  . GLN A 30  ? 0.0690 0.0703 0.0774 -0.0053 0.0011  -0.0067 28  GLN A CA  
217  C  C   . GLN A 30  ? 0.0650 0.0698 0.0775 -0.0051 0.0086  -0.0059 28  GLN A C   
218  O  O   . GLN A 30  ? 0.0736 0.0839 0.0787 -0.0134 0.0079  -0.0043 28  GLN A O   
219  C  CB  . GLN A 30  ? 0.0724 0.0776 0.0868 -0.0049 -0.0018 -0.0087 28  GLN A CB  
220  C  CG  . GLN A 30  ? 0.0736 0.0799 0.0899 -0.0034 0.0000  -0.0102 28  GLN A CG  
221  C  CD  . GLN A 30  ? 0.0660 0.0779 0.0914 -0.0029 0.0030  -0.0115 28  GLN A CD  
222  O  OE1 . GLN A 30  ? 0.0734 0.0834 0.0950 -0.0049 0.0086  -0.0146 28  GLN A OE1 
223  N  NE2 . GLN A 30  ? 0.0578 0.0736 0.0990 -0.0062 0.0062  -0.0111 28  GLN A NE2 
224  N  N   . SER A 31  ? 0.0609 0.0623 0.0738 -0.0054 0.0136  -0.0055 29  SER A N   
225  C  CA  . SER A 31  ? 0.0620 0.0555 0.0718 -0.0039 0.0153  -0.0052 29  SER A CA  
226  C  C   . SER A 31  ? 0.0654 0.0574 0.0707 -0.0019 0.0177  -0.0029 29  SER A C   
227  O  O   . SER A 31  ? 0.0645 0.0628 0.0766 -0.0014 0.0241  -0.0126 29  SER A O   
228  C  CB  . SER A 31  ? 0.0634 0.0563 0.0713 -0.0027 0.0157  -0.0065 29  SER A CB  
229  O  OG  . SER A 31  ? 0.0680 0.0612 0.0720 0.0016  0.0172  -0.0108 29  SER A OG  
230  N  N   . PRO A 32  ? 0.0656 0.0554 0.0683 0.0010  0.0161  -0.0020 30  PRO A N   
231  C  CA  . PRO A 32  ? 0.0703 0.0528 0.0644 -0.0001 0.0146  -0.0013 30  PRO A CA  
232  C  C   . PRO A 32  ? 0.0697 0.0577 0.0634 0.0031  0.0142  -0.0006 30  PRO A C   
233  O  O   . PRO A 32  ? 0.0725 0.0666 0.0646 0.0021  0.0107  0.0001  30  PRO A O   
234  C  CB  . PRO A 32  ? 0.0711 0.0565 0.0640 0.0027  0.0147  -0.0029 30  PRO A CB  
235  C  CG  . PRO A 32  ? 0.0728 0.0579 0.0684 0.0019  0.0156  -0.0048 30  PRO A CG  
236  C  CD  . PRO A 32  ? 0.0708 0.0576 0.0683 0.0007  0.0174  -0.0023 30  PRO A CD  
237  N  N   . VAL A 33  ? 0.0729 0.0643 0.0596 0.0052  0.0123  0.0051  31  VAL A N   
238  C  CA  . VAL A 33  ? 0.0811 0.0627 0.0650 0.0053  0.0142  0.0055  31  VAL A CA  
239  C  C   . VAL A 33  ? 0.0817 0.0646 0.0642 0.0083  0.0117  0.0065  31  VAL A C   
240  O  O   . VAL A 33  ? 0.0735 0.0693 0.0785 0.0024  0.0086  0.0093  31  VAL A O   
241  C  CB  . VAL A 33  ? 0.0898 0.0679 0.0731 0.0042  0.0143  0.0012  31  VAL A CB  
242  C  CG1 . VAL A 33  ? 0.0981 0.0706 0.0850 0.0033  0.0134  -0.0019 31  VAL A CG1 
243  C  CG2 . VAL A 33  ? 0.0911 0.0705 0.0789 0.0046  0.0164  0.0002  31  VAL A CG2 
244  N  N   . ASP A 34  ? 0.0858 0.0627 0.0701 0.0091  0.0119  0.0096  32  ASP A N   
245  C  CA  . ASP A 34  ? 0.0954 0.0679 0.0705 0.0092  0.0166  0.0070  32  ASP A CA  
246  C  C   . ASP A 34  ? 0.0994 0.0728 0.0657 0.0086  0.0204  0.0075  32  ASP A C   
247  O  O   . ASP A 34  ? 0.1065 0.0960 0.0706 0.0085  0.0234  -0.0060 32  ASP A O   
248  C  CB  . ASP A 34  ? 0.1018 0.0785 0.0783 0.0109  0.0141  0.0118  32  ASP A CB  
249  C  CG  . ASP A 34  ? 0.1126 0.0849 0.0793 0.0073  0.0194  0.0179  32  ASP A CG  
250  O  OD1 . ASP A 34  ? 0.1158 0.0735 0.0867 0.0039  0.0130  0.0185  32  ASP A OD1 
251  O  OD2 . ASP A 34  ? 0.1476 0.1115 0.0975 -0.0051 0.0170  0.0301  32  ASP A OD2 
252  N  N   . ILE A 35  ? 0.1040 0.0789 0.0665 0.0118  0.0254  0.0051  33  ILE A N   
253  C  CA  . ILE A 35  ? 0.1109 0.0811 0.0754 0.0159  0.0273  0.0085  33  ILE A CA  
254  C  C   . ILE A 35  ? 0.1293 0.0824 0.0791 0.0205  0.0306  0.0099  33  ILE A C   
255  O  O   . ILE A 35  ? 0.1271 0.0823 0.0855 0.0142  0.0307  0.0101  33  ILE A O   
256  C  CB  . ILE A 35  ? 0.1054 0.0805 0.0915 0.0180  0.0261  0.0111  33  ILE A CB  
257  C  CG1 . ILE A 35  ? 0.1098 0.0899 0.1009 0.0194  0.0210  0.0182  33  ILE A CG1 
258  C  CG2 . ILE A 35  ? 0.1100 0.0916 0.0991 0.0176  0.0281  0.0094  33  ILE A CG2 
259  C  CD1 . ILE A 35  ? 0.1112 0.0965 0.1123 0.0206  0.0208  0.0217  33  ILE A CD1 
260  N  N   A ASP A 36  ? 0.1417 0.0931 0.0803 0.0209  0.0299  0.0170  34  ASP A N   
261  N  N   B ASP A 36  ? 0.1428 0.0886 0.0788 0.0219  0.0321  0.0118  34  ASP A N   
262  C  CA  A ASP A 36  ? 0.1498 0.1079 0.0827 0.0263  0.0326  0.0254  34  ASP A CA  
263  C  CA  B ASP A 36  ? 0.1521 0.0980 0.0797 0.0288  0.0369  0.0158  34  ASP A CA  
264  C  C   A ASP A 36  ? 0.1544 0.1118 0.0843 0.0366  0.0390  0.0252  34  ASP A C   
265  C  C   B ASP A 36  ? 0.1553 0.1072 0.0833 0.0374  0.0409  0.0190  34  ASP A C   
266  O  O   A ASP A 36  ? 0.1727 0.1254 0.0824 0.0415  0.0387  0.0212  34  ASP A O   
267  O  O   B ASP A 36  ? 0.1713 0.1243 0.0820 0.0401  0.0395  0.0128  34  ASP A O   
268  C  CB  A ASP A 36  ? 0.1632 0.1257 0.0931 0.0267  0.0264  0.0298  34  ASP A CB  
269  C  CB  B ASP A 36  ? 0.1664 0.1051 0.0873 0.0322  0.0354  0.0129  34  ASP A CB  
270  C  CG  A ASP A 36  ? 0.1698 0.1438 0.1018 0.0261  0.0225  0.0400  34  ASP A CG  
271  C  CG  B ASP A 36  ? 0.1749 0.1100 0.0922 0.0333  0.0358  0.0129  34  ASP A CG  
272  O  OD1 A ASP A 36  ? 0.1723 0.1569 0.1023 0.0269  0.0159  0.0521  34  ASP A OD1 
273  O  OD1 B ASP A 36  ? 0.1895 0.1031 0.1026 0.0371  0.0319  0.0193  34  ASP A OD1 
274  O  OD2 A ASP A 36  ? 0.2017 0.1716 0.1281 0.0247  0.0092  0.0523  34  ASP A OD2 
275  O  OD2 B ASP A 36  ? 0.1883 0.1226 0.1004 0.0416  0.0427  0.0137  34  ASP A OD2 
276  N  N   . THR A 37  ? 0.1565 0.1216 0.0911 0.0398  0.0470  0.0307  35  THR A N   
277  C  CA  . THR A 37  ? 0.1616 0.1360 0.0995 0.0469  0.0515  0.0353  35  THR A CA  
278  C  C   . THR A 37  ? 0.1873 0.1291 0.0997 0.0533  0.0548  0.0384  35  THR A C   
279  O  O   . THR A 37  ? 0.1962 0.1649 0.1193 0.0630  0.0649  0.0226  35  THR A O   
280  C  CB  . THR A 37  ? 0.1635 0.1626 0.1172 0.0400  0.0489  0.0335  35  THR A CB  
281  O  OG1 . THR A 37  ? 0.1730 0.1682 0.1276 0.0243  0.0481  0.0324  35  THR A OG1 
282  C  CG2 . THR A 37  ? 0.1671 0.1773 0.1196 0.0371  0.0427  0.0300  35  THR A CG2 
283  N  N   . HIS A 38  ? 0.2121 0.1227 0.0894 0.0557  0.0668  0.0471  36  HIS A N   
284  C  CA  . HIS A 38  ? 0.2489 0.1366 0.0875 0.0401  0.0571  0.0467  36  HIS A CA  
285  C  C   . HIS A 38  ? 0.2655 0.1524 0.0928 0.0511  0.0538  0.0316  36  HIS A C   
286  O  O   . HIS A 38  ? 0.2653 0.2108 0.1071 0.0539  0.0482  0.0082  36  HIS A O   
287  C  CB  . HIS A 38  ? 0.2749 0.1403 0.1059 0.0295  0.0410  0.0479  36  HIS A CB  
288  C  CG  . HIS A 38  ? 0.2872 0.1445 0.1345 0.0287  0.0241  0.0374  36  HIS A CG  
289  N  ND1 . HIS A 38  ? 0.3061 0.1683 0.1673 0.0140  0.0041  0.0271  36  HIS A ND1 
290  C  CD2 . HIS A 38  ? 0.2878 0.1533 0.1486 0.0308  0.0008  0.0461  36  HIS A CD2 
291  C  CE1 . HIS A 38  ? 0.3076 0.1797 0.1809 0.0132  0.0045  0.0250  36  HIS A CE1 
292  N  NE2 . HIS A 38  ? 0.2914 0.1753 0.1779 0.0254  0.0059  0.0324  36  HIS A NE2 
293  N  N   . THR A 39  ? 0.2608 0.1403 0.1273 0.0715  0.0489  0.0176  37  THR A N   
294  C  CA  . THR A 39  ? 0.2719 0.1564 0.1541 0.0724  0.0328  0.0225  37  THR A CA  
295  C  C   . THR A 39  ? 0.2505 0.1523 0.1426 0.0778  0.0295  0.0124  37  THR A C   
296  O  O   . THR A 39  ? 0.2830 0.1596 0.1496 0.0863  0.0049  0.0015  37  THR A O   
297  C  CB  . THR A 39  ? 0.2889 0.1811 0.2223 0.0807  -0.0003 0.0229  37  THR A CB  
298  O  OG1 . THR A 39  ? 0.3291 0.2112 0.2829 0.0856  -0.0071 0.0360  37  THR A OG1 
299  C  CG2 . THR A 39  ? 0.3050 0.2126 0.2237 0.0788  0.0014  0.0184  37  THR A CG2 
300  N  N   . ALA A 40  ? 0.2255 0.1368 0.1142 0.0687  0.0399  0.0203  38  ALA A N   
301  C  CA  . ALA A 40  ? 0.2100 0.1432 0.1107 0.0710  0.0535  0.0149  38  ALA A CA  
302  C  C   . ALA A 40  ? 0.2125 0.1708 0.1247 0.0793  0.0615  0.0185  38  ALA A C   
303  O  O   . ALA A 40  ? 0.2520 0.2077 0.1765 0.0686  0.0692  0.0280  38  ALA A O   
304  C  CB  . ALA A 40  ? 0.1982 0.1364 0.1130 0.0621  0.0483  0.0237  38  ALA A CB  
305  N  N   . LYS A 41  ? 0.2187 0.1899 0.1067 0.0920  0.0430  0.0065  39  LYS A N   
306  C  CA  . LYS A 41  ? 0.2072 0.2210 0.1055 0.0987  0.0293  0.0101  39  LYS A CA  
307  C  C   . LYS A 41  ? 0.1734 0.2138 0.0718 0.0760  0.0285  0.0066  39  LYS A C   
308  O  O   . LYS A 41  ? 0.1387 0.2037 0.0700 0.0591  0.0263  0.0141  39  LYS A O   
309  C  CB  . LYS A 41  ? 0.2241 0.2337 0.1331 0.1056  0.0152  -0.0056 39  LYS A CB  
310  C  CG  . LYS A 41  ? 0.2256 0.2635 0.1511 0.1074  0.0086  -0.0065 39  LYS A CG  
311  C  CD  . LYS A 41  ? 0.2337 0.2767 0.1634 0.1071  -0.0092 -0.0086 39  LYS A CD  
312  C  CE  . LYS A 41  ? 0.2349 0.3111 0.1918 0.1163  -0.0006 -0.0303 39  LYS A CE  
313  N  NZ  . LYS A 41  ? 0.2729 0.3429 0.2064 0.1088  -0.0192 -0.0120 39  LYS A NZ  
314  N  N   . TYR A 42  ? 0.1910 0.2302 0.0977 0.0579  0.0407  0.0127  40  TYR A N   
315  C  CA  . TYR A 42  ? 0.1781 0.2441 0.0831 0.0392  0.0412  0.0070  40  TYR A CA  
316  C  C   . TYR A 42  ? 0.1593 0.2401 0.0813 0.0579  0.0275  -0.0109 40  TYR A C   
317  O  O   . TYR A 42  ? 0.1715 0.2541 0.0827 0.0733  0.0207  -0.0121 40  TYR A O   
318  C  CB  . TYR A 42  ? 0.2026 0.2765 0.0929 0.0035  0.0479  0.0158  40  TYR A CB  
319  C  CG  . TYR A 42  ? 0.2090 0.3190 0.1119 -0.0155 0.0460  0.0093  40  TYR A CG  
320  C  CD1 . TYR A 42  ? 0.1898 0.3433 0.1216 -0.0270 0.0381  0.0014  40  TYR A CD1 
321  C  CD2 . TYR A 42  ? 0.2104 0.3614 0.1286 -0.0110 0.0468  0.0026  40  TYR A CD2 
322  C  CE1 . TYR A 42  ? 0.2024 0.3752 0.1442 -0.0165 0.0299  -0.0054 40  TYR A CE1 
323  C  CE2 . TYR A 42  ? 0.1933 0.3885 0.1549 -0.0141 0.0448  0.0031  40  TYR A CE2 
324  C  CZ  . TYR A 42  ? 0.1861 0.3983 0.1597 -0.0165 0.0347  0.0007  40  TYR A CZ  
325  O  OH  . TYR A 42  ? 0.1976 0.4443 0.2404 -0.0004 0.0319  -0.0017 40  TYR A OH  
326  N  N   . ASP A 43  ? 0.1560 0.2355 0.0844 0.0687  0.0223  -0.0181 41  ASP A N   
327  C  CA  . ASP A 43  ? 0.1844 0.2487 0.1037 0.0774  0.0103  -0.0163 41  ASP A CA  
328  C  C   . ASP A 43  ? 0.2009 0.2819 0.1106 0.0903  0.0208  0.0033  41  ASP A C   
329  O  O   . ASP A 43  ? 0.1940 0.2835 0.1105 0.0773  0.0198  0.0057  41  ASP A O   
330  C  CB  . ASP A 43  ? 0.2077 0.2443 0.1493 0.0693  -0.0149 -0.0191 41  ASP A CB  
331  C  CG  . ASP A 43  ? 0.2603 0.2636 0.1884 0.0542  -0.0266 -0.0105 41  ASP A CG  
332  O  OD1 . ASP A 43  ? 0.3292 0.2433 0.1904 0.0588  -0.0359 -0.0420 41  ASP A OD1 
333  O  OD2 . ASP A 43  ? 0.3143 0.2846 0.2665 0.0112  -0.0563 -0.0151 41  ASP A OD2 
334  N  N   . PRO A 44  ? 0.2180 0.3238 0.1462 0.1155  0.0463  0.0199  42  PRO A N   
335  C  CA  . PRO A 44  ? 0.2285 0.3453 0.1679 0.1219  0.0591  0.0179  42  PRO A CA  
336  C  C   . PRO A 44  ? 0.2660 0.3539 0.1803 0.1243  0.0477  0.0153  42  PRO A C   
337  O  O   . PRO A 44  ? 0.2834 0.3987 0.2594 0.1490  0.0414  0.0246  42  PRO A O   
338  C  CB  . PRO A 44  ? 0.2490 0.3702 0.1841 0.1127  0.0620  0.0196  42  PRO A CB  
339  C  CG  . PRO A 44  ? 0.2684 0.3708 0.1817 0.1071  0.0547  0.0222  42  PRO A CG  
340  C  CD  . PRO A 44  ? 0.2561 0.3433 0.1580 0.1121  0.0472  0.0222  42  PRO A CD  
341  N  N   . SER A 45  ? 0.2764 0.3232 0.1633 0.1253  0.0424  0.0041  43  SER A N   
342  C  CA  . SER A 45  ? 0.3383 0.3236 0.2141 0.0931  0.0183  0.0041  43  SER A CA  
343  C  C   . SER A 45  ? 0.2954 0.2922 0.2153 0.0747  0.0097  0.0123  43  SER A C   
344  O  O   . SER A 45  ? 0.3544 0.3081 0.2848 0.0781  -0.0095 0.0415  43  SER A O   
345  C  CB  . SER A 45  ? 0.3778 0.3362 0.2317 0.0843  0.0171  0.0016  43  SER A CB  
346  O  OG  . SER A 45  ? 0.4113 0.3593 0.1898 0.0645  0.0305  -0.0023 43  SER A OG  
347  N  N   A LEU A 46  ? 0.2645 0.2659 0.1635 0.0619  0.0015  0.0228  44  LEU A N   
348  N  N   B LEU A 46  ? 0.2539 0.2734 0.1957 0.0461  0.0048  0.0117  44  LEU A N   
349  C  CA  A LEU A 46  ? 0.2221 0.2385 0.1502 0.0444  -0.0018 0.0242  44  LEU A CA  
350  C  CA  B LEU A 46  ? 0.2089 0.2495 0.1810 0.0297  0.0071  0.0139  44  LEU A CA  
351  C  C   A LEU A 46  ? 0.2111 0.2211 0.1566 0.0456  0.0088  0.0205  44  LEU A C   
352  C  C   B LEU A 46  ? 0.2043 0.2510 0.1971 0.0181  0.0092  0.0180  44  LEU A C   
353  O  O   A LEU A 46  ? 0.2000 0.2345 0.1369 0.0641  0.0337  0.0001  44  LEU A O   
354  O  O   B LEU A 46  ? 0.2029 0.2724 0.2219 0.0102  0.0020  0.0401  44  LEU A O   
355  C  CB  A LEU A 46  ? 0.2078 0.2225 0.1170 0.0328  -0.0082 0.0346  44  LEU A CB  
356  C  CB  B LEU A 46  ? 0.1911 0.2429 0.1473 0.0206  0.0125  0.0131  44  LEU A CB  
357  C  CG  A LEU A 46  ? 0.1991 0.2135 0.1094 0.0255  -0.0119 0.0388  44  LEU A CG  
358  C  CG  B LEU A 46  ? 0.1864 0.2282 0.1384 0.0112  0.0141  0.0113  44  LEU A CG  
359  C  CD1 A LEU A 46  ? 0.1956 0.2102 0.1051 0.0249  -0.0108 0.0388  44  LEU A CD1 
360  C  CD1 B LEU A 46  ? 0.1886 0.2236 0.1298 0.0068  0.0161  0.0070  44  LEU A CD1 
361  C  CD2 A LEU A 46  ? 0.1987 0.2113 0.1110 0.0197  -0.0186 0.0418  44  LEU A CD2 
362  C  CD2 B LEU A 46  ? 0.1855 0.2232 0.1371 0.0071  0.0163  0.0090  44  LEU A CD2 
363  N  N   A LYS A 47  ? 0.1830 0.2052 0.1635 0.0376  0.0117  0.0230  45  LYS A N   
364  N  N   B LYS A 47  ? 0.1888 0.2428 0.1985 0.0180  0.0086  0.0130  45  LYS A N   
365  C  CA  A LYS A 47  ? 0.1663 0.1953 0.1707 0.0363  0.0208  0.0194  45  LYS A CA  
366  C  CA  B LYS A 47  ? 0.1867 0.2265 0.1943 0.0132  0.0111  0.0151  45  LYS A CA  
367  C  C   A LYS A 47  ? 0.1300 0.1883 0.1595 0.0357  0.0290  0.0265  45  LYS A C   
368  C  C   B LYS A 47  ? 0.1582 0.2165 0.1867 0.0043  0.0188  0.0148  45  LYS A C   
369  O  O   A LYS A 47  ? 0.1207 0.1640 0.1314 0.0304  0.0365  0.0185  45  LYS A O   
370  O  O   B LYS A 47  ? 0.1582 0.1947 0.1749 -0.0001 0.0301  0.0131  45  LYS A O   
371  C  CB  A LYS A 47  ? 0.1868 0.1997 0.1897 0.0319  0.0137  0.0121  45  LYS A CB  
372  C  CB  B LYS A 47  ? 0.2008 0.2240 0.2083 0.0162  0.0058  0.0142  45  LYS A CB  
373  C  CG  A LYS A 47  ? 0.2169 0.2139 0.2137 0.0279  0.0096  0.0048  45  LYS A CG  
374  C  CG  B LYS A 47  ? 0.2261 0.2236 0.2174 0.0140  0.0061  0.0167  45  LYS A CG  
375  C  CD  A LYS A 47  ? 0.2372 0.2266 0.2315 0.0254  0.0097  0.0066  45  LYS A CD  
376  C  CD  B LYS A 47  ? 0.2454 0.2339 0.2320 0.0102  0.0123  0.0240  45  LYS A CD  
377  C  CE  A LYS A 47  ? 0.2540 0.2416 0.2456 0.0259  0.0103  0.0037  45  LYS A CE  
378  C  CE  B LYS A 47  ? 0.2634 0.2480 0.2513 0.0041  0.0027  0.0222  45  LYS A CE  
379  N  NZ  A LYS A 47  ? 0.2685 0.2483 0.2586 0.0250  0.0110  0.0068  45  LYS A NZ  
380  N  NZ  B LYS A 47  ? 0.2706 0.2605 0.2618 -0.0027 0.0030  0.0188  45  LYS A NZ  
381  N  N   A PRO A 48  ? 0.1084 0.1893 0.1575 0.0331  0.0374  0.0342  46  PRO A N   
382  N  N   B PRO A 48  ? 0.1397 0.2102 0.1861 -0.0087 0.0195  0.0080  46  PRO A N   
383  C  CA  A PRO A 48  ? 0.0966 0.1888 0.1598 0.0256  0.0314  0.0377  46  PRO A CA  
384  C  CA  B PRO A 48  ? 0.1336 0.2025 0.1821 -0.0123 0.0182  0.0121  46  PRO A CA  
385  C  C   A PRO A 48  ? 0.0885 0.1803 0.1606 0.0169  0.0280  0.0375  46  PRO A C   
386  C  C   B PRO A 48  ? 0.1134 0.1894 0.1762 -0.0203 0.0144  0.0100  46  PRO A C   
387  O  O   A PRO A 48  ? 0.1027 0.1848 0.1501 0.0173  0.0374  0.0369  46  PRO A O   
388  O  O   B PRO A 48  ? 0.1016 0.1800 0.1612 -0.0288 0.0098  0.0121  46  PRO A O   
389  C  CB  A PRO A 48  ? 0.0977 0.2029 0.1665 0.0286  0.0318  0.0392  46  PRO A CB  
390  C  CB  B PRO A 48  ? 0.1366 0.2127 0.1890 -0.0143 0.0173  0.0108  46  PRO A CB  
391  C  CG  A PRO A 48  ? 0.1049 0.2059 0.1699 0.0324  0.0352  0.0360  46  PRO A CG  
392  C  CG  B PRO A 48  ? 0.1441 0.2208 0.1944 -0.0045 0.0194  0.0055  46  PRO A CG  
393  C  CD  A PRO A 48  ? 0.1063 0.2032 0.1646 0.0327  0.0406  0.0327  46  PRO A CD  
394  C  CD  B PRO A 48  ? 0.1438 0.2167 0.1867 -0.0027 0.0222  0.0058  46  PRO A CD  
395  N  N   A LEU A 49  ? 0.0780 0.1697 0.1580 -0.0002 0.0269  0.0352  47  LEU A N   
396  N  N   B LEU A 49  ? 0.1076 0.1870 0.1835 -0.0203 0.0076  0.0147  47  LEU A N   
397  C  CA  A LEU A 49  ? 0.0682 0.1646 0.1628 -0.0130 0.0191  0.0337  47  LEU A CA  
398  C  CA  B LEU A 49  ? 0.0925 0.1819 0.1920 -0.0264 0.0074  0.0180  47  LEU A CA  
399  C  C   A LEU A 49  ? 0.0793 0.1635 0.1739 -0.0200 0.0084  0.0291  47  LEU A C   
400  C  C   B LEU A 49  ? 0.0915 0.1725 0.1822 -0.0266 0.0085  0.0218  47  LEU A C   
401  O  O   A LEU A 49  ? 0.0837 0.1609 0.1943 -0.0272 0.0006  0.0298  47  LEU A O   
402  O  O   B LEU A 49  ? 0.0880 0.1713 0.1755 -0.0243 0.0196  0.0221  47  LEU A O   
403  C  CB  A LEU A 49  ? 0.0700 0.1659 0.1638 -0.0126 0.0169  0.0344  47  LEU A CB  
404  C  CB  B LEU A 49  ? 0.1133 0.1895 0.2098 -0.0265 0.0059  0.0178  47  LEU A CB  
405  C  CG  A LEU A 49  ? 0.0607 0.1745 0.1662 -0.0085 0.0162  0.0363  47  LEU A CG  
406  C  CG  B LEU A 49  ? 0.1192 0.2060 0.2258 -0.0281 0.0067  0.0146  47  LEU A CG  
407  C  CD1 A LEU A 49  ? 0.0728 0.1715 0.1767 -0.0086 0.0100  0.0333  47  LEU A CD1 
408  C  CD1 B LEU A 49  ? 0.1166 0.2080 0.2254 -0.0257 0.0036  0.0174  47  LEU A CD1 
409  C  CD2 A LEU A 49  ? 0.0676 0.1763 0.1679 -0.0150 0.0165  0.0381  47  LEU A CD2 
410  C  CD2 B LEU A 49  ? 0.1146 0.2106 0.2334 -0.0293 0.0097  0.0069  47  LEU A CD2 
411  N  N   . SER A 50  ? 0.0840 0.1572 0.1596 -0.0249 0.0049  0.0231  48  SER A N   
412  C  CA  . SER A 50  ? 0.0996 0.1664 0.1540 -0.0226 0.0166  0.0142  48  SER A CA  
413  C  C   . SER A 50  ? 0.1070 0.1656 0.1443 -0.0341 0.0202  0.0017  48  SER A C   
414  O  O   . SER A 50  ? 0.1091 0.1636 0.1452 -0.0341 0.0201  -0.0220 48  SER A O   
415  C  CB  . SER A 50  ? 0.1184 0.1788 0.1700 -0.0097 0.0261  0.0130  48  SER A CB  
416  O  OG  . SER A 50  ? 0.1689 0.1975 0.1969 0.0032  0.0282  0.0278  48  SER A OG  
417  N  N   . VAL A 51  ? 0.1233 0.1795 0.1532 -0.0529 0.0219  0.0000  49  VAL A N   
418  C  CA  . VAL A 51  ? 0.1407 0.1953 0.1667 -0.0600 0.0309  -0.0097 49  VAL A CA  
419  C  C   . VAL A 51  ? 0.1376 0.2180 0.1682 -0.0664 0.0221  -0.0119 49  VAL A C   
420  O  O   . VAL A 51  ? 0.1554 0.2901 0.1783 -0.1033 0.0191  0.0098  49  VAL A O   
421  C  CB  . VAL A 51  ? 0.1820 0.2002 0.1883 -0.0562 0.0444  -0.0196 49  VAL A CB  
422  C  CG1 . VAL A 51  ? 0.2121 0.2063 0.1922 -0.0532 0.0486  -0.0174 49  VAL A CG1 
423  C  CG2 . VAL A 51  ? 0.1877 0.1847 0.2171 -0.0531 0.0423  -0.0208 49  VAL A CG2 
424  N  N   . SER A 52  ? 0.1184 0.2225 0.1610 -0.0551 0.0121  -0.0150 50  SER A N   
425  C  CA  . SER A 52  ? 0.1206 0.2366 0.1834 -0.0325 0.0101  -0.0146 50  SER A CA  
426  C  C   . SER A 52  ? 0.1101 0.2149 0.1790 -0.0193 -0.0008 -0.0058 50  SER A C   
427  O  O   . SER A 52  ? 0.1267 0.1964 0.1811 -0.0125 -0.0072 -0.0063 50  SER A O   
428  C  CB  . SER A 52  ? 0.1553 0.2611 0.1972 -0.0266 0.0078  -0.0167 50  SER A CB  
429  O  OG  . SER A 52  ? 0.2103 0.3124 0.2342 -0.0164 0.0114  -0.0203 50  SER A OG  
430  N  N   . TYR A 53  ? 0.1074 0.1973 0.1811 -0.0254 0.0046  -0.0033 51  TYR A N   
431  C  CA  . TYR A 53  ? 0.1099 0.1870 0.1762 -0.0137 -0.0023 -0.0004 51  TYR A CA  
432  C  C   . TYR A 53  ? 0.1086 0.2042 0.1764 -0.0048 0.0010  0.0140  51  TYR A C   
433  O  O   . TYR A 53  ? 0.1218 0.2156 0.1633 -0.0001 0.0021  0.0125  51  TYR A O   
434  C  CB  . TYR A 53  ? 0.1190 0.1661 0.1718 -0.0141 -0.0042 -0.0090 51  TYR A CB  
435  C  CG  . TYR A 53  ? 0.1121 0.1373 0.1524 -0.0231 -0.0012 -0.0114 51  TYR A CG  
436  C  CD1 . TYR A 53  ? 0.1101 0.1251 0.1502 -0.0204 -0.0020 -0.0119 51  TYR A CD1 
437  C  CD2 . TYR A 53  ? 0.1144 0.1232 0.1344 -0.0265 0.0038  -0.0125 51  TYR A CD2 
438  C  CE1 . TYR A 53  ? 0.1018 0.1137 0.1284 -0.0280 -0.0023 -0.0159 51  TYR A CE1 
439  C  CE2 . TYR A 53  ? 0.1143 0.1082 0.1292 -0.0287 -0.0001 -0.0106 51  TYR A CE2 
440  C  CZ  . TYR A 53  ? 0.1051 0.1088 0.1219 -0.0314 0.0017  -0.0115 51  TYR A CZ  
441  O  OH  . TYR A 53  ? 0.1006 0.1031 0.1291 -0.0254 0.0052  -0.0137 51  TYR A OH  
442  N  N   . ASP A 54  ? 0.1070 0.2413 0.2026 -0.0069 -0.0046 0.0208  52  ASP A N   
443  C  CA  . ASP A 54  ? 0.1196 0.2617 0.2325 0.0130  -0.0118 0.0253  52  ASP A CA  
444  C  C   . ASP A 54  ? 0.1365 0.2503 0.2286 0.0214  -0.0208 0.0264  52  ASP A C   
445  O  O   . ASP A 54  ? 0.2005 0.2405 0.2277 0.0011  -0.0439 0.0362  52  ASP A O   
446  C  CB  . ASP A 54  ? 0.1417 0.3164 0.2672 0.0178  -0.0116 0.0250  52  ASP A CB  
447  C  CG  . ASP A 54  ? 0.1959 0.3638 0.3136 0.0263  -0.0052 0.0219  52  ASP A CG  
448  O  OD1 . ASP A 54  ? 0.2822 0.4407 0.3333 0.0146  0.0151  0.0020  52  ASP A OD1 
449  O  OD2 . ASP A 54  ? 0.2980 0.4167 0.3800 0.0322  -0.0081 0.0484  52  ASP A OD2 
450  N  N   . GLN A 55  ? 0.1314 0.2341 0.2281 0.0316  -0.0042 0.0221  53  GLN A N   
451  C  CA  . GLN A 55  ? 0.1542 0.2353 0.2337 0.0184  -0.0015 0.0154  53  GLN A CA  
452  C  C   . GLN A 55  ? 0.1497 0.1993 0.1944 0.0091  0.0026  -0.0028 53  GLN A C   
453  O  O   . GLN A 55  ? 0.1602 0.2033 0.1935 0.0059  0.0039  0.0012  53  GLN A O   
454  C  CB  . GLN A 55  ? 0.1748 0.2564 0.2522 0.0202  0.0074  0.0164  53  GLN A CB  
455  C  CG  . GLN A 55  ? 0.1897 0.2759 0.2682 0.0142  0.0162  0.0250  53  GLN A CG  
456  C  CD  . GLN A 55  ? 0.2321 0.3159 0.2852 0.0031  0.0140  0.0431  53  GLN A CD  
457  O  OE1 . GLN A 55  ? 0.3030 0.3691 0.3185 -0.0127 0.0149  0.0654  53  GLN A OE1 
458  N  NE2 . GLN A 55  ? 0.2471 0.3418 0.2903 -0.0013 0.0160  0.0468  53  GLN A NE2 
459  N  N   . ALA A 56  ? 0.1222 0.1724 0.1843 -0.0034 0.0020  -0.0117 54  ALA A N   
460  C  CA  . ALA A 56  ? 0.1168 0.1585 0.1801 0.0014  -0.0084 -0.0187 54  ALA A CA  
461  C  C   . ALA A 56  ? 0.1283 0.1649 0.1739 -0.0006 -0.0116 -0.0256 54  ALA A C   
462  O  O   . ALA A 56  ? 0.1386 0.2193 0.1909 -0.0177 -0.0038 -0.0482 54  ALA A O   
463  C  CB  . ALA A 56  ? 0.1330 0.1648 0.1915 0.0046  -0.0054 -0.0203 54  ALA A CB  
464  N  N   . THR A 57  ? 0.1102 0.1306 0.1560 0.0136  -0.0201 -0.0060 55  THR A N   
465  C  CA  . THR A 57  ? 0.1245 0.1232 0.1594 0.0222  -0.0234 0.0121  55  THR A CA  
466  C  C   . THR A 57  ? 0.1092 0.1037 0.1315 0.0143  -0.0235 0.0178  55  THR A C   
467  O  O   . THR A 57  ? 0.1055 0.0876 0.1352 0.0097  -0.0150 0.0144  55  THR A O   
468  C  CB  . THR A 57  ? 0.1696 0.1427 0.1964 0.0298  -0.0263 0.0211  55  THR A CB  
469  O  OG1 . THR A 57  ? 0.2164 0.1794 0.2718 0.0422  -0.0351 0.0154  55  THR A OG1 
470  C  CG2 . THR A 57  ? 0.1926 0.1467 0.2063 0.0308  -0.0271 0.0287  55  THR A CG2 
471  N  N   . SER A 58  ? 0.1036 0.0891 0.1271 0.0104  -0.0234 0.0222  56  SER A N   
472  C  CA  . SER A 58  ? 0.1133 0.0827 0.1182 0.0067  -0.0196 0.0153  56  SER A CA  
473  C  C   . SER A 58  ? 0.1185 0.0843 0.1195 0.0141  -0.0115 0.0157  56  SER A C   
474  O  O   . SER A 58  ? 0.1233 0.0950 0.1227 0.0171  -0.0098 0.0270  56  SER A O   
475  C  CB  . SER A 58  ? 0.1271 0.0820 0.1157 -0.0014 -0.0228 0.0155  56  SER A CB  
476  O  OG  . SER A 58  ? 0.1349 0.0848 0.1243 -0.0104 -0.0318 0.0183  56  SER A OG  
477  N  N   . LEU A 59  ? 0.1225 0.0822 0.1107 0.0144  -0.0047 0.0166  57  LEU A N   
478  C  CA  . LEU A 59  ? 0.1382 0.0765 0.1214 0.0157  0.0036  0.0192  57  LEU A CA  
479  C  C   . LEU A 59  ? 0.1359 0.0760 0.1073 0.0160  0.0026  0.0211  57  LEU A C   
480  O  O   . LEU A 59  ? 0.1446 0.0983 0.1080 0.0239  -0.0019 0.0247  57  LEU A O   
481  C  CB  . LEU A 59  ? 0.1722 0.0892 0.1467 0.0037  0.0131  0.0192  57  LEU A CB  
482  C  CG  . LEU A 59  ? 0.2054 0.1044 0.1715 -0.0003 0.0145  0.0118  57  LEU A CG  
483  C  CD1 . LEU A 59  ? 0.2238 0.1152 0.1840 -0.0096 0.0176  -0.0016 57  LEU A CD1 
484  C  CD2 . LEU A 59  ? 0.2246 0.1155 0.1941 0.0081  0.0131  0.0180  57  LEU A CD2 
485  N  N   . ARG A 60  ? 0.1272 0.0749 0.1044 0.0187  0.0029  0.0165  58  ARG A N   
486  C  CA  . ARG A 60  ? 0.1234 0.0815 0.0961 0.0134  0.0068  0.0210  58  ARG A CA  
487  C  C   . ARG A 60  ? 0.1153 0.0760 0.0756 0.0101  0.0039  0.0177  58  ARG A C   
488  O  O   . ARG A 60  ? 0.1275 0.0791 0.0752 0.0156  0.0050  0.0130  58  ARG A O   
489  C  CB  . ARG A 60  ? 0.1407 0.0973 0.1199 0.0080  0.0103  0.0269  58  ARG A CB  
490  C  CG  . ARG A 60  ? 0.1488 0.1322 0.1479 -0.0032 0.0158  0.0274  58  ARG A CG  
491  C  CD  . ARG A 60  ? 0.1544 0.1463 0.1714 -0.0077 0.0211  0.0299  58  ARG A CD  
492  N  NE  . ARG A 60  ? 0.1504 0.1466 0.1845 -0.0199 0.0300  0.0282  58  ARG A NE  
493  C  CZ  . ARG A 60  ? 0.1491 0.1370 0.1967 -0.0241 0.0412  0.0329  58  ARG A CZ  
494  N  NH1 . ARG A 60  ? 0.1531 0.1481 0.2139 -0.0263 0.0489  0.0237  58  ARG A NH1 
495  N  NH2 . ARG A 60  ? 0.1570 0.1276 0.1932 -0.0245 0.0474  0.0345  58  ARG A NH2 
496  N  N   . ILE A 61  ? 0.1076 0.0840 0.0622 0.0091  0.0019  0.0134  59  ILE A N   
497  C  CA  . ILE A 61  ? 0.1079 0.0839 0.0673 0.0063  0.0023  0.0142  59  ILE A CA  
498  C  C   . ILE A 61  ? 0.1128 0.0867 0.0679 0.0014  0.0062  0.0159  59  ILE A C   
499  O  O   . ILE A 61  ? 0.1213 0.1193 0.0695 0.0095  0.0101  0.0229  59  ILE A O   
500  C  CB  . ILE A 61  ? 0.1058 0.0815 0.0772 0.0119  0.0069  0.0148  59  ILE A CB  
501  C  CG1 . ILE A 61  ? 0.1150 0.0833 0.0753 0.0133  0.0065  0.0112  59  ILE A CG1 
502  C  CG2 . ILE A 61  ? 0.1123 0.0854 0.0842 0.0187  0.0065  0.0089  59  ILE A CG2 
503  C  CD1 . ILE A 61  ? 0.1235 0.0862 0.0798 0.0101  0.0072  0.0081  59  ILE A CD1 
504  N  N   . LEU A 62  ? 0.1042 0.0817 0.0746 -0.0057 0.0100  0.0176  60  LEU A N   
505  C  CA  . LEU A 62  ? 0.1001 0.0823 0.0860 -0.0021 0.0110  0.0189  60  LEU A CA  
506  C  C   . LEU A 62  ? 0.0967 0.0799 0.0747 0.0022  0.0169  0.0165  60  LEU A C   
507  O  O   . LEU A 62  ? 0.0986 0.0902 0.0792 0.0090  0.0229  0.0224  60  LEU A O   
508  C  CB  . LEU A 62  ? 0.1097 0.0821 0.1109 -0.0070 0.0142  0.0206  60  LEU A CB  
509  C  CG  . LEU A 62  ? 0.1168 0.0883 0.1232 -0.0165 0.0163  0.0233  60  LEU A CG  
510  C  CD1 . LEU A 62  ? 0.1246 0.0895 0.1255 -0.0146 0.0188  0.0203  60  LEU A CD1 
511  C  CD2 . LEU A 62  ? 0.1335 0.1008 0.1346 -0.0193 0.0193  0.0206  60  LEU A CD2 
512  N  N   . ASN A 63  ? 0.1017 0.0778 0.0694 0.0034  0.0186  0.0108  61  ASN A N   
513  C  CA  . ASN A 63  ? 0.1018 0.0790 0.0745 -0.0002 0.0212  0.0114  61  ASN A CA  
514  C  C   . ASN A 63  ? 0.1035 0.0753 0.0750 -0.0025 0.0181  0.0154  61  ASN A C   
515  O  O   . ASN A 63  ? 0.1151 0.0852 0.0826 -0.0107 0.0255  0.0140  61  ASN A O   
516  C  CB  . ASN A 63  ? 0.1017 0.0810 0.0799 -0.0007 0.0248  0.0089  61  ASN A CB  
517  C  CG  . ASN A 63  ? 0.1049 0.0793 0.0790 0.0003  0.0232  0.0077  61  ASN A CG  
518  O  OD1 . ASN A 63  ? 0.1043 0.0798 0.0859 0.0061  0.0140  0.0093  61  ASN A OD1 
519  N  ND2 . ASN A 63  ? 0.1099 0.0829 0.0851 0.0017  0.0325  0.0029  61  ASN A ND2 
520  N  N   . ASN A 64  ? 0.1051 0.0746 0.0813 -0.0078 0.0163  0.0119  62  ASN A N   
521  C  CA  . ASN A 64  ? 0.1065 0.0910 0.0970 -0.0107 0.0156  0.0104  62  ASN A CA  
522  C  C   . ASN A 64  ? 0.1099 0.1021 0.1058 -0.0143 0.0119  0.0167  62  ASN A C   
523  O  O   . ASN A 64  ? 0.1233 0.1273 0.1326 -0.0247 0.0054  0.0114  62  ASN A O   
524  C  CB  . ASN A 64  ? 0.1164 0.0971 0.0991 -0.0070 0.0109  0.0062  62  ASN A CB  
525  C  CG  . ASN A 64  ? 0.1248 0.0996 0.1042 -0.0072 0.0117  0.0052  62  ASN A CG  
526  O  OD1 . ASN A 64  ? 0.1328 0.1013 0.1064 -0.0075 0.0149  0.0088  62  ASN A OD1 
527  N  ND2 . ASN A 64  ? 0.1557 0.1129 0.1274 -0.0017 0.0205  0.0076  62  ASN A ND2 
528  N  N   . GLY A 65  ? 0.1009 0.0994 0.1015 -0.0134 0.0143  0.0160  63  GLY A N   
529  C  CA  . GLY A 65  ? 0.1032 0.1101 0.1116 -0.0100 0.0140  0.0161  63  GLY A CA  
530  C  C   . GLY A 65  ? 0.1091 0.1054 0.1122 -0.0072 0.0104  0.0186  63  GLY A C   
531  O  O   . GLY A 65  ? 0.1243 0.1150 0.1265 0.0055  0.0100  0.0170  63  GLY A O   
532  N  N   A HIS A 66  ? 0.1048 0.1061 0.1058 -0.0060 0.0077  0.0262  64  HIS A N   
533  N  N   B HIS A 66  ? 0.1043 0.1044 0.1022 -0.0121 0.0093  0.0238  64  HIS A N   
534  C  CA  A HIS A 66  ? 0.1104 0.1107 0.1041 -0.0068 0.0035  0.0267  64  HIS A CA  
535  C  CA  B HIS A 66  ? 0.1064 0.1076 0.1006 -0.0175 0.0072  0.0222  64  HIS A CA  
536  C  C   A HIS A 66  ? 0.1067 0.1022 0.0945 -0.0083 0.0072  0.0258  64  HIS A C   
537  C  C   B HIS A 66  ? 0.1035 0.0952 0.0882 -0.0169 0.0070  0.0226  64  HIS A C   
538  O  O   A HIS A 66  ? 0.1097 0.1030 0.0997 -0.0026 0.0101  0.0287  64  HIS A O   
539  O  O   B HIS A 66  ? 0.1032 0.0867 0.0853 -0.0205 0.0048  0.0216  64  HIS A O   
540  C  CB  A HIS A 66  ? 0.1190 0.1252 0.1099 -0.0062 -0.0022 0.0265  64  HIS A CB  
541  C  CB  B HIS A 66  ? 0.1118 0.1240 0.1074 -0.0238 0.0068  0.0190  64  HIS A CB  
542  C  CG  A HIS A 66  ? 0.1346 0.1435 0.1231 -0.0017 -0.0083 0.0184  64  HIS A CG  
543  C  CG  B HIS A 66  ? 0.1222 0.1487 0.1244 -0.0307 0.0046  0.0123  64  HIS A CG  
544  N  ND1 A HIS A 66  ? 0.1493 0.1500 0.1470 -0.0002 -0.0119 0.0146  64  HIS A ND1 
545  N  ND1 B HIS A 66  ? 0.1301 0.1686 0.1456 -0.0329 0.0039  0.0019  64  HIS A ND1 
546  C  CD2 A HIS A 66  ? 0.1408 0.1481 0.1337 -0.0036 -0.0094 0.0152  64  HIS A CD2 
547  C  CD2 B HIS A 66  ? 0.1287 0.1592 0.1434 -0.0370 0.0089  0.0098  64  HIS A CD2 
548  C  CE1 A HIS A 66  ? 0.1554 0.1517 0.1452 -0.0029 -0.0163 0.0083  64  HIS A CE1 
549  C  CE1 B HIS A 66  ? 0.1317 0.1714 0.1457 -0.0350 0.0063  0.0067  64  HIS A CE1 
550  N  NE2 A HIS A 66  ? 0.1536 0.1510 0.1412 0.0000  -0.0158 0.0104  64  HIS A NE2 
551  N  NE2 B HIS A 66  ? 0.1350 0.1678 0.1566 -0.0391 0.0078  0.0077  64  HIS A NE2 
552  N  N   . ALA A 67  ? 0.1030 0.0870 0.0920 -0.0100 0.0104  0.0236  65  ALA A N   
553  C  CA  . ALA A 67  ? 0.1004 0.0877 0.0821 -0.0075 0.0074  0.0220  65  ALA A CA  
554  C  C   . ALA A 67  ? 0.0990 0.0828 0.0750 -0.0037 0.0100  0.0217  65  ALA A C   
555  O  O   . ALA A 67  ? 0.1052 0.0990 0.0878 -0.0097 0.0144  0.0245  65  ALA A O   
556  C  CB  . ALA A 67  ? 0.1034 0.0999 0.0893 -0.0024 0.0086  0.0231  65  ALA A CB  
557  N  N   . PHE A 68  ? 0.0996 0.0822 0.0721 0.0008  0.0120  0.0198  66  PHE A N   
558  C  CA  . PHE A 68  ? 0.1026 0.0875 0.0752 0.0090  0.0118  0.0111  66  PHE A CA  
559  C  C   . PHE A 68  ? 0.1035 0.0776 0.0722 0.0071  0.0132  0.0106  66  PHE A C   
560  O  O   . PHE A 68  ? 0.1175 0.0706 0.0804 0.0047  0.0135  0.0178  66  PHE A O   
561  C  CB  . PHE A 68  ? 0.1115 0.0990 0.0698 0.0119  0.0098  0.0106  66  PHE A CB  
562  C  CG  . PHE A 68  ? 0.1168 0.1044 0.0720 0.0081  0.0009  0.0014  66  PHE A CG  
563  C  CD1 . PHE A 68  ? 0.1161 0.1107 0.0732 0.0096  -0.0087 0.0003  66  PHE A CD1 
564  C  CD2 . PHE A 68  ? 0.1242 0.1105 0.0760 0.0094  -0.0025 -0.0091 66  PHE A CD2 
565  C  CE1 . PHE A 68  ? 0.1199 0.1206 0.0829 0.0075  -0.0123 -0.0012 66  PHE A CE1 
566  C  CE2 . PHE A 68  ? 0.1335 0.1134 0.0856 0.0058  -0.0076 -0.0102 66  PHE A CE2 
567  C  CZ  . PHE A 68  ? 0.1235 0.1165 0.0796 0.0014  -0.0131 -0.0075 66  PHE A CZ  
568  N  N   . ASN A 69  ? 0.1007 0.0782 0.0703 0.0088  0.0117  0.0162  67  ASN A N   
569  C  CA  . ASN A 69  ? 0.1001 0.0778 0.0728 0.0052  0.0117  0.0149  67  ASN A CA  
570  C  C   . ASN A 69  ? 0.1001 0.0708 0.0670 0.0069  0.0100  0.0145  67  ASN A C   
571  O  O   . ASN A 69  ? 0.1049 0.0823 0.0655 0.0071  0.0142  0.0147  67  ASN A O   
572  C  CB  . ASN A 69  ? 0.1091 0.0948 0.0929 -0.0020 0.0087  0.0127  67  ASN A CB  
573  C  CG  . ASN A 69  ? 0.1172 0.1059 0.1083 -0.0133 0.0027  0.0119  67  ASN A CG  
574  O  OD1 . ASN A 69  ? 0.1530 0.1504 0.1908 -0.0281 -0.0159 0.0014  67  ASN A OD1 
575  N  ND2 . ASN A 69  ? 0.1187 0.1252 0.0956 -0.0173 0.0014  0.0207  67  ASN A ND2 
576  N  N   . VAL A 70  ? 0.0988 0.0577 0.0679 0.0078  0.0114  0.0110  68  VAL A N   
577  C  CA  . VAL A 70  ? 0.1026 0.0620 0.0706 0.0088  0.0109  0.0067  68  VAL A CA  
578  C  C   . VAL A 70  ? 0.1040 0.0585 0.0693 0.0101  0.0122  0.0079  68  VAL A C   
579  O  O   . VAL A 70  ? 0.1055 0.0599 0.0665 0.0132  0.0110  0.0050  68  VAL A O   
580  C  CB  . VAL A 70  ? 0.1038 0.0678 0.0836 0.0078  0.0109  0.0036  68  VAL A CB  
581  C  CG1 . VAL A 70  ? 0.1055 0.0799 0.0870 0.0108  0.0055  0.0025  68  VAL A CG1 
582  C  CG2 . VAL A 70  ? 0.1000 0.0729 0.0848 0.0034  0.0175  -0.0013 68  VAL A CG2 
583  N  N   . GLU A 71  ? 0.1117 0.0588 0.0738 0.0098  0.0126  0.0117  69  GLU A N   
584  C  CA  . GLU A 71  ? 0.1128 0.0597 0.0883 0.0084  0.0108  0.0136  69  GLU A CA  
585  C  C   . GLU A 71  ? 0.1123 0.0569 0.0905 0.0102  0.0028  0.0106  69  GLU A C   
586  O  O   . GLU A 71  ? 0.1253 0.0724 0.0984 0.0194  -0.0080 0.0014  69  GLU A O   
587  C  CB  . GLU A 71  ? 0.1221 0.0685 0.0989 0.0103  0.0210  0.0197  69  GLU A CB  
588  C  CG  . GLU A 71  ? 0.1302 0.0817 0.1179 0.0107  0.0284  0.0212  69  GLU A CG  
589  C  CD  . GLU A 71  ? 0.1474 0.1095 0.1438 0.0076  0.0334  0.0301  69  GLU A CD  
590  O  OE1 . GLU A 71  ? 0.1568 0.1254 0.1590 -0.0012 0.0483  0.0459  69  GLU A OE1 
591  O  OE2 . GLU A 71  ? 0.1586 0.1330 0.1788 0.0021  0.0349  0.0259  69  GLU A OE2 
592  N  N   . PHE A 72  ? 0.1026 0.0566 0.0914 0.0074  0.0004  0.0102  70  PHE A N   
593  C  CA  . PHE A 72  ? 0.1057 0.0559 0.1050 0.0078  -0.0004 0.0112  70  PHE A CA  
594  C  C   . PHE A 72  ? 0.1140 0.0571 0.1315 0.0076  -0.0075 0.0082  70  PHE A C   
595  O  O   . PHE A 72  ? 0.1183 0.0599 0.1486 0.0019  -0.0124 0.0078  70  PHE A O   
596  C  CB  . PHE A 72  ? 0.1013 0.0556 0.0966 0.0106  0.0017  0.0116  70  PHE A CB  
597  C  CG  . PHE A 72  ? 0.0975 0.0566 0.0872 0.0095  0.0069  0.0130  70  PHE A CG  
598  C  CD1 . PHE A 72  ? 0.1031 0.0617 0.0944 0.0118  0.0114  0.0145  70  PHE A CD1 
599  C  CD2 . PHE A 72  ? 0.1017 0.0581 0.0921 0.0059  0.0026  0.0127  70  PHE A CD2 
600  C  CE1 . PHE A 72  ? 0.1085 0.0675 0.1009 0.0085  0.0133  0.0156  70  PHE A CE1 
601  C  CE2 . PHE A 72  ? 0.1071 0.0668 0.0960 0.0003  0.0040  0.0105  70  PHE A CE2 
602  C  CZ  . PHE A 72  ? 0.1150 0.0652 0.0997 0.0005  0.0094  0.0103  70  PHE A CZ  
603  N  N   . ASP A 73  ? 0.1244 0.0580 0.1702 0.0053  -0.0215 0.0090  71  ASP A N   
604  C  CA  . ASP A 73  ? 0.1359 0.0596 0.1957 0.0128  -0.0227 0.0207  71  ASP A CA  
605  C  C   . ASP A 73  ? 0.1399 0.0646 0.2093 0.0050  -0.0065 0.0097  71  ASP A C   
606  O  O   . ASP A 73  ? 0.1501 0.1076 0.2326 -0.0032 0.0153  -0.0113 71  ASP A O   
607  C  CB  . ASP A 73  ? 0.1579 0.0735 0.2179 0.0165  -0.0353 0.0224  71  ASP A CB  
608  C  CG  . ASP A 73  ? 0.1830 0.0812 0.2467 0.0259  -0.0426 0.0179  71  ASP A CG  
609  O  OD1 . ASP A 73  ? 0.2094 0.0687 0.2690 0.0178  -0.0408 0.0180  71  ASP A OD1 
610  O  OD2 . ASP A 73  ? 0.2092 0.1002 0.2996 0.0242  -0.0569 0.0129  71  ASP A OD2 
611  N  N   . ASP A 74  ? 0.1468 0.0648 0.1999 0.0004  -0.0057 0.0238  72  ASP A N   
612  C  CA  . ASP A 74  ? 0.1689 0.0711 0.2037 -0.0039 0.0040  0.0125  72  ASP A CA  
613  C  C   . ASP A 74  ? 0.1885 0.0746 0.2341 -0.0092 0.0064  0.0093  72  ASP A C   
614  O  O   . ASP A 74  ? 0.2330 0.0766 0.2555 -0.0171 0.0086  -0.0057 72  ASP A O   
615  C  CB  . ASP A 74  ? 0.1758 0.0709 0.1867 -0.0027 0.0049  0.0146  72  ASP A CB  
616  C  CG  . ASP A 74  ? 0.1760 0.0930 0.1610 -0.0041 0.0039  0.0169  72  ASP A CG  
617  O  OD1 . ASP A 74  ? 0.1730 0.1365 0.1541 -0.0161 0.0015  0.0377  72  ASP A OD1 
618  O  OD2 . ASP A 74  ? 0.1792 0.1330 0.1561 -0.0053 0.0069  0.0071  72  ASP A OD2 
619  N  N   . SER A 75  ? 0.1722 0.0632 0.2552 -0.0079 0.0154  0.0090  73  SER A N   
620  C  CA  . SER A 75  ? 0.1895 0.0648 0.2779 0.0001  0.0174  0.0033  73  SER A CA  
621  C  C   . SER A 75  ? 0.1891 0.0699 0.2895 0.0030  0.0189  -0.0199 73  SER A C   
622  O  O   . SER A 75  ? 0.1979 0.0688 0.2864 0.0129  0.0115  -0.0172 73  SER A O   
623  C  CB  . SER A 75  ? 0.2207 0.0924 0.2890 -0.0030 0.0232  0.0148  73  SER A CB  
624  O  OG  . SER A 75  ? 0.2377 0.0721 0.2936 0.0132  0.0250  0.0296  73  SER A OG  
625  N  N   . GLN A 76  ? 0.1935 0.0903 0.3063 0.0086  0.0196  -0.0137 74  GLN A N   
626  C  CA  . GLN A 76  ? 0.1987 0.1193 0.3110 0.0088  0.0169  -0.0214 74  GLN A CA  
627  C  C   . GLN A 76  ? 0.1936 0.1569 0.2852 -0.0104 -0.0051 -0.0237 74  GLN A C   
628  O  O   . GLN A 76  ? 0.1906 0.1377 0.2533 -0.0379 -0.0083 -0.0072 74  GLN A O   
629  C  CB  . GLN A 76  ? 0.2259 0.1475 0.3426 0.0021  0.0149  -0.0059 74  GLN A CB  
630  C  CG  . GLN A 76  ? 0.2304 0.1806 0.3699 0.0094  0.0107  0.0073  74  GLN A CG  
631  C  CD  . GLN A 76  ? 0.2302 0.2074 0.3788 0.0162  0.0040  0.0187  74  GLN A CD  
632  O  OE1 . GLN A 76  ? 0.2650 0.2654 0.3949 0.0291  -0.0019 0.0315  74  GLN A OE1 
633  N  NE2 . GLN A 76  ? 0.2320 0.2035 0.3831 0.0214  0.0046  0.0253  74  GLN A NE2 
634  N  N   . ASP A 77  ? 0.2456 0.2190 0.2861 -0.0008 -0.0256 -0.0363 75  ASP A N   
635  C  CA  . ASP A 77  ? 0.2524 0.2425 0.2954 0.0105  -0.0420 -0.0256 75  ASP A CA  
636  C  C   . ASP A 77  ? 0.2289 0.2410 0.2771 0.0172  -0.0600 -0.0061 75  ASP A C   
637  O  O   . ASP A 77  ? 0.2761 0.2458 0.3148 0.0381  -0.0654 -0.0019 75  ASP A O   
638  C  CB  . ASP A 77  ? 0.2891 0.2617 0.2991 0.0353  -0.0455 -0.0099 75  ASP A CB  
639  C  CG  . ASP A 77  ? 0.2971 0.2801 0.3035 0.0361  -0.0352 -0.0091 75  ASP A CG  
640  O  OD1 . ASP A 77  ? 0.2942 0.3375 0.3022 0.0388  -0.0285 0.0011  75  ASP A OD1 
641  O  OD2 . ASP A 77  ? 0.3368 0.3128 0.3480 0.0337  -0.0257 -0.0028 75  ASP A OD2 
642  N  N   . LYS A 78  ? 0.2082 0.1950 0.2752 0.0258  -0.0727 0.0178  76  LYS A N   
643  C  CA  . LYS A 78  ? 0.2200 0.1735 0.3006 0.0023  -0.0644 0.0150  76  LYS A CA  
644  C  C   . LYS A 78  ? 0.2164 0.1965 0.2897 0.0056  -0.0606 0.0088  76  LYS A C   
645  O  O   . LYS A 78  ? 0.2309 0.2477 0.3102 -0.0013 -0.0724 -0.0049 76  LYS A O   
646  C  CB  . LYS A 78  ? 0.2611 0.1752 0.3166 -0.0117 -0.0658 0.0282  76  LYS A CB  
647  C  CG  . LYS A 78  ? 0.2885 0.1799 0.3426 -0.0130 -0.0605 0.0305  76  LYS A CG  
648  C  CD  . LYS A 78  ? 0.3017 0.2055 0.3624 -0.0263 -0.0540 0.0304  76  LYS A CD  
649  C  CE  . LYS A 78  ? 0.3184 0.2315 0.3849 -0.0192 -0.0600 0.0380  76  LYS A CE  
650  N  NZ  . LYS A 78  ? 0.3502 0.2500 0.4054 -0.0179 -0.0569 0.0344  76  LYS A NZ  
651  N  N   . ALA A 79  ? 0.1809 0.1947 0.2560 0.0059  -0.0602 0.0020  77  ALA A N   
652  C  CA  . ALA A 79  ? 0.1464 0.1786 0.2159 -0.0001 -0.0517 0.0060  77  ALA A CA  
653  C  C   . ALA A 79  ? 0.1227 0.1579 0.2105 -0.0125 -0.0433 -0.0047 77  ALA A C   
654  O  O   . ALA A 79  ? 0.1224 0.2005 0.2381 -0.0106 -0.0263 -0.0351 77  ALA A O   
655  C  CB  . ALA A 79  ? 0.1611 0.1959 0.2075 0.0027  -0.0592 0.0030  77  ALA A CB  
656  N  N   . VAL A 80  ? 0.1300 0.1378 0.1875 -0.0105 -0.0427 -0.0067 78  VAL A N   
657  C  CA  . VAL A 80  ? 0.1425 0.1291 0.1902 -0.0140 -0.0340 -0.0005 78  VAL A CA  
658  C  C   . VAL A 80  ? 0.1221 0.1081 0.1780 -0.0200 -0.0236 -0.0039 78  VAL A C   
659  O  O   . VAL A 80  ? 0.1185 0.1470 0.1854 -0.0333 -0.0394 0.0081  78  VAL A O   
660  C  CB  . VAL A 80  ? 0.1830 0.1487 0.2130 -0.0029 -0.0249 -0.0018 78  VAL A CB  
661  C  CG1 . VAL A 80  ? 0.1799 0.1413 0.2237 0.0106  -0.0260 0.0026  78  VAL A CG1 
662  C  CG2 . VAL A 80  ? 0.1948 0.1626 0.2196 0.0079  -0.0172 -0.0035 78  VAL A CG2 
663  N  N   . LEU A 81  ? 0.1058 0.1029 0.1609 -0.0198 -0.0098 -0.0058 79  LEU A N   
664  C  CA  . LEU A 81  ? 0.1058 0.0985 0.1525 -0.0185 0.0054  -0.0052 79  LEU A CA  
665  C  C   . LEU A 81  ? 0.1215 0.1042 0.1398 -0.0206 0.0124  -0.0020 79  LEU A C   
666  O  O   . LEU A 81  ? 0.1288 0.1163 0.1460 -0.0291 0.0163  -0.0133 79  LEU A O   
667  C  CB  . LEU A 81  ? 0.1067 0.1133 0.1593 -0.0156 0.0098  0.0020  79  LEU A CB  
668  C  CG  . LEU A 81  ? 0.1161 0.1199 0.1609 -0.0014 0.0212  0.0035  79  LEU A CG  
669  C  CD1 . LEU A 81  ? 0.1293 0.1302 0.1793 0.0001  0.0238  0.0172  79  LEU A CD1 
670  C  CD2 . LEU A 81  ? 0.1196 0.1218 0.1655 0.0059  0.0191  0.0013  79  LEU A CD2 
671  N  N   . LYS A 82  ? 0.1280 0.1097 0.1529 -0.0143 0.0252  -0.0025 80  LYS A N   
672  C  CA  . LYS A 82  ? 0.1505 0.1153 0.1632 -0.0084 0.0293  0.0006  80  LYS A CA  
673  C  C   . LYS A 82  ? 0.1298 0.1186 0.1626 -0.0072 0.0352  0.0008  80  LYS A C   
674  O  O   . LYS A 82  ? 0.1200 0.1224 0.1587 -0.0194 0.0134  0.0028  80  LYS A O   
675  C  CB  . LYS A 82  ? 0.2061 0.1487 0.1858 0.0063  0.0264  0.0040  80  LYS A CB  
676  C  CG  . LYS A 82  ? 0.2281 0.1734 0.2125 -0.0003 0.0328  0.0048  80  LYS A CG  
677  C  CD  . LYS A 82  ? 0.2572 0.2135 0.2486 0.0064  0.0224  -0.0016 80  LYS A CD  
678  C  CE  . LYS A 82  ? 0.2884 0.2514 0.2796 -0.0038 0.0240  -0.0015 80  LYS A CE  
679  N  NZ  . LYS A 82  ? 0.3432 0.2872 0.2994 -0.0091 0.0301  0.0029  80  LYS A NZ  
680  N  N   . GLY A 83  ? 0.1362 0.1231 0.1753 -0.0067 0.0442  -0.0005 81  GLY A N   
681  C  CA  . GLY A 83  ? 0.1296 0.1181 0.1761 -0.0024 0.0580  0.0023  81  GLY A CA  
682  C  C   . GLY A 83  ? 0.1304 0.1106 0.1779 -0.0021 0.0615  0.0041  81  GLY A C   
683  O  O   . GLY A 83  ? 0.1322 0.1200 0.1525 -0.0241 0.0557  -0.0079 81  GLY A O   
684  N  N   . GLY A 84  ? 0.1242 0.1275 0.1965 -0.0001 0.0649  0.0149  82  GLY A N   
685  C  CA  . GLY A 84  ? 0.1389 0.1262 0.2112 0.0126  0.0597  0.0129  82  GLY A CA  
686  C  C   . GLY A 84  ? 0.1426 0.1265 0.2053 0.0238  0.0589  0.0112  82  GLY A C   
687  O  O   . GLY A 84  ? 0.1706 0.1697 0.2233 0.0376  0.0843  0.0008  82  GLY A O   
688  N  N   . PRO A 85  ? 0.1279 0.1209 0.1813 0.0231  0.0504  0.0161  83  PRO A N   
689  C  CA  . PRO A 85  ? 0.1434 0.1369 0.1803 0.0230  0.0409  0.0055  83  PRO A CA  
690  C  C   . PRO A 85  ? 0.1444 0.1325 0.1711 0.0137  0.0352  -0.0070 83  PRO A C   
691  O  O   . PRO A 85  ? 0.1783 0.1742 0.1879 -0.0036 0.0114  0.0021  83  PRO A O   
692  C  CB  . PRO A 85  ? 0.1455 0.1352 0.1753 0.0261  0.0392  0.0119  83  PRO A CB  
693  C  CG  . PRO A 85  ? 0.1344 0.1290 0.1692 0.0290  0.0442  0.0123  83  PRO A CG  
694  C  CD  . PRO A 85  ? 0.1325 0.1275 0.1792 0.0242  0.0437  0.0130  83  PRO A CD  
695  N  N   . LEU A 86  ? 0.1320 0.1041 0.1473 0.0071  0.0349  -0.0173 84  LEU A N   
696  C  CA  . LEU A 86  ? 0.1279 0.1004 0.1453 0.0079  0.0368  -0.0281 84  LEU A CA  
697  C  C   . LEU A 86  ? 0.1465 0.1153 0.1576 0.0079  0.0416  -0.0433 84  LEU A C   
698  O  O   . LEU A 86  ? 0.1426 0.1427 0.1879 0.0145  0.0385  -0.0546 84  LEU A O   
699  C  CB  . LEU A 86  ? 0.1155 0.0852 0.1348 0.0122  0.0359  -0.0215 84  LEU A CB  
700  C  CG  . LEU A 86  ? 0.1101 0.0838 0.1317 0.0114  0.0345  -0.0226 84  LEU A CG  
701  C  CD1 . LEU A 86  ? 0.1169 0.0925 0.1410 0.0102  0.0305  -0.0201 84  LEU A CD1 
702  C  CD2 . LEU A 86  ? 0.1125 0.0849 0.1287 0.0159  0.0343  -0.0206 84  LEU A CD2 
703  N  N   . ASP A 87  ? 0.1702 0.1212 0.1807 0.0045  0.0420  -0.0625 85  ASP A N   
704  C  CA  . ASP A 87  ? 0.2157 0.1349 0.2011 0.0056  0.0393  -0.0648 85  ASP A CA  
705  C  C   . ASP A 87  ? 0.2151 0.1277 0.2150 -0.0012 0.0485  -0.0523 85  ASP A C   
706  O  O   . ASP A 87  ? 0.2361 0.1756 0.2186 0.0083  0.0689  -0.0390 85  ASP A O   
707  C  CB  . ASP A 87  ? 0.2659 0.1688 0.2185 -0.0011 0.0310  -0.0709 85  ASP A CB  
708  C  CG  . ASP A 87  ? 0.3010 0.2267 0.2558 -0.0154 0.0269  -0.0637 85  ASP A CG  
709  O  OD1 . ASP A 87  ? 0.3354 0.2904 0.2857 -0.0209 0.0239  -0.0491 85  ASP A OD1 
710  O  OD2 . ASP A 87  ? 0.3480 0.3155 0.2957 -0.0176 0.0238  -0.0629 85  ASP A OD2 
711  N  N   . GLY A 88  ? 0.2275 0.1498 0.2164 -0.0206 0.0353  -0.0368 86  GLY A N   
712  C  CA  . GLY A 88  ? 0.2166 0.1239 0.2077 -0.0195 0.0338  -0.0335 86  GLY A CA  
713  C  C   . GLY A 88  ? 0.2000 0.1146 0.2035 -0.0158 0.0232  -0.0311 86  GLY A C   
714  O  O   . GLY A 88  ? 0.2467 0.1498 0.2221 -0.0441 0.0209  -0.0121 86  GLY A O   
715  N  N   A THR A 89  ? 0.1678 0.0913 0.1871 -0.0114 0.0243  -0.0302 87  THR A N   
716  N  N   B THR A 89  ? 0.1602 0.0955 0.1886 -0.0099 0.0252  -0.0330 87  THR A N   
717  C  CA  A THR A 89  ? 0.1516 0.0907 0.1835 0.0002  0.0247  -0.0274 87  THR A CA  
718  C  CA  B THR A 89  ? 0.1407 0.0980 0.1859 0.0026  0.0269  -0.0303 87  THR A CA  
719  C  C   A THR A 89  ? 0.1316 0.0803 0.1620 -0.0005 0.0183  -0.0263 87  THR A C   
720  C  C   B THR A 89  ? 0.1257 0.0831 0.1647 -0.0002 0.0193  -0.0273 87  THR A C   
721  O  O   A THR A 89  ? 0.1395 0.0627 0.1627 0.0007  0.0171  -0.0256 87  THR A O   
722  O  O   B THR A 89  ? 0.1353 0.0677 0.1682 -0.0019 0.0166  -0.0258 87  THR A O   
723  C  CB  A THR A 89  ? 0.1616 0.1024 0.1926 0.0054  0.0265  -0.0232 87  THR A CB  
724  C  CB  B THR A 89  ? 0.1389 0.1041 0.1969 0.0086  0.0320  -0.0311 87  THR A CB  
725  O  OG1 A THR A 89  ? 0.1752 0.1132 0.1936 0.0066  0.0243  -0.0171 87  THR A OG1 
726  O  OG1 B THR A 89  ? 0.1379 0.1247 0.2120 0.0199  0.0394  -0.0305 87  THR A OG1 
727  C  CG2 A THR A 89  ? 0.1656 0.0953 0.1978 0.0064  0.0317  -0.0211 87  THR A CG2 
728  C  CG2 B THR A 89  ? 0.1494 0.1091 0.2004 0.0100  0.0281  -0.0291 87  THR A CG2 
729  N  N   . TYR A 90  ? 0.1055 0.0777 0.1452 -0.0026 0.0133  -0.0252 88  TYR A N   
730  C  CA  . TYR A 90  ? 0.1060 0.0756 0.1327 0.0011  0.0078  -0.0190 88  TYR A CA  
731  C  C   . TYR A 90  ? 0.1030 0.0835 0.1336 -0.0015 -0.0042 -0.0095 88  TYR A C   
732  O  O   . TYR A 90  ? 0.1280 0.1198 0.1506 -0.0235 -0.0156 -0.0009 88  TYR A O   
733  C  CB  . TYR A 90  ? 0.1115 0.0634 0.1297 0.0029  0.0071  -0.0204 88  TYR A CB  
734  C  CG  . TYR A 90  ? 0.1071 0.0576 0.1150 0.0035  0.0147  -0.0166 88  TYR A CG  
735  C  CD1 . TYR A 90  ? 0.1029 0.0660 0.1125 0.0054  0.0166  -0.0191 88  TYR A CD1 
736  C  CD2 . TYR A 90  ? 0.1053 0.0536 0.1101 0.0046  0.0138  -0.0157 88  TYR A CD2 
737  C  CE1 . TYR A 90  ? 0.1042 0.0688 0.1023 0.0021  0.0184  -0.0184 88  TYR A CE1 
738  C  CE2 . TYR A 90  ? 0.1007 0.0606 0.1050 0.0033  0.0148  -0.0154 88  TYR A CE2 
739  C  CZ  . TYR A 90  ? 0.1040 0.0669 0.1056 0.0024  0.0143  -0.0239 88  TYR A CZ  
740  O  OH  . TYR A 90  ? 0.1089 0.0808 0.1008 -0.0007 0.0191  -0.0260 88  TYR A OH  
741  N  N   . ARG A 91  ? 0.0970 0.0627 0.1195 0.0036  -0.0062 -0.0060 89  ARG A N   
742  C  CA  . ARG A 91  ? 0.1155 0.0752 0.1209 0.0043  -0.0039 0.0055  89  ARG A CA  
743  C  C   . ARG A 91  ? 0.1015 0.0644 0.0999 0.0015  -0.0006 0.0066  89  ARG A C   
744  O  O   . ARG A 91  ? 0.0980 0.0647 0.1000 0.0051  0.0014  0.0063  89  ARG A O   
745  C  CB  . ARG A 91  ? 0.1469 0.0878 0.1428 0.0062  -0.0045 0.0075  89  ARG A CB  
746  C  CG  . ARG A 91  ? 0.1896 0.1182 0.1519 0.0065  -0.0032 0.0109  89  ARG A CG  
747  C  CD  . ARG A 91  ? 0.2200 0.1312 0.1576 0.0121  -0.0016 0.0345  89  ARG A CD  
748  N  NE  . ARG A 91  ? 0.2624 0.1483 0.1611 0.0045  0.0007  0.0437  89  ARG A NE  
749  C  CZ  . ARG A 91  ? 0.2809 0.1434 0.1673 0.0178  0.0075  0.0429  89  ARG A CZ  
750  N  NH1 . ARG A 91  ? 0.3008 0.1320 0.1853 0.0187  0.0121  0.0640  89  ARG A NH1 
751  N  NH2 . ARG A 91  ? 0.3067 0.1438 0.1681 0.0233  0.0064  0.0449  89  ARG A NH2 
752  N  N   . LEU A 92  ? 0.0966 0.0663 0.0987 0.0010  0.0001  0.0047  90  LEU A N   
753  C  CA  . LEU A 92  ? 0.1046 0.0638 0.0953 -0.0040 0.0015  0.0060  90  LEU A CA  
754  C  C   . LEU A 92  ? 0.1063 0.0583 0.0901 -0.0066 -0.0027 0.0137  90  LEU A C   
755  O  O   . LEU A 92  ? 0.1038 0.0815 0.1075 0.0002  -0.0053 0.0289  90  LEU A O   
756  C  CB  . LEU A 92  ? 0.1089 0.0716 0.0917 -0.0082 0.0029  0.0013  90  LEU A CB  
757  C  CG  . LEU A 92  ? 0.1151 0.0778 0.0958 -0.0123 0.0073  -0.0052 90  LEU A CG  
758  C  CD1 . LEU A 92  ? 0.1234 0.0738 0.0980 -0.0111 0.0097  -0.0084 90  LEU A CD1 
759  C  CD2 . LEU A 92  ? 0.1196 0.0922 0.1023 -0.0143 0.0075  -0.0087 90  LEU A CD2 
760  N  N   . ILE A 93  ? 0.1109 0.0506 0.0796 -0.0050 0.0014  0.0106  91  ILE A N   
761  C  CA  . ILE A 93  ? 0.1159 0.0385 0.0805 -0.0060 0.0033  0.0063  91  ILE A CA  
762  C  C   . ILE A 93  ? 0.1063 0.0399 0.0699 -0.0054 0.0047  0.0047  91  ILE A C   
763  O  O   . ILE A 93  ? 0.1059 0.0438 0.0679 -0.0026 0.0000  0.0052  91  ILE A O   
764  C  CB  . ILE A 93  ? 0.1254 0.0521 0.0844 -0.0140 0.0025  0.0008  91  ILE A CB  
765  C  CG1 . ILE A 93  ? 0.1291 0.0724 0.0978 -0.0214 0.0036  0.0022  91  ILE A CG1 
766  C  CG2 . ILE A 93  ? 0.1240 0.0532 0.0847 -0.0174 -0.0005 -0.0026 91  ILE A CG2 
767  C  CD1 . ILE A 93  ? 0.1384 0.0812 0.1091 -0.0275 0.0070  -0.0021 91  ILE A CD1 
768  N  N   . GLN A 94  ? 0.1049 0.0379 0.0725 -0.0023 0.0085  0.0024  92  GLN A N   
769  C  CA  . GLN A 94  ? 0.1017 0.0407 0.0688 -0.0007 0.0080  0.0054  92  GLN A CA  
770  C  C   . GLN A 94  ? 0.0960 0.0438 0.0630 0.0019  0.0057  0.0081  92  GLN A C   
771  O  O   . GLN A 94  ? 0.1077 0.0436 0.0607 -0.0020 0.0107  0.0063  92  GLN A O   
772  C  CB  . GLN A 94  ? 0.1049 0.0473 0.0843 -0.0023 0.0078  0.0077  92  GLN A CB  
773  C  CG  . GLN A 94  ? 0.1080 0.0542 0.0975 -0.0021 0.0043  0.0047  92  GLN A CG  
774  C  CD  . GLN A 94  ? 0.1064 0.0665 0.1047 0.0001  -0.0023 0.0048  92  GLN A CD  
775  O  OE1 . GLN A 94  ? 0.1101 0.0613 0.1144 0.0034  -0.0132 0.0141  92  GLN A OE1 
776  N  NE2 . GLN A 94  ? 0.1211 0.0957 0.1519 0.0019  -0.0055 0.0034  92  GLN A NE2 
777  N  N   . PHE A 95  ? 0.0948 0.0438 0.0550 0.0061  0.0048  0.0078  93  PHE A N   
778  C  CA  . PHE A 95  ? 0.0882 0.0423 0.0556 0.0040  0.0077  0.0044  93  PHE A CA  
779  C  C   . PHE A 95  ? 0.0839 0.0421 0.0546 0.0021  0.0093  0.0017  93  PHE A C   
780  O  O   . PHE A 95  ? 0.0941 0.0466 0.0573 0.0036  0.0098  0.0043  93  PHE A O   
781  C  CB  . PHE A 95  ? 0.0863 0.0468 0.0627 0.0041  0.0048  0.0073  93  PHE A CB  
782  C  CG  . PHE A 95  ? 0.0860 0.0507 0.0706 0.0023  0.0036  0.0061  93  PHE A CG  
783  C  CD1 . PHE A 95  ? 0.0893 0.0570 0.0772 0.0069  0.0012  0.0003  93  PHE A CD1 
784  C  CD2 . PHE A 95  ? 0.0886 0.0522 0.0744 0.0049  0.0030  0.0076  93  PHE A CD2 
785  C  CE1 . PHE A 95  ? 0.0927 0.0594 0.0758 0.0054  0.0013  0.0014  93  PHE A CE1 
786  C  CE2 . PHE A 95  ? 0.0898 0.0580 0.0777 0.0054  0.0019  0.0078  93  PHE A CE2 
787  C  CZ  . PHE A 95  ? 0.0925 0.0614 0.0715 0.0052  0.0021  0.0064  93  PHE A CZ  
788  N  N   . HIS A 96  ? 0.0827 0.0432 0.0541 0.0063  0.0099  -0.0007 94  HIS A N   
789  C  CA  . HIS A 96  ? 0.0807 0.0425 0.0479 0.0037  0.0121  -0.0012 94  HIS A CA  
790  C  C   . HIS A 96  ? 0.0757 0.0414 0.0470 0.0032  0.0152  -0.0007 94  HIS A C   
791  O  O   . HIS A 96  ? 0.0848 0.0440 0.0530 0.0072  0.0203  0.0041  94  HIS A O   
792  C  CB  . HIS A 96  ? 0.0824 0.0446 0.0566 0.0033  0.0119  0.0008  94  HIS A CB  
793  C  CG  . HIS A 96  ? 0.0789 0.0423 0.0614 0.0028  0.0109  -0.0011 94  HIS A CG  
794  N  ND1 . HIS A 96  ? 0.0803 0.0472 0.0666 0.0033  0.0124  -0.0040 94  HIS A ND1 
795  C  CD2 . HIS A 96  ? 0.0799 0.0427 0.0608 0.0039  0.0085  -0.0006 94  HIS A CD2 
796  C  CE1 . HIS A 96  ? 0.0777 0.0435 0.0683 0.0037  0.0079  -0.0014 94  HIS A CE1 
797  N  NE2 . HIS A 96  ? 0.0796 0.0386 0.0595 0.0024  0.0074  0.0010  94  HIS A NE2 
798  N  N   . PHE A 97  ? 0.0771 0.0450 0.0467 0.0026  0.0227  0.0009  95  PHE A N   
799  C  CA  . PHE A 97  ? 0.0771 0.0510 0.0536 0.0014  0.0191  0.0041  95  PHE A CA  
800  C  C   . PHE A 97  ? 0.0773 0.0472 0.0596 0.0034  0.0187  0.0053  95  PHE A C   
801  O  O   . PHE A 97  ? 0.0813 0.0564 0.0675 0.0031  0.0211  0.0111  95  PHE A O   
802  C  CB  . PHE A 97  ? 0.0781 0.0553 0.0624 0.0012  0.0175  0.0010  95  PHE A CB  
803  C  CG  . PHE A 97  ? 0.0795 0.0586 0.0680 0.0033  0.0132  -0.0022 95  PHE A CG  
804  C  CD1 . PHE A 97  ? 0.0821 0.0642 0.0747 0.0031  0.0105  0.0002  95  PHE A CD1 
805  C  CD2 . PHE A 97  ? 0.0822 0.0627 0.0694 -0.0008 0.0092  -0.0053 95  PHE A CD2 
806  C  CE1 . PHE A 97  ? 0.0879 0.0676 0.0748 0.0085  0.0045  -0.0006 95  PHE A CE1 
807  C  CE2 . PHE A 97  ? 0.0844 0.0699 0.0801 0.0027  0.0105  -0.0069 95  PHE A CE2 
808  C  CZ  . PHE A 97  ? 0.0814 0.0689 0.0845 0.0089  0.0059  -0.0075 95  PHE A CZ  
809  N  N   . HIS A 98  ? 0.0695 0.0456 0.0617 0.0011  0.0177  0.0050  96  HIS A N   
810  C  CA  . HIS A 98  ? 0.0694 0.0457 0.0659 0.0018  0.0137  0.0023  96  HIS A CA  
811  C  C   . HIS A 98  ? 0.0700 0.0460 0.0698 -0.0012 0.0164  0.0021  96  HIS A C   
812  O  O   . HIS A 98  ? 0.0707 0.0452 0.0745 -0.0036 0.0198  0.0058  96  HIS A O   
813  C  CB  . HIS A 98  ? 0.0704 0.0502 0.0733 0.0036  0.0123  -0.0037 96  HIS A CB  
814  C  CG  . HIS A 98  ? 0.0677 0.0509 0.0756 0.0009  0.0083  -0.0040 96  HIS A CG  
815  N  ND1 . HIS A 98  ? 0.0698 0.0532 0.0940 0.0035  0.0105  -0.0083 96  HIS A ND1 
816  C  CD2 . HIS A 98  ? 0.0651 0.0518 0.0845 -0.0007 0.0073  -0.0036 96  HIS A CD2 
817  C  CE1 . HIS A 98  ? 0.0678 0.0476 0.0904 -0.0002 0.0067  -0.0036 96  HIS A CE1 
818  N  NE2 . HIS A 98  ? 0.0642 0.0503 0.0778 -0.0019 0.0065  -0.0019 96  HIS A NE2 
819  N  N   . TRP A 99  ? 0.0749 0.0427 0.0655 -0.0020 0.0166  0.0015  97  TRP A N   
820  C  CA  . TRP A 99  ? 0.0846 0.0447 0.0688 0.0006  0.0151  0.0000  97  TRP A CA  
821  C  C   . TRP A 99  ? 0.0856 0.0406 0.0699 -0.0023 0.0152  -0.0031 97  TRP A C   
822  O  O   . TRP A 99  ? 0.0867 0.0428 0.0790 -0.0034 0.0226  -0.0004 97  TRP A O   
823  C  CB  . TRP A 99  ? 0.0851 0.0460 0.0665 0.0044  0.0130  -0.0051 97  TRP A CB  
824  C  CG  . TRP A 99  ? 0.0882 0.0504 0.0637 0.0055  0.0125  -0.0041 97  TRP A CG  
825  C  CD1 . TRP A 99  ? 0.0955 0.0577 0.0651 0.0056  0.0172  -0.0024 97  TRP A CD1 
826  C  CD2 . TRP A 99  ? 0.0942 0.0540 0.0499 0.0024  0.0153  -0.0013 97  TRP A CD2 
827  N  NE1 . TRP A 99  ? 0.0980 0.0571 0.0590 0.0055  0.0247  -0.0081 97  TRP A NE1 
828  C  CE2 . TRP A 99  ? 0.0946 0.0526 0.0527 0.0002  0.0201  -0.0001 97  TRP A CE2 
829  C  CE3 . TRP A 99  ? 0.0920 0.0559 0.0465 0.0057  0.0172  0.0011  97  TRP A CE3 
830  C  CZ2 . TRP A 99  ? 0.0984 0.0592 0.0543 0.0011  0.0214  0.0049  97  TRP A CZ2 
831  C  CZ3 . TRP A 99  ? 0.0950 0.0609 0.0487 0.0022  0.0168  0.0026  97  TRP A CZ3 
832  C  CH2 . TRP A 99  ? 0.1004 0.0591 0.0484 0.0020  0.0193  0.0074  97  TRP A CH2 
833  N  N   . GLY A 100 ? 0.0962 0.0381 0.0771 0.0011  0.0104  -0.0020 98  GLY A N   
834  C  CA  . GLY A 100 ? 0.1014 0.0383 0.0768 0.0003  0.0112  -0.0031 98  GLY A CA  
835  C  C   . GLY A 100 ? 0.1072 0.0418 0.0824 0.0001  0.0108  -0.0077 98  GLY A C   
836  O  O   . GLY A 100 ? 0.1172 0.0548 0.0882 -0.0023 0.0073  -0.0161 98  GLY A O   
837  N  N   . SER A 101 ? 0.1122 0.0487 0.0908 0.0060  0.0141  -0.0160 99  SER A N   
838  C  CA  . SER A 101 ? 0.1257 0.0576 0.1081 0.0075  0.0191  -0.0218 99  SER A CA  
839  C  C   . SER A 101 ? 0.1426 0.0606 0.1195 0.0075  0.0169  -0.0255 99  SER A C   
840  O  O   . SER A 101 ? 0.1597 0.0806 0.1277 0.0020  0.0180  -0.0353 99  SER A O   
841  C  CB  . SER A 101 ? 0.1293 0.0603 0.1239 0.0069  0.0244  -0.0218 99  SER A CB  
842  O  OG  . SER A 101 ? 0.1269 0.0584 0.1447 0.0148  0.0260  -0.0209 99  SER A OG  
843  N  N   . LEU A 102 ? 0.1392 0.0583 0.1363 0.0017  0.0230  -0.0222 100 LEU A N   
844  C  CA  . LEU A 102 ? 0.1634 0.0573 0.1473 0.0048  0.0301  -0.0203 100 LEU A CA  
845  C  C   . LEU A 102 ? 0.1588 0.0591 0.1330 -0.0022 0.0301  -0.0167 100 LEU A C   
846  O  O   . LEU A 102 ? 0.1543 0.0482 0.1265 -0.0021 0.0294  -0.0165 100 LEU A O   
847  C  CB  . LEU A 102 ? 0.1903 0.0882 0.1684 0.0119  0.0310  -0.0124 100 LEU A CB  
848  C  CG  . LEU A 102 ? 0.2041 0.0962 0.1787 0.0212  0.0310  -0.0100 100 LEU A CG  
849  C  CD1 . LEU A 102 ? 0.2026 0.1262 0.1914 0.0252  0.0322  -0.0044 100 LEU A CD1 
850  C  CD2 . LEU A 102 ? 0.2279 0.1137 0.1953 0.0218  0.0392  -0.0192 100 LEU A CD2 
851  N  N   . ASP A 103 ? 0.1532 0.0482 0.1285 -0.0021 0.0288  -0.0194 101 ASP A N   
852  C  CA  . ASP A 103 ? 0.1518 0.0631 0.1263 -0.0112 0.0287  -0.0125 101 ASP A CA  
853  C  C   . ASP A 103 ? 0.1515 0.0694 0.1253 -0.0140 0.0310  -0.0077 101 ASP A C   
854  O  O   . ASP A 103 ? 0.1643 0.0879 0.1383 0.0013  0.0328  -0.0073 101 ASP A O   
855  C  CB  . ASP A 103 ? 0.1540 0.0800 0.1355 -0.0205 0.0314  -0.0090 101 ASP A CB  
856  C  CG  . ASP A 103 ? 0.1671 0.0972 0.1513 -0.0253 0.0256  -0.0177 101 ASP A CG  
857  O  OD1 . ASP A 103 ? 0.1788 0.1111 0.1503 -0.0254 0.0125  -0.0092 101 ASP A OD1 
858  O  OD2 . ASP A 103 ? 0.1875 0.1417 0.1879 -0.0462 0.0154  -0.0174 101 ASP A OD2 
859  N  N   . GLY A 104 ? 0.1521 0.0687 0.1263 -0.0160 0.0295  0.0015  102 GLY A N   
860  C  CA  . GLY A 104 ? 0.1530 0.0796 0.1326 -0.0163 0.0266  0.0069  102 GLY A CA  
861  C  C   . GLY A 104 ? 0.1413 0.0748 0.1188 -0.0102 0.0267  0.0020  102 GLY A C   
862  O  O   . GLY A 104 ? 0.1453 0.0918 0.1247 -0.0193 0.0248  0.0114  102 GLY A O   
863  N  N   . GLN A 105 ? 0.1295 0.0644 0.1060 -0.0064 0.0214  -0.0003 103 GLN A N   
864  C  CA  . GLN A 105 ? 0.1158 0.0579 0.1014 0.0021  0.0237  -0.0018 103 GLN A CA  
865  C  C   . GLN A 105 ? 0.0983 0.0545 0.0897 -0.0006 0.0253  -0.0008 103 GLN A C   
866  O  O   . GLN A 105 ? 0.1131 0.0574 0.1035 0.0060  0.0202  -0.0075 103 GLN A O   
867  C  CB  . GLN A 105 ? 0.1192 0.0585 0.1064 0.0084  0.0277  0.0040  103 GLN A CB  
868  C  CG  . GLN A 105 ? 0.1277 0.0686 0.1150 0.0147  0.0334  0.0102  103 GLN A CG  
869  C  CD  . GLN A 105 ? 0.1399 0.0747 0.1356 0.0245  0.0363  0.0218  103 GLN A CD  
870  O  OE1 . GLN A 105 ? 0.1790 0.1190 0.1723 0.0420  0.0455  0.0473  103 GLN A OE1 
871  N  NE2 . GLN A 105 ? 0.1335 0.0868 0.1349 0.0245  0.0383  0.0177  103 GLN A NE2 
872  N  N   . GLY A 106 ? 0.0928 0.0555 0.0759 0.0004  0.0250  -0.0020 104 GLY A N   
873  C  CA  . GLY A 106 ? 0.0885 0.0553 0.0742 -0.0004 0.0226  0.0009  104 GLY A CA  
874  C  C   . GLY A 106 ? 0.0831 0.0503 0.0719 0.0018  0.0212  0.0050  104 GLY A C   
875  O  O   . GLY A 106 ? 0.0947 0.0535 0.0858 0.0011  0.0184  0.0075  104 GLY A O   
876  N  N   . SER A 107 ? 0.0837 0.0422 0.0666 0.0009  0.0220  0.0031  105 SER A N   
877  C  CA  . SER A 107 ? 0.0827 0.0397 0.0696 0.0028  0.0192  0.0009  105 SER A CA  
878  C  C   . SER A 107 ? 0.0768 0.0408 0.0706 0.0033  0.0184  -0.0029 105 SER A C   
879  O  O   . SER A 107 ? 0.0899 0.0422 0.0862 0.0058  0.0127  -0.0086 105 SER A O   
880  C  CB  . SER A 107 ? 0.0857 0.0414 0.0772 -0.0002 0.0203  -0.0001 105 SER A CB  
881  O  OG  . SER A 107 ? 0.0932 0.0464 0.0814 -0.0014 0.0237  0.0024  105 SER A OG  
882  N  N   . GLU A 108 ? 0.0788 0.0425 0.0722 0.0025  0.0173  -0.0026 106 GLU A N   
883  C  CA  . GLU A 108 ? 0.0727 0.0460 0.0663 0.0019  0.0145  0.0000  106 GLU A CA  
884  C  C   . GLU A 108 ? 0.0742 0.0418 0.0637 0.0017  0.0102  0.0003  106 GLU A C   
885  O  O   . GLU A 108 ? 0.0799 0.0543 0.0716 0.0066  0.0051  -0.0042 106 GLU A O   
886  C  CB  . GLU A 108 ? 0.0767 0.0479 0.0649 -0.0024 0.0162  -0.0002 106 GLU A CB  
887  C  CG  . GLU A 108 ? 0.0803 0.0519 0.0724 -0.0004 0.0194  0.0030  106 GLU A CG  
888  C  CD  . GLU A 108 ? 0.0735 0.0490 0.0709 0.0030  0.0225  0.0025  106 GLU A CD  
889  O  OE1 . GLU A 108 ? 0.0684 0.0459 0.0853 0.0039  0.0240  -0.0012 106 GLU A OE1 
890  O  OE2 . GLU A 108 ? 0.0740 0.0613 0.0978 0.0065  0.0253  0.0037  106 GLU A OE2 
891  N  N   . HIS A 109 ? 0.0771 0.0453 0.0623 0.0017  0.0110  0.0034  107 HIS A N   
892  C  CA  . HIS A 109 ? 0.0793 0.0481 0.0604 0.0023  0.0088  0.0024  107 HIS A CA  
893  C  C   . HIS A 109 ? 0.0860 0.0549 0.0681 -0.0007 0.0111  0.0033  107 HIS A C   
894  O  O   . HIS A 109 ? 0.0855 0.0577 0.0660 -0.0044 0.0162  0.0050  107 HIS A O   
895  C  CB  . HIS A 109 ? 0.0759 0.0464 0.0671 -0.0002 0.0071  0.0019  107 HIS A CB  
896  C  CG  . HIS A 109 ? 0.0775 0.0447 0.0670 0.0016  0.0085  -0.0003 107 HIS A CG  
897  N  ND1 . HIS A 109 ? 0.0778 0.0429 0.0685 0.0011  0.0098  -0.0006 107 HIS A ND1 
898  C  CD2 . HIS A 109 ? 0.0766 0.0490 0.0652 0.0044  0.0059  0.0004  107 HIS A CD2 
899  C  CE1 . HIS A 109 ? 0.0809 0.0431 0.0683 0.0040  0.0074  -0.0010 107 HIS A CE1 
900  N  NE2 . HIS A 109 ? 0.0766 0.0487 0.0674 0.0023  0.0086  -0.0049 107 HIS A NE2 
901  N  N   . THR A 110 ? 0.0893 0.0527 0.0684 -0.0046 0.0146  0.0047  108 THR A N   
902  C  CA  . THR A 110 ? 0.0942 0.0514 0.0721 -0.0001 0.0186  0.0039  108 THR A CA  
903  C  C   . THR A 110 ? 0.0964 0.0551 0.0717 0.0015  0.0186  0.0053  108 THR A C   
904  O  O   . THR A 110 ? 0.0944 0.0544 0.0705 -0.0021 0.0216  0.0054  108 THR A O   
905  C  CB  . THR A 110 ? 0.0978 0.0566 0.0764 0.0037  0.0176  0.0024  108 THR A CB  
906  O  OG1 . THR A 110 ? 0.0950 0.0604 0.0841 0.0116  0.0148  0.0042  108 THR A OG1 
907  C  CG2 . THR A 110 ? 0.1018 0.0633 0.0786 0.0014  0.0172  0.0016  108 THR A CG2 
908  N  N   . VAL A 111 ? 0.0976 0.0583 0.0784 0.0022  0.0213  0.0106  109 VAL A N   
909  C  CA  . VAL A 111 ? 0.1085 0.0686 0.0807 0.0006  0.0237  0.0144  109 VAL A CA  
910  C  C   . VAL A 111 ? 0.1169 0.0693 0.0825 0.0021  0.0308  0.0180  109 VAL A C   
911  O  O   . VAL A 111 ? 0.1238 0.0691 0.0889 0.0025  0.0271  0.0170  109 VAL A O   
912  C  CB  . VAL A 111 ? 0.1090 0.0849 0.0821 0.0034  0.0203  0.0235  109 VAL A CB  
913  C  CG1 . VAL A 111 ? 0.1101 0.0955 0.0871 0.0053  0.0225  0.0264  109 VAL A CG1 
914  C  CG2 . VAL A 111 ? 0.1133 0.0912 0.0873 0.0009  0.0169  0.0283  109 VAL A CG2 
915  N  N   . ASP A 112 ? 0.1299 0.0713 0.0846 0.0072  0.0289  0.0208  110 ASP A N   
916  C  CA  . ASP A 112 ? 0.1432 0.0781 0.0939 0.0090  0.0314  0.0277  110 ASP A CA  
917  C  C   . ASP A 112 ? 0.1507 0.0694 0.0940 0.0149  0.0297  0.0309  110 ASP A C   
918  O  O   . ASP A 112 ? 0.1624 0.0712 0.1033 0.0131  0.0340  0.0410  110 ASP A O   
919  C  CB  . ASP A 112 ? 0.1560 0.0903 0.1103 0.0062  0.0306  0.0298  110 ASP A CB  
920  C  CG  . ASP A 112 ? 0.1586 0.1075 0.1172 0.0071  0.0318  0.0274  110 ASP A CG  
921  O  OD1 . ASP A 112 ? 0.1574 0.1113 0.1164 0.0107  0.0348  0.0290  110 ASP A OD1 
922  O  OD2 . ASP A 112 ? 0.1712 0.1465 0.1348 0.0074  0.0446  0.0277  110 ASP A OD2 
923  N  N   . LYS A 113 ? 0.1472 0.0736 0.0960 0.0165  0.0323  0.0271  111 LYS A N   
924  C  CA  . LYS A 113 ? 0.1583 0.0767 0.1014 0.0235  0.0343  0.0255  111 LYS A CA  
925  C  C   . LYS A 113 ? 0.1608 0.0710 0.0941 0.0161  0.0440  0.0169  111 LYS A C   
926  O  O   . LYS A 113 ? 0.1739 0.0900 0.1051 0.0260  0.0521  0.0048  111 LYS A O   
927  C  CB  . LYS A 113 ? 0.1680 0.1001 0.1078 0.0375  0.0344  0.0302  111 LYS A CB  
928  C  CG  . LYS A 113 ? 0.1889 0.1320 0.1339 0.0502  0.0243  0.0186  111 LYS A CG  
929  C  CD  . LYS A 113 ? 0.2038 0.1757 0.1563 0.0452  0.0207  0.0137  111 LYS A CD  
930  C  CE  . LYS A 113 ? 0.2293 0.2039 0.1883 0.0431  0.0080  0.0167  111 LYS A CE  
931  N  NZ  . LYS A 113 ? 0.2587 0.2434 0.2264 0.0466  -0.0021 0.0134  111 LYS A NZ  
932  N  N   . LYS A 114 ? 0.1585 0.0661 0.0919 0.0064  0.0423  0.0106  112 LYS A N   
933  C  CA  . LYS A 114 ? 0.1606 0.0786 0.1041 -0.0088 0.0338  0.0089  112 LYS A CA  
934  C  C   . LYS A 114 ? 0.1359 0.0631 0.0862 -0.0018 0.0269  0.0049  112 LYS A C   
935  O  O   . LYS A 114 ? 0.1239 0.0644 0.0911 -0.0022 0.0253  0.0022  112 LYS A O   
936  C  CB  . LYS A 114 ? 0.1812 0.1128 0.1297 -0.0370 0.0368  -0.0078 112 LYS A CB  
937  C  CG  . LYS A 114 ? 0.1927 0.1536 0.1556 -0.0529 0.0377  -0.0203 112 LYS A CG  
938  C  CD  . LYS A 114 ? 0.2138 0.1804 0.1894 -0.0457 0.0345  -0.0082 112 LYS A CD  
939  C  CE  . LYS A 114 ? 0.2241 0.1919 0.2105 -0.0535 0.0266  -0.0010 112 LYS A CE  
940  N  NZ  . LYS A 114 ? 0.2214 0.2019 0.2102 -0.0430 0.0230  0.0074  112 LYS A NZ  
941  N  N   . LYS A 115 ? 0.1373 0.0541 0.0926 0.0126  0.0236  0.0088  113 LYS A N   
942  C  CA  . LYS A 115 ? 0.1307 0.0566 0.0998 0.0078  0.0252  0.0085  113 LYS A CA  
943  C  C   . LYS A 115 ? 0.1287 0.0475 0.1119 0.0053  0.0198  0.0076  113 LYS A C   
944  O  O   . LYS A 115 ? 0.1547 0.0460 0.1296 0.0048  0.0072  0.0106  113 LYS A O   
945  C  CB  . LYS A 115 ? 0.1275 0.0711 0.1066 0.0163  0.0234  0.0078  113 LYS A CB  
946  C  CG  . LYS A 115 ? 0.1292 0.0886 0.1124 0.0232  0.0222  0.0045  113 LYS A CG  
947  C  CD  . LYS A 115 ? 0.1350 0.1117 0.1294 0.0299  0.0185  0.0005  113 LYS A CD  
948  C  CE  . LYS A 115 ? 0.1453 0.1431 0.1619 0.0231  0.0138  -0.0031 113 LYS A CE  
949  N  NZ  . LYS A 115 ? 0.1803 0.1887 0.1904 0.0205  0.0024  -0.0130 113 LYS A NZ  
950  N  N   . TYR A 116 ? 0.1085 0.0464 0.1020 0.0028  0.0183  0.0049  114 TYR A N   
951  C  CA  . TYR A 116 ? 0.1030 0.0442 0.0978 -0.0027 0.0183  0.0059  114 TYR A CA  
952  C  C   . TYR A 116 ? 0.0934 0.0462 0.0963 -0.0068 0.0186  0.0000  114 TYR A C   
953  O  O   . TYR A 116 ? 0.0963 0.0531 0.0972 -0.0151 0.0229  -0.0025 114 TYR A O   
954  C  CB  . TYR A 116 ? 0.1042 0.0438 0.0996 -0.0060 0.0224  0.0048  114 TYR A CB  
955  C  CG  . TYR A 116 ? 0.1135 0.0480 0.1022 -0.0041 0.0236  0.0042  114 TYR A CG  
956  C  CD1 . TYR A 116 ? 0.1423 0.0648 0.1092 0.0028  0.0258  0.0033  114 TYR A CD1 
957  C  CD2 . TYR A 116 ? 0.1226 0.0660 0.1203 -0.0083 0.0289  0.0043  114 TYR A CD2 
958  C  CE1 . TYR A 116 ? 0.1573 0.0868 0.1108 0.0086  0.0361  -0.0014 114 TYR A CE1 
959  C  CE2 . TYR A 116 ? 0.1383 0.0890 0.1303 -0.0069 0.0377  0.0087  114 TYR A CE2 
960  C  CZ  . TYR A 116 ? 0.1603 0.1088 0.1274 0.0017  0.0512  0.0096  114 TYR A CZ  
961  O  OH  . TYR A 116 ? 0.2051 0.1692 0.1475 0.0101  0.0780  0.0015  114 TYR A OH  
962  N  N   . ALA A 117 ? 0.0943 0.0477 0.0934 -0.0121 0.0192  0.0006  115 ALA A N   
963  C  CA  . ALA A 117 ? 0.0942 0.0422 0.0891 -0.0097 0.0185  -0.0028 115 ALA A CA  
964  C  C   . ALA A 117 ? 0.0906 0.0420 0.0825 -0.0066 0.0200  -0.0021 115 ALA A C   
965  O  O   . ALA A 117 ? 0.0941 0.0479 0.0953 -0.0045 0.0258  -0.0073 115 ALA A O   
966  C  CB  . ALA A 117 ? 0.1018 0.0487 0.0906 -0.0122 0.0167  -0.0034 115 ALA A CB  
967  N  N   . ALA A 118 ? 0.0884 0.0468 0.0764 -0.0015 0.0231  -0.0012 116 ALA A N   
968  C  CA  . ALA A 118 ? 0.0848 0.0464 0.0698 -0.0007 0.0203  -0.0024 116 ALA A CA  
969  C  C   . ALA A 118 ? 0.0769 0.0420 0.0649 0.0002  0.0172  -0.0003 116 ALA A C   
970  O  O   . ALA A 118 ? 0.0776 0.0419 0.0726 -0.0013 0.0191  0.0017  116 ALA A O   
971  C  CB  . ALA A 118 ? 0.0822 0.0482 0.0677 0.0018  0.0222  -0.0038 116 ALA A CB  
972  N  N   . GLU A 119 ? 0.0749 0.0422 0.0661 0.0000  0.0188  0.0030  117 GLU A N   
973  C  CA  . GLU A 119 ? 0.0765 0.0438 0.0662 0.0052  0.0155  0.0063  117 GLU A CA  
974  C  C   . GLU A 119 ? 0.0763 0.0457 0.0656 0.0055  0.0183  0.0090  117 GLU A C   
975  O  O   . GLU A 119 ? 0.0819 0.0592 0.0818 0.0078  0.0264  0.0184  117 GLU A O   
976  C  CB  . GLU A 119 ? 0.0790 0.0469 0.0705 0.0043  0.0110  0.0073  117 GLU A CB  
977  C  CG  . GLU A 119 ? 0.0824 0.0520 0.0751 0.0030  0.0074  0.0043  117 GLU A CG  
978  C  CD  . GLU A 119 ? 0.0817 0.0484 0.0719 0.0009  0.0065  0.0024  117 GLU A CD  
979  O  OE1 . GLU A 119 ? 0.0862 0.0587 0.0786 0.0093  0.0108  -0.0033 117 GLU A OE1 
980  O  OE2 . GLU A 119 ? 0.0995 0.0538 0.0655 -0.0021 0.0002  0.0001  117 GLU A OE2 
981  N  N   . LEU A 120 ? 0.0717 0.0430 0.0602 0.0048  0.0140  0.0061  118 LEU A N   
982  C  CA  . LEU A 120 ? 0.0738 0.0436 0.0622 0.0032  0.0104  0.0021  118 LEU A CA  
983  C  C   . LEU A 120 ? 0.0713 0.0452 0.0528 0.0028  0.0121  -0.0021 118 LEU A C   
984  O  O   . LEU A 120 ? 0.0765 0.0445 0.0504 0.0011  0.0136  0.0002  118 LEU A O   
985  C  CB  . LEU A 120 ? 0.0774 0.0525 0.0698 0.0025  0.0066  0.0033  118 LEU A CB  
986  C  CG  . LEU A 120 ? 0.0820 0.0574 0.0761 0.0017  0.0032  0.0007  118 LEU A CG  
987  C  CD1 . LEU A 120 ? 0.0881 0.0559 0.0775 0.0016  0.0033  -0.0020 118 LEU A CD1 
988  C  CD2 . LEU A 120 ? 0.0853 0.0691 0.0846 0.0011  -0.0003 0.0021  118 LEU A CD2 
989  N  N   . HIS A 121 ? 0.0692 0.0395 0.0554 0.0049  0.0124  -0.0059 119 HIS A N   
990  C  CA  . HIS A 121 ? 0.0673 0.0444 0.0558 0.0035  0.0086  -0.0071 119 HIS A CA  
991  C  C   . HIS A 121 ? 0.0681 0.0407 0.0555 0.0016  0.0077  -0.0058 119 HIS A C   
992  O  O   . HIS A 121 ? 0.0788 0.0475 0.0622 0.0068  0.0144  -0.0032 119 HIS A O   
993  C  CB  . HIS A 121 ? 0.0652 0.0480 0.0601 0.0055  0.0079  -0.0068 119 HIS A CB  
994  C  CG  . HIS A 121 ? 0.0641 0.0486 0.0569 0.0060  0.0063  -0.0055 119 HIS A CG  
995  N  ND1 . HIS A 121 ? 0.0674 0.0529 0.0591 0.0091  0.0060  -0.0018 119 HIS A ND1 
996  C  CD2 . HIS A 121 ? 0.0639 0.0546 0.0639 0.0062  0.0064  -0.0025 119 HIS A CD2 
997  C  CE1 . HIS A 121 ? 0.0640 0.0510 0.0585 0.0109  0.0057  -0.0024 119 HIS A CE1 
998  N  NE2 . HIS A 121 ? 0.0695 0.0560 0.0637 0.0096  0.0058  -0.0005 119 HIS A NE2 
999  N  N   . LEU A 122 ? 0.0725 0.0384 0.0617 0.0017  0.0071  -0.0038 120 LEU A N   
1000 C  CA  . LEU A 122 ? 0.0758 0.0414 0.0658 0.0003  0.0034  -0.0004 120 LEU A CA  
1001 C  C   . LEU A 122 ? 0.0751 0.0373 0.0582 0.0001  0.0069  0.0009  120 LEU A C   
1002 O  O   . LEU A 122 ? 0.0777 0.0369 0.0575 0.0019  0.0049  -0.0002 120 LEU A O   
1003 C  CB  . LEU A 122 ? 0.0813 0.0456 0.0763 -0.0003 0.0021  -0.0024 120 LEU A CB  
1004 C  CG  . LEU A 122 ? 0.0951 0.0582 0.0818 -0.0054 0.0023  -0.0034 120 LEU A CG  
1005 C  CD1 . LEU A 122 ? 0.1218 0.0729 0.0888 -0.0159 0.0040  0.0004  120 LEU A CD1 
1006 C  CD2 . LEU A 122 ? 0.1017 0.0742 0.0917 -0.0028 -0.0040 -0.0026 120 LEU A CD2 
1007 N  N   . VAL A 123 ? 0.0822 0.0403 0.0598 -0.0035 0.0091  0.0037  121 VAL A N   
1008 C  CA  . VAL A 123 ? 0.0834 0.0419 0.0623 -0.0038 0.0095  0.0062  121 VAL A CA  
1009 C  C   . VAL A 123 ? 0.0853 0.0428 0.0673 -0.0018 0.0085  0.0014  121 VAL A C   
1010 O  O   . VAL A 123 ? 0.0979 0.0467 0.0669 0.0026  0.0032  -0.0024 121 VAL A O   
1011 C  CB  . VAL A 123 ? 0.0866 0.0507 0.0673 -0.0045 0.0174  0.0082  121 VAL A CB  
1012 C  CG1 . VAL A 123 ? 0.0857 0.0552 0.0753 -0.0050 0.0213  0.0083  121 VAL A CG1 
1013 C  CG2 . VAL A 123 ? 0.0893 0.0553 0.0697 -0.0044 0.0215  0.0095  121 VAL A CG2 
1014 N  N   . HIS A 124 ? 0.0848 0.0368 0.0721 -0.0004 0.0041  -0.0009 122 HIS A N   
1015 C  CA  . HIS A 124 ? 0.0835 0.0387 0.0763 -0.0001 0.0044  -0.0008 122 HIS A CA  
1016 C  C   . HIS A 124 ? 0.0892 0.0428 0.0778 -0.0023 0.0032  -0.0006 122 HIS A C   
1017 O  O   . HIS A 124 ? 0.0936 0.0508 0.0812 -0.0077 -0.0019 0.0043  122 HIS A O   
1018 C  CB  . HIS A 124 ? 0.0831 0.0398 0.0798 0.0034  0.0078  -0.0028 122 HIS A CB  
1019 C  CG  . HIS A 124 ? 0.0830 0.0438 0.0867 0.0000  0.0087  -0.0016 122 HIS A CG  
1020 N  ND1 . HIS A 124 ? 0.0801 0.0408 0.0927 -0.0016 0.0110  -0.0009 122 HIS A ND1 
1021 C  CD2 . HIS A 124 ? 0.0837 0.0521 0.0869 0.0014  0.0089  0.0017  122 HIS A CD2 
1022 C  CE1 . HIS A 124 ? 0.0778 0.0457 0.0947 -0.0008 0.0121  0.0007  122 HIS A CE1 
1023 N  NE2 . HIS A 124 ? 0.0796 0.0554 0.0955 -0.0029 0.0096  0.0053  122 HIS A NE2 
1024 N  N   . TRP A 125 ? 0.0907 0.0417 0.0806 0.0000  0.0035  -0.0027 123 TRP A N   
1025 C  CA  . TRP A 125 ? 0.0965 0.0455 0.0823 -0.0018 0.0055  -0.0046 123 TRP A CA  
1026 C  C   . TRP A 125 ? 0.0939 0.0445 0.0884 0.0029  0.0039  -0.0056 123 TRP A C   
1027 O  O   . TRP A 125 ? 0.0904 0.0510 0.0927 0.0020  0.0043  -0.0097 123 TRP A O   
1028 C  CB  . TRP A 125 ? 0.1121 0.0536 0.0921 -0.0054 0.0100  -0.0056 123 TRP A CB  
1029 C  CG  . TRP A 125 ? 0.1324 0.0528 0.0966 -0.0092 0.0085  -0.0041 123 TRP A CG  
1030 C  CD1 . TRP A 125 ? 0.1439 0.0542 0.0973 -0.0036 0.0072  -0.0035 123 TRP A CD1 
1031 C  CD2 . TRP A 125 ? 0.1550 0.0513 0.1042 -0.0108 0.0075  -0.0065 123 TRP A CD2 
1032 N  NE1 . TRP A 125 ? 0.1559 0.0532 0.0999 -0.0076 0.0022  -0.0027 123 TRP A NE1 
1033 C  CE2 . TRP A 125 ? 0.1631 0.0491 0.1073 -0.0063 0.0042  -0.0005 123 TRP A CE2 
1034 C  CE3 . TRP A 125 ? 0.1731 0.0518 0.1068 -0.0152 0.0066  -0.0065 123 TRP A CE3 
1035 C  CZ2 . TRP A 125 ? 0.1844 0.0577 0.1142 -0.0052 -0.0002 -0.0017 123 TRP A CZ2 
1036 C  CZ3 . TRP A 125 ? 0.1893 0.0528 0.1122 -0.0115 0.0102  -0.0105 123 TRP A CZ3 
1037 C  CH2 . TRP A 125 ? 0.1908 0.0557 0.1180 -0.0055 0.0058  -0.0038 123 TRP A CH2 
1038 N  N   . ASN A 126 ? 0.0956 0.0473 0.0974 0.0069  0.0043  -0.0162 124 ASN A N   
1039 C  CA  . ASN A 126 ? 0.1015 0.0511 0.1030 0.0029  0.0093  -0.0174 124 ASN A CA  
1040 C  C   . ASN A 126 ? 0.1018 0.0512 0.1056 0.0066  0.0094  -0.0194 124 ASN A C   
1041 O  O   . ASN A 126 ? 0.1043 0.0595 0.0981 0.0027  0.0187  -0.0196 124 ASN A O   
1042 C  CB  . ASN A 126 ? 0.1052 0.0542 0.1058 -0.0005 0.0128  -0.0152 124 ASN A CB  
1043 C  CG  . ASN A 126 ? 0.1168 0.0616 0.1029 -0.0001 0.0185  -0.0119 124 ASN A CG  
1044 O  OD1 . ASN A 126 ? 0.1175 0.0774 0.1107 0.0048  0.0123  -0.0181 124 ASN A OD1 
1045 N  ND2 . ASN A 126 ? 0.1316 0.0829 0.1027 -0.0005 0.0176  -0.0150 124 ASN A ND2 
1046 N  N   . THR A 127 ? 0.1098 0.0550 0.1223 0.0108  0.0102  -0.0127 125 THR A N   
1047 C  CA  . THR A 127 ? 0.1326 0.0667 0.1429 0.0146  0.0098  -0.0068 125 THR A CA  
1048 C  C   . THR A 127 ? 0.1565 0.0540 0.1529 0.0169  0.0166  -0.0074 125 THR A C   
1049 O  O   . THR A 127 ? 0.1766 0.0681 0.1655 0.0147  0.0062  0.0128  125 THR A O   
1050 C  CB  . THR A 127 ? 0.1434 0.0894 0.1638 0.0224  -0.0050 -0.0010 125 THR A CB  
1051 O  OG1 . THR A 127 ? 0.1586 0.1116 0.2030 0.0346  0.0080  -0.0072 125 THR A OG1 
1052 C  CG2 . THR A 127 ? 0.1461 0.1072 0.1671 0.0264  -0.0148 -0.0012 125 THR A CG2 
1053 N  N   . LYS A 128 ? 0.1714 0.0433 0.1500 0.0035  0.0249  -0.0219 127 LYS A N   
1054 C  CA  . LYS A 128 ? 0.1877 0.0667 0.1485 -0.0122 0.0294  -0.0297 127 LYS A CA  
1055 C  C   . LYS A 128 ? 0.1770 0.0542 0.1451 -0.0109 0.0211  -0.0235 127 LYS A C   
1056 O  O   . LYS A 128 ? 0.1965 0.0625 0.1788 -0.0181 0.0300  -0.0320 127 LYS A O   
1057 C  CB  . LYS A 128 ? 0.2070 0.1009 0.1536 -0.0305 0.0350  -0.0293 127 LYS A CB  
1058 C  CG  . LYS A 128 ? 0.2254 0.1277 0.1627 -0.0327 0.0418  -0.0246 127 LYS A CG  
1059 C  CD  . LYS A 128 ? 0.2609 0.1826 0.1890 -0.0359 0.0479  -0.0118 127 LYS A CD  
1060 C  CE  . LYS A 128 ? 0.2807 0.2200 0.1944 -0.0282 0.0507  0.0075  127 LYS A CE  
1061 N  NZ  . LYS A 128 ? 0.3127 0.2841 0.2109 -0.0233 0.0503  0.0182  127 LYS A NZ  
1062 N  N   . TYR A 129 ? 0.1631 0.0563 0.1293 -0.0078 0.0152  -0.0178 128 TYR A N   
1063 C  CA  . TYR A 129 ? 0.1583 0.0659 0.1273 -0.0110 0.0147  -0.0175 128 TYR A CA  
1064 C  C   . TYR A 129 ? 0.1507 0.0668 0.1253 -0.0021 0.0179  -0.0098 128 TYR A C   
1065 O  O   . TYR A 129 ? 0.1506 0.0905 0.1328 -0.0110 0.0172  -0.0052 128 TYR A O   
1066 C  CB  . TYR A 129 ? 0.1538 0.0714 0.1369 -0.0095 0.0153  -0.0218 128 TYR A CB  
1067 C  CG  . TYR A 129 ? 0.1569 0.0719 0.1356 -0.0010 0.0158  -0.0268 128 TYR A CG  
1068 C  CD1 . TYR A 129 ? 0.1773 0.0815 0.1337 0.0017  0.0151  -0.0324 128 TYR A CD1 
1069 C  CD2 . TYR A 129 ? 0.1523 0.0696 0.1312 -0.0010 0.0109  -0.0330 128 TYR A CD2 
1070 C  CE1 . TYR A 129 ? 0.1845 0.0923 0.1246 0.0056  0.0100  -0.0423 128 TYR A CE1 
1071 C  CE2 . TYR A 129 ? 0.1552 0.0854 0.1258 0.0065  0.0120  -0.0347 128 TYR A CE2 
1072 C  CZ  . TYR A 129 ? 0.1770 0.0968 0.1207 0.0112  0.0122  -0.0411 128 TYR A CZ  
1073 O  OH  . TYR A 129 ? 0.2211 0.1211 0.1172 0.0204  0.0109  -0.0539 128 TYR A OH  
1074 N  N   . GLY A 130 ? 0.1509 0.0603 0.1287 -0.0002 0.0123  -0.0083 129 GLY A N   
1075 C  CA  . GLY A 130 ? 0.1656 0.0582 0.1336 0.0029  0.0144  -0.0005 129 GLY A CA  
1076 C  C   . GLY A 130 ? 0.1727 0.0571 0.1149 0.0060  0.0116  0.0092  129 GLY A C   
1077 O  O   . GLY A 130 ? 0.1996 0.0651 0.1148 0.0136  0.0046  0.0101  129 GLY A O   
1078 N  N   . ASP A 131 ? 0.1793 0.0650 0.1050 0.0102  0.0176  0.0071  130 ASP A N   
1079 C  CA  . ASP A 131 ? 0.1906 0.0744 0.1040 0.0157  0.0241  0.0073  130 ASP A CA  
1080 C  C   . ASP A 131 ? 0.1816 0.0688 0.0819 0.0099  0.0201  0.0046  130 ASP A C   
1081 O  O   . ASP A 131 ? 0.1809 0.0680 0.0742 0.0068  0.0127  -0.0002 130 ASP A O   
1082 C  CB  . ASP A 131 ? 0.2054 0.0767 0.1190 0.0150  0.0339  0.0096  130 ASP A CB  
1083 C  CG  . ASP A 131 ? 0.2126 0.0723 0.1256 0.0122  0.0481  0.0177  130 ASP A CG  
1084 O  OD1 . ASP A 131 ? 0.2376 0.1107 0.1500 -0.0128 0.0257  0.0096  130 ASP A OD1 
1085 O  OD2 . ASP A 131 ? 0.2312 0.0985 0.1619 -0.0037 0.0708  0.0308  130 ASP A OD2 
1086 N  N   . PHE A 132 ? 0.1815 0.0704 0.0910 0.0055  0.0129  0.0000  131 PHE A N   
1087 C  CA  . PHE A 132 ? 0.1679 0.0670 0.0799 -0.0027 0.0184  -0.0019 131 PHE A CA  
1088 C  C   . PHE A 132 ? 0.1608 0.0577 0.0841 -0.0110 0.0273  0.0016  131 PHE A C   
1089 O  O   . PHE A 132 ? 0.1523 0.0548 0.0823 -0.0109 0.0249  -0.0009 131 PHE A O   
1090 C  CB  . PHE A 132 ? 0.1702 0.0707 0.0847 -0.0034 0.0156  -0.0070 131 PHE A CB  
1091 C  CG  . PHE A 132 ? 0.1619 0.0742 0.0966 -0.0068 0.0159  -0.0112 131 PHE A CG  
1092 C  CD1 . PHE A 132 ? 0.1544 0.0825 0.0981 -0.0173 0.0163  -0.0107 131 PHE A CD1 
1093 C  CD2 . PHE A 132 ? 0.1671 0.0760 0.1180 -0.0090 0.0191  -0.0137 131 PHE A CD2 
1094 C  CE1 . PHE A 132 ? 0.1659 0.0882 0.1141 -0.0203 0.0124  -0.0127 131 PHE A CE1 
1095 C  CE2 . PHE A 132 ? 0.1678 0.1017 0.1300 -0.0043 0.0152  -0.0109 131 PHE A CE2 
1096 C  CZ  . PHE A 132 ? 0.1750 0.0913 0.1270 -0.0096 0.0126  -0.0145 131 PHE A CZ  
1097 N  N   . GLY A 133 ? 0.1658 0.0680 0.0829 -0.0083 0.0324  0.0056  132 GLY A N   
1098 C  CA  . GLY A 133 ? 0.1580 0.0711 0.0934 -0.0134 0.0403  -0.0014 132 GLY A CA  
1099 C  C   . GLY A 133 ? 0.1535 0.0785 0.1046 -0.0217 0.0348  0.0000  132 GLY A C   
1100 O  O   . GLY A 133 ? 0.1471 0.0963 0.1190 -0.0194 0.0305  -0.0092 132 GLY A O   
1101 N  N   . LYS A 134 ? 0.1540 0.0702 0.0991 -0.0240 0.0305  0.0007  133 LYS A N   
1102 C  CA  . LYS A 134 ? 0.1497 0.0683 0.1037 -0.0313 0.0239  -0.0026 133 LYS A CA  
1103 C  C   . LYS A 134 ? 0.1319 0.0707 0.0889 -0.0310 0.0154  -0.0045 133 LYS A C   
1104 O  O   . LYS A 134 ? 0.1227 0.0760 0.0896 -0.0375 0.0090  -0.0034 133 LYS A O   
1105 C  CB  . LYS A 134 ? 0.1665 0.0711 0.1281 -0.0393 0.0273  0.0022  133 LYS A CB  
1106 C  CG  . LYS A 134 ? 0.2059 0.1146 0.1565 -0.0254 0.0242  0.0059  133 LYS A CG  
1107 C  CD  . LYS A 134 ? 0.2319 0.1355 0.1836 -0.0262 0.0180  0.0056  133 LYS A CD  
1108 C  CE  . LYS A 134 ? 0.2575 0.1750 0.2162 -0.0228 0.0220  0.0159  133 LYS A CE  
1109 N  NZ  . LYS A 134 ? 0.2899 0.2219 0.2422 -0.0176 0.0220  0.0041  133 LYS A NZ  
1110 N  N   . ALA A 135 ? 0.1268 0.0718 0.0822 -0.0338 0.0161  -0.0017 134 ALA A N   
1111 C  CA  . ALA A 135 ? 0.1159 0.0741 0.0802 -0.0316 0.0135  0.0011  134 ALA A CA  
1112 C  C   . ALA A 135 ? 0.1065 0.0758 0.0905 -0.0322 0.0155  -0.0008 134 ALA A C   
1113 O  O   . ALA A 135 ? 0.1000 0.0841 0.0921 -0.0256 0.0128  -0.0051 134 ALA A O   
1114 C  CB  . ALA A 135 ? 0.1142 0.0696 0.0761 -0.0302 0.0113  0.0026  134 ALA A CB  
1115 N  N   . VAL A 136 ? 0.1093 0.0769 0.0950 -0.0232 0.0183  0.0040  135 VAL A N   
1116 C  CA  . VAL A 136 ? 0.1194 0.0813 0.1065 -0.0188 0.0189  0.0041  135 VAL A CA  
1117 C  C   . VAL A 136 ? 0.1176 0.0914 0.1075 -0.0183 0.0209  0.0080  135 VAL A C   
1118 O  O   . VAL A 136 ? 0.1198 0.0999 0.1169 -0.0097 0.0217  0.0122  135 VAL A O   
1119 C  CB  . VAL A 136 ? 0.1344 0.0909 0.1112 -0.0122 0.0171  -0.0012 135 VAL A CB  
1120 C  CG1 . VAL A 136 ? 0.1512 0.1028 0.1185 -0.0112 0.0131  -0.0002 135 VAL A CG1 
1121 C  CG2 . VAL A 136 ? 0.1356 0.0887 0.1110 -0.0097 0.0192  -0.0055 135 VAL A CG2 
1122 N  N   . GLN A 137 ? 0.1111 0.0894 0.1026 -0.0234 0.0164  0.0083  136 GLN A N   
1123 C  CA  . GLN A 137 ? 0.1156 0.1113 0.1144 -0.0317 0.0142  0.0032  136 GLN A CA  
1124 C  C   . GLN A 137 ? 0.1175 0.1069 0.1057 -0.0277 0.0082  -0.0043 136 GLN A C   
1125 O  O   . GLN A 137 ? 0.1166 0.1350 0.1095 -0.0307 0.0034  -0.0068 136 GLN A O   
1126 C  CB  . GLN A 137 ? 0.1333 0.1346 0.1283 -0.0447 0.0138  0.0105  136 GLN A CB  
1127 C  CG  . GLN A 137 ? 0.1542 0.1677 0.1534 -0.0539 0.0186  0.0110  136 GLN A CG  
1128 C  CD  . GLN A 137 ? 0.1933 0.2265 0.1901 -0.0409 0.0200  0.0008  136 GLN A CD  
1129 O  OE1 . GLN A 137 ? 0.2252 0.3246 0.2463 -0.0251 0.0167  -0.0033 136 GLN A OE1 
1130 N  NE2 . GLN A 137 ? 0.2351 0.2528 0.2046 -0.0323 0.0207  0.0040  136 GLN A NE2 
1131 N  N   . GLN A 138 ? 0.1109 0.1025 0.0963 -0.0199 0.0100  -0.0089 137 GLN A N   
1132 C  CA  . GLN A 138 ? 0.1115 0.0977 0.0872 -0.0153 0.0080  -0.0090 137 GLN A CA  
1133 C  C   . GLN A 138 ? 0.1138 0.1080 0.0759 -0.0132 0.0092  -0.0054 137 GLN A C   
1134 O  O   . GLN A 138 ? 0.1120 0.0883 0.0700 -0.0076 0.0082  -0.0016 137 GLN A O   
1135 C  CB  . GLN A 138 ? 0.1224 0.0968 0.0909 -0.0146 0.0088  -0.0072 137 GLN A CB  
1136 C  CG  . GLN A 138 ? 0.1445 0.1076 0.1063 -0.0111 0.0130  -0.0054 137 GLN A CG  
1137 C  CD  . GLN A 138 ? 0.1671 0.1235 0.1286 -0.0163 0.0057  -0.0054 137 GLN A CD  
1138 O  OE1 . GLN A 138 ? 0.1801 0.1111 0.1488 -0.0231 -0.0084 -0.0293 137 GLN A OE1 
1139 N  NE2 . GLN A 138 ? 0.1866 0.1342 0.1346 -0.0183 0.0050  0.0017  137 GLN A NE2 
1140 N  N   A PRO A 139 ? 0.1086 0.1171 0.0762 -0.0130 0.0074  -0.0095 138 PRO A N   
1141 N  N   B PRO A 139 ? 0.1147 0.1174 0.0808 -0.0134 0.0066  -0.0081 138 PRO A N   
1142 C  CA  A PRO A 139 ? 0.1110 0.1221 0.0784 -0.0103 0.0070  -0.0037 138 PRO A CA  
1143 C  CA  B PRO A 139 ? 0.1169 0.1222 0.0851 -0.0107 0.0065  -0.0017 138 PRO A CA  
1144 C  C   A PRO A 139 ? 0.1094 0.1185 0.0820 -0.0102 0.0062  -0.0032 138 PRO A C   
1145 C  C   B PRO A 139 ? 0.1116 0.1174 0.0880 -0.0107 0.0091  -0.0007 138 PRO A C   
1146 O  O   A PRO A 139 ? 0.1204 0.1207 0.0858 -0.0051 0.0067  0.0018  138 PRO A O   
1147 O  O   B PRO A 139 ? 0.1159 0.1187 0.1006 -0.0072 0.0113  0.0067  138 PRO A O   
1148 C  CB  A PRO A 139 ? 0.1140 0.1281 0.0800 -0.0104 0.0079  -0.0050 138 PRO A CB  
1149 C  CB  B PRO A 139 ? 0.1245 0.1301 0.0886 -0.0099 0.0057  -0.0032 138 PRO A CB  
1150 C  CG  A PRO A 139 ? 0.1105 0.1290 0.0793 -0.0111 0.0066  -0.0114 138 PRO A CG  
1151 C  CG  B PRO A 139 ? 0.1275 0.1307 0.0920 -0.0118 0.0024  -0.0087 138 PRO A CG  
1152 C  CD  A PRO A 139 ? 0.1141 0.1253 0.0815 -0.0151 0.0042  -0.0110 138 PRO A CD  
1153 C  CD  B PRO A 139 ? 0.1246 0.1265 0.0894 -0.0164 0.0019  -0.0096 138 PRO A CD  
1154 N  N   . ASP A 140 ? 0.1024 0.1164 0.0887 -0.0124 0.0098  -0.0040 139 ASP A N   
1155 C  CA  . ASP A 140 ? 0.1004 0.1130 0.0898 -0.0079 0.0158  -0.0065 139 ASP A CA  
1156 C  C   . ASP A 140 ? 0.0910 0.0882 0.0835 -0.0098 0.0177  -0.0053 139 ASP A C   
1157 O  O   . ASP A 140 ? 0.1004 0.0950 0.0943 -0.0009 0.0196  -0.0054 139 ASP A O   
1158 C  CB  . ASP A 140 ? 0.1192 0.1401 0.1003 -0.0020 0.0215  -0.0161 139 ASP A CB  
1159 C  CG  . ASP A 140 ? 0.1304 0.1507 0.1065 0.0055  0.0272  -0.0230 139 ASP A CG  
1160 O  OD1 . ASP A 140 ? 0.1554 0.1244 0.1253 0.0071  0.0313  -0.0315 139 ASP A OD1 
1161 O  OD2 . ASP A 140 ? 0.1616 0.1743 0.1437 0.0147  0.0334  -0.0466 139 ASP A OD2 
1162 N  N   . GLY A 141 ? 0.0811 0.0650 0.0721 -0.0008 0.0116  -0.0046 140 GLY A N   
1163 C  CA  . GLY A 141 ? 0.0873 0.0641 0.0735 -0.0022 0.0114  -0.0025 140 GLY A CA  
1164 C  C   . GLY A 141 ? 0.0835 0.0531 0.0742 -0.0009 0.0101  -0.0040 140 GLY A C   
1165 O  O   . GLY A 141 ? 0.0930 0.0499 0.0739 -0.0008 0.0074  -0.0070 140 GLY A O   
1166 N  N   . LEU A 142 ? 0.0816 0.0495 0.0796 -0.0019 0.0071  -0.0028 141 LEU A N   
1167 C  CA  . LEU A 142 ? 0.0879 0.0495 0.0775 0.0001  0.0094  0.0000  141 LEU A CA  
1168 C  C   . LEU A 142 ? 0.0861 0.0472 0.0759 0.0015  0.0086  -0.0004 141 LEU A C   
1169 O  O   . LEU A 142 ? 0.0821 0.0548 0.0739 0.0035  0.0098  -0.0026 141 LEU A O   
1170 C  CB  . LEU A 142 ? 0.0962 0.0514 0.0890 0.0000  0.0132  0.0002  141 LEU A CB  
1171 C  CG  . LEU A 142 ? 0.1122 0.0647 0.1051 0.0017  0.0192  0.0028  141 LEU A CG  
1172 C  CD1 . LEU A 142 ? 0.1111 0.0599 0.0990 0.0015  0.0187  0.0019  141 LEU A CD1 
1173 C  CD2 . LEU A 142 ? 0.1264 0.0706 0.1149 0.0041  0.0215  0.0054  141 LEU A CD2 
1174 N  N   . ALA A 143 ? 0.0837 0.0487 0.0713 -0.0043 0.0086  0.0029  142 ALA A N   
1175 C  CA  . ALA A 143 ? 0.0841 0.0474 0.0705 -0.0066 0.0065  0.0001  142 ALA A CA  
1176 C  C   . ALA A 143 ? 0.0853 0.0476 0.0669 -0.0036 0.0035  -0.0003 142 ALA A C   
1177 O  O   . ALA A 143 ? 0.0953 0.0493 0.0758 -0.0064 -0.0010 0.0030  142 ALA A O   
1178 C  CB  . ALA A 143 ? 0.0864 0.0558 0.0756 -0.0112 0.0076  -0.0016 142 ALA A CB  
1179 N  N   . VAL A 144 ? 0.0845 0.0503 0.0616 -0.0042 0.0042  0.0019  143 VAL A N   
1180 C  CA  . VAL A 144 ? 0.0853 0.0540 0.0623 -0.0021 0.0077  0.0013  143 VAL A CA  
1181 C  C   . VAL A 144 ? 0.0852 0.0484 0.0566 -0.0029 0.0082  0.0022  143 VAL A C   
1182 O  O   . VAL A 144 ? 0.0907 0.0516 0.0613 -0.0008 0.0076  0.0065  143 VAL A O   
1183 C  CB  . VAL A 144 ? 0.0844 0.0648 0.0671 0.0008  0.0062  -0.0004 143 VAL A CB  
1184 C  CG1 . VAL A 144 ? 0.0811 0.0650 0.0753 0.0064  0.0084  -0.0030 143 VAL A CG1 
1185 C  CG2 . VAL A 144 ? 0.0850 0.0760 0.0721 0.0000  0.0074  0.0019  143 VAL A CG2 
1186 N  N   . LEU A 145 ? 0.0827 0.0496 0.0585 -0.0033 0.0104  0.0028  144 LEU A N   
1187 C  CA  . LEU A 145 ? 0.0827 0.0606 0.0599 -0.0059 0.0149  0.0004  144 LEU A CA  
1188 C  C   . LEU A 145 ? 0.0865 0.0531 0.0563 -0.0076 0.0166  -0.0020 144 LEU A C   
1189 O  O   . LEU A 145 ? 0.1122 0.0557 0.0624 -0.0088 0.0198  -0.0014 144 LEU A O   
1190 C  CB  . LEU A 145 ? 0.0970 0.0822 0.0735 -0.0045 0.0081  0.0019  144 LEU A CB  
1191 C  CG  . LEU A 145 ? 0.1062 0.0943 0.0944 -0.0046 0.0071  -0.0016 144 LEU A CG  
1192 C  CD1 . LEU A 145 ? 0.1097 0.1161 0.1096 -0.0128 0.0054  0.0085  144 LEU A CD1 
1193 C  CD2 . LEU A 145 ? 0.1070 0.1145 0.0953 -0.0009 0.0064  -0.0027 144 LEU A CD2 
1194 N  N   . GLY A 146 ? 0.0809 0.0487 0.0524 -0.0059 0.0180  -0.0041 145 GLY A N   
1195 C  CA  . GLY A 146 ? 0.0798 0.0515 0.0588 -0.0036 0.0184  -0.0045 145 GLY A CA  
1196 C  C   . GLY A 146 ? 0.0764 0.0496 0.0557 -0.0021 0.0167  -0.0028 145 GLY A C   
1197 O  O   . GLY A 146 ? 0.0917 0.0607 0.0661 -0.0088 0.0239  -0.0057 145 GLY A O   
1198 N  N   . ILE A 147 ? 0.0738 0.0441 0.0546 -0.0035 0.0156  -0.0001 146 ILE A N   
1199 C  CA  . ILE A 147 ? 0.0734 0.0473 0.0642 -0.0041 0.0126  0.0003  146 ILE A CA  
1200 C  C   . ILE A 147 ? 0.0749 0.0478 0.0658 -0.0032 0.0150  -0.0015 146 ILE A C   
1201 O  O   . ILE A 147 ? 0.0837 0.0481 0.0698 -0.0044 0.0201  0.0007  146 ILE A O   
1202 C  CB  . ILE A 147 ? 0.0804 0.0566 0.0766 -0.0017 0.0068  0.0007  146 ILE A CB  
1203 C  CG1 . ILE A 147 ? 0.0858 0.0647 0.0843 0.0000  0.0058  0.0011  146 ILE A CG1 
1204 C  CG2 . ILE A 147 ? 0.0875 0.0668 0.0917 -0.0020 0.0036  -0.0005 146 ILE A CG2 
1205 C  CD1 . ILE A 147 ? 0.0832 0.0601 0.0907 -0.0025 0.0050  0.0024  146 ILE A CD1 
1206 N  N   . PHE A 148 ? 0.0756 0.0457 0.0651 -0.0006 0.0176  0.0000  147 PHE A N   
1207 C  CA  . PHE A 148 ? 0.0770 0.0475 0.0702 -0.0017 0.0149  0.0003  147 PHE A CA  
1208 C  C   . PHE A 148 ? 0.0786 0.0527 0.0773 -0.0074 0.0156  -0.0040 147 PHE A C   
1209 O  O   . PHE A 148 ? 0.0792 0.0665 0.0791 -0.0046 0.0167  -0.0094 147 PHE A O   
1210 C  CB  . PHE A 148 ? 0.0783 0.0467 0.0716 -0.0010 0.0126  0.0002  147 PHE A CB  
1211 C  CG  . PHE A 148 ? 0.0800 0.0468 0.0703 -0.0021 0.0119  0.0028  147 PHE A CG  
1212 C  CD1 . PHE A 148 ? 0.0820 0.0521 0.0747 -0.0003 0.0115  -0.0007 147 PHE A CD1 
1213 C  CD2 . PHE A 148 ? 0.0813 0.0509 0.0738 -0.0010 0.0133  0.0058  147 PHE A CD2 
1214 C  CE1 . PHE A 148 ? 0.0784 0.0587 0.0812 -0.0019 0.0086  0.0032  147 PHE A CE1 
1215 C  CE2 . PHE A 148 ? 0.0854 0.0568 0.0786 -0.0008 0.0117  0.0030  147 PHE A CE2 
1216 C  CZ  . PHE A 148 ? 0.0840 0.0541 0.0765 -0.0044 0.0064  0.0007  147 PHE A CZ  
1217 N  N   . LEU A 149 ? 0.0814 0.0483 0.0761 -0.0087 0.0125  -0.0057 148 LEU A N   
1218 C  CA  . LEU A 149 ? 0.0878 0.0478 0.0844 -0.0095 0.0083  -0.0046 148 LEU A CA  
1219 C  C   . LEU A 149 ? 0.0940 0.0506 0.0906 -0.0083 0.0075  -0.0017 148 LEU A C   
1220 O  O   . LEU A 149 ? 0.1020 0.0532 0.0957 0.0010  0.0138  0.0025  148 LEU A O   
1221 C  CB  . LEU A 149 ? 0.0944 0.0514 0.0847 -0.0091 0.0057  -0.0028 148 LEU A CB  
1222 C  CG  . LEU A 149 ? 0.1015 0.0482 0.0900 -0.0108 0.0055  -0.0026 148 LEU A CG  
1223 C  CD1 . LEU A 149 ? 0.1146 0.0504 0.0879 -0.0108 0.0034  -0.0019 148 LEU A CD1 
1224 C  CD2 . LEU A 149 ? 0.1044 0.0588 0.0972 -0.0115 0.0053  0.0012  148 LEU A CD2 
1225 N  N   . LYS A 150 ? 0.1076 0.0526 0.1122 -0.0114 -0.0001 -0.0013 149 LYS A N   
1226 C  CA  . LYS A 150 ? 0.1268 0.0581 0.1224 -0.0109 -0.0016 0.0019  149 LYS A CA  
1227 C  C   . LYS A 150 ? 0.1344 0.0664 0.1238 -0.0051 -0.0086 0.0034  149 LYS A C   
1228 O  O   . LYS A 150 ? 0.1478 0.0714 0.1167 0.0093  -0.0135 -0.0035 149 LYS A O   
1229 C  CB  . LYS A 150 ? 0.1512 0.0779 0.1410 -0.0215 0.0008  0.0094  149 LYS A CB  
1230 C  CG  . LYS A 150 ? 0.1686 0.0998 0.1644 -0.0232 0.0041  0.0150  149 LYS A CG  
1231 C  CD  . LYS A 150 ? 0.2007 0.1444 0.1885 -0.0277 0.0061  0.0202  149 LYS A CD  
1232 C  CE  . LYS A 150 ? 0.2265 0.1978 0.2149 -0.0264 0.0184  0.0234  149 LYS A CE  
1233 N  NZ  . LYS A 150 ? 0.2425 0.2347 0.2265 -0.0351 0.0233  0.0278  149 LYS A NZ  
1234 N  N   . VAL A 151 ? 0.1446 0.0668 0.1230 -0.0007 -0.0173 -0.0023 150 VAL A N   
1235 C  CA  . VAL A 151 ? 0.1403 0.0661 0.1245 -0.0001 -0.0163 -0.0060 150 VAL A CA  
1236 C  C   . VAL A 151 ? 0.1500 0.0748 0.1345 -0.0069 -0.0141 -0.0028 150 VAL A C   
1237 O  O   . VAL A 151 ? 0.1635 0.0879 0.1475 -0.0029 -0.0229 0.0043  150 VAL A O   
1238 C  CB  . VAL A 151 ? 0.1456 0.0777 0.1309 -0.0003 -0.0106 -0.0094 150 VAL A CB  
1239 C  CG1 . VAL A 151 ? 0.1501 0.0876 0.1334 -0.0006 -0.0081 -0.0100 150 VAL A CG1 
1240 C  CG2 . VAL A 151 ? 0.1451 0.0952 0.1323 -0.0039 -0.0095 -0.0123 150 VAL A CG2 
1241 N  N   . GLY A 152 ? 0.1424 0.0665 0.1302 -0.0193 -0.0174 0.0014  151 GLY A N   
1242 C  CA  . GLY A 152 ? 0.1391 0.0807 0.1340 -0.0237 -0.0122 0.0031  151 GLY A CA  
1243 C  C   . GLY A 152 ? 0.1369 0.0793 0.1318 -0.0304 -0.0127 -0.0022 151 GLY A C   
1244 O  O   . GLY A 152 ? 0.1384 0.0804 0.1316 -0.0248 -0.0132 -0.0043 151 GLY A O   
1245 N  N   A SER A 153 ? 0.1364 0.0929 0.1440 -0.0293 -0.0094 -0.0030 152 SER A N   
1246 N  N   B SER A 153 ? 0.1421 0.0971 0.1415 -0.0284 -0.0112 -0.0043 152 SER A N   
1247 C  CA  A SER A 153 ? 0.1309 0.0971 0.1560 -0.0285 -0.0072 -0.0044 152 SER A CA  
1248 C  CA  B SER A 153 ? 0.1422 0.1052 0.1528 -0.0268 -0.0110 -0.0061 152 SER A CA  
1249 C  C   A SER A 153 ? 0.1335 0.0882 0.1458 -0.0237 -0.0078 -0.0078 152 SER A C   
1250 C  C   B SER A 153 ? 0.1390 0.0931 0.1443 -0.0227 -0.0094 -0.0100 152 SER A C   
1251 O  O   A SER A 153 ? 0.1316 0.0873 0.1394 -0.0214 -0.0139 -0.0047 152 SER A O   
1252 O  O   B SER A 153 ? 0.1343 0.0893 0.1419 -0.0223 -0.0142 -0.0087 152 SER A O   
1253 C  CB  A SER A 153 ? 0.1342 0.1083 0.1721 -0.0323 -0.0004 -0.0040 152 SER A CB  
1254 C  CB  B SER A 153 ? 0.1525 0.1290 0.1666 -0.0285 -0.0064 -0.0037 152 SER A CB  
1255 O  OG  A SER A 153 ? 0.1323 0.1262 0.1943 -0.0321 0.0087  0.0080  152 SER A OG  
1256 O  OG  B SER A 153 ? 0.1799 0.1593 0.1872 -0.0227 -0.0090 -0.0097 152 SER A OG  
1257 N  N   . ALA A 154 ? 0.1353 0.0860 0.1362 -0.0243 -0.0117 -0.0143 153 ALA A N   
1258 C  CA  . ALA A 154 ? 0.1310 0.0912 0.1340 -0.0164 -0.0112 -0.0109 153 ALA A CA  
1259 C  C   . ALA A 154 ? 0.1258 0.0892 0.1391 -0.0108 -0.0052 -0.0075 153 ALA A C   
1260 O  O   . ALA A 154 ? 0.1326 0.0965 0.1579 -0.0191 -0.0011 -0.0151 153 ALA A O   
1261 C  CB  . ALA A 154 ? 0.1381 0.1040 0.1308 -0.0087 -0.0123 -0.0081 153 ALA A CB  
1262 N  N   . LYS A 155 ? 0.1232 0.0841 0.1401 -0.0029 -0.0050 0.0017  154 LYS A N   
1263 C  CA  . LYS A 155 ? 0.1349 0.0853 0.1445 -0.0083 0.0013  0.0030  154 LYS A CA  
1264 C  C   . LYS A 155 ? 0.1183 0.0931 0.1595 -0.0090 -0.0067 0.0020  154 LYS A C   
1265 O  O   . LYS A 155 ? 0.1139 0.0866 0.1389 -0.0093 -0.0067 -0.0018 154 LYS A O   
1266 C  CB  . LYS A 155 ? 0.1468 0.0853 0.1498 -0.0030 -0.0067 0.0081  154 LYS A CB  
1267 C  CG  . LYS A 155 ? 0.1700 0.0904 0.1588 -0.0056 -0.0024 0.0065  154 LYS A CG  
1268 C  CD  . LYS A 155 ? 0.1945 0.1126 0.1649 -0.0005 0.0042  0.0014  154 LYS A CD  
1269 C  CE  . LYS A 155 ? 0.2151 0.1332 0.1772 0.0048  0.0153  0.0000  154 LYS A CE  
1270 N  NZ  . LYS A 155 ? 0.2284 0.1629 0.2050 -0.0011 0.0216  0.0020  154 LYS A NZ  
1271 N  N   . PRO A 156 ? 0.1184 0.1151 0.1748 -0.0112 -0.0110 0.0126  155 PRO A N   
1272 C  CA  . PRO A 156 ? 0.1122 0.1319 0.1809 -0.0099 -0.0129 0.0160  155 PRO A CA  
1273 C  C   . PRO A 156 ? 0.1211 0.1341 0.1811 -0.0057 -0.0133 0.0260  155 PRO A C   
1274 O  O   . PRO A 156 ? 0.1284 0.1580 0.1782 0.0024  -0.0159 0.0369  155 PRO A O   
1275 C  CB  . PRO A 156 ? 0.1177 0.1533 0.2071 -0.0090 -0.0136 0.0183  155 PRO A CB  
1276 C  CG  . PRO A 156 ? 0.1363 0.1673 0.2142 -0.0126 -0.0098 0.0191  155 PRO A CG  
1277 C  CD  . PRO A 156 ? 0.1261 0.1418 0.1934 -0.0102 -0.0057 0.0219  155 PRO A CD  
1278 N  N   . GLY A 157 ? 0.1172 0.1079 0.1914 -0.0020 -0.0028 0.0225  156 GLY A N   
1279 C  CA  . GLY A 157 ? 0.1310 0.1003 0.1861 -0.0049 0.0025  0.0230  156 GLY A CA  
1280 C  C   . GLY A 157 ? 0.1333 0.0942 0.1788 -0.0120 -0.0009 0.0131  156 GLY A C   
1281 O  O   . GLY A 157 ? 0.1538 0.0968 0.2080 -0.0144 0.0067  0.0167  156 GLY A O   
1282 N  N   . LEU A 158 ? 0.1168 0.0879 0.1481 -0.0182 0.0033  0.0073  157 LEU A N   
1283 C  CA  . LEU A 158 ? 0.1084 0.0842 0.1442 -0.0248 -0.0028 -0.0042 157 LEU A CA  
1284 C  C   . LEU A 158 ? 0.1169 0.0805 0.1411 -0.0249 -0.0067 -0.0034 157 LEU A C   
1285 O  O   . LEU A 158 ? 0.1217 0.0912 0.1323 -0.0324 -0.0078 -0.0032 157 LEU A O   
1286 C  CB  . LEU A 158 ? 0.1097 0.0977 0.1470 -0.0228 -0.0041 -0.0052 157 LEU A CB  
1287 C  CG  . LEU A 158 ? 0.1096 0.1113 0.1343 -0.0220 -0.0091 -0.0049 157 LEU A CG  
1288 C  CD1 . LEU A 158 ? 0.1163 0.1125 0.1307 -0.0248 -0.0096 -0.0082 157 LEU A CD1 
1289 C  CD2 . LEU A 158 ? 0.1216 0.1267 0.1356 -0.0112 -0.0071 -0.0051 157 LEU A CD2 
1290 N  N   . GLN A 159 ? 0.1261 0.0959 0.1356 -0.0281 -0.0081 -0.0020 158 GLN A N   
1291 C  CA  . GLN A 159 ? 0.1346 0.1063 0.1375 -0.0262 -0.0139 -0.0048 158 GLN A CA  
1292 C  C   . GLN A 159 ? 0.1319 0.1055 0.1381 -0.0271 -0.0208 -0.0080 158 GLN A C   
1293 O  O   . GLN A 159 ? 0.1315 0.1025 0.1274 -0.0243 -0.0209 -0.0100 158 GLN A O   
1294 C  CB  . GLN A 159 ? 0.1434 0.1083 0.1499 -0.0285 -0.0164 -0.0045 158 GLN A CB  
1295 C  CG  . GLN A 159 ? 0.1589 0.1137 0.1500 -0.0260 -0.0165 -0.0075 158 GLN A CG  
1296 C  CD  . GLN A 159 ? 0.1629 0.1069 0.1418 -0.0289 -0.0142 -0.0117 158 GLN A CD  
1297 O  OE1 . GLN A 159 ? 0.1642 0.0916 0.1290 -0.0184 -0.0203 -0.0093 158 GLN A OE1 
1298 N  NE2 . GLN A 159 ? 0.1805 0.1283 0.1379 -0.0358 -0.0157 -0.0200 158 GLN A NE2 
1299 N  N   . LYS A 160 ? 0.1344 0.1185 0.1329 -0.0225 -0.0210 -0.0021 159 LYS A N   
1300 C  CA  . LYS A 160 ? 0.1491 0.1175 0.1419 -0.0187 -0.0235 0.0001  159 LYS A CA  
1301 C  C   . LYS A 160 ? 0.1428 0.1087 0.1295 -0.0284 -0.0132 -0.0042 159 LYS A C   
1302 O  O   . LYS A 160 ? 0.1529 0.1313 0.1188 -0.0368 -0.0193 -0.0033 159 LYS A O   
1303 C  CB  . LYS A 160 ? 0.1769 0.1406 0.1703 -0.0131 -0.0182 0.0055  159 LYS A CB  
1304 C  CG  . LYS A 160 ? 0.2156 0.1969 0.2102 -0.0053 -0.0160 0.0054  159 LYS A CG  
1305 C  CD  . LYS A 160 ? 0.2729 0.2672 0.2428 0.0008  -0.0119 -0.0022 159 LYS A CD  
1306 C  CE  . LYS A 160 ? 0.3106 0.3142 0.2667 0.0022  -0.0214 -0.0022 159 LYS A CE  
1307 N  NZ  . LYS A 160 ? 0.3575 0.3590 0.3029 0.0059  -0.0186 -0.0112 159 LYS A NZ  
1308 N  N   . VAL A 161 ? 0.1301 0.1050 0.1295 -0.0283 -0.0056 -0.0076 160 VAL A N   
1309 C  CA  . VAL A 161 ? 0.1246 0.0976 0.1253 -0.0313 -0.0008 -0.0107 160 VAL A CA  
1310 C  C   . VAL A 161 ? 0.1256 0.0955 0.1199 -0.0276 -0.0007 -0.0152 160 VAL A C   
1311 O  O   . VAL A 161 ? 0.1316 0.1059 0.1261 -0.0202 0.0005  -0.0155 160 VAL A O   
1312 C  CB  . VAL A 161 ? 0.1246 0.1026 0.1288 -0.0309 0.0045  -0.0069 160 VAL A CB  
1313 C  CG1 . VAL A 161 ? 0.1262 0.1093 0.1383 -0.0380 0.0097  -0.0018 160 VAL A CG1 
1314 C  CG2 . VAL A 161 ? 0.1376 0.1098 0.1325 -0.0226 0.0003  -0.0119 160 VAL A CG2 
1315 N  N   . VAL A 162 ? 0.1341 0.0890 0.1231 -0.0240 0.0073  -0.0226 161 VAL A N   
1316 C  CA  . VAL A 162 ? 0.1574 0.1001 0.1367 -0.0166 0.0103  -0.0256 161 VAL A CA  
1317 C  C   . VAL A 162 ? 0.1694 0.1080 0.1352 -0.0270 0.0121  -0.0264 161 VAL A C   
1318 O  O   . VAL A 162 ? 0.1845 0.1189 0.1468 -0.0228 0.0273  -0.0300 161 VAL A O   
1319 C  CB  . VAL A 162 ? 0.1705 0.0984 0.1596 -0.0089 0.0114  -0.0267 161 VAL A CB  
1320 C  CG1 . VAL A 162 ? 0.1750 0.1114 0.1732 -0.0115 0.0071  -0.0284 161 VAL A CG1 
1321 C  CG2 . VAL A 162 ? 0.1772 0.0929 0.1719 -0.0086 0.0150  -0.0214 161 VAL A CG2 
1322 N  N   . ASP A 163 ? 0.1807 0.1326 0.1116 -0.0360 0.0075  -0.0258 162 ASP A N   
1323 C  CA  . ASP A 163 ? 0.2033 0.1589 0.1167 -0.0423 0.0053  -0.0242 162 ASP A CA  
1324 C  C   . ASP A 163 ? 0.2156 0.1586 0.1194 -0.0405 0.0094  -0.0158 162 ASP A C   
1325 O  O   . ASP A 163 ? 0.2931 0.1954 0.1338 -0.0492 0.0199  -0.0309 162 ASP A O   
1326 C  CB  . ASP A 163 ? 0.2286 0.2130 0.1335 -0.0422 0.0028  -0.0160 162 ASP A CB  
1327 C  CG  . ASP A 163 ? 0.2424 0.2210 0.1663 -0.0427 -0.0033 -0.0307 162 ASP A CG  
1328 O  OD1 . ASP A 163 ? 0.2574 0.2351 0.2255 -0.0569 -0.0040 -0.0258 162 ASP A OD1 
1329 O  OD2 . ASP A 163 ? 0.2694 0.2680 0.2196 -0.0533 0.0046  -0.0206 162 ASP A OD2 
1330 N  N   . VAL A 164 ? 0.1703 0.1466 0.0874 -0.0311 0.0013  -0.0138 163 VAL A N   
1331 C  CA  . VAL A 164 ? 0.1706 0.1435 0.1109 -0.0206 0.0130  0.0009  163 VAL A CA  
1332 C  C   . VAL A 164 ? 0.1619 0.1282 0.1001 -0.0182 0.0159  0.0026  163 VAL A C   
1333 O  O   . VAL A 164 ? 0.1642 0.1335 0.1069 -0.0205 0.0247  0.0031  163 VAL A O   
1334 C  CB  . VAL A 164 ? 0.1775 0.1426 0.1397 -0.0153 0.0153  0.0085  163 VAL A CB  
1335 C  CG1 . VAL A 164 ? 0.1799 0.1330 0.1393 -0.0187 0.0263  0.0062  163 VAL A CG1 
1336 C  CG2 . VAL A 164 ? 0.1872 0.1618 0.1423 -0.0118 0.0211  0.0126  163 VAL A CG2 
1337 N  N   . LEU A 165 ? 0.1570 0.1123 0.1118 -0.0190 0.0117  0.0014  164 LEU A N   
1338 C  CA  . LEU A 165 ? 0.1557 0.1063 0.1172 -0.0131 0.0188  0.0027  164 LEU A CA  
1339 C  C   . LEU A 165 ? 0.1735 0.1165 0.1201 -0.0126 0.0199  -0.0025 164 LEU A C   
1340 O  O   . LEU A 165 ? 0.1639 0.1171 0.1248 0.0015  0.0221  0.0067  164 LEU A O   
1341 C  CB  . LEU A 165 ? 0.1543 0.1074 0.1247 -0.0112 0.0136  0.0114  164 LEU A CB  
1342 C  CG  . LEU A 165 ? 0.1461 0.1082 0.1248 -0.0044 0.0071  0.0211  164 LEU A CG  
1343 C  CD1 . LEU A 165 ? 0.1508 0.1163 0.1345 -0.0018 0.0044  0.0257  164 LEU A CD1 
1344 C  CD2 . LEU A 165 ? 0.1449 0.1174 0.1187 -0.0015 0.0089  0.0172  164 LEU A CD2 
1345 N  N   . ASP A 166 ? 0.2036 0.1485 0.1348 -0.0136 0.0280  -0.0219 165 ASP A N   
1346 C  CA  . ASP A 166 ? 0.2380 0.1797 0.1440 -0.0198 0.0331  -0.0218 165 ASP A CA  
1347 C  C   . ASP A 166 ? 0.2195 0.1925 0.1353 -0.0160 0.0376  -0.0086 165 ASP A C   
1348 O  O   . ASP A 166 ? 0.2646 0.2289 0.1986 0.0060  0.0718  -0.0132 165 ASP A O   
1349 C  CB  . ASP A 166 ? 0.2752 0.2249 0.1830 -0.0284 0.0303  -0.0316 165 ASP A CB  
1350 C  CG  . ASP A 166 ? 0.3228 0.2781 0.2341 -0.0253 0.0189  -0.0197 165 ASP A CG  
1351 O  OD1 . ASP A 166 ? 0.3657 0.3372 0.3016 -0.0135 -0.0025 -0.0156 165 ASP A OD1 
1352 O  OD2 . ASP A 166 ? 0.3686 0.3427 0.2864 -0.0439 0.0128  -0.0385 165 ASP A OD2 
1353 N  N   . SER A 167 ? 0.1783 0.1748 0.1104 -0.0139 0.0070  0.0021  166 SER A N   
1354 C  CA  . SER A 167 ? 0.1698 0.1774 0.1066 -0.0083 0.0099  0.0124  166 SER A CA  
1355 C  C   . SER A 167 ? 0.1450 0.1495 0.0898 -0.0067 0.0124  0.0134  166 SER A C   
1356 O  O   . SER A 167 ? 0.1758 0.1677 0.0957 -0.0113 0.0096  0.0235  166 SER A O   
1357 C  CB  . SER A 167 ? 0.1768 0.1947 0.1239 -0.0078 0.0064  0.0179  166 SER A CB  
1358 O  OG  . SER A 167 ? 0.1881 0.1949 0.1525 0.0020  0.0051  0.0151  166 SER A OG  
1359 N  N   . ILE A 168 ? 0.1370 0.1152 0.0834 -0.0007 0.0092  0.0061  167 ILE A N   
1360 C  CA  . ILE A 168 ? 0.1274 0.1065 0.0948 0.0014  0.0131  0.0010  167 ILE A CA  
1361 C  C   . ILE A 168 ? 0.1249 0.0941 0.0825 0.0005  0.0218  0.0005  167 ILE A C   
1362 O  O   . ILE A 168 ? 0.1228 0.0931 0.0887 -0.0012 0.0208  0.0020  167 ILE A O   
1363 C  CB  . ILE A 168 ? 0.1279 0.1066 0.0994 0.0029  0.0131  0.0027  167 ILE A CB  
1364 C  CG1 . ILE A 168 ? 0.1177 0.1081 0.0992 0.0020  0.0160  -0.0008 167 ILE A CG1 
1365 C  CG2 . ILE A 168 ? 0.1322 0.1116 0.1131 0.0070  0.0075  -0.0026 167 ILE A CG2 
1366 C  CD1 . ILE A 168 ? 0.1266 0.1139 0.1060 0.0023  0.0184  0.0000  167 ILE A CD1 
1367 N  N   . LYS A 169 ? 0.1353 0.0961 0.0796 -0.0009 0.0229  -0.0009 168 LYS A N   
1368 C  CA  . LYS A 169 ? 0.1431 0.0949 0.0844 -0.0008 0.0255  -0.0031 168 LYS A CA  
1369 C  C   . LYS A 169 ? 0.1379 0.0875 0.0829 -0.0047 0.0325  0.0057  168 LYS A C   
1370 O  O   . LYS A 169 ? 0.1407 0.0784 0.0876 -0.0061 0.0285  0.0117  168 LYS A O   
1371 C  CB  . LYS A 169 ? 0.1633 0.1128 0.1107 0.0007  0.0211  -0.0148 168 LYS A CB  
1372 C  CG  . LYS A 169 ? 0.1839 0.1281 0.1332 0.0034  0.0219  -0.0198 168 LYS A CG  
1373 C  CD  . LYS A 169 ? 0.2205 0.1485 0.1625 0.0028  0.0188  -0.0296 168 LYS A CD  
1374 C  CE  . LYS A 169 ? 0.2509 0.1810 0.1990 0.0108  0.0176  -0.0278 168 LYS A CE  
1375 N  NZ  . LYS A 169 ? 0.2932 0.2173 0.2325 0.0153  0.0178  -0.0297 168 LYS A NZ  
1376 N  N   . THR A 170 ? 0.1220 0.0877 0.0848 -0.0009 0.0301  0.0145  169 THR A N   
1377 C  CA  . THR A 170 ? 0.1231 0.0853 0.0882 -0.0025 0.0346  0.0141  169 THR A CA  
1378 C  C   . THR A 170 ? 0.1172 0.0872 0.0921 0.0005  0.0315  0.0067  169 THR A C   
1379 O  O   . THR A 170 ? 0.1192 0.0889 0.1029 -0.0041 0.0255  0.0007  169 THR A O   
1380 C  CB  . THR A 170 ? 0.1344 0.0930 0.0969 0.0025  0.0405  0.0169  169 THR A CB  
1381 O  OG1 . THR A 170 ? 0.1394 0.1128 0.0918 0.0068  0.0446  0.0153  169 THR A OG1 
1382 C  CG2 . THR A 170 ? 0.1401 0.0951 0.1002 0.0020  0.0424  0.0176  169 THR A CG2 
1383 N  N   . LYS A 171 ? 0.1173 0.0982 0.0951 0.0026  0.0319  0.0090  170 LYS A N   
1384 C  CA  . LYS A 171 ? 0.1198 0.1057 0.0986 -0.0033 0.0329  0.0122  170 LYS A CA  
1385 C  C   . LYS A 171 ? 0.1288 0.1051 0.1017 -0.0086 0.0339  0.0126  170 LYS A C   
1386 O  O   . LYS A 171 ? 0.1434 0.1219 0.0957 -0.0139 0.0372  0.0101  170 LYS A O   
1387 C  CB  . LYS A 171 ? 0.1293 0.1217 0.1157 -0.0043 0.0306  0.0116  170 LYS A CB  
1388 C  CG  . LYS A 171 ? 0.1487 0.1431 0.1365 -0.0078 0.0311  0.0110  170 LYS A CG  
1389 C  CD  . LYS A 171 ? 0.1631 0.1765 0.1714 -0.0001 0.0374  0.0085  170 LYS A CD  
1390 C  CE  . LYS A 171 ? 0.2112 0.2177 0.2182 -0.0001 0.0252  0.0104  170 LYS A CE  
1391 N  NZ  . LYS A 171 ? 0.2562 0.2679 0.2532 0.0083  0.0197  0.0100  170 LYS A NZ  
1392 N  N   . GLY A 172 ? 0.1313 0.0904 0.1113 -0.0104 0.0317  0.0203  171 GLY A N   
1393 C  CA  . GLY A 172 ? 0.1465 0.0921 0.1265 -0.0117 0.0215  0.0250  171 GLY A CA  
1394 C  C   . GLY A 172 ? 0.1536 0.0928 0.1248 -0.0046 0.0175  0.0305  171 GLY A C   
1395 O  O   . GLY A 172 ? 0.1917 0.0899 0.1669 -0.0064 0.0079  0.0361  171 GLY A O   
1396 N  N   . LYS A 173 ? 0.1445 0.0916 0.1120 0.0013  0.0223  0.0307  172 LYS A N   
1397 C  CA  . LYS A 173 ? 0.1453 0.1121 0.1129 0.0066  0.0243  0.0205  172 LYS A CA  
1398 C  C   . LYS A 173 ? 0.1383 0.1054 0.0946 0.0146  0.0234  0.0204  172 LYS A C   
1399 O  O   . LYS A 173 ? 0.1250 0.1043 0.0925 0.0137  0.0261  0.0185  172 LYS A O   
1400 C  CB  . LYS A 173 ? 0.1546 0.1350 0.1339 0.0101  0.0233  0.0073  172 LYS A CB  
1401 C  CG  . LYS A 173 ? 0.1721 0.1751 0.1640 0.0176  0.0238  0.0046  172 LYS A CG  
1402 C  CD  . LYS A 173 ? 0.2093 0.2198 0.2045 0.0198  0.0227  -0.0026 172 LYS A CD  
1403 C  CE  . LYS A 173 ? 0.2339 0.2486 0.2266 0.0295  0.0301  -0.0099 172 LYS A CE  
1404 N  NZ  . LYS A 173 ? 0.2482 0.2790 0.2702 0.0343  0.0435  -0.0185 172 LYS A NZ  
1405 N  N   . SER A 174 ? 0.1440 0.1282 0.0945 0.0215  0.0246  0.0323  173 SER A N   
1406 C  CA  . SER A 174 ? 0.1506 0.1343 0.0850 0.0300  0.0209  0.0221  173 SER A CA  
1407 C  C   . SER A 174 ? 0.1551 0.1472 0.0835 0.0426  0.0132  0.0195  173 SER A C   
1408 O  O   . SER A 174 ? 0.1728 0.1586 0.0884 0.0449  0.0103  0.0241  173 SER A O   
1409 C  CB  . SER A 174 ? 0.1639 0.1481 0.1046 0.0308  0.0213  0.0105  173 SER A CB  
1410 O  OG  . SER A 174 ? 0.1851 0.1494 0.1301 0.0280  0.0159  0.0125  173 SER A OG  
1411 N  N   . ALA A 175 ? 0.1554 0.1555 0.0758 0.0487  0.0125  0.0187  174 ALA A N   
1412 C  CA  . ALA A 175 ? 0.1609 0.1576 0.0796 0.0490  0.0045  0.0124  174 ALA A CA  
1413 C  C   . ALA A 175 ? 0.1570 0.1485 0.0820 0.0450  -0.0011 0.0163  174 ALA A C   
1414 O  O   . ALA A 175 ? 0.1403 0.1341 0.0766 0.0472  0.0088  0.0225  174 ALA A O   
1415 C  CB  . ALA A 175 ? 0.1662 0.1646 0.0845 0.0474  0.0013  0.0059  174 ALA A CB  
1416 N  N   . ASP A 176 ? 0.1605 0.1780 0.0912 0.0519  -0.0052 0.0176  175 ASP A N   
1417 C  CA  . ASP A 176 ? 0.1664 0.1892 0.1086 0.0499  -0.0128 0.0093  175 ASP A CA  
1418 C  C   . ASP A 176 ? 0.1479 0.1661 0.1272 0.0397  -0.0118 -0.0054 175 ASP A C   
1419 O  O   . ASP A 176 ? 0.1623 0.1934 0.1551 0.0289  -0.0099 -0.0264 175 ASP A O   
1420 C  CB  . ASP A 176 ? 0.1952 0.2291 0.1359 0.0495  -0.0233 0.0184  175 ASP A CB  
1421 C  CG  . ASP A 176 ? 0.2583 0.2798 0.1804 0.0213  -0.0265 0.0148  175 ASP A CG  
1422 O  OD1 . ASP A 176 ? 0.2980 0.3367 0.2357 0.0036  -0.0572 0.0024  175 ASP A OD1 
1423 O  OD2 . ASP A 176 ? 0.3173 0.3360 0.2110 -0.0038 -0.0339 0.0130  175 ASP A OD2 
1424 N  N   . PHE A 177 ? 0.1270 0.1321 0.1195 0.0276  -0.0030 -0.0029 176 PHE A N   
1425 C  CA  . PHE A 177 ? 0.1270 0.1161 0.1208 0.0215  -0.0042 -0.0064 176 PHE A CA  
1426 C  C   . PHE A 177 ? 0.1263 0.1117 0.1123 0.0273  -0.0036 0.0056  176 PHE A C   
1427 O  O   . PHE A 177 ? 0.1393 0.1607 0.1282 0.0566  -0.0264 -0.0124 176 PHE A O   
1428 C  CB  . PHE A 177 ? 0.1323 0.1072 0.1364 0.0153  -0.0054 -0.0098 176 PHE A CB  
1429 C  CG  . PHE A 177 ? 0.1436 0.1012 0.1395 0.0082  -0.0032 -0.0147 176 PHE A CG  
1430 C  CD1 . PHE A 177 ? 0.1591 0.0994 0.1452 0.0018  0.0106  -0.0155 176 PHE A CD1 
1431 C  CD2 . PHE A 177 ? 0.1435 0.1049 0.1341 0.0048  -0.0137 -0.0186 176 PHE A CD2 
1432 C  CE1 . PHE A 177 ? 0.1713 0.1112 0.1459 -0.0034 0.0077  -0.0119 176 PHE A CE1 
1433 C  CE2 . PHE A 177 ? 0.1494 0.1133 0.1439 0.0084  -0.0036 -0.0126 176 PHE A CE2 
1434 C  CZ  . PHE A 177 ? 0.1607 0.1169 0.1418 -0.0028 0.0051  -0.0091 176 PHE A CZ  
1435 N  N   . THR A 178 ? 0.1303 0.1056 0.1027 0.0291  -0.0028 0.0197  177 THR A N   
1436 C  CA  . THR A 178 ? 0.1277 0.0944 0.1068 0.0224  -0.0068 0.0314  177 THR A CA  
1437 C  C   . THR A 178 ? 0.1278 0.0877 0.1112 0.0088  -0.0149 0.0279  177 THR A C   
1438 O  O   . THR A 178 ? 0.1502 0.0871 0.1187 0.0007  -0.0204 0.0279  177 THR A O   
1439 C  CB  . THR A 178 ? 0.1355 0.1157 0.1235 0.0301  -0.0102 0.0409  177 THR A CB  
1440 O  OG1 . THR A 178 ? 0.1936 0.1533 0.1224 0.0438  -0.0019 0.0394  177 THR A OG1 
1441 C  CG2 . THR A 178 ? 0.1512 0.1402 0.1510 0.0221  0.0030  0.0444  177 THR A CG2 
1442 N  N   . ASN A 179 ? 0.1175 0.0844 0.1099 -0.0009 -0.0150 0.0239  178 ASN A N   
1443 C  CA  . ASN A 179 ? 0.1216 0.1039 0.1158 -0.0063 -0.0137 0.0273  178 ASN A CA  
1444 C  C   . ASN A 179 ? 0.1248 0.1044 0.1141 -0.0131 -0.0116 0.0304  178 ASN A C   
1445 O  O   . ASN A 179 ? 0.1521 0.1328 0.1709 -0.0266 -0.0254 0.0629  178 ASN A O   
1446 C  CB  . ASN A 179 ? 0.1200 0.1092 0.1193 -0.0056 -0.0135 0.0276  178 ASN A CB  
1447 C  CG  . ASN A 179 ? 0.1350 0.1102 0.1363 0.0050  -0.0158 0.0242  178 ASN A CG  
1448 O  OD1 . ASN A 179 ? 0.1518 0.1261 0.1680 0.0134  -0.0007 0.0241  178 ASN A OD1 
1449 N  ND2 . ASN A 179 ? 0.1493 0.1082 0.1300 0.0144  -0.0268 0.0402  178 ASN A ND2 
1450 N  N   . PHE A 180 ? 0.1297 0.0857 0.1018 -0.0063 -0.0093 0.0306  179 PHE A N   
1451 C  CA  . PHE A 180 ? 0.1278 0.0914 0.0936 -0.0084 -0.0021 0.0311  179 PHE A CA  
1452 C  C   . PHE A 180 ? 0.1251 0.0902 0.0962 -0.0073 -0.0032 0.0282  179 PHE A C   
1453 O  O   . PHE A 180 ? 0.1505 0.0959 0.0975 -0.0124 -0.0081 0.0205  179 PHE A O   
1454 C  CB  . PHE A 180 ? 0.1279 0.0909 0.0927 -0.0051 0.0008  0.0290  179 PHE A CB  
1455 C  CG  . PHE A 180 ? 0.1270 0.0897 0.1015 0.0012  0.0016  0.0272  179 PHE A CG  
1456 C  CD1 . PHE A 180 ? 0.1443 0.0949 0.1111 -0.0020 0.0003  0.0256  179 PHE A CD1 
1457 C  CD2 . PHE A 180 ? 0.1131 0.0862 0.0981 0.0019  0.0047  0.0257  179 PHE A CD2 
1458 C  CE1 . PHE A 180 ? 0.1400 0.0858 0.1164 0.0016  -0.0028 0.0231  179 PHE A CE1 
1459 C  CE2 . PHE A 180 ? 0.1154 0.0879 0.1006 0.0027  0.0028  0.0273  179 PHE A CE2 
1460 C  CZ  . PHE A 180 ? 0.1275 0.0857 0.1090 0.0012  0.0011  0.0278  179 PHE A CZ  
1461 N  N   . ASP A 181 ? 0.1219 0.0915 0.1085 -0.0075 -0.0020 0.0187  180 ASP A N   
1462 C  CA  . ASP A 181 ? 0.1178 0.0984 0.1141 -0.0003 0.0001  0.0167  180 ASP A CA  
1463 C  C   . ASP A 181 ? 0.1145 0.0867 0.1096 0.0006  0.0065  0.0172  180 ASP A C   
1464 O  O   . ASP A 181 ? 0.1207 0.0884 0.1099 0.0012  0.0130  0.0105  180 ASP A O   
1465 C  CB  . ASP A 181 ? 0.1183 0.1199 0.1326 0.0049  0.0002  0.0165  180 ASP A CB  
1466 C  CG  . ASP A 181 ? 0.1184 0.1454 0.1512 0.0080  0.0058  0.0201  180 ASP A CG  
1467 O  OD1 . ASP A 181 ? 0.1269 0.1286 0.1526 0.0296  0.0163  0.0143  180 ASP A OD1 
1468 O  OD2 . ASP A 181 ? 0.1359 0.2454 0.2000 -0.0006 0.0135  0.0066  180 ASP A OD2 
1469 N  N   . PRO A 182 ? 0.1131 0.0878 0.0997 0.0003  0.0077  0.0160  181 PRO A N   
1470 C  CA  . PRO A 182 ? 0.1074 0.1028 0.1027 0.0015  0.0075  0.0194  181 PRO A CA  
1471 C  C   . PRO A 182 ? 0.0980 0.1055 0.1036 0.0046  0.0072  0.0206  181 PRO A C   
1472 O  O   . PRO A 182 ? 0.0963 0.0986 0.1092 0.0000  0.0015  0.0248  181 PRO A O   
1473 C  CB  . PRO A 182 ? 0.1116 0.1096 0.1054 -0.0021 0.0085  0.0160  181 PRO A CB  
1474 C  CG  . PRO A 182 ? 0.1184 0.1041 0.1029 -0.0071 0.0056  0.0137  181 PRO A CG  
1475 C  CD  . PRO A 182 ? 0.1151 0.0929 0.1033 -0.0047 0.0056  0.0154  181 PRO A CD  
1476 N  N   . ARG A 183 ? 0.0947 0.1025 0.1074 0.0039  0.0113  0.0262  182 ARG A N   
1477 C  CA  . ARG A 183 ? 0.1020 0.1092 0.1165 0.0000  0.0165  0.0265  182 ARG A CA  
1478 C  C   . ARG A 183 ? 0.1040 0.1092 0.1156 -0.0075 0.0122  0.0245  182 ARG A C   
1479 O  O   . ARG A 183 ? 0.1086 0.1212 0.1176 -0.0119 0.0236  0.0284  182 ARG A O   
1480 C  CB  . ARG A 183 ? 0.1165 0.1133 0.1308 0.0079  0.0227  0.0262  182 ARG A CB  
1481 C  CG  . ARG A 183 ? 0.1333 0.1237 0.1447 0.0140  0.0345  0.0220  182 ARG A CG  
1482 C  CD  . ARG A 183 ? 0.1516 0.1466 0.1698 0.0253  0.0516  0.0233  182 ARG A CD  
1483 N  NE  . ARG A 183 ? 0.1597 0.1644 0.1859 0.0377  0.0581  0.0279  182 ARG A NE  
1484 C  CZ  . ARG A 183 ? 0.1632 0.2030 0.2173 0.0481  0.0661  0.0383  182 ARG A CZ  
1485 N  NH1 . ARG A 183 ? 0.1901 0.2200 0.2510 0.0585  0.0653  0.0270  182 ARG A NH1 
1486 N  NH2 . ARG A 183 ? 0.1774 0.2376 0.2444 0.0622  0.0564  0.0407  182 ARG A NH2 
1487 N  N   . GLY A 184 ? 0.1106 0.1005 0.1154 -0.0081 0.0003  0.0213  183 GLY A N   
1488 C  CA  . GLY A 184 ? 0.1223 0.0984 0.1321 -0.0065 -0.0042 0.0148  183 GLY A CA  
1489 C  C   . GLY A 184 ? 0.1302 0.0970 0.1328 -0.0028 -0.0089 0.0158  183 GLY A C   
1490 O  O   . GLY A 184 ? 0.1460 0.1021 0.1596 -0.0022 -0.0167 0.0114  183 GLY A O   
1491 N  N   . LEU A 185 ? 0.1187 0.0988 0.1261 -0.0026 -0.0126 0.0208  184 LEU A N   
1492 C  CA  . LEU A 185 ? 0.1152 0.1027 0.1217 0.0000  -0.0105 0.0237  184 LEU A CA  
1493 C  C   . LEU A 185 ? 0.1056 0.1063 0.1228 -0.0101 -0.0081 0.0290  184 LEU A C   
1494 O  O   . LEU A 185 ? 0.1157 0.1243 0.1395 0.0012  -0.0034 0.0473  184 LEU A O   
1495 C  CB  . LEU A 185 ? 0.1173 0.1177 0.1117 0.0045  -0.0111 0.0262  184 LEU A CB  
1496 C  CG  . LEU A 185 ? 0.1350 0.1320 0.1187 0.0094  -0.0071 0.0248  184 LEU A CG  
1497 C  CD1 . LEU A 185 ? 0.1376 0.1486 0.1282 0.0099  -0.0041 0.0285  184 LEU A CD1 
1498 C  CD2 . LEU A 185 ? 0.1578 0.1459 0.1246 0.0138  0.0009  0.0140  184 LEU A CD2 
1499 N  N   . LEU A 186 ? 0.1034 0.1168 0.1117 -0.0083 -0.0093 0.0254  185 LEU A N   
1500 C  CA  . LEU A 186 ? 0.1132 0.1260 0.1130 -0.0195 -0.0088 0.0284  185 LEU A CA  
1501 C  C   . LEU A 186 ? 0.1287 0.1333 0.1164 -0.0329 -0.0128 0.0300  185 LEU A C   
1502 O  O   . LEU A 186 ? 0.1813 0.1784 0.1417 -0.0647 -0.0389 0.0507  185 LEU A O   
1503 C  CB  . LEU A 186 ? 0.1082 0.1303 0.1136 -0.0133 -0.0072 0.0247  185 LEU A CB  
1504 C  CG  . LEU A 186 ? 0.1081 0.1303 0.1196 -0.0044 -0.0081 0.0213  185 LEU A CG  
1505 C  CD1 . LEU A 186 ? 0.1125 0.1419 0.1143 0.0014  -0.0034 0.0225  185 LEU A CD1 
1506 C  CD2 . LEU A 186 ? 0.1180 0.1319 0.1417 -0.0096 -0.0153 0.0202  185 LEU A CD2 
1507 N  N   . PRO A 187 ? 0.1160 0.1140 0.1154 -0.0220 -0.0048 0.0286  186 PRO A N   
1508 C  CA  . PRO A 187 ? 0.1177 0.1138 0.1268 -0.0170 -0.0050 0.0285  186 PRO A CA  
1509 C  C   . PRO A 187 ? 0.1022 0.1051 0.1369 -0.0256 -0.0169 0.0306  186 PRO A C   
1510 O  O   . PRO A 187 ? 0.0946 0.1024 0.1667 -0.0070 -0.0205 0.0436  186 PRO A O   
1511 C  CB  . PRO A 187 ? 0.1102 0.1162 0.1243 -0.0080 0.0030  0.0256  186 PRO A CB  
1512 C  CG  . PRO A 187 ? 0.1050 0.1106 0.1120 -0.0038 0.0018  0.0233  186 PRO A CG  
1513 C  CD  . PRO A 187 ? 0.1071 0.1085 0.1087 -0.0100 0.0015  0.0207  186 PRO A CD  
1514 N  N   . GLU A 188 ? 0.1112 0.1191 0.1456 -0.0317 -0.0110 0.0300  187 GLU A N   
1515 C  CA  . GLU A 188 ? 0.1025 0.1304 0.1558 -0.0260 -0.0149 0.0220  187 GLU A CA  
1516 C  C   . GLU A 188 ? 0.0884 0.1239 0.1469 -0.0152 -0.0045 0.0226  187 GLU A C   
1517 O  O   . GLU A 188 ? 0.1016 0.1452 0.1568 0.0044  0.0077  0.0155  187 GLU A O   
1518 C  CB  . GLU A 188 ? 0.1403 0.1597 0.1858 -0.0420 -0.0212 0.0222  187 GLU A CB  
1519 C  CG  . GLU A 188 ? 0.1845 0.2057 0.2264 -0.0271 -0.0089 0.0185  187 GLU A CG  
1520 C  CD  . GLU A 188 ? 0.1984 0.2283 0.2633 -0.0290 0.0029  0.0189  187 GLU A CD  
1521 O  OE1 . GLU A 188 ? 0.1864 0.2251 0.3180 -0.0550 -0.0032 -0.0097 187 GLU A OE1 
1522 O  OE2 . GLU A 188 ? 0.2581 0.2694 0.3031 -0.0324 0.0248  0.0482  187 GLU A OE2 
1523 N  N   . SER A 189 ? 0.0755 0.1216 0.1262 -0.0192 -0.0016 0.0170  188 SER A N   
1524 C  CA  . SER A 189 ? 0.0820 0.1306 0.1301 -0.0212 0.0010  0.0166  188 SER A CA  
1525 C  C   . SER A 189 ? 0.0762 0.1312 0.1322 -0.0213 0.0001  0.0054  188 SER A C   
1526 O  O   . SER A 189 ? 0.0795 0.1440 0.1316 -0.0246 0.0044  -0.0061 188 SER A O   
1527 C  CB  . SER A 189 ? 0.0977 0.1393 0.1351 -0.0216 0.0014  0.0250  188 SER A CB  
1528 O  OG  . SER A 189 ? 0.1123 0.1503 0.1348 -0.0260 0.0030  0.0225  188 SER A OG  
1529 N  N   . LEU A 190 ? 0.0855 0.1196 0.1405 -0.0195 0.0024  0.0034  189 LEU A N   
1530 C  CA  . LEU A 190 ? 0.0940 0.1310 0.1452 -0.0205 -0.0024 0.0031  189 LEU A CA  
1531 C  C   . LEU A 190 ? 0.0913 0.1361 0.1295 -0.0250 0.0061  -0.0018 189 LEU A C   
1532 O  O   . LEU A 190 ? 0.1309 0.1500 0.1562 -0.0396 -0.0091 -0.0032 189 LEU A O   
1533 C  CB  . LEU A 190 ? 0.1055 0.1398 0.1710 -0.0174 -0.0049 0.0077  189 LEU A CB  
1534 C  CG  . LEU A 190 ? 0.1055 0.1448 0.1875 -0.0085 -0.0121 0.0155  189 LEU A CG  
1535 C  CD1 . LEU A 190 ? 0.1293 0.1408 0.2077 -0.0067 -0.0123 0.0189  189 LEU A CD1 
1536 C  CD2 . LEU A 190 ? 0.1149 0.1685 0.1930 -0.0084 -0.0141 0.0243  189 LEU A CD2 
1537 N  N   . ASP A 191 ? 0.0791 0.1438 0.1095 -0.0213 0.0149  -0.0046 190 ASP A N   
1538 C  CA  . ASP A 191 ? 0.0894 0.1481 0.1001 -0.0256 0.0156  -0.0044 190 ASP A CA  
1539 C  C   . ASP A 191 ? 0.0821 0.1256 0.0897 -0.0198 0.0116  -0.0012 190 ASP A C   
1540 O  O   . ASP A 191 ? 0.0733 0.1251 0.0894 -0.0222 0.0118  -0.0030 190 ASP A O   
1541 C  CB  . ASP A 191 ? 0.1052 0.1739 0.1179 -0.0381 0.0121  0.0006  190 ASP A CB  
1542 C  CG  . ASP A 191 ? 0.1335 0.2083 0.1508 -0.0440 0.0210  0.0012  190 ASP A CG  
1543 O  OD1 . ASP A 191 ? 0.1382 0.2693 0.1685 -0.0349 0.0394  -0.0191 190 ASP A OD1 
1544 O  OD2 . ASP A 191 ? 0.1696 0.2566 0.2021 -0.0616 0.0286  0.0308  190 ASP A OD2 
1545 N  N   . TYR A 192 ? 0.0758 0.1096 0.0763 -0.0170 0.0159  0.0016  191 TYR A N   
1546 C  CA  . TYR A 192 ? 0.0782 0.1025 0.0763 -0.0177 0.0127  0.0037  191 TYR A CA  
1547 C  C   . TYR A 192 ? 0.0799 0.0922 0.0657 -0.0107 0.0134  0.0056  191 TYR A C   
1548 O  O   . TYR A 192 ? 0.0814 0.1075 0.0672 -0.0060 0.0162  0.0031  191 TYR A O   
1549 C  CB  . TYR A 192 ? 0.0880 0.1076 0.0885 -0.0186 0.0085  0.0105  191 TYR A CB  
1550 C  CG  . TYR A 192 ? 0.0914 0.0991 0.0887 -0.0252 0.0056  0.0166  191 TYR A CG  
1551 C  CD1 . TYR A 192 ? 0.0971 0.1044 0.1013 -0.0245 0.0013  0.0104  191 TYR A CD1 
1552 C  CD2 . TYR A 192 ? 0.1008 0.1010 0.0931 -0.0184 0.0031  0.0174  191 TYR A CD2 
1553 C  CE1 . TYR A 192 ? 0.1072 0.1044 0.1039 -0.0251 -0.0023 0.0147  191 TYR A CE1 
1554 C  CE2 . TYR A 192 ? 0.1066 0.1051 0.1023 -0.0155 0.0018  0.0175  191 TYR A CE2 
1555 C  CZ  . TYR A 192 ? 0.1154 0.1054 0.1060 -0.0160 -0.0002 0.0182  191 TYR A CZ  
1556 O  OH  . TYR A 192 ? 0.1403 0.1210 0.1146 -0.0072 -0.0005 0.0124  191 TYR A OH  
1557 N  N   . TRP A 193 ? 0.0794 0.0809 0.0643 -0.0082 0.0124  0.0031  192 TRP A N   
1558 C  CA  . TRP A 193 ? 0.0812 0.0781 0.0608 -0.0094 0.0185  0.0071  192 TRP A CA  
1559 C  C   . TRP A 193 ? 0.0800 0.0774 0.0595 -0.0128 0.0194  0.0048  192 TRP A C   
1560 O  O   . TRP A 193 ? 0.1004 0.0925 0.0631 -0.0201 0.0190  0.0063  192 TRP A O   
1561 C  CB  . TRP A 193 ? 0.0845 0.0823 0.0697 -0.0057 0.0189  0.0061  192 TRP A CB  
1562 C  CG  . TRP A 193 ? 0.0867 0.0794 0.0742 0.0003  0.0192  0.0109  192 TRP A CG  
1563 C  CD1 . TRP A 193 ? 0.0961 0.0848 0.0790 0.0030  0.0187  0.0130  192 TRP A CD1 
1564 C  CD2 . TRP A 193 ? 0.0871 0.0874 0.0825 0.0019  0.0161  0.0099  192 TRP A CD2 
1565 N  NE1 . TRP A 193 ? 0.1093 0.0860 0.0868 0.0030  0.0177  0.0208  192 TRP A NE1 
1566 C  CE2 . TRP A 193 ? 0.1031 0.0807 0.0946 0.0049  0.0145  0.0098  192 TRP A CE2 
1567 C  CE3 . TRP A 193 ? 0.0867 0.0942 0.0919 0.0024  0.0133  0.0051  192 TRP A CE3 
1568 C  CZ2 . TRP A 193 ? 0.1085 0.0823 0.1106 0.0014  0.0099  0.0102  192 TRP A CZ2 
1569 C  CZ3 . TRP A 193 ? 0.0941 0.1030 0.1082 0.0060  0.0125  -0.0040 192 TRP A CZ3 
1570 C  CH2 . TRP A 193 ? 0.1010 0.1024 0.1193 0.0040  0.0073  -0.0036 192 TRP A CH2 
1571 N  N   . THR A 194 ? 0.0750 0.0747 0.0547 -0.0118 0.0193  0.0039  193 THR A N   
1572 C  CA  . THR A 194 ? 0.0768 0.0755 0.0606 -0.0071 0.0184  0.0035  193 THR A CA  
1573 C  C   . THR A 194 ? 0.0799 0.0799 0.0602 -0.0051 0.0174  0.0003  193 THR A C   
1574 O  O   . THR A 194 ? 0.0893 0.0954 0.0627 -0.0127 0.0170  0.0008  193 THR A O   
1575 C  CB  . THR A 194 ? 0.0762 0.0818 0.0707 -0.0027 0.0156  -0.0011 193 THR A CB  
1576 O  OG1 . THR A 194 ? 0.0750 0.0777 0.0823 -0.0001 0.0134  -0.0038 193 THR A OG1 
1577 C  CG2 . THR A 194 ? 0.0812 0.0862 0.0768 -0.0012 0.0158  -0.0001 193 THR A CG2 
1578 N  N   . TYR A 195 ? 0.0785 0.0752 0.0575 -0.0048 0.0134  -0.0007 194 TYR A N   
1579 C  CA  . TYR A 195 ? 0.0763 0.0756 0.0582 -0.0027 0.0134  -0.0001 194 TYR A CA  
1580 C  C   . TYR A 195 ? 0.0738 0.0725 0.0577 -0.0017 0.0143  -0.0058 194 TYR A C   
1581 O  O   . TYR A 195 ? 0.0739 0.0769 0.0535 -0.0037 0.0113  -0.0072 194 TYR A O   
1582 C  CB  . TYR A 195 ? 0.0762 0.0697 0.0566 -0.0029 0.0125  -0.0009 194 TYR A CB  
1583 C  CG  . TYR A 195 ? 0.0786 0.0643 0.0599 -0.0015 0.0137  -0.0028 194 TYR A CG  
1584 C  CD1 . TYR A 195 ? 0.0774 0.0608 0.0573 0.0030  0.0141  -0.0011 194 TYR A CD1 
1585 C  CD2 . TYR A 195 ? 0.0785 0.0650 0.0563 0.0002  0.0125  -0.0027 194 TYR A CD2 
1586 C  CE1 . TYR A 195 ? 0.0762 0.0561 0.0591 0.0020  0.0116  -0.0051 194 TYR A CE1 
1587 C  CE2 . TYR A 195 ? 0.0776 0.0618 0.0573 -0.0008 0.0130  -0.0026 194 TYR A CE2 
1588 C  CZ  . TYR A 195 ? 0.0774 0.0570 0.0602 0.0022  0.0132  -0.0044 194 TYR A CZ  
1589 O  OH  . TYR A 195 ? 0.0806 0.0565 0.0615 0.0022  0.0166  -0.0038 194 TYR A OH  
1590 N  N   . PRO A 196 ? 0.0749 0.0778 0.0660 -0.0009 0.0145  -0.0140 195 PRO A N   
1591 C  CA  . PRO A 196 ? 0.0737 0.0788 0.0694 0.0000  0.0150  -0.0138 195 PRO A CA  
1592 C  C   . PRO A 196 ? 0.0695 0.0705 0.0637 0.0011  0.0104  -0.0115 195 PRO A C   
1593 O  O   . PRO A 196 ? 0.0739 0.0856 0.0642 0.0122  0.0114  -0.0041 195 PRO A O   
1594 C  CB  . PRO A 196 ? 0.0800 0.0897 0.0755 -0.0036 0.0148  -0.0162 195 PRO A CB  
1595 C  CG  . PRO A 196 ? 0.0858 0.0948 0.0732 -0.0040 0.0145  -0.0190 195 PRO A CG  
1596 C  CD  . PRO A 196 ? 0.0886 0.0961 0.0736 -0.0040 0.0148  -0.0134 195 PRO A CD  
1597 N  N   . GLY A 197 ? 0.0650 0.0644 0.0657 0.0008  0.0125  -0.0077 196 GLY A N   
1598 C  CA  . GLY A 197 ? 0.0634 0.0617 0.0693 -0.0016 0.0131  -0.0066 196 GLY A CA  
1599 C  C   . GLY A 197 ? 0.0617 0.0563 0.0711 -0.0030 0.0133  -0.0054 196 GLY A C   
1600 O  O   . GLY A 197 ? 0.0684 0.0561 0.0748 -0.0047 0.0125  -0.0082 196 GLY A O   
1601 N  N   . SER A 198 ? 0.0672 0.0556 0.0706 -0.0037 0.0125  -0.0041 197 SER A N   
1602 C  CA  . SER A 198 ? 0.0655 0.0544 0.0707 -0.0018 0.0141  -0.0034 197 SER A CA  
1603 C  C   . SER A 198 ? 0.0619 0.0533 0.0730 -0.0025 0.0151  -0.0042 197 SER A C   
1604 O  O   . SER A 198 ? 0.0610 0.0527 0.0717 -0.0025 0.0136  -0.0051 197 SER A O   
1605 C  CB  . SER A 198 ? 0.0671 0.0573 0.0687 -0.0021 0.0175  -0.0068 197 SER A CB  
1606 O  OG  . SER A 198 ? 0.0670 0.0604 0.0741 0.0005  0.0179  -0.0089 197 SER A OG  
1607 N  N   . LEU A 199 ? 0.0694 0.0578 0.0710 0.0006  0.0155  -0.0056 198 LEU A N   
1608 C  CA  . LEU A 199 ? 0.0750 0.0669 0.0726 0.0000  0.0157  -0.0047 198 LEU A CA  
1609 C  C   . LEU A 199 ? 0.0727 0.0647 0.0771 -0.0010 0.0091  -0.0063 198 LEU A C   
1610 O  O   . LEU A 199 ? 0.0649 0.0741 0.0729 0.0027  0.0106  -0.0074 198 LEU A O   
1611 C  CB  . LEU A 199 ? 0.0910 0.0774 0.0778 0.0001  0.0184  0.0020  198 LEU A CB  
1612 C  CG  . LEU A 199 ? 0.1136 0.0882 0.0979 0.0024  0.0211  0.0075  198 LEU A CG  
1613 C  CD1 . LEU A 199 ? 0.1281 0.0939 0.1087 -0.0015 0.0206  0.0105  198 LEU A CD1 
1614 C  CD2 . LEU A 199 ? 0.1180 0.1008 0.1083 0.0118  0.0295  0.0170  198 LEU A CD2 
1615 N  N   . THR A 200 ? 0.0702 0.0614 0.0797 0.0064  0.0040  -0.0108 199 THR A N   
1616 C  CA  . THR A 200 ? 0.0699 0.0608 0.0793 0.0026  0.0020  -0.0079 199 THR A CA  
1617 C  C   . THR A 200 ? 0.0694 0.0630 0.0857 0.0038  0.0044  -0.0086 199 THR A C   
1618 O  O   . THR A 200 ? 0.0687 0.0636 0.0929 0.0046  0.0117  -0.0071 199 THR A O   
1619 C  CB  . THR A 200 ? 0.0754 0.0614 0.0707 -0.0020 0.0068  -0.0084 199 THR A CB  
1620 O  OG1 . THR A 200 ? 0.0809 0.0710 0.0718 -0.0084 0.0014  -0.0040 199 THR A OG1 
1621 C  CG2 . THR A 200 ? 0.0832 0.0688 0.0732 -0.0045 0.0097  -0.0062 199 THR A CG2 
1622 N  N   . THR A 201 ? 0.0919 0.0744 0.0933 0.0049  0.0136  -0.0061 200 THR A N   
1623 C  CA  . THR A 201 ? 0.1131 0.0874 0.1007 0.0033  0.0180  -0.0078 200 THR A CA  
1624 C  C   . THR A 201 ? 0.1137 0.0880 0.0977 -0.0006 0.0228  -0.0030 200 THR A C   
1625 O  O   . THR A 201 ? 0.1153 0.0802 0.0989 -0.0108 0.0274  -0.0039 200 THR A O   
1626 C  CB  . THR A 201 ? 0.1368 0.1103 0.1135 0.0021  0.0138  0.0001  200 THR A CB  
1627 O  OG1 . THR A 201 ? 0.1822 0.1288 0.1361 0.0135  -0.0062 -0.0051 200 THR A OG1 
1628 C  CG2 . THR A 201 ? 0.1660 0.1267 0.1240 -0.0029 0.0062  -0.0049 200 THR A CG2 
1629 N  N   . PRO A 202 ? 0.1180 0.1011 0.0963 0.0029  0.0279  -0.0105 201 PRO A N   
1630 C  CA  . PRO A 202 ? 0.1226 0.1103 0.1037 -0.0014 0.0283  -0.0073 201 PRO A CA  
1631 C  C   . PRO A 202 ? 0.1381 0.1156 0.1114 -0.0049 0.0312  0.0027  201 PRO A C   
1632 O  O   . PRO A 202 ? 0.1617 0.1313 0.1221 -0.0001 0.0254  0.0027  201 PRO A O   
1633 C  CB  . PRO A 202 ? 0.1194 0.1280 0.1146 -0.0003 0.0300  -0.0093 201 PRO A CB  
1634 C  CG  . PRO A 202 ? 0.1228 0.1262 0.1061 0.0041  0.0274  -0.0131 201 PRO A CG  
1635 C  CD  . PRO A 202 ? 0.1208 0.1040 0.0953 0.0053  0.0243  -0.0126 201 PRO A CD  
1636 N  N   . PRO A 203 ? 0.1342 0.1106 0.1139 -0.0041 0.0367  0.0095  202 PRO A N   
1637 C  CA  . PRO A 203 ? 0.1262 0.1070 0.1180 -0.0116 0.0363  0.0047  202 PRO A CA  
1638 C  C   . PRO A 203 ? 0.1025 0.0884 0.1081 -0.0120 0.0313  -0.0061 202 PRO A C   
1639 O  O   . PRO A 203 ? 0.1027 0.0964 0.1284 -0.0222 0.0256  -0.0065 202 PRO A O   
1640 C  CB  . PRO A 203 ? 0.1370 0.1129 0.1275 -0.0138 0.0358  0.0085  202 PRO A CB  
1641 C  CG  . PRO A 203 ? 0.1466 0.1186 0.1327 -0.0086 0.0298  0.0130  202 PRO A CG  
1642 C  CD  . PRO A 203 ? 0.1448 0.1149 0.1252 -0.0073 0.0321  0.0190  202 PRO A CD  
1643 N  N   . LEU A 204 ? 0.0850 0.0834 0.1000 -0.0105 0.0259  -0.0111 203 LEU A N   
1644 C  CA  . LEU A 204 ? 0.0723 0.0701 0.0928 -0.0074 0.0225  -0.0130 203 LEU A CA  
1645 C  C   . LEU A 204 ? 0.0729 0.0690 0.0941 -0.0049 0.0238  -0.0133 203 LEU A C   
1646 O  O   . LEU A 204 ? 0.0822 0.0708 0.0951 -0.0106 0.0184  -0.0161 203 LEU A O   
1647 C  CB  . LEU A 204 ? 0.0712 0.0815 0.0917 -0.0030 0.0219  -0.0141 203 LEU A CB  
1648 C  CG  . LEU A 204 ? 0.0711 0.0871 0.0949 -0.0027 0.0225  -0.0157 203 LEU A CG  
1649 C  CD1 . LEU A 204 ? 0.0726 0.0939 0.1052 -0.0049 0.0201  -0.0175 203 LEU A CD1 
1650 C  CD2 . LEU A 204 ? 0.0742 0.0889 0.1014 -0.0005 0.0197  -0.0148 203 LEU A CD2 
1651 N  N   . LEU A 205 ? 0.0797 0.0644 0.0987 -0.0050 0.0238  -0.0132 204 LEU A N   
1652 C  CA  . LEU A 205 ? 0.0851 0.0656 0.1121 -0.0060 0.0278  -0.0099 204 LEU A CA  
1653 C  C   . LEU A 205 ? 0.0796 0.0617 0.1032 -0.0069 0.0215  -0.0088 204 LEU A C   
1654 O  O   . LEU A 205 ? 0.0749 0.0653 0.1001 -0.0080 0.0155  -0.0099 204 LEU A O   
1655 C  CB  . LEU A 205 ? 0.0960 0.0712 0.1287 -0.0061 0.0338  0.0002  204 LEU A CB  
1656 C  CG  . LEU A 205 ? 0.1139 0.0784 0.1418 -0.0064 0.0423  0.0128  204 LEU A CG  
1657 C  CD1 . LEU A 205 ? 0.1231 0.0886 0.1487 -0.0030 0.0506  0.0193  204 LEU A CD1 
1658 C  CD2 . LEU A 205 ? 0.1221 0.0995 0.1654 -0.0154 0.0431  0.0214  204 LEU A CD2 
1659 N  N   . GLU A 206 ? 0.0755 0.0680 0.1027 -0.0165 0.0144  -0.0152 205 GLU A N   
1660 C  CA  . GLU A 206 ? 0.0818 0.0707 0.0957 -0.0084 0.0062  -0.0157 205 GLU A CA  
1661 C  C   . GLU A 206 ? 0.0815 0.0708 0.0924 -0.0070 0.0066  -0.0177 205 GLU A C   
1662 O  O   . GLU A 206 ? 0.0992 0.0946 0.0974 0.0052  0.0021  -0.0285 205 GLU A O   
1663 C  CB  . GLU A 206 ? 0.0906 0.0773 0.0999 -0.0031 0.0004  -0.0182 205 GLU A CB  
1664 C  CG  . GLU A 206 ? 0.0900 0.0828 0.1040 -0.0016 0.0010  -0.0232 205 GLU A CG  
1665 C  CD  . GLU A 206 ? 0.0910 0.0964 0.1127 -0.0020 0.0001  -0.0233 205 GLU A CD  
1666 O  OE1 . GLU A 206 ? 0.1147 0.1145 0.1396 0.0020  -0.0051 -0.0371 205 GLU A OE1 
1667 O  OE2 . GLU A 206 ? 0.0990 0.1006 0.1089 -0.0034 -0.0070 -0.0187 205 GLU A OE2 
1668 N  N   . CYS A 207 ? 0.0796 0.0573 0.0829 -0.0089 0.0080  -0.0162 206 CYS A N   
1669 C  CA  . CYS A 207 ? 0.0832 0.0594 0.0867 -0.0066 0.0081  -0.0097 206 CYS A CA  
1670 C  C   . CYS A 207 ? 0.0793 0.0533 0.0883 -0.0019 0.0084  -0.0085 206 CYS A C   
1671 O  O   . CYS A 207 ? 0.0933 0.0606 0.1114 -0.0005 -0.0038 -0.0068 206 CYS A O   
1672 C  CB  . CYS A 207 ? 0.0980 0.0656 0.0941 -0.0083 0.0101  -0.0061 206 CYS A CB  
1673 S  SG  . CYS A 207 ? 0.1194 0.0769 0.0896 -0.0061 0.0103  -0.0017 206 CYS A SG  
1674 N  N   . VAL A 208 ? 0.0681 0.0530 0.0873 -0.0026 0.0115  -0.0028 207 VAL A N   
1675 C  CA  . VAL A 208 ? 0.0719 0.0487 0.0833 -0.0020 0.0102  -0.0044 207 VAL A CA  
1676 C  C   . VAL A 208 ? 0.0698 0.0499 0.0793 0.0005  0.0075  -0.0044 207 VAL A C   
1677 O  O   . VAL A 208 ? 0.0826 0.0695 0.0873 0.0039  0.0069  0.0019  207 VAL A O   
1678 C  CB  . VAL A 208 ? 0.0725 0.0509 0.0843 0.0014  0.0125  -0.0052 207 VAL A CB  
1679 C  CG1 . VAL A 208 ? 0.0719 0.0507 0.0847 0.0006  0.0133  -0.0055 207 VAL A CG1 
1680 C  CG2 . VAL A 208 ? 0.0774 0.0577 0.0855 0.0009  0.0120  -0.0035 207 VAL A CG2 
1681 N  N   . THR A 209 ? 0.0710 0.0514 0.0777 0.0004  0.0072  -0.0023 208 THR A N   
1682 C  CA  . THR A 209 ? 0.0735 0.0540 0.0793 -0.0004 0.0081  -0.0056 208 THR A CA  
1683 C  C   . THR A 209 ? 0.0672 0.0513 0.0770 -0.0028 0.0057  -0.0040 208 THR A C   
1684 O  O   . THR A 209 ? 0.0743 0.0544 0.0772 0.0015  -0.0020 -0.0037 208 THR A O   
1685 C  CB  . THR A 209 ? 0.0779 0.0612 0.0864 -0.0009 0.0108  -0.0090 208 THR A CB  
1686 O  OG1 . THR A 209 ? 0.0887 0.0678 0.0951 0.0001  0.0159  -0.0232 208 THR A OG1 
1687 C  CG2 . THR A 209 ? 0.0869 0.0704 0.0915 -0.0019 0.0129  -0.0094 208 THR A CG2 
1688 N  N   . TRP A 210 ? 0.0634 0.0481 0.0708 0.0010  0.0095  -0.0069 209 TRP A N   
1689 C  CA  . TRP A 210 ? 0.0644 0.0449 0.0698 -0.0008 0.0108  -0.0028 209 TRP A CA  
1690 C  C   . TRP A 210 ? 0.0639 0.0468 0.0659 -0.0008 0.0144  -0.0005 209 TRP A C   
1691 O  O   . TRP A 210 ? 0.0694 0.0581 0.0653 -0.0013 0.0111  -0.0033 209 TRP A O   
1692 C  CB  . TRP A 210 ? 0.0667 0.0445 0.0682 0.0005  0.0122  0.0000  209 TRP A CB  
1693 C  CG  . TRP A 210 ? 0.0609 0.0445 0.0738 0.0004  0.0111  0.0008  209 TRP A CG  
1694 C  CD1 . TRP A 210 ? 0.0662 0.0514 0.0786 -0.0026 0.0113  0.0009  209 TRP A CD1 
1695 C  CD2 . TRP A 210 ? 0.0646 0.0461 0.0783 -0.0008 0.0097  0.0011  209 TRP A CD2 
1696 N  NE1 . TRP A 210 ? 0.0644 0.0533 0.0849 -0.0009 0.0135  -0.0007 209 TRP A NE1 
1697 C  CE2 . TRP A 210 ? 0.0659 0.0477 0.0834 0.0011  0.0107  0.0018  209 TRP A CE2 
1698 C  CE3 . TRP A 210 ? 0.0644 0.0456 0.0760 0.0010  0.0087  0.0000  209 TRP A CE3 
1699 C  CZ2 . TRP A 210 ? 0.0674 0.0502 0.0893 0.0036  0.0150  0.0015  209 TRP A CZ2 
1700 C  CZ3 . TRP A 210 ? 0.0750 0.0465 0.0795 0.0050  0.0072  -0.0013 209 TRP A CZ3 
1701 C  CH2 . TRP A 210 ? 0.0772 0.0472 0.0821 0.0079  0.0107  -0.0026 209 TRP A CH2 
1702 N  N   . ILE A 211 ? 0.0643 0.0504 0.0672 -0.0046 0.0143  0.0015  210 ILE A N   
1703 C  CA  . ILE A 211 ? 0.0679 0.0572 0.0689 -0.0035 0.0151  -0.0026 210 ILE A CA  
1704 C  C   . ILE A 211 ? 0.0706 0.0543 0.0624 -0.0046 0.0160  -0.0027 210 ILE A C   
1705 O  O   . ILE A 211 ? 0.0882 0.0618 0.0657 -0.0022 0.0130  -0.0084 210 ILE A O   
1706 C  CB  . ILE A 211 ? 0.0723 0.0610 0.0812 0.0008  0.0157  -0.0029 210 ILE A CB  
1707 C  CG1 . ILE A 211 ? 0.0803 0.0660 0.0937 0.0027  0.0166  -0.0055 210 ILE A CG1 
1708 C  CG2 . ILE A 211 ? 0.0726 0.0647 0.0841 0.0017  0.0135  -0.0024 210 ILE A CG2 
1709 C  CD1 . ILE A 211 ? 0.0907 0.0731 0.1063 0.0045  0.0104  -0.0037 210 ILE A CD1 
1710 N  N   . VAL A 212 ? 0.0722 0.0557 0.0625 -0.0025 0.0151  -0.0028 211 VAL A N   
1711 C  CA  . VAL A 212 ? 0.0731 0.0589 0.0639 -0.0043 0.0169  -0.0008 211 VAL A CA  
1712 C  C   . VAL A 212 ? 0.0744 0.0625 0.0657 -0.0114 0.0159  0.0031  211 VAL A C   
1713 O  O   . VAL A 212 ? 0.0800 0.0713 0.0682 -0.0136 0.0202  0.0017  211 VAL A O   
1714 C  CB  . VAL A 212 ? 0.0782 0.0648 0.0723 -0.0014 0.0164  0.0008  211 VAL A CB  
1715 C  CG1 . VAL A 212 ? 0.0799 0.0617 0.0805 -0.0003 0.0137  0.0012  211 VAL A CG1 
1716 C  CG2 . VAL A 212 ? 0.0805 0.0657 0.0764 0.0001  0.0140  0.0014  211 VAL A CG2 
1717 N  N   . LEU A 213 ? 0.0732 0.0694 0.0731 -0.0158 0.0158  0.0026  212 LEU A N   
1718 C  CA  . LEU A 213 ? 0.0736 0.0781 0.0840 -0.0167 0.0123  0.0008  212 LEU A CA  
1719 C  C   . LEU A 213 ? 0.0804 0.0783 0.0801 -0.0211 0.0091  0.0023  212 LEU A C   
1720 O  O   . LEU A 213 ? 0.0916 0.0836 0.0899 -0.0184 0.0078  0.0023  212 LEU A O   
1721 C  CB  . LEU A 213 ? 0.0747 0.0829 0.0907 -0.0138 0.0105  0.0000  212 LEU A CB  
1722 C  CG  . LEU A 213 ? 0.0833 0.0882 0.1012 -0.0106 0.0062  0.0037  212 LEU A CG  
1723 C  CD1 . LEU A 213 ? 0.0918 0.0949 0.1144 -0.0094 0.0011  0.0054  212 LEU A CD1 
1724 C  CD2 . LEU A 213 ? 0.0904 0.0930 0.1084 -0.0032 0.0092  0.0055  212 LEU A CD2 
1725 N  N   . LYS A 214 ? 0.0889 0.0850 0.0875 -0.0225 0.0095  0.0046  213 LYS A N   
1726 C  CA  . LYS A 214 ? 0.1062 0.0960 0.0927 -0.0221 0.0053  0.0118  213 LYS A CA  
1727 C  C   . LYS A 214 ? 0.0969 0.0872 0.0956 -0.0176 0.0085  0.0125  213 LYS A C   
1728 O  O   . LYS A 214 ? 0.1063 0.0966 0.1357 -0.0075 -0.0016 0.0168  213 LYS A O   
1729 C  CB  . LYS A 214 ? 0.1354 0.1234 0.1023 -0.0337 0.0081  0.0152  213 LYS A CB  
1730 C  CG  . LYS A 214 ? 0.1694 0.1507 0.1385 -0.0330 0.0032  0.0268  213 LYS A CG  
1731 C  CD  . LYS A 214 ? 0.2153 0.1865 0.1674 -0.0304 0.0106  0.0355  213 LYS A CD  
1732 C  CE  . LYS A 214 ? 0.2547 0.2140 0.2086 -0.0259 0.0159  0.0463  213 LYS A CE  
1733 N  NZ  . LYS A 214 ? 0.3004 0.2599 0.2450 -0.0284 0.0217  0.0501  213 LYS A NZ  
1734 N  N   . GLU A 215 ? 0.0938 0.0836 0.0995 -0.0178 0.0050  0.0103  214 GLU A N   
1735 C  CA  . GLU A 215 ? 0.0887 0.0826 0.1023 -0.0188 0.0065  0.0084  214 GLU A CA  
1736 C  C   . GLU A 215 ? 0.0894 0.0758 0.0956 -0.0160 0.0086  0.0060  214 GLU A C   
1737 O  O   . GLU A 215 ? 0.0870 0.0817 0.0876 -0.0110 0.0099  0.0099  214 GLU A O   
1738 C  CB  . GLU A 215 ? 0.0909 0.0932 0.1193 -0.0218 0.0055  0.0065  214 GLU A CB  
1739 C  CG  . GLU A 215 ? 0.1093 0.1153 0.1458 -0.0252 0.0020  -0.0020 214 GLU A CG  
1740 C  CD  . GLU A 215 ? 0.1269 0.1438 0.1859 -0.0305 -0.0018 -0.0066 214 GLU A CD  
1741 O  OE1 . GLU A 215 ? 0.1168 0.1188 0.2188 -0.0252 -0.0098 0.0100  214 GLU A OE1 
1742 O  OE2 . GLU A 215 ? 0.1946 0.1773 0.2594 -0.0420 -0.0163 -0.0087 214 GLU A OE2 
1743 N  N   . PRO A 216 ? 0.1020 0.0788 0.0996 -0.0116 0.0066  0.0087  215 PRO A N   
1744 C  CA  . PRO A 216 ? 0.1016 0.0796 0.0996 -0.0145 0.0127  0.0064  215 PRO A CA  
1745 C  C   . PRO A 216 ? 0.1041 0.0907 0.1029 -0.0197 0.0113  -0.0022 215 PRO A C   
1746 O  O   . PRO A 216 ? 0.1078 0.1276 0.0986 -0.0313 0.0159  0.0003  215 PRO A O   
1747 C  CB  . PRO A 216 ? 0.1130 0.0867 0.1072 -0.0077 0.0062  0.0021  215 PRO A CB  
1748 C  CG  . PRO A 216 ? 0.1321 0.1121 0.1347 -0.0084 0.0089  0.0070  215 PRO A CG  
1749 C  CD  . PRO A 216 ? 0.1100 0.0863 0.1180 -0.0126 0.0103  0.0120  215 PRO A CD  
1750 N  N   . ILE A 217 ? 0.1016 0.0803 0.0988 -0.0138 0.0084  -0.0098 216 ILE A N   
1751 C  CA  . ILE A 217 ? 0.1055 0.0812 0.1018 -0.0091 0.0051  -0.0083 216 ILE A CA  
1752 C  C   . ILE A 217 ? 0.1080 0.0752 0.1145 -0.0107 -0.0021 -0.0086 216 ILE A C   
1753 O  O   . ILE A 217 ? 0.0988 0.0818 0.1234 -0.0155 -0.0011 -0.0173 216 ILE A O   
1754 C  CB  . ILE A 217 ? 0.1114 0.0805 0.0984 -0.0061 0.0090  -0.0097 216 ILE A CB  
1755 C  CG1 . ILE A 217 ? 0.1136 0.0774 0.1093 -0.0020 0.0111  -0.0095 216 ILE A CG1 
1756 C  CG2 . ILE A 217 ? 0.1164 0.0874 0.1096 -0.0023 0.0106  -0.0087 216 ILE A CG2 
1757 C  CD1 . ILE A 217 ? 0.1212 0.0873 0.1146 -0.0009 0.0165  -0.0072 216 ILE A CD1 
1758 N  N   A SER A 218 ? 0.1102 0.0740 0.1201 -0.0104 -0.0054 -0.0093 217 SER A N   
1759 N  N   B SER A 218 ? 0.1149 0.0781 0.1210 -0.0094 -0.0060 -0.0125 217 SER A N   
1760 N  N   C SER A 218 ? 0.1139 0.0752 0.1193 -0.0091 -0.0062 -0.0117 217 SER A N   
1761 C  CA  A SER A 218 ? 0.1135 0.0718 0.1188 -0.0123 -0.0093 -0.0076 217 SER A CA  
1762 C  CA  B SER A 218 ? 0.1225 0.0809 0.1197 -0.0097 -0.0100 -0.0129 217 SER A CA  
1763 C  CA  C SER A 218 ? 0.1206 0.0743 0.1182 -0.0094 -0.0107 -0.0117 217 SER A CA  
1764 C  C   A SER A 218 ? 0.1189 0.0676 0.1193 -0.0104 -0.0128 -0.0076 217 SER A C   
1765 C  C   B SER A 218 ? 0.1239 0.0707 0.1203 -0.0100 -0.0130 -0.0108 217 SER A C   
1766 C  C   C SER A 218 ? 0.1228 0.0692 0.1188 -0.0090 -0.0134 -0.0101 217 SER A C   
1767 O  O   A SER A 218 ? 0.1214 0.0746 0.1257 -0.0065 -0.0144 -0.0061 217 SER A O   
1768 O  O   B SER A 218 ? 0.1257 0.0736 0.1268 -0.0101 -0.0141 -0.0097 217 SER A O   
1769 O  O   C SER A 218 ? 0.1248 0.0753 0.1243 -0.0057 -0.0146 -0.0087 217 SER A O   
1770 C  CB  A SER A 218 ? 0.1127 0.0725 0.1217 -0.0138 -0.0081 -0.0017 217 SER A CB  
1771 C  CB  B SER A 218 ? 0.1290 0.0884 0.1235 -0.0108 -0.0094 -0.0108 217 SER A CB  
1772 C  CB  C SER A 218 ? 0.1239 0.0761 0.1211 -0.0097 -0.0108 -0.0089 217 SER A CB  
1773 O  OG  A SER A 218 ? 0.1161 0.0730 0.1268 -0.0209 -0.0039 0.0041  217 SER A OG  
1774 O  OG  B SER A 218 ? 0.1352 0.1022 0.1331 -0.0099 -0.0090 -0.0082 217 SER A OG  
1775 O  OG  C SER A 218 ? 0.1368 0.0787 0.1255 -0.0118 -0.0093 -0.0095 217 SER A OG  
1776 N  N   . VAL A 219 ? 0.1268 0.0696 0.1135 -0.0110 -0.0147 -0.0121 218 VAL A N   
1777 C  CA  . VAL A 219 ? 0.1306 0.0613 0.1183 -0.0109 -0.0157 -0.0101 218 VAL A CA  
1778 C  C   . VAL A 219 ? 0.1301 0.0586 0.1204 -0.0077 -0.0154 -0.0073 218 VAL A C   
1779 O  O   . VAL A 219 ? 0.1387 0.0561 0.1276 -0.0116 -0.0199 -0.0046 218 VAL A O   
1780 C  CB  . VAL A 219 ? 0.1367 0.0593 0.1334 -0.0118 -0.0149 -0.0067 218 VAL A CB  
1781 C  CG1 . VAL A 219 ? 0.1425 0.0638 0.1401 -0.0142 -0.0191 -0.0091 218 VAL A CG1 
1782 C  CG2 . VAL A 219 ? 0.1379 0.0542 0.1456 -0.0131 -0.0127 -0.0084 218 VAL A CG2 
1783 N  N   . SER A 220 ? 0.1290 0.0532 0.1163 -0.0067 -0.0112 -0.0058 219 SER A N   
1784 C  CA  . SER A 220 ? 0.1297 0.0556 0.1301 -0.0090 -0.0066 -0.0050 219 SER A CA  
1785 C  C   . SER A 220 ? 0.1299 0.0557 0.1323 -0.0086 -0.0035 -0.0066 219 SER A C   
1786 O  O   . SER A 220 ? 0.1272 0.0607 0.1338 -0.0143 -0.0031 -0.0001 219 SER A O   
1787 C  CB  . SER A 220 ? 0.1274 0.0681 0.1270 -0.0085 -0.0040 -0.0059 219 SER A CB  
1788 O  OG  . SER A 220 ? 0.1292 0.0847 0.1350 -0.0165 -0.0026 -0.0026 219 SER A OG  
1789 N  N   A SER A 221 ? 0.1330 0.0595 0.1473 -0.0106 -0.0004 -0.0048 220 SER A N   
1790 N  N   B SER A 221 ? 0.1312 0.0532 0.1433 -0.0094 -0.0011 -0.0054 220 SER A N   
1791 C  CA  A SER A 221 ? 0.1369 0.0781 0.1632 -0.0067 0.0009  -0.0034 220 SER A CA  
1792 C  CA  B SER A 221 ? 0.1331 0.0603 0.1543 -0.0038 -0.0005 -0.0046 220 SER A CA  
1793 C  C   A SER A 221 ? 0.1305 0.0714 0.1643 -0.0083 0.0022  -0.0068 220 SER A C   
1794 C  C   B SER A 221 ? 0.1288 0.0642 0.1582 -0.0064 0.0006  -0.0080 220 SER A C   
1795 O  O   A SER A 221 ? 0.1268 0.0715 0.1800 -0.0102 0.0076  -0.0037 220 SER A O   
1796 O  O   B SER A 221 ? 0.1225 0.0651 0.1691 -0.0068 0.0024  -0.0098 220 SER A O   
1797 C  CB  A SER A 221 ? 0.1487 0.0935 0.1771 -0.0034 0.0044  -0.0038 220 SER A CB  
1798 C  CB  B SER A 221 ? 0.1408 0.0650 0.1611 0.0014  0.0019  -0.0030 220 SER A CB  
1799 O  OG  A SER A 221 ? 0.1591 0.1279 0.1936 -0.0036 0.0128  -0.0046 220 SER A OG  
1800 O  OG  B SER A 221 ? 0.1448 0.0597 0.1587 0.0011  0.0075  -0.0046 220 SER A OG  
1801 N  N   . GLU A 222 ? 0.1286 0.0681 0.1606 -0.0062 0.0022  -0.0075 221 GLU A N   
1802 C  CA  . GLU A 222 ? 0.1424 0.0887 0.1570 0.0003  0.0011  -0.0118 221 GLU A CA  
1803 C  C   . GLU A 222 ? 0.1360 0.0830 0.1441 0.0019  0.0060  -0.0061 221 GLU A C   
1804 O  O   . GLU A 222 ? 0.1433 0.0910 0.1418 0.0007  0.0203  -0.0136 221 GLU A O   
1805 C  CB  . GLU A 222 ? 0.1627 0.1128 0.1718 -0.0021 -0.0013 -0.0262 221 GLU A CB  
1806 C  CG  . GLU A 222 ? 0.1966 0.1306 0.1940 -0.0033 -0.0106 -0.0386 221 GLU A CG  
1807 C  CD  . GLU A 222 ? 0.2139 0.1284 0.2308 -0.0162 -0.0143 -0.0444 221 GLU A CD  
1808 O  OE1 . GLU A 222 ? 0.2272 0.1480 0.2397 -0.0321 -0.0154 -0.0511 221 GLU A OE1 
1809 O  OE2 . GLU A 222 ? 0.2940 0.1441 0.3149 -0.0350 -0.0145 -0.0573 221 GLU A OE2 
1810 N  N   . GLN A 223 ? 0.1238 0.0710 0.1313 -0.0078 0.0017  -0.0057 222 GLN A N   
1811 C  CA  . GLN A 223 ? 0.1186 0.0707 0.1231 -0.0095 -0.0018 0.0008  222 GLN A CA  
1812 C  C   . GLN A 223 ? 0.1158 0.0777 0.1293 -0.0098 0.0000  0.0092  222 GLN A C   
1813 O  O   . GLN A 223 ? 0.1186 0.0868 0.1331 -0.0108 0.0033  0.0087  222 GLN A O   
1814 C  CB  . GLN A 223 ? 0.1175 0.0712 0.1097 -0.0095 -0.0040 -0.0004 222 GLN A CB  
1815 C  CG  . GLN A 223 ? 0.1152 0.0684 0.1100 -0.0123 -0.0032 -0.0035 222 GLN A CG  
1816 C  CD  . GLN A 223 ? 0.1161 0.0681 0.1131 -0.0084 -0.0013 -0.0065 222 GLN A CD  
1817 O  OE1 . GLN A 223 ? 0.1154 0.0728 0.1189 -0.0077 0.0000  -0.0087 222 GLN A OE1 
1818 N  NE2 . GLN A 223 ? 0.1255 0.0753 0.1085 -0.0076 0.0027  -0.0022 222 GLN A NE2 
1819 N  N   . VAL A 224 ? 0.1115 0.0871 0.1338 -0.0142 -0.0007 0.0218  223 VAL A N   
1820 C  CA  . VAL A 224 ? 0.1251 0.1113 0.1398 -0.0183 -0.0039 0.0219  223 VAL A CA  
1821 C  C   . VAL A 224 ? 0.1178 0.0996 0.1471 -0.0220 0.0040  0.0197  223 VAL A C   
1822 O  O   . VAL A 224 ? 0.1240 0.1046 0.1402 -0.0215 0.0057  0.0189  223 VAL A O   
1823 C  CB  . VAL A 224 ? 0.1433 0.1479 0.1550 -0.0174 -0.0035 0.0337  223 VAL A CB  
1824 C  CG1 . VAL A 224 ? 0.1517 0.1669 0.1780 -0.0230 -0.0044 0.0311  223 VAL A CG1 
1825 C  CG2 . VAL A 224 ? 0.1546 0.1685 0.1519 -0.0171 -0.0016 0.0294  223 VAL A CG2 
1826 N  N   . LEU A 225 ? 0.1184 0.1109 0.1622 -0.0222 0.0133  0.0089  224 LEU A N   
1827 C  CA  . LEU A 225 ? 0.1346 0.1197 0.1794 -0.0184 0.0209  0.0039  224 LEU A CA  
1828 C  C   . LEU A 225 ? 0.1245 0.1208 0.1664 -0.0264 0.0184  0.0011  224 LEU A C   
1829 O  O   . LEU A 225 ? 0.1236 0.1203 0.1806 -0.0252 0.0277  -0.0072 224 LEU A O   
1830 C  CB  . LEU A 225 ? 0.1645 0.1340 0.2093 -0.0192 0.0249  -0.0001 224 LEU A CB  
1831 C  CG  . LEU A 225 ? 0.2071 0.1596 0.2347 -0.0130 0.0247  0.0005  224 LEU A CG  
1832 C  CD1 . LEU A 225 ? 0.2153 0.1823 0.2503 -0.0135 0.0264  -0.0010 224 LEU A CD1 
1833 C  CD2 . LEU A 225 ? 0.2184 0.1638 0.2437 -0.0085 0.0211  -0.0065 224 LEU A CD2 
1834 N  N   . LYS A 226 ? 0.1209 0.1262 0.1375 -0.0276 0.0162  0.0032  225 LYS A N   
1835 C  CA  . LYS A 226 ? 0.1265 0.1337 0.1333 -0.0232 0.0161  0.0070  225 LYS A CA  
1836 C  C   . LYS A 226 ? 0.1216 0.1104 0.1064 -0.0136 0.0136  0.0122  225 LYS A C   
1837 O  O   . LYS A 226 ? 0.1347 0.1215 0.1017 -0.0191 0.0119  0.0172  225 LYS A O   
1838 C  CB  . LYS A 226 ? 0.1387 0.1676 0.1476 -0.0319 0.0099  0.0124  225 LYS A CB  
1839 C  CG  . LYS A 226 ? 0.1778 0.2057 0.1808 -0.0378 0.0123  0.0019  225 LYS A CG  
1840 C  CD  . LYS A 226 ? 0.2006 0.2321 0.2128 -0.0439 0.0082  -0.0098 225 LYS A CD  
1841 C  CE  . LYS A 226 ? 0.2299 0.2495 0.2290 -0.0474 0.0204  -0.0196 225 LYS A CE  
1842 N  NZ  . LYS A 226 ? 0.2330 0.2663 0.2416 -0.0466 0.0357  -0.0272 225 LYS A NZ  
1843 N  N   . PHE A 227 ? 0.1143 0.1003 0.1044 -0.0039 0.0200  0.0094  226 PHE A N   
1844 C  CA  . PHE A 227 ? 0.1150 0.0882 0.1040 -0.0002 0.0213  0.0087  226 PHE A CA  
1845 C  C   . PHE A 227 ? 0.1150 0.0868 0.0925 -0.0001 0.0250  0.0079  226 PHE A C   
1846 O  O   . PHE A 227 ? 0.1163 0.0846 0.0891 -0.0023 0.0228  0.0021  226 PHE A O   
1847 C  CB  . PHE A 227 ? 0.1169 0.0981 0.1112 0.0057  0.0219  0.0036  226 PHE A CB  
1848 C  CG  . PHE A 227 ? 0.1112 0.1087 0.1292 0.0046  0.0201  -0.0096 226 PHE A CG  
1849 C  CD1 . PHE A 227 ? 0.1378 0.1422 0.1429 0.0173  0.0202  -0.0111 226 PHE A CD1 
1850 C  CD2 . PHE A 227 ? 0.1303 0.1428 0.1544 0.0104  0.0089  -0.0279 226 PHE A CD2 
1851 C  CE1 . PHE A 227 ? 0.1317 0.1458 0.1632 0.0209  0.0161  -0.0101 226 PHE A CE1 
1852 C  CE2 . PHE A 227 ? 0.1407 0.1575 0.1672 0.0090  0.0042  -0.0399 226 PHE A CE2 
1853 C  CZ  . PHE A 227 ? 0.1294 0.1436 0.1801 0.0124  0.0070  -0.0310 226 PHE A CZ  
1854 N  N   . ARG A 228 ? 0.1098 0.0832 0.0894 -0.0002 0.0262  0.0033  227 ARG A N   
1855 C  CA  . ARG A 228 ? 0.1181 0.0916 0.0926 0.0037  0.0209  0.0012  227 ARG A CA  
1856 C  C   . ARG A 228 ? 0.1222 0.0999 0.0944 0.0045  0.0241  0.0006  227 ARG A C   
1857 O  O   . ARG A 228 ? 0.1203 0.1197 0.1105 0.0136  0.0245  0.0040  227 ARG A O   
1858 C  CB  . ARG A 228 ? 0.1280 0.0893 0.0927 0.0018  0.0155  -0.0023 227 ARG A CB  
1859 C  CG  . ARG A 228 ? 0.1271 0.0851 0.0908 0.0011  0.0115  0.0000  227 ARG A CG  
1860 C  CD  . ARG A 228 ? 0.1516 0.0836 0.1025 -0.0051 0.0068  -0.0015 227 ARG A CD  
1861 N  NE  . ARG A 228 ? 0.1655 0.0759 0.1040 -0.0172 0.0008  -0.0040 227 ARG A NE  
1862 C  CZ  . ARG A 228 ? 0.1821 0.0887 0.1195 -0.0316 -0.0055 -0.0123 227 ARG A CZ  
1863 N  NH1 . ARG A 228 ? 0.1968 0.1066 0.1542 -0.0388 -0.0169 -0.0221 227 ARG A NH1 
1864 N  NH2 . ARG A 228 ? 0.1960 0.0927 0.1284 -0.0356 0.0018  -0.0114 227 ARG A NH2 
1865 N  N   . LYS A 229 ? 0.1277 0.1043 0.0848 -0.0021 0.0235  -0.0094 228 LYS A N   
1866 C  CA  . LYS A 229 ? 0.1483 0.1088 0.0900 -0.0070 0.0293  -0.0147 228 LYS A CA  
1867 C  C   . LYS A 229 ? 0.1419 0.0955 0.0730 -0.0040 0.0251  -0.0141 228 LYS A C   
1868 O  O   . LYS A 229 ? 0.1601 0.1044 0.0823 -0.0073 0.0321  -0.0121 228 LYS A O   
1869 C  CB  . LYS A 229 ? 0.1732 0.1357 0.1035 -0.0138 0.0248  -0.0159 228 LYS A CB  
1870 C  CG  . LYS A 229 ? 0.2108 0.1715 0.1473 -0.0296 0.0192  -0.0199 228 LYS A CG  
1871 C  CD  . LYS A 229 ? 0.2449 0.2168 0.1936 -0.0408 0.0100  -0.0179 228 LYS A CD  
1872 C  CE  . LYS A 229 ? 0.2801 0.2514 0.2440 -0.0502 0.0016  -0.0200 228 LYS A CE  
1873 N  NZ  . LYS A 229 ? 0.3158 0.2898 0.2791 -0.0526 0.0011  -0.0279 228 LYS A NZ  
1874 N  N   . LEU A 230 ? 0.1321 0.0813 0.0770 0.0029  0.0278  -0.0111 229 LEU A N   
1875 C  CA  . LEU A 230 ? 0.1265 0.0817 0.0796 0.0058  0.0291  -0.0055 229 LEU A CA  
1876 C  C   . LEU A 230 ? 0.1236 0.0725 0.0749 0.0100  0.0326  -0.0122 229 LEU A C   
1877 O  O   . LEU A 230 ? 0.1295 0.0738 0.0847 0.0062  0.0265  -0.0050 229 LEU A O   
1878 C  CB  . LEU A 230 ? 0.1225 0.0805 0.0837 0.0083  0.0257  -0.0022 229 LEU A CB  
1879 C  CG  . LEU A 230 ? 0.1216 0.0867 0.0971 0.0072  0.0216  -0.0038 229 LEU A CG  
1880 C  CD1 . LEU A 230 ? 0.1235 0.0972 0.1000 0.0031  0.0204  -0.0062 229 LEU A CD1 
1881 C  CD2 . LEU A 230 ? 0.1298 0.0976 0.1103 0.0114  0.0236  0.0014  229 LEU A CD2 
1882 N  N   . ASN A 231 ? 0.1258 0.0769 0.0792 0.0084  0.0314  -0.0107 230 ASN A N   
1883 C  CA  . ASN A 231 ? 0.1253 0.0793 0.0817 0.0084  0.0350  -0.0056 230 ASN A CA  
1884 C  C   . ASN A 231 ? 0.1152 0.0804 0.0833 0.0054  0.0349  -0.0001 230 ASN A C   
1885 O  O   . ASN A 231 ? 0.1237 0.0839 0.0917 0.0089  0.0303  -0.0020 230 ASN A O   
1886 C  CB  . ASN A 231 ? 0.1338 0.0897 0.0897 0.0083  0.0400  -0.0050 230 ASN A CB  
1887 C  CG  . ASN A 231 ? 0.1589 0.1101 0.0976 0.0128  0.0393  -0.0129 230 ASN A CG  
1888 O  OD1 . ASN A 231 ? 0.2152 0.1128 0.1005 0.0100  0.0480  -0.0138 230 ASN A OD1 
1889 N  ND2 . ASN A 231 ? 0.1535 0.1134 0.1022 0.0139  0.0312  -0.0110 230 ASN A ND2 
1890 N  N   . PHE A 232 ? 0.1154 0.0864 0.0902 0.0049  0.0294  0.0027  231 PHE A N   
1891 C  CA  . PHE A 232 ? 0.1158 0.0957 0.1039 -0.0031 0.0288  0.0046  231 PHE A CA  
1892 C  C   . PHE A 232 ? 0.1236 0.1021 0.1133 -0.0088 0.0261  0.0105  231 PHE A C   
1893 O  O   . PHE A 232 ? 0.1342 0.1117 0.1212 -0.0235 0.0208  0.0090  231 PHE A O   
1894 C  CB  . PHE A 232 ? 0.1208 0.1025 0.1029 -0.0062 0.0284  0.0053  231 PHE A CB  
1895 C  CG  . PHE A 232 ? 0.1203 0.0955 0.1021 -0.0106 0.0285  0.0024  231 PHE A CG  
1896 C  CD1 . PHE A 232 ? 0.1245 0.0906 0.1038 -0.0109 0.0244  -0.0026 231 PHE A CD1 
1897 C  CD2 . PHE A 232 ? 0.1234 0.0972 0.1011 -0.0021 0.0291  -0.0016 231 PHE A CD2 
1898 C  CE1 . PHE A 232 ? 0.1299 0.0994 0.1038 -0.0107 0.0250  -0.0054 231 PHE A CE1 
1899 C  CE2 . PHE A 232 ? 0.1231 0.0974 0.0979 -0.0039 0.0272  -0.0007 231 PHE A CE2 
1900 C  CZ  . PHE A 232 ? 0.1246 0.1044 0.0951 -0.0116 0.0271  -0.0048 231 PHE A CZ  
1901 N  N   . ASN A 233 ? 0.1265 0.1123 0.1171 -0.0095 0.0353  0.0191  232 ASN A N   
1902 C  CA  . ASN A 233 ? 0.1335 0.1294 0.1222 0.0029  0.0421  0.0229  232 ASN A CA  
1903 C  C   . ASN A 233 ? 0.1251 0.1248 0.1156 0.0093  0.0489  0.0230  232 ASN A C   
1904 O  O   . ASN A 233 ? 0.1286 0.1191 0.1199 0.0181  0.0442  0.0138  232 ASN A O   
1905 C  CB  . ASN A 233 ? 0.1428 0.1391 0.1370 0.0121  0.0492  0.0234  232 ASN A CB  
1906 C  CG  . ASN A 233 ? 0.1442 0.1328 0.1292 0.0289  0.0515  0.0113  232 ASN A CG  
1907 O  OD1 . ASN A 233 ? 0.1480 0.1369 0.1478 0.0362  0.0537  0.0132  232 ASN A OD1 
1908 N  ND2 . ASN A 233 ? 0.1796 0.1379 0.1282 0.0287  0.0502  0.0021  232 ASN A ND2 
1909 N  N   . GLY A 234 ? 0.1289 0.1443 0.1242 0.0105  0.0499  0.0317  233 GLY A N   
1910 C  CA  . GLY A 234 ? 0.1399 0.1349 0.1275 0.0233  0.0496  0.0323  233 GLY A CA  
1911 C  C   . GLY A 234 ? 0.1441 0.1410 0.1253 0.0341  0.0533  0.0273  233 GLY A C   
1912 O  O   . GLY A 234 ? 0.1755 0.1641 0.1325 0.0510  0.0646  0.0233  233 GLY A O   
1913 N  N   . GLU A 235 ? 0.1565 0.1324 0.1184 0.0331  0.0550  0.0224  234 GLU A N   
1914 C  CA  . GLU A 235 ? 0.1761 0.1422 0.1215 0.0303  0.0556  0.0198  234 GLU A CA  
1915 C  C   . GLU A 235 ? 0.1904 0.1555 0.1410 0.0444  0.0604  0.0319  234 GLU A C   
1916 O  O   . GLU A 235 ? 0.1789 0.2047 0.1390 0.0296  0.0615  0.0351  234 GLU A O   
1917 C  CB  . GLU A 235 ? 0.1717 0.1425 0.1367 0.0191  0.0492  0.0150  234 GLU A CB  
1918 C  CG  . GLU A 235 ? 0.1809 0.1506 0.1478 0.0059  0.0542  0.0145  234 GLU A CG  
1919 C  CD  . GLU A 235 ? 0.2068 0.1856 0.1898 0.0033  0.0398  0.0076  234 GLU A CD  
1920 O  OE1 . GLU A 235 ? 0.2102 0.2018 0.2190 0.0054  0.0452  0.0301  234 GLU A OE1 
1921 O  OE2 . GLU A 235 ? 0.2827 0.2374 0.2217 0.0154  0.0201  0.0005  234 GLU A OE2 
1922 N  N   . GLY A 236 ? 0.2271 0.1801 0.1488 0.0644  0.0785  0.0345  235 GLY A N   
1923 C  CA  . GLY A 236 ? 0.2415 0.2269 0.1743 0.0844  0.0863  0.0416  235 GLY A CA  
1924 C  C   . GLY A 236 ? 0.2456 0.2603 0.1805 0.1057  0.1044  0.0486  235 GLY A C   
1925 O  O   . GLY A 236 ? 0.2764 0.3332 0.2172 0.1328  0.1094  0.0549  235 GLY A O   
1926 N  N   . GLU A 237 ? 0.2210 0.2778 0.1936 0.1193  0.1010  0.0864  236 GLU A N   
1927 C  CA  . GLU A 237 ? 0.2055 0.2901 0.2200 0.1085  0.1088  0.1062  236 GLU A CA  
1928 C  C   . GLU A 237 ? 0.2144 0.3039 0.2231 0.1032  0.1376  0.1043  236 GLU A C   
1929 O  O   . GLU A 237 ? 0.2617 0.2874 0.2413 0.1181  0.1360  0.0857  236 GLU A O   
1930 C  CB  . GLU A 237 ? 0.2210 0.3201 0.2452 0.0818  0.1045  0.1063  236 GLU A CB  
1931 C  CG  . GLU A 237 ? 0.2406 0.3364 0.2633 0.0581  0.1017  0.1096  236 GLU A CG  
1932 C  CD  . GLU A 237 ? 0.2758 0.3493 0.3098 0.0291  0.0842  0.1071  236 GLU A CD  
1933 O  OE1 . GLU A 237 ? 0.2360 0.3483 0.3147 0.0308  0.0648  0.1177  236 GLU A OE1 
1934 O  OE2 . GLU A 237 ? 0.3354 0.3654 0.3646 0.0168  0.0859  0.1053  236 GLU A OE2 
1935 N  N   . PRO A 238 ? 0.2091 0.3164 0.2547 0.0879  0.1375  0.1210  237 PRO A N   
1936 C  CA  . PRO A 238 ? 0.2170 0.3001 0.2381 0.0841  0.1342  0.1052  237 PRO A CA  
1937 C  C   . PRO A 238 ? 0.1986 0.2607 0.2042 0.0869  0.1182  0.0795  237 PRO A C   
1938 O  O   . PRO A 238 ? 0.2036 0.2681 0.2306 0.1027  0.1134  0.0920  237 PRO A O   
1939 C  CB  . PRO A 238 ? 0.2250 0.3208 0.2636 0.0844  0.1367  0.1132  237 PRO A CB  
1940 C  CG  . PRO A 238 ? 0.2241 0.3343 0.2771 0.0834  0.1300  0.1237  237 PRO A CG  
1941 C  CD  . PRO A 238 ? 0.2217 0.3298 0.2768 0.0832  0.1225  0.1294  237 PRO A CD  
1942 N  N   . GLU A 239 ? 0.1919 0.2458 0.1833 0.0911  0.1029  0.0236  238 GLU A N   
1943 C  CA  . GLU A 239 ? 0.1821 0.2048 0.1832 0.0697  0.0838  0.0015  238 GLU A CA  
1944 C  C   . GLU A 239 ? 0.1648 0.1588 0.1698 0.0577  0.0696  0.0047  238 GLU A C   
1945 O  O   . GLU A 239 ? 0.1635 0.1578 0.1848 0.0670  0.0659  -0.0005 238 GLU A O   
1946 C  CB  . GLU A 239 ? 0.2313 0.2101 0.2064 0.0622  0.0628  -0.0243 238 GLU A CB  
1947 C  CG  . GLU A 239 ? 0.2546 0.2189 0.2224 0.0473  0.0518  -0.0471 238 GLU A CG  
1948 C  CD  . GLU A 239 ? 0.2845 0.2304 0.2427 0.0344  0.0350  -0.0714 238 GLU A CD  
1949 O  OE1 . GLU A 239 ? 0.3362 0.2673 0.2942 0.0236  0.0237  -0.1150 238 GLU A OE1 
1950 O  OE2 . GLU A 239 ? 0.2612 0.1883 0.2066 0.0153  0.0271  -0.0827 238 GLU A OE2 
1951 N  N   . GLU A 240 ? 0.1526 0.1258 0.1398 0.0357  0.0570  0.0170  239 GLU A N   
1952 C  CA  . GLU A 240 ? 0.1516 0.1344 0.1460 0.0345  0.0505  0.0129  239 GLU A CA  
1953 C  C   . GLU A 240 ? 0.1310 0.1030 0.1266 0.0341  0.0486  0.0144  239 GLU A C   
1954 O  O   . GLU A 240 ? 0.1475 0.0983 0.1616 0.0278  0.0567  0.0045  239 GLU A O   
1955 C  CB  . GLU A 240 ? 0.1867 0.1689 0.1747 0.0224  0.0452  0.0150  239 GLU A CB  
1956 C  CG  . GLU A 240 ? 0.2115 0.2191 0.2073 0.0347  0.0435  0.0141  239 GLU A CG  
1957 C  CD  . GLU A 240 ? 0.2339 0.2432 0.2352 0.0517  0.0503  0.0095  239 GLU A CD  
1958 O  OE1 . GLU A 240 ? 0.2750 0.2580 0.2860 0.0473  0.0466  -0.0062 239 GLU A OE1 
1959 O  OE2 . GLU A 240 ? 0.2776 0.3150 0.2892 0.0503  0.0496  0.0260  239 GLU A OE2 
1960 N  N   . LEU A 241 ? 0.1175 0.0861 0.1132 0.0328  0.0421  0.0017  240 LEU A N   
1961 C  CA  . LEU A 241 ? 0.1147 0.0839 0.1143 0.0228  0.0367  0.0039  240 LEU A CA  
1962 C  C   . LEU A 241 ? 0.1105 0.0807 0.0991 0.0139  0.0339  0.0057  240 LEU A C   
1963 O  O   . LEU A 241 ? 0.1092 0.0907 0.1039 0.0205  0.0286  0.0017  240 LEU A O   
1964 C  CB  . LEU A 241 ? 0.1225 0.0851 0.1302 0.0259  0.0341  0.0006  240 LEU A CB  
1965 C  CG  . LEU A 241 ? 0.1406 0.0999 0.1448 0.0231  0.0308  -0.0072 240 LEU A CG  
1966 C  CD1 . LEU A 241 ? 0.1529 0.1032 0.1645 0.0236  0.0229  -0.0110 240 LEU A CD1 
1967 C  CD2 . LEU A 241 ? 0.1533 0.0949 0.1435 0.0201  0.0315  -0.0072 240 LEU A CD2 
1968 N  N   . MET A 242 ? 0.1093 0.0777 0.0797 0.0132  0.0322  0.0006  241 MET A N   
1969 C  CA  . MET A 242 ? 0.1082 0.0748 0.0854 0.0120  0.0290  -0.0045 241 MET A CA  
1970 C  C   . MET A 242 ? 0.1033 0.0707 0.0818 0.0083  0.0242  -0.0049 241 MET A C   
1971 O  O   . MET A 242 ? 0.1092 0.0825 0.0791 0.0098  0.0262  -0.0056 241 MET A O   
1972 C  CB  . MET A 242 ? 0.1115 0.0804 0.0831 0.0103  0.0310  -0.0086 241 MET A CB  
1973 C  CG  . MET A 242 ? 0.1193 0.0740 0.0887 0.0050  0.0318  -0.0119 241 MET A CG  
1974 S  SD  . MET A 242 ? 0.1277 0.0721 0.1079 0.0050  0.0408  -0.0002 241 MET A SD  
1975 C  CE  . MET A 242 ? 0.1308 0.0739 0.1143 0.0007  0.0410  0.0053  241 MET A CE  
1976 N  N   . VAL A 243 ? 0.1001 0.0651 0.0772 0.0053  0.0240  0.0031  242 VAL A N   
1977 C  CA  . VAL A 243 ? 0.1026 0.0655 0.0801 0.0026  0.0193  0.0041  242 VAL A CA  
1978 C  C   . VAL A 243 ? 0.0960 0.0609 0.0777 0.0035  0.0176  0.0008  242 VAL A C   
1979 O  O   . VAL A 243 ? 0.0961 0.0747 0.0826 -0.0016 0.0159  -0.0016 242 VAL A O   
1980 C  CB  . VAL A 243 ? 0.1147 0.0723 0.0886 0.0020  0.0182  -0.0013 242 VAL A CB  
1981 C  CG1 . VAL A 243 ? 0.1251 0.0813 0.0958 -0.0037 0.0164  -0.0040 242 VAL A CG1 
1982 C  CG2 . VAL A 243 ? 0.1216 0.0710 0.0981 0.0036  0.0197  -0.0044 242 VAL A CG2 
1983 N  N   . ASP A 244 ? 0.0955 0.0586 0.0755 0.0059  0.0145  0.0004  243 ASP A N   
1984 C  CA  . ASP A 244 ? 0.0920 0.0585 0.0830 0.0101  0.0132  -0.0004 243 ASP A CA  
1985 C  C   . ASP A 244 ? 0.0845 0.0557 0.0756 0.0080  0.0135  -0.0008 243 ASP A C   
1986 O  O   . ASP A 244 ? 0.0836 0.0624 0.0961 0.0081  0.0087  -0.0012 243 ASP A O   
1987 C  CB  . ASP A 244 ? 0.0926 0.0605 0.0884 0.0116  0.0128  -0.0032 243 ASP A CB  
1988 C  CG  . ASP A 244 ? 0.1034 0.0604 0.1019 0.0139  0.0129  -0.0051 243 ASP A CG  
1989 O  OD1 . ASP A 244 ? 0.1023 0.0587 0.1004 0.0092  0.0114  -0.0031 243 ASP A OD1 
1990 O  OD2 . ASP A 244 ? 0.1253 0.0591 0.1232 0.0170  0.0222  -0.0107 243 ASP A OD2 
1991 N  N   . ASN A 245 ? 0.0813 0.0478 0.0717 0.0063  0.0125  -0.0011 244 ASN A N   
1992 C  CA  . ASN A 245 ? 0.0820 0.0480 0.0737 0.0060  0.0193  0.0016  244 ASN A CA  
1993 C  C   . ASN A 245 ? 0.0808 0.0481 0.0674 0.0064  0.0178  0.0013  244 ASN A C   
1994 O  O   . ASN A 245 ? 0.1033 0.0561 0.0673 0.0156  0.0219  0.0003  244 ASN A O   
1995 C  CB  . ASN A 245 ? 0.0807 0.0589 0.0782 0.0077  0.0206  0.0064  244 ASN A CB  
1996 C  CG  . ASN A 245 ? 0.0844 0.0662 0.0934 0.0019  0.0150  0.0167  244 ASN A CG  
1997 O  OD1 . ASN A 245 ? 0.0792 0.0655 0.1014 0.0026  0.0140  0.0170  244 ASN A OD1 
1998 N  ND2 . ASN A 245 ? 0.0924 0.0917 0.1162 -0.0061 0.0070  0.0357  244 ASN A ND2 
1999 N  N   . TRP A 246 ? 0.0765 0.0496 0.0616 0.0053  0.0154  -0.0011 245 TRP A N   
2000 C  CA  . TRP A 246 ? 0.0747 0.0515 0.0629 0.0057  0.0143  -0.0013 245 TRP A CA  
2001 C  C   . TRP A 246 ? 0.0695 0.0559 0.0675 0.0047  0.0133  -0.0014 245 TRP A C   
2002 O  O   . TRP A 246 ? 0.0767 0.0670 0.0770 0.0105  0.0049  -0.0010 245 TRP A O   
2003 C  CB  . TRP A 246 ? 0.0782 0.0566 0.0675 0.0029  0.0164  -0.0022 245 TRP A CB  
2004 C  CG  . TRP A 246 ? 0.0834 0.0587 0.0725 0.0057  0.0139  -0.0004 245 TRP A CG  
2005 C  CD1 . TRP A 246 ? 0.0854 0.0565 0.0727 0.0055  0.0132  0.0023  245 TRP A CD1 
2006 C  CD2 . TRP A 246 ? 0.0917 0.0614 0.0784 0.0080  0.0146  0.0006  245 TRP A CD2 
2007 N  NE1 . TRP A 246 ? 0.0897 0.0571 0.0801 0.0056  0.0130  0.0014  245 TRP A NE1 
2008 C  CE2 . TRP A 246 ? 0.0946 0.0603 0.0858 0.0079  0.0120  0.0020  245 TRP A CE2 
2009 C  CE3 . TRP A 246 ? 0.1038 0.0676 0.0820 0.0099  0.0148  0.0032  245 TRP A CE3 
2010 C  CZ2 . TRP A 246 ? 0.1086 0.0628 0.0991 0.0103  0.0133  0.0042  245 TRP A CZ2 
2011 C  CZ3 . TRP A 246 ? 0.1156 0.0732 0.0935 0.0070  0.0106  0.0090  245 TRP A CZ3 
2012 C  CH2 . TRP A 246 ? 0.1166 0.0696 0.1008 0.0117  0.0108  0.0138  245 TRP A CH2 
2013 N  N   . ARG A 247 ? 0.0662 0.0585 0.0693 0.0105  0.0127  -0.0028 246 ARG A N   
2014 C  CA  . ARG A 247 ? 0.0672 0.0710 0.0757 0.0067  0.0145  -0.0039 246 ARG A CA  
2015 C  C   . ARG A 247 ? 0.0706 0.0730 0.0813 0.0091  0.0148  -0.0052 246 ARG A C   
2016 O  O   . ARG A 247 ? 0.0735 0.0721 0.0874 0.0040  0.0118  -0.0104 246 ARG A O   
2017 C  CB  . ARG A 247 ? 0.0661 0.0714 0.0745 0.0011  0.0147  -0.0030 246 ARG A CB  
2018 C  CG  . ARG A 247 ? 0.0633 0.0735 0.0741 -0.0021 0.0155  -0.0029 246 ARG A CG  
2019 C  CD  . ARG A 247 ? 0.0666 0.0793 0.0786 -0.0043 0.0141  -0.0085 246 ARG A CD  
2020 N  NE  . ARG A 247 ? 0.0662 0.0853 0.0891 -0.0104 0.0143  -0.0128 246 ARG A NE  
2021 C  CZ  . ARG A 247 ? 0.0704 0.0926 0.0826 -0.0164 0.0179  -0.0181 246 ARG A CZ  
2022 N  NH1 . ARG A 247 ? 0.0774 0.0950 0.0866 -0.0188 0.0152  -0.0231 246 ARG A NH1 
2023 N  NH2 . ARG A 247 ? 0.0781 0.1065 0.0881 -0.0170 0.0181  -0.0246 246 ARG A NH2 
2024 N  N   . PRO A 248 ? 0.0765 0.0822 0.0871 0.0133  0.0171  -0.0001 247 PRO A N   
2025 C  CA  . PRO A 248 ? 0.0835 0.0859 0.0879 0.0126  0.0176  -0.0017 247 PRO A CA  
2026 C  C   . PRO A 248 ? 0.0830 0.0765 0.0804 0.0112  0.0143  -0.0003 247 PRO A C   
2027 O  O   . PRO A 248 ? 0.0877 0.0714 0.0831 0.0047  0.0095  0.0060  247 PRO A O   
2028 C  CB  . PRO A 248 ? 0.0970 0.0970 0.1018 0.0222  0.0177  0.0019  247 PRO A CB  
2029 C  CG  . PRO A 248 ? 0.0978 0.1062 0.1132 0.0250  0.0166  -0.0001 247 PRO A CG  
2030 C  CD  . PRO A 248 ? 0.0831 0.0946 0.1037 0.0195  0.0129  0.0000  247 PRO A CD  
2031 N  N   . ALA A 249 ? 0.0969 0.0786 0.0804 0.0110  0.0168  -0.0019 248 ALA A N   
2032 C  CA  . ALA A 249 ? 0.0927 0.0877 0.0762 0.0137  0.0164  -0.0001 248 ALA A CA  
2033 C  C   . ALA A 249 ? 0.0908 0.0912 0.0767 0.0190  0.0108  0.0005  248 ALA A C   
2034 O  O   . ALA A 249 ? 0.0977 0.0935 0.0867 0.0237  0.0063  -0.0008 248 ALA A O   
2035 C  CB  . ALA A 249 ? 0.0998 0.0965 0.0823 0.0081  0.0209  0.0012  248 ALA A CB  
2036 N  N   . GLN A 250 ? 0.0796 0.0914 0.0798 0.0165  0.0059  -0.0016 249 GLN A N   
2037 C  CA  . GLN A 250 ? 0.0814 0.1035 0.0830 0.0175  0.0004  -0.0028 249 GLN A CA  
2038 C  C   . GLN A 250 ? 0.0913 0.1094 0.0870 0.0198  0.0004  -0.0053 249 GLN A C   
2039 O  O   . GLN A 250 ? 0.0971 0.1054 0.0988 0.0166  0.0037  -0.0079 249 GLN A O   
2040 C  CB  . GLN A 250 ? 0.0861 0.1064 0.0892 0.0101  0.0007  -0.0045 249 GLN A CB  
2041 C  CG  . GLN A 250 ? 0.0970 0.1141 0.0935 0.0095  0.0014  -0.0031 249 GLN A CG  
2042 C  CD  . GLN A 250 ? 0.0963 0.1250 0.0928 -0.0004 0.0107  -0.0091 249 GLN A CD  
2043 O  OE1 . GLN A 250 ? 0.0974 0.1580 0.1232 -0.0068 0.0135  -0.0281 249 GLN A OE1 
2044 N  NE2 . GLN A 250 ? 0.0975 0.1233 0.0950 0.0053  0.0062  -0.0104 249 GLN A NE2 
2045 N  N   . PRO A 251 ? 0.1040 0.1289 0.0944 0.0286  -0.0041 -0.0149 250 PRO A N   
2046 C  CA  . PRO A 251 ? 0.1177 0.1454 0.0963 0.0381  -0.0048 -0.0140 250 PRO A CA  
2047 C  C   . PRO A 251 ? 0.1220 0.1237 0.0925 0.0365  -0.0050 -0.0044 250 PRO A C   
2048 O  O   . PRO A 251 ? 0.1147 0.1223 0.0983 0.0406  -0.0070 0.0013  250 PRO A O   
2049 C  CB  . PRO A 251 ? 0.1294 0.1671 0.1107 0.0419  -0.0122 -0.0131 250 PRO A CB  
2050 C  CG  . PRO A 251 ? 0.1338 0.1759 0.1145 0.0339  -0.0128 -0.0152 250 PRO A CG  
2051 C  CD  . PRO A 251 ? 0.1140 0.1510 0.1049 0.0311  -0.0111 -0.0167 250 PRO A CD  
2052 N  N   . LEU A 252 ? 0.1320 0.1193 0.0961 0.0374  -0.0043 0.0094  251 LEU A N   
2053 C  CA  . LEU A 252 ? 0.1346 0.1145 0.0905 0.0265  -0.0006 0.0015  251 LEU A CA  
2054 C  C   . LEU A 252 ? 0.1246 0.1167 0.0831 0.0333  -0.0016 -0.0008 251 LEU A C   
2055 O  O   . LEU A 252 ? 0.1167 0.1127 0.0856 0.0268  -0.0047 -0.0011 251 LEU A O   
2056 C  CB  . LEU A 252 ? 0.1559 0.1207 0.1089 0.0125  0.0077  -0.0015 251 LEU A CB  
2057 C  CG  . LEU A 252 ? 0.1638 0.1315 0.1256 0.0004  0.0158  -0.0077 251 LEU A CG  
2058 C  CD1 . LEU A 252 ? 0.1618 0.1463 0.1309 -0.0008 0.0125  -0.0165 251 LEU A CD1 
2059 C  CD2 . LEU A 252 ? 0.1691 0.1487 0.1402 -0.0048 0.0191  0.0000  251 LEU A CD2 
2060 N  N   . LYS A 253 ? 0.1351 0.1268 0.0892 0.0477  -0.0077 -0.0083 252 LYS A N   
2061 C  CA  . LYS A 253 ? 0.1442 0.1616 0.0997 0.0382  -0.0090 -0.0159 252 LYS A CA  
2062 C  C   . LYS A 253 ? 0.1382 0.1660 0.1038 0.0325  -0.0059 -0.0189 252 LYS A C   
2063 O  O   . LYS A 253 ? 0.1801 0.1731 0.1223 0.0256  0.0025  -0.0159 252 LYS A O   
2064 C  CB  . LYS A 253 ? 0.1531 0.1708 0.1202 0.0298  -0.0018 -0.0276 252 LYS A CB  
2065 C  CG  . LYS A 253 ? 0.1700 0.1881 0.1444 0.0304  0.0083  -0.0307 252 LYS A CG  
2066 C  CD  . LYS A 253 ? 0.1807 0.2071 0.1704 0.0307  0.0151  -0.0244 252 LYS A CD  
2067 C  CE  . LYS A 253 ? 0.1849 0.2253 0.2097 0.0326  0.0212  -0.0234 252 LYS A CE  
2068 N  NZ  . LYS A 253 ? 0.1906 0.2474 0.2373 0.0249  0.0110  -0.0173 252 LYS A NZ  
2069 N  N   . ASN A 254 ? 0.1369 0.1742 0.0888 0.0308  -0.0045 -0.0282 253 ASN A N   
2070 C  CA  . ASN A 254 ? 0.1518 0.1901 0.1087 0.0267  0.0060  -0.0250 253 ASN A CA  
2071 C  C   . ASN A 254 ? 0.1497 0.1636 0.1216 0.0308  0.0112  -0.0151 253 ASN A C   
2072 O  O   . ASN A 254 ? 0.1767 0.1667 0.1593 0.0345  0.0082  -0.0169 253 ASN A O   
2073 C  CB  . ASN A 254 ? 0.1681 0.2061 0.1377 0.0210  0.0042  -0.0287 253 ASN A CB  
2074 C  CG  . ASN A 254 ? 0.2053 0.2281 0.1528 0.0138  0.0147  -0.0305 253 ASN A CG  
2075 O  OD1 . ASN A 254 ? 0.2441 0.2672 0.1759 -0.0037 0.0283  -0.0218 253 ASN A OD1 
2076 N  ND2 . ASN A 254 ? 0.2200 0.2325 0.1801 -0.0006 0.0089  -0.0365 253 ASN A ND2 
2077 N  N   . ARG A 255 ? 0.1287 0.1417 0.0982 0.0269  0.0142  0.0015  254 ARG A N   
2078 C  CA  . ARG A 255 ? 0.1140 0.1212 0.0900 0.0236  0.0160  -0.0033 254 ARG A CA  
2079 C  C   . ARG A 255 ? 0.1334 0.1291 0.1096 0.0206  0.0234  -0.0063 254 ARG A C   
2080 O  O   . ARG A 255 ? 0.1456 0.1355 0.1526 0.0149  0.0417  0.0118  254 ARG A O   
2081 C  CB  . ARG A 255 ? 0.1125 0.1089 0.0778 0.0201  0.0135  -0.0040 254 ARG A CB  
2082 C  CG  . ARG A 255 ? 0.1094 0.0948 0.0654 0.0226  0.0132  -0.0030 254 ARG A CG  
2083 C  CD  . ARG A 255 ? 0.1082 0.0910 0.0647 0.0199  0.0117  -0.0007 254 ARG A CD  
2084 N  NE  . ARG A 255 ? 0.0996 0.0852 0.0670 0.0210  0.0050  0.0045  254 ARG A NE  
2085 C  CZ  . ARG A 255 ? 0.0886 0.0786 0.0684 0.0139  0.0033  0.0056  254 ARG A CZ  
2086 N  NH1 . ARG A 255 ? 0.0825 0.0819 0.0734 0.0155  0.0060  0.0085  254 ARG A NH1 
2087 N  NH2 . ARG A 255 ? 0.0907 0.0756 0.0669 0.0132  -0.0053 0.0024  254 ARG A NH2 
2088 N  N   . GLN A 256 ? 0.1300 0.1480 0.1211 0.0117  0.0143  -0.0137 255 GLN A N   
2089 C  CA  . GLN A 256 ? 0.1513 0.1745 0.1317 0.0077  0.0070  -0.0122 255 GLN A CA  
2090 C  C   . GLN A 256 ? 0.1387 0.1519 0.1218 0.0111  -0.0005 0.0050  255 GLN A C   
2091 O  O   . GLN A 256 ? 0.1873 0.1455 0.1860 0.0037  -0.0183 0.0008  255 GLN A O   
2092 C  CB  . GLN A 256 ? 0.1753 0.2097 0.1637 0.0036  0.0185  -0.0103 255 GLN A CB  
2093 C  CG  . GLN A 256 ? 0.2198 0.2397 0.1954 0.0013  0.0166  0.0004  255 GLN A CG  
2094 C  CD  . GLN A 256 ? 0.2504 0.2681 0.2319 0.0109  0.0269  0.0072  255 GLN A CD  
2095 O  OE1 . GLN A 256 ? 0.3096 0.2876 0.2687 0.0227  0.0283  0.0026  255 GLN A OE1 
2096 N  NE2 . GLN A 256 ? 0.2652 0.3046 0.2473 0.0047  0.0301  0.0223  255 GLN A NE2 
2097 N  N   . ILE A 257 ? 0.1087 0.1319 0.0982 0.0104  0.0076  0.0108  256 ILE A N   
2098 C  CA  . ILE A 257 ? 0.1108 0.1244 0.0894 0.0111  0.0126  0.0093  256 ILE A CA  
2099 C  C   . ILE A 257 ? 0.1076 0.1179 0.0817 0.0052  0.0175  0.0119  256 ILE A C   
2100 O  O   . ILE A 257 ? 0.1203 0.1235 0.0886 0.0194  0.0238  0.0189  256 ILE A O   
2101 C  CB  . ILE A 257 ? 0.1170 0.1139 0.0902 0.0162  0.0071  0.0105  256 ILE A CB  
2102 C  CG1 . ILE A 257 ? 0.1236 0.1191 0.1122 0.0201  0.0105  0.0070  256 ILE A CG1 
2103 C  CG2 . ILE A 257 ? 0.1249 0.1231 0.0972 0.0120  0.0058  0.0071  256 ILE A CG2 
2104 C  CD1 . ILE A 257 ? 0.1381 0.1329 0.1174 0.0159  0.0145  0.0060  256 ILE A CD1 
2105 N  N   A LYS A 258 ? 0.1030 0.1161 0.0809 0.0013  0.0166  0.0094  257 LYS A N   
2106 N  N   B LYS A 258 ? 0.1030 0.1180 0.0813 -0.0008 0.0185  0.0115  257 LYS A N   
2107 C  CA  A LYS A 258 ? 0.1083 0.1216 0.0845 0.0002  0.0173  0.0059  257 LYS A CA  
2108 C  CA  B LYS A 258 ? 0.1087 0.1251 0.0848 -0.0037 0.0206  0.0094  257 LYS A CA  
2109 C  C   A LYS A 258 ? 0.1054 0.1191 0.0741 -0.0059 0.0196  0.0080  257 LYS A C   
2110 C  C   B LYS A 258 ? 0.1060 0.1207 0.0747 -0.0078 0.0211  0.0099  257 LYS A C   
2111 O  O   A LYS A 258 ? 0.1112 0.1236 0.0699 -0.0215 0.0175  0.0030  257 LYS A O   
2112 O  O   B LYS A 258 ? 0.1120 0.1246 0.0709 -0.0238 0.0183  0.0051  257 LYS A O   
2113 C  CB  A LYS A 258 ? 0.1212 0.1303 0.0955 0.0063  0.0164  -0.0007 257 LYS A CB  
2114 C  CB  B LYS A 258 ? 0.1221 0.1363 0.0972 -0.0009 0.0230  0.0058  257 LYS A CB  
2115 C  CG  A LYS A 258 ? 0.1405 0.1460 0.1156 0.0099  0.0118  -0.0062 257 LYS A CG  
2116 C  CG  B LYS A 258 ? 0.1415 0.1536 0.1148 -0.0021 0.0222  0.0044  257 LYS A CG  
2117 C  CD  A LYS A 258 ? 0.1613 0.1632 0.1339 0.0155  0.0074  -0.0066 257 LYS A CD  
2118 C  CD  B LYS A 258 ? 0.1668 0.1732 0.1328 -0.0004 0.0213  0.0028  257 LYS A CD  
2119 C  CE  A LYS A 258 ? 0.1809 0.1786 0.1520 0.0189  0.0047  -0.0083 257 LYS A CE  
2120 C  CE  B LYS A 258 ? 0.1806 0.1966 0.1432 -0.0012 0.0183  0.0023  257 LYS A CE  
2121 N  NZ  A LYS A 258 ? 0.1951 0.1910 0.1680 0.0238  0.0061  -0.0061 257 LYS A NZ  
2122 N  NZ  B LYS A 258 ? 0.2019 0.2150 0.1644 -0.0003 0.0224  0.0003  257 LYS A NZ  
2123 N  N   . ALA A 259 ? 0.1036 0.1235 0.0731 -0.0105 0.0225  0.0077  258 ALA A N   
2124 C  CA  . ALA A 259 ? 0.0995 0.1204 0.0799 -0.0094 0.0253  0.0025  258 ALA A CA  
2125 C  C   . ALA A 259 ? 0.0928 0.1212 0.0780 -0.0102 0.0269  -0.0027 258 ALA A C   
2126 O  O   . ALA A 259 ? 0.1024 0.1386 0.0798 -0.0016 0.0303  -0.0085 258 ALA A O   
2127 C  CB  . ALA A 259 ? 0.1043 0.1249 0.0945 -0.0095 0.0281  0.0006  258 ALA A CB  
2128 N  N   . SER A 260 ? 0.0957 0.1252 0.0811 -0.0089 0.0257  -0.0009 259 SER A N   
2129 C  CA  . SER A 260 ? 0.1010 0.1313 0.0979 -0.0101 0.0253  -0.0008 259 SER A CA  
2130 C  C   . SER A 260 ? 0.1019 0.1447 0.1061 -0.0111 0.0320  0.0058  259 SER A C   
2131 O  O   . SER A 260 ? 0.1086 0.1787 0.1355 -0.0055 0.0413  0.0036  259 SER A O   
2132 C  CB  . SER A 260 ? 0.1041 0.1235 0.1049 -0.0073 0.0173  0.0031  259 SER A CB  
2133 O  OG  . SER A 260 ? 0.1033 0.1300 0.0975 -0.0129 0.0151  -0.0023 259 SER A OG  
2134 N  N   . PHE A 261 ? 0.1117 0.1477 0.1187 -0.0173 0.0307  0.0146  260 PHE A N   
2135 C  CA  . PHE A 261 ? 0.1489 0.1556 0.1387 -0.0282 0.0308  0.0236  260 PHE A CA  
2136 C  C   . PHE A 261 ? 0.1985 0.1920 0.1629 -0.0415 0.0281  0.0428  260 PHE A C   
2137 O  O   . PHE A 261 ? 0.2451 0.1916 0.1590 -0.0442 0.0035  0.0685  260 PHE A O   
2138 C  CB  . PHE A 261 ? 0.1423 0.1358 0.1448 -0.0226 0.0208  0.0171  260 PHE A CB  
2139 C  CG  . PHE A 261 ? 0.1457 0.1284 0.1535 -0.0171 0.0134  0.0181  260 PHE A CG  
2140 C  CD1 . PHE A 261 ? 0.1437 0.1300 0.1484 -0.0179 0.0107  0.0100  260 PHE A CD1 
2141 C  CD2 . PHE A 261 ? 0.1718 0.1428 0.1815 -0.0159 0.0211  0.0267  260 PHE A CD2 
2142 C  CE1 . PHE A 261 ? 0.1484 0.1325 0.1543 -0.0149 0.0106  0.0114  260 PHE A CE1 
2143 C  CE2 . PHE A 261 ? 0.1836 0.1470 0.1877 -0.0054 0.0171  0.0222  260 PHE A CE2 
2144 C  CZ  . PHE A 261 ? 0.1653 0.1468 0.1861 -0.0029 0.0132  0.0084  260 PHE A CZ  
2145 N  N   . LYS A 262 ? 0.2571 0.2508 0.2032 -0.0621 0.0395  0.0605  261 LYS A N   
2146 C  CA  . LYS A 262 ? 0.3241 0.2934 0.2559 -0.0529 0.0377  0.0699  261 LYS A CA  
2147 C  C   . LYS A 262 ? 0.3746 0.3389 0.2981 -0.0426 0.0421  0.0620  261 LYS A C   
2148 O  O   . LYS A 262 ? 0.4686 0.3871 0.3490 -0.0431 0.0711  0.0703  261 LYS A O   
2149 C  CB  . LYS A 262 ? 0.3593 0.2920 0.2976 -0.0626 0.0402  0.0856  261 LYS A CB  
2150 C  CG  . LYS A 262 ? 0.4043 0.3257 0.3385 -0.0603 0.0339  0.0763  261 LYS A CG  
2151 C  CD  . LYS A 262 ? 0.4407 0.3657 0.3781 -0.0575 0.0241  0.0597  261 LYS A CD  
2152 C  CE  . LYS A 262 ? 0.4628 0.4042 0.4060 -0.0547 0.0296  0.0477  261 LYS A CE  
2153 N  NZ  . LYS A 262 ? 0.4804 0.4320 0.4350 -0.0503 0.0300  0.0406  261 LYS A NZ  
2193 ZN ZN  . ZN  C .   ? 0.0777 0.0587 0.0765 0.0037  0.0072  -0.0036 302 ZN  A ZN  
# 
